CNRS Nantes University US2B US2B
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***  OXIDOREDUCTASE 01-DEC-17 6F5K  ***

elNémo ID: 240226134522715038

Job options:

ID        	=	 240226134522715038
JOBID     	=	 OXIDOREDUCTASE 01-DEC-17 6F5K
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    OXIDOREDUCTASE                          01-DEC-17   6F5K              
TITLE     CRYSTAL STRUCTURE OF LACCASE FROM MYCELIOPHTHORA THERMOPHILA          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EXTRACELLULAR LACCASE, LCC1;                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 OTHER_DETAILS: IN THE STRUCTURE HIS98 IS OXIDIZED TO AN OXO-HIS (OHI)
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCELIOPHTHORA THERMOPHILA;                     
SOURCE   3 ORGANISM_COMMON: SPOROTRICHUM THERMOPHILE;                           
SOURCE   4 ORGANISM_TAXID: 78579;                                               
SOURCE   5 STRAIN: ATCC 42464 / BCRC 31852 / DSM 1799;                          
SOURCE   6 GENE: LCC1, MYCTH_51627;                                             
SOURCE   7 EXPRESSION_SYSTEM: ASPERGILLUS ORYZAE;                               
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 5062                                        
KEYWDS    LACCASE, ASCOMYCETES, OXIDOREDUCTASE                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.A.ERNST,L.J.JOERGENSEN,K.PIONTEK,C.BUKH,L.H.OESTERGAARD,S.LARSEN,   
AUTHOR   2 M.J.BJERRUM                                                          
REVDAT   5   17-JAN-24 6F5K    1       REMARK                                   
REVDAT   4   15-NOV-23 6F5K    1       HETSYN LINK   ATOM                       
REVDAT   3   29-JUL-20 6F5K    1       COMPND REMARK HETNAM LINK                
REVDAT   3 2                   1       SITE   ATOM                              
REVDAT   2   26-JUN-19 6F5K    1       JRNL                                     
REVDAT   1   12-DEC-18 6F5K    0                                                
JRNL        AUTH   H.A.ERNST,L.J.JORGENSEN,C.BUKH,K.PIONTEK,D.A.PLATTNER,       
JRNL        AUTH 2 L.H.OSTERGAARD,S.LARSEN,M.J.BJERRUM                          
JRNL        TITL   A COMPARATIVE STRUCTURAL ANALYSIS OF THE SURFACE PROPERTIES  
JRNL        TITL 2 OF ASCO-LACCASES.                                            
JRNL        REF    PLOS ONE                      V.  13 06589 2018              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   30395580                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0206589                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.62 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.62                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.23                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 85258                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.152                           
REMARK   3   R VALUE            (WORKING SET) : 0.150                           
REMARK   3   FREE R VALUE                     : 0.189                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4497                            
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  1.6620 -  1.6200    0.99     6170   310  0.3010 0.3150        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.20                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.066            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.44                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.40000                                             
REMARK   3    B22 (A**2) : 2.65000                                              
REMARK   3    B33 (A**2) : 0.75000                                              
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      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: 'HYDROGENS                                
REMARK   4                                                                      
REMARK   4 6F5K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-DEC-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200007779.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-APR-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : MASSIF-1                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.966                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 2M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA 0.5.24                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 89938                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.620                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.230                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 4.900                              
REMARK 200  R MERGE                    (I) : 0.10900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 7.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.62                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.68                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.86600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 2Q9O                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.52                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 3 UL PROTEIN (66 MG/ML) + 2 UL           
REMARK 280  RESERVOIR SOLUTION (0.1 M HEPES PH 7.5, 34 % PEG 400, 0.22 M        
REMARK 280  CACL2, 0.05 M GLYCINE), VAPOR DIFFUSION, HANGING DROP,              
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       81.81200            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       81.81200            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       33.72450            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       64.21300            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       33.72450            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       64.21300            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       81.81200            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       33.72450            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       64.21300            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       81.81200            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       33.72450            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       64.21300            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7400 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20740 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 27.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F                      
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     GLN A     1                                                      
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     GLN A   2    CG   CD   OE1  NE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    SER A    63     O    HOH A   702              2.09            
REMARK 500   O    HOH A  1045     O    HOH A  1183              2.09            
REMARK 500   OD1  ASP A   530     O    HOH A   703              2.18            
REMARK 500   O    HOH A  1047     O    HOH A  1158              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   841     O    HOH A  1000     3554     2.09            
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    SER A 142     -134.10     47.61                                   
REMARK 500    GLU A 235      -36.56   -151.04                                   
REMARK 500    ASP A 253     -128.74     48.17                                   
REMARK 500    ASN A 381      108.90   -163.67                                   
REMARK 500    ASN A 472       67.80     35.89                                   
REMARK 500    ARG A 476     -168.63   -167.37                                   
REMARK 500    ASN A 495       83.58   -154.55                                   
REMARK 500    ASP A 556     -157.20   -160.85                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 HIS A  438     ASP A  439                  149.05                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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     2PE A  628                                                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU A 602  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  93   NE2                                                    
REMARK 620 2 HIS A 434   NE2 169.9                                              
REMARK 620 3 HOH A1094   O    91.7  96.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU A 604  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  95   ND1                                                    
REMARK 620 2 HIS A 138   NE2 137.2                                              
REMARK 620 3 HIS A 504   NE2 105.9 112.5                                        
REMARK 620 4  OH A 629   O   122.2  84.6  78.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU A 603  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 140   NE2                                                    
REMARK 620 2 HIS A 436   NE2 114.3                                              
REMARK 620 3 HIS A 502   NE2 113.3 114.4                                        
REMARK 620 4  OH A 629   O    93.0 123.8  95.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 605  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 VAL A 341   O                                                      
REMARK 620 2 ASP A 530   OD1  25.7                                              
REMARK 620 3 ASP A 534   OD1  22.1   3.9                                        
REMARK 620 4 ASP A 534   OD2  21.6   4.3   2.8                                  
REMARK 620 5 HOH A 703   O    25.8   1.4   3.7   5.0                            
REMARK 620 6 HOH A 781   O    26.0   2.7   5.6   4.5   4.1                      
REMARK 620 7 HOH A 975   O    25.1   0.6   3.5   3.7   1.7   2.6                
REMARK 620 8 HOH A 999   O    22.0   3.8   0.5   2.4   3.8   5.4   3.4          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 606  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LEU A 363   O                                                      
REMARK 620 2 HOH A 828   O    95.8                                              
REMARK 620 3 HOH A 858   O    76.7  77.9                                        
REMARK 620 4 HOH A1106   O    90.9 148.6 133.4                                  
REMARK 620 5 HOH A1124   O    82.2  66.5 136.1  84.2                            
REMARK 620 6 HOH A1156   O   117.2 135.7  81.7  64.3 142.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU A 601  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 431   ND1                                                    
REMARK 620 2 CYS A 503   SG  128.4                                              
REMARK 620 3 HIS A 508   ND1 105.6 126.0                                        
REMARK 620 N                    1     2                                         
DBREF  6F5K A    1   559  UNP    G2QG31   G2QG31_MYCTT    48    602             
SEQADV 6F5K ASN A   62  UNP  G2QG31              INSERTION                      
SEQADV 6F5K SER A   63  UNP  G2QG31              INSERTION                      
SEQADV 6F5K ILE A   64  UNP  G2QG31              INSERTION                      
SEQADV 6F5K ILE A   65  UNP  G2QG31              INSERTION                      
SEQADV 6F5K GLY A   66  UNP  G2QG31    ARG   109 CONFLICT                       
SEQADV 6F5K ARG A  545  UNP  G2QG31    HIS   588 CONFLICT                       
SEQRES   1 A  559  GLN GLN SER CYS ASN THR PRO SER ASN ARG ALA CYS TRP          
SEQRES   2 A  559  THR ASP GLY TYR ASP ILE ASN THR ASP TYR GLU VAL ASP          
SEQRES   3 A  559  SER PRO ASP THR GLY VAL VAL ARG PRO TYR THR LEU THR          
SEQRES   4 A  559  LEU THR GLU VAL ASP ASN TRP THR GLY PRO ASP GLY VAL          
SEQRES   5 A  559  VAL LYS GLU LYS VAL MET LEU VAL ASN ASN SER ILE ILE          
SEQRES   6 A  559  GLY PRO THR ILE PHE ALA ASP TRP GLY ASP THR ILE GLN          
SEQRES   7 A  559  VAL THR VAL ILE ASN ASN LEU GLU THR ASN GLY THR SER          
SEQRES   8 A  559  ILE HIS TRP HIS GLY LEU OHI GLN LYS GLY THR ASN LEU          
SEQRES   9 A  559  HIS ASP GLY ALA ASN GLY ILE THR GLU CYS PRO ILE PRO          
SEQRES  10 A  559  PRO LYS GLY GLY ARG LYS VAL TYR ARG PHE LYS ALA GLN          
SEQRES  11 A  559  GLN TYR GLY THR SER TRP TYR HIS SER HIS PHE SER ALA          
SEQRES  12 A  559  GLN TYR GLY ASN GLY VAL VAL GLY ALA ILE GLN ILE ASN          
SEQRES  13 A  559  GLY PRO ALA SER LEU PRO TYR ASP THR ASP LEU GLY VAL          
SEQRES  14 A  559  PHE PRO ILE SER ASP TYR TYR TYR SER SER ALA ASP GLU          
SEQRES  15 A  559  LEU VAL GLU LEU THR LYS ASN SER GLY ALA PRO PHE SER          
SEQRES  16 A  559  ASP ASN VAL LEU PHE ASN GLY THR ALA LYS HIS PRO GLU          
SEQRES  17 A  559  THR GLY GLU GLY GLU TYR ALA ASN VAL THR LEU THR PRO          
SEQRES  18 A  559  GLY ARG ARG HIS ARG LEU ARG LEU ILE ASN THR SER VAL          
SEQRES  19 A  559  GLU ASN HIS PHE GLN VAL SER LEU VAL ASN HIS THR MET          
SEQRES  20 A  559  THR ILE ILE ALA ALA ASP MET VAL PRO VAL ASN ALA MET          
SEQRES  21 A  559  THR VAL ASP SER LEU PHE LEU GLY VAL GLY GLN ARG TYR          
SEQRES  22 A  559  ASP VAL VAL ILE GLU ALA SER ARG THR PRO GLY ASN TYR          
SEQRES  23 A  559  TRP PHE ASN VAL THR PHE GLY GLY GLY LEU LEU CYS GLY          
SEQRES  24 A  559  GLY SER ARG ASN PRO TYR PRO ALA ALA ILE PHE HIS TYR          
SEQRES  25 A  559  ALA GLY ALA PRO GLY GLY PRO PRO THR ASP GLU GLY LYS          
SEQRES  26 A  559  ALA PRO VAL ASP HIS ASN CYS LEU ASP LEU PRO ASN LEU          
SEQRES  27 A  559  LYS PRO VAL VAL ALA ARG ASP VAL PRO LEU SER GLY PHE          
SEQRES  28 A  559  ALA LYS ARG PRO ASP ASN THR LEU ASP VAL THR LEU ASP          
SEQRES  29 A  559  THR THR GLY THR PRO LEU PHE VAL TRP LYS VAL ASN GLY          
SEQRES  30 A  559  SER ALA ILE ASN ILE ASP TRP GLY ARG PRO VAL VAL ASP          
SEQRES  31 A  559  TYR VAL LEU THR GLN ASN THR SER PHE PRO PRO GLY TYR          
SEQRES  32 A  559  ASN ILE VAL GLU VAL ASN GLY ALA ASP GLN TRP SER TYR          
SEQRES  33 A  559  TRP LEU ILE GLU ASN ASP PRO GLY ALA PRO PHE THR LEU          
SEQRES  34 A  559  PRO HIS PRO MET HIS LEU HIS GLY HIS ASP PHE TYR VAL          
SEQRES  35 A  559  LEU GLY ARG SER PRO ASP GLU SER PRO ALA SER ASN GLU          
SEQRES  36 A  559  ARG HIS VAL PHE ASP PRO ALA ARG ASP ALA GLY LEU LEU          
SEQRES  37 A  559  SER GLY ALA ASN PRO VAL ARG ARG ASP VAL THR MET LEU          
SEQRES  38 A  559  PRO ALA PHE GLY TRP VAL VAL LEU ALA PHE ARG ALA ASP          
SEQRES  39 A  559  ASN PRO GLY ALA TRP LEU PHE HIS CYS HIS ILE ALA TRP          
SEQRES  40 A  559  HIS VAL SER GLY GLY LEU GLY VAL VAL TYR LEU GLU ARG          
SEQRES  41 A  559  ALA ASP ASP LEU ARG GLY ALA VAL SER ASP ALA ASP ALA          
SEQRES  42 A  559  ASP ASP LEU ASP ARG LEU CYS ALA ASP TRP ARG ARG TYR          
SEQRES  43 A  559  TRP PRO THR ASN PRO TYR PRO LYS SER ASP SER GLY LEU          
MODRES 6F5K OHI A   98  HIS  MODIFIED RESIDUE                                   
HET    OHI  A  98      16                                                       
HET    NAG  B   1      26                                                       
HET    NAG  B   2      26                                                       
HET    BMA  B   3      20                                                       
HET    MAN  B   4      20                                                       
HET    MAN  B   5      21                                                       
HET    NAG  C   1      26                                                       
HET    NAG  C   2      27                                                       
HET    NAG  D   1      26                                                       
HET    NAG  D   2      26                                                       
HET    BMA  D   3      20                                                       
HET    MAN  D   4      20                                                       
HET    MAN  D   5      20                                                       
HET    MAN  D   6      21                                                       
HET    NAG  E   1      26                                                       
HET    NAG  E   2      26                                                       
HET    BMA  E   3      21                                                       
HET    NAG  F   1      26                                                       
HET    NAG  F   2      26                                                       
HET    BMA  F   3      21                                                       
HET     CU  A 601       1                                                       
HET     CU  A 602       1                                                       
HET     CU  A 603       1                                                       
HET     CU  A 604       1                                                       
HET     CA  A 605       1                                                       
HET     CA  A 606       1                                                       
HET    NAG  A 626      27                                                       
HET    NAG  A 627      27                                                       
HET    2PE  A 628      23                                                       
HET     OH  A 629       1                                                       
HETNAM     OHI 3-(2-OXO-2H-IMIDAZOL-4-YL)-L-ALANINE                             
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     BMA BETA-D-MANNOPYRANOSE                                             
HETNAM     MAN ALPHA-D-MANNOPYRANOSE                                            
HETNAM      CU COPPER (II) ION                                                  
HETNAM      CA CALCIUM ION                                                      
HETNAM     2PE NONAETHYLENE GLYCOL                                              
HETNAM      OH HYDROXIDE ION                                                    
HETSYN     NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-           
HETSYN   2 NAG  D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-          
HETSYN   3 NAG  2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE                         
HETSYN     BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE                               
HETSYN     MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE                              
FORMUL   1  OHI    C6 H7 N3 O3                                                  
FORMUL   2  NAG    12(C8 H15 N O6)                                              
FORMUL   2  BMA    4(C6 H12 O6)                                                 
FORMUL   2  MAN    5(C6 H12 O6)                                                 
FORMUL   7   CU    4(CU 2+)                                                     
FORMUL  11   CA    2(CA 2+)                                                     
FORMUL  15  2PE    C18 H38 O10                                                  
FORMUL  16   OH    H O 1-                                                       
FORMUL  17  HOH   *526(H2 O)                                                    
HELIX    1 AA1 THR A  102  ASP A  106  5                                   5    
HELIX    2 AA2 ALA A  143  GLY A  148  5                                   6    
HELIX    3 AA3 SER A  179  SER A  190  1                                  12    
HELIX    4 AA4 GLY A  293  LEU A  297  5                                   5    
HELIX    5 AA5 ARG A  354  ASP A  356  5                                   3    
HELIX    6 AA6 PRO A  387  THR A  394  1                                   8    
HELIX    7 AA7 PRO A  400  TYR A  403  5                                   4    
HELIX    8 AA8 ASP A  460  ALA A  465  1                                   6    
HELIX    9 AA9 GLY A  466  LEU A  468  5                                   3    
HELIX   10 AB1 ILE A  505  GLY A  511  1                                   7    
HELIX   11 AB2 ARG A  520  VAL A  528  1                                   9    
HELIX   12 AB3 SER A  529  TRP A  547  1                                  19    
HELIX   13 AB4 PRO A  548  ASN A  550  5                                   3    
SHEET    1 AA1 2 CYS A  12  THR A  14  0                                        
SHEET    2 AA1 2 TYR A  17  ASP A  18 -1  O  TYR A  17   N  THR A  14           
SHEET    1 AA2 4 VAL A  53  VAL A  60  0                                        
SHEET    2 AA2 4 VAL A  33  THR A  47 -1  N  TRP A  46   O  LYS A  54           
SHEET    3 AA2 4 THR A  76  ASN A  84  1  O  ILE A  82   N  LEU A  38           
SHEET    4 AA2 4 GLY A 121  LYS A 128 -1  O  TYR A 125   N  VAL A  79           
SHEET    1 AA3 4 GLY A  66  ASP A  72  0                                        
SHEET    2 AA3 4 VAL A 150  ASN A 156  1  O  VAL A 150   N  GLY A  66           
SHEET    3 AA3 4 GLY A 133  SER A 139 -1  N  TYR A 137   O  GLY A 151           
SHEET    4 AA3 4 ILE A  92  HIS A  95 -1  N  HIS A  93   O  HIS A 138           
SHEET    1 AA4 6 ASN A 197  PHE A 200  0                                        
SHEET    2 AA4 6 THR A 165  TYR A 175 -1  N  SER A 173   O  LEU A 199           
SHEET    3 AA4 6 ARG A 224  ASN A 231  1  O  ILE A 230   N  ILE A 172           
SHEET    4 AA4 6 ARG A 272  GLU A 278 -1  O  VAL A 275   N  LEU A 227           
SHEET    5 AA4 6 MET A 247  ALA A 252 -1  N  ILE A 250   O  ASP A 274           
SHEET    6 AA4 6 VAL A 255  VAL A 262 -1  O  MET A 260   N  ILE A 249           
SHEET    1 AA5 5 ASN A 216  LEU A 219  0                                        
SHEET    2 AA5 5 ALA A 307  TYR A 312  1  O  HIS A 311   N  LEU A 219           
SHEET    3 AA5 5 ASN A 285  THR A 291 -1  N  TYR A 286   O  PHE A 310           
SHEET    4 AA5 5 PHE A 238  LEU A 242 -1  N  SER A 241   O  ASN A 289           
SHEET    5 AA5 5 LEU A 265  LEU A 267 -1  O  LEU A 267   N  PHE A 238           
SHEET    1 AA6 6 VAL A 372  VAL A 375  0                                        
SHEET    2 AA6 6 THR A 358  ASP A 364 -1  N  ASP A 364   O  VAL A 372           
SHEET    3 AA6 6 TRP A 414  ASN A 421  1  O  LEU A 418   N  LEU A 359           
SHEET    4 AA6 6 TRP A 486  ARG A 492 -1  O  VAL A 487   N  ILE A 419           
SHEET    5 AA6 6 PHE A 440  ARG A 445 -1  N  TYR A 441   O  ALA A 490           
SHEET    6 AA6 6 VAL A 474  ARG A 476 -1  O  ARG A 476   N  PHE A 440           
SHEET    1 AA7 5 ILE A 405  VAL A 408  0                                        
SHEET    2 AA7 5 GLY A 514  GLU A 519  1  O  VAL A 516   N  VAL A 406           
SHEET    3 AA7 5 GLY A 497  CYS A 503 -1  N  TRP A 499   O  TYR A 517           
SHEET    4 AA7 5 HIS A 431  LEU A 435 -1  N  HIS A 434   O  HIS A 502           
SHEET    5 AA7 5 VAL A 478  LEU A 481 -1  O  LEU A 481   N  HIS A 431           
SSBOND   1 CYS A    4    CYS A   12                          1555   1555  2.03  
SSBOND   2 CYS A  114    CYS A  540                          1555   1555  2.05  
SSBOND   3 CYS A  298    CYS A  332                          1555   1555  2.03  
LINK         ND2 ASN A  61                 C1  NAG B   1     1555   1555  1.43  
LINK         ND2 ASN A  88                 C1  NAG C   1     1555   1555  1.45  
LINK         C   LEU A  97                 N   OHI A  98     1555   1555  1.33  
LINK         C   OHI A  98                 N   GLN A  99     1555   1555  1.33  
LINK         ND2 ASN A 201                 C1  NAG D   1     1555   1555  1.44  
LINK         ND2 ASN A 216                 C1  NAG E   1     1555   1555  1.43  
LINK         ND2 ASN A 289                 C1  NAG F   1     1555   1555  1.44  
LINK         ND2 ASN A 376                 C1  NAG A 626     1555   1555  1.44  
LINK         ND2 ASN A 396                 C1  NAG A 627     1555   1555  1.44  
LINK         O4  NAG B   1                 C1  NAG B   2     1555   1555  1.45  
LINK         O4  NAG B   2                 C1  BMA B   3     1555   1555  1.44  
LINK         O6  BMA B   3                 C1  MAN B   4     1555   1555  1.45  
LINK         O3  MAN B   4                 C1  MAN B   5     1555   1555  1.44  
LINK         O4  NAG C   1                 C1  NAG C   2     1555   1555  1.42  
LINK         O4  NAG D   1                 C1  NAG D   2     1555   1555  1.43  
LINK         O4  NAG D   2                 C1  BMA D   3     1555   1555  1.43  
LINK         O3  BMA D   3                 C1  MAN D   4     1555   1555  1.44  
LINK         O2  MAN D   4                 C1  MAN D   5     1555   1555  1.44  
LINK         O2  MAN D   5                 C1  MAN D   6     1555   1555  1.44  
LINK         O4  NAG E   1                 C1  NAG E   2     1555   1555  1.42  
LINK         O4  NAG E   2                 C1  BMA E   3     1555   1555  1.44  
LINK         O4  NAG F   1                 C1  NAG F   2     1555   1555  1.44  
LINK         O4  NAG F   2                 C1  BMA F   3     1555   1555  1.44  
LINK         NE2 HIS A  93                CU    CU A 602     1555   1555  1.91  
LINK         ND1 HIS A  95                CU    CU A 604     1555   1555  1.95  
LINK         NE2 HIS A 138                CU    CU A 604     1555   1555  2.04  
LINK         NE2 HIS A 140                CU    CU A 603     1555   1555  2.09  
LINK         O   VAL A 341                CA    CA A 605     1555   8455  2.40  
LINK         O   LEU A 363                CA    CA A 606     1555   1555  2.29  
LINK         ND1 HIS A 431                CU    CU A 601     1555   1555  2.01  
LINK         NE2 HIS A 434                CU    CU A 602     1555   1555  1.89  
LINK         NE2 HIS A 436                CU    CU A 603     1555   1555  2.01  
LINK         NE2 HIS A 502                CU    CU A 603     1555   1555  2.08  
LINK         SG  CYS A 503                CU    CU A 601     1555   1555  2.16  
LINK         NE2 HIS A 504                CU    CU A 604     1555   1555  2.08  
LINK         ND1 HIS A 508                CU    CU A 601     1555   1555  2.02  
LINK         OD1BASP A 530                CA    CA A 605     1555   1555  3.10  
LINK         OD1 ASP A 534                CA    CA A 605     1555   1555  2.64  
LINK         OD2 ASP A 534                CA    CA A 605     1555   1555  2.39  
LINK        CU    CU A 602                 O   HOH A1094     1555   1555  2.61  
LINK        CU    CU A 603                 O    OH A 629     1555   1555  2.15  
LINK        CU    CU A 604                 O    OH A 629     1555   1555  2.58  
LINK        CA    CA A 605                 O   HOH A 703     1555   1555  2.35  
LINK        CA    CA A 605                 O   HOH A 781     1555   1555  2.40  
LINK        CA    CA A 605                 O   HOH A 975     1555   8555  2.46  
LINK        CA    CA A 605                 O   HOH A 999     1555   1555  2.27  
LINK        CA    CA A 606                 O   HOH A 828     1555   1555  2.46  
LINK        CA    CA A 606                 O   HOH A 858     1555   1555  2.39  
LINK        CA    CA A 606                 O   HOH A1106     1555   1555  2.34  
LINK        CA    CA A 606                 O   HOH A1124     1555   1555  2.50  
LINK        CA    CA A 606                 O   HOH A1156     1555   1555  2.81  
CISPEP   1 THR A  368    PRO A  369          0        -7.10                     
CRYST1   67.449  128.426  163.624  90.00  90.00  90.00 C 2 2 21      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014826  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007787  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006112        0.00000                         
ATOM      1  N   GLN A   2      11.963  10.659   8.845  1.00 50.39           N  
ANISOU    1  N   GLN A   2     6349   6516   6283     95   -255   1033       N  
ATOM      2  CA  GLN A   2      12.154   9.493   7.990  1.00 43.08           C  
ANISOU    2  CA  GLN A   2     5464   5494   5408    129   -260   1041       C  
ATOM      3  C   GLN A   2      11.135   9.488   6.859  1.00 49.84           C  
ANISOU    3  C   GLN A   2     6344   6307   6287    114   -239   1015       C  
ATOM      4  O   GLN A   2       9.974   9.840   7.064  1.00 34.22           O  
ANISOU    4  O   GLN A   2     4363   4359   4279     60   -227   1013       O  
ATOM      5  CB  GLN A   2      12.035   8.202   8.795  1.00 50.85           C  
ANISOU    5  CB  GLN A   2     6486   6444   6390    113   -280   1090       C  
ATOM      6  HA  GLN A   2      13.045   9.527   7.609  1.00 51.69           H  
ATOM      7  HB2 GLN A   2      11.113   7.903   8.768  1.00 61.02           H  
ATOM      8  HB3 GLN A   2      12.610   7.532   8.391  1.00 61.02           H  
ATOM      9  N   SER A   3      11.568   9.055   5.677  1.00 31.94           N  
ANISOU    9  N   SER A   3     4097   3969   4070    160   -235    994       N  
ATOM     10  CA  SER A   3      10.723   9.093   4.493  1.00 27.88           C  
ANISOU   10  CA  SER A   3     3602   3411   3580    150   -215    965       C  
ATOM     11  C   SER A   3       9.728   7.940   4.461  1.00 35.40           C  
ANISOU   11  C   SER A   3     4607   4303   4541    110   -219    988       C  
ATOM     12  O   SER A   3      10.043   6.811   4.849  1.00 28.79           O  
ANISOU   12  O   SER A   3     3805   3418   3716    119   -238   1018       O  
ATOM     13  CB  SER A   3      11.577   9.042   3.224  1.00 39.61           C  
ANISOU   13  CB  SER A   3     5090   4845   5113    214   -208    928       C  
ATOM     14  OG  SER A   3      10.760   8.876   2.076  1.00 35.64           O  
ANISOU   14  OG  SER A   3     4615   4292   4634    202   -188    885       O  
ATOM     15  H   SER A   3      12.352   8.733   5.535  1.00 38.33           H  
ATOM     16  HA  SER A   3      10.220   9.923   4.513  1.00 33.45           H  
ATOM     17  HB2 SER A   3      12.072   9.873   3.142  1.00 47.53           H  
ATOM     18  HB3 SER A   3      12.192   8.294   3.286  1.00 47.53           H  
ATOM     19  HG  SER A   3      11.010   8.203   1.641  1.00 42.77           H  
ATOM     20  N   CYS A   4       8.524   8.232   3.971  1.00 29.35           N  
ANISOU   20  N   CYS A   4     3846   3540   3767     65   -200    961       N  
ATOM     21  CA  CYS A   4       7.513   7.223   3.682  1.00 23.42           C  
ANISOU   21  CA  CYS A   4     3142   2729   3027     23   -202    978       C  
ATOM     22  C   CYS A   4       7.206   7.145   2.192  1.00 24.04           C  
ANISOU   22  C   CYS A   4     3241   2749   3143     38   -184    921       C  
ATOM     23  O   CYS A   4       6.196   6.552   1.798  1.00 26.17           O  
ANISOU   23  O   CYS A   4     3545   2980   3418     -6   -180    919       O  
ATOM     24  CB  CYS A   4       6.234   7.525   4.456  1.00 30.74           C  
ANISOU   24  CB  CYS A   4     4056   3719   3905    -53   -194    989       C  
ATOM     25  SG  CYS A   4       5.713   9.246   4.275  1.00 31.12           S  
ANISOU   25  SG  CYS A   4     4045   3860   3918    -64   -164    918       S  
ATOM     26  H   CYS A   4       8.264   9.032   3.794  1.00 35.22           H  
ATOM     27  HA  CYS A   4       7.840   6.357   3.974  1.00 28.10           H  
ATOM     28  HB2 CYS A   4       5.521   6.957   4.125  1.00 36.89           H  
ATOM     29  HB3 CYS A   4       6.385   7.353   5.399  1.00 36.89           H  
ATOM     30  N   ASN A   5       8.045   7.747   1.361  1.00 21.00           N  
ANISOU   30  N   ASN A   5     2837   2361   2782     94   -173    875       N  
ATOM     31  CA  ASN A   5       7.829   7.798  -0.080  1.00 19.79           C  
ANISOU   31  CA  ASN A   5     2698   2162   2658    110   -154    818       C  
ATOM     32  C   ASN A   5       8.422   6.541  -0.699  1.00 28.25           C  
ANISOU   32  C   ASN A   5     3819   3137   3778    151   -166    832       C  
ATOM     33  O   ASN A   5       9.642   6.347  -0.672  1.00 27.24           O  
ANISOU   33  O   ASN A   5     3686   2994   3671    212   -177    844       O  
ATOM     34  CB  ASN A   5       8.471   9.061  -0.651  1.00 20.88           C  
ANISOU   34  CB  ASN A   5     2790   2347   2794    148   -136    765       C  
ATOM     35  CG  ASN A   5       8.242   9.219  -2.139  1.00 24.00           C  
ANISOU   35  CG  ASN A   5     3196   2705   3215    162   -116    706       C  
ATOM     36  OD1 ASN A   5       9.102   8.876  -2.952  1.00 20.89           O  
ANISOU   36  OD1 ASN A   5     2814   2266   2855    214   -115    689       O  
ATOM     37  ND2 ASN A   5       7.086   9.766  -2.506  1.00 18.33           N  
ANISOU   37  ND2 ASN A   5     2473   2013   2480    116   -101    674       N  
ATOM     38  H   ASN A   5       8.765   8.144   1.613  1.00 25.20           H  
ATOM     39  HA  ASN A   5       6.880   7.814  -0.279  1.00 23.74           H  
ATOM     40  HB2 ASN A   5       8.093   9.835  -0.206  1.00 25.05           H  
ATOM     41  HB3 ASN A   5       9.429   9.025  -0.498  1.00 25.05           H  
ATOM     42 HD21 ASN A   5       6.909   9.877  -3.340  1.00 22.00           H  
ATOM     43 HD22 ASN A   5       6.517  10.008  -1.909  1.00 22.00           H  
ATOM     44  N   THR A   6       7.568   5.696  -1.257  1.00 22.29           N  
ANISOU   44  N   THR A   6     3112   2318   3038    119   -166    829       N  
ATOM     45  CA  THR A   6       7.966   4.421  -1.836  1.00 24.36           C  
ANISOU   45  CA  THR A   6     3431   2478   3345    151   -179    840       C  
ATOM     46  C   THR A   6       7.316   4.238  -3.192  1.00 23.44           C  
ANISOU   46  C   THR A   6     3343   2314   3249    139   -162    784       C  
ATOM     47  O   THR A   6       6.369   4.948  -3.544  1.00 25.43           O  
ANISOU   47  O   THR A   6     3575   2609   3478     94   -144    750       O  
ATOM     48  CB  THR A   6       7.541   3.255  -0.933  1.00 28.05           C  
ANISOU   48  CB  THR A   6     3945   2908   3805    112   -202    897       C  
ATOM     49  OG1 THR A   6       6.112   3.141  -1.009  1.00 26.41           O  
ANISOU   49  OG1 THR A   6     3754   2699   3580     32   -198    901       O  
ATOM     50  CG2 THR A   6       7.967   3.490   0.500  1.00 31.43           C  
ANISOU   50  CG2 THR A   6     4343   3401   4198    109   -216    942       C  
ATOM     51  H   THR A   6       6.724   5.848  -1.311  1.00 26.74           H  
ATOM     52  HA  THR A   6       8.930   4.420  -1.939  1.00 29.23           H  
ATOM     53  HB  THR A   6       7.962   2.430  -1.221  1.00 33.66           H  
ATOM     54  HG1 THR A   6       5.751   3.790  -0.616  1.00 31.69           H  
ATOM     55 HG21 THR A   6       7.639   2.773   1.065  1.00 37.72           H  
ATOM     56 HG22 THR A   6       8.934   3.519   0.557  1.00 37.72           H  
ATOM     57 HG23 THR A   6       7.606   4.332   0.819  1.00 37.72           H  
ATOM     58  N   PRO A   7       7.771   3.250  -3.965  1.00 23.68           N  
ANISOU   58  N   PRO A   7     3423   2254   3321    178   -168    775       N  
ATOM     59  CA  PRO A   7       7.112   2.978  -5.251  1.00 23.68           C  
ANISOU   59  CA  PRO A   7     3455   2204   3337    162   -153    723       C  
ATOM     60  C   PRO A   7       5.612   2.771  -5.145  1.00 25.95           C  
ANISOU   60  C   PRO A   7     3763   2494   3602     73   -154    730       C  
ATOM     61  O   PRO A   7       4.876   3.233  -6.025  1.00 25.01           O  
ANISOU   61  O   PRO A   7     3635   2391   3475     45   -135    681       O  
ATOM     62  CB  PRO A   7       7.826   1.711  -5.739  1.00 25.88           C  
ANISOU   62  CB  PRO A   7     3794   2379   3662    214   -167    727       C  
ATOM     63  CG  PRO A   7       9.186   1.820  -5.156  1.00 29.52           C  
ANISOU   63  CG  PRO A   7     4228   2866   4123    284   -173    742       C  
ATOM     64  CD  PRO A   7       9.004   2.458  -3.799  1.00 28.89           C  
ANISOU   64  CD  PRO A   7     4104   2865   4006    248   -183    792       C  
ATOM     65  HA  PRO A   7       7.288   3.710  -5.864  1.00 28.41           H  
ATOM     66  HB2 PRO A   7       7.367   0.921  -5.413  1.00 31.06           H  
ATOM     67  HB3 PRO A   7       7.860   1.698  -6.709  1.00 31.06           H  
ATOM     68  HG2 PRO A   7       9.577   0.937  -5.071  1.00 35.43           H  
ATOM     69  HG3 PRO A   7       9.742   2.376  -5.725  1.00 35.43           H  
ATOM     70  HD2 PRO A   7       8.893   1.783  -3.112  1.00 34.66           H  
ATOM     71  HD3 PRO A   7       9.757   3.031  -3.583  1.00 34.66           H  
ATOM     72  N   SER A   8       5.133   2.092  -4.102  1.00 24.04           N  
ANISOU   72  N   SER A   8     3545   2242   3348     26   -174    792       N  
ATOM     73  CA  SER A   8       3.707   1.822  -3.957  1.00 28.21           C  
ANISOU   73  CA  SER A   8     4090   2776   3852    -64   -176    803       C  
ATOM     74  C   SER A   8       2.955   2.951  -3.270  1.00 25.46           C  
ANISOU   74  C   SER A   8     3680   2540   3455   -111   -162    804       C  
ATOM     75  O   SER A   8       1.720   2.988  -3.332  1.00 30.43           O  
ANISOU   75  O   SER A   8     4307   3194   4061   -180   -156    799       O  
ATOM     76  CB  SER A   8       3.495   0.529  -3.166  1.00 26.27           C  
ANISOU   76  CB  SER A   8     3895   2482   3606    -95   -194    853       C  
ATOM     77  OG  SER A   8       4.078   0.619  -1.876  1.00 38.75           O  
ANISOU   77  OG  SER A   8     5451   4107   5165    -79   -204    900       O  
ATOM     78  H   SER A   8       5.617   1.778  -3.464  1.00 28.85           H  
ATOM     79  HA  SER A   8       3.325   1.701  -4.840  1.00 33.85           H  
ATOM     80  HB2 SER A   8       2.542   0.371  -3.070  1.00 31.53           H  
ATOM     81  HB3 SER A   8       3.906  -0.206  -3.647  1.00 31.53           H  
ATOM     82  HG  SER A   8       4.913   0.677  -1.942  1.00 46.50           H  
ATOM     83  N   ASN A   9       3.666   3.860  -2.611  1.00 23.47           N  
ANISOU   83  N   ASN A   9     3377   2356   3186    -74   -158    810       N  
ATOM     84  CA  ASN A   9       3.041   5.000  -1.950  1.00 23.21           C  
ANISOU   84  CA  ASN A   9     3285   2428   3107   -110   -145    805       C  
ATOM     85  C   ASN A   9       3.900   6.238  -2.220  1.00 18.67           C  
ANISOU   85  C   ASN A   9     2658   1904   2530    -50   -130    763       C  
ATOM     86  O   ASN A   9       4.696   6.676  -1.384  1.00 21.63           O  
ANISOU   86  O   ASN A   9     3005   2321   2892    -22   -136    786       O  
ATOM     87  CB  ASN A   9       2.863   4.741  -0.459  1.00 26.89           C  
ANISOU   87  CB  ASN A   9     3745   2933   3541   -148   -161    872       C  
ATOM     88  CG  ASN A   9       2.040   5.810   0.212  1.00 25.41           C  
ANISOU   88  CG  ASN A   9     3501   2851   3302   -191   -146    863       C  
ATOM     89  OD1 ASN A   9       1.634   6.783  -0.423  1.00 27.42           O  
ANISOU   89  OD1 ASN A   9     3721   3148   3547   -188   -125    808       O  
ATOM     90  ND2 ASN A   9       1.781   5.634   1.498  1.00 33.18           N  
ANISOU   90  ND2 ASN A   9     4476   3879   4250   -231   -157    917       N  
ATOM     91  H   ASN A   9       4.522   3.836  -2.532  1.00 28.17           H  
ATOM     92  HA  ASN A   9       2.168   5.157  -2.344  1.00 27.85           H  
ATOM     93  HB2 ASN A   9       2.412   3.891  -0.335  1.00 32.27           H  
ATOM     94  HB3 ASN A   9       3.734   4.720  -0.033  1.00 32.27           H  
ATOM     95 HD21 ASN A   9       1.315   6.216   1.926  1.00 39.81           H  
ATOM     96 HD22 ASN A   9       2.079   4.938   1.906  1.00 39.81           H  
ATOM     97  N   ARG A  10       3.742   6.806  -3.416  1.00 19.05           N  
ANISOU   97  N   ARG A  10     2697   1950   2590    -35   -111    702       N  
ATOM     98  CA  ARG A  10       4.416   8.054  -3.748  1.00 21.33           C  
ANISOU   98  CA  ARG A  10     2939   2290   2874     10    -96    661       C  
ATOM     99  C   ARG A  10       3.682   9.264  -3.186  1.00 17.82           C  
ANISOU   99  C   ARG A  10     2445   1939   2387    -24    -84    648       C  
ATOM    100  O   ARG A  10       4.255  10.359  -3.148  1.00 18.33           O  
ANISOU  100  O   ARG A  10     2470   2052   2442      8    -76    624       O  
ATOM    101  CB  ARG A  10       4.564   8.188  -5.266  1.00 19.76           C  
ANISOU  101  CB  ARG A  10     2751   2054   2703     39    -81    603       C  
ATOM    102  CG  ARG A  10       5.489   7.160  -5.915  1.00 21.79           C  
ANISOU  102  CG  ARG A  10     3052   2225   3003     89    -89    604       C  
ATOM    103  CD  ARG A  10       6.936   7.338  -5.480  1.00 20.57           C  
ANISOU  103  CD  ARG A  10     2876   2080   2859    153    -95    621       C  
ATOM    104  NE  ARG A  10       7.795   6.414  -6.207  1.00 20.84           N  
ANISOU  104  NE  ARG A  10     2947   2036   2933    207    -99    614       N  
ATOM    105  CZ  ARG A  10       9.078   6.200  -5.943  1.00 24.91           C  
ANISOU  105  CZ  ARG A  10     3456   2542   3468    269   -108    632       C  
ATOM    106  NH1 ARG A  10       9.686   6.845  -4.958  1.00 24.74           N  
ANISOU  106  NH1 ARG A  10     3392   2583   3426    282   -115    660       N  
ATOM    107  NH2 ARG A  10       9.755   5.333  -6.673  1.00 24.14           N  
ANISOU  107  NH2 ARG A  10     3393   2373   3408    320   -110    620       N  
ATOM    108  H   ARG A  10       3.253   6.487  -4.048  1.00 22.86           H  
ATOM    109  HA  ARG A  10       5.311   8.043  -3.374  1.00 25.59           H  
ATOM    110  HB2 ARG A  10       3.688   8.088  -5.670  1.00 23.71           H  
ATOM    111  HB3 ARG A  10       4.922   9.068  -5.463  1.00 23.71           H  
ATOM    112  HG2 ARG A  10       5.204   6.269  -5.661  1.00 26.15           H  
ATOM    113  HG3 ARG A  10       5.449   7.259  -6.879  1.00 26.15           H  
ATOM    114  HD2 ARG A  10       7.224   8.245  -5.668  1.00 24.68           H  
ATOM    115  HD3 ARG A  10       7.016   7.155  -4.531  1.00 24.68           H  
ATOM    116  HE  ARG A  10       7.445   5.974  -6.858  1.00 25.00           H  
ATOM    117 HH11 ARG A  10       9.248   7.410  -4.480  1.00 29.69           H  
ATOM    118 HH12 ARG A  10      10.517   6.697  -4.796  1.00 29.69           H  
ATOM    119 HH21 ARG A  10       9.364   4.912  -7.313  1.00 28.97           H  
ATOM    120 HH22 ARG A  10      10.586   5.188  -6.508  1.00 28.97           H  
ATOM    121  N   ALA A  11       2.446   9.090  -2.723  1.00 19.46           N  
ANISOU  121  N   ALA A  11     2653   2173   2568    -87    -84    664       N  
ATOM    122  CA  ALA A  11       1.715  10.213  -2.153  1.00 21.06           C  
ANISOU  122  CA  ALA A  11     2807   2465   2729   -115    -72    649       C  
ATOM    123  C   ALA A  11       2.340  10.692  -0.852  1.00 18.98           C  
ANISOU  123  C   ALA A  11     2514   2257   2439   -103    -79    680       C  
ATOM    124  O   ALA A  11       2.234  11.879  -0.523  1.00 18.58           O  
ANISOU  124  O   ALA A  11     2422   2276   2361    -99    -68    655       O  
ATOM    125  CB  ALA A  11       0.257   9.822  -1.917  1.00 22.85           C  
ANISOU  125  CB  ALA A  11     3038   2713   2932   -185    -70    662       C  
ATOM    126  H   ALA A  11       2.015   8.346  -2.726  1.00 23.35           H  
ATOM    127  HA  ALA A  11       1.736  10.947  -2.787  1.00 25.27           H  
ATOM    128  HB1 ALA A  11      -0.229   9.895  -2.753  1.00 27.42           H  
ATOM    129  HB2 ALA A  11       0.223   8.908  -1.593  1.00 27.42           H  
ATOM    130  HB3 ALA A  11      -0.127  10.421  -1.257  1.00 27.42           H  
ATOM    131  N   CYS A  12       2.977   9.795  -0.101  1.00 20.15           N  
ANISOU  131  N   CYS A  12     2686   2376   2593    -98    -98    734       N  
ATOM    132  CA  CYS A  12       3.556  10.119   1.197  1.00 18.62           C  
ANISOU  132  CA  CYS A  12     2468   2235   2371    -92   -108    771       C  
ATOM    133  C   CYS A  12       4.950  10.693   1.010  1.00 19.34           C  
ANISOU  133  C   CYS A  12     2541   2326   2480    -27   -110    755       C  
ATOM    134  O   CYS A  12       5.689  10.263   0.124  1.00 21.79           O  
ANISOU  134  O   CYS A  12     2874   2574   2831     16   -113    743       O  
ATOM    135  CB  CYS A  12       3.628   8.857   2.061  1.00 22.55           C  
ANISOU  135  CB  CYS A  12     3000   2700   2868   -116   -131    841       C  
ATOM    136  SG  CYS A  12       3.728   9.112   3.863  1.00 30.42           S  
ANISOU  136  SG  CYS A  12     3967   3780   3811   -144   -143    896       S  
ATOM    137  H   CYS A  12       3.089   8.974  -0.330  1.00 24.18           H  
ATOM    138  HA  CYS A  12       3.009  10.778   1.652  1.00 22.34           H  
ATOM    139  HB2 CYS A  12       2.831   8.331   1.892  1.00 27.06           H  
ATOM    140  HB3 CYS A  12       4.417   8.358   1.800  1.00 27.06           H  
ATOM    141  N   TRP A  13       5.314  11.661   1.852  1.00 18.36           N  
ANISOU  141  N   TRP A  13     2378   2276   2324    -21   -110    754       N  
ATOM    142  CA  TRP A  13       6.676  12.193   1.853  1.00 17.74           C  
ANISOU  142  CA  TRP A  13     2279   2206   2256     33   -115    746       C  
ATOM    143  C   TRP A  13       7.350  11.916   3.192  1.00 21.57           C  
ANISOU  143  C   TRP A  13     2755   2721   2718     34   -136    802       C  
ATOM    144  O   TRP A  13       8.309  11.141   3.241  1.00 24.93           O  
ANISOU  144  O   TRP A  13     3198   3105   3170     69   -154    837       O  
ATOM    145  CB  TRP A  13       6.659  13.680   1.504  1.00 20.53           C  
ANISOU  145  CB  TRP A  13     2595   2612   2595     42    -98    689       C  
ATOM    146  CG  TRP A  13       8.012  14.187   1.262  1.00 18.74           C  
ANISOU  146  CG  TRP A  13     2351   2388   2383     92   -102    677       C  
ATOM    147  CD1 TRP A  13       8.677  15.113   1.997  1.00 18.34           C  
ANISOU  147  CD1 TRP A  13     2266   2397   2306    101   -107    675       C  
ATOM    148  CD2 TRP A  13       8.916  13.755   0.236  1.00 15.89           C  
ANISOU  148  CD2 TRP A  13     2003   1969   2064    140   -102    667       C  
ATOM    149  NE1 TRP A  13       9.936  15.301   1.487  1.00 19.50           N  
ANISOU  149  NE1 TRP A  13     2402   2530   2476    148   -111    666       N  
ATOM    150  CE2 TRP A  13      10.110  14.476   0.407  1.00 20.30           C  
ANISOU  150  CE2 TRP A  13     2531   2562   2620    174   -107    660       C  
ATOM    151  CE3 TRP A  13       8.832  12.824  -0.806  1.00 17.03           C  
ANISOU  151  CE3 TRP A  13     2183   2039   2248    156    -99    660       C  
ATOM    152  CZ2 TRP A  13      11.211  14.311  -0.433  1.00 21.10           C  
ANISOU  152  CZ2 TRP A  13     2631   2631   2755    225   -107    649       C  
ATOM    153  CZ3 TRP A  13       9.931  12.659  -1.640  1.00 19.10           C  
ANISOU  153  CZ3 TRP A  13     2447   2267   2544    209    -98    646       C  
ATOM    154  CH2 TRP A  13      11.103  13.399  -1.446  1.00 20.08           C  
ANISOU  154  CH2 TRP A  13     2535   2431   2662    244   -102    641       C  
ATOM    155  H   TRP A  13       4.792  12.024   2.431  1.00 22.04           H  
ATOM    156  HA  TRP A  13       7.199  11.743   1.171  1.00 21.29           H  
ATOM    157  HB2 TRP A  13       6.134  13.815   0.700  1.00 24.64           H  
ATOM    158  HB3 TRP A  13       6.273  14.179   2.241  1.00 24.64           H  
ATOM    159  HD1 TRP A  13       8.329  15.556   2.737  1.00 22.01           H  
ATOM    160  HE1 TRP A  13      10.523  15.849   1.795  1.00 23.40           H  
ATOM    161  HE3 TRP A  13       8.058  12.326  -0.937  1.00 20.43           H  
ATOM    162  HZ2 TRP A  13      11.990  14.804  -0.309  1.00 25.32           H  
ATOM    163  HZ3 TRP A  13       9.886  12.048  -2.340  1.00 22.92           H  
ATOM    164  HH2 TRP A  13      11.825  13.267  -2.019  1.00 24.09           H  
ATOM    165  N   THR A  14       6.897  12.537   4.276  1.00 21.91           N  
ANISOU  165  N   THR A  14     2771   2839   2713     -2   -136    812       N  
ATOM    166  CA ATHR A  14       7.387  12.290   5.622  0.65 15.23           C  
ANISOU  166  CA ATHR A  14     1916   2032   1837    -11   -156    867       C  
ATOM    167  CA BTHR A  14       7.344  12.149   5.609  0.35 29.86           C  
ANISOU  167  CA BTHR A  14     3774   3879   3692    -13   -157    871       C  
ATOM    168  C   THR A  14       6.197  12.430   6.569  1.00 26.42           C  
ANISOU  168  C   THR A  14     3324   3510   3204    -73   -150    880       C  
ATOM    169  O   THR A  14       5.082  12.758   6.151  1.00 21.90           O  
ANISOU  169  O   THR A  14     2748   2950   2624   -103   -130    845       O  
ATOM    170  CB ATHR A  14       8.507  13.260   6.033  0.65 21.23           C  
ANISOU  170  CB ATHR A  14     2640   2844   2584     23   -161    854       C  
ATOM    171  CB BTHR A  14       8.649  12.867   5.968  0.35 29.18           C  
ANISOU  171  CB BTHR A  14     3657   3830   3602     29   -166    867       C  
ATOM    172  OG1ATHR A  14       8.027  14.610   5.987  0.65 34.83           O  
ANISOU  172  OG1ATHR A  14     4331   4624   4278      9   -142    798       O  
ATOM    173  OG1BTHR A  14       9.180  12.321   7.183  0.35 30.87           O  
ANISOU  173  OG1BTHR A  14     3870   4066   3792     23   -191    931       O  
ATOM    174  CG2ATHR A  14       9.723  13.132   5.120  0.65 29.41           C  
ANISOU  174  CG2ATHR A  14     3679   3830   3666     83   -166    842       C  
ATOM    175  CG2BTHR A  14       8.421  14.363   6.109  0.35 12.26           C  
ANISOU  175  CG2BTHR A  14     1476   1758   1425     19   -150    815       C  
ATOM    176  H  ATHR A  14       6.277  13.133   4.254  0.65 26.29           H  
ATOM    177  H  BTHR A  14       6.331  13.185   4.265  0.35 26.29           H  
ATOM    178  HA ATHR A  14       7.748  11.390   5.655  0.65 18.27           H  
ATOM    179  HA BTHR A  14       7.530  11.198   5.653  0.35 35.83           H  
ATOM    180  HB ATHR A  14       8.786  13.041   6.936  0.65 25.48           H  
ATOM    181  HB BTHR A  14       9.299  12.739   5.260  0.35 35.02           H  
ATOM    182  HG1ATHR A  14       8.628  15.138   6.244  0.65 41.80           H  
ATOM    183  HG1BTHR A  14       8.778  12.648   7.844  0.35 37.04           H  
ATOM    184 HG21ATHR A  14      10.151  13.996   5.015  0.65 35.29           H  
ATOM    185 HG21BTHR A  14       7.927  14.697   5.345  0.35 14.72           H  
ATOM    186 HG22ATHR A  14      10.360  12.509   5.503  0.65 35.29           H  
ATOM    187 HG22BTHR A  14       7.915  14.546   6.916  0.35 14.72           H  
ATOM    188 HG23ATHR A  14       9.450  12.807   4.248  0.65 35.29           H  
ATOM    189 HG23BTHR A  14       9.273  14.825   6.160  0.35 14.72           H  
ATOM    190  N   ASP A  15       6.442  12.233   7.859  1.00 25.92           N  
ANISOU  190  N   ASP A  15     3252   3492   3104    -92   -166    930       N  
ATOM    191  CA AASP A  15       5.382  12.465   8.828  0.61 42.52           C  
ANISOU  191  CA AASP A  15     5338   5665   5151   -151   -158    940       C  
ATOM    192  CA BASP A  15       5.395  12.475   8.845  0.39 37.43           C  
ANISOU  192  CA BASP A  15     4694   5022   4507   -151   -159    941       C  
ATOM    193  C   ASP A  15       4.885  13.901   8.699  1.00 29.76           C  
ANISOU  193  C   ASP A  15     3686   4113   3510   -153   -134    872       C  
ATOM    194  O   ASP A  15       5.662  14.856   8.807  1.00 30.46           O  
ANISOU  194  O   ASP A  15     3750   4233   3592   -122   -134    843       O  
ATOM    195  CB AASP A  15       5.858  12.196  10.250  0.61 34.86           C  
ANISOU  195  CB AASP A  15     4361   4744   4141   -168   -180   1000       C  
ATOM    196  CB BASP A  15       5.922  12.234  10.256  0.39 30.55           C  
ANISOU  196  CB BASP A  15     3814   4200   3595   -165   -180    999       C  
ATOM    197  CG AASP A  15       4.773  12.465  11.271  0.61 32.41           C  
ANISOU  197  CG AASP A  15     4030   4513   3770   -227   -169   1002       C  
ATOM    198  CG BASP A  15       5.539  10.869  10.788  0.39 34.81           C  
ANISOU  198  CG BASP A  15     4387   4701   4138   -199   -194   1048       C  
ATOM    199  OD1AASP A  15       3.652  11.940  11.093  0.61 35.47           O  
ANISOU  199  OD1AASP A  15     4433   4891   4155   -270   -158   1008       O  
ATOM    200  OD1BASP A  15       6.220   9.882  10.440  0.39 54.62           O  
ANISOU  200  OD1BASP A  15     6929   7132   6690   -169   -212   1073       O  
ATOM    201  OD2AASP A  15       5.031  13.215  12.235  0.61 65.37           O  
ANISOU  201  OD2AASP A  15     8175   8763   7902   -233   -169    993       O  
ATOM    202  OD2BASP A  15       4.547  10.780  11.541  0.39 51.01           O  
ANISOU  202  OD2BASP A  15     6431   6802   6149   -254   -187   1056       O  
ATOM    203  H  AASP A  15       7.192  11.972   8.190  0.61 31.10           H  
ATOM    204  H  BASP A  15       7.191  11.964   8.186  0.39 31.10           H  
ATOM    205  HA AASP A  15       4.654  11.849   8.651  0.61 51.02           H  
ATOM    206  HA BASP A  15       4.662  11.858   8.699  0.39 44.92           H  
ATOM    207  HB2AASP A  15       6.123  11.266  10.327  0.61 41.83           H  
ATOM    208  HB2BASP A  15       6.890  12.295  10.249  0.39 36.67           H  
ATOM    209  HB3AASP A  15       6.612  12.773  10.449  0.61 41.83           H  
ATOM    210  HB3BASP A  15       5.553  12.905  10.852  0.39 36.67           H  
ATOM    211  N   GLY A  16       3.592  14.047   8.434  1.00 24.08           N  
ANISOU  211  N   GLY A  16     2961   3410   2776   -189   -114    846       N  
ATOM    212  CA  GLY A  16       2.984  15.346   8.314  1.00 22.63           C  
ANISOU  212  CA  GLY A  16     2745   3284   2570   -190    -92    782       C  
ATOM    213  C   GLY A  16       3.028  15.975   6.939  1.00 22.70           C  
ANISOU  213  C   GLY A  16     2754   3250   2618   -153    -78    722       C  
ATOM    214  O   GLY A  16       2.439  17.049   6.757  1.00 24.91           O  
ANISOU  214  O   GLY A  16     3010   3571   2882   -152    -61    669       O  
ATOM    215  H   GLY A  16       3.046  13.393   8.319  1.00 28.89           H  
ATOM    216  HA2 GLY A  16       2.052  15.273   8.571  1.00 27.16           H  
ATOM    217  HA3 GLY A  16       3.433  15.952   8.925  1.00 27.16           H  
ATOM    218  N   TYR A  17       3.702  15.355   5.968  1.00 18.71           N  
ANISOU  218  N   TYR A  17     2277   2666   2165   -122    -86    729       N  
ATOM    219  CA  TYR A  17       3.924  15.955   4.655  1.00 17.14           C  
ANISOU  219  CA  TYR A  17     2079   2430   2004    -85    -76    675       C  
ATOM    220  C   TYR A  17       3.584  14.950   3.569  1.00 22.39           C  
ANISOU  220  C   TYR A  17     2779   3019   2711    -86    -75    680       C  
ATOM    221  O   TYR A  17       4.141  13.846   3.540  1.00 21.62           O  
ANISOU  221  O   TYR A  17     2711   2867   2638    -78    -90    722       O  
ATOM    222  CB  TYR A  17       5.372  16.441   4.512  1.00 20.58           C  
ANISOU  222  CB  TYR A  17     2507   2855   2456    -37    -85    667       C  
ATOM    223  CG  TYR A  17       5.654  17.637   5.378  1.00 19.73           C  
ANISOU  223  CG  TYR A  17     2367   2820   2308    -37    -85    647       C  
ATOM    224  CD1 TYR A  17       5.350  18.924   4.942  1.00 22.06           C  
ANISOU  224  CD1 TYR A  17     2644   3141   2596    -28    -70    587       C  
ATOM    225  CD2 TYR A  17       6.202  17.479   6.640  1.00 21.04           C  
ANISOU  225  CD2 TYR A  17     2523   3029   2443    -47   -101    688       C  
ATOM    226  CE1 TYR A  17       5.598  20.017   5.736  1.00 26.26           C  
ANISOU  226  CE1 TYR A  17     3152   3734   3092    -30    -70    566       C  
ATOM    227  CE2 TYR A  17       6.444  18.564   7.442  1.00 30.33           C  
ANISOU  227  CE2 TYR A  17     3672   4271   3579    -50   -100    667       C  
ATOM    228  CZ  TYR A  17       6.137  19.828   6.987  1.00 26.64           C  
ANISOU  228  CZ  TYR A  17     3190   3824   3107    -42    -85    604       C  
ATOM    229  OH  TYR A  17       6.380  20.913   7.794  1.00 30.01           O  
ANISOU  229  OH  TYR A  17     3596   4313   3495    -45    -86    580       O  
ATOM    230  H   TYR A  17       4.046  14.571   6.051  1.00 22.45           H  
ATOM    231  HA  TYR A  17       3.328  16.713   4.548  1.00 20.57           H  
ATOM    232  HB2 TYR A  17       5.975  15.728   4.775  1.00 24.69           H  
ATOM    233  HB3 TYR A  17       5.535  16.690   3.589  1.00 24.69           H  
ATOM    234  HD1 TYR A  17       4.973  19.046   4.101  1.00 26.47           H  
ATOM    235  HD2 TYR A  17       6.408  16.626   6.948  1.00 25.25           H  
ATOM    236  HE1 TYR A  17       5.405  20.874   5.431  1.00 31.52           H  
ATOM    237  HE2 TYR A  17       6.812  18.447   8.288  1.00 36.39           H  
ATOM    238  HH  TYR A  17       5.851  21.536   7.605  1.00 36.02           H  
ATOM    239  N   ASP A  18       2.653  15.317   2.696  1.00 15.90           N  
ANISOU  239  N   ASP A  18     1954   2192   1895    -96    -58    637       N  
ATOM    240  CA  ASP A  18       2.265  14.423   1.618  1.00 18.71           C  
ANISOU  240  CA  ASP A  18     2342   2479   2287   -102    -57    636       C  
ATOM    241  C   ASP A  18       1.742  15.247   0.449  1.00 18.72           C  
ANISOU  241  C   ASP A  18     2332   2479   2300    -90    -40    576       C  
ATOM    242  O   ASP A  18       1.847  16.477   0.431  1.00 15.71           O  
ANISOU  242  O   ASP A  18     1924   2140   1907    -71    -32    538       O  
ATOM    243  CB  ASP A  18       1.255  13.382   2.131  1.00 18.81           C  
ANISOU  243  CB  ASP A  18     2371   2491   2284   -158    -61    678       C  
ATOM    244  CG  ASP A  18      -0.010  14.010   2.703  1.00 27.06           C  
ANISOU  244  CG  ASP A  18     3383   3616   3283   -201    -46    662       C  
ATOM    245  OD1 ASP A  18      -0.430  15.076   2.210  1.00 19.44           O  
ANISOU  245  OD1 ASP A  18     2392   2683   2313   -188    -31    610       O  
ATOM    246  OD2 ASP A  18      -0.578  13.439   3.664  1.00 23.60           O  
ANISOU  246  OD2 ASP A  18     2944   3209   2814   -247    -51    705       O  
ATOM    247  H   ASP A  18       2.239  16.071   2.708  1.00 19.08           H  
ATOM    248  HA  ASP A  18       3.053  13.952   1.303  1.00 22.45           H  
ATOM    249  HB2 ASP A  18       0.996  12.806   1.395  1.00 22.57           H  
ATOM    250  HB3 ASP A  18       1.672  12.858   2.832  1.00 22.57           H  
ATOM    251  N   ILE A  19       1.220  14.542  -0.559  1.00 16.10           N  
ANISOU  251  N   ILE A  19     2027   2094   1996   -101    -37    568       N  
ATOM    252  CA  ILE A  19       0.772  15.164  -1.796  1.00 16.21           C  
ANISOU  252  CA  ILE A  19     2036   2099   2024    -90    -24    515       C  
ATOM    253  C   ILE A  19      -0.366  16.141  -1.561  1.00 16.99           C  
ANISOU  253  C   ILE A  19     2099   2266   2088   -113    -12    486       C  
ATOM    254  O   ILE A  19      -0.633  16.998  -2.412  1.00 17.01           O  
ANISOU  254  O   ILE A  19     2089   2276   2098    -95     -2    440       O  
ATOM    255  CB  ILE A  19       0.361  14.060  -2.797  1.00 16.48           C  
ANISOU  255  CB  ILE A  19     2108   2065   2088   -106    -26    518       C  
ATOM    256  CG1 ILE A  19       0.207  14.638  -4.206  1.00 15.95           C  
ANISOU  256  CG1 ILE A  19     2040   1980   2041    -85    -16    466       C  
ATOM    257  CG2 ILE A  19      -0.931  13.388  -2.368  1.00 19.43           C  
ANISOU  257  CG2 ILE A  19     2484   2457   2440   -167    -26    542       C  
ATOM    258  CD1 ILE A  19       1.527  15.109  -4.827  1.00 18.38           C  
ANISOU  258  CD1 ILE A  19     2350   2260   2373    -30    -15    445       C  
ATOM    259  H   ILE A  19       1.115  13.688  -0.549  1.00 19.32           H  
ATOM    260  HA  ILE A  19       1.506  15.672  -2.176  1.00 19.45           H  
ATOM    261  HB  ILE A  19       1.066  13.394  -2.806  1.00 19.77           H  
ATOM    262 HG12 ILE A  19      -0.165  13.955  -4.785  1.00 19.14           H  
ATOM    263 HG13 ILE A  19      -0.390  15.401  -4.166  1.00 19.14           H  
ATOM    264 HG21 ILE A  19      -1.049  12.574  -2.882  1.00 23.31           H  
ATOM    265 HG22 ILE A  19      -0.879  13.178  -1.423  1.00 23.31           H  
ATOM    266 HG23 ILE A  19      -1.671  13.993  -2.533  1.00 23.31           H  
ATOM    267 HD11 ILE A  19       1.332  15.689  -5.579  1.00 22.06           H  
ATOM    268 HD12 ILE A  19       2.035  15.594  -4.158  1.00 22.06           H  
ATOM    269 HD13 ILE A  19       2.029  14.335  -5.127  1.00 22.06           H  
ATOM    270  N   ASN A  20      -1.054  16.028  -0.431  1.00 15.74           N  
ANISOU  270  N   ASN A  20     1924   2163   1894   -150    -11    511       N  
ATOM    271  CA  ASN A  20      -2.185  16.892  -0.129  1.00 17.32           C  
ANISOU  271  CA  ASN A  20     2087   2434   2059   -169      2    483       C  
ATOM    272  C   ASN A  20      -1.800  18.100   0.711  1.00 14.45           C  
ANISOU  272  C   ASN A  20     1693   2130   1667   -146      6    464       C  
ATOM    273  O   ASN A  20      -2.629  19.002   0.881  1.00 18.53           O  
ANISOU  273  O   ASN A  20     2179   2704   2158   -148     18    431       O  
ATOM    274  CB  ASN A  20      -3.271  16.080   0.579  1.00 17.39           C  
ANISOU  274  CB  ASN A  20     2092   2477   2040   -228      4    518       C  
ATOM    275  CG  ASN A  20      -3.926  15.070  -0.344  1.00 21.31           C  
ANISOU  275  CG  ASN A  20     2614   2922   2559   -259      1    526       C  
ATOM    276  OD1 ASN A  20      -4.221  15.377  -1.495  1.00 23.38           O  
ANISOU  276  OD1 ASN A  20     2878   3163   2843   -245      6    488       O  
ATOM    277  ND2 ASN A  20      -4.126  13.855   0.146  1.00 28.27           N  
ANISOU  277  ND2 ASN A  20     3520   3784   3437   -303     -8    576       N  
ATOM    278  H   ASN A  20      -0.882  15.451   0.183  1.00 18.89           H  
ATOM    279  HA  ASN A  20      -2.562  17.230  -0.956  1.00 20.78           H  
ATOM    280  HB2 ASN A  20      -2.875  15.599   1.322  1.00 20.87           H  
ATOM    281  HB3 ASN A  20      -3.958  16.683   0.902  1.00 20.87           H  
ATOM    282 HD21 ASN A  20      -4.495  13.250  -0.342  1.00 33.92           H  
ATOM    283 HD22 ASN A  20      -3.888  13.671   0.951  1.00 33.92           H  
ATOM    284  N   THR A  21      -0.569  18.144   1.223  1.00 16.67           N  
ANISOU  284  N   THR A  21     1982   2400   1952   -121     -4    482       N  
ATOM    285  CA  THR A  21      -0.092  19.304   1.963  1.00 18.76           C  
ANISOU  285  CA  THR A  21     2222   2715   2191   -100     -3    462       C  
ATOM    286  C   THR A  21      -0.172  20.535   1.075  1.00 17.85           C  
ANISOU  286  C   THR A  21     2096   2599   2087    -68      6    404       C  
ATOM    287  O   THR A  21       0.133  20.468  -0.117  1.00 17.06           O  
ANISOU  287  O   THR A  21     2014   2446   2024    -48      5    388       O  
ATOM    288  CB  THR A  21       1.352  19.082   2.421  1.00 19.12           C  
ANISOU  288  CB  THR A  21     2279   2739   2246    -78    -18    491       C  
ATOM    289  OG1 THR A  21       1.418  17.912   3.247  1.00 17.29           O  
ANISOU  289  OG1 THR A  21     2061   2505   2005   -106    -29    550       O  
ATOM    290  CG2 THR A  21       1.877  20.300   3.190  1.00 21.49           C  
ANISOU  290  CG2 THR A  21     2555   3092   2517    -61    -19    468       C  
ATOM    291  H   THR A  21       0.010  17.512   1.155  1.00 20.00           H  
ATOM    292  HA  THR A  21      -0.638  19.443   2.753  1.00 22.51           H  
ATOM    293  HB  THR A  21       1.922  18.958   1.646  1.00 22.94           H  
ATOM    294  HG1 THR A  21       0.975  17.289   2.899  1.00 20.75           H  
ATOM    295 HG21 THR A  21       2.731  20.090   3.601  1.00 25.79           H  
ATOM    296 HG22 THR A  21       1.996  21.049   2.585  1.00 25.79           H  
ATOM    297 HG23 THR A  21       1.247  20.552   3.883  1.00 25.79           H  
ATOM    298  N   ASP A  22      -0.620  21.655   1.641  1.00 16.60           N  
ANISOU  298  N   ASP A  22     1910   2499   1896    -64     13    372       N  
ATOM    299  CA  ASP A  22      -0.607  22.916   0.899  1.00 16.63           C  
ANISOU  299  CA  ASP A  22     1909   2500   1911    -32     18    319       C  
ATOM    300  C   ASP A  22       0.828  23.427   0.909  1.00 13.44           C  
ANISOU  300  C   ASP A  22     1514   2073   1519     -3      7    317       C  
ATOM    301  O   ASP A  22       1.262  24.111   1.839  1.00 16.38           O  
ANISOU  301  O   ASP A  22     1875   2483   1865      1      4    311       O  
ATOM    302  CB  ASP A  22      -1.559  23.947   1.485  1.00 22.25           C  
ANISOU  302  CB  ASP A  22     2592   3276   2586    -32     28    283       C  
ATOM    303  CG  ASP A  22      -1.697  25.176   0.590  1.00 29.77           C  
ANISOU  303  CG  ASP A  22     3543   4216   3553      2     31    231       C  
ATOM    304  OD1 ASP A  22      -0.883  25.314  -0.354  1.00 23.96           O  
ANISOU  304  OD1 ASP A  22     2827   3426   2851     22     24    225       O  
ATOM    305  OD2 ASP A  22      -2.615  25.994   0.809  1.00 25.42           O  
ANISOU  305  OD2 ASP A  22     2971   3708   2979      8     40    196       O  
ATOM    306  H   ASP A  22      -0.932  21.709   2.440  1.00 19.91           H  
ATOM    307  HA  ASP A  22      -0.896  22.747  -0.011  1.00 19.96           H  
ATOM    308  HB2 ASP A  22      -2.436  23.547   1.589  1.00 26.70           H  
ATOM    309  HB3 ASP A  22      -1.222  24.237   2.348  1.00 26.70           H  
ATOM    310  N   TYR A  23       1.570  23.099  -0.154  1.00 17.76           N  
ANISOU  310  N   TYR A  23     2081   2560   2105     15      2    320       N  
ATOM    311  CA  TYR A  23       2.990  23.424  -0.235  1.00 16.21           C  
ANISOU  311  CA  TYR A  23     1891   2343   1923     40     -8    323       C  
ATOM    312  C   TYR A  23       3.250  24.923  -0.331  1.00 18.10           C  
ANISOU  312  C   TYR A  23     2122   2601   2153     58     -8    280       C  
ATOM    313  O   TYR A  23       4.395  25.342  -0.140  1.00 22.32           O  
ANISOU  313  O   TYR A  23     2657   3134   2689     71    -17    282       O  
ATOM    314  CB  TYR A  23       3.640  22.709  -1.443  1.00 15.95           C  
ANISOU  314  CB  TYR A  23     1881   2248   1934     56    -10    332       C  
ATOM    315  CG  TYR A  23       2.872  22.921  -2.718  1.00 15.60           C  
ANISOU  315  CG  TYR A  23     1843   2177   1908     60     -1    300       C  
ATOM    316  CD1 TYR A  23       3.053  24.068  -3.464  1.00 16.94           C  
ANISOU  316  CD1 TYR A  23     2010   2342   2084     80      1    261       C  
ATOM    317  CD2 TYR A  23       1.926  22.000  -3.151  1.00 15.15           C  
ANISOU  317  CD2 TYR A  23     1795   2101   1858     40      4    309       C  
ATOM    318  CE1 TYR A  23       2.334  24.294  -4.601  1.00 15.40           C  
ANISOU  318  CE1 TYR A  23     1821   2127   1902     83      7    235       C  
ATOM    319  CE2 TYR A  23       1.194  22.224  -4.295  1.00 15.57           C  
ANISOU  319  CE2 TYR A  23     1854   2137   1926     41     11    280       C  
ATOM    320  CZ  TYR A  23       1.407  23.385  -5.007  1.00 14.28           C  
ANISOU  320  CZ  TYR A  23     1686   1972   1768     64     12    243       C  
ATOM    321  OH  TYR A  23       0.714  23.687  -6.148  1.00 18.54           O  
ANISOU  321  OH  TYR A  23     2230   2497   2319     67     16    216       O  
ATOM    322  H   TYR A  23       1.270  22.685  -0.846  1.00 21.31           H  
ATOM    323  HA  TYR A  23       3.421  23.096   0.571  1.00 19.45           H  
ATOM    324  HB2 TYR A  23       4.537  23.056  -1.571  1.00 19.15           H  
ATOM    325  HB3 TYR A  23       3.674  21.756  -1.267  1.00 19.15           H  
ATOM    326  HD1 TYR A  23       3.677  24.699  -3.186  1.00 20.33           H  
ATOM    327  HD2 TYR A  23       1.786  21.221  -2.662  1.00 18.17           H  
ATOM    328  HE1 TYR A  23       2.478  25.068  -5.096  1.00 18.48           H  
ATOM    329  HE2 TYR A  23       0.565  21.603  -4.583  1.00 18.69           H  
ATOM    330  HH  TYR A  23       0.244  23.031  -6.381  1.00 22.25           H  
ATOM    331  N   GLU A  24       2.238  25.734  -0.634  1.00 17.40           N  
ANISOU  331  N   GLU A  24     2026   2528   2056     60      0    241       N  
ATOM    332  CA  GLU A  24       2.416  27.180  -0.601  1.00 20.62           C  
ANISOU  332  CA  GLU A  24     2431   2951   2453     77     -2    201       C  
ATOM    333  C   GLU A  24       2.377  27.729   0.814  1.00 26.15           C  
ANISOU  333  C   GLU A  24     3117   3707   3113     69     -3    195       C  
ATOM    334  O   GLU A  24       2.728  28.895   1.013  1.00 25.44           O  
ANISOU  334  O   GLU A  24     3028   3626   3011     81     -8    164       O  
ATOM    335  CB  GLU A  24       1.362  27.857  -1.473  1.00 23.19           C  
ANISOU  335  CB  GLU A  24     2756   3270   2785     88      5    163       C  
ATOM    336  CG  GLU A  24       1.705  27.740  -2.952  1.00 25.09           C  
ANISOU  336  CG  GLU A  24     3014   3456   3064    101      4    158       C  
ATOM    337  CD  GLU A  24       0.666  28.346  -3.863  1.00 29.21           C  
ANISOU  337  CD  GLU A  24     3535   3971   3592    111      8    126       C  
ATOM    338  OE1 GLU A  24       0.597  27.904  -5.023  1.00 32.68           O  
ANISOU  338  OE1 GLU A  24     3986   4375   4058    113      9    128       O  
ATOM    339  OE2 GLU A  24      -0.082  29.249  -3.430  1.00 81.88           O  
ANISOU  339  OE2 GLU A  24    10194  10674  10242    120     10     97       O  
ATOM    340  H   GLU A  24       1.450  25.473  -0.859  1.00 20.88           H  
ATOM    341  HA  GLU A  24       3.279  27.409  -0.979  1.00 24.74           H  
ATOM    342  HB2 GLU A  24       0.502  27.434  -1.324  1.00 27.83           H  
ATOM    343  HB3 GLU A  24       1.313  28.798  -1.244  1.00 27.83           H  
ATOM    344  HG2 GLU A  24       2.545  28.197  -3.115  1.00 30.11           H  
ATOM    345  HG3 GLU A  24       1.788  26.801  -3.180  1.00 30.11           H  
ATOM    346  N   VAL A  25       1.977  26.916   1.790  1.00 17.92           N  
ANISOU  346  N   VAL A  25     2063   2701   2046     46      0    225       N  
ATOM    347  CA  VAL A  25       2.004  27.293   3.195  1.00 20.34           C  
ANISOU  347  CA  VAL A  25     2355   3064   2308     34     -1    224       C  
ATOM    348  C   VAL A  25       3.062  26.515   3.965  1.00 25.90           C  
ANISOU  348  C   VAL A  25     3061   3774   3006     21    -14    272       C  
ATOM    349  O   VAL A  25       3.741  27.073   4.831  1.00 27.48           O  
ANISOU  349  O   VAL A  25     3255   4005   3180     19    -22    269       O  
ATOM    350  CB  VAL A  25       0.612  27.088   3.836  1.00 20.97           C  
ANISOU  350  CB  VAL A  25     2416   3197   2356     15     13    220       C  
ATOM    351  CG1 VAL A  25       0.642  27.435   5.333  1.00 47.56           C  
ANISOU  351  CG1 VAL A  25     5768   6630   5673      1     13    219       C  
ATOM    352  CG2 VAL A  25      -0.426  27.910   3.115  1.00 26.22           C  
ANISOU  352  CG2 VAL A  25     3074   3861   3026     34     23    172       C  
ATOM    353  H   VAL A  25       1.680  26.120   1.655  1.00 21.51           H  
ATOM    354  HA  VAL A  25       2.236  28.233   3.257  1.00 24.41           H  
ATOM    355  HB  VAL A  25       0.367  26.153   3.755  1.00 25.17           H  
ATOM    356 HG11 VAL A  25      -0.041  26.920   5.790  1.00 57.07           H  
ATOM    357 HG12 VAL A  25       1.517  27.216   5.690  1.00 57.07           H  
ATOM    358 HG13 VAL A  25       0.469  28.384   5.441  1.00 57.07           H  
ATOM    359 HG21 VAL A  25      -0.996  27.317   2.601  1.00 31.46           H  
ATOM    360 HG22 VAL A  25      -0.955  28.393   3.768  1.00 31.46           H  
ATOM    361 HG23 VAL A  25       0.021  28.535   2.523  1.00 31.46           H  
ATOM    362  N   ASP A  26       3.189  25.224   3.683  1.00 21.25           N  
ANISOU  362  N   ASP A  26     2480   3155   2438     11    -16    317       N  
ATOM    363  CA  ASP A  26       3.969  24.304   4.495  1.00 20.76           C  
ANISOU  363  CA  ASP A  26     2419   3100   2368     -2    -28    369       C  
ATOM    364  C   ASP A  26       5.004  23.611   3.628  1.00 23.64           C  
ANISOU  364  C   ASP A  26     2800   3404   2776     18    -38    394       C  
ATOM    365  O   ASP A  26       4.680  23.101   2.552  1.00 24.02           O  
ANISOU  365  O   ASP A  26     2862   3405   2858     25    -32    391       O  
ATOM    366  CB  ASP A  26       3.070  23.252   5.148  1.00 25.10           C  
ANISOU  366  CB  ASP A  26     2966   3673   2897    -34    -24    406       C  
ATOM    367  CG  ASP A  26       2.250  23.813   6.264  1.00 38.71           C  
ANISOU  367  CG  ASP A  26     4668   5471   4569    -55    -15    390       C  
ATOM    368  OD1 ASP A  26       2.856  24.299   7.237  1.00 33.08           O  
ANISOU  368  OD1 ASP A  26     3946   4798   3824    -57    -23    391       O  
ATOM    369  OD2 ASP A  26       1.007  23.782   6.159  1.00 29.20           O  
ANISOU  369  OD2 ASP A  26     3453   4287   3353    -69      0    375       O  
ATOM    370  H   ASP A  26       2.820  24.849   3.003  1.00 25.50           H  
ATOM    371  HA  ASP A  26       4.427  24.804   5.188  1.00 24.91           H  
ATOM    372  HB2 ASP A  26       2.465  22.894   4.480  1.00 30.12           H  
ATOM    373  HB3 ASP A  26       3.623  22.541   5.508  1.00 30.12           H  
ATOM    374  N   SER A  27       6.237  23.578   4.103  1.00 21.74           N  
ANISOU  374  N   SER A  27     2557   3169   2534     27    -53    416       N  
ATOM    375  CA  SER A  27       7.272  22.773   3.478  1.00 21.32           C  
ANISOU  375  CA  SER A  27     2515   3068   2519     48    -63    446       C  
ATOM    376  C   SER A  27       8.086  22.116   4.577  1.00 25.20           C  
ANISOU  376  C   SER A  27     2999   3582   2993     43    -80    497       C  
ATOM    377  O   SER A  27       8.221  22.680   5.669  1.00 25.26           O  
ANISOU  377  O   SER A  27     2991   3645   2960     28    -86    498       O  
ATOM    378  CB  SER A  27       8.196  23.614   2.590  1.00 27.09           C  
ANISOU  378  CB  SER A  27     3244   3777   3273     74    -64    415       C  
ATOM    379  OG  SER A  27       8.940  24.536   3.366  1.00 47.71           O  
ANISOU  379  OG  SER A  27     5840   6432   5857     71    -74    406       O  
ATOM    380  H   SER A  27       6.500  24.018   4.794  1.00 26.09           H  
ATOM    381  HA  SER A  27       6.870  22.088   2.921  1.00 25.59           H  
ATOM    382  HB2 SER A  27       8.810  23.024   2.126  1.00 32.51           H  
ATOM    383  HB3 SER A  27       7.657  24.104   1.949  1.00 32.51           H  
ATOM    384  HG  SER A  27       9.493  24.126   3.847  1.00 57.26           H  
ATOM    385  N   PRO A  28       8.649  20.939   4.322  1.00 21.45           N  
ANISOU  385  N   PRO A  28     2536   3066   2546     56    -89    540       N  
ATOM    386  CA  PRO A  28       9.536  20.346   5.327  1.00 29.51           C  
ANISOU  386  CA  PRO A  28     3550   4108   3554     58   -109    591       C  
ATOM    387  C   PRO A  28      10.680  21.307   5.619  1.00 25.05           C  
ANISOU  387  C   PRO A  28     2963   3579   2976     71   -120    577       C  
ATOM    388  O   PRO A  28      11.148  22.035   4.742  1.00 33.04           O  
ANISOU  388  O   PRO A  28     3971   4574   4008     90   -114    540       O  
ATOM    389  CB  PRO A  28      10.015  19.045   4.674  1.00 41.74           C  
ANISOU  389  CB  PRO A  28     5119   5593   5146     82   -116    628       C  
ATOM    390  CG  PRO A  28       9.057  18.788   3.536  1.00 27.92           C  
ANISOU  390  CG  PRO A  28     3390   3794   3424     80    -98    600       C  
ATOM    391  CD  PRO A  28       8.578  20.133   3.088  1.00 20.59           C  
ANISOU  391  CD  PRO A  28     2449   2889   2484     75    -83    541       C  
ATOM    392  HA  PRO A  28       9.065  20.120   6.144  1.00 35.41           H  
ATOM    393  HB2 PRO A  28      10.920  19.157   4.345  1.00 50.08           H  
ATOM    394  HB3 PRO A  28       9.984  18.323   5.321  1.00 50.08           H  
ATOM    395  HG2 PRO A  28       9.520  18.332   2.816  1.00 33.50           H  
ATOM    396  HG3 PRO A  28       8.315  18.247   3.849  1.00 33.50           H  
ATOM    397  HD2 PRO A  28       9.159  20.497   2.402  1.00 24.70           H  
ATOM    398  HD3 PRO A  28       7.667  20.084   2.758  1.00 24.70           H  
ATOM    399  N   ASP A  29      11.084  21.362   6.876  1.00 35.42           N  
ANISOU  399  N   ASP A  29     4262   4944   4252     56   -135    605       N  
ATOM    400  CA  ASP A  29      12.241  22.162   7.270  1.00 65.16           C  
ANISOU  400  CA  ASP A  29     8006   8748   8002     63   -149    598       C  
ATOM    401  C   ASP A  29      13.384  21.165   7.421  1.00 33.73           C  
ANISOU  401  C   ASP A  29     4020   4756   4042     88   -170    653       C  
ATOM    402  O   ASP A  29      13.631  20.624   8.500  1.00 45.98           O  
ANISOU  402  O   ASP A  29     5564   6338   5567     77   -187    700       O  
ATOM    403  CB  ASP A  29      11.960  22.969   8.527  1.00 99.21           C  
ANISOU  403  CB  ASP A  29    12305  13132  12259     31   -154    586       C  
ATOM    404  CG  ASP A  29      11.254  24.290   8.220  1.00108.53           C  
ANISOU  404  CG  ASP A  29    13488  14324  13426     20   -136    520       C  
ATOM    405  OD1 ASP A  29      11.431  24.834   7.105  1.00 51.54           O  
ANISOU  405  OD1 ASP A  29     6275   7068   6240     39   -128    484       O  
ATOM    406  OD2 ASP A  29      10.524  24.787   9.102  1.00 78.08           O  
ANISOU  406  OD2 ASP A  29     9627  10514   9526     -5   -132    503       O  
ATOM    407  H   ASP A  29      10.704  20.943   7.524  1.00 42.50           H  
ATOM    408  HA  ASP A  29      12.471  22.811   6.587  1.00 78.19           H  
ATOM    409  HB2 ASP A  29      11.390  22.451   9.117  1.00119.05           H  
ATOM    410  HB3 ASP A  29      12.800  23.170   8.970  1.00119.05           H  
ATOM    411  N   THR A  30      14.058  20.895   6.305  1.00 26.21           N  
ANISOU  411  N   THR A  30     3070   3756   3135    123   -167    648       N  
ATOM    412  CA  THR A  30      15.102  19.889   6.280  1.00 26.11           C  
ANISOU  412  CA  THR A  30     3050   3723   3146    157   -185    696       C  
ATOM    413  C   THR A  30      16.384  20.358   6.942  1.00 25.02           C  
ANISOU  413  C   THR A  30     2879   3640   2988    164   -205    712       C  
ATOM    414  O   THR A  30      17.174  19.520   7.387  1.00 30.54           O  
ANISOU  414  O   THR A  30     3569   4342   3692    186   -226    763       O  
ATOM    415  CB  THR A  30      15.418  19.495   4.835  1.00 24.83           C  
ANISOU  415  CB  THR A  30     2899   3499   3036    195   -173    679       C  
ATOM    416  OG1 THR A  30      16.023  20.608   4.167  1.00 25.54           O  
ANISOU  416  OG1 THR A  30     2970   3605   3130    202   -165    635       O  
ATOM    417  CG2 THR A  30      14.145  19.098   4.113  1.00 25.64           C  
ANISOU  417  CG2 THR A  30     3034   3550   3157    185   -153    660       C  
ATOM    418  H   THR A  30      13.926  21.283   5.550  1.00 31.46           H  
ATOM    419  HA  THR A  30      14.780  19.105   6.752  1.00 31.33           H  
ATOM    420  HB  THR A  30      16.026  18.739   4.820  1.00 29.79           H  
ATOM    421  HG1 THR A  30      15.660  21.324   4.416  1.00 30.65           H  
ATOM    422 HG21 THR A  30      13.685  19.890   3.792  1.00 30.77           H  
ATOM    423 HG22 THR A  30      14.356  18.529   3.356  1.00 30.77           H  
ATOM    424 HG23 THR A  30      13.558  18.615   4.715  1.00 30.77           H  
ATOM    425  N   GLY A  31      16.602  21.669   7.015  1.00 26.91           N  
ANISOU  425  N   GLY A  31     3102   3921   3204    145   -203    670       N  
ATOM    426  CA  GLY A  31      17.871  22.189   7.466  1.00 38.16           C  
ANISOU  426  CA  GLY A  31     4494   5395   4612    148   -222    679       C  
ATOM    427  C   GLY A  31      19.000  21.965   6.494  1.00 39.84           C  
ANISOU  427  C   GLY A  31     4688   5586   4862    188   -223    682       C  
ATOM    428  O   GLY A  31      20.156  22.238   6.829  1.00 31.59           O  
ANISOU  428  O   GLY A  31     3611   4585   3807    194   -241    697       O  
ATOM    429  H   GLY A  31      16.026  22.272   6.807  1.00 32.30           H  
ATOM    430  HA2 GLY A  31      17.786  23.144   7.613  1.00 45.80           H  
ATOM    431  HA3 GLY A  31      18.107  21.761   8.304  1.00 45.80           H  
ATOM    432  N   VAL A  32      18.702  21.481   5.294  1.00 21.99           N  
ANISOU  432  N   VAL A  32     2447   3264   2646    215   -205    668       N  
ATOM    433  CA  VAL A  32      19.724  21.091   4.332  1.00 20.61           C  
ANISOU  433  CA  VAL A  32     2256   3067   2508    259   -204    672       C  
ATOM    434  C   VAL A  32      19.928  22.222   3.337  1.00 21.39           C  
ANISOU  434  C   VAL A  32     2346   3167   2613    250   -188    619       C  
ATOM    435  O   VAL A  32      18.966  22.866   2.892  1.00 21.47           O  
ANISOU  435  O   VAL A  32     2379   3157   2620    227   -171    578       O  
ATOM    436  CB  VAL A  32      19.343  19.785   3.610  1.00 23.13           C  
ANISOU  436  CB  VAL A  32     2603   3315   2870    295   -195    688       C  
ATOM    437  CG1 VAL A  32      20.304  19.491   2.470  1.00 29.47           C  
ANISOU  437  CG1 VAL A  32     3391   4095   3711    341   -188    680       C  
ATOM    438  CG2 VAL A  32      19.345  18.614   4.586  1.00 27.11           C  
ANISOU  438  CG2 VAL A  32     3115   3814   3370    305   -215    749       C  
ATOM    439  H   VAL A  32      17.898  21.367   5.011  1.00 26.39           H  
ATOM    440  HA  VAL A  32      20.559  20.947   4.804  1.00 24.73           H  
ATOM    441  HB  VAL A  32      18.451  19.893   3.244  1.00 27.75           H  
ATOM    442 HG11 VAL A  32      20.124  18.601   2.127  1.00 35.36           H  
ATOM    443 HG12 VAL A  32      20.172  20.148   1.769  1.00 35.36           H  
ATOM    444 HG13 VAL A  32      21.213  19.539   2.803  1.00 35.36           H  
ATOM    445 HG21 VAL A  32      18.825  17.887   4.209  1.00 32.53           H  
ATOM    446 HG22 VAL A  32      20.259  18.326   4.732  1.00 32.53           H  
ATOM    447 HG23 VAL A  32      18.951  18.902   5.425  1.00 32.53           H  
ATOM    448  N   VAL A  33      21.191  22.472   2.998  1.00 16.69           N  
ANISOU  448  N   VAL A  33     1717   2600   2025    269   -195    621       N  
ATOM    449  CA  VAL A  33      21.565  23.383   1.926  1.00 14.83           C  
ANISOU  449  CA  VAL A  33     1471   2364   1798    264   -181    579       C  
ATOM    450  C   VAL A  33      22.182  22.570   0.797  1.00 17.40           C  
ANISOU  450  C   VAL A  33     1790   2658   2166    314   -170    583       C  
ATOM    451  O   VAL A  33      22.997  21.667   1.031  1.00 21.82           O  
ANISOU  451  O   VAL A  33     2328   3225   2738    352   -181    621       O  
ATOM    452  CB  VAL A  33      22.531  24.485   2.406  1.00 26.53           C  
ANISOU  452  CB  VAL A  33     2919   3913   3249    236   -196    572       C  
ATOM    453  CG1 VAL A  33      22.900  25.415   1.246  1.00 21.58           C  
ANISOU  453  CG1 VAL A  33     2285   3283   2632    227   -182    532       C  
ATOM    454  CG2 VAL A  33      21.890  25.264   3.547  1.00 28.35           C  
ANISOU  454  CG2 VAL A  33     3161   4174   3437    190   -207    563       C  
ATOM    455  H   VAL A  33      21.866  22.111   3.389  1.00 20.03           H  
ATOM    456  HA  VAL A  33      20.765  23.820   1.594  1.00 17.79           H  
ATOM    457  HB  VAL A  33      23.351  24.082   2.731  1.00 31.84           H  
ATOM    458 HG11 VAL A  33      22.436  26.259   1.358  1.00 25.90           H  
ATOM    459 HG12 VAL A  33      23.859  25.561   1.251  1.00 25.90           H  
ATOM    460 HG13 VAL A  33      22.633  24.999   0.411  1.00 25.90           H  
ATOM    461 HG21 VAL A  33      22.445  26.031   3.756  1.00 34.02           H  
ATOM    462 HG22 VAL A  33      21.008  25.558   3.271  1.00 34.02           H  
ATOM    463 HG23 VAL A  33      21.818  24.686   4.322  1.00 34.02           H  
ATOM    464  N   ARG A  34      21.772  22.890  -0.425  1.00 15.31           N  
ANISOU  464  N   ARG A  34     1542   2356   1920    314   -147    544       N  
ATOM    465  CA  ARG A  34      22.297  22.261  -1.629  1.00 17.88           C  
ANISOU  465  CA  ARG A  34     1861   2652   2281    358   -132    538       C  
ATOM    466  C   ARG A  34      23.111  23.277  -2.406  1.00 19.98           C  
ANISOU  466  C   ARG A  34     2098   2952   2540    346   -125    510       C  
ATOM    467  O   ARG A  34      22.542  24.058  -3.187  1.00 18.99           O  
ANISOU  467  O   ARG A  34     1993   2808   2414    321   -110    472       O  
ATOM    468  CB  ARG A  34      21.156  21.734  -2.498  1.00 20.15           C  
ANISOU  468  CB  ARG A  34     2192   2870   2592    365   -112    516       C  
ATOM    469  CG  ARG A  34      20.250  20.782  -1.786  1.00 21.62           C  
ANISOU  469  CG  ARG A  34     2410   3022   2783    367   -118    542       C  
ATOM    470  CD  ARG A  34      20.741  19.363  -1.903  1.00 32.37           C  
ANISOU  470  CD  ARG A  34     3774   4350   4176    419   -122    575       C  
ATOM    471  NE  ARG A  34      19.962  18.478  -1.051  1.00 39.35           N  
ANISOU  471  NE  ARG A  34     4687   5206   5059    414   -134    609       N  
ATOM    472  CZ  ARG A  34      19.678  17.214  -1.343  1.00 46.25           C  
ANISOU  472  CZ  ARG A  34     5591   6020   5962    444   -132    626       C  
ATOM    473  NH1 ARG A  34      20.090  16.675  -2.484  1.00 65.43           N  
ANISOU  473  NH1 ARG A  34     8024   8410   8425    486   -119    608       N  
ATOM    474  NH2 ARG A  34      18.968  16.495  -0.489  1.00 41.31           N  
ANISOU  474  NH2 ARG A  34     4991   5373   5331    430   -145    660       N  
ATOM    475  H   ARG A  34      21.174  23.486  -0.586  1.00 18.37           H  
ATOM    476  HA  ARG A  34      22.869  21.519  -1.379  1.00 21.46           H  
ATOM    477  HB2 ARG A  34      20.620  22.484  -2.799  1.00 24.17           H  
ATOM    478  HB3 ARG A  34      21.534  21.269  -3.261  1.00 24.17           H  
ATOM    479  HG2 ARG A  34      20.214  21.016  -0.845  1.00 25.95           H  
ATOM    480  HG3 ARG A  34      19.363  20.831  -2.175  1.00 25.95           H  
ATOM    481  HD2 ARG A  34      20.653  19.064  -2.822  1.00 38.85           H  
ATOM    482  HD3 ARG A  34      21.670  19.318  -1.628  1.00 38.85           H  
ATOM    483  HE  ARG A  34      19.665  18.794  -0.309  1.00 47.22           H  
ATOM    484 HH11 ARG A  34      20.546  17.146  -3.041  1.00 78.51           H  
ATOM    485 HH12 ARG A  34      19.902  15.856  -2.665  1.00 78.51           H  
ATOM    486 HH21 ARG A  34      18.695  16.846   0.246  1.00 49.57           H  
ATOM    487 HH22 ARG A  34      18.779  15.675  -0.670  1.00 49.57           H  
ATOM    488  N   PRO A  35      24.430  23.316  -2.239  1.00 19.19           N  
ANISOU  488  N   PRO A  35     1952   2904   2434    361   -136    529       N  
ATOM    489  CA  PRO A  35      25.234  24.274  -3.002  1.00 19.35           C  
ANISOU  489  CA  PRO A  35     1943   2962   2447    344   -128    505       C  
ATOM    490  C   PRO A  35      25.634  23.706  -4.354  1.00 17.50           C  
ANISOU  490  C   PRO A  35     1701   2705   2242    386   -106    491       C  
ATOM    491  O   PRO A  35      25.961  22.526  -4.493  1.00 21.66           O  
ANISOU  491  O   PRO A  35     2221   3214   2795    440   -104    511       O  
ATOM    492  CB  PRO A  35      26.463  24.504  -2.110  1.00 18.90           C  
ANISOU  492  CB  PRO A  35     1835   2979   2368    340   -152    535       C  
ATOM    493  CG  PRO A  35      26.332  23.550  -0.939  1.00 25.38           C  
ANISOU  493  CG  PRO A  35     2658   3797   3186    362   -171    577       C  
ATOM    494  CD  PRO A  35      25.243  22.567  -1.269  1.00 18.66           C  
ANISOU  494  CD  PRO A  35     1854   2871   2364    389   -158    576       C  
ATOM    495  HA  PRO A  35      24.767  25.116  -3.117  1.00 23.22           H  
ATOM    496  HB2 PRO A  35      27.270  24.315  -2.615  1.00 22.68           H  
ATOM    497  HB3 PRO A  35      26.472  25.424  -1.802  1.00 22.68           H  
ATOM    498  HG2 PRO A  35      27.174  23.087  -0.808  1.00 30.45           H  
ATOM    499  HG3 PRO A  35      26.101  24.052  -0.142  1.00 30.45           H  
ATOM    500  HD2 PRO A  35      25.609  21.762  -1.667  1.00 22.39           H  
ATOM    501  HD3 PRO A  35      24.726  22.342  -0.480  1.00 22.39           H  
ATOM    502  N   TYR A  36      25.581  24.572  -5.361  1.00 18.44           N  
ANISOU  502  N   TYR A  36     1825   2824   2359    361    -90    456       N  
ATOM    503  CA  TYR A  36      25.994  24.248  -6.718  1.00 18.37           C  
ANISOU  503  CA  TYR A  36     1806   2805   2370    391    -67    438       C  
ATOM    504  C   TYR A  36      26.823  25.411  -7.237  1.00 16.82           C  
ANISOU  504  C   TYR A  36     1576   2663   2152    355    -64    423       C  
ATOM    505  O   TYR A  36      26.598  26.562  -6.855  1.00 19.49           O  
ANISOU  505  O   TYR A  36     1922   3016   2465    300    -75    414       O  
ATOM    506  CB  TYR A  36      24.803  24.029  -7.685  1.00 20.93           C  
ANISOU  506  CB  TYR A  36     2181   3060   2713    393    -46    407       C  
ATOM    507  CG  TYR A  36      24.021  22.761  -7.435  1.00 18.51           C  
ANISOU  507  CG  TYR A  36     1907   2694   2430    428    -45    419       C  
ATOM    508  CD1 TYR A  36      24.339  21.579  -8.089  1.00 22.81           C  
ANISOU  508  CD1 TYR A  36     2451   3211   3004    484    -32    421       C  
ATOM    509  CD2 TYR A  36      22.969  22.745  -6.535  1.00 17.62           C  
ANISOU  509  CD2 TYR A  36     1827   2556   2310    405    -56    428       C  
ATOM    510  CE1 TYR A  36      23.636  20.418  -7.841  1.00 21.84           C  
ANISOU  510  CE1 TYR A  36     2364   3031   2904    512    -34    433       C  
ATOM    511  CE2 TYR A  36      22.267  21.595  -6.286  1.00 20.10           C  
ANISOU  511  CE2 TYR A  36     2173   2820   2645    430    -57    443       C  
ATOM    512  CZ  TYR A  36      22.600  20.440  -6.940  1.00 19.34           C  
ANISOU  512  CZ  TYR A  36     2079   2691   2578    482    -47    446       C  
ATOM    513  OH  TYR A  36      21.894  19.298  -6.677  1.00 23.53           O  
ANISOU  513  OH  TYR A  36     2646   3165   3128    503    -50    462       O  
ATOM    514  H   TYR A  36      25.300  25.380  -5.278  1.00 22.13           H  
ATOM    515  HA  TYR A  36      26.514  23.429  -6.702  1.00 22.05           H  
ATOM    516  HB2 TYR A  36      24.190  24.775  -7.594  1.00 25.12           H  
ATOM    517  HB3 TYR A  36      25.144  23.990  -8.592  1.00 25.12           H  
ATOM    518  HD1 TYR A  36      25.037  21.569  -8.703  1.00 27.37           H  
ATOM    519  HD2 TYR A  36      22.736  23.528  -6.092  1.00 21.14           H  
ATOM    520  HE1 TYR A  36      23.861  19.629  -8.279  1.00 26.21           H  
ATOM    521  HE2 TYR A  36      21.567  21.600  -5.674  1.00 24.12           H  
ATOM    522  HH  TYR A  36      21.707  19.258  -5.859  1.00 28.23           H  
ATOM    523  N   THR A  37      27.764  25.114  -8.123  1.00 17.39           N  
ANISOU  523  N   THR A  37     1612   2763   2233    385    -49    419       N  
ATOM    524  CA  THR A  37      28.476  26.140  -8.877  1.00 18.96           C  
ANISOU  524  CA  THR A  37     1782   3008   2412    349    -42    403       C  
ATOM    525  C   THR A  37      28.266  25.855 -10.356  1.00 16.98           C  
ANISOU  525  C   THR A  37     1546   2729   2178    369    -12    374       C  
ATOM    526  O   THR A  37      28.453  24.715 -10.798  1.00 22.01           O  
ANISOU  526  O   THR A  37     2176   3349   2839    429      2    374       O  
ATOM    527  CB  THR A  37      29.967  26.177  -8.533  1.00 20.88           C  
ANISOU  527  CB  THR A  37     1957   3335   2642    357    -52    427       C  
ATOM    528  OG1 THR A  37      30.130  26.649  -7.189  1.00 23.10           O  
ANISOU  528  OG1 THR A  37     2228   3648   2902    325    -81    451       O  
ATOM    529  CG2 THR A  37      30.736  27.107  -9.489  1.00 26.87           C  
ANISOU  529  CG2 THR A  37     2684   4144   3382    321    -40    411       C  
ATOM    530  H   THR A  37      28.011  24.312  -8.308  1.00 20.87           H  
ATOM    531  HA  THR A  37      28.121  27.018  -8.666  1.00 22.75           H  
ATOM    532  HB  THR A  37      30.337  25.284  -8.620  1.00 25.06           H  
ATOM    533  HG1 THR A  37      29.711  27.369  -7.084  1.00 27.73           H  
ATOM    534 HG21 THR A  37      31.656  27.199  -9.194  1.00 32.24           H  
ATOM    535 HG22 THR A  37      30.729  26.739 -10.387  1.00 32.24           H  
ATOM    536 HG23 THR A  37      30.322  27.983  -9.505  1.00 32.24           H  
ATOM    537  N   LEU A  38      27.841  26.881 -11.100  1.00 18.03           N  
ANISOU  537  N   LEU A  38     1700   2852   2297    321     -4    350       N  
ATOM    538  CA  LEU A  38      27.652  26.821 -12.546  1.00 16.53           C  
ANISOU  538  CA  LEU A  38     1523   2643   2115    329     22    322       C  
ATOM    539  C   LEU A  38      28.594  27.816 -13.209  1.00 17.52           C  
ANISOU  539  C   LEU A  38     1612   2831   2215    288     27    318       C  
ATOM    540  O   LEU A  38      28.679  28.968 -12.773  1.00 20.34           O  
ANISOU  540  O   LEU A  38     1971   3210   2549    230     10    322       O  
ATOM    541  CB  LEU A  38      26.217  27.158 -12.936  1.00 17.27           C  
ANISOU  541  CB  LEU A  38     1679   2669   2213    304     26    299       C  
ATOM    542  CG  LEU A  38      25.139  26.308 -12.275  1.00 16.59           C  
ANISOU  542  CG  LEU A  38     1633   2524   2148    331     20    303       C  
ATOM    543  CD1 LEU A  38      23.783  26.796 -12.732  1.00 21.57           C  
ANISOU  543  CD1 LEU A  38     2316   3100   2778    302     24    279       C  
ATOM    544  CD2 LEU A  38      25.320  24.839 -12.591  1.00 21.54           C  
ANISOU  544  CD2 LEU A  38     2254   3128   2801    396     34    306       C  
ATOM    545  H   LEU A  38      27.650  27.652 -10.771  1.00 21.63           H  
ATOM    546  HA  LEU A  38      27.857  25.925 -12.856  1.00 19.84           H  
ATOM    547  HB2 LEU A  38      26.045  28.082 -12.694  1.00 20.72           H  
ATOM    548  HB3 LEU A  38      26.127  27.044 -13.895  1.00 20.72           H  
ATOM    549  HG  LEU A  38      25.202  26.393 -11.311  1.00 19.91           H  
ATOM    550 HD11 LEU A  38      23.101  26.421 -12.154  1.00 25.88           H  
ATOM    551 HD12 LEU A  38      23.763  27.765 -12.682  1.00 25.88           H  
ATOM    552 HD13 LEU A  38      23.636  26.509 -13.647  1.00 25.88           H  
ATOM    553 HD21 LEU A  38      24.532  24.354 -12.302  1.00 25.84           H  
ATOM    554 HD22 LEU A  38      25.440  24.735 -13.548  1.00 25.84           H  
ATOM    555 HD23 LEU A  38      26.102  24.510 -12.122  1.00 25.84           H  
ATOM    556  N   THR A  39      29.289  27.383 -14.260  1.00 17.77           N  
ANISOU  556  N   THR A  39     1612   2890   2248    317     51    308       N  
ATOM    557  CA ATHR A  39      30.263  28.214 -14.960  0.72 25.04           C  
ANISOU  557  CA ATHR A  39     2492   3880   3144    280     59    306       C  
ATOM    558  CA BTHR A  39      30.253  28.227 -14.957  0.28 11.07           C  
ANISOU  558  CA BTHR A  39      723   2109   1374    279     59    306       C  
ATOM    559  C   THR A  39      29.857  28.317 -16.423  1.00 19.17           C  
ANISOU  559  C   THR A  39     1772   3114   2398    274     85    277       C  
ATOM    560  O   THR A  39      29.668  27.293 -17.088  1.00 21.73           O  
ANISOU  560  O   THR A  39     2102   3413   2741    328    107    261       O  
ATOM    561  CB ATHR A  39      31.672  27.633 -14.817  0.72 22.68           C  
ANISOU  561  CB ATHR A  39     2119   3656   2841    319     64    323       C  
ATOM    562  CB BTHR A  39      31.680  27.695 -14.797  0.28 24.29           C  
ANISOU  562  CB BTHR A  39     2323   3862   3044    316     63    323       C  
ATOM    563  OG1ATHR A  39      31.980  27.462 -13.426  0.72 25.63           O  
ANISOU  563  OG1ATHR A  39     2474   4048   3217    327     37    352       O  
ATOM    564  OG1BTHR A  39      31.744  26.326 -15.211  0.28 27.49           O  
ANISOU  564  OG1BTHR A  39     2722   4248   3476    395     83    314       O  
ATOM    565  CG2ATHR A  39      32.693  28.555 -15.449  0.72 25.14           C  
ANISOU  565  CG2ATHR A  39     2384   4048   3122    272     71    324       C  
ATOM    566  CG2BTHR A  39      32.122  27.806 -13.341  0.28 35.86           C  
ANISOU  566  CG2BTHR A  39     3763   5357   4503    308     33    354       C  
ATOM    567  H  ATHR A  39      29.209  26.593 -14.591  0.72 21.32           H  
ATOM    568  H  BTHR A  39      29.216  26.592 -14.590  0.28 21.32           H  
ATOM    569  HA ATHR A  39      30.264  29.109 -14.585  0.72 30.05           H  
ATOM    570  HA BTHR A  39      30.228  29.123 -14.584  0.28 13.28           H  
ATOM    571  HB ATHR A  39      31.718  26.775 -15.268  0.72 27.21           H  
ATOM    572  HB BTHR A  39      32.282  28.219 -15.348  0.28 29.15           H  
ATOM    573  HG1ATHR A  39      32.179  28.202 -13.083  0.72 30.76           H  
ATOM    574  HG1BTHR A  39      31.689  26.276 -16.048  0.28 32.99           H  
ATOM    575 HG21ATHR A  39      33.588  28.217 -15.291  0.72 30.17           H  
ATOM    576 HG21BTHR A  39      32.599  27.003 -13.078  0.28 43.03           H  
ATOM    577 HG22ATHR A  39      32.541  28.613 -16.405  0.72 30.17           H  
ATOM    578 HG22BTHR A  39      32.708  28.571 -13.230  0.28 43.03           H  
ATOM    579 HG23ATHR A  39      32.620  29.443 -15.064  0.72 30.17           H  
ATOM    580 HG23BTHR A  39      31.349  27.916 -12.767  0.28 43.03           H  
ATOM    581  N   LEU A  40      29.699  29.547 -16.910  1.00 20.54           N  
ANISOU  581  N   LEU A  40     1962   3295   2548    209     81    272       N  
ATOM    582  CA ALEU A  40      29.367  29.788 -18.304  0.49 21.76           C  
ANISOU  582  CA ALEU A  40     2137   3437   2695    194    103    249       C  
ATOM    583  CA BLEU A  40      29.365  29.793 -18.305  0.51 21.66           C  
ANISOU  583  CA BLEU A  40     2124   3424   2682    194    103    249       C  
ATOM    584  C   LEU A  40      30.631  30.064 -19.101  1.00 19.97           C  
ANISOU  584  C   LEU A  40     1852   3293   2443    180    120    252       C  
ATOM    585  O   LEU A  40      31.493  30.834 -18.668  1.00 22.12           O  
ANISOU  585  O   LEU A  40     2087   3624   2693    137    106    272       O  
ATOM    586  CB ALEU A  40      28.431  30.979 -18.469  0.49 13.61           C  
ANISOU  586  CB ALEU A  40     1158   2362   1651    132     88    243       C  
ATOM    587  CB BLEU A  40      28.428  30.992 -18.448  0.51 19.70           C  
ANISOU  587  CB BLEU A  40     1930   3133   2422    131     88    244       C  
ATOM    588  CG ALEU A  40      27.147  30.986 -17.654  0.49 17.29           C  
ANISOU  588  CG ALEU A  40     1680   2755   2136    134     70    240       C  
ATOM    589  CG BLEU A  40      26.984  30.857 -17.981  0.51 25.15           C  
ANISOU  589  CG BLEU A  40     2681   3742   3133    140     76    234       C  
ATOM    590  CD1ALEU A  40      26.326  32.219 -18.027  0.49 15.73           C  
ANISOU  590  CD1ALEU A  40     1530   2522   1925     78     58    232       C  
ATOM    591  CD1BLEU A  40      26.908  30.706 -16.474  0.51 27.40           C  
ANISOU  591  CD1BLEU A  40     2964   4019   3427    149     53    251       C  
ATOM    592  CD2ALEU A  40      26.361  29.717 -17.876  0.49 21.23           C  
ANISOU  592  CD2ALEU A  40     2202   3203   2662    194     85    225       C  
ATOM    593  CD2BLEU A  40      26.190  32.072 -18.455  0.51 32.56           C  
ANISOU  593  CD2BLEU A  40     3666   4646   4057     84     66    226       C  
ATOM    594  H  ALEU A  40      29.780  30.263 -16.441  0.49 24.65           H  
ATOM    595  H  BLEU A  40      29.781  30.264 -16.441  0.51 24.65           H  
ATOM    596  HA ALEU A  40      28.927  28.996 -18.649  0.49 26.11           H  
ATOM    597  HA BLEU A  40      28.919  29.009 -18.661  0.51 26.00           H  
ATOM    598  HB2ALEU A  40      28.923  31.778 -18.224  0.49 16.33           H  
ATOM    599  HB2BLEU A  40      28.814  31.724 -17.941  0.51 23.64           H  
ATOM    600  HB3ALEU A  40      28.170  31.023 -19.402  0.49 16.33           H  
ATOM    601  HB3BLEU A  40      28.393  31.223 -19.389  0.51 23.64           H  
ATOM    602  HG ALEU A  40      27.355  31.025 -16.707  0.49 20.75           H  
ATOM    603  HG BLEU A  40      26.590  30.057 -18.362  0.51 30.18           H  
ATOM    604 HD11ALEU A  40      25.588  32.308 -17.404  0.49 18.88           H  
ATOM    605 HD11BLEU A  40      26.019  30.956 -16.176  0.51 32.88           H  
ATOM    606 HD12ALEU A  40      26.895  33.003 -17.979  0.49 18.88           H  
ATOM    607 HD12BLEU A  40      27.087  29.782 -16.240  0.51 32.88           H  
ATOM    608 HD13ALEU A  40      25.987  32.111 -18.929  0.49 18.88           H  
ATOM    609 HD13BLEU A  40      27.569  31.285 -16.064  0.51 32.88           H  
ATOM    610 HD21ALEU A  40      25.555  29.928 -18.372  0.49 25.48           H  
ATOM    611 HD21BLEU A  40      25.248  31.922 -18.279  0.51 39.07           H  
ATOM    612 HD22ALEU A  40      26.906  29.092 -18.379  0.49 25.48           H  
ATOM    613 HD22BLEU A  40      26.495  32.857 -17.973  0.51 39.07           H  
ATOM    614 HD23ALEU A  40      26.129  29.335 -17.015  0.49 25.48           H  
ATOM    615 HD23BLEU A  40      26.334  32.192 -19.407  0.51 39.07           H  
ATOM    616  N   THR A  41      30.715  29.453 -20.278  1.00 17.28           N  
ANISOU  616  N   THR A  41     1504   2959   2102    212    150    230       N  
ATOM    617  CA  THR A  41      31.808  29.676 -21.206  1.00 18.71           C  
ANISOU  617  CA  THR A  41     1632   3221   2257    198    171    229       C  
ATOM    618  C   THR A  41      31.250  29.888 -22.604  1.00 19.91           C  
ANISOU  618  C   THR A  41     1817   3353   2396    180    192    205       C  
ATOM    619  O   THR A  41      30.127  29.492 -22.934  1.00 21.52           O  
ANISOU  619  O   THR A  41     2075   3484   2617    199    196    186       O  
ATOM    620  CB  THR A  41      32.801  28.507 -21.213  1.00 23.49           C  
ANISOU  620  CB  THR A  41     2176   3878   2872    272    191    226       C  
ATOM    621  OG1 THR A  41      32.111  27.294 -21.535  1.00 24.43           O  
ANISOU  621  OG1 THR A  41     2328   3934   3021    341    207    201       O  
ATOM    622  CG2 THR A  41      33.473  28.402 -19.852  1.00 25.17           C  
ANISOU  622  CG2 THR A  41     2350   4122   3092    284    168    255       C  
ATOM    623  H   THR A  41      30.132  28.890 -20.566  1.00 20.73           H  
ATOM    624  HA  THR A  41      32.288  30.477 -20.942  1.00 22.46           H  
ATOM    625  HB  THR A  41      33.492  28.647 -21.879  1.00 28.19           H  
ATOM    626  HG1 THR A  41      31.581  27.426 -22.174  1.00 29.32           H  
ATOM    627 HG21 THR A  41      33.944  27.557 -19.779  1.00 30.20           H  
ATOM    628 HG22 THR A  41      34.107  29.127 -19.739  1.00 30.20           H  
ATOM    629 HG23 THR A  41      32.807  28.453 -19.149  1.00 30.20           H  
ATOM    630  N   GLU A  42      32.080  30.524 -23.413  1.00 22.89           N  
ANISOU  630  N   GLU A  42     2156   3802   2739    139    206    208       N  
ATOM    631  CA  GLU A  42      31.793  30.873 -24.793  1.00 24.10           C  
ANISOU  631  CA  GLU A  42     2329   3957   2869    111    225    192       C  
ATOM    632  C   GLU A  42      32.704  30.023 -25.660  1.00 21.09           C  
ANISOU  632  C   GLU A  42     1893   3645   2478    158    262    173       C  
ATOM    633  O   GLU A  42      33.910  29.973 -25.410  1.00 23.88           O  
ANISOU  633  O   GLU A  42     2177   4079   2817    165    269    186       O  
ATOM    634  CB  GLU A  42      32.062  32.360 -24.990  1.00 27.13           C  
ANISOU  634  CB  GLU A  42     2716   4374   3220     18    209    214       C  
ATOM    635  CG  GLU A  42      31.520  32.958 -26.237  1.00 30.64           C  
ANISOU  635  CG  GLU A  42     3198   4803   3642    -25    218    205       C  
ATOM    636  CD  GLU A  42      31.414  34.465 -26.124  1.00 29.54           C  
ANISOU  636  CD  GLU A  42     3086   4657   3479   -114    190    231       C  
ATOM    637  OE1 GLU A  42      31.250  34.969 -24.990  1.00 22.18           O  
ANISOU  637  OE1 GLU A  42     2170   3696   2561   -134    159    247       O  
ATOM    638  OE2 GLU A  42      31.496  35.143 -27.169  1.00 28.41           O  
ANISOU  638  OE2 GLU A  42     2951   4538   3306   -165    197    235       O  
ATOM    639  H   GLU A  42      32.864  30.778 -23.168  1.00 27.47           H  
ATOM    640  HA  GLU A  42      30.873  30.698 -25.046  1.00 28.92           H  
ATOM    641  HB2 GLU A  42      31.668  32.841 -24.246  1.00 32.56           H  
ATOM    642  HB3 GLU A  42      33.023  32.495 -25.001  1.00 32.56           H  
ATOM    643  HG2 GLU A  42      32.110  32.747 -26.977  1.00 36.77           H  
ATOM    644  HG3 GLU A  42      30.635  32.600 -26.406  1.00 36.77           H  
ATOM    645  N   VAL A  43      32.148  29.325 -26.648  1.00 21.45           N  
ANISOU  645  N   VAL A  43     1964   3659   2527    194    287    142       N  
ATOM    646  CA  VAL A  43      32.965  28.465 -27.498  1.00 25.58           C  
ANISOU  646  CA  VAL A  43     2438   4244   3038    246    324    117       C  
ATOM    647  C   VAL A  43      32.661  28.748 -28.962  1.00 30.23           C  
ANISOU  647  C   VAL A  43     3046   4844   3596    215    348     96       C  
ATOM    648  O   VAL A  43      31.495  28.740 -29.370  1.00 22.96           O  
ANISOU  648  O   VAL A  43     2190   3850   2683    207    343     81       O  
ATOM    649  CB  VAL A  43      32.752  26.968 -27.198  1.00 24.07           C  
ANISOU  649  CB  VAL A  43     2252   4006   2886    342    336     93       C  
ATOM    650  CG1 VAL A  43      33.630  26.115 -28.127  1.00 31.59           C  
ANISOU  650  CG1 VAL A  43     3170   5006   3828    392    369     62       C  
ATOM    651  CG2 VAL A  43      33.043  26.670 -25.740  1.00 25.51           C  
ANISOU  651  CG2 VAL A  43     2416   4178   3097    371    311    118       C  
ATOM    652  H   VAL A  43      31.309  29.334 -26.840  1.00 25.74           H  
ATOM    653  HA  VAL A  43      33.895  28.690 -27.337  1.00 30.70           H  
ATOM    654  HB  VAL A  43      31.825  26.736 -27.364  1.00 28.88           H  
ATOM    655 HG11 VAL A  43      33.224  26.087 -29.008  1.00 37.91           H  
ATOM    656 HG12 VAL A  43      34.513  26.514 -28.182  1.00 37.91           H  
ATOM    657 HG13 VAL A  43      33.695  25.218 -27.764  1.00 37.91           H  
ATOM    658 HG21 VAL A  43      33.748  26.006 -25.689  1.00 30.61           H  
ATOM    659 HG22 VAL A  43      33.325  27.487 -25.301  1.00 30.61           H  
ATOM    660 HG23 VAL A  43      32.237  26.330 -25.321  1.00 30.61           H  
ATOM    661  N   ASP A  44      33.709  28.966 -29.753  1.00 26.68           N  
ANISOU  661  N   ASP A  44     2539   4490   3108    199    373     94       N  
ATOM    662  CA  ASP A  44      33.570  29.184 -31.186  1.00 29.47           C  
ANISOU  662  CA  ASP A  44     2904   4866   3426    170    397     74       C  
ATOM    663  C   ASP A  44      33.832  27.882 -31.936  1.00 24.24           C  
ANISOU  663  C   ASP A  44     2239   4201   2772    246    426     29       C  
ATOM    664  O   ASP A  44      34.603  27.029 -31.488  1.00 29.42           O  
ANISOU  664  O   ASP A  44     2865   4864   3449    306    428     20       O  
ATOM    665  CB  ASP A  44      34.524  30.280 -31.669  1.00 31.08           C  
ANISOU  665  CB  ASP A  44     3078   5147   3585     92    392     98       C  
ATOM    666  CG  ASP A  44      34.295  31.613 -30.964  1.00 42.41           C  
ANISOU  666  CG  ASP A  44     4524   6578   5011     10    360    141       C  
ATOM    667  OD1 ASP A  44      33.138  31.936 -30.624  1.00 34.20           O  
ANISOU  667  OD1 ASP A  44     3549   5452   3992     -6    336    146       O  
ATOM    668  OD2 ASP A  44      35.283  32.346 -30.752  1.00 38.17           O  
ANISOU  668  OD2 ASP A  44     3954   6096   4452    -39    346    167       O  
ATOM    669  H   ASP A  44      34.522  28.991 -29.474  1.00 32.02           H  
ATOM    670  HA  ASP A  44      32.667  29.474 -31.387  1.00 35.36           H  
ATOM    671  HB2 ASP A  44      35.438  30.002 -31.497  1.00 37.30           H  
ATOM    672  HB3 ASP A  44      34.393  30.416 -32.620  1.00 37.30           H  
ATOM    673  N   ASN A  45      33.142  27.723 -33.068  1.00 24.31           N  
ANISOU  673  N   ASN A  45     2281   4194   2763    243    447      1       N  
ATOM    674  CA  ASN A  45      33.336  26.590 -33.978  1.00 23.85           C  
ANISOU  674  CA  ASN A  45     2225   4133   2705    304    476    -46       C  
ATOM    675  C   ASN A  45      33.191  25.265 -33.242  1.00 27.92           C  
ANISOU  675  C   ASN A  45     2751   4586   3271    393    476    -67       C  
ATOM    676  O   ASN A  45      34.057  24.390 -33.282  1.00 33.69           O  
ANISOU  676  O   ASN A  45     3455   5332   4013    449    487    -86       O  
ATOM    677  CB  ASN A  45      34.681  26.705 -34.676  1.00 25.06           C  
ANISOU  677  CB  ASN A  45     2327   4370   2825    292    492    -49       C  
ATOM    678  CG  ASN A  45      34.832  28.024 -35.381  1.00 35.36           C  
ANISOU  678  CG  ASN A  45     3626   5731   4079    198    488    -24       C  
ATOM    679  OD1 ASN A  45      33.958  28.421 -36.148  1.00 34.87           O  
ANISOU  679  OD1 ASN A  45     3603   5651   3997    160    493    -29       O  
ATOM    680  ND2 ASN A  45      35.903  28.746 -35.075  1.00 44.76           N  
ANISOU  680  ND2 ASN A  45     4770   6985   5250    156    476      7       N  
ATOM    681  H   ASN A  45      32.540  28.274 -33.339  1.00 29.18           H  
ATOM    682  HA  ASN A  45      32.643  26.607 -34.656  1.00 28.62           H  
ATOM    683  HB2 ASN A  45      35.390  26.628 -34.019  1.00 30.07           H  
ATOM    684  HB3 ASN A  45      34.761  25.997 -35.334  1.00 30.07           H  
ATOM    685 HD21 ASN A  45      36.031  29.508 -35.454  1.00 53.71           H  
ATOM    686 HD22 ASN A  45      36.469  28.453 -34.498  1.00 53.71           H  
ATOM    687  N   TRP A  46      32.053  25.125 -32.585  1.00 29.03           N  
ANISOU  687  N   TRP A  46     2934   4655   3441    406    461    -63       N  
ATOM    688  CA  TRP A  46      31.745  23.978 -31.749  1.00 25.80           C  
ANISOU  688  CA  TRP A  46     2545   4175   3082    480    453    -74       C  
ATOM    689  C   TRP A  46      30.971  22.955 -32.554  1.00 28.75           C  
ANISOU  689  C   TRP A  46     2968   4491   3466    525    472   -122       C  
ATOM    690  O   TRP A  46      29.972  23.291 -33.195  1.00 24.34           O  
ANISOU  690  O   TRP A  46     2455   3900   2893    488    472   -132       O  
ATOM    691  CB  TRP A  46      30.929  24.465 -30.567  1.00 28.03           C  
ANISOU  691  CB  TRP A  46     2861   4398   3391    454    416    -39       C  
ATOM    692  CG  TRP A  46      30.439  23.496 -29.567  1.00 30.76           C  
ANISOU  692  CG  TRP A  46     3237   4666   3786    512    400    -40       C  
ATOM    693  CD1 TRP A  46      31.146  22.950 -28.540  1.00 23.41           C  
ANISOU  693  CD1 TRP A  46     2269   3747   2881    562    392    -24       C  
ATOM    694  CD2 TRP A  46      29.092  23.019 -29.427  1.00 26.06           C  
ANISOU  694  CD2 TRP A  46     2714   3970   3219    518    386    -52       C  
ATOM    695  NE1 TRP A  46      30.324  22.162 -27.765  1.00 25.54           N  
ANISOU  695  NE1 TRP A  46     2586   3925   3192    599    374    -23       N  
ATOM    696  CE2 TRP A  46      29.062  22.178 -28.297  1.00 29.88           C  
ANISOU  696  CE2 TRP A  46     3203   4407   3744    572    371    -41       C  
ATOM    697  CE3 TRP A  46      27.913  23.216 -30.152  1.00 24.70           C  
ANISOU  697  CE3 TRP A  46     2601   3746   3039    483    384    -68       C  
ATOM    698  CZ2 TRP A  46      27.897  21.529 -27.878  1.00 22.88           C  
ANISOU  698  CZ2 TRP A  46     2379   3425   2890    587    355    -47       C  
ATOM    699  CZ3 TRP A  46      26.757  22.575 -29.731  1.00 24.93           C  
ANISOU  699  CZ3 TRP A  46     2689   3683   3101    500    368    -76       C  
ATOM    700  CH2 TRP A  46      26.759  21.738 -28.610  1.00 27.17           C  
ANISOU  700  CH2 TRP A  46     2977   3923   3425    550    355    -65       C  
ATOM    701  H   TRP A  46      31.418  25.704 -32.608  1.00 34.84           H  
ATOM    702  HA  TRP A  46      32.552  23.543 -31.431  1.00 30.96           H  
ATOM    703  HB2 TRP A  46      31.476  25.101 -30.081  1.00 33.64           H  
ATOM    704  HB3 TRP A  46      30.142  24.907 -30.923  1.00 33.64           H  
ATOM    705  HD1 TRP A  46      32.053  23.090 -28.384  1.00 28.10           H  
ATOM    706  HE1 TRP A  46      30.564  21.730 -27.061  1.00 30.64           H  
ATOM    707  HE3 TRP A  46      27.903  23.767 -30.901  1.00 29.64           H  
ATOM    708  HZ2 TRP A  46      27.894  20.976 -27.131  1.00 27.46           H  
ATOM    709  HZ3 TRP A  46      25.967  22.703 -30.203  1.00 29.92           H  
ATOM    710  HH2 TRP A  46      25.970  21.316 -28.357  1.00 32.61           H  
ATOM    711  N   THR A  47      31.439  21.713 -32.525  1.00 31.46           N  
ANISOU  711  N   THR A  47     3310   4807   3836    595    481   -148       N  
ATOM    712  CA  THR A  47      30.746  20.627 -33.204  1.00 32.56           C  
ANISOU  712  CA  THR A  47     3499   4881   3990    639    497   -195       C  
ATOM    713  C   THR A  47      29.568  20.182 -32.344  1.00 25.20           C  
ANISOU  713  C   THR A  47     2621   3857   3098    660    475   -188       C  
ATOM    714  O   THR A  47      29.753  19.639 -31.249  1.00 28.19           O  
ANISOU  714  O   THR A  47     2998   4198   3515    698    456   -170       O  
ATOM    715  CB  THR A  47      31.693  19.467 -33.482  1.00 34.76           C  
ANISOU  715  CB  THR A  47     3760   5162   4285    703    514   -225       C  
ATOM    716  OG1 THR A  47      32.733  19.898 -34.367  1.00 34.35           O  
ANISOU  716  OG1 THR A  47     3660   5200   4192    682    536   -233       O  
ATOM    717  CG2 THR A  47      30.927  18.320 -34.119  1.00 31.67           C  
ANISOU  717  CG2 THR A  47     3427   4695   3912    745    527   -274       C  
ATOM    718  H   THR A  47      32.158  21.474 -32.118  1.00 37.75           H  
ATOM    719  HA  THR A  47      30.407  20.948 -34.054  1.00 39.07           H  
ATOM    720  HB  THR A  47      32.090  19.156 -32.654  1.00 41.71           H  
ATOM    721  HG1 THR A  47      32.400  20.211 -35.071  1.00 41.22           H  
ATOM    722 HG21 THR A  47      30.507  17.779 -33.432  1.00 38.01           H  
ATOM    723 HG22 THR A  47      30.240  18.668 -34.710  1.00 38.01           H  
ATOM    724 HG23 THR A  47      31.532  17.763 -34.634  1.00 38.01           H  
ATOM    725  N   GLY A  48      28.358  20.400 -32.847  1.00 25.10           N  
ANISOU  725  N   GLY A  48     2662   3799   3077    626    472   -201       N  
ATOM    726  CA  GLY A  48      27.159  20.098 -32.110  1.00 27.21           C  
ANISOU  726  CA  GLY A  48     2991   3968   3381    621    443   -190       C  
ATOM    727  C   GLY A  48      26.733  18.655 -32.260  1.00 21.52           C  
ANISOU  727  C   GLY A  48     2312   3175   2690    686    452   -229       C  
ATOM    728  O   GLY A  48      27.360  17.861 -32.973  1.00 23.72           O  
ANISOU  728  O   GLY A  48     2576   3473   2963    736    480   -268       O  
ATOM    729  H   GLY A  48      28.212  20.729 -33.629  1.00 30.12           H  
ATOM    730  HA2 GLY A  48      27.309  20.276 -31.169  1.00 32.66           H  
ATOM    731  HA3 GLY A  48      26.437  20.664 -32.428  1.00 32.66           H  
ATOM    732  N   PRO A  49      25.629  18.296 -31.596  1.00 23.07           N  
ANISOU  732  N   PRO A  49     2564   3283   2918    679    426   -218       N  
ATOM    733  CA  PRO A  49      25.249  16.874 -31.510  1.00 23.93           C  
ANISOU  733  CA  PRO A  49     2715   3315   3062    739    429   -248       C  
ATOM    734  C   PRO A  49      24.744  16.263 -32.806  1.00 32.74           C  
ANISOU  734  C   PRO A  49     3871   4406   4161    745    451   -302       C  
ATOM    735  O   PRO A  49      24.689  15.030 -32.895  1.00 28.20           O  
ANISOU  735  O   PRO A  49     3327   3777   3612    802    459   -335       O  
ATOM    736  CB  PRO A  49      24.152  16.855 -30.431  1.00 29.19           C  
ANISOU  736  CB  PRO A  49     3427   3904   3760    713    393   -215       C  
ATOM    737  CG  PRO A  49      23.745  18.259 -30.215  1.00 32.87           C  
ANISOU  737  CG  PRO A  49     3884   4401   4204    639    375   -180       C  
ATOM    738  CD  PRO A  49      24.837  19.160 -30.701  1.00 22.92           C  
ANISOU  738  CD  PRO A  49     2564   3236   2908    622    392   -175       C  
ATOM    739  HA  PRO A  49      26.018  16.366 -31.205  1.00 28.72           H  
ATOM    740  HB2 PRO A  49      23.401  16.326 -30.743  1.00 35.03           H  
ATOM    741  HB3 PRO A  49      24.509  16.474 -29.613  1.00 35.03           H  
ATOM    742  HG2 PRO A  49      22.929  18.429 -30.711  1.00 39.44           H  
ATOM    743  HG3 PRO A  49      23.594  18.401 -29.268  1.00 39.44           H  
ATOM    744  HD2 PRO A  49      24.469  19.914 -31.188  1.00 27.50           H  
ATOM    745  HD3 PRO A  49      25.377  19.476 -29.960  1.00 27.50           H  
ATOM    746  N   ASP A  50      24.341  17.057 -33.799  1.00 23.62           N  
ANISOU  746  N   ASP A  50     2722   3286   2966    687    459   -314       N  
ATOM    747  CA  ASP A  50      23.952  16.494 -35.087  1.00 21.64           C  
ANISOU  747  CA  ASP A  50     2504   3023   2693    692    481   -367       C  
ATOM    748  C   ASP A  50      25.043  16.669 -36.144  1.00 21.65           C  
ANISOU  748  C   ASP A  50     2457   3117   2653    707    519   -397       C  
ATOM    749  O   ASP A  50      24.775  16.507 -37.340  1.00 25.35           O  
ANISOU  749  O   ASP A  50     2945   3597   3090    696    539   -439       O  
ATOM    750  CB  ASP A  50      22.607  17.075 -35.557  1.00 24.35           C  
ANISOU  750  CB  ASP A  50     2896   3336   3020    620    464   -364       C  
ATOM    751  CG  ASP A  50      22.668  18.546 -35.976  1.00 22.36           C  
ANISOU  751  CG  ASP A  50     2616   3154   2726    551    460   -336       C  
ATOM    752  OD1 ASP A  50      23.749  19.173 -35.975  1.00 24.98           O  
ANISOU  752  OD1 ASP A  50     2891   3562   3038    550    473   -320       O  
ATOM    753  OD2 ASP A  50      21.584  19.075 -36.318  1.00 23.64           O  
ANISOU  753  OD2 ASP A  50     2814   3292   2875    496    443   -329       O  
ATOM    754  H   ASP A  50      24.287  17.914 -33.747  1.00 28.34           H  
ATOM    755  HA  ASP A  50      23.811  15.541 -34.977  1.00 25.96           H  
ATOM    756  HB2 ASP A  50      22.299  16.564 -36.322  1.00 29.22           H  
ATOM    757  HB3 ASP A  50      21.968  17.003 -34.831  1.00 29.22           H  
ATOM    758  N   GLY A  51      26.272  16.980 -35.722  1.00 26.38           N  
ANISOU  758  N   GLY A  51     2992   3781   3251    727    526   -375       N  
ATOM    759  CA  GLY A  51      27.412  17.048 -36.610  1.00 24.36           C  
ANISOU  759  CA  GLY A  51     2690   3601   2964    729    553   -393       C  
ATOM    760  C   GLY A  51      27.705  18.414 -37.191  1.00 29.39           C  
ANISOU  760  C   GLY A  51     3287   4331   3548    665    562   -373       C  
ATOM    761  O   GLY A  51      28.823  18.643 -37.670  1.00 27.07           O  
ANISOU  761  O   GLY A  51     2944   4111   3230    662    580   -373       O  
ATOM    762  H   GLY A  51      26.464  17.158 -34.903  1.00 31.66           H  
ATOM    763  HA2 GLY A  51      28.200  16.762 -36.122  1.00 29.23           H  
ATOM    764  HA3 GLY A  51      27.262  16.440 -37.351  1.00 29.23           H  
ATOM    765  N   VAL A  52      26.729  19.319 -37.195  1.00 28.45           N  
ANISOU  765  N   VAL A  52     3193   4204   3412    606    545   -352       N  
ATOM    766  CA  VAL A  52      26.948  20.649 -37.745  1.00 28.80           C  
ANISOU  766  CA  VAL A  52     3211   4324   3409    532    546   -325       C  
ATOM    767  C   VAL A  52      27.799  21.454 -36.775  1.00 26.51           C  
ANISOU  767  C   VAL A  52     2866   4082   3125    517    532   -275       C  
ATOM    768  O   VAL A  52      27.623  21.375 -35.552  1.00 24.48           O  
ANISOU  768  O   VAL A  52     2616   3776   2909    531    506   -246       O  
ATOM    769  CB  VAL A  52      25.600  21.335 -38.025  1.00 24.16           C  
ANISOU  769  CB  VAL A  52     2681   3687   2813    463    519   -310       C  
ATOM    770  CG1 VAL A  52      25.799  22.795 -38.409  1.00 26.16           C  
ANISOU  770  CG1 VAL A  52     2910   4005   3022    386    512   -273       C  
ATOM    771  CG2 VAL A  52      24.848  20.587 -39.125  1.00 30.91           C  
ANISOU  771  CG2 VAL A  52     3582   4509   3651    472    534   -362       C  
ATOM    772  H   VAL A  52      25.937  19.189 -36.887  1.00 34.14           H  
ATOM    773  HA  VAL A  52      27.426  20.581 -38.586  1.00 34.56           H  
ATOM    774  HB  VAL A  52      25.066  21.314 -37.216  1.00 29.00           H  
ATOM    775 HG11 VAL A  52      25.073  23.070 -38.991  1.00 31.39           H  
ATOM    776 HG12 VAL A  52      25.800  23.336 -37.604  1.00 31.39           H  
ATOM    777 HG13 VAL A  52      26.647  22.888 -38.871  1.00 31.39           H  
ATOM    778 HG21 VAL A  52      24.036  21.072 -39.339  1.00 37.09           H  
ATOM    779 HG22 VAL A  52      25.414  20.526 -39.910  1.00 37.09           H  
ATOM    780 HG23 VAL A  52      24.627  19.697 -38.807  1.00 37.09           H  
ATOM    781  N   VAL A  53      28.747  22.211 -37.315  1.00 27.21           N  
ANISOU  781  N   VAL A  53     2900   4269   3170    486    550   -265       N  
ATOM    782  CA  VAL A  53      29.610  23.067 -36.513  1.00 25.97           C  
ANISOU  782  CA  VAL A  53     2689   4166   3011    460    537   -217       C  
ATOM    783  C   VAL A  53      28.921  24.415 -36.338  1.00 26.32           C  
ANISOU  783  C   VAL A  53     2761   4196   3042    372    505   -174       C  
ATOM    784  O   VAL A  53      28.597  25.083 -37.324  1.00 26.46           O  
ANISOU  784  O   VAL A  53     2794   4238   3020    316    510   -174       O  
ATOM    785  CB  VAL A  53      30.987  23.243 -37.169  1.00 31.00           C  
ANISOU  785  CB  VAL A  53     3273   4889   3618    449    555   -219       C  
ATOM    786  CG1 VAL A  53      31.857  24.156 -36.307  1.00 28.48           C  
ANISOU  786  CG1 VAL A  53     2902   4622   3296    414    537   -169       C  
ATOM    787  CG2 VAL A  53      31.657  21.889 -37.409  1.00 32.45           C  
ANISOU  787  CG2 VAL A  53     3449   5059   3824    527    575   -260       C  
ATOM    788  H   VAL A  53      28.911  22.246 -38.159  1.00 32.65           H  
ATOM    789  HA  VAL A  53      29.734  22.664 -35.639  1.00 31.16           H  
ATOM    790  HB  VAL A  53      30.879  23.661 -38.038  1.00 37.20           H  
ATOM    791 HG11 VAL A  53      32.791  23.977 -36.499  1.00 34.17           H  
ATOM    792 HG12 VAL A  53      31.648  25.080 -36.514  1.00 34.17           H  
ATOM    793 HG13 VAL A  53      31.672  23.977 -35.371  1.00 34.17           H  
ATOM    794 HG21 VAL A  53      31.415  21.285 -36.689  1.00 38.95           H  
ATOM    795 HG22 VAL A  53      31.353  21.532 -38.257  1.00 38.95           H  
ATOM    796 HG23 VAL A  53      32.619  22.012 -37.427  1.00 38.95           H  
ATOM    797  N   LYS A  54      28.702  24.827 -35.092  1.00 23.44           N  
ANISOU  797  N   LYS A  54     2404   3792   2711    359    472   -135       N  
ATOM    798  CA  LYS A  54      28.084  26.122 -34.843  1.00 23.21           C  
ANISOU  798  CA  LYS A  54     2402   3744   2672    281    440    -95       C  
ATOM    799  C   LYS A  54      29.141  27.200 -34.646  1.00 24.41           C  
ANISOU  799  C   LYS A  54     2501   3979   2796    232    436    -58       C  
ATOM    800  O   LYS A  54      30.169  26.973 -34.002  1.00 23.62           O  
ANISOU  800  O   LYS A  54     2345   3925   2703    261    443    -49       O  
ATOM    801  CB  LYS A  54      27.161  26.058 -33.629  1.00 22.07           C  
ANISOU  801  CB  LYS A  54     2301   3511   2574    288    405    -77       C  
ATOM    802  CG  LYS A  54      25.819  25.466 -33.972  1.00 21.36           C  
ANISOU  802  CG  LYS A  54     2276   3340   2501    301    399   -102       C  
ATOM    803  CD  LYS A  54      24.842  25.572 -32.825  1.00 21.49           C  
ANISOU  803  CD  LYS A  54     2332   3277   2556    296    364    -80       C  
ATOM    804  CE  LYS A  54      24.527  27.013 -32.486  1.00 21.46           C  
ANISOU  804  CE  LYS A  54     2339   3276   2540    227    335    -41       C  
ATOM    805  NZ  LYS A  54      23.361  27.089 -31.572  1.00 21.25           N  
ANISOU  805  NZ  LYS A  54     2358   3171   2546    223    304    -28       N  
ATOM    806  H   LYS A  54      28.901  24.379 -34.386  1.00 28.13           H  
ATOM    807  HA  LYS A  54      27.551  26.368 -35.614  1.00 27.85           H  
ATOM    808  HB2 LYS A  54      27.571  25.505 -32.946  1.00 26.49           H  
ATOM    809  HB3 LYS A  54      27.020  26.955 -33.289  1.00 26.49           H  
ATOM    810  HG2 LYS A  54      25.446  25.940 -34.731  1.00 25.64           H  
ATOM    811  HG3 LYS A  54      25.930  24.527 -34.188  1.00 25.64           H  
ATOM    812  HD2 LYS A  54      24.013  25.130 -33.069  1.00 25.79           H  
ATOM    813  HD3 LYS A  54      25.224  25.152 -32.039  1.00 25.79           H  
ATOM    814  HE2 LYS A  54      25.291  27.418 -32.045  1.00 25.76           H  
ATOM    815  HE3 LYS A  54      24.316  27.500 -33.298  1.00 25.76           H  
ATOM    816  HZ1 LYS A  54      22.696  26.586 -31.885  1.00 25.50           H  
ATOM    817  HZ2 LYS A  54      23.588  26.796 -30.763  1.00 25.50           H  
ATOM    818  HZ3 LYS A  54      23.080  27.931 -31.507  1.00 25.50           H  
ATOM    819  N   GLU A  55      28.872  28.380 -35.212  1.00 24.09           N  
ANISOU  819  N   GLU A  55     2477   3955   2721    154    424    -35       N  
ATOM    820  CA  GLU A  55      29.798  29.503 -35.101  1.00 24.95           C  
ANISOU  820  CA  GLU A  55     2542   4137   2800     94    418      2       C  
ATOM    821  C   GLU A  55      30.097  29.824 -33.644  1.00 22.01           C  
ANISOU  821  C   GLU A  55     2155   3749   2459     93    390     34       C  
ATOM    822  O   GLU A  55      31.259  30.027 -33.271  1.00 24.64           O  
ANISOU  822  O   GLU A  55     2427   4154   2780     88    396     51       O  
ATOM    823  CB  GLU A  55      29.206  30.716 -35.825  1.00 26.06           C  
ANISOU  823  CB  GLU A  55     2722   4271   2907     11    401     25       C  
ATOM    824  CG  GLU A  55      29.773  32.081 -35.457  1.00 66.59           C  
ANISOU  824  CG  GLU A  55     7839   9443   8020    -66    378     73       C  
ATOM    825  CD  GLU A  55      28.975  33.224 -36.086  1.00 38.67           C  
ANISOU  825  CD  GLU A  55     4356   5876   4460   -140    354     96       C  
ATOM    826  OE1 GLU A  55      27.877  32.964 -36.626  1.00 79.76           O  
ANISOU  826  OE1 GLU A  55     9612  11023   9669   -128    351     78       O  
ATOM    827  OE2 GLU A  55      29.444  34.380 -36.038  1.00 50.73           O  
ANISOU  827  OE2 GLU A  55     5876   7437   5963   -210    338    134       O  
ATOM    828  H   GLU A  55      28.163  28.556 -35.666  1.00 28.91           H  
ATOM    829  HA  GLU A  55      30.640  29.276 -35.526  1.00 29.94           H  
ATOM    830  HB2 GLU A  55      29.351  30.597 -36.777  1.00 31.27           H  
ATOM    831  HB3 GLU A  55      28.256  30.744 -35.635  1.00 31.27           H  
ATOM    832  HG2 GLU A  55      29.746  32.188 -34.493  1.00 79.91           H  
ATOM    833  HG3 GLU A  55      30.688  32.142 -35.772  1.00 79.91           H  
ATOM    834  N   LYS A  56      29.070  29.864 -32.804  1.00 20.16           N  
ANISOU  834  N   LYS A  56     1973   3426   2262     98    360     42       N  
ATOM    835  CA  LYS A  56      29.286  30.220 -31.414  1.00 24.31           C  
ANISOU  835  CA  LYS A  56     2489   3936   2813     93    332     71       C  
ATOM    836  C   LYS A  56      28.174  29.635 -30.561  1.00 26.27           C  
ANISOU  836  C   LYS A  56     2786   4089   3107    132    312     64       C  
ATOM    837  O   LYS A  56      26.999  29.693 -30.933  1.00 23.57           O  
ANISOU  837  O   LYS A  56     2501   3685   2771    122    303     54       O  
ATOM    838  CB  LYS A  56      29.343  31.741 -31.226  1.00 25.66           C  
ANISOU  838  CB  LYS A  56     2669   4119   2962      8    304    110       C  
ATOM    839  CG  LYS A  56      29.897  32.152 -29.858  1.00 23.75           C  
ANISOU  839  CG  LYS A  56     2402   3885   2735     -3    280    138       C  
ATOM    840  CD  LYS A  56      29.731  33.632 -29.620  1.00 33.32           C  
ANISOU  840  CD  LYS A  56     3640   5087   3931    -86    248    171       C  
ATOM    841  CE  LYS A  56      30.760  34.434 -30.392  1.00 27.36           C  
ANISOU  841  CE  LYS A  56     2846   4419   3129   -148    259    189       C  
ATOM    842  NZ  LYS A  56      32.105  34.332 -29.777  1.00 25.56           N  
ANISOU  842  NZ  LYS A  56     2545   4272   2894   -146    265    203       N  
ATOM    843  H   LYS A  56      28.254  29.691 -33.013  1.00 24.20           H  
ATOM    844  HA  LYS A  56      30.127  29.838 -31.120  1.00 29.18           H  
ATOM    845  HB2 LYS A  56      29.918  32.122 -31.908  1.00 30.79           H  
ATOM    846  HB3 LYS A  56      28.447  32.103 -31.307  1.00 30.79           H  
ATOM    847  HG2 LYS A  56      29.420  31.675 -29.162  1.00 28.50           H  
ATOM    848  HG3 LYS A  56      30.843  31.941 -29.818  1.00 28.50           H  
ATOM    849  HD2 LYS A  56      28.848  33.907 -29.910  1.00 39.98           H  
ATOM    850  HD3 LYS A  56      29.843  33.820 -28.675  1.00 39.98           H  
ATOM    851  HE2 LYS A  56      30.814  34.097 -31.300  1.00 32.83           H  
ATOM    852  HE3 LYS A  56      30.499  35.368 -30.399  1.00 32.83           H  
ATOM    853  HZ1 LYS A  56      32.731  34.360 -30.409  1.00 30.67           H  
ATOM    854  HZ2 LYS A  56      32.234  35.008 -29.213  1.00 30.67           H  
ATOM    855  HZ3 LYS A  56      32.178  33.565 -29.332  1.00 30.67           H  
ATOM    856  N   VAL A  57      28.567  29.062 -29.422  1.00 17.86           N  
ANISOU  856  N   VAL A  57     1697   3018   2072    176    306     70       N  
ATOM    857  CA  VAL A  57      27.636  28.602 -28.405  1.00 17.04           C  
ANISOU  857  CA  VAL A  57     1634   2833   2008    205    284     71       C  
ATOM    858  C   VAL A  57      28.082  29.168 -27.064  1.00 18.72           C  
ANISOU  858  C   VAL A  57     1826   3057   2231    187    257    104       C  
ATOM    859  O   VAL A  57      29.215  29.621 -26.891  1.00 17.85           O  
ANISOU  859  O   VAL A  57     1663   3018   2102    167    259    122       O  
ATOM    860  CB  VAL A  57      27.535  27.061 -28.330  1.00 20.43           C  
ANISOU  860  CB  VAL A  57     2064   3232   2468    286    302     43       C  
ATOM    861  CG1 VAL A  57      26.976  26.512 -29.646  1.00 24.82           C  
ANISOU  861  CG1 VAL A  57     2648   3770   3013    300    325      7       C  
ATOM    862  CG2 VAL A  57      28.885  26.429 -28.007  1.00 19.66           C  
ANISOU  862  CG2 VAL A  57     1900   3198   2372    335    318     45       C  
ATOM    863  H   VAL A  57      29.392  28.929 -29.217  1.00 21.44           H  
ATOM    864  HA  VAL A  57      26.751  28.941 -28.611  1.00 20.45           H  
ATOM    865  HB  VAL A  57      26.929  26.823 -27.611  1.00 24.52           H  
ATOM    866 HG11 VAL A  57      26.577  25.643 -29.482  1.00 29.78           H  
ATOM    867 HG12 VAL A  57      26.305  27.125 -29.985  1.00 29.78           H  
ATOM    868 HG13 VAL A  57      27.700  26.428 -30.286  1.00 29.78           H  
ATOM    869 HG21 VAL A  57      28.793  25.464 -28.020  1.00 23.59           H  
ATOM    870 HG22 VAL A  57      29.533  26.709 -28.673  1.00 23.59           H  
ATOM    871 HG23 VAL A  57      29.169  26.723 -27.127  1.00 23.59           H  
ATOM    872  N   MET A  58      27.160  29.149 -26.115  1.00 19.30           N  
ANISOU  872  N   MET A  58     1940   3062   2332    192    232    112       N  
ATOM    873  CA  MET A  58      27.404  29.627 -24.762  1.00 19.10           C  
ANISOU  873  CA  MET A  58     1903   3038   2317    176    206    140       C  
ATOM    874  C   MET A  58      26.886  28.528 -23.854  1.00 22.10           C  
ANISOU  874  C   MET A  58     2298   3366   2734    235    200    135       C  
ATOM    875  O   MET A  58      25.692  28.211 -23.893  1.00 22.27           O  
ANISOU  875  O   MET A  58     2370   3319   2772    244    195    122       O  
ATOM    876  CB  MET A  58      26.707  30.960 -24.505  1.00 16.49           C  
ANISOU  876  CB  MET A  58     1613   2677   1976    110    177    155       C  
ATOM    877  CG  MET A  58      27.169  32.071 -25.451  1.00 18.70           C  
ANISOU  877  CG  MET A  58     1885   3002   2218     47    180    164       C  
ATOM    878  SD  MET A  58      26.436  33.674 -25.108  1.00 18.82           S  
ANISOU  878  SD  MET A  58     1951   2976   2224    -27    144    183       S  
ATOM    879  CE  MET A  58      27.253  34.691 -26.335  1.00 19.46           C  
ANISOU  879  CE  MET A  58     2013   3120   2260    -94    152    196       C  
ATOM    880  H   MET A  58      26.360  28.855 -26.235  1.00 23.16           H  
ATOM    881  HA  MET A  58      28.346  29.787 -24.600  1.00 22.92           H  
ATOM    882  HB2 MET A  58      25.751  30.844 -24.624  1.00 19.79           H  
ATOM    883  HB3 MET A  58      26.895  31.244 -23.596  1.00 19.79           H  
ATOM    884  HG2 MET A  58      28.132  32.165 -25.374  1.00 22.44           H  
ATOM    885  HG3 MET A  58      26.932  31.826 -26.359  1.00 22.44           H  
ATOM    886  HE1 MET A  58      26.939  35.604 -26.248  1.00 23.35           H  
ATOM    887  HE2 MET A  58      28.211  34.655 -26.187  1.00 23.35           H  
ATOM    888  HE3 MET A  58      27.042  34.350 -27.218  1.00 23.35           H  
ATOM    889  N   LEU A  59      27.785  27.940 -23.065  1.00 19.66           N  
ANISOU  889  N   LEU A  59     1945   3090   2436    272    200    147       N  
ATOM    890  CA  LEU A  59      27.556  26.664 -22.405  1.00 16.42           C  
ANISOU  890  CA  LEU A  59     1540   2640   2059    338    200    143       C  
ATOM    891  C   LEU A  59      27.604  26.814 -20.892  1.00 17.33           C  
ANISOU  891  C   LEU A  59     1650   2748   2186    335    172    172       C  
ATOM    892  O   LEU A  59      28.291  27.689 -20.364  1.00 21.20           O  
ANISOU  892  O   LEU A  59     2109   3287   2658    296    158    194       O  
ATOM    893  CB  LEU A  59      28.611  25.645 -22.841  1.00 19.85           C  
ANISOU  893  CB  LEU A  59     1927   3120   2497    400    226    131       C  
ATOM    894  CG  LEU A  59      28.830  25.488 -24.345  1.00 23.19           C  
ANISOU  894  CG  LEU A  59     2342   3568   2900    405    258    101       C  
ATOM    895  CD1 LEU A  59      30.052  24.610 -24.605  1.00 28.35           C  
ANISOU  895  CD1 LEU A  59     2937   4280   3554    468    282     91       C  
ATOM    896  CD2 LEU A  59      27.599  24.903 -24.979  1.00 25.47           C  
ANISOU  896  CD2 LEU A  59     2693   3781   3203    419    265     73       C  
ATOM    897  H   LEU A  59      28.558  28.276 -22.895  1.00 23.59           H  
ATOM    898  HA  LEU A  59      26.672  26.340 -22.639  1.00 19.71           H  
ATOM    899  HB2 LEU A  59      29.461  25.909 -22.455  1.00 23.83           H  
ATOM    900  HB3 LEU A  59      28.349  24.776 -22.499  1.00 23.83           H  
ATOM    901  HG  LEU A  59      28.994  26.354 -24.750  1.00 27.83           H  
ATOM    902 HD11 LEU A  59      30.216  24.572 -25.561  1.00 34.02           H  
ATOM    903 HD12 LEU A  59      30.819  24.994 -24.153  1.00 34.02           H  
ATOM    904 HD13 LEU A  59      29.879  23.718 -24.264  1.00 34.02           H  
ATOM    905 HD21 LEU A  59      27.364  25.430 -25.758  1.00 30.56           H  
ATOM    906 HD22 LEU A  59      27.784  23.988 -25.242  1.00 30.56           H  
ATOM    907 HD23 LEU A  59      26.873  24.922 -24.336  1.00 30.56           H  
ATOM    908  N   VAL A  60      26.840  25.959 -20.208  1.00 16.29           N  
ANISOU  908  N   VAL A  60     1550   2556   2084    372    163    173       N  
ATOM    909  CA  VAL A  60      26.898  25.804 -18.756  1.00 19.36           C  
ANISOU  909  CA  VAL A  60     1931   2938   2485    381    139    200       C  
ATOM    910  C   VAL A  60      27.681  24.528 -18.475  1.00 19.25           C  
ANISOU  910  C   VAL A  60     1884   2938   2491    452    148    205       C  
ATOM    911  O   VAL A  60      27.264  23.432 -18.873  1.00 18.59           O  
ANISOU  911  O   VAL A  60     1826   2808   2431    500    161    188       O  
ATOM    912  CB  VAL A  60      25.497  25.727 -18.121  1.00 17.74           C  
ANISOU  912  CB  VAL A  60     1784   2660   2296    370    123    200       C  
ATOM    913  CG1 VAL A  60      25.599  25.720 -16.573  1.00 16.71           C  
ANISOU  913  CG1 VAL A  60     1645   2534   2172    371     97    230       C  
ATOM    914  CG2 VAL A  60      24.587  26.852 -18.637  1.00 18.69           C  
ANISOU  914  CG2 VAL A  60     1943   2758   2401    313    118    188       C  
ATOM    915  H   VAL A  60      26.262  25.441 -20.579  1.00 19.55           H  
ATOM    916  HA  VAL A  60      27.358  26.566 -18.371  1.00 23.23           H  
ATOM    917  HB  VAL A  60      25.080  24.892 -18.387  1.00 21.29           H  
ATOM    918 HG11 VAL A  60      25.729  26.629 -16.261  1.00 20.06           H  
ATOM    919 HG12 VAL A  60      24.779  25.357 -16.204  1.00 20.06           H  
ATOM    920 HG13 VAL A  60      26.353  25.168 -16.309  1.00 20.06           H  
ATOM    921 HG21 VAL A  60      23.664  26.626 -18.441  1.00 22.43           H  
ATOM    922 HG22 VAL A  60      24.826  27.681 -18.193  1.00 22.43           H  
ATOM    923 HG23 VAL A  60      24.708  26.943 -19.595  1.00 22.43           H  
ATOM    924  N   ASN A  61      28.813  24.662 -17.799  1.00 19.37           N  
ANISOU  924  N   ASN A  61     1845   3016   2498    459    139    229       N  
ATOM    925  CA  ASN A  61      29.682  23.521 -17.527  1.00 22.68           C  
ANISOU  925  CA  ASN A  61     2226   3457   2936    530    144    238       C  
ATOM    926  C   ASN A  61      29.949  22.692 -18.786  1.00 21.45           C  
ANISOU  926  C   ASN A  61     2064   3300   2788    581    177    206       C  
ATOM    927  O   ASN A  61      29.870  21.465 -18.788  1.00 23.49           O  
ANISOU  927  O   ASN A  61     2334   3518   3073    646    184    198       O  
ATOM    928  CB  ASN A  61      29.077  22.691 -16.379  1.00 20.87           C  
ANISOU  928  CB  ASN A  61     2026   3169   2733    562    124    257       C  
ATOM    929  CG  ASN A  61      29.381  23.326 -15.065  1.00 24.62           C  
ANISOU  929  CG  ASN A  61     2480   3678   3197    530     94    292       C  
ATOM    930  OD1 ASN A  61      29.016  24.480 -14.841  1.00 21.83           O  
ANISOU  930  OD1 ASN A  61     2140   3333   2823    465     82    294       O  
ATOM    931  ND2 ASN A  61      30.084  22.618 -14.204  1.00 23.21           N  
ANISOU  931  ND2 ASN A  61     2268   3522   3030    575     82    319       N  
ATOM    932  H   ASN A  61      29.103  25.409 -17.485  1.00 23.24           H  
ATOM    933  HA  ASN A  61      30.556  23.836 -17.247  1.00 27.22           H  
ATOM    934  HB2 ASN A  61      28.114  22.642 -16.484  1.00 25.04           H  
ATOM    935  HB3 ASN A  61      29.457  21.798 -16.387  1.00 25.04           H  
ATOM    936 HD21 ASN A  61      30.268  21.794 -14.367  1.00 27.85           H  
ATOM    937  N   ASN A  62      30.278  23.394 -19.871  1.00 20.06           N  
ANISOU  937  N   ASN A  62     1870   3167   2585    548    197    186       N  
ATOM    938  CA AASN A  62      30.755  22.778 -21.106  0.46 20.45           C  
ANISOU  938  CA AASN A  62     1901   3239   2632    590    230    155       C  
ATOM    939  CA BASN A  62      30.755  22.806 -21.125  0.54 21.83           C  
ANISOU  939  CA BASN A  62     2075   3414   2805    588    230    154       C  
ATOM    940  C   ASN A  62      29.695  21.957 -21.831  1.00 27.49           C  
ANISOU  940  C   ASN A  62     2854   4049   3542    616    244    122       C  
ATOM    941  O   ASN A  62      30.035  21.060 -22.606  1.00 34.53           O  
ANISOU  941  O   ASN A  62     3738   4942   4442    672    269     94       O  
ATOM    942  CB AASN A  62      31.972  21.883 -20.838  0.46 31.67           C  
ANISOU  942  CB AASN A  62     3283   4689   4063    644    232    156       C  
ATOM    943  CB BASN A  62      32.028  21.977 -20.901  0.54 26.41           C  
ANISOU  943  CB BASN A  62     2612   4028   3392    640    233    156       C  
ATOM    944  CG AASN A  62      33.092  22.621 -20.164  0.46 21.27           C  
ANISOU  944  CG AASN A  62     1910   3449   2723    612    216    186       C  
ATOM    945  CG BASN A  62      32.913  21.914 -22.139  0.54 26.33           C  
ANISOU  945  CG BASN A  62     2570   4072   3361    648    262    127       C  
ATOM    946  OD1AASN A  62      33.379  23.769 -20.500  0.46 40.33           O  
ANISOU  946  OD1AASN A  62     4296   5922   5105    554    218    192       O  
ATOM    947  OD1BASN A  62      32.926  22.837 -22.956  0.54 25.45           O  
ANISOU  947  OD1BASN A  62     2445   4007   3219    600    277    119       O  
ATOM    948  ND2AASN A  62      33.733  21.973 -19.199  0.46 38.11           N  
ANISOU  948  ND2AASN A  62     4026   5581   4871    647    197    205       N  
ATOM    949  ND2BASN A  62      33.657  20.821 -22.281  0.54 31.71           N  
ANISOU  949  ND2BASN A  62     3239   4749   4058    708    270    111       N  
ATOM    950  H  AASN A  62      30.231  24.252 -19.912  0.46 24.07           H  
ATOM    951  H  BASN A  62      30.232  24.252 -19.906  0.54 24.07           H  
ATOM    952  HA AASN A  62      31.011  23.501 -21.701  0.46 24.54           H  
ATOM    953  HA BASN A  62      30.965  23.540 -21.724  0.54 26.19           H  
ATOM    954  HB2AASN A  62      31.705  21.150 -20.262  0.46 38.01           H  
ATOM    955  HB2BASN A  62      32.544  22.376 -20.183  0.54 31.69           H  
ATOM    956  HB3AASN A  62      32.303  21.538 -21.682  0.46 38.01           H  
ATOM    957  HB3BASN A  62      31.777  21.070 -20.665  0.54 31.69           H  
ATOM    958 HD21AASN A  62      34.382  22.354 -18.783  0.46 45.73           H  
ATOM    959 HD21BASN A  62      34.173  20.738 -22.963  0.54 38.05           H  
ATOM    960 HD22AASN A  62      33.499  21.172 -18.990  0.46 45.73           H  
ATOM    961 HD22BASN A  62      33.621  20.197 -21.690  0.54 38.05           H  
ATOM    962  N   SER A  63      28.411  22.236 -21.608  1.00 26.92           N  
ANISOU  962  N   SER A  63     2842   3909   3477    578    229    122       N  
ATOM    963  CA  SER A  63      27.341  21.540 -22.317  1.00 25.61           C  
ANISOU  963  CA  SER A  63     2735   3670   3326    594    240     92       C  
ATOM    964  C   SER A  63      26.250  22.534 -22.698  1.00 22.02           C  
ANISOU  964  C   SER A  63     2322   3189   2854    524    232     87       C  
ATOM    965  O   SER A  63      26.133  23.604 -22.094  1.00 26.85           O  
ANISOU  965  O   SER A  63     2931   3818   3453    472    212    110       O  
ATOM    966  CB  SER A  63      26.748  20.406 -21.468  1.00 37.23           C  
ANISOU  966  CB  SER A  63     4243   5069   4835    638    226    100       C  
ATOM    967  OG  SER A  63      25.611  19.849 -22.102  1.00 45.05           O  
ANISOU  967  OG  SER A  63     5292   5988   5836    639    233     73       O  
ATOM    968  H   SER A  63      28.135  22.828 -21.048  1.00 32.30           H  
ATOM    969  HA  SER A  63      27.697  21.157 -23.135  1.00 30.73           H  
ATOM    970  HB2 SER A  63      27.417  19.714 -21.353  1.00 44.68           H  
ATOM    971  HB3 SER A  63      26.486  20.762 -20.605  1.00 44.68           H  
ATOM    972  HG  SER A  63      25.683  19.920 -22.936  1.00 54.06           H  
ATOM    973  N   ILE A  64      25.461  22.196 -23.728  1.00 29.86           N  
ANISOU  973  N   ILE A  64     3356   4142   3847    524    248     55       N  
ATOM    974  CA  ILE A  64      24.301  23.029 -24.040  1.00 28.39           C  
ANISOU  974  CA  ILE A  64     3214   3925   3649    465    237     52       C  
ATOM    975  C   ILE A  64      23.111  22.679 -23.157  1.00 24.64           C  
ANISOU  975  C   ILE A  64     2785   3378   3198    463    215     62       C  
ATOM    976  O   ILE A  64      22.072  23.350 -23.226  1.00 27.48           O  
ANISOU  976  O   ILE A  64     3179   3711   3552    419    203     62       O  
ATOM    977  CB  ILE A  64      23.813  22.975 -25.502  1.00 35.53           C  
ANISOU  977  CB  ILE A  64     4143   4820   4536    454    258     17       C  
ATOM    978  CG1 ILE A  64      23.692  21.537 -25.985  1.00 25.57           C  
ANISOU  978  CG1 ILE A  64     2901   3518   3295    513    276    -14       C  
ATOM    979  CG2 ILE A  64      24.746  23.778 -26.406  1.00 36.56           C  
ANISOU  979  CG2 ILE A  64     4233   5026   4631    429    275     13       C  
ATOM    980  CD1 ILE A  64      23.045  21.425 -27.359  1.00 43.85           C  
ANISOU  980  CD1 ILE A  64     5249   5819   5594    498    294    -51       C  
ATOM    981  H   ILE A  64      25.576  21.515 -24.240  1.00 35.83           H  
ATOM    982  HA  ILE A  64      24.607  23.938 -23.893  1.00 34.07           H  
ATOM    983  HB  ILE A  64      22.930  23.375 -25.538  1.00 42.63           H  
ATOM    984 HG12 ILE A  64      24.579  21.148 -26.039  1.00 30.68           H  
ATOM    985 HG13 ILE A  64      23.148  21.038 -25.356  1.00 30.68           H  
ATOM    986 HG21 ILE A  64      25.112  24.521 -25.901  1.00 43.87           H  
ATOM    987 HG22 ILE A  64      25.463  23.201 -26.712  1.00 43.87           H  
ATOM    988 HG23 ILE A  64      24.242  24.110 -27.165  1.00 43.87           H  
ATOM    989 HD11 ILE A  64      23.058  20.496 -27.639  1.00 52.62           H  
ATOM    990 HD12 ILE A  64      22.130  21.741 -27.303  1.00 52.62           H  
ATOM    991 HD13 ILE A  64      23.545  21.968 -27.989  1.00 52.62           H  
ATOM    992  N   ILE A  65      23.229  21.645 -22.328  1.00 29.69           N  
ANISOU  992  N   ILE A  65     3426   3989   3866    510    209     72       N  
ATOM    993  CA  ILE A  65      22.345  21.462 -21.184  1.00 24.06           C  
ANISOU  993  CA  ILE A  65     2743   3227   3172    501    186     94       C  
ATOM    994  C   ILE A  65      23.222  21.403 -19.949  1.00 19.15           C  
ANISOU  994  C   ILE A  65     2083   2635   2557    521    171    127       C  
ATOM    995  O   ILE A  65      24.071  20.510 -19.818  1.00 21.36           O  
ANISOU  995  O   ILE A  65     2339   2925   2851    575    178    130       O  
ATOM    996  CB  ILE A  65      21.475  20.205 -21.276  1.00 23.83           C  
ANISOU  996  CB  ILE A  65     2760   3125   3168    531    188     79       C  
ATOM    997  CG1 ILE A  65      20.767  20.149 -22.621  1.00 27.30           C  
ANISOU  997  CG1 ILE A  65     3232   3543   3598    516    204     42       C  
ATOM    998  CG2 ILE A  65      20.434  20.205 -20.130  1.00 24.24           C  
ANISOU  998  CG2 ILE A  65     2842   3135   3232    508    163    103       C  
ATOM    999  CD1 ILE A  65      19.906  18.926 -22.782  1.00 38.61           C  
ANISOU  999  CD1 ILE A  65     4712   4904   5053    538    206     26       C  
ATOM   1000  H   ILE A  65      23.823  21.030 -22.412  1.00 35.63           H  
ATOM   1001  HA  ILE A  65      21.747  22.225 -21.132  1.00 28.87           H  
ATOM   1002  HB  ILE A  65      22.045  19.425 -21.194  1.00 28.59           H  
ATOM   1003 HG12 ILE A  65      20.198  20.929 -22.711  1.00 32.76           H  
ATOM   1004 HG13 ILE A  65      21.433  20.141 -23.327  1.00 32.76           H  
ATOM   1005 HG21 ILE A  65      20.828  20.617 -19.345  1.00 29.08           H  
ATOM   1006 HG22 ILE A  65      19.654  20.708 -20.411  1.00 29.08           H  
ATOM   1007 HG23 ILE A  65      20.183  19.289 -19.931  1.00 29.08           H  
ATOM   1008 HD11 ILE A  65      19.269  18.889 -22.052  1.00 46.33           H  
ATOM   1009 HD12 ILE A  65      19.435  18.980 -23.629  1.00 46.33           H  
ATOM   1010 HD13 ILE A  65      20.471  18.137 -22.768  1.00 46.33           H  
ATOM   1011  N   GLY A  66      23.008  22.332 -19.045  1.00 19.41           N  
ANISOU 1011  N   GLY A  66     2112   2683   2579    480    149    151       N  
ATOM   1012  CA  GLY A  66      23.808  22.401 -17.866  1.00 17.90           C  
ANISOU 1012  CA  GLY A  66     1886   2527   2390    490    133    183       C  
ATOM   1013  C   GLY A  66      23.470  21.309 -16.870  1.00 18.46           C  
ANISOU 1013  C   GLY A  66     1975   2553   2487    526    120    203       C  
ATOM   1014  O   GLY A  66      22.539  20.509 -17.050  1.00 19.09           O  
ANISOU 1014  O   GLY A  66     2099   2571   2584    538    123    192       O  
ATOM   1015  H   GLY A  66      22.398  22.936 -19.098  1.00 23.29           H  
ATOM   1016  HA2 GLY A  66      24.743  22.314 -18.108  1.00 21.48           H  
ATOM   1017  HA3 GLY A  66      23.672  23.259 -17.435  1.00 21.48           H  
ATOM   1018  N   PRO A  67      24.235  21.283 -15.790  1.00 19.91           N  
ANISOU 1018  N   PRO A  67     2124   2770   2670    539    104    234       N  
ATOM   1019  CA  PRO A  67      23.956  20.336 -14.706  1.00 20.55           C  
ANISOU 1019  CA  PRO A  67     2221   2814   2772    568     87    260       C  
ATOM   1020  C   PRO A  67      22.570  20.545 -14.107  1.00 17.55           C  
ANISOU 1020  C   PRO A  67     1888   2388   2391    528     73    265       C  
ATOM   1021  O   PRO A  67      22.105  21.675 -13.955  1.00 17.91           O  
ANISOU 1021  O   PRO A  67     1938   2450   2416    477     67    262       O  
ATOM   1022  CB  PRO A  67      25.060  20.640 -13.684  1.00 19.21           C  
ANISOU 1022  CB  PRO A  67     2001   2706   2592    574     70    294       C  
ATOM   1023  CG  PRO A  67      26.157  21.346 -14.483  1.00 22.67           C  
ANISOU 1023  CG  PRO A  67     2390   3212   3011    568     85    281       C  
ATOM   1024  CD  PRO A  67      25.444  22.098 -15.557  1.00 28.67           C  
ANISOU 1024  CD  PRO A  67     3178   3958   3759    526    100    248       C  
ATOM   1025  HA  PRO A  67      24.034  19.423 -15.024  1.00 24.66           H  
ATOM   1026  HB2 PRO A  67      24.713  21.217 -12.986  1.00 23.05           H  
ATOM   1027  HB3 PRO A  67      25.389  19.814 -13.298  1.00 23.05           H  
ATOM   1028  HG2 PRO A  67      26.647  21.952 -13.905  1.00 27.20           H  
ATOM   1029  HG3 PRO A  67      26.760  20.689 -14.864  1.00 27.20           H  
ATOM   1030  HD2 PRO A  67      25.208  22.989 -15.257  1.00 34.41           H  
ATOM   1031  HD3 PRO A  67      25.985  22.150 -16.360  1.00 34.41           H  
ATOM   1032  N   THR A  68      21.919  19.442 -13.727  1.00 16.29           N  
ANISOU 1032  N   THR A  68     1762   2172   2254    551     68    275       N  
ATOM   1033  CA  THR A  68      20.613  19.530 -13.081  1.00 17.16           C  
ANISOU 1033  CA  THR A  68     1913   2246   2363    515     55    282       C  
ATOM   1034  C   THR A  68      20.763  19.966 -11.627  1.00 18.76           C  
ANISOU 1034  C   THR A  68     2096   2480   2551    496     32    318       C  
ATOM   1035  O   THR A  68      21.611  19.443 -10.895  1.00 22.02           O  
ANISOU 1035  O   THR A  68     2485   2912   2970    527     21    347       O  
ATOM   1036  CB  THR A  68      19.881  18.188 -13.159  1.00 16.27           C  
ANISOU 1036  CB  THR A  68     1843   2063   2276    540     57    283       C  
ATOM   1037  OG1 THR A  68      19.629  17.884 -14.537  1.00 18.20           O  
ANISOU 1037  OG1 THR A  68     2109   2279   2529    550     78    245       O  
ATOM   1038  CG2 THR A  68      18.555  18.217 -12.387  1.00 17.21           C  
ANISOU 1038  CG2 THR A  68     1996   2152   2390    500     43    296       C  
ATOM   1039  H   THR A  68      22.211  18.640 -13.833  1.00 19.54           H  
ATOM   1040  HA  THR A  68      20.079  20.196 -13.542  1.00 20.60           H  
ATOM   1041  HB  THR A  68      20.430  17.498 -12.755  1.00 19.52           H  
ATOM   1042  HG1 THR A  68      19.292  17.117 -14.605  1.00 21.84           H  
ATOM   1043 HG21 THR A  68      18.035  17.424 -12.592  1.00 20.65           H  
ATOM   1044 HG22 THR A  68      18.727  18.243 -11.433  1.00 20.65           H  
ATOM   1045 HG23 THR A  68      18.043  19.002 -12.637  1.00 20.65           H  
ATOM   1046  N   ILE A  69      19.952  20.938 -11.222  1.00 16.02           N  
ANISOU 1046  N   ILE A  69     1762   2141   2185    446     24    314       N  
ATOM   1047  CA  ILE A  69      19.863  21.332  -9.820  1.00 16.78           C  
ANISOU 1047  CA  ILE A  69     1848   2262   2264    423      3    342       C  
ATOM   1048  C   ILE A  69      18.949  20.334  -9.105  1.00 18.35           C  
ANISOU 1048  C   ILE A  69     2080   2416   2475    428     -5    362       C  
ATOM   1049  O   ILE A  69      17.726  20.378  -9.260  1.00 19.06           O  
ANISOU 1049  O   ILE A  69     2203   2474   2564    403     -1    348       O  
ATOM   1050  CB  ILE A  69      19.322  22.764  -9.668  1.00 15.92           C  
ANISOU 1050  CB  ILE A  69     1742   2177   2129    371     -1    325       C  
ATOM   1051  CG1 ILE A  69      20.124  23.779 -10.492  1.00 17.16           C  
ANISOU 1051  CG1 ILE A  69     1875   2372   2275    358      6    306       C  
ATOM   1052  CG2 ILE A  69      19.327  23.179  -8.190  1.00 18.15           C  
ANISOU 1052  CG2 ILE A  69     2014   2491   2392    349    -22    351       C  
ATOM   1053  CD1 ILE A  69      21.607  23.767 -10.231  1.00 19.76           C  
ANISOU 1053  CD1 ILE A  69     2156   2752   2599    377      1    325       C  
ATOM   1054  H   ILE A  69      19.439  21.390 -11.744  1.00 19.22           H  
ATOM   1055  HA  ILE A  69      20.747  21.288  -9.424  1.00 20.13           H  
ATOM   1056  HB  ILE A  69      18.413  22.760 -10.007  1.00 19.10           H  
ATOM   1057 HG12 ILE A  69      19.991  23.585 -11.433  1.00 20.60           H  
ATOM   1058 HG13 ILE A  69      19.798  24.669 -10.286  1.00 20.60           H  
ATOM   1059 HG21 ILE A  69      19.215  24.141  -8.132  1.00 21.78           H  
ATOM   1060 HG22 ILE A  69      18.596  22.733  -7.734  1.00 21.78           H  
ATOM   1061 HG23 ILE A  69      20.172  22.920  -7.792  1.00 21.78           H  
ATOM   1062 HD11 ILE A  69      21.988  24.607 -10.533  1.00 23.71           H  
ATOM   1063 HD12 ILE A  69      21.760  23.658  -9.279  1.00 23.71           H  
ATOM   1064 HD13 ILE A  69      22.008  23.029 -10.717  1.00 23.71           H  
ATOM   1065  N   PHE A  70      19.543  19.436  -8.319  1.00 16.02           N  
ANISOU 1065  N   PHE A  70     1775   2121   2190    460    -18    397       N  
ATOM   1066  CA  PHE A  70      18.790  18.477  -7.524  1.00 19.29           C  
ANISOU 1066  CA  PHE A  70     2220   2497   2613    461    -29    424       C  
ATOM   1067  C   PHE A  70      18.593  19.002  -6.103  1.00 20.06           C  
ANISOU 1067  C   PHE A  70     2306   2633   2683    429    -49    452       C  
ATOM   1068  O   PHE A  70      19.531  19.520  -5.488  1.00 19.00           O  
ANISOU 1068  O   PHE A  70     2135   2551   2533    430    -60    468       O  
ATOM   1069  CB  PHE A  70      19.504  17.122  -7.434  1.00 19.72           C  
ANISOU 1069  CB  PHE A  70     2276   2523   2695    516    -35    451       C  
ATOM   1070  CG  PHE A  70      19.515  16.315  -8.711  1.00 17.09           C  
ANISOU 1070  CG  PHE A  70     1965   2138   2390    551    -16    424       C  
ATOM   1071  CD1 PHE A  70      18.446  15.495  -9.038  1.00 22.84           C  
ANISOU 1071  CD1 PHE A  70     2743   2800   3134    545    -12    417       C  
ATOM   1072  CD2 PHE A  70      20.618  16.323  -9.549  1.00 23.16           C  
ANISOU 1072  CD2 PHE A  70     2705   2927   3168    592     -4    407       C  
ATOM   1073  CE1 PHE A  70      18.465  14.730 -10.192  1.00 25.65           C  
ANISOU 1073  CE1 PHE A  70     3123   3109   3516    576      4    390       C  
ATOM   1074  CE2 PHE A  70      20.637  15.553 -10.697  1.00 23.63           C  
ANISOU 1074  CE2 PHE A  70     2786   2941   3251    626     14    379       C  
ATOM   1075  CZ  PHE A  70      19.560  14.757 -11.014  1.00 23.04           C  
ANISOU 1075  CZ  PHE A  70     2764   2797   3192    619     17    369       C  
ATOM   1076  H   PHE A  70      20.396  19.365  -8.233  1.00 19.22           H  
ATOM   1077  HA  PHE A  70      17.927  18.352  -7.948  1.00 23.15           H  
ATOM   1078  HB2 PHE A  70      20.427  17.278  -7.182  1.00 23.67           H  
ATOM   1079  HB3 PHE A  70      19.061  16.586  -6.757  1.00 23.67           H  
ATOM   1080  HD1 PHE A  70      17.708  15.457  -8.475  1.00 27.41           H  
ATOM   1081  HD2 PHE A  70      21.354  16.851  -9.337  1.00 27.79           H  
ATOM   1082  HE1 PHE A  70      17.733  14.199 -10.410  1.00 30.79           H  
ATOM   1083  HE2 PHE A  70      21.380  15.573 -11.257  1.00 28.36           H  
ATOM   1084  HZ  PHE A  70      19.576  14.237 -11.785  1.00 27.64           H  
ATOM   1085  N   ALA A  71      17.377  18.845  -5.580  1.00 16.10           N  
ANISOU 1085  N   ALA A  71     1834   2109   2174    398    -52    458       N  
ATOM   1086  CA  ALA A  71      17.105  19.113  -4.174  1.00 15.76           C  
ANISOU 1086  CA  ALA A  71     1785   2100   2105    370    -70    486       C  
ATOM   1087  C   ALA A  71      15.891  18.301  -3.742  1.00 16.26           C  
ANISOU 1087  C   ALA A  71     1884   2123   2170    352    -72    502       C  
ATOM   1088  O   ALA A  71      15.201  17.682  -4.559  1.00 18.00           O  
ANISOU 1088  O   ALA A  71     2135   2292   2411    356    -61    487       O  
ATOM   1089  CB  ALA A  71      16.879  20.607  -3.910  1.00 16.91           C  
ANISOU 1089  CB  ALA A  71     1914   2291   2218    330    -70    461       C  
ATOM   1090  H   ALA A  71      16.689  18.582  -6.025  1.00 19.32           H  
ATOM   1091  HA  ALA A  71      17.870  18.822  -3.653  1.00 18.92           H  
ATOM   1092  HB1 ALA A  71      16.767  20.745  -2.956  1.00 20.29           H  
ATOM   1093  HB2 ALA A  71      17.649  21.104  -4.228  1.00 20.29           H  
ATOM   1094  HB3 ALA A  71      16.082  20.894  -4.382  1.00 20.29           H  
ATOM   1095  N   ASP A  72      15.664  18.299  -2.433  1.00 16.90           N  
ANISOU 1095  N   ASP A  72     1961   2234   2227    331    -88    534       N  
ATOM   1096  CA  ASP A  72      14.441  17.805  -1.831  1.00 16.11           C  
ANISOU 1096  CA  ASP A  72     1888   2115   2116    300    -90    550       C  
ATOM   1097  C   ASP A  72      13.563  18.972  -1.398  1.00 15.98           C  
ANISOU 1097  C   ASP A  72     1865   2140   2066    256    -86    524       C  
ATOM   1098  O   ASP A  72      14.054  20.039  -1.014  1.00 16.62           O  
ANISOU 1098  O   ASP A  72     1920   2269   2124    248    -90    512       O  
ATOM   1099  CB  ASP A  72      14.716  16.951  -0.595  1.00 14.84           C  
ANISOU 1099  CB  ASP A  72     1728   1963   1948    303   -112    606       C  
ATOM   1100  CG  ASP A  72      15.388  15.646  -0.909  1.00 23.50           C  
ANISOU 1100  CG  ASP A  72     2840   3010   3080    348   -120    635       C  
ATOM   1101  OD1 ASP A  72      15.196  15.086  -2.007  1.00 23.00           O  
ANISOU 1101  OD1 ASP A  72     2800   2890   3047    368   -107    614       O  
ATOM   1102  OD2 ASP A  72      16.123  15.174  -0.023  1.00 33.39           O  
ANISOU 1102  OD2 ASP A  72     4080   4278   4328    366   -140    680       O  
ATOM   1103  H   ASP A  72      16.229  18.592  -1.855  1.00 20.28           H  
ATOM   1104  HA  ASP A  72      13.980  17.264  -2.491  1.00 19.33           H  
ATOM   1105  HB2 ASP A  72      15.294  17.446   0.006  1.00 17.81           H  
ATOM   1106  HB3 ASP A  72      13.874  16.754  -0.157  1.00 17.81           H  
ATOM   1107  N   TRP A  73      12.258  18.733  -1.426  1.00 15.70           N  
ANISOU 1107  N   TRP A  73     1853   2086   2027    229    -78    517       N  
ATOM   1108  CA  TRP A  73      11.272  19.644  -0.863  1.00 15.85           C  
ANISOU 1108  CA  TRP A  73     1867   2144   2013    191    -73    498       C  
ATOM   1109  C   TRP A  73      11.702  20.102   0.521  1.00 15.38           C  
ANISOU 1109  C   TRP A  73     1785   2143   1918    177    -88    520       C  
ATOM   1110  O   TRP A  73      11.977  19.285   1.405  1.00 18.35           O  
ANISOU 1110  O   TRP A  73     2161   2524   2287    177   -102    566       O  
ATOM   1111  CB  TRP A  73       9.935  18.905  -0.829  1.00 15.72           C  
ANISOU 1111  CB  TRP A  73     1875   2102   1996    165    -67    505       C  
ATOM   1112  CG  TRP A  73       8.718  19.669  -0.476  1.00 14.78           C  
ANISOU 1112  CG  TRP A  73     1751   2018   1847    130    -59    481       C  
ATOM   1113  CD1 TRP A  73       8.503  21.013  -0.587  1.00 17.64           C  
ANISOU 1113  CD1 TRP A  73     2097   2413   2191    124    -52    440       C  
ATOM   1114  CD2 TRP A  73       7.510  19.106   0.028  1.00 14.18           C  
ANISOU 1114  CD2 TRP A  73     1687   1946   1756     97    -56    497       C  
ATOM   1115  NE1 TRP A  73       7.236  21.322  -0.153  1.00 17.08           N  
ANISOU 1115  NE1 TRP A  73     2025   2368   2096     95    -45    427       N  
ATOM   1116  CE2 TRP A  73       6.604  20.165   0.223  1.00 14.89           C  
ANISOU 1116  CE2 TRP A  73     1762   2078   1818     76    -46    462       C  
ATOM   1117  CE3 TRP A  73       7.109  17.803   0.337  1.00 17.19           C  
ANISOU 1117  CE3 TRP A  73     2088   2299   2143     82    -62    538       C  
ATOM   1118  CZ2 TRP A  73       5.319  19.963   0.708  1.00 16.00           C  
ANISOU 1118  CZ2 TRP A  73     1903   2242   1936     42    -40    465       C  
ATOM   1119  CZ3 TRP A  73       5.842  17.605   0.826  1.00 15.75           C  
ANISOU 1119  CZ3 TRP A  73     1908   2137   1937     41    -57    544       C  
ATOM   1120  CH2 TRP A  73       4.957  18.680   1.004  1.00 14.34           C  
ANISOU 1120  CH2 TRP A  73     1710   2009   1730     22    -45    508       C  
ATOM   1121  H   TRP A  73      11.907  18.030  -1.774  1.00 18.84           H  
ATOM   1122  HA  TRP A  73      11.174  20.443  -1.404  1.00 19.02           H  
ATOM   1123  HB2 TRP A  73       9.782  18.534  -1.712  1.00 18.87           H  
ATOM   1124  HB3 TRP A  73      10.011  18.190  -0.177  1.00 18.87           H  
ATOM   1125  HD1 TRP A  73       9.123  21.628  -0.909  1.00 21.16           H  
ATOM   1126  HE1 TRP A  73       6.896  22.111  -0.123  1.00 20.50           H  
ATOM   1127  HE3 TRP A  73       7.688  17.086   0.213  1.00 20.62           H  
ATOM   1128  HZ2 TRP A  73       4.729  20.672   0.826  1.00 19.21           H  
ATOM   1129  HZ3 TRP A  73       5.565  16.745   1.043  1.00 18.90           H  
ATOM   1130  HH2 TRP A  73       4.103  18.514   1.332  1.00 17.21           H  
ATOM   1131  N   GLY A  74      11.792  21.414   0.697  1.00 17.31           N  
ANISOU 1131  N   GLY A  74     2011   2428   2138    165    -86    488       N  
ATOM   1132  CA  GLY A  74      12.176  21.995   1.958  1.00 18.20           C  
ANISOU 1132  CA  GLY A  74     2103   2598   2214    149   -100    501       C  
ATOM   1133  C   GLY A  74      13.631  22.402   2.058  1.00 23.26           C  
ANISOU 1133  C   GLY A  74     2720   3263   2855    167   -113    508       C  
ATOM   1134  O   GLY A  74      13.980  23.150   2.977  1.00 23.53           O  
ANISOU 1134  O   GLY A  74     2737   3348   2855    150   -124    507       O  
ATOM   1135  H   GLY A  74      11.630  21.992   0.081  1.00 20.77           H  
ATOM   1136  HA2 GLY A  74      11.637  22.787   2.111  1.00 21.84           H  
ATOM   1137  HA3 GLY A  74      12.000  21.352   2.662  1.00 21.84           H  
ATOM   1138  N   ASP A  75      14.486  21.927   1.150  1.00 16.83           N  
ANISOU 1138  N   ASP A  75     1902   2416   2074    200   -112    513       N  
ATOM   1139  CA  ASP A  75      15.885  22.321   1.152  1.00 18.61           C  
ANISOU 1139  CA  ASP A  75     2100   2670   2300    216   -123    519       C  
ATOM   1140  C   ASP A  75      16.056  23.791   0.772  1.00 19.97           C  
ANISOU 1140  C   ASP A  75     2262   2867   2458    198   -118    474       C  
ATOM   1141  O   ASP A  75      15.199  24.405   0.130  1.00 20.84           O  
ANISOU 1141  O   ASP A  75     2390   2957   2571    186   -104    436       O  
ATOM   1142  CB  ASP A  75      16.705  21.519   0.141  1.00 16.56           C  
ANISOU 1142  CB  ASP A  75     1838   2374   2080    259   -119    529       C  
ATOM   1143  CG  ASP A  75      16.887  20.081   0.523  1.00 20.70           C  
ANISOU 1143  CG  ASP A  75     2371   2873   2622    285   -129    576       C  
ATOM   1144  OD1 ASP A  75      16.610  19.692   1.676  1.00 20.27           O  
ANISOU 1144  OD1 ASP A  75     2319   2837   2546    269   -143    611       O  
ATOM   1145  OD2 ASP A  75      17.334  19.328  -0.359  1.00 19.93           O  
ANISOU 1145  OD2 ASP A  75     2279   2736   2560    322   -123    579       O  
ATOM   1146  H   ASP A  75      14.278  21.376   0.524  1.00 20.19           H  
ATOM   1147  HA  ASP A  75      16.214  22.161   2.050  1.00 22.33           H  
ATOM   1148  HB2 ASP A  75      16.254  21.542  -0.718  1.00 19.87           H  
ATOM   1149  HB3 ASP A  75      17.585  21.919   0.064  1.00 19.87           H  
ATOM   1150  N   THR A  76      17.210  24.337   1.140  1.00 18.13           N  
ANISOU 1150  N   THR A  76     2001   2676   2211    197   -131    481       N  
ATOM   1151  CA  THR A  76      17.682  25.612   0.623  1.00 15.18           C  
ANISOU 1151  CA  THR A  76     1618   2320   1831    182   -129    445       C  
ATOM   1152  C   THR A  76      18.649  25.311  -0.513  1.00 16.68           C  
ANISOU 1152  C   THR A  76     1793   2494   2052    212   -123    446       C  
ATOM   1153  O   THR A  76      19.501  24.426  -0.384  1.00 17.76           O  
ANISOU 1153  O   THR A  76     1909   2638   2200    241   -130    480       O  
ATOM   1154  CB  THR A  76      18.371  26.436   1.704  1.00 23.99           C  
ANISOU 1154  CB  THR A  76     2711   3495   2909    156   -149    449       C  
ATOM   1155  OG1 THR A  76      17.416  26.771   2.714  1.00 26.11           O  
ANISOU 1155  OG1 THR A  76     2995   3780   3146    129   -152    441       O  
ATOM   1156  CG2 THR A  76      18.936  27.707   1.111  1.00 23.97           C  
ANISOU 1156  CG2 THR A  76     2702   3505   2902    138   -149    415       C  
ATOM   1157  H   THR A  76      17.749  23.975   1.705  1.00 21.76           H  
ATOM   1158  HA  THR A  76      16.939  26.141   0.294  1.00 18.22           H  
ATOM   1159  HB  THR A  76      19.099  25.929   2.096  1.00 28.79           H  
ATOM   1160  HG1 THR A  76      16.775  27.196   2.374  1.00 31.33           H  
ATOM   1161 HG21 THR A  76      19.292  28.272   1.814  1.00 28.77           H  
ATOM   1162 HG22 THR A  76      19.648  27.494   0.487  1.00 28.77           H  
ATOM   1163 HG23 THR A  76      18.240  28.192   0.640  1.00 28.77           H  
ATOM   1164  N   ILE A  77      18.501  26.030  -1.621  1.00 16.60           N  
ANISOU 1164  N   ILE A  77     1792   2464   2052    206   -109    410       N  
ATOM   1165  CA  ILE A  77      19.345  25.875  -2.799  1.00 17.48           C  
ANISOU 1165  CA  ILE A  77     1888   2564   2187    230   -100    404       C  
ATOM   1166  C   ILE A  77      20.218  27.111  -2.918  1.00 21.19           C  
ANISOU 1166  C   ILE A  77     2338   3076   2640    204   -107    389       C  
ATOM   1167  O   ILE A  77      19.723  28.237  -2.802  1.00 18.97           O  
ANISOU 1167  O   ILE A  77     2071   2796   2339    170   -109    361       O  
ATOM   1168  CB  ILE A  77      18.499  25.687  -4.069  1.00 16.43           C  
ANISOU 1168  CB  ILE A  77     1785   2379   2080    239    -79    377       C  
ATOM   1169  CG1 ILE A  77      17.689  24.396  -3.971  1.00 18.77           C  
ANISOU 1169  CG1 ILE A  77     2103   2634   2394    260    -73    394       C  
ATOM   1170  CG2 ILE A  77      19.379  25.686  -5.299  1.00 17.88           C  
ANISOU 1170  CG2 ILE A  77     1953   2560   2282    258    -68    367       C  
ATOM   1171  CD1 ILE A  77      16.542  24.312  -4.952  1.00 19.40           C  
ANISOU 1171  CD1 ILE A  77     2215   2666   2489    258    -56    366       C  
ATOM   1172  H   ILE A  77      17.897  26.635  -1.714  1.00 19.92           H  
ATOM   1173  HA  ILE A  77      19.916  25.099  -2.688  1.00 20.97           H  
ATOM   1174  HB  ILE A  77      17.881  26.431  -4.145  1.00 19.72           H  
ATOM   1175 HG12 ILE A  77      18.279  23.646  -4.143  1.00 22.52           H  
ATOM   1176 HG13 ILE A  77      17.318  24.330  -3.078  1.00 22.52           H  
ATOM   1177 HG21 ILE A  77      19.574  26.602  -5.549  1.00 21.46           H  
ATOM   1178 HG22 ILE A  77      20.204  25.216  -5.096  1.00 21.46           H  
ATOM   1179 HG23 ILE A  77      18.912  25.238  -6.021  1.00 21.46           H  
ATOM   1180 HD11 ILE A  77      16.862  23.921  -5.780  1.00 23.28           H  
ATOM   1181 HD12 ILE A  77      15.842  23.757  -4.573  1.00 23.28           H  
ATOM   1182 HD13 ILE A  77      16.202  25.205  -5.118  1.00 23.28           H  
ATOM   1183  N   GLN A  78      21.505  26.909  -3.169  1.00 17.91           N  
ANISOU 1183  N   GLN A  78     1886   2690   2229    220   -111    406       N  
ATOM   1184  CA  GLN A  78      22.454  28.010  -3.263  1.00 15.66           C  
ANISOU 1184  CA  GLN A  78     1576   2449   1925    191   -119    396       C  
ATOM   1185  C   GLN A  78      23.323  27.786  -4.490  1.00 17.15           C  
ANISOU 1185  C   GLN A  78     1742   2642   2134    213   -105    393       C  
ATOM   1186  O   GLN A  78      24.159  26.879  -4.492  1.00 21.35           O  
ANISOU 1186  O   GLN A  78     2242   3193   2678    251   -105    419       O  
ATOM   1187  CB  GLN A  78      23.308  28.089  -2.005  1.00 21.61           C  
ANISOU 1187  CB  GLN A  78     2296   3260   2652    179   -143    424       C  
ATOM   1188  CG  GLN A  78      24.349  29.158  -2.048  1.00 26.64           C  
ANISOU 1188  CG  GLN A  78     2905   3948   3269    145   -154    417       C  
ATOM   1189  CD  GLN A  78      25.267  29.062  -0.868  1.00 46.59           C  
ANISOU 1189  CD  GLN A  78     5394   6536   5771    138   -178    449       C  
ATOM   1190  OE1 GLN A  78      24.873  29.370   0.252  1.00 33.25           O  
ANISOU 1190  OE1 GLN A  78     3717   4861   4056    113   -193    452       O  
ATOM   1191  NE2 GLN A  78      26.490  28.593  -1.098  1.00 34.01           N  
ANISOU 1191  NE2 GLN A  78     3753   4983   4184    161   -181    474       N  
ATOM   1192  H   GLN A  78      21.855  26.133  -3.290  1.00 21.49           H  
ATOM   1193  HA  GLN A  78      21.978  28.848  -3.373  1.00 18.79           H  
ATOM   1194  HB2 GLN A  78      22.730  28.270  -1.247  1.00 25.93           H  
ATOM   1195  HB3 GLN A  78      23.760  27.240  -1.882  1.00 25.93           H  
ATOM   1196  HG2 GLN A  78      24.877  29.062  -2.857  1.00 31.97           H  
ATOM   1197  HG3 GLN A  78      23.920  30.028  -2.034  1.00 31.97           H  
ATOM   1198 HE21 GLN A  78      26.719  28.363  -1.895  1.00 40.81           H  
ATOM   1199 HE22 GLN A  78      27.052  28.520  -0.451  1.00 40.81           H  
ATOM   1200  N   VAL A  79      23.143  28.610  -5.523  1.00 17.77           N  
ANISOU 1200  N   VAL A  79     1834   2705   2213    192    -93    363       N  
ATOM   1201  CA  VAL A  79      23.836  28.422  -6.796  1.00 14.19           C  
ANISOU 1201  CA  VAL A  79     1362   2256   1775    210    -76    357       C  
ATOM   1202  C   VAL A  79      24.773  29.603  -7.028  1.00 17.16           C  
ANISOU 1202  C   VAL A  79     1713   2679   2129    169    -84    350       C  
ATOM   1203  O   VAL A  79      24.321  30.743  -7.205  1.00 17.23           O  
ANISOU 1203  O   VAL A  79     1747   2675   2124    126    -88    328       O  
ATOM   1204  CB  VAL A  79      22.864  28.268  -7.977  1.00 15.97           C  
ANISOU 1204  CB  VAL A  79     1624   2424   2020    220    -55    330       C  
ATOM   1205  CG1 VAL A  79      23.629  27.881  -9.253  1.00 17.68           C  
ANISOU 1205  CG1 VAL A  79     1818   2649   2251    244    -36    324       C  
ATOM   1206  CG2 VAL A  79      21.785  27.252  -7.685  1.00 15.93           C  
ANISOU 1206  CG2 VAL A  79     1649   2371   2033    248    -51    334       C  
ATOM   1207  H   VAL A  79      22.618  29.291  -5.506  1.00 21.32           H  
ATOM   1208  HA  VAL A  79      24.377  27.620  -6.723  1.00 17.03           H  
ATOM   1209  HB  VAL A  79      22.430  29.123  -8.119  1.00 19.17           H  
ATOM   1210 HG11 VAL A  79      23.044  27.996 -10.019  1.00 21.22           H  
ATOM   1211 HG12 VAL A  79      24.407  28.453  -9.342  1.00 21.22           H  
ATOM   1212 HG13 VAL A  79      23.906  26.954  -9.186  1.00 21.22           H  
ATOM   1213 HG21 VAL A  79      21.310  27.052  -8.507  1.00 19.12           H  
ATOM   1214 HG22 VAL A  79      22.196  26.446  -7.336  1.00 19.12           H  
ATOM   1215 HG23 VAL A  79      21.172  27.622  -7.030  1.00 19.12           H  
ATOM   1216  N   THR A  80      26.076  29.328  -7.027  1.00 17.02           N  
ANISOU 1216  N   THR A  80     1644   2716   2108    182    -86    371       N  
ATOM   1217  CA  THR A  80      27.084  30.299  -7.436  1.00 19.13           C  
ANISOU 1217  CA  THR A  80     1880   3033   2355    143    -90    368       C  
ATOM   1218  C   THR A  80      27.171  30.241  -8.953  1.00 18.43           C  
ANISOU 1218  C   THR A  80     1793   2931   2280    154    -65    350       C  
ATOM   1219  O   THR A  80      27.395  29.163  -9.514  1.00 21.12           O  
ANISOU 1219  O   THR A  80     2117   3267   2642    206    -48    354       O  
ATOM   1220  CB  THR A  80      28.436  29.972  -6.809  1.00 18.88           C  
ANISOU 1220  CB  THR A  80     1787   3073   2312    154   -103    398       C  
ATOM   1221  OG1 THR A  80      28.314  29.981  -5.382  1.00 18.28           O  
ANISOU 1221  OG1 THR A  80     1714   3011   2222    143   -127    416       O  
ATOM   1222  CG2 THR A  80      29.495  30.984  -7.189  1.00 20.30           C  
ANISOU 1222  CG2 THR A  80     1932   3312   2468    106   -108    397       C  
ATOM   1223  H   THR A  80      26.407  28.570  -6.788  1.00 20.43           H  
ATOM   1224  HA  THR A  80      26.839  31.191  -7.145  1.00 22.95           H  
ATOM   1225  HB  THR A  80      28.716  29.100  -7.130  1.00 22.65           H  
ATOM   1226  HG1 THR A  80      27.984  29.255  -5.117  1.00 21.94           H  
ATOM   1227 HG21 THR A  80      30.337  30.758  -6.765  1.00 24.36           H  
ATOM   1228 HG22 THR A  80      29.618  30.989  -8.151  1.00 24.36           H  
ATOM   1229 HG23 THR A  80      29.225  31.870  -6.901  1.00 24.36           H  
ATOM   1230  N   VAL A  81      26.972  31.378  -9.616  1.00 16.86           N  
ANISOU 1230  N   VAL A  81     1614   2723   2067    106    -64    330       N  
ATOM   1231  CA  VAL A  81      27.069  31.466 -11.070  1.00 15.51           C  
ANISOU 1231  CA  VAL A  81     1445   2545   1902    107    -41    314       C  
ATOM   1232  C   VAL A  81      28.312  32.272 -11.423  1.00 20.18           C  
ANISOU 1232  C   VAL A  81     1994   3203   2470     66    -45    322       C  
ATOM   1233  O   VAL A  81      28.459  33.421 -10.991  1.00 20.18           O  
ANISOU 1233  O   VAL A  81     2004   3217   2448      8    -64    322       O  
ATOM   1234  CB  VAL A  81      25.813  32.098 -11.691  1.00 17.21           C  
ANISOU 1234  CB  VAL A  81     1719   2698   2121     85    -37    288       C  
ATOM   1235  CG1 VAL A  81      26.023  32.300 -13.186  1.00 17.50           C  
ANISOU 1235  CG1 VAL A  81     1755   2738   2158     78    -17    275       C  
ATOM   1236  CG2 VAL A  81      24.603  31.226 -11.430  1.00 21.58           C  
ANISOU 1236  CG2 VAL A  81     2308   3194   2698    124    -32    281       C  
ATOM   1237  H   VAL A  81      26.776  32.124  -9.235  1.00 20.23           H  
ATOM   1238  HA  VAL A  81      27.173  30.570 -11.428  1.00 18.61           H  
ATOM   1239  HB  VAL A  81      25.651  32.964 -11.286  1.00 20.65           H  
ATOM   1240 HG11 VAL A  81      25.158  32.359 -13.621  1.00 21.01           H  
ATOM   1241 HG12 VAL A  81      26.521  33.121 -13.326  1.00 21.01           H  
ATOM   1242 HG13 VAL A  81      26.521  31.547 -13.540  1.00 21.01           H  
ATOM   1243 HG21 VAL A  81      23.804  31.705 -11.700  1.00 25.90           H  
ATOM   1244 HG22 VAL A  81      24.687  30.407 -11.943  1.00 25.90           H  
ATOM   1245 HG23 VAL A  81      24.560  31.020 -10.483  1.00 25.90           H  
ATOM   1246  N   ILE A  82      29.204  31.672 -12.210  1.00 20.73           N  
ANISOU 1246  N   ILE A  82     2019   3314   2543     94    -26    327       N  
ATOM   1247  CA  ILE A  82      30.429  32.323 -12.659  1.00 17.31           C  
ANISOU 1247  CA  ILE A  82     1538   2952   2086     56    -25    336       C  
ATOM   1248  C   ILE A  82      30.306  32.581 -14.154  1.00 21.20           C  
ANISOU 1248  C   ILE A  82     2043   3435   2576     45     -1    318       C  
ATOM   1249  O   ILE A  82      30.170  31.645 -14.953  1.00 19.15           O  
ANISOU 1249  O   ILE A  82     1780   3163   2334     96     24    307       O  
ATOM   1250  CB  ILE A  82      31.676  31.487 -12.336  1.00 22.06           C  
ANISOU 1250  CB  ILE A  82     2069   3626   2688     97    -22    358       C  
ATOM   1251  CG1 ILE A  82      31.776  31.264 -10.828  1.00 26.91           C  
ANISOU 1251  CG1 ILE A  82     2673   4252   3301    104    -48    380       C  
ATOM   1252  CG2 ILE A  82      32.935  32.175 -12.844  1.00 24.17           C  
ANISOU 1252  CG2 ILE A  82     2281   3976   2927     54    -19    367       C  
ATOM   1253  CD1 ILE A  82      32.828  30.251 -10.438  1.00 26.46           C  
ANISOU 1253  CD1 ILE A  82     2551   4254   3250    159    -48    404       C  
ATOM   1254  H   ILE A  82      29.115  30.867 -12.502  1.00 24.88           H  
ATOM   1255  HA  ILE A  82      30.517  33.179 -12.210  1.00 20.77           H  
ATOM   1256  HB  ILE A  82      31.591  30.630 -12.783  1.00 26.48           H  
ATOM   1257 HG12 ILE A  82      32.001  32.106 -10.401  1.00 32.29           H  
ATOM   1258 HG13 ILE A  82      30.920  30.945 -10.501  1.00 32.29           H  
ATOM   1259 HG21 ILE A  82      32.761  32.542 -13.725  1.00 29.00           H  
ATOM   1260 HG22 ILE A  82      33.175  32.887 -12.231  1.00 29.00           H  
ATOM   1261 HG23 ILE A  82      33.652  31.524 -12.893  1.00 29.00           H  
ATOM   1262 HD11 ILE A  82      32.769  30.086  -9.484  1.00 31.76           H  
ATOM   1263 HD12 ILE A  82      32.670  29.428 -10.927  1.00 31.76           H  
ATOM   1264 HD13 ILE A  82      33.704  30.604 -10.659  1.00 31.76           H  
ATOM   1265  N   ASN A  83      30.357  33.854 -14.527  1.00 17.92           N  
ANISOU 1265  N   ASN A  83     1645   3026   2138    -23    -10    314       N  
ATOM   1266  CA  ASN A  83      30.200  34.250 -15.919  1.00 17.71           C  
ANISOU 1266  CA  ASN A  83     1634   2990   2104    -44      8    301       C  
ATOM   1267  C   ASN A  83      31.566  34.406 -16.567  1.00 18.56           C  
ANISOU 1267  C   ASN A  83     1679   3185   2189    -65     20    313       C  
ATOM   1268  O   ASN A  83      32.181  35.472 -16.484  1.00 19.32           O  
ANISOU 1268  O   ASN A  83     1763   3319   2258   -133      5    325       O  
ATOM   1269  CB  ASN A  83      29.425  35.555 -16.030  1.00 15.28           C  
ANISOU 1269  CB  ASN A  83     1385   2634   1785   -106    -10    293       C  
ATOM   1270  CG  ASN A  83      29.245  35.986 -17.469  1.00 15.62           C  
ANISOU 1270  CG  ASN A  83     1447   2668   1820   -130      6    283       C  
ATOM   1271  OD1 ASN A  83      29.629  35.263 -18.391  1.00 20.02           O  
ANISOU 1271  OD1 ASN A  83     1975   3255   2378    -99     33    279       O  
ATOM   1272  ND2 ASN A  83      28.627  37.143 -17.673  1.00 17.38           N  
ANISOU 1272  ND2 ASN A  83     1722   2849   2033   -182    -11    279       N  
ATOM   1273  H   ASN A  83      30.482  34.510 -13.986  1.00 21.50           H  
ATOM   1274  HA  ASN A  83      29.719  33.539 -16.371  1.00 21.25           H  
ATOM   1275  HB2 ASN A  83      28.546  35.439 -15.636  1.00 18.33           H  
ATOM   1276  HB3 ASN A  83      29.908  36.254 -15.562  1.00 18.33           H  
ATOM   1277 HD21 ASN A  83      28.502  37.429 -18.474  1.00 20.86           H  
ATOM   1278 HD22 ASN A  83      28.351  37.607 -17.003  1.00 20.86           H  
ATOM   1279  N   ASN A  84      32.021  33.359 -17.259  1.00 17.69           N  
ANISOU 1279  N   ASN A  84     1529   3105   2088     -9     49    308       N  
ATOM   1280  CA  ASN A  84      33.269  33.407 -18.007  1.00 17.39           C  
ANISOU 1280  CA  ASN A  84     1427   3154   2026    -22     67    315       C  
ATOM   1281  C   ASN A  84      33.047  33.598 -19.502  1.00 19.97           C  
ANISOU 1281  C   ASN A  84     1769   3476   2341    -36     92    299       C  
ATOM   1282  O   ASN A  84      33.915  33.233 -20.305  1.00 23.59           O  
ANISOU 1282  O   ASN A  84     2176   4002   2787    -21    117    297       O  
ATOM   1283  CB  ASN A  84      34.092  32.147 -17.772  1.00 25.78           C  
ANISOU 1283  CB  ASN A  84     2426   4267   3101     53     82    320       C  
ATOM   1284  CG  ASN A  84      34.695  32.106 -16.397  1.00 28.36           C  
ANISOU 1284  CG  ASN A  84     2718   4629   3427     54     56    345       C  
ATOM   1285  OD1 ASN A  84      34.894  33.142 -15.756  1.00 23.84           O  
ANISOU 1285  OD1 ASN A  84     2148   4073   2834    -12     30    359       O  
ATOM   1286  ND2 ASN A  84      34.990  30.905 -15.929  1.00 28.87           N  
ANISOU 1286  ND2 ASN A  84     2751   4705   3515    131     61    350       N  
ATOM   1287  H   ASN A  84      31.615  32.602 -17.306  1.00 21.23           H  
ATOM   1288  HA  ASN A  84      33.778  34.163 -17.675  1.00 20.87           H  
ATOM   1289  HB2 ASN A  84      33.520  31.370 -17.873  1.00 30.93           H  
ATOM   1290  HB3 ASN A  84      34.814  32.114 -18.419  1.00 30.93           H  
ATOM   1291 HD21 ASN A  84      35.338  30.822 -15.147  1.00 34.65           H  
ATOM   1292 HD22 ASN A  84      34.834  30.207 -16.407  1.00 34.65           H  
ATOM   1293  N   LEU A  85      31.910  34.165 -19.886  1.00 18.46           N  
ANISOU 1293  N   LEU A  85     1648   3212   2154    -63     85    287       N  
ATOM   1294  CA  LEU A  85      31.715  34.614 -21.253  1.00 19.36           C  
ANISOU 1294  CA  LEU A  85     1780   3325   2251    -94    102    277       C  
ATOM   1295  C   LEU A  85      32.669  35.765 -21.571  1.00 20.04           C  
ANISOU 1295  C   LEU A  85     1838   3478   2299   -174     94    297       C  
ATOM   1296  O   LEU A  85      33.258  36.386 -20.680  1.00 22.50           O  
ANISOU 1296  O   LEU A  85     2131   3820   2600   -215     71    316       O  
ATOM   1297  CB  LEU A  85      30.276  35.060 -21.460  1.00 18.69           C  
ANISOU 1297  CB  LEU A  85     1776   3148   2179   -107     91    264       C  
ATOM   1298  CG  LEU A  85      29.225  33.996 -21.159  1.00 18.60           C  
ANISOU 1298  CG  LEU A  85     1796   3069   2202    -38     96    245       C  
ATOM   1299  CD1 LEU A  85      27.852  34.608 -21.303  1.00 21.19           C  
ANISOU 1299  CD1 LEU A  85     2197   3317   2538    -60     81    235       C  
ATOM   1300  CD2 LEU A  85      29.365  32.781 -22.073  1.00 20.10           C  
ANISOU 1300  CD2 LEU A  85     1964   3273   2400     22    130    226       C  
ATOM   1301  H   LEU A  85      31.234  34.300 -19.372  1.00 22.15           H  
ATOM   1302  HA  LEU A  85      31.901  33.882 -21.862  1.00 23.23           H  
ATOM   1303  HB2 LEU A  85      30.102  35.816 -20.878  1.00 22.43           H  
ATOM   1304  HB3 LEU A  85      30.167  35.324 -22.387  1.00 22.43           H  
ATOM   1305  HG  LEU A  85      29.349  33.677 -20.252  1.00 22.32           H  
ATOM   1306 HD11 LEU A  85      27.186  33.904 -21.259  1.00 25.43           H  
ATOM   1307 HD12 LEU A  85      27.711  35.241 -20.581  1.00 25.43           H  
ATOM   1308 HD13 LEU A  85      27.797  35.064 -22.157  1.00 25.43           H  
ATOM   1309 HD21 LEU A  85      28.558  32.246 -22.012  1.00 24.12           H  
ATOM   1310 HD22 LEU A  85      29.493  33.085 -22.985  1.00 24.12           H  
ATOM   1311 HD23 LEU A  85      30.130  32.258 -21.788  1.00 24.12           H  
ATOM   1312  N   GLU A  86      32.767  36.092 -22.863  1.00 20.43           N  
ANISOU 1312  N   GLU A  86     1889   3548   2326   -203    113    293       N  
ATOM   1313  CA AGLU A  86      33.726  37.096 -23.304  0.58 24.16           C  
ANISOU 1313  CA AGLU A  86     2330   4090   2758   -281    109    315       C  
ATOM   1314  CA BGLU A  86      33.730  37.095 -23.311  0.42 24.71           C  
ANISOU 1314  CA BGLU A  86     2400   4160   2828   -281    110    315       C  
ATOM   1315  C   GLU A  86      33.183  38.516 -23.190  1.00 20.04           C  
ANISOU 1315  C   GLU A  86     1872   3517   2226   -362     77    328       C  
ATOM   1316  O   GLU A  86      33.902  39.418 -22.747  1.00 25.77           O  
ANISOU 1316  O   GLU A  86     2582   4280   2929   -429     56    350       O  
ATOM   1317  CB AGLU A  86      34.151  36.826 -24.752  0.58 25.05           C  
ANISOU 1317  CB AGLU A  86     2414   4258   2847   -280    144    307       C  
ATOM   1318  CB BGLU A  86      34.142  36.816 -24.755  0.42 26.48           C  
ANISOU 1318  CB BGLU A  86     2596   4438   3029   -280    145    307       C  
ATOM   1319  CG AGLU A  86      34.900  35.514 -24.950  0.58 36.90           C  
ANISOU 1319  CG AGLU A  86     3844   5822   4353   -204    178    292       C  
ATOM   1320  CG BGLU A  86      34.573  35.381 -24.995  0.42 29.28           C  
ANISOU 1320  CG BGLU A  86     2896   4833   3396   -192    179    286       C  
ATOM   1321  CD AGLU A  86      36.192  35.446 -24.157  0.58 50.46           C  
ANISOU 1321  CD AGLU A  86     5486   7626   6060   -206    173    312       C  
ATOM   1322  CD BGLU A  86      35.201  35.154 -26.358  0.42 70.12           C  
ANISOU 1322  CD BGLU A  86     8027  10077   8536   -193    216    277       C  
ATOM   1323  OE1AGLU A  86      36.746  36.515 -23.826  0.58 38.15           O  
ANISOU 1323  OE1AGLU A  86     3926   6093   4477   -282    148    335       O  
ATOM   1324  OE1BGLU A  86      35.312  36.118 -27.147  0.42 30.41           O  
ANISOU 1324  OE1BGLU A  86     3010   5071   3474   -268    214    290       O  
ATOM   1325  OE2AGLU A  86      36.651  34.323 -23.860  0.58 56.27           O  
ANISOU 1325  OE2AGLU A  86     6188   8377   6814   -128    186    299       O  
ATOM   1326  OE2BGLU A  86      35.589  33.999 -26.637  0.42 40.26           O  
ANISOU 1326  OE2BGLU A  86     4204   6328   4764   -119    245    256       O  
ATOM   1327  H  AGLU A  86      32.293  35.747 -23.493  0.58 24.52           H  
ATOM   1328  H  BGLU A  86      32.292  35.750 -23.494  0.42 24.52           H  
ATOM   1329  HA AGLU A  86      34.513  37.031 -22.742  0.58 28.99           H  
ATOM   1330  HA BGLU A  86      34.516  37.032 -22.747  0.42 29.65           H  
ATOM   1331  HB2AGLU A  86      33.357  36.798 -25.308  0.58 30.07           H  
ATOM   1332  HB2BGLU A  86      33.388  37.002 -25.337  0.42 31.78           H  
ATOM   1333  HB3AGLU A  86      34.735  37.544 -25.042  0.58 30.07           H  
ATOM   1334  HB3BGLU A  86      34.888  37.392 -24.985  0.42 31.78           H  
ATOM   1335  HG2AGLU A  86      34.333  34.781 -24.663  0.58 44.28           H  
ATOM   1336  HG2BGLU A  86      35.227  35.134 -24.322  0.42 35.14           H  
ATOM   1337  HG3AGLU A  86      35.120  35.415 -25.890  0.58 44.28           H  
ATOM   1338  HG3BGLU A  86      33.795  34.805 -24.927  0.42 35.14           H  
ATOM   1339  N   THR A  87      31.933  38.743 -23.597  1.00 22.98           N  
ANISOU 1339  N   THR A  87     2315   3804   2612   -358     71    315       N  
ATOM   1340  CA  THR A  87      31.373  40.091 -23.546  1.00 20.64           C  
ANISOU 1340  CA  THR A  87     2083   3454   2307   -428     39    326       C  
ATOM   1341  C   THR A  87      30.037  40.168 -22.823  1.00 21.71           C  
ANISOU 1341  C   THR A  87     2285   3490   2474   -399     18    311       C  
ATOM   1342  O   THR A  87      29.767  41.173 -22.158  1.00 21.61           O  
ANISOU 1342  O   THR A  87     2313   3438   2461   -444    -14    319       O  
ATOM   1343  CB  THR A  87      31.166  40.673 -24.961  1.00 24.16           C  
ANISOU 1343  CB  THR A  87     2555   3896   2728   -471     48    332       C  
ATOM   1344  OG1 THR A  87      30.209  39.873 -25.672  1.00 22.60           O  
ANISOU 1344  OG1 THR A  87     2382   3656   2547   -411     68    309       O  
ATOM   1345  CG2 THR A  87      32.478  40.735 -25.720  1.00 29.38           C  
ANISOU 1345  CG2 THR A  87     3150   4661   3351   -510     69    349       C  
ATOM   1346  H   THR A  87      31.400  38.141 -23.901  1.00 27.58           H  
ATOM   1347  HA  THR A  87      32.020  40.638 -23.074  1.00 24.77           H  
ATOM   1348  HB  THR A  87      30.831  41.581 -24.896  1.00 28.99           H  
ATOM   1349  HG1 THR A  87      29.434  40.170 -25.542  1.00 27.12           H  
ATOM   1350 HG21 THR A  87      32.935  41.568 -25.525  1.00 35.25           H  
ATOM   1351 HG22 THR A  87      33.048  39.994 -25.459  1.00 35.25           H  
ATOM   1352 HG23 THR A  87      32.312  40.683 -26.675  1.00 35.25           H  
ATOM   1353  N   ASN A  88      29.179  39.154 -22.972  1.00 20.07           N  
ANISOU 1353  N   ASN A  88     2091   3242   2293   -328     35    289       N  
ATOM   1354  CA  ASN A  88      27.823  39.237 -22.455  1.00 18.69           C  
ANISOU 1354  CA  ASN A  88     1978   2978   2145   -303     17    275       C  
ATOM   1355  C   ASN A  88      27.829  39.232 -20.933  1.00 16.77           C  
ANISOU 1355  C   ASN A  88     1733   2722   1917   -292     -4    275       C  
ATOM   1356  O   ASN A  88      28.538  38.440 -20.304  1.00 19.79           O  
ANISOU 1356  O   ASN A  88     2065   3152   2305   -260      6    278       O  
ATOM   1357  CB  ASN A  88      26.947  38.043 -22.866  1.00 17.36           C  
ANISOU 1357  CB  ASN A  88     1819   2776   2000   -231     40    252       C  
ATOM   1358  CG  ASN A  88      26.512  38.033 -24.326  1.00 14.69           C  
ANISOU 1358  CG  ASN A  88     1502   2430   1652   -236     57    244       C  
ATOM   1359  OD1 ASN A  88      25.692  37.180 -24.691  1.00 17.00           O  
ANISOU 1359  OD1 ASN A  88     1810   2688   1962   -185     71    225       O  
ATOM   1360  ND2 ASN A  88      27.040  38.931 -25.166  1.00 16.07           N  
ANISOU 1360  ND2 ASN A  88     1676   2635   1795   -297     54    261       N  
ATOM   1361  H   ASN A  88      29.361  38.412 -23.366  1.00 24.09           H  
ATOM   1362  HA  ASN A  88      27.447  40.054 -22.819  1.00 22.43           H  
ATOM   1363  HB2 ASN A  88      27.446  37.227 -22.707  1.00 20.83           H  
ATOM   1364  HB3 ASN A  88      26.143  38.051 -22.324  1.00 20.83           H  
ATOM   1365 HD21 ASN A  88      27.592  39.522 -24.874  1.00 19.28           H  
ATOM   1366  N   GLY A  89      26.979  40.055 -20.341  1.00 17.76           N  
ANISOU 1366  N   GLY A  89     1914   2784   2049   -313    -31    271       N  
ATOM   1367  CA  GLY A  89      26.512  39.779 -19.005  1.00 18.68           C  
ANISOU 1367  CA  GLY A  89     2040   2871   2185   -282    -45    262       C  
ATOM   1368  C   GLY A  89      25.676  38.513 -19.018  1.00 14.68           C  
ANISOU 1368  C   GLY A  89     1535   2336   1706   -208    -25    245       C  
ATOM   1369  O   GLY A  89      25.439  37.890 -20.054  1.00 15.57           O  
ANISOU 1369  O   GLY A  89     1645   2448   1823   -181     -2    238       O  
ATOM   1370  H   GLY A  89      26.662  40.773 -20.693  1.00 21.31           H  
ATOM   1371  HA2 GLY A  89      27.266  39.657 -18.407  1.00 22.41           H  
ATOM   1372  HA3 GLY A  89      25.970  40.516 -18.682  1.00 22.41           H  
ATOM   1373  N   THR A  90      25.240  38.107 -17.831  1.00 16.43           N  
ANISOU 1373  N   THR A  90     1762   2536   1944   -177    -35    240       N  
ATOM   1374  CA  THR A  90      24.258  37.041 -17.741  1.00 12.42           C  
ANISOU 1374  CA  THR A  90     1267   1990   1462   -116    -22    225       C  
ATOM   1375  C   THR A  90      23.445  37.223 -16.467  1.00 16.39           C  
ANISOU 1375  C   THR A  90     1799   2454   1976   -107    -42    218       C  
ATOM   1376  O   THR A  90      23.861  37.913 -15.533  1.00 18.65           O  
ANISOU 1376  O   THR A  90     2083   2754   2250   -138    -62    224       O  
ATOM   1377  CB  THR A  90      24.905  35.646 -17.763  1.00 16.96           C  
ANISOU 1377  CB  THR A  90     1792   2606   2048    -65      2    229       C  
ATOM   1378  OG1 THR A  90      23.909  34.662 -18.075  1.00 17.83           O  
ANISOU 1378  OG1 THR A  90     1922   2671   2180    -14     17    213       O  
ATOM   1379  CG2 THR A  90      25.531  35.309 -16.407  1.00 15.44           C  
ANISOU 1379  CG2 THR A  90     1566   2444   1857    -53     -9    242       C  
ATOM   1380  H   THR A  90      25.496  38.430 -17.076  1.00 19.71           H  
ATOM   1381  HA  THR A  90      23.661  37.105 -18.502  1.00 14.91           H  
ATOM   1382  HB  THR A  90      25.606  35.632 -18.433  1.00 20.36           H  
ATOM   1383  HG1 THR A  90      24.152  33.908 -17.794  1.00 21.39           H  
ATOM   1384 HG21 THR A  90      26.024  34.476 -16.467  1.00 18.53           H  
ATOM   1385 HG22 THR A  90      26.138  36.016 -16.137  1.00 18.53           H  
ATOM   1386 HG23 THR A  90      24.837  35.217 -15.735  1.00 18.53           H  
ATOM   1387  N   SER A  91      22.246  36.636 -16.481  1.00 17.87           N  
ANISOU 1387  N   SER A  91     2014   2593   2183    -68    -35    203       N  
ATOM   1388  CA ASER A  91      21.369  36.535 -15.319  0.49 20.57           C  
ANISOU 1388  CA ASER A  91     2378   2904   2535    -50    -48    195       C  
ATOM   1389  CA BSER A  91      21.394  36.519 -15.304  0.51 13.03           C  
ANISOU 1389  CA BSER A  91     1421   1949   1580    -49    -48    196       C  
ATOM   1390  C   SER A  91      20.655  35.198 -15.438  1.00 19.58           C  
ANISOU 1390  C   SER A  91     2250   2757   2431      4    -29    189       C  
ATOM   1391  O   SER A  91      20.092  34.897 -16.496  1.00 17.30           O  
ANISOU 1391  O   SER A  91     1977   2446   2150     18    -16    179       O  
ATOM   1392  CB ASER A  91      20.352  37.682 -15.252  0.49 19.00           C  
ANISOU 1392  CB ASER A  91     2230   2655   2332    -73    -67    180       C  
ATOM   1393  CB BSER A  91      20.405  37.679 -15.175  0.51 16.60           C  
ANISOU 1393  CB BSER A  91     1926   2354   2029    -74    -68    181       C  
ATOM   1394  OG ASER A  91      19.458  37.682 -16.355  0.49 24.72           O  
ANISOU 1394  OG ASER A  91     2984   3343   3066    -63    -59    169       O  
ATOM   1395  OG BSER A  91      21.061  38.868 -14.762  0.51 25.69           O  
ANISOU 1395  OG BSER A  91     3083   3518   3161   -124    -89    186       O  
ATOM   1396  H  ASER A  91      21.905  36.275 -17.183  0.49 21.44           H  
ATOM   1397  H  BSER A  91      21.895  36.289 -17.185  0.51 21.44           H  
ATOM   1398  HA ASER A  91      21.887  36.573 -14.499  0.49 24.69           H  
ATOM   1399  HA BSER A  91      21.932  36.526 -14.497  0.51 15.63           H  
ATOM   1400  HB2ASER A  91      19.836  37.589 -14.436  0.49 22.80           H  
ATOM   1401  HB2BSER A  91      19.988  37.834 -16.036  0.51 19.93           H  
ATOM   1402  HB3ASER A  91      20.835  38.523 -15.245  0.49 22.80           H  
ATOM   1403  HB3BSER A  91      19.732  37.447 -14.516  0.51 19.93           H  
ATOM   1404  HG ASER A  91      19.523  36.959 -16.778  0.49 29.66           H  
ATOM   1405  HG BSER A  91      20.531  39.352 -14.326  0.51 30.83           H  
ATOM   1406  N   ILE A  92      20.676  34.400 -14.384  1.00 15.29           N  
ANISOU 1406  N   ILE A  92     1690   2223   1896     32    -30    196       N  
ATOM   1407  CA  ILE A  92      20.106  33.064 -14.446  1.00 12.18           C  
ANISOU 1407  CA  ILE A  92     1295   1810   1524     79    -14    194       C  
ATOM   1408  C   ILE A  92      18.787  33.093 -13.692  1.00 14.53           C  
ANISOU 1408  C   ILE A  92     1626   2069   1828     86    -23    184       C  
ATOM   1409  O   ILE A  92      18.748  33.410 -12.496  1.00 13.12           O  
ANISOU 1409  O   ILE A  92     1447   1899   1641     77    -39    188       O  
ATOM   1410  CB  ILE A  92      21.062  31.996 -13.901  1.00 13.61           C  
ANISOU 1410  CB  ILE A  92     1434   2027   1711    110     -7    213       C  
ATOM   1411  CG1 ILE A  92      22.417  32.058 -14.621  1.00 17.42           C  
ANISOU 1411  CG1 ILE A  92     1877   2559   2184    103      2    221       C  
ATOM   1412  CG2 ILE A  92      20.428  30.628 -14.098  1.00 16.81           C  
ANISOU 1412  CG2 ILE A  92     1846   2402   2139    156      8    210       C  
ATOM   1413  CD1 ILE A  92      22.324  31.775 -16.116  1.00 20.50           C  
ANISOU 1413  CD1 ILE A  92     2272   2939   2579    113     24    208       C  
ATOM   1414  H   ILE A  92      21.014  34.612 -13.623  1.00 18.34           H  
ATOM   1415  HA  ILE A  92      19.921  32.834 -15.370  1.00 14.62           H  
ATOM   1416  HB  ILE A  92      21.217  32.160 -12.958  1.00 16.34           H  
ATOM   1417 HG12 ILE A  92      22.791  32.946 -14.509  1.00 20.91           H  
ATOM   1418 HG13 ILE A  92      23.010  31.397 -14.229  1.00 20.91           H  
ATOM   1419 HG21 ILE A  92      21.093  29.944 -13.923  1.00 20.17           H  
ATOM   1420 HG22 ILE A  92      19.686  30.532 -13.481  1.00 20.17           H  
ATOM   1421 HG23 ILE A  92      20.111  30.555 -15.011  1.00 20.17           H  
ATOM   1422 HD11 ILE A  92      23.199  31.902 -16.516  1.00 24.60           H  
ATOM   1423 HD12 ILE A  92      22.030  30.860 -16.247  1.00 24.60           H  
ATOM   1424 HD13 ILE A  92      21.686  32.388 -16.514  1.00 24.60           H  
ATOM   1425  N   HIS A  93      17.712  32.795 -14.412  1.00 14.02           N  
ANISOU 1425  N   HIS A  93     1587   1966   1774    101    -14    170       N  
ATOM   1426  CA  HIS A  93      16.362  32.746 -13.877  1.00 13.13           C  
ANISOU 1426  CA  HIS A  93     1502   1820   1668    109    -20    159       C  
ATOM   1427  C   HIS A  93      15.972  31.298 -13.583  1.00 12.37           C  
ANISOU 1427  C   HIS A  93     1399   1713   1588    144     -8    165       C  
ATOM   1428  O   HIS A  93      16.237  30.402 -14.390  1.00 13.45           O  
ANISOU 1428  O   HIS A  93     1528   1846   1736    165      8    167       O  
ATOM   1429  CB  HIS A  93      15.406  33.397 -14.877  1.00 14.80           C  
ANISOU 1429  CB  HIS A  93     1745   1999   1879     99    -20    140       C  
ATOM   1430  CG  HIS A  93      13.971  33.230 -14.519  1.00 13.66           C  
ANISOU 1430  CG  HIS A  93     1623   1825   1741    112    -23    128       C  
ATOM   1431  ND1 HIS A  93      13.465  33.604 -13.293  1.00 12.72           N  
ANISOU 1431  ND1 HIS A  93     1510   1708   1616    110    -35    125       N  
ATOM   1432  CD2 HIS A  93      12.937  32.710 -15.216  1.00 14.04           C  
ANISOU 1432  CD2 HIS A  93     1686   1848   1799    127    -14    118       C  
ATOM   1433  CE1 HIS A  93      12.176  33.321 -13.253  1.00 14.31           C  
ANISOU 1433  CE1 HIS A  93     1726   1888   1823    123    -33    114       C  
ATOM   1434  NE2 HIS A  93      11.832  32.777 -14.405  1.00 14.01           N  
ANISOU 1434  NE2 HIS A  93     1694   1833   1796    132    -21    110       N  
ATOM   1435  H   HIS A  93      17.745  32.609 -15.251  1.00 16.82           H  
ATOM   1436  HA  HIS A  93      16.304  33.225 -13.035  1.00 15.76           H  
ATOM   1437  HB2 HIS A  93      15.594  34.348 -14.917  1.00 17.76           H  
ATOM   1438  HB3 HIS A  93      15.544  32.995 -15.749  1.00 17.76           H  
ATOM   1439  HD1 HIS A  93      13.917  33.964 -12.656  1.00 15.27           H  
ATOM   1440  HD2 HIS A  93      12.969  32.371 -16.081  1.00 16.85           H  
ATOM   1441  HE1 HIS A  93      11.607  33.479 -12.534  1.00 17.17           H  
ATOM   1442  N   TRP A  94      15.377  31.071 -12.401  1.00 13.47           N  
ANISOU 1442  N   TRP A  94     1542   1850   1726    149    -16    170       N  
ATOM   1443  CA  TRP A  94      14.975  29.734 -11.918  1.00 12.64           C  
ANISOU 1443  CA  TRP A  94     1434   1735   1635    176     -9    182       C  
ATOM   1444  C   TRP A  94      13.491  29.617 -12.257  1.00 13.24           C  
ANISOU 1444  C   TRP A  94     1538   1777   1717    177     -5    165       C  
ATOM   1445  O   TRP A  94      12.611  29.957 -11.466  1.00 16.36           O  
ANISOU 1445  O   TRP A  94     1942   2170   2103    169    -13    160       O  
ATOM   1446  CB  TRP A  94      15.312  29.548 -10.415  1.00 13.22           C  
ANISOU 1446  CB  TRP A  94     1491   1833   1699    176    -20    201       C  
ATOM   1447  CG  TRP A  94      16.640  30.170 -10.197  1.00 14.74           C  
ANISOU 1447  CG  TRP A  94     1659   2063   1880    163    -29    211       C  
ATOM   1448  CD1 TRP A  94      16.876  31.457  -9.823  1.00 14.01           C  
ANISOU 1448  CD1 TRP A  94     1569   1987   1767    132    -43    202       C  
ATOM   1449  CD2 TRP A  94      17.923  29.588 -10.474  1.00 14.36           C  
ANISOU 1449  CD2 TRP A  94     1579   2040   1837    179    -23    228       C  
ATOM   1450  NE1 TRP A  94      18.225  31.715  -9.840  1.00 14.38           N  
ANISOU 1450  NE1 TRP A  94     1587   2070   1805    121    -48    215       N  
ATOM   1451  CE2 TRP A  94      18.890  30.587 -10.241  1.00 13.95           C  
ANISOU 1451  CE2 TRP A  94     1509   2026   1767    151    -35    231       C  
ATOM   1452  CE3 TRP A  94      18.350  28.322 -10.891  1.00 15.94           C  
ANISOU 1452  CE3 TRP A  94     1766   2235   2056    214    -10    240       C  
ATOM   1453  CZ2 TRP A  94      20.264  30.360 -10.410  1.00 17.75           C  
ANISOU 1453  CZ2 TRP A  94     1952   2546   2246    158    -33    247       C  
ATOM   1454  CZ3 TRP A  94      19.718  28.097 -11.059  1.00 18.22           C  
ANISOU 1454  CZ3 TRP A  94     2018   2559   2344    227     -8    254       C  
ATOM   1455  CH2 TRP A  94      20.658  29.110 -10.810  1.00 16.08           C  
ANISOU 1455  CH2 TRP A  94     1723   2334   2054    198    -19    258       C  
ATOM   1456  H   TRP A  94      15.190  31.697 -11.842  1.00 16.17           H  
ATOM   1457  HA  TRP A  94      15.455  29.027 -12.376  1.00 15.17           H  
ATOM   1458  HB2 TRP A  94      14.650  29.991  -9.862  1.00 15.86           H  
ATOM   1459  HB3 TRP A  94      15.353  28.605 -10.192  1.00 15.86           H  
ATOM   1460  HD1 TRP A  94      16.219  32.073  -9.591  1.00 16.81           H  
ATOM   1461  HE1 TRP A  94      18.592  32.465  -9.632  1.00 17.25           H  
ATOM   1462  HE3 TRP A  94      17.735  27.644 -11.053  1.00 19.13           H  
ATOM   1463  HZ2 TRP A  94      20.886  31.034 -10.255  1.00 21.30           H  
ATOM   1464  HZ3 TRP A  94      20.012  27.261 -11.340  1.00 21.86           H  
ATOM   1465  HH2 TRP A  94      21.563  28.930 -10.920  1.00 19.30           H  
ATOM   1466  N   HIS A  95      13.225  29.133 -13.461  1.00 11.46           N  
ANISOU 1466  N   HIS A  95     1322   1530   1503    186      8    155       N  
ATOM   1467  CA  HIS A  95      11.893  29.208 -14.028  1.00 13.17           C  
ANISOU 1467  CA  HIS A  95     1562   1719   1722    182     10    138       C  
ATOM   1468  C   HIS A  95      10.957  28.240 -13.333  1.00 17.89           C  
ANISOU 1468  C   HIS A  95     2166   2305   2328    191     12    144       C  
ATOM   1469  O   HIS A  95      11.114  27.020 -13.440  1.00 20.24           O  
ANISOU 1469  O   HIS A  95     2462   2589   2639    207     20    155       O  
ATOM   1470  CB  HIS A  95      11.932  28.896 -15.521  1.00 13.67           C  
ANISOU 1470  CB  HIS A  95     1634   1767   1793    187     22    126       C  
ATOM   1471  CG  HIS A  95      10.580  28.888 -16.165  1.00 16.68           C  
ANISOU 1471  CG  HIS A  95     2036   2124   2176    183     23    110       C  
ATOM   1472  ND1 HIS A  95      10.302  29.592 -17.315  1.00 16.49           N  
ANISOU 1472  ND1 HIS A  95     2026   2094   2147    172     23     95       N  
ATOM   1473  CD2 HIS A  95       9.420  28.286 -15.807  1.00 19.58           C  
ANISOU 1473  CD2 HIS A  95     2413   2477   2548    185     23    108       C  
ATOM   1474  CE1 HIS A  95       9.035  29.421 -17.644  1.00 14.12           C  
ANISOU 1474  CE1 HIS A  95     1740   1777   1848    171     22     84       C  
ATOM   1475  NE2 HIS A  95       8.474  28.637 -16.741  1.00 19.29           N  
ANISOU 1475  NE2 HIS A  95     2393   2428   2510    177     22     91       N  
ATOM   1476  H   HIS A  95      13.803  28.753 -13.972  1.00 13.75           H  
ATOM   1477  HA  HIS A  95      11.559  30.109 -13.898  1.00 15.80           H  
ATOM   1478  HB2 HIS A  95      12.470  29.569 -15.967  1.00 16.40           H  
ATOM   1479  HB3 HIS A  95      12.326  28.019 -15.648  1.00 16.40           H  
ATOM   1480  HD2 HIS A  95       9.288  27.738 -15.067  1.00 23.49           H  
ATOM   1481  HE1 HIS A  95       8.610  29.789 -18.384  1.00 16.94           H  
ATOM   1482  HE2 HIS A  95       7.651  28.386 -16.738  1.00 23.15           H  
ATOM   1483  N   GLY A  96       9.922  28.781 -12.721  1.00 15.08           N  
ANISOU 1483  N   GLY A  96     1817   1950   1961    181      4    136       N  
ATOM   1484  CA  GLY A  96       8.956  27.977 -12.022  1.00 18.32           C  
ANISOU 1484  CA  GLY A  96     2230   2356   2373    182      5    143       C  
ATOM   1485  C   GLY A  96       9.088  28.023 -10.521  1.00 23.67           C  
ANISOU 1485  C   GLY A  96     2896   3058   3038    178     -3    158       C  
ATOM   1486  O   GLY A  96       8.155  27.611  -9.822  1.00 19.34           O  
ANISOU 1486  O   GLY A  96     2350   2515   2485    174     -3    163       O  
ATOM   1487  H   GLY A  96       9.760  29.626 -12.700  1.00 18.09           H  
ATOM   1488  HA2 GLY A  96       8.065  28.284 -12.254  1.00 21.98           H  
ATOM   1489  HA3 GLY A  96       9.055  27.054 -12.303  1.00 21.98           H  
ATOM   1490  N   LEU A  97      10.210  28.515 -10.005  1.00 15.98           N  
ANISOU 1490  N   LEU A  97     1909   2106   2056    177    -10    167       N  
ATOM   1491  CA  LEU A  97      10.396  28.682  -8.563  1.00 14.69           C  
ANISOU 1491  CA  LEU A  97     1734   1972   1876    171    -20    180       C  
ATOM   1492  C   LEU A  97       9.822  30.042  -8.154  1.00 17.89           C  
ANISOU 1492  C   LEU A  97     2146   2389   2262    157    -28    156       C  
ATOM   1493  O   LEU A  97      10.176  31.079  -8.720  1.00 22.50           O  
ANISOU 1493  O   LEU A  97     2737   2969   2844    150    -34    140       O  
ATOM   1494  CB  LEU A  97      11.874  28.543  -8.194  1.00 15.86           C  
ANISOU 1494  CB  LEU A  97     1862   2140   2023    175    -25    201       C  
ATOM   1495  CG  LEU A  97      12.516  27.242  -8.705  1.00 21.85           C  
ANISOU 1495  CG  LEU A  97     2614   2883   2803    197    -16    221       C  
ATOM   1496  CD1 LEU A  97      13.852  27.013  -8.018  1.00 37.52           C  
ANISOU 1496  CD1 LEU A  97     4574   4896   4784    205    -24    246       C  
ATOM   1497  CD2 LEU A  97      11.615  26.019  -8.534  1.00 29.23           C  
ANISOU 1497  CD2 LEU A  97     3562   3794   3749    205    -10    233       C  
ATOM   1498  H   LEU A  97      10.887  28.763 -10.472  1.00 19.17           H  
ATOM   1499  HA  LEU A  97       9.933  27.991  -8.062  1.00 17.63           H  
ATOM   1500  HB2 LEU A  97      12.362  29.287  -8.579  1.00 19.03           H  
ATOM   1501  HB3 LEU A  97      11.957  28.556  -7.228  1.00 19.03           H  
ATOM   1502  HG  LEU A  97      12.655  27.344  -9.660  1.00 26.22           H  
ATOM   1503 HD11 LEU A  97      14.135  26.099  -8.173  1.00 45.02           H  
ATOM   1504 HD12 LEU A  97      14.505  27.629  -8.385  1.00 45.02           H  
ATOM   1505 HD13 LEU A  97      13.748  27.170  -7.066  1.00 45.02           H  
ATOM   1506 HD21 LEU A  97      12.038  25.254  -8.954  1.00 35.07           H  
ATOM   1507 HD22 LEU A  97      11.490  25.849  -7.587  1.00 35.07           H  
ATOM   1508 HD23 LEU A  97      10.759  26.196  -8.954  1.00 35.07           H  
HETATM 1509  CE1 OHI A  98       5.269  29.217  -9.015  1.00 55.44           C  
ANISOU 1509  CE1 OHI A  98     6925   7116   7022    158     -9    118       C  
HETATM 1510  ND1 OHI A  98       6.282  30.139  -8.455  1.00 32.41           N  
ANISOU 1510  ND1 OHI A  98     4005   4213   4095    158    -18    116       N  
HETATM 1511  NE2 OHI A  98       4.455  28.654  -7.878  1.00 32.32           N  
ANISOU 1511  NE2 OHI A  98     3987   4215   4080    150     -6    128       N  
HETATM 1512  CD2 OHI A  98       4.930  29.183  -6.795  1.00 29.33           C  
ANISOU 1512  CD2 OHI A  98     3599   3861   3683    148    -13    130       C  
HETATM 1513  CG  OHI A  98       6.090  30.136  -7.165  1.00 26.48           C  
ANISOU 1513  CG  OHI A  98     3244   3491   3325    152    -21    121       C  
HETATM 1514  CB  OHI A  98       6.870  30.893  -6.162  1.00 33.09           C  
ANISOU 1514  CB  OHI A  98     4076   4352   4143    147    -31    120       C  
HETATM 1515  CA  OHI A  98       8.174  31.231  -6.906  1.00 20.59           C  
ANISOU 1515  CA  OHI A  98     2497   2754   2573    147    -36    125       C  
HETATM 1516  N   OHI A  98       8.936  30.043  -7.164  1.00 15.65           N  
ANISOU 1516  N   OHI A  98     1861   2121   1963    152    -30    153       N  
HETATM 1517  C   OHI A  98       8.922  32.310  -6.151  1.00 18.91           C  
ANISOU 1517  C   OHI A  98     2282   2561   2341    136    -49    116       C  
HETATM 1518  O   OHI A  98       8.471  33.446  -6.057  1.00 15.13           O  
ANISOU 1518  O   OHI A  98     1816   2080   1851    133    -56     89       O  
HETATM 1519  O12 OHI A  98       5.160  28.984 -10.211  1.00 42.97           O  
ANISOU 1519  O12 OHI A  98     5355   5512   5458    161     -5    113       O  
HETATM 1520  HD2 OHI A  98       4.591  29.009  -5.769  1.00 35.19           H  
HETATM 1521  HB1 OHI A  98       7.083  30.278  -5.243  1.00 39.70           H  
HETATM 1522  HB2 OHI A  98       6.339  31.833  -5.839  1.00 39.70           H  
HETATM 1523  HA  OHI A  98       7.904  31.728  -7.889  1.00 24.71           H  
HETATM 1524  H   OHI A  98       8.598  29.276  -6.617  1.00 18.78           H  
ATOM   1525  N   GLN A  99      10.093  31.972  -5.623  1.00 17.13           N  
ANISOU 1525  N   GLN A  99     2042   2354   2112    130    -54    139       N  
ATOM   1526  CA  GLN A  99      10.931  32.966  -4.953  1.00 12.48           C  
ANISOU 1526  CA  GLN A  99     1452   1787   1504    114    -68    132       C  
ATOM   1527  C   GLN A  99      10.139  33.732  -3.884  1.00 14.10           C  
ANISOU 1527  C   GLN A  99     1665   2010   1682    108    -74    108       C  
ATOM   1528  O   GLN A  99      10.219  34.959  -3.811  1.00 14.62           O  
ANISOU 1528  O   GLN A  99     1746   2071   1737     98    -85     82       O  
ATOM   1529  CB  GLN A  99      11.513  33.962  -5.967  1.00 13.65           C  
ANISOU 1529  CB  GLN A  99     1613   1915   1660    105    -74    117       C  
ATOM   1530  CG  GLN A  99      12.397  33.333  -7.049  1.00 15.01           C  
ANISOU 1530  CG  GLN A  99     1775   2077   1853    110    -67    137       C  
ATOM   1531  CD  GLN A  99      13.731  32.832  -6.527  1.00 16.57           C  
ANISOU 1531  CD  GLN A  99     1946   2305   2046    106    -71    164       C  
ATOM   1532  OE1 GLN A  99      14.124  33.120  -5.390  1.00 15.90           O  
ANISOU 1532  OE1 GLN A  99     1850   2249   1940     94    -83    169       O  
ATOM   1533  NE2 GLN A  99      14.453  32.093  -7.372  1.00 16.45           N  
ANISOU 1533  NE2 GLN A  99     1916   2286   2049    118    -62    181       N  
ATOM   1534  H   GLN A  99      10.425  31.179  -5.637  1.00 20.55           H  
ATOM   1535  HA  GLN A  99      11.666  32.504  -4.521  1.00 14.98           H  
ATOM   1536  HB2 GLN A  99      10.779  34.412  -6.414  1.00 16.39           H  
ATOM   1537  HB3 GLN A  99      12.055  34.609  -5.487  1.00 16.39           H  
ATOM   1538  HG2 GLN A  99      11.927  32.578  -7.436  1.00 18.02           H  
ATOM   1539  HG3 GLN A  99      12.576  33.998  -7.732  1.00 18.02           H  
ATOM   1540 HE21 GLN A  99      14.154  31.926  -8.161  1.00 19.74           H  
ATOM   1541 HE22 GLN A  99      15.217  31.784  -7.127  1.00 19.74           H  
ATOM   1542  N   LYS A 100       9.387  33.014  -3.051  1.00 14.64           N  
ANISOU 1542  N   LYS A 100     1723   2098   1739    112    -68    117       N  
ATOM   1543  CA  LYS A 100       8.525  33.652  -2.062  1.00 16.94           C  
ANISOU 1543  CA  LYS A 100     2019   2414   2004    109    -69     92       C  
ATOM   1544  C   LYS A 100       9.384  34.367  -1.025  1.00 18.39           C  
ANISOU 1544  C   LYS A 100     2200   2626   2161     92    -84     87       C  
ATOM   1545  O   LYS A 100      10.150  33.730  -0.296  1.00 17.78           O  
ANISOU 1545  O   LYS A 100     2106   2578   2073     82    -88    116       O  
ATOM   1546  CB  LYS A 100       7.616  32.618  -1.405  1.00 25.54           C  
ANISOU 1546  CB  LYS A 100     3095   3526   3084    112    -58    107       C  
ATOM   1547  CG  LYS A 100       6.702  33.164  -0.304  1.00 34.87           C  
ANISOU 1547  CG  LYS A 100     4274   4742   4232    110    -56     82       C  
ATOM   1548  CD  LYS A 100       5.451  33.818  -0.869  1.00 48.88           C  
ANISOU 1548  CD  LYS A 100     6059   6502   6012    126    -49     46       C  
ATOM   1549  CE  LYS A 100       4.501  32.796  -1.484  1.00 60.35           C  
ANISOU 1549  CE  LYS A 100     7502   7946   7481    132    -36     61       C  
ATOM   1550  NZ  LYS A 100       4.141  31.698  -0.543  1.00 69.44           N  
ANISOU 1550  NZ  LYS A 100     8636   9134   8615    119    -28     90       N  
ATOM   1551  H   LYS A 100       9.358  32.154  -3.040  1.00 17.56           H  
ATOM   1552  HA  LYS A 100       7.958  34.308  -2.497  1.00 20.33           H  
ATOM   1553  HB2 LYS A 100       7.048  32.230  -2.088  1.00 30.65           H  
ATOM   1554  HB3 LYS A 100       8.172  31.930  -1.006  1.00 30.65           H  
ATOM   1555  HG2 LYS A 100       6.427  32.434   0.273  1.00 41.84           H  
ATOM   1556  HG3 LYS A 100       7.185  33.829   0.210  1.00 41.84           H  
ATOM   1557  HD2 LYS A 100       4.981  34.277  -0.156  1.00 58.66           H  
ATOM   1558  HD3 LYS A 100       5.705  34.449  -1.560  1.00 58.66           H  
ATOM   1559  HE2 LYS A 100       3.683  33.245  -1.747  1.00 72.42           H  
ATOM   1560  HE3 LYS A 100       4.925  32.398  -2.260  1.00 72.42           H  
ATOM   1561  HZ1 LYS A 100       3.552  31.151  -0.924  1.00 83.33           H  
ATOM   1562  HZ2 LYS A 100       4.868  31.233  -0.325  1.00 83.33           H  
ATOM   1563  HZ3 LYS A 100       3.783  32.037   0.198  1.00 83.33           H  
ATOM   1564  N   GLY A 101       9.255  35.694  -0.975  1.00 14.84           N  
ANISOU 1564  N   GLY A 101     1770   2167   1700     88    -93     50       N  
ATOM   1565  CA  GLY A 101      10.094  36.536  -0.154  1.00 15.83           C  
ANISOU 1565  CA  GLY A 101     1900   2313   1800     66   -109     38       C  
ATOM   1566  C   GLY A 101      11.532  36.668  -0.593  1.00 18.64           C  
ANISOU 1566  C   GLY A 101     2252   2665   2166     48   -120     58       C  
ATOM   1567  O   GLY A 101      12.328  37.243   0.157  1.00 17.13           O  
ANISOU 1567  O   GLY A 101     2060   2497   1952     25   -135     54       O  
ATOM   1568  H   GLY A 101       8.670  36.136  -1.424  1.00 17.80           H  
ATOM   1569  HA2 GLY A 101       9.711  37.428  -0.140  1.00 18.99           H  
ATOM   1570  HA3 GLY A 101      10.096  36.180   0.748  1.00 18.99           H  
ATOM   1571  N   THR A 102      11.892  36.180  -1.784  1.00 15.59           N  
ANISOU 1571  N   THR A 102     1861   2252   1809     56   -114     78       N  
ATOM   1572  CA  THR A 102      13.262  36.236  -2.289  1.00 12.60           C  
ANISOU 1572  CA  THR A 102     1472   1876   1439     40   -122     98       C  
ATOM   1573  C   THR A 102      13.302  36.803  -3.708  1.00 11.45           C  
ANISOU 1573  C   THR A 102     1345   1689   1316     40   -121     87       C  
ATOM   1574  O   THR A 102      14.078  36.345  -4.556  1.00 14.62           O  
ANISOU 1574  O   THR A 102     1733   2088   1735     40   -117    108       O  
ATOM   1575  CB  THR A 102      13.930  34.858  -2.247  1.00 13.91           C  
ANISOU 1575  CB  THR A 102     1606   2063   1615     50   -116    140       C  
ATOM   1576  OG1 THR A 102      13.160  33.896  -2.979  1.00 14.27           O  
ANISOU 1576  OG1 THR A 102     1653   2084   1686     75    -99    149       O  
ATOM   1577  CG2 THR A 102      14.079  34.358  -0.807  1.00 17.21           C  
ANISOU 1577  CG2 THR A 102     2006   2525   2007     44   -122    157       C  
ATOM   1578  H   THR A 102      11.342  35.804  -2.328  1.00 18.70           H  
ATOM   1579  HA  THR A 102      13.765  36.835  -1.714  1.00 15.12           H  
ATOM   1580  HB  THR A 102      14.810  34.943  -2.646  1.00 16.69           H  
ATOM   1581  HG1 THR A 102      13.514  33.136  -2.916  1.00 17.13           H  
ATOM   1582 HG21 THR A 102      14.518  33.493  -0.800  1.00 20.65           H  
ATOM   1583 HG22 THR A 102      14.610  34.985  -0.291  1.00 20.65           H  
ATOM   1584 HG23 THR A 102      13.205  34.270  -0.394  1.00 20.65           H  
ATOM   1585  N   ASN A 103      12.466  37.822  -3.974  1.00 15.05           N  
ANISOU 1585  N   ASN A 103     1833   2116   1771     41   -125     53       N  
ATOM   1586  CA  ASN A 103      12.388  38.451  -5.293  1.00 14.90           C  
ANISOU 1586  CA  ASN A 103     1835   2056   1771     40   -127     44       C  
ATOM   1587  C   ASN A 103      13.763  38.768  -5.864  1.00 14.07           C  
ANISOU 1587  C   ASN A 103     1724   1956   1668     13   -135     60       C  
ATOM   1588  O   ASN A 103      13.977  38.626  -7.071  1.00 12.32           O  
ANISOU 1588  O   ASN A 103     1503   1715   1463     14   -129     70       O  
ATOM   1589  CB  ASN A 103      11.533  39.733  -5.204  1.00 12.53           C  
ANISOU 1589  CB  ASN A 103     1572   1726   1463     43   -138      5       C  
ATOM   1590  CG  ASN A 103      11.336  40.447  -6.560  1.00 12.00           C  
ANISOU 1590  CG  ASN A 103     1532   1614   1414     43   -142     -3       C  
ATOM   1591  OD1 ASN A 103      11.562  41.653  -6.654  1.00 14.02           O  
ANISOU 1591  OD1 ASN A 103     1818   1845   1664     25   -160    -20       O  
ATOM   1592  ND2 ASN A 103      10.862  39.724  -7.576  1.00 12.84           N  
ANISOU 1592  ND2 ASN A 103     1630   1707   1540     62   -128     10       N  
ATOM   1593  H   ASN A 103      11.928  38.169  -3.400  1.00 18.06           H  
ATOM   1594  HA  ASN A 103      11.959  37.831  -5.903  1.00 17.88           H  
ATOM   1595  HB2 ASN A 103      10.655  39.500  -4.863  1.00 15.04           H  
ATOM   1596  HB3 ASN A 103      11.968  40.357  -4.602  1.00 15.04           H  
ATOM   1597 HD21 ASN A 103      10.741  40.090  -8.344  1.00 15.40           H  
ATOM   1598 HD22 ASN A 103      10.678  38.892  -7.462  1.00 15.40           H  
ATOM   1599  N   LEU A 104      14.711  39.194  -5.028  1.00 13.63           N  
ANISOU 1599  N   LEU A 104     1660   1928   1591    -15   -149     64       N  
ATOM   1600  CA  LEU A 104      15.996  39.641  -5.564  1.00 14.81           C  
ANISOU 1600  CA  LEU A 104     1803   2086   1739    -48   -159     78       C  
ATOM   1601  C   LEU A 104      16.902  38.493  -5.993  1.00 14.14           C  
ANISOU 1601  C   LEU A 104     1676   2031   1665    -40   -146    114       C  
ATOM   1602  O   LEU A 104      18.031  38.751  -6.434  1.00 15.83           O  
ANISOU 1602  O   LEU A 104     1875   2262   1876    -65   -152    128       O  
ATOM   1603  CB  LEU A 104      16.718  40.524  -4.547  1.00 14.89           C  
ANISOU 1603  CB  LEU A 104     1818   2118   1722    -84   -180     69       C  
ATOM   1604  CG  LEU A 104      16.403  42.011  -4.726  1.00 15.24           C  
ANISOU 1604  CG  LEU A 104     1911   2121   1760   -107   -198     37       C  
ATOM   1605  CD1 LEU A 104      14.935  42.323  -4.573  1.00 14.46           C  
ANISOU 1605  CD1 LEU A 104     1844   1986   1666    -75   -194      5       C  
ATOM   1606  CD2 LEU A 104      17.213  42.842  -3.730  1.00 17.51           C  
ANISOU 1606  CD2 LEU A 104     2204   2430   2018   -149   -220     27       C  
ATOM   1607  H   LEU A 104      14.636  39.232  -4.172  1.00 16.36           H  
ATOM   1608  HA  LEU A 104      15.824  40.181  -6.351  1.00 17.77           H  
ATOM   1609  HB2 LEU A 104      16.444  40.264  -3.653  1.00 17.87           H  
ATOM   1610  HB3 LEU A 104      17.675  40.404  -4.648  1.00 17.87           H  
ATOM   1611  HG  LEU A 104      16.649  42.251  -5.633  1.00 18.29           H  
ATOM   1612 HD11 LEU A 104      14.782  43.247  -4.824  1.00 17.36           H  
ATOM   1613 HD12 LEU A 104      14.425  41.734  -5.152  1.00 17.36           H  
ATOM   1614 HD13 LEU A 104      14.677  42.183  -3.649  1.00 17.36           H  
ATOM   1615 HD21 LEU A 104      17.237  43.763  -4.034  1.00 21.01           H  
ATOM   1616 HD22 LEU A 104      16.789  42.792  -2.859  1.00 21.01           H  
ATOM   1617 HD23 LEU A 104      18.114  42.486  -3.680  1.00 21.01           H  
ATOM   1618  N   HIS A 105      16.425  37.252  -5.890  1.00 13.95           N  
ANISOU 1618  N   HIS A 105     1634   2012   1653     -6   -130    127       N  
ATOM   1619  CA  HIS A 105      17.093  36.067  -6.411  1.00 12.92           C  
ANISOU 1619  CA  HIS A 105     1471   1900   1539     13   -117    156       C  
ATOM   1620  C   HIS A 105      16.400  35.480  -7.633  1.00 15.47           C  
ANISOU 1620  C   HIS A 105     1804   2188   1887     38    -98    154       C  
ATOM   1621  O   HIS A 105      16.775  34.393  -8.080  1.00 15.14           O  
ANISOU 1621  O   HIS A 105     1740   2154   1860     60    -85    173       O  
ATOM   1622  CB  HIS A 105      17.189  35.044  -5.286  1.00 12.02           C  
ANISOU 1622  CB  HIS A 105     1332   1816   1419     30   -116    177       C  
ATOM   1623  CG  HIS A 105      18.022  35.531  -4.149  1.00 16.32           C  
ANISOU 1623  CG  HIS A 105     1861   2402   1936      3   -134    184       C  
ATOM   1624  ND1 HIS A 105      19.355  35.214  -4.021  1.00 19.30           N  
ANISOU 1624  ND1 HIS A 105     2203   2821   2309     -6   -140    210       N  
ATOM   1625  CD2 HIS A 105      17.740  36.383  -3.136  1.00 14.77           C  
ANISOU 1625  CD2 HIS A 105     1682   2215   1715    -19   -149    164       C  
ATOM   1626  CE1 HIS A 105      19.849  35.811  -2.952  1.00 23.65           C  
ANISOU 1626  CE1 HIS A 105     2748   3407   2833    -34   -159    210       C  
ATOM   1627  NE2 HIS A 105      18.888  36.525  -2.395  1.00 16.46           N  
ANISOU 1627  NE2 HIS A 105     1871   2476   1909    -44   -165    180       N  
ATOM   1628  H   HIS A 105      15.680  37.068  -5.503  1.00 16.73           H  
ATOM   1629  HA  HIS A 105      17.990  36.295  -6.701  1.00 15.51           H  
ATOM   1630  HB2 HIS A 105      16.298  34.858  -4.949  1.00 14.42           H  
ATOM   1631  HB3 HIS A 105      17.591  34.231  -5.629  1.00 14.42           H  
ATOM   1632  HD2 HIS A 105      16.922  36.795  -2.972  1.00 17.73           H  
ATOM   1633  HE1 HIS A 105      20.723  35.741  -2.643  1.00 28.39           H  
ATOM   1634  HE2 HIS A 105      18.967  37.002  -1.683  1.00 19.76           H  
ATOM   1635  N   ASP A 106      15.438  36.198  -8.219  1.00 13.60           N  
ANISOU 1635  N   ASP A 106     1599   1914   1654     37    -99    130       N  
ATOM   1636  CA  ASP A 106      14.687  35.688  -9.361  1.00 14.52           C  
ANISOU 1636  CA  ASP A 106     1726   2000   1790     58    -84    126       C  
ATOM   1637  C   ASP A 106      15.507  35.632 -10.645  1.00 13.15           C  
ANISOU 1637  C   ASP A 106     1544   1826   1626     52    -76    136       C  
ATOM   1638  O   ASP A 106      15.155  34.875 -11.556  1.00 15.37           O  
ANISOU 1638  O   ASP A 106     1825   2093   1923     72    -61    138       O  
ATOM   1639  CB  ASP A 106      13.450  36.557  -9.585  1.00 13.29           C  
ANISOU 1639  CB  ASP A 106     1605   1810   1635     60    -90     99       C  
ATOM   1640  CG  ASP A 106      12.476  35.957 -10.574  1.00 13.18           C  
ANISOU 1640  CG  ASP A 106     1599   1770   1638     82    -76     95       C  
ATOM   1641  OD1 ASP A 106      12.207  34.737 -10.496  1.00 14.62           O  
ANISOU 1641  OD1 ASP A 106     1766   1958   1830    102    -62    106       O  
ATOM   1642  OD2 ASP A 106      11.950  36.727 -11.400  1.00 15.03           O  
ANISOU 1642  OD2 ASP A 106     1858   1978   1875     79    -81     80       O  
ATOM   1643  H   ASP A 106      15.200  36.988  -7.973  1.00 16.32           H  
ATOM   1644  HA  ASP A 106      14.405  34.781  -9.159  1.00 17.42           H  
ATOM   1645  HB2 ASP A 106      12.987  36.670  -8.740  1.00 15.95           H  
ATOM   1646  HB3 ASP A 106      13.730  37.420  -9.927  1.00 15.95           H  
ATOM   1647  N   GLY A 107      16.575  36.417 -10.746  1.00 13.61           N  
ANISOU 1647  N   GLY A 107     1596   1904   1672     21    -87    141       N  
ATOM   1648  CA  GLY A 107      17.449  36.334 -11.898  1.00 15.21           C  
ANISOU 1648  CA  GLY A 107     1784   2117   1878     12    -78    152       C  
ATOM   1649  C   GLY A 107      16.922  36.971 -13.164  1.00 17.33           C  
ANISOU 1649  C   GLY A 107     2081   2352   2150      3    -77    140       C  
ATOM   1650  O   GLY A 107      17.284  36.537 -14.262  1.00 16.16           O  
ANISOU 1650  O   GLY A 107     1922   2210   2008      7    -62    147       O  
ATOM   1651  H   GLY A 107      16.811  37.002 -10.162  1.00 16.34           H  
ATOM   1652  HA2 GLY A 107      18.288  36.769 -11.679  1.00 18.25           H  
ATOM   1653  HA3 GLY A 107      17.617  35.399 -12.090  1.00 18.25           H  
ATOM   1654  N   ALA A 108      16.098  38.011 -13.048  1.00 12.79           N  
ANISOU 1654  N   ALA A 108     1543   1745   1571     -9    -92    123       N  
ATOM   1655  CA  ALA A 108      15.575  38.736 -14.208  1.00 16.68           C  
ANISOU 1655  CA  ALA A 108     2066   2205   2066    -19    -96    115       C  
ATOM   1656  C   ALA A 108      16.330  40.058 -14.338  1.00 12.47           C  
ANISOU 1656  C   ALA A 108     1550   1670   1517    -64   -115    118       C  
ATOM   1657  O   ALA A 108      16.011  41.029 -13.647  1.00 13.64           O  
ANISOU 1657  O   ALA A 108     1727   1798   1659    -77   -135    104       O  
ATOM   1658  CB  ALA A 108      14.071  38.950 -14.059  1.00 19.34           C  
ANISOU 1658  CB  ALA A 108     2434   2504   2411      5   -100     94       C  
ATOM   1659  H   ALA A 108      15.822  38.321 -12.294  1.00 15.34           H  
ATOM   1660  HA  ALA A 108      15.740  38.222 -15.014  1.00 20.01           H  
ATOM   1661  HB1 ALA A 108      13.740  39.422 -14.839  1.00 23.21           H  
ATOM   1662  HB2 ALA A 108      13.635  38.087 -13.985  1.00 23.21           H  
ATOM   1663  HB3 ALA A 108      13.904  39.474 -13.259  1.00 23.21           H  
ATOM   1664  N   ASN A 109      17.343  40.109 -15.214  1.00 14.83           N  
ANISOU 1664  N   ASN A 109     1833   1992   1810    -89   -110    134       N  
ATOM   1665  CA  ASN A 109      18.142  41.330 -15.287  1.00 14.97           C  
ANISOU 1665  CA  ASN A 109     1866   2013   1811   -140   -129    141       C  
ATOM   1666  C   ASN A 109      17.265  42.497 -15.737  1.00 12.80           C  
ANISOU 1666  C   ASN A 109     1645   1683   1536   -152   -148    129       C  
ATOM   1667  O   ASN A 109      16.367  42.339 -16.574  1.00 13.31           O  
ANISOU 1667  O   ASN A 109     1727   1720   1611   -130   -143    124       O  
ATOM   1668  CB  ASN A 109      19.379  41.204 -16.203  1.00 13.50           C  
ANISOU 1668  CB  ASN A 109     1649   1868   1613   -170   -119    163       C  
ATOM   1669  CG  ASN A 109      19.138  40.449 -17.511  1.00 15.28           C  
ANISOU 1669  CG  ASN A 109     1865   2095   1846   -148    -96    167       C  
ATOM   1670  OD1 ASN A 109      20.063  39.819 -18.037  1.00 18.46           O  
ANISOU 1670  OD1 ASN A 109     2228   2542   2243   -149    -78    180       O  
ATOM   1671  ND2 ASN A 109      17.929  40.532 -18.056  1.00 17.31           N  
ANISOU 1671  ND2 ASN A 109     2156   2308   2114   -127    -97    154       N  
ATOM   1672  H   ASN A 109      17.575  39.478 -15.751  1.00 17.80           H  
ATOM   1673  HA  ASN A 109      18.494  41.505 -14.400  1.00 17.97           H  
ATOM   1674  HB2 ASN A 109      19.684  42.095 -16.434  1.00 16.20           H  
ATOM   1675  HB3 ASN A 109      20.074  40.731 -15.719  1.00 16.20           H  
ATOM   1676 HD21 ASN A 109      17.760  40.120 -18.791  1.00 20.77           H  
ATOM   1677 HD22 ASN A 109      17.316  40.999 -17.673  1.00 20.77           H  
ATOM   1678  N   GLY A 110      17.536  43.674 -15.172  1.00 14.12           N  
ANISOU 1678  N   GLY A 110     1840   1833   1692   -188   -173    124       N  
ATOM   1679  CA  GLY A 110      16.717  44.847 -15.382  1.00 16.49           C  
ANISOU 1679  CA  GLY A 110     2196   2076   1994   -195   -196    110       C  
ATOM   1680  C   GLY A 110      15.475  44.891 -14.529  1.00 13.88           C  
ANISOU 1680  C   GLY A 110     1887   1714   1674   -153   -201     82       C  
ATOM   1681  O   GLY A 110      14.808  45.935 -14.476  1.00 15.67           O  
ANISOU 1681  O   GLY A 110     2160   1892   1902   -153   -222     66       O  
ATOM   1682  H   GLY A 110      18.207  43.813 -14.652  1.00 16.95           H  
ATOM   1683  HA2 GLY A 110      17.244  45.637 -15.185  1.00 19.79           H  
ATOM   1684  HA3 GLY A 110      16.442  44.875 -16.312  1.00 19.79           H  
ATOM   1685  N   ILE A 111      15.133  43.783 -13.881  1.00 14.71           N  
ANISOU 1685  N   ILE A 111     1958   1845   1786   -116   -182     76       N  
ATOM   1686  CA  ILE A 111      13.952  43.684 -13.034  1.00 13.84           C  
ANISOU 1686  CA  ILE A 111     1860   1718   1682    -76   -183     51       C  
ATOM   1687  C   ILE A 111      14.360  43.522 -11.573  1.00 13.71           C  
ANISOU 1687  C   ILE A 111     1825   1730   1653    -80   -185     43       C  
ATOM   1688  O   ILE A 111      14.088  44.388 -10.741  1.00 14.37           O  
ANISOU 1688  O   ILE A 111     1937   1795   1728    -86   -203     21       O  
ATOM   1689  CB  ILE A 111      13.042  42.518 -13.482  1.00 14.02           C  
ANISOU 1689  CB  ILE A 111     1862   1746   1720    -33   -161     52       C  
ATOM   1690  CG1 ILE A 111      12.852  42.455 -15.004  1.00 19.42           C  
ANISOU 1690  CG1 ILE A 111     2554   2414   2412    -33   -156     64       C  
ATOM   1691  CG2 ILE A 111      11.673  42.604 -12.779  1.00 14.29           C  
ANISOU 1691  CG2 ILE A 111     1910   1760   1759      4   -163     26       C  
ATOM   1692  CD1 ILE A 111      12.178  43.638 -15.587  1.00 20.38           C  
ANISOU 1692  CD1 ILE A 111     2721   2488   2535    -37   -177     55       C  
ATOM   1693  H   ILE A 111      15.587  43.053 -13.919  1.00 17.65           H  
ATOM   1694  HA  ILE A 111      13.440  44.504 -13.119  1.00 16.61           H  
ATOM   1695  HB  ILE A 111      13.495  41.701 -13.220  1.00 16.83           H  
ATOM   1696 HG12 ILE A 111      13.724  42.379 -15.422  1.00 23.31           H  
ATOM   1697 HG13 ILE A 111      12.314  41.676 -15.217  1.00 23.31           H  
ATOM   1698 HG21 ILE A 111      11.067  41.967 -13.189  1.00 17.15           H  
ATOM   1699 HG22 ILE A 111      11.787  42.394 -11.839  1.00 17.15           H  
ATOM   1700 HG23 ILE A 111      11.323  43.503 -12.877  1.00 17.15           H  
ATOM   1701 HD11 ILE A 111      12.234  43.589 -16.554  1.00 24.46           H  
ATOM   1702 HD12 ILE A 111      11.248  43.641 -15.309  1.00 24.46           H  
ATOM   1703 HD13 ILE A 111      12.620  44.441 -15.270  1.00 24.46           H  
ATOM   1704  N   THR A 112      15.042  42.418 -11.249  1.00 14.35           N  
ANISOU 1704  N   THR A 112     1861   1858   1732    -77   -168     61       N  
ATOM   1705  CA  THR A 112      15.441  42.070  -9.893  1.00 13.50           C  
ANISOU 1705  CA  THR A 112     1731   1785   1612    -79   -170     60       C  
ATOM   1706  C   THR A 112      16.947  42.145  -9.658  1.00 16.79           C  
ANISOU 1706  C   THR A 112     2122   2242   2015   -118   -176     80       C  
ATOM   1707  O   THR A 112      17.391  41.956  -8.516  1.00 15.30           O  
ANISOU 1707  O   THR A 112     1914   2086   1812   -125   -181     81       O  
ATOM   1708  CB  THR A 112      14.942  40.649  -9.572  1.00 13.51           C  
ANISOU 1708  CB  THR A 112     1700   1809   1623    -39   -148     68       C  
ATOM   1709  OG1 THR A 112      15.616  39.698 -10.409  1.00 15.31           O  
ANISOU 1709  OG1 THR A 112     1897   2058   1862    -34   -131     93       O  
ATOM   1710  CG2 THR A 112      13.433  40.536  -9.817  1.00 14.36           C  
ANISOU 1710  CG2 THR A 112     1828   1884   1744     -3   -141     49       C  
ATOM   1711  H   THR A 112      15.293  41.833 -11.828  1.00 17.21           H  
ATOM   1712  HA  THR A 112      15.029  42.690  -9.271  1.00 16.20           H  
ATOM   1713  HB  THR A 112      15.123  40.454  -8.639  1.00 16.21           H  
ATOM   1714  HG1 THR A 112      15.063  39.147 -10.720  1.00 18.37           H  
ATOM   1715 HG21 THR A 112      13.257  40.452 -10.767  1.00 17.23           H  
ATOM   1716 HG22 THR A 112      13.081  39.756  -9.361  1.00 17.23           H  
ATOM   1717 HG23 THR A 112      12.982  41.327  -9.481  1.00 17.23           H  
ATOM   1718  N   GLU A 113      17.739  42.400 -10.695  1.00 14.83           N  
ANISOU 1718  N   GLU A 113     1870   1998   1767   -146   -176     98       N  
ATOM   1719  CA  GLU A 113      19.187  42.478 -10.565  1.00 14.08           C  
ANISOU 1719  CA  GLU A 113     1745   1949   1657   -186   -181    118       C  
ATOM   1720  C   GLU A 113      19.731  43.156 -11.809  1.00 16.35           C  
ANISOU 1720  C   GLU A 113     2044   2227   1942   -223   -185    130       C  
ATOM   1721  O   GLU A 113      19.030  43.299 -12.815  1.00 14.36           O  
ANISOU 1721  O   GLU A 113     1816   1938   1701   -210   -180    127       O  
ATOM   1722  CB  GLU A 113      19.836  41.100 -10.416  1.00 16.52           C  
ANISOU 1722  CB  GLU A 113     1998   2310   1970   -162   -161    140       C  
ATOM   1723  CG  GLU A 113      19.622  40.154 -11.601  1.00 13.72           C  
ANISOU 1723  CG  GLU A 113     1627   1953   1635   -130   -136    151       C  
ATOM   1724  CD  GLU A 113      20.212  38.774 -11.335  1.00 18.62           C  
ANISOU 1724  CD  GLU A 113     2198   2617   2262   -100   -119    170       C  
ATOM   1725  OE1 GLU A 113      20.122  38.311 -10.179  1.00 20.35           O  
ANISOU 1725  OE1 GLU A 113     2404   2851   2478    -84   -122    171       O  
ATOM   1726  OE2 GLU A 113      20.774  38.153 -12.261  1.00 21.77           O  
ANISOU 1726  OE2 GLU A 113     2570   3035   2666    -91   -102    183       O  
ATOM   1727  H   GLU A 113      17.456  42.533 -11.496  1.00 17.80           H  
ATOM   1728  HA  GLU A 113      19.393  43.003  -9.776  1.00 16.90           H  
ATOM   1729  HB2 GLU A 113      20.793  41.221 -10.310  1.00 19.83           H  
ATOM   1730  HB3 GLU A 113      19.467  40.669  -9.630  1.00 19.83           H  
ATOM   1731  HG2 GLU A 113      18.671  40.053 -11.762  1.00 16.47           H  
ATOM   1732  HG3 GLU A 113      20.055  40.524 -12.387  1.00 16.47           H  
ATOM   1733  N   CYS A 114      20.998  43.577 -11.727  1.00 16.42           N  
ANISOU 1733  N   CYS A 114     2034   2273   1933   -272   -195    146       N  
ATOM   1734  CA  CYS A 114      21.804  43.882 -12.900  1.00 14.30           C  
ANISOU 1734  CA  CYS A 114     1756   2020   1658   -308   -192    167       C  
ATOM   1735  C   CYS A 114      22.482  42.606 -13.375  1.00 16.75           C  
ANISOU 1735  C   CYS A 114     2006   2385   1972   -283   -165    187       C  
ATOM   1736  O   CYS A 114      22.629  41.652 -12.608  1.00 17.62           O  
ANISOU 1736  O   CYS A 114     2081   2526   2087   -250   -155    190       O  
ATOM   1737  CB  CYS A 114      22.849  44.942 -12.567  1.00 15.74           C  
ANISOU 1737  CB  CYS A 114     1944   2222   1816   -377   -216    175       C  
ATOM   1738  SG  CYS A 114      22.165  46.552 -12.102  1.00 18.14           S  
ANISOU 1738  SG  CYS A 114     2326   2452   2114   -411   -251    149       S  
ATOM   1739  H   CYS A 114      21.417  43.694 -10.985  1.00 19.70           H  
ATOM   1740  HA  CYS A 114      21.250  44.239 -13.612  1.00 17.16           H  
ATOM   1741  HB2 CYS A 114      23.384  44.625 -11.823  1.00 18.89           H  
ATOM   1742  HB3 CYS A 114      23.411  45.076 -13.346  1.00 18.89           H  
ATOM   1743  N   PRO A 115      22.924  42.545 -14.626  1.00 15.70           N  
ANISOU 1743  N   PRO A 115     1861   2268   1838   -297   -152    201       N  
ATOM   1744  CA  PRO A 115      23.622  41.340 -15.088  1.00 13.46           C  
ANISOU 1744  CA  PRO A 115     1520   2037   1557   -269   -125    216       C  
ATOM   1745  C   PRO A 115      24.978  41.154 -14.422  1.00 17.98           C  
ANISOU 1745  C   PRO A 115     2039   2680   2113   -291   -128    234       C  
ATOM   1746  O   PRO A 115      25.625  42.109 -13.982  1.00 17.04           O  
ANISOU 1746  O   PRO A 115     1924   2576   1975   -346   -150    240       O  
ATOM   1747  CB  PRO A 115      23.785  41.573 -16.598  1.00 16.39           C  
ANISOU 1747  CB  PRO A 115     1895   2409   1922   -288   -114    225       C  
ATOM   1748  CG  PRO A 115      22.863  42.671 -16.936  1.00 16.63           C  
ANISOU 1748  CG  PRO A 115     1990   2375   1954   -310   -133    214       C  
ATOM   1749  CD  PRO A 115      22.736  43.521 -15.713  1.00 15.84           C  
ANISOU 1749  CD  PRO A 115     1918   2252   1849   -333   -161    204       C  
ATOM   1750  HA  PRO A 115      23.073  40.557 -14.923  1.00 16.15           H  
ATOM   1751  HB2 PRO A 115      24.702  41.821 -16.794  1.00 19.66           H  
ATOM   1752  HB3 PRO A 115      23.549  40.766 -17.081  1.00 19.66           H  
ATOM   1753  HG2 PRO A 115      23.230  43.186 -17.671  1.00 19.96           H  
ATOM   1754  HG3 PRO A 115      22.001  42.304 -17.185  1.00 19.96           H  
ATOM   1755  HD2 PRO A 115      23.424  44.204 -15.691  1.00 19.01           H  
ATOM   1756  HD3 PRO A 115      21.858  43.932 -15.665  1.00 19.01           H  
ATOM   1757  N   ILE A 116      25.402  39.893 -14.363  1.00 16.53           N  
ANISOU 1757  N   ILE A 116     1805   2537   1939   -246   -107    242       N  
ATOM   1758  CA  ILE A 116      26.736  39.501 -13.913  1.00 17.50           C  
ANISOU 1758  CA  ILE A 116     1866   2735   2049   -254   -105    262       C  
ATOM   1759  C   ILE A 116      27.733  39.847 -15.009  1.00 20.18           C  
ANISOU 1759  C   ILE A 116     2177   3122   2370   -293    -96    276       C  
ATOM   1760  O   ILE A 116      27.579  39.370 -16.145  1.00 18.45           O  
ANISOU 1760  O   ILE A 116     1953   2900   2158   -271    -72    274       O  
ATOM   1761  CB  ILE A 116      26.810  37.997 -13.613  1.00 16.81           C  
ANISOU 1761  CB  ILE A 116     1738   2669   1979   -186    -85    267       C  
ATOM   1762  CG1 ILE A 116      25.739  37.577 -12.614  1.00 17.13           C  
ANISOU 1762  CG1 ILE A 116     1808   2664   2036   -150    -92    255       C  
ATOM   1763  CG2 ILE A 116      28.194  37.627 -13.083  1.00 17.35           C  
ANISOU 1763  CG2 ILE A 116     1741   2818   2035   -191    -87    289       C  
ATOM   1764  CD1 ILE A 116      25.486  36.090 -12.615  1.00 17.18           C  
ANISOU 1764  CD1 ILE A 116     1793   2669   2065    -82    -71    258       C  
ATOM   1765  H   ILE A 116      24.916  39.220 -14.588  1.00 19.84           H  
ATOM   1766  HA  ILE A 116      26.947  39.996 -13.106  1.00 21.00           H  
ATOM   1767  HB  ILE A 116      26.649  37.525 -14.445  1.00 20.17           H  
ATOM   1768 HG12 ILE A 116      26.022  37.833 -11.723  1.00 20.55           H  
ATOM   1769 HG13 ILE A 116      24.907  38.023 -12.838  1.00 20.55           H  
ATOM   1770 HG21 ILE A 116      28.199  36.686 -12.844  1.00 20.82           H  
ATOM   1771 HG22 ILE A 116      28.853  37.797 -13.774  1.00 20.82           H  
ATOM   1772 HG23 ILE A 116      28.387  38.167 -12.301  1.00 20.82           H  
ATOM   1773 HD11 ILE A 116      24.642  35.914 -12.171  1.00 20.61           H  
ATOM   1774 HD12 ILE A 116      25.450  35.777 -13.532  1.00 20.61           H  
ATOM   1775 HD13 ILE A 116      26.207  35.647 -12.142  1.00 20.61           H  
ATOM   1776  N   PRO A 117      28.764  40.637 -14.737  1.00 17.15           N  
ANISOU 1776  N   PRO A 117     1771   2784   1961   -353   -112    291       N  
ATOM   1777  CA  PRO A 117      29.729  40.999 -15.790  1.00 18.19           C  
ANISOU 1777  CA  PRO A 117     1872   2968   2071   -397   -103    307       C  
ATOM   1778  C   PRO A 117      30.480  39.777 -16.313  1.00 18.09           C  
ANISOU 1778  C   PRO A 117     1790   3020   2062   -349    -72    316       C  
ATOM   1779  O   PRO A 117      30.636  38.783 -15.594  1.00 20.04           O  
ANISOU 1779  O   PRO A 117     2003   3287   2323   -296    -65    317       O  
ATOM   1780  CB  PRO A 117      30.690  41.972 -15.090  1.00 27.36           C  
ANISOU 1780  CB  PRO A 117     3019   4172   3206   -470   -130    322       C  
ATOM   1781  CG  PRO A 117      29.959  42.460 -13.893  1.00 21.88           C  
ANISOU 1781  CG  PRO A 117     2372   3423   2517   -474   -157    307       C  
ATOM   1782  CD  PRO A 117      29.020  41.363 -13.477  1.00 19.31           C  
ANISOU 1782  CD  PRO A 117     2053   3063   2220   -393   -142    292       C  
ATOM   1783  HA  PRO A 117      29.274  41.447 -16.520  1.00 21.83           H  
ATOM   1784  HB2 PRO A 117      31.500  41.504 -14.833  1.00 32.84           H  
ATOM   1785  HB3 PRO A 117      30.905  42.706 -15.686  1.00 32.84           H  
ATOM   1786  HG2 PRO A 117      30.593  42.652 -13.184  1.00 26.25           H  
ATOM   1787  HG3 PRO A 117      29.465  43.262 -14.121  1.00 26.25           H  
ATOM   1788  HD2 PRO A 117      29.438  40.781 -12.823  1.00 23.17           H  
ATOM   1789  HD3 PRO A 117      28.198  41.731 -13.118  1.00 23.17           H  
ATOM   1790  N   PRO A 118      30.960  39.842 -17.546  1.00 17.98           N  
ANISOU 1790  N   PRO A 118     1757   3041   2035   -367    -52    322       N  
ATOM   1791  CA  PRO A 118      31.700  38.719 -18.133  1.00 17.85           C  
ANISOU 1791  CA  PRO A 118     1674   3087   2019   -320    -21    326       C  
ATOM   1792  C   PRO A 118      33.119  38.627 -17.572  1.00 21.32           C  
ANISOU 1792  C   PRO A 118     2039   3621   2440   -337    -24    346       C  
ATOM   1793  O   PRO A 118      33.510  39.361 -16.666  1.00 23.82           O  
ANISOU 1793  O   PRO A 118     2355   3953   2742   -386    -52    358       O  
ATOM   1794  CB  PRO A 118      31.700  39.061 -19.630  1.00 20.88           C  
ANISOU 1794  CB  PRO A 118     2068   3478   2388   -346     -2    325       C  
ATOM   1795  CG  PRO A 118      31.717  40.557 -19.648  1.00 18.55           C  
ANISOU 1795  CG  PRO A 118     1813   3165   2070   -434    -30    336       C  
ATOM   1796  CD  PRO A 118      30.794  40.949 -18.508  1.00 18.32           C  
ANISOU 1796  CD  PRO A 118     1839   3061   2060   -430    -59    326       C  
ATOM   1797  HA  PRO A 118      31.242  37.879 -17.978  1.00 21.42           H  
ATOM   1798  HB2 PRO A 118      32.489  38.695 -20.059  1.00 25.06           H  
ATOM   1799  HB3 PRO A 118      30.900  38.713 -20.055  1.00 25.06           H  
ATOM   1800  HG2 PRO A 118      32.618  40.883 -19.497  1.00 22.26           H  
ATOM   1801  HG3 PRO A 118      31.384  40.885 -20.497  1.00 22.26           H  
ATOM   1802  HD2 PRO A 118      31.069  41.793 -18.116  1.00 21.98           H  
ATOM   1803  HD3 PRO A 118      29.875  41.009 -18.812  1.00 21.98           H  
ATOM   1804  N   LYS A 119      33.879  37.673 -18.117  1.00 19.93           N  
ANISOU 1804  N   LYS A 119     1800   3510   2263   -292      4    349       N  
ATOM   1805  CA  LYS A 119      35.293  37.481 -17.780  1.00 24.48           C  
ANISOU 1805  CA  LYS A 119     2293   4188   2820   -301      6    369       C  
ATOM   1806  C   LYS A 119      35.502  37.324 -16.273  1.00 28.60           C  
ANISOU 1806  C   LYS A 119     2800   4719   3349   -290    -20    379       C  
ATOM   1807  O   LYS A 119      36.468  37.819 -15.689  1.00 26.83           O  
ANISOU 1807  O   LYS A 119     2533   4561   3101   -336    -38    399       O  
ATOM   1808  CB  LYS A 119      36.139  38.622 -18.356  1.00 23.39           C  
ANISOU 1808  CB  LYS A 119     2136   4110   2643   -392      0    386       C  
ATOM   1809  CG  LYS A 119      36.163  38.607 -19.885  1.00 25.61           C  
ANISOU 1809  CG  LYS A 119     2413   4406   2910   -399     30    380       C  
ATOM   1810  CD  LYS A 119      37.053  39.687 -20.465  1.00 45.17           C  
ANISOU 1810  CD  LYS A 119     4870   6948   5346   -492     24    400       C  
ATOM   1811  CE  LYS A 119      37.139  39.565 -21.979  1.00 84.42           C  
ANISOU 1811  CE  LYS A 119     9838  11938  10300   -490     56    393       C  
ATOM   1812  NZ  LYS A 119      37.430  40.874 -22.626  1.00 75.06           N  
ANISOU 1812  NZ  LYS A 119     8683  10758   9079   -586     40    409       N  
ATOM   1813  H   LYS A 119      33.591  37.109 -18.699  1.00 23.92           H  
ATOM   1814  HA  LYS A 119      35.597  36.652 -18.182  1.00 29.38           H  
ATOM   1815  HB2 LYS A 119      35.768  39.471 -18.068  1.00 28.07           H  
ATOM   1816  HB3 LYS A 119      37.051  38.534 -18.038  1.00 28.07           H  
ATOM   1817  HG2 LYS A 119      36.497  37.748 -20.188  1.00 30.73           H  
ATOM   1818  HG3 LYS A 119      35.263  38.749 -20.217  1.00 30.73           H  
ATOM   1819  HD2 LYS A 119      36.688  40.559 -20.247  1.00 54.21           H  
ATOM   1820  HD3 LYS A 119      37.947  39.601 -20.098  1.00 54.21           H  
ATOM   1821  HE2 LYS A 119      37.851  38.948 -22.210  1.00101.30           H  
ATOM   1822  HE3 LYS A 119      36.293  39.238 -22.322  1.00101.30           H  
ATOM   1823  HZ1 LYS A 119      38.034  41.321 -22.150  1.00 90.08           H  
ATOM   1824  HZ2 LYS A 119      37.747  40.744 -23.447  1.00 90.08           H  
ATOM   1825  HZ3 LYS A 119      36.686  41.360 -22.677  1.00 90.08           H  
ATOM   1826  N   GLY A 120      34.595  36.595 -15.633  1.00 23.06           N  
ANISOU 1826  N   GLY A 120     2132   3952   2677   -229    -23    368       N  
ATOM   1827  CA  GLY A 120      34.784  36.223 -14.252  1.00 24.12           C  
ANISOU 1827  CA  GLY A 120     2248   4099   2819   -207    -44    379       C  
ATOM   1828  C   GLY A 120      33.855  36.848 -13.235  1.00 22.10           C  
ANISOU 1828  C   GLY A 120     2055   3774   2567   -233    -73    372       C  
ATOM   1829  O   GLY A 120      34.051  36.625 -12.033  1.00 23.48           O  
ANISOU 1829  O   GLY A 120     2214   3966   2742   -223    -92    383       O  
ATOM   1830  H   GLY A 120      33.864  36.309 -15.984  1.00 27.67           H  
ATOM   1831  HA2 GLY A 120      34.678  35.261 -14.182  1.00 28.95           H  
ATOM   1832  HA3 GLY A 120      35.689  36.460 -13.997  1.00 28.95           H  
ATOM   1833  N   GLY A 121      32.851  37.610 -13.657  1.00 21.46           N  
ANISOU 1833  N   GLY A 121     2044   3620   2488   -264    -77    355       N  
ATOM   1834  CA  GLY A 121      31.842  38.056 -12.717  1.00 21.12           C  
ANISOU 1834  CA  GLY A 121     2062   3509   2454   -272   -100    343       C  
ATOM   1835  C   GLY A 121      31.159  36.875 -12.058  1.00 19.69           C  
ANISOU 1835  C   GLY A 121     1886   3296   2300   -197    -93    338       C  
ATOM   1836  O   GLY A 121      31.084  35.780 -12.617  1.00 20.86           O  
ANISOU 1836  O   GLY A 121     2014   3443   2468   -136    -68    337       O  
ATOM   1837  H   GLY A 121      32.734  37.877 -14.466  1.00 25.75           H  
ATOM   1838  HA2 GLY A 121      32.254  38.602 -12.029  1.00 25.34           H  
ATOM   1839  HA3 GLY A 121      31.174  38.585 -13.181  1.00 25.34           H  
ATOM   1840  N   ARG A 122      30.682  37.079 -10.839  1.00 20.60           N  
ANISOU 1840  N   ARG A 122     2026   3387   2414   -202   -116    336       N  
ATOM   1841  CA  ARG A 122      29.996  35.986 -10.174  1.00 24.49           C  
ANISOU 1841  CA  ARG A 122     2525   3849   2929   -137   -111    335       C  
ATOM   1842  C   ARG A 122      28.980  36.550  -9.202  1.00 27.12           C  
ANISOU 1842  C   ARG A 122     2913   4130   3260   -154   -131    320       C  
ATOM   1843  O   ARG A 122      29.085  37.693  -8.748  1.00 26.56           O  
ANISOU 1843  O   ARG A 122     2863   4060   3168   -213   -154    314       O  
ATOM   1844  CB  ARG A 122      30.969  35.053  -9.441  1.00 25.53           C  
ANISOU 1844  CB  ARG A 122     2593   4047   3061   -101   -114    361       C  
ATOM   1845  CG  ARG A 122      31.469  35.576  -8.106  1.00 42.88           C  
ANISOU 1845  CG  ARG A 122     4775   6284   5234   -139   -144    374       C  
ATOM   1846  CD  ARG A 122      32.328  34.532  -7.427  1.00 38.17           C  
ANISOU 1846  CD  ARG A 122     4115   5748   4639    -94   -148    402       C  
ATOM   1847  NE  ARG A 122      33.432  34.153  -8.299  1.00 41.03           N  
ANISOU 1847  NE  ARG A 122     4416   6172   5001    -79   -131    415       N  
ATOM   1848  CZ  ARG A 122      34.115  33.020  -8.201  1.00 97.68           C  
ANISOU 1848  CZ  ARG A 122    11536  13390  12187    -18   -122    435       C  
ATOM   1849  NH1 ARG A 122      33.812  32.132  -7.263  1.00 53.24           N  
ANISOU 1849  NH1 ARG A 122     5909   7746   6573     31   -132    449       N  
ATOM   1850  NH2 ARG A 122      35.098  32.775  -9.054  1.00 45.68           N  
ANISOU 1850  NH2 ARG A 122     4894   6863   5599     -5   -105    441       N  
ATOM   1851  H   ARG A 122      30.740  37.812 -10.395  1.00 24.72           H  
ATOM   1852  HA  ARG A 122      29.524  35.464 -10.843  1.00 29.38           H  
ATOM   1853  HB2 ARG A 122      30.520  34.210  -9.274  1.00 30.64           H  
ATOM   1854  HB3 ARG A 122      31.744  34.910 -10.007  1.00 30.64           H  
ATOM   1855  HG2 ARG A 122      32.003  36.373  -8.248  1.00 51.45           H  
ATOM   1856  HG3 ARG A 122      30.715  35.780  -7.532  1.00 51.45           H  
ATOM   1857  HD2 ARG A 122      32.691  34.892  -6.603  1.00 45.80           H  
ATOM   1858  HD3 ARG A 122      31.796  33.743  -7.238  1.00 45.80           H  
ATOM   1859  HE  ARG A 122      33.658  34.703  -8.920  1.00 49.24           H  
ATOM   1860 HH11 ARG A 122      33.169  32.289  -6.714  1.00 63.89           H  
ATOM   1861 HH12 ARG A 122      34.257  31.399  -7.205  1.00 63.89           H  
ATOM   1862 HH21 ARG A 122      35.291  33.349  -9.665  1.00 54.82           H  
ATOM   1863 HH22 ARG A 122      35.545  32.042  -8.996  1.00 54.82           H  
ATOM   1864  N   LYS A 123      27.985  35.724  -8.900  1.00 18.14           N  
ANISOU 1864  N   LYS A 123     1800   2947   2145   -103   -123    314       N  
ATOM   1865  CA  LYS A 123      27.093  35.985  -7.790  1.00 24.63           C  
ANISOU 1865  CA  LYS A 123     2661   3734   2963   -107   -140    303       C  
ATOM   1866  C   LYS A 123      26.518  34.671  -7.287  1.00 19.69           C  
ANISOU 1866  C   LYS A 123     2032   3092   2358    -46   -130    312       C  
ATOM   1867  O   LYS A 123      26.621  33.624  -7.933  1.00 23.69           O  
ANISOU 1867  O   LYS A 123     2519   3597   2887      2   -110    320       O  
ATOM   1868  CB  LYS A 123      25.969  36.944  -8.183  1.00 29.71           C  
ANISOU 1868  CB  LYS A 123     3368   4312   3608   -132   -142    274       C  
ATOM   1869  CG  LYS A 123      25.020  36.380  -9.228  1.00 21.02           C  
ANISOU 1869  CG  LYS A 123     2293   3160   2534    -93   -119    262       C  
ATOM   1870  CD  LYS A 123      23.795  37.239  -9.350  1.00 32.59           C  
ANISOU 1870  CD  LYS A 123     3818   4563   4000   -109   -125    235       C  
ATOM   1871  CE  LYS A 123      22.872  37.031  -8.173  1.00 22.41           C  
ANISOU 1871  CE  LYS A 123     2551   3252   2712    -90   -133    226       C  
ATOM   1872  NZ  LYS A 123      21.879  38.115  -8.071  1.00 31.21           N  
ANISOU 1872  NZ  LYS A 123     3719   4319   3821   -111   -145    198       N  
ATOM   1873  H   LYS A 123      27.808  35.000  -9.330  1.00 21.77           H  
ATOM   1874  HA  LYS A 123      27.605  36.388  -7.071  1.00 29.56           H  
ATOM   1875  HB2 LYS A 123      25.448  37.155  -7.393  1.00 35.65           H  
ATOM   1876  HB3 LYS A 123      26.363  37.753  -8.547  1.00 35.65           H  
ATOM   1877  HG2 LYS A 123      25.465  36.353 -10.089  1.00 25.23           H  
ATOM   1878  HG3 LYS A 123      24.745  35.487  -8.968  1.00 25.23           H  
ATOM   1879  HD2 LYS A 123      24.056  38.173  -9.375  1.00 39.10           H  
ATOM   1880  HD3 LYS A 123      23.317  37.006 -10.161  1.00 39.10           H  
ATOM   1881  HE2 LYS A 123      22.398  36.192  -8.281  1.00 26.89           H  
ATOM   1882  HE3 LYS A 123      23.393  37.016  -7.355  1.00 26.89           H  
ATOM   1883  HZ1 LYS A 123      21.449  38.061  -7.294  1.00 37.45           H  
ATOM   1884  HZ2 LYS A 123      22.285  38.905  -8.123  1.00 37.45           H  
ATOM   1885  HZ3 LYS A 123      21.289  38.050  -8.734  1.00 37.45           H  
ATOM   1886  N   VAL A 124      25.910  34.742  -6.112  1.00 18.47           N  
ANISOU 1886  N   VAL A 124     1898   2925   2195    -48   -145    309       N  
ATOM   1887  CA  VAL A 124      25.297  33.585  -5.480  1.00 19.72           C  
ANISOU 1887  CA  VAL A 124     2057   3067   2368      1   -140    320       C  
ATOM   1888  C   VAL A 124      23.796  33.818  -5.424  1.00 21.44           C  
ANISOU 1888  C   VAL A 124     2330   3223   2592      3   -136    294       C  
ATOM   1889  O   VAL A 124      23.330  34.804  -4.841  1.00 22.03           O  
ANISOU 1889  O   VAL A 124     2434   3287   2648    -31   -150    275       O  
ATOM   1890  CB  VAL A 124      25.870  33.332  -4.076  1.00 23.71           C  
ANISOU 1890  CB  VAL A 124     2533   3621   2853     -3   -161    344       C  
ATOM   1891  CG1 VAL A 124      25.200  32.098  -3.479  1.00 22.33           C  
ANISOU 1891  CG1 VAL A 124     2364   3426   2693     46   -156    359       C  
ATOM   1892  CG2 VAL A 124      27.396  33.183  -4.123  1.00 20.96           C  
ANISOU 1892  CG2 VAL A 124     2125   3342   2496     -7   -168    370       C  
ATOM   1893  H   VAL A 124      25.840  35.467  -5.654  1.00 22.16           H  
ATOM   1894  HA  VAL A 124      25.463  32.799  -6.023  1.00 23.66           H  
ATOM   1895  HB  VAL A 124      25.684  34.092  -3.503  1.00 28.45           H  
ATOM   1896 HG11 VAL A 124      25.624  31.888  -2.632  1.00 26.79           H  
ATOM   1897 HG12 VAL A 124      24.259  32.285  -3.340  1.00 26.79           H  
ATOM   1898 HG13 VAL A 124      25.303  31.354  -4.093  1.00 26.79           H  
ATOM   1899 HG21 VAL A 124      27.685  32.644  -3.370  1.00 25.15           H  
ATOM   1900 HG22 VAL A 124      27.646  32.750  -4.954  1.00 25.15           H  
ATOM   1901 HG23 VAL A 124      27.801  34.063  -4.074  1.00 25.15           H  
ATOM   1902  N   TYR A 125      23.039  32.910  -6.025  1.00 18.24           N  
ANISOU 1902  N   TYR A 125     1939   2779   2214     45   -116    292       N  
ATOM   1903  CA  TYR A 125      21.593  32.901  -5.885  1.00 14.34           C  
ANISOU 1903  CA  TYR A 125     1488   2234   1726     53   -112    273       C  
ATOM   1904  C   TYR A 125      21.214  31.957  -4.754  1.00 18.84           C  
ANISOU 1904  C   TYR A 125     2053   2810   2296     78   -116    292       C  
ATOM   1905  O   TYR A 125      21.753  30.853  -4.662  1.00 17.47           O  
ANISOU 1905  O   TYR A 125     1852   2652   2134    110   -112    319       O  
ATOM   1906  CB  TYR A 125      20.919  32.431  -7.169  1.00 15.37           C  
ANISOU 1906  CB  TYR A 125     1637   2319   1882     79    -90    261       C  
ATOM   1907  CG  TYR A 125      21.129  33.313  -8.373  1.00 13.48           C  
ANISOU 1907  CG  TYR A 125     1408   2070   1643     55    -85    244       C  
ATOM   1908  CD1 TYR A 125      22.247  33.161  -9.190  1.00 13.77           C  
ANISOU 1908  CD1 TYR A 125     1413   2137   1682     55    -76    255       C  
ATOM   1909  CD2 TYR A 125      20.185  34.271  -8.723  1.00 16.65           C  
ANISOU 1909  CD2 TYR A 125     1851   2433   2041     34    -88    218       C  
ATOM   1910  CE1 TYR A 125      22.435  33.966 -10.317  1.00 14.66           C  
ANISOU 1910  CE1 TYR A 125     1536   2244   1792     29    -72    242       C  
ATOM   1911  CE2 TYR A 125      20.356  35.074  -9.853  1.00 15.00           C  
ANISOU 1911  CE2 TYR A 125     1656   2213   1832     11    -85    207       C  
ATOM   1912  CZ  TYR A 125      21.483  34.911 -10.644  1.00 11.12           C  
ANISOU 1912  CZ  TYR A 125     1132   1753   1340      6    -77    220       C  
ATOM   1913  OH  TYR A 125      21.671  35.687 -11.765  1.00 15.58           O  
ANISOU 1913  OH  TYR A 125     1709   2311   1901    -21    -74    212       O  
ATOM   1914  H   TYR A 125      23.345  32.281  -6.525  1.00 21.89           H  
ATOM   1915  HA  TYR A 125      21.279  33.798  -5.690  1.00 17.21           H  
ATOM   1916  HB2 TYR A 125      21.266  31.552  -7.391  1.00 18.44           H  
ATOM   1917  HB3 TYR A 125      19.964  32.380  -7.011  1.00 18.44           H  
ATOM   1918  HD1 TYR A 125      22.880  32.513  -8.981  1.00 16.53           H  
ATOM   1919  HD2 TYR A 125      19.426  34.379  -8.196  1.00 19.98           H  
ATOM   1920  HE1 TYR A 125      23.196  33.866 -10.842  1.00 17.59           H  
ATOM   1921  HE2 TYR A 125      19.718  35.714 -10.073  1.00 18.00           H  
ATOM   1922  HH  TYR A 125      21.096  36.298 -11.790  1.00 18.70           H  
ATOM   1923  N   ARG A 126      20.290  32.385  -3.898  1.00 17.46           N  
ANISOU 1923  N   ARG A 126     1904   2624   2106     64   -124    277       N  
ATOM   1924  CA  ARG A 126      19.847  31.538  -2.796  1.00 17.59           C  
ANISOU 1924  CA  ARG A 126     1918   2649   2116     81   -127    296       C  
ATOM   1925  C   ARG A 126      18.335  31.607  -2.673  1.00 17.60           C  
ANISOU 1925  C   ARG A 126     1956   2613   2119     83   -119    274       C  
ATOM   1926  O   ARG A 126      17.762  32.698  -2.610  1.00 18.80           O  
ANISOU 1926  O   ARG A 126     2131   2754   2257     60   -123    243       O  
ATOM   1927  CB  ARG A 126      20.506  31.949  -1.475  1.00 27.13           C  
ANISOU 1927  CB  ARG A 126     3106   3908   3292     55   -149    308       C  
ATOM   1928  CG  ARG A 126      20.305  30.928  -0.353  1.00 90.32           C  
ANISOU 1928  CG  ARG A 126    11099  11930  11287     73   -155    338       C  
ATOM   1929  CD  ARG A 126      21.184  31.231   0.857  1.00 38.57           C  
ANISOU 1929  CD  ARG A 126     4519   5436   4700     50   -178    356       C  
ATOM   1930  NE  ARG A 126      22.565  31.467   0.446  1.00 83.32           N  
ANISOU 1930  NE  ARG A 126    10151  11137  10368     42   -186    369       N  
ATOM   1931  CZ  ARG A 126      23.450  32.176   1.138  1.00115.08           C  
ANISOU 1931  CZ  ARG A 126    14153  15211  14362      8   -207    372       C  
ATOM   1932  NH1 ARG A 126      23.110  32.729   2.294  1.00107.24           N  
ANISOU 1932  NH1 ARG A 126    13173  14239  13335    -21   -222    362       N  
ATOM   1933  NH2 ARG A 126      24.678  32.337   0.665  1.00 91.68           N  
ANISOU 1933  NH2 ARG A 126    11154  12282  11400      1   -213    385       N  
ATOM   1934  H   ARG A 126      19.909  33.156  -3.935  1.00 20.95           H  
ATOM   1935  HA  ARG A 126      20.089  30.619  -2.987  1.00 21.11           H  
ATOM   1936  HB2 ARG A 126      21.460  32.049  -1.619  1.00 32.55           H  
ATOM   1937  HB3 ARG A 126      20.125  32.792  -1.183  1.00 32.55           H  
ATOM   1938  HG2 ARG A 126      19.379  30.946  -0.067  1.00108.38           H  
ATOM   1939  HG3 ARG A 126      20.534  30.044  -0.680  1.00108.38           H  
ATOM   1940  HD2 ARG A 126      20.856  32.026   1.306  1.00 46.28           H  
ATOM   1941  HD3 ARG A 126      21.169  30.476   1.466  1.00 46.28           H  
ATOM   1942  HE  ARG A 126      22.824  31.123  -0.298  1.00 99.98           H  
ATOM   1943 HH11 ARG A 126      22.312  32.629   2.601  1.00128.69           H  
ATOM   1944 HH12 ARG A 126      23.686  33.187   2.738  1.00128.69           H  
ATOM   1945 HH21 ARG A 126      24.899  31.983  -0.087  1.00110.02           H  
ATOM   1946 HH22 ARG A 126      25.254  32.795   1.110  1.00110.02           H  
ATOM   1947  N   PHE A 127      17.693  30.445  -2.633  1.00 16.10           N  
ANISOU 1947  N   PHE A 127     1769   2404   1945    111   -109    290       N  
ATOM   1948  CA  PHE A 127      16.243  30.395  -2.565  1.00 18.88           C  
ANISOU 1948  CA  PHE A 127     2150   2726   2298    113   -100    272       C  
ATOM   1949  C   PHE A 127      15.820  29.051  -1.998  1.00 23.00           C  
ANISOU 1949  C   PHE A 127     2668   3245   2826    133    -96    301       C  
ATOM   1950  O   PHE A 127      16.623  28.131  -1.844  1.00 19.98           O  
ANISOU 1950  O   PHE A 127     2266   2874   2453    152   -100    335       O  
ATOM   1951  CB  PHE A 127      15.624  30.630  -3.938  1.00 17.01           C  
ANISOU 1951  CB  PHE A 127     1934   2445   2083    121    -85    247       C  
ATOM   1952  CG  PHE A 127      16.277  29.840  -5.036  1.00 15.21           C  
ANISOU 1952  CG  PHE A 127     1695   2202   1883    143    -74    260       C  
ATOM   1953  CD1 PHE A 127      15.829  28.569  -5.343  1.00 18.97           C  
ANISOU 1953  CD1 PHE A 127     2176   2653   2380    170    -62    275       C  
ATOM   1954  CD2 PHE A 127      17.334  30.370  -5.767  1.00 16.62           C  
ANISOU 1954  CD2 PHE A 127     1859   2392   2063    137    -75    257       C  
ATOM   1955  CE1 PHE A 127      16.419  27.832  -6.366  1.00 23.96           C  
ANISOU 1955  CE1 PHE A 127     2800   3268   3036    194    -51    282       C  
ATOM   1956  CE2 PHE A 127      17.929  29.639  -6.796  1.00 19.14           C  
ANISOU 1956  CE2 PHE A 127     2165   2701   2404    160    -62    266       C  
ATOM   1957  CZ  PHE A 127      17.470  28.364  -7.090  1.00 21.97           C  
ANISOU 1957  CZ  PHE A 127     2530   3032   2785    192    -50    277       C  
ATOM   1958  H   PHE A 127      18.077  29.675  -2.645  1.00 19.32           H  
ATOM   1959  HA  PHE A 127      15.928  31.085  -1.960  1.00 22.66           H  
ATOM   1960  HB2 PHE A 127      14.689  30.376  -3.906  1.00 20.41           H  
ATOM   1961  HB3 PHE A 127      15.706  31.571  -4.160  1.00 20.41           H  
ATOM   1962  HD1 PHE A 127      15.124  28.202  -4.860  1.00 22.77           H  
ATOM   1963  HD2 PHE A 127      17.648  31.223  -5.568  1.00 19.94           H  
ATOM   1964  HE1 PHE A 127      16.105  26.979  -6.563  1.00 28.76           H  
ATOM   1965  HE2 PHE A 127      18.631  30.005  -7.283  1.00 22.96           H  
ATOM   1966  HZ  PHE A 127      17.867  27.870  -7.770  1.00 26.36           H  
ATOM   1967  N   LYS A 128      14.538  28.949  -1.694  1.00 20.94           N  
ANISOU 1967  N   LYS A 128     2426   2970   2559    130    -89    290       N  
ATOM   1968  CA  LYS A 128      14.018  27.818  -0.947  1.00 24.10           C  
ANISOU 1968  CA  LYS A 128     2826   3373   2957    138    -88    319       C  
ATOM   1969  C   LYS A 128      13.210  26.929  -1.877  1.00 17.24           C  
ANISOU 1969  C   LYS A 128     1975   2459   2118    154    -73    319       C  
ATOM   1970  O   LYS A 128      12.530  27.416  -2.783  1.00 23.16           O  
ANISOU 1970  O   LYS A 128     2740   3183   2878    153    -62    288       O  
ATOM   1971  CB  LYS A 128      13.161  28.301   0.228  1.00 27.99           C  
ANISOU 1971  CB  LYS A 128     3324   3895   3415    116    -92    308       C  
ATOM   1972  CG  LYS A 128      12.550  27.201   1.080  1.00 54.70           C  
ANISOU 1972  CG  LYS A 128     6706   7287   6789    115    -92    340       C  
ATOM   1973  CD  LYS A 128      13.431  26.757   2.224  1.00 53.15           C  
ANISOU 1973  CD  LYS A 128     6490   7131   6573    111   -109    380       C  
ATOM   1974  CE  LYS A 128      12.579  26.066   3.281  1.00 90.02           C  
ANISOU 1974  CE  LYS A 128    11163  11820  11220     98   -109    403       C  
ATOM   1975  NZ  LYS A 128      13.136  26.227   4.642  1.00 98.52           N  
ANISOU 1975  NZ  LYS A 128    12222  12952  12258     81   -126    424       N  
ATOM   1976  H   LYS A 128      13.944  29.530  -1.913  1.00 25.13           H  
ATOM   1977  HA  LYS A 128      14.743  27.285  -0.585  1.00 28.92           H  
ATOM   1978  HB2 LYS A 128      13.718  28.842   0.809  1.00 33.58           H  
ATOM   1979  HB3 LYS A 128      12.431  28.834  -0.124  1.00 33.58           H  
ATOM   1980  HG2 LYS A 128      11.717  27.525   1.458  1.00 65.64           H  
ATOM   1981  HG3 LYS A 128      12.382  26.428   0.519  1.00 65.64           H  
ATOM   1982  HD2 LYS A 128      14.098  26.131   1.901  1.00 63.78           H  
ATOM   1983  HD3 LYS A 128      13.864  27.527   2.624  1.00 63.78           H  
ATOM   1984  HE2 LYS A 128      11.688  26.449   3.272  1.00108.02           H  
ATOM   1985  HE3 LYS A 128      12.534  25.117   3.083  1.00108.02           H  
ATOM   1986  HZ1 LYS A 128      12.610  25.824   5.236  1.00118.22           H  
ATOM   1987  HZ2 LYS A 128      13.948  25.865   4.683  1.00118.22           H  
ATOM   1988  HZ3 LYS A 128      13.194  27.091   4.847  1.00118.22           H  
ATOM   1989  N   ALA A 129      13.293  25.621  -1.654  1.00 17.27           N  
ANISOU 1989  N   ALA A 129     1976   2450   2134    169    -73    355       N  
ATOM   1990  CA  ALA A 129      12.454  24.674  -2.384  1.00 17.18           C  
ANISOU 1990  CA  ALA A 129     1986   2396   2147    180    -60    357       C  
ATOM   1991  C   ALA A 129      11.151  24.498  -1.607  1.00 18.03           C  
ANISOU 1991  C   ALA A 129     2104   2512   2236    158    -58    359       C  
ATOM   1992  O   ALA A 129      10.930  23.503  -0.915  1.00 19.72           O  
ANISOU 1992  O   ALA A 129     2320   2726   2446    156    -62    393       O  
ATOM   1993  CB  ALA A 129      13.182  23.353  -2.587  1.00 23.15           C  
ANISOU 1993  CB  ALA A 129     2741   3128   2929    207    -62    392       C  
ATOM   1994  H   ALA A 129      13.827  25.258  -1.085  1.00 20.72           H  
ATOM   1995  HA  ALA A 129      12.245  25.037  -3.259  1.00 20.62           H  
ATOM   1996  HB1 ALA A 129      12.562  22.705  -2.958  1.00 27.78           H  
ATOM   1997  HB2 ALA A 129      13.921  23.491  -3.199  1.00 27.78           H  
ATOM   1998  HB3 ALA A 129      13.514  23.041  -1.731  1.00 27.78           H  
ATOM   1999  N   GLN A 130      10.280  25.506  -1.717  1.00 15.20           N  
ANISOU 1999  N   GLN A 130     1750   2163   1862    143    -52    322       N  
ATOM   2000  CA  GLN A 130       8.948  25.489  -1.110  1.00 17.80           C  
ANISOU 2000  CA  GLN A 130     2084   2507   2171    125    -47    316       C  
ATOM   2001  C   GLN A 130       7.915  24.899  -2.045  1.00 26.81           C  
ANISOU 2001  C   GLN A 130     3241   3612   3333    125    -34    307       C  
ATOM   2002  O   GLN A 130       6.708  25.048  -1.820  1.00 49.37           O  
ANISOU 2002  O   GLN A 130     6100   6483   6176    111    -27    294       O  
ATOM   2003  CB  GLN A 130       8.537  26.901  -0.702  1.00 21.08           C  
ANISOU 2003  CB  GLN A 130     2496   2954   2559    113    -47    278       C  
ATOM   2004  CG  GLN A 130       9.500  27.468   0.316  1.00 73.28           C  
ANISOU 2004  CG  GLN A 130     9093   9604   9145    106    -61    285       C  
ATOM   2005  CD  GLN A 130       9.113  28.824   0.854  1.00 49.38           C  
ANISOU 2005  CD  GLN A 130     6067   6607   6089     94    -63    246       C  
ATOM   2006  OE1 GLN A 130       9.256  29.839   0.175  1.00 37.08           O  
ANISOU 2006  OE1 GLN A 130     4518   5033   4539     98    -64    214       O  
ATOM   2007  NE2 GLN A 130       8.656  28.853   2.101  1.00 66.22           N  
ANISOU 2007  NE2 GLN A 130     8192   8782   8186     79    -65    250       N  
ATOM   2008  H   GLN A 130      10.445  26.230  -2.151  1.00 18.24           H  
ATOM   2009  HA  GLN A 130       8.972  24.951  -0.303  1.00 21.35           H  
ATOM   2010  HB2 GLN A 130       8.538  27.477  -1.483  1.00 25.30           H  
ATOM   2011  HB3 GLN A 130       7.650  26.879  -0.308  1.00 25.30           H  
ATOM   2012  HG2 GLN A 130       9.550  26.858   1.068  1.00 87.94           H  
ATOM   2013  HG3 GLN A 130      10.372  27.556  -0.099  1.00 87.94           H  
ATOM   2014 HE21 GLN A 130       8.595  28.124   2.553  1.00 79.46           H  
ATOM   2015 HE22 GLN A 130       8.422  29.601   2.456  1.00 79.46           H  
ATOM   2016  N   GLN A 131       8.394  24.296  -3.123  1.00 17.40           N  
ANISOU 2016  N   GLN A 131     2059   2378   2173    143    -31    312       N  
ATOM   2017  CA  GLN A 131       7.624  23.578  -4.114  1.00 13.95           C  
ANISOU 2017  CA  GLN A 131     1639   1901   1758    144    -20    306       C  
ATOM   2018  C   GLN A 131       8.414  22.318  -4.413  1.00 15.19           C  
ANISOU 2018  C   GLN A 131     1807   2024   1942    161    -23    336       C  
ATOM   2019  O   GLN A 131       9.593  22.215  -4.067  1.00 17.70           O  
ANISOU 2019  O   GLN A 131     2113   2349   2262    178    -31    355       O  
ATOM   2020  CB  GLN A 131       7.465  24.374  -5.400  1.00 17.47           C  
ANISOU 2020  CB  GLN A 131     2092   2329   2218    152    -13    268       C  
ATOM   2021  CG  GLN A 131       6.939  25.768  -5.238  1.00 21.12           C  
ANISOU 2021  CG  GLN A 131     2547   2818   2659    143    -14    235       C  
ATOM   2022  CD  GLN A 131       7.438  26.681  -6.346  1.00 17.01           C  
ANISOU 2022  CD  GLN A 131     2032   2282   2150    154    -13    209       C  
ATOM   2023  OE1 GLN A 131       8.387  27.435  -6.146  1.00 16.82           O  
ANISOU 2023  OE1 GLN A 131     2001   2272   2120    157    -20    205       O  
ATOM   2024  NE2 GLN A 131       6.820  26.598  -7.527  1.00 17.23           N  
ANISOU 2024  NE2 GLN A 131     2071   2282   2193    157     -6    191       N  
ATOM   2025  H   GLN A 131       9.232  24.291  -3.314  1.00 20.88           H  
ATOM   2026  HA  GLN A 131       6.738  23.378  -3.774  1.00 16.73           H  
ATOM   2027  HB2 GLN A 131       8.334  24.442  -5.826  1.00 20.97           H  
ATOM   2028  HB3 GLN A 131       6.849  23.899  -5.979  1.00 20.97           H  
ATOM   2029  HG2 GLN A 131       5.970  25.752  -5.269  1.00 25.34           H  
ATOM   2030  HG3 GLN A 131       7.238  26.128  -4.388  1.00 25.34           H  
ATOM   2031 HE21 GLN A 131       6.170  26.045  -7.634  1.00 20.67           H  
ATOM   2032 HE22 GLN A 131       7.072  27.097  -8.180  1.00 20.67           H  
ATOM   2033  N   TYR A 132       7.790  21.378  -5.111  1.00 16.27           N  
ANISOU 2033  N   TYR A 132     1963   2120   2098    159    -16    339       N  
ATOM   2034  CA  TYR A 132       8.500  20.197  -5.588  1.00 15.37           C  
ANISOU 2034  CA  TYR A 132     1865   1963   2013    181    -17    360       C  
ATOM   2035  C   TYR A 132       8.003  19.877  -6.991  1.00 14.19           C  
ANISOU 2035  C   TYR A 132     1735   1771   1885    184     -6    333       C  
ATOM   2036  O   TYR A 132       6.862  20.180  -7.357  1.00 13.93           O  
ANISOU 2036  O   TYR A 132     1708   1740   1844    162      0    312       O  
ATOM   2037  CB  TYR A 132       8.331  18.987  -4.628  1.00 15.16           C  
ANISOU 2037  CB  TYR A 132     1850   1926   1986    172    -26    404       C  
ATOM   2038  CG  TYR A 132       6.891  18.713  -4.303  1.00 13.02           C  
ANISOU 2038  CG  TYR A 132     1589   1659   1700    135    -24    407       C  
ATOM   2039  CD1 TYR A 132       6.272  19.350  -3.244  1.00 15.13           C  
ANISOU 2039  CD1 TYR A 132     1838   1979   1933    110    -25    410       C  
ATOM   2040  CD2 TYR A 132       6.139  17.839  -5.080  1.00 13.75           C  
ANISOU 2040  CD2 TYR A 132     1706   1706   1810    124    -18    403       C  
ATOM   2041  CE1 TYR A 132       4.932  19.123  -2.962  1.00 13.85           C  
ANISOU 2041  CE1 TYR A 132     1679   1829   1754     75    -21    411       C  
ATOM   2042  CE2 TYR A 132       4.794  17.610  -4.815  1.00 13.11           C  
ANISOU 2042  CE2 TYR A 132     1632   1637   1714     85    -15    406       C  
ATOM   2043  CZ  TYR A 132       4.192  18.261  -3.756  1.00 14.21           C  
ANISOU 2043  CZ  TYR A 132     1747   1833   1818     62    -16    410       C  
ATOM   2044  OH  TYR A 132       2.855  18.057  -3.468  1.00 16.18           O  
ANISOU 2044  OH  TYR A 132     1996   2103   2050     23    -12    412       O  
ATOM   2045  H   TYR A 132       6.957  21.402  -5.321  1.00 19.52           H  
ATOM   2046  HA  TYR A 132       9.453  20.371  -5.642  1.00 18.45           H  
ATOM   2047  HB2 TYR A 132       8.702  18.195  -5.047  1.00 18.19           H  
ATOM   2048  HB3 TYR A 132       8.798  19.173  -3.798  1.00 18.19           H  
ATOM   2049  HD1 TYR A 132       6.759  19.938  -2.714  1.00 18.16           H  
ATOM   2050  HD2 TYR A 132       6.544  17.398  -5.792  1.00 16.49           H  
ATOM   2051  HE1 TYR A 132       4.531  19.549  -2.239  1.00 16.62           H  
ATOM   2052  HE2 TYR A 132       4.304  17.024  -5.346  1.00 15.74           H  
ATOM   2053  HH  TYR A 132       2.500  17.589  -4.069  1.00 19.42           H  
ATOM   2054  N   GLY A 133       8.883  19.272  -7.776  1.00 15.02           N  
ANISOU 2054  N   GLY A 133     1850   1842   2016    214     -3    333       N  
ATOM   2055  CA  GLY A 133       8.559  18.954  -9.147  1.00 15.22           C  
ANISOU 2055  CA  GLY A 133     1895   1829   2059    218      8    306       C  
ATOM   2056  C   GLY A 133       9.685  19.295 -10.094  1.00 16.98           C  
ANISOU 2056  C   GLY A 133     2109   2049   2295    249     16    286       C  
ATOM   2057  O   GLY A 133      10.849  19.380  -9.696  1.00 15.35           O  
ANISOU 2057  O   GLY A 133     1883   1858   2090    273     11    302       O  
ATOM   2058  H   GLY A 133       9.675  19.038  -7.535  1.00 18.03           H  
ATOM   2059  HA2 GLY A 133       8.372  18.005  -9.221  1.00 18.26           H  
ATOM   2060  HA3 GLY A 133       7.771  19.453  -9.414  1.00 18.26           H  
ATOM   2061  N   THR A 134       9.331  19.539 -11.347  1.00 14.40           N  
ANISOU 2061  N   THR A 134     1792   1705   1973    247     26    254       N  
ATOM   2062  CA  THR A 134      10.288  19.739 -12.424  1.00 13.93           C  
ANISOU 2062  CA  THR A 134     1727   1642   1924    273     36    233       C  
ATOM   2063  C   THR A 134      10.247  21.181 -12.906  1.00 15.49           C  
ANISOU 2063  C   THR A 134     1909   1873   2104    259     38    209       C  
ATOM   2064  O   THR A 134       9.186  21.688 -13.284  1.00 14.24           O  
ANISOU 2064  O   THR A 134     1759   1716   1937    236     39    191       O  
ATOM   2065  CB  THR A 134       9.965  18.802 -13.590  1.00 18.45           C  
ANISOU 2065  CB  THR A 134     2328   2168   2515    280     46    214       C  
ATOM   2066  OG1 THR A 134       9.874  17.444 -13.137  1.00 15.75           O  
ANISOU 2066  OG1 THR A 134     2009   1786   2189    288     41    237       O  
ATOM   2067  CG2 THR A 134      11.013  18.911 -14.680  1.00 19.86           C  
ANISOU 2067  CG2 THR A 134     2499   2346   2700    309     58    193       C  
ATOM   2068  H   THR A 134       8.512  19.595 -11.606  1.00 17.27           H  
ATOM   2069  HA  THR A 134      11.182  19.559 -12.096  1.00 16.72           H  
ATOM   2070  HB  THR A 134       9.109  19.059 -13.968  1.00 22.14           H  
ATOM   2071  HG1 THR A 134       9.073  17.247 -12.977  1.00 18.90           H  
ATOM   2072 HG21 THR A 134      10.770  19.612 -15.304  1.00 23.83           H  
ATOM   2073 HG22 THR A 134      11.876  19.121 -14.290  1.00 23.83           H  
ATOM   2074 HG23 THR A 134      11.081  18.071 -15.160  1.00 23.83           H  
ATOM   2075  N   SER A 135      11.406  21.826 -12.919  1.00 16.30           N  
ANISOU 2075  N   SER A 135     1988   2002   2202    274     38    210       N  
ATOM   2076  CA  SER A 135      11.530  23.193 -13.399  1.00 17.23           C  
ANISOU 2076  CA  SER A 135     2095   2148   2305    260     39    190       C  
ATOM   2077  C   SER A 135      12.788  23.257 -14.262  1.00 14.53           C  
ANISOU 2077  C   SER A 135     1738   1815   1968    280     48    183       C  
ATOM   2078  O   SER A 135      13.383  22.231 -14.608  1.00 15.84           O  
ANISOU 2078  O   SER A 135     1905   1964   2150    308     56    186       O  
ATOM   2079  CB  SER A 135      11.551  24.187 -12.226  1.00 21.04           C  
ANISOU 2079  CB  SER A 135     2560   2665   2767    243     26    201       C  
ATOM   2080  OG  SER A 135      10.246  24.499 -11.747  1.00 24.53           O  
ANISOU 2080  OG  SER A 135     3013   3107   3199    222     21    195       O  
ATOM   2081  H   SER A 135      12.148  21.485 -12.649  1.00 19.55           H  
ATOM   2082  HA  SER A 135      10.764  23.413 -13.952  1.00 20.68           H  
ATOM   2083  HB2 SER A 135      12.061  23.795 -11.500  1.00 25.24           H  
ATOM   2084  HB3 SER A 135      11.974  25.007 -12.524  1.00 25.24           H  
ATOM   2085  HG  SER A 135       9.881  25.061 -12.253  1.00 29.43           H  
ATOM   2086  N   TRP A 136      13.207  24.466 -14.614  1.00 15.24           N  
ANISOU 2086  N   TRP A 136     1815   1934   2044    267     47    172       N  
ATOM   2087  CA  TRP A 136      14.422  24.620 -15.395  1.00 16.06           C  
ANISOU 2087  CA  TRP A 136     1899   2055   2146    280     56    167       C  
ATOM   2088  C   TRP A 136      15.001  25.996 -15.130  1.00 13.88           C  
ANISOU 2088  C   TRP A 136     1605   1818   1851    258     47    169       C  
ATOM   2089  O   TRP A 136      14.319  26.885 -14.616  1.00 16.04           O  
ANISOU 2089  O   TRP A 136     1887   2094   2112    234     35    166       O  
ATOM   2090  CB  TRP A 136      14.174  24.420 -16.892  1.00 15.57           C  
ANISOU 2090  CB  TRP A 136     1853   1975   2088    283     72    141       C  
ATOM   2091  CG  TRP A 136      13.200  25.352 -17.571  1.00 14.48           C  
ANISOU 2091  CG  TRP A 136     1733   1832   1937    254     69    122       C  
ATOM   2092  CD1 TRP A 136      11.898  25.610 -17.226  1.00 15.91           C  
ANISOU 2092  CD1 TRP A 136     1932   1997   2115    236     59    119       C  
ATOM   2093  CD2 TRP A 136      13.456  26.111 -18.751  1.00 14.78           C  
ANISOU 2093  CD2 TRP A 136     1770   1882   1962    241     75    106       C  
ATOM   2094  NE1 TRP A 136      11.336  26.489 -18.127  1.00 18.93           N  
ANISOU 2094  NE1 TRP A 136     2326   2380   2486    217     58    101       N  
ATOM   2095  CE2 TRP A 136      12.274  26.807 -19.073  1.00 16.29           C  
ANISOU 2095  CE2 TRP A 136     1982   2060   2145    218     66     95       C  
ATOM   2096  CE3 TRP A 136      14.574  26.263 -19.571  1.00 13.92           C  
ANISOU 2096  CE3 TRP A 136     1644   1798   1847    247     86    102       C  
ATOM   2097  CZ2 TRP A 136      12.189  27.650 -20.175  1.00 13.35           C  
ANISOU 2097  CZ2 TRP A 136     1618   1696   1760    200     67     82       C  
ATOM   2098  CZ3 TRP A 136      14.490  27.096 -20.648  1.00 14.82           C  
ANISOU 2098  CZ3 TRP A 136     1764   1921   1945    225     89     88       C  
ATOM   2099  CH2 TRP A 136      13.308  27.782 -20.947  1.00 15.80           C  
ANISOU 2099  CH2 TRP A 136     1912   2027   2062    202     78     80       C  
ATOM   2100  H   TRP A 136      12.810  25.201 -14.415  1.00 18.29           H  
ATOM   2101  HA  TRP A 136      15.069  23.955 -15.112  1.00 19.27           H  
ATOM   2102  HB2 TRP A 136      15.023  24.521 -17.350  1.00 18.68           H  
ATOM   2103  HB3 TRP A 136      13.834  23.520 -17.019  1.00 18.68           H  
ATOM   2104  HD1 TRP A 136      11.458  25.244 -16.492  1.00 19.09           H  
ATOM   2105  HE1 TRP A 136      10.530  26.788 -18.099  1.00 22.72           H  
ATOM   2106  HE3 TRP A 136      15.362  25.805 -19.388  1.00 16.70           H  
ATOM   2107  HZ2 TRP A 136      11.403  28.104 -20.378  1.00 16.03           H  
ATOM   2108  HZ3 TRP A 136      15.234  27.210 -21.195  1.00 17.78           H  
ATOM   2109  HH2 TRP A 136      13.284  28.342 -21.689  1.00 18.95           H  
ATOM   2110  N   TYR A 137      16.278  26.160 -15.463  1.00 14.10           N  
ANISOU 2110  N   TYR A 137     1606   1876   1876    266     52    173       N  
ATOM   2111  CA  TYR A 137      16.916  27.464 -15.364  1.00 12.76           C  
ANISOU 2111  CA  TYR A 137     1420   1742   1686    239     44    174       C  
ATOM   2112  C   TYR A 137      17.435  27.890 -16.732  1.00 15.05           C  
ANISOU 2112  C   TYR A 137     1704   2044   1968    231     56    160       C  
ATOM   2113  O   TYR A 137      17.741  27.063 -17.597  1.00 15.28           O  
ANISOU 2113  O   TYR A 137     1730   2069   2007    255     74    151       O  
ATOM   2114  CB  TYR A 137      18.046  27.475 -14.310  1.00 15.52           C  
ANISOU 2114  CB  TYR A 137     1736   2130   2031    244     34    198       C  
ATOM   2115  CG  TYR A 137      19.215  26.551 -14.557  1.00 14.75           C  
ANISOU 2115  CG  TYR A 137     1608   2053   1943    280     46    209       C  
ATOM   2116  CD1 TYR A 137      20.305  26.970 -15.305  1.00 14.73           C  
ANISOU 2116  CD1 TYR A 137     1577   2088   1930    276     54    205       C  
ATOM   2117  CD2 TYR A 137      19.241  25.266 -14.019  1.00 14.30           C  
ANISOU 2117  CD2 TYR A 137     1550   1978   1905    317     47    223       C  
ATOM   2118  CE1 TYR A 137      21.392  26.137 -15.518  1.00 15.74           C  
ANISOU 2118  CE1 TYR A 137     1672   2242   2068    313     66    213       C  
ATOM   2119  CE2 TYR A 137      20.314  24.419 -14.239  1.00 18.18           C  
ANISOU 2119  CE2 TYR A 137     2014   2487   2408    356     56    232       C  
ATOM   2120  CZ  TYR A 137      21.394  24.863 -14.990  1.00 13.64           C  
ANISOU 2120  CZ  TYR A 137     1406   1955   1823    357     66    225       C  
ATOM   2121  OH  TYR A 137      22.479  24.036 -15.219  1.00 16.97           O  
ANISOU 2121  OH  TYR A 137     1795   2398   2253    400     77    231       O  
ATOM   2122  H   TYR A 137      16.790  25.530 -15.747  1.00 16.92           H  
ATOM   2123  HA  TYR A 137      16.264  28.124 -15.082  1.00 15.31           H  
ATOM   2124  HB2 TYR A 137      18.403  28.376 -14.262  1.00 18.62           H  
ATOM   2125  HB3 TYR A 137      17.662  27.224 -13.456  1.00 18.62           H  
ATOM   2126  HD1 TYR A 137      20.306  27.826 -15.669  1.00 17.67           H  
ATOM   2127  HD2 TYR A 137      18.525  24.972 -13.503  1.00 17.16           H  
ATOM   2128  HE1 TYR A 137      22.118  26.437 -16.017  1.00 18.89           H  
ATOM   2129  HE2 TYR A 137      20.311  23.559 -13.886  1.00 21.82           H  
ATOM   2130  HH  TYR A 137      22.231  23.234 -15.228  1.00 20.36           H  
ATOM   2131  N   HIS A 138      17.504  29.201 -16.926  1.00 14.96           N  
ANISOU 2131  N   HIS A 138     1696   2048   1940    196     47    156       N  
ATOM   2132  CA  HIS A 138      17.963  29.735 -18.196  1.00 15.51           C  
ANISOU 2132  CA  HIS A 138     1762   2132   1997    180     56    146       C  
ATOM   2133  C   HIS A 138      18.354  31.191 -18.025  1.00 14.76           C  
ANISOU 2133  C   HIS A 138     1666   2059   1882    138     41    153       C  
ATOM   2134  O   HIS A 138      17.847  31.891 -17.147  1.00 14.55           O  
ANISOU 2134  O   HIS A 138     1655   2022   1852    121     22    155       O  
ATOM   2135  CB  HIS A 138      16.884  29.575 -19.281  1.00 12.30           C  
ANISOU 2135  CB  HIS A 138     1388   1692   1594    180     64    127       C  
ATOM   2136  CG  HIS A 138      15.605  30.300 -18.991  1.00 16.03           C  
ANISOU 2136  CG  HIS A 138     1892   2134   2064    161     48    121       C  
ATOM   2137  ND1 HIS A 138      15.442  31.646 -19.236  1.00 15.34           N  
ANISOU 2137  ND1 HIS A 138     1818   2048   1962    128     34    119       N  
ATOM   2138  CD2 HIS A 138      14.417  29.858 -18.513  1.00 12.85           C  
ANISOU 2138  CD2 HIS A 138     1509   1701   1673    171     44    116       C  
ATOM   2139  CE1 HIS A 138      14.216  32.007 -18.903  1.00 14.39           C  
ANISOU 2139  CE1 HIS A 138     1723   1899   1844    125     22    112       C  
ATOM   2140  NE2 HIS A 138      13.572  30.941 -18.462  1.00 14.63           N  
ANISOU 2140  NE2 HIS A 138     1755   1913   1889    149     29    109       N  
ATOM   2141  H   HIS A 138      17.292  29.796 -16.341  1.00 17.95           H  
ATOM   2142  HA  HIS A 138      18.758  29.258 -18.482  1.00 18.61           H  
ATOM   2143  HB2 HIS A 138      17.233  29.920 -20.118  1.00 14.76           H  
ATOM   2144  HB3 HIS A 138      16.673  28.633 -19.372  1.00 14.76           H  
ATOM   2145  HD1 HIS A 138      16.045  32.169 -19.556  1.00 18.41           H  
ATOM   2146  HD2 HIS A 138      14.212  28.985 -18.266  1.00 15.42           H  
ATOM   2147  HE1 HIS A 138      13.865  32.866 -18.968  1.00 17.26           H  
ATOM   2148  N   SER A 139      19.275  31.631 -18.873  1.00 13.99           N  
ANISOU 2148  N   SER A 139     1551   1994   1770    120     48    154       N  
ATOM   2149  CA  SER A 139      19.606  33.044 -18.925  1.00 11.19           C  
ANISOU 2149  CA  SER A 139     1202   1655   1396     74     32    160       C  
ATOM   2150  C   SER A 139      18.377  33.874 -19.283  1.00 14.21           C  
ANISOU 2150  C   SER A 139     1629   1995   1777     54     20    149       C  
ATOM   2151  O   SER A 139      17.525  33.451 -20.071  1.00 16.07           O  
ANISOU 2151  O   SER A 139     1884   2203   2018     69     29    136       O  
ATOM   2152  CB  SER A 139      20.689  33.302 -19.970  1.00 16.46           C  
ANISOU 2152  CB  SER A 139     1844   2365   2046     55     45    165       C  
ATOM   2153  OG  SER A 139      21.045  34.673 -19.959  1.00 16.61           O  
ANISOU 2153  OG  SER A 139     1870   2396   2045      4     27    174       O  
ATOM   2154  H   SER A 139      19.718  31.138 -19.421  1.00 16.79           H  
ATOM   2155  HA  SER A 139      19.934  33.319 -18.055  1.00 13.43           H  
ATOM   2156  HB2 SER A 139      21.470  32.766 -19.761  1.00 19.75           H  
ATOM   2157  HB3 SER A 139      20.350  33.066 -20.848  1.00 19.75           H  
ATOM   2158  HG  SER A 139      20.801  35.039 -20.674  1.00 19.93           H  
ATOM   2159  N   HIS A 140      18.310  35.085 -18.723  1.00 14.17           N  
ANISOU 2159  N   HIS A 140     1640   1983   1761     22     -3    153       N  
ATOM   2160  CA  HIS A 140      17.330  36.089 -19.122  1.00 12.68           C  
ANISOU 2160  CA  HIS A 140     1493   1756   1568      2    -18    144       C  
ATOM   2161  C   HIS A 140      17.992  37.297 -19.787  1.00 16.56           C  
ANISOU 2161  C   HIS A 140     1993   2259   2039    -45    -29    154       C  
ATOM   2162  O   HIS A 140      17.342  38.331 -19.964  1.00 15.77           O  
ANISOU 2162  O   HIS A 140     1930   2126   1935    -65    -48    150       O  
ATOM   2163  CB  HIS A 140      16.476  36.522 -17.921  1.00 19.25           C  
ANISOU 2163  CB  HIS A 140     2347   2561   2406      7    -37    137       C  
ATOM   2164  CG  HIS A 140      15.001  36.415 -18.176  1.00 14.23           C  
ANISOU 2164  CG  HIS A 140     1741   1886   1782     27    -38    121       C  
ATOM   2165  ND1 HIS A 140      14.399  37.011 -19.261  1.00 19.73           N  
ANISOU 2165  ND1 HIS A 140     2464   2559   2474     16    -43    116       N  
ATOM   2166  CD2 HIS A 140      14.018  35.758 -17.515  1.00 13.57           C  
ANISOU 2166  CD2 HIS A 140     1661   1786   1710     56    -36    112       C  
ATOM   2167  CE1 HIS A 140      13.106  36.740 -19.252  1.00 19.06           C  
ANISOU 2167  CE1 HIS A 140     2396   2447   2400     40    -44    103       C  
ATOM   2168  NE2 HIS A 140      12.850  35.973 -18.208  1.00 19.50           N  
ANISOU 2168  NE2 HIS A 140     2437   2506   2464     62    -39    100       N  
ATOM   2169  H   HIS A 140      18.836  35.350 -18.097  1.00 17.00           H  
ATOM   2170  HA  HIS A 140      16.721  35.694 -19.766  1.00 15.21           H  
ATOM   2171  HB2 HIS A 140      16.690  35.956 -17.163  1.00 23.10           H  
ATOM   2172  HB3 HIS A 140      16.676  37.448 -17.711  1.00 23.10           H  
ATOM   2173  HD1 HIS A 140      14.802  37.487 -19.854  1.00 23.68           H  
ATOM   2174  HD2 HIS A 140      14.115  35.256 -16.738  1.00 16.29           H  
ATOM   2175  HE1 HIS A 140      12.483  37.039 -19.875  1.00 22.88           H  
ATOM   2176  N   PHE A 141      19.260  37.178 -20.187  1.00 14.38           N  
ANISOU 2176  N   PHE A 141     1684   2030   1751    -62    -18    166       N  
ATOM   2177  CA  PHE A 141      20.015  38.264 -20.826  1.00 14.55           C  
ANISOU 2177  CA  PHE A 141     1708   2071   1750   -113    -27    179       C  
ATOM   2178  C   PHE A 141      19.675  38.279 -22.316  1.00 18.04           C  
ANISOU 2178  C   PHE A 141     2165   2506   2184   -119    -16    177       C  
ATOM   2179  O   PHE A 141      20.259  37.554 -23.122  1.00 16.26           O  
ANISOU 2179  O   PHE A 141     1910   2316   1950   -110      8    178       O  
ATOM   2180  CB  PHE A 141      21.505  38.060 -20.575  1.00 15.56           C  
ANISOU 2180  CB  PHE A 141     1786   2261   1864   -129    -18    194       C  
ATOM   2181  CG  PHE A 141      22.375  39.206 -21.001  1.00 13.81           C  
ANISOU 2181  CG  PHE A 141     1564   2066   1617   -190    -30    211       C  
ATOM   2182  CD1 PHE A 141      22.629  40.263 -20.135  1.00 15.97           C  
ANISOU 2182  CD1 PHE A 141     1853   2331   1883   -231    -57    218       C  
ATOM   2183  CD2 PHE A 141      22.982  39.204 -22.239  1.00 16.26           C  
ANISOU 2183  CD2 PHE A 141     1857   2412   1910   -211    -14    220       C  
ATOM   2184  CE1 PHE A 141      23.455  41.307 -20.503  1.00 16.47           C  
ANISOU 2184  CE1 PHE A 141     1917   2417   1922   -293    -70    236       C  
ATOM   2185  CE2 PHE A 141      23.797  40.250 -22.617  1.00 18.21           C  
ANISOU 2185  CE2 PHE A 141     2102   2686   2131   -273    -25    238       C  
ATOM   2186  CZ  PHE A 141      24.032  41.307 -21.745  1.00 16.14           C  
ANISOU 2186  CZ  PHE A 141     1858   2411   1862   -316    -54    248       C  
ATOM   2187  H   PHE A 141      19.719  36.457 -20.098  1.00 17.26           H  
ATOM   2188  HA  PHE A 141      19.751  39.122 -20.460  1.00 17.46           H  
ATOM   2189  HB2 PHE A 141      21.642  37.927 -19.624  1.00 18.67           H  
ATOM   2190  HB3 PHE A 141      21.796  37.275 -21.065  1.00 18.67           H  
ATOM   2191  HD1 PHE A 141      22.235  40.268 -19.293  1.00 19.16           H  
ATOM   2192  HD2 PHE A 141      22.840  38.494 -22.822  1.00 19.52           H  
ATOM   2193  HE1 PHE A 141      23.618  42.005 -19.911  1.00 19.76           H  
ATOM   2194  HE2 PHE A 141      24.191  40.249 -23.459  1.00 21.85           H  
ATOM   2195  HZ  PHE A 141      24.581  42.012 -22.004  1.00 19.36           H  
ATOM   2196  N   SER A 142      18.705  39.108 -22.694  1.00 16.03           N  
ANISOU 2196  N   SER A 142     1956   2206   1928   -133    -34    174       N  
ATOM   2197  CA  SER A 142      18.149  39.064 -24.056  1.00 16.17           C  
ANISOU 2197  CA  SER A 142     1992   2213   1939   -133    -26    172       C  
ATOM   2198  C   SER A 142      17.849  37.600 -24.388  1.00 16.89           C  
ANISOU 2198  C   SER A 142     2062   2314   2042    -86      1    156       C  
ATOM   2199  O   SER A 142      17.286  36.889 -23.545  1.00 15.46           O  
ANISOU 2199  O   SER A 142     1878   2114   1882    -50      3    145       O  
ATOM   2200  CB  SER A 142      19.108  39.762 -25.009  1.00 17.73           C  
ANISOU 2200  CB  SER A 142     2182   2444   2108   -183    -26    191       C  
ATOM   2201  OG  SER A 142      19.206  41.140 -24.718  1.00 19.42           O  
ANISOU 2201  OG  SER A 142     2428   2636   2313   -228    -55    206       O  
ATOM   2202  H   SER A 142      18.352  39.704 -22.184  1.00 19.23           H  
ATOM   2203  HA  SER A 142      17.304  39.541 -24.066  1.00 19.40           H  
ATOM   2204  HB2 SER A 142      19.986  39.359 -24.922  1.00 21.27           H  
ATOM   2205  HB3 SER A 142      18.783  39.655 -25.917  1.00 21.27           H  
ATOM   2206  HG  SER A 142      18.440  41.484 -24.693  1.00 23.30           H  
ATOM   2207  N   ALA A 143      18.217  37.099 -25.570  1.00 15.94           N  
ANISOU 2207  N   ALA A 143     1926   2222   1908    -87     22    155       N  
ATOM   2208  CA  ALA A 143      17.883  35.738 -25.974  1.00 14.66           C  
ANISOU 2208  CA  ALA A 143     1751   2061   1756    -44     47    136       C  
ATOM   2209  C   ALA A 143      19.040  34.767 -25.756  1.00 15.19           C  
ANISOU 2209  C   ALA A 143     1772   2174   1826    -22     71    134       C  
ATOM   2210  O   ALA A 143      19.098  33.715 -26.406  1.00 16.89           O  
ANISOU 2210  O   ALA A 143     1975   2401   2043      7     95    118       O  
ATOM   2211  CB  ALA A 143      17.447  35.710 -27.441  1.00 15.30           C  
ANISOU 2211  CB  ALA A 143     1849   2142   1821    -54     55    130       C  
ATOM   2212  H   ALA A 143      18.665  37.538 -26.158  1.00 19.13           H  
ATOM   2213  HA  ALA A 143      17.136  35.437 -25.434  1.00 17.59           H  
ATOM   2214  HB1 ALA A 143      18.141  36.113 -27.985  1.00 18.36           H  
ATOM   2215  HB2 ALA A 143      17.308  34.789 -27.711  1.00 18.36           H  
ATOM   2216  HB3 ALA A 143      16.621  36.211 -27.534  1.00 18.36           H  
ATOM   2217  N   GLN A 144      19.958  35.114 -24.851  1.00 16.66           N  
ANISOU 2217  N   GLN A 144     1933   2386   2011    -34     64    148       N  
ATOM   2218  CA  GLN A 144      21.175  34.343 -24.638  1.00 15.29           C  
ANISOU 2218  CA  GLN A 144     1709   2264   1836    -15     84    150       C  
ATOM   2219  C   GLN A 144      20.919  32.862 -24.412  1.00 16.19           C  
ANISOU 2219  C   GLN A 144     1812   2365   1974     44    103    134       C  
ATOM   2220  O   GLN A 144      21.765  32.032 -24.761  1.00 17.58           O  
ANISOU 2220  O   GLN A 144     1953   2579   2148     70    126    128       O  
ATOM   2221  CB  GLN A 144      21.917  34.918 -23.436  1.00 14.21           C  
ANISOU 2221  CB  GLN A 144     1553   2148   1700    -34     67    168       C  
ATOM   2222  CG  GLN A 144      23.215  34.269 -23.118  1.00 15.86           C  
ANISOU 2222  CG  GLN A 144     1706   2414   1905    -17     83    175       C  
ATOM   2223  CD  GLN A 144      23.835  34.898 -21.898  1.00 17.31           C  
ANISOU 2223  CD  GLN A 144     1873   2617   2086    -41     62    193       C  
ATOM   2224  OE1 GLN A 144      23.536  34.500 -20.780  1.00 16.87           O  
ANISOU 2224  OE1 GLN A 144     1820   2542   2049    -15     52    194       O  
ATOM   2225  NE2 GLN A 144      24.660  35.922 -22.106  1.00 17.25           N  
ANISOU 2225  NE2 GLN A 144     1852   2647   2053    -95     53    209       N  
ATOM   2226  H   GLN A 144      19.899  35.803 -24.340  1.00 19.99           H  
ATOM   2227  HA  GLN A 144      21.723  34.416 -25.435  1.00 18.35           H  
ATOM   2228  HB2 GLN A 144      22.097  35.856 -23.608  1.00 17.06           H  
ATOM   2229  HB3 GLN A 144      21.349  34.827 -22.654  1.00 17.06           H  
ATOM   2230  HG2 GLN A 144      23.071  33.327 -22.941  1.00 19.03           H  
ATOM   2231  HG3 GLN A 144      23.823  34.378 -23.865  1.00 19.03           H  
ATOM   2232 HE21 GLN A 144      24.814  36.194 -22.907  1.00 20.69           H  
ATOM   2233 HE22 GLN A 144      25.037  36.312 -21.439  1.00 20.69           H  
ATOM   2234  N   TYR A 145      19.796  32.496 -23.791  1.00 14.10           N  
ANISOU 2234  N   TYR A 145     1577   2049   1731     66     92    126       N  
ATOM   2235  CA  TYR A 145      19.615  31.077 -23.497  1.00 13.91           C  
ANISOU 2235  CA  TYR A 145     1544   2010   1729    117    107    114       C  
ATOM   2236  C   TYR A 145      19.490  30.261 -24.767  1.00 15.74           C  
ANISOU 2236  C   TYR A 145     1781   2243   1958    137    131     93       C  
ATOM   2237  O   TYR A 145      19.762  29.056 -24.747  1.00 16.75           O  
ANISOU 2237  O   TYR A 145     1895   2370   2100    179    149     82       O  
ATOM   2238  CB  TYR A 145      18.428  30.849 -22.551  1.00 15.34           C  
ANISOU 2238  CB  TYR A 145     1755   2142   1932    131     92    112       C  
ATOM   2239  CG  TYR A 145      16.984  30.696 -23.041  1.00 16.10           C  
ANISOU 2239  CG  TYR A 145     1890   2192   2034    133     88     97       C  
ATOM   2240  CD1 TYR A 145      16.503  29.486 -23.545  1.00 17.13           C  
ANISOU 2240  CD1 TYR A 145     2030   2302   2177    163    105     80       C  
ATOM   2241  CD2 TYR A 145      16.064  31.723 -22.853  1.00 18.28           C  
ANISOU 2241  CD2 TYR A 145     2195   2444   2307    107     67     99       C  
ATOM   2242  CE1 TYR A 145      15.161  29.337 -23.920  1.00 14.83           C  
ANISOU 2242  CE1 TYR A 145     1772   1974   1891    161    100     67       C  
ATOM   2243  CE2 TYR A 145      14.720  31.575 -23.216  1.00 18.30           C  
ANISOU 2243  CE2 TYR A 145     2228   2411   2315    112     63     86       C  
ATOM   2244  CZ  TYR A 145      14.272  30.379 -23.730  1.00 14.23           C  
ANISOU 2244  CZ  TYR A 145     1716   1880   1809    136     78     71       C  
ATOM   2245  OH  TYR A 145      12.941  30.251 -24.079  1.00 15.93           O  
ANISOU 2245  OH  TYR A 145     1959   2065   2028    136     72     60       O  
ATOM   2246  H   TYR A 145      19.160  33.019 -23.543  1.00 16.92           H  
ATOM   2247  HA  TYR A 145      20.390  30.751 -23.014  1.00 16.69           H  
ATOM   2248  HB2 TYR A 145      18.619  30.033 -22.062  1.00 18.41           H  
ATOM   2249  HB3 TYR A 145      18.412  31.604 -21.942  1.00 18.41           H  
ATOM   2250  HD1 TYR A 145      17.084  28.766 -23.635  1.00 20.56           H  
ATOM   2251  HD2 TYR A 145      16.348  32.524 -22.477  1.00 21.94           H  
ATOM   2252  HE1 TYR A 145      14.868  28.539 -24.296  1.00 17.80           H  
ATOM   2253  HE2 TYR A 145      14.130  32.286 -23.111  1.00 21.96           H  
ATOM   2254  HH  TYR A 145      12.693  29.455 -23.975  1.00 19.11           H  
ATOM   2255  N   GLY A 146      19.141  30.904 -25.879  1.00 15.28           N  
ANISOU 2255  N   GLY A 146     1740   2185   1879    107    132     87       N  
ATOM   2256  CA  GLY A 146      19.148  30.240 -27.161  1.00 12.98           C  
ANISOU 2256  CA  GLY A 146     1451   1904   1577    119    155     66       C  
ATOM   2257  C   GLY A 146      20.522  29.790 -27.610  1.00 17.98           C  
ANISOU 2257  C   GLY A 146     2039   2594   2197    134    181     62       C  
ATOM   2258  O   GLY A 146      20.622  28.983 -28.538  1.00 20.32           O  
ANISOU 2258  O   GLY A 146     2333   2900   2488    156    204     39       O  
ATOM   2259  H   GLY A 146      18.895  31.728 -25.911  1.00 18.33           H  
ATOM   2260  HA2 GLY A 146      18.577  29.457 -27.113  1.00 15.58           H  
ATOM   2261  HA3 GLY A 146      18.797  30.846 -27.832  1.00 15.58           H  
ATOM   2262  N   ASN A 147      21.588  30.302 -26.988  1.00 16.11           N  
ANISOU 2262  N   ASN A 147     1767   2400   1955    121    176     83       N  
ATOM   2263  CA  ASN A 147      22.939  29.860 -27.315  1.00 18.49           C  
ANISOU 2263  CA  ASN A 147     2018   2763   2243    138    200     81       C  
ATOM   2264  C   ASN A 147      23.375  28.643 -26.517  1.00 18.08           C  
ANISOU 2264  C   ASN A 147     1942   2709   2219    198    210     75       C  
ATOM   2265  O   ASN A 147      24.425  28.061 -26.822  1.00 17.69           O  
ANISOU 2265  O   ASN A 147     1850   2707   2163    227    232     68       O  
ATOM   2266  CB  ASN A 147      23.948  30.990 -27.099  1.00 16.70           C  
ANISOU 2266  CB  ASN A 147     1760   2592   1993     92    191    107       C  
ATOM   2267  CG  ASN A 147      23.868  32.032 -28.179  1.00 20.32           C  
ANISOU 2267  CG  ASN A 147     2233   3068   2419     36    190    112       C  
ATOM   2268  OD1 ASN A 147      23.506  31.729 -29.321  1.00 17.91           O  
ANISOU 2268  OD1 ASN A 147     1942   2762   2100     39    206     94       O  
ATOM   2269  ND2 ASN A 147      24.196  33.272 -27.836  1.00 19.91           N  
ANISOU 2269  ND2 ASN A 147     2181   3032   2352    -18    168    138       N  
ATOM   2270  H   ASN A 147      21.551  30.904 -26.374  1.00 19.33           H  
ATOM   2271  HA  ASN A 147      22.961  29.628 -28.257  1.00 22.19           H  
ATOM   2272  HB2 ASN A 147      23.767  31.420 -26.249  1.00 20.04           H  
ATOM   2273  HB3 ASN A 147      24.845  30.621 -27.100  1.00 20.04           H  
ATOM   2274 HD21 ASN A 147      24.166  33.903 -28.420  1.00 23.89           H  
ATOM   2275 HD22 ASN A 147      24.439  33.445 -27.029  1.00 23.89           H  
ATOM   2276  N   GLY A 148      22.586  28.239 -25.526  1.00 16.00           N  
ANISOU 2276  N   GLY A 148     1704   2391   1984    217    193     79       N  
ATOM   2277  CA  GLY A 148      22.899  27.074 -24.733  1.00 15.53           C  
ANISOU 2277  CA  GLY A 148     1629   2321   1952    272    198     78       C  
ATOM   2278  C   GLY A 148      22.897  27.259 -23.227  1.00 17.53           C  
ANISOU 2278  C   GLY A 148     1877   2564   2221    272    174    104       C  
ATOM   2279  O   GLY A 148      23.267  26.327 -22.510  1.00 18.34           O  
ANISOU 2279  O   GLY A 148     1963   2663   2344    316    175    109       O  
ATOM   2280  H   GLY A 148      21.856  28.633 -25.295  1.00 19.20           H  
ATOM   2281  HA2 GLY A 148      22.251  26.382 -24.938  1.00 18.64           H  
ATOM   2282  HA3 GLY A 148      23.783  26.763 -24.983  1.00 18.64           H  
ATOM   2283  N   VAL A 149      22.478  28.416 -22.722  1.00 17.75           N  
ANISOU 2283  N   VAL A 149     1921   2586   2240    225    151    119       N  
ATOM   2284  CA  VAL A 149      22.552  28.689 -21.268  1.00 18.04           C  
ANISOU 2284  CA  VAL A 149     1950   2619   2285    220    128    142       C  
ATOM   2285  C   VAL A 149      21.221  28.247 -20.667  1.00 15.07           C  
ANISOU 2285  C   VAL A 149     1615   2179   1929    233    117    138       C  
ATOM   2286  O   VAL A 149      20.339  29.050 -20.331  1.00 13.89           O  
ANISOU 2286  O   VAL A 149     1496   2004   1777    202     99    139       O  
ATOM   2287  CB  VAL A 149      22.894  30.150 -20.968  1.00 19.55           C  
ANISOU 2287  CB  VAL A 149     2136   2839   2454    164    109    158       C  
ATOM   2288  CG1 VAL A 149      23.042  30.334 -19.454  1.00 16.58           C  
ANISOU 2288  CG1 VAL A 149     1750   2465   2084    161     87    178       C  
ATOM   2289  CG2 VAL A 149      24.152  30.560 -21.709  1.00 14.92           C  
ANISOU 2289  CG2 VAL A 149     1508   2318   1843    144    122    163       C  
ATOM   2290  H   VAL A 149      22.148  29.060 -23.187  1.00 21.31           H  
ATOM   2291  HA  VAL A 149      23.246  28.131 -20.885  1.00 21.65           H  
ATOM   2292  HB  VAL A 149      22.180  30.732 -21.275  1.00 23.46           H  
ATOM   2293 HG11 VAL A 149      23.486  31.178 -19.280  1.00 19.89           H  
ATOM   2294 HG12 VAL A 149      22.161  30.334 -19.048  1.00 19.89           H  
ATOM   2295 HG13 VAL A 149      23.570  29.602 -19.098  1.00 19.89           H  
ATOM   2296 HG21 VAL A 149      23.928  30.744 -22.635  1.00 17.90           H  
ATOM   2297 HG22 VAL A 149      24.519  31.356 -21.293  1.00 17.90           H  
ATOM   2298 HG23 VAL A 149      24.796  29.836 -21.663  1.00 17.90           H  
ATOM   2299  N   VAL A 150      21.107  26.923 -20.475  1.00 15.47           N  
ANISOU 2299  N   VAL A 150     1668   2207   2003    280    126    132       N  
ATOM   2300  CA AVAL A 150      19.894  26.235 -20.030  0.55 13.97           C  
ANISOU 2300  CA AVAL A 150     1516   1960   1833    295    120    128       C  
ATOM   2301  CA BVAL A 150      19.910  26.312 -19.919  0.45 15.99           C  
ANISOU 2301  CA BVAL A 150     1771   2218   2089    293    118    130       C  
ATOM   2302  C   VAL A 150      20.308  25.053 -19.161  1.00 13.27           C  
ANISOU 2302  C   VAL A 150     1412   1863   1766    340    120    141       C  
ATOM   2303  O   VAL A 150      21.339  24.426 -19.430  1.00 17.54           O  
ANISOU 2303  O   VAL A 150     1924   2430   2311    375    134    141       O  
ATOM   2304  CB AVAL A 150      19.089  25.712 -21.247  0.55 16.40           C  
ANISOU 2304  CB AVAL A 150     1854   2233   2144    302    135    101       C  
ATOM   2305  CB BVAL A 150      18.832  25.927 -20.967  0.45 19.80           C  
ANISOU 2305  CB BVAL A 150     2291   2658   2575    293    128    105       C  
ATOM   2306  CG1AVAL A 150      17.906  24.863 -20.819  0.55 21.68           C  
ANISOU 2306  CG1AVAL A 150     2558   2846   2833    315    130     97       C  
ATOM   2307  CG1BVAL A 150      18.285  27.150 -21.668  0.45 19.77           C  
ANISOU 2307  CG1BVAL A 150     2304   2657   2550    248    122     98       C  
ATOM   2308  CG2AVAL A 150      18.639  26.850 -22.128  0.55 17.82           C  
ANISOU 2308  CG2AVAL A 150     2049   2420   2302    258    133     91       C  
ATOM   2309  CG2BVAL A 150      19.373  24.900 -21.961  0.45 20.54           C  
ANISOU 2309  CG2BVAL A 150     2376   2754   2673    329    153     85       C  
ATOM   2310  H  AVAL A 150      21.757  26.375 -20.604  0.55 18.56           H  
ATOM   2311  H  BVAL A 150      21.725  26.356 -20.665  0.45 18.56           H  
ATOM   2312  HA AVAL A 150      19.352  26.846 -19.507  0.55 16.77           H  
ATOM   2313  HA BVAL A 150      19.529  26.974 -19.321  0.45 19.19           H  
ATOM   2314  HB AVAL A 150      19.678  25.142 -21.766  0.55 19.68           H  
ATOM   2315  HB BVAL A 150      18.089  25.512 -20.502  0.45 23.76           H  
ATOM   2316 HG11AVAL A 150      17.453  24.531 -21.609  0.55 26.02           H  
ATOM   2317 HG11BVAL A 150      17.631  27.578 -21.092  0.45 23.72           H  
ATOM   2318 HG12AVAL A 150      18.227  24.120 -20.284  0.55 26.02           H  
ATOM   2319 HG12BVAL A 150      19.015  27.762 -21.851  0.45 23.72           H  
ATOM   2320 HG13AVAL A 150      17.299  25.410 -20.295  0.55 26.02           H  
ATOM   2321 HG13BVAL A 150      17.865  26.877 -22.498  0.45 23.72           H  
ATOM   2322 HG21AVAL A 150      18.078  26.499 -22.836  0.55 21.38           H  
ATOM   2323 HG21BVAL A 150      19.930  25.354 -22.612  0.45 24.64           H  
ATOM   2324 HG22AVAL A 150      18.138  27.485 -21.592  0.55 21.38           H  
ATOM   2325 HG22BVAL A 150      19.897  24.241 -21.479  0.45 24.64           H  
ATOM   2326 HG23AVAL A 150      19.420  27.282 -22.508  0.55 21.38           H  
ATOM   2327 HG23BVAL A 150      18.628  24.468 -22.406  0.45 24.64           H  
ATOM   2328  N   GLY A 151      19.458  24.682 -18.200  1.00 15.46           N  
ANISOU 2328  N   GLY A 151     1713   2103   2057    343    106    152       N  
ATOM   2329  CA  GLY A 151      19.582  23.431 -17.467  1.00 15.37           C  
ANISOU 2329  CA  GLY A 151     1702   2071   2068    384    104    166       C  
ATOM   2330  C   GLY A 151      18.283  23.108 -16.760  1.00 15.42           C  
ANISOU 2330  C   GLY A 151     1745   2031   2085    373     91    172       C  
ATOM   2331  O   GLY A 151      17.347  23.911 -16.749  1.00 15.84           O  
ANISOU 2331  O   GLY A 151     1818   2076   2127    337     84    165       O  
ATOM   2332  H   GLY A 151      18.784  25.153 -17.949  1.00 18.55           H  
ATOM   2333  HA2 GLY A 151      19.794  22.709 -18.080  1.00 18.45           H  
ATOM   2334  HA3 GLY A 151      20.290  23.503 -16.808  1.00 18.45           H  
ATOM   2335  N   ALA A 152      18.232  21.927 -16.145  1.00 17.29           N  
ANISOU 2335  N   ALA A 152     1989   2239   2341    405     88    186       N  
ATOM   2336  CA  ALA A 152      17.019  21.478 -15.473  1.00 16.75           C  
ANISOU 2336  CA  ALA A 152     1954   2129   2281    393     78    194       C  
ATOM   2337  C   ALA A 152      17.105  21.626 -13.957  1.00 17.02           C  
ANISOU 2337  C   ALA A 152     1976   2181   2311    386     58    227       C  
ATOM   2338  O   ALA A 152      18.184  21.749 -13.373  1.00 16.42           O  
ANISOU 2338  O   ALA A 152     1866   2141   2231    400     52    246       O  
ATOM   2339  CB  ALA A 152      16.713  20.015 -15.818  1.00 18.06           C  
ANISOU 2339  CB  ALA A 152     2148   2243   2472    425     85    189       C  
ATOM   2340  H   ALA A 152      18.888  21.373 -16.106  1.00 20.75           H  
ATOM   2341  HA  ALA A 152      16.290  22.039 -15.782  1.00 20.10           H  
ATOM   2342  HB1 ALA A 152      15.969  19.711 -15.274  1.00 21.68           H  
ATOM   2343  HB2 ALA A 152      16.482  19.953 -16.758  1.00 21.68           H  
ATOM   2344  HB3 ALA A 152      17.499  19.476 -15.634  1.00 21.68           H  
ATOM   2345  N   ILE A 153      15.929  21.612 -13.332  1.00 15.45           N  
ANISOU 2345  N   ILE A 153     1801   1959   2109    362     49    232       N  
ATOM   2346  CA  ILE A 153      15.770  21.631 -11.884  1.00 17.08           C  
ANISOU 2346  CA  ILE A 153     2002   2180   2309    352     31    262       C  
ATOM   2347  C   ILE A 153      14.855  20.471 -11.512  1.00 17.31           C  
ANISOU 2347  C   ILE A 153     2062   2163   2353    356     28    274       C  
ATOM   2348  O   ILE A 153      13.763  20.341 -12.075  1.00 16.33           O  
ANISOU 2348  O   ILE A 153     1965   2009   2231    338     34    256       O  
ATOM   2349  CB  ILE A 153      15.167  22.965 -11.400  1.00 14.66           C  
ANISOU 2349  CB  ILE A 153     1693   1899   1978    311     22    254       C  
ATOM   2350  CG1 ILE A 153      16.045  24.150 -11.799  1.00 18.08           C  
ANISOU 2350  CG1 ILE A 153     2102   2372   2397    301     23    243       C  
ATOM   2351  CG2 ILE A 153      14.946  22.916  -9.905  1.00 15.55           C  
ANISOU 2351  CG2 ILE A 153     1800   2027   2079    301      6    282       C  
ATOM   2352  CD1 ILE A 153      15.390  25.503 -11.521  1.00 20.42           C  
ANISOU 2352  CD1 ILE A 153     2405   2682   2672    263     14    230       C  
ATOM   2353  H   ILE A 153      15.177  21.591 -13.748  1.00 18.54           H  
ATOM   2354  HA  ILE A 153      16.631  21.510 -11.452  1.00 20.50           H  
ATOM   2355  HB  ILE A 153      14.309  23.089 -11.835  1.00 17.59           H  
ATOM   2356 HG12 ILE A 153      16.874  24.111 -11.297  1.00 21.70           H  
ATOM   2357 HG13 ILE A 153      16.230  24.098 -12.750  1.00 21.70           H  
ATOM   2358 HG21 ILE A 153      14.557  23.757  -9.616  1.00 18.66           H  
ATOM   2359 HG22 ILE A 153      14.344  22.185  -9.698  1.00 18.66           H  
ATOM   2360 HG23 ILE A 153      15.799  22.777  -9.464  1.00 18.66           H  
ATOM   2361 HD11 ILE A 153      15.946  26.205 -11.893  1.00 24.50           H  
ATOM   2362 HD12 ILE A 153      14.514  25.521 -11.936  1.00 24.50           H  
ATOM   2363 HD13 ILE A 153      15.304  25.621 -10.562  1.00 24.50           H  
ATOM   2364  N   GLN A 154      15.298  19.623 -10.587  1.00 14.81           N  
ANISOU 2364  N   GLN A 154     1741   1842   2044    376     18    307       N  
ATOM   2365  CA  GLN A 154      14.505  18.488 -10.120  1.00 14.81           C  
ANISOU 2365  CA  GLN A 154     1772   1798   2057    376     12    326       C  
ATOM   2366  C   GLN A 154      14.459  18.566  -8.599  1.00 15.21           C  
ANISOU 2366  C   GLN A 154     1812   1876   2092    362     -6    363       C  
ATOM   2367  O   GLN A 154      15.468  18.319  -7.930  1.00 17.91           O  
ANISOU 2367  O   GLN A 154     2132   2239   2436    386    -17    391       O  
ATOM   2368  CB  GLN A 154      15.081  17.151 -10.592  1.00 15.89           C  
ANISOU 2368  CB  GLN A 154     1924   1892   2223    420     16    333       C  
ATOM   2369  CG  GLN A 154      14.285  15.972 -10.078  1.00 18.54           C  
ANISOU 2369  CG  GLN A 154     2296   2176   2572    415      7    356       C  
ATOM   2370  CD  GLN A 154      14.738  14.664 -10.640  1.00 23.01           C  
ANISOU 2370  CD  GLN A 154     2886   2688   3168    458     10    357       C  
ATOM   2371  OE1 GLN A 154      15.217  14.604 -11.759  1.00 21.27           O  
ANISOU 2371  OE1 GLN A 154     2665   2457   2958    484     26    325       O  
ATOM   2372  NE2 GLN A 154      14.595  13.603  -9.861  1.00 22.09           N  
ANISOU 2372  NE2 GLN A 154     2794   2534   3065    466     -4    393       N  
ATOM   2373  H   GLN A 154      16.068  19.686 -10.210  1.00 17.77           H  
ATOM   2374  HA  GLN A 154      13.603  18.552 -10.470  1.00 17.77           H  
ATOM   2375  HB2 GLN A 154      15.068  17.125 -11.562  1.00 19.07           H  
ATOM   2376  HB3 GLN A 154      15.991  17.066 -10.270  1.00 19.07           H  
ATOM   2377  HG2 GLN A 154      14.375  15.929  -9.113  1.00 22.25           H  
ATOM   2378  HG3 GLN A 154      13.353  16.093 -10.319  1.00 22.25           H  
ATOM   2379 HE21 GLN A 154      14.255  13.689  -9.076  1.00 26.51           H  
ATOM   2380 HE22 GLN A 154      14.842  12.829 -10.141  1.00 26.51           H  
ATOM   2381  N   ILE A 155      13.309  18.947  -8.056  1.00 14.81           N  
ANISOU 2381  N   ILE A 155     1772   1831   2024    323    -10    362       N  
ATOM   2382  CA  ILE A 155      13.106  19.008  -6.615  1.00 15.32           C  
ANISOU 2382  CA  ILE A 155     1828   1924   2069    304    -25    395       C  
ATOM   2383  C   ILE A 155      12.217  17.834  -6.234  1.00 18.15           C  
ANISOU 2383  C   ILE A 155     2218   2244   2436    294    -29    418       C  
ATOM   2384  O   ILE A 155      11.022  17.817  -6.557  1.00 15.28           O  
ANISOU 2384  O   ILE A 155     1874   1863   2068    266    -22    402       O  
ATOM   2385  CB  ILE A 155      12.489  20.340  -6.172  1.00 13.76           C  
ANISOU 2385  CB  ILE A 155     1618   1770   1841    269    -26    376       C  
ATOM   2386  CG1 ILE A 155      13.426  21.495  -6.523  1.00 15.71           C  
ANISOU 2386  CG1 ILE A 155     1839   2051   2080    274    -25    356       C  
ATOM   2387  CG2 ILE A 155      12.233  20.282  -4.689  1.00 15.55           C  
ANISOU 2387  CG2 ILE A 155     1838   2027   2044    250    -40    407       C  
ATOM   2388  CD1 ILE A 155      12.819  22.846  -6.376  1.00 23.00           C  
ANISOU 2388  CD1 ILE A 155     2758   3002   2978    244    -25    330       C  
ATOM   2389  H   ILE A 155      12.619  19.180  -8.514  1.00 17.77           H  
ATOM   2390  HA  ILE A 155      13.961  18.909  -6.167  1.00 18.39           H  
ATOM   2391  HB  ILE A 155      11.651  20.489  -6.637  1.00 16.51           H  
ATOM   2392 HG12 ILE A 155      14.198  21.455  -5.938  1.00 18.85           H  
ATOM   2393 HG13 ILE A 155      13.704  21.398  -7.447  1.00 18.85           H  
ATOM   2394 HG21 ILE A 155      11.387  19.835  -4.532  1.00 18.66           H  
ATOM   2395 HG22 ILE A 155      12.953  19.790  -4.264  1.00 18.66           H  
ATOM   2396 HG23 ILE A 155      12.200  21.186  -4.339  1.00 18.66           H  
ATOM   2397 HD11 ILE A 155      12.026  22.898  -6.933  1.00 27.60           H  
ATOM   2398 HD12 ILE A 155      12.579  22.984  -5.446  1.00 27.60           H  
ATOM   2399 HD13 ILE A 155      13.464  23.514  -6.654  1.00 27.60           H  
ATOM   2400  N   ASN A 156      12.795  16.841  -5.564  1.00 16.10           N  
ANISOU 2400  N   ASN A 156     1962   1968   2186    315    -42    458       N  
ATOM   2401  CA  ASN A 156      12.036  15.642  -5.238  1.00 14.86           C  
ANISOU 2401  CA  ASN A 156     1839   1767   2039    303    -48    485       C  
ATOM   2402  C   ASN A 156      11.012  15.930  -4.149  1.00 15.74           C  
ANISOU 2402  C   ASN A 156     1950   1911   2120    256    -55    502       C  
ATOM   2403  O   ASN A 156      11.196  16.811  -3.304  1.00 15.62           O  
ANISOU 2403  O   ASN A 156     1906   1951   2076    244    -60    507       O  
ATOM   2404  CB  ASN A 156      12.972  14.520  -4.808  1.00 15.39           C  
ANISOU 2404  CB  ASN A 156     1914   1807   2127    342    -63    526       C  
ATOM   2405  CG  ASN A 156      13.798  13.993  -5.953  1.00 20.77           C  
ANISOU 2405  CG  ASN A 156     2603   2448   2842    391    -54    506       C  
ATOM   2406  OD1 ASN A 156      13.265  13.609  -6.993  1.00 23.51           O  
ANISOU 2406  OD1 ASN A 156     2977   2749   3205    390    -41    477       O  
ATOM   2407  ND2 ASN A 156      15.108  14.000  -5.786  1.00 29.63           N  
ANISOU 2407  ND2 ASN A 156     3696   3591   3970    433    -60    519       N  
ATOM   2408  H   ASN A 156      13.611  16.837  -5.292  1.00 19.31           H  
ATOM   2409  HA  ASN A 156      11.555  15.341  -6.024  1.00 17.83           H  
ATOM   2410  HB2 ASN A 156      13.578  14.855  -4.128  1.00 18.47           H  
ATOM   2411  HB3 ASN A 156      12.447  13.787  -4.452  1.00 18.47           H  
ATOM   2412 HD21 ASN A 156      15.623  13.710  -6.410  1.00 35.55           H  
ATOM   2413 HD22 ASN A 156      15.446  14.296  -5.052  1.00 35.55           H  
ATOM   2414  N   GLY A 157       9.905  15.184  -4.207  1.00 13.59           N  
ANISOU 2414  N   GLY A 157     1708   1604   1851    229    -53    509       N  
ATOM   2415  CA  GLY A 157       8.817  15.271  -3.261  1.00 14.19           C  
ANISOU 2415  CA  GLY A 157     1784   1709   1898    182    -57    526       C  
ATOM   2416  C   GLY A 157       7.770  14.219  -3.591  1.00 15.61           C  
ANISOU 2416  C   GLY A 157     2001   1841   2090    155    -56    535       C  
ATOM   2417  O   GLY A 157       8.040  13.265  -4.326  1.00 16.24           O  
ANISOU 2417  O   GLY A 157     2110   1858   2201    176    -57    536       O  
ATOM   2418  H   GLY A 157       9.764  14.596  -4.818  1.00 16.31           H  
ATOM   2419  HA2 GLY A 157       9.146  15.120  -2.361  1.00 17.03           H  
ATOM   2420  HA3 GLY A 157       8.408  16.150  -3.305  1.00 17.03           H  
ATOM   2421  N   PRO A 158       6.558  14.361  -3.067  1.00 14.85           N  
ANISOU 2421  N   PRO A 158     1903   1772   1967    108    -54    539       N  
ATOM   2422  CA  PRO A 158       5.524  13.345  -3.308  1.00 16.23           C  
ANISOU 2422  CA  PRO A 158     2112   1906   2150     73    -54    551       C  
ATOM   2423  C   PRO A 158       4.961  13.461  -4.720  1.00 15.68           C  
ANISOU 2423  C   PRO A 158     2054   1806   2097     72    -40    504       C  
ATOM   2424  O   PRO A 158       5.274  14.386  -5.471  1.00 15.72           O  
ANISOU 2424  O   PRO A 158     2042   1826   2106     94    -29    464       O  
ATOM   2425  CB  PRO A 158       4.464  13.658  -2.244  1.00 17.50           C  
ANISOU 2425  CB  PRO A 158     2255   2124   2270     23    -54    567       C  
ATOM   2426  CG  PRO A 158       4.611  15.138  -1.998  1.00 15.67           C  
ANISOU 2426  CG  PRO A 158     1982   1958   2014     33    -46    535       C  
ATOM   2427  CD  PRO A 158       6.098  15.425  -2.154  1.00 15.68           C  
ANISOU 2427  CD  PRO A 158     1975   1950   2032     83    -51    534       C  
ATOM   2428  HA  PRO A 158       5.867  12.449  -3.165  1.00 19.48           H  
ATOM   2429  HB2 PRO A 158       3.580  13.445  -2.582  1.00 21.00           H  
ATOM   2430  HB3 PRO A 158       4.641  13.149  -1.437  1.00 21.00           H  
ATOM   2431  HG2 PRO A 158       4.094  15.634  -2.652  1.00 18.81           H  
ATOM   2432  HG3 PRO A 158       4.309  15.355  -1.103  1.00 18.81           H  
ATOM   2433  HD2 PRO A 158       6.241  16.301  -2.545  1.00 18.82           H  
ATOM   2434  HD3 PRO A 158       6.552  15.366  -1.298  1.00 18.82           H  
ATOM   2435  N   ALA A 159       4.111  12.494  -5.074  1.00 17.16           N  
ANISOU 2435  N   ALA A 159     2274   1950   2294     40    -41    511       N  
ATOM   2436  CA  ALA A 159       3.505  12.450  -6.401  1.00 17.14           C  
ANISOU 2436  CA  ALA A 159     2288   1918   2307     33    -31    470       C  
ATOM   2437  C   ALA A 159       2.083  11.910  -6.294  1.00 16.55           C  
ANISOU 2437  C   ALA A 159     2227   1843   2217    -27    -32    480       C  
ATOM   2438  O   ALA A 159       1.711  11.282  -5.300  1.00 17.60           O  
ANISOU 2438  O   ALA A 159     2368   1982   2338    -60    -42    523       O  
ATOM   2439  CB  ALA A 159       4.342  11.600  -7.370  1.00 15.80           C  
ANISOU 2439  CB  ALA A 159     2153   1674   2174     71    -32    461       C  
ATOM   2440  H   ALA A 159       3.869  11.849  -4.558  1.00 20.59           H  
ATOM   2441  HA  ALA A 159       3.448  13.351  -6.757  1.00 20.57           H  
ATOM   2442  HB1 ALA A 159       3.935  11.632  -8.250  1.00 18.95           H  
ATOM   2443  HB2 ALA A 159       5.242  11.959  -7.408  1.00 18.95           H  
ATOM   2444  HB3 ALA A 159       4.364  10.685  -7.049  1.00 18.95           H  
ATOM   2445  N   SER A 160       1.286  12.170  -7.332  1.00 16.82           N  
ANISOU 2445  N   SER A 160     2262   1876   2253    -44    -22    441       N  
ATOM   2446  CA  SER A 160      -0.132  11.829  -7.354  1.00 16.55           C  
ANISOU 2446  CA  SER A 160     2232   1854   2203   -102    -22    443       C  
ATOM   2447  C   SER A 160      -0.413  10.450  -7.944  1.00 17.53           C  
ANISOU 2447  C   SER A 160     2408   1904   2349   -127    -29    453       C  
ATOM   2448  O   SER A 160      -1.582  10.078  -8.094  1.00 16.70           O  
ANISOU 2448  O   SER A 160     2309   1804   2232   -181    -30    453       O  
ATOM   2449  CB  SER A 160      -0.901  12.894  -8.147  1.00 15.33           C  
ANISOU 2449  CB  SER A 160     2047   1743   2034   -108     -9    396       C  
ATOM   2450  OG  SER A 160      -0.429  12.954  -9.482  1.00 16.57           O  
ANISOU 2450  OG  SER A 160     2222   1860   2216    -77     -4    359       O  
ATOM   2451  H   SER A 160       1.555  12.554  -8.053  1.00 20.18           H  
ATOM   2452  HA  SER A 160      -0.465  11.825  -6.443  1.00 19.86           H  
ATOM   2453  HB2 SER A 160      -1.844  12.665  -8.153  1.00 18.39           H  
ATOM   2454  HB3 SER A 160      -0.772  13.758  -7.725  1.00 18.39           H  
ATOM   2455  HG  SER A 160      -0.075  12.223  -9.695  1.00 19.89           H  
ATOM   2456  N   LEU A 161       0.613   9.696  -8.308  1.00 17.78           N  
ANISOU 2456  N   LEU A 161     2476   1866   2413    -89    -35    458       N  
ATOM   2457  CA  LEU A 161       0.462   8.311  -8.722  1.00 17.82           C  
ANISOU 2457  CA  LEU A 161     2538   1792   2442   -108    -46    470       C  
ATOM   2458  C   LEU A 161       1.683   7.535  -8.257  1.00 20.03           C  
ANISOU 2458  C   LEU A 161     2846   2017   2748    -64    -58    503       C  
ATOM   2459  O   LEU A 161       2.793   8.078  -8.223  1.00 19.55           O  
ANISOU 2459  O   LEU A 161     2764   1968   2695     -7    -54    495       O  
ATOM   2460  CB  LEU A 161       0.332   8.204 -10.249  1.00 20.29           C  
ANISOU 2460  CB  LEU A 161     2872   2066   2773   -100    -37    419       C  
ATOM   2461  CG  LEU A 161      -0.704   7.269 -10.872  1.00 45.93           C  
ANISOU 2461  CG  LEU A 161     6159   5269   6023   -156    -43    412       C  
ATOM   2462  CD1 LEU A 161      -2.100   7.450 -10.334  1.00 23.72           C  
ANISOU 2462  CD1 LEU A 161     3323   2513   3177   -226    -45    428       C  
ATOM   2463  CD2 LEU A 161      -0.665   7.532 -12.387  1.00 29.47           C  
ANISOU 2463  CD2 LEU A 161     4081   3166   3949   -136    -32    355       C  
ATOM   2464  H   LEU A 161       1.427   9.973  -8.322  1.00 21.33           H  
ATOM   2465  HA  LEU A 161      -0.328   7.918  -8.319  1.00 21.39           H  
ATOM   2466  HB2 LEU A 161       0.125   9.092 -10.581  1.00 24.35           H  
ATOM   2467  HB3 LEU A 161       1.193   7.915 -10.589  1.00 24.35           H  
ATOM   2468  HG  LEU A 161      -0.487   6.349 -10.655  1.00 55.12           H  
ATOM   2469 HD11 LEU A 161      -2.642   6.690 -10.597  1.00 28.46           H  
ATOM   2470 HD12 LEU A 161      -2.060   7.509  -9.367  1.00 28.46           H  
ATOM   2471 HD13 LEU A 161      -2.476   8.266 -10.700  1.00 28.46           H  
ATOM   2472 HD21 LEU A 161      -1.144   6.824 -12.843  1.00 35.36           H  
ATOM   2473 HD22 LEU A 161      -1.085   8.387 -12.569  1.00 35.36           H  
ATOM   2474 HD23 LEU A 161       0.260   7.548 -12.680  1.00 35.36           H  
ATOM   2475  N   PRO A 162       1.515   6.263  -7.896  1.00 20.13           N  
ANISOU 2475  N   PRO A 162     2907   1968   2773    -90    -74    540       N  
ATOM   2476  CA  PRO A 162       2.695   5.421  -7.651  1.00 20.26           C  
ANISOU 2476  CA  PRO A 162     2958   1920   2821    -39    -87    567       C  
ATOM   2477  C   PRO A 162       3.467   5.162  -8.934  1.00 19.68           C  
ANISOU 2477  C   PRO A 162     2910   1788   2781     16    -79    522       C  
ATOM   2478  O   PRO A 162       2.904   5.104 -10.030  1.00 21.53           O  
ANISOU 2478  O   PRO A 162     3159   2001   3019     -2    -70    479       O  
ATOM   2479  CB  PRO A 162       2.111   4.121  -7.081  1.00 24.24           C  
ANISOU 2479  CB  PRO A 162     3514   2366   3329    -90   -108    616       C  
ATOM   2480  CG  PRO A 162       0.691   4.091  -7.554  1.00 31.74           C  
ANISOU 2480  CG  PRO A 162     4469   3330   4260   -162   -102    597       C  
ATOM   2481  CD  PRO A 162       0.248   5.536  -7.676  1.00 21.37           C  
ANISOU 2481  CD  PRO A 162     3090   2114   2917   -167    -83    562       C  
ATOM   2482  HA  PRO A 162       3.277   5.829  -6.990  1.00 24.31           H  
ATOM   2483  HB2 PRO A 162       2.607   3.360  -7.421  1.00 29.09           H  
ATOM   2484  HB3 PRO A 162       2.154   4.138  -6.112  1.00 29.09           H  
ATOM   2485  HG2 PRO A 162       0.645   3.646  -8.414  1.00 38.09           H  
ATOM   2486  HG3 PRO A 162       0.143   3.620  -6.907  1.00 38.09           H  
ATOM   2487  HD2 PRO A 162      -0.351   5.651  -8.431  1.00 25.64           H  
ATOM   2488  HD3 PRO A 162      -0.184   5.835  -6.861  1.00 25.64           H  
ATOM   2489  N   TYR A 163       4.778   5.005  -8.784  1.00 22.30           N  
ANISOU 2489  N   TYR A 163     3242   2097   3135     84    -83    531       N  
ATOM   2490  CA  TYR A 163       5.627   4.629  -9.905  1.00 20.18           C  
ANISOU 2490  CA  TYR A 163     2997   1772   2898    142    -76    492       C  
ATOM   2491  C   TYR A 163       6.898   4.001  -9.361  1.00 22.10           C  
ANISOU 2491  C   TYR A 163     3253   1977   3168    206    -89    524       C  
ATOM   2492  O   TYR A 163       7.333   4.306  -8.249  1.00 19.85           O  
ANISOU 2492  O   TYR A 163     2939   1734   2871    216    -99    567       O  
ATOM   2493  CB  TYR A 163       5.971   5.828 -10.806  1.00 17.67           C  
ANISOU 2493  CB  TYR A 163     2633   1509   2571    171    -52    437       C  
ATOM   2494  CG  TYR A 163       6.656   6.954 -10.076  1.00 18.60           C  
ANISOU 2494  CG  TYR A 163     2692   1704   2671    197    -49    450       C  
ATOM   2495  CD1 TYR A 163       8.038   6.969  -9.909  1.00 21.43           C  
ANISOU 2495  CD1 TYR A 163     3035   2062   3046    264    -50    459       C  
ATOM   2496  CD2 TYR A 163       5.918   7.999  -9.547  1.00 21.03           C  
ANISOU 2496  CD2 TYR A 163     2958   2087   2945    155    -44    454       C  
ATOM   2497  CE1 TYR A 163       8.662   7.997  -9.217  1.00 18.53           C  
ANISOU 2497  CE1 TYR A 163     2613   1766   2660    281    -49    471       C  
ATOM   2498  CE2 TYR A 163       6.526   9.032  -8.869  1.00 19.97           C  
ANISOU 2498  CE2 TYR A 163     2775   2021   2794    175    -42    463       C  
ATOM   2499  CZ  TYR A 163       7.891   9.026  -8.708  1.00 20.36           C  
ANISOU 2499  CZ  TYR A 163     2811   2068   2858    235    -45    472       C  
ATOM   2500  OH  TYR A 163       8.476  10.052  -8.021  1.00 19.00           O  
ANISOU 2500  OH  TYR A 163     2590   1963   2666    249    -44    481       O  
ATOM   2501  H   TYR A 163       5.200   5.112  -8.042  1.00 26.76           H  
ATOM   2502  HA  TYR A 163       5.159   3.975 -10.447  1.00 24.21           H  
ATOM   2503  HB2 TYR A 163       6.564   5.527 -11.512  1.00 21.20           H  
ATOM   2504  HB3 TYR A 163       5.150   6.177 -11.187  1.00 21.20           H  
ATOM   2505  HD1 TYR A 163       8.551   6.280 -10.266  1.00 25.72           H  
ATOM   2506  HD2 TYR A 163       4.993   8.003  -9.651  1.00 25.23           H  
ATOM   2507  HE1 TYR A 163       9.584   7.995  -9.097  1.00 22.23           H  
ATOM   2508  HE2 TYR A 163       6.016   9.728  -8.522  1.00 23.97           H  
ATOM   2509  HH  TYR A 163       7.966  10.313  -7.407  1.00 22.80           H  
ATOM   2510  N   ASP A 164       7.516   3.160 -10.175  1.00 19.44           N  
ANISOU 2510  N   ASP A 164     2958   1564   2865    254    -89    502       N  
ATOM   2511  CA  ASP A 164       8.655   2.393  -9.698  1.00 22.99           C  
ANISOU 2511  CA  ASP A 164     3426   1967   3343    318   -105    534       C  
ATOM   2512  C   ASP A 164       9.965   3.152  -9.817  1.00 23.94           C  
ANISOU 2512  C   ASP A 164     3493   2138   3467    390    -93    518       C  
ATOM   2513  O   ASP A 164      10.767   3.147  -8.875  1.00 26.98           O  
ANISOU 2513  O   ASP A 164     3856   2543   3854    424   -107    561       O  
ATOM   2514  CB  ASP A 164       8.736   1.084 -10.473  1.00 24.27           C  
ANISOU 2514  CB  ASP A 164     3660   2021   3542    340   -111    516       C  
ATOM   2515  CG  ASP A 164       7.480   0.280 -10.336  1.00 25.83           C  
ANISOU 2515  CG  ASP A 164     3910   2170   3736    262   -123    534       C  
ATOM   2516  OD1 ASP A 164       7.163  -0.113  -9.195  1.00 28.27           O  
ANISOU 2516  OD1 ASP A 164     4225   2483   4032    227   -139    591       O  
ATOM   2517  OD2 ASP A 164       6.782   0.093 -11.350  1.00 23.59           O  
ANISOU 2517  OD2 ASP A 164     3656   1855   3453    231   -114    489       O  
ATOM   2518  H   ASP A 164       7.298   3.018 -10.995  1.00 23.33           H  
ATOM   2519  HA  ASP A 164       8.530   2.188  -8.758  1.00 27.59           H  
ATOM   2520  HB2 ASP A 164       8.872   1.277 -11.414  1.00 29.13           H  
ATOM   2521  HB3 ASP A 164       9.474   0.555 -10.133  1.00 29.13           H  
ATOM   2522  N   THR A 165      10.174   3.823 -10.948  1.00 21.52           N  
ANISOU 2522  N   THR A 165     3162   1856   3157    410    -68    459       N  
ATOM   2523  CA  THR A 165      11.458   4.400 -11.323  1.00 21.40           C  
ANISOU 2523  CA  THR A 165     3103   1880   3148    480    -55    436       C  
ATOM   2524  C   THR A 165      11.265   5.812 -11.853  1.00 18.75           C  
ANISOU 2524  C   THR A 165     2715   1625   2783    458    -33    398       C  
ATOM   2525  O   THR A 165      10.394   6.043 -12.694  1.00 22.85           O  
ANISOU 2525  O   THR A 165     3248   2142   3293    419    -21    360       O  
ATOM   2526  CB  THR A 165      12.119   3.533 -12.402  1.00 28.43           C  
ANISOU 2526  CB  THR A 165     4030   2702   4071    540    -47    397       C  
ATOM   2527  OG1 THR A 165      12.410   2.241 -11.858  1.00 48.38           O  
ANISOU 2527  OG1 THR A 165     6594   5167   6623    554    -79    423       O  
ATOM   2528  CG2 THR A 165      13.382   4.169 -12.933  1.00 30.07           C  
ANISOU 2528  CG2 THR A 165     4183   2963   4278    601    -32    363       C  
ATOM   2529  H   THR A 165       9.561   3.960 -11.535  1.00 25.82           H  
ATOM   2530  HA  THR A 165      12.030   4.457 -10.542  1.00 25.68           H  
ATOM   2531  HB  THR A 165      11.511   3.440 -13.152  1.00 34.12           H  
ATOM   2532  HG1 THR A 165      12.795   2.322 -11.116  1.00 58.06           H  
ATOM   2533 HG21 THR A 165      13.826   3.563 -13.547  1.00 36.08           H  
ATOM   2534 HG22 THR A 165      13.168   4.991 -13.403  1.00 36.08           H  
ATOM   2535 HG23 THR A 165      13.985   4.373 -12.201  1.00 36.08           H  
ATOM   2536  N   ASP A 166      12.086   6.750 -11.377  1.00 18.34           N  
ANISOU 2536  N   ASP A 166     2606   1645   2718    483    -30    408       N  
ATOM   2537  CA  ASP A 166      12.150   8.104 -11.932  1.00 17.80           C  
ANISOU 2537  CA  ASP A 166     2490   1649   2626    474    -11    372       C  
ATOM   2538  C   ASP A 166      13.244   8.127 -12.994  1.00 21.51           C  
ANISOU 2538  C   ASP A 166     2946   2118   3110    535      7    332       C  
ATOM   2539  O   ASP A 166      14.428   7.969 -12.679  1.00 23.84           O  
ANISOU 2539  O   ASP A 166     3218   2423   3417    591      3    348       O  
ATOM   2540  CB  ASP A 166      12.424   9.119 -10.821  1.00 22.04           C  
ANISOU 2540  CB  ASP A 166     2975   2262   3137    461    -18    404       C  
ATOM   2541  CG  ASP A 166      12.275  10.578 -11.266  1.00 26.22           C  
ANISOU 2541  CG  ASP A 166     3462   2861   3639    438     -2    371       C  
ATOM   2542  OD1 ASP A 166      12.202  10.868 -12.475  1.00 23.73           O  
ANISOU 2542  OD1 ASP A 166     3148   2542   3325    442     16    326       O  
ATOM   2543  OD2 ASP A 166      12.229  11.450 -10.375  1.00 30.73           O  
ANISOU 2543  OD2 ASP A 166     3999   3490   4187    416     -8    392       O  
ATOM   2544  H   ASP A 166      12.625   6.623 -10.719  1.00 22.01           H  
ATOM   2545  HA  ASP A 166      11.306   8.336 -12.352  1.00 21.36           H  
ATOM   2546  HB2 ASP A 166      11.798   8.965 -10.096  1.00 26.45           H  
ATOM   2547  HB3 ASP A 166      13.333   8.998 -10.505  1.00 26.45           H  
ATOM   2548  N   LEU A 167      12.851   8.315 -14.256  1.00 19.77           N  
ANISOU 2548  N   LEU A 167     2736   1888   2886    524     26    281       N  
ATOM   2549  CA  LEU A 167      13.819   8.368 -15.344  1.00 22.17           C  
ANISOU 2549  CA  LEU A 167     3026   2197   3198    577     45    239       C  
ATOM   2550  C   LEU A 167      14.559   9.694 -15.397  1.00 21.28           C  
ANISOU 2550  C   LEU A 167     2850   2170   3064    585     57    232       C  
ATOM   2551  O   LEU A 167      15.567   9.801 -16.104  1.00 21.30           O  
ANISOU 2551  O   LEU A 167     2831   2192   3071    632     72    207       O  
ATOM   2552  CB  LEU A 167      13.119   8.132 -16.678  1.00 21.10           C  
ANISOU 2552  CB  LEU A 167     2926   2028   3062    557     61    188       C  
ATOM   2553  CG  LEU A 167      12.434   6.777 -16.845  1.00 23.84           C  
ANISOU 2553  CG  LEU A 167     3342   2285   3432    548     51    185       C  
ATOM   2554  CD1 LEU A 167      11.551   6.815 -18.083  1.00 30.19           C  
ANISOU 2554  CD1 LEU A 167     4173   3074   4225    510     65    135       C  
ATOM   2555  CD2 LEU A 167      13.447   5.645 -16.943  1.00 27.40           C  
ANISOU 2555  CD2 LEU A 167     3818   2677   3915    620     49    184       C  
ATOM   2556  H   LEU A 167      12.034   8.414 -14.504  1.00 23.72           H  
ATOM   2557  HA  LEU A 167      14.471   7.661 -15.215  1.00 26.60           H  
ATOM   2558  HB2 LEU A 167      12.437   8.814 -16.787  1.00 25.32           H  
ATOM   2559  HB3 LEU A 167      13.780   8.208 -17.384  1.00 25.32           H  
ATOM   2560  HG  LEU A 167      11.887   6.596 -16.064  1.00 28.61           H  
ATOM   2561 HD11 LEU A 167      10.951   7.575 -18.019  1.00 36.23           H  
ATOM   2562 HD12 LEU A 167      12.113   6.903 -18.869  1.00 36.23           H  
ATOM   2563 HD13 LEU A 167      11.040   5.992 -18.132  1.00 36.23           H  
ATOM   2564 HD21 LEU A 167      13.022   4.816 -16.674  1.00 32.88           H  
ATOM   2565 HD22 LEU A 167      13.756   5.577 -17.860  1.00 32.88           H  
ATOM   2566 HD23 LEU A 167      14.195   5.839 -16.356  1.00 32.88           H  
ATOM   2567  N   GLY A 168      14.062  10.703 -14.703  1.00 19.37           N  
ANISOU 2567  N   GLY A 168     2582   1981   2798    539     50    252       N  
ATOM   2568  CA  GLY A 168      14.741  11.971 -14.626  1.00 21.84           C  
ANISOU 2568  CA  GLY A 168     2839   2369   3089    541     56    249       C  
ATOM   2569  C   GLY A 168      14.258  12.950 -15.672  1.00 19.02           C  
ANISOU 2569  C   GLY A 168     2474   2042   2712    509     73    208       C  
ATOM   2570  O   GLY A 168      13.279  12.736 -16.394  1.00 18.32           O  
ANISOU 2570  O   GLY A 168     2417   1922   2622    480     78    183       O  
ATOM   2571  H   GLY A 168      13.323  10.674 -14.263  1.00 23.25           H  
ATOM   2572  HA2 GLY A 168      14.594  12.362 -13.751  1.00 26.20           H  
ATOM   2573  HA3 GLY A 168      15.693  11.833 -14.754  1.00 26.20           H  
ATOM   2574  N   VAL A 169      14.986  14.062 -15.748  1.00 16.66           N  
ANISOU 2574  N   VAL A 169     2129   1806   2396    513     80    204       N  
ATOM   2575  CA  VAL A 169      14.577  15.151 -16.616  1.00 14.50           C  
ANISOU 2575  CA  VAL A 169     1844   1565   2100    480     92    172       C  
ATOM   2576  C   VAL A 169      14.792  14.760 -18.074  1.00 14.02           C  
ANISOU 2576  C   VAL A 169     1798   1485   2044    501    112    130       C  
ATOM   2577  O   VAL A 169      15.750  14.062 -18.426  1.00 18.50           O  
ANISOU 2577  O   VAL A 169     2362   2041   2627    551    121    121       O  
ATOM   2578  CB  VAL A 169      15.349  16.440 -16.272  1.00 16.27           C  
ANISOU 2578  CB  VAL A 169     2020   1859   2304    475     91    181       C  
ATOM   2579  CG1 VAL A 169      15.012  16.862 -14.855  1.00 18.50           C  
ANISOU 2579  CG1 VAL A 169     2292   2161   2578    450     71    218       C  
ATOM   2580  CG2 VAL A 169      16.837  16.241 -16.436  1.00 20.40           C  
ANISOU 2580  CG2 VAL A 169     2510   2406   2834    525     98    183       C  
ATOM   2581  H   VAL A 169      15.713  14.207 -15.311  1.00 20.00           H  
ATOM   2582  HA  VAL A 169      13.631  15.320 -16.481  1.00 17.40           H  
ATOM   2583  HB  VAL A 169      15.086  17.146 -16.883  1.00 19.53           H  
ATOM   2584 HG11 VAL A 169      15.525  17.654 -14.631  1.00 22.20           H  
ATOM   2585 HG12 VAL A 169      14.063  17.056 -14.801  1.00 22.20           H  
ATOM   2586 HG13 VAL A 169      15.237  16.139 -14.249  1.00 22.20           H  
ATOM   2587 HG21 VAL A 169      17.289  17.083 -16.267  1.00 24.48           H  
ATOM   2588 HG22 VAL A 169      17.138  15.571 -15.803  1.00 24.48           H  
ATOM   2589 HG23 VAL A 169      17.019  15.945 -17.342  1.00 24.48           H  
ATOM   2590  N   PHE A 170      13.898  15.239 -18.936  1.00 14.25           N  
ANISOU 2590  N   PHE A 170     1842   1514   2058    464    119    102       N  
ATOM   2591  CA  PHE A 170      13.962  14.974 -20.375  1.00 14.96           C  
ANISOU 2591  CA  PHE A 170     1948   1592   2147    474    138     59       C  
ATOM   2592  C   PHE A 170      13.636  16.275 -21.087  1.00 17.26           C  
ANISOU 2592  C   PHE A 170     2221   1929   2410    438    143     42       C  
ATOM   2593  O   PHE A 170      12.520  16.476 -21.585  1.00 16.52           O  
ANISOU 2593  O   PHE A 170     2148   1822   2305    400    141     27       O  
ATOM   2594  CB  PHE A 170      12.998  13.858 -20.773  1.00 16.63           C  
ANISOU 2594  CB  PHE A 170     2212   1737   2372    464    136     43       C  
ATOM   2595  CG  PHE A 170      13.331  13.182 -22.078  1.00 18.34           C  
ANISOU 2595  CG  PHE A 170     2449   1928   2592    491    155     -1       C  
ATOM   2596  CD1 PHE A 170      14.598  12.658 -22.314  1.00 18.96           C  
ANISOU 2596  CD1 PHE A 170     2514   2007   2682    550    168    -11       C  
ATOM   2597  CD2 PHE A 170      12.354  13.030 -23.049  1.00 22.30           C  
ANISOU 2597  CD2 PHE A 170     2983   2408   3083    457    159    -33       C  
ATOM   2598  CE1 PHE A 170      14.885  12.006 -23.503  1.00 20.76           C  
ANISOU 2598  CE1 PHE A 170     2762   2213   2912    577    187    -55       C  
ATOM   2599  CE2 PHE A 170      12.632  12.394 -24.239  1.00 19.65           C  
ANISOU 2599  CE2 PHE A 170     2669   2050   2748    480    176    -76       C  
ATOM   2600  CZ  PHE A 170      13.901  11.875 -24.467  1.00 17.96           C  
ANISOU 2600  CZ  PHE A 170     2443   1834   2545    541    191    -89       C  
ATOM   2601  H   PHE A 170      13.231  15.731 -18.706  1.00 17.10           H  
ATOM   2602  HA  PHE A 170      14.854  14.690 -20.628  1.00 17.96           H  
ATOM   2603  HB2 PHE A 170      13.008  13.179 -20.080  1.00 19.96           H  
ATOM   2604  HB3 PHE A 170      12.107  14.234 -20.856  1.00 19.96           H  
ATOM   2605  HD1 PHE A 170      15.260  12.746 -21.666  1.00 22.75           H  
ATOM   2606  HD2 PHE A 170      11.500  13.363 -22.896  1.00 26.76           H  
ATOM   2607  HE1 PHE A 170      15.734  11.659 -23.653  1.00 24.91           H  
ATOM   2608  HE2 PHE A 170      11.972  12.312 -24.888  1.00 23.58           H  
ATOM   2609  HZ  PHE A 170      14.088  11.439 -25.267  1.00 21.55           H  
ATOM   2610  N   PRO A 171      14.586  17.208 -21.119  1.00 16.17           N  
ANISOU 2610  N   PRO A 171     2041   1844   2257    446    149     46       N  
ATOM   2611  CA  PRO A 171      14.350  18.477 -21.813  1.00 16.70           C  
ANISOU 2611  CA  PRO A 171     2095   1953   2298    411    152     33       C  
ATOM   2612  C   PRO A 171      14.398  18.280 -23.314  1.00 16.67           C  
ANISOU 2612  C   PRO A 171     2103   1947   2284    415    172     -6       C  
ATOM   2613  O   PRO A 171      15.252  17.560 -23.837  1.00 19.03           O  
ANISOU 2613  O   PRO A 171     2399   2243   2591    454    188    -24       O  
ATOM   2614  CB  PRO A 171      15.496  19.374 -21.332  1.00 18.56           C  
ANISOU 2614  CB  PRO A 171     2285   2243   2524    419    152     52       C  
ATOM   2615  CG  PRO A 171      16.584  18.424 -20.951  1.00 21.87           C  
ANISOU 2615  CG  PRO A 171     2690   2658   2962    470    157     60       C  
ATOM   2616  CD  PRO A 171      15.912  17.157 -20.473  1.00 20.62           C  
ANISOU 2616  CD  PRO A 171     2570   2437   2829    484    149     66       C  
ATOM   2617  HA  PRO A 171      13.502  18.868 -21.551  1.00 20.04           H  
ATOM   2618  HB2 PRO A 171      15.781  19.961 -22.049  1.00 22.27           H  
ATOM   2619  HB3 PRO A 171      15.208  19.898 -20.568  1.00 22.27           H  
ATOM   2620  HG2 PRO A 171      17.140  18.243 -21.725  1.00 26.24           H  
ATOM   2621  HG3 PRO A 171      17.120  18.813 -20.242  1.00 26.24           H  
ATOM   2622  HD2 PRO A 171      16.407  16.374 -20.762  1.00 24.75           H  
ATOM   2623  HD3 PRO A 171      15.825  17.156 -19.507  1.00 24.75           H  
ATOM   2624  N   ILE A 172      13.463  18.929 -23.997  1.00 15.61           N  
ANISOU 2624  N   ILE A 172     1983   1817   2132    375    169    -20       N  
ATOM   2625  CA  ILE A 172      13.343  18.884 -25.449  1.00 14.41           C  
ANISOU 2625  CA  ILE A 172     1843   1668   1963    368    184    -56       C  
ATOM   2626  C   ILE A 172      13.414  20.321 -25.941  1.00 13.83           C  
ANISOU 2626  C   ILE A 172     1748   1644   1862    337    183    -53       C  
ATOM   2627  O   ILE A 172      12.727  21.196 -25.402  1.00 15.10           O  
ANISOU 2627  O   ILE A 172     1907   1812   2017    307    166    -34       O  
ATOM   2628  CB  ILE A 172      12.037  18.192 -25.883  1.00 16.86           C  
ANISOU 2628  CB  ILE A 172     2196   1932   2276    347    179    -74       C  
ATOM   2629  CG1 ILE A 172      11.952  16.814 -25.221  1.00 17.75           C  
ANISOU 2629  CG1 ILE A 172     2334   1991   2419    372    176    -70       C  
ATOM   2630  CG2 ILE A 172      11.972  18.101 -27.425  1.00 17.36           C  
ANISOU 2630  CG2 ILE A 172     2273   2003   2320    340    195   -113       C  
ATOM   2631  CD1 ILE A 172      10.612  16.128 -25.390  1.00 20.34           C  
ANISOU 2631  CD1 ILE A 172     2703   2272   2751    342    167    -80       C  
ATOM   2632  H   ILE A 172      12.863  19.420 -23.625  1.00 18.73           H  
ATOM   2633  HA  ILE A 172      14.079  18.387 -25.840  1.00 17.29           H  
ATOM   2634  HB  ILE A 172      11.273  18.714 -25.592  1.00 20.23           H  
ATOM   2635 HG12 ILE A 172      12.629  16.239 -25.611  1.00 21.30           H  
ATOM   2636 HG13 ILE A 172      12.112  16.916 -24.269  1.00 21.30           H  
ATOM   2637 HG21 ILE A 172      11.216  17.549 -27.678  1.00 20.83           H  
ATOM   2638 HG22 ILE A 172      11.866  18.994 -27.790  1.00 20.83           H  
ATOM   2639 HG23 ILE A 172      12.795  17.705 -27.754  1.00 20.83           H  
ATOM   2640 HD11 ILE A 172      10.482  15.505 -24.658  1.00 24.40           H  
ATOM   2641 HD12 ILE A 172       9.911  16.798 -25.383  1.00 24.40           H  
ATOM   2642 HD13 ILE A 172      10.606  15.652 -26.235  1.00 24.40           H  
ATOM   2643  N   SER A 173      14.277  20.578 -26.925  1.00 13.89           N  
ANISOU 2643  N   SER A 173     1738   1687   1851    346    201    -71       N  
ATOM   2644  CA  SER A 173      14.508  21.955 -27.323  1.00 15.67           C  
ANISOU 2644  CA  SER A 173     1944   1960   2051    315    198    -62       C  
ATOM   2645  C   SER A 173      14.702  22.112 -28.820  1.00 15.71           C  
ANISOU 2645  C   SER A 173     1950   1990   2028    305    215    -90       C  
ATOM   2646  O   SER A 173      15.355  21.285 -29.463  1.00 17.62           O  
ANISOU 2646  O   SER A 173     2190   2236   2269    335    237   -115       O  
ATOM   2647  CB  SER A 173      15.748  22.543 -26.633  1.00 20.52           C  
ANISOU 2647  CB  SER A 173     2517   2616   2664    326    199    -38       C  
ATOM   2648  OG  SER A 173      15.862  23.913 -26.965  1.00 18.49           O  
ANISOU 2648  OG  SER A 173     2246   2397   2382    289    192    -28       O  
ATOM   2649  H   SER A 173      14.724  19.985 -27.359  1.00 16.66           H  
ATOM   2650  HA  SER A 173      13.708  22.446 -27.080  1.00 18.81           H  
ATOM   2651  HB2 SER A 173      15.655  22.451 -25.672  1.00 24.62           H  
ATOM   2652  HB3 SER A 173      16.540  22.071 -26.936  1.00 24.62           H  
ATOM   2653  HG  SER A 173      16.525  24.250 -26.574  1.00 22.19           H  
ATOM   2654  N   ASP A 174      14.176  23.206 -29.367  1.00 15.88           N  
ANISOU 2654  N   ASP A 174     1976   2031   2026    265    206    -84       N  
ATOM   2655  CA  ASP A 174      14.597  23.570 -30.708  1.00 17.72           C  
ANISOU 2655  CA  ASP A 174     2204   2302   2227    251    221   -102       C  
ATOM   2656  C   ASP A 174      16.101  23.867 -30.710  1.00 18.05           C  
ANISOU 2656  C   ASP A 174     2205   2395   2260    266    237    -95       C  
ATOM   2657  O   ASP A 174      16.723  24.146 -29.678  1.00 17.49           O  
ANISOU 2657  O   ASP A 174     2110   2335   2202    276    230    -71       O  
ATOM   2658  CB  ASP A 174      13.771  24.734 -31.281  1.00 16.59           C  
ANISOU 2658  CB  ASP A 174     2074   2170   2061    205    204    -93       C  
ATOM   2659  CG  ASP A 174      13.674  25.957 -30.378  1.00 16.86           C  
ANISOU 2659  CG  ASP A 174     2098   2210   2098    183    181    -58       C  
ATOM   2660  OD1 ASP A 174      14.461  26.113 -29.419  1.00 13.86           O  
ANISOU 2660  OD1 ASP A 174     1694   1840   1730    196    180    -40       O  
ATOM   2661  OD2 ASP A 174      12.776  26.794 -30.667  1.00 15.33           O  
ANISOU 2661  OD2 ASP A 174     1921   2011   1892    152    162    -50       O  
ATOM   2662  H   ASP A 174      13.601  23.728 -28.997  1.00 19.06           H  
ATOM   2663  HA  ASP A 174      14.438  22.830 -31.315  1.00 21.26           H  
ATOM   2664  HB2 ASP A 174      14.177  25.020 -32.114  1.00 19.91           H  
ATOM   2665  HB3 ASP A 174      12.867  24.420 -31.442  1.00 19.91           H  
ATOM   2666  N   TYR A 175      16.688  23.742 -31.893  1.00 14.07           N  
ANISOU 2666  N   TYR A 175     1691   1926   1729    268    260   -118       N  
ATOM   2667  CA  TYR A 175      18.124  23.873 -32.090  1.00 15.68           C  
ANISOU 2667  CA  TYR A 175     1852   2186   1919    284    280   -118       C  
ATOM   2668  C   TYR A 175      18.333  24.612 -33.398  1.00 16.82           C  
ANISOU 2668  C   TYR A 175     1991   2380   2020    248    291   -125       C  
ATOM   2669  O   TYR A 175      17.775  24.226 -34.426  1.00 17.28           O  
ANISOU 2669  O   TYR A 175     2074   2431   2062    242    300   -153       O  
ATOM   2670  CB  TYR A 175      18.778  22.489 -32.099  1.00 15.62           C  
ANISOU 2670  CB  TYR A 175     1836   2170   1929    342    304   -146       C  
ATOM   2671  CG  TYR A 175      20.285  22.454 -32.209  1.00 16.78           C  
ANISOU 2671  CG  TYR A 175     1933   2378   2065    370    327   -147       C  
ATOM   2672  CD1 TYR A 175      21.100  23.112 -31.295  1.00 16.68           C  
ANISOU 2672  CD1 TYR A 175     1881   2400   2057    366    318   -113       C  
ATOM   2673  CD2 TYR A 175      20.893  21.723 -33.210  1.00 18.71           C  
ANISOU 2673  CD2 TYR A 175     2168   2649   2294    401    358   -185       C  
ATOM   2674  CE1 TYR A 175      22.480  23.053 -31.397  1.00 18.53           C  
ANISOU 2674  CE1 TYR A 175     2063   2696   2279    391    338   -114       C  
ATOM   2675  CE2 TYR A 175      22.265  21.663 -33.323  1.00 24.86           C  
ANISOU 2675  CE2 TYR A 175     2895   3490   3061    430    380   -188       C  
ATOM   2676  CZ  TYR A 175      23.057  22.325 -32.417  1.00 21.72           C  
ANISOU 2676  CZ  TYR A 175     2456   3130   2669    424    370   -151       C  
ATOM   2677  OH  TYR A 175      24.426  22.252 -32.541  1.00 23.69           O  
ANISOU 2677  OH  TYR A 175     2648   3448   2905    452    392   -154       O  
ATOM   2678  H   TYR A 175      16.261  23.576 -32.620  1.00 16.88           H  
ATOM   2679  HA  TYR A 175      18.546  24.389 -31.385  1.00 18.82           H  
ATOM   2680  HB2 TYR A 175      18.543  22.040 -31.272  1.00 18.75           H  
ATOM   2681  HB3 TYR A 175      18.427  21.995 -32.856  1.00 18.75           H  
ATOM   2682  HD1 TYR A 175      20.712  23.599 -30.604  1.00 20.02           H  
ATOM   2683  HD2 TYR A 175      20.365  21.261 -33.821  1.00 22.46           H  
ATOM   2684  HE1 TYR A 175      23.015  23.502 -30.782  1.00 22.23           H  
ATOM   2685  HE2 TYR A 175      22.654  21.175 -34.012  1.00 29.83           H  
ATOM   2686  HH  TYR A 175      24.763  23.017 -32.462  1.00 28.43           H  
ATOM   2687  N   TYR A 176      19.096  25.698 -33.345  1.00 17.55           N  
ANISOU 2687  N   TYR A 176     2053   2522   2093    220    288    -99       N  
ATOM   2688  CA  TYR A 176      19.382  26.509 -34.517  1.00 14.87           C  
ANISOU 2688  CA  TYR A 176     1706   2234   1710    179    297    -98       C  
ATOM   2689  C   TYR A 176      20.888  26.568 -34.724  1.00 18.10           C  
ANISOU 2689  C   TYR A 176     2063   2714   2099    189    321    -97       C  
ATOM   2690  O   TYR A 176      21.661  26.604 -33.759  1.00 18.59           O  
ANISOU 2690  O   TYR A 176     2094   2790   2179    206    319    -80       O  
ATOM   2691  CB  TYR A 176      18.803  27.932 -34.370  1.00 19.24           C  
ANISOU 2691  CB  TYR A 176     2276   2782   2252    124    266    -63       C  
ATOM   2692  CG  TYR A 176      17.317  27.965 -34.059  1.00 16.36           C  
ANISOU 2692  CG  TYR A 176     1955   2353   1907    117    240    -61       C  
ATOM   2693  CD1 TYR A 176      16.859  27.762 -32.766  1.00 15.56           C  
ANISOU 2693  CD1 TYR A 176     1861   2207   1843    136    223    -50       C  
ATOM   2694  CD2 TYR A 176      16.372  28.208 -35.056  1.00 15.31           C  
ANISOU 2694  CD2 TYR A 176     1854   2212   1753     90    233    -69       C  
ATOM   2695  CE1 TYR A 176      15.504  27.777 -32.461  1.00 17.12           C  
ANISOU 2695  CE1 TYR A 176     2093   2354   2056    130    201    -49       C  
ATOM   2696  CE2 TYR A 176      15.001  28.238 -34.755  1.00 17.02           C  
ANISOU 2696  CE2 TYR A 176     2104   2376   1986     85    208    -67       C  
ATOM   2697  CZ  TYR A 176      14.579  28.020 -33.448  1.00 17.05           C  
ANISOU 2697  CZ  TYR A 176     2112   2338   2027    105    194    -58       C  
ATOM   2698  OH  TYR A 176      13.247  28.029 -33.086  1.00 16.14           O  
ANISOU 2698  OH  TYR A 176     2025   2180   1928    101    172    -56       O  
ATOM   2699  H   TYR A 176      19.464  25.988 -32.624  1.00 21.06           H  
ATOM   2700  HA  TYR A 176      18.980  26.108 -35.304  1.00 17.85           H  
ATOM   2701  HB2 TYR A 176      19.266  28.382 -33.646  1.00 23.09           H  
ATOM   2702  HB3 TYR A 176      18.941  28.411 -35.202  1.00 23.09           H  
ATOM   2703  HD1 TYR A 176      17.475  27.612 -32.085  1.00 18.67           H  
ATOM   2704  HD2 TYR A 176      16.654  28.352 -35.930  1.00 18.38           H  
ATOM   2705  HE1 TYR A 176      15.222  27.623 -31.588  1.00 20.54           H  
ATOM   2706  HE2 TYR A 176      14.379  28.403 -35.426  1.00 20.42           H  
ATOM   2707  HH  TYR A 176      12.853  27.368 -33.424  1.00 19.37           H  
ATOM   2708  N   TYR A 177      21.303  26.562 -35.984  1.00 17.98           N  
ANISOU 2708  N   TYR A 177     2038   2749   2046    177    345   -117       N  
ATOM   2709  CA  TYR A 177      22.714  26.741 -36.286  1.00 18.83           C  
ANISOU 2709  CA  TYR A 177     2091   2936   2127    179    370   -115       C  
ATOM   2710  C   TYR A 177      23.127  28.199 -36.159  1.00 24.93           C  
ANISOU 2710  C   TYR A 177     2846   3749   2876    117    352    -71       C  
ATOM   2711  O   TYR A 177      24.266  28.484 -35.772  1.00 25.47           O  
ANISOU 2711  O   TYR A 177     2868   3872   2939    116    360    -55       O  
ATOM   2712  CB  TYR A 177      22.999  26.206 -37.678  1.00 26.95           C  
ANISOU 2712  CB  TYR A 177     3113   4008   3118    187    403   -153       C  
ATOM   2713  CG  TYR A 177      22.602  24.759 -37.842  1.00 22.92           C  
ANISOU 2713  CG  TYR A 177     2626   3454   2631    247    420   -200       C  
ATOM   2714  CD1 TYR A 177      22.729  23.851 -36.791  1.00 21.12           C  
ANISOU 2714  CD1 TYR A 177     2394   3181   2448    303    418   -206       C  
ATOM   2715  CD2 TYR A 177      22.101  24.301 -39.049  1.00 22.98           C  
ANISOU 2715  CD2 TYR A 177     2660   3461   2611    243    435   -238       C  
ATOM   2716  CE1 TYR A 177      22.366  22.524 -36.946  1.00 22.22           C  
ANISOU 2716  CE1 TYR A 177     2560   3272   2609    355    430   -248       C  
ATOM   2717  CE2 TYR A 177      21.741  22.981 -39.218  1.00 21.20           C  
ANISOU 2717  CE2 TYR A 177     2460   3191   2405    294    449   -283       C  
ATOM   2718  CZ  TYR A 177      21.870  22.093 -38.165  1.00 27.22           C  
ANISOU 2718  CZ  TYR A 177     3222   3904   3215    350    446   -288       C  
ATOM   2719  OH  TYR A 177      21.502  20.775 -38.347  1.00 25.15           O  
ANISOU 2719  OH  TYR A 177     2992   3591   2974    397    458   -332       O  
ATOM   2720  H   TYR A 177      20.797  26.457 -36.672  1.00 21.58           H  
ATOM   2721  HA  TYR A 177      23.256  26.234 -35.662  1.00 22.59           H  
ATOM   2722  HB2 TYR A 177      22.501  26.729 -38.325  1.00 32.34           H  
ATOM   2723  HB3 TYR A 177      23.951  26.278 -37.855  1.00 32.34           H  
ATOM   2724  HD1 TYR A 177      23.063  24.141 -35.973  1.00 25.34           H  
ATOM   2725  HD2 TYR A 177      22.005  24.894 -39.759  1.00 27.58           H  
ATOM   2726  HE1 TYR A 177      22.454  21.927 -36.238  1.00 26.66           H  
ATOM   2727  HE2 TYR A 177      21.412  22.688 -40.037  1.00 25.44           H  
ATOM   2728  HH  TYR A 177      21.524  20.366 -37.613  1.00 30.18           H  
ATOM   2729  N   SER A 178      22.223  29.130 -36.454  1.00 18.78           N  
ANISOU 2729  N   SER A 178     2106   2943   2085     66    327    -51       N  
ATOM   2730  CA  SER A 178      22.498  30.529 -36.185  1.00 17.71           C  
ANISOU 2730  CA  SER A 178     1965   2828   1935      9    304     -8       C  
ATOM   2731  C   SER A 178      22.505  30.790 -34.685  1.00 17.47           C  
ANISOU 2731  C   SER A 178     1931   2762   1943     18    280     15       C  
ATOM   2732  O   SER A 178      21.878  30.074 -33.898  1.00 21.18           O  
ANISOU 2732  O   SER A 178     2419   3177   2451     59    272      3       O  
ATOM   2733  CB  SER A 178      21.453  31.433 -36.834  1.00 19.34           C  
ANISOU 2733  CB  SER A 178     2218   3006   2123    -41    279      8       C  
ATOM   2734  OG  SER A 178      21.508  31.337 -38.245  1.00 25.53           O  
ANISOU 2734  OG  SER A 178     3004   3832   2865    -59    299     -8       O  
ATOM   2735  H   SER A 178      21.453  28.976 -36.805  1.00 22.53           H  
ATOM   2736  HA  SER A 178      23.366  30.750 -36.557  1.00 21.25           H  
ATOM   2737  HB2 SER A 178      20.571  31.163 -36.534  1.00 23.21           H  
ATOM   2738  HB3 SER A 178      21.625  32.352 -36.574  1.00 23.21           H  
ATOM   2739  HG  SER A 178      22.199  31.719 -38.532  1.00 30.64           H  
ATOM   2740  N   SER A 179      23.201  31.850 -34.296  1.00 18.20           N  
ANISOU 2740  N   SER A 179     2005   2888   2024    -25    266     48       N  
ATOM   2741  CA  SER A 179      23.239  32.249 -32.900  1.00 18.93           C  
ANISOU 2741  CA  SER A 179     2096   2951   2146    -24    242     71       C  
ATOM   2742  C   SER A 179      21.945  32.951 -32.480  1.00 20.86           C  
ANISOU 2742  C   SER A 179     2395   3124   2408    -45    206     84       C  
ATOM   2743  O   SER A 179      21.150  33.404 -33.308  1.00 17.79           O  
ANISOU 2743  O   SER A 179     2041   2715   2002    -71    197     85       O  
ATOM   2744  CB  SER A 179      24.417  33.190 -32.657  1.00 17.79           C  
ANISOU 2744  CB  SER A 179     1914   2867   1980    -69    237    101       C  
ATOM   2745  OG  SER A 179      24.141  34.464 -33.211  1.00 18.87           O  
ANISOU 2745  OG  SER A 179     2079   3002   2090   -135    217    126       O  
ATOM   2746  H   SER A 179      23.659  32.354 -34.821  1.00 21.85           H  
ATOM   2747  HA  SER A 179      23.340  31.455 -32.352  1.00 22.71           H  
ATOM   2748  HB2 SER A 179      24.561  33.281 -31.702  1.00 21.35           H  
ATOM   2749  HB3 SER A 179      25.211  32.823 -33.078  1.00 21.35           H  
ATOM   2750  HG  SER A 179      24.753  35.003 -33.010  1.00 22.65           H  
ATOM   2751  N   ALA A 180      21.760  33.063 -31.161  1.00 18.12           N  
ANISOU 2751  N   ALA A 180     2052   2742   2091    -33    186     95       N  
ATOM   2752  CA  ALA A 180      20.601  33.773 -30.629  1.00 17.00           C  
ANISOU 2752  CA  ALA A 180     1956   2537   1965    -49    154    106       C  
ATOM   2753  C   ALA A 180      20.573  35.237 -31.072  1.00 15.56           C  
ANISOU 2753  C   ALA A 180     1795   2358   1757   -111    131    132       C  
ATOM   2754  O   ALA A 180      19.508  35.759 -31.426  1.00 17.39           O  
ANISOU 2754  O   ALA A 180     2070   2549   1989   -124    112    135       O  
ATOM   2755  CB  ALA A 180      20.585  33.665 -29.102  1.00 18.61           C  
ANISOU 2755  CB  ALA A 180     2154   2715   2201    -27    139    113       C  
ATOM   2756  H   ALA A 180      22.285  32.741 -30.561  1.00 21.74           H  
ATOM   2757  HA  ALA A 180      19.796  33.354 -30.973  1.00 20.40           H  
ATOM   2758  HB1 ALA A 180      19.926  34.283 -28.749  1.00 22.33           H  
ATOM   2759  HB2 ALA A 180      20.354  32.757 -28.852  1.00 22.33           H  
ATOM   2760  HB3 ALA A 180      21.465  33.889 -28.761  1.00 22.33           H  
ATOM   2761  N   ASP A 181      21.724  35.920 -31.060  1.00 17.09           N  
ANISOU 2761  N   ASP A 181     1961   2603   1930   -149    132    154       N  
ATOM   2762  CA  ASP A 181      21.754  37.318 -31.489  1.00 18.38           C  
ANISOU 2762  CA  ASP A 181     2149   2767   2068   -213    109    182       C  
ATOM   2763  C   ASP A 181      21.450  37.447 -32.976  1.00 16.53           C  
ANISOU 2763  C   ASP A 181     1931   2547   1802   -235    118    181       C  
ATOM   2764  O   ASP A 181      20.763  38.385 -33.398  1.00 17.50           O  
ANISOU 2764  O   ASP A 181     2097   2637   1916   -270     92    198       O  
ATOM   2765  CB  ASP A 181      23.105  37.943 -31.151  1.00 19.87           C  
ANISOU 2765  CB  ASP A 181     2301   3010   2238   -255    109    205       C  
ATOM   2766  CG  ASP A 181      23.228  38.267 -29.677  1.00 25.57           C  
ANISOU 2766  CG  ASP A 181     3022   3707   2986   -252     87    213       C  
ATOM   2767  OD1 ASP A 181      22.742  39.341 -29.240  1.00 27.16           O  
ANISOU 2767  OD1 ASP A 181     3264   3863   3191   -284     55    228       O  
ATOM   2768  OD2 ASP A 181      23.766  37.415 -28.944  1.00 21.98           O  
ANISOU 2768  OD2 ASP A 181     2528   3275   2547   -213    102    202       O  
ATOM   2769  H   ASP A 181      22.485  35.605 -30.813  1.00 20.51           H  
ATOM   2770  HA  ASP A 181      21.072  37.810 -31.005  1.00 22.06           H  
ATOM   2771  HB2 ASP A 181      23.811  37.320 -31.384  1.00 23.84           H  
ATOM   2772  HB3 ASP A 181      23.210  38.766 -31.652  1.00 23.84           H  
ATOM   2773  N   GLU A 182      21.932  36.502 -33.782  1.00 16.52           N  
ANISOU 2773  N   GLU A 182     1898   2595   1785   -214    152    161       N  
ATOM   2774  CA  GLU A 182      21.594  36.495 -35.201  1.00 15.81           C  
ANISOU 2774  CA  GLU A 182     1823   2522   1662   -232    163    156       C  
ATOM   2775  C   GLU A 182      20.094  36.305 -35.406  1.00 15.27           C  
ANISOU 2775  C   GLU A 182     1803   2389   1611   -210    147    142       C  
ATOM   2776  O   GLU A 182      19.500  36.907 -36.311  1.00 18.38           O  
ANISOU 2776  O   GLU A 182     2229   2774   1982   -241    133    154       O  
ATOM   2777  CB  GLU A 182      22.399  35.399 -35.908  1.00 18.75           C  
ANISOU 2777  CB  GLU A 182     2151   2959   2016   -204    206    128       C  
ATOM   2778  CG  GLU A 182      23.879  35.775 -36.143  1.00 22.19           C  
ANISOU 2778  CG  GLU A 182     2535   3478   2418   -239    224    145       C  
ATOM   2779  CD  GLU A 182      24.818  34.591 -36.404  1.00 35.59           C  
ANISOU 2779  CD  GLU A 182     4176   5238   4107   -194    266    114       C  
ATOM   2780  OE1 GLU A 182      24.365  33.428 -36.502  1.00 23.84           O  
ANISOU 2780  OE1 GLU A 182     2693   3728   2639   -135    284     78       O  
ATOM   2781  OE2 GLU A 182      26.038  34.841 -36.499  1.00 37.99           O  
ANISOU 2781  OE2 GLU A 182     4431   5617   4386   -217    282    127       O  
ATOM   2782  H   GLU A 182      22.451  35.861 -33.537  1.00 19.83           H  
ATOM   2783  HA  GLU A 182      21.833  37.347 -35.600  1.00 18.97           H  
ATOM   2784  HB2 GLU A 182      22.380  34.597 -35.364  1.00 22.51           H  
ATOM   2785  HB3 GLU A 182      21.997  35.224 -36.773  1.00 22.51           H  
ATOM   2786  HG2 GLU A 182      23.928  36.360 -36.915  1.00 26.63           H  
ATOM   2787  HG3 GLU A 182      24.207  36.237 -35.355  1.00 26.63           H  
ATOM   2788  N   LEU A 183      19.465  35.460 -34.579  1.00 15.75           N  
ANISOU 2788  N   LEU A 183     1868   2406   1710   -158    147    120       N  
ATOM   2789  CA  LEU A 183      18.040  35.175 -34.713  1.00 18.76           C  
ANISOU 2789  CA  LEU A 183     2289   2731   2108   -137    133    106       C  
ATOM   2790  C   LEU A 183      17.173  36.305 -34.168  1.00 18.73           C  
ANISOU 2790  C   LEU A 183     2324   2675   2117   -157     94    130       C  
ATOM   2791  O   LEU A 183      16.077  36.544 -34.688  1.00 16.57           O  
ANISOU 2791  O   LEU A 183     2085   2370   1842   -160     77    130       O  
ATOM   2792  CB  LEU A 183      17.710  33.855 -34.009  1.00 15.50           C  
ANISOU 2792  CB  LEU A 183     1868   2294   1730    -78    148     76       C  
ATOM   2793  CG  LEU A 183      18.265  32.612 -34.713  1.00 16.54           C  
ANISOU 2793  CG  LEU A 183     1973   2462   1850    -48    185     45       C  
ATOM   2794  CD1 LEU A 183      18.297  31.428 -33.745  1.00 19.20           C  
ANISOU 2794  CD1 LEU A 183     2296   2774   2224      6    197     24       C  
ATOM   2795  CD2 LEU A 183      17.448  32.283 -35.946  1.00 25.48           C  
ANISOU 2795  CD2 LEU A 183     3130   3589   2961    -53    190     26       C  
ATOM   2796  H   LEU A 183      19.844  35.038 -33.932  1.00 18.90           H  
ATOM   2797  HA  LEU A 183      17.823  35.073 -35.653  1.00 22.51           H  
ATOM   2798  HB2 LEU A 183      18.085  33.880 -33.114  1.00 18.61           H  
ATOM   2799  HB3 LEU A 183      16.746  33.762 -33.962  1.00 18.61           H  
ATOM   2800  HG  LEU A 183      19.173  32.789 -35.005  1.00 19.85           H  
ATOM   2801 HD11 LEU A 183      18.879  30.741 -34.106  1.00 23.04           H  
ATOM   2802 HD12 LEU A 183      18.633  31.730 -32.887  1.00 23.04           H  
ATOM   2803 HD13 LEU A 183      17.398  31.079 -33.644  1.00 23.04           H  
ATOM   2804 HD21 LEU A 183      17.934  31.640 -36.485  1.00 30.57           H  
ATOM   2805 HD22 LEU A 183      16.597  31.908 -35.670  1.00 30.57           H  
ATOM   2806 HD23 LEU A 183      17.302  33.097 -36.454  1.00 30.57           H  
ATOM   2807  N   VAL A 184      17.637  37.025 -33.150  1.00 14.35           N  
ANISOU 2807  N   VAL A 184     1765   2111   1575   -171     77    149       N  
ATOM   2808  CA  VAL A 184      16.941  38.245 -32.756  1.00 17.67           C  
ANISOU 2808  CA  VAL A 184     2225   2485   2003   -195     40    170       C  
ATOM   2809  C   VAL A 184      16.958  39.253 -33.901  1.00 16.52           C  
ANISOU 2809  C   VAL A 184     2104   2350   1823   -245     26    196       C  
ATOM   2810  O   VAL A 184      15.941  39.892 -34.203  1.00 17.39           O  
ANISOU 2810  O   VAL A 184     2254   2419   1934   -252     -1    205       O  
ATOM   2811  CB  VAL A 184      17.569  38.815 -31.470  1.00 18.10           C  
ANISOU 2811  CB  VAL A 184     2271   2532   2074   -204     26    183       C  
ATOM   2812  CG1 VAL A 184      17.145  40.250 -31.242  1.00 21.14           C  
ANISOU 2812  CG1 VAL A 184     2698   2877   2458   -239    -11    207       C  
ATOM   2813  CG2 VAL A 184      17.201  37.930 -30.269  1.00 15.39           C  
ANISOU 2813  CG2 VAL A 184     1916   2166   1767   -153     32    162       C  
ATOM   2814  H   VAL A 184      18.333  36.836 -32.683  1.00 17.22           H  
ATOM   2815  HA  VAL A 184      16.013  38.035 -32.565  1.00 21.20           H  
ATOM   2816  HB  VAL A 184      18.534  38.816 -31.565  1.00 21.72           H  
ATOM   2817 HG11 VAL A 184      17.616  40.600 -30.470  1.00 25.37           H  
ATOM   2818 HG12 VAL A 184      17.365  40.773 -32.029  1.00 25.37           H  
ATOM   2819 HG13 VAL A 184      16.188  40.276 -31.085  1.00 25.37           H  
ATOM   2820 HG21 VAL A 184      17.322  38.439 -29.453  1.00 18.47           H  
ATOM   2821 HG22 VAL A 184      16.275  37.653 -30.353  1.00 18.47           H  
ATOM   2822 HG23 VAL A 184      17.779  37.151 -30.262  1.00 18.47           H  
ATOM   2823  N   GLU A 185      18.118  39.427 -34.542  1.00 17.98           N  
ANISOU 2823  N   GLU A 185     2264   2594   1976   -282     42    209       N  
ATOM   2824  CA  GLU A 185      18.210  40.368 -35.651  1.00 18.86           C  
ANISOU 2824  CA  GLU A 185     2396   2720   2050   -336     29    237       C  
ATOM   2825  C   GLU A 185      17.277  39.956 -36.777  1.00 16.65           C  
ANISOU 2825  C   GLU A 185     2136   2436   1755   -325     32    226       C  
ATOM   2826  O   GLU A 185      16.609  40.798 -37.389  1.00 19.56           O  
ANISOU 2826  O   GLU A 185     2543   2779   2109   -351      5    248       O  
ATOM   2827  CB  GLU A 185      19.651  40.447 -36.154  1.00 21.40           C  
ANISOU 2827  CB  GLU A 185     2679   3117   2336   -377     53    250       C  
ATOM   2828  CG  GLU A 185      19.858  41.374 -37.336  1.00 23.12           C  
ANISOU 2828  CG  GLU A 185     2916   3360   2509   -440     42    282       C  
ATOM   2829  CD  GLU A 185      19.558  42.820 -37.014  1.00 34.76           C  
ANISOU 2829  CD  GLU A 185     4438   4783   3988   -483     -2    319       C  
ATOM   2830  OE1 GLU A 185      19.691  43.211 -35.834  1.00 37.47           O  
ANISOU 2830  OE1 GLU A 185     4785   5092   4359   -479    -19    322       O  
ATOM   2831  OE2 GLU A 185      19.191  43.563 -37.951  1.00 53.60           O  
ANISOU 2831  OE2 GLU A 185     6857   7160   6347   -521    -22    346       O  
ATOM   2832  H   GLU A 185      18.852  39.020 -34.356  1.00 21.58           H  
ATOM   2833  HA  GLU A 185      17.953  41.251 -35.343  1.00 22.63           H  
ATOM   2834  HB2 GLU A 185      20.213  40.765 -35.431  1.00 25.68           H  
ATOM   2835  HB3 GLU A 185      19.931  39.559 -36.427  1.00 25.68           H  
ATOM   2836  HG2 GLU A 185      20.784  41.318 -37.622  1.00 27.75           H  
ATOM   2837  HG3 GLU A 185      19.271  41.100 -38.058  1.00 27.75           H  
ATOM   2838  N   LEU A 186      17.229  38.655 -37.067  1.00 16.23           N  
ANISOU 2838  N   LEU A 186     2058   2406   1704   -285     64    191       N  
ATOM   2839  CA  LEU A 186      16.350  38.155 -38.115  1.00 17.68           C  
ANISOU 2839  CA  LEU A 186     2257   2588   1871   -275     69    176       C  
ATOM   2840  C   LEU A 186      14.894  38.461 -37.795  1.00 17.62           C  
ANISOU 2840  C   LEU A 186     2290   2514   1889   -256     36    178       C  
ATOM   2841  O   LEU A 186      14.148  38.957 -38.650  1.00 18.41           O  
ANISOU 2841  O   LEU A 186     2420   2606   1971   -274     16    192       O  
ATOM   2842  CB  LEU A 186      16.540  36.645 -38.290  1.00 19.50           C  
ANISOU 2842  CB  LEU A 186     2458   2845   2106   -232    107    134       C  
ATOM   2843  CG  LEU A 186      15.511  35.935 -39.177  1.00 18.52           C  
ANISOU 2843  CG  LEU A 186     2353   2711   1972   -214    111    110       C  
ATOM   2844  CD1 LEU A 186      15.660  36.355 -40.641  1.00 22.16           C  
ANISOU 2844  CD1 LEU A 186     2821   3217   2381   -258    114    122       C  
ATOM   2845  CD2 LEU A 186      15.609  34.411 -39.072  1.00 22.40           C  
ANISOU 2845  CD2 LEU A 186     2822   3210   2478   -166    144     65       C  
ATOM   2846  H   LEU A 186      17.692  38.046 -36.674  1.00 19.48           H  
ATOM   2847  HA  LEU A 186      16.585  38.592 -38.949  1.00 21.21           H  
ATOM   2848  HB2 LEU A 186      17.412  36.494 -38.686  1.00 23.40           H  
ATOM   2849  HB3 LEU A 186      16.497  36.231 -37.414  1.00 23.40           H  
ATOM   2850  HG  LEU A 186      14.633  36.199 -38.860  1.00 22.22           H  
ATOM   2851 HD11 LEU A 186      14.916  35.998 -41.150  1.00 26.59           H  
ATOM   2852 HD12 LEU A 186      15.663  37.323 -40.693  1.00 26.59           H  
ATOM   2853 HD13 LEU A 186      16.496  36.003 -40.987  1.00 26.59           H  
ATOM   2854 HD21 LEU A 186      15.098  34.012 -39.794  1.00 26.88           H  
ATOM   2855 HD22 LEU A 186      16.540  34.149 -39.141  1.00 26.88           H  
ATOM   2856 HD23 LEU A 186      15.249  34.130 -38.217  1.00 26.88           H  
ATOM   2857  N   THR A 187      14.463  38.149 -36.570  1.00 15.91           N  
ANISOU 2857  N   THR A 187     2073   2257   1715   -218     29    164       N  
ATOM   2858  CA  THR A 187      13.047  38.232 -36.232  1.00 15.61           C  
ANISOU 2858  CA  THR A 187     2064   2166   1701   -192      4    159       C  
ATOM   2859  C   THR A 187      12.582  39.653 -35.949  1.00 15.39           C  
ANISOU 2859  C   THR A 187     2072   2097   1678   -213    -36    190       C  
ATOM   2860  O   THR A 187      11.375  39.882 -35.824  1.00 20.79           O  
ANISOU 2860  O   THR A 187     2781   2743   2377   -194    -60    189       O  
ATOM   2861  CB  THR A 187      12.726  37.315 -35.043  1.00 18.58           C  
ANISOU 2861  CB  THR A 187     2425   2517   2116   -145     14    133       C  
ATOM   2862  OG1 THR A 187      13.555  37.637 -33.921  1.00 17.47           O  
ANISOU 2862  OG1 THR A 187     2270   2375   1992   -146     14    142       O  
ATOM   2863  CG2 THR A 187      12.938  35.850 -35.454  1.00 17.44           C  
ANISOU 2863  CG2 THR A 187     2256   2400   1969   -120     49    101       C  
ATOM   2864  H   THR A 187      14.969  37.890 -35.925  1.00 19.09           H  
ATOM   2865  HA  THR A 187      12.529  37.908 -36.987  1.00 18.73           H  
ATOM   2866  HB  THR A 187      11.802  37.435 -34.775  1.00 22.29           H  
ATOM   2867  HG1 THR A 187      14.342  37.380 -34.062  1.00 20.96           H  
ATOM   2868 HG21 THR A 187      13.081  35.302 -34.667  1.00 20.92           H  
ATOM   2869 HG22 THR A 187      12.158  35.522 -35.929  1.00 20.92           H  
ATOM   2870 HG23 THR A 187      13.713  35.777 -36.034  1.00 20.92           H  
ATOM   2871  N   LYS A 188      13.489  40.623 -35.894  1.00 15.63           N  
ANISOU 2871  N   LYS A 188     2107   2138   1695   -254    -46    218       N  
ATOM   2872  CA  LYS A 188      13.048  42.009 -35.913  1.00 18.22           C  
ANISOU 2872  CA  LYS A 188     2477   2426   2022   -279    -86    249       C  
ATOM   2873  C   LYS A 188      12.323  42.348 -37.207  1.00 18.45           C  
ANISOU 2873  C   LYS A 188     2531   2455   2023   -295   -102    265       C  
ATOM   2874  O   LYS A 188      11.442  43.216 -37.216  1.00 19.16           O  
ANISOU 2874  O   LYS A 188     2659   2500   2121   -293   -138    283       O  
ATOM   2875  CB  LYS A 188      14.245  42.938 -35.741  1.00 17.82           C  
ANISOU 2875  CB  LYS A 188     2426   2388   1955   -328    -92    277       C  
ATOM   2876  CG  LYS A 188      14.771  43.032 -34.332  1.00 17.93           C  
ANISOU 2876  CG  LYS A 188     2427   2387   1997   -318    -92    270       C  
ATOM   2877  CD  LYS A 188      15.947  43.987 -34.257  1.00 23.78           C  
ANISOU 2877  CD  LYS A 188     3171   3146   2720   -376   -101    299       C  
ATOM   2878  CE  LYS A 188      16.377  44.144 -32.800  1.00 34.11           C  
ANISOU 2878  CE  LYS A 188     4469   4436   4054   -366   -106    290       C  
ATOM   2879  NZ  LYS A 188      17.647  44.896 -32.686  1.00 48.38           N  
ANISOU 2879  NZ  LYS A 188     6270   6272   5843   -425   -110    316       N  
ATOM   2880  H   LYS A 188      14.340  40.510 -35.847  1.00 18.76           H  
ATOM   2881  HA  LYS A 188      12.438  42.149 -35.173  1.00 21.87           H  
ATOM   2882  HB2 LYS A 188      14.968  42.616 -36.302  1.00 21.38           H  
ATOM   2883  HB3 LYS A 188      13.984  43.831 -36.016  1.00 21.38           H  
ATOM   2884  HG2 LYS A 188      14.070  43.360 -33.747  1.00 21.51           H  
ATOM   2885  HG3 LYS A 188      15.066  42.157 -34.038  1.00 21.51           H  
ATOM   2886  HD2 LYS A 188      16.692  43.633 -34.768  1.00 28.54           H  
ATOM   2887  HD3 LYS A 188      15.689  44.855 -34.604  1.00 28.54           H  
ATOM   2888  HE2 LYS A 188      15.691  44.628 -32.314  1.00 40.93           H  
ATOM   2889  HE3 LYS A 188      16.506  43.267 -32.407  1.00 40.93           H  
ATOM   2890  HZ1 LYS A 188      17.767  45.166 -31.846  1.00 58.06           H  
ATOM   2891  HZ2 LYS A 188      18.331  44.378 -32.923  1.00 58.06           H  
ATOM   2892  HZ3 LYS A 188      17.628  45.610 -33.218  1.00 58.06           H  
ATOM   2893  N   ASN A 189      12.685  41.697 -38.315  1.00 17.95           N  
ANISOU 2893  N   ASN A 189     2450   2444   1927   -310    -77    260       N  
ATOM   2894  CA  ASN A 189      12.121  42.079 -39.604  1.00 16.49           C  
ANISOU 2894  CA  ASN A 189     2289   2268   1709   -334    -93    279       C  
ATOM   2895  C   ASN A 189      11.622  40.907 -40.440  1.00 18.67           C  
ANISOU 2895  C   ASN A 189     2549   2575   1969   -314    -70    249       C  
ATOM   2896  O   ASN A 189      11.180  41.122 -41.575  1.00 21.01           O  
ANISOU 2896  O   ASN A 189     2863   2888   2233   -335    -81    263       O  
ATOM   2897  CB  ASN A 189      13.143  42.895 -40.407  1.00 18.86           C  
ANISOU 2897  CB  ASN A 189     2595   2604   1967   -397    -95    315       C  
ATOM   2898  CG  ASN A 189      13.386  44.267 -39.804  1.00 20.44           C  
ANISOU 2898  CG  ASN A 189     2827   2762   2179   -426   -130    351       C  
ATOM   2899  OD1 ASN A 189      12.507  45.132 -39.805  1.00 20.66           O  
ANISOU 2899  OD1 ASN A 189     2896   2736   2216   -423   -169    372       O  
ATOM   2900  ND2 ASN A 189      14.584  44.471 -39.285  1.00 24.84           N  
ANISOU 2900  ND2 ASN A 189     3363   3340   2733   -454   -116    358       N  
ATOM   2901  H   ASN A 189      13.245  41.044 -38.341  1.00 21.54           H  
ATOM   2902  HA  ASN A 189      11.346  42.635 -39.433  1.00 19.79           H  
ATOM   2903  HB2 ASN A 189      13.988  42.418 -40.424  1.00 22.63           H  
ATOM   2904  HB3 ASN A 189      12.813  43.016 -41.311  1.00 22.63           H  
ATOM   2905 HD21 ASN A 189      14.775  45.230 -38.930  1.00 29.80           H  
ATOM   2906 HD22 ASN A 189      15.173  43.844 -39.302  1.00 29.80           H  
ATOM   2907  N   SER A 190      11.644  39.690 -39.898  1.00 18.64           N  
ANISOU 2907  N   SER A 190     2517   2579   1987   -275    -40    210       N  
ATOM   2908  CA  SER A 190      11.021  38.535 -40.526  1.00 17.71           C  
ANISOU 2908  CA  SER A 190     2390   2477   1861   -252    -22    177       C  
ATOM   2909  C   SER A 190      10.327  37.716 -39.446  1.00 19.07           C  
ANISOU 2909  C   SER A 190     2554   2613   2078   -202    -18    147       C  
ATOM   2910  O   SER A 190      10.610  37.862 -38.255  1.00 22.50           O  
ANISOU 2910  O   SER A 190     2982   3024   2545   -186    -20    148       O  
ATOM   2911  CB  SER A 190      12.041  37.662 -41.265  1.00 24.37           C  
ANISOU 2911  CB  SER A 190     3204   3382   2674   -263     20    156       C  
ATOM   2912  OG  SER A 190      12.697  38.395 -42.280  1.00 26.20           O  
ANISOU 2912  OG  SER A 190     3440   3656   2860   -313     19    184       O  
ATOM   2913  H   SER A 190      12.025  39.507 -39.149  1.00 22.37           H  
ATOM   2914  HA  SER A 190      10.362  38.834 -41.171  1.00 21.25           H  
ATOM   2915  HB2 SER A 190      12.702  37.343 -40.630  1.00 29.24           H  
ATOM   2916  HB3 SER A 190      11.579  36.910 -41.668  1.00 29.24           H  
ATOM   2917  HG  SER A 190      13.497  38.145 -42.344  1.00 31.44           H  
ATOM   2918  N   GLY A 191       9.408  36.857 -39.866  1.00 18.36           N  
ANISOU 2918  N   GLY A 191     2467   2522   1988   -183    -14    122       N  
ATOM   2919  CA  GLY A 191       8.773  35.954 -38.934  1.00 21.33           C  
ANISOU 2919  CA  GLY A 191     2834   2869   2402   -142     -8     94       C  
ATOM   2920  C   GLY A 191       9.738  34.915 -38.386  1.00 17.49           C  
ANISOU 2920  C   GLY A 191     2320   2397   1929   -122     29     68       C  
ATOM   2921  O   GLY A 191      10.875  34.756 -38.834  1.00 18.65           O  
ANISOU 2921  O   GLY A 191     2449   2582   2054   -136     54     66       O  
ATOM   2922  H   GLY A 191       9.139  36.782 -40.679  1.00 22.03           H  
ATOM   2923  HA2 GLY A 191       8.414  36.461 -38.189  1.00 25.60           H  
ATOM   2924  HA3 GLY A 191       8.047  35.491 -39.380  1.00 25.60           H  
ATOM   2925  N   ALA A 192       9.261  34.181 -37.393  1.00 18.07           N  
ANISOU 2925  N   ALA A 192     2387   2440   2038    -88     33     49       N  
ATOM   2926  CA  ALA A 192      10.093  33.176 -36.748  1.00 17.56           C  
ANISOU 2926  CA  ALA A 192     2299   2382   1992    -64     63     27       C  
ATOM   2927  C   ALA A 192      10.479  32.090 -37.746  1.00 18.64           C  
ANISOU 2927  C   ALA A 192     2427   2549   2106    -61     94     -3       C  
ATOM   2928  O   ALA A 192       9.607  31.581 -38.460  1.00 16.38           O  
ANISOU 2928  O   ALA A 192     2156   2259   1808    -62     91    -20       O  
ATOM   2929  CB  ALA A 192       9.338  32.556 -35.574  1.00 18.10           C  
ANISOU 2929  CB  ALA A 192     2367   2411   2100    -31     58     15       C  
ATOM   2930  H   ALA A 192       8.465  34.241 -37.073  1.00 21.68           H  
ATOM   2931  HA  ALA A 192      10.906  33.591 -36.420  1.00 21.07           H  
ATOM   2932  HB1 ALA A 192       8.464  32.266 -35.877  1.00 21.72           H  
ATOM   2933  HB2 ALA A 192       9.841  31.797 -35.240  1.00 21.72           H  
ATOM   2934  HB3 ALA A 192       9.242  33.221 -34.874  1.00 21.72           H  
ATOM   2935  N   PRO A 193      11.748  31.681 -37.806  1.00 14.74           N  
ANISOU 2935  N   PRO A 193     1909   2086   1604    -56    123    -12       N  
ATOM   2936  CA  PRO A 193      12.130  30.590 -38.709  1.00 16.73           C  
ANISOU 2936  CA  PRO A 193     2154   2366   1836    -46    154    -47       C  
ATOM   2937  C   PRO A 193      11.850  29.234 -38.079  1.00 17.39           C  
ANISOU 2937  C   PRO A 193     2238   2418   1953     -5    168    -79       C  
ATOM   2938  O   PRO A 193      11.609  29.107 -36.876  1.00 16.68           O  
ANISOU 2938  O   PRO A 193     2146   2293   1900     16    158    -72       O  
ATOM   2939  CB  PRO A 193      13.636  30.793 -38.900  1.00 18.87           C  
ANISOU 2939  CB  PRO A 193     2395   2687   2089    -53    178    -42       C  
ATOM   2940  CG  PRO A 193      14.078  31.346 -37.564  1.00 15.28           C  
ANISOU 2940  CG  PRO A 193     1926   2215   1664    -45    166    -17       C  
ATOM   2941  CD  PRO A 193      12.937  32.263 -37.142  1.00 17.73           C  
ANISOU 2941  CD  PRO A 193     2265   2483   1988    -60    128      8       C  
ATOM   2942  HA  PRO A 193      11.673  30.669 -39.561  1.00 20.07           H  
ATOM   2943  HB2 PRO A 193      14.069  29.948 -39.094  1.00 22.65           H  
ATOM   2944  HB3 PRO A 193      13.804  31.425 -39.617  1.00 22.65           H  
ATOM   2945  HG2 PRO A 193      14.200  30.623 -36.928  1.00 18.34           H  
ATOM   2946  HG3 PRO A 193      14.906  31.841 -37.665  1.00 18.34           H  
ATOM   2947  HD2 PRO A 193      12.830  32.255 -36.178  1.00 21.27           H  
ATOM   2948  HD3 PRO A 193      13.094  33.169 -37.451  1.00 21.27           H  
ATOM   2949  N   PHE A 194      11.876  28.218 -38.931  1.00 15.20           N  
ANISOU 2949  N   PHE A 194     1965   2152   1659      5    191   -115       N  
ATOM   2950  CA  PHE A 194      11.874  26.855 -38.452  1.00 12.53           C  
ANISOU 2950  CA  PHE A 194     1627   1783   1349     43    208   -147       C  
ATOM   2951  C   PHE A 194      13.170  26.590 -37.699  1.00 13.21           C  
ANISOU 2951  C   PHE A 194     1684   1883   1454     74    228   -145       C  
ATOM   2952  O   PHE A 194      14.222  27.154 -38.017  1.00 15.22           O  
ANISOU 2952  O   PHE A 194     1913   2184   1686     63    241   -135       O  
ATOM   2953  CB  PHE A 194      11.791  25.859 -39.604  1.00 17.03           C  
ANISOU 2953  CB  PHE A 194     2210   2365   1894     47    230   -190       C  
ATOM   2954  CG  PHE A 194      10.445  25.772 -40.291  1.00 15.05           C  
ANISOU 2954  CG  PHE A 194     1990   2098   1629     22    211   -199       C  
ATOM   2955  CD1 PHE A 194       9.302  26.317 -39.746  1.00 17.67           C  
ANISOU 2955  CD1 PHE A 194     2335   2400   1978      8    178   -175       C  
ATOM   2956  CD2 PHE A 194      10.339  25.112 -41.507  1.00 19.27           C  
ANISOU 2956  CD2 PHE A 194     2538   2652   2130     14    227   -236       C  
ATOM   2957  CE1 PHE A 194       8.081  26.196 -40.401  1.00 18.24           C  
ANISOU 2957  CE1 PHE A 194     2430   2465   2035    -14    160   -183       C  
ATOM   2958  CE2 PHE A 194       9.122  25.002 -42.162  1.00 19.11           C  
ANISOU 2958  CE2 PHE A 194     2545   2623   2095    -11    208   -245       C  
ATOM   2959  CZ  PHE A 194       7.995  25.538 -41.602  1.00 17.14           C  
ANISOU 2959  CZ  PHE A 194     2304   2345   1863    -25    174   -217       C  
ATOM   2960  H   PHE A 194      11.896  28.294 -39.788  1.00 18.24           H  
ATOM   2961  HA  PHE A 194      11.104  26.723 -37.877  1.00 15.03           H  
ATOM   2962  HB2 PHE A 194      12.443  26.114 -40.276  1.00 20.43           H  
ATOM   2963  HB3 PHE A 194      11.998  24.976 -39.260  1.00 20.43           H  
ATOM   2964  HD1 PHE A 194       9.348  26.768 -38.935  1.00 21.20           H  
ATOM   2965  HD2 PHE A 194      11.098  24.737 -41.890  1.00 23.12           H  
ATOM   2966  HE1 PHE A 194       7.316  26.563 -40.021  1.00 21.89           H  
ATOM   2967  HE2 PHE A 194       9.072  24.565 -42.981  1.00 22.94           H  
ATOM   2968  HZ  PHE A 194       7.175  25.457 -42.033  1.00 20.57           H  
ATOM   2969  N   SER A 195      13.100  25.687 -36.729  1.00 15.23           N  
ANISOU 2969  N   SER A 195     1940   2099   1747    109    232   -155       N  
ATOM   2970  CA  SER A 195      14.312  25.177 -36.119  1.00 14.85           C  
ANISOU 2970  CA  SER A 195     1864   2063   1717    145    253   -159       C  
ATOM   2971  C   SER A 195      15.061  24.306 -37.119  1.00 13.40           C  
ANISOU 2971  C   SER A 195     1672   1908   1512    167    286   -198       C  
ATOM   2972  O   SER A 195      14.475  23.696 -38.016  1.00 15.33           O  
ANISOU 2972  O   SER A 195     1942   2143   1741    163    293   -230       O  
ATOM   2973  CB  SER A 195      13.991  24.368 -34.860  1.00 16.36           C  
ANISOU 2973  CB  SER A 195     2062   2202   1953    178    246   -158       C  
ATOM   2974  OG  SER A 195      13.067  23.321 -35.119  1.00 17.30           O  
ANISOU 2974  OG  SER A 195     2214   2279   2082    187    246   -186       O  
ATOM   2975  H   SER A 195      12.371  25.358 -36.412  1.00 18.27           H  
ATOM   2976  HA  SER A 195      14.881  25.916 -35.853  1.00 17.82           H  
ATOM   2977  HB2 SER A 195      14.814  23.980 -34.522  1.00 19.64           H  
ATOM   2978  HB3 SER A 195      13.609  24.964 -34.198  1.00 19.64           H  
ATOM   2979  HG  SER A 195      12.574  23.201 -34.449  1.00 20.76           H  
ATOM   2980  N   ASP A 196      16.376  24.240 -36.954  1.00 16.26           N  
ANISOU 2980  N   ASP A 196     1998   2308   1871    190    308   -198       N  
ATOM   2981  CA  ASP A 196      17.171  23.349 -37.788  1.00 15.60           C  
ANISOU 2981  CA  ASP A 196     1902   2255   1771    221    342   -238       C  
ATOM   2982  C   ASP A 196      17.053  21.902 -37.333  1.00 16.32           C  
ANISOU 2982  C   ASP A 196     2010   2293   1898    274    352   -269       C  
ATOM   2983  O   ASP A 196      17.104  20.987 -38.166  1.00 17.85           O  
ANISOU 2983  O   ASP A 196     2219   2484   2080    295    373   -313       O  
ATOM   2984  CB  ASP A 196      18.619  23.834 -37.778  1.00 19.08           C  
ANISOU 2984  CB  ASP A 196     2292   2763   2195    227    362   -226       C  
ATOM   2985  CG  ASP A 196      18.777  25.169 -38.486  1.00 25.44           C  
ANISOU 2985  CG  ASP A 196     3086   3622   2957    170    355   -200       C  
ATOM   2986  OD1 ASP A 196      18.474  25.235 -39.692  1.00 24.56           O  
ANISOU 2986  OD1 ASP A 196     2990   3535   2809    146    364   -218       O  
ATOM   2987  OD2 ASP A 196      19.164  26.164 -37.843  1.00 20.69           O  
ANISOU 2987  OD2 ASP A 196     2464   3038   2358    146    340   -160       O  
ATOM   2988  H   ASP A 196      16.826  24.693 -36.377  1.00 19.51           H  
ATOM   2989  HA  ASP A 196      16.862  23.374 -38.707  1.00 18.72           H  
ATOM   2990  HB2 ASP A 196      18.914  23.941 -36.860  1.00 22.90           H  
ATOM   2991  HB3 ASP A 196      19.177  23.183 -38.232  1.00 22.90           H  
ATOM   2992  N   ASN A 197      16.873  21.692 -36.031  1.00 18.60           N  
ANISOU 2992  N   ASN A 197     2301   2538   2228    293    335   -247       N  
ATOM   2993  CA  ASN A 197      16.680  20.368 -35.461  1.00 17.62           C  
ANISOU 2993  CA  ASN A 197     2198   2355   2141    338    338   -268       C  
ATOM   2994  C   ASN A 197      15.963  20.526 -34.126  1.00 19.02           C  
ANISOU 2994  C   ASN A 197     2388   2486   2354    330    308   -232       C  
ATOM   2995  O   ASN A 197      15.718  21.641 -33.654  1.00 17.22           O  
ANISOU 2995  O   ASN A 197     2148   2273   2122    297    288   -197       O  
ATOM   2996  CB  ASN A 197      18.015  19.642 -35.289  1.00 16.06           C  
ANISOU 2996  CB  ASN A 197     1969   2179   1954    395    363   -283       C  
ATOM   2997  CG  ASN A 197      17.899  18.160 -35.543  1.00 18.07           C  
ANISOU 2997  CG  ASN A 197     2254   2383   2227    441    378   -327       C  
ATOM   2998  OD1 ASN A 197      16.826  17.578 -35.395  1.00 18.20           O  
ANISOU 2998  OD1 ASN A 197     2316   2338   2261    432    362   -335       O  
ATOM   2999  ND2 ASN A 197      19.003  17.540 -35.925  1.00 21.62           N  
ANISOU 2999  ND2 ASN A 197     2681   2861   2673    491    407   -356       N  
ATOM   3000  H   ASN A 197      16.859  22.320 -35.443  1.00 22.32           H  
ATOM   3001  HA  ASN A 197      16.120  19.837 -36.048  1.00 21.14           H  
ATOM   3002  HB2 ASN A 197      18.658  20.006 -35.916  1.00 19.27           H  
ATOM   3003  HB3 ASN A 197      18.330  19.768 -34.380  1.00 19.27           H  
ATOM   3004 HD21 ASN A 197      18.989  16.695 -36.083  1.00 25.94           H  
ATOM   3005 HD22 ASN A 197      19.735  17.982 -36.016  1.00 25.94           H  
ATOM   3006  N   VAL A 198      15.618  19.385 -33.534  1.00 14.86           N  
ANISOU 3006  N   VAL A 198     1884   1901   1860    362    305   -243       N  
ATOM   3007  CA  VAL A 198      15.059  19.302 -32.191  1.00 16.80           C  
ANISOU 3007  CA  VAL A 198     2139   2104   2140    362    281   -212       C  
ATOM   3008  C   VAL A 198      15.909  18.325 -31.398  1.00 19.71           C  
ANISOU 3008  C   VAL A 198     2497   2451   2540    417    290   -212       C  
ATOM   3009  O   VAL A 198      16.099  17.176 -31.816  1.00 18.63           O  
ANISOU 3009  O   VAL A 198     2381   2285   2413    453    305   -245       O  
ATOM   3010  CB  VAL A 198      13.591  18.844 -32.212  1.00 15.53           C  
ANISOU 3010  CB  VAL A 198     2024   1890   1988    336    264   -220       C  
ATOM   3011  CG1 VAL A 198      13.038  18.755 -30.811  1.00 18.06           C  
ANISOU 3011  CG1 VAL A 198     2350   2173   2340    335    241   -187       C  
ATOM   3012  CG2 VAL A 198      12.769  19.805 -33.047  1.00 17.50           C  
ANISOU 3012  CG2 VAL A 198     2281   2164   2206    286    254   -220       C  
ATOM   3013  H   VAL A 198      15.704  18.616 -33.909  1.00 17.83           H  
ATOM   3014  HA  VAL A 198      15.100  20.172 -31.765  1.00 20.16           H  
ATOM   3015  HB  VAL A 198      13.539  17.960 -32.607  1.00 18.64           H  
ATOM   3016 HG11 VAL A 198      12.183  18.298 -30.838  1.00 21.67           H  
ATOM   3017 HG12 VAL A 198      13.660  18.260 -30.256  1.00 21.67           H  
ATOM   3018 HG13 VAL A 198      12.923  19.652 -30.459  1.00 21.67           H  
ATOM   3019 HG21 VAL A 198      11.831  19.685 -32.834  1.00 21.00           H  
ATOM   3020 HG22 VAL A 198      13.041  20.713 -32.842  1.00 21.00           H  
ATOM   3021 HG23 VAL A 198      12.923  19.618 -33.986  1.00 21.00           H  
ATOM   3022  N   LEU A 199      16.409  18.773 -30.258  1.00 16.07           N  
ANISOU 3022  N   LEU A 199     2008   2004   2095    425    278   -175       N  
ATOM   3023  CA  LEU A 199      17.290  17.959 -29.439  1.00 17.38           C  
ANISOU 3023  CA  LEU A 199     2158   2157   2289    479    283   -167       C  
ATOM   3024  C   LEU A 199      16.511  17.416 -28.254  1.00 18.37           C  
ANISOU 3024  C   LEU A 199     2311   2224   2446    479    260   -143       C  
ATOM   3025  O   LEU A 199      15.772  18.151 -27.588  1.00 17.07           O  
ANISOU 3025  O   LEU A 199     2148   2057   2281    441    239   -116       O  
ATOM   3026  CB  LEU A 199      18.501  18.758 -28.967  1.00 20.53           C  
ANISOU 3026  CB  LEU A 199     2502   2618   2679    488    286   -141       C  
ATOM   3027  CG  LEU A 199      19.406  19.340 -30.054  1.00 21.53           C  
ANISOU 3027  CG  LEU A 199     2596   2814   2772    484    310   -159       C  
ATOM   3028  CD1 LEU A 199      20.635  19.965 -29.410  1.00 26.73           C  
ANISOU 3028  CD1 LEU A 199     3199   3531   3427    494    311   -130       C  
ATOM   3029  CD2 LEU A 199      19.835  18.315 -31.064  1.00 24.91           C  
ANISOU 3029  CD2 LEU A 199     3030   3239   3195    526    338   -205       C  
ATOM   3030  H   LEU A 199      16.249  19.554 -29.935  1.00 19.29           H  
ATOM   3031  HA  LEU A 199      17.619  17.210 -29.961  1.00 20.86           H  
ATOM   3032  HB2 LEU A 199      18.179  19.503 -28.436  1.00 24.63           H  
ATOM   3033  HB3 LEU A 199      19.051  18.174 -28.422  1.00 24.63           H  
ATOM   3034  HG  LEU A 199      18.898  20.013 -30.534  1.00 25.84           H  
ATOM   3035 HD11 LEU A 199      21.159  20.410 -30.095  1.00 32.08           H  
ATOM   3036 HD12 LEU A 199      20.349  20.608 -28.742  1.00 32.08           H  
ATOM   3037 HD13 LEU A 199      21.163  19.266 -28.992  1.00 32.08           H  
ATOM   3038 HD21 LEU A 199      20.307  18.760 -31.785  1.00 29.89           H  
ATOM   3039 HD22 LEU A 199      20.420  17.672 -30.633  1.00 29.89           H  
ATOM   3040 HD23 LEU A 199      19.049  17.865 -31.412  1.00 29.89           H  
ATOM   3041  N   PHE A 200      16.665  16.124 -28.018  1.00 18.75           N  
ANISOU 3041  N   PHE A 200     2380   2223   2521    523    264   -155       N  
ATOM   3042  CA  PHE A 200      16.076  15.435 -26.882  1.00 20.64           C  
ANISOU 3042  CA  PHE A 200     2645   2405   2791    527    244   -131       C  
ATOM   3043  C   PHE A 200      17.206  15.180 -25.899  1.00 20.79           C  
ANISOU 3043  C   PHE A 200     2632   2438   2831    575    242   -104       C  
ATOM   3044  O   PHE A 200      18.162  14.472 -26.229  1.00 18.85           O  
ANISOU 3044  O   PHE A 200     2375   2193   2593    628    258   -123       O  
ATOM   3045  CB  PHE A 200      15.426  14.128 -27.320  1.00 15.84           C  
ANISOU 3045  CB  PHE A 200     2091   1728   2200    539    246   -160       C  
ATOM   3046  CG  PHE A 200      14.295  14.303 -28.287  1.00 17.59           C  
ANISOU 3046  CG  PHE A 200     2344   1940   2401    491    246   -187       C  
ATOM   3047  CD1 PHE A 200      14.538  14.610 -29.619  1.00 17.74           C  
ANISOU 3047  CD1 PHE A 200     2357   1992   2390    487    266   -224       C  
ATOM   3048  CD2 PHE A 200      12.988  14.135 -27.869  1.00 19.05           C  
ANISOU 3048  CD2 PHE A 200     2562   2085   2593    450    225   -174       C  
ATOM   3049  CE1 PHE A 200      13.498  14.759 -30.508  1.00 19.86           C  
ANISOU 3049  CE1 PHE A 200     2654   2255   2638    442    263   -246       C  
ATOM   3050  CE2 PHE A 200      11.948  14.281 -28.748  1.00 16.41           C  
ANISOU 3050  CE2 PHE A 200     2253   1745   2239    407    223   -198       C  
ATOM   3051  CZ  PHE A 200      12.202  14.586 -30.077  1.00 19.11           C  
ANISOU 3051  CZ  PHE A 200     2590   2119   2552    404    241   -233       C  
ATOM   3052  H   PHE A 200      17.126  15.605 -28.524  1.00 22.50           H  
ATOM   3053  HA  PHE A 200      15.389  15.975 -26.459  1.00 24.76           H  
ATOM   3054  HB2 PHE A 200      16.098  13.575 -27.748  1.00 19.01           H  
ATOM   3055  HB3 PHE A 200      15.076  13.677 -26.536  1.00 19.01           H  
ATOM   3056  HD1 PHE A 200      15.413  14.716 -29.914  1.00 21.29           H  
ATOM   3057  HD2 PHE A 200      12.813  13.921 -26.981  1.00 22.87           H  
ATOM   3058  HE1 PHE A 200      13.670  14.976 -31.396  1.00 23.83           H  
ATOM   3059  HE2 PHE A 200      11.072  14.174 -28.455  1.00 19.70           H  
ATOM   3060  HZ  PHE A 200      11.497  14.674 -30.676  1.00 22.93           H  
ATOM   3061  N   ASN A 201      17.120  15.776 -24.716  1.00 18.78           N  
ANISOU 3061  N   ASN A 201     2358   2196   2580    557    222    -62       N  
ATOM   3062  CA  ASN A 201      18.198  15.657 -23.735  1.00 18.03           C  
ANISOU 3062  CA  ASN A 201     2228   2122   2500    596    217    -32       C  
ATOM   3063  C   ASN A 201      19.552  15.931 -24.384  1.00 18.38           C  
ANISOU 3063  C   ASN A 201     2226   2227   2530    629    239    -48       C  
ATOM   3064  O   ASN A 201      20.538  15.230 -24.145  1.00 22.32           O  
ANISOU 3064  O   ASN A 201     2706   2730   3046    686    245    -46       O  
ATOM   3065  CB  ASN A 201      18.192  14.277 -23.090  1.00 18.57           C  
ANISOU 3065  CB  ASN A 201     2325   2127   2602    638    209    -24       C  
ATOM   3066  CG  ASN A 201      18.519  14.324 -21.621  1.00 17.50           C  
ANISOU 3066  CG  ASN A 201     2170   1998   2480    648    188     24       C  
ATOM   3067  OD1 ASN A 201      18.720  15.397 -21.046  1.00 20.34           O  
ANISOU 3067  OD1 ASN A 201     2495   2410   2824    620    179     49       O  
ATOM   3068  ND2 ASN A 201      18.559  13.152 -20.994  1.00 19.98           N  
ANISOU 3068  ND2 ASN A 201     2509   2258   2824    684    177     39       N  
ATOM   3069  H   ASN A 201      16.453  16.252 -24.457  1.00 22.53           H  
ATOM   3070  HA  ASN A 201      18.055  16.319 -23.042  1.00 21.63           H  
ATOM   3071  HB2 ASN A 201      17.311  13.884 -23.190  1.00 22.28           H  
ATOM   3072  HB3 ASN A 201      18.855  13.720 -23.528  1.00 22.28           H  
ATOM   3073 HD21 ASN A 201      18.422  12.429 -21.439  1.00 23.98           H  
ATOM   3074  N   GLY A 202      19.586  16.937 -25.255  1.00 20.44           N  
ANISOU 3074  N   GLY A 202     2470   2537   2760    594    250    -63       N  
ATOM   3075  CA  GLY A 202      20.821  17.383 -25.862  1.00 21.66           C  
ANISOU 3075  CA  GLY A 202     2576   2760   2895    612    270    -73       C  
ATOM   3076  C   GLY A 202      21.290  16.646 -27.096  1.00 22.44           C  
ANISOU 3076  C   GLY A 202     2677   2862   2986    650    299   -119       C  
ATOM   3077  O   GLY A 202      22.392  16.939 -27.575  1.00 24.11           O  
ANISOU 3077  O   GLY A 202     2843   3137   3180    670    319   -128       O  
ATOM   3078  H   GLY A 202      18.894  17.379 -25.510  1.00 24.53           H  
ATOM   3079  HA2 GLY A 202      20.715  18.315 -26.110  1.00 25.99           H  
ATOM   3080  HA3 GLY A 202      21.526  17.310 -25.200  1.00 25.99           H  
ATOM   3081  N   THR A 203      20.512  15.726 -27.660  1.00 20.51           N  
ANISOU 3081  N   THR A 203     2484   2556   2752    660    304   -150       N  
ATOM   3082  CA  THR A 203      21.011  15.002 -28.820  1.00 23.07           C  
ANISOU 3082  CA  THR A 203     2812   2884   3069    699    332   -199       C  
ATOM   3083  C   THR A 203      19.904  14.702 -29.822  1.00 21.12           C  
ANISOU 3083  C   THR A 203     2619   2596   2811    669    337   -236       C  
ATOM   3084  O   THR A 203      18.712  14.717 -29.504  1.00 22.66           O  
ANISOU 3084  O   THR A 203     2852   2743   3013    628    317   -224       O  
ATOM   3085  CB  THR A 203      21.717  13.700 -28.397  1.00 26.04           C  
ANISOU 3085  CB  THR A 203     3192   3224   3479    777    337   -207       C  
ATOM   3086  OG1 THR A 203      22.296  13.078 -29.551  1.00 31.73           O  
ANISOU 3086  OG1 THR A 203     3910   3956   4188    820    368   -258       O  
ATOM   3087  CG2 THR A 203      20.746  12.732 -27.733  1.00 24.81           C  
ANISOU 3087  CG2 THR A 203     3095   2974   3358    780    316   -198       C  
ATOM   3088  H   THR A 203      19.722  15.513 -27.397  1.00 24.61           H  
ATOM   3089  HA  THR A 203      21.640  15.577 -29.282  1.00 27.68           H  
ATOM   3090  HB  THR A 203      22.411  13.910 -27.753  1.00 31.25           H  
ATOM   3091  HG1 THR A 203      22.710  13.649 -30.007  1.00 38.07           H  
ATOM   3092 HG21 THR A 203      21.211  11.921 -27.474  1.00 29.77           H  
ATOM   3093 HG22 THR A 203      20.360  13.139 -26.942  1.00 29.77           H  
ATOM   3094 HG23 THR A 203      20.032  12.502 -28.349  1.00 29.77           H  
ATOM   3095  N   ALA A 204      20.339  14.434 -31.050  1.00 17.95           N  
ANISOU 3095  N   ALA A 204     2214   2219   2387    688    365   -281       N  
ATOM   3096  CA  ALA A 204      19.471  14.142 -32.179  1.00 21.20           C  
ANISOU 3096  CA  ALA A 204     2671   2605   2781    662    373   -323       C  
ATOM   3097  C   ALA A 204      20.363  13.682 -33.319  1.00 22.90           C  
ANISOU 3097  C   ALA A 204     2870   2855   2975    704    408   -373       C  
ATOM   3098  O   ALA A 204      21.575  13.914 -33.305  1.00 22.76           O  
ANISOU 3098  O   ALA A 204     2800   2899   2950    740    425   -370       O  
ATOM   3099  CB  ALA A 204      18.655  15.362 -32.610  1.00 23.50           C  
ANISOU 3099  CB  ALA A 204     2963   2928   3040    587    363   -309       C  
ATOM   3100  H   ALA A 204      21.172  14.415 -31.261  1.00 21.54           H  
ATOM   3101  HA  ALA A 204      18.849  13.436 -31.942  1.00 25.44           H  
ATOM   3102  HB1 ALA A 204      18.027  15.094 -33.299  1.00 28.20           H  
ATOM   3103  HB2 ALA A 204      18.175  15.709 -31.842  1.00 28.20           H  
ATOM   3104  HB3 ALA A 204      19.258  16.039 -32.957  1.00 28.20           H  
ATOM   3105  N   LYS A 205      19.751  13.024 -34.300  1.00 22.98           N  
ANISOU 3105  N   LYS A 205     2926   2829   2974    700    418   -420       N  
ATOM   3106  CA  LYS A 205      20.390  12.778 -35.582  1.00 24.67           C  
ANISOU 3106  CA  LYS A 205     3130   3087   3156    725    453   -473       C  
ATOM   3107  C   LYS A 205      20.083  13.922 -36.540  1.00 27.66           C  
ANISOU 3107  C   LYS A 205     3494   3531   3484    660    459   -474       C  
ATOM   3108  O   LYS A 205      19.013  14.540 -36.480  1.00 23.40           O  
ANISOU 3108  O   LYS A 205     2978   2976   2938    598    436   -452       O  
ATOM   3109  CB  LYS A 205      19.914  11.467 -36.204  1.00 25.80           C  
ANISOU 3109  CB  LYS A 205     3334   3158   3310    752    461   -529       C  
ATOM   3110  CG  LYS A 205      20.516  10.231 -35.572  1.00 30.05           C  
ANISOU 3110  CG  LYS A 205     3881   3640   3896    816    458   -534       C  
ATOM   3111  CD  LYS A 205      20.560   9.057 -36.551  1.00 25.57           C  
ANISOU 3111  CD  LYS A 205     3350   3032   3333    835    475   -595       C  
ATOM   3112  CE  LYS A 205      21.227   7.857 -35.890  1.00 37.33           C  
ANISOU 3112  CE  LYS A 205     4843   4466   4875    890    467   -593       C  
ATOM   3113  NZ  LYS A 205      20.988   6.599 -36.645  1.00 98.02           N  
ANISOU 3113  NZ  LYS A 205    12581  12089  12574    904    476   -648       N  
ATOM   3114  H   LYS A 205      18.954  12.707 -34.243  1.00 27.57           H  
ATOM   3115  HA  LYS A 205      21.348  12.714 -35.448  1.00 29.60           H  
ATOM   3116  HB2 LYS A 205      18.950  11.408 -36.107  1.00 30.96           H  
ATOM   3117  HB3 LYS A 205      20.153  11.464 -37.144  1.00 30.96           H  
ATOM   3118  HG2 LYS A 205      21.423  10.426 -35.289  1.00 36.06           H  
ATOM   3119  HG3 LYS A 205      19.979   9.969 -34.807  1.00 36.06           H  
ATOM   3120  HD2 LYS A 205      19.658   8.810 -36.807  1.00 30.68           H  
ATOM   3121  HD3 LYS A 205      21.073   9.305 -37.336  1.00 30.68           H  
ATOM   3122  HE2 LYS A 205      22.185   8.008 -35.849  1.00 44.80           H  
ATOM   3123  HE3 LYS A 205      20.870   7.746 -34.996  1.00 44.80           H  
ATOM   3124  HZ1 LYS A 205      21.273   5.902 -36.171  1.00117.63           H  
ATOM   3125  HZ2 LYS A 205      20.118   6.502 -36.807  1.00117.63           H  
ATOM   3126  HZ3 LYS A 205      21.425   6.621 -37.419  1.00117.63           H  
ATOM   3127  N   HIS A 206      21.033  14.189 -37.431  1.00 24.37           N  
ANISOU 3127  N   HIS A 206     3038   3191   3032    675    490   -500       N  
ATOM   3128  CA  HIS A 206      20.824  15.156 -38.499  1.00 23.30           C  
ANISOU 3128  CA  HIS A 206     2890   3118   2843    616    499   -506       C  
ATOM   3129  C   HIS A 206      19.818  14.606 -39.501  1.00 32.33           C  
ANISOU 3129  C   HIS A 206     4092   4224   3969    593    501   -551       C  
ATOM   3130  O   HIS A 206      19.939  13.447 -39.916  1.00 27.65           O  
ANISOU 3130  O   HIS A 206     3527   3594   3384    639    518   -602       O  
ATOM   3131  CB  HIS A 206      22.141  15.454 -39.200  1.00 22.67           C  
ANISOU 3131  CB  HIS A 206     2753   3134   2728    640    534   -523       C  
ATOM   3132  CG  HIS A 206      22.100  16.684 -40.045  1.00 23.90           C  
ANISOU 3132  CG  HIS A 206     2886   3365   2830    574    538   -510       C  
ATOM   3133  ND1 HIS A 206      21.562  16.701 -41.313  1.00 22.40           N  
ANISOU 3133  ND1 HIS A 206     2723   3190   2597    540    550   -545       N  
ATOM   3134  CD2 HIS A 206      22.511  17.949 -39.793  1.00 24.62           C  
ANISOU 3134  CD2 HIS A 206     2934   3519   2903    531    530   -462       C  
ATOM   3135  CE1 HIS A 206      21.651  17.920 -41.810  1.00 25.67           C  
ANISOU 3135  CE1 HIS A 206     3111   3674   2970    481    548   -517       C  
ATOM   3136  NE2 HIS A 206      22.228  18.696 -40.910  1.00 30.17           N  
ANISOU 3136  NE2 HIS A 206     3639   4270   3553    474    536   -467       N  
ATOM   3137  H   HIS A 206      21.811  13.822 -37.440  1.00 29.25           H  
ATOM   3138  HA  HIS A 206      20.477  15.982 -38.127  1.00 27.96           H  
ATOM   3139  HB2 HIS A 206      22.832  15.577 -38.530  1.00 27.21           H  
ATOM   3140  HB3 HIS A 206      22.366  14.706 -39.775  1.00 27.21           H  
ATOM   3141  HD2 HIS A 206      22.909  18.254 -39.010  1.00 29.55           H  
ATOM   3142  HE1 HIS A 206      21.357  18.188 -42.651  1.00 30.81           H  
ATOM   3143  HE2 HIS A 206      22.399  19.533 -41.008  1.00 36.20           H  
ATOM   3144  N   PRO A 207      18.828  15.399 -39.926  1.00 23.60           N  
ANISOU 3144  N   PRO A 207     3005   3124   2838    522    483   -535       N  
ATOM   3145  CA  PRO A 207      17.798  14.860 -40.832  1.00 23.42           C  
ANISOU 3145  CA  PRO A 207     3037   3065   2798    496    481   -576       C  
ATOM   3146  C   PRO A 207      18.308  14.509 -42.223  1.00 24.34           C  
ANISOU 3146  C   PRO A 207     3152   3229   2868    509    516   -634       C  
ATOM   3147  O   PRO A 207      17.651  13.722 -42.918  1.00 27.53           O  
ANISOU 3147  O   PRO A 207     3604   3594   3263    505    519   -681       O  
ATOM   3148  CB  PRO A 207      16.755  15.990 -40.886  1.00 28.16           C  
ANISOU 3148  CB  PRO A 207     3645   3677   3380    420    452   -535       C  
ATOM   3149  CG  PRO A 207      17.524  17.238 -40.557  1.00 26.77           C  
ANISOU 3149  CG  PRO A 207     3413   3569   3190    405    452   -489       C  
ATOM   3150  CD  PRO A 207      18.563  16.802 -39.553  1.00 22.90           C  
ANISOU 3150  CD  PRO A 207     2891   3072   2737    465    460   -478       C  
ATOM   3151  HA  PRO A 207      17.398  14.069 -40.438  1.00 28.11           H  
ATOM   3152  HB2 PRO A 207      16.370  16.043 -41.774  1.00 33.80           H  
ATOM   3153  HB3 PRO A 207      16.058  15.829 -40.231  1.00 33.80           H  
ATOM   3154  HG2 PRO A 207      17.943  17.589 -41.358  1.00 32.12           H  
ATOM   3155  HG3 PRO A 207      16.930  17.902 -40.175  1.00 32.12           H  
ATOM   3156  HD2 PRO A 207      19.367  17.339 -39.633  1.00 27.48           H  
ATOM   3157  HD3 PRO A 207      18.214  16.859 -38.649  1.00 27.48           H  
ATOM   3158  N   GLU A 208      19.443  15.057 -42.661  1.00 27.12           N  
ANISOU 3158  N   GLU A 208     3449   3666   3188    522    543   -635       N  
ATOM   3159  CA  GLU A 208      19.975  14.743 -43.983  1.00 23.92           C  
ANISOU 3159  CA  GLU A 208     3038   3317   2734    535    579   -692       C  
ATOM   3160  C   GLU A 208      21.197  13.834 -43.944  1.00 31.37           C  
ANISOU 3160  C   GLU A 208     3957   4265   3695    611    610   -723       C  
ATOM   3161  O   GLU A 208      21.277  12.874 -44.719  1.00 34.87           O  
ANISOU 3161  O   GLU A 208     4433   4683   4134    632    628   -770       O  
ATOM   3162  CB  GLU A 208      20.330  16.037 -44.736  1.00 27.22           C  
ANISOU 3162  CB  GLU A 208     3413   3835   3095    481    588   -668       C  
ATOM   3163  CG  GLU A 208      19.230  17.087 -44.773  1.00 30.37           C  
ANISOU 3163  CG  GLU A 208     3831   4228   3480    401    553   -622       C  
ATOM   3164  CD  GLU A 208      17.950  16.574 -45.399  1.00 66.89           C  
ANISOU 3164  CD  GLU A 208     8517   8801   8096    372    539   -653       C  
ATOM   3165  OE1 GLU A 208      18.030  15.719 -46.306  1.00 80.28           O  
ANISOU 3165  OE1 GLU A 208    10234  10499   9768    392    563   -714       O  
ATOM   3166  OE2 GLU A 208      16.861  17.022 -44.980  1.00 58.43           O  
ANISOU 3166  OE2 GLU A 208     7472   7690   7040    328    503   -617       O  
ATOM   3167  H   GLU A 208      19.919  15.612 -42.208  1.00 32.54           H  
ATOM   3168  HA  GLU A 208      19.280  14.283 -44.478  1.00 28.70           H  
ATOM   3169  HB2 GLU A 208      21.101  16.440 -44.307  1.00 32.67           H  
ATOM   3170  HB3 GLU A 208      20.544  15.808 -45.654  1.00 32.67           H  
ATOM   3171  HG2 GLU A 208      19.029  17.366 -43.866  1.00 36.44           H  
ATOM   3172  HG3 GLU A 208      19.535  17.846 -45.294  1.00 36.44           H  
ATOM   3173  N   THR A 209      22.162  14.115 -43.066  1.00 26.22           N  
ANISOU 3173  N   THR A 209     3254   3639   3069    642    611   -685       N  
ATOM   3174  CA  THR A 209      23.403  13.353 -43.006  1.00 34.53           C  
ANISOU 3174  CA  THR A 209     4278   4697   4143    700    633   -697       C  
ATOM   3175  C   THR A 209      23.316  12.117 -42.115  1.00 37.66           C  
ANISOU 3175  C   THR A 209     4708   4995   4605    756    621   -704       C  
ATOM   3176  O   THR A 209      24.136  11.203 -42.261  1.00 32.97           O  
ANISOU 3176  O   THR A 209     4108   4388   4031    806    639   -729       O  
ATOM   3177  CB  THR A 209      24.552  14.232 -42.485  1.00 28.58           C  
ANISOU 3177  CB  THR A 209     3449   4023   3386    703    638   -651       C  
ATOM   3178  OG1 THR A 209      24.365  14.484 -41.084  1.00 29.40           O  
ANISOU 3178  OG1 THR A 209     3546   4093   3532    712    609   -606       O  
ATOM   3179  CG2 THR A 209      24.621  15.567 -43.220  1.00 34.58           C  
ANISOU 3179  CG2 THR A 209     4176   4878   4085    638    644   -632       C  
ATOM   3180  H   THR A 209      22.118  14.750 -42.487  1.00 31.46           H  
ATOM   3181  HA  THR A 209      23.616  13.067 -43.909  1.00 41.43           H  
ATOM   3182  HB  THR A 209      25.389  13.766 -42.634  1.00 34.29           H  
ATOM   3183  HG1 THR A 209      24.842  15.131 -40.842  1.00 35.28           H  
ATOM   3184 HG21 THR A 209      24.844  16.277 -42.599  1.00 41.50           H  
ATOM   3185 HG22 THR A 209      25.301  15.529 -43.912  1.00 41.50           H  
ATOM   3186 HG23 THR A 209      23.765  15.764 -43.631  1.00 41.50           H  
ATOM   3187  N   GLY A 210      22.364  12.067 -41.190  1.00 35.47           N  
ANISOU 3187  N   GLY A 210     4466   4650   4361    747    589   -682       N  
ATOM   3188  CA  GLY A 210      22.322  10.977 -40.241  1.00 30.32           C  
ANISOU 3188  CA  GLY A 210     3843   3908   3771    793    573   -679       C  
ATOM   3189  C   GLY A 210      23.399  10.999 -39.178  1.00 31.89           C  
ANISOU 3189  C   GLY A 210     3988   4123   4004    835    568   -638       C  
ATOM   3190  O   GLY A 210      23.455  10.076 -38.359  1.00 33.75           O  
ANISOU 3190  O   GLY A 210     4244   4288   4291    874    553   -632       O  
ATOM   3191  H   GLY A 210      21.739  12.650 -41.098  1.00 42.56           H  
ATOM   3192  HA2 GLY A 210      21.464  10.995 -39.789  1.00 36.39           H  
ATOM   3193  HA3 GLY A 210      22.406  10.142 -40.726  1.00 36.39           H  
ATOM   3194  N   GLU A 211      24.255  12.016 -39.157  1.00 28.29           N  
ANISOU 3194  N   GLU A 211     3466   3759   3521    825    578   -610       N  
ATOM   3195  CA  GLU A 211      25.239  12.138 -38.090  1.00 24.63           C  
ANISOU 3195  CA  GLU A 211     2952   3318   3088    858    570   -568       C  
ATOM   3196  C   GLU A 211      24.529  12.418 -36.773  1.00 34.72           C  
ANISOU 3196  C   GLU A 211     4245   4547   4398    847    534   -520       C  
ATOM   3197  O   GLU A 211      23.424  12.964 -36.741  1.00 26.53           O  
ANISOU 3197  O   GLU A 211     3240   3491   3348    806    520   -512       O  
ATOM   3198  CB  GLU A 211      26.240  13.244 -38.415  1.00 38.32           C  
ANISOU 3198  CB  GLU A 211     4614   5165   4782    837    587   -547       C  
ATOM   3199  CG  GLU A 211      27.030  12.967 -39.705  1.00 32.80           C  
ANISOU 3199  CG  GLU A 211     3895   4521   4048    848    623   -590       C  
ATOM   3200  CD  GLU A 211      28.210  13.903 -39.903  1.00 54.29           C  
ANISOU 3200  CD  GLU A 211     6541   7351   6734    832    638   -566       C  
ATOM   3201  OE1 GLU A 211      28.128  15.070 -39.473  1.00 32.52           O  
ANISOU 3201  OE1 GLU A 211     3755   4640   3960    787    623   -523       O  
ATOM   3202  OE2 GLU A 211      29.226  13.469 -40.485  1.00 63.10           O  
ANISOU 3202  OE2 GLU A 211     7627   8508   7841    864    663   -590       O  
ATOM   3203  H   GLU A 211      24.287  12.644 -39.744  1.00 33.94           H  
ATOM   3204  HA  GLU A 211      25.742  11.314 -37.997  1.00 29.56           H  
ATOM   3205  HB2 GLU A 211      25.762  14.080 -38.529  1.00 45.99           H  
ATOM   3206  HB3 GLU A 211      26.874  13.320 -37.685  1.00 45.99           H  
ATOM   3207  HG2 GLU A 211      27.372  12.060 -39.675  1.00 39.36           H  
ATOM   3208  HG3 GLU A 211      26.436  13.073 -40.465  1.00 39.36           H  
ATOM   3209  N   GLY A 212      25.166  12.026 -35.679  1.00 27.61           N  
ANISOU 3209  N   GLY A 212     3323   3628   3540    886    519   -490       N  
ATOM   3210  CA  GLY A 212      24.565  12.160 -34.367  1.00 25.31           C  
ANISOU 3210  CA  GLY A 212     3048   3288   3282    880    486   -444       C  
ATOM   3211  C   GLY A 212      23.901  10.876 -33.910  1.00 28.33           C  
ANISOU 3211  C   GLY A 212     3493   3562   3710    905    467   -455       C  
ATOM   3212  O   GLY A 212      24.011   9.818 -34.535  1.00 32.20           O  
ANISOU 3212  O   GLY A 212     4011   4012   4213    934    479   -498       O  
ATOM   3213  H   GLY A 212      25.952  11.678 -35.674  1.00 33.14           H  
ATOM   3214  HA2 GLY A 212      25.249  12.398 -33.722  1.00 30.38           H  
ATOM   3215  HA3 GLY A 212      23.895  12.860 -34.389  1.00 30.38           H  
ATOM   3216  N   GLU A 213      23.181  10.990 -32.789  1.00 26.68           N  
ANISOU 3216  N   GLU A 213     3307   3306   3526    891    437   -413       N  
ATOM   3217  CA  GLU A 213      22.542   9.848 -32.150  1.00 30.98           C  
ANISOU 3217  CA  GLU A 213     3907   3749   4114    908    413   -411       C  
ATOM   3218  C   GLU A 213      21.190  10.257 -31.577  1.00 33.75           C  
ANISOU 3218  C   GLU A 213     4301   4055   4467    862    390   -382       C  
ATOM   3219  O   GLU A 213      21.019  11.380 -31.091  1.00 26.11           O  
ANISOU 3219  O   GLU A 213     3307   3131   3483    833    384   -345       O  
ATOM   3220  CB  GLU A 213      23.402   9.268 -31.009  1.00 36.59           C  
ANISOU 3220  CB  GLU A 213     4592   4444   4866    952    396   -376       C  
ATOM   3221  CG  GLU A 213      24.783   8.782 -31.417  1.00 73.86           C  
ANISOU 3221  CG  GLU A 213     9268   9204   9591   1003    416   -399       C  
ATOM   3222  CD  GLU A 213      24.730   7.594 -32.356  1.00127.37           C  
ANISOU 3222  CD  GLU A 213    16086  15928  16379   1031    433   -456       C  
ATOM   3223  OE1 GLU A 213      23.676   6.924 -32.408  1.00 50.15           O  
ANISOU 3223  OE1 GLU A 213     6372   6067   6616   1015    420   -471       O  
ATOM   3224  OE2 GLU A 213      25.741   7.333 -33.045  1.00 68.60           O  
ANISOU 3224  OE2 GLU A 213     8610   8528   8928   1066    459   -486       O  
ATOM   3225  H   GLU A 213      23.050  11.734 -32.377  1.00 32.02           H  
ATOM   3226  HA  GLU A 213      22.402   9.164 -32.824  1.00 37.17           H  
ATOM   3227  HB2 GLU A 213      23.524   9.958 -30.338  1.00 43.91           H  
ATOM   3228  HB3 GLU A 213      22.930   8.512 -30.625  1.00 43.91           H  
ATOM   3229  HG2 GLU A 213      25.250   9.501 -31.869  1.00 88.63           H  
ATOM   3230  HG3 GLU A 213      25.272   8.516 -30.623  1.00 88.63           H  
ATOM   3231  N   TYR A 214      20.233   9.328 -31.621  1.00 22.02           N  
ANISOU 3231  N   TYR A 214     2882   2482   3002    853    377   -400       N  
ATOM   3232  CA  TYR A 214      18.983   9.528 -30.904  1.00 22.19           C  
ANISOU 3232  CA  TYR A 214     2945   2453   3032    813    353   -368       C  
ATOM   3233  C   TYR A 214      19.232   9.433 -29.405  1.00 23.19           C  
ANISOU 3233  C   TYR A 214     3056   2562   3192    827    327   -311       C  
ATOM   3234  O   TYR A 214      20.024   8.606 -28.940  1.00 23.57           O  
ANISOU 3234  O   TYR A 214     3093   2592   3271    870    320   -305       O  
ATOM   3235  CB  TYR A 214      17.930   8.485 -31.290  1.00 27.54           C  
ANISOU 3235  CB  TYR A 214     3698   3044   3723    794    344   -399       C  
ATOM   3236  CG  TYR A 214      17.599   8.425 -32.760  1.00 24.22           C  
ANISOU 3236  CG  TYR A 214     3300   2633   3269    776    366   -458       C  
ATOM   3237  CD1 TYR A 214      16.887   9.446 -33.383  1.00 23.09           C  
ANISOU 3237  CD1 TYR A 214     3149   2536   3087    710    366   -458       C  
ATOM   3238  CD2 TYR A 214      17.991   7.340 -33.526  1.00 26.80           C  
ANISOU 3238  CD2 TYR A 214     3646   2931   3605    804    377   -508       C  
ATOM   3239  CE1 TYR A 214      16.593   9.381 -34.737  1.00 34.04           C  
ANISOU 3239  CE1 TYR A 214     4556   3937   4440    690    384   -511       C  
ATOM   3240  CE2 TYR A 214      17.695   7.264 -34.865  1.00 27.15           C  
ANISOU 3240  CE2 TYR A 214     3712   2988   3617    786    397   -564       C  
ATOM   3241  CZ  TYR A 214      17.001   8.282 -35.468  1.00 25.06           C  
ANISOU 3241  CZ  TYR A 214     3451   2766   3307    739    404   -568       C  
ATOM   3242  OH  TYR A 214      16.728   8.189 -36.812  1.00 27.32           O  
ANISOU 3242  OH  TYR A 214     3757   3067   3556    719    422   -623       O  
ATOM   3243  H   TYR A 214      20.285   8.586 -32.053  1.00 26.42           H  
ATOM   3244  HA  TYR A 214      18.634  10.403 -31.136  1.00 26.62           H  
ATOM   3245  HB2 TYR A 214      18.255   7.609 -31.029  1.00 33.05           H  
ATOM   3246  HB3 TYR A 214      17.109   8.688 -30.815  1.00 33.05           H  
ATOM   3247  HD1 TYR A 214      16.606  10.179 -32.886  1.00 27.71           H  
ATOM   3248  HD2 TYR A 214      18.465   6.648 -33.125  1.00 32.16           H  
ATOM   3249  HE1 TYR A 214      16.125  10.072 -35.149  1.00 40.84           H  
ATOM   3250  HE2 TYR A 214      17.963   6.525 -35.361  1.00 32.58           H  
ATOM   3251  HH  TYR A 214      16.457   8.929 -37.103  1.00 32.78           H  
ATOM   3252  N   ALA A 215      18.548  10.275 -28.643  1.00 23.38           N  
ANISOU 3252  N   ALA A 215     3074   2598   3213    775    308   -266       N  
ATOM   3253  CA  ALA A 215      18.415  10.004 -27.222  1.00 25.03           C  
ANISOU 3253  CA  ALA A 215     3287   2771   3453    781    281   -216       C  
ATOM   3254  C   ALA A 215      17.826   8.607 -27.041  1.00 20.68           C  
ANISOU 3254  C   ALA A 215     2802   2121   2933    797    268   -226       C  
ATOM   3255  O   ALA A 215      17.021   8.134 -27.849  1.00 24.80           O  
ANISOU 3255  O   ALA A 215     3374   2600   3450    774    273   -263       O  
ATOM   3256  CB  ALA A 215      17.544  11.061 -26.551  1.00 20.63           C  
ANISOU 3256  CB  ALA A 215     2720   2237   2882    711    260   -175       C  
ATOM   3257  H   ALA A 215      18.160  10.992 -28.916  1.00 28.06           H  
ATOM   3258  HA  ALA A 215      19.279  10.038 -26.782  1.00 30.04           H  
ATOM   3259  HB1 ALA A 215      17.472  10.857 -25.605  1.00 24.76           H  
ATOM   3260  HB2 ALA A 215      17.955  11.931 -26.671  1.00 24.76           H  
ATOM   3261  HB3 ALA A 215      16.665  11.051 -26.960  1.00 24.76           H  
ATOM   3262  N   ASN A 216      18.240   7.941 -25.972  1.00 21.68           N  
ANISOU 3262  N   ASN A 216     2926   2219   3092    823    246   -192       N  
ATOM   3263  CA  ASN A 216      17.940   6.524 -25.773  1.00 21.22           C  
ANISOU 3263  CA  ASN A 216     2920   2074   3067    834    228   -198       C  
ATOM   3264  C   ASN A 216      17.553   6.343 -24.312  1.00 22.73           C  
ANISOU 3264  C   ASN A 216     3124   2233   3281    820    198   -138       C  
ATOM   3265  O   ASN A 216      18.410   6.368 -23.425  1.00 28.71           O  
ANISOU 3265  O   ASN A 216     3842   3015   4050    851    186   -103       O  
ATOM   3266  CB  ASN A 216      19.144   5.683 -26.168  1.00 25.16           C  
ANISOU 3266  CB  ASN A 216     3401   2573   3585    894    237   -227       C  
ATOM   3267  CG  ASN A 216      18.906   4.208 -26.035  1.00 30.38           C  
ANISOU 3267  CG  ASN A 216     4117   3142   4284    910    220   -236       C  
ATOM   3268  OD1 ASN A 216      17.828   3.756 -25.646  1.00 30.72           O  
ANISOU 3268  OD1 ASN A 216     4214   3121   4338    872    200   -220       O  
ATOM   3269  ND2 ASN A 216      19.925   3.438 -26.376  1.00 30.50           N  
ANISOU 3269  ND2 ASN A 216     4118   3152   4319    965    229   -261       N  
ATOM   3270  H   ASN A 216      18.703   8.291 -25.337  1.00 26.02           H  
ATOM   3271  HA  ASN A 216      17.182   6.248 -26.311  1.00 25.46           H  
ATOM   3272  HB2 ASN A 216      19.366   5.867 -27.094  1.00 30.19           H  
ATOM   3273  HB3 ASN A 216      19.892   5.917 -25.595  1.00 30.19           H  
ATOM   3274 HD21 ASN A 216      20.654   3.794 -26.662  1.00 36.60           H  
ATOM   3275  N   VAL A 217      16.256   6.186 -24.074  1.00 22.78           N  
ANISOU 3275  N   VAL A 217     3181   2188   3288    771    185   -126       N  
ATOM   3276  CA  VAL A 217      15.692   6.084 -22.735  1.00 23.76           C  
ANISOU 3276  CA  VAL A 217     3319   2284   3426    746    158    -68       C  
ATOM   3277  C   VAL A 217      15.303   4.632 -22.506  1.00 25.79           C  
ANISOU 3277  C   VAL A 217     3634   2452   3714    745    136    -67       C  
ATOM   3278  O   VAL A 217      14.568   4.050 -23.312  1.00 24.06           O  
ANISOU 3278  O   VAL A 217     3465   2183   3496    721    140   -104       O  
ATOM   3279  CB  VAL A 217      14.477   7.014 -22.572  1.00 23.57           C  
ANISOU 3279  CB  VAL A 217     3297   2282   3377    673    155    -52       C  
ATOM   3280  CG1 VAL A 217      13.950   6.930 -21.161  1.00 23.75           C  
ANISOU 3280  CG1 VAL A 217     3325   2288   3410    644    127      7       C  
ATOM   3281  CG2 VAL A 217      14.840   8.446 -22.938  1.00 22.65           C  
ANISOU 3281  CG2 VAL A 217     3119   2259   3229    659    170    -59       C  
ATOM   3282  H   VAL A 217      15.664   6.134 -24.696  1.00 27.34           H  
ATOM   3283  HA  VAL A 217      16.357   6.334 -22.075  1.00 28.51           H  
ATOM   3284  HB  VAL A 217      13.775   6.729 -23.178  1.00 28.29           H  
ATOM   3285 HG11 VAL A 217      13.248   7.590 -21.046  1.00 28.50           H  
ATOM   3286 HG12 VAL A 217      13.595   6.040 -21.008  1.00 28.50           H  
ATOM   3287 HG13 VAL A 217      14.675   7.108 -20.541  1.00 28.50           H  
ATOM   3288 HG21 VAL A 217      15.213   8.458 -23.834  1.00 27.18           H  
ATOM   3289 HG22 VAL A 217      14.039   8.993 -22.906  1.00 27.18           H  
ATOM   3290 HG23 VAL A 217      15.493   8.778 -22.303  1.00 27.18           H  
ATOM   3291  N   THR A 218      15.783   4.046 -21.413  1.00 26.50           N  
ANISOU 3291  N   THR A 218     3718   2520   3829    769    113    -24       N  
ATOM   3292  CA  THR A 218      15.565   2.628 -21.162  1.00 29.41           C  
ANISOU 3292  CA  THR A 218     4139   2803   4231    773     92    -20       C  
ATOM   3293  C   THR A 218      14.394   2.425 -20.206  1.00 26.81           C  
ANISOU 3293  C   THR A 218     3850   2431   3904    716     67     28       C  
ATOM   3294  O   THR A 218      14.348   3.014 -19.119  1.00 27.81           O  
ANISOU 3294  O   THR A 218     3952   2592   4023    703     56     80       O  
ATOM   3295  CB  THR A 218      16.826   1.952 -20.616  1.00 44.70           C  
ANISOU 3295  CB  THR A 218     6051   4736   6198    836     79     -3       C  
ATOM   3296  OG1 THR A 218      17.841   1.958 -21.628  1.00 51.06           O  
ANISOU 3296  OG1 THR A 218     6825   5574   7002    887    104    -53       O  
ATOM   3297  CG2 THR A 218      16.527   0.500 -20.227  1.00 39.02           C  
ANISOU 3297  CG2 THR A 218     5388   3922   5516    837     55     11       C  
ATOM   3298  H   THR A 218      16.236   4.451 -20.805  1.00 31.79           H  
ATOM   3299  HA  THR A 218      15.336   2.200 -22.002  1.00 35.29           H  
ATOM   3300  HB  THR A 218      17.137   2.429 -19.831  1.00 53.64           H  
ATOM   3301  HG1 THR A 218      17.796   2.667 -22.077  1.00 61.27           H  
ATOM   3302 HG21 THR A 218      16.390   0.435 -19.268  1.00 46.83           H  
ATOM   3303 HG22 THR A 218      15.726   0.193 -20.680  1.00 46.83           H  
ATOM   3304 HG23 THR A 218      17.270  -0.071 -20.479  1.00 46.83           H  
ATOM   3305  N   LEU A 219      13.446   1.601 -20.635  1.00 24.03           N  
ANISOU 3305  N   LEU A 219     3559   2009   3561    678     61     10       N  
ATOM   3306  CA  LEU A 219      12.315   1.203 -19.818  1.00 23.19           C  
ANISOU 3306  CA  LEU A 219     3497   1857   3459    618     38     53       C  
ATOM   3307  C   LEU A 219      12.542  -0.210 -19.302  1.00 32.91           C  
ANISOU 3307  C   LEU A 219     4764   3013   4729    634     15     74       C  
ATOM   3308  O   LEU A 219      13.064  -1.069 -20.019  1.00 32.73           O  
ANISOU 3308  O   LEU A 219     4758   2949   4729    672     20     36       O  
ATOM   3309  CB  LEU A 219      11.018   1.262 -20.619  1.00 27.82           C  
ANISOU 3309  CB  LEU A 219     4126   2419   4026    554     46     22       C  
ATOM   3310  CG  LEU A 219      10.664   2.609 -21.246  1.00 24.47           C  
ANISOU 3310  CG  LEU A 219     3672   2060   3564    534     70     -2       C  
ATOM   3311  CD1 LEU A 219       9.438   2.405 -22.125  1.00 26.69           C  
ANISOU 3311  CD1 LEU A 219     4002   2308   3830    472     73    -38       C  
ATOM   3312  CD2 LEU A 219      10.412   3.671 -20.206  1.00 20.81           C  
ANISOU 3312  CD2 LEU A 219     3162   1663   3083    504     64     48       C  
ATOM   3313  H   LEU A 219      13.441   1.250 -21.420  1.00 28.83           H  
ATOM   3314  HA  LEU A 219      12.225   1.803 -19.061  1.00 27.83           H  
ATOM   3315  HB2 LEU A 219      11.083   0.619 -21.343  1.00 33.39           H  
ATOM   3316  HB3 LEU A 219      10.288   1.022 -20.027  1.00 33.39           H  
ATOM   3317  HG  LEU A 219      11.408   2.933 -21.778  1.00 29.36           H  
ATOM   3318 HD11 LEU A 219       9.062   3.271 -22.348  1.00 32.02           H  
ATOM   3319 HD12 LEU A 219       9.704   1.941 -22.934  1.00 32.02           H  
ATOM   3320 HD13 LEU A 219       8.786   1.877 -21.639  1.00 32.02           H  
ATOM   3321 HD21 LEU A 219      10.842   4.495 -20.485  1.00 24.97           H  
ATOM   3322 HD22 LEU A 219       9.455   3.810 -20.122  1.00 24.97           H  
ATOM   3323 HD23 LEU A 219      10.780   3.377 -19.359  1.00 24.97           H  
ATOM   3324  N   THR A 220      12.168  -0.431 -18.047  1.00 25.78           N  
ANISOU 3324  N   THR A 220     3870   2093   3832    607    -10    137       N  
ATOM   3325  CA  THR A 220      12.178  -1.760 -17.452  1.00 26.22           C  
ANISOU 3325  CA  THR A 220     3965   2074   3923    609    -32    168       C  
ATOM   3326  C   THR A 220      10.852  -2.447 -17.742  1.00 33.87           C  
ANISOU 3326  C   THR A 220     4998   2980   4891    538    -37    162       C  
ATOM   3327  O   THR A 220       9.805  -1.952 -17.301  1.00 25.72           O  
ANISOU 3327  O   THR A 220     3974   1965   3834    472    -43    189       O  
ATOM   3328  CB  THR A 220      12.388  -1.658 -15.951  1.00 31.48           C  
ANISOU 3328  CB  THR A 220     4610   2758   4592    608    -56    242       C  
ATOM   3329  OG1 THR A 220      13.610  -0.956 -15.691  1.00 32.55           O  
ANISOU 3329  OG1 THR A 220     4684   2959   4723    668    -54    245       O  
ATOM   3330  CG2 THR A 220      12.438  -3.032 -15.307  1.00 36.15           C  
ANISOU 3330  CG2 THR A 220     5242   3273   5220    611    -77    280       C  
ATOM   3331  H   THR A 220      11.898   0.183 -17.509  1.00 30.94           H  
ATOM   3332  HA  THR A 220      12.893  -2.293 -17.832  1.00 31.46           H  
ATOM   3333  HB  THR A 220      11.645  -1.178 -15.554  1.00 37.77           H  
ATOM   3334  HG1 THR A 220      14.047  -0.866 -16.402  1.00 39.06           H  
ATOM   3335 HG21 THR A 220      12.627  -2.948 -14.359  1.00 43.38           H  
ATOM   3336 HG22 THR A 220      11.586  -3.483 -15.420  1.00 43.38           H  
ATOM   3337 HG23 THR A 220      13.134  -3.567 -15.720  1.00 43.38           H  
ATOM   3338  N   PRO A 221      10.839  -3.568 -18.460  1.00 27.21           N  
ANISOU 3338  N   PRO A 221     4199   2068   4073    546    -36    127       N  
ATOM   3339  CA  PRO A 221       9.562  -4.212 -18.790  1.00 32.90           C  
ANISOU 3339  CA  PRO A 221     4978   2732   4788    472    -42    117       C  
ATOM   3340  C   PRO A 221       8.667  -4.365 -17.569  1.00 28.31           C  
ANISOU 3340  C   PRO A 221     4416   2141   4201    407    -63    186       C  
ATOM   3341  O   PRO A 221       9.097  -4.830 -16.510  1.00 29.11           O  
ANISOU 3341  O   PRO A 221     4515   2226   4321    426    -78    241       O  
ATOM   3342  CB  PRO A 221       9.988  -5.573 -19.354  1.00 27.86           C  
ANISOU 3342  CB  PRO A 221     4383   2015   4187    506    -43     86       C  
ATOM   3343  CG  PRO A 221      11.355  -5.321 -19.923  1.00 30.49           C  
ANISOU 3343  CG  PRO A 221     4674   2379   4532    594    -26     48       C  
ATOM   3344  CD  PRO A 221      11.994  -4.305 -19.014  1.00 26.46           C  
ANISOU 3344  CD  PRO A 221     4100   1942   4009    622    -29     92       C  
ATOM   3345  HA  PRO A 221       9.094  -3.703 -19.470  1.00 39.47           H  
ATOM   3346  HB2 PRO A 221      10.020  -6.233 -18.644  1.00 33.43           H  
ATOM   3347  HB3 PRO A 221       9.368  -5.857 -20.044  1.00 33.43           H  
ATOM   3348  HG2 PRO A 221      11.865  -6.146 -19.929  1.00 36.59           H  
ATOM   3349  HG3 PRO A 221      11.276  -4.973 -20.825  1.00 36.59           H  
ATOM   3350  HD2 PRO A 221      12.496  -4.742 -18.308  1.00 31.75           H  
ATOM   3351  HD3 PRO A 221      12.575  -3.711 -19.515  1.00 31.75           H  
ATOM   3352  N   GLY A 222       7.408  -3.962 -17.728  1.00 30.26           N  
ANISOU 3352  N   GLY A 222     4679   2402   4416    328    -64    184       N  
ATOM   3353  CA  GLY A 222       6.396  -4.165 -16.721  1.00 31.47           C  
ANISOU 3353  CA  GLY A 222     4852   2549   4558    254    -82    242       C  
ATOM   3354  C   GLY A 222       6.292  -3.077 -15.681  1.00 35.14           C  
ANISOU 3354  C   GLY A 222     5272   3084   4996    240    -86    292       C  
ATOM   3355  O   GLY A 222       5.312  -3.056 -14.925  1.00 41.95           O  
ANISOU 3355  O   GLY A 222     6144   3957   5838    169    -99    335       O  
ATOM   3356  H   GLY A 222       7.119  -3.560 -18.431  1.00 36.31           H  
ATOM   3357  HA2 GLY A 222       5.534  -4.235 -17.160  1.00 37.77           H  
ATOM   3358  HA3 GLY A 222       6.583  -4.997 -16.259  1.00 37.77           H  
ATOM   3359  N   ARG A 223       7.257  -2.172 -15.620  1.00 27.32           N  
ANISOU 3359  N   ARG A 223     4232   2147   4002    302    -76    287       N  
ATOM   3360  CA  ARG A 223       7.347  -1.199 -14.546  1.00 24.77           C  
ANISOU 3360  CA  ARG A 223     3865   1889   3657    299    -81    337       C  
ATOM   3361  C   ARG A 223       6.752   0.138 -14.965  1.00 27.27           C  
ANISOU 3361  C   ARG A 223     4156   2268   3935    269    -66    314       C  
ATOM   3362  O   ARG A 223       6.527   0.407 -16.148  1.00 25.04           O  
ANISOU 3362  O   ARG A 223     3879   1989   3646    266    -49    256       O  
ATOM   3363  CB  ARG A 223       8.806  -1.019 -14.121  1.00 26.75           C  
ANISOU 3363  CB  ARG A 223     4073   2165   3926    384    -81    351       C  
ATOM   3364  CG  ARG A 223       9.422  -2.290 -13.532  1.00 33.32           C  
ANISOU 3364  CG  ARG A 223     4926   2938   4795    416    -97    384       C  
ATOM   3365  CD  ARG A 223       8.643  -2.751 -12.301  1.00 47.39           C  
ANISOU 3365  CD  ARG A 223     6733   4706   6567    356   -114    453       C  
ATOM   3366  NE  ARG A 223       9.225  -3.934 -11.673  1.00 57.83           N  
ANISOU 3366  NE  ARG A 223     8079   5974   7921    388   -126    491       N  
ATOM   3367  CZ  ARG A 223      10.217  -3.901 -10.788  1.00115.18           C  
ANISOU 3367  CZ  ARG A 223    15309  13259  15194    440   -134    534       C  
ATOM   3368  NH1 ARG A 223      10.754  -2.743 -10.426  1.00113.18           N  
ANISOU 3368  NH1 ARG A 223    14996  13084  14923    464   -134    542       N  
ATOM   3369  NH2 ARG A 223      10.677  -5.031 -10.269  1.00121.96           N  
ANISOU 3369  NH2 ARG A 223    16194  14064  16082    467   -145    568       N  
ATOM   3370  H   ARG A 223       7.884  -2.102 -16.204  1.00 32.79           H  
ATOM   3371  HA  ARG A 223       6.838  -1.517 -13.784  1.00 29.72           H  
ATOM   3372  HB2 ARG A 223       9.330  -0.765 -14.897  1.00 32.10           H  
ATOM   3373  HB3 ARG A 223       8.854  -0.324 -13.447  1.00 32.10           H  
ATOM   3374  HG2 ARG A 223       9.399  -2.998 -14.194  1.00 39.98           H  
ATOM   3375  HG3 ARG A 223      10.338  -2.113 -13.267  1.00 39.98           H  
ATOM   3376  HD2 ARG A 223       8.636  -2.037 -11.645  1.00 56.87           H  
ATOM   3377  HD3 ARG A 223       7.735  -2.968 -12.565  1.00 56.87           H  
ATOM   3378  HE  ARG A 223       8.904  -4.703 -11.888  1.00 69.40           H  
ATOM   3379 HH11 ARG A 223      10.461  -2.009 -10.764  1.00135.81           H  
ATOM   3380 HH12 ARG A 223      11.396  -2.727  -9.854  1.00135.81           H  
ATOM   3381 HH21 ARG A 223      10.333  -5.783 -10.504  1.00146.35           H  
ATOM   3382 HH22 ARG A 223      11.319  -5.012  -9.697  1.00146.35           H  
ATOM   3383  N   ARG A 224       6.500   0.972 -13.961  1.00 22.04           N  
ANISOU 3383  N   ARG A 224     3446   1679   3249    242    -70    356       N  
ATOM   3384  CA  ARG A 224       5.974   2.315 -14.140  1.00 22.68           C  
ANISOU 3384  CA  ARG A 224     3466   1857   3295    208    -53    336       C  
ATOM   3385  C   ARG A 224       7.102   3.323 -13.983  1.00 24.75           C  
ANISOU 3385  C   ARG A 224     3666   2186   3553    271    -40    332       C  
ATOM   3386  O   ARG A 224       7.827   3.293 -12.981  1.00 20.28           O  
ANISOU 3386  O   ARG A 224     3083   1630   2993    303    -51    376       O  
ATOM   3387  CB  ARG A 224       4.893   2.616 -13.105  1.00 20.92           C  
ANISOU 3387  CB  ARG A 224     3225   1679   3044    134    -65    382       C  
ATOM   3388  CG  ARG A 224       3.603   1.863 -13.275  1.00 34.49           C  
ANISOU 3388  CG  ARG A 224     4991   3356   4758     56    -76    385       C  
ATOM   3389  CD  ARG A 224       2.436   2.826 -13.116  1.00 89.29           C  
ANISOU 3389  CD  ARG A 224    11885  10382  11660    -10    -69    383       C  
ATOM   3390  NE  ARG A 224       1.359   2.268 -12.304  1.00108.38           N  
ANISOU 3390  NE  ARG A 224    14322  12794  14063    -86    -86    428       N  
ATOM   3391  CZ  ARG A 224       0.587   2.985 -11.492  1.00112.67           C  
ANISOU 3391  CZ  ARG A 224    14820  13418  14574   -134    -85    454       C  
ATOM   3392  NH1 ARG A 224       0.779   4.291 -11.373  1.00 39.50           N  
ANISOU 3392  NH1 ARG A 224     5488   4234   5286   -110    -70    439       N  
ATOM   3393  NH2 ARG A 224      -0.368   2.396 -10.789  1.00 97.68           N  
ANISOU 3393  NH2 ARG A 224    12939  11515  12661   -205   -100    494       N  
ATOM   3394  H   ARG A 224       6.631   0.770 -13.135  1.00 26.45           H  
ATOM   3395  HA  ARG A 224       5.595   2.392 -15.029  1.00 27.22           H  
ATOM   3396  HB2 ARG A 224       5.242   2.396 -12.227  1.00 25.10           H  
ATOM   3397  HB3 ARG A 224       4.683   3.562 -13.151  1.00 25.10           H  
ATOM   3398  HG2 ARG A 224       3.566   1.467 -14.159  1.00 41.39           H  
ATOM   3399  HG3 ARG A 224       3.534   1.171 -12.599  1.00 41.39           H  
ATOM   3400  HD2 ARG A 224       2.749   3.637 -12.685  1.00107.15           H  
ATOM   3401  HD3 ARG A 224       2.075   3.035 -13.992  1.00107.15           H  
ATOM   3402  HE  ARG A 224       1.215   1.421 -12.354  1.00130.05           H  
ATOM   3403 HH11 ARG A 224       1.403   4.677 -11.821  1.00 47.40           H  
ATOM   3404 HH12 ARG A 224       0.279   4.753 -10.847  1.00 47.40           H  
ATOM   3405 HH21 ARG A 224      -0.491   1.548 -10.857  1.00117.22           H  
ATOM   3406 HH22 ARG A 224      -0.866   2.862 -10.264  1.00117.22           H  
ATOM   3407  N   HIS A 225       7.219   4.239 -14.940  1.00 18.72           N  
ANISOU 3407  N   HIS A 225     2868   1470   2776    282    -18    283       N  
ATOM   3408  CA  HIS A 225       8.350   5.152 -14.985  1.00 19.51           C  
ANISOU 3408  CA  HIS A 225     2914   1628   2872    339     -5    273       C  
ATOM   3409  C   HIS A 225       7.868   6.590 -15.022  1.00 21.77           C  
ANISOU 3409  C   HIS A 225     3145   2002   3125    305      6    262       C  
ATOM   3410  O   HIS A 225       7.014   6.935 -15.844  1.00 20.47           O  
ANISOU 3410  O   HIS A 225     2983   1849   2945    266     15    228       O  
ATOM   3411  CB  HIS A 225       9.219   4.903 -16.219  1.00 17.81           C  
ANISOU 3411  CB  HIS A 225     2708   1384   2673    398     12    222       C  
ATOM   3412  CG  HIS A 225       9.631   3.480 -16.396  1.00 18.45           C  
ANISOU 3412  CG  HIS A 225     2851   1371   2790    436      3    220       C  
ATOM   3413  ND1 HIS A 225       8.767   2.502 -16.839  1.00 25.68           N  
ANISOU 3413  ND1 HIS A 225     3830   2212   3714    398     -5    207       N  
ATOM   3414  CD2 HIS A 225      10.825   2.875 -16.209  1.00 30.25           C  
ANISOU 3414  CD2 HIS A 225     4352   2832   4311    511      0    229       C  
ATOM   3415  CE1 HIS A 225       9.410   1.351 -16.907  1.00 28.49           C  
ANISOU 3415  CE1 HIS A 225     4225   2496   4103    444    -14    205       C  
ATOM   3416  NE2 HIS A 225      10.659   1.551 -16.530  1.00 27.99           N  
ANISOU 3416  NE2 HIS A 225     4118   2466   4051    509    -14    216       N  
ATOM   3417  H   HIS A 225       6.650   4.348 -15.576  1.00 22.46           H  
ATOM   3418  HA  HIS A 225       8.874   5.018 -14.180  1.00 23.41           H  
ATOM   3419  HB2 HIS A 225       8.720   5.166 -17.008  1.00 21.37           H  
ATOM   3420  HB3 HIS A 225      10.026   5.436 -16.143  1.00 21.37           H  
ATOM   3421  HD1 HIS A 225       7.939   2.623 -17.039  1.00 30.81           H  
ATOM   3422  HD2 HIS A 225      11.610   3.279 -15.918  1.00 36.30           H  
ATOM   3423  HE1 HIS A 225       9.045   0.539 -17.176  1.00 34.19           H  
ATOM   3424  N   ARG A 226       8.442   7.428 -14.157  1.00 19.59           N  
ANISOU 3424  N   ARG A 226     2820   1787   2838    322      5    289       N  
ATOM   3425  CA  ARG A 226       8.225   8.867 -14.224  1.00 15.54           C  
ANISOU 3425  CA  ARG A 226     2255   1354   2295    303     16    274       C  
ATOM   3426  C   ARG A 226       9.190   9.488 -15.225  1.00 20.27           C  
ANISOU 3426  C   ARG A 226     2829   1978   2896    349     34    234       C  
ATOM   3427  O   ARG A 226      10.392   9.202 -15.210  1.00 18.68           O  
ANISOU 3427  O   ARG A 226     2620   1767   2712    405     36    237       O  
ATOM   3428  CB  ARG A 226       8.418   9.501 -12.847  1.00 16.74           C  
ANISOU 3428  CB  ARG A 226     2370   1560   2432    297      5    318       C  
ATOM   3429  CG  ARG A 226       8.210  11.009 -12.812  1.00 16.59           C  
ANISOU 3429  CG  ARG A 226     2301   1619   2384    278     14    304       C  
ATOM   3430  CD  ARG A 226       8.382  11.529 -11.401  1.00 17.70           C  
ANISOU 3430  CD  ARG A 226     2409   1807   2507    271      2    345       C  
ATOM   3431  NE  ARG A 226       7.923  12.902 -11.251  1.00 16.62           N  
ANISOU 3431  NE  ARG A 226     2235   1737   2342    245      8    331       N  
ATOM   3432  CZ  ARG A 226       7.520  13.429 -10.101  1.00 18.81           C  
ANISOU 3432  CZ  ARG A 226     2491   2060   2598    219      0    358       C  
ATOM   3433  NH1 ARG A 226       7.504  12.689  -8.997  1.00 18.17           N  
ANISOU 3433  NH1 ARG A 226     2421   1968   2517    210    -15    402       N  
ATOM   3434  NH2 ARG A 226       7.122  14.691 -10.060  1.00 15.32           N  
ANISOU 3434  NH2 ARG A 226     2017   1672   2131    201      5    339       N  
ATOM   3435  H   ARG A 226       8.965   7.183 -13.520  1.00 23.51           H  
ATOM   3436  HA  ARG A 226       7.316   9.043 -14.515  1.00 18.64           H  
ATOM   3437  HB2 ARG A 226       7.783   9.102 -12.232  1.00 20.09           H  
ATOM   3438  HB3 ARG A 226       9.325   9.323 -12.550  1.00 20.09           H  
ATOM   3439  HG2 ARG A 226       8.863  11.442 -13.384  1.00 19.91           H  
ATOM   3440  HG3 ARG A 226       7.312  11.222 -13.113  1.00 19.91           H  
ATOM   3441  HD2 ARG A 226       7.870  10.973 -10.793  1.00 21.23           H  
ATOM   3442  HD3 ARG A 226       9.323  11.499 -11.164  1.00 21.23           H  
ATOM   3443  HE  ARG A 226       7.913  13.403 -11.950  1.00 19.94           H  
ATOM   3444 HH11 ARG A 226       7.755  11.867  -9.026  1.00 21.81           H  
ATOM   3445 HH12 ARG A 226       7.242  13.032  -8.253  1.00 21.81           H  
ATOM   3446 HH21 ARG A 226       7.125  15.166 -10.777  1.00 18.38           H  
ATOM   3447 HH22 ARG A 226       6.860  15.036  -9.317  1.00 18.38           H  
ATOM   3448  N   LEU A 227       8.658  10.336 -16.100  1.00 16.88           N  
ANISOU 3448  N   LEU A 227     2385   1581   2448    324     47    198       N  
ATOM   3449  CA  LEU A 227       9.437  11.060 -17.095  1.00 18.56           C  
ANISOU 3449  CA  LEU A 227     2572   1826   2655    355     64    161       C  
ATOM   3450  C   LEU A 227       9.127  12.541 -16.939  1.00 17.72           C  
ANISOU 3450  C   LEU A 227     2422   1790   2521    328     67    160       C  
ATOM   3451  O   LEU A 227       7.955  12.933 -16.932  1.00 16.81           O  
ANISOU 3451  O   LEU A 227     2309   1689   2390    281     63    157       O  
ATOM   3452  CB  LEU A 227       9.100  10.580 -18.504  1.00 16.50           C  
ANISOU 3452  CB  LEU A 227     2343   1528   2397    352     77    114       C  
ATOM   3453  CG  LEU A 227       9.857  11.225 -19.667  1.00 15.71           C  
ANISOU 3453  CG  LEU A 227     2221   1459   2288    381     97     74       C  
ATOM   3454  CD1 LEU A 227      11.310  10.763 -19.684  1.00 17.48           C  
ANISOU 3454  CD1 LEU A 227     2436   1674   2530    448    105     73       C  
ATOM   3455  CD2 LEU A 227       9.136  10.912 -20.982  1.00 19.18           C  
ANISOU 3455  CD2 LEU A 227     2694   1874   2721    358    106     30       C  
ATOM   3456  H   LEU A 227       7.817  10.512 -16.137  1.00 20.26           H  
ATOM   3457  HA  LEU A 227      10.387  10.924 -16.955  1.00 22.27           H  
ATOM   3458  HB2 LEU A 227       9.281   9.628 -18.544  1.00 19.80           H  
ATOM   3459  HB3 LEU A 227       8.157  10.745 -18.657  1.00 19.80           H  
ATOM   3460  HG  LEU A 227       9.874  12.189 -19.562  1.00 18.85           H  
ATOM   3461 HD11 LEU A 227      11.632  10.767 -20.599  1.00 20.97           H  
ATOM   3462 HD12 LEU A 227      11.841  11.370 -19.145  1.00 20.97           H  
ATOM   3463 HD13 LEU A 227      11.361   9.866 -19.319  1.00 20.97           H  
ATOM   3464 HD21 LEU A 227       9.664  11.254 -21.721  1.00 23.02           H  
ATOM   3465 HD22 LEU A 227       9.035   9.951 -21.066  1.00 23.02           H  
ATOM   3466 HD23 LEU A 227       8.265  11.337 -20.973  1.00 23.02           H  
ATOM   3467  N   ARG A 228      10.171  13.354 -16.809  1.00 15.97           N  
ANISOU 3467  N   ARG A 228     2161   1614   2293    358     72    162       N  
ATOM   3468  CA  ARG A 228      10.044  14.771 -16.473  1.00 14.03           C  
ANISOU 3468  CA  ARG A 228     1877   1431   2024    336     71    166       C  
ATOM   3469  C   ARG A 228      10.294  15.600 -17.731  1.00 16.56           C  
ANISOU 3469  C   ARG A 228     2183   1777   2331    339     86    128       C  
ATOM   3470  O   ARG A 228      11.417  16.026 -18.005  1.00 15.91           O  
ANISOU 3470  O   ARG A 228     2075   1722   2247    369     95    122       O  
ATOM   3471  CB  ARG A 228      11.004  15.131 -15.355  1.00 14.68           C  
ANISOU 3471  CB  ARG A 228     1926   1546   2104    359     63    199       C  
ATOM   3472  CG  ARG A 228      10.732  14.374 -14.060  1.00 17.43           C  
ANISOU 3472  CG  ARG A 228     2287   1874   2460    352     47    240       C  
ATOM   3473  CD  ARG A 228      11.799  14.684 -13.047  1.00 16.47           C  
ANISOU 3473  CD  ARG A 228     2133   1789   2337    378     38    272       C  
ATOM   3474  NE  ARG A 228      11.584  14.015 -11.769  1.00 15.51           N  
ANISOU 3474  NE  ARG A 228     2022   1654   2218    370     21    315       N  
ATOM   3475  CZ  ARG A 228      10.960  14.559 -10.726  1.00 19.41           C  
ANISOU 3475  CZ  ARG A 228     2503   2182   2691    335     11    338       C  
ATOM   3476  NH1 ARG A 228      10.457  15.782 -10.796  1.00 16.01           N  
ANISOU 3476  NH1 ARG A 228     2051   1797   2237    306     16    319       N  
ATOM   3477  NH2 ARG A 228      10.830  13.864  -9.607  1.00 17.90           N  
ANISOU 3477  NH2 ARG A 228     2322   1980   2501    328     -5    380       N  
ATOM   3478  H   ARG A 228      10.986  13.099 -16.913  1.00 19.16           H  
ATOM   3479  HA  ARG A 228       9.136  14.952 -16.184  1.00 16.84           H  
ATOM   3480  HB2 ARG A 228      11.908  14.922 -15.638  1.00 17.61           H  
ATOM   3481  HB3 ARG A 228      10.926  16.080 -15.168  1.00 17.61           H  
ATOM   3482  HG2 ARG A 228       9.873  14.643 -13.699  1.00 20.91           H  
ATOM   3483  HG3 ARG A 228      10.735  13.419 -14.233  1.00 20.91           H  
ATOM   3484  HD2 ARG A 228      12.657  14.394 -13.395  1.00 19.77           H  
ATOM   3485  HD3 ARG A 228      11.812  15.640 -12.886  1.00 19.77           H  
ATOM   3486  HE  ARG A 228      11.882  13.213 -11.683  1.00 18.61           H  
ATOM   3487 HH11 ARG A 228      10.531  16.236 -11.522  1.00 19.22           H  
ATOM   3488 HH12 ARG A 228      10.056  16.122 -10.115  1.00 19.22           H  
ATOM   3489 HH21 ARG A 228      11.147  13.066  -9.557  1.00 21.48           H  
ATOM   3490 HH22 ARG A 228      10.428  14.210  -8.930  1.00 21.48           H  
ATOM   3491  N   LEU A 229       9.221  15.849 -18.480  1.00 15.23           N  
ANISOU 3491  N   LEU A 229     2030   1605   2151    304     88    105       N  
ATOM   3492  CA  LEU A 229       9.301  16.584 -19.734  1.00 13.34           C  
ANISOU 3492  CA  LEU A 229     1782   1388   1897    301    100     71       C  
ATOM   3493  C   LEU A 229       9.422  18.087 -19.510  1.00 13.17           C  
ANISOU 3493  C   LEU A 229     1726   1421   1855    288     97     77       C  
ATOM   3494  O   LEU A 229       8.703  18.666 -18.694  1.00 14.16           O  
ANISOU 3494  O   LEU A 229     1843   1565   1972    264     86     93       O  
ATOM   3495  CB  LEU A 229       8.054  16.302 -20.572  1.00 15.20           C  
ANISOU 3495  CB  LEU A 229     2047   1602   2127    267    100     48       C  
ATOM   3496  CG  LEU A 229       7.885  14.872 -21.066  1.00 16.18           C  
ANISOU 3496  CG  LEU A 229     2212   1667   2267    273    104     33       C  
ATOM   3497  CD1 LEU A 229       6.498  14.653 -21.595  1.00 14.64           C  
ANISOU 3497  CD1 LEU A 229     2041   1457   2063    228     98     18       C  
ATOM   3498  CD2 LEU A 229       8.904  14.589 -22.150  1.00 18.50           C  
ANISOU 3498  CD2 LEU A 229     2509   1953   2565    311    122      2       C  
ATOM   3499  H   LEU A 229       8.424  15.598 -18.279  1.00 18.27           H  
ATOM   3500  HA  LEU A 229      10.094  16.295 -20.212  1.00 16.00           H  
ATOM   3501  HB2 LEU A 229       7.275  16.513 -20.034  1.00 18.24           H  
ATOM   3502  HB3 LEU A 229       8.081  16.874 -21.355  1.00 18.24           H  
ATOM   3503  HG  LEU A 229       8.024  14.258 -20.328  1.00 19.41           H  
ATOM   3504 HD11 LEU A 229       6.329  13.699 -21.653  1.00 17.56           H  
ATOM   3505 HD12 LEU A 229       5.860  15.065 -20.991  1.00 17.56           H  
ATOM   3506 HD13 LEU A 229       6.428  15.055 -22.475  1.00 17.56           H  
ATOM   3507 HD21 LEU A 229       8.806  13.670 -22.443  1.00 22.19           H  
ATOM   3508 HD22 LEU A 229       8.749  15.192 -22.894  1.00 22.19           H  
ATOM   3509 HD23 LEU A 229       9.794  14.729 -21.791  1.00 22.19           H  
ATOM   3510  N   ILE A 230      10.315  18.723 -20.274  1.00 13.36           N  
ANISOU 3510  N   ILE A 230     1732   1473   1872    304    108     61       N  
ATOM   3511  CA  ILE A 230      10.518  20.168 -20.227  1.00 12.45           C  
ANISOU 3511  CA  ILE A 230     1589   1404   1736    290    105     64       C  
ATOM   3512  C   ILE A 230      10.699  20.655 -21.656  1.00 14.09           C  
ANISOU 3512  C   ILE A 230     1798   1626   1931    286    117     35       C  
ATOM   3513  O   ILE A 230      11.521  20.099 -22.390  1.00 15.26           O  
ANISOU 3513  O   ILE A 230     1945   1770   2082    311    132     20       O  
ATOM   3514  CB  ILE A 230      11.772  20.571 -19.420  1.00 12.63           C  
ANISOU 3514  CB  ILE A 230     1580   1457   1760    312    103     85       C  
ATOM   3515  CG1 ILE A 230      11.827  19.861 -18.070  1.00 14.99           C  
ANISOU 3515  CG1 ILE A 230     1879   1742   2074    323     93    115       C  
ATOM   3516  CG2 ILE A 230      11.844  22.098 -19.263  1.00 14.15           C  
ANISOU 3516  CG2 ILE A 230     1752   1693   1933    289     96     89       C  
ATOM   3517  CD1 ILE A 230      13.195  19.947 -17.398  1.00 17.11           C  
ANISOU 3517  CD1 ILE A 230     2118   2039   2346    352     92    136       C  
ATOM   3518  H   ILE A 230      10.825  18.324 -20.840  1.00 16.04           H  
ATOM   3519  HA  ILE A 230       9.736  20.573 -19.821  1.00 14.93           H  
ATOM   3520  HB  ILE A 230      12.551  20.281 -19.920  1.00 15.15           H  
ATOM   3521 HG12 ILE A 230      11.178  20.268 -17.475  1.00 17.99           H  
ATOM   3522 HG13 ILE A 230      11.617  18.923 -18.199  1.00 17.99           H  
ATOM   3523 HG21 ILE A 230      12.657  22.328 -18.786  1.00 16.98           H  
ATOM   3524 HG22 ILE A 230      11.850  22.506 -20.143  1.00 16.98           H  
ATOM   3525 HG23 ILE A 230      11.071  22.401 -18.762  1.00 16.98           H  
ATOM   3526 HD11 ILE A 230      13.224  19.318 -16.659  1.00 20.54           H  
ATOM   3527 HD12 ILE A 230      13.880  19.725 -18.048  1.00 20.54           H  
ATOM   3528 HD13 ILE A 230      13.330  20.849 -17.070  1.00 20.54           H  
ATOM   3529  N   ASN A 231       9.974  21.703 -22.046  1.00 13.19           N  
ANISOU 3529  N   ASN A 231     1682   1530   1798    256    110     29       N  
ATOM   3530  CA  ASN A 231      10.259  22.386 -23.311  1.00 13.40           C  
ANISOU 3530  CA  ASN A 231     1706   1579   1807    248    118      9       C  
ATOM   3531  C   ASN A 231      11.166  23.579 -23.015  1.00 12.84           C  
ANISOU 3531  C   ASN A 231     1607   1547   1724    246    115     24       C  
ATOM   3532  O   ASN A 231      10.720  24.605 -22.494  1.00 13.41           O  
ANISOU 3532  O   ASN A 231     1674   1632   1789    226    100     35       O  
ATOM   3533  CB  ASN A 231       8.972  22.814 -24.006  1.00 10.85           C  
ANISOU 3533  CB  ASN A 231     1400   1251   1470    218    110     -4       C  
ATOM   3534  CG  ASN A 231       9.239  23.428 -25.358  1.00 15.99           C  
ANISOU 3534  CG  ASN A 231     2051   1923   2100    208    117    -21       C  
ATOM   3535  OD1 ASN A 231      10.389  23.706 -25.691  1.00 13.71           O  
ANISOU 3535  OD1 ASN A 231     1746   1657   1805    220    128    -22       O  
ATOM   3536  ND2 ASN A 231       8.199  23.625 -26.153  1.00 14.74           N  
ANISOU 3536  ND2 ASN A 231     1910   1761   1930    186    111    -34       N  
ATOM   3537  H   ASN A 231       9.317  22.035 -21.600  1.00 15.82           H  
ATOM   3538  HA  ASN A 231      10.732  21.779 -23.902  1.00 16.08           H  
ATOM   3539  HB2 ASN A 231       8.404  22.038 -24.132  1.00 13.02           H  
ATOM   3540  HB3 ASN A 231       8.517  23.472 -23.458  1.00 13.02           H  
ATOM   3541 HD21 ASN A 231       8.312  23.973 -26.931  1.00 17.69           H  
ATOM   3542 HD22 ASN A 231       7.410  23.406 -25.890  1.00 17.69           H  
ATOM   3543  N   THR A 232      12.459  23.427 -23.305  1.00 13.28           N  
ANISOU 3543  N   THR A 232     1643   1622   1779    268    128     22       N  
ATOM   3544  CA  THR A 232      13.448  24.466 -23.054  1.00 14.35           C  
ANISOU 3544  CA  THR A 232     1751   1799   1903    262    126     36       C  
ATOM   3545  C   THR A 232      13.738  25.307 -24.298  1.00 13.74           C  
ANISOU 3545  C   THR A 232     1670   1749   1802    242    133     24       C  
ATOM   3546  O   THR A 232      14.755  26.009 -24.339  1.00 14.84           O  
ANISOU 3546  O   THR A 232     1784   1924   1929    237    135     33       O  
ATOM   3547  CB  THR A 232      14.756  23.856 -22.540  1.00 16.07           C  
ANISOU 3547  CB  THR A 232     1943   2033   2132    296    135     46       C  
ATOM   3548  OG1 THR A 232      15.272  22.941 -23.512  1.00 16.28           O  
ANISOU 3548  OG1 THR A 232     1970   2055   2161    322    156     25       O  
ATOM   3549  CG2 THR A 232      14.564  23.087 -21.242  1.00 15.80           C  
ANISOU 3549  CG2 THR A 232     1910   1974   2118    314    126     65       C  
ATOM   3550  H   THR A 232      12.789  22.714 -23.655  1.00 15.93           H  
ATOM   3551  HA  THR A 232      13.094  25.049 -22.364  1.00 17.22           H  
ATOM   3552  HB  THR A 232      15.376  24.584 -22.376  1.00 19.29           H  
ATOM   3553  HG1 THR A 232      16.078  23.117 -23.673  1.00 19.54           H  
ATOM   3554 HG21 THR A 232      13.790  22.506 -21.312  1.00 18.96           H  
ATOM   3555 HG22 THR A 232      15.348  22.546 -21.058  1.00 18.96           H  
ATOM   3556 HG23 THR A 232      14.429  23.705 -20.507  1.00 18.96           H  
ATOM   3557  N   SER A 233      12.861  25.251 -25.304  1.00 12.96           N  
ANISOU 3557  N   SER A 233     1595   1635   1694    228    135      5       N  
ATOM   3558  CA  SER A 233      13.056  25.958 -26.561  1.00 12.74           C  
ANISOU 3558  CA  SER A 233     1568   1632   1642    208    141     -6       C  
ATOM   3559  C   SER A 233      13.037  27.474 -26.388  1.00 11.78           C  
ANISOU 3559  C   SER A 233     1440   1530   1504    177    123     13       C  
ATOM   3560  O   SER A 233      12.533  28.014 -25.399  1.00 13.73           O  
ANISOU 3560  O   SER A 233     1691   1766   1759    170    105     27       O  
ATOM   3561  CB  SER A 233      11.938  25.621 -27.553  1.00 14.14           C  
ANISOU 3561  CB  SER A 233     1773   1788   1810    196    141    -27       C  
ATOM   3562  OG  SER A 233      11.967  24.277 -27.968  1.00 15.37           O  
ANISOU 3562  OG  SER A 233     1940   1924   1976    218    157    -49       O  
ATOM   3563  H   SER A 233      12.130  24.800 -25.280  1.00 15.55           H  
ATOM   3564  HA  SER A 233      13.921  25.683 -26.903  1.00 15.29           H  
ATOM   3565  HB2 SER A 233      11.085  25.793 -27.127  1.00 16.96           H  
ATOM   3566  HB3 SER A 233      12.039  26.186 -28.335  1.00 16.96           H  
ATOM   3567  HG  SER A 233      11.932  23.769 -27.300  1.00 18.44           H  
ATOM   3568  N   VAL A 234      13.533  28.159 -27.425  1.00 13.10           N  
ANISOU 3568  N   VAL A 234     1604   1727   1648    157    128     10       N  
ATOM   3569  CA  VAL A 234      13.272  29.581 -27.580  1.00 15.18           C  
ANISOU 3569  CA  VAL A 234     1875   1999   1895    123    109     25       C  
ATOM   3570  C   VAL A 234      11.975  29.896 -28.334  1.00 12.11           C  
ANISOU 3570  C   VAL A 234     1515   1590   1497    107     96     18       C  
ATOM   3571  O   VAL A 234      11.439  31.002 -28.172  1.00 14.77           O  
ANISOU 3571  O   VAL A 234     1864   1919   1828     87     75     31       O  
ATOM   3572  CB  VAL A 234      14.433  30.306 -28.291  1.00 13.95           C  
ANISOU 3572  CB  VAL A 234     1701   1885   1714    102    117     34       C  
ATOM   3573  CG1 VAL A 234      15.632  30.443 -27.360  1.00 18.85           C  
ANISOU 3573  CG1 VAL A 234     2290   2531   2340    108    120     49       C  
ATOM   3574  CG2 VAL A 234      14.846  29.595 -29.598  1.00 16.34           C  
ANISOU 3574  CG2 VAL A 234     1998   2210   1999    108    142     13       C  
ATOM   3575  H   VAL A 234      14.020  27.820 -28.047  1.00 15.73           H  
ATOM   3576  HA  VAL A 234      13.189  29.933 -26.679  1.00 18.22           H  
ATOM   3577  HB  VAL A 234      14.121  31.193 -28.532  1.00 16.74           H  
ATOM   3578 HG11 VAL A 234      16.324  30.953 -27.810  1.00 22.62           H  
ATOM   3579 HG12 VAL A 234      15.354  30.903 -26.553  1.00 22.62           H  
ATOM   3580 HG13 VAL A 234      15.963  29.558 -27.139  1.00 22.62           H  
ATOM   3581 HG21 VAL A 234      15.301  30.231 -30.173  1.00 19.61           H  
ATOM   3582 HG22 VAL A 234      15.441  28.860 -29.383  1.00 19.61           H  
ATOM   3583 HG23 VAL A 234      14.051  29.260 -30.040  1.00 19.61           H  
ATOM   3584  N   GLU A 235      11.440  28.960 -29.136  1.00 13.35           N  
ANISOU 3584  N   GLU A 235     1683   1736   1651    115    108     -4       N  
ATOM   3585  CA  GLU A 235      10.216  29.245 -29.886  1.00 12.03           C  
ANISOU 3585  CA  GLU A 235     1540   1556   1473     98     95    -10       C  
ATOM   3586  C   GLU A 235       9.329  28.035 -30.188  1.00 11.41           C  
ANISOU 3586  C   GLU A 235     1476   1455   1403    109    101    -32       C  
ATOM   3587  O   GLU A 235       8.097  28.159 -30.190  1.00 14.17           O  
ANISOU 3587  O   GLU A 235     1841   1790   1755    100     85    -33       O  
ATOM   3588  CB  GLU A 235      10.551  29.934 -31.224  1.00 15.01           C  
ANISOU 3588  CB  GLU A 235     1922   1962   1819     72     96     -9       C  
ATOM   3589  CG  GLU A 235       9.308  30.408 -31.973  1.00 13.04           C  
ANISOU 3589  CG  GLU A 235     1695   1703   1556     54     77     -9       C  
ATOM   3590  CD  GLU A 235       8.727  29.373 -32.926  1.00 16.40           C  
ANISOU 3590  CD  GLU A 235     2133   2127   1972     56     89    -36       C  
ATOM   3591  OE1 GLU A 235       9.387  28.335 -33.148  1.00 15.12           O  
ANISOU 3591  OE1 GLU A 235     1964   1970   1812     71    114    -56       O  
ATOM   3592  OE2 GLU A 235       7.612  29.605 -33.459  1.00 17.55           O  
ANISOU 3592  OE2 GLU A 235     2294   2266   2108     42     72    -37       O  
ATOM   3593  H   GLU A 235      11.763  28.173 -29.257  1.00 16.01           H  
ATOM   3594  HA  GLU A 235       9.700  29.825 -29.304  1.00 14.43           H  
ATOM   3595  HB2 GLU A 235      11.110  30.708 -31.050  1.00 18.01           H  
ATOM   3596  HB3 GLU A 235      11.022  29.306 -31.793  1.00 18.01           H  
ATOM   3597  HG2 GLU A 235       8.621  30.631 -31.325  1.00 15.65           H  
ATOM   3598  HG3 GLU A 235       9.539  31.192 -32.495  1.00 15.65           H  
ATOM   3599  N   ASN A 236       9.929  26.873 -30.466  1.00 13.23           N  
ANISOU 3599  N   ASN A 236     1703   1685   1638    128    124    -52       N  
ATOM   3600  CA  ASN A 236       9.156  25.709 -30.883  1.00 13.44           C  
ANISOU 3600  CA  ASN A 236     1749   1687   1670    134    131    -76       C  
ATOM   3601  C   ASN A 236       8.249  25.227 -29.753  1.00 16.30           C  
ANISOU 3601  C   ASN A 236     2118   2016   2058    141    118    -69       C  
ATOM   3602  O   ASN A 236       8.714  24.990 -28.630  1.00 14.34           O  
ANISOU 3602  O   ASN A 236     1858   1759   1831    159    119    -56       O  
ATOM   3603  CB  ASN A 236      10.056  24.523 -31.259  1.00 12.65           C  
ANISOU 3603  CB  ASN A 236     1647   1586   1574    160    158    -99       C  
ATOM   3604  CG  ASN A 236      10.585  24.539 -32.692  1.00 13.48           C  
ANISOU 3604  CG  ASN A 236     1752   1721   1648    152    175   -120       C  
ATOM   3605  OD1 ASN A 236      11.210  23.561 -33.101  1.00 14.69           O  
ANISOU 3605  OD1 ASN A 236     1906   1873   1802    175    197   -146       O  
ATOM   3606  ND2 ASN A 236      10.383  25.617 -33.435  1.00 15.13           N  
ANISOU 3606  ND2 ASN A 236     1961   1957   1829    122    165   -111       N  
ATOM   3607  H   ASN A 236      10.777  26.737 -30.420  1.00 15.88           H  
ATOM   3608  HA  ASN A 236       8.636  25.984 -31.654  1.00 16.13           H  
ATOM   3609  HB2 ASN A 236      10.824  24.521 -30.667  1.00 15.18           H  
ATOM   3610  HB3 ASN A 236       9.548  23.704 -31.147  1.00 15.18           H  
ATOM   3611 HD21 ASN A 236      10.674  25.643 -34.244  1.00 18.15           H  
ATOM   3612 HD22 ASN A 236       9.961  26.291 -33.109  1.00 18.15           H  
ATOM   3613  N   HIS A 237       6.975  25.012 -30.083  1.00 12.53           N  
ANISOU 3613  N   HIS A 237     1658   1525   1578    124    106    -77       N  
ATOM   3614  CA  HIS A 237       5.997  24.343 -29.237  1.00 12.22           C  
ANISOU 3614  CA  HIS A 237     1627   1458   1558    124     97    -75       C  
ATOM   3615  C   HIS A 237       5.753  22.936 -29.778  1.00 17.13           C  
ANISOU 3615  C   HIS A 237     2269   2055   2184    126    109   -101       C  
ATOM   3616  O   HIS A 237       5.412  22.774 -30.956  1.00 17.33           O  
ANISOU 3616  O   HIS A 237     2309   2087   2190    110    112   -122       O  
ATOM   3617  CB  HIS A 237       4.662  25.094 -29.226  1.00 11.46           C  
ANISOU 3617  CB  HIS A 237     1532   1369   1453    103     75    -67       C  
ATOM   3618  CG  HIS A 237       4.720  26.497 -28.701  1.00 11.57           C  
ANISOU 3618  CG  HIS A 237     1532   1399   1464    103     59    -45       C  
ATOM   3619  ND1 HIS A 237       5.573  27.459 -29.199  1.00 12.49           N  
ANISOU 3619  ND1 HIS A 237     1644   1536   1566    100     60    -38       N  
ATOM   3620  CD2 HIS A 237       3.958  27.120 -27.769  1.00 13.59           C  
ANISOU 3620  CD2 HIS A 237     1781   1656   1728    103     42    -31       C  
ATOM   3621  CE1 HIS A 237       5.358  28.603 -28.572  1.00 17.55           C  
ANISOU 3621  CE1 HIS A 237     2278   2181   2208     98     42    -20       C  
ATOM   3622  NE2 HIS A 237       4.391  28.421 -27.693  1.00 14.91           N  
ANISOU 3622  NE2 HIS A 237     1942   1836   1887    103     32    -17       N  
ATOM   3623  H   HIS A 237       6.641  25.262 -30.835  1.00 15.04           H  
ATOM   3624  HA  HIS A 237       6.343  24.296 -28.332  1.00 14.66           H  
ATOM   3625  HB2 HIS A 237       4.330  25.139 -30.136  1.00 13.75           H  
ATOM   3626  HB3 HIS A 237       4.039  24.602 -28.669  1.00 13.75           H  
ATOM   3627  HD1 HIS A 237       6.154  27.335 -29.820  1.00 14.99           H  
ATOM   3628  HD2 HIS A 237       3.271  26.737 -27.273  1.00 16.31           H  
ATOM   3629  HE1 HIS A 237       5.811  29.400 -28.725  1.00 21.06           H  
ATOM   3630  N   PHE A 238       5.877  21.931 -28.917  1.00 13.69           N  
ANISOU 3630  N   PHE A 238     1839   1590   1772    141    115    -99       N  
ATOM   3631  CA  PHE A 238       5.929  20.547 -29.349  1.00 14.58           C  
ANISOU 3631  CA  PHE A 238     1976   1671   1893    148    127   -123       C  
ATOM   3632  C   PHE A 238       4.655  19.780 -29.015  1.00 17.03           C  
ANISOU 3632  C   PHE A 238     2306   1952   2212    126    115   -125       C  
ATOM   3633  O   PHE A 238       4.061  19.968 -27.950  1.00 16.68           O  
ANISOU 3633  O   PHE A 238     2253   1907   2180    119    102   -101       O  
ATOM   3634  CB  PHE A 238       7.090  19.811 -28.672  1.00 15.46           C  
ANISOU 3634  CB  PHE A 238     2084   1764   2027    186    142   -120       C  
ATOM   3635  CG  PHE A 238       8.439  20.426 -28.894  1.00 16.92           C  
ANISOU 3635  CG  PHE A 238     2244   1981   2204    208    155   -117       C  
ATOM   3636  CD1 PHE A 238       8.891  20.713 -30.166  1.00 16.26           C  
ANISOU 3636  CD1 PHE A 238     2159   1923   2096    205    168   -139       C  
ATOM   3637  CD2 PHE A 238       9.271  20.693 -27.817  1.00 14.30           C  
ANISOU 3637  CD2 PHE A 238     1889   1657   1887    230    155    -92       C  
ATOM   3638  CE1 PHE A 238      10.145  21.254 -30.362  1.00 15.82           C  
ANISOU 3638  CE1 PHE A 238     2077   1902   2030    222    182   -136       C  
ATOM   3639  CE2 PHE A 238      10.528  21.230 -28.012  1.00 14.45           C  
ANISOU 3639  CE2 PHE A 238     1883   1711   1898    247    167    -89       C  
ATOM   3640  CZ  PHE A 238      10.960  21.525 -29.282  1.00 16.16           C  
ANISOU 3640  CZ  PHE A 238     2095   1954   2089    242    180   -110       C  
ATOM   3641  H   PHE A 238       5.934  22.034 -28.065  1.00 16.43           H  
ATOM   3642  HA  PHE A 238       6.032  20.556 -30.314  1.00 17.50           H  
ATOM   3643  HB2 PHE A 238       6.930  19.798 -27.715  1.00 18.55           H  
ATOM   3644  HB3 PHE A 238       7.123  18.905 -29.015  1.00 18.55           H  
ATOM   3645  HD1 PHE A 238       8.346  20.539 -30.899  1.00 19.51           H  
ATOM   3646  HD2 PHE A 238       8.979  20.508 -26.954  1.00 17.16           H  
ATOM   3647  HE1 PHE A 238      10.442  21.438 -31.224  1.00 18.98           H  
ATOM   3648  HE2 PHE A 238      11.082  21.392 -27.283  1.00 17.35           H  
ATOM   3649  HZ  PHE A 238      11.798  21.906 -29.413  1.00 19.39           H  
ATOM   3650  N   GLN A 239       4.271  18.884 -29.921  1.00 14.66           N  
ANISOU 3650  N   GLN A 239     2033   1632   1906    113    120   -153       N  
ATOM   3651  CA  GLN A 239       3.392  17.763 -29.619  1.00 16.02           C  
ANISOU 3651  CA  GLN A 239     2231   1765   2090     95    113   -158       C  
ATOM   3652  C   GLN A 239       4.276  16.533 -29.459  1.00 17.30           C  
ANISOU 3652  C   GLN A 239     2416   1883   2275    125    128   -171       C  
ATOM   3653  O   GLN A 239       5.078  16.230 -30.349  1.00 17.19           O  
ANISOU 3653  O   GLN A 239     2412   1866   2254    145    145   -199       O  
ATOM   3654  CB  GLN A 239       2.363  17.554 -30.733  1.00 13.50           C  
ANISOU 3654  CB  GLN A 239     1930   1450   1749     58    106   -183       C  
ATOM   3655  CG  GLN A 239       1.591  18.832 -31.069  1.00 15.85           C  
ANISOU 3655  CG  GLN A 239     2204   1795   2024     36     90   -171       C  
ATOM   3656  CD  GLN A 239       0.642  18.725 -32.269  1.00 15.49           C  
ANISOU 3656  CD  GLN A 239     2172   1762   1952      0     81   -194       C  
ATOM   3657  OE1 GLN A 239      -0.259  19.553 -32.419  1.00 15.19           O  
ANISOU 3657  OE1 GLN A 239     2116   1756   1898    -20     64   -182       O  
ATOM   3658  NE2 GLN A 239       0.862  17.736 -33.135  1.00 17.66           N  
ANISOU 3658  NE2 GLN A 239     2478   2014   2220     -5     93   -228       N  
ATOM   3659  H   GLN A 239       4.518  18.909 -30.744  1.00 17.60           H  
ATOM   3660  HA  GLN A 239       2.895  17.919 -28.800  1.00 19.22           H  
ATOM   3661  HB2 GLN A 239       2.822  17.260 -31.536  1.00 16.20           H  
ATOM   3662  HB3 GLN A 239       1.724  16.882 -30.451  1.00 16.20           H  
ATOM   3663  HG2 GLN A 239       1.056  19.079 -30.298  1.00 19.03           H  
ATOM   3664  HG3 GLN A 239       2.230  19.534 -31.267  1.00 19.03           H  
ATOM   3665 HE21 GLN A 239       1.514  17.191 -33.008  1.00 21.20           H  
ATOM   3666 HE22 GLN A 239       0.351  17.644 -33.820  1.00 21.20           H  
ATOM   3667  N   VAL A 240       4.159  15.845 -28.323  1.00 15.05           N  
ANISOU 3667  N   VAL A 240     2139   1564   2015    130    122   -150       N  
ATOM   3668  CA  VAL A 240       4.981  14.665 -28.085  1.00 16.96           C  
ANISOU 3668  CA  VAL A 240     2405   1759   2280    162    133   -158       C  
ATOM   3669  C   VAL A 240       4.085  13.450 -27.910  1.00 14.42           C  
ANISOU 3669  C   VAL A 240     2123   1384   1971    135    123   -163       C  
ATOM   3670  O   VAL A 240       2.958  13.533 -27.407  1.00 15.91           O  
ANISOU 3670  O   VAL A 240     2310   1578   2156     95    107   -144       O  
ATOM   3671  CB  VAL A 240       5.924  14.820 -26.869  1.00 16.76           C  
ANISOU 3671  CB  VAL A 240     2357   1735   2276    199    134   -126       C  
ATOM   3672  CG1 VAL A 240       6.841  15.993 -27.090  1.00 17.81           C  
ANISOU 3672  CG1 VAL A 240     2453   1920   2396    220    144   -123       C  
ATOM   3673  CG2 VAL A 240       5.141  14.974 -25.558  1.00 18.99           C  
ANISOU 3673  CG2 VAL A 240     2630   2018   2567    176    116    -88       C  
ATOM   3674  H   VAL A 240       3.616  16.044 -27.686  1.00 18.06           H  
ATOM   3675  HA  VAL A 240       5.532  14.527 -28.871  1.00 20.35           H  
ATOM   3676  HB  VAL A 240       6.456  14.014 -26.782  1.00 20.11           H  
ATOM   3677 HG11 VAL A 240       7.736  15.664 -27.268  1.00 21.38           H  
ATOM   3678 HG12 VAL A 240       6.520  16.506 -27.847  1.00 21.38           H  
ATOM   3679 HG13 VAL A 240       6.845  16.545 -26.293  1.00 21.38           H  
ATOM   3680 HG21 VAL A 240       5.663  15.509 -24.940  1.00 22.79           H  
ATOM   3681 HG22 VAL A 240       4.297  15.413 -25.744  1.00 22.79           H  
ATOM   3682 HG23 VAL A 240       4.981  14.095 -25.181  1.00 22.79           H  
ATOM   3683  N   SER A 241       4.600  12.310 -28.356  1.00 17.21           N  
ANISOU 3683  N   SER A 241     2513   1688   2338    156    133   -189       N  
ATOM   3684  CA  SER A 241       3.864  11.060 -28.302  1.00 19.27           C  
ANISOU 3684  CA  SER A 241     2821   1890   2610    130    123   -197       C  
ATOM   3685  C   SER A 241       4.866   9.917 -28.330  1.00 22.02           C  
ANISOU 3685  C   SER A 241     3202   2178   2984    177    135   -214       C  
ATOM   3686  O   SER A 241       5.894  10.006 -29.006  1.00 23.24           O  
ANISOU 3686  O   SER A 241     3350   2343   3135    220    154   -241       O  
ATOM   3687  CB  SER A 241       2.880  10.941 -29.472  1.00 21.76           C  
ANISOU 3687  CB  SER A 241     3157   2210   2901     84    120   -231       C  
ATOM   3688  OG  SER A 241       3.540  11.077 -30.721  1.00 23.00           O  
ANISOU 3688  OG  SER A 241     3318   2381   3041    106    137   -272       O  
ATOM   3689  H   SER A 241       5.385  12.236 -28.700  1.00 20.65           H  
ATOM   3690  HA  SER A 241       3.357  11.008 -27.477  1.00 23.12           H  
ATOM   3691  HB2 SER A 241       2.454  10.071 -29.436  1.00 26.11           H  
ATOM   3692  HB3 SER A 241       2.214  11.641 -29.393  1.00 26.11           H  
ATOM   3693  HG  SER A 241       3.414  11.847 -31.031  1.00 27.60           H  
ATOM   3694  N   LEU A 242       4.568   8.858 -27.584  1.00 19.30           N  
ANISOU 3694  N   LEU A 242     2894   1774   2664    169    122   -198       N  
ATOM   3695  CA  LEU A 242       5.359   7.631 -27.589  1.00 20.30           C  
ANISOU 3695  CA  LEU A 242     3063   1831   2818    212    128   -213       C  
ATOM   3696  C   LEU A 242       4.570   6.550 -28.322  1.00 19.68           C  
ANISOU 3696  C   LEU A 242     3045   1693   2739    176    122   -247       C  
ATOM   3697  O   LEU A 242       3.468   6.187 -27.897  1.00 19.65           O  
ANISOU 3697  O   LEU A 242     3061   1669   2736    120    103   -228       O  
ATOM   3698  CB  LEU A 242       5.697   7.195 -26.160  1.00 20.82           C  
ANISOU 3698  CB  LEU A 242     3130   1867   2914    233    116   -164       C  
ATOM   3699  CG  LEU A 242       6.493   5.902 -25.955  1.00 23.27           C  
ANISOU 3699  CG  LEU A 242     3485   2099   3258    282    117   -170       C  
ATOM   3700  CD1 LEU A 242       7.814   5.951 -26.708  1.00 24.97           C  
ANISOU 3700  CD1 LEU A 242     3687   2324   3475    351    141   -206       C  
ATOM   3701  CD2 LEU A 242       6.759   5.629 -24.465  1.00 22.70           C  
ANISOU 3701  CD2 LEU A 242     3408   2007   3211    297    102   -113       C  
ATOM   3702  H   LEU A 242       3.892   8.827 -27.053  1.00 23.16           H  
ATOM   3703  HA  LEU A 242       6.193   7.774 -28.063  1.00 24.36           H  
ATOM   3704  HB2 LEU A 242       6.216   7.906 -25.753  1.00 24.99           H  
ATOM   3705  HB3 LEU A 242       4.859   7.081 -25.684  1.00 24.99           H  
ATOM   3706  HG  LEU A 242       5.959   5.172 -26.305  1.00 27.93           H  
ATOM   3707 HD11 LEU A 242       8.238   5.081 -26.658  1.00 29.96           H  
ATOM   3708 HD12 LEU A 242       7.641   6.182 -27.634  1.00 29.96           H  
ATOM   3709 HD13 LEU A 242       8.384   6.622 -26.301  1.00 29.96           H  
ATOM   3710 HD21 LEU A 242       7.368   6.302 -24.124  1.00 27.24           H  
ATOM   3711 HD22 LEU A 242       5.919   5.667 -23.982  1.00 27.24           H  
ATOM   3712 HD23 LEU A 242       7.154   4.748 -24.372  1.00 27.24           H  
ATOM   3713  N   VAL A 243       5.131   6.034 -29.419  1.00 20.32           N  
ANISOU 3713  N   VAL A 243     3154   1749   2817    205    138   -299       N  
ATOM   3714  CA  VAL A 243       4.416   5.041 -30.213  1.00 21.30           C  
ANISOU 3714  CA  VAL A 243     3338   1818   2937    169    132   -338       C  
ATOM   3715  C   VAL A 243       3.919   3.919 -29.313  1.00 25.63           C  
ANISOU 3715  C   VAL A 243     3935   2287   3514    146    111   -312       C  
ATOM   3716  O   VAL A 243       4.672   3.364 -28.504  1.00 22.30           O  
ANISOU 3716  O   VAL A 243     3526   1822   3126    193    109   -289       O  
ATOM   3717  CB  VAL A 243       5.316   4.490 -31.333  1.00 20.52           C  
ANISOU 3717  CB  VAL A 243     3267   1693   2837    219    154   -399       C  
ATOM   3718  CG1 VAL A 243       4.614   3.361 -32.092  1.00 24.37           C  
ANISOU 3718  CG1 VAL A 243     3825   2114   3322    182    147   -442       C  
ATOM   3719  CG2 VAL A 243       5.692   5.578 -32.288  1.00 22.03           C  
ANISOU 3719  CG2 VAL A 243     3412   1966   2993    229    174   -424       C  
ATOM   3720  H   VAL A 243       5.910   6.239 -29.718  1.00 24.38           H  
ATOM   3721  HA  VAL A 243       3.649   5.476 -30.619  1.00 25.56           H  
ATOM   3722  HB  VAL A 243       6.122   4.135 -30.926  1.00 24.62           H  
ATOM   3723 HG11 VAL A 243       5.186   3.065 -32.817  1.00 29.25           H  
ATOM   3724 HG12 VAL A 243       4.448   2.626 -31.481  1.00 29.25           H  
ATOM   3725 HG13 VAL A 243       3.775   3.693 -32.446  1.00 29.25           H  
ATOM   3726 HG21 VAL A 243       6.444   6.071 -31.925  1.00 26.44           H  
ATOM   3727 HG22 VAL A 243       5.936   5.181 -33.139  1.00 26.44           H  
ATOM   3728 HG23 VAL A 243       4.934   6.171 -32.406  1.00 26.44           H  
ATOM   3729  N   ASN A 244       2.634   3.596 -29.455  1.00 23.32           N  
ANISOU 3729  N   ASN A 244     3669   1981   3210     72     93   -312       N  
ATOM   3730  CA  ASN A 244       1.950   2.480 -28.809  1.00 25.61           C  
ANISOU 3730  CA  ASN A 244     4013   2197   3520     31     71   -291       C  
ATOM   3731  C   ASN A 244       1.887   2.596 -27.293  1.00 24.92           C  
ANISOU 3731  C   ASN A 244     3904   2113   3453     28     57   -224       C  
ATOM   3732  O   ASN A 244       1.574   1.608 -26.619  1.00 26.40           O  
ANISOU 3732  O   ASN A 244     4137   2233   3661      6     40   -200       O  
ATOM   3733  CB  ASN A 244       2.591   1.140 -29.191  1.00 29.80           C  
ANISOU 3733  CB  ASN A 244     4616   2630   4078     69     74   -327       C  
ATOM   3734  CG  ASN A 244       1.862   0.455 -30.321  1.00 46.10           C  
ANISOU 3734  CG  ASN A 244     6735   4656   6126     21     70   -380       C  
ATOM   3735  OD1 ASN A 244       1.849   0.946 -31.449  1.00 63.13           O  
ANISOU 3735  OD1 ASN A 244     8876   6858   8253     19     84   -426       O  
ATOM   3736  ND2 ASN A 244       1.242  -0.682 -30.026  1.00 83.35           N  
ANISOU 3736  ND2 ASN A 244    11496   9313  10861    -22     47   -370       N  
ATOM   3737  H   ASN A 244       2.103   4.046 -29.960  1.00 27.98           H  
ATOM   3738  HA  ASN A 244       1.033   2.486 -29.125  1.00 30.73           H  
ATOM   3739  HB2 ASN A 244       3.506   1.295 -29.473  1.00 35.76           H  
ATOM   3740  HB3 ASN A 244       2.576   0.550 -28.421  1.00 35.76           H  
ATOM   3741 HD21 ASN A 244       0.813  -1.109 -30.636  1.00100.02           H  
ATOM   3742 HD22 ASN A 244       1.269  -0.991 -29.223  1.00100.02           H  
ATOM   3743  N   HIS A 245       2.171   3.767 -26.734  1.00 20.20           N  
ANISOU 3743  N   HIS A 245     3239   1590   2845     48     64   -194       N  
ATOM   3744  CA  HIS A 245       2.124   3.963 -25.294  1.00 19.99           C  
ANISOU 3744  CA  HIS A 245     3188   1576   2832     44     52   -132       C  
ATOM   3745  C   HIS A 245       1.313   5.212 -24.994  1.00 23.01           C  
ANISOU 3745  C   HIS A 245     3510   2047   3186      4     49   -110       C  
ATOM   3746  O   HIS A 245       1.311   6.165 -25.778  1.00 25.86           O  
ANISOU 3746  O   HIS A 245     3836   2466   3523      8     60   -135       O  
ATOM   3747  CB  HIS A 245       3.527   4.123 -24.663  1.00 21.70           C  
ANISOU 3747  CB  HIS A 245     3382   1791   3070    124     62   -113       C  
ATOM   3748  CG  HIS A 245       4.364   2.883 -24.718  1.00 21.96           C  
ANISOU 3748  CG  HIS A 245     3471   1736   3136    174     62   -127       C  
ATOM   3749  ND1 HIS A 245       4.920   2.415 -25.888  1.00 23.55           N  
ANISOU 3749  ND1 HIS A 245     3703   1904   3340    210     77   -184       N  
ATOM   3750  CD2 HIS A 245       4.747   2.020 -23.748  1.00 19.11           C  
ANISOU 3750  CD2 HIS A 245     3140   1314   2806    196     48    -90       C  
ATOM   3751  CE1 HIS A 245       5.598   1.309 -25.640  1.00 23.96           C  
ANISOU 3751  CE1 HIS A 245     3803   1876   3426    256     72   -185       C  
ATOM   3752  NE2 HIS A 245       5.513   1.050 -24.347  1.00 24.76           N  
ANISOU 3752  NE2 HIS A 245     3906   1957   3545    249     54   -126       N  
ATOM   3753  H   HIS A 245       2.397   4.469 -27.176  1.00 24.24           H  
ATOM   3754  HA  HIS A 245       1.703   3.189 -24.889  1.00 23.99           H  
ATOM   3755  HB2 HIS A 245       4.004   4.822 -25.138  1.00 26.04           H  
ATOM   3756  HB3 HIS A 245       3.423   4.368 -23.730  1.00 26.04           H  
ATOM   3757  HD1 HIS A 245       4.839   2.785 -26.660  1.00 28.26           H  
ATOM   3758  HD2 HIS A 245       4.532   2.073 -22.845  1.00 22.93           H  
ATOM   3759  HE1 HIS A 245       6.058   0.800 -26.267  1.00 28.75           H  
ATOM   3760  N   THR A 246       0.606   5.188 -23.866  1.00 25.43           N  
ANISOU 3760  N   THR A 246     3807   2363   3493    -36     33    -62       N  
ATOM   3761  CA  THR A 246       0.005   6.396 -23.334  1.00 22.89           C  
ANISOU 3761  CA  THR A 246     3424   2126   3148    -60     31    -36       C  
ATOM   3762  C   THR A 246       0.954   7.008 -22.309  1.00 21.07           C  
ANISOU 3762  C   THR A 246     3155   1921   2928     -9     36     -2       C  
ATOM   3763  O   THR A 246       1.948   6.401 -21.901  1.00 22.60           O  
ANISOU 3763  O   THR A 246     3370   2070   3147     37     38      9       O  
ATOM   3764  CB  THR A 246      -1.357   6.130 -22.691  1.00 21.57           C  
ANISOU 3764  CB  THR A 246     3258   1968   2969   -135     14     -6       C  
ATOM   3765  OG1 THR A 246      -1.243   5.120 -21.684  1.00 23.43           O  
ANISOU 3765  OG1 THR A 246     3530   2147   3227   -142      1     32       O  
ATOM   3766  CG2 THR A 246      -2.369   5.684 -23.730  1.00 26.03           C  
ANISOU 3766  CG2 THR A 246     3851   2520   3517   -192      7    -40       C  
ATOM   3767  H   THR A 246       0.464   4.482 -23.396  1.00 30.52           H  
ATOM   3768  HA  THR A 246      -0.149   7.017 -24.064  1.00 27.47           H  
ATOM   3769  HB  THR A 246      -1.673   6.952 -22.285  1.00 25.88           H  
ATOM   3770  HG1 THR A 246      -0.656   5.338 -21.124  1.00 28.12           H  
ATOM   3771 HG21 THR A 246      -3.139   5.288 -23.293  1.00 31.23           H  
ATOM   3772 HG22 THR A 246      -2.662   6.445 -24.255  1.00 31.23           H  
ATOM   3773 HG23 THR A 246      -1.970   5.028 -24.322  1.00 31.23           H  
ATOM   3774  N   MET A 247       0.641   8.232 -21.910  1.00 15.76           N  
ANISOU 3774  N   MET A 247     2427   1324   2235    -17     38     14       N  
ATOM   3775  CA  MET A 247       1.344   8.950 -20.858  1.00 18.35           C  
ANISOU 3775  CA  MET A 247     2716   1688   2567     18     40     47       C  
ATOM   3776  C   MET A 247       0.289   9.413 -19.869  1.00 20.19           C  
ANISOU 3776  C   MET A 247     2919   1968   2783    -29     29     82       C  
ATOM   3777  O   MET A 247      -0.739   9.965 -20.278  1.00 17.28           O  
ANISOU 3777  O   MET A 247     2532   1642   2392    -68     27     70       O  
ATOM   3778  CB  MET A 247       2.117  10.145 -21.414  1.00 20.51           C  
ANISOU 3778  CB  MET A 247     2949   2012   2830     60     55     26       C  
ATOM   3779  CG  MET A 247       3.218   9.787 -22.398  1.00 20.18           C  
ANISOU 3779  CG  MET A 247     2928   1939   2802    109     69    -10       C  
ATOM   3780  SD  MET A 247       3.998  11.260 -23.097  1.00 22.49           S  
ANISOU 3780  SD  MET A 247     3171   2298   3075    144     86    -31       S  
ATOM   3781  CE  MET A 247       2.721  11.784 -24.232  1.00 24.66           C  
ANISOU 3781  CE  MET A 247     3445   2605   3321     92     83    -62       C  
ATOM   3782  H   MET A 247      -0.006   8.687 -22.249  1.00 18.91           H  
ATOM   3783  HA  MET A 247       1.993   8.374 -20.424  1.00 22.02           H  
ATOM   3784  HB2 MET A 247       1.493  10.729 -21.873  1.00 24.61           H  
ATOM   3785  HB3 MET A 247       2.529  10.617 -20.673  1.00 24.61           H  
ATOM   3786  HG2 MET A 247       3.899   9.270 -21.940  1.00 24.22           H  
ATOM   3787  HG3 MET A 247       2.840   9.268 -23.125  1.00 24.22           H  
ATOM   3788  HE1 MET A 247       2.149  12.430 -23.788  1.00 29.60           H  
ATOM   3789  HE2 MET A 247       3.136  12.190 -25.009  1.00 29.60           H  
ATOM   3790  HE3 MET A 247       2.200  11.011 -24.501  1.00 29.60           H  
ATOM   3791  N   THR A 248       0.517   9.169 -18.587  1.00 18.05           N  
ANISOU 3791  N   THR A 248     2645   1694   2521    -25     22    125       N  
ATOM   3792  CA  THR A 248      -0.399   9.631 -17.552  1.00 16.53           C  
ANISOU 3792  CA  THR A 248     2420   1551   2308    -66     14    158       C  
ATOM   3793  C   THR A 248       0.230  10.831 -16.851  1.00 16.94           C  
ANISOU 3793  C   THR A 248     2423   1662   2352    -29     19    171       C  
ATOM   3794  O   THR A 248       1.246  10.699 -16.160  1.00 17.34           O  
ANISOU 3794  O   THR A 248     2473   1699   2417      9     19    193       O  
ATOM   3795  CB  THR A 248      -0.740   8.512 -16.574  1.00 15.37           C  
ANISOU 3795  CB  THR A 248     2304   1365   2170    -99      0    199       C  
ATOM   3796  OG1 THR A 248      -1.348   7.433 -17.296  1.00 20.80           O  
ANISOU 3796  OG1 THR A 248     3042   1997   2866   -138     -7    184       O  
ATOM   3797  CG2 THR A 248      -1.708   9.035 -15.532  1.00 20.62           C  
ANISOU 3797  CG2 THR A 248     2932   2094   2810   -142     -6    231       C  
ATOM   3798  H   THR A 248       1.199   8.737 -18.291  1.00 21.66           H  
ATOM   3799  HA  THR A 248      -1.229   9.922 -17.962  1.00 19.83           H  
ATOM   3800  HB  THR A 248       0.058   8.190 -16.127  1.00 18.44           H  
ATOM   3801  HG1 THR A 248      -2.034   7.705 -17.697  1.00 24.97           H  
ATOM   3802 HG21 THR A 248      -1.873   8.354 -14.861  1.00 24.75           H  
ATOM   3803 HG22 THR A 248      -1.338   9.820 -15.099  1.00 24.75           H  
ATOM   3804 HG23 THR A 248      -2.550   9.274 -15.951  1.00 24.75           H  
ATOM   3805  N   ILE A 249      -0.380  12.001 -17.056  1.00 16.32           N  
ANISOU 3805  N   ILE A 249     2304   1646   2251    -41     23    156       N  
ATOM   3806  CA  ILE A 249       0.099  13.240 -16.465  1.00 15.53           C  
ANISOU 3806  CA  ILE A 249     2161   1600   2140    -11     27    164       C  
ATOM   3807  C   ILE A 249      -0.136  13.220 -14.967  1.00 16.25           C  
ANISOU 3807  C   ILE A 249     2235   1716   2223    -27     20    205       C  
ATOM   3808  O   ILE A 249      -1.260  12.975 -14.508  1.00 16.74           O  
ANISOU 3808  O   ILE A 249     2293   1797   2270    -73     14    219       O  
ATOM   3809  CB  ILE A 249      -0.622  14.447 -17.081  1.00 14.30           C  
ANISOU 3809  CB  ILE A 249     1972   1498   1963    -22     30    138       C  
ATOM   3810  CG1 ILE A 249      -0.378  14.487 -18.579  1.00 14.53           C  
ANISOU 3810  CG1 ILE A 249     2018   1508   1996    -10     37     99       C  
ATOM   3811  CG2 ILE A 249      -0.176  15.757 -16.399  1.00 16.29           C  
ANISOU 3811  CG2 ILE A 249     2184   1802   2204      6     33    145       C  
ATOM   3812  CD1 ILE A 249      -1.324  15.407 -19.308  1.00 19.76           C  
ANISOU 3812  CD1 ILE A 249     2658   2215   2637    -30     35     77       C  
ATOM   3813  H   ILE A 249      -1.083  12.101 -17.540  1.00 19.58           H  
ATOM   3814  HA  ILE A 249       1.051  13.309 -16.640  1.00 18.64           H  
ATOM   3815  HB  ILE A 249      -1.575  14.352 -16.931  1.00 17.16           H  
ATOM   3816 HG12 ILE A 249       0.526  14.798 -18.742  1.00 17.44           H  
ATOM   3817 HG13 ILE A 249      -0.492  13.594 -18.939  1.00 17.44           H  
ATOM   3818 HG21 ILE A 249      -0.566  16.508 -16.872  1.00 19.55           H  
ATOM   3819 HG22 ILE A 249      -0.480  15.753 -15.478  1.00 19.55           H  
ATOM   3820 HG23 ILE A 249       0.792  15.815 -16.427  1.00 19.55           H  
ATOM   3821 HD11 ILE A 249      -1.268  15.229 -20.260  1.00 23.72           H  
ATOM   3822 HD12 ILE A 249      -2.228  15.244 -18.995  1.00 23.72           H  
ATOM   3823 HD13 ILE A 249      -1.072  16.327 -19.129  1.00 23.72           H  
ATOM   3824  N   ILE A 250       0.908  13.533 -14.202  1.00 16.82           N  
ANISOU 3824  N   ILE A 250     2294   1796   2301     11     21    223       N  
ATOM   3825  CA  ILE A 250       0.794  13.683 -12.756  1.00 14.21           C  
ANISOU 3825  CA  ILE A 250     1943   1499   1958      0     15    261       C  
ATOM   3826  C   ILE A 250       1.220  15.058 -12.262  1.00 15.56           C  
ANISOU 3826  C   ILE A 250     2071   1727   2112     24     18    256       C  
ATOM   3827  O   ILE A 250       0.998  15.363 -11.081  1.00 15.19           O  
ANISOU 3827  O   ILE A 250     2004   1720   2049     13     14    281       O  
ATOM   3828  CB  ILE A 250       1.586  12.589 -11.999  1.00 18.10           C  
ANISOU 3828  CB  ILE A 250     2463   1946   2468     13      6    298       C  
ATOM   3829  CG1 ILE A 250       3.084  12.663 -12.314  1.00 13.72           C  
ANISOU 3829  CG1 ILE A 250     1910   1369   1934     72     10    291       C  
ATOM   3830  CG2 ILE A 250       1.018  11.229 -12.327  1.00 16.85           C  
ANISOU 3830  CG2 ILE A 250     2350   1728   2323    -19      0    306       C  
ATOM   3831  CD1 ILE A 250       3.984  11.817 -11.387  1.00 18.30           C  
ANISOU 3831  CD1 ILE A 250     2505   1918   2529     96      0    332       C  
ATOM   3832  H   ILE A 250       1.703  13.664 -14.504  1.00 20.18           H  
ATOM   3833  HA  ILE A 250      -0.142  13.574 -12.526  1.00 17.06           H  
ATOM   3834  HB  ILE A 250       1.491  12.746 -11.046  1.00 21.72           H  
ATOM   3835 HG12 ILE A 250       3.223  12.349 -13.221  1.00 16.47           H  
ATOM   3836 HG13 ILE A 250       3.370  13.586 -12.235  1.00 16.47           H  
ATOM   3837 HG21 ILE A 250       1.241  10.613 -11.611  1.00 20.21           H  
ATOM   3838 HG22 ILE A 250       0.055  11.301 -12.413  1.00 20.21           H  
ATOM   3839 HG23 ILE A 250       1.402  10.919 -13.162  1.00 20.21           H  
ATOM   3840 HD11 ILE A 250       4.898  12.131 -11.462  1.00 21.96           H  
ATOM   3841 HD12 ILE A 250       3.674  11.914 -10.473  1.00 21.96           H  
ATOM   3842 HD13 ILE A 250       3.930  10.887 -11.658  1.00 21.96           H  
ATOM   3843  N   ALA A 251       1.826  15.898 -13.098  1.00 13.71           N  
ANISOU 3843  N   ALA A 251     1827   1501   1882     56     26    226       N  
ATOM   3844  CA  ALA A 251       2.076  17.279 -12.720  1.00 13.67           C  
ANISOU 3844  CA  ALA A 251     1786   1548   1860     71     28    219       C  
ATOM   3845  C   ALA A 251       2.170  18.124 -13.977  1.00 15.77           C  
ANISOU 3845  C   ALA A 251     2046   1819   2126     86     34    182       C  
ATOM   3846  O   ALA A 251       2.578  17.644 -15.039  1.00 14.87           O  
ANISOU 3846  O   ALA A 251     1954   1670   2027     97     39    165       O  
ATOM   3847  CB  ALA A 251       3.358  17.454 -11.904  1.00 14.11           C  
ANISOU 3847  CB  ALA A 251     1831   1609   1920    103     25    240       C  
ATOM   3848  H   ALA A 251       2.099  15.690 -13.886  1.00 16.45           H  
ATOM   3849  HA  ALA A 251       1.331  17.582 -12.178  1.00 16.41           H  
ATOM   3850  HB1 ALA A 251       3.398  18.364 -11.570  1.00 16.93           H  
ATOM   3851  HB2 ALA A 251       3.348  16.829 -11.162  1.00 16.93           H  
ATOM   3852  HB3 ALA A 251       4.122  17.278 -12.475  1.00 16.93           H  
ATOM   3853  N   ALA A 252       1.768  19.386 -13.839  1.00 12.58           N  
ANISOU 3853  N   ALA A 252     1615   1459   1704     84     33    169       N  
ATOM   3854  CA  ALA A 252       1.928  20.406 -14.863  1.00 14.28           C  
ANISOU 3854  CA  ALA A 252     1823   1685   1916     98     36    140       C  
ATOM   3855  C   ALA A 252       2.754  21.536 -14.270  1.00 13.60           C  
ANISOU 3855  C   ALA A 252     1717   1628   1822    120     34    143       C  
ATOM   3856  O   ALA A 252       2.419  22.052 -13.196  1.00 13.99           O  
ANISOU 3856  O   ALA A 252     1748   1709   1858    114     30    153       O  
ATOM   3857  CB  ALA A 252       0.582  20.944 -15.335  1.00 15.06           C  
ANISOU 3857  CB  ALA A 252     1914   1809   2001     76     33    122       C  
ATOM   3858  H   ALA A 252       1.385  19.682 -13.129  1.00 15.09           H  
ATOM   3859  HA  ALA A 252       2.386  20.033 -15.632  1.00 17.13           H  
ATOM   3860  HB1 ALA A 252       0.732  21.610 -16.024  1.00 18.08           H  
ATOM   3861  HB2 ALA A 252       0.057  20.210 -15.693  1.00 18.08           H  
ATOM   3862  HB3 ALA A 252       0.120  21.344 -14.582  1.00 18.08           H  
ATOM   3863  N   ASP A 253       3.825  21.916 -14.964  1.00 11.89           N  
ANISOU 3863  N   ASP A 253     1502   1402   1614    143     38    132       N  
ATOM   3864  CA  ASP A 253       4.808  22.859 -14.414  1.00 11.79           C  
ANISOU 3864  CA  ASP A 253     1472   1413   1596    160     36    137       C  
ATOM   3865  C   ASP A 253       5.141  22.355 -13.005  1.00 12.21           C  
ANISOU 3865  C   ASP A 253     1518   1474   1648    162     31    167       C  
ATOM   3866  O   ASP A 253       5.479  21.172 -12.858  1.00 15.62           O  
ANISOU 3866  O   ASP A 253     1962   1879   2094    167     33    184       O  
ATOM   3867  CB  ASP A 253       4.265  24.279 -14.520  1.00 12.68           C  
ANISOU 3867  CB  ASP A 253     1572   1553   1691    155     30    120       C  
ATOM   3868  CG  ASP A 253       4.003  24.705 -15.969  1.00 14.81           C  
ANISOU 3868  CG  ASP A 253     1852   1813   1962    154     32     96       C  
ATOM   3869  OD1 ASP A 253       4.408  23.969 -16.902  1.00 13.78           O  
ANISOU 3869  OD1 ASP A 253     1735   1658   1842    158     40     90       O  
ATOM   3870  OD2 ASP A 253       3.369  25.771 -16.160  1.00 13.45           O  
ANISOU 3870  OD2 ASP A 253     1674   1658   1778    149     25     82       O  
ATOM   3871  H   ASP A 253       4.006  21.642 -15.759  1.00 14.27           H  
ATOM   3872  HA  ASP A 253       5.627  22.831 -14.934  1.00 14.15           H  
ATOM   3873  HB2 ASP A 253       3.426  24.335 -14.035  1.00 15.21           H  
ATOM   3874  HB3 ASP A 253       4.910  24.895 -14.138  1.00 15.21           H  
ATOM   3875  N   MET A 254       5.075  23.191 -11.962  1.00 13.29           N  
ANISOU 3875  N   MET A 254     1637   1646   1768    158     25    173       N  
ATOM   3876  CA  MET A 254       5.394  22.764 -10.598  1.00 15.22           C  
ANISOU 3876  CA  MET A 254     1873   1905   2007    156     20    202       C  
ATOM   3877  C   MET A 254       4.151  22.440  -9.767  1.00 15.87           C  
ANISOU 3877  C   MET A 254     1952   2004   2074    131     18    212       C  
ATOM   3878  O   MET A 254       4.177  22.539  -8.530  1.00 15.22           O  
ANISOU 3878  O   MET A 254     1858   1950   1976    125     13    230       O  
ATOM   3879  CB  MET A 254       6.223  23.831  -9.882  1.00 17.99           C  
ANISOU 3879  CB  MET A 254     2205   2288   2344    165     14    202       C  
ATOM   3880  CG  MET A 254       7.644  23.940 -10.359  1.00 23.37           C  
ANISOU 3880  CG  MET A 254     2882   2960   3036    186     14    204       C  
ATOM   3881  SD  MET A 254       8.635  22.508  -9.892  1.00 21.61           S  
ANISOU 3881  SD  MET A 254     2662   2719   2831    205     14    239       S  
ATOM   3882  CE  MET A 254       9.228  22.945  -8.259  1.00 25.66           C  
ANISOU 3882  CE  MET A 254     3152   3275   3323    202      1    265       C  
ATOM   3883  H   MET A 254       4.844  24.017 -12.024  1.00 15.95           H  
ATOM   3884  HA  MET A 254       5.930  21.959 -10.671  1.00 18.27           H  
ATOM   3885  HB2 MET A 254       5.801  24.694 -10.019  1.00 21.59           H  
ATOM   3886  HB3 MET A 254       6.247  23.620  -8.935  1.00 21.59           H  
ATOM   3887  HG2 MET A 254       7.650  24.008 -11.327  1.00 28.04           H  
ATOM   3888  HG3 MET A 254       8.051  24.729  -9.969  1.00 28.04           H  
ATOM   3889  HE1 MET A 254       9.973  22.367  -8.029  1.00 30.80           H  
ATOM   3890  HE2 MET A 254       9.518  23.871  -8.266  1.00 30.80           H  
ATOM   3891  HE3 MET A 254       8.508  22.828  -7.620  1.00 30.80           H  
ATOM   3892  N   VAL A 255       3.069  22.033 -10.419  1.00 13.80           N  
ANISOU 3892  N   VAL A 255     1700   1729   1815    114     21    201       N  
ATOM   3893  CA  VAL A 255       1.806  21.808  -9.721  1.00 11.25           C  
ANISOU 3893  CA  VAL A 255     1368   1430   1474     87     21    208       C  
ATOM   3894  C   VAL A 255       1.341  20.374  -9.939  1.00 12.93           C  
ANISOU 3894  C   VAL A 255     1602   1610   1699     65     22    226       C  
ATOM   3895  O   VAL A 255       0.953  20.004 -11.056  1.00 13.68           O  
ANISOU 3895  O   VAL A 255     1713   1678   1806     59     24    210       O  
ATOM   3896  CB  VAL A 255       0.737  22.824 -10.168  1.00 13.97           C  
ANISOU 3896  CB  VAL A 255     1700   1803   1805     81     22    178       C  
ATOM   3897  CG1 VAL A 255      -0.640  22.497  -9.530  1.00 15.88           C  
ANISOU 3897  CG1 VAL A 255     1928   2076   2028     52     23    185       C  
ATOM   3898  CG2 VAL A 255       1.226  24.234  -9.836  1.00 15.77           C  
ANISOU 3898  CG2 VAL A 255     1913   2056   2022    102     18    162       C  
ATOM   3899  H   VAL A 255       3.040  21.879 -11.265  1.00 16.56           H  
ATOM   3900  HA  VAL A 255       1.956  21.919  -8.769  1.00 13.49           H  
ATOM   3901  HB  VAL A 255       0.600  22.775 -11.127  1.00 16.77           H  
ATOM   3902 HG11 VAL A 255      -1.268  23.201  -9.755  1.00 19.05           H  
ATOM   3903 HG12 VAL A 255      -0.955  21.648  -9.878  1.00 19.05           H  
ATOM   3904 HG13 VAL A 255      -0.536  22.441  -8.567  1.00 19.05           H  
ATOM   3905 HG21 VAL A 255       0.520  24.868 -10.035  1.00 18.92           H  
ATOM   3906 HG22 VAL A 255       1.453  24.276  -8.894  1.00 18.92           H  
ATOM   3907 HG23 VAL A 255       2.009  24.431 -10.374  1.00 18.92           H  
ATOM   3908  N   PRO A 256       1.364  19.535  -8.905  1.00 12.69           N  
ANISOU 3908  N   PRO A 256     1576   1581   1665     51     18    260       N  
ATOM   3909  CA  PRO A 256       0.809  18.186  -9.057  1.00 14.22           C  
ANISOU 3909  CA  PRO A 256     1794   1741   1868     24     16    279       C  
ATOM   3910  C   PRO A 256      -0.663  18.223  -9.424  1.00 16.09           C  
ANISOU 3910  C   PRO A 256     2024   1998   2092    -11     19    264       C  
ATOM   3911  O   PRO A 256      -1.441  19.017  -8.888  1.00 15.91           O  
ANISOU 3911  O   PRO A 256     1972   2028   2044    -21     21    256       O  
ATOM   3912  CB  PRO A 256       1.025  17.554  -7.678  1.00 12.82           C  
ANISOU 3912  CB  PRO A 256     1616   1573   1681     12     10    321       C  
ATOM   3913  CG  PRO A 256       2.207  18.280  -7.149  1.00 12.39           C  
ANISOU 3913  CG  PRO A 256     1547   1536   1625     45      7    324       C  
ATOM   3914  CD  PRO A 256       2.046  19.697  -7.608  1.00 12.68           C  
ANISOU 3914  CD  PRO A 256     1562   1605   1651     58     13    286       C  
ATOM   3915  HA  PRO A 256       1.302  17.691  -9.730  1.00 17.07           H  
ATOM   3916  HB2 PRO A 256       0.245  17.694  -7.118  1.00 15.38           H  
ATOM   3917  HB3 PRO A 256       1.205  16.605  -7.767  1.00 15.38           H  
ATOM   3918  HG2 PRO A 256       2.215  18.231  -6.180  1.00 14.87           H  
ATOM   3919  HG3 PRO A 256       3.019  17.892  -7.508  1.00 14.87           H  
ATOM   3920  HD2 PRO A 256       1.500  20.204  -6.988  1.00 15.22           H  
ATOM   3921  HD3 PRO A 256       2.909  20.127  -7.719  1.00 15.22           H  
ATOM   3922  N   VAL A 257      -1.046  17.323 -10.327  1.00 12.39           N  
ANISOU 3922  N   VAL A 257     1581   1488   1638    -28     19    260       N  
ATOM   3923  CA  VAL A 257      -2.428  17.225 -10.760  1.00 12.47           C  
ANISOU 3923  CA  VAL A 257     1585   1517   1637    -65     19    248       C  
ATOM   3924  C   VAL A 257      -2.937  15.800 -10.604  1.00 14.24           C  
ANISOU 3924  C   VAL A 257     1836   1709   1865   -107     14    274       C  
ATOM   3925  O   VAL A 257      -2.175  14.829 -10.578  1.00 15.07           O  
ANISOU 3925  O   VAL A 257     1975   1760   1992   -100     10    293       O  
ATOM   3926  CB  VAL A 257      -2.629  17.684 -12.225  1.00 15.40           C  
ANISOU 3926  CB  VAL A 257     1960   1876   2016    -54     22    210       C  
ATOM   3927  CG1 VAL A 257      -2.197  19.121 -12.386  1.00 15.35           C  
ANISOU 3927  CG1 VAL A 257     1930   1899   2004    -18     25    187       C  
ATOM   3928  CG2 VAL A 257      -1.877  16.777 -13.216  1.00 15.10           C  
ANISOU 3928  CG2 VAL A 257     1961   1771   2005    -44     22    204       C  
ATOM   3929  H   VAL A 257      -0.516  16.758 -10.701  1.00 14.87           H  
ATOM   3930  HA  VAL A 257      -2.953  17.792 -10.174  1.00 14.97           H  
ATOM   3931  HB  VAL A 257      -3.573  17.616 -12.437  1.00 18.48           H  
ATOM   3932 HG11 VAL A 257      -2.626  19.494 -13.171  1.00 18.42           H  
ATOM   3933 HG12 VAL A 257      -2.460  19.620 -11.597  1.00 18.42           H  
ATOM   3934 HG13 VAL A 257      -1.233  19.151 -12.490  1.00 18.42           H  
ATOM   3935 HG21 VAL A 257      -2.170  16.983 -14.117  1.00 18.12           H  
ATOM   3936 HG22 VAL A 257      -0.924  16.940 -13.132  1.00 18.12           H  
ATOM   3937 HG23 VAL A 257      -2.073  15.850 -13.007  1.00 18.12           H  
ATOM   3938  N   ASN A 258      -4.260  15.686 -10.538  1.00 14.94           N  
ANISOU 3938  N   ASN A 258     1910   1832   1935   -150     14    274       N  
ATOM   3939  CA  ASN A 258      -4.888  14.375 -10.559  1.00 16.12           C  
ANISOU 3939  CA  ASN A 258     2087   1951   2087   -200      8    296       C  
ATOM   3940  C   ASN A 258      -4.578  13.690 -11.885  1.00 14.69           C  
ANISOU 3940  C   ASN A 258     1946   1702   1932   -196      6    276       C  
ATOM   3941  O   ASN A 258      -4.620  14.311 -12.949  1.00 15.07           O  
ANISOU 3941  O   ASN A 258     1988   1754   1984   -177      9    240       O  
ATOM   3942  CB  ASN A 258      -6.397  14.501 -10.356  1.00 15.92           C  
ANISOU 3942  CB  ASN A 258     2031   1986   2034   -249      8    296       C  
ATOM   3943  CG  ASN A 258      -6.767  15.071  -8.986  1.00 19.01           C  
ANISOU 3943  CG  ASN A 258     2381   2446   2394   -256     13    315       C  
ATOM   3944  OD1 ASN A 258      -6.089  14.845  -7.985  1.00 18.04           O  
ANISOU 3944  OD1 ASN A 258     2265   2319   2270   -248     11    344       O  
ATOM   3945  ND2 ASN A 258      -7.873  15.794  -8.942  1.00 20.12           N  
ANISOU 3945  ND2 ASN A 258     2480   2656   2510   -270     18    298       N  
ATOM   3946  H   ASN A 258      -4.809  16.345 -10.481  1.00 17.93           H  
ATOM   3947  HA  ASN A 258      -4.545  13.827  -9.836  1.00 19.34           H  
ATOM   3948  HB2 ASN A 258      -6.759  15.093 -11.034  1.00 19.11           H  
ATOM   3949  HB3 ASN A 258      -6.801  13.622 -10.433  1.00 19.11           H  
ATOM   3950 HD21 ASN A 258      -8.131  16.141  -8.199  1.00 24.15           H  
ATOM   3951 HD22 ASN A 258      -8.334  15.918  -9.658  1.00 24.15           H  
ATOM   3952  N   ALA A 259      -4.252  12.404 -11.818  1.00 17.28           N  
ANISOU 3952  N   ALA A 259     2318   1968   2278   -212     -1    298       N  
ATOM   3953  CA  ALA A 259      -3.739  11.698 -12.984  1.00 13.98           C  
ANISOU 3953  CA  ALA A 259     1944   1480   1888   -199     -3    277       C  
ATOM   3954  C   ALA A 259      -4.667  11.846 -14.184  1.00 19.30           C  
ANISOU 3954  C   ALA A 259     2616   2162   2553   -225     -2    241       C  
ATOM   3955  O   ALA A 259      -5.889  11.730 -14.066  1.00 16.93           O  
ANISOU 3955  O   ALA A 259     2302   1898   2234   -277     -6    247       O  
ATOM   3956  CB  ALA A 259      -3.555  10.218 -12.642  1.00 16.21           C  
ANISOU 3956  CB  ALA A 259     2277   1694   2187   -222    -13    309       C  
ATOM   3957  H   ALA A 259      -4.318  11.918 -11.112  1.00 20.73           H  
ATOM   3958  HA  ALA A 259      -2.881  12.076 -13.233  1.00 16.77           H  
ATOM   3959  HB1 ALA A 259      -3.192   9.758 -13.415  1.00 19.45           H  
ATOM   3960  HB2 ALA A 259      -2.943  10.141 -11.893  1.00 19.45           H  
ATOM   3961  HB3 ALA A 259      -4.416   9.839 -12.406  1.00 19.45           H  
ATOM   3962  N   MET A 260      -4.071  12.093 -15.350  1.00 19.17           N  
ANISOU 3962  N   MET A 260     2613   2120   2552   -191      4    206       N  
ATOM   3963  CA  MET A 260      -4.816  12.222 -16.599  1.00 17.19           C  
ANISOU 3963  CA  MET A 260     2363   1875   2293   -212      3    171       C  
ATOM   3964  C   MET A 260      -4.036  11.511 -17.692  1.00 16.30           C  
ANISOU 3964  C   MET A 260     2298   1693   2203   -192      6    146       C  
ATOM   3965  O   MET A 260      -2.918  11.917 -18.022  1.00 16.23           O  
ANISOU 3965  O   MET A 260     2290   1670   2206   -139     14    132       O  
ATOM   3966  CB  MET A 260      -5.033  13.689 -16.968  1.00 14.93           C  
ANISOU 3966  CB  MET A 260     2031   1651   1990   -188      9    148       C  
ATOM   3967  CG  MET A 260      -5.841  13.883 -18.226  1.00 20.23           C  
ANISOU 3967  CG  MET A 260     2700   2336   2650   -210      6    116       C  
ATOM   3968  SD  MET A 260      -5.741  15.589 -18.807  1.00 22.84           S  
ANISOU 3968  SD  MET A 260     2989   2720   2968   -168     10     90       S  
ATOM   3969  CE  MET A 260      -6.764  16.425 -17.597  1.00 23.02           C  
ANISOU 3969  CE  MET A 260     2959   2820   2968   -182      7    109       C  
ATOM   3970  H   MET A 260      -3.222  12.191 -15.443  1.00 23.01           H  
ATOM   3971  HA  MET A 260      -5.686  11.806 -16.497  1.00 20.63           H  
ATOM   3972  HB2 MET A 260      -5.505  14.127 -16.243  1.00 17.91           H  
ATOM   3973  HB3 MET A 260      -4.169  14.108 -17.104  1.00 17.91           H  
ATOM   3974  HG2 MET A 260      -5.499  13.302 -18.922  1.00 24.27           H  
ATOM   3975  HG3 MET A 260      -6.772  13.675 -18.047  1.00 24.27           H  
ATOM   3976  HE1 MET A 260      -6.200  16.752 -16.879  1.00 27.62           H  
ATOM   3977  HE2 MET A 260      -7.218  17.167 -18.026  1.00 27.62           H  
ATOM   3978  HE3 MET A 260      -7.415  15.797 -17.247  1.00 27.62           H  
ATOM   3979  N   THR A 261      -4.621  10.450 -18.243  1.00 18.00           N  
ANISOU 3979  N   THR A 261     2552   1867   2422   -234     -2    139       N  
ATOM   3980  CA  THR A 261      -3.969   9.657 -19.276  1.00 17.80           C  
ANISOU 3980  CA  THR A 261     2575   1772   2416   -218      0    111       C  
ATOM   3981  C   THR A 261      -4.295  10.232 -20.648  1.00 20.33           C  
ANISOU 3981  C   THR A 261     2887   2115   2723   -219      5     67       C  
ATOM   3982  O   THR A 261      -5.463  10.498 -20.957  1.00 17.76           O  
ANISOU 3982  O   THR A 261     2542   1831   2376   -264     -2     60       O  
ATOM   3983  CB  THR A 261      -4.406   8.193 -19.188  1.00 20.40           C  
ANISOU 3983  CB  THR A 261     2958   2038   2756   -265    -11    123       C  
ATOM   3984  OG1 THR A 261      -4.083   7.686 -17.886  1.00 19.55           O  
ANISOU 3984  OG1 THR A 261     2859   1910   2660   -264    -17    169       O  
ATOM   3985  CG2 THR A 261      -3.703   7.342 -20.250  1.00 22.64           C  
ANISOU 3985  CG2 THR A 261     3297   2244   3060   -243     -9     89       C  
ATOM   3986  H   THR A 261      -5.405  10.169 -18.031  1.00 21.60           H  
ATOM   3987  HA  THR A 261      -3.007   9.691 -19.153  1.00 21.36           H  
ATOM   3988  HB  THR A 261      -5.362   8.132 -19.342  1.00 24.48           H  
ATOM   3989  HG1 THR A 261      -4.634   7.973 -17.321  1.00 23.46           H  
ATOM   3990 HG21 THR A 261      -4.027   6.428 -20.211  1.00 27.17           H  
ATOM   3991 HG22 THR A 261      -3.880   7.701 -21.134  1.00 27.17           H  
ATOM   3992 HG23 THR A 261      -2.745   7.343 -20.096  1.00 27.17           H  
ATOM   3993  N   VAL A 262      -3.250  10.427 -21.460  1.00 18.39           N  
ANISOU 3993  N   VAL A 262     2653   1846   2488   -169     16     38       N  
ATOM   3994  CA  VAL A 262      -3.358  11.002 -22.794  1.00 17.49           C  
ANISOU 3994  CA  VAL A 262     2533   1753   2360   -164     21     -2       C  
ATOM   3995  C   VAL A 262      -2.542  10.169 -23.780  1.00 17.86           C  
ANISOU 3995  C   VAL A 262     2627   1736   2421   -142     28    -35       C  
ATOM   3996  O   VAL A 262      -1.628   9.431 -23.408  1.00 17.34           O  
ANISOU 3996  O   VAL A 262     2591   1618   2380   -110     32    -28       O  
ATOM   3997  CB  VAL A 262      -2.902  12.484 -22.821  1.00 19.34           C  
ANISOU 3997  CB  VAL A 262     2720   2046   2584   -124     28     -4       C  
ATOM   3998  CG1 VAL A 262      -3.731  13.328 -21.839  1.00 17.77           C  
ANISOU 3998  CG1 VAL A 262     2474   1907   2370   -142     21     23       C  
ATOM   3999  CG2 VAL A 262      -1.424  12.612 -22.502  1.00 16.02           C  
ANISOU 3999  CG2 VAL A 262     2301   1604   2183    -65     40      1       C  
ATOM   4000  H   VAL A 262      -2.442  10.224 -21.246  1.00 22.07           H  
ATOM   4001  HA  VAL A 262      -4.283  10.959 -23.080  1.00 20.99           H  
ATOM   4002  HB  VAL A 262      -3.046  12.825 -23.718  1.00 23.21           H  
ATOM   4003 HG11 VAL A 262      -3.345  14.216 -21.782  1.00 21.32           H  
ATOM   4004 HG12 VAL A 262      -4.644  13.384 -22.164  1.00 21.32           H  
ATOM   4005 HG13 VAL A 262      -3.716  12.904 -20.967  1.00 21.32           H  
ATOM   4006 HG21 VAL A 262      -1.202  13.551 -22.404  1.00 19.23           H  
ATOM   4007 HG22 VAL A 262      -1.237  12.140 -21.675  1.00 19.23           H  
ATOM   4008 HG23 VAL A 262      -0.909  12.224 -23.227  1.00 19.23           H  
ATOM   4009  N   ASP A 263      -2.903  10.285 -25.060  1.00 17.46           N  
ANISOU 4009  N   ASP A 263     2585   1695   2355   -157     30    -72       N  
ATOM   4010  CA  ASP A 263      -2.136   9.661 -26.131  1.00 17.82           C  
ANISOU 4010  CA  ASP A 263     2671   1693   2408   -133     40   -112       C  
ATOM   4011  C   ASP A 263      -0.986  10.535 -26.619  1.00 17.04           C  
ANISOU 4011  C   ASP A 263     2548   1618   2307    -74     56   -128       C  
ATOM   4012  O   ASP A 263       0.000  10.018 -27.157  1.00 21.89           O  
ANISOU 4012  O   ASP A 263     3190   2194   2933    -36     69   -152       O  
ATOM   4013  CB  ASP A 263      -3.046   9.354 -27.325  1.00 24.49           C  
ANISOU 4013  CB  ASP A 263     3535   2538   3230   -181     33   -147       C  
ATOM   4014  CG  ASP A 263      -4.088   8.298 -27.017  1.00 34.69           C  
ANISOU 4014  CG  ASP A 263     4860   3797   4524   -244     16   -137       C  
ATOM   4015  OD1 ASP A 263      -3.785   7.373 -26.236  1.00 34.21           O  
ANISOU 4015  OD1 ASP A 263     4832   3679   4488   -242     13   -117       O  
ATOM   4016  OD2 ASP A 263      -5.211   8.391 -27.555  1.00 38.35           O  
ANISOU 4016  OD2 ASP A 263     5316   4292   4964   -297      5   -147       O  
ATOM   4017  H   ASP A 263      -3.592  10.722 -25.332  1.00 20.96           H  
ATOM   4018  HA  ASP A 263      -1.771   8.827 -25.795  1.00 21.39           H  
ATOM   4019  HB2 ASP A 263      -3.510  10.165 -27.585  1.00 29.38           H  
ATOM   4020  HB3 ASP A 263      -2.503   9.032 -28.061  1.00 29.38           H  
ATOM   4021  N   SER A 264      -1.124  11.850 -26.493  1.00 17.52           N  
ANISOU 4021  N   SER A 264     2561   1745   2352    -68     56   -116       N  
ATOM   4022  CA  SER A 264      -0.117  12.799 -26.935  1.00 15.05           C  
ANISOU 4022  CA  SER A 264     2223   1461   2034    -22     70   -126       C  
ATOM   4023  C   SER A 264      -0.281  14.044 -26.079  1.00 16.50           C  
ANISOU 4023  C   SER A 264     2359   1700   2212    -16     65    -95       C  
ATOM   4024  O   SER A 264      -1.301  14.226 -25.413  1.00 20.23           O  
ANISOU 4024  O   SER A 264     2816   2194   2678    -48     52    -74       O  
ATOM   4025  CB  SER A 264      -0.260  13.149 -28.417  1.00 21.07           C  
ANISOU 4025  CB  SER A 264     2990   2244   2772    -31     74   -164       C  
ATOM   4026  OG  SER A 264      -1.465  13.848 -28.667  1.00 19.28           O  
ANISOU 4026  OG  SER A 264     2740   2064   2522    -71     60   -160       O  
ATOM   4027  H   SER A 264      -1.814  12.226 -26.143  1.00 21.03           H  
ATOM   4028  HA  SER A 264       0.767  12.420 -26.811  1.00 18.06           H  
ATOM   4029  HB2 SER A 264       0.488  13.709 -28.680  1.00 25.28           H  
ATOM   4030  HB3 SER A 264      -0.259  12.329 -28.934  1.00 25.28           H  
ATOM   4031  HG  SER A 264      -2.113  13.314 -28.659  1.00 23.14           H  
ATOM   4032  N   LEU A 265       0.719  14.919 -26.123  1.00 15.25           N  
ANISOU 4032  N   LEU A 265     2177   1564   2052     25     75    -94       N  
ATOM   4033  CA  LEU A 265       0.799  16.035 -25.192  1.00 18.23           C  
ANISOU 4033  CA  LEU A 265     2515   1984   2428     36     70    -65       C  
ATOM   4034  C   LEU A 265       1.399  17.265 -25.848  1.00 16.49           C  
ANISOU 4034  C   LEU A 265     2272   1802   2193     58     76    -75       C  
ATOM   4035  O   LEU A 265       2.425  17.171 -26.524  1.00 16.78           O  
ANISOU 4035  O   LEU A 265     2316   1830   2231     85     90    -92       O  
ATOM   4036  CB  LEU A 265       1.630  15.585 -23.990  1.00 17.77           C  
ANISOU 4036  CB  LEU A 265     2457   1902   2392     64     74    -39       C  
ATOM   4037  CG  LEU A 265       1.817  16.426 -22.749  1.00 24.13           C  
ANISOU 4037  CG  LEU A 265     3229   2740   3198     76     69     -8       C  
ATOM   4038  CD1 LEU A 265       0.479  16.792 -22.168  1.00 35.13           C  
ANISOU 4038  CD1 LEU A 265     4607   4163   4580     39     56      7       C  
ATOM   4039  CD2 LEU A 265       2.631  15.567 -21.775  1.00 20.98           C  
ANISOU 4039  CD2 LEU A 265     2842   2307   2822     99     71     15       C  
ATOM   4040  H   LEU A 265       1.367  14.885 -26.688  1.00 18.29           H  
ATOM   4041  HA  LEU A 265      -0.088  16.311 -24.912  1.00 21.88           H  
ATOM   4042  HB2 LEU A 265       1.234  14.756 -23.679  1.00 21.32           H  
ATOM   4043  HB3 LEU A 265       2.526  15.419 -24.323  1.00 21.32           H  
ATOM   4044  HG  LEU A 265       2.276  17.261 -22.932  1.00 28.95           H  
ATOM   4045 HD11 LEU A 265       0.546  17.662 -21.745  1.00 42.16           H  
ATOM   4046 HD12 LEU A 265      -0.178  16.821 -22.882  1.00 42.16           H  
ATOM   4047 HD13 LEU A 265       0.226  16.124 -21.512  1.00 42.16           H  
ATOM   4048 HD21 LEU A 265       2.332  14.646 -21.840  1.00 25.17           H  
ATOM   4049 HD22 LEU A 265       3.570  15.628 -22.009  1.00 25.17           H  
ATOM   4050 HD23 LEU A 265       2.492  15.896 -20.873  1.00 25.17           H  
ATOM   4051  N   PHE A 266       0.754  18.419 -25.653  1.00 13.53           N  
ANISOU 4051  N   PHE A 266     1868   1470   1803     47     66    -64       N  
ATOM   4052  CA  PHE A 266       1.272  19.699 -26.123  1.00 11.26           C  
ANISOU 4052  CA  PHE A 266     1560   1216   1502     64     67    -66       C  
ATOM   4053  C   PHE A 266       2.117  20.343 -25.030  1.00 14.36           C  
ANISOU 4053  C   PHE A 266     1930   1620   1905     91     69    -43       C  
ATOM   4054  O   PHE A 266       1.635  20.551 -23.909  1.00 16.01           O  
ANISOU 4054  O   PHE A 266     2125   1838   2118     86     60    -22       O  
ATOM   4055  CB  PHE A 266       0.129  20.629 -26.515  1.00 13.94           C  
ANISOU 4055  CB  PHE A 266     1883   1591   1821     41     52    -67       C  
ATOM   4056  CG  PHE A 266       0.582  21.968 -26.993  1.00 13.26           C  
ANISOU 4056  CG  PHE A 266     1782   1535   1722     55     49    -66       C  
ATOM   4057  CD1 PHE A 266       0.977  22.144 -28.301  1.00 13.87           C  
ANISOU 4057  CD1 PHE A 266     1868   1617   1783     54     55    -85       C  
ATOM   4058  CD2 PHE A 266       0.627  23.048 -26.130  1.00 15.70           C  
ANISOU 4058  CD2 PHE A 266     2068   1865   2033     67     41    -47       C  
ATOM   4059  CE1 PHE A 266       1.399  23.378 -28.744  1.00 13.70           C  
ANISOU 4059  CE1 PHE A 266     1836   1622   1748     62     51    -80       C  
ATOM   4060  CE2 PHE A 266       1.049  24.284 -26.571  1.00 14.61           C  
ANISOU 4060  CE2 PHE A 266     1920   1747   1882     77     37    -44       C  
ATOM   4061  CZ  PHE A 266       1.426  24.450 -27.882  1.00 15.54           C  
ANISOU 4061  CZ  PHE A 266     2050   1870   1986     73     41    -59       C  
ATOM   4062  H   PHE A 266       0.001  18.482 -25.243  1.00 16.23           H  
ATOM   4063  HA  PHE A 266       1.833  19.546 -26.899  1.00 13.51           H  
ATOM   4064  HB2 PHE A 266      -0.379  20.216 -27.230  1.00 16.72           H  
ATOM   4065  HB3 PHE A 266      -0.440  20.767 -25.741  1.00 16.72           H  
ATOM   4066  HD1 PHE A 266       0.957  21.424 -28.889  1.00 16.64           H  
ATOM   4067  HD2 PHE A 266       0.369  22.940 -25.243  1.00 18.84           H  
ATOM   4068  HE1 PHE A 266       1.666  23.487 -29.628  1.00 16.44           H  
ATOM   4069  HE2 PHE A 266       1.078  25.004 -25.983  1.00 17.53           H  
ATOM   4070  HZ  PHE A 266       1.700  25.285 -28.186  1.00 18.65           H  
ATOM   4071  N   LEU A 267       3.376  20.650 -25.351  1.00 14.60           N  
ANISOU 4071  N   LEU A 267     1957   1653   1936    117     80    -47       N  
ATOM   4072  CA  LEU A 267       4.254  21.390 -24.451  1.00 15.18           C  
ANISOU 4072  CA  LEU A 267     2009   1744   2016    139     81    -27       C  
ATOM   4073  C   LEU A 267       4.613  22.730 -25.074  1.00 18.98           C  
ANISOU 4073  C   LEU A 267     2475   2256   2479    140     78    -30       C  
ATOM   4074  O   LEU A 267       5.429  22.793 -25.999  1.00 15.31           O  
ANISOU 4074  O   LEU A 267     2014   1798   2007    148     90    -43       O  
ATOM   4075  CB  LEU A 267       5.528  20.615 -24.146  1.00 25.85           C  
ANISOU 4075  CB  LEU A 267     3363   3075   3384    169     94    -24       C  
ATOM   4076  CG  LEU A 267       5.349  19.449 -23.189  1.00 30.15           C  
ANISOU 4076  CG  LEU A 267     3920   3587   3948    172     92    -10       C  
ATOM   4077  CD1 LEU A 267       5.626  18.157 -23.921  1.00 38.51           C  
ANISOU 4077  CD1 LEU A 267     5009   4606   5018    182    103    -30       C  
ATOM   4078  CD2 LEU A 267       6.265  19.652 -22.012  1.00 19.53           C  
ANISOU 4078  CD2 LEU A 267     2555   2251   2613    196     92     16       C  
ATOM   4079  H   LEU A 267       3.744  20.435 -26.098  1.00 17.52           H  
ATOM   4080  HA  LEU A 267       3.763  21.543 -23.629  1.00 18.22           H  
ATOM   4081  HB2 LEU A 267       5.879  20.260 -24.977  1.00 31.02           H  
ATOM   4082  HB3 LEU A 267       6.170  21.224 -23.748  1.00 31.02           H  
ATOM   4083  HG  LEU A 267       4.441  19.394 -22.851  1.00 36.18           H  
ATOM   4084 HD11 LEU A 267       5.335  17.413 -23.370  1.00 46.22           H  
ATOM   4085 HD12 LEU A 267       5.139  18.158 -24.759  1.00 46.22           H  
ATOM   4086 HD13 LEU A 267       6.579  18.089 -24.092  1.00 46.22           H  
ATOM   4087 HD21 LEU A 267       6.319  18.825 -21.508  1.00 23.43           H  
ATOM   4088 HD22 LEU A 267       7.145  19.900 -22.336  1.00 23.43           H  
ATOM   4089 HD23 LEU A 267       5.907  20.358 -21.451  1.00 23.43           H  
ATOM   4090  N   GLY A 268       4.034  23.797 -24.543  1.00 15.25           N  
ANISOU 4090  N   GLY A 268     1989   1806   2001    132     64    -17       N  
ATOM   4091  CA  GLY A 268       4.446  25.127 -24.931  1.00 17.15           C  
ANISOU 4091  CA  GLY A 268     2219   2070   2227    133     59    -14       C  
ATOM   4092  C   GLY A 268       5.835  25.454 -24.420  1.00 15.77           C  
ANISOU 4092  C   GLY A 268     2032   1903   2058    151     66     -3       C  
ATOM   4093  O   GLY A 268       6.409  24.768 -23.572  1.00 14.26           O  
ANISOU 4093  O   GLY A 268     1836   1703   1882    166     73      6       O  
ATOM   4094  H   GLY A 268       3.404  23.775 -23.958  1.00 18.30           H  
ATOM   4095  HA2 GLY A 268       4.450  25.195 -25.899  1.00 20.58           H  
ATOM   4096  HA3 GLY A 268       3.824  25.778 -24.571  1.00 20.58           H  
ATOM   4097  N   VAL A 269       6.381  26.552 -24.933  1.00 13.52           N  
ANISOU 4097  N   VAL A 269     1741   1637   1759    147     63     -1       N  
ATOM   4098  CA  VAL A 269       7.710  26.969 -24.508  1.00 15.06           C  
ANISOU 4098  CA  VAL A 269     1921   1846   1955    158     68     10       C  
ATOM   4099  C   VAL A 269       7.678  27.201 -23.005  1.00 13.37           C  
ANISOU 4099  C   VAL A 269     1695   1632   1751    164     59     27       C  
ATOM   4100  O   VAL A 269       6.847  27.962 -22.492  1.00 13.71           O  
ANISOU 4100  O   VAL A 269     1740   1679   1792    156     44     31       O  
ATOM   4101  CB  VAL A 269       8.166  28.212 -25.269  1.00 12.80           C  
ANISOU 4101  CB  VAL A 269     1632   1580   1649    144     63     13       C  
ATOM   4102  CG1 VAL A 269       9.498  28.702 -24.723  1.00 15.49           C  
ANISOU 4102  CG1 VAL A 269     1955   1939   1990    148     66     26       C  
ATOM   4103  CG2 VAL A 269       8.260  27.901 -26.757  1.00 15.97           C  
ANISOU 4103  CG2 VAL A 269     2044   1987   2036    136     74     -4       C  
ATOM   4104  H   VAL A 269       6.010  27.063 -25.516  1.00 16.23           H  
ATOM   4105  HA  VAL A 269       8.346  26.262 -24.702  1.00 18.07           H  
ATOM   4106  HB  VAL A 269       7.519  28.924 -25.150  1.00 15.36           H  
ATOM   4107 HG11 VAL A 269       9.596  29.645 -24.930  1.00 18.58           H  
ATOM   4108 HG12 VAL A 269       9.514  28.571 -23.762  1.00 18.58           H  
ATOM   4109 HG13 VAL A 269      10.215  28.197 -25.138  1.00 18.58           H  
ATOM   4110 HG21 VAL A 269       8.588  26.996 -26.871  1.00 19.16           H  
ATOM   4111 HG22 VAL A 269       7.379  27.987 -27.154  1.00 19.16           H  
ATOM   4112 HG23 VAL A 269       8.872  28.529 -27.172  1.00 19.16           H  
ATOM   4113  N   GLY A 270       8.573  26.526 -22.293  1.00 11.99           N  
ANISOU 4113  N   GLY A 270     1510   1457   1589    181     68     36       N  
ATOM   4114  CA  GLY A 270       8.719  26.694 -20.871  1.00 11.13           C  
ANISOU 4114  CA  GLY A 270     1389   1354   1487    186     60     54       C  
ATOM   4115  C   GLY A 270       7.826  25.818 -20.032  1.00 13.34           C  
ANISOU 4115  C   GLY A 270     1674   1616   1777    188     57     59       C  
ATOM   4116  O   GLY A 270       7.974  25.804 -18.803  1.00 14.00           O  
ANISOU 4116  O   GLY A 270     1747   1707   1865    192     52     75       O  
ATOM   4117  H   GLY A 270       9.118  25.952 -22.630  1.00 14.39           H  
ATOM   4118  HA2 GLY A 270       9.637  26.498 -20.628  1.00 13.36           H  
ATOM   4119  HA3 GLY A 270       8.523  27.617 -20.645  1.00 13.36           H  
ATOM   4120  N   GLN A 271       6.884  25.118 -20.652  1.00 11.72           N  
ANISOU 4120  N   GLN A 271     1485   1394   1575    181     60     47       N  
ATOM   4121  CA  GLN A 271       6.033  24.205 -19.917  1.00 11.20           C  
ANISOU 4121  CA  GLN A 271     1426   1312   1519    176     58     54       C  
ATOM   4122  C   GLN A 271       6.778  22.930 -19.557  1.00 11.55           C  
ANISOU 4122  C   GLN A 271     1475   1335   1580    193     67     64       C  
ATOM   4123  O   GLN A 271       7.718  22.501 -20.238  1.00 13.68           O  
ANISOU 4123  O   GLN A 271     1747   1595   1854    211     78     56       O  
ATOM   4124  CB  GLN A 271       4.780  23.871 -20.721  1.00 13.66           C  
ANISOU 4124  CB  GLN A 271     1752   1612   1825    158     56     39       C  
ATOM   4125  CG  GLN A 271       3.848  25.056 -20.841  1.00 14.15           C  
ANISOU 4125  CG  GLN A 271     1807   1696   1873    145     43     34       C  
ATOM   4126  CD  GLN A 271       2.489  24.671 -21.375  1.00 13.58           C  
ANISOU 4126  CD  GLN A 271     1744   1621   1796    126     38     23       C  
ATOM   4127  OE1 GLN A 271       2.378  23.879 -22.310  1.00 15.01           O  
ANISOU 4127  OE1 GLN A 271     1940   1786   1978    118     44     10       O  
ATOM   4128  NE2 GLN A 271       1.443  25.227 -20.777  1.00 13.47           N  
ANISOU 4128  NE2 GLN A 271     1717   1626   1774    118     27     26       N  
ATOM   4129  H   GLN A 271       6.720  25.155 -21.496  1.00 14.07           H  
ATOM   4130  HA  GLN A 271       5.755  24.630 -19.090  1.00 13.44           H  
ATOM   4131  HB2 GLN A 271       5.039  23.597 -21.615  1.00 16.39           H  
ATOM   4132  HB3 GLN A 271       4.301  23.151 -20.280  1.00 16.39           H  
ATOM   4133  HG2 GLN A 271       3.726  25.452 -19.964  1.00 16.98           H  
ATOM   4134  HG3 GLN A 271       4.237  25.705 -21.447  1.00 16.98           H  
ATOM   4135 HE21 GLN A 271       1.562  25.773 -20.124  1.00 16.16           H  
ATOM   4136 HE22 GLN A 271       0.647  25.041 -21.043  1.00 16.16           H  
ATOM   4137  N   ARG A 272       6.363  22.351 -18.441  1.00 12.88           N  
ANISOU 4137  N   ARG A 272     1644   1496   1755    190     62     82       N  
ATOM   4138  CA  ARG A 272       6.789  21.031 -18.029  1.00 12.64           C  
ANISOU 4138  CA  ARG A 272     1624   1437   1742    204     66     95       C  
ATOM   4139  C   ARG A 272       5.554  20.166 -17.831  1.00 13.97           C  
ANISOU 4139  C   ARG A 272     1812   1583   1913    180     62     98       C  
ATOM   4140  O   ARG A 272       4.476  20.655 -17.471  1.00 12.84           O  
ANISOU 4140  O   ARG A 272     1662   1460   1758    157     54     99       O  
ATOM   4141  CB  ARG A 272       7.600  21.061 -16.723  1.00 12.81           C  
ANISOU 4141  CB  ARG A 272     1628   1472   1766    219     61    123       C  
ATOM   4142  CG  ARG A 272       8.956  21.756 -16.811  1.00 14.49           C  
ANISOU 4142  CG  ARG A 272     1820   1709   1976    240     64    124       C  
ATOM   4143  CD  ARG A 272       8.829  23.262 -16.708  1.00 13.87           C  
ANISOU 4143  CD  ARG A 272     1726   1665   1879    224     57    118       C  
ATOM   4144  NE  ARG A 272       8.506  23.692 -15.354  1.00 14.32           N  
ANISOU 4144  NE  ARG A 272     1772   1742   1929    215     46    136       N  
ATOM   4145  CZ  ARG A 272       7.823  24.790 -15.051  1.00 15.15           C  
ANISOU 4145  CZ  ARG A 272     1871   1867   2017    198     37    128       C  
ATOM   4146  NH1 ARG A 272       7.336  25.583 -16.003  1.00 14.18           N  
ANISOU 4146  NH1 ARG A 272     1755   1745   1888    189     37    108       N  
ATOM   4147  NH2 ARG A 272       7.608  25.081 -13.781  1.00 17.53           N  
ANISOU 4147  NH2 ARG A 272     2163   2188   2310    192     29    142       N  
ATOM   4148  H   ARG A 272       5.816  22.720 -17.890  1.00 15.46           H  
ATOM   4149  HA  ARG A 272       7.357  20.646 -18.715  1.00 15.17           H  
ATOM   4150  HB2 ARG A 272       7.079  21.527 -16.050  1.00 15.37           H  
ATOM   4151  HB3 ARG A 272       7.761  20.146 -16.443  1.00 15.37           H  
ATOM   4152  HG2 ARG A 272       9.520  21.450 -16.083  1.00 17.39           H  
ATOM   4153  HG3 ARG A 272       9.369  21.544 -17.662  1.00 17.39           H  
ATOM   4154  HD2 ARG A 272       9.670  23.672 -16.964  1.00 16.64           H  
ATOM   4155  HD3 ARG A 272       8.120  23.564 -17.298  1.00 16.64           H  
ATOM   4156  HE  ARG A 272       8.779  23.199 -14.704  1.00 17.19           H  
ATOM   4157 HH11 ARG A 272       7.463  25.388 -16.831  1.00 17.02           H  
ATOM   4158 HH12 ARG A 272       6.896  26.290 -15.790  1.00 17.02           H  
ATOM   4159 HH21 ARG A 272       7.910  24.563 -13.164  1.00 21.04           H  
ATOM   4160 HH22 ARG A 272       7.167  25.788 -13.570  1.00 21.04           H  
ATOM   4161  N   TYR A 273       5.732  18.872 -18.056  1.00 13.09           N  
ANISOU 4161  N   TYR A 273     1723   1432   1818    188     66     99       N  
ATOM   4162  CA  TYR A 273       4.786  17.876 -17.591  1.00 12.62           C  
ANISOU 4162  CA  TYR A 273     1685   1348   1764    164     60    111       C  
ATOM   4163  C   TYR A 273       5.549  16.703 -17.005  1.00 12.95           C  
ANISOU 4163  C   TYR A 273     1742   1351   1826    185     60    133       C  
ATOM   4164  O   TYR A 273       6.472  16.186 -17.640  1.00 15.49           O  
ANISOU 4164  O   TYR A 273     2076   1648   2162    216     68    121       O  
ATOM   4165  CB  TYR A 273       3.896  17.353 -18.714  1.00 16.34           C  
ANISOU 4165  CB  TYR A 273     2180   1794   2233    140     62     86       C  
ATOM   4166  CG  TYR A 273       2.758  18.246 -19.104  1.00 16.16           C  
ANISOU 4166  CG  TYR A 273     2144   1806   2191    112     57     73       C  
ATOM   4167  CD1 TYR A 273       1.637  18.363 -18.304  1.00 16.36           C  
ANISOU 4167  CD1 TYR A 273     2158   1853   2206     83     48     88       C  
ATOM   4168  CD2 TYR A 273       2.787  18.945 -20.290  1.00 14.93           C  
ANISOU 4168  CD2 TYR A 273     1985   1663   2026    115     61     46       C  
ATOM   4169  CE1 TYR A 273       0.589  19.162 -18.670  1.00 14.57           C  
ANISOU 4169  CE1 TYR A 273     1916   1658   1962     63     43     75       C  
ATOM   4170  CE2 TYR A 273       1.745  19.749 -20.663  1.00 15.49           C  
ANISOU 4170  CE2 TYR A 273     2043   1762   2078     93     54     37       C  
ATOM   4171  CZ  TYR A 273       0.645  19.848 -19.850  1.00 14.06           C  
ANISOU 4171  CZ  TYR A 273     1850   1602   1890     69     45     50       C  
ATOM   4172  OH  TYR A 273      -0.415  20.637 -20.204  1.00 15.98           O  
ANISOU 4172  OH  TYR A 273     2079   1878   2117     53     37     40       O  
ATOM   4173  H   TYR A 273       6.404  18.545 -18.482  1.00 15.70           H  
ATOM   4174  HA  TYR A 273       4.227  18.284 -16.911  1.00 15.15           H  
ATOM   4175  HB2 TYR A 273       4.445  17.224 -19.503  1.00 19.60           H  
ATOM   4176  HB3 TYR A 273       3.515  16.507 -18.432  1.00 19.60           H  
ATOM   4177  HD1 TYR A 273       1.595  17.891 -17.504  1.00 19.64           H  
ATOM   4178  HD2 TYR A 273       3.528  18.870 -20.848  1.00 17.92           H  
ATOM   4179  HE1 TYR A 273      -0.156  19.237 -18.119  1.00 17.48           H  
ATOM   4180  HE2 TYR A 273       1.782  20.224 -21.462  1.00 18.58           H  
ATOM   4181  HH  TYR A 273      -0.151  21.273 -20.686  1.00 19.18           H  
ATOM   4182  N   ASP A 274       5.143  16.265 -15.821  1.00 12.79           N  
ANISOU 4182  N   ASP A 274     1724   1330   1807    170     50    164       N  
ATOM   4183  CA  ASP A 274       5.573  14.980 -15.292  1.00 13.96           C  
ANISOU 4183  CA  ASP A 274     1896   1433   1974    182     45    188       C  
ATOM   4184  C   ASP A 274       4.566  13.929 -15.733  1.00 15.53           C  
ANISOU 4184  C   ASP A 274     2133   1589   2180    150     42    182       C  
ATOM   4185  O   ASP A 274       3.361  14.095 -15.510  1.00 15.53           O  
ANISOU 4185  O   ASP A 274     2130   1608   2164    107     37    185       O  
ATOM   4186  CB  ASP A 274       5.654  15.003 -13.768  1.00 13.83           C  
ANISOU 4186  CB  ASP A 274     1865   1438   1953    177     34    229       C  
ATOM   4187  CG  ASP A 274       6.810  15.833 -13.254  1.00 17.54           C  
ANISOU 4187  CG  ASP A 274     2302   1944   2417    210     35    238       C  
ATOM   4188  OD1 ASP A 274       6.800  17.072 -13.420  1.00 20.59           O  
ANISOU 4188  OD1 ASP A 274     2663   2374   2788    207     38    221       O  
ATOM   4189  OD2 ASP A 274       7.725  15.233 -12.661  1.00 19.56           O  
ANISOU 4189  OD2 ASP A 274     2559   2185   2686    237     30    263       O  
ATOM   4190  H   ASP A 274       4.614  16.699 -15.301  1.00 15.35           H  
ATOM   4191  HA  ASP A 274       6.456  14.765 -15.630  1.00 16.75           H  
ATOM   4192  HB2 ASP A 274       4.834  15.380 -13.414  1.00 16.60           H  
ATOM   4193  HB3 ASP A 274       5.769  14.096 -13.445  1.00 16.60           H  
ATOM   4194  N   VAL A 275       5.049  12.860 -16.364  1.00 16.09           N  
ANISOU 4194  N   VAL A 275     2239   1604   2272    170     45    172       N  
ATOM   4195  CA  VAL A 275       4.171  11.787 -16.807  1.00 16.70           C  
ANISOU 4195  CA  VAL A 275     2358   1631   2356    137     41    165       C  
ATOM   4196  C   VAL A 275       4.682  10.447 -16.306  1.00 15.95           C  
ANISOU 4196  C   VAL A 275     2301   1473   2287    154     33    189       C  
ATOM   4197  O   VAL A 275       5.874  10.263 -16.047  1.00 17.52           O  
ANISOU 4197  O   VAL A 275     2495   1659   2501    204     35    199       O  
ATOM   4198  CB  VAL A 275       4.008  11.745 -18.350  1.00 16.56           C  
ANISOU 4198  CB  VAL A 275     2357   1597   2337    136     52    117       C  
ATOM   4199  CG1 VAL A 275       3.464  13.070 -18.857  1.00 17.54           C  
ANISOU 4199  CG1 VAL A 275     2447   1782   2437    119     56     97       C  
ATOM   4200  CG2 VAL A 275       5.322  11.374 -19.070  1.00 16.99           C  
ANISOU 4200  CG2 VAL A 275     2424   1622   2410    192     63     95       C  
ATOM   4201  H   VAL A 275       5.881  12.738 -16.544  1.00 19.31           H  
ATOM   4202  HA  VAL A 275       3.301  11.944 -16.408  1.00 20.04           H  
ATOM   4203  HB  VAL A 275       3.372  11.044 -18.564  1.00 19.87           H  
ATOM   4204 HG11 VAL A 275       3.268  12.990 -19.803  1.00 21.05           H  
ATOM   4205 HG12 VAL A 275       2.654  13.286 -18.369  1.00 21.05           H  
ATOM   4206 HG13 VAL A 275       4.130  13.760 -18.714  1.00 21.05           H  
ATOM   4207 HG21 VAL A 275       5.187  11.439 -20.028  1.00 20.39           H  
ATOM   4208 HG22 VAL A 275       6.019  11.989 -18.792  1.00 20.39           H  
ATOM   4209 HG23 VAL A 275       5.568  10.467 -18.831  1.00 20.39           H  
ATOM   4210  N   VAL A 276       3.758   9.506 -16.165  1.00 16.52           N  
ANISOU 4210  N   VAL A 276     2410   1506   2363    112     23    201       N  
ATOM   4211  CA  VAL A 276       4.088   8.129 -15.836  1.00 16.84           C  
ANISOU 4211  CA  VAL A 276     2497   1472   2428    122     12    222       C  
ATOM   4212  C   VAL A 276       3.810   7.284 -17.066  1.00 20.64           C  
ANISOU 4212  C   VAL A 276     3027   1894   2922    114     16    183       C  
ATOM   4213  O   VAL A 276       2.734   7.380 -17.670  1.00 20.32           O  
ANISOU 4213  O   VAL A 276     2993   1863   2866     65     16    162       O  
ATOM   4214  CB  VAL A 276       3.301   7.614 -14.619  1.00 20.57           C  
ANISOU 4214  CB  VAL A 276     2980   1940   2894     75     -5    271       C  
ATOM   4215  CG1 VAL A 276       3.609   6.129 -14.370  1.00 20.33           C  
ANISOU 4215  CG1 VAL A 276     3009   1824   2893     82    -19    294       C  
ATOM   4216  CG2 VAL A 276       3.646   8.451 -13.401  1.00 17.04           C  
ANISOU 4216  CG2 VAL A 276     2486   1555   2432     85     -8    306       C  
ATOM   4217  H   VAL A 276       2.915   9.648 -16.258  1.00 19.83           H  
ATOM   4218  HA  VAL A 276       5.031   8.069 -15.618  1.00 20.20           H  
ATOM   4219  HB  VAL A 276       2.349   7.693 -14.788  1.00 24.68           H  
ATOM   4220 HG11 VAL A 276       2.775   5.651 -14.242  1.00 24.40           H  
ATOM   4221 HG12 VAL A 276       4.081   5.772 -15.138  1.00 24.40           H  
ATOM   4222 HG13 VAL A 276       4.161   6.050 -13.576  1.00 24.40           H  
ATOM   4223 HG21 VAL A 276       2.941   8.356 -12.742  1.00 20.44           H  
ATOM   4224 HG22 VAL A 276       4.488   8.139 -13.032  1.00 20.44           H  
ATOM   4225 HG23 VAL A 276       3.726   9.380 -13.668  1.00 20.44           H  
ATOM   4226  N   ILE A 277       4.791   6.473 -17.439  1.00 18.94           N  
ANISOU 4226  N   ILE A 277     2844   1620   2734    165     18    171       N  
ATOM   4227  CA  ILE A 277       4.692   5.560 -18.566  1.00 16.21           C  
ANISOU 4227  CA  ILE A 277     2550   1208   2401    167     21    131       C  
ATOM   4228  C   ILE A 277       4.814   4.141 -18.033  1.00 20.79           C  
ANISOU 4228  C   ILE A 277     3188   1702   3009    171      4    158       C  
ATOM   4229  O   ILE A 277       5.776   3.822 -17.324  1.00 22.37           O  
ANISOU 4229  O   ILE A 277     3388   1882   3229    221     -1    187       O  
ATOM   4230  CB  ILE A 277       5.774   5.855 -19.620  1.00 18.50           C  
ANISOU 4230  CB  ILE A 277     2830   1504   2697    229     42     86       C  
ATOM   4231  CG1 ILE A 277       5.476   7.194 -20.299  1.00 21.30           C  
ANISOU 4231  CG1 ILE A 277     3136   1935   3021    212     55     58       C  
ATOM   4232  CG2 ILE A 277       5.831   4.741 -20.649  1.00 25.08           C  
ANISOU 4232  CG2 ILE A 277     3722   2260   3546    240     45     44       C  
ATOM   4233  CD1 ILE A 277       6.645   7.790 -21.038  1.00 21.49           C  
ANISOU 4233  CD1 ILE A 277     3132   1988   3044    270     75     28       C  
ATOM   4234  H   ILE A 277       5.550   6.436 -17.038  1.00 22.73           H  
ATOM   4235  HA  ILE A 277       3.823   5.649 -18.989  1.00 19.45           H  
ATOM   4236  HB  ILE A 277       6.636   5.907 -19.179  1.00 22.21           H  
ATOM   4237 HG12 ILE A 277       4.760   7.063 -20.939  1.00 25.56           H  
ATOM   4238 HG13 ILE A 277       5.203   7.831 -19.620  1.00 25.56           H  
ATOM   4239 HG21 ILE A 277       6.501   4.960 -21.315  1.00 30.09           H  
ATOM   4240 HG22 ILE A 277       6.067   3.912 -20.204  1.00 30.09           H  
ATOM   4241 HG23 ILE A 277       4.961   4.655 -21.070  1.00 30.09           H  
ATOM   4242 HD11 ILE A 277       6.357   8.605 -21.479  1.00 25.78           H  
ATOM   4243 HD12 ILE A 277       7.352   7.989 -20.404  1.00 25.78           H  
ATOM   4244 HD13 ILE A 277       6.961   7.152 -21.696  1.00 25.78           H  
ATOM   4245  N   GLU A 278       3.844   3.293 -18.377  1.00 21.55           N  
ANISOU 4245  N   GLU A 278     3336   1746   3107    117     -6    150       N  
ATOM   4246  CA AGLU A 278       3.882   1.886 -18.000  0.52 24.97           C  
ANISOU 4246  CA AGLU A 278     3834   2085   3567    114    -24    172       C  
ATOM   4247  CA BGLU A 278       3.860   1.881 -18.011  0.48 25.64           C  
ANISOU 4247  CA BGLU A 278     3920   2170   3651    113    -24    172       C  
ATOM   4248  C   GLU A 278       4.463   1.079 -19.156  1.00 25.74           C  
ANISOU 4248  C   GLU A 278     3983   2110   3687    158    -16    120       C  
ATOM   4249  O   GLU A 278       3.954   1.136 -20.281  1.00 25.23           O  
ANISOU 4249  O   GLU A 278     3931   2045   3609    132     -7     71       O  
ATOM   4250  CB AGLU A 278       2.493   1.368 -17.631  0.52 43.12           C  
ANISOU 4250  CB AGLU A 278     6163   4367   5854     24    -42    197       C  
ATOM   4251  CB BGLU A 278       2.450   1.361 -17.732  0.48 17.49           C  
ANISOU 4251  CB BGLU A 278     2919   1120   2607     22    -41    193       C  
ATOM   4252  CG AGLU A 278       2.484  -0.120 -17.324  0.52 30.62           C  
ANISOU 4252  CG AGLU A 278     4658   2679   4299     14    -63    220       C  
ATOM   4253  CG BGLU A 278       1.765   1.976 -16.544  0.48 25.51           C  
ANISOU 4253  CG BGLU A 278     3891   2203   3600    -25    -49    244       C  
ATOM   4254  CD AGLU A 278       1.524  -0.486 -16.215  0.52 36.47           C  
ANISOU 4254  CD AGLU A 278     5409   3421   5029    -60    -84    279       C  
ATOM   4255  CD BGLU A 278       0.502   1.235 -16.157  0.48 37.46           C  
ANISOU 4255  CD BGLU A 278     5439   3690   5103   -112    -68    272       C  
ATOM   4256  OE1AGLU A 278       0.677  -1.376 -16.436  0.52 52.24           O  
ANISOU 4256  OE1AGLU A 278     7460   5363   7028   -122    -98    279       O  
ATOM   4257  OE1BGLU A 278       0.155   0.244 -16.836  0.48 37.36           O  
ANISOU 4257  OE1BGLU A 278     5488   3603   5103   -138    -76    251       O  
ATOM   4258  OE2AGLU A 278       1.621   0.111 -15.123  0.52 66.37           O  
ANISOU 4258  OE2AGLU A 278     9149   7266   8803    -60    -86    325       O  
ATOM   4259  OE2BGLU A 278      -0.140   1.645 -15.168  0.48 38.00           O  
ANISOU 4259  OE2BGLU A 278     5473   3816   5150   -156    -74    314       O  
ATOM   4260  H  AGLU A 278       3.150   3.516 -18.834  0.52 25.86           H  
ATOM   4261  H  BGLU A 278       3.152   3.520 -18.834  0.48 25.86           H  
ATOM   4262  HA AGLU A 278       4.456   1.780 -17.226  0.52 29.96           H  
ATOM   4263  HA BGLU A 278       4.397   1.777 -17.210  0.48 30.76           H  
ATOM   4264  HB2AGLU A 278       2.179   1.839 -16.844  0.52 51.74           H  
ATOM   4265  HB2BGLU A 278       1.898   1.538 -18.509  0.48 20.99           H  
ATOM   4266  HB3AGLU A 278       1.889   1.525 -18.374  0.52 51.74           H  
ATOM   4267  HB3BGLU A 278       2.503   0.405 -17.573  0.48 20.99           H  
ATOM   4268  HG2AGLU A 278       2.221  -0.605 -18.121  0.52 36.75           H  
ATOM   4269  HG2BGLU A 278       2.369   1.959 -15.785  0.48 30.62           H  
ATOM   4270  HG3AGLU A 278       3.375  -0.391 -17.050  0.52 36.75           H  
ATOM   4271  HG3BGLU A 278       1.524   2.892 -16.756  0.48 30.62           H  
ATOM   4272  N   ALA A 279       5.525   0.324 -18.876  1.00 24.98           N  
ANISOU 4272  N   ALA A 279     3915   1954   3623    224    -21    131       N  
ATOM   4273  CA  ALA A 279       6.196  -0.475 -19.905  1.00 25.27           C  
ANISOU 4273  CA  ALA A 279     3977   1943   3683    272    -12     78       C  
ATOM   4274  C   ALA A 279       5.501  -1.831 -20.048  1.00 24.94           C  
ANISOU 4274  C   ALA A 279     3993   1825   3658    225    -29     75       C  
ATOM   4275  O   ALA A 279       6.061  -2.897 -19.783  1.00 30.15           O  
ANISOU 4275  O   ALA A 279     4675   2430   4352    258    -38     86       O  
ATOM   4276  CB  ALA A 279       7.672  -0.640 -19.566  1.00 30.48           C  
ANISOU 4276  CB  ALA A 279     4606   2606   4369    360     -9     87       C  
ATOM   4277  H   ALA A 279       5.878   0.257 -18.094  1.00 29.98           H  
ATOM   4278  HA  ALA A 279       6.123  -0.009 -20.753  1.00 30.33           H  
ATOM   4279  HB1 ALA A 279       7.776  -1.397 -18.969  1.00 36.58           H  
ATOM   4280  HB2 ALA A 279       8.169  -0.793 -20.384  1.00 36.58           H  
ATOM   4281  HB3 ALA A 279       7.989   0.168 -19.132  1.00 36.58           H  
ATOM   4282  N   SER A 280       4.251  -1.771 -20.510  1.00 29.99           N  
ANISOU 4282  N   SER A 280     4657   2464   4274    147    -32     60       N  
ATOM   4283  CA  SER A 280       3.392  -2.945 -20.592  1.00 32.79           C  
ANISOU 4283  CA  SER A 280     5063   2757   4638     87    -49     61       C  
ATOM   4284  C   SER A 280       3.214  -3.465 -22.011  1.00 37.33           C  
ANISOU 4284  C   SER A 280     5671   3301   5214     82    -40     -8       C  
ATOM   4285  O   SER A 280       2.372  -4.341 -22.238  1.00 37.98           O  
ANISOU 4285  O   SER A 280     5796   3338   5297     22    -54    -14       O  
ATOM   4286  CB  SER A 280       2.014  -2.625 -20.008  1.00 35.98           C  
ANISOU 4286  CB  SER A 280     5469   3189   5014     -9    -63     99       C  
ATOM   4287  OG  SER A 280       1.428  -1.532 -20.699  1.00 35.11           O  
ANISOU 4287  OG  SER A 280     5336   3136   4870    -39    -51     68       O  
ATOM   4288  H   SER A 280       3.877  -1.047 -20.784  1.00 35.99           H  
ATOM   4289  HA  SER A 280       3.806  -3.648 -20.068  1.00 39.35           H  
ATOM   4290  HB2 SER A 280       1.441  -3.403 -20.100  1.00 43.18           H  
ATOM   4291  HB3 SER A 280       2.112  -2.393 -19.072  1.00 43.18           H  
ATOM   4292  HG  SER A 280       1.756  -1.470 -21.470  1.00 42.14           H  
ATOM   4293  N   ARG A 281       3.945  -2.927 -22.975  1.00 25.84           N  
ANISOU 4293  N   ARG A 281     4195   1871   3752    137    -18    -61       N  
ATOM   4294  CA  ARG A 281       3.809  -3.372 -24.351  1.00 28.78           C  
ANISOU 4294  CA  ARG A 281     4595   2220   4120    133     -9   -129       C  
ATOM   4295  C   ARG A 281       4.863  -4.431 -24.655  1.00 40.83           C  
ANISOU 4295  C   ARG A 281     6142   3689   5683    202     -6   -155       C  
ATOM   4296  O   ARG A 281       5.738  -4.739 -23.838  1.00 27.09           O  
ANISOU 4296  O   ARG A 281     4389   1932   3971    257    -10   -120       O  
ATOM   4297  CB  ARG A 281       3.918  -2.193 -25.323  1.00 36.30           C  
ANISOU 4297  CB  ARG A 281     5514   3238   5039    146     15   -174       C  
ATOM   4298  CG  ARG A 281       3.025  -0.990 -24.972  1.00 46.64           C  
ANISOU 4298  CG  ARG A 281     6797   4610   6314     89     14   -147       C  
ATOM   4299  CD  ARG A 281       1.545  -1.358 -24.793  1.00 46.46           C  
ANISOU 4299  CD  ARG A 281     6803   4573   6276    -11     -7   -130       C  
ATOM   4300  NE  ARG A 281       0.706  -0.856 -25.883  1.00 86.43           N  
ANISOU 4300  NE  ARG A 281    11867   9669  11304    -63      0   -174       N  
ATOM   4301  CZ  ARG A 281      -0.017  -1.617 -26.703  1.00107.29           C  
ANISOU 4301  CZ  ARG A 281    14546  12282  13939   -113     -9   -209       C  
ATOM   4302  NH1 ARG A 281      -0.036  -2.938 -26.572  1.00 83.78           N  
ANISOU 4302  NH1 ARG A 281    11609   9236  10987   -120    -24   -207       N  
ATOM   4303  NH2 ARG A 281      -0.736  -1.045 -27.659  1.00 83.86           N  
ANISOU 4303  NH2 ARG A 281    11571   9356  10935   -158     -3   -246       N  
ATOM   4304  H   ARG A 281       4.526  -2.305 -22.855  1.00 31.01           H  
ATOM   4305  HA  ARG A 281       2.931  -3.765 -24.477  1.00 34.54           H  
ATOM   4306  HB2 ARG A 281       4.837  -1.883 -25.331  1.00 43.56           H  
ATOM   4307  HB3 ARG A 281       3.663  -2.498 -26.208  1.00 43.56           H  
ATOM   4308  HG2 ARG A 281       3.336  -0.601 -24.140  1.00 55.96           H  
ATOM   4309  HG3 ARG A 281       3.084  -0.337 -25.686  1.00 55.96           H  
ATOM   4310  HD2 ARG A 281       1.459  -2.324 -24.769  1.00 55.75           H  
ATOM   4311  HD3 ARG A 281       1.221  -0.975 -23.963  1.00 55.75           H  
ATOM   4312  HE  ARG A 281       0.678  -0.004 -26.002  1.00103.72           H  
ATOM   4313 HH11 ARG A 281       0.423  -3.315 -25.950  1.00100.53           H  
ATOM   4314 HH12 ARG A 281      -0.508  -3.417 -27.109  1.00100.53           H  
ATOM   4315 HH21 ARG A 281      -0.734  -0.190 -27.745  1.00100.63           H  
ATOM   4316 HH22 ARG A 281      -1.205  -1.530 -28.192  1.00100.63           H  
ATOM   4317  N   THR A 282       4.751  -5.006 -25.842  1.00 31.58           N  
ANISOU 4317  N   THR A 282     5002   2488   4510    199      1   -216       N  
ATOM   4318  CA  THR A 282       5.735  -5.968 -26.300  1.00 33.84           C  
ANISOU 4318  CA  THR A 282     5307   2722   4828    266      8   -251       C  
ATOM   4319  C   THR A 282       7.128  -5.357 -26.186  1.00 34.06           C  
ANISOU 4319  C   THR A 282     5283   2794   4866    357     27   -253       C  
ATOM   4320  O   THR A 282       7.347  -4.239 -26.674  1.00 35.70           O  
ANISOU 4320  O   THR A 282     5448   3072   5044    371     46   -274       O  
ATOM   4321  CB  THR A 282       5.455  -6.363 -27.750  1.00 54.47           C  
ANISOU 4321  CB  THR A 282     7950   5318   7427    251     18   -326       C  
ATOM   4322  OG1 THR A 282       4.110  -6.841 -27.860  1.00 43.39           O  
ANISOU 4322  OG1 THR A 282     6590   3885   6010    160     -1   -323       O  
ATOM   4323  CG2 THR A 282       6.426  -7.440 -28.205  1.00 47.27           C  
ANISOU 4323  CG2 THR A 282     7062   4348   6550    319     25   -364       C  
ATOM   4324  H   THR A 282       4.115  -4.857 -26.402  1.00 37.90           H  
ATOM   4325  HA  THR A 282       5.693  -6.770 -25.755  1.00 40.61           H  
ATOM   4326  HB  THR A 282       5.570  -5.593 -28.328  1.00 65.36           H  
ATOM   4327  HG1 THR A 282       3.592  -6.203 -28.034  1.00 52.07           H  
ATOM   4328 HG21 THR A 282       6.177  -8.295 -27.821  1.00 56.72           H  
ATOM   4329 HG22 THR A 282       6.410  -7.513 -29.173  1.00 56.72           H  
ATOM   4330 HG23 THR A 282       7.326  -7.217 -27.921  1.00 56.72           H  
ATOM   4331  N   PRO A 283       8.079  -6.037 -25.548  1.00 32.45           N  
ANISOU 4331  N   PRO A 283     5076   2553   4700    418     22   -230       N  
ATOM   4332  CA  PRO A 283       9.433  -5.480 -25.450  1.00 34.04           C  
ANISOU 4332  CA  PRO A 283     5223   2803   4909    503     39   -232       C  
ATOM   4333  C   PRO A 283       9.998  -5.171 -26.826  1.00 42.77           C  
ANISOU 4333  C   PRO A 283     6310   3942   5997    542     67   -305       C  
ATOM   4334  O   PRO A 283       9.979  -6.007 -27.733  1.00 33.47           O  
ANISOU 4334  O   PRO A 283     5170   2720   4828    546     73   -358       O  
ATOM   4335  CB  PRO A 283      10.222  -6.584 -24.740  1.00 39.01           C  
ANISOU 4335  CB  PRO A 283     5867   3370   5586    555     27   -204       C  
ATOM   4336  CG  PRO A 283       9.203  -7.292 -23.932  1.00 44.77           C  
ANISOU 4336  CG  PRO A 283     6644   4040   6325    488      0   -156       C  
ATOM   4337  CD  PRO A 283       7.940  -7.274 -24.757  1.00 36.67           C  
ANISOU 4337  CD  PRO A 283     5655   3007   5270    409     -1   -191       C  
ATOM   4338  HA  PRO A 283       9.438  -4.676 -24.907  1.00 40.85           H  
ATOM   4339  HB2 PRO A 283      10.627  -7.178 -25.393  1.00 46.81           H  
ATOM   4340  HB3 PRO A 283      10.908  -6.195 -24.176  1.00 46.81           H  
ATOM   4341  HG2 PRO A 283       9.492  -8.203 -23.766  1.00 53.72           H  
ATOM   4342  HG3 PRO A 283       9.071  -6.828 -23.091  1.00 53.72           H  
ATOM   4343  HD2 PRO A 283       7.891  -8.051 -25.334  1.00 44.00           H  
ATOM   4344  HD3 PRO A 283       7.155  -7.234 -24.188  1.00 44.00           H  
ATOM   4345  N   GLY A 284      10.496  -3.954 -26.972  1.00 39.99           N  
ANISOU 4345  N   GLY A 284     5902   3673   5619    567     85   -309       N  
ATOM   4346  CA  GLY A 284      11.036  -3.530 -28.239  1.00 31.32           C  
ANISOU 4346  CA  GLY A 284     4780   2620   4498    599    114   -373       C  
ATOM   4347  C   GLY A 284      11.555  -2.119 -28.136  1.00 25.70           C  
ANISOU 4347  C   GLY A 284     4005   2002   3760    621    131   -360       C  
ATOM   4348  O   GLY A 284      11.876  -1.631 -27.051  1.00 26.77           O  
ANISOU 4348  O   GLY A 284     4106   2162   3902    635    122   -305       O  
ATOM   4349  H   GLY A 284      10.531  -3.358 -26.353  1.00 47.99           H  
ATOM   4350  HA2 GLY A 284      11.765  -4.114 -28.500  1.00 37.58           H  
ATOM   4351  HA3 GLY A 284      10.346  -3.562 -28.920  1.00 37.58           H  
ATOM   4352  N   ASN A 285      11.630  -1.473 -29.288  1.00 30.15           N  
ANISOU 4352  N   ASN A 285     4550   2616   4289    621    156   -412       N  
ATOM   4353  CA  ASN A 285      12.085  -0.097 -29.393  1.00 32.50           C  
ANISOU 4353  CA  ASN A 285     4788   3004   4555    637    176   -406       C  
ATOM   4354  C   ASN A 285      10.963   0.738 -29.977  1.00 24.02           C  
ANISOU 4354  C   ASN A 285     3726   1960   3439    569    180   -419       C  
ATOM   4355  O   ASN A 285      10.347   0.348 -30.974  1.00 26.59           O  
ANISOU 4355  O   ASN A 285     4089   2264   3749    536    183   -467       O  
ATOM   4356  CB  ASN A 285      13.333  -0.008 -30.254  1.00 25.49           C  
ANISOU 4356  CB  ASN A 285     3862   2161   3662    702    205   -452       C  
ATOM   4357  CG  ASN A 285      14.479  -0.760 -29.655  1.00 37.03           C  
ANISOU 4357  CG  ASN A 285     5306   3600   5164    770    202   -437       C  
ATOM   4358  OD1 ASN A 285      14.964  -0.405 -28.583  1.00 30.94           O  
ANISOU 4358  OD1 ASN A 285     4499   2849   4406    792    191   -385       O  
ATOM   4359  ND2 ASN A 285      14.921  -1.812 -30.333  1.00 36.22           N  
ANISOU 4359  ND2 ASN A 285     5227   3454   5081    804    210   -484       N  
ATOM   4360  H   ASN A 285      11.416  -1.822 -30.044  1.00 36.18           H  
ATOM   4361  HA  ASN A 285      12.302   0.257 -28.516  1.00 39.00           H  
ATOM   4362  HB2 ASN A 285      13.146  -0.385 -31.128  1.00 30.59           H  
ATOM   4363  HB3 ASN A 285      13.594   0.922 -30.343  1.00 30.59           H  
ATOM   4364 HD21 ASN A 285      15.578  -2.275 -30.028  1.00 43.47           H  
ATOM   4365 HD22 ASN A 285      14.550  -2.030 -31.078  1.00 43.47           H  
ATOM   4366  N   TYR A 286      10.707   1.881 -29.360  1.00 22.10           N  
ANISOU 4366  N   TYR A 286     3451   1767   3179    549    180   -378       N  
ATOM   4367  CA  TYR A 286       9.566   2.712 -29.710  1.00 21.81           C  
ANISOU 4367  CA  TYR A 286     3424   1755   3106    483    182   -381       C  
ATOM   4368  C   TYR A 286      10.014   4.150 -29.891  1.00 18.90           C  
ANISOU 4368  C   TYR A 286     2992   1482   2710    493    202   -374       C  
ATOM   4369  O   TYR A 286      10.770   4.674 -29.067  1.00 25.19           O  
ANISOU 4369  O   TYR A 286     3740   2314   3516    528    202   -335       O  
ATOM   4370  CB  TYR A 286       8.492   2.603 -28.623  1.00 23.18           C  
ANISOU 4370  CB  TYR A 286     3624   1892   3291    426    155   -328       C  
ATOM   4371  CG  TYR A 286       7.888   1.218 -28.519  1.00 24.73           C  
ANISOU 4371  CG  TYR A 286     3879   2006   3512    396    132   -331       C  
ATOM   4372  CD1 TYR A 286       6.776   0.863 -29.278  1.00 29.67           C  
ANISOU 4372  CD1 TYR A 286     4547   2606   4119    330    125   -363       C  
ATOM   4373  CD2 TYR A 286       8.434   0.261 -27.675  1.00 20.66           C  
ANISOU 4373  CD2 TYR A 286     3374   1440   3037    430    116   -302       C  
ATOM   4374  CE1 TYR A 286       6.222  -0.403 -29.191  1.00 26.76           C  
ANISOU 4374  CE1 TYR A 286     4231   2164   3772    298    103   -365       C  
ATOM   4375  CE2 TYR A 286       7.886  -1.004 -27.580  1.00 24.27           C  
ANISOU 4375  CE2 TYR A 286     3884   1820   3516    400     95   -303       C  
ATOM   4376  CZ  TYR A 286       6.780  -1.333 -28.337  1.00 29.75           C  
ANISOU 4376  CZ  TYR A 286     4621   2490   4192    334     89   -335       C  
ATOM   4377  OH  TYR A 286       6.241  -2.599 -28.244  1.00 29.19           O  
ANISOU 4377  OH  TYR A 286     4604   2344   4144    301     69   -335       O  
ATOM   4378  H   TYR A 286      11.190   2.202 -28.725  1.00 26.52           H  
ATOM   4379  HA  TYR A 286       9.188   2.426 -30.556  1.00 26.17           H  
ATOM   4380  HB2 TYR A 286       8.890   2.820 -27.766  1.00 27.82           H  
ATOM   4381  HB3 TYR A 286       7.777   3.226 -28.825  1.00 27.82           H  
ATOM   4382  HD1 TYR A 286       6.399   1.488 -29.854  1.00 35.60           H  
ATOM   4383  HD2 TYR A 286       9.181   0.475 -27.164  1.00 24.80           H  
ATOM   4384  HE1 TYR A 286       5.479  -0.626 -29.704  1.00 32.11           H  
ATOM   4385  HE2 TYR A 286       8.261  -1.633 -27.007  1.00 29.12           H  
ATOM   4386  HH  TYR A 286       5.511  -2.632 -28.657  1.00 35.03           H  
ATOM   4387  N   TRP A 287       9.547   4.785 -30.966  1.00 23.64           N  
ANISOU 4387  N   TRP A 287     3581   2130   3272    454    213   -408       N  
ATOM   4388  CA  TRP A 287       9.873   6.182 -31.188  1.00 22.13           C  
ANISOU 4388  CA  TRP A 287     3322   2035   3052    450    225   -397       C  
ATOM   4389  C   TRP A 287       9.144   7.062 -30.181  1.00 22.88           C  
ANISOU 4389  C   TRP A 287     3385   2164   3145    402    204   -338       C  
ATOM   4390  O   TRP A 287       7.957   6.870 -29.903  1.00 19.98           O  
ANISOU 4390  O   TRP A 287     3043   1772   2776    344    184   -324       O  
ATOM   4391  CB  TRP A 287       9.473   6.660 -32.578  1.00 20.21           C  
ANISOU 4391  CB  TRP A 287     3077   1834   2766    416    238   -442       C  
ATOM   4392  CG  TRP A 287      10.165   6.066 -33.729  1.00 20.69           C  
ANISOU 4392  CG  TRP A 287     3160   1884   2817    457    263   -505       C  
ATOM   4393  CD1 TRP A 287       9.589   5.336 -34.718  1.00 20.26           C  
ANISOU 4393  CD1 TRP A 287     3158   1791   2748    433    265   -556       C  
ATOM   4394  CD2 TRP A 287      11.558   6.158 -34.050  1.00 20.99           C  
ANISOU 4394  CD2 TRP A 287     3166   1956   2853    528    290   -526       C  
ATOM   4395  NE1 TRP A 287      10.530   4.968 -35.644  1.00 23.06           N  
ANISOU 4395  NE1 TRP A 287     3517   2152   3092    486    294   -611       N  
ATOM   4396  CE2 TRP A 287      11.750   5.455 -35.253  1.00 27.08           C  
ANISOU 4396  CE2 TRP A 287     3973   2707   3609    546    310   -593       C  
ATOM   4397  CE3 TRP A 287      12.661   6.764 -33.438  1.00 21.72           C  
ANISOU 4397  CE3 TRP A 287     3201   2096   2954    576    300   -495       C  
ATOM   4398  CZ2 TRP A 287      12.998   5.334 -35.855  1.00 23.45           C  
ANISOU 4398  CZ2 TRP A 287     3482   2284   3144    607    336   -627       C  
ATOM   4399  CZ3 TRP A 287      13.901   6.645 -34.041  1.00 22.26           C  
ANISOU 4399  CZ3 TRP A 287     3247   2196   3016    640    329   -530       C  
ATOM   4400  CH2 TRP A 287      14.058   5.938 -35.238  1.00 24.62           C  
ANISOU 4400  CH2 TRP A 287     3572   2482   3300    653    346   -594       C  
ATOM   4401  H   TRP A 287       9.047   4.432 -31.571  1.00 28.37           H  
ATOM   4402  HA  TRP A 287      10.835   6.269 -31.096  1.00 26.56           H  
ATOM   4403  HB2 TRP A 287       8.528   6.475 -32.695  1.00 24.25           H  
ATOM   4404  HB3 TRP A 287       9.632   7.616 -32.620  1.00 24.25           H  
ATOM   4405  HD1 TRP A 287       8.686   5.118 -34.761  1.00 24.31           H  
ATOM   4406  HE1 TRP A 287      10.379   4.508 -36.355  1.00 27.67           H  
ATOM   4407  HE3 TRP A 287      12.563   7.236 -32.642  1.00 26.06           H  
ATOM   4408  HZ2 TRP A 287      13.108   4.859 -36.647  1.00 28.14           H  
ATOM   4409  HZ3 TRP A 287      14.642   7.041 -33.644  1.00 26.72           H  
ATOM   4410  HH2 TRP A 287      14.902   5.878 -35.623  1.00 29.54           H  
ATOM   4411  N   PHE A 288       9.859   8.042 -29.658  1.00 20.31           N  
ANISOU 4411  N   PHE A 288     3002   1899   2816    425    209   -308       N  
ATOM   4412  CA  PHE A 288       9.272   9.184 -28.970  1.00 19.42           C  
ANISOU 4412  CA  PHE A 288     2850   1838   2691    382    195   -264       C  
ATOM   4413  C   PHE A 288       9.354  10.353 -29.944  1.00 19.59           C  
ANISOU 4413  C   PHE A 288     2835   1932   2675    366    208   -283       C  
ATOM   4414  O   PHE A 288      10.443  10.879 -30.199  1.00 17.88           O  
ANISOU 4414  O   PHE A 288     2583   1760   2450    404    226   -289       O  
ATOM   4415  CB  PHE A 288      10.018   9.458 -27.671  1.00 17.66           C  
ANISOU 4415  CB  PHE A 288     2594   1628   2489    415    189   -216       C  
ATOM   4416  CG  PHE A 288       9.376  10.500 -26.804  1.00 16.39           C  
ANISOU 4416  CG  PHE A 288     2399   1510   2318    374    173   -173       C  
ATOM   4417  CD1 PHE A 288       9.725  11.835 -26.939  1.00 20.61           C  
ANISOU 4417  CD1 PHE A 288     2884   2116   2830    370    179   -165       C  
ATOM   4418  CD2 PHE A 288       8.439  10.151 -25.837  1.00 23.24           C  
ANISOU 4418  CD2 PHE A 288     3286   2347   3199    338    151   -140       C  
ATOM   4419  CE1 PHE A 288       9.147  12.810 -26.137  1.00 20.11           C  
ANISOU 4419  CE1 PHE A 288     2794   2089   2759    336    164   -128       C  
ATOM   4420  CE2 PHE A 288       7.861  11.127 -25.023  1.00 21.38           C  
ANISOU 4420  CE2 PHE A 288     3017   2155   2952    304    138   -103       C  
ATOM   4421  CZ  PHE A 288       8.219  12.454 -25.175  1.00 18.11           C  
ANISOU 4421  CZ  PHE A 288     2557   1808   2518    306    145    -99       C  
ATOM   4422  H   PHE A 288      10.718   8.070 -29.689  1.00 24.37           H  
ATOM   4423  HA  PHE A 288       8.344   9.026 -28.739  1.00 23.30           H  
ATOM   4424  HB2 PHE A 288      10.063   8.636 -27.159  1.00 21.20           H  
ATOM   4425  HB3 PHE A 288      10.913   9.765 -27.886  1.00 21.20           H  
ATOM   4426  HD1 PHE A 288      10.356  12.081 -27.576  1.00 24.73           H  
ATOM   4427  HD2 PHE A 288       8.195   9.260 -25.733  1.00 27.89           H  
ATOM   4428  HE1 PHE A 288       9.384  13.702 -26.248  1.00 24.14           H  
ATOM   4429  HE2 PHE A 288       7.235  10.885 -24.379  1.00 25.66           H  
ATOM   4430  HZ  PHE A 288       7.838  13.106 -24.632  1.00 21.74           H  
ATOM   4431  N   ASN A 289       8.205  10.750 -30.488  1.00 18.34           N  
ANISOU 4431  N   ASN A 289     2687   1789   2493    308    199   -291       N  
ATOM   4432  CA  ASN A 289       8.139  11.694 -31.588  1.00 18.30           C  
ANISOU 4432  CA  ASN A 289     2660   1843   2452    289    209   -313       C  
ATOM   4433  C   ASN A 289       7.748  13.096 -31.147  1.00 16.67           C  
ANISOU 4433  C   ASN A 289     2410   1694   2229    259    197   -275       C  
ATOM   4434  O   ASN A 289       6.869  13.276 -30.299  1.00 17.40           O  
ANISOU 4434  O   ASN A 289     2502   1778   2331    229    177   -244       O  
ATOM   4435  CB  ASN A 289       7.095  11.256 -32.611  1.00 20.13           C  
ANISOU 4435  CB  ASN A 289     2929   2056   2662    244    204   -348       C  
ATOM   4436  CG  ASN A 289       7.472  10.025 -33.385  1.00 22.10           C  
ANISOU 4436  CG  ASN A 289     3225   2257   2917    269    219   -399       C  
ATOM   4437  OD1 ASN A 289       7.080   8.907 -33.045  1.00 20.36           O  
ANISOU 4437  OD1 ASN A 289     3049   1968   2720    266    209   -405       O  
ATOM   4438  ND2 ASN A 289       8.217  10.232 -34.466  1.00 18.25           N  
ANISOU 4438  ND2 ASN A 289     2726   1803   2404    293    242   -436       N  
ATOM   4439  H   ASN A 289       7.434  10.475 -30.225  1.00 22.01           H  
ATOM   4440  HA  ASN A 289       9.029  11.727 -31.973  1.00 21.96           H  
ATOM   4441  HB2 ASN A 289       6.264  11.068 -32.147  1.00 24.15           H  
ATOM   4442  HB3 ASN A 289       6.963  11.975 -33.249  1.00 24.15           H  
ATOM   4443 HD21 ASN A 289       8.471  11.037 -34.632  1.00 21.90           H  
ATOM   4444  N   VAL A 290       8.353  14.083 -31.800  1.00 16.92           N  
ANISOU 4444  N   VAL A 290     2410   1783   2236    265    209   -281       N  
ATOM   4445  CA  VAL A 290       7.868  15.455 -31.814  1.00 15.87           C  
ANISOU 4445  CA  VAL A 290     2246   1702   2081    232    197   -257       C  
ATOM   4446  C   VAL A 290       7.163  15.694 -33.141  1.00 17.34           C  
ANISOU 4446  C   VAL A 290     2446   1910   2234    196    197   -286       C  
ATOM   4447  O   VAL A 290       7.684  15.350 -34.213  1.00 18.54           O  
ANISOU 4447  O   VAL A 290     2608   2068   2367    208    216   -323       O  
ATOM   4448  CB  VAL A 290       9.024  16.449 -31.604  1.00 15.29           C  
ANISOU 4448  CB  VAL A 290     2130   1679   2002    257    207   -238       C  
ATOM   4449  CG1 VAL A 290       8.701  17.821 -32.165  1.00 14.56           C  
ANISOU 4449  CG1 VAL A 290     2015   1639   1878    224    201   -229       C  
ATOM   4450  CG2 VAL A 290       9.364  16.549 -30.107  1.00 17.29           C  
ANISOU 4450  CG2 VAL A 290     2363   1922   2283    276    198   -199       C  
ATOM   4451  H   VAL A 290       9.072  13.974 -32.259  1.00 20.31           H  
ATOM   4452  HA  VAL A 290       7.225  15.585 -31.100  1.00 19.04           H  
ATOM   4453  HB  VAL A 290       9.797  16.118 -32.087  1.00 18.35           H  
ATOM   4454 HG11 VAL A 290       9.500  18.371 -32.134  1.00 17.47           H  
ATOM   4455 HG12 VAL A 290       8.401  17.725 -33.082  1.00 17.47           H  
ATOM   4456 HG13 VAL A 290       8.001  18.225 -31.628  1.00 17.47           H  
ATOM   4457 HG21 VAL A 290       9.998  17.272 -29.974  1.00 20.74           H  
ATOM   4458 HG22 VAL A 290       8.551  16.728 -29.609  1.00 20.74           H  
ATOM   4459 HG23 VAL A 290       9.753  15.710 -29.814  1.00 20.74           H  
ATOM   4460  N   THR A 291       5.970  16.274 -33.058  1.00 16.60           N  
ANISOU 4460  N   THR A 291     2351   1828   2129    152    176   -269       N  
ATOM   4461  CA  THR A 291       5.234  16.767 -34.204  1.00 17.41           C  
ANISOU 4461  CA  THR A 291     2457   1960   2197    116    170   -286       C  
ATOM   4462  C   THR A 291       4.747  18.179 -33.902  1.00 15.43           C  
ANISOU 4462  C   THR A 291     2176   1752   1935     95    152   -251       C  
ATOM   4463  O   THR A 291       4.761  18.647 -32.759  1.00 16.73           O  
ANISOU 4463  O   THR A 291     2321   1917   2120    104    143   -218       O  
ATOM   4464  CB  THR A 291       4.058  15.849 -34.563  1.00 19.15           C  
ANISOU 4464  CB  THR A 291     2713   2147   2415     81    159   -307       C  
ATOM   4465  OG1 THR A 291       3.196  15.677 -33.432  1.00 19.33           O  
ANISOU 4465  OG1 THR A 291     2737   2148   2461     63    140   -278       O  
ATOM   4466  CG2 THR A 291       4.563  14.491 -35.001  1.00 18.34           C  
ANISOU 4466  CG2 THR A 291     2649   1998   2322    101    176   -347       C  
ATOM   4467  H   THR A 291       5.555  16.394 -32.315  1.00 19.92           H  
ATOM   4468  HA  THR A 291       5.820  16.804 -34.976  1.00 20.89           H  
ATOM   4469  HB  THR A 291       3.557  16.252 -35.289  1.00 22.98           H  
ATOM   4470  HG1 THR A 291       3.622  15.331 -32.797  1.00 23.20           H  
ATOM   4471 HG21 THR A 291       3.864  14.014 -35.475  1.00 22.01           H  
ATOM   4472 HG22 THR A 291       5.328  14.595 -35.588  1.00 22.01           H  
ATOM   4473 HG23 THR A 291       4.829  13.971 -34.227  1.00 22.01           H  
ATOM   4474  N   PHE A 292       4.328  18.864 -34.957  1.00 14.09           N  
ANISOU 4474  N   PHE A 292     2004   1619   1733     69    147   -259       N  
ATOM   4475  CA  PHE A 292       3.876  20.243 -34.873  1.00 13.83           C  
ANISOU 4475  CA  PHE A 292     1946   1624   1686     52    129   -229       C  
ATOM   4476  C   PHE A 292       2.460  20.340 -35.416  1.00 17.61           C  
ANISOU 4476  C   PHE A 292     2434   2112   2147     13    107   -233       C  
ATOM   4477  O   PHE A 292       2.113  19.669 -36.393  1.00 18.82           O  
ANISOU 4477  O   PHE A 292     2610   2262   2281     -6    110   -263       O  
ATOM   4478  CB  PHE A 292       4.811  21.170 -35.643  1.00 16.42           C  
ANISOU 4478  CB  PHE A 292     2258   1993   1989     59    139   -228       C  
ATOM   4479  CG  PHE A 292       6.204  21.212 -35.091  1.00 13.79           C  
ANISOU 4479  CG  PHE A 292     1908   1663   1671     94    158   -221       C  
ATOM   4480  CD1 PHE A 292       6.518  22.043 -34.030  1.00 15.57           C  
ANISOU 4480  CD1 PHE A 292     2109   1895   1912    105    150   -186       C  
ATOM   4481  CD2 PHE A 292       7.197  20.406 -35.629  1.00 16.19           C  
ANISOU 4481  CD2 PHE A 292     2217   1963   1970    118    185   -250       C  
ATOM   4482  CE1 PHE A 292       7.807  22.080 -33.526  1.00 16.12           C  
ANISOU 4482  CE1 PHE A 292     2160   1971   1994    134    166   -179       C  
ATOM   4483  CE2 PHE A 292       8.488  20.424 -35.119  1.00 15.57           C  
ANISOU 4483  CE2 PHE A 292     2117   1893   1905    153    202   -243       C  
ATOM   4484  CZ  PHE A 292       8.798  21.268 -34.079  1.00 16.26           C  
ANISOU 4484  CZ  PHE A 292     2179   1990   2008    159    192   -206       C  
ATOM   4485  H   PHE A 292       4.297  18.539 -35.753  1.00 16.91           H  
ATOM   4486  HA  PHE A 292       3.863  20.537 -33.949  1.00 16.60           H  
ATOM   4487  HB2 PHE A 292       4.865  20.866 -36.562  1.00 19.71           H  
ATOM   4488  HB3 PHE A 292       4.452  22.071 -35.612  1.00 19.71           H  
ATOM   4489  HD1 PHE A 292       5.860  22.581 -33.653  1.00 18.69           H  
ATOM   4490  HD2 PHE A 292       6.995  19.846 -36.343  1.00 19.43           H  
ATOM   4491  HE1 PHE A 292       8.012  22.647 -32.818  1.00 19.34           H  
ATOM   4492  HE2 PHE A 292       9.140  19.867 -35.479  1.00 18.68           H  
ATOM   4493  HZ  PHE A 292       9.665  21.298 -33.745  1.00 19.51           H  
ATOM   4494  N   GLY A 293       1.645  21.159 -34.753  1.00 16.19           N  
ANISOU 4494  N   GLY A 293     2236   1945   1972      2     86   -203       N  
ATOM   4495  CA  GLY A 293       0.278  21.402 -35.160  1.00 18.17           C  
ANISOU 4495  CA  GLY A 293     2486   2212   2205    -31     63   -201       C  
ATOM   4496  C   GLY A 293       0.026  22.868 -35.434  1.00 16.08           C  
ANISOU 4496  C   GLY A 293     2201   1986   1923    -34     45   -177       C  
ATOM   4497  O   GLY A 293       0.961  23.643 -35.671  1.00 15.90           O  
ANISOU 4497  O   GLY A 293     2170   1978   1892    -19     52   -168       O  
ATOM   4498  H   GLY A 293       1.872  21.593 -34.046  1.00 19.43           H  
ATOM   4499  HA2 GLY A 293       0.087  20.900 -35.968  1.00 21.80           H  
ATOM   4500  HA3 GLY A 293      -0.325  21.111 -34.458  1.00 21.80           H  
ATOM   4501  N   GLY A 294      -1.247  23.251 -35.424  1.00 16.78           N  
ANISOU 4501  N   GLY A 294     2280   2091   2005    -54     21   -166       N  
ATOM   4502  CA  GLY A 294      -1.614  24.652 -35.464  1.00 15.59           C  
ANISOU 4502  CA  GLY A 294     2111   1970   1844    -50      0   -140       C  
ATOM   4503  C   GLY A 294      -1.147  25.384 -36.694  1.00 14.25           C  
ANISOU 4503  C   GLY A 294     1946   1825   1643    -57     -2   -140       C  
ATOM   4504  O   GLY A 294      -0.897  26.591 -36.629  1.00 17.61           O  
ANISOU 4504  O   GLY A 294     2362   2264   2064    -47    -12   -116       O  
ATOM   4505  H   GLY A 294      -1.918  22.715 -35.394  1.00 20.14           H  
ATOM   4506  HA2 GLY A 294      -2.581  24.723 -35.425  1.00 18.71           H  
ATOM   4507  HA3 GLY A 294      -1.234  25.097 -34.690  1.00 18.71           H  
ATOM   4508  N   GLY A 295      -1.034  24.691 -37.824  1.00 15.83           N  
ANISOU 4508  N   GLY A 295     2164   2032   1819    -76      8   -166       N  
ATOM   4509  CA  GLY A 295      -0.579  25.346 -39.032  1.00 20.55           C  
ANISOU 4509  CA  GLY A 295     2767   2660   2381    -86      8   -166       C  
ATOM   4510  C   GLY A 295       0.834  25.855 -38.929  1.00 21.60           C  
ANISOU 4510  C   GLY A 295     2896   2794   2516    -67     26   -157       C  
ATOM   4511  O   GLY A 295       1.207  26.792 -39.642  1.00 20.05           O  
ANISOU 4511  O   GLY A 295     2699   2625   2295    -75     20   -142       O  
ATOM   4512  H   GLY A 295      -1.213  23.855 -37.912  1.00 19.00           H  
ATOM   4513  HA2 GLY A 295      -0.622  24.717 -39.769  1.00 24.66           H  
ATOM   4514  HA3 GLY A 295      -1.160  26.098 -39.224  1.00 24.66           H  
ATOM   4515  N   LEU A 296       1.627  25.266 -38.035  1.00 15.85           N  
ANISOU 4515  N   LEU A 296     2165   2039   1816    -43     48   -164       N  
ATOM   4516  CA  LEU A 296       3.009  25.656 -37.781  1.00 17.83           C  
ANISOU 4516  CA  LEU A 296     2408   2295   2073    -23     66   -156       C  
ATOM   4517  C   LEU A 296       3.118  27.068 -37.211  1.00 16.00           C  
ANISOU 4517  C   LEU A 296     2161   2071   1847    -18     48   -118       C  
ATOM   4518  O   LEU A 296       4.191  27.671 -37.258  1.00 21.11           O  
ANISOU 4518  O   LEU A 296     2801   2731   2488    -14     58   -106       O  
ATOM   4519  CB  LEU A 296       3.854  25.510 -39.056  1.00 15.51           C  
ANISOU 4519  CB  LEU A 296     2120   2028   1744    -32     86   -176       C  
ATOM   4520  CG  LEU A 296       3.699  24.129 -39.705  1.00 18.14           C  
ANISOU 4520  CG  LEU A 296     2474   2351   2069    -37    103   -219       C  
ATOM   4521  CD1 LEU A 296       4.542  24.015 -40.965  1.00 24.98           C  
ANISOU 4521  CD1 LEU A 296     3345   3251   2897    -44    124   -242       C  
ATOM   4522  CD2 LEU A 296       4.066  22.991 -38.746  1.00 22.42           C  
ANISOU 4522  CD2 LEU A 296     3020   2851   2648     -9    120   -235       C  
ATOM   4523  H   LEU A 296       1.371  24.608 -37.544  1.00 19.01           H  
ATOM   4524  HA  LEU A 296       3.381  25.063 -37.110  1.00 21.40           H  
ATOM   4525  HB2 LEU A 296       3.575  26.180 -39.699  1.00 18.61           H  
ATOM   4526  HB3 LEU A 296       4.789  25.635 -38.831  1.00 18.61           H  
ATOM   4527  HG  LEU A 296       2.762  24.033 -39.940  1.00 21.77           H  
ATOM   4528 HD11 LEU A 296       4.136  23.364 -41.559  1.00 29.98           H  
ATOM   4529 HD12 LEU A 296       4.579  24.882 -41.400  1.00 29.98           H  
ATOM   4530 HD13 LEU A 296       5.436  23.728 -40.722  1.00 29.98           H  
ATOM   4531 HD21 LEU A 296       5.000  23.074 -38.502  1.00 26.91           H  
ATOM   4532 HD22 LEU A 296       3.509  23.054 -37.954  1.00 26.91           H  
ATOM   4533 HD23 LEU A 296       3.914  22.143 -39.191  1.00 26.91           H  
ATOM   4534  N   LEU A 297       2.032  27.603 -36.644  1.00 15.39           N  
ANISOU 4534  N   LEU A 297     2079   1986   1781    -20     22   -100       N  
ATOM   4535  CA  LEU A 297       2.040  28.963 -36.119  1.00 13.66           C  
ANISOU 4535  CA  LEU A 297     1851   1770   1568    -13      3    -68       C  
ATOM   4536  C   LEU A 297       2.692  29.051 -34.756  1.00 15.34           C  
ANISOU 4536  C   LEU A 297     2053   1963   1812     10     11    -58       C  
ATOM   4537  O   LEU A 297       2.944  30.158 -34.272  1.00 15.15           O  
ANISOU 4537  O   LEU A 297     2024   1939   1792     16     -2    -36       O  
ATOM   4538  CB  LEU A 297       0.616  29.515 -36.040  1.00 12.99           C  
ANISOU 4538  CB  LEU A 297     1765   1689   1483    -17    -28    -56       C  
ATOM   4539  CG  LEU A 297      -0.010  29.783 -37.413  1.00 14.63           C  
ANISOU 4539  CG  LEU A 297     1982   1923   1656    -41    -44    -56       C  
ATOM   4540  CD1 LEU A 297      -1.509  30.006 -37.307  1.00 19.23           C  
ANISOU 4540  CD1 LEU A 297     2556   2512   2240    -42    -73    -49       C  
ATOM   4541  CD2 LEU A 297       0.669  30.973 -38.090  1.00 19.39           C  
ANISOU 4541  CD2 LEU A 297     2591   2540   2237    -49    -53    -32       C  
ATOM   4542  H   LEU A 297       1.281  27.195 -36.553  1.00 18.46           H  
ATOM   4543  HA  LEU A 297       2.535  29.529 -36.732  1.00 16.39           H  
ATOM   4544  HB2 LEU A 297       0.056  28.871 -35.579  1.00 15.59           H  
ATOM   4545  HB3 LEU A 297       0.631  30.352 -35.551  1.00 15.59           H  
ATOM   4546  HG  LEU A 297       0.127  29.001 -37.970  1.00 17.56           H  
ATOM   4547 HD11 LEU A 297      -1.831  30.394 -38.136  1.00 23.08           H  
ATOM   4548 HD12 LEU A 297      -1.945  29.153 -37.150  1.00 23.08           H  
ATOM   4549 HD13 LEU A 297      -1.687  30.609 -36.568  1.00 23.08           H  
ATOM   4550 HD21 LEU A 297       0.134  31.251 -38.849  1.00 23.27           H  
ATOM   4551 HD22 LEU A 297       0.741  31.700 -37.452  1.00 23.27           H  
ATOM   4552 HD23 LEU A 297       1.552  30.705 -38.387  1.00 23.27           H  
ATOM   4553  N   CYS A 298       2.977  27.924 -34.123  1.00 14.78           N  
ANISOU 4553  N   CYS A 298     1979   1874   1761     23     30    -75       N  
ATOM   4554  CA  CYS A 298       3.774  27.958 -32.906  1.00 15.63           C  
ANISOU 4554  CA  CYS A 298     2076   1969   1894     44     40    -65       C  
ATOM   4555  C   CYS A 298       4.972  27.033 -33.044  1.00 16.64           C  
ANISOU 4555  C   CYS A 298     2202   2094   2025     55     68    -81       C  
ATOM   4556  O   CYS A 298       5.412  26.403 -32.080  1.00 15.93           O  
ANISOU 4556  O   CYS A 298     2107   1988   1960     75     79    -82       O  
ATOM   4557  CB  CYS A 298       2.937  27.634 -31.671  1.00 15.17           C  
ANISOU 4557  CB  CYS A 298     2011   1891   1861     54     31    -60       C  
ATOM   4558  SG  CYS A 298       2.100  26.058 -31.590  1.00 15.30           S  
ANISOU 4558  SG  CYS A 298     2037   1889   1889     48     38    -82       S  
ATOM   4559  H   CYS A 298       2.723  27.142 -34.375  1.00 17.73           H  
ATOM   4560  HA  CYS A 298       4.113  28.858 -32.778  1.00 18.76           H  
ATOM   4561  HB2 CYS A 298       3.525  27.672 -30.900  1.00 18.20           H  
ATOM   4562  HB3 CYS A 298       2.249  28.314 -31.597  1.00 18.20           H  
ATOM   4563  N   GLY A 299       5.528  26.965 -34.249  1.00 14.31           N  
ANISOU 4563  N   GLY A 299     1913   1819   1704     45     81    -94       N  
ATOM   4564  CA  GLY A 299       6.776  26.262 -34.475  1.00 18.32           C  
ANISOU 4564  CA  GLY A 299     2416   2334   2211     60    109   -111       C  
ATOM   4565  C   GLY A 299       6.717  25.232 -35.581  1.00 14.19           C  
ANISOU 4565  C   GLY A 299     1909   1813   1670     56    126   -145       C  
ATOM   4566  O   GLY A 299       5.678  24.622 -35.844  1.00 14.83           O  
ANISOU 4566  O   GLY A 299     2006   1878   1751     45    118   -160       O  
ATOM   4567  H   GLY A 299       5.195  27.323 -34.956  1.00 17.17           H  
ATOM   4568  HA2 GLY A 299       7.463  26.907 -34.706  1.00 21.98           H  
ATOM   4569  HA3 GLY A 299       7.033  25.806 -33.658  1.00 21.98           H  
ATOM   4570  N   GLY A 300       7.858  25.042 -36.242  1.00 14.07           N  
ANISOU 4570  N   GLY A 300     1886   1821   1638     64    150   -160       N  
ATOM   4571  CA  GLY A 300       8.098  23.938 -37.146  1.00 15.51           C  
ANISOU 4571  CA  GLY A 300     2082   2005   1807     70    173   -199       C  
ATOM   4572  C   GLY A 300       9.590  23.681 -37.181  1.00 16.68           C  
ANISOU 4572  C   GLY A 300     2210   2173   1954     97    201   -208       C  
ATOM   4573  O   GLY A 300      10.387  24.450 -36.633  1.00 15.31           O  
ANISOU 4573  O   GLY A 300     2013   2020   1785    103    202   -182       O  
ATOM   4574  H   GLY A 300       8.537  25.567 -36.176  1.00 16.88           H  
ATOM   4575  HA2 GLY A 300       7.639  23.141 -36.837  1.00 18.61           H  
ATOM   4576  HA3 GLY A 300       7.786  24.157 -38.038  1.00 18.61           H  
ATOM   4577  N   SER A 301       9.973  22.598 -37.843  1.00 18.08           N  
ANISOU 4577  N   SER A 301     2398   2348   2123    114    225   -248       N  
ATOM   4578  CA  SER A 301      11.378  22.239 -37.869  1.00 16.85           C  
ANISOU 4578  CA  SER A 301     2220   2214   1968    147    254   -261       C  
ATOM   4579  C   SER A 301      11.780  21.747 -39.245  1.00 22.67           C  
ANISOU 4579  C   SER A 301     2965   2982   2668    147    280   -301       C  
ATOM   4580  O   SER A 301      10.984  21.128 -39.958  1.00 21.22           O  
ANISOU 4580  O   SER A 301     2810   2780   2472    134    278   -331       O  
ATOM   4581  CB  SER A 301      11.709  21.144 -36.849  1.00 18.22           C  
ANISOU 4581  CB  SER A 301     2396   2342   2183    191    263   -270       C  
ATOM   4582  OG  SER A 301      13.103  20.902 -36.796  1.00 19.20           O  
ANISOU 4582  OG  SER A 301     2493   2494   2309    227    288   -278       O  
ATOM   4583  H   SER A 301       9.448  22.070 -38.273  1.00 21.69           H  
ATOM   4584  HA  SER A 301      11.891  23.036 -37.666  1.00 20.22           H  
ATOM   4585  HB2 SER A 301      11.405  21.427 -35.973  1.00 21.86           H  
ATOM   4586  HB3 SER A 301      11.257  20.325 -37.108  1.00 21.86           H  
ATOM   4587  HG  SER A 301      13.380  20.994 -36.008  1.00 23.04           H  
ATOM   4588  N   ARG A 302      13.045  22.001 -39.591  1.00 16.17           N  
ANISOU 4588  N   ARG A 302     2112   2207   1827    161    304   -304       N  
ATOM   4589  CA  ARG A 302      13.633  21.459 -40.809  1.00 16.18           C  
ANISOU 4589  CA  ARG A 302     2112   2243   1792    169    334   -347       C  
ATOM   4590  C   ARG A 302      13.900  19.964 -40.703  1.00 19.46           C  
ANISOU 4590  C   ARG A 302     2543   2620   2231    218    355   -392       C  
ATOM   4591  O   ARG A 302      14.124  19.324 -41.734  1.00 24.16           O  
ANISOU 4591  O   ARG A 302     3150   3231   2798    227    378   -438       O  
ATOM   4592  CB  ARG A 302      14.919  22.222 -41.146  1.00 18.43           C  
ANISOU 4592  CB  ARG A 302     2355   2599   2049    168    353   -334       C  
ATOM   4593  CG  ARG A 302      14.668  23.701 -41.522  1.00 21.54           C  
ANISOU 4593  CG  ARG A 302     2741   3032   2411    113    333   -292       C  
ATOM   4594  CD  ARG A 302      15.972  24.518 -41.640  1.00 33.32           C  
ANISOU 4594  CD  ARG A 302     4190   4590   3880    106    349   -270       C  
ATOM   4595  NE  ARG A 302      15.793  25.896 -42.123  1.00117.18           N  
ANISOU 4595  NE  ARG A 302    14809  15246  14467     50    330   -232       N  
ATOM   4596  CZ  ARG A 302      15.889  27.016 -41.392  1.00150.23           C  
ANISOU 4596  CZ  ARG A 302    18984  19432  18665     27    306   -184       C  
ATOM   4597  NH1 ARG A 302      16.156  27.007 -40.085  1.00 31.11           N  
ANISOU 4597  NH1 ARG A 302     3884   4315   3620     52    298   -167       N  
ATOM   4598  NH2 ARG A 302      15.709  28.184 -41.996  1.00 65.06           N  
ANISOU 4598  NH2 ARG A 302     8202   8673   7844    -22    289   -153       N  
ATOM   4599  H   ARG A 302      13.585  22.488 -39.132  1.00 19.41           H  
ATOM   4600  HA  ARG A 302      13.022  21.589 -41.551  1.00 19.41           H  
ATOM   4601  HB2 ARG A 302      15.505  22.205 -40.373  1.00 22.12           H  
ATOM   4602  HB3 ARG A 302      15.351  21.791 -41.900  1.00 22.12           H  
ATOM   4603  HG2 ARG A 302      14.214  23.737 -42.378  1.00 25.85           H  
ATOM   4604  HG3 ARG A 302      14.118  24.113 -40.837  1.00 25.85           H  
ATOM   4605  HD2 ARG A 302      16.386  24.568 -40.764  1.00 39.98           H  
ATOM   4606  HD3 ARG A 302      16.565  24.066 -42.261  1.00 39.98           H  
ATOM   4607  HE  ARG A 302      15.609  25.993 -42.957  1.00140.61           H  
ATOM   4608 HH11 ARG A 302      16.276  26.260 -39.676  1.00 37.33           H  
ATOM   4609 HH12 ARG A 302      16.209  27.748 -39.652  1.00 37.33           H  
ATOM   4610 HH21 ARG A 302      15.535  28.210 -42.838  1.00 78.07           H  
ATOM   4611 HH22 ARG A 302      15.765  28.914 -41.546  1.00 78.07           H  
ATOM   4612  N   ASN A 303      13.868  19.395 -39.494  1.00 22.82           N  
ANISOU 4612  N   ASN A 303     2973   2993   2705    250    346   -381       N  
ATOM   4613  CA  ASN A 303      13.870  17.948 -39.328  1.00 20.70           C  
ANISOU 4613  CA  ASN A 303     2732   2671   2464    292    358   -420       C  
ATOM   4614  C   ASN A 303      12.421  17.491 -39.400  1.00 17.60           C  
ANISOU 4614  C   ASN A 303     2385   2224   2078    261    335   -429       C  
ATOM   4615  O   ASN A 303      11.634  17.831 -38.505  1.00 19.30           O  
ANISOU 4615  O   ASN A 303     2605   2411   2317    242    308   -393       O  
ATOM   4616  CB  ASN A 303      14.489  17.544 -38.000  1.00 21.14           C  
ANISOU 4616  CB  ASN A 303     2771   2695   2565    337    357   -399       C  
ATOM   4617  CG  ASN A 303      14.568  16.036 -37.836  1.00 23.03           C  
ANISOU 4617  CG  ASN A 303     3041   2874   2833    384    368   -436       C  
ATOM   4618  OD1 ASN A 303      13.879  15.289 -38.530  1.00 22.35           O  
ANISOU 4618  OD1 ASN A 303     2997   2755   2740    374    369   -474       O  
ATOM   4619  ND2 ASN A 303      15.400  15.583 -36.912  1.00 22.76           N  
ANISOU 4619  ND2 ASN A 303     2990   2825   2833    434    373   -425       N  
ATOM   4620  H   ASN A 303      13.846  19.831 -38.754  1.00 27.39           H  
ATOM   4621  HA  ASN A 303      14.388  17.528 -40.032  1.00 24.84           H  
ATOM   4622  HB2 ASN A 303      15.390  17.901 -37.948  1.00 25.36           H  
ATOM   4623  HB3 ASN A 303      13.949  17.899 -37.276  1.00 25.36           H  
ATOM   4624 HD21 ASN A 303      15.479  14.736 -36.782  1.00 27.31           H  
ATOM   4625 HD22 ASN A 303      15.862  16.135 -36.441  1.00 27.31           H  
ATOM   4626  N   PRO A 304      12.017  16.742 -40.429  1.00 20.04           N  
ANISOU 4626  N   PRO A 304     2726   2522   2364    254    345   -476       N  
ATOM   4627  CA  PRO A 304      10.592  16.398 -40.570  1.00 22.49           C  
ANISOU 4627  CA  PRO A 304     3078   2790   2677    215    321   -482       C  
ATOM   4628  C   PRO A 304      10.083  15.434 -39.514  1.00 21.60           C  
ANISOU 4628  C   PRO A 304     2993   2603   2613    231    307   -479       C  
ATOM   4629  O   PRO A 304       8.865  15.372 -39.297  1.00 25.99           O  
ANISOU 4629  O   PRO A 304     3571   3128   3174    194    282   -468       O  
ATOM   4630  CB  PRO A 304      10.521  15.768 -41.968  1.00 21.17           C  
ANISOU 4630  CB  PRO A 304     2937   2635   2471    207    339   -539       C  
ATOM   4631  CG  PRO A 304      11.883  15.172 -42.159  1.00 25.00           C  
ANISOU 4631  CG  PRO A 304     3409   3132   2957    263    374   -572       C  
ATOM   4632  CD  PRO A 304      12.842  16.136 -41.490  1.00 21.66           C  
ANISOU 4632  CD  PRO A 304     2933   2754   2542    281    379   -528       C  
ATOM   4633  HA  PRO A 304      10.055  17.206 -40.548  1.00 26.99           H  
ATOM   4634  HB2 PRO A 304       9.832  15.085 -41.994  1.00 25.40           H  
ATOM   4635  HB3 PRO A 304      10.338  16.449 -42.634  1.00 25.40           H  
ATOM   4636  HG2 PRO A 304      11.922  14.299 -41.740  1.00 30.00           H  
ATOM   4637  HG3 PRO A 304      12.077  15.094 -43.107  1.00 30.00           H  
ATOM   4638  HD2 PRO A 304      13.600  15.663 -41.112  1.00 25.99           H  
ATOM   4639  HD3 PRO A 304      13.150  16.809 -42.117  1.00 25.99           H  
ATOM   4640  N   TYR A 305      10.963  14.667 -38.871  1.00 21.75           N  
ANISOU 4640  N   TYR A 305     3010   2591   2663    284    322   -486       N  
ATOM   4641  CA  TYR A 305      10.561  13.625 -37.925  1.00 25.44           C  
ANISOU 4641  CA  TYR A 305     3509   2982   3175    302    310   -484       C  
ATOM   4642  C   TYR A 305      11.537  13.597 -36.757  1.00 22.24           C  
ANISOU 4642  C   TYR A 305     3075   2569   2805    350    314   -454       C  
ATOM   4643  O   TYR A 305      12.271  12.622 -36.555  1.00 21.92           O  
ANISOU 4643  O   TYR A 305     3046   2495   2789    402    329   -475       O  
ATOM   4644  CB  TYR A 305      10.487  12.260 -38.617  1.00 24.69           C  
ANISOU 4644  CB  TYR A 305     3462   2837   3081    319    323   -541       C  
ATOM   4645  CG  TYR A 305       9.538  12.218 -39.791  1.00 24.39           C  
ANISOU 4645  CG  TYR A 305     3454   2809   3005    268    318   -574       C  
ATOM   4646  CD1 TYR A 305       8.164  12.195 -39.596  1.00 33.89           C  
ANISOU 4646  CD1 TYR A 305     4681   3985   4211    215    289   -559       C  
ATOM   4647  CD2 TYR A 305      10.016  12.198 -41.093  1.00 34.52           C  
ANISOU 4647  CD2 TYR A 305     4737   4132   4246    272    342   -620       C  
ATOM   4648  CE1 TYR A 305       7.293  12.161 -40.663  1.00 32.31           C  
ANISOU 4648  CE1 TYR A 305     4504   3797   3974    167    282   -587       C  
ATOM   4649  CE2 TYR A 305       9.155  12.164 -42.165  1.00 33.15           C  
ANISOU 4649  CE2 TYR A 305     4591   3971   4035    224    336   -649       C  
ATOM   4650  CZ  TYR A 305       7.793  12.150 -41.944  1.00 39.14           C  
ANISOU 4650  CZ  TYR A 305     5372   4702   4798    172    305   -632       C  
ATOM   4651  OH  TYR A 305       6.927  12.113 -43.011  1.00 49.80           O  
ANISOU 4651  OH  TYR A 305     6746   6068   6108    122    297   -660       O  
ATOM   4652  H   TYR A 305      11.815  14.734 -38.969  1.00 26.10           H  
ATOM   4653  HA  TYR A 305       9.683  13.843 -37.575  1.00 30.53           H  
ATOM   4654  HB2 TYR A 305      11.371  12.028 -38.944  1.00 29.63           H  
ATOM   4655  HB3 TYR A 305      10.189  11.599 -37.973  1.00 29.63           H  
ATOM   4656  HD1 TYR A 305       7.826  12.202 -38.730  1.00 40.67           H  
ATOM   4657  HD2 TYR A 305      10.934  12.208 -41.244  1.00 41.42           H  
ATOM   4658  HE1 TYR A 305       6.375  12.147 -40.518  1.00 38.77           H  
ATOM   4659  HE2 TYR A 305       9.488  12.150 -43.033  1.00 39.79           H  
ATOM   4660  HH  TYR A 305       7.341  12.275 -43.723  1.00 59.76           H  
ATOM   4661  N   PRO A 306      11.562  14.656 -35.952  1.00 19.48           N  
ANISOU 4661  N   PRO A 306     2689   2250   2461    336    300   -404       N  
ATOM   4662  CA  PRO A 306      12.419  14.649 -34.759  1.00 21.71           C  
ANISOU 4662  CA  PRO A 306     2945   2528   2776    377    300   -372       C  
ATOM   4663  C   PRO A 306      11.944  13.592 -33.779  1.00 19.36           C  
ANISOU 4663  C   PRO A 306     2681   2156   2520    391    286   -363       C  
ATOM   4664  O   PRO A 306      10.742  13.436 -33.554  1.00 19.10           O  
ANISOU 4664  O   PRO A 306     2677   2090   2492    351    265   -355       O  
ATOM   4665  CB  PRO A 306      12.262  16.056 -34.175  1.00 19.64           C  
ANISOU 4665  CB  PRO A 306     2647   2310   2506    346    284   -324       C  
ATOM   4666  CG  PRO A 306      11.253  16.756 -35.006  1.00 20.53           C  
ANISOU 4666  CG  PRO A 306     2770   2444   2586    292    273   -328       C  
ATOM   4667  CD  PRO A 306      10.652  15.811 -35.997  1.00 20.54           C  
ANISOU 4667  CD  PRO A 306     2813   2416   2576    282    279   -374       C  
ATOM   4668  HA  PRO A 306      13.349  14.506 -34.997  1.00 26.06           H  
ATOM   4669  HB2 PRO A 306      11.961  15.992 -33.255  1.00 23.57           H  
ATOM   4670  HB3 PRO A 306      13.114  16.518 -34.213  1.00 23.57           H  
ATOM   4671  HG2 PRO A 306      10.560  17.103 -34.423  1.00 24.64           H  
ATOM   4672  HG3 PRO A 306      11.690  17.486 -35.473  1.00 24.64           H  
ATOM   4673  HD2 PRO A 306       9.755  15.556 -35.730  1.00 24.65           H  
ATOM   4674  HD3 PRO A 306      10.636  16.204 -36.883  1.00 24.65           H  
ATOM   4675  N   ALA A 307      12.892  12.869 -33.186  1.00 19.81           N  
ANISOU 4675  N   ALA A 307     2733   2189   2605    448    295   -363       N  
ATOM   4676  CA  ALA A 307      12.504  11.743 -32.352  1.00 20.23           C  
ANISOU 4676  CA  ALA A 307     2825   2166   2697    463    281   -356       C  
ATOM   4677  C   ALA A 307      13.637  11.316 -31.435  1.00 20.66           C  
ANISOU 4677  C   ALA A 307     2858   2209   2781    525    286   -336       C  
ATOM   4678  O   ALA A 307      14.813  11.591 -31.686  1.00 21.56           O  
ANISOU 4678  O   ALA A 307     2935   2370   2888    565    306   -344       O  
ATOM   4679  CB  ALA A 307      12.063  10.549 -33.211  1.00 20.62           C  
ANISOU 4679  CB  ALA A 307     2930   2158   2746    465    288   -406       C  
ATOM   4680  H   ALA A 307      13.738  13.009 -33.251  1.00 23.77           H  
ATOM   4681  HA  ALA A 307      11.775  12.039 -31.785  1.00 24.28           H  
ATOM   4682  HB1 ALA A 307      11.753   9.838 -32.627  1.00 24.74           H  
ATOM   4683  HB2 ALA A 307      11.345  10.831 -33.799  1.00 24.74           H  
ATOM   4684  HB3 ALA A 307      12.818  10.241 -33.735  1.00 24.74           H  
ATOM   4685  N   ALA A 308      13.244  10.617 -30.370  1.00 21.77           N  
ANISOU 4685  N   ALA A 308     3025   2291   2957    529    266   -309       N  
ATOM   4686  CA  ALA A 308      14.114   9.850 -29.494  1.00 18.35           C  
ANISOU 4686  CA  ALA A 308     2590   1825   2558    589    265   -292       C  
ATOM   4687  C   ALA A 308      13.664   8.391 -29.519  1.00 22.82           C  
ANISOU 4687  C   ALA A 308     3221   2299   3150    602    258   -314       C  
ATOM   4688  O   ALA A 308      12.648   8.041 -30.130  1.00 20.12           O  
ANISOU 4688  O   ALA A 308     2922   1923   2798    559    253   -339       O  
ATOM   4689  CB  ALA A 308      14.081  10.399 -28.065  1.00 18.10           C  
ANISOU 4689  CB  ALA A 308     2531   1807   2541    578    244   -232       C  
ATOM   4690  H   ALA A 308      12.422  10.574 -30.123  1.00 26.13           H  
ATOM   4691  HA  ALA A 308      15.031   9.901 -29.807  1.00 22.02           H  
ATOM   4692  HB1 ALA A 308      14.680   9.875 -27.511  1.00 21.73           H  
ATOM   4693  HB2 ALA A 308      14.366  11.326 -28.076  1.00 21.73           H  
ATOM   4694  HB3 ALA A 308      13.175  10.336 -27.723  1.00 21.73           H  
ATOM   4695  N   ILE A 309      14.432   7.532 -28.857  1.00 22.20           N  
ANISOU 4695  N   ILE A 309     3151   2179   3105    662    256   -304       N  
ATOM   4696  CA  ILE A 309      14.132   6.106 -28.803  1.00 20.33           C  
ANISOU 4696  CA  ILE A 309     2980   1847   2898    682    248   -321       C  
ATOM   4697  C   ILE A 309      13.903   5.714 -27.354  1.00 21.82           C  
ANISOU 4697  C   ILE A 309     3179   1993   3118    679    219   -263       C  
ATOM   4698  O   ILE A 309      14.698   6.065 -26.472  1.00 23.33           O  
ANISOU 4698  O   ILE A 309     3326   2218   3320    710    214   -224       O  
ATOM   4699  CB  ILE A 309      15.251   5.238 -29.411  1.00 27.04           C  
ANISOU 4699  CB  ILE A 309     3820   2692   3762    740    260   -361       C  
ATOM   4700  CG1 ILE A 309      15.434   5.534 -30.900  1.00 20.48           C  
ANISOU 4700  CG1 ILE A 309     2983   1902   2896    741    289   -421       C  
ATOM   4701  CG2 ILE A 309      14.938   3.752 -29.179  1.00 33.79           C  
ANISOU 4701  CG2 ILE A 309     4730   3454   4654    744    239   -367       C  
ATOM   4702  CD1 ILE A 309      16.630   4.816 -31.543  1.00 24.72           C  
ANISOU 4702  CD1 ILE A 309     3500   2449   3443    799    307   -462       C  
ATOM   4703  H   ILE A 309      15.141   7.757 -28.426  1.00 26.64           H  
ATOM   4704  HA  ILE A 309      13.319   5.951 -29.308  1.00 24.40           H  
ATOM   4705  HB  ILE A 309      16.085   5.459 -28.967  1.00 32.45           H  
ATOM   4706 HG12 ILE A 309      14.634   5.253 -31.372  1.00 24.58           H  
ATOM   4707 HG13 ILE A 309      15.568   6.488 -31.013  1.00 24.58           H  
ATOM   4708 HG21 ILE A 309      15.350   3.229 -29.885  1.00 40.55           H  
ATOM   4709 HG22 ILE A 309      15.295   3.484 -28.318  1.00 40.55           H  
ATOM   4710 HG23 ILE A 309      13.976   3.626 -29.192  1.00 40.55           H  
ATOM   4711 HD11 ILE A 309      16.316   4.293 -32.297  1.00 29.66           H  
ATOM   4712 HD12 ILE A 309      17.271   5.479 -31.844  1.00 29.66           H  
ATOM   4713 HD13 ILE A 309      17.040   4.234 -30.885  1.00 29.66           H  
ATOM   4714  N   PHE A 310      12.816   4.994 -27.115  1.00 23.08           N  
ANISOU 4714  N   PHE A 310     3397   2083   3290    636    200   -257       N  
ATOM   4715  CA  PHE A 310      12.557   4.342 -25.840  1.00 25.49           C  
ANISOU 4715  CA  PHE A 310     3722   2338   3626    629    171   -206       C  
ATOM   4716  C   PHE A 310      12.733   2.843 -26.034  1.00 25.01           C  
ANISOU 4716  C   PHE A 310     3704   2204   3597    649    159   -228       C  
ATOM   4717  O   PHE A 310      12.049   2.228 -26.863  1.00 24.82           O  
ANISOU 4717  O   PHE A 310     3727   2136   3569    619    160   -267       O  
ATOM   4718  CB  PHE A 310      11.166   4.677 -25.320  1.00 24.08           C  
ANISOU 4718  CB  PHE A 310     3560   2153   3436    550    153   -175       C  
ATOM   4719  CG  PHE A 310      11.082   6.012 -24.632  1.00 19.40           C  
ANISOU 4719  CG  PHE A 310     2904   1643   2823    522    149   -134       C  
ATOM   4720  CD1 PHE A 310      11.465   7.177 -25.280  1.00 21.29           C  
ANISOU 4720  CD1 PHE A 310     3094   1962   3035    523    167   -153       C  
ATOM   4721  CD2 PHE A 310      10.602   6.105 -23.339  1.00 22.95           C  
ANISOU 4721  CD2 PHE A 310     3349   2091   3282    493    127    -79       C  
ATOM   4722  CE1 PHE A 310      11.380   8.414 -24.646  1.00 21.07           C  
ANISOU 4722  CE1 PHE A 310     3013   2002   2990    498    162   -118       C  
ATOM   4723  CE2 PHE A 310      10.503   7.337 -22.703  1.00 22.76           C  
ANISOU 4723  CE2 PHE A 310     3270   2140   3238    469    124    -47       C  
ATOM   4724  CZ  PHE A 310      10.888   8.496 -23.364  1.00 23.24           C  
ANISOU 4724  CZ  PHE A 310     3284   2272   3273    472    141    -67       C  
ATOM   4725  H   PHE A 310      12.195   4.866 -27.696  1.00 27.70           H  
ATOM   4726  HA  PHE A 310      13.195   4.644 -25.175  1.00 30.59           H  
ATOM   4727  HB2 PHE A 310      10.548   4.691 -26.068  1.00 28.90           H  
ATOM   4728  HB3 PHE A 310      10.899   3.998 -24.682  1.00 28.90           H  
ATOM   4729  HD1 PHE A 310      11.784   7.131 -26.152  1.00 25.55           H  
ATOM   4730  HD2 PHE A 310      10.341   5.334 -22.889  1.00 27.55           H  
ATOM   4731  HE1 PHE A 310      11.656   9.184 -25.089  1.00 25.28           H  
ATOM   4732  HE2 PHE A 310      10.179   7.386 -21.833  1.00 27.31           H  
ATOM   4733  HZ  PHE A 310      10.813   9.322 -22.943  1.00 27.88           H  
ATOM   4734  N   HIS A 311      13.643   2.270 -25.254  1.00 22.00           N  
ANISOU 4734  N   HIS A 311     3305   1808   3246    697    147   -200       N  
ATOM   4735  CA  HIS A 311      14.114   0.901 -25.416  1.00 27.43           C  
ANISOU 4735  CA  HIS A 311     4022   2432   3967    733    140   -220       C  
ATOM   4736  C   HIS A 311      13.734   0.091 -24.186  1.00 28.40           C  
ANISOU 4736  C   HIS A 311     4177   2492   4122    717    107   -165       C  
ATOM   4737  O   HIS A 311      14.075   0.475 -23.062  1.00 27.99           O  
ANISOU 4737  O   HIS A 311     4093   2465   4075    728     94   -111       O  
ATOM   4738  CB  HIS A 311      15.631   0.896 -25.612  1.00 24.75           C  
ANISOU 4738  CB  HIS A 311     3632   2134   3639    808    155   -235       C  
ATOM   4739  CG  HIS A 311      16.256  -0.454 -25.473  1.00 29.67           C  
ANISOU 4739  CG  HIS A 311     4277   2694   4304    855    146   -242       C  
ATOM   4740  ND1 HIS A 311      16.213  -1.397 -26.475  1.00 34.58           N  
ANISOU 4740  ND1 HIS A 311     4938   3264   4937    866    156   -297       N  
ATOM   4741  CD2 HIS A 311      16.939  -1.022 -24.451  1.00 26.37           C  
ANISOU 4741  CD2 HIS A 311     3847   2253   3919    893    127   -199       C  
ATOM   4742  CE1 HIS A 311      16.839  -2.490 -26.077  1.00 31.65           C  
ANISOU 4742  CE1 HIS A 311     4580   2839   4606    911    146   -289       C  
ATOM   4743  NE2 HIS A 311      17.294  -2.288 -24.854  1.00 30.35           N  
ANISOU 4743  NE2 HIS A 311     4385   2691   4456    929    127   -229       N  
ATOM   4744  H   HIS A 311      14.017   2.675 -24.594  1.00 26.40           H  
ATOM   4745  HA  HIS A 311      13.686   0.492 -26.184  1.00 32.91           H  
ATOM   4746  HB2 HIS A 311      15.831   1.223 -26.503  1.00 29.71           H  
ATOM   4747  HB3 HIS A 311      16.033   1.477 -24.947  1.00 29.71           H  
ATOM   4748  HD1 HIS A 311      15.836  -1.291 -27.241  1.00 41.50           H  
ATOM   4749  HD2 HIS A 311      17.132  -0.630 -23.630  1.00 31.64           H  
ATOM   4750  HE1 HIS A 311      16.943  -3.270 -26.574  1.00 37.98           H  
ATOM   4751  HE2 HIS A 311      17.739  -2.855 -24.385  1.00 36.42           H  
ATOM   4752  N   TYR A 312      13.031  -1.022 -24.399  1.00 27.94           N  
ANISOU 4752  N   TYR A 312     4180   2353   4082    689     95   -178       N  
ATOM   4753  CA  TYR A 312      12.784  -1.968 -23.320  1.00 21.79           C  
ANISOU 4753  CA  TYR A 312     3435   1509   3336    678     66   -128       C  
ATOM   4754  C   TYR A 312      14.071  -2.711 -22.995  1.00 30.06           C  
ANISOU 4754  C   TYR A 312     4464   2538   4420    754     63   -122       C  
ATOM   4755  O   TYR A 312      14.707  -3.284 -23.885  1.00 30.32           O  
ANISOU 4755  O   TYR A 312     4502   2554   4466    798     79   -173       O  
ATOM   4756  CB  TYR A 312      11.701  -2.977 -23.704  1.00 25.74           C  
ANISOU 4756  CB  TYR A 312     4005   1929   3845    624     55   -145       C  
ATOM   4757  CG  TYR A 312      10.292  -2.473 -23.528  1.00 21.02           C  
ANISOU 4757  CG  TYR A 312     3431   1338   3220    538     46   -127       C  
ATOM   4758  CD1 TYR A 312       9.852  -1.354 -24.216  1.00 23.33           C  
ANISOU 4758  CD1 TYR A 312     3702   1690   3473    511     64   -154       C  
ATOM   4759  CD2 TYR A 312       9.392  -3.122 -22.684  1.00 26.03           C  
ANISOU 4759  CD2 TYR A 312     4105   1920   3865    483     21    -81       C  
ATOM   4760  CE1 TYR A 312       8.557  -0.877 -24.063  1.00 22.27           C  
ANISOU 4760  CE1 TYR A 312     3586   1563   3314    433     56   -137       C  
ATOM   4761  CE2 TYR A 312       8.089  -2.657 -22.530  1.00 28.37           C  
ANISOU 4761  CE2 TYR A 312     4417   2227   4134    401     13    -64       C  
ATOM   4762  CZ  TYR A 312       7.680  -1.532 -23.223  1.00 26.22           C  
ANISOU 4762  CZ  TYR A 312     4123   2014   3824    378     31    -93       C  
ATOM   4763  OH  TYR A 312       6.394  -1.057 -23.075  1.00 25.83           O  
ANISOU 4763  OH  TYR A 312     4087   1979   3748    298     23    -77       O  
ATOM   4764  H   TYR A 312      12.689  -1.249 -25.154  1.00 33.53           H  
ATOM   4765  HA  TYR A 312      12.475  -1.483 -22.539  1.00 26.15           H  
ATOM   4766  HB2 TYR A 312      11.814  -3.211 -24.639  1.00 30.88           H  
ATOM   4767  HB3 TYR A 312      11.802  -3.766 -23.150  1.00 30.88           H  
ATOM   4768  HD1 TYR A 312      10.435  -0.914 -24.792  1.00 28.00           H  
ATOM   4769  HD2 TYR A 312       9.667  -3.878 -22.217  1.00 31.24           H  
ATOM   4770  HE1 TYR A 312       8.282  -0.119 -24.525  1.00 26.73           H  
ATOM   4771  HE2 TYR A 312       7.498  -3.100 -21.965  1.00 34.04           H  
ATOM   4772  HH  TYR A 312       6.043  -1.386 -22.387  1.00 30.99           H  
ATOM   4773  N   ALA A 313      14.463  -2.693 -21.726  1.00 34.90           N  
ANISOU 4773  N   ALA A 313     5055   3157   5048    769     43    -60       N  
ATOM   4774  CA  ALA A 313      15.611  -3.472 -21.293  1.00 47.04           C  
ANISOU 4774  CA  ALA A 313     6578   4671   6622    837     35    -46       C  
ATOM   4775  C   ALA A 313      15.443  -4.931 -21.693  1.00 28.71           C  
ANISOU 4775  C   ALA A 313     4318   2254   4336    844     30    -69       C  
ATOM   4776  O   ALA A 313      14.383  -5.528 -21.486  1.00 31.30           O  
ANISOU 4776  O   ALA A 313     4702   2520   4669    787     15    -53       O  
ATOM   4777  CB  ALA A 313      15.780  -3.351 -19.781  1.00 26.86           C  
ANISOU 4777  CB  ALA A 313     4003   2126   4077    836      8     30       C  
ATOM   4778  H   ALA A 313      14.084  -2.240 -21.101  1.00 41.88           H  
ATOM   4779  HA  ALA A 313      16.415  -3.129 -21.716  1.00 56.44           H  
ATOM   4780  HB1 ALA A 313      16.376  -4.051 -19.473  1.00 32.23           H  
ATOM   4781  HB2 ALA A 313      16.156  -2.482 -19.574  1.00 32.23           H  
ATOM   4782  HB3 ALA A 313      14.912  -3.446 -19.358  1.00 32.23           H  
ATOM   4783  N   GLY A 314      16.497  -5.498 -22.279  1.00 31.51           N  
ANISOU 4783  N   GLY A 314     4662   2598   4713    914     44   -107       N  
ATOM   4784  CA  GLY A 314      16.485  -6.864 -22.739  1.00 36.19           C  
ANISOU 4784  CA  GLY A 314     5310   3100   5339    931     43   -136       C  
ATOM   4785  C   GLY A 314      16.072  -7.048 -24.182  1.00 39.68           C  
ANISOU 4785  C   GLY A 314     5783   3527   5766    916     66   -212       C  
ATOM   4786  O   GLY A 314      16.410  -8.075 -24.782  1.00 35.68           O  
ANISOU 4786  O   GLY A 314     5310   2961   5286    951     73   -252       O  
ATOM   4787  H   GLY A 314      17.243  -5.093 -22.419  1.00 37.81           H  
ATOM   4788  HA2 GLY A 314      17.376  -7.234 -22.637  1.00 43.42           H  
ATOM   4789  HA3 GLY A 314      15.868  -7.371 -22.188  1.00 43.42           H  
ATOM   4790  N   ALA A 315      15.346  -6.091 -24.756  1.00 32.41           N  
ANISOU 4790  N   ALA A 315     4853   2656   4803    865     78   -235       N  
ATOM   4791  CA  ALA A 315      14.959  -6.164 -26.151  1.00 39.27           C  
ANISOU 4791  CA  ALA A 315     5747   3521   5652    848    100   -307       C  
ATOM   4792  C   ALA A 315      16.182  -5.950 -27.036  1.00 30.23           C  
ANISOU 4792  C   ALA A 315     4557   2426   4502    920    131   -360       C  
ATOM   4793  O   ALA A 315      17.247  -5.542 -26.565  1.00 30.60           O  
ANISOU 4793  O   ALA A 315     4548   2524   4556    974    136   -338       O  
ATOM   4794  CB  ALA A 315      13.883  -5.126 -26.461  1.00 34.79           C  
ANISOU 4794  CB  ALA A 315     5178   3000   5039    776    102   -311       C  
ATOM   4795  H   ALA A 315      15.066  -5.386 -24.351  1.00 38.89           H  
ATOM   4796  HA  ALA A 315      14.591  -7.042 -26.339  1.00 47.12           H  
ATOM   4797  HB1 ALA A 315      13.576  -5.251 -27.373  1.00 41.74           H  
ATOM   4798  HB2 ALA A 315      13.143  -5.244 -25.844  1.00 41.74           H  
ATOM   4799  HB3 ALA A 315      14.261  -4.238 -26.358  1.00 41.74           H  
ATOM   4800  N   PRO A 316      16.058  -6.227 -28.331  1.00 35.67           N  
ANISOU 4800  N   PRO A 316     5269   3106   5178    918    153   -430       N  
ATOM   4801  CA  PRO A 316      17.168  -5.960 -29.253  1.00 38.24           C  
ANISOU 4801  CA  PRO A 316     5550   3488   5493    980    187   -482       C  
ATOM   4802  C   PRO A 316      17.479  -4.474 -29.365  1.00 62.48           C  
ANISOU 4802  C   PRO A 316     8552   6667   8521    976    204   -475       C  
ATOM   4803  O   PRO A 316      16.673  -3.609 -29.017  1.00 44.31           O  
ANISOU 4803  O   PRO A 316     6246   4395   6194    920    193   -445       O  
ATOM   4804  CB  PRO A 316      16.662  -6.513 -30.594  1.00 37.43           C  
ANISOU 4804  CB  PRO A 316     5493   3351   5377    959    203   -557       C  
ATOM   4805  CG  PRO A 316      15.568  -7.461 -30.241  1.00 42.74           C  
ANISOU 4805  CG  PRO A 316     6241   3928   6072    906    174   -541       C  
ATOM   4806  CD  PRO A 316      14.939  -6.926 -28.987  1.00 42.38           C  
ANISOU 4806  CD  PRO A 316     6188   3890   6025    861    146   -464       C  
ATOM   4807  HA  PRO A 316      17.962  -6.439 -28.967  1.00 45.89           H  
ATOM   4808  HB2 PRO A 316      16.328  -5.788 -31.144  1.00 44.91           H  
ATOM   4809  HB3 PRO A 316      17.383  -6.973 -31.053  1.00 44.91           H  
ATOM   4810  HG2 PRO A 316      14.920  -7.493 -30.962  1.00 51.29           H  
ATOM   4811  HG3 PRO A 316      15.939  -8.344 -30.088  1.00 51.29           H  
ATOM   4812  HD2 PRO A 316      14.219  -6.310 -29.195  1.00 50.86           H  
ATOM   4813  HD3 PRO A 316      14.607  -7.648 -28.430  1.00 50.86           H  
ATOM   4814  N   GLY A 317      18.676  -4.189 -29.876  1.00 36.95           N  
ANISOU 4814  N   GLY A 317     5264   3492   5281   1036    232   -504       N  
ATOM   4815  CA  GLY A 317      19.083  -2.836 -30.174  1.00 34.41           C  
ANISOU 4815  CA  GLY A 317     4878   3276   4918   1035    254   -505       C  
ATOM   4816  C   GLY A 317      18.535  -2.371 -31.511  1.00 30.10           C  
ANISOU 4816  C   GLY A 317     4344   2762   4330    998    278   -564       C  
ATOM   4817  O   GLY A 317      17.632  -2.965 -32.096  1.00 40.25           O  
ANISOU 4817  O   GLY A 317     5689   3992   5614    959    273   -597       O  
ATOM   4818  H   GLY A 317      19.274  -4.779 -30.059  1.00 44.34           H  
ATOM   4819  HA2 GLY A 317      18.758  -2.239 -29.481  1.00 41.29           H  
ATOM   4820  HA3 GLY A 317      20.052  -2.787 -30.203  1.00 41.29           H  
ATOM   4821  N   GLY A 318      19.105  -1.271 -31.999  1.00 34.18           N  
ANISOU 4821  N   GLY A 318     4803   3375   4810   1006    304   -575       N  
ATOM   4822  CA  GLY A 318      18.710  -0.719 -33.272  1.00 42.07           C  
ANISOU 4822  CA  GLY A 318     5804   4417   5764    974    329   -627       C  
ATOM   4823  C   GLY A 318      17.522   0.209 -33.137  1.00 41.85           C  
ANISOU 4823  C   GLY A 318     5790   4406   5704    902    315   -604       C  
ATOM   4824  O   GLY A 318      17.012   0.447 -32.040  1.00 34.37           O  
ANISOU 4824  O   GLY A 318     4849   3440   4771    878    288   -547       O  
ATOM   4825  H   GLY A 318      19.727  -0.830 -31.602  1.00 41.02           H  
ATOM   4826  HA2 GLY A 318      19.450  -0.220 -33.653  1.00 50.49           H  
ATOM   4827  HA3 GLY A 318      18.471  -1.439 -33.877  1.00 50.49           H  
ATOM   4828  N   PRO A 319      17.062   0.760 -34.253  1.00 35.00           N  
ANISOU 4828  N   PRO A 319     4927   3578   4793    867    334   -646       N  
ATOM   4829  CA  PRO A 319      15.986   1.752 -34.197  1.00 27.83           C  
ANISOU 4829  CA  PRO A 319     4026   2694   3852    802    323   -624       C  
ATOM   4830  C   PRO A 319      14.620   1.093 -34.180  1.00 36.42           C  
ANISOU 4830  C   PRO A 319     5186   3705   4948    745    297   -628       C  
ATOM   4831  O   PRO A 319      14.459  -0.044 -34.650  1.00 32.18           O  
ANISOU 4831  O   PRO A 319     4694   3105   4428    748    294   -667       O  
ATOM   4832  CB  PRO A 319      16.204   2.572 -35.478  1.00 30.06           C  
ANISOU 4832  CB  PRO A 319     4282   3057   4084    794    356   -670       C  
ATOM   4833  CG  PRO A 319      16.820   1.603 -36.427  1.00 32.06           C  
ANISOU 4833  CG  PRO A 319     4546   3292   4342    830    378   -731       C  
ATOM   4834  CD  PRO A 319      17.677   0.679 -35.593  1.00 37.35           C  
ANISOU 4834  CD  PRO A 319     5210   3916   5065    890    370   -711       C  
ATOM   4835  HA  PRO A 319      16.077   2.321 -33.417  1.00 33.39           H  
ATOM   4836  HB2 PRO A 319      15.355   2.900 -35.813  1.00 36.08           H  
ATOM   4837  HB3 PRO A 319      16.801   3.316 -35.300  1.00 36.08           H  
ATOM   4838  HG2 PRO A 319      16.122   1.106 -36.882  1.00 38.47           H  
ATOM   4839  HG3 PRO A 319      17.362   2.082 -37.074  1.00 38.47           H  
ATOM   4840  HD2 PRO A 319      17.641  -0.228 -35.935  1.00 44.82           H  
ATOM   4841  HD3 PRO A 319      18.597   0.988 -35.570  1.00 44.82           H  
ATOM   4842  N   PRO A 320      13.613   1.772 -33.627  1.00 26.39           N  
ANISOU 4842  N   PRO A 320     3928   2436   3664    689    279   -588       N  
ATOM   4843  CA  PRO A 320      12.236   1.276 -33.755  1.00 24.96           C  
ANISOU 4843  CA  PRO A 320     3808   2194   3480    623    257   -594       C  
ATOM   4844  C   PRO A 320      11.893   1.012 -35.213  1.00 28.67           C  
ANISOU 4844  C   PRO A 320     4306   2669   3919    600    272   -663       C  
ATOM   4845  O   PRO A 320      12.442   1.641 -36.121  1.00 29.81           O  
ANISOU 4845  O   PRO A 320     4416   2880   4029    618    299   -698       O  
ATOM   4846  CB  PRO A 320      11.387   2.420 -33.187  1.00 26.45           C  
ANISOU 4846  CB  PRO A 320     3987   2416   3647    571    248   -548       C  
ATOM   4847  CG  PRO A 320      12.323   3.189 -32.279  1.00 26.91           C  
ANISOU 4847  CG  PRO A 320     3986   2523   3714    616    254   -502       C  
ATOM   4848  CD  PRO A 320      13.676   3.073 -32.932  1.00 26.43           C  
ANISOU 4848  CD  PRO A 320     3886   2503   3653    681    280   -538       C  
ATOM   4849  HA  PRO A 320      12.105   0.474 -33.226  1.00 29.95           H  
ATOM   4850  HB2 PRO A 320      11.064   2.981 -33.908  1.00 31.74           H  
ATOM   4851  HB3 PRO A 320      10.638   2.058 -32.687  1.00 31.74           H  
ATOM   4852  HG2 PRO A 320      12.043   4.116 -32.223  1.00 32.29           H  
ATOM   4853  HG3 PRO A 320      12.330   2.790 -31.395  1.00 32.29           H  
ATOM   4854  HD2 PRO A 320      13.816   3.795 -33.565  1.00 31.72           H  
ATOM   4855  HD3 PRO A 320      14.382   3.074 -32.267  1.00 31.72           H  
ATOM   4856  N   THR A 321      10.942   0.104 -35.431  1.00 33.67           N  
ANISOU 4856  N   THR A 321     4998   3233   4560    556    252   -681       N  
ATOM   4857  CA  THR A 321      10.468  -0.199 -36.772  1.00 38.59           C  
ANISOU 4857  CA  THR A 321     5653   3859   5153    525    260   -745       C  
ATOM   4858  C   THR A 321       9.031   0.242 -37.028  1.00 33.46           C  
ANISOU 4858  C   THR A 321     5031   3212   4469    438    244   -740       C  
ATOM   4859  O   THR A 321       8.608   0.257 -38.189  1.00 43.78           O  
ANISOU 4859  O   THR A 321     6354   4539   5740    407    250   -789       O  
ATOM   4860  CB  THR A 321      10.593  -1.706 -37.050  1.00 38.28           C  
ANISOU 4860  CB  THR A 321     5659   3740   5147    543    253   -784       C  
ATOM   4861  OG1 THR A 321       9.871  -2.447 -36.059  1.00 40.01           O  
ANISOU 4861  OG1 THR A 321     5920   3880   5402    512    220   -741       O  
ATOM   4862  CG2 THR A 321      12.053  -2.121 -37.026  1.00 44.90           C  
ANISOU 4862  CG2 THR A 321     6465   4581   6012    630    275   -800       C  
ATOM   4863  H   THR A 321      10.557  -0.351 -34.810  1.00 40.40           H  
ATOM   4864  HA  THR A 321      11.030   0.270 -37.409  1.00 46.31           H  
ATOM   4865  HB  THR A 321      10.226  -1.906 -37.925  1.00 45.94           H  
ATOM   4866  HG1 THR A 321       9.044  -2.350 -36.173  1.00 48.01           H  
ATOM   4867 HG21 THR A 321      12.134  -3.026 -36.687  1.00 53.88           H  
ATOM   4868 HG22 THR A 321      12.422  -2.086 -37.922  1.00 53.88           H  
ATOM   4869 HG23 THR A 321      12.558  -1.523 -36.454  1.00 53.88           H  
ATOM   4870  N   ASP A 322       8.280   0.608 -35.994  1.00 31.53           N  
ANISOU 4870  N   ASP A 322     4791   2953   4234    398    223   -681       N  
ATOM   4871  CA  ASP A 322       6.905   1.076 -36.144  1.00 24.67           C  
ANISOU 4871  CA  ASP A 322     3943   2093   3336    314    208   -671       C  
ATOM   4872  C   ASP A 322       6.915   2.600 -36.141  1.00 27.15           C  
ANISOU 4872  C   ASP A 322     4212   2488   3617    306    225   -650       C  
ATOM   4873  O   ASP A 322       7.173   3.221 -35.105  1.00 29.15           O  
ANISOU 4873  O   ASP A 322     4432   2759   3886    323    223   -598       O  
ATOM   4874  CB  ASP A 322       6.018   0.539 -35.023  1.00 26.64           C  
ANISOU 4874  CB  ASP A 322     4224   2282   3616    268    177   -622       C  
ATOM   4875  CG  ASP A 322       4.565   0.954 -35.177  1.00 33.34           C  
ANISOU 4875  CG  ASP A 322     5090   3143   4434    177    161   -613       C  
ATOM   4876  OD1 ASP A 322       4.243   1.688 -36.136  1.00 33.78           O  
ANISOU 4876  OD1 ASP A 322     5134   3255   4447    150    173   -643       O  
ATOM   4877  OD2 ASP A 322       3.742   0.544 -34.333  1.00 37.23           O  
ANISOU 4877  OD2 ASP A 322     5606   3595   4945    130    136   -574       O  
ATOM   4878  H   ASP A 322       8.551   0.593 -35.178  1.00 37.83           H  
ATOM   4879  HA  ASP A 322       6.551   0.765 -36.992  1.00 29.60           H  
ATOM   4880  HB2 ASP A 322       6.055  -0.430 -35.027  1.00 31.97           H  
ATOM   4881  HB3 ASP A 322       6.339   0.880 -34.174  1.00 31.97           H  
ATOM   4882  N   GLU A 323       6.624   3.206 -37.295  1.00 27.16           N  
ANISOU 4882  N   GLU A 323     4207   2542   3571    277    239   -688       N  
ATOM   4883  CA  GLU A 323       6.641   4.661 -37.387  1.00 25.60           C  
ANISOU 4883  CA  GLU A 323     3941   2442   3344    261    245   -659       C  
ATOM   4884  C   GLU A 323       5.475   5.307 -36.651  1.00 25.20           C  
ANISOU 4884  C   GLU A 323     3870   2414   3293    195    217   -603       C  
ATOM   4885  O   GLU A 323       5.525   6.511 -36.375  1.00 27.21           O  
ANISOU 4885  O   GLU A 323     4066   2738   3534    189    216   -566       O  
ATOM   4886  CB  GLU A 323       6.637   5.090 -38.857  1.00 27.95           C  
ANISOU 4886  CB  GLU A 323     4231   2798   3590    244    263   -709       C  
ATOM   4887  CG  GLU A 323       7.927   4.756 -39.572  1.00 30.08           C  
ANISOU 4887  CG  GLU A 323     4502   3075   3854    315    296   -760       C  
ATOM   4888  CD  GLU A 323       7.932   5.162 -41.034  1.00 45.44           C  
ANISOU 4888  CD  GLU A 323     6440   5082   5744    296    315   -810       C  
ATOM   4889  OE1 GLU A 323       6.917   5.689 -41.537  1.00 35.52           O  
ANISOU 4889  OE1 GLU A 323     5181   3861   4454    227    299   -805       O  
ATOM   4890  OE2 GLU A 323       8.970   4.949 -41.690  1.00 34.00           O  
ANISOU 4890  OE2 GLU A 323     4981   3654   4284    350    342   -852       O  
ATOM   4891  H   GLU A 323       6.417   2.803 -38.026  1.00 32.60           H  
ATOM   4892  HA  GLU A 323       7.459   4.989 -36.981  1.00 30.72           H  
ATOM   4893  HB2 GLU A 323       5.914   4.634 -39.315  1.00 33.54           H  
ATOM   4894  HB3 GLU A 323       6.507   6.050 -38.905  1.00 33.54           H  
ATOM   4895  HG2 GLU A 323       8.657   5.221 -39.133  1.00 36.10           H  
ATOM   4896  HG3 GLU A 323       8.071   3.798 -39.530  1.00 36.10           H  
ATOM   4897  N   GLY A 324       4.435   4.542 -36.336  1.00 30.18           N  
ANISOU 4897  N   GLY A 324     4546   2986   3935    144    193   -598       N  
ATOM   4898  CA  GLY A 324       3.299   5.065 -35.604  1.00 25.72           C  
ANISOU 4898  CA  GLY A 324     3960   2443   3369     83    167   -547       C  
ATOM   4899  C   GLY A 324       2.471   6.016 -36.447  1.00 30.39           C  
ANISOU 4899  C   GLY A 324     4522   3110   3916     29    162   -553       C  
ATOM   4900  O   GLY A 324       2.712   6.229 -37.634  1.00 35.58           O  
ANISOU 4900  O   GLY A 324     5178   3799   4540     32    176   -596       O  
ATOM   4901  H   GLY A 324       4.366   3.709 -36.538  1.00 36.22           H  
ATOM   4902  HA2 GLY A 324       2.731   4.331 -35.321  1.00 30.86           H  
ATOM   4903  HA3 GLY A 324       3.612   5.543 -34.821  1.00 30.86           H  
ATOM   4904  N   LYS A 325       1.472   6.602 -35.799  1.00 31.41           N  
ANISOU 4904  N   LYS A 325     4624   3269   4043    -19    140   -508       N  
ATOM   4905  CA  LYS A 325       0.575   7.541 -36.447  1.00 39.25           C  
ANISOU 4905  CA  LYS A 325     5585   4332   4996    -69    130   -505       C  
ATOM   4906  C   LYS A 325       0.738   8.929 -35.844  1.00 31.92           C  
ANISOU 4906  C   LYS A 325     4592   3471   4066    -54    129   -457       C  
ATOM   4907  O   LYS A 325       1.076   9.083 -34.665  1.00 31.09           O  
ANISOU 4907  O   LYS A 325     4467   3355   3989    -28    127   -417       O  
ATOM   4908  CB  LYS A 325      -0.884   7.096 -36.316  1.00 39.23           C  
ANISOU 4908  CB  LYS A 325     5603   4314   4987   -144    102   -496       C  
ATOM   4909  CG  LYS A 325      -1.111   5.618 -36.580  1.00 83.91           C  
ANISOU 4909  CG  LYS A 325    11332   9891  10657   -166     97   -533       C  
ATOM   4910  CD  LYS A 325      -2.587   5.304 -36.773  1.00102.66           C  
ANISOU 4910  CD  LYS A 325    13723  12269  13014   -251     71   -532       C  
ATOM   4911  CE  LYS A 325      -2.910   5.042 -38.238  1.00 98.30           C  
ANISOU 4911  CE  LYS A 325    13199  11727  12422   -283     72   -589       C  
ATOM   4912  NZ  LYS A 325      -4.319   4.595 -38.430  1.00105.77           N  
ANISOU 4912  NZ  LYS A 325    14165  12673  13351   -369     45   -590       N  
ATOM   4913  H   LYS A 325       1.295   6.466 -34.968  1.00 37.70           H  
ATOM   4914  HA  LYS A 325       0.796   7.589 -37.391  1.00 47.10           H  
ATOM   4915  HB2 LYS A 325      -1.185   7.283 -35.413  1.00 47.07           H  
ATOM   4916  HB3 LYS A 325      -1.418   7.594 -36.954  1.00 47.07           H  
ATOM   4917  HG2 LYS A 325      -0.636   5.359 -37.385  1.00100.69           H  
ATOM   4918  HG3 LYS A 325      -0.787   5.103 -35.824  1.00100.69           H  
ATOM   4919  HD2 LYS A 325      -2.817   4.512 -36.263  1.00123.19           H  
ATOM   4920  HD3 LYS A 325      -3.119   6.058 -36.474  1.00123.19           H  
ATOM   4921  HE2 LYS A 325      -2.780   5.859 -38.744  1.00117.96           H  
ATOM   4922  HE3 LYS A 325      -2.323   4.346 -38.574  1.00117.96           H  
ATOM   4923  HZ1 LYS A 325      -4.533   4.628 -39.293  1.00126.93           H  
ATOM   4924  HZ2 LYS A 325      -4.415   3.759 -38.140  1.00126.93           H  
ATOM   4925  HZ3 LYS A 325      -4.871   5.124 -37.974  1.00126.93           H  
ATOM   4926  N   ALA A 326       0.491   9.937 -36.669  1.00 31.00           N  
ANISOU 4926  N   ALA A 326     4444   3421   3912    -70    129   -462       N  
ATOM   4927  CA  ALA A 326       0.554  11.300 -36.181  1.00 35.59           C  
ANISOU 4927  CA  ALA A 326     4969   4063   4489    -60    125   -420       C  
ATOM   4928  C   ALA A 326      -0.512  11.496 -35.110  1.00 21.26           C  
ANISOU 4928  C   ALA A 326     3137   2251   2688    -94    101   -376       C  
ATOM   4929  O   ALA A 326      -1.617  10.944 -35.220  1.00 25.26           O  
ANISOU 4929  O   ALA A 326     3665   2745   3189   -146     84   -382       O  
ATOM   4930  CB  ALA A 326       0.349  12.304 -37.314  1.00 39.78           C  
ANISOU 4930  CB  ALA A 326     5476   4660   4978    -77    125   -431       C  
ATOM   4931  H   ALA A 326       0.289   9.859 -37.501  1.00 37.20           H  
ATOM   4932  HA  ALA A 326       1.430  11.468 -35.799  1.00 42.70           H  
ATOM   4933  HB1 ALA A 326       0.527  13.197 -36.980  1.00 47.73           H  
ATOM   4934  HB2 ALA A 326       0.961  12.094 -38.037  1.00 47.73           H  
ATOM   4935  HB3 ALA A 326      -0.567  12.244 -37.627  1.00 47.73           H  
ATOM   4936  N   PRO A 327      -0.213  12.251 -34.060  1.00 25.32           N  
ANISOU 4936  N   PRO A 327     3615   2786   3221    -70    100   -334       N  
ATOM   4937  CA  PRO A 327      -1.233  12.566 -33.061  1.00 25.21           C  
ANISOU 4937  CA  PRO A 327     3578   2785   3214   -100     80   -295       C  
ATOM   4938  C   PRO A 327      -2.231  13.577 -33.597  1.00 16.71           C  
ANISOU 4938  C   PRO A 327     2471   1771   2107   -135     64   -288       C  
ATOM   4939  O   PRO A 327      -2.078  14.154 -34.677  1.00 21.24           O  
ANISOU 4939  O   PRO A 327     3038   2379   2653   -134     68   -308       O  
ATOM   4940  CB  PRO A 327      -0.424  13.141 -31.894  1.00 26.17           C  
ANISOU 4940  CB  PRO A 327     3671   2913   3360    -57     86   -259       C  
ATOM   4941  CG  PRO A 327       0.780  13.736 -32.547  1.00 29.28           C  
ANISOU 4941  CG  PRO A 327     4052   3327   3744    -14    105   -274       C  
ATOM   4942  CD  PRO A 327       1.102  12.818 -33.703  1.00 27.19           C  
ANISOU 4942  CD  PRO A 327     3828   3033   3470    -13    118   -323       C  
ATOM   4943  HA  PRO A 327      -1.698  11.765 -32.772  1.00 30.25           H  
ATOM   4944  HB2 PRO A 327      -0.942  13.817 -31.430  1.00 31.40           H  
ATOM   4945  HB3 PRO A 327      -0.175  12.433 -31.279  1.00 31.40           H  
ATOM   4946  HG2 PRO A 327       0.575  14.630 -32.862  1.00 35.13           H  
ATOM   4947  HG3 PRO A 327       1.515  13.768 -31.915  1.00 35.13           H  
ATOM   4948  HD2 PRO A 327       1.477  13.316 -34.446  1.00 32.63           H  
ATOM   4949  HD3 PRO A 327       1.716  12.119 -33.428  1.00 32.63           H  
ATOM   4950  N   VAL A 328      -3.293  13.764 -32.814  1.00 19.13           N  
ANISOU 4950  N   VAL A 328     2757   2094   2416   -166     46   -259       N  
ATOM   4951  CA  VAL A 328      -4.257  14.806 -33.109  1.00 19.67           C  
ANISOU 4951  CA  VAL A 328     2789   2224   2460   -190     29   -246       C  
ATOM   4952  C   VAL A 328      -3.544  16.156 -33.100  1.00 22.87           C  
ANISOU 4952  C   VAL A 328     3161   2667   2861   -148     35   -231       C  
ATOM   4953  O   VAL A 328      -2.556  16.364 -32.385  1.00 22.53           O  
ANISOU 4953  O   VAL A 328     3111   2610   2838   -109     48   -217       O  
ATOM   4954  CB  VAL A 328      -5.409  14.776 -32.091  1.00 26.83           C  
ANISOU 4954  CB  VAL A 328     3675   3146   3374   -221     12   -216       C  
ATOM   4955  CG1 VAL A 328      -4.909  15.255 -30.724  1.00 30.08           C  
ANISOU 4955  CG1 VAL A 328     4063   3558   3810   -186     17   -182       C  
ATOM   4956  CG2 VAL A 328      -6.579  15.616 -32.585  1.00 43.69           C  
ANISOU 4956  CG2 VAL A 328     5777   5344   5481   -250     -8   -210       C  
ATOM   4957  H   VAL A 328      -3.474  13.303 -32.111  1.00 22.95           H  
ATOM   4958  HA  VAL A 328      -4.636  14.664 -33.991  1.00 23.60           H  
ATOM   4959  HB  VAL A 328      -5.729  13.866 -31.990  1.00 32.20           H  
ATOM   4960 HG11 VAL A 328      -5.638  15.203 -30.086  1.00 36.10           H  
ATOM   4961 HG12 VAL A 328      -4.178  14.686 -30.438  1.00 36.10           H  
ATOM   4962 HG13 VAL A 328      -4.604  16.172 -30.803  1.00 36.10           H  
ATOM   4963 HG21 VAL A 328      -7.409  15.189 -32.320  1.00 52.43           H  
ATOM   4964 HG22 VAL A 328      -6.522  16.500 -32.189  1.00 52.43           H  
ATOM   4965 HG23 VAL A 328      -6.535  15.683 -33.551  1.00 52.43           H  
ATOM   4966  N   ASP A 329      -4.030  17.070 -33.929  1.00 18.59           N  
ANISOU 4966  N   ASP A 329     2600   2173   2291   -160     24   -233       N  
ATOM   4967  CA  ASP A 329      -3.517  18.435 -33.963  1.00 16.85           C  
ANISOU 4967  CA  ASP A 329     2350   1989   2064   -129     24   -215       C  
ATOM   4968  C   ASP A 329      -3.950  19.148 -32.691  1.00 15.65           C  
ANISOU 4968  C   ASP A 329     2166   1853   1928   -118     14   -180       C  
ATOM   4969  O   ASP A 329      -5.150  19.283 -32.437  1.00 18.41           O  
ANISOU 4969  O   ASP A 329     2497   2227   2271   -144     -4   -169       O  
ATOM   4970  CB  ASP A 329      -4.060  19.124 -35.216  1.00 18.52           C  
ANISOU 4970  CB  ASP A 329     2554   2242   2239   -149     11   -224       C  
ATOM   4971  CG  ASP A 329      -3.468  20.507 -35.472  1.00 21.71           C  
ANISOU 4971  CG  ASP A 329     2936   2678   2633   -122     10   -208       C  
ATOM   4972  OD1 ASP A 329      -2.943  21.173 -34.553  1.00 15.64           O  
ANISOU 4972  OD1 ASP A 329     2151   1908   1884    -92     14   -184       O  
ATOM   4973  OD2 ASP A 329      -3.571  20.944 -36.640  1.00 24.50           O  
ANISOU 4973  OD2 ASP A 329     3293   3061   2957   -134      4   -217       O  
ATOM   4974  H   ASP A 329      -4.666  16.926 -34.490  1.00 22.31           H  
ATOM   4975  HA  ASP A 329      -2.548  18.455 -34.002  1.00 20.22           H  
ATOM   4976  HB2 ASP A 329      -3.859  18.571 -35.987  1.00 22.22           H  
ATOM   4977  HB3 ASP A 329      -5.020  19.227 -35.123  1.00 22.22           H  
ATOM   4978  N   HIS A 330      -2.981  19.588 -31.877  1.00 15.82           N  
ANISOU 4978  N   HIS A 330     2177   1864   1968    -81     25   -163       N  
ATOM   4979  CA  HIS A 330      -3.275  20.268 -30.614  1.00 14.95           C  
ANISOU 4979  CA  HIS A 330     2039   1770   1873    -68     17   -133       C  
ATOM   4980  C   HIS A 330      -3.555  21.764 -30.780  1.00 15.38           C  
ANISOU 4980  C   HIS A 330     2065   1865   1913    -57      3   -119       C  
ATOM   4981  O   HIS A 330      -3.882  22.430 -29.793  1.00 15.21           O  
ANISOU 4981  O   HIS A 330     2020   1860   1901    -45     -4    -98       O  
ATOM   4982  CB  HIS A 330      -2.126  20.038 -29.625  1.00 13.70           C  
ANISOU 4982  CB  HIS A 330     1884   1583   1740    -36     33   -122       C  
ATOM   4983  CG  HIS A 330      -2.086  18.648 -29.062  1.00 15.64           C  
ANISOU 4983  CG  HIS A 330     2153   1786   2005    -46     40   -124       C  
ATOM   4984  ND1 HIS A 330      -2.611  18.332 -27.825  1.00 17.24           N  
ANISOU 4984  ND1 HIS A 330     2346   1983   2222    -55     34   -102       N  
ATOM   4985  CD2 HIS A 330      -1.622  17.486 -29.580  1.00 18.19           C  
ANISOU 4985  CD2 HIS A 330     2510   2068   2334    -48     52   -147       C  
ATOM   4986  CE1 HIS A 330      -2.447  17.041 -27.597  1.00 18.31           C  
ANISOU 4986  CE1 HIS A 330     2510   2073   2372    -64     40   -107       C  
ATOM   4987  NE2 HIS A 330      -1.860  16.504 -28.650  1.00 17.38           N  
ANISOU 4987  NE2 HIS A 330     2422   1931   2252    -58     50   -135       N  
ATOM   4988  H   HIS A 330      -2.141  19.502 -32.038  1.00 18.98           H  
ATOM   4989  HA  HIS A 330      -4.076  19.879 -30.228  1.00 17.94           H  
ATOM   4990  HB2 HIS A 330      -1.285  20.197 -30.081  1.00 16.44           H  
ATOM   4991  HB3 HIS A 330      -2.223  20.656 -28.884  1.00 16.44           H  
ATOM   4992  HD1 HIS A 330      -2.986  18.889 -27.287  1.00 20.69           H  
ATOM   4993  HD2 HIS A 330      -1.217  17.375 -30.410  1.00 21.83           H  
ATOM   4994  HE1 HIS A 330      -2.702  16.588 -26.826  1.00 21.97           H  
ATOM   4995  N   ASN A 331      -3.476  22.311 -31.990  1.00 14.92           N  
ANISOU 4995  N   ASN A 331     2010   1826   1832    -61     -1   -129       N  
ATOM   4996  CA  ASN A 331      -3.948  23.672 -32.262  1.00 14.58           C  
ANISOU 4996  CA  ASN A 331     1946   1820   1774    -54    -20   -114       C  
ATOM   4997  C   ASN A 331      -3.192  24.739 -31.465  1.00 14.60           C  
ANISOU 4997  C   ASN A 331     1935   1822   1790    -21    -18    -94       C  
ATOM   4998  O   ASN A 331      -3.744  25.799 -31.165  1.00 15.17           O  
ANISOU 4998  O   ASN A 331     1989   1916   1860    -11    -35    -78       O  
ATOM   4999  CB  ASN A 331      -5.452  23.805 -31.980  1.00 15.05           C  
ANISOU 4999  CB  ASN A 331     1983   1906   1828    -72    -41   -106       C  
ATOM   5000  CG  ASN A 331      -6.300  22.955 -32.902  1.00 22.20           C  
ANISOU 5000  CG  ASN A 331     2899   2821   2715   -111    -48   -124       C  
ATOM   5001  OD1 ASN A 331      -6.038  22.872 -34.097  1.00 19.26           O  
ANISOU 5001  OD1 ASN A 331     2544   2451   2322   -123    -48   -140       O  
ATOM   5002  ND2 ASN A 331      -7.320  22.312 -32.346  1.00 25.34           N  
ANISOU 5002  ND2 ASN A 331     3286   3226   3116   -136    -55   -123       N  
ATOM   5003  H   ASN A 331      -3.151  21.910 -32.678  1.00 17.90           H  
ATOM   5004  HA  ASN A 331      -3.780  23.843 -33.202  1.00 17.50           H  
ATOM   5005  HB2 ASN A 331      -5.629  23.526 -31.068  1.00 18.06           H  
ATOM   5006  HB3 ASN A 331      -5.715  24.731 -32.101  1.00 18.06           H  
ATOM   5007 HD21 ASN A 331      -7.831  21.816 -32.829  1.00 30.41           H  
ATOM   5008 HD22 ASN A 331      -7.471  22.392 -31.503  1.00 30.41           H  
ATOM   5009  N   CYS A 332      -1.926  24.479 -31.125  1.00 14.24           N  
ANISOU 5009  N   CYS A 332     1899   1753   1757     -3      1    -95       N  
ATOM   5010  CA  CYS A 332      -1.108  25.418 -30.345  1.00 11.51           C  
ANISOU 5010  CA  CYS A 332     1542   1407   1423     24      3    -76       C  
ATOM   5011  C   CYS A 332      -1.780  25.772 -29.021  1.00 14.49           C  
ANISOU 5011  C   CYS A 332     1900   1790   1815     32     -7    -60       C  
ATOM   5012  O   CYS A 332      -1.735  26.919 -28.572  1.00 15.50           O  
ANISOU 5012  O   CYS A 332     2016   1929   1943     48    -17    -46       O  
ATOM   5013  CB  CYS A 332      -0.797  26.683 -31.152  1.00 11.82           C  
ANISOU 5013  CB  CYS A 332     1581   1466   1444     27     -7    -69       C  
ATOM   5014  SG  CYS A 332       0.328  26.356 -32.543  1.00 14.48           S  
ANISOU 5014  SG  CYS A 332     1937   1804   1761     20     11    -86       S  
ATOM   5015  H   CYS A 332      -1.511  23.757 -31.338  1.00 17.08           H  
ATOM   5016  HA  CYS A 332      -0.267  24.983 -30.134  1.00 13.81           H  
ATOM   5017  HB2 CYS A 332      -1.624  27.042 -31.510  1.00 14.18           H  
ATOM   5018  HB3 CYS A 332      -0.377  27.335 -30.570  1.00 14.18           H  
ATOM   5019  N   LEU A 333      -2.435  24.778 -28.407  1.00 14.53           N  
ANISOU 5019  N   LEU A 333     1904   1788   1830     20     -4    -63       N  
ATOM   5020  CA  LEU A 333      -3.163  24.955 -27.164  1.00 11.62           C  
ANISOU 5020  CA  LEU A 333     1515   1430   1471     23    -12    -49       C  
ATOM   5021  C   LEU A 333      -2.787  23.871 -26.170  1.00 14.52           C  
ANISOU 5021  C   LEU A 333     1888   1774   1857     22      2    -44       C  
ATOM   5022  O   LEU A 333      -2.701  22.687 -26.526  1.00 13.34           O  
ANISOU 5022  O   LEU A 333     1758   1600   1711      6     11    -54       O  
ATOM   5023  CB  LEU A 333      -4.678  24.895 -27.352  1.00 12.99           C  
ANISOU 5023  CB  LEU A 333     1673   1630   1632      2    -27    -51       C  
ATOM   5024  CG  LEU A 333      -5.290  26.002 -28.204  1.00 14.08           C  
ANISOU 5024  CG  LEU A 333     1800   1796   1752      6    -46    -51       C  
ATOM   5025  CD1 LEU A 333      -6.737  25.678 -28.531  1.00 17.43           C  
ANISOU 5025  CD1 LEU A 333     2209   2250   2164    -18    -61    -56       C  
ATOM   5026  CD2 LEU A 333      -5.158  27.345 -27.483  1.00 12.82           C  
ANISOU 5026  CD2 LEU A 333     1626   1648   1598     38    -55    -38       C  
ATOM   5027  H   LEU A 333      -2.466  23.973 -28.709  1.00 17.44           H  
ATOM   5028  HA  LEU A 333      -2.919  25.826 -26.812  1.00 13.95           H  
ATOM   5029  HB2 LEU A 333      -4.896  24.051 -27.778  1.00 15.59           H  
ATOM   5030  HB3 LEU A 333      -5.094  24.943 -26.477  1.00 15.59           H  
ATOM   5031  HG  LEU A 333      -4.815  26.073 -29.047  1.00 16.89           H  
ATOM   5032 HD11 LEU A 333      -7.063  26.315 -29.186  1.00 20.92           H  
ATOM   5033 HD12 LEU A 333      -6.785  24.779 -28.892  1.00 20.92           H  
ATOM   5034 HD13 LEU A 333      -7.265  25.737 -27.720  1.00 20.92           H  
ATOM   5035 HD21 LEU A 333      -5.971  27.516 -26.983  1.00 15.39           H  
ATOM   5036 HD22 LEU A 333      -4.400  27.307 -26.880  1.00 15.39           H  
ATOM   5037 HD23 LEU A 333      -5.022  28.044 -28.141  1.00 15.39           H  
ATOM   5038  N   ASP A 334      -2.592  24.288 -24.922  1.00 14.13           N  
ANISOU 5038  N   ASP A 334     1824   1730   1817     38      3    -28       N  
ATOM   5039  CA  ASP A 334      -2.360  23.376 -23.817  1.00 11.76           C  
ANISOU 5039  CA  ASP A 334     1525   1412   1532     36     12    -17       C  
ATOM   5040  C   ASP A 334      -3.682  22.961 -23.168  1.00 16.03           C  
ANISOU 5040  C   ASP A 334     2051   1972   2068     12      5    -11       C  
ATOM   5041  O   ASP A 334      -4.738  23.547 -23.409  1.00 15.43           O  
ANISOU 5041  O   ASP A 334     1956   1928   1979      4     -7    -14       O  
ATOM   5042  CB  ASP A 334      -1.397  23.999 -22.792  1.00 12.17           C  
ANISOU 5042  CB  ASP A 334     1567   1464   1592     63     16     -3       C  
ATOM   5043  CG  ASP A 334      -1.822  25.385 -22.275  1.00 17.04           C  
ANISOU 5043  CG  ASP A 334     2162   2112   2200     76      5      1       C  
ATOM   5044  OD1 ASP A 334      -2.414  26.195 -23.017  1.00 13.35           O  
ANISOU 5044  OD1 ASP A 334     1690   1660   1721     77     -7     -6       O  
ATOM   5045  OD2 ASP A 334      -1.495  25.692 -21.104  1.00 13.47           O  
ANISOU 5045  OD2 ASP A 334     1699   1666   1753     89      6     13       O  
ATOM   5046  H   ASP A 334      -2.591  25.116 -24.689  1.00 16.96           H  
ATOM   5047  HA  ASP A 334      -1.938  22.570 -24.154  1.00 14.12           H  
ATOM   5048  HB2 ASP A 334      -1.336  23.407 -22.025  1.00 14.60           H  
ATOM   5049  HB3 ASP A 334      -0.525  24.096 -23.205  1.00 14.60           H  
ATOM   5050  N   LEU A 335      -3.608  21.931 -22.335  1.00 13.81           N  
ANISOU 5050  N   LEU A 335     1777   1674   1798      1     12      1       N  
ATOM   5051  CA  LEU A 335      -4.805  21.331 -21.765  1.00 15.17           C  
ANISOU 5051  CA  LEU A 335     1937   1863   1964    -31      6      9       C  
ATOM   5052  C   LEU A 335      -5.580  22.314 -20.898  1.00 18.21           C  
ANISOU 5052  C   LEU A 335     2286   2296   2338    -23     -1     18       C  
ATOM   5053  O   LEU A 335      -4.992  22.959 -20.017  1.00 16.60           O  
ANISOU 5053  O   LEU A 335     2072   2097   2137      2      2     26       O  
ATOM   5054  CB  LEU A 335      -4.424  20.121 -20.922  1.00 14.76           C  
ANISOU 5054  CB  LEU A 335     1903   1780   1926    -43     14     26       C  
ATOM   5055  CG  LEU A 335      -4.013  18.895 -21.723  1.00 16.78           C  
ANISOU 5055  CG  LEU A 335     2197   1986   2192    -57     19     15       C  
ATOM   5056  CD1 LEU A 335      -3.249  17.937 -20.818  1.00 18.36           C  
ANISOU 5056  CD1 LEU A 335     2416   2147   2411    -51     26     35       C  
ATOM   5057  CD2 LEU A 335      -5.244  18.236 -22.325  1.00 22.43           C  
ANISOU 5057  CD2 LEU A 335     2919   2708   2897   -102     11      6       C  
ATOM   5058  H   LEU A 335      -2.876  21.559 -22.081  1.00 16.58           H  
ATOM   5059  HA  LEU A 335      -5.383  21.063 -22.497  1.00 18.20           H  
ATOM   5060  HB2 LEU A 335      -3.677  20.364 -20.354  1.00 17.72           H  
ATOM   5061  HB3 LEU A 335      -5.188  19.873 -20.378  1.00 17.72           H  
ATOM   5062  HG  LEU A 335      -3.429  19.144 -22.457  1.00 20.13           H  
ATOM   5063 HD11 LEU A 335      -2.810  17.268 -21.366  1.00 22.03           H  
ATOM   5064 HD12 LEU A 335      -2.589  18.438 -20.314  1.00 22.03           H  
ATOM   5065 HD13 LEU A 335      -3.874  17.510 -20.212  1.00 22.03           H  
ATOM   5066 HD21 LEU A 335      -5.057  17.296 -22.475  1.00 26.92           H  
ATOM   5067 HD22 LEU A 335      -5.986  18.331 -21.708  1.00 26.92           H  
ATOM   5068 HD23 LEU A 335      -5.455  18.669 -23.166  1.00 26.92           H  
ATOM   5069  N   PRO A 336      -6.897  22.414 -21.073  1.00 16.54           N  
ANISOU 5069  N   PRO A 336     2052   2120   2111    -44    -10     14       N  
ATOM   5070  CA  PRO A 336      -7.697  23.343 -20.268  1.00 14.91           C  
ANISOU 5070  CA  PRO A 336     1808   1964   1893    -32    -16     18       C  
ATOM   5071  C   PRO A 336      -8.325  22.741 -19.023  1.00 16.33           C  
ANISOU 5071  C   PRO A 336     1969   2168   2066    -55    -11     34       C  
ATOM   5072  O   PRO A 336      -8.967  23.485 -18.275  1.00 19.08           O  
ANISOU 5072  O   PRO A 336     2284   2562   2403    -42    -13     35       O  
ATOM   5073  CB  PRO A 336      -8.790  23.769 -21.262  1.00 18.30           C  
ANISOU 5073  CB  PRO A 336     2221   2425   2308    -41    -29      4       C  
ATOM   5074  CG  PRO A 336      -9.011  22.566 -22.086  1.00 17.22           C  
ANISOU 5074  CG  PRO A 336     2106   2266   2171    -81    -29      0       C  
ATOM   5075  CD  PRO A 336      -7.661  21.906 -22.231  1.00 16.28           C  
ANISOU 5075  CD  PRO A 336     2026   2090   2069    -75    -18      1       C  
ATOM   5076  HA  PRO A 336      -7.165  24.113 -20.014  1.00 17.89           H  
ATOM   5077  HB2 PRO A 336      -9.597  24.020 -20.784  1.00 21.96           H  
ATOM   5078  HB3 PRO A 336      -8.480  24.513 -21.802  1.00 21.96           H  
ATOM   5079  HG2 PRO A 336      -9.635  21.974 -21.639  1.00 20.66           H  
ATOM   5080  HG3 PRO A 336      -9.361  22.824 -22.953  1.00 20.66           H  
ATOM   5081  HD2 PRO A 336      -7.744  20.941 -22.191  1.00 19.54           H  
ATOM   5082  HD3 PRO A 336      -7.238  22.168 -23.064  1.00 19.54           H  
ATOM   5083  N   ASN A 337      -8.148  21.433 -18.785  1.00 14.94           N  
ANISOU 5083  N   ASN A 337     1815   1963   1898    -87     -5     47       N  
ATOM   5084  CA  ASN A 337      -8.955  20.704 -17.815  1.00 17.33           C  
ANISOU 5084  CA  ASN A 337     2101   2292   2191   -122     -4     66       C  
ATOM   5085  C   ASN A 337      -8.109  19.965 -16.785  1.00 17.20           C  
ANISOU 5085  C   ASN A 337     2105   2244   2186   -125      5     89       C  
ATOM   5086  O   ASN A 337      -8.620  19.061 -16.112  1.00 17.80           O  
ANISOU 5086  O   ASN A 337     2181   2326   2256   -163      6    109       O  
ATOM   5087  CB  ASN A 337      -9.891  19.720 -18.529  1.00 21.77           C  
ANISOU 5087  CB  ASN A 337     2670   2854   2747   -173    -10     64       C  
ATOM   5088  CG  ASN A 337      -9.142  18.690 -19.370  1.00 30.48           C  
ANISOU 5088  CG  ASN A 337     3823   3890   3867   -186     -8     58       C  
ATOM   5089  OD1 ASN A 337      -8.043  18.943 -19.873  1.00 22.42           O  
ANISOU 5089  OD1 ASN A 337     2826   2832   2861   -152     -4     48       O  
ATOM   5090  ND2 ASN A 337      -9.742  17.516 -19.519  1.00 50.34           N  
ANISOU 5090  ND2 ASN A 337     6356   6392   6381   -237    -12     65       N  
ATOM   5091  H   ASN A 337      -7.558  20.947 -19.181  1.00 17.92           H  
ATOM   5092  HA  ASN A 337      -9.496  21.346 -17.329  1.00 20.79           H  
ATOM   5093  HB2 ASN A 337     -10.413  19.243 -17.866  1.00 26.12           H  
ATOM   5094  HB3 ASN A 337     -10.479  20.217 -19.119  1.00 26.12           H  
ATOM   5095 HD21 ASN A 337      -9.366  16.897 -19.983  1.00 60.41           H  
ATOM   5096 HD22 ASN A 337     -10.506  17.374 -19.152  1.00 60.41           H  
ATOM   5097  N   LEU A 338      -6.840  20.344 -16.634  1.00 15.87           N  
ANISOU 5097  N   LEU A 338     1953   2046   2032    -87     10     89       N  
ATOM   5098  CA  LEU A 338      -5.996  19.784 -15.589  1.00 13.73           C  
ANISOU 5098  CA  LEU A 338     1695   1752   1769    -84     15    113       C  
ATOM   5099  C   LEU A 338      -6.527  20.191 -14.227  1.00 14.19           C  
ANISOU 5099  C   LEU A 338     1720   1862   1809    -88     17    128       C  
ATOM   5100  O   LEU A 338      -6.968  21.327 -14.038  1.00 17.20           O  
ANISOU 5100  O   LEU A 338     2071   2288   2177    -68     16    114       O  
ATOM   5101  CB  LEU A 338      -4.564  20.282 -15.732  1.00 13.65           C  
ANISOU 5101  CB  LEU A 338     1700   1712   1775    -41     19    108       C  
ATOM   5102  CG  LEU A 338      -3.851  19.864 -17.009  1.00 12.71           C  
ANISOU 5102  CG  LEU A 338     1613   1545   1673    -32     21     92       C  
ATOM   5103  CD1 LEU A 338      -2.722  20.828 -17.316  1.00 18.44           C  
ANISOU 5103  CD1 LEU A 338     2338   2264   2404      9     24     82       C  
ATOM   5104  CD2 LEU A 338      -3.348  18.462 -16.845  1.00 16.31           C  
ANISOU 5104  CD2 LEU A 338     2101   1952   2145    -45     24    108       C  
ATOM   5105  H   LEU A 338      -6.443  20.926 -17.127  1.00 19.05           H  
ATOM   5106  HA  LEU A 338      -5.994  18.816 -15.662  1.00 16.47           H  
ATOM   5107  HB2 LEU A 338      -4.576  21.252 -15.711  1.00 16.38           H  
ATOM   5108  HB3 LEU A 338      -4.047  19.941 -14.986  1.00 16.38           H  
ATOM   5109  HG  LEU A 338      -4.458  19.886 -17.764  1.00 15.26           H  
ATOM   5110 HD11 LEU A 338      -2.270  20.538 -18.124  1.00 22.13           H  
ATOM   5111 HD12 LEU A 338      -3.091  21.716 -17.445  1.00 22.13           H  
ATOM   5112 HD13 LEU A 338      -2.099  20.833 -16.572  1.00 22.13           H  
ATOM   5113 HD21 LEU A 338      -3.137  18.098 -17.720  1.00 19.57           H  
ATOM   5114 HD22 LEU A 338      -2.551  18.474 -16.292  1.00 19.57           H  
ATOM   5115 HD23 LEU A 338      -4.037  17.926 -16.422  1.00 19.57           H  
ATOM   5116  N   LYS A 339      -6.474  19.271 -13.275  1.00 12.71           N  
ANISOU 5116  N   LYS A 339     1540   1668   1620   -113     19    156       N  
ATOM   5117  CA  LYS A 339      -7.021  19.519 -11.942  1.00 13.54           C  
ANISOU 5117  CA  LYS A 339     1614   1827   1703   -124     22    173       C  
ATOM   5118  C   LYS A 339      -5.949  19.386 -10.874  1.00 14.55           C  
ANISOU 5118  C   LYS A 339     1752   1941   1834   -107     24    196       C  
ATOM   5119  O   LYS A 339      -5.524  18.257 -10.567  1.00 15.92           O  
ANISOU 5119  O   LYS A 339     1953   2078   2019   -127     23    223       O  
ATOM   5120  CB  LYS A 339      -8.171  18.549 -11.666  1.00 13.47           C  
ANISOU 5120  CB  LYS A 339     1598   1840   1680   -180     21    191       C  
ATOM   5121  CG  LYS A 339      -9.397  18.802 -12.534  1.00 16.25           C  
ANISOU 5121  CG  LYS A 339     1928   2227   2021   -199     17    169       C  
ATOM   5122  CD  LYS A 339     -10.044  20.116 -12.133  1.00 22.49           C  
ANISOU 5122  CD  LYS A 339     2670   3086   2789   -172     20    151       C  
ATOM   5123  CE  LYS A 339     -11.261  20.456 -12.975  1.00 32.95           C  
ANISOU 5123  CE  LYS A 339     3967   4451   4103   -184     15    131       C  
ATOM   5124  NZ  LYS A 339     -11.873  21.719 -12.468  1.00 49.92           N  
ANISOU 5124  NZ  LYS A 339     6068   6666   6231   -151     17    113       N  
ATOM   5125  H   LYS A 339      -6.126  18.491 -13.375  1.00 15.25           H  
ATOM   5126  HA  LYS A 339      -7.347  20.432 -11.905  1.00 16.25           H  
ATOM   5127  HB2 LYS A 339      -7.866  17.645 -11.837  1.00 16.16           H  
ATOM   5128  HB3 LYS A 339      -8.440  18.639 -10.738  1.00 16.16           H  
ATOM   5129  HG2 LYS A 339      -9.134  18.855 -13.466  1.00 19.51           H  
ATOM   5130  HG3 LYS A 339     -10.040  18.086 -12.411  1.00 19.51           H  
ATOM   5131  HD2 LYS A 339     -10.328  20.059 -11.207  1.00 26.99           H  
ATOM   5132  HD3 LYS A 339      -9.398  20.832 -12.238  1.00 26.99           H  
ATOM   5133  HE2 LYS A 339     -10.997  20.585 -13.900  1.00 39.54           H  
ATOM   5134  HE3 LYS A 339     -11.915  19.743 -12.913  1.00 39.54           H  
ATOM   5135  HZ1 LYS A 339     -12.676  21.551 -12.122  1.00 59.90           H  
ATOM   5136  HZ2 LYS A 339     -11.356  22.077 -11.838  1.00 59.90           H  
ATOM   5137  HZ3 LYS A 339     -11.963  22.303 -13.133  1.00 59.90           H  
ATOM   5138  N   PRO A 340      -5.483  20.482 -10.278  1.00 14.48           N  
ANISOU 5138  N   PRO A 340     1724   1960   1818    -73     27    187       N  
ATOM   5139  CA  PRO A 340      -4.489  20.367  -9.201  1.00 16.48           C  
ANISOU 5139  CA  PRO A 340     1983   2207   2070    -61     27    210       C  
ATOM   5140  C   PRO A 340      -4.968  19.473  -8.065  1.00 14.43           C  
ANISOU 5140  C   PRO A 340     1720   1970   1794   -100     28    245       C  
ATOM   5141  O   PRO A 340      -6.137  19.500  -7.674  1.00 15.76           O  
ANISOU 5141  O   PRO A 340     1861   2188   1938   -128     31    246       O  
ATOM   5142  CB  PRO A 340      -4.305  21.817  -8.738  1.00 15.64           C  
ANISOU 5142  CB  PRO A 340     1852   2140   1950    -27     29    189       C  
ATOM   5143  CG  PRO A 340      -4.589  22.631  -9.997  1.00 13.24           C  
ANISOU 5143  CG  PRO A 340     1546   1829   1654     -7     27    155       C  
ATOM   5144  CD  PRO A 340      -5.684  21.879 -10.711  1.00 13.46           C  
ANISOU 5144  CD  PRO A 340     1574   1857   1682    -41     26    154       C  
ATOM   5145  HA  PRO A 340      -3.655  20.016  -9.550  1.00 19.77           H  
ATOM   5146  HB2 PRO A 340      -4.937  22.028  -8.033  1.00 18.77           H  
ATOM   5147  HB3 PRO A 340      -3.398  21.957  -8.424  1.00 18.77           H  
ATOM   5148  HG2 PRO A 340      -4.882  23.523  -9.755  1.00 15.88           H  
ATOM   5149  HG3 PRO A 340      -3.789  22.681 -10.545  1.00 15.88           H  
ATOM   5150  HD2 PRO A 340      -6.557  22.202 -10.439  1.00 16.15           H  
ATOM   5151  HD3 PRO A 340      -5.586  21.959 -11.673  1.00 16.15           H  
ATOM   5152  N   VAL A 341      -4.038  18.667  -7.543  1.00 14.27           N  
ANISOU 5152  N   VAL A 341     1724   1914   1785   -100     24    277       N  
ATOM   5153  CA  VAL A 341      -4.347  17.801  -6.409  1.00 14.87           C  
ANISOU 5153  CA  VAL A 341     1800   2006   1844   -137     22    316       C  
ATOM   5154  C   VAL A 341      -4.788  18.637  -5.217  1.00 15.48           C  
ANISOU 5154  C   VAL A 341     1838   2158   1886   -139     28    316       C  
ATOM   5155  O   VAL A 341      -5.780  18.331  -4.543  1.00 16.09           O  
ANISOU 5155  O   VAL A 341     1896   2282   1936   -177     31    331       O  
ATOM   5156  CB  VAL A 341      -3.134  16.927  -6.048  1.00 15.29           C  
ANISOU 5156  CB  VAL A 341     1886   2006   1917   -127     14    350       C  
ATOM   5157  CG1 VAL A 341      -3.406  16.162  -4.736  1.00 16.51           C  
ANISOU 5157  CG1 VAL A 341     2040   2183   2050   -164     10    396       C  
ATOM   5158  CG2 VAL A 341      -2.805  15.986  -7.190  1.00 14.95           C  
ANISOU 5158  CG2 VAL A 341     1884   1889   1908   -126     10    348       C  
ATOM   5159  H   VAL A 341      -3.228  18.603  -7.825  1.00 17.13           H  
ATOM   5160  HA  VAL A 341      -5.078  17.216  -6.663  1.00 17.85           H  
ATOM   5161  HB  VAL A 341      -2.356  17.488  -5.905  1.00 18.34           H  
ATOM   5162 HG11 VAL A 341      -2.806  15.402  -4.684  1.00 19.81           H  
ATOM   5163 HG12 VAL A 341      -3.252  16.758  -3.986  1.00 19.81           H  
ATOM   5164 HG13 VAL A 341      -4.327  15.857  -4.734  1.00 19.81           H  
ATOM   5165 HG21 VAL A 341      -1.986  15.510  -6.981  1.00 17.94           H  
ATOM   5166 HG22 VAL A 341      -3.534  15.356  -7.300  1.00 17.94           H  
ATOM   5167 HG23 VAL A 341      -2.689  16.503  -8.002  1.00 17.94           H  
ATOM   5168  N   VAL A 342      -4.040  19.691  -4.922  1.00 13.57           N  
ANISOU 5168  N   VAL A 342     1584   1930   1640    -99     29    298       N  
ATOM   5169  CA  VAL A 342      -4.393  20.642  -3.875  1.00 15.98           C  
ANISOU 5169  CA  VAL A 342     1856   2304   1912    -93     34    288       C  
ATOM   5170  C   VAL A 342      -5.341  21.639  -4.536  1.00 14.31           C  
ANISOU 5170  C   VAL A 342     1620   2124   1694    -80     40    245       C  
ATOM   5171  O   VAL A 342      -4.916  22.553  -5.249  1.00 14.36           O  
ANISOU 5171  O   VAL A 342     1630   2112   1715    -44     38    214       O  
ATOM   5172  CB  VAL A 342      -3.137  21.279  -3.280  1.00 13.92           C  
ANISOU 5172  CB  VAL A 342     1598   2040   1650    -60     30    288       C  
ATOM   5173  CG1 VAL A 342      -3.474  22.438  -2.387  1.00 14.88           C  
ANISOU 5173  CG1 VAL A 342     1688   2226   1738    -49     36    265       C  
ATOM   5174  CG2 VAL A 342      -2.298  20.232  -2.500  1.00 15.87           C  
ANISOU 5174  CG2 VAL A 342     1864   2265   1900    -74     22    336       C  
ATOM   5175  H   VAL A 342      -3.305  19.882  -5.325  1.00 16.28           H  
ATOM   5176  HA  VAL A 342      -4.870  20.217  -3.145  1.00 19.18           H  
ATOM   5177  HB  VAL A 342      -2.604  21.617  -4.017  1.00 16.70           H  
ATOM   5178 HG11 VAL A 342      -2.652  22.830  -2.054  1.00 17.85           H  
ATOM   5179 HG12 VAL A 342      -3.972  23.095  -2.897  1.00 17.85           H  
ATOM   5180 HG13 VAL A 342      -4.012  22.118  -1.645  1.00 17.85           H  
ATOM   5181 HG21 VAL A 342      -1.407  20.587  -2.355  1.00 19.04           H  
ATOM   5182 HG22 VAL A 342      -2.727  20.055  -1.648  1.00 19.04           H  
ATOM   5183 HG23 VAL A 342      -2.248  19.416  -3.022  1.00 19.04           H  
ATOM   5184  N   ALA A 343      -6.637  21.429  -4.335  1.00 13.42           N  
ANISOU 5184  N   ALA A 343     1481   2059   1558   -111     46    245       N  
ATOM   5185  CA  ALA A 343      -7.647  22.200  -5.044  1.00 13.93           C  
ANISOU 5185  CA  ALA A 343     1522   2154   1619   -100     50    209       C  
ATOM   5186  C   ALA A 343      -7.855  23.557  -4.387  1.00 16.82           C  
ANISOU 5186  C   ALA A 343     1857   2574   1961    -66     55    177       C  
ATOM   5187  O   ALA A 343      -7.808  23.704  -3.163  1.00 17.65           O  
ANISOU 5187  O   ALA A 343     1947   2722   2038    -70     61    186       O  
ATOM   5188  CB  ALA A 343      -8.978  21.447  -5.074  1.00 14.89           C  
ANISOU 5188  CB  ALA A 343     1622   2313   1724   -147     54    221       C  
ATOM   5189  H   ALA A 343      -6.958  20.843  -3.793  1.00 16.10           H  
ATOM   5190  HA  ALA A 343      -7.350  22.342  -5.957  1.00 16.72           H  
ATOM   5191  HB1 ALA A 343      -9.593  21.917  -5.659  1.00 17.87           H  
ATOM   5192  HB2 ALA A 343      -8.826  20.549  -5.408  1.00 17.87           H  
ATOM   5193  HB3 ALA A 343      -9.340  21.409  -4.175  1.00 17.87           H  
ATOM   5194  N   ARG A 344      -8.120  24.553  -5.224  1.00 14.69           N  
ANISOU 5194  N   ARG A 344     1580   2301   1701    -31     53    140       N  
ATOM   5195  CA  ARG A 344      -8.381  25.905  -4.762  1.00 15.25           C  
ANISOU 5195  CA  ARG A 344     1628   2413   1754      7     56    105       C  
ATOM   5196  C   ARG A 344      -9.541  26.466  -5.563  1.00 19.67           C  
ANISOU 5196  C   ARG A 344     2162   2999   2312     21     56     77       C  
ATOM   5197  O   ARG A 344      -9.721  26.133  -6.733  1.00 20.96           O  
ANISOU 5197  O   ARG A 344     2338   3130   2498     15     49     78       O  
ATOM   5198  CB  ARG A 344      -7.139  26.786  -4.901  1.00 20.32           C  
ANISOU 5198  CB  ARG A 344     2296   3012   2412     45     48     90       C  
ATOM   5199  CG  ARG A 344      -5.952  26.256  -4.123  1.00 30.76           C  
ANISOU 5199  CG  ARG A 344     3638   4313   3735     33     47    119       C  
ATOM   5200  CD  ARG A 344      -5.174  27.357  -3.450  1.00 47.82           C  
ANISOU 5200  CD  ARG A 344     5804   6481   5887     63     44     99       C  
ATOM   5201  NE  ARG A 344      -3.937  26.862  -2.851  1.00 35.20           N  
ANISOU 5201  NE  ARG A 344     4224   4861   4291     53     40    128       N  
ATOM   5202  CZ  ARG A 344      -2.750  26.860  -3.457  1.00 50.73           C  
ANISOU 5202  CZ  ARG A 344     6217   6774   6285     66     31    135       C  
ATOM   5203  NH1 ARG A 344      -2.620  27.319  -4.694  1.00 43.53           N  
ANISOU 5203  NH1 ARG A 344     5319   5823   5398     85     26    116       N  
ATOM   5204  NH2 ARG A 344      -1.686  26.399  -2.816  1.00 33.36           N  
ANISOU 5204  NH2 ARG A 344     4027   4563   4084     59     27    163       N  
ATOM   5205  H   ARG A 344      -8.154  24.465  -6.079  1.00 17.63           H  
ATOM   5206  HA  ARG A 344      -8.634  25.907  -3.826  1.00 18.30           H  
ATOM   5207  HB2 ARG A 344      -6.888  26.832  -5.837  1.00 24.38           H  
ATOM   5208  HB3 ARG A 344      -7.344  27.674  -4.569  1.00 24.38           H  
ATOM   5209  HG2 ARG A 344      -6.268  25.646  -3.438  1.00 36.91           H  
ATOM   5210  HG3 ARG A 344      -5.355  25.792  -4.730  1.00 36.91           H  
ATOM   5211  HD2 ARG A 344      -4.944  28.033  -4.107  1.00 57.39           H  
ATOM   5212  HD3 ARG A 344      -5.716  27.748  -2.747  1.00 57.39           H  
ATOM   5213  HE  ARG A 344      -3.977  26.550  -2.051  1.00 42.24           H  
ATOM   5214 HH11 ARG A 344      -3.306  27.623  -5.114  1.00 52.24           H  
ATOM   5215 HH12 ARG A 344      -1.849  27.313  -5.076  1.00 52.24           H  
ATOM   5216 HH21 ARG A 344      -1.763  26.102  -2.013  1.00 40.03           H  
ATOM   5217 HH22 ARG A 344      -0.919  26.396  -3.204  1.00 40.03           H  
ATOM   5218  N   ASP A 345     -10.354  27.279  -4.905  1.00 16.50           N  
ANISOU 5218  N   ASP A 345     1725   2661   1884     41     63     52       N  
ATOM   5219  CA  ASP A 345     -11.391  28.037  -5.583  1.00 17.81           C  
ANISOU 5219  CA  ASP A 345     1864   2854   2048     68     60     20       C  
ATOM   5220  C   ASP A 345     -10.954  29.489  -5.692  1.00 20.58           C  
ANISOU 5220  C   ASP A 345     2227   3186   2407    125     53    -16       C  
ATOM   5221  O   ASP A 345     -10.463  30.076  -4.725  1.00 24.86           O  
ANISOU 5221  O   ASP A 345     2771   3739   2934    143     57    -28       O  
ATOM   5222  CB  ASP A 345     -12.725  27.976  -4.837  1.00 23.46           C  
ANISOU 5222  CB  ASP A 345     2527   3660   2728     56     73     14       C  
ATOM   5223  CG  ASP A 345     -13.339  26.598  -4.848  1.00 29.17           C  
ANISOU 5223  CG  ASP A 345     3237   4405   3442     -6     78     49       C  
ATOM   5224  OD1 ASP A 345     -13.177  25.887  -5.861  1.00 24.97           O  
ANISOU 5224  OD1 ASP A 345     2728   3823   2935    -29     69     66       O  
ATOM   5225  OD2 ASP A 345     -13.969  26.227  -3.833  1.00 29.57           O  
ANISOU 5225  OD2 ASP A 345     3254   4523   3459    -34     91     60       O  
ATOM   5226  H   ASP A 345     -10.323  27.408  -4.055  1.00 19.81           H  
ATOM   5227  HA  ASP A 345     -11.527  27.664  -6.468  1.00 21.37           H  
ATOM   5228  HB2 ASP A 345     -12.582  28.233  -3.913  1.00 28.16           H  
ATOM   5229  HB3 ASP A 345     -13.351  28.586  -5.258  1.00 28.16           H  
ATOM   5230  N   VAL A 346     -11.146  30.073  -6.860  1.00 17.25           N  
ANISOU 5230  N   VAL A 346     1813   2735   2006    152     41    -33       N  
ATOM   5231  CA  VAL A 346     -10.857  31.484  -7.085  1.00 13.90           C  
ANISOU 5231  CA  VAL A 346     1402   2288   1590    205     31    -67       C  
ATOM   5232  C   VAL A 346     -12.183  32.232  -7.037  1.00 15.31           C  
ANISOU 5232  C   VAL A 346     1540   2525   1753    239     32    -97       C  
ATOM   5233  O   VAL A 346     -13.128  31.825  -7.725  1.00 19.29           O  
ANISOU 5233  O   VAL A 346     2018   3053   2257    228     31    -92       O  
ATOM   5234  CB  VAL A 346     -10.154  31.708  -8.434  1.00 15.28           C  
ANISOU 5234  CB  VAL A 346     1614   2392   1798    214     16    -64       C  
ATOM   5235  CG1 VAL A 346      -9.927  33.183  -8.650  1.00 19.31           C  
ANISOU 5235  CG1 VAL A 346     2142   2880   2317    265      3    -95       C  
ATOM   5236  CG2 VAL A 346      -8.833  30.938  -8.489  1.00 15.87           C  
ANISOU 5236  CG2 VAL A 346     1725   2416   1889    185     16    -35       C  
ATOM   5237  H   VAL A 346     -11.450  29.665  -7.554  1.00 20.70           H  
ATOM   5238  HA  VAL A 346     -10.278  31.821  -6.384  1.00 16.68           H  
ATOM   5239  HB  VAL A 346     -10.716  31.373  -9.150  1.00 18.33           H  
ATOM   5240 HG11 VAL A 346      -9.153  33.303  -9.221  1.00 23.18           H  
ATOM   5241 HG12 VAL A 346     -10.713  33.564  -9.072  1.00 23.18           H  
ATOM   5242 HG13 VAL A 346      -9.774  33.608  -7.791  1.00 23.18           H  
ATOM   5243 HG21 VAL A 346      -8.464  31.009  -9.384  1.00 19.04           H  
ATOM   5244 HG22 VAL A 346      -8.217  31.322  -7.846  1.00 19.04           H  
ATOM   5245 HG23 VAL A 346      -9.000  30.008  -8.273  1.00 19.04           H  
ATOM   5246  N   PRO A 347     -12.306  33.290  -6.237  1.00 17.15           N  
ANISOU 5246  N   PRO A 347     1764   2782   1970    280     35   -129       N  
ATOM   5247  CA  PRO A 347     -13.557  34.056  -6.226  1.00 21.49           C  
ANISOU 5247  CA  PRO A 347     2275   3386   2506    322     36   -162       C  
ATOM   5248  C   PRO A 347     -13.830  34.624  -7.604  1.00 23.37           C  
ANISOU 5248  C   PRO A 347     2524   3586   2771    351     16   -169       C  
ATOM   5249  O   PRO A 347     -12.955  35.217  -8.236  1.00 20.31           O  
ANISOU 5249  O   PRO A 347     2181   3130   2408    368      0   -171       O  
ATOM   5250  CB  PRO A 347     -13.299  35.167  -5.203  1.00 26.53           C  
ANISOU 5250  CB  PRO A 347     2919   4034   3129    364     39   -198       C  
ATOM   5251  CG  PRO A 347     -12.169  34.694  -4.398  1.00 21.96           C  
ANISOU 5251  CG  PRO A 347     2366   3434   2544    330     46   -179       C  
ATOM   5252  CD  PRO A 347     -11.336  33.805  -5.258  1.00 18.58           C  
ANISOU 5252  CD  PRO A 347     1969   2947   2143    290     38   -140       C  
ATOM   5253  HA  PRO A 347     -14.300  33.511  -5.925  1.00 25.79           H  
ATOM   5254  HB2 PRO A 347     -13.076  35.992  -5.662  1.00 31.84           H  
ATOM   5255  HB3 PRO A 347     -14.087  35.296  -4.651  1.00 31.84           H  
ATOM   5256  HG2 PRO A 347     -11.648  35.457  -4.100  1.00 26.36           H  
ATOM   5257  HG3 PRO A 347     -12.505  34.203  -3.632  1.00 26.36           H  
ATOM   5258  HD2 PRO A 347     -10.633  34.308  -5.698  1.00 22.29           H  
ATOM   5259  HD3 PRO A 347     -10.951  33.082  -4.739  1.00 22.29           H  
ATOM   5260  N   LEU A 348     -15.048  34.424  -8.070  1.00 22.50           N  
ANISOU 5260  N   LEU A 348     2371   3524   2653    354     15   -171       N  
ATOM   5261  CA  LEU A 348     -15.475  34.864  -9.391  1.00 26.57           C  
ANISOU 5261  CA  LEU A 348     2890   4016   3189    379     -5   -175       C  
ATOM   5262  C   LEU A 348     -16.861  35.464  -9.252  1.00 40.11           C  
ANISOU 5262  C   LEU A 348     4550   5802   4886    422     -5   -202       C  
ATOM   5263  O   LEU A 348     -17.823  35.045  -9.904  1.00 68.23           O  
ANISOU 5263  O   LEU A 348     8076   9404   8444    412     -9   -193       O  
ATOM   5264  CB  LEU A 348     -15.429  33.712 -10.384  1.00 39.43           C  
ANISOU 5264  CB  LEU A 348     4525   5626   4829    325     -9   -140       C  
ATOM   5265  CG  LEU A 348     -14.399  33.787 -11.516  1.00 46.09           C  
ANISOU 5265  CG  LEU A 348     5423   6387   5704    320    -25   -127       C  
ATOM   5266  CD1 LEU A 348     -14.845  32.828 -12.603  1.00 34.36           C  
ANISOU 5266  CD1 LEU A 348     3930   4903   4224    280    -31   -105       C  
ATOM   5267  CD2 LEU A 348     -14.241  35.189 -12.066  1.00 35.15           C  
ANISOU 5267  CD2 LEU A 348     4060   4963   4333    377    -45   -150       C  
ATOM   5268  H   LEU A 348     -15.666  34.024  -7.627  1.00 27.00           H  
ATOM   5269  HA  LEU A 348     -14.880  35.549  -9.734  1.00 31.88           H  
ATOM   5270  HB2 LEU A 348     -15.240  32.901  -9.887  1.00 47.31           H  
ATOM   5271  HB3 LEU A 348     -16.301  33.649 -10.804  1.00 47.31           H  
ATOM   5272  HG  LEU A 348     -13.524  33.540 -11.179  1.00 55.31           H  
ATOM   5273 HD11 LEU A 348     -14.063  32.491 -13.067  1.00 41.24           H  
ATOM   5274 HD12 LEU A 348     -15.331  32.093 -12.197  1.00 41.24           H  
ATOM   5275 HD13 LEU A 348     -15.420  33.301 -13.225  1.00 41.24           H  
ATOM   5276 HD21 LEU A 348     -13.839  35.139 -12.947  1.00 42.18           H  
ATOM   5277 HD22 LEU A 348     -15.115  35.606 -12.125  1.00 42.18           H  
ATOM   5278 HD23 LEU A 348     -13.671  35.700 -11.471  1.00 42.18           H  
ATOM   5279  N   SER A 349     -16.984  36.423  -8.345  1.00 62.41           N  
ANISOU 5279  N   SER A 349     7368   8648   7698    472      1   -236       N  
ATOM   5280  CA  SER A 349     -18.247  37.087  -8.051  1.00 81.73           C  
ANISOU 5280  CA  SER A 349     9762  11165  10127    524      4   -268       C  
ATOM   5281  C   SER A 349     -18.102  38.542  -8.477  1.00 32.78           C  
ANISOU 5281  C   SER A 349     3593   4914   3947    597    -18   -299       C  
ATOM   5282  O   SER A 349     -17.344  39.301  -7.864  1.00 58.71           O  
ANISOU 5282  O   SER A 349     6916   8158   7235    622    -19   -320       O  
ATOM   5283  CB  SER A 349     -18.592  36.977  -6.569  1.00 51.62           C  
ANISOU 5283  CB  SER A 349     5911   7425   6276    523     30   -286       C  
ATOM   5284  OG  SER A 349     -17.985  35.837  -5.985  1.00111.07           O  
ANISOU 5284  OG  SER A 349    13450  14959  13795    453     46   -255       O  
ATOM   5285  H   SER A 349     -16.327  36.714  -7.871  1.00 74.89           H  
ATOM   5286  HA  SER A 349     -18.965  36.676  -8.557  1.00 98.08           H  
ATOM   5287  HB2 SER A 349     -18.274  37.771  -6.112  1.00 61.94           H  
ATOM   5288  HB3 SER A 349     -19.555  36.903  -6.475  1.00 61.94           H  
ATOM   5289  HG  SER A 349     -18.102  35.845  -5.153  1.00133.29           H  
ATOM   5290  N   GLY A 350     -18.818  38.920  -9.530  1.00 45.07           N  
ANISOU 5290  N   GLY A 350     5143   6465   5518    622    -38   -297       N  
ATOM   5291  CA  GLY A 350     -18.740  40.271 -10.039  1.00 84.82           C  
ANISOU 5291  CA  GLY A 350    10219  11436  10572    679    -63   -316       C  
ATOM   5292  C   GLY A 350     -17.510  40.599 -10.850  1.00 82.21           C  
ANISOU 5292  C   GLY A 350     9946  11018  10273    682    -83   -304       C  
ATOM   5293  O   GLY A 350     -17.099  41.764 -10.880  1.00 35.57           O  
ANISOU 5293  O   GLY A 350     4085   5050   4379    722   -100   -322       O  
ATOM   5294  H   GLY A 350     -19.356  38.410  -9.966  1.00 54.09           H  
ATOM   5295  HA2 GLY A 350     -19.513  40.431 -10.603  1.00101.78           H  
ATOM   5296  HA3 GLY A 350     -18.766  40.883  -9.287  1.00101.78           H  
ATOM   5297  N   PHE A 351     -16.902  39.612 -11.512  1.00 74.08           N  
ANISOU 5297  N   PHE A 351     8932   9963   9252    621    -83   -267       N  
ATOM   5298  CA  PHE A 351     -15.815  39.913 -12.432  1.00 57.52           C  
ANISOU 5298  CA  PHE A 351     6896   7777   7181    609   -102   -249       C  
ATOM   5299  C   PHE A 351     -16.373  40.561 -13.693  1.00 45.33           C  
ANISOU 5299  C   PHE A 351     5356   6214   5652    645   -131   -246       C  
ATOM   5300  O   PHE A 351     -17.396  40.128 -14.232  1.00 46.85           O  
ANISOU 5300  O   PHE A 351     5504   6459   5838    643   -134   -238       O  
ATOM   5301  CB  PHE A 351     -15.027  38.663 -12.834  1.00 73.13           C  
ANISOU 5301  CB  PHE A 351     8890   9733   9162    536    -93   -213       C  
ATOM   5302  CG  PHE A 351     -14.038  38.915 -13.957  1.00 80.68           C  
ANISOU 5302  CG  PHE A 351     9901  10612  10143    524   -112   -194       C  
ATOM   5303  CD1 PHE A 351     -12.743  39.323 -13.680  1.00 45.01           C  
ANISOU 5303  CD1 PHE A 351     5433   6033   5635    517   -113   -194       C  
ATOM   5304  CD2 PHE A 351     -14.413  38.774 -15.288  1.00 37.70           C  
ANISOU 5304  CD2 PHE A 351     4457   5160   4709    518   -130   -177       C  
ATOM   5305  CE1 PHE A 351     -11.835  39.574 -14.705  1.00 28.69           C  
ANISOU 5305  CE1 PHE A 351     3412   3901   3587    504   -130   -176       C  
ATOM   5306  CE2 PHE A 351     -13.511  39.032 -16.314  1.00 28.27           C  
ANISOU 5306  CE2 PHE A 351     3311   3899   3532    506   -146   -160       C  
ATOM   5307  CZ  PHE A 351     -12.220  39.427 -16.019  1.00 39.25           C  
ANISOU 5307  CZ  PHE A 351     4749   5232   4931    498   -145   -159       C  
ATOM   5308  H   PHE A 351     -17.098  38.777 -11.445  1.00 88.90           H  
ATOM   5309  HA  PHE A 351     -15.200  40.514 -11.983  1.00 69.02           H  
ATOM   5310  HB2 PHE A 351     -14.530  38.344 -12.064  1.00 87.75           H  
ATOM   5311  HB3 PHE A 351     -15.650  37.981 -13.132  1.00 87.75           H  
ATOM   5312  HD1 PHE A 351     -12.476  39.431 -12.795  1.00 54.01           H  
ATOM   5313  HD2 PHE A 351     -15.278  38.504 -15.495  1.00 45.24           H  
ATOM   5314  HE1 PHE A 351     -10.968  39.842 -14.502  1.00 34.43           H  
ATOM   5315  HE2 PHE A 351     -13.776  38.938 -17.201  1.00 33.92           H  
ATOM   5316  HZ  PHE A 351     -11.614  39.593 -16.704  1.00 47.10           H  
ATOM   5317  N   ALA A 352     -15.677  41.587 -14.173  1.00 62.67           N  
ANISOU 5317  N   ALA A 352     7607   8338   7869    673   -153   -249       N  
ATOM   5318  CA  ALA A 352     -16.028  42.238 -15.425  1.00 35.02           C  
ANISOU 5318  CA  ALA A 352     4118   4806   4382    703   -184   -240       C  
ATOM   5319  C   ALA A 352     -14.784  42.904 -15.992  1.00 44.71           C  
ANISOU 5319  C   ALA A 352     5417   5943   5629    695   -202   -228       C  
ATOM   5320  O   ALA A 352     -13.885  43.309 -15.249  1.00 36.68           O  
ANISOU 5320  O   ALA A 352     4435   4887   4614    693   -196   -240       O  
ATOM   5321  CB  ALA A 352     -17.145  43.268 -15.237  1.00 43.25           C  
ANISOU 5321  CB  ALA A 352     5143   5869   5420    764   -194   -264       C  
ATOM   5322  H   ALA A 352     -14.990  41.929 -13.786  1.00 75.21           H  
ATOM   5323  HA  ALA A 352     -16.337  41.572 -16.059  1.00 42.02           H  
ATOM   5324  HB1 ALA A 352     -17.285  43.738 -16.074  1.00 51.90           H  
ATOM   5325  HB2 ALA A 352     -17.958  42.807 -14.976  1.00 51.90           H  
ATOM   5326  HB3 ALA A 352     -16.883  43.895 -14.545  1.00 51.90           H  
ATOM   5327  N   LYS A 353     -14.751  43.012 -17.316  1.00 33.22           N  
ANISOU 5327  N   LYS A 353     3980   4458   4185    688   -225   -203       N  
ATOM   5328  CA  LYS A 353     -13.636  43.639 -18.012  1.00 40.84           C  
ANISOU 5328  CA  LYS A 353     5009   5342   5165    676   -244   -187       C  
ATOM   5329  C   LYS A 353     -13.588  45.133 -17.717  1.00 37.28           C  
ANISOU 5329  C   LYS A 353     4596   4844   4726    736   -266   -209       C  
ATOM   5330  O   LYS A 353     -14.589  45.837 -17.887  1.00 40.03           O  
ANISOU 5330  O   LYS A 353     4930   5204   5075    782   -281   -220       O  
ATOM   5331  CB  LYS A 353     -13.778  43.389 -19.514  1.00 32.18           C  
ANISOU 5331  CB  LYS A 353     3917   4237   4072    656   -263   -156       C  
ATOM   5332  CG  LYS A 353     -12.893  44.243 -20.390  1.00 30.23           C  
ANISOU 5332  CG  LYS A 353     3732   3915   3839    653   -289   -137       C  
ATOM   5333  CD  LYS A 353     -13.180  44.027 -21.868  1.00 37.29           C  
ANISOU 5333  CD  LYS A 353     4626   4810   4731    637   -308   -108       C  
ATOM   5334  CE  LYS A 353     -12.072  44.639 -22.728  1.00 41.90           C  
ANISOU 5334  CE  LYS A 353     5272   5325   5324    615   -327    -84       C  
ATOM   5335  NZ  LYS A 353     -12.565  45.167 -24.032  1.00 58.41           N  
ANISOU 5335  NZ  LYS A 353     7373   7404   7414    631   -361    -61       N  
ATOM   5336  H   LYS A 353     -15.370  42.728 -17.842  1.00 39.87           H  
ATOM   5337  HA  LYS A 353     -12.798  43.256 -17.708  1.00 49.01           H  
ATOM   5338  HB2 LYS A 353     -13.558  42.462 -19.693  1.00 38.61           H  
ATOM   5339  HB3 LYS A 353     -14.697  43.567 -19.768  1.00 38.61           H  
ATOM   5340  HG2 LYS A 353     -13.046  45.178 -20.185  1.00 36.27           H  
ATOM   5341  HG3 LYS A 353     -11.965  44.015 -20.225  1.00 36.27           H  
ATOM   5342  HD2 LYS A 353     -13.226  43.076 -22.055  1.00 44.74           H  
ATOM   5343  HD3 LYS A 353     -14.021  44.452 -22.101  1.00 44.74           H  
ATOM   5344  HE2 LYS A 353     -11.667  45.375 -22.243  1.00 50.28           H  
ATOM   5345  HE3 LYS A 353     -11.406  43.958 -22.915  1.00 50.28           H  
ATOM   5346  HZ1 LYS A 353     -13.179  45.796 -23.893  1.00 70.09           H  
ATOM   5347  HZ2 LYS A 353     -11.890  45.519 -24.493  1.00 70.09           H  
ATOM   5348  HZ3 LYS A 353     -12.929  44.509 -24.509  1.00 70.09           H  
ATOM   5349  N   ARG A 354     -12.420  45.613 -17.297  1.00 30.20           N  
ANISOU 5349  N   ARG A 354     3749   3890   3836    721   -266   -213       N  
ATOM   5350  CA  ARG A 354     -12.176  47.018 -17.008  1.00 26.83           C  
ANISOU 5350  CA  ARG A 354     3370   3405   3421    766   -288   -233       C  
ATOM   5351  C   ARG A 354     -10.778  47.416 -17.453  1.00 31.21           C  
ANISOU 5351  C   ARG A 354     3987   3885   3985    726   -301   -213       C  
ATOM   5352  O   ARG A 354      -9.890  46.566 -17.576  1.00 23.02           O  
ANISOU 5352  O   ARG A 354     2952   2850   2943    666   -283   -192       O  
ATOM   5353  CB  ARG A 354     -12.313  47.324 -15.509  1.00 33.12           C  
ANISOU 5353  CB  ARG A 354     4156   4221   4206    787   -269   -273       C  
ATOM   5354  CG  ARG A 354     -13.646  46.943 -14.892  1.00 45.89           C  
ANISOU 5354  CG  ARG A 354     5710   5918   5807    811   -249   -293       C  
ATOM   5355  CD  ARG A 354     -13.724  47.433 -13.447  1.00 86.67           C  
ANISOU 5355  CD  ARG A 354    10874  11098  10959    833   -233   -334       C  
ATOM   5356  NE  ARG A 354     -12.477  47.158 -12.737  1.00 78.53           N  
ANISOU 5356  NE  ARG A 354     9869  10043   9926    805   -222   -339       N  
ATOM   5357  CZ  ARG A 354     -12.215  46.032 -12.080  1.00 98.15           C  
ANISOU 5357  CZ  ARG A 354    12319  12577  12396    770   -194   -336       C  
ATOM   5358  NH1 ARG A 354     -13.119  45.063 -12.018  1.00 88.68           N  
ANISOU 5358  NH1 ARG A 354    11059  11454  11183    762   -175   -330       N  
ATOM   5359  NH2 ARG A 354     -11.043  45.876 -11.480  1.00 48.01           N  
ANISOU 5359  NH2 ARG A 354     5999   6202   6042    728   -184   -333       N  
ATOM   5360  H   ARG A 354     -11.728  45.119 -17.167  1.00 36.24           H  
ATOM   5361  HA  ARG A 354     -12.819  47.542 -17.511  1.00 32.20           H  
ATOM   5362  HB2 ARG A 354     -11.623  46.837 -15.032  1.00 39.74           H  
ATOM   5363  HB3 ARG A 354     -12.195  48.278 -15.379  1.00 39.74           H  
ATOM   5364  HG2 ARG A 354     -14.367  47.352 -15.397  1.00 55.07           H  
ATOM   5365  HG3 ARG A 354     -13.743  45.978 -14.898  1.00 55.07           H  
ATOM   5366  HD2 ARG A 354     -13.880  48.390 -13.438  1.00104.01           H  
ATOM   5367  HD3 ARG A 354     -14.447  46.975 -12.989  1.00104.01           H  
ATOM   5368  HE  ARG A 354     -11.870  47.767 -12.745  1.00 94.23           H  
ATOM   5369 HH11 ARG A 354     -13.881  45.160 -12.405  1.00106.42           H  
ATOM   5370 HH12 ARG A 354     -12.944  44.337 -11.591  1.00106.42           H  
ATOM   5371 HH21 ARG A 354     -10.455  46.502 -11.517  1.00 57.61           H  
ATOM   5372 HH22 ARG A 354     -10.871  45.149 -11.054  1.00 57.61           H  
ATOM   5373  N   PRO A 355     -10.539  48.711 -17.656  1.00 33.09           N  
ANISOU 5373  N   PRO A 355     4278   4058   4235    754   -329   -218       N  
ATOM   5374  CA  PRO A 355      -9.173  49.154 -17.975  1.00 26.24           C  
ANISOU 5374  CA  PRO A 355     3472   3124   3376    713   -342   -199       C  
ATOM   5375  C   PRO A 355      -8.129  48.663 -16.984  1.00 32.46           C  
ANISOU 5375  C   PRO A 355     4262   3916   4154    668   -315   -208       C  
ATOM   5376  O   PRO A 355      -6.997  48.375 -17.391  1.00 32.63           O  
ANISOU 5376  O   PRO A 355     4307   3914   4176    613   -312   -182       O  
ATOM   5377  CB  PRO A 355      -9.292  50.685 -17.966  1.00 34.55           C  
ANISOU 5377  CB  PRO A 355     4574   4115   4438    748   -370   -212       C  
ATOM   5378  CG  PRO A 355     -10.739  50.950 -18.254  1.00 35.16           C  
ANISOU 5378  CG  PRO A 355     4617   4228   4515    792   -374   -218       C  
ATOM   5379  CD  PRO A 355     -11.494  49.834 -17.599  1.00 49.97           C  
ANISOU 5379  CD  PRO A 355     6422   6186   6376    800   -344   -235       C  
ATOM   5380  HA  PRO A 355      -8.929  48.859 -18.866  1.00 31.49           H  
ATOM   5381  HB2 PRO A 355      -9.040  51.033 -17.096  1.00 41.46           H  
ATOM   5382  HB3 PRO A 355      -8.724  51.067 -18.653  1.00 41.46           H  
ATOM   5383  HG2 PRO A 355     -10.996  51.807 -17.878  1.00 42.19           H  
ATOM   5384  HG3 PRO A 355     -10.888  50.950 -19.212  1.00 42.19           H  
ATOM   5385  HD2 PRO A 355     -11.713  50.056 -16.680  1.00 59.96           H  
ATOM   5386  HD3 PRO A 355     -12.303  49.627 -18.092  1.00 59.96           H  
ATOM   5387  N   ASP A 356      -8.461  48.536 -15.703  1.00 25.52           N  
ANISOU 5387  N   ASP A 356     3357   3072   3266    690   -295   -243       N  
ATOM   5388  CA  ASP A 356      -7.460  48.144 -14.721  1.00 22.71           C  
ANISOU 5388  CA  ASP A 356     3007   2722   2901    649   -274   -250       C  
ATOM   5389  C   ASP A 356      -7.303  46.630 -14.577  1.00 26.10           C  
ANISOU 5389  C   ASP A 356     3389   3210   3319    603   -242   -232       C  
ATOM   5390  O   ASP A 356      -6.551  46.181 -13.706  1.00 24.68           O  
ANISOU 5390  O   ASP A 356     3206   3043   3129    572   -223   -236       O  
ATOM   5391  CB  ASP A 356      -7.774  48.757 -13.355  1.00 25.24           C  
ANISOU 5391  CB  ASP A 356     3328   3051   3212    688   -268   -297       C  
ATOM   5392  CG  ASP A 356      -9.105  48.309 -12.804  1.00 41.85           C  
ANISOU 5392  CG  ASP A 356     5372   5226   5304    731   -250   -321       C  
ATOM   5393  OD1 ASP A 356      -9.757  47.441 -13.419  1.00 51.44           O  
ANISOU 5393  OD1 ASP A 356     6544   6485   6517    724   -242   -300       O  
ATOM   5394  OD2 ASP A 356      -9.503  48.833 -11.746  1.00 91.72           O  
ANISOU 5394  OD2 ASP A 356    11684  11556  11610    771   -245   -362       O  
ATOM   5395  H   ASP A 356      -9.249  48.670 -15.386  1.00 30.62           H  
ATOM   5396  HA  ASP A 356      -6.608  48.499 -15.019  1.00 27.26           H  
ATOM   5397  HB2 ASP A 356      -7.086  48.493 -12.724  1.00 30.29           H  
ATOM   5398  HB3 ASP A 356      -7.795  49.723 -13.439  1.00 30.29           H  
ATOM   5399  N   ASN A 357      -7.988  45.833 -15.397  1.00 21.90           N  
ANISOU 5399  N   ASN A 357     2821   2712   2786    599   -237   -212       N  
ATOM   5400  CA  ASN A 357      -7.758  44.393 -15.370  1.00 16.62           C  
ANISOU 5400  CA  ASN A 357     2117   2087   2110    552   -210   -192       C  
ATOM   5401  C   ASN A 357      -7.625  43.813 -16.774  1.00 16.07           C  
ANISOU 5401  C   ASN A 357     2050   2010   2047    521   -216   -158       C  
ATOM   5402  O   ASN A 357      -7.786  42.603 -16.950  1.00 17.80           O  
ANISOU 5402  O   ASN A 357     2236   2268   2261    492   -197   -144       O  
ATOM   5403  CB  ASN A 357      -8.860  43.659 -14.583  1.00 19.81           C  
ANISOU 5403  CB  ASN A 357     2464   2562   2500    568   -189   -208       C  
ATOM   5404  CG  ASN A 357     -10.239  43.754 -15.230  1.00 34.40           C  
ANISOU 5404  CG  ASN A 357     4281   4441   4348    606   -200   -212       C  
ATOM   5405  OD1 ASN A 357     -10.376  44.108 -16.397  1.00 23.09           O  
ANISOU 5405  OD1 ASN A 357     2865   2981   2926    613   -222   -195       O  
ATOM   5406  ND2 ASN A 357     -11.270  43.424 -14.464  1.00 27.85           N  
ANISOU 5406  ND2 ASN A 357     3402   3674   3504    630   -185   -232       N  
ATOM   5407  H   ASN A 357      -8.578  46.099 -15.963  1.00 26.28           H  
ATOM   5408  HA  ASN A 357      -6.922  44.229 -14.906  1.00 19.94           H  
ATOM   5409  HB2 ASN A 357      -8.626  42.720 -14.520  1.00 23.77           H  
ATOM   5410  HB3 ASN A 357      -8.921  44.046 -13.696  1.00 23.77           H  
ATOM   5411 HD21 ASN A 357     -12.069  43.460 -14.778  1.00 33.41           H  
ATOM   5412 HD22 ASN A 357     -11.138  43.174 -13.651  1.00 33.41           H  
ATOM   5413  N   THR A 358      -7.298  44.642 -17.770  1.00 17.48           N  
ANISOU 5413  N   THR A 358     2267   2138   2235    525   -242   -143       N  
ATOM   5414  CA  THR A 358      -7.176  44.225 -19.165  1.00 14.75           C  
ANISOU 5414  CA  THR A 358     1927   1786   1892    498   -250   -112       C  
ATOM   5415  C   THR A 358      -5.781  44.562 -19.680  1.00 18.91           C  
ANISOU 5415  C   THR A 358     2499   2263   2423    459   -257    -92       C  
ATOM   5416  O   THR A 358      -5.303  45.681 -19.479  1.00 20.97           O  
ANISOU 5416  O   THR A 358     2800   2478   2689    470   -275    -97       O  
ATOM   5417  CB  THR A 358      -8.225  44.928 -20.038  1.00 16.59           C  
ANISOU 5417  CB  THR A 358     2160   2014   2129    538   -278   -110       C  
ATOM   5418  OG1 THR A 358      -9.540  44.636 -19.550  1.00 22.74           O  
ANISOU 5418  OG1 THR A 358     2891   2847   2903    576   -271   -129       O  
ATOM   5419  CG2 THR A 358      -8.133  44.476 -21.507  1.00 20.39           C  
ANISOU 5419  CG2 THR A 358     2645   2493   2608    507   -286    -77       C  
ATOM   5420  H   THR A 358      -7.137  45.479 -17.654  1.00 20.97           H  
ATOM   5421  HA  THR A 358      -7.304  43.265 -19.224  1.00 17.70           H  
ATOM   5422  HB  THR A 358      -8.061  45.884 -20.003  1.00 19.90           H  
ATOM   5423  HG1 THR A 358      -9.688  43.811 -19.599  1.00 27.29           H  
ATOM   5424 HG21 THR A 358      -8.958  44.687 -21.971  1.00 24.46           H  
ATOM   5425 HG22 THR A 358      -7.398  44.930 -21.948  1.00 24.46           H  
ATOM   5426 HG23 THR A 358      -7.982  43.519 -21.550  1.00 24.46           H  
ATOM   5427  N   LEU A 359      -5.129  43.604 -20.339  1.00 17.53           N  
ANISOU 5427  N   LEU A 359     2317   2098   2244    413   -242    -69       N  
ATOM   5428  CA  LEU A 359      -3.854  43.849 -21.014  1.00 13.95           C  
ANISOU 5428  CA  LEU A 359     1900   1609   1791    375   -248    -47       C  
ATOM   5429  C   LEU A 359      -3.957  43.334 -22.441  1.00 14.11           C  
ANISOU 5429  C   LEU A 359     1917   1637   1806    353   -251    -23       C  
ATOM   5430  O   LEU A 359      -4.129  42.129 -22.647  1.00 15.95           O  
ANISOU 5430  O   LEU A 359     2120   1905   2035    335   -230    -20       O  
ATOM   5431  CB  LEU A 359      -2.689  43.156 -20.299  1.00 16.96           C  
ANISOU 5431  CB  LEU A 359     2277   1998   2170    339   -223    -46       C  
ATOM   5432  CG  LEU A 359      -2.286  43.697 -18.928  1.00 14.76           C  
ANISOU 5432  CG  LEU A 359     2007   1709   1892    348   -221    -66       C  
ATOM   5433  CD1 LEU A 359      -1.274  42.751 -18.293  1.00 18.03           C  
ANISOU 5433  CD1 LEU A 359     2405   2143   2302    314   -195    -61       C  
ATOM   5434  CD2 LEU A 359      -1.742  45.105 -19.007  1.00 17.75           C  
ANISOU 5434  CD2 LEU A 359     2434   2036   2275    351   -247    -67       C  
ATOM   5435  H   LEU A 359      -5.409  42.794 -20.409  1.00 21.03           H  
ATOM   5436  HA  LEU A 359      -3.684  44.804 -21.027  1.00 16.74           H  
ATOM   5437  HB2 LEU A 359      -2.929  42.224 -20.175  1.00 20.35           H  
ATOM   5438  HB3 LEU A 359      -1.907  43.224 -20.869  1.00 20.35           H  
ATOM   5439  HG  LEU A 359      -3.074  43.745 -18.365  1.00 17.71           H  
ATOM   5440 HD11 LEU A 359      -0.518  42.649 -18.892  1.00 21.64           H  
ATOM   5441 HD12 LEU A 359      -0.978  43.126 -17.448  1.00 21.64           H  
ATOM   5442 HD13 LEU A 359      -1.696  41.891 -18.143  1.00 21.64           H  
ATOM   5443 HD21 LEU A 359      -1.066  45.144 -19.701  1.00 21.30           H  
ATOM   5444 HD22 LEU A 359      -2.468  45.713 -19.217  1.00 21.30           H  
ATOM   5445 HD23 LEU A 359      -1.351  45.341 -18.151  1.00 21.30           H  
ATOM   5446  N   ASP A 360      -3.862  44.226 -23.420  1.00 15.17           N  
ANISOU 5446  N   ASP A 360     2084   1738   1940    353   -277     -6       N  
ATOM   5447  CA  ASP A 360      -3.909  43.824 -24.817  1.00 17.38           C  
ANISOU 5447  CA  ASP A 360     2364   2027   2211    330   -282     17       C  
ATOM   5448  C   ASP A 360      -2.508  43.647 -25.374  1.00 14.60           C  
ANISOU 5448  C   ASP A 360     2034   1662   1852    281   -272     37       C  
ATOM   5449  O   ASP A 360      -1.696  44.575 -25.331  1.00 15.83           O  
ANISOU 5449  O   ASP A 360     2224   1781   2009    269   -286     46       O  
ATOM   5450  CB  ASP A 360      -4.655  44.853 -25.668  1.00 15.35           C  
ANISOU 5450  CB  ASP A 360     2129   1749   1954    357   -317     30       C  
ATOM   5451  CG  ASP A 360      -6.148  44.719 -25.557  1.00 24.69           C  
ANISOU 5451  CG  ASP A 360     3278   2963   3138    401   -325     16       C  
ATOM   5452  OD1 ASP A 360      -6.616  44.126 -24.565  1.00 18.71           O  
ANISOU 5452  OD1 ASP A 360     2487   2237   2385    416   -305     -7       O  
ATOM   5453  OD2 ASP A 360      -6.854  45.183 -26.475  1.00 28.36           O  
ANISOU 5453  OD2 ASP A 360     3749   3426   3600    419   -351     30       O  
ATOM   5454  H   ASP A 360      -3.770  45.072 -23.296  1.00 18.20           H  
ATOM   5455  HA  ASP A 360      -4.373  42.974 -24.866  1.00 20.85           H  
ATOM   5456  HB2 ASP A 360      -4.410  45.744 -25.375  1.00 18.42           H  
ATOM   5457  HB3 ASP A 360      -4.410  44.731 -26.599  1.00 18.42           H  
ATOM   5458  N   VAL A 361      -2.242  42.462 -25.915  1.00 13.90           N  
ANISOU 5458  N   VAL A 361     1923   1603   1755    252   -250     42       N  
ATOM   5459  CA  VAL A 361      -1.021  42.202 -26.664  1.00 13.56           C  
ANISOU 5459  CA  VAL A 361     1894   1556   1701    209   -239     60       C  
ATOM   5460  C   VAL A 361      -1.253  42.700 -28.079  1.00 18.37           C  
ANISOU 5460  C   VAL A 361     2523   2159   2298    199   -261     82       C  
ATOM   5461  O   VAL A 361      -2.273  42.364 -28.687  1.00 15.85           O  
ANISOU 5461  O   VAL A 361     2189   1860   1973    212   -268     82       O  
ATOM   5462  CB  VAL A 361      -0.702  40.699 -26.669  1.00 13.28           C  
ANISOU 5462  CB  VAL A 361     1828   1554   1663    189   -206     53       C  
ATOM   5463  CG1 VAL A 361       0.479  40.394 -27.581  1.00 20.00           C  
ANISOU 5463  CG1 VAL A 361     2690   2408   2501    150   -194     69       C  
ATOM   5464  CG2 VAL A 361      -0.418  40.189 -25.256  1.00 14.48           C  
ANISOU 5464  CG2 VAL A 361     1962   1713   1826    196   -186     37       C  
ATOM   5465  H   VAL A 361      -2.764  41.781 -25.861  1.00 16.68           H  
ATOM   5466  HA  VAL A 361      -0.272  42.670 -26.263  1.00 16.27           H  
ATOM   5467  HB  VAL A 361      -1.481  40.232 -27.009  1.00 15.93           H  
ATOM   5468 HG11 VAL A 361       0.676  39.446 -27.537  1.00 24.00           H  
ATOM   5469 HG12 VAL A 361       0.248  40.642 -28.490  1.00 24.00           H  
ATOM   5470 HG13 VAL A 361       1.248  40.906 -27.284  1.00 24.00           H  
ATOM   5471 HG21 VAL A 361      -0.010  39.311 -25.314  1.00 17.38           H  
ATOM   5472 HG22 VAL A 361       0.186  40.806 -24.814  1.00 17.38           H  
ATOM   5473 HG23 VAL A 361      -1.253  40.135 -24.766  1.00 17.38           H  
ATOM   5474  N   THR A 362      -0.341  43.510 -28.607  1.00 14.95           N  
ANISOU 5474  N   THR A 362     2124   1701   1857    173   -274    103       N  
ATOM   5475  CA  THR A 362      -0.482  43.945 -29.988  1.00 14.89           C  
ANISOU 5475  CA  THR A 362     2136   1690   1832    158   -294    128       C  
ATOM   5476  C   THR A 362       0.843  43.840 -30.731  1.00 15.06           C  
ANISOU 5476  C   THR A 362     2169   1717   1835    108   -282    147       C  
ATOM   5477  O   THR A 362       1.925  43.813 -30.137  1.00 15.68           O  
ANISOU 5477  O   THR A 362     2250   1792   1918     88   -266    144       O  
ATOM   5478  CB  THR A 362      -1.009  45.394 -30.119  1.00 15.07           C  
ANISOU 5478  CB  THR A 362     2194   1671   1860    181   -335    142       C  
ATOM   5479  OG1 THR A 362      -0.062  46.308 -29.547  1.00 17.98           O  
ANISOU 5479  OG1 THR A 362     2596   2000   2235    167   -343    148       O  
ATOM   5480  CG2 THR A 362      -2.392  45.550 -29.463  1.00 18.83           C  
ANISOU 5480  CG2 THR A 362     2655   2148   2353    237   -348    122       C  
ATOM   5481  H   THR A 362       0.350  43.811 -28.194  1.00 17.94           H  
ATOM   5482  HA  THR A 362      -1.121  43.347 -30.406  1.00 17.87           H  
ATOM   5483  HB  THR A 362      -1.120  45.612 -31.057  1.00 18.08           H  
ATOM   5484  HG1 THR A 362      -0.178  46.359 -28.717  1.00 21.57           H  
ATOM   5485 HG21 THR A 362      -2.816  44.682 -29.372  1.00 22.60           H  
ATOM   5486 HG22 THR A 362      -2.299  45.949 -28.583  1.00 22.60           H  
ATOM   5487 HG23 THR A 362      -2.956  46.120 -30.009  1.00 22.60           H  
ATOM   5488  N   LEU A 363       0.732  43.743 -32.048  1.00 13.20           N  
ANISOU 5488  N   LEU A 363     1939   1497   1578     87   -289    165       N  
ATOM   5489  CA  LEU A 363       1.880  43.779 -32.941  1.00 14.48           C  
ANISOU 5489  CA  LEU A 363     2114   1670   1717     40   -280    186       C  
ATOM   5490  C   LEU A 363       1.795  45.062 -33.753  1.00 16.06           C  
ANISOU 5490  C   LEU A 363     2354   1842   1904     27   -317    219       C  
ATOM   5491  O   LEU A 363       0.794  45.318 -34.427  1.00 16.85           O  
ANISOU 5491  O   LEU A 363     2462   1942   1999     44   -341    230       O  
ATOM   5492  CB  LEU A 363       1.920  42.558 -33.855  1.00 16.88           C  
ANISOU 5492  CB  LEU A 363     2394   2020   2002     21   -255    179       C  
ATOM   5493  CG  LEU A 363       3.043  42.538 -34.895  1.00 15.76           C  
ANISOU 5493  CG  LEU A 363     2260   1898   1830    -26   -243    197       C  
ATOM   5494  CD1 LEU A 363       4.420  42.443 -34.257  1.00 14.71           C  
ANISOU 5494  CD1 LEU A 363     2120   1768   1700    -48   -220    194       C  
ATOM   5495  CD2 LEU A 363       2.825  41.373 -35.881  1.00 15.97           C  
ANISOU 5495  CD2 LEU A 363     2266   1968   1835    -37   -222    185       C  
ATOM   5496  H   LEU A 363      -0.020  43.654 -32.457  1.00 15.84           H  
ATOM   5497  HA  LEU A 363       2.700  43.781 -32.424  1.00 17.37           H  
ATOM   5498  HB2 LEU A 363       2.026  41.768 -33.302  1.00 20.26           H  
ATOM   5499  HB3 LEU A 363       1.080  42.513 -34.338  1.00 20.26           H  
ATOM   5500  HG  LEU A 363       3.020  43.378 -35.381  1.00 18.91           H  
ATOM   5501 HD11 LEU A 363       5.077  42.269 -34.949  1.00 17.65           H  
ATOM   5502 HD12 LEU A 363       4.621  43.281 -33.813  1.00 17.65           H  
ATOM   5503 HD13 LEU A 363       4.420  41.719 -33.612  1.00 17.65           H  
ATOM   5504 HD21 LEU A 363       3.286  41.572 -36.712  1.00 19.17           H  
ATOM   5505 HD22 LEU A 363       3.181  40.559 -35.492  1.00 19.17           H  
ATOM   5506 HD23 LEU A 363       1.875  41.273 -36.046  1.00 19.17           H  
ATOM   5507  N   ASP A 364       2.838  45.856 -33.684  1.00 15.27           N  
ANISOU 5507  N   ASP A 364     2282   1721   1800     -4   -324    238       N  
ATOM   5508  CA  ASP A 364       2.934  47.097 -34.434  1.00 15.04           C  
ANISOU 5508  CA  ASP A 364     2297   1662   1758    -25   -360    274       C  
ATOM   5509  C   ASP A 364       3.910  46.862 -35.577  1.00 16.94           C  
ANISOU 5509  C   ASP A 364     2536   1936   1963    -81   -346    298       C  
ATOM   5510  O   ASP A 364       5.110  46.692 -35.343  1.00 15.95           O  
ANISOU 5510  O   ASP A 364     2402   1826   1831   -116   -323    298       O  
ATOM   5511  CB  ASP A 364       3.389  48.225 -33.514  1.00 15.63           C  
ANISOU 5511  CB  ASP A 364     2404   1683   1850    -25   -379    279       C  
ATOM   5512  CG  ASP A 364       3.396  49.576 -34.197  1.00 26.32           C  
ANISOU 5512  CG  ASP A 364     3812   2994   3195    -44   -422    318       C  
ATOM   5513  OD1 ASP A 364       3.233  49.639 -35.431  1.00 20.61           O  
ANISOU 5513  OD1 ASP A 364     3097   2286   2446    -64   -433    346       O  
ATOM   5514  OD2 ASP A 364       3.562  50.589 -33.492  1.00 29.43           O  
ANISOU 5514  OD2 ASP A 364     4242   3335   3606    -39   -445    321       O  
ATOM   5515  H   ASP A 364       3.527  45.695 -33.194  1.00 18.33           H  
ATOM   5516  HA  ASP A 364       2.075  47.344 -34.813  1.00 18.05           H  
ATOM   5517  HB2 ASP A 364       2.787  48.277 -32.755  1.00 18.75           H  
ATOM   5518  HB3 ASP A 364       4.291  48.039 -33.209  1.00 18.75           H  
ATOM   5519  N   THR A 365       3.395  46.818 -36.806  1.00 15.67           N  
ANISOU 5519  N   THR A 365     2381   1795   1778    -91   -358    317       N  
ATOM   5520  CA  THR A 365       4.234  46.629 -37.981  1.00 17.44           C  
ANISOU 5520  CA  THR A 365     2605   2058   1964   -144   -345    339       C  
ATOM   5521  C   THR A 365       4.367  47.903 -38.806  1.00 23.15           C  
ANISOU 5521  C   THR A 365     3374   2755   2666   -176   -384    386       C  
ATOM   5522  O   THR A 365       4.737  47.834 -39.982  1.00 20.31           O  
ANISOU 5522  O   THR A 365     3018   2431   2269   -218   -381    410       O  
ATOM   5523  CB  THR A 365       3.677  45.512 -38.869  1.00 18.17           C  
ANISOU 5523  CB  THR A 365     2668   2200   2035   -140   -327    324       C  
ATOM   5524  OG1 THR A 365       2.338  45.846 -39.260  1.00 18.38           O  
ANISOU 5524  OG1 THR A 365     2706   2214   2065   -109   -361    334       O  
ATOM   5525  CG2 THR A 365       3.718  44.173 -38.133  1.00 19.43           C  
ANISOU 5525  CG2 THR A 365     2785   2384   2212   -118   -287    280       C  
ATOM   5526  H   THR A 365       2.557  46.897 -36.980  1.00 18.81           H  
ATOM   5527  HA  THR A 365       5.116  46.366 -37.675  1.00 20.93           H  
ATOM   5528  HB  THR A 365       4.216  45.414 -39.670  1.00 21.80           H  
ATOM   5529  HG1 THR A 365       1.876  45.148 -39.328  1.00 22.06           H  
ATOM   5530 HG21 THR A 365       4.588  43.759 -38.246  1.00 23.31           H  
ATOM   5531 HG22 THR A 365       3.556  44.310 -37.187  1.00 23.31           H  
ATOM   5532 HG23 THR A 365       3.038  43.579 -38.487  1.00 23.31           H  
ATOM   5533  N   THR A 366       4.074  49.065 -38.219  1.00 17.80           N  
ANISOU 5533  N   THR A 366     2736   2017   2012   -159   -420    401       N  
ATOM   5534  CA  THR A 366       4.051  50.308 -38.978  1.00 19.68           C  
ANISOU 5534  CA  THR A 366     3024   2219   2233   -184   -463    449       C  
ATOM   5535  C   THR A 366       5.375  51.063 -38.944  1.00 25.58           C  
ANISOU 5535  C   THR A 366     3800   2952   2968   -244   -465    476       C  
ATOM   5536  O   THR A 366       5.494  52.099 -39.609  1.00 26.62           O  
ANISOU 5536  O   THR A 366     3977   3054   3083   -276   -500    520       O  
ATOM   5537  CB  THR A 366       2.945  51.253 -38.474  1.00 24.00           C  
ANISOU 5537  CB  THR A 366     3606   2702   2812   -130   -507    453       C  
ATOM   5538  OG1 THR A 366       3.286  51.753 -37.173  1.00 27.56           O  
ANISOU 5538  OG1 THR A 366     4071   3107   3295   -115   -508    433       O  
ATOM   5539  CG2 THR A 366       1.594  50.550 -38.443  1.00 28.68           C  
ANISOU 5539  CG2 THR A 366     4165   3315   3417    -71   -506    426       C  
ATOM   5540  H   THR A 366       3.886  49.153 -37.384  1.00 21.36           H  
ATOM   5541  HA  THR A 366       3.849  50.072 -39.897  1.00 23.61           H  
ATOM   5542  HB  THR A 366       2.862  52.004 -39.082  1.00 28.80           H  
ATOM   5543  HG1 THR A 366       2.589  51.883 -36.723  1.00 33.08           H  
ATOM   5544 HG21 THR A 366       1.057  50.830 -39.201  1.00 34.42           H  
ATOM   5545 HG22 THR A 366       1.720  49.589 -38.483  1.00 34.42           H  
ATOM   5546 HG23 THR A 366       1.123  50.772 -37.624  1.00 34.42           H  
ATOM   5547  N   GLY A 367       6.371  50.576 -38.203  1.00 25.07           N  
ANISOU 5547  N   GLY A 367     3709   2908   2909   -263   -430    453       N  
ATOM   5548  CA  GLY A 367       7.610  51.297 -38.019  1.00 33.63           C  
ANISOU 5548  CA  GLY A 367     4815   3980   3983   -320   -433    475       C  
ATOM   5549  C   GLY A 367       8.830  50.441 -38.315  1.00 22.86           C  
ANISOU 5549  C   GLY A 367     3408   2687   2592   -366   -387    469       C  
ATOM   5550  O   GLY A 367       8.805  49.537 -39.157  1.00 24.94           O  
ANISOU 5550  O   GLY A 367     3638   3007   2830   -370   -362    463       O  
ATOM   5551  H   GLY A 367       6.341  49.819 -37.797  1.00 30.09           H  
ATOM   5552  HA2 GLY A 367       7.626  52.065 -38.612  1.00 40.35           H  
ATOM   5553  HA3 GLY A 367       7.669  51.604 -37.101  1.00 40.35           H  
ATOM   5554  N   THR A 368       9.908  50.749 -37.589  1.00 30.33           N  
ANISOU 5554  N   THR A 368     4352   3629   3541   -399   -378    469       N  
ATOM   5555  CA  THR A 368      11.195  50.070 -37.685  1.00 31.21           C  
ANISOU 5555  CA  THR A 368     4422   3807   3630   -440   -338    464       C  
ATOM   5556  C   THR A 368      11.631  49.704 -36.271  1.00 28.72           C  
ANISOU 5556  C   THR A 368     4081   3485   3346   -418   -319    430       C  
ATOM   5557  O   THR A 368      11.576  50.558 -35.372  1.00 34.94           O  
ANISOU 5557  O   THR A 368     4901   4217   4157   -414   -345    431       O  
ATOM   5558  CB  THR A 368      12.246  50.973 -38.353  1.00 44.57           C  
ANISOU 5558  CB  THR A 368     6138   5510   5288   -520   -350    510       C  
ATOM   5559  OG1 THR A 368      11.832  51.297 -39.685  1.00 53.37           O  
ANISOU 5559  OG1 THR A 368     7276   6633   6370   -543   -369    545       O  
ATOM   5560  CG2 THR A 368      13.597  50.280 -38.401  1.00 44.06           C  
ANISOU 5560  CG2 THR A 368     6022   5520   5198   -560   -307    503       C  
ATOM   5561  H   THR A 368       9.914  51.381 -37.005  1.00 36.39           H  
ATOM   5562  HA  THR A 368      11.109  49.264 -38.218  1.00 37.45           H  
ATOM   5563  HB  THR A 368      12.339  51.789 -37.837  1.00 53.49           H  
ATOM   5564  HG1 THR A 368      12.395  51.806 -40.045  1.00 64.05           H  
ATOM   5565 HG21 THR A 368      14.229  50.821 -38.899  1.00 52.87           H  
ATOM   5566 HG22 THR A 368      13.935  50.150 -37.501  1.00 52.87           H  
ATOM   5567 HG23 THR A 368      13.511  49.416 -38.833  1.00 52.87           H  
ATOM   5568  N   PRO A 369      12.011  48.446 -36.007  1.00 22.35           N  
ANISOU 5568  N   PRO A 369     3219   2732   2540   -399   -276    398       N  
ATOM   5569  CA  PRO A 369      11.919  47.309 -36.922  1.00 22.91           C  
ANISOU 5569  CA  PRO A 369     3253   2862   2590   -390   -244    385       C  
ATOM   5570  C   PRO A 369      10.472  46.954 -37.238  1.00 21.24           C  
ANISOU 5570  C   PRO A 369     3050   2629   2390   -340   -255    371       C  
ATOM   5571  O   PRO A 369       9.535  47.539 -36.693  1.00 17.88           O  
ANISOU 5571  O   PRO A 369     2654   2148   1992   -307   -286    370       O  
ATOM   5572  CB  PRO A 369      12.607  46.189 -36.149  1.00 21.54           C  
ANISOU 5572  CB  PRO A 369     3028   2728   2429   -371   -202    350       C  
ATOM   5573  CG  PRO A 369      12.319  46.497 -34.764  1.00 26.71           C  
ANISOU 5573  CG  PRO A 369     3693   3335   3122   -341   -216    334       C  
ATOM   5574  CD  PRO A 369      12.415  48.006 -34.658  1.00 24.46           C  
ANISOU 5574  CD  PRO A 369     3459   2999   2835   -376   -257    367       C  
ATOM   5575  HA  PRO A 369      12.403  47.471 -37.747  1.00 27.49           H  
ATOM   5576  HB2 PRO A 369      12.235  45.330 -36.402  1.00 25.85           H  
ATOM   5577  HB3 PRO A 369      13.562  46.201 -36.321  1.00 25.85           H  
ATOM   5578  HG2 PRO A 369      11.427  46.192 -34.537  1.00 32.06           H  
ATOM   5579  HG3 PRO A 369      12.973  46.069 -34.189  1.00 32.06           H  
ATOM   5580  HD2 PRO A 369      11.808  48.348 -33.984  1.00 29.35           H  
ATOM   5581  HD3 PRO A 369      13.323  48.285 -34.459  1.00 29.35           H  
ATOM   5582  N   LEU A 370      10.303  45.996 -38.145  1.00 18.12           N  
ANISOU 5582  N   LEU A 370     2629   2282   1973   -336   -231    360       N  
ATOM   5583  CA  LEU A 370       8.968  45.638 -38.607  1.00 17.11           C  
ANISOU 5583  CA  LEU A 370     2507   2144   1850   -299   -243    350       C  
ATOM   5584  C   LEU A 370       8.143  44.978 -37.510  1.00 15.18           C  
ANISOU 5584  C   LEU A 370     2246   1876   1646   -239   -237    312       C  
ATOM   5585  O   LEU A 370       6.941  45.234 -37.406  1.00 18.43           O  
ANISOU 5585  O   LEU A 370     2674   2255   2074   -204   -262    310       O  
ATOM   5586  CB  LEU A 370       9.083  44.715 -39.816  1.00 19.45           C  
ANISOU 5586  CB  LEU A 370     2780   2501   2110   -314   -216    343       C  
ATOM   5587  CG  LEU A 370       7.797  44.269 -40.509  1.00 23.67           C  
ANISOU 5587  CG  LEU A 370     3317   3037   2638   -286   -227    334       C  
ATOM   5588  CD1 LEU A 370       6.941  45.459 -40.931  1.00 20.40           C  
ANISOU 5588  CD1 LEU A 370     2947   2583   2222   -288   -277    371       C  
ATOM   5589  CD2 LEU A 370       8.153  43.386 -41.701  1.00 21.14           C  
ANISOU 5589  CD2 LEU A 370     2975   2781   2277   -311   -198    325       C  
ATOM   5590  H   LEU A 370      10.937  45.540 -38.506  1.00 21.74           H  
ATOM   5591  HA  LEU A 370       8.503  46.447 -38.872  1.00 20.53           H  
ATOM   5592  HB2 LEU A 370       9.615  45.172 -40.485  1.00 23.34           H  
ATOM   5593  HB3 LEU A 370       9.537  43.907 -39.526  1.00 23.34           H  
ATOM   5594  HG  LEU A 370       7.256  43.756 -39.888  1.00 28.40           H  
ATOM   5595 HD11 LEU A 370       6.184  45.136 -41.445  1.00 24.48           H  
ATOM   5596 HD12 LEU A 370       6.629  45.920 -40.137  1.00 24.48           H  
ATOM   5597 HD13 LEU A 370       7.478  46.058 -41.472  1.00 24.48           H  
ATOM   5598 HD21 LEU A 370       7.379  43.311 -42.281  1.00 25.37           H  
ATOM   5599 HD22 LEU A 370       8.891  43.790 -42.184  1.00 25.37           H  
ATOM   5600 HD23 LEU A 370       8.411  42.508 -41.378  1.00 25.37           H  
ATOM   5601  N   PHE A 371       8.752  44.107 -36.702  1.00 15.40           N  
ANISOU 5601  N   PHE A 371     2240   1924   1689   -226   -203    284       N  
ATOM   5602  CA  PHE A 371       8.026  43.375 -35.663  1.00 15.46           C  
ANISOU 5602  CA  PHE A 371     2228   1915   1731   -175   -194    250       C  
ATOM   5603  C   PHE A 371       8.313  44.011 -34.311  1.00 15.10           C  
ANISOU 5603  C   PHE A 371     2191   1833   1713   -165   -205    248       C  
ATOM   5604  O   PHE A 371       9.354  43.757 -33.699  1.00 17.18           O  
ANISOU 5604  O   PHE A 371     2435   2113   1980   -179   -184    241       O  
ATOM   5605  CB  PHE A 371       8.395  41.890 -35.663  1.00 16.39           C  
ANISOU 5605  CB  PHE A 371     2305   2075   1848   -163   -152    219       C  
ATOM   5606  CG  PHE A 371       7.869  41.151 -36.851  1.00 17.39           C  
ANISOU 5606  CG  PHE A 371     2426   2232   1951   -164   -142    211       C  
ATOM   5607  CD1 PHE A 371       8.630  41.054 -38.001  1.00 17.11           C  
ANISOU 5607  CD1 PHE A 371     2385   2238   1877   -202   -128    222       C  
ATOM   5608  CD2 PHE A 371       6.604  40.575 -36.838  1.00 20.53           C  
ANISOU 5608  CD2 PHE A 371     2820   2619   2361   -131   -148    192       C  
ATOM   5609  CE1 PHE A 371       8.144  40.392 -39.138  1.00 18.78           C  
ANISOU 5609  CE1 PHE A 371     2593   2480   2062   -206   -119    213       C  
ATOM   5610  CE2 PHE A 371       6.111  39.901 -37.968  1.00 24.43           C  
ANISOU 5610  CE2 PHE A 371     3310   3143   2831   -137   -141    184       C  
ATOM   5611  CZ  PHE A 371       6.888  39.812 -39.118  1.00 21.16           C  
ANISOU 5611  CZ  PHE A 371     2894   2768   2377   -174   -127    193       C  
ATOM   5612  H   PHE A 371       9.591  43.923 -36.739  1.00 18.48           H  
ATOM   5613  HA  PHE A 371       7.076  43.459 -35.843  1.00 18.55           H  
ATOM   5614  HB2 PHE A 371       9.361  41.807 -35.664  1.00 19.67           H  
ATOM   5615  HB3 PHE A 371       8.027  41.475 -34.867  1.00 19.67           H  
ATOM   5616  HD1 PHE A 371       9.478  41.435 -38.021  1.00 20.53           H  
ATOM   5617  HD2 PHE A 371       6.078  40.637 -36.074  1.00 24.63           H  
ATOM   5618  HE1 PHE A 371       8.666  40.343 -39.906  1.00 22.54           H  
ATOM   5619  HE2 PHE A 371       5.266  39.514 -37.947  1.00 29.32           H  
ATOM   5620  HZ  PHE A 371       6.566  39.366 -39.868  1.00 25.39           H  
ATOM   5621  N   VAL A 372       7.385  44.844 -33.851  1.00 14.55           N  
ANISOU 5621  N   VAL A 372     2150   1715   1662   -140   -238    252       N  
ATOM   5622  CA  VAL A 372       7.441  45.443 -32.523  1.00 14.15           C  
ANISOU 5622  CA  VAL A 372     2111   1626   1639   -124   -250    243       C  
ATOM   5623  C   VAL A 372       6.220  44.967 -31.751  1.00 13.00           C  
ANISOU 5623  C   VAL A 372     1954   1467   1520    -68   -251    214       C  
ATOM   5624  O   VAL A 372       5.084  45.262 -32.143  1.00 15.25           O  
ANISOU 5624  O   VAL A 372     2252   1734   1807    -43   -274    217       O  
ATOM   5625  CB  VAL A 372       7.483  46.977 -32.583  1.00 16.64           C  
ANISOU 5625  CB  VAL A 372     2477   1893   1953   -144   -290    271       C  
ATOM   5626  CG1 VAL A 372       7.393  47.558 -31.173  1.00 17.85           C  
ANISOU 5626  CG1 VAL A 372     2644   2004   2134   -121   -303    254       C  
ATOM   5627  CG2 VAL A 372       8.751  47.438 -33.277  1.00 18.82           C  
ANISOU 5627  CG2 VAL A 372     2763   2188   2201   -207   -289    301       C  
ATOM   5628  H   VAL A 372       6.695  45.082 -34.305  1.00 17.46           H  
ATOM   5629  HA  VAL A 372       8.239  45.135 -32.065  1.00 16.98           H  
ATOM   5630  HB  VAL A 372       6.725  47.303 -33.095  1.00 19.97           H  
ATOM   5631 HG11 VAL A 372       7.684  48.483 -31.192  1.00 21.42           H  
ATOM   5632 HG12 VAL A 372       6.474  47.507 -30.868  1.00 21.42           H  
ATOM   5633 HG13 VAL A 372       7.966  47.043 -30.583  1.00 21.42           H  
ATOM   5634 HG21 VAL A 372       8.695  48.393 -33.437  1.00 22.59           H  
ATOM   5635 HG22 VAL A 372       9.512  47.243 -32.707  1.00 22.59           H  
ATOM   5636 HG23 VAL A 372       8.840  46.966 -34.120  1.00 22.59           H  
ATOM   5637  N   TRP A 373       6.457  44.245 -30.657  1.00 13.91           N  
ANISOU 5637  N   TRP A 373     2041   1593   1652    -50   -228    189       N  
ATOM   5638  CA  TRP A 373       5.406  43.689 -29.815  1.00 13.10           C  
ANISOU 5638  CA  TRP A 373     1921   1485   1572     -3   -224    162       C  
ATOM   5639  C   TRP A 373       5.151  44.643 -28.661  1.00 13.79           C  
ANISOU 5639  C   TRP A 373     2029   1532   1678     18   -246    155       C  
ATOM   5640  O   TRP A 373       6.092  45.231 -28.123  1.00 14.39           O  
ANISOU 5640  O   TRP A 373     2119   1595   1755     -6   -249    161       O  
ATOM   5641  CB  TRP A 373       5.807  42.314 -29.286  1.00 13.62           C  
ANISOU 5641  CB  TRP A 373     1946   1584   1643      4   -188    142       C  
ATOM   5642  CG  TRP A 373       5.901  41.301 -30.371  1.00 14.10           C  
ANISOU 5642  CG  TRP A 373     1990   1681   1688     -8   -166    141       C  
ATOM   5643  CD1 TRP A 373       7.030  40.875 -31.005  1.00 13.44           C  
ANISOU 5643  CD1 TRP A 373     1894   1627   1586    -39   -145    148       C  
ATOM   5644  CD2 TRP A 373       4.811  40.593 -30.968  1.00 13.43           C  
ANISOU 5644  CD2 TRP A 373     1895   1607   1601     10   -164    130       C  
ATOM   5645  NE1 TRP A 373       6.709  39.934 -31.957  1.00 16.54           N  
ANISOU 5645  NE1 TRP A 373     2273   2045   1965    -39   -129    140       N  
ATOM   5646  CE2 TRP A 373       5.351  39.741 -31.948  1.00 15.58           C  
ANISOU 5646  CE2 TRP A 373     2155   1912   1854    -11   -142    129       C  
ATOM   5647  CE3 TRP A 373       3.429  40.589 -30.758  1.00 16.76           C  
ANISOU 5647  CE3 TRP A 373     2316   2017   2034     42   -180    121       C  
ATOM   5648  CZ2 TRP A 373       4.551  38.905 -32.731  1.00 16.74           C  
ANISOU 5648  CZ2 TRP A 373     2292   2076   1991     -5   -135    118       C  
ATOM   5649  CZ3 TRP A 373       2.641  39.753 -31.525  1.00 18.03           C  
ANISOU 5649  CZ3 TRP A 373     2465   2200   2186     47   -174    112       C  
ATOM   5650  CH2 TRP A 373       3.201  38.925 -32.501  1.00 15.28           C  
ANISOU 5650  CH2 TRP A 373     2109   1880   1819     22   -153    111       C  
ATOM   5651  H   TRP A 373       7.248  44.060 -30.375  1.00 16.70           H  
ATOM   5652  HA  TRP A 373       4.586  43.580 -30.321  1.00 15.72           H  
ATOM   5653  HB2 TRP A 373       6.675  42.379 -28.857  1.00 16.34           H  
ATOM   5654  HB3 TRP A 373       5.143  42.012 -28.647  1.00 16.34           H  
ATOM   5655  HD1 TRP A 373       7.891  41.176 -30.821  1.00 16.13           H  
ATOM   5656  HE1 TRP A 373       7.268  39.533 -32.473  1.00 19.85           H  
ATOM   5657  HE3 TRP A 373       3.047  41.140 -30.113  1.00 20.11           H  
ATOM   5658  HZ2 TRP A 373       4.921  38.355 -33.384  1.00 20.08           H  
ATOM   5659  HZ3 TRP A 373       1.721  39.741 -31.389  1.00 21.64           H  
ATOM   5660  HH2 TRP A 373       2.645  38.376 -33.005  1.00 18.34           H  
ATOM   5661  N   LYS A 374       3.880  44.818 -28.302  1.00 12.97           N  
ANISOU 5661  N   LYS A 374     1928   1411   1589     60   -261    142       N  
ATOM   5662  CA  LYS A 374       3.502  45.774 -27.276  1.00 15.54           C  
ANISOU 5662  CA  LYS A 374     2276   1698   1931     86   -283    130       C  
ATOM   5663  C   LYS A 374       2.464  45.160 -26.354  1.00 14.36           C  
ANISOU 5663  C   LYS A 374     2098   1561   1796    133   -272    101       C  
ATOM   5664  O   LYS A 374       1.675  44.305 -26.761  1.00 15.28           O  
ANISOU 5664  O   LYS A 374     2188   1705   1912    148   -262     95       O  
ATOM   5665  CB  LYS A 374       2.934  47.066 -27.880  1.00 15.43           C  
ANISOU 5665  CB  LYS A 374     2306   1641   1917     96   -322    148       C  
ATOM   5666  CG  LYS A 374       3.914  47.778 -28.788  1.00 17.49           C  
ANISOU 5666  CG  LYS A 374     2599   1887   2159     45   -336    181       C  
ATOM   5667  CD  LYS A 374       3.348  49.075 -29.306  1.00 19.96           C  
ANISOU 5667  CD  LYS A 374     2961   2150   2474     55   -378    201       C  
ATOM   5668  CE  LYS A 374       4.393  49.851 -30.066  1.00 18.02           C  
ANISOU 5668  CE  LYS A 374     2751   1887   2210     -2   -394    237       C  
ATOM   5669  NZ  LYS A 374       3.782  51.039 -30.691  1.00 25.70           N  
ANISOU 5669  NZ  LYS A 374     3773   2809   3183      7   -437    262       N  
ATOM   5670  H   LYS A 374       3.218  44.388 -28.644  1.00 15.56           H  
ATOM   5671  HA  LYS A 374       4.288  45.993 -26.752  1.00 18.65           H  
ATOM   5672  HB2 LYS A 374       2.146  46.849 -28.403  1.00 18.52           H  
ATOM   5673  HB3 LYS A 374       2.699  47.673 -27.161  1.00 18.52           H  
ATOM   5674  HG2 LYS A 374       4.725  47.975 -28.293  1.00 20.99           H  
ATOM   5675  HG3 LYS A 374       4.119  47.210 -29.547  1.00 20.99           H  
ATOM   5676  HD2 LYS A 374       2.608  48.889 -29.904  1.00 23.96           H  
ATOM   5677  HD3 LYS A 374       3.045  49.617 -28.560  1.00 23.96           H  
ATOM   5678  HE2 LYS A 374       5.090  50.144 -29.458  1.00 21.63           H  
ATOM   5679  HE3 LYS A 374       4.773  49.293 -30.762  1.00 21.63           H  
ATOM   5680  HZ1 LYS A 374       3.141  50.790 -31.257  1.00 30.84           H  
ATOM   5681  HZ2 LYS A 374       3.427  51.564 -30.066  1.00 30.84           H  
ATOM   5682  HZ3 LYS A 374       4.399  51.499 -31.139  1.00 30.84           H  
ATOM   5683  N   VAL A 375       2.462  45.605 -25.107  1.00 14.94           N  
ANISOU 5683  N   VAL A 375     2177   1617   1883    151   -276     82       N  
ATOM   5684  CA  VAL A 375       1.405  45.245 -24.173  1.00 15.71           C  
ANISOU 5684  CA  VAL A 375     2251   1727   1992    196   -270     55       C  
ATOM   5685  C   VAL A 375       0.849  46.550 -23.623  1.00 16.74           C  
ANISOU 5685  C   VAL A 375     2414   1814   2131    228   -300     43       C  
ATOM   5686  O   VAL A 375       1.610  47.417 -23.177  1.00 15.73           O  
ANISOU 5686  O   VAL A 375     2319   1654   2005    212   -312     44       O  
ATOM   5687  CB  VAL A 375       1.888  44.319 -23.046  1.00 11.80           C  
ANISOU 5687  CB  VAL A 375     1724   1260   1499    191   -241     38       C  
ATOM   5688  CG1 VAL A 375       0.691  43.875 -22.211  1.00 16.49           C  
ANISOU 5688  CG1 VAL A 375     2290   1873   2100    233   -234     14       C  
ATOM   5689  CG2 VAL A 375       2.593  43.087 -23.588  1.00 12.79           C  
ANISOU 5689  CG2 VAL A 375     1824   1420   1618    161   -213     50       C  
ATOM   5690  H   VAL A 375       3.068  46.119 -24.777  1.00 17.93           H  
ATOM   5691  HA  VAL A 375       0.701  44.765 -24.637  1.00 18.85           H  
ATOM   5692  HB  VAL A 375       2.522  44.811 -22.501  1.00 14.16           H  
ATOM   5693 HG11 VAL A 375       0.993  43.249 -21.534  1.00 19.78           H  
ATOM   5694 HG12 VAL A 375       0.294  44.653 -21.790  1.00 19.78           H  
ATOM   5695 HG13 VAL A 375       0.043  43.446 -22.792  1.00 19.78           H  
ATOM   5696 HG21 VAL A 375       3.260  42.797 -22.946  1.00 15.35           H  
ATOM   5697 HG22 VAL A 375       1.939  42.384 -23.727  1.00 15.35           H  
ATOM   5698 HG23 VAL A 375       3.020  43.313 -24.429  1.00 15.35           H  
ATOM   5699  N   ASN A 376      -0.467  46.713 -23.718  1.00 17.74           N  
ANISOU 5699  N   ASN A 376     2534   1942   2264    273   -312     33       N  
ATOM   5700  CA  ASN A 376      -1.116  47.974 -23.383  1.00 15.81           C  
ANISOU 5700  CA  ASN A 376     2322   1656   2030    313   -343     22       C  
ATOM   5701  C   ASN A 376      -0.398  49.152 -24.040  1.00 18.51           C  
ANISOU 5701  C   ASN A 376     2719   1943   2370    287   -373     46       C  
ATOM   5702  O   ASN A 376      -0.187  50.205 -23.432  1.00 18.85           O  
ANISOU 5702  O   ASN A 376     2800   1940   2420    296   -393     36       O  
ATOM   5703  CB  ASN A 376      -1.202  48.144 -21.867  1.00 18.41           C  
ANISOU 5703  CB  ASN A 376     2645   1983   2366    338   -334    -13       C  
ATOM   5704  CG  ASN A 376      -2.101  49.278 -21.465  1.00 20.80           C  
ANISOU 5704  CG  ASN A 376     2973   2250   2679    391   -362    -33       C  
ATOM   5705  OD1 ASN A 376      -3.077  49.590 -22.151  1.00 26.64           O  
ANISOU 5705  OD1 ASN A 376     3714   2986   3424    426   -381    -28       O  
ATOM   5706  ND2 ASN A 376      -1.779  49.903 -20.341  1.00 19.32           N  
ANISOU 5706  ND2 ASN A 376     2806   2039   2495    401   -365    -59       N  
ATOM   5707  H   ASN A 376      -1.011  46.100 -23.978  1.00 21.29           H  
ATOM   5708  HA  ASN A 376      -2.021  47.966 -23.733  1.00 18.98           H  
ATOM   5709  HB2 ASN A 376      -1.553  47.328 -21.476  1.00 22.09           H  
ATOM   5710  HB3 ASN A 376      -0.315  48.324 -21.518  1.00 22.09           H  
ATOM   5711 HD21 ASN A 376      -1.109  49.619 -19.882  1.00 23.18           H  
ATOM   5712  N   GLY A 377      -0.010  48.957 -25.300  1.00 18.54           N  
ANISOU 5712  N   GLY A 377     2729   1953   2362    252   -376     78       N  
ATOM   5713  CA  GLY A 377       0.509  50.020 -26.132  1.00 19.15           C  
ANISOU 5713  CA  GLY A 377     2857   1986   2434    225   -406    109       C  
ATOM   5714  C   GLY A 377       1.973  50.350 -25.969  1.00 15.79           C  
ANISOU 5714  C   GLY A 377     2455   1544   2001    168   -402    122       C  
ATOM   5715  O   GLY A 377       2.413  51.370 -26.510  1.00 19.25           O  
ANISOU 5715  O   GLY A 377     2940   1938   2434    142   -430    147       O  
ATOM   5716  H   GLY A 377      -0.041  48.196 -25.699  1.00 22.25           H  
ATOM   5717  HA2 GLY A 377       0.370  49.774 -27.060  1.00 22.98           H  
ATOM   5718  HA3 GLY A 377       0.007  50.828 -25.941  1.00 22.98           H  
ATOM   5719  N   SER A 378       2.746  49.529 -25.257  1.00 15.23           N  
ANISOU 5719  N   SER A 378     2352   1507   1926    146   -370    108       N  
ATOM   5720  CA  SER A 378       4.145  49.833 -24.990  1.00 16.22           C  
ANISOU 5720  CA  SER A 378     2493   1625   2043     93   -366    119       C  
ATOM   5721  C   SER A 378       4.998  48.585 -25.133  1.00 14.19           C  
ANISOU 5721  C   SER A 378     2191   1425   1775     60   -329    124       C  
ATOM   5722  O   SER A 378       4.682  47.541 -24.557  1.00 14.73           O  
ANISOU 5722  O   SER A 378     2218   1530   1849     83   -303    104       O  
ATOM   5723  CB  SER A 378       4.324  50.410 -23.578  1.00 16.11           C  
ANISOU 5723  CB  SER A 378     2495   1585   2040    105   -372     91       C  
ATOM   5724  OG  SER A 378       5.695  50.595 -23.268  1.00 18.17           O  
ANISOU 5724  OG  SER A 378     2765   1847   2291     51   -367    101       O  
ATOM   5725  H   SER A 378       2.477  48.786 -24.918  1.00 18.27           H  
ATOM   5726  HA  SER A 378       4.449  50.479 -25.646  1.00 19.46           H  
ATOM   5727  HB2 SER A 378       3.873  51.268 -23.529  1.00 19.33           H  
ATOM   5728  HB3 SER A 378       3.937  49.795 -22.935  1.00 19.33           H  
ATOM   5729  HG  SER A 378       5.776  51.149 -22.642  1.00 21.80           H  
ATOM   5730  N   ALA A 379       6.084  48.700 -25.884  1.00 15.41           N  
ANISOU 5730  N   ALA A 379     2354   1588   1913      6   -328    152       N  
ATOM   5731  CA  ALA A 379       7.062  47.626 -25.952  1.00 13.51           C  
ANISOU 5731  CA  ALA A 379     2072   1400   1661    -24   -293    155       C  
ATOM   5732  C   ALA A 379       7.942  47.658 -24.713  1.00 13.29           C  
ANISOU 5732  C   ALA A 379     2036   1377   1637    -38   -284    142       C  
ATOM   5733  O   ALA A 379       8.526  48.697 -24.391  1.00 18.07           O  
ANISOU 5733  O   ALA A 379     2676   1951   2240    -66   -305    149       O  
ATOM   5734  CB  ALA A 379       7.920  47.778 -27.203  1.00 16.51           C  
ANISOU 5734  CB  ALA A 379     2460   1794   2018    -75   -293    189       C  
ATOM   5735  H   ALA A 379       6.278  49.388 -26.362  1.00 18.49           H  
ATOM   5736  HA  ALA A 379       6.607  46.770 -25.992  1.00 16.21           H  
ATOM   5737  HB1 ALA A 379       8.568  47.056 -27.231  1.00 19.81           H  
ATOM   5738  HB2 ALA A 379       7.348  47.740 -27.985  1.00 19.81           H  
ATOM   5739  HB3 ALA A 379       8.379  48.632 -27.169  1.00 19.81           H  
ATOM   5740  N   ILE A 380       8.072  46.520 -24.029  1.00 15.80           N  
ANISOU 5740  N   ILE A 380     2309   1734   1960    -23   -254    124       N  
ATOM   5741  CA  ILE A 380       8.918  46.505 -22.842  1.00 13.86           C  
ANISOU 5741  CA  ILE A 380     2052   1499   1715    -37   -247    114       C  
ATOM   5742  C   ILE A 380      10.367  46.748 -23.256  1.00 16.96           C  
ANISOU 5742  C   ILE A 380     2444   1909   2090    -94   -244    138       C  
ATOM   5743  O   ILE A 380      10.825  46.303 -24.319  1.00 15.71           O  
ANISOU 5743  O   ILE A 380     2271   1780   1920   -116   -231    158       O  
ATOM   5744  CB  ILE A 380       8.758  45.205 -22.033  1.00 13.98           C  
ANISOU 5744  CB  ILE A 380     2021   1553   1738     -8   -217     95       C  
ATOM   5745  CG1 ILE A 380       9.310  45.427 -20.610  1.00 15.08           C  
ANISOU 5745  CG1 ILE A 380     2157   1694   1879    -13   -218     81       C  
ATOM   5746  CG2 ILE A 380       9.444  44.021 -22.694  1.00 14.87           C  
ANISOU 5746  CG2 ILE A 380     2096   1711   1843    -23   -188    107       C  
ATOM   5747  CD1 ILE A 380       9.022  44.277 -19.648  1.00 16.41           C  
ANISOU 5747  CD1 ILE A 380     2286   1894   2054     17   -194     64       C  
ATOM   5748  H   ILE A 380       7.695  45.773 -24.226  1.00 18.96           H  
ATOM   5749  HA  ILE A 380       8.638  47.225 -22.256  1.00 16.63           H  
ATOM   5750  HB  ILE A 380       7.812  44.991 -21.994  1.00 16.78           H  
ATOM   5751 HG12 ILE A 380      10.273  45.534 -20.663  1.00 18.10           H  
ATOM   5752 HG13 ILE A 380       8.907  46.229 -20.242  1.00 18.10           H  
ATOM   5753 HG21 ILE A 380       9.075  43.200 -22.333  1.00 17.84           H  
ATOM   5754 HG22 ILE A 380       9.290  44.060 -23.651  1.00 17.84           H  
ATOM   5755 HG23 ILE A 380      10.396  44.065 -22.510  1.00 17.84           H  
ATOM   5756 HD11 ILE A 380       9.505  44.428 -18.821  1.00 19.69           H  
ATOM   5757 HD12 ILE A 380       8.068  44.244 -19.472  1.00 19.69           H  
ATOM   5758 HD13 ILE A 380       9.312  43.446 -20.054  1.00 19.69           H  
ATOM   5759  N   ASN A 381      11.085  47.488 -22.419  1.00 17.60           N  
ANISOU 5759  N   ASN A 381     2541   1977   2169   -120   -257    136       N  
ATOM   5760  CA  ASN A 381      12.462  47.873 -22.702  1.00 13.33           C  
ANISOU 5760  CA  ASN A 381     2000   1454   1610   -181   -259    160       C  
ATOM   5761  C   ASN A 381      13.041  48.331 -21.376  1.00 17.97           C  
ANISOU 5761  C   ASN A 381     2593   2036   2198   -195   -268    146       C  
ATOM   5762  O   ASN A 381      12.638  49.381 -20.866  1.00 19.19           O  
ANISOU 5762  O   ASN A 381     2792   2139   2358   -193   -296    135       O  
ATOM   5763  CB  ASN A 381      12.518  48.983 -23.730  1.00 16.43           C  
ANISOU 5763  CB  ASN A 381     2439   1811   1992   -216   -286    186       C  
ATOM   5764  CG  ASN A 381      13.922  49.322 -24.131  1.00 24.89           C  
ANISOU 5764  CG  ASN A 381     3506   2909   3042   -284   -286    213       C  
ATOM   5765  OD1 ASN A 381      14.817  48.479 -24.079  1.00 26.40           O  
ANISOU 5765  OD1 ASN A 381     3649   3159   3223   -299   -258    216       O  
ATOM   5766  ND2 ASN A 381      14.125  50.555 -24.566  1.00 42.97           N  
ANISOU 5766  ND2 ASN A 381     5846   5158   5323   -326   -317    234       N  
ATOM   5767  H   ASN A 381      10.793  47.785 -21.667  1.00 21.12           H  
ATOM   5768  HA  ASN A 381      12.965  47.120 -23.049  1.00 15.99           H  
ATOM   5769  HB2 ASN A 381      12.037  48.704 -24.525  1.00 19.71           H  
ATOM   5770  HB3 ASN A 381      12.111  49.781 -23.358  1.00 19.71           H  
ATOM   5771 HD21 ASN A 381      14.912  50.801 -24.808  1.00 51.56           H  
ATOM   5772 HD22 ASN A 381      13.469  51.110 -24.606  1.00 51.56           H  
ATOM   5773  N   ILE A 382      13.942  47.549 -20.798  1.00 16.61           N  
ANISOU 5773  N   ILE A 382     2376   1915   2021   -207   -246    146       N  
ATOM   5774  CA  ILE A 382      14.511  47.902 -19.515  1.00 13.84           C  
ANISOU 5774  CA  ILE A 382     2025   1566   1668   -222   -254    133       C  
ATOM   5775  C   ILE A 382      15.984  48.265 -19.681  1.00 15.55           C  
ANISOU 5775  C   ILE A 382     2231   1813   1863   -288   -257    157       C  
ATOM   5776  O   ILE A 382      16.596  48.059 -20.732  1.00 15.77           O  
ANISOU 5776  O   ILE A 382     2242   1870   1879   -316   -247    182       O  
ATOM   5777  CB  ILE A 382      14.298  46.798 -18.451  1.00 16.88           C  
ANISOU 5777  CB  ILE A 382     2367   1984   2061   -182   -232    113       C  
ATOM   5778  CG1 ILE A 382      14.695  45.400 -18.927  1.00 18.11           C  
ANISOU 5778  CG1 ILE A 382     2469   2194   2216   -169   -199    124       C  
ATOM   5779  CG2 ILE A 382      12.814  46.773 -18.027  1.00 21.61           C  
ANISOU 5779  CG2 ILE A 382     2985   2550   2676   -126   -236     86       C  
ATOM   5780  CD1 ILE A 382      16.177  45.194 -19.127  1.00 17.38           C  
ANISOU 5780  CD1 ILE A 382     2344   2151   2108   -213   -189    146       C  
ATOM   5781  H   ILE A 382      14.235  46.813 -21.132  1.00 19.93           H  
ATOM   5782  HA  ILE A 382      14.061  48.700 -19.196  1.00 16.61           H  
ATOM   5783  HB  ILE A 382      14.881  47.024 -17.709  1.00 20.25           H  
ATOM   5784 HG12 ILE A 382      14.398  44.755 -18.266  1.00 21.73           H  
ATOM   5785 HG13 ILE A 382      14.259  45.229 -19.776  1.00 21.73           H  
ATOM   5786 HG21 ILE A 382      12.654  45.986 -17.483  1.00 25.93           H  
ATOM   5787 HG22 ILE A 382      12.618  47.574 -17.516  1.00 25.93           H  
ATOM   5788 HG23 ILE A 382      12.259  46.744 -18.822  1.00 25.93           H  
ATOM   5789 HD11 ILE A 382      16.385  44.255 -19.002  1.00 20.85           H  
ATOM   5790 HD12 ILE A 382      16.415  45.468 -20.027  1.00 20.85           H  
ATOM   5791 HD13 ILE A 382      16.660  45.730 -18.479  1.00 20.85           H  
ATOM   5792  N   ASP A 383      16.524  48.889 -18.636  1.00 17.55           N  
ANISOU 5792  N   ASP A 383     2496   2060   2111   -314   -274    148       N  
ATOM   5793  CA  ASP A 383      17.928  49.267 -18.543  1.00 20.10           C  
ANISOU 5793  CA  ASP A 383     2806   2417   2414   -380   -279    168       C  
ATOM   5794  C   ASP A 383      18.581  48.278 -17.588  1.00 16.18           C  
ANISOU 5794  C   ASP A 383     2252   1982   1915   -368   -258    162       C  
ATOM   5795  O   ASP A 383      18.251  48.243 -16.398  1.00 18.17           O  
ANISOU 5795  O   ASP A 383     2507   2226   2173   -345   -263    138       O  
ATOM   5796  CB  ASP A 383      18.053  50.703 -18.046  1.00 19.38           C  
ANISOU 5796  CB  ASP A 383     2773   2272   2316   -422   -316    162       C  
ATOM   5797  CG  ASP A 383      19.487  51.181 -17.934  1.00 24.16           C  
ANISOU 5797  CG  ASP A 383     3369   2913   2899   -498   -326    184       C  
ATOM   5798  OD1 ASP A 383      20.432  50.372 -18.008  1.00 21.71           O  
ANISOU 5798  OD1 ASP A 383     2998   2674   2577   -513   -303    199       O  
ATOM   5799  OD2 ASP A 383      19.665  52.404 -17.766  1.00 32.46           O  
ANISOU 5799  OD2 ASP A 383     4473   3917   3943   -543   -358    184       O  
ATOM   5800  H   ASP A 383      16.073  49.113 -17.939  1.00 21.06           H  
ATOM   5801  HA  ASP A 383      18.369  49.213 -19.405  1.00 24.12           H  
ATOM   5802  HB2 ASP A 383      17.592  51.290 -18.666  1.00 23.25           H  
ATOM   5803  HB3 ASP A 383      17.649  50.767 -17.167  1.00 23.25           H  
ATOM   5804  N   TRP A 384      19.496  47.469 -18.119  1.00 16.44           N  
ANISOU 5804  N   TRP A 384     2232   2076   1938   -382   -234    183       N  
ATOM   5805  CA  TRP A 384      20.167  46.456 -17.320  1.00 14.88           C  
ANISOU 5805  CA  TRP A 384     1977   1939   1739   -367   -214    181       C  
ATOM   5806  C   TRP A 384      20.839  47.034 -16.081  1.00 16.99           C  
ANISOU 5806  C   TRP A 384     2246   2217   1994   -401   -234    176       C  
ATOM   5807  O   TRP A 384      21.034  46.315 -15.094  1.00 19.75           O  
ANISOU 5807  O   TRP A 384     2560   2600   2345   -377   -225    168       O  
ATOM   5808  CB  TRP A 384      21.224  45.751 -18.168  1.00 20.61           C  
ANISOU 5808  CB  TRP A 384     2649   2729   2452   -384   -191    206       C  
ATOM   5809  CG  TRP A 384      20.721  44.747 -19.145  1.00 17.05           C  
ANISOU 5809  CG  TRP A 384     2181   2287   2012   -340   -164    206       C  
ATOM   5810  CD1 TRP A 384      19.675  43.888 -18.974  1.00 14.29           C  
ANISOU 5810  CD1 TRP A 384     1830   1917   1683   -279   -150    188       C  
ATOM   5811  CD2 TRP A 384      21.258  44.477 -20.448  1.00 15.84           C  
ANISOU 5811  CD2 TRP A 384     2006   2167   1846   -358   -146    225       C  
ATOM   5812  NE1 TRP A 384      19.524  43.102 -20.091  1.00 16.29           N  
ANISOU 5812  NE1 TRP A 384     2065   2185   1938   -258   -127    193       N  
ATOM   5813  CE2 TRP A 384      20.484  43.441 -21.008  1.00 17.55           C  
ANISOU 5813  CE2 TRP A 384     2212   2379   2077   -303   -123    214       C  
ATOM   5814  CE3 TRP A 384      22.319  45.007 -21.193  1.00 18.35           C  
ANISOU 5814  CE3 TRP A 384     2311   2522   2139   -417   -147    249       C  
ATOM   5815  CZ2 TRP A 384      20.735  42.927 -22.277  1.00 17.29           C  
ANISOU 5815  CZ2 TRP A 384     2159   2375   2035   -303   -101    223       C  
ATOM   5816  CZ3 TRP A 384      22.565  44.494 -22.450  1.00 17.65           C  
ANISOU 5816  CZ3 TRP A 384     2199   2466   2039   -416   -124    260       C  
ATOM   5817  CH2 TRP A 384      21.772  43.469 -22.983  1.00 18.97           C  
ANISOU 5817  CH2 TRP A 384     2360   2627   2222   -358   -101    246       C  
ATOM   5818  H   TRP A 384      19.747  47.486 -18.942  1.00 19.73           H  
ATOM   5819  HA  TRP A 384      19.499  45.816 -17.029  1.00 17.86           H  
ATOM   5820  HB2 TRP A 384      21.705  46.425 -18.674  1.00 24.73           H  
ATOM   5821  HB3 TRP A 384      21.832  45.288 -17.571  1.00 24.73           H  
ATOM   5822  HD1 TRP A 384      19.143  43.841 -18.213  1.00 17.15           H  
ATOM   5823  HE1 TRP A 384      18.924  42.495 -20.197  1.00 19.54           H  
ATOM   5824  HE3 TRP A 384      22.845  45.692 -20.848  1.00 22.02           H  
ATOM   5825  HZ2 TRP A 384      20.216  42.240 -22.631  1.00 20.75           H  
ATOM   5826  HZ3 TRP A 384      23.271  44.833 -22.952  1.00 21.17           H  
ATOM   5827  HH2 TRP A 384      21.955  43.151 -23.837  1.00 22.77           H  
ATOM   5828  N   GLY A 385      21.240  48.305 -16.124  1.00 18.60           N  
ANISOU 5828  N   GLY A 385     2490   2394   2184   -460   -262    181       N  
ATOM   5829  CA  GLY A 385      21.944  48.929 -15.020  1.00 18.39           C  
ANISOU 5829  CA  GLY A 385     2467   2378   2142   -502   -283    175       C  
ATOM   5830  C   GLY A 385      21.068  49.645 -14.021  1.00 18.02           C  
ANISOU 5830  C   GLY A 385     2474   2272   2103   -485   -306    142       C  
ATOM   5831  O   GLY A 385      21.571  50.164 -13.019  1.00 21.59           O  
ANISOU 5831  O   GLY A 385     2933   2729   2540   -518   -324    132       O  
ATOM   5832  H   GLY A 385      21.111  48.828 -16.795  1.00 22.32           H  
ATOM   5833  HA2 GLY A 385      22.437  48.244 -14.542  1.00 22.07           H  
ATOM   5834  HA3 GLY A 385      22.570  49.576 -15.380  1.00 22.07           H  
ATOM   5835  N   ARG A 386      19.762  49.679 -14.268  1.00 15.68           N  
ANISOU 5835  N   ARG A 386     2212   1920   1826   -434   -305    124       N  
ATOM   5836  CA  ARG A 386      18.810  50.415 -13.436  1.00 17.14           C  
ANISOU 5836  CA  ARG A 386     2449   2046   2018   -410   -325     89       C  
ATOM   5837  C   ARG A 386      17.594  49.531 -13.234  1.00 17.54           C  
ANISOU 5837  C   ARG A 386     2485   2092   2088   -334   -304     70       C  
ATOM   5838  O   ARG A 386      16.513  49.802 -13.769  1.00 18.19           O  
ANISOU 5838  O   ARG A 386     2601   2126   2185   -299   -308     60       O  
ATOM   5839  CB  ARG A 386      18.411  51.738 -14.088  1.00 23.27           C  
ANISOU 5839  CB  ARG A 386     3297   2748   2798   -434   -354     88       C  
ATOM   5840  CG  ARG A 386      19.496  52.796 -14.121  1.00 29.96           C  
ANISOU 5840  CG  ARG A 386     4172   3586   3625   -516   -381    103       C  
ATOM   5841  CD  ARG A 386      19.759  53.380 -12.731  1.00 42.20           C  
ANISOU 5841  CD  ARG A 386     5743   5128   5164   -537   -401     74       C  
ATOM   5842  NE  ARG A 386      18.558  53.917 -12.084  1.00115.17           N  
ANISOU 5842  NE  ARG A 386    15036  14304  14418   -489   -415     33       N  
ATOM   5843  CZ  ARG A 386      18.153  55.186 -12.153  1.00 88.13           C  
ANISOU 5843  CZ  ARG A 386    11687  10801  10998   -503   -447     17       C  
ATOM   5844  NH1 ARG A 386      18.838  56.083 -12.850  1.00103.91           N  
ANISOU 5844  NH1 ARG A 386    13723  12770  12988   -570   -471     42       N  
ATOM   5845  NH2 ARG A 386      17.050  55.561 -11.520  1.00 63.42           N  
ANISOU 5845  NH2 ARG A 386     8595   7620   7880   -448   -455    -24       N  
ATOM   5846  H   ARG A 386      19.393  49.271 -14.929  1.00 18.82           H  
ATOM   5847  HA  ARG A 386      19.217  50.613 -12.577  1.00 20.57           H  
ATOM   5848  HB2 ARG A 386      18.152  51.560 -15.006  1.00 27.93           H  
ATOM   5849  HB3 ARG A 386      17.660  52.107 -13.597  1.00 27.93           H  
ATOM   5850  HG2 ARG A 386      20.321  52.400 -14.444  1.00 35.95           H  
ATOM   5851  HG3 ARG A 386      19.223  53.518 -14.707  1.00 35.95           H  
ATOM   5852  HD2 ARG A 386      20.116  52.682 -12.160  1.00 50.64           H  
ATOM   5853  HD3 ARG A 386      20.400  54.103 -12.812  1.00 50.64           H  
ATOM   5854  HE  ARG A 386      18.078  53.372 -11.624  1.00138.20           H  
ATOM   5855 HH11 ARG A 386      19.554  55.849 -13.265  1.00124.69           H  
ATOM   5856 HH12 ARG A 386      18.567  56.898 -12.886  1.00124.69           H  
ATOM   5857 HH21 ARG A 386      16.599  54.986 -11.066  1.00 76.10           H  
ATOM   5858 HH22 ARG A 386      16.787  56.378 -11.562  1.00 76.10           H  
ATOM   5859  N   PRO A 387      17.741  48.436 -12.495  1.00 15.32           N  
ANISOU 5859  N   PRO A 387     2152   1863   1805   -307   -283     67       N  
ATOM   5860  CA  PRO A 387      16.644  47.470 -12.424  1.00 15.00           C  
ANISOU 5860  CA  PRO A 387     2094   1824   1782   -241   -261     55       C  
ATOM   5861  C   PRO A 387      15.465  48.014 -11.636  1.00 13.71           C  
ANISOU 5861  C   PRO A 387     1969   1617   1623   -206   -273     19       C  
ATOM   5862  O   PRO A 387      15.589  48.909 -10.793  1.00 15.82           O  
ANISOU 5862  O   PRO A 387     2268   1865   1880   -226   -294     -2       O  
ATOM   5863  CB  PRO A 387      17.264  46.250 -11.737  1.00 19.55           C  
ANISOU 5863  CB  PRO A 387     2610   2466   2353   -231   -240     66       C  
ATOM   5864  CG  PRO A 387      18.451  46.763 -11.018  1.00 18.90           C  
ANISOU 5864  CG  PRO A 387     2520   2412   2249   -283   -256     71       C  
ATOM   5865  CD  PRO A 387      18.949  47.960 -11.793  1.00 18.64           C  
ANISOU 5865  CD  PRO A 387     2526   2347   2208   -338   -278     80       C  
ATOM   5866  HA  PRO A 387      16.353  47.220 -13.315  1.00 18.00           H  
ATOM   5867  HB2 PRO A 387      16.625  45.863 -11.118  1.00 23.46           H  
ATOM   5868  HB3 PRO A 387      17.521  45.594 -12.403  1.00 23.46           H  
ATOM   5869  HG2 PRO A 387      18.197  47.021 -10.118  1.00 22.68           H  
ATOM   5870  HG3 PRO A 387      19.131  46.072 -10.984  1.00 22.68           H  
ATOM   5871  HD2 PRO A 387      19.291  48.641 -11.193  1.00 22.37           H  
ATOM   5872  HD3 PRO A 387      19.636  47.700 -12.425  1.00 22.37           H  
ATOM   5873  N   VAL A 388      14.300  47.430 -11.935  1.00 15.86           N  
ANISOU 5873  N   VAL A 388     2237   1878   1912   -152   -258     10       N  
ATOM   5874  CA  VAL A 388      13.058  47.845 -11.295  1.00 15.17           C  
ANISOU 5874  CA  VAL A 388     2178   1757   1830   -110   -266    -25       C  
ATOM   5875  C   VAL A 388      13.231  47.938  -9.785  1.00 16.35           C  
ANISOU 5875  C   VAL A 388     2323   1928   1964   -113   -269    -49       C  
ATOM   5876  O   VAL A 388      12.794  48.912  -9.162  1.00 15.42           O  
ANISOU 5876  O   VAL A 388     2245   1773   1840   -108   -288    -80       O  
ATOM   5877  CB  VAL A 388      11.907  46.886 -11.652  1.00 15.85           C  
ANISOU 5877  CB  VAL A 388     2240   1850   1931    -56   -244    -28       C  
ATOM   5878  CG1 VAL A 388      10.646  47.266 -10.857  1.00 16.40           C  
ANISOU 5878  CG1 VAL A 388     2331   1898   2004    -11   -249    -65       C  
ATOM   5879  CG2 VAL A 388      11.607  46.937 -13.119  1.00 16.24           C  
ANISOU 5879  CG2 VAL A 388     2301   1875   1994    -52   -244     -9       C  
ATOM   5880  H   VAL A 388      14.205  46.792 -12.504  1.00 19.04           H  
ATOM   5881  HA  VAL A 388      12.836  48.727 -11.633  1.00 18.21           H  
ATOM   5882  HB  VAL A 388      12.174  45.982 -11.423  1.00 19.02           H  
ATOM   5883 HG11 VAL A 388      10.322  48.125 -11.171  1.00 19.68           H  
ATOM   5884 HG12 VAL A 388       9.969  46.586 -10.996  1.00 19.68           H  
ATOM   5885 HG13 VAL A 388      10.872  47.322  -9.915  1.00 19.68           H  
ATOM   5886 HG21 VAL A 388      10.903  46.301 -13.320  1.00 19.48           H  
ATOM   5887 HG22 VAL A 388      11.319  47.833 -13.352  1.00 19.48           H  
ATOM   5888 HG23 VAL A 388      12.410  46.708 -13.614  1.00 19.48           H  
ATOM   5889  N   VAL A 389      13.844  46.920  -9.164  1.00 16.83           N  
ANISOU 5889  N   VAL A 389     2334   2046   2015   -118   -252    -35       N  
ATOM   5890  CA  VAL A 389      13.892  46.899  -7.704  1.00 16.44           C  
ANISOU 5890  CA  VAL A 389     2277   2023   1948   -116   -255    -56       C  
ATOM   5891  C   VAL A 389      14.811  47.997  -7.161  1.00 15.88           C  
ANISOU 5891  C   VAL A 389     2235   1942   1858   -168   -281    -66       C  
ATOM   5892  O   VAL A 389      14.661  48.403  -6.004  1.00 16.26           O  
ANISOU 5892  O   VAL A 389     2296   1993   1888   -169   -290    -95       O  
ATOM   5893  CB  VAL A 389      14.316  45.525  -7.134  1.00 12.91           C  
ANISOU 5893  CB  VAL A 389     1771   1639   1495   -108   -233    -35       C  
ATOM   5894  CG1 VAL A 389      13.266  44.451  -7.455  1.00 14.89           C  
ANISOU 5894  CG1 VAL A 389     2000   1895   1763    -58   -209    -32       C  
ATOM   5895  CG2 VAL A 389      15.679  45.103  -7.636  1.00 14.50           C  
ANISOU 5895  CG2 VAL A 389     1940   1874   1694   -145   -230      1       C  
ATOM   5896  H   VAL A 389      14.225  46.255  -9.554  1.00 20.20           H  
ATOM   5897  HA  VAL A 389      12.985  47.057  -7.400  1.00 19.73           H  
ATOM   5898  HB  VAL A 389      14.377  45.614  -6.170  1.00 15.49           H  
ATOM   5899 HG11 VAL A 389      13.575  43.596  -7.116  1.00 17.87           H  
ATOM   5900 HG12 VAL A 389      12.428  44.692  -7.031  1.00 17.87           H  
ATOM   5901 HG13 VAL A 389      13.148  44.403  -8.417  1.00 17.87           H  
ATOM   5902 HG21 VAL A 389      15.871  44.208  -7.314  1.00 17.40           H  
ATOM   5903 HG22 VAL A 389      15.675  45.112  -8.606  1.00 17.40           H  
ATOM   5904 HG23 VAL A 389      16.345  45.724  -7.302  1.00 17.40           H  
ATOM   5905  N   ASP A 390      15.742  48.515  -7.966  1.00 16.05           N  
ANISOU 5905  N   ASP A 390     2267   1952   1878   -216   -293    -43       N  
ATOM   5906  CA  ASP A 390      16.538  49.652  -7.513  1.00 18.86           C  
ANISOU 5906  CA  ASP A 390     2658   2293   2216   -271   -321    -53       C  
ATOM   5907  C   ASP A 390      15.677  50.907  -7.397  1.00 23.47           C  
ANISOU 5907  C   ASP A 390     3310   2804   2804   -260   -344    -90       C  
ATOM   5908  O   ASP A 390      15.842  51.689  -6.453  1.00 20.40           O  
ANISOU 5908  O   ASP A 390     2952   2401   2398   -281   -363   -119       O  
ATOM   5909  CB  ASP A 390      17.718  49.874  -8.458  1.00 19.25           C  
ANISOU 5909  CB  ASP A 390     2699   2352   2262   -328   -328    -17       C  
ATOM   5910  CG  ASP A 390      18.637  50.975  -7.989  1.00 39.85           C  
ANISOU 5910  CG  ASP A 390     5340   4952   4851   -395   -358    -22       C  
ATOM   5911  OD1 ASP A 390      19.135  50.882  -6.847  1.00 33.74           O  
ANISOU 5911  OD1 ASP A 390     4548   4216   4056   -412   -362    -33       O  
ATOM   5912  OD2 ASP A 390      18.859  51.927  -8.764  1.00 43.80           O  
ANISOU 5912  OD2 ASP A 390     5883   5407   5353   -433   -377    -15       O  
ATOM   5913  H   ASP A 390      15.928  48.235  -8.758  1.00 19.25           H  
ATOM   5914  HA  ASP A 390      16.902  49.459  -6.635  1.00 22.64           H  
ATOM   5915  HB2 ASP A 390      18.235  49.055  -8.517  1.00 23.10           H  
ATOM   5916  HB3 ASP A 390      17.380  50.117  -9.334  1.00 23.10           H  
ATOM   5917  N   TYR A 391      14.740  51.103  -8.331  1.00 19.27           N  
ANISOU 5917  N   TYR A 391     2804   2225   2294   -224   -343    -92       N  
ATOM   5918  CA  TYR A 391      13.750  52.168  -8.188  1.00 23.27           C  
ANISOU 5918  CA  TYR A 391     3371   2664   2808   -196   -362   -129       C  
ATOM   5919  C   TYR A 391      12.976  52.018  -6.884  1.00 21.86           C  
ANISOU 5919  C   TYR A 391     3188   2500   2619   -154   -354   -172       C  
ATOM   5920  O   TYR A 391      12.825  52.979  -6.119  1.00 22.07           O  
ANISOU 5920  O   TYR A 391     3258   2492   2634   -157   -374   -209       O  
ATOM   5921  CB  TYR A 391      12.785  52.149  -9.376  1.00 19.29           C  
ANISOU 5921  CB  TYR A 391     2881   2122   2329   -155   -358   -120       C  
ATOM   5922  CG  TYR A 391      13.345  52.754 -10.638  1.00 19.27           C  
ANISOU 5922  CG  TYR A 391     2906   2083   2332   -197   -375    -88       C  
ATOM   5923  CD1 TYR A 391      14.116  52.003 -11.521  1.00 22.68           C  
ANISOU 5923  CD1 TYR A 391     3297   2557   2764   -226   -359    -45       C  
ATOM   5924  CD2 TYR A 391      13.104  54.083 -10.950  1.00 22.76           C  
ANISOU 5924  CD2 TYR A 391     3418   2449   2779   -208   -407   -100       C  
ATOM   5925  CE1 TYR A 391      14.636  52.571 -12.690  1.00 20.79           C  
ANISOU 5925  CE1 TYR A 391     3083   2292   2526   -268   -374    -15       C  
ATOM   5926  CE2 TYR A 391      13.614  54.654 -12.101  1.00 22.56           C  
ANISOU 5926  CE2 TYR A 391     3422   2393   2758   -251   -424    -66       C  
ATOM   5927  CZ  TYR A 391      14.377  53.898 -12.970  1.00 23.82           C  
ANISOU 5927  CZ  TYR A 391     3536   2601   2914   -283   -406    -23       C  
ATOM   5928  OH  TYR A 391      14.878  54.487 -14.110  1.00 27.33           O  
ANISOU 5928  OH  TYR A 391     4008   3018   3356   -329   -422     10       O  
ATOM   5929  H   TYR A 391      14.656  50.638  -9.049  1.00 23.13           H  
ATOM   5930  HA  TYR A 391      14.210  53.021  -8.180  1.00 27.93           H  
ATOM   5931  HB2 TYR A 391      12.551  51.228  -9.570  1.00 23.15           H  
ATOM   5932  HB3 TYR A 391      11.990  52.651  -9.137  1.00 23.15           H  
ATOM   5933  HD1 TYR A 391      14.288  51.109 -11.332  1.00 27.21           H  
ATOM   5934  HD2 TYR A 391      12.588  54.600 -10.374  1.00 27.31           H  
ATOM   5935  HE1 TYR A 391      15.152  52.061 -13.272  1.00 24.95           H  
ATOM   5936  HE2 TYR A 391      13.443  55.548 -12.291  1.00 27.08           H  
ATOM   5937  HH  TYR A 391      15.491  54.013 -14.432  1.00 32.79           H  
ATOM   5938  N   VAL A 392      12.487  50.807  -6.613  1.00 18.89           N  
ANISOU 5938  N   VAL A 392     2758   2174   2245   -114   -326   -166       N  
ATOM   5939  CA  VAL A 392      11.706  50.564  -5.407  1.00 17.77           C  
ANISOU 5939  CA  VAL A 392     2606   2056   2091    -75   -315   -202       C  
ATOM   5940  C   VAL A 392      12.529  50.884  -4.165  1.00 18.86           C  
ANISOU 5940  C   VAL A 392     2746   2220   2199   -114   -326   -219       C  
ATOM   5941  O   VAL A 392      12.068  51.578  -3.249  1.00 20.21           O  
ANISOU 5941  O   VAL A 392     2949   2376   2356   -101   -336   -263       O  
ATOM   5942  CB  VAL A 392      11.202  49.109  -5.383  1.00 20.34           C  
ANISOU 5942  CB  VAL A 392     2872   2436   2422    -39   -284   -183       C  
ATOM   5943  CG1 VAL A 392      10.511  48.824  -4.063  1.00 21.58           C  
ANISOU 5943  CG1 VAL A 392     3013   2627   2560     -8   -272   -216       C  
ATOM   5944  CG2 VAL A 392      10.285  48.831  -6.578  1.00 24.39           C  
ANISOU 5944  CG2 VAL A 392     3384   2923   2962     -1   -274   -172       C  
ATOM   5945  H   VAL A 392      12.593  50.113  -7.110  1.00 22.67           H  
ATOM   5946  HA  VAL A 392      10.936  51.154  -5.415  1.00 21.33           H  
ATOM   5947  HB  VAL A 392      11.956  48.503  -5.461  1.00 24.41           H  
ATOM   5948 HG11 VAL A 392       9.990  48.010  -4.148  1.00 25.90           H  
ATOM   5949 HG12 VAL A 392      11.182  48.715  -3.372  1.00 25.90           H  
ATOM   5950 HG13 VAL A 392       9.928  49.568  -3.844  1.00 25.90           H  
ATOM   5951 HG21 VAL A 392       9.585  48.218  -6.303  1.00 29.27           H  
ATOM   5952 HG22 VAL A 392       9.893  49.667  -6.876  1.00 29.27           H  
ATOM   5953 HG23 VAL A 392      10.808  48.438  -7.293  1.00 29.27           H  
ATOM   5954  N   LEU A 393      13.760  50.382  -4.109  1.00 18.67           N  
ANISOU 5954  N   LEU A 393     2689   2241   2164   -162   -325   -185       N  
ATOM   5955  CA  LEU A 393      14.526  50.538  -2.880  1.00 21.05           C  
ANISOU 5955  CA  LEU A 393     2983   2579   2434   -199   -335   -198       C  
ATOM   5956  C   LEU A 393      14.956  51.983  -2.656  1.00 21.58           C  
ANISOU 5956  C   LEU A 393     3113   2597   2490   -242   -367   -225       C  
ATOM   5957  O   LEU A 393      15.051  52.413  -1.503  1.00 25.52           O  
ANISOU 5957  O   LEU A 393     3627   3107   2963   -255   -378   -259       O  
ATOM   5958  CB  LEU A 393      15.741  49.614  -2.875  1.00 18.62           C  
ANISOU 5958  CB  LEU A 393     2620   2337   2119   -236   -326   -153       C  
ATOM   5959  CG  LEU A 393      15.385  48.127  -2.793  1.00 22.20           C  
ANISOU 5959  CG  LEU A 393     3014   2841   2579   -195   -296   -129       C  
ATOM   5960  CD1 LEU A 393      16.647  47.256  -2.804  1.00 26.15           C  
ANISOU 5960  CD1 LEU A 393     3462   3403   3073   -226   -291    -85       C  
ATOM   5961  CD2 LEU A 393      14.532  47.759  -1.576  1.00 33.38           C  
ANISOU 5961  CD2 LEU A 393     4420   4284   3978   -158   -286   -158       C  
ATOM   5962  H   LEU A 393      14.161  49.963  -4.744  1.00 22.41           H  
ATOM   5963  HA  LEU A 393      13.958  50.277  -2.139  1.00 25.26           H  
ATOM   5964  HB2 LEU A 393      16.242  49.755  -3.694  1.00 22.35           H  
ATOM   5965  HB3 LEU A 393      16.293  49.830  -2.107  1.00 22.35           H  
ATOM   5966  HG  LEU A 393      14.848  47.942  -3.580  1.00 26.64           H  
ATOM   5967 HD11 LEU A 393      16.556  46.560  -2.135  1.00 31.39           H  
ATOM   5968 HD12 LEU A 393      16.749  46.859  -3.683  1.00 31.39           H  
ATOM   5969 HD13 LEU A 393      17.416  47.812  -2.601  1.00 31.39           H  
ATOM   5970 HD21 LEU A 393      14.036  46.949  -1.771  1.00 40.05           H  
ATOM   5971 HD22 LEU A 393      15.116  47.613  -0.814  1.00 40.05           H  
ATOM   5972 HD23 LEU A 393      13.919  48.486  -1.388  1.00 40.05           H  
ATOM   5973  N   THR A 394      15.226  52.743  -3.722  1.00 21.25           N  
ANISOU 5973  N   THR A 394     3109   2500   2464   -268   -385   -212       N  
ATOM   5974  CA  THR A 394      15.574  54.154  -3.590  1.00 22.06           C  
ANISOU 5974  CA  THR A 394     3280   2545   2559   -311   -418   -237       C  
ATOM   5975  C   THR A 394      14.342  55.056  -3.577  1.00 22.32           C  
ANISOU 5975  C   THR A 394     3373   2502   2604   -261   -430   -283       C  
ATOM   5976  O   THR A 394      14.480  56.284  -3.583  1.00 27.99           O  
ANISOU 5976  O   THR A 394     4158   3156   3320   -288   -459   -305       O  
ATOM   5977  CB  THR A 394      16.527  54.585  -4.713  1.00 24.49           C  
ANISOU 5977  CB  THR A 394     3601   2831   2875   -370   -434   -196       C  
ATOM   5978  OG1 THR A 394      15.890  54.453  -5.988  1.00 23.88           O  
ANISOU 5978  OG1 THR A 394     3529   2718   2825   -337   -426   -176       O  
ATOM   5979  CG2 THR A 394      17.793  53.736  -4.693  1.00 29.21           C  
ANISOU 5979  CG2 THR A 394     4133   3507   3457   -417   -424   -154       C  
ATOM   5980  H   THR A 394      15.211  52.458  -4.534  1.00 25.50           H  
ATOM   5981  HA  THR A 394      16.047  54.275  -2.751  1.00 26.48           H  
ATOM   5982  HB  THR A 394      16.771  55.514  -4.579  1.00 29.39           H  
ATOM   5983  HG1 THR A 394      15.116  54.779  -5.958  1.00 28.65           H  
ATOM   5984 HG21 THR A 394      18.422  54.063  -5.355  1.00 35.05           H  
ATOM   5985 HG22 THR A 394      18.207  53.778  -3.817  1.00 35.05           H  
ATOM   5986 HG23 THR A 394      17.576  52.812  -4.895  1.00 35.05           H  
ATOM   5987  N   GLN A 395      13.149  54.462  -3.535  1.00 24.12           N  
ANISOU 5987  N   GLN A 395     3580   2739   2844   -189   -407   -297       N  
ATOM   5988  CA  GLN A 395      11.877  55.184  -3.566  1.00 24.89           C  
ANISOU 5988  CA  GLN A 395     3725   2776   2956   -130   -413   -339       C  
ATOM   5989  C   GLN A 395      11.818  56.188  -4.716  1.00 27.86           C  
ANISOU 5989  C   GLN A 395     4161   3069   3356   -139   -440   -329       C  
ATOM   5990  O   GLN A 395      11.394  57.336  -4.559  1.00 29.59           O  
ANISOU 5990  O   GLN A 395     4445   3218   3578   -126   -464   -367       O  
ATOM   5991  CB  GLN A 395      11.610  55.862  -2.222  1.00 31.95           C  
ANISOU 5991  CB  GLN A 395     4652   3664   3826   -120   -423   -398       C  
ATOM   5992  CG  GLN A 395      11.217  54.870  -1.144  1.00 36.41           C  
ANISOU 5992  CG  GLN A 395     5158   4306   4368    -90   -394   -413       C  
ATOM   5993  CD  GLN A 395      10.914  55.529   0.177  1.00 48.55           C  
ANISOU 5993  CD  GLN A 395     6726   5842   5877    -79   -402   -474       C  
ATOM   5994  OE1 GLN A 395      11.819  55.972   0.885  1.00 48.79           O  
ANISOU 5994  OE1 GLN A 395     6775   5880   5882   -134   -419   -486       O  
ATOM   5995  NE2 GLN A 395       9.633  55.595   0.524  1.00 60.56           N  
ANISOU 5995  NE2 GLN A 395     8251   7358   7401     -9   -389   -515       N  
ATOM   5996  H   GLN A 395      13.048  53.610  -3.486  1.00 28.94           H  
ATOM   5997  HA  GLN A 395      11.171  54.538  -3.727  1.00 29.87           H  
ATOM   5998  HB2 GLN A 395      12.415  56.320  -1.932  1.00 38.35           H  
ATOM   5999  HB3 GLN A 395      10.885  56.498  -2.326  1.00 38.35           H  
ATOM   6000  HG2 GLN A 395      10.423  54.392  -1.430  1.00 43.69           H  
ATOM   6001  HG3 GLN A 395      11.948  54.247  -1.008  1.00 43.69           H  
ATOM   6002 HE21 GLN A 395       9.030  55.272   0.004  1.00 72.67           H  
ATOM   6003 HE22 GLN A 395       9.408  55.961   1.269  1.00 72.67           H  
ATOM   6004  N   ASN A 396      12.227  55.731  -5.895  1.00 24.16           N  
ANISOU 6004  N   ASN A 396     3670   2608   2903   -160   -434   -278       N  
ATOM   6005  CA  ASN A 396      12.119  56.501  -7.129  1.00 23.29           C  
ANISOU 6005  CA  ASN A 396     3608   2428   2814   -168   -456   -258       C  
ATOM   6006  C   ASN A 396      10.944  55.939  -7.921  1.00 29.33           C  
ANISOU 6006  C   ASN A 396     4350   3190   3602   -100   -438   -250       C  
ATOM   6007  O   ASN A 396      10.961  54.762  -8.296  1.00 26.50           O  
ANISOU 6007  O   ASN A 396     3931   2890   3248    -91   -410   -220       O  
ATOM   6008  CB  ASN A 396      13.418  56.403  -7.928  1.00 28.11           C  
ANISOU 6008  CB  ASN A 396     4206   3055   3420   -244   -462   -206       C  
ATOM   6009  CG  ASN A 396      13.461  57.355  -9.112  1.00 33.53           C  
ANISOU 6009  CG  ASN A 396     4950   3668   4122   -267   -489   -184       C  
ATOM   6010  OD1 ASN A 396      12.431  57.738  -9.661  1.00 32.90           O  
ANISOU 6010  OD1 ASN A 396     4903   3536   4064   -216   -497   -194       O  
ATOM   6011  ND2 ASN A 396      14.664  57.734  -9.514  1.00 29.06           N  
ANISOU 6011  ND2 ASN A 396     4394   3102   3544   -347   -505   -152       N  
ATOM   6012  H   ASN A 396      12.581  54.956  -6.006  1.00 28.99           H  
ATOM   6013  HA  ASN A 396      11.952  57.438  -6.941  1.00 27.95           H  
ATOM   6014  HB2 ASN A 396      14.163  56.616  -7.346  1.00 33.74           H  
ATOM   6015  HB3 ASN A 396      13.511  55.499  -8.268  1.00 33.74           H  
ATOM   6016 HD21 ASN A 396      15.368  57.445  -9.114  1.00 34.87           H  
ATOM   6017  N   THR A 397       9.918  56.757  -8.155  1.00 25.12           N  
ANISOU 6017  N   THR A 397     3867   2590   3086    -51   -454   -277       N  
ATOM   6018  CA  THR A 397       8.721  56.295  -8.848  1.00 25.74           C  
ANISOU 6018  CA  THR A 397     3925   2670   3186     16   -440   -272       C  
ATOM   6019  C   THR A 397       8.692  56.714 -10.312  1.00 23.67           C  
ANISOU 6019  C   THR A 397     3693   2358   2943      6   -458   -234       C  
ATOM   6020  O   THR A 397       7.692  56.475 -10.999  1.00 28.83           O  
ANISOU 6020  O   THR A 397     4336   3004   3614     59   -453   -228       O  
ATOM   6021  CB  THR A 397       7.461  56.808  -8.145  1.00 39.56           C  
ANISOU 6021  CB  THR A 397     5699   4392   4940     89   -444   -327       C  
ATOM   6022  OG1 THR A 397       7.514  58.237  -8.066  1.00 41.46           O  
ANISOU 6022  OG1 THR A 397     6020   4547   5185     83   -481   -353       O  
ATOM   6023  CG2 THR A 397       7.348  56.214  -6.749  1.00 43.60           C  
ANISOU 6023  CG2 THR A 397     6170   4966   5428    104   -420   -362       C  
ATOM   6024  H   THR A 397       9.896  57.584  -7.920  1.00 30.14           H  
ATOM   6025  HA  THR A 397       8.710  55.326  -8.811  1.00 30.89           H  
ATOM   6026  HB  THR A 397       6.673  56.543  -8.645  1.00 47.47           H  
ATOM   6027  HG1 THR A 397       7.847  58.552  -8.770  1.00 49.75           H  
ATOM   6028 HG21 THR A 397       6.535  56.526  -6.320  1.00 52.32           H  
ATOM   6029 HG22 THR A 397       7.324  55.246  -6.801  1.00 52.32           H  
ATOM   6030 HG23 THR A 397       8.110  56.482  -6.211  1.00 52.32           H  
ATOM   6031  N   SER A 398       9.771  57.321 -10.802  1.00 26.92           N  
ANISOU 6031  N   SER A 398     4139   2740   3350    -64   -480   -206       N  
ATOM   6032  CA  SER A 398       9.839  57.820 -12.175  1.00 30.07           C  
ANISOU 6032  CA  SER A 398     4572   3091   3762    -83   -500   -167       C  
ATOM   6033  C   SER A 398      10.361  56.736 -13.119  1.00 21.68           C  
ANISOU 6033  C   SER A 398     3450   2090   2698   -111   -476   -117       C  
ATOM   6034  O   SER A 398      11.393  56.879 -13.776  1.00 30.16           O  
ANISOU 6034  O   SER A 398     4529   3167   3763   -177   -483    -79       O  
ATOM   6035  CB  SER A 398      10.716  59.063 -12.231  1.00 38.18           C  
ANISOU 6035  CB  SER A 398     5668   4055   4783   -149   -538   -161       C  
ATOM   6036  OG  SER A 398      10.314  59.984 -11.239  1.00 37.60           O  
ANISOU 6036  OG  SER A 398     5648   3928   4709   -124   -558   -213       O  
ATOM   6037  H   SER A 398      10.489  57.458 -10.351  1.00 32.30           H  
ATOM   6038  HA  SER A 398       8.944  58.060 -12.461  1.00 36.08           H  
ATOM   6039  HB2 SER A 398      11.639  58.810 -12.076  1.00 45.81           H  
ATOM   6040  HB3 SER A 398      10.628  59.476 -13.104  1.00 45.81           H  
ATOM   6041  HG  SER A 398       9.476  60.018 -11.201  1.00 45.12           H  
ATOM   6042  N   PHE A 399       9.615  55.639 -13.181  1.00 21.83           N  
ANISOU 6042  N   PHE A 399     3413   2159   2723    -59   -446   -118       N  
ATOM   6043  CA  PHE A 399       9.956  54.567 -14.102  1.00 24.96           C  
ANISOU 6043  CA  PHE A 399     3756   2609   3119    -75   -421    -77       C  
ATOM   6044  C   PHE A 399       9.863  55.059 -15.546  1.00 26.37           C  
ANISOU 6044  C   PHE A 399     3966   2746   3306    -89   -439    -42       C  
ATOM   6045  O   PHE A 399       8.888  55.727 -15.910  1.00 25.72           O  
ANISOU 6045  O   PHE A 399     3924   2610   3238    -46   -459    -52       O  
ATOM   6046  CB  PHE A 399       9.010  53.375 -13.928  1.00 22.72           C  
ANISOU 6046  CB  PHE A 399     3416   2375   2843    -15   -390    -88       C  
ATOM   6047  CG  PHE A 399       9.084  52.713 -12.586  1.00 18.14           C  
ANISOU 6047  CG  PHE A 399     2798   1845   2251     -3   -369   -115       C  
ATOM   6048  CD1 PHE A 399      10.107  51.831 -12.289  1.00 20.52           C  
ANISOU 6048  CD1 PHE A 399     3053   2205   2539    -42   -348    -96       C  
ATOM   6049  CD2 PHE A 399       8.106  52.943 -11.635  1.00 20.07           C  
ANISOU 6049  CD2 PHE A 399     3050   2079   2497     49   -369   -159       C  
ATOM   6050  CE1 PHE A 399      10.165  51.213 -11.067  1.00 20.94           C  
ANISOU 6050  CE1 PHE A 399     3072   2304   2581    -31   -332   -116       C  
ATOM   6051  CE2 PHE A 399       8.161  52.328 -10.411  1.00 23.34           C  
ANISOU 6051  CE2 PHE A 399     3429   2543   2897     57   -350   -181       C  
ATOM   6052  CZ  PHE A 399       9.193  51.464 -10.123  1.00 25.01           C  
ANISOU 6052  CZ  PHE A 399     3598   2811   3096     15   -332   -158       C  
ATOM   6053  H   PHE A 399       8.913  55.492 -12.707  1.00 26.20           H  
ATOM   6054  HA  PHE A 399      10.865  54.281 -13.919  1.00 29.95           H  
ATOM   6055  HB2 PHE A 399       8.098  53.683 -14.053  1.00 27.27           H  
ATOM   6056  HB3 PHE A 399       9.229  52.707 -14.597  1.00 27.27           H  
ATOM   6057  HD1 PHE A 399      10.762  51.655 -12.925  1.00 24.63           H  
ATOM   6058  HD2 PHE A 399       7.403  53.521 -11.828  1.00 24.08           H  
ATOM   6059  HE1 PHE A 399      10.860  50.625 -10.875  1.00 25.13           H  
ATOM   6060  HE2 PHE A 399       7.502  52.494  -9.776  1.00 28.01           H  
ATOM   6061  HZ  PHE A 399       9.234  51.049  -9.292  1.00 30.02           H  
ATOM   6062  N   PRO A 400      10.829  54.720 -16.401  1.00 20.37           N  
ANISOU 6062  N   PRO A 400     3188   2016   2537   -144   -433      0       N  
ATOM   6063  CA  PRO A 400      10.668  55.001 -17.828  1.00 24.27           C  
ANISOU 6063  CA  PRO A 400     3703   2484   3036   -155   -445     35       C  
ATOM   6064  C   PRO A 400       9.444  54.302 -18.381  1.00 22.45           C  
ANISOU 6064  C   PRO A 400     3446   2266   2818    -89   -430     32       C  
ATOM   6065  O   PRO A 400       9.044  53.229 -17.892  1.00 24.11           O  
ANISOU 6065  O   PRO A 400     3603   2527   3030    -53   -400     16       O  
ATOM   6066  CB  PRO A 400      11.961  54.448 -18.446  1.00 25.52           C  
ANISOU 6066  CB  PRO A 400     3824   2696   3175   -221   -429     74       C  
ATOM   6067  CG  PRO A 400      12.950  54.422 -17.327  1.00 29.34           C  
ANISOU 6067  CG  PRO A 400     4294   3209   3647   -259   -424     60       C  
ATOM   6068  CD  PRO A 400      12.142  54.116 -16.100  1.00 22.35           C  
ANISOU 6068  CD  PRO A 400     3396   2326   2769   -200   -415     16       C  
ATOM   6069  HA  PRO A 400      10.604  55.956 -17.988  1.00 29.13           H  
ATOM   6070  HB2 PRO A 400      11.805  53.555 -18.791  1.00 30.62           H  
ATOM   6071  HB3 PRO A 400      12.261  55.032 -19.160  1.00 30.62           H  
ATOM   6072  HG2 PRO A 400      13.612  53.731 -17.487  1.00 35.21           H  
ATOM   6073  HG3 PRO A 400      13.384  55.286 -17.250  1.00 35.21           H  
ATOM   6074  HD2 PRO A 400      12.061  53.159 -15.969  1.00 26.82           H  
ATOM   6075  HD3 PRO A 400      12.539  54.525 -15.315  1.00 26.82           H  
ATOM   6076  N   PRO A 401       8.828  54.861 -19.427  1.00 26.83           N  
ANISOU 6076  N   PRO A 401     4035   2778   3380    -76   -451     51       N  
ATOM   6077  CA  PRO A 401       7.580  54.270 -19.946  1.00 27.83           C  
ANISOU 6077  CA  PRO A 401     4137   2917   3519    -13   -441     47       C  
ATOM   6078  C   PRO A 401       7.727  52.822 -20.396  1.00 33.86           C  
ANISOU 6078  C   PRO A 401     4833   3754   4276    -16   -403     61       C  
ATOM   6079  O   PRO A 401       6.779  52.034 -20.245  1.00 23.50           O  
ANISOU 6079  O   PRO A 401     3487   2470   2973     36   -385     44       O  
ATOM   6080  CB  PRO A 401       7.213  55.191 -21.124  1.00 24.28           C  
ANISOU 6080  CB  PRO A 401     3739   2411   3074    -16   -474     76       C  
ATOM   6081  CG  PRO A 401       7.998  56.440 -20.926  1.00 37.42           C  
ANISOU 6081  CG  PRO A 401     5467   4016   4734    -65   -507     83       C  
ATOM   6082  CD  PRO A 401       9.255  56.040 -20.204  1.00 33.13           C  
ANISOU 6082  CD  PRO A 401     4896   3517   4176   -121   -487     80       C  
ATOM   6083  HA  PRO A 401       6.889  54.324 -19.267  1.00 33.39           H  
ATOM   6084  HB2 PRO A 401       7.453  54.763 -21.960  1.00 29.13           H  
ATOM   6085  HB3 PRO A 401       6.261  55.378 -21.108  1.00 29.13           H  
ATOM   6086  HG2 PRO A 401       8.209  56.831 -21.788  1.00 44.90           H  
ATOM   6087  HG3 PRO A 401       7.484  57.067 -20.394  1.00 44.90           H  
ATOM   6088  HD2 PRO A 401       9.956  55.806 -20.832  1.00 39.76           H  
ATOM   6089  HD3 PRO A 401       9.559  56.750 -19.617  1.00 39.76           H  
ATOM   6090  N   GLY A 402       8.893  52.454 -20.945  1.00 21.11           N  
ANISOU 6090  N   GLY A 402     3201   2174   2646    -75   -391     91       N  
ATOM   6091  CA  GLY A 402       9.195  51.111 -21.414  1.00 20.90           C  
ANISOU 6091  CA  GLY A 402     3115   2214   2612    -80   -356    104       C  
ATOM   6092  C   GLY A 402       9.317  50.065 -20.326  1.00 17.78           C  
ANISOU 6092  C   GLY A 402     2670   1867   2219    -61   -326     80       C  
ATOM   6093  O   GLY A 402       9.392  48.872 -20.642  1.00 17.18           O  
ANISOU 6093  O   GLY A 402     2546   1840   2141    -54   -297     87       O  
ATOM   6094  H   GLY A 402       9.552  52.995 -21.060  1.00 25.33           H  
ATOM   6095  HA2 GLY A 402       8.490  50.828 -22.018  1.00 25.08           H  
ATOM   6096  HA3 GLY A 402      10.035  51.133 -21.898  1.00 25.08           H  
ATOM   6097  N   TYR A 403       9.343  50.475 -19.061  1.00 15.06           N  
ANISOU 6097  N   TYR A 403     2337   1509   1878    -52   -333     53       N  
ATOM   6098  CA  TYR A 403       9.358  49.512 -17.966  1.00 15.47           C  
ANISOU 6098  CA  TYR A 403     2342   1605   1929    -32   -307     32       C  
ATOM   6099  C   TYR A 403       8.021  48.801 -17.783  1.00 17.17           C  
ANISOU 6099  C   TYR A 403     2534   1833   2156     29   -293     12       C  
ATOM   6100  O   TYR A 403       7.975  47.777 -17.094  1.00 15.95           O  
ANISOU 6100  O   TYR A 403     2338   1722   2001     44   -268      2       O  
ATOM   6101  CB  TYR A 403       9.789  50.224 -16.681  1.00 16.36           C  
ANISOU 6101  CB  TYR A 403     2477   1703   2037    -45   -320      9       C  
ATOM   6102  CG  TYR A 403      11.296  50.277 -16.511  1.00 15.20           C  
ANISOU 6102  CG  TYR A 403     2320   1580   1874   -108   -319     28       C  
ATOM   6103  CD1 TYR A 403      12.115  50.674 -17.558  1.00 16.72           C  
ANISOU 6103  CD1 TYR A 403     2527   1767   2058   -159   -329     61       C  
ATOM   6104  CD2 TYR A 403      11.897  49.913 -15.317  1.00 18.16           C  
ANISOU 6104  CD2 TYR A 403     2669   1990   2239   -119   -309     14       C  
ATOM   6105  CE1 TYR A 403      13.486  50.715 -17.426  1.00 19.47           C  
ANISOU 6105  CE1 TYR A 403     2861   2146   2390   -218   -327     79       C  
ATOM   6106  CE2 TYR A 403      13.280  49.951 -15.174  1.00 19.20           C  
ANISOU 6106  CE2 TYR A 403     2788   2152   2356   -176   -310     33       C  
ATOM   6107  CZ  TYR A 403      14.069  50.347 -16.239  1.00 21.95           C  
ANISOU 6107  CZ  TYR A 403     3148   2496   2698   -226   -318     65       C  
ATOM   6108  OH  TYR A 403      15.446  50.396 -16.132  1.00 20.14           O  
ANISOU 6108  OH  TYR A 403     2899   2302   2450   -284   -318     84       O  
ATOM   6109  H   TYR A 403       9.353  51.298 -18.812  1.00 18.08           H  
ATOM   6110  HA  TYR A 403      10.012  48.819 -18.149  1.00 18.56           H  
ATOM   6111  HB2 TYR A 403       9.458  51.136 -16.700  1.00 19.63           H  
ATOM   6112  HB3 TYR A 403       9.418  49.752 -15.920  1.00 19.63           H  
ATOM   6113  HD1 TYR A 403      11.730  50.918 -18.368  1.00 20.06           H  
ATOM   6114  HD2 TYR A 403      11.369  49.640 -14.602  1.00 21.79           H  
ATOM   6115  HE1 TYR A 403      14.015  50.991 -18.139  1.00 23.36           H  
ATOM   6116  HE2 TYR A 403      13.673  49.711 -14.366  1.00 23.04           H  
ATOM   6117  HH  TYR A 403      15.762  49.618 -16.142  1.00 24.16           H  
ATOM   6118  N   ASN A 404       6.944  49.300 -18.385  1.00 16.32           N  
ANISOU 6118  N   ASN A 404     2451   1690   2058     63   -309      8       N  
ATOM   6119  CA  ASN A 404       5.661  48.597 -18.404  1.00 13.91           C  
ANISOU 6119  CA  ASN A 404     2119   1403   1762    117   -296     -6       C  
ATOM   6120  C   ASN A 404       5.235  48.153 -17.006  1.00 11.80           C  
ANISOU 6120  C   ASN A 404     1826   1162   1495    147   -281    -38       C  
ATOM   6121  O   ASN A 404       4.792  47.025 -16.781  1.00 14.29           O  
ANISOU 6121  O   ASN A 404     2098   1520   1811    165   -256    -42       O  
ATOM   6122  CB  ASN A 404       5.732  47.426 -19.382  1.00 15.41           C  
ANISOU 6122  CB  ASN A 404     2271   1633   1950    107   -273     17       C  
ATOM   6123  CG  ASN A 404       5.705  47.894 -20.822  1.00 14.87           C  
ANISOU 6123  CG  ASN A 404     2229   1543   1880     91   -290     44       C  
ATOM   6124  OD1 ASN A 404       5.840  49.089 -21.100  1.00 18.72           O  
ANISOU 6124  OD1 ASN A 404     2762   1983   2367     79   -319     51       O  
ATOM   6125  ND2 ASN A 404       5.505  46.967 -21.743  1.00 15.42           N  
ANISOU 6125  ND2 ASN A 404     2270   1642   1946     91   -273     58       N  
ATOM   6126  H   ASN A 404       6.931  50.056 -18.795  1.00 19.58           H  
ATOM   6127  HA  ASN A 404       4.970  49.207 -18.707  1.00 16.69           H  
ATOM   6128  HB2 ASN A 404       6.557  46.938 -19.237  1.00 18.49           H  
ATOM   6129  HB3 ASN A 404       4.971  46.842 -19.238  1.00 18.49           H  
ATOM   6130 HD21 ASN A 404       5.481  47.185 -22.575  1.00 18.50           H  
ATOM   6131 HD22 ASN A 404       5.398  46.146 -21.511  1.00 18.50           H  
ATOM   6132  N   ILE A 405       5.312  49.091 -16.068  1.00 15.37           N  
ANISOU 6132  N   ILE A 405     2308   1585   1945    151   -298    -62       N  
ATOM   6133  CA  ILE A 405       4.998  48.799 -14.675  1.00 18.24           C  
ANISOU 6133  CA  ILE A 405     2652   1975   2304    175   -285    -94       C  
ATOM   6134  C   ILE A 405       3.491  48.708 -14.497  1.00 13.40           C  
ANISOU 6134  C   ILE A 405     2026   1366   1698    235   -282   -118       C  
ATOM   6135  O   ILE A 405       2.759  49.659 -14.800  1.00 17.25           O  
ANISOU 6135  O   ILE A 405     2548   1812   2194    266   -305   -131       O  
ATOM   6136  CB  ILE A 405       5.574  49.883 -13.746  1.00 15.22           C  
ANISOU 6136  CB  ILE A 405     2308   1560   1913    158   -304   -116       C  
ATOM   6137  CG1 ILE A 405       7.098  49.934 -13.832  1.00 15.93           C  
ANISOU 6137  CG1 ILE A 405     2404   1656   1994     93   -306    -91       C  
ATOM   6138  CG2 ILE A 405       5.127  49.650 -12.295  1.00 16.51           C  
ANISOU 6138  CG2 ILE A 405     2453   1753   2068    186   -292   -152       C  
ATOM   6139  CD1 ILE A 405       7.782  48.676 -13.398  1.00 20.86           C  
ANISOU 6139  CD1 ILE A 405     2974   2342   2609     74   -278    -78       C  
ATOM   6140  H   ILE A 405       5.545  49.906 -16.214  1.00 18.44           H  
ATOM   6141  HA  ILE A 405       5.390  47.942 -14.447  1.00 21.89           H  
ATOM   6142  HB  ILE A 405       5.227  50.738 -14.046  1.00 18.26           H  
ATOM   6143 HG12 ILE A 405       7.351  50.103 -14.753  1.00 19.12           H  
ATOM   6144 HG13 ILE A 405       7.417  50.653 -13.264  1.00 19.12           H  
ATOM   6145 HG21 ILE A 405       5.671  50.196 -11.706  1.00 19.82           H  
ATOM   6146 HG22 ILE A 405       4.194  49.899 -12.208  1.00 19.82           H  
ATOM   6147 HG23 ILE A 405       5.241  48.712 -12.076  1.00 19.82           H  
ATOM   6148 HD11 ILE A 405       8.740  48.780 -13.514  1.00 25.03           H  
ATOM   6149 HD12 ILE A 405       7.578  48.512 -12.463  1.00 25.03           H  
ATOM   6150 HD13 ILE A 405       7.462  47.939 -13.940  1.00 25.03           H  
ATOM   6151  N   VAL A 406       3.034  47.586 -13.950  1.00 14.77           N  
ANISOU 6151  N   VAL A 406     2152   1592   1868    252   -255   -125       N  
ATOM   6152  CA  VAL A 406       1.636  47.361 -13.602  1.00 14.37           C  
ANISOU 6152  CA  VAL A 406     2079   1562   1820    304   -248   -148       C  
ATOM   6153  C   VAL A 406       1.604  47.109 -12.095  1.00 14.81           C  
ANISOU 6153  C   VAL A 406     2115   1651   1861    312   -233   -176       C  
ATOM   6154  O   VAL A 406       2.035  46.043 -11.637  1.00 16.70           O  
ANISOU 6154  O   VAL A 406     2319   1934   2093    290   -211   -164       O  
ATOM   6155  CB  VAL A 406       1.040  46.179 -14.380  1.00 15.26           C  
ANISOU 6155  CB  VAL A 406     2151   1710   1937    310   -230   -128       C  
ATOM   6156  CG1 VAL A 406      -0.393  45.938 -13.961  1.00 19.14           C  
ANISOU 6156  CG1 VAL A 406     2616   2230   2428    358   -222   -152       C  
ATOM   6157  CG2 VAL A 406       1.134  46.412 -15.903  1.00 18.01           C  
ANISOU 6157  CG2 VAL A 406     2519   2029   2294    298   -244   -100       C  
ATOM   6158  H   VAL A 406       3.538  46.914 -13.764  1.00 17.72           H  
ATOM   6159  HA  VAL A 406       1.107  48.149 -13.799  1.00 17.25           H  
ATOM   6160  HB  VAL A 406       1.554  45.383 -14.172  1.00 18.31           H  
ATOM   6161 HG11 VAL A 406      -0.701  45.106 -14.353  1.00 22.97           H  
ATOM   6162 HG12 VAL A 406      -0.435  45.883 -12.993  1.00 22.97           H  
ATOM   6163 HG13 VAL A 406      -0.942  46.674 -14.274  1.00 22.97           H  
ATOM   6164 HG21 VAL A 406       0.751  45.648 -16.363  1.00 21.61           H  
ATOM   6165 HG22 VAL A 406       0.641  47.216 -16.131  1.00 21.61           H  
ATOM   6166 HG23 VAL A 406       2.066  46.514 -16.150  1.00 21.61           H  
ATOM   6167  N   GLU A 407       1.121  48.085 -11.319  1.00 14.54           N  
ANISOU 6167  N   GLU A 407     2105   1597   1823    343   -246   -213       N  
ATOM   6168  CA  GLU A 407       1.115  47.954  -9.863  1.00 16.42           C  
ANISOU 6168  CA  GLU A 407     2328   1869   2042    348   -233   -242       C  
ATOM   6169  C   GLU A 407       0.037  46.977  -9.405  1.00 20.05           C  
ANISOU 6169  C   GLU A 407     2736   2388   2495    378   -208   -250       C  
ATOM   6170  O   GLU A 407      -1.088  47.000  -9.905  1.00 18.84           O  
ANISOU 6170  O   GLU A 407     2571   2238   2350    417   -209   -257       O  
ATOM   6171  CB  GLU A 407       0.869  49.309  -9.197  1.00 20.00           C  
ANISOU 6171  CB  GLU A 407     2825   2283   2492    375   -254   -284       C  
ATOM   6172  CG  GLU A 407       1.977  50.312  -9.389  1.00 28.82           C  
ANISOU 6172  CG  GLU A 407     3997   3343   3611    338   -280   -279       C  
ATOM   6173  CD  GLU A 407       1.940  51.435  -8.364  1.00 75.58           C  
ANISOU 6173  CD  GLU A 407     9959   9235   9522    354   -295   -326       C  
ATOM   6174  OE1 GLU A 407       1.038  51.446  -7.498  1.00 53.16           O  
ANISOU 6174  OE1 GLU A 407     7102   6422   6672    399   -284   -364       O  
ATOM   6175  OE2 GLU A 407       2.831  52.307  -8.422  1.00 55.43           O  
ANISOU 6175  OE2 GLU A 407     7456   6634   6971    320   -318   -325       O  
ATOM   6176  H   GLU A 407       0.793  48.826 -11.609  1.00 17.45           H  
ATOM   6177  HA  GLU A 407       1.982  47.619  -9.584  1.00 19.70           H  
ATOM   6178  HB2 GLU A 407       0.059  49.693  -9.568  1.00 24.00           H  
ATOM   6179  HB3 GLU A 407       0.764  49.170  -8.243  1.00 24.00           H  
ATOM   6180  HG2 GLU A 407       2.831  49.859  -9.308  1.00 34.59           H  
ATOM   6181  HG3 GLU A 407       1.894  50.709 -10.271  1.00 34.59           H  
ATOM   6182  N   VAL A 408       0.379  46.124  -8.439  1.00 15.87           N  
ANISOU 6182  N   VAL A 408     2174   1907   1949    358   -188   -248       N  
ATOM   6183  CA  VAL A 408      -0.573  45.211  -7.811  1.00 14.09           C  
ANISOU 6183  CA  VAL A 408     1901   1740   1711    379   -164   -255       C  
ATOM   6184  C   VAL A 408      -0.395  45.373  -6.309  1.00 13.78           C  
ANISOU 6184  C   VAL A 408     1857   1731   1646    378   -156   -283       C  
ATOM   6185  O   VAL A 408       0.655  45.011  -5.763  1.00 16.92           O  
ANISOU 6185  O   VAL A 408     2254   2141   2034    339   -153   -268       O  
ATOM   6186  CB  VAL A 408      -0.365  43.745  -8.226  1.00 16.02           C  
ANISOU 6186  CB  VAL A 408     2108   2018   1960    351   -144   -216       C  
ATOM   6187  CG1 VAL A 408      -1.338  42.851  -7.468  1.00 18.51           C  
ANISOU 6187  CG1 VAL A 408     2379   2394   2261    365   -122   -222       C  
ATOM   6188  CG2 VAL A 408      -0.520  43.565  -9.742  1.00 16.64           C  
ANISOU 6188  CG2 VAL A 408     2192   2070   2061    350   -151   -191       C  
ATOM   6189  H   VAL A 408       1.177  46.057  -8.126  1.00 19.04           H  
ATOM   6190  HA  VAL A 408      -1.475  45.463  -8.062  1.00 16.90           H  
ATOM   6191  HB  VAL A 408       0.541  43.481  -7.999  1.00 19.22           H  
ATOM   6192 HG11 VAL A 408      -1.312  41.960  -7.850  1.00 22.21           H  
ATOM   6193 HG12 VAL A 408      -1.075  42.818  -6.534  1.00 22.21           H  
ATOM   6194 HG13 VAL A 408      -2.232  43.219  -7.546  1.00 22.21           H  
ATOM   6195 HG21 VAL A 408      -0.863  42.675  -9.921  1.00 19.97           H  
ATOM   6196 HG22 VAL A 408      -1.140  44.232 -10.077  1.00 19.97           H  
ATOM   6197 HG23 VAL A 408       0.346  43.677 -10.164  1.00 19.97           H  
ATOM   6198  N   ASN A 409      -1.402  45.928  -5.643  1.00 15.98           N  
ANISOU 6198  N   ASN A 409     2133   2026   1914    421   -155   -324       N  
ATOM   6199  CA  ASN A 409      -1.297  46.245  -4.231  1.00 19.74           C  
ANISOU 6199  CA  ASN A 409     2610   2530   2362    423   -149   -357       C  
ATOM   6200  C   ASN A 409      -2.329  45.505  -3.397  1.00 23.71           C  
ANISOU 6200  C   ASN A 409     3062   3104   2842    443   -124   -370       C  
ATOM   6201  O   ASN A 409      -3.377  45.072  -3.883  1.00 20.79           O  
ANISOU 6201  O   ASN A 409     2662   2758   2480    469   -114   -366       O  
ATOM   6202  CB  ASN A 409      -1.428  47.756  -4.023  1.00 24.06           C  
ANISOU 6202  CB  ASN A 409     3205   3028   2909    454   -171   -403       C  
ATOM   6203  CG  ASN A 409      -0.244  48.504  -4.576  1.00 29.08           C  
ANISOU 6203  CG  ASN A 409     3893   3598   3559    421   -197   -390       C  
ATOM   6204  OD1 ASN A 409       0.902  48.154  -4.288  1.00 23.78           O  
ANISOU 6204  OD1 ASN A 409     3224   2934   2880    371   -196   -368       O  
ATOM   6205  ND2 ASN A 409      -0.502  49.513  -5.403  1.00 30.48           N  
ANISOU 6205  ND2 ASN A 409     4112   3712   3757    446   -220   -400       N  
ATOM   6206  H   ASN A 409      -2.160  46.131  -5.996  1.00 19.18           H  
ATOM   6207  HA  ASN A 409      -0.434  45.945  -3.907  1.00 23.69           H  
ATOM   6208  HB2 ASN A 409      -2.226  48.072  -4.476  1.00 28.87           H  
ATOM   6209  HB3 ASN A 409      -1.489  47.943  -3.074  1.00 28.87           H  
ATOM   6210 HD21 ASN A 409       0.145  49.968  -5.741  1.00 36.58           H  
ATOM   6211 HD22 ASN A 409      -1.315  49.712  -5.599  1.00 36.58           H  
ATOM   6212  N   GLY A 410      -1.995  45.357  -2.116  1.00 21.86           N  
ANISOU 6212  N   GLY A 410     2818   2910   2577    427   -113   -385       N  
ATOM   6213  CA  GLY A 410      -2.881  44.731  -1.159  1.00 20.71           C  
ANISOU 6213  CA  GLY A 410     2627   2838   2403    441    -89   -398       C  
ATOM   6214  C   GLY A 410      -2.475  43.313  -0.819  1.00 15.78           C  
ANISOU 6214  C   GLY A 410     1967   2262   1769    396    -72   -353       C  
ATOM   6215  O   GLY A 410      -2.533  42.419  -1.668  1.00 18.78           O  
ANISOU 6215  O   GLY A 410     2328   2638   2168    382    -67   -314       O  
ATOM   6216  H   GLY A 410      -1.249  45.617  -1.778  1.00 26.23           H  
ATOM   6217  HA2 GLY A 410      -2.885  45.251  -0.340  1.00 24.85           H  
ATOM   6218  HA3 GLY A 410      -3.780  44.710  -1.523  1.00 24.85           H  
ATOM   6219  N   ALA A 411      -2.044  43.093   0.416  1.00 21.08           N  
ANISOU 6219  N   ALA A 411     2629   2974   2408    374    -63   -359       N  
ATOM   6220  CA  ALA A 411      -1.628  41.760   0.823  1.00 22.60           C  
ANISOU 6220  CA  ALA A 411     2790   3209   2589    334    -49   -314       C  
ATOM   6221  C   ALA A 411      -2.773  40.771   0.650  1.00 18.27           C  
ANISOU 6221  C   ALA A 411     2198   2706   2038    342    -29   -297       C  
ATOM   6222  O   ALA A 411      -3.889  41.009   1.118  1.00 21.44           O  
ANISOU 6222  O   ALA A 411     2577   3149   2420    371    -17   -328       O  
ATOM   6223  CB  ALA A 411      -1.168  41.766   2.279  1.00 25.14           C  
ANISOU 6223  CB  ALA A 411     3107   3577   2870    313    -44   -326       C  
ATOM   6224  H   ALA A 411      -1.983  43.691   1.031  1.00 25.30           H  
ATOM   6225  HA  ALA A 411      -0.884  41.480   0.268  1.00 27.12           H  
ATOM   6226  HB1 ALA A 411      -0.704  40.935   2.466  1.00 30.17           H  
ATOM   6227  HB2 ALA A 411      -0.570  42.517   2.418  1.00 30.17           H  
ATOM   6228  HB3 ALA A 411      -1.943  41.849   2.855  1.00 30.17           H  
ATOM   6229  N   ASP A 412      -2.479  39.652  -0.019  1.00 18.05           N  
ANISOU 6229  N   ASP A 412     2157   2671   2031    314    -26   -248       N  
ATOM   6230  CA  ASP A 412      -3.400  38.534  -0.230  1.00 17.69           C  
ANISOU 6230  CA  ASP A 412     2073   2663   1984    308     -9   -224       C  
ATOM   6231  C   ASP A 412      -4.593  38.900  -1.100  1.00 18.81           C  
ANISOU 6231  C   ASP A 412     2205   2799   2142    345     -8   -244       C  
ATOM   6232  O   ASP A 412      -5.579  38.161  -1.148  1.00 20.11           O  
ANISOU 6232  O   ASP A 412     2334   3006   2300    343      6   -234       O  
ATOM   6233  CB  ASP A 412      -3.854  37.947   1.111  1.00 19.51           C  
ANISOU 6233  CB  ASP A 412     2271   2969   2174    294      9   -223       C  
ATOM   6234  CG  ASP A 412      -2.700  37.325   1.872  1.00 23.97           C  
ANISOU 6234  CG  ASP A 412     2840   3542   2725    254      8   -191       C  
ATOM   6235  OD1 ASP A 412      -1.776  36.803   1.207  1.00 23.94           O  
ANISOU 6235  OD1 ASP A 412     2852   3497   2748    233     -1   -155       O  
ATOM   6236  OD2 ASP A 412      -2.685  37.393   3.116  1.00 27.10           O  
ANISOU 6236  OD2 ASP A 412     3226   3987   3083    245     14   -202       O  
ATOM   6237  H   ASP A 412      -1.709  39.514  -0.377  1.00 21.66           H  
ATOM   6238  HA  ASP A 412      -2.929  37.836  -0.711  1.00 21.22           H  
ATOM   6239  HB2 ASP A 412      -4.234  38.652   1.657  1.00 23.42           H  
ATOM   6240  HB3 ASP A 412      -4.518  37.258   0.950  1.00 23.42           H  
ATOM   6241  N   GLN A 413      -4.506  40.011  -1.825  1.00 18.79           N  
ANISOU 6241  N   GLN A 413     2235   2746   2161    374    -26   -269       N  
ATOM   6242  CA  GLN A 413      -5.513  40.328  -2.816  1.00 19.05           C  
ANISOU 6242  CA  GLN A 413     2260   2766   2212    408    -30   -280       C  
ATOM   6243  C   GLN A 413      -5.501  39.286  -3.926  1.00 16.21           C  
ANISOU 6243  C   GLN A 413     1891   2392   1876    383    -29   -237       C  
ATOM   6244  O   GLN A 413      -4.527  38.555  -4.125  1.00 20.67           O  
ANISOU 6244  O   GLN A 413     2466   2936   2451    346    -29   -202       O  
ATOM   6245  CB  GLN A 413      -5.262  41.699  -3.434  1.00 20.73           C  
ANISOU 6245  CB  GLN A 413     2516   2916   2444    441    -53   -308       C  
ATOM   6246  CG  GLN A 413      -5.859  42.848  -2.673  1.00 22.16           C  
ANISOU 6246  CG  GLN A 413     2704   3109   2607    486    -55   -361       C  
ATOM   6247  CD  GLN A 413      -7.372  42.799  -2.644  1.00 25.94           C  
ANISOU 6247  CD  GLN A 413     3141   3640   3076    526    -43   -382       C  
ATOM   6248  OE1 GLN A 413      -8.010  42.165  -3.487  1.00 29.42           O  
ANISOU 6248  OE1 GLN A 413     3556   4091   3531    525    -40   -359       O  
ATOM   6249  NE2 GLN A 413      -7.956  43.448  -1.648  1.00 29.31           N  
ANISOU 6249  NE2 GLN A 413     3557   4103   3476    561    -35   -428       N  
ATOM   6250  H   GLN A 413      -3.876  40.592  -1.760  1.00 22.55           H  
ATOM   6251  HA  GLN A 413      -6.382  40.338  -2.386  1.00 22.86           H  
ATOM   6252  HB2 GLN A 413      -4.304  41.846  -3.481  1.00 24.87           H  
ATOM   6253  HB3 GLN A 413      -5.643  41.710  -4.326  1.00 24.87           H  
ATOM   6254  HG2 GLN A 413      -5.540  42.821  -1.757  1.00 26.59           H  
ATOM   6255  HG3 GLN A 413      -5.593  43.680  -3.093  1.00 26.59           H  
ATOM   6256 HE21 GLN A 413      -7.477  43.864  -1.067  1.00 35.17           H  
ATOM   6257 HE22 GLN A 413      -8.813  43.454  -1.582  1.00 35.17           H  
ATOM   6258  N   TRP A 414      -6.602  39.237  -4.659  1.00 14.27           N  
ANISOU 6258  N   TRP A 414     1626   2158   1640    406    -28   -241       N  
ATOM   6259  CA  TRP A 414      -6.679  38.495  -5.904  1.00 13.65           C  
ANISOU 6259  CA  TRP A 414     1545   2058   1586    388    -31   -209       C  
ATOM   6260  C   TRP A 414      -6.520  39.481  -7.047  1.00 18.04           C  
ANISOU 6260  C   TRP A 414     2134   2555   2167    414    -53   -219       C  
ATOM   6261  O   TRP A 414      -7.170  40.531  -7.059  1.00 18.21           O  
ANISOU 6261  O   TRP A 414     2159   2572   2187    458    -63   -251       O  
ATOM   6262  CB  TRP A 414      -8.005  37.750  -6.026  1.00 14.79           C  
ANISOU 6262  CB  TRP A 414     1642   2256   1720    389    -18   -204       C  
ATOM   6263  CG  TRP A 414      -8.050  36.525  -5.176  1.00 18.77           C  
ANISOU 6263  CG  TRP A 414     2118   2808   2204    349      1   -180       C  
ATOM   6264  CD1 TRP A 414      -8.553  36.414  -3.911  1.00 25.65           C  
ANISOU 6264  CD1 TRP A 414     2961   3742   3042    349     17   -193       C  
ATOM   6265  CD2 TRP A 414      -7.554  35.229  -5.526  1.00 16.39           C  
ANISOU 6265  CD2 TRP A 414     1819   2495   1912    304      6   -138       C  
ATOM   6266  NE1 TRP A 414      -8.408  35.123  -3.456  1.00 26.31           N  
ANISOU 6266  NE1 TRP A 414     3028   3853   3115    302     30   -157       N  
ATOM   6267  CE2 TRP A 414      -7.800  34.377  -4.433  1.00 22.19           C  
ANISOU 6267  CE2 TRP A 414     2526   3283   2621    276     23   -124       C  
ATOM   6268  CE3 TRP A 414      -6.941  34.703  -6.666  1.00 21.64           C  
ANISOU 6268  CE3 TRP A 414     2506   3110   2606    284     -2   -112       C  
ATOM   6269  CZ2 TRP A 414      -7.451  33.031  -4.448  1.00 27.46           C  
ANISOU 6269  CZ2 TRP A 414     3193   3949   3293    231     30    -83       C  
ATOM   6270  CZ3 TRP A 414      -6.593  33.371  -6.676  1.00 25.72           C  
ANISOU 6270  CZ3 TRP A 414     3020   3626   3126    244      7    -76       C  
ATOM   6271  CH2 TRP A 414      -6.846  32.548  -5.576  1.00 19.58           C  
ANISOU 6271  CH2 TRP A 414     2220   2896   2325    218     21    -61       C  
ATOM   6272  H   TRP A 414      -7.334  39.637  -4.449  1.00 17.13           H  
ATOM   6273  HA  TRP A 414      -5.972  37.833  -5.943  1.00 16.39           H  
ATOM   6274  HB2 TRP A 414      -8.725  38.337  -5.747  1.00 17.74           H  
ATOM   6275  HB3 TRP A 414      -8.134  37.483  -6.949  1.00 17.74           H  
ATOM   6276  HD1 TRP A 414      -8.938  37.109  -3.427  1.00 30.78           H  
ATOM   6277  HE1 TRP A 414      -8.658  34.833  -2.686  1.00 31.57           H  
ATOM   6278  HE3 TRP A 414      -6.773  35.242  -7.404  1.00 25.97           H  
ATOM   6279  HZ2 TRP A 414      -7.623  32.480  -3.719  1.00 32.96           H  
ATOM   6280  HZ3 TRP A 414      -6.181  33.013  -7.429  1.00 30.86           H  
ATOM   6281  HH2 TRP A 414      -6.597  31.653  -5.611  1.00 23.50           H  
ATOM   6282  N   SER A 415      -5.660  39.141  -8.000  1.00 14.36           N  
ANISOU 6282  N   SER A 415     1691   2044   1722    388    -61   -190       N  
ATOM   6283  CA  SER A 415      -5.302  40.010  -9.118  1.00 14.41           C  
ANISOU 6283  CA  SER A 415     1734   1992   1750    402    -82   -191       C  
ATOM   6284  C   SER A 415      -5.778  39.318 -10.392  1.00 14.00           C  
ANISOU 6284  C   SER A 415     1670   1937   1713    392    -83   -168       C  
ATOM   6285  O   SER A 415      -5.288  38.236 -10.727  1.00 15.48           O  
ANISOU 6285  O   SER A 415     1852   2124   1905    356    -74   -139       O  
ATOM   6286  CB  SER A 415      -3.793  40.264  -9.129  1.00 17.54           C  
ANISOU 6286  CB  SER A 415     2166   2344   2153    375    -90   -178       C  
ATOM   6287  OG  SER A 415      -3.430  41.254 -10.080  1.00 16.72           O  
ANISOU 6287  OG  SER A 415     2099   2187   2066    386   -112   -181       O  
ATOM   6288  H   SER A 415      -5.256  38.383  -8.020  1.00 17.23           H  
ATOM   6289  HA  SER A 415      -5.747  40.869  -9.052  1.00 17.30           H  
ATOM   6290  HB2 SER A 415      -3.521  40.564  -8.248  1.00 21.04           H  
ATOM   6291  HB3 SER A 415      -3.339  39.437  -9.353  1.00 21.04           H  
ATOM   6292  HG  SER A 415      -3.837  41.971  -9.918  1.00 20.06           H  
ATOM   6293  N   TYR A 416      -6.743  39.922 -11.087  1.00 14.38           N  
ANISOU 6293  N   TYR A 416     1714   1983   1767    426    -96   -181       N  
ATOM   6294  CA  TYR A 416      -7.353  39.325 -12.268  1.00 15.00           C  
ANISOU 6294  CA  TYR A 416     1778   2066   1855    418    -99   -162       C  
ATOM   6295  C   TYR A 416      -6.941  40.058 -13.538  1.00 14.73           C  
ANISOU 6295  C   TYR A 416     1780   1978   1838    425   -121   -154       C  
ATOM   6296  O   TYR A 416      -6.857  41.288 -13.555  1.00 14.34           O  
ANISOU 6296  O   TYR A 416     1758   1897   1794    455   -139   -171       O  
ATOM   6297  CB  TYR A 416      -8.882  39.372 -12.196  1.00 17.15           C  
ANISOU 6297  CB  TYR A 416     2010   2388   2117    450    -97   -179       C  
ATOM   6298  CG  TYR A 416      -9.489  38.719 -10.984  1.00 16.47           C  
ANISOU 6298  CG  TYR A 416     1883   2367   2010    444    -75   -188       C  
ATOM   6299  CD1 TYR A 416      -9.542  39.382  -9.770  1.00 15.40           C  
ANISOU 6299  CD1 TYR A 416     1744   2250   1859    469    -70   -216       C  
ATOM   6300  CD2 TYR A 416     -10.036  37.444 -11.056  1.00 16.23           C  
ANISOU 6300  CD2 TYR A 416     1817   2378   1971    411    -60   -168       C  
ATOM   6301  CE1 TYR A 416     -10.111  38.797  -8.663  1.00 18.60           C  
ANISOU 6301  CE1 TYR A 416     2109   2718   2238    462    -49   -223       C  
ATOM   6302  CE2 TYR A 416     -10.612  36.849  -9.942  1.00 21.70           C  
ANISOU 6302  CE2 TYR A 416     2473   3132   2642    400    -41   -172       C  
ATOM   6303  CZ  TYR A 416     -10.637  37.532  -8.749  1.00 22.19           C  
ANISOU 6303  CZ  TYR A 416     2529   3216   2686    426    -34   -199       C  
ATOM   6304  OH  TYR A 416     -11.196  36.963  -7.629  1.00 21.43           O  
ANISOU 6304  OH  TYR A 416     2395   3186   2562    413    -14   -203       O  
ATOM   6305  H   TYR A 416      -7.064  40.693 -10.886  1.00 17.26           H  
ATOM   6306  HA  TYR A 416      -7.049  38.405 -12.315  1.00 18.00           H  
ATOM   6307  HB2 TYR A 416      -9.159  40.301 -12.195  1.00 20.58           H  
ATOM   6308  HB3 TYR A 416      -9.238  38.921 -12.978  1.00 20.58           H  
ATOM   6309  HD1 TYR A 416      -9.186  40.238  -9.702  1.00 18.48           H  
ATOM   6310  HD2 TYR A 416     -10.016  36.982 -11.863  1.00 19.47           H  
ATOM   6311  HE1 TYR A 416     -10.139  39.259  -7.856  1.00 22.31           H  
ATOM   6312  HE2 TYR A 416     -10.978  35.996 -10.003  1.00 26.04           H  
ATOM   6313  HH  TYR A 416     -10.970  37.393  -6.944  1.00 25.72           H  
ATOM   6314  N   TRP A 417      -6.777  39.301 -14.628  1.00 12.92           N  
ANISOU 6314  N   TRP A 417     1551   1740   1618    397   -121   -129       N  
ATOM   6315  CA  TRP A 417      -6.276  39.860 -15.883  1.00 12.94           C  
ANISOU 6315  CA  TRP A 417     1588   1696   1633    394   -140   -116       C  
ATOM   6316  C   TRP A 417      -6.920  39.174 -17.071  1.00 14.32           C  
ANISOU 6316  C   TRP A 417     1748   1884   1810    383   -142   -100       C  
ATOM   6317  O   TRP A 417      -6.806  37.958 -17.245  1.00 15.31           O  
ANISOU 6317  O   TRP A 417     1857   2027   1934    349   -126    -86       O  
ATOM   6318  CB  TRP A 417      -4.744  39.748 -15.957  1.00 14.37           C  
ANISOU 6318  CB  TRP A 417     1799   1841   1819    360   -136   -100       C  
ATOM   6319  CG  TRP A 417      -4.180  40.532 -14.852  1.00 15.38           C  
ANISOU 6319  CG  TRP A 417     1943   1957   1943    371   -138   -117       C  
ATOM   6320  CD1 TRP A 417      -3.781  40.063 -13.639  1.00 18.28           C  
ANISOU 6320  CD1 TRP A 417     2298   2348   2302    359   -122   -122       C  
ATOM   6321  CD2 TRP A 417      -4.042  41.956 -14.802  1.00 15.38           C  
ANISOU 6321  CD2 TRP A 417     1977   1920   1947    396   -160   -133       C  
ATOM   6322  NE1 TRP A 417      -3.387  41.105 -12.842  1.00 17.19           N  
ANISOU 6322  NE1 TRP A 417     2181   2192   2158    373   -131   -142       N  
ATOM   6323  CE2 TRP A 417      -3.538  42.279 -13.532  1.00 17.37           C  
ANISOU 6323  CE2 TRP A 417     2235   2175   2190    396   -155   -150       C  
ATOM   6324  CE3 TRP A 417      -4.301  42.989 -15.708  1.00 17.20           C  
ANISOU 6324  CE3 TRP A 417     2236   2114   2187    418   -186   -133       C  
ATOM   6325  CZ2 TRP A 417      -3.264  43.592 -13.150  1.00 17.19           C  
ANISOU 6325  CZ2 TRP A 417     2248   2116   2168    415   -173   -171       C  
ATOM   6326  CZ3 TRP A 417      -4.025  44.291 -15.327  1.00 23.67           C  
ANISOU 6326  CZ3 TRP A 417     3092   2894   3008    438   -205   -151       C  
ATOM   6327  CH2 TRP A 417      -3.508  44.580 -14.062  1.00 17.86           C  
ANISOU 6327  CH2 TRP A 417     2363   2158   2264    436   -198   -171       C  
ATOM   6328  H   TRP A 417      -6.951  38.459 -14.664  1.00 15.50           H  
ATOM   6329  HA  TRP A 417      -6.534  40.794 -15.923  1.00 15.53           H  
ATOM   6330  HB2 TRP A 417      -4.472  38.821 -15.864  1.00 17.24           H  
ATOM   6331  HB3 TRP A 417      -4.423  40.104 -16.800  1.00 17.24           H  
ATOM   6332  HD1 TRP A 417      -3.777  39.168 -13.388  1.00 21.94           H  
ATOM   6333  HE1 TRP A 417      -3.092  41.034 -12.037  1.00 20.63           H  
ATOM   6334  HE3 TRP A 417      -4.653  42.805 -16.549  1.00 20.65           H  
ATOM   6335  HZ2 TRP A 417      -2.928  43.788 -12.305  1.00 20.63           H  
ATOM   6336  HZ3 TRP A 417      -4.186  44.985 -15.924  1.00 28.41           H  
ATOM   6337  HH2 TRP A 417      -3.325  45.463 -13.836  1.00 21.43           H  
ATOM   6338  N   LEU A 418      -7.588  39.972 -17.886  1.00 13.62           N  
ANISOU 6338  N   LEU A 418     1664   1785   1724    410   -164   -103       N  
ATOM   6339  CA  LEU A 418      -7.993  39.562 -19.214  1.00 15.59           C  
ANISOU 6339  CA  LEU A 418     1910   2038   1974    397   -172    -86       C  
ATOM   6340  C   LEU A 418      -6.864  39.915 -20.168  1.00 13.63           C  
ANISOU 6340  C   LEU A 418     1704   1741   1733    376   -183    -68       C  
ATOM   6341  O   LEU A 418      -6.501  41.090 -20.306  1.00 14.05           O  
ANISOU 6341  O   LEU A 418     1789   1757   1791    394   -202    -69       O  
ATOM   6342  CB  LEU A 418      -9.288  40.250 -19.614  1.00 13.63           C  
ANISOU 6342  CB  LEU A 418     1645   1809   1725    439   -193    -95       C  
ATOM   6343  CG  LEU A 418      -9.692  40.105 -21.080  1.00 11.72           C  
ANISOU 6343  CG  LEU A 418     1405   1567   1482    430   -209    -77       C  
ATOM   6344  CD1 LEU A 418     -10.059  38.684 -21.428  1.00 16.06           C  
ANISOU 6344  CD1 LEU A 418     1924   2156   2024    391   -192    -68       C  
ATOM   6345  CD2 LEU A 418     -10.832  41.069 -21.360  1.00 16.20           C  
ANISOU 6345  CD2 LEU A 418     1960   2145   2049    481   -235    -85       C  
ATOM   6346  H   LEU A 418      -7.822  40.775 -17.685  1.00 16.34           H  
ATOM   6347  HA  LEU A 418      -8.152  38.605 -19.247  1.00 18.70           H  
ATOM   6348  HB2 LEU A 418     -10.007  39.879 -19.079  1.00 16.36           H  
ATOM   6349  HB3 LEU A 418      -9.196  41.199 -19.433  1.00 16.36           H  
ATOM   6350  HG  LEU A 418      -8.940  40.324 -21.654  1.00 14.07           H  
ATOM   6351 HD11 LEU A 418      -9.683  38.464 -22.295  1.00 19.28           H  
ATOM   6352 HD12 LEU A 418      -9.700  38.090 -20.751  1.00 19.28           H  
ATOM   6353 HD13 LEU A 418     -11.026  38.607 -21.458  1.00 19.28           H  
ATOM   6354 HD21 LEU A 418     -11.033  41.054 -22.309  1.00 19.44           H  
ATOM   6355 HD22 LEU A 418     -11.611  40.793 -20.852  1.00 19.44           H  
ATOM   6356 HD23 LEU A 418     -10.563  41.962 -21.094  1.00 19.44           H  
ATOM   6357  N   ILE A 419      -6.289  38.894 -20.792  1.00 12.88           N  
ANISOU 6357  N   ILE A 419     1610   1647   1637    336   -169    -52       N  
ATOM   6358  CA  ILE A 419      -5.229  39.062 -21.772  1.00 11.87           C  
ANISOU 6358  CA  ILE A 419     1515   1485   1511    311   -175    -34       C  
ATOM   6359  C   ILE A 419      -5.856  38.852 -23.139  1.00 11.34           C  
ANISOU 6359  C   ILE A 419     1444   1426   1437    304   -187    -23       C  
ATOM   6360  O   ILE A 419      -6.349  37.755 -23.438  1.00 14.00           O  
ANISOU 6360  O   ILE A 419     1758   1792   1769    286   -175    -22       O  
ATOM   6361  CB  ILE A 419      -4.071  38.076 -21.550  1.00 10.96           C  
ANISOU 6361  CB  ILE A 419     1401   1366   1396    275   -151    -26       C  
ATOM   6362  CG1 ILE A 419      -3.618  38.047 -20.084  1.00 15.72           C  
ANISOU 6362  CG1 ILE A 419     1998   1972   2002    280   -138    -36       C  
ATOM   6363  CG2 ILE A 419      -2.917  38.431 -22.508  1.00 16.18           C  
ANISOU 6363  CG2 ILE A 419     2094   1996   2058    253   -156    -10       C  
ATOM   6364  CD1 ILE A 419      -3.157  39.357 -19.520  1.00 18.85           C  
ANISOU 6364  CD1 ILE A 419     2418   2342   2401    298   -152    -44       C  
ATOM   6365  H   ILE A 419      -6.504  38.072 -20.657  1.00 15.46           H  
ATOM   6366  HA  ILE A 419      -4.869  39.960 -21.709  1.00 14.25           H  
ATOM   6367  HB  ILE A 419      -4.381  37.179 -21.749  1.00 13.15           H  
ATOM   6368 HG12 ILE A 419      -4.363  37.746 -19.541  1.00 18.86           H  
ATOM   6369 HG13 ILE A 419      -2.878  37.424 -20.007  1.00 18.86           H  
ATOM   6370 HG21 ILE A 419      -2.161  37.854 -22.319  1.00 19.42           H  
ATOM   6371 HG22 ILE A 419      -3.213  38.300 -23.422  1.00 19.42           H  
ATOM   6372 HG23 ILE A 419      -2.667  39.358 -22.371  1.00 19.42           H  
ATOM   6373 HD11 ILE A 419      -2.338  39.623 -19.966  1.00 22.62           H  
ATOM   6374 HD12 ILE A 419      -3.845  40.024 -19.667  1.00 22.62           H  
ATOM   6375 HD13 ILE A 419      -2.996  39.252 -18.569  1.00 22.62           H  
ATOM   6376  N   GLU A 420      -5.819  39.887 -23.971  1.00 13.31           N  
ANISOU 6376  N   GLU A 420     1721   1651   1687    315   -212    -14       N  
ATOM   6377  CA  GLU A 420      -6.428  39.846 -25.292  1.00 17.05           C  
ANISOU 6377  CA  GLU A 420     2194   2134   2152    311   -227     -1       C  
ATOM   6378  C   GLU A 420      -5.349  39.801 -26.362  1.00 14.68           C  
ANISOU 6378  C   GLU A 420     1922   1811   1844    275   -227     18       C  
ATOM   6379  O   GLU A 420      -4.398  40.591 -26.308  1.00 15.02           O  
ANISOU 6379  O   GLU A 420     1996   1821   1891    270   -234     26       O  
ATOM   6380  CB  GLU A 420      -7.314  41.065 -25.548  1.00 15.63           C  
ANISOU 6380  CB  GLU A 420     2020   1946   1973    353   -260      0       C  
ATOM   6381  CG  GLU A 420      -8.373  41.317 -24.499  1.00 16.63           C  
ANISOU 6381  CG  GLU A 420     2118   2097   2106    396   -261    -22       C  
ATOM   6382  CD  GLU A 420      -9.345  42.407 -24.924  1.00 21.79           C  
ANISOU 6382  CD  GLU A 420     2773   2746   2760    443   -294    -21       C  
ATOM   6383  OE1 GLU A 420      -8.999  43.612 -24.837  1.00 19.33           O  
ANISOU 6383  OE1 GLU A 420     2498   2389   2457    467   -315    -19       O  
ATOM   6384  OE2 GLU A 420     -10.450  42.047 -25.386  1.00 19.97           O  
ANISOU 6384  OE2 GLU A 420     2509   2556   2523    453   -301    -20       O  
ATOM   6385  H   GLU A 420      -5.440  40.636 -23.786  1.00 15.98           H  
ATOM   6386  HA  GLU A 420      -6.969  39.043 -25.346  1.00 20.47           H  
ATOM   6387  HB2 GLU A 420      -6.749  41.853 -25.586  1.00 18.76           H  
ATOM   6388  HB3 GLU A 420      -7.768  40.942 -26.396  1.00 18.76           H  
ATOM   6389  HG2 GLU A 420      -8.877  40.501 -24.352  1.00 19.96           H  
ATOM   6390  HG3 GLU A 420      -7.946  41.595 -23.674  1.00 19.96           H  
ATOM   6391  N   ASN A 421      -5.527  38.927 -27.357  1.00 12.58           N  
ANISOU 6391  N   ASN A 421     1647   1566   1566    249   -221     24       N  
ATOM   6392  CA  ASN A 421      -4.553  38.777 -28.434  1.00 12.69           C  
ANISOU 6392  CA  ASN A 421     1685   1568   1570    215   -218     39       C  
ATOM   6393  C   ASN A 421      -4.937  39.665 -29.611  1.00 13.42           C  
ANISOU 6393  C   ASN A 421     1796   1654   1650    219   -248     57       C  
ATOM   6394  O   ASN A 421      -5.614  39.246 -30.554  1.00 14.60           O  
ANISOU 6394  O   ASN A 421     1936   1828   1785    210   -255     61       O  
ATOM   6395  CB  ASN A 421      -4.428  37.325 -28.873  1.00 13.38           C  
ANISOU 6395  CB  ASN A 421     1757   1679   1650    184   -193     32       C  
ATOM   6396  CG  ASN A 421      -3.165  37.075 -29.653  1.00 12.71           C  
ANISOU 6396  CG  ASN A 421     1693   1582   1554    152   -180     41       C  
ATOM   6397  OD1 ASN A 421      -2.456  38.007 -30.035  1.00 14.78           O  
ANISOU 6397  OD1 ASN A 421     1980   1825   1812    148   -192     56       O  
ATOM   6398  ND2 ASN A 421      -2.859  35.811 -29.879  1.00 16.28           N  
ANISOU 6398  ND2 ASN A 421     2136   2047   2003    130   -156     31       N  
ATOM   6399  H   ASN A 421      -6.210  38.408 -27.427  1.00 15.09           H  
ATOM   6400  HA  ASN A 421      -3.698  39.081 -28.091  1.00 15.23           H  
ATOM   6401  HB2 ASN A 421      -4.418  36.755 -28.089  1.00 16.06           H  
ATOM   6402  HB3 ASN A 421      -5.183  37.097 -29.438  1.00 16.06           H  
ATOM   6403 HD21 ASN A 421      -2.148  35.612 -30.320  1.00 19.54           H  
ATOM   6404 HD22 ASN A 421      -3.372  35.186 -29.585  1.00 19.54           H  
ATOM   6405  N   ASP A 422      -4.498  40.918 -29.530  1.00 12.26           N  
ANISOU 6405  N   ASP A 422     1679   1472   1508    231   -268     69       N  
ATOM   6406  CA  ASP A 422      -4.550  41.868 -30.636  1.00 12.27           C  
ANISOU 6406  CA  ASP A 422     1708   1457   1497    229   -298     93       C  
ATOM   6407  C   ASP A 422      -5.925  41.920 -31.307  1.00 16.46           C  
ANISOU 6407  C   ASP A 422     2222   2013   2020    251   -321     97       C  
ATOM   6408  O   ASP A 422      -6.042  41.693 -32.518  1.00 15.38           O  
ANISOU 6408  O   ASP A 422     2088   1892   1862    228   -329    112       O  
ATOM   6409  CB  ASP A 422      -3.456  41.540 -31.645  1.00 12.13           C  
ANISOU 6409  CB  ASP A 422     1708   1441   1461    182   -286    109       C  
ATOM   6410  CG  ASP A 422      -2.898  42.781 -32.362  1.00 12.68           C  
ANISOU 6410  CG  ASP A 422     1818   1479   1521    170   -313    137       C  
ATOM   6411  OD1 ASP A 422      -3.520  43.869 -32.299  1.00 16.30           O  
ANISOU 6411  OD1 ASP A 422     2294   1912   1986    201   -345    148       O  
ATOM   6412  OD2 ASP A 422      -1.823  42.670 -32.998  1.00 15.90           O  
ANISOU 6412  OD2 ASP A 422     2241   1889   1914    131   -302    150       O  
ATOM   6413  H   ASP A 422      -4.153  41.251 -28.817  1.00 14.71           H  
ATOM   6414  HA  ASP A 422      -4.390  42.760 -30.290  1.00 14.72           H  
ATOM   6415  HB2 ASP A 422      -2.721  41.109 -31.182  1.00 14.56           H  
ATOM   6416  HB3 ASP A 422      -3.819  40.945 -32.319  1.00 14.56           H  
ATOM   6417  N   PRO A 423      -6.977  42.252 -30.560  1.00 14.65           N  
ANISOU 6417  N   PRO A 423     1973   1790   1804    295   -333     84       N  
ATOM   6418  CA  PRO A 423      -8.316  42.306 -31.160  1.00 13.14           C  
ANISOU 6418  CA  PRO A 423     1759   1629   1604    318   -356     88       C  
ATOM   6419  C   PRO A 423      -8.345  43.170 -32.407  1.00 16.85           C  
ANISOU 6419  C   PRO A 423     2258   2082   2060    316   -390    119       C  
ATOM   6420  O   PRO A 423      -7.876  44.312 -32.409  1.00 17.90           O  
ANISOU 6420  O   PRO A 423     2430   2171   2200    328   -411    134       O  
ATOM   6421  CB  PRO A 423      -9.184  42.914 -30.051  1.00 20.04           C  
ANISOU 6421  CB  PRO A 423     2616   2503   2497    374   -366     71       C  
ATOM   6422  CG  PRO A 423      -8.476  42.644 -28.816  1.00 20.99           C  
ANISOU 6422  CG  PRO A 423     2735   2609   2630    370   -338     51       C  
ATOM   6423  CD  PRO A 423      -7.000  42.660 -29.144  1.00 15.60           C  
ANISOU 6423  CD  PRO A 423     2090   1894   1944    327   -327     64       C  
ATOM   6424  HA  PRO A 423      -8.619  41.410 -31.372  1.00 15.77           H  
ATOM   6425  HB2 PRO A 423      -9.278  43.869 -30.193  1.00 24.05           H  
ATOM   6426  HB3 PRO A 423     -10.057  42.492 -30.049  1.00 24.05           H  
ATOM   6427  HG2 PRO A 423      -8.688  43.332 -28.165  1.00 25.18           H  
ATOM   6428  HG3 PRO A 423      -8.739  41.774 -28.477  1.00 25.18           H  
ATOM   6429  HD2 PRO A 423      -6.629  43.550 -29.034  1.00 18.72           H  
ATOM   6430  HD3 PRO A 423      -6.514  42.028 -28.592  1.00 18.72           H  
ATOM   6431  N   GLY A 424      -8.912  42.613 -33.472  1.00 16.40           N  
ANISOU 6431  N   GLY A 424     2186   2063   1983    298   -397    128       N  
ATOM   6432  CA  GLY A 424      -9.089  43.319 -34.718  1.00 20.19           C  
ANISOU 6432  CA  GLY A 424     2689   2538   2445    294   -431    159       C  
ATOM   6433  C   GLY A 424      -7.901  43.285 -35.647  1.00 18.74           C  
ANISOU 6433  C   GLY A 424     2539   2340   2241    243   -424    179       C  
ATOM   6434  O   GLY A 424      -8.006  43.790 -36.772  1.00 20.50           O  
ANISOU 6434  O   GLY A 424     2781   2564   2444    232   -451    208       O  
ATOM   6435  H   GLY A 424      -9.207  41.805 -33.490  1.00 19.68           H  
ATOM   6436  HA2 GLY A 424      -9.843  42.931 -35.189  1.00 24.23           H  
ATOM   6437  HA3 GLY A 424      -9.283  44.249 -34.522  1.00 24.23           H  
ATOM   6438  N   ALA A 425      -6.781  42.710 -35.214  1.00 14.99           N  
ANISOU 6438  N   ALA A 425     2070   1856   1770    212   -390    166       N  
ATOM   6439  CA  ALA A 425      -5.585  42.682 -36.035  1.00 14.01           C  
ANISOU 6439  CA  ALA A 425     1974   1724   1626    165   -380    183       C  
ATOM   6440  C   ALA A 425      -5.778  41.746 -37.224  1.00 13.14           C  
ANISOU 6440  C   ALA A 425     1850   1657   1484    130   -372    183       C  
ATOM   6441  O   ALA A 425      -6.541  40.781 -37.154  1.00 15.81           O  
ANISOU 6441  O   ALA A 425     2156   2030   1822    132   -361    162       O  
ATOM   6442  CB  ALA A 425      -4.380  42.221 -35.219  1.00 17.17           C  
ANISOU 6442  CB  ALA A 425     2376   2110   2037    146   -344    166       C  
ATOM   6443  H   ALA A 425      -6.690  42.329 -34.448  1.00 17.99           H  
ATOM   6444  HA  ALA A 425      -5.406  43.575 -36.367  1.00 16.82           H  
ATOM   6445  HB1 ALA A 425      -3.601  42.190 -35.796  1.00 20.60           H  
ATOM   6446  HB2 ALA A 425      -4.230  42.849 -34.495  1.00 20.60           H  
ATOM   6447  HB3 ALA A 425      -4.561  41.338 -34.859  1.00 20.60           H  
ATOM   6448  N   PRO A 426      -5.088  42.008 -38.327  1.00 17.85           N  
ANISOU 6448  N   PRO A 426     2472   2257   2054     94   -377    207       N  
ATOM   6449  CA  PRO A 426      -5.192  41.095 -39.477  1.00 16.61           C  
ANISOU 6449  CA  PRO A 426     2304   2143   1863     58   -367    203       C  
ATOM   6450  C   PRO A 426      -4.523  39.742 -39.246  1.00 16.21           C  
ANISOU 6450  C   PRO A 426     2236   2110   1812     33   -322    170       C  
ATOM   6451  O   PRO A 426      -5.040  38.726 -39.731  1.00 17.61           O  
ANISOU 6451  O   PRO A 426     2395   2321   1975     19   -312    152       O  
ATOM   6452  CB  PRO A 426      -4.521  41.888 -40.608  1.00 14.13           C  
ANISOU 6452  CB  PRO A 426     2024   1825   1519     27   -385    238       C  
ATOM   6453  CG  PRO A 426      -3.571  42.834 -39.896  1.00 16.13           C  
ANISOU 6453  CG  PRO A 426     2305   2032   1793     31   -386    252       C  
ATOM   6454  CD  PRO A 426      -4.250  43.191 -38.600  1.00 17.59           C  
ANISOU 6454  CD  PRO A 426     2479   2188   2016     82   -395    238       C  
ATOM   6455  HA  PRO A 426      -6.123  40.944 -39.702  1.00 19.93           H  
ATOM   6456  HB2 PRO A 426      -4.039  41.286 -41.196  1.00 16.95           H  
ATOM   6457  HB3 PRO A 426      -5.190  42.379 -41.111  1.00 16.95           H  
ATOM   6458  HG2 PRO A 426      -2.726  42.387 -39.731  1.00 19.36           H  
ATOM   6459  HG3 PRO A 426      -3.427  43.625 -40.439  1.00 19.36           H  
ATOM   6460  HD2 PRO A 426      -3.599  43.324 -37.893  1.00 21.11           H  
ATOM   6461  HD3 PRO A 426      -4.796  43.986 -38.702  1.00 21.11           H  
ATOM   6462  N   PHE A 427      -3.414  39.694 -38.502  1.00 14.85           N  
ANISOU 6462  N   PHE A 427     2071   1914   1656     28   -296    162       N  
ATOM   6463  CA  PHE A 427      -2.644  38.474 -38.277  1.00 12.41           C  
ANISOU 6463  CA  PHE A 427     1750   1618   1348      9   -255    134       C  
ATOM   6464  C   PHE A 427      -2.232  38.418 -36.818  1.00 13.55           C  
ANISOU 6464  C   PHE A 427     1886   1735   1527     31   -238    121       C  
ATOM   6465  O   PHE A 427      -1.721  39.408 -36.288  1.00 15.86           O  
ANISOU 6465  O   PHE A 427     2195   2000   1832     41   -248    136       O  
ATOM   6466  CB  PHE A 427      -1.394  38.441 -39.170  1.00 16.23           C  
ANISOU 6466  CB  PHE A 427     2250   2112   1804    -30   -238    143       C  
ATOM   6467  CG  PHE A 427      -1.709  38.548 -40.625  1.00 15.71           C  
ANISOU 6467  CG  PHE A 427     2195   2076   1699    -56   -254    158       C  
ATOM   6468  CD1 PHE A 427      -2.111  37.432 -41.333  1.00 16.39           C  
ANISOU 6468  CD1 PHE A 427     2267   2196   1764    -72   -240    135       C  
ATOM   6469  CD2 PHE A 427      -1.641  39.767 -41.280  1.00 15.06           C  
ANISOU 6469  CD2 PHE A 427     2136   1986   1598    -65   -285    196       C  
ATOM   6470  CE1 PHE A 427      -2.429  37.522 -42.675  1.00 15.96           C  
ANISOU 6470  CE1 PHE A 427     2221   2173   1669    -98   -256    148       C  
ATOM   6471  CE2 PHE A 427      -1.972  39.875 -42.620  1.00 16.95           C  
ANISOU 6471  CE2 PHE A 427     2386   2257   1799    -90   -303    213       C  
ATOM   6472  CZ  PHE A 427      -2.357  38.744 -43.325  1.00 14.94           C  
ANISOU 6472  CZ  PHE A 427     2114   2041   1520   -107   -287    188       C  
ATOM   6473  H   PHE A 427      -3.079  40.380 -38.106  1.00 17.82           H  
ATOM   6474  HA  PHE A 427      -3.193  37.699 -38.477  1.00 14.89           H  
ATOM   6475  HB2 PHE A 427      -0.819  39.186 -38.933  1.00 19.47           H  
ATOM   6476  HB3 PHE A 427      -0.927  37.603 -39.026  1.00 19.47           H  
ATOM   6477  HD1 PHE A 427      -2.169  36.611 -40.902  1.00 19.67           H  
ATOM   6478  HD2 PHE A 427      -1.368  40.524 -40.814  1.00 18.07           H  
ATOM   6479  HE1 PHE A 427      -2.691  36.762 -43.142  1.00 19.15           H  
ATOM   6480  HE2 PHE A 427      -1.937  40.701 -43.045  1.00 20.34           H  
ATOM   6481  HZ  PHE A 427      -2.566  38.805 -44.230  1.00 17.92           H  
ATOM   6482  N   THR A 428      -2.445  37.270 -36.174  1.00 13.89           N  
ANISOU 6482  N   THR A 428     1906   1787   1584     37   -213     93       N  
ATOM   6483  CA  THR A 428      -2.000  37.066 -34.803  1.00 11.46           C  
ANISOU 6483  CA  THR A 428     1589   1460   1306     55   -195     80       C  
ATOM   6484  C   THR A 428      -1.330  35.700 -34.673  1.00 12.47           C  
ANISOU 6484  C   THR A 428     1705   1597   1435     39   -158     58       C  
ATOM   6485  O   THR A 428      -1.448  34.838 -35.549  1.00 16.00           O  
ANISOU 6485  O   THR A 428     2151   2065   1864     19   -148     46       O  
ATOM   6486  CB  THR A 428      -3.161  37.179 -33.781  1.00 12.91           C  
ANISOU 6486  CB  THR A 428     1754   1640   1512     89   -208     72       C  
ATOM   6487  OG1 THR A 428      -4.081  36.093 -33.943  1.00 15.71           O  
ANISOU 6487  OG1 THR A 428     2086   2020   1862     84   -201     55       O  
ATOM   6488  CG2 THR A 428      -3.904  38.503 -33.949  1.00 13.74           C  
ANISOU 6488  CG2 THR A 428     1869   1734   1616    112   -245     92       C  
ATOM   6489  H   THR A 428      -2.848  36.592 -36.518  1.00 16.66           H  
ATOM   6490  HA  THR A 428      -1.347  37.750 -34.587  1.00 13.76           H  
ATOM   6491  HB  THR A 428      -2.790  37.145 -32.885  1.00 15.49           H  
ATOM   6492  HG1 THR A 428      -3.690  35.362 -33.805  1.00 18.85           H  
ATOM   6493 HG21 THR A 428      -4.570  38.600 -33.251  1.00 16.48           H  
ATOM   6494 HG22 THR A 428      -3.279  39.243 -33.894  1.00 16.48           H  
ATOM   6495 HG23 THR A 428      -4.346  38.527 -34.812  1.00 16.48           H  
ATOM   6496  N   LEU A 429      -0.613  35.525 -33.572  1.00 13.79           N  
ANISOU 6496  N   LEU A 429     1867   1748   1623     49   -140     51       N  
ATOM   6497  CA  LEU A 429       0.117  34.301 -33.290  1.00 11.16           C  
ANISOU 6497  CA  LEU A 429     1525   1418   1297     42   -108     32       C  
ATOM   6498  C   LEU A 429      -0.243  33.789 -31.905  1.00 14.14           C  
ANISOU 6498  C   LEU A 429     1887   1786   1702     62    -99     22       C  
ATOM   6499  O   LEU A 429      -0.562  34.580 -31.014  1.00 14.00           O  
ANISOU 6499  O   LEU A 429     1865   1756   1697     82   -114     29       O  
ATOM   6500  CB  LEU A 429       1.631  34.536 -33.343  1.00 14.18           C  
ANISOU 6500  CB  LEU A 429     1916   1798   1676     30    -91     39       C  
ATOM   6501  CG  LEU A 429       2.221  34.943 -34.693  1.00 14.73           C  
ANISOU 6501  CG  LEU A 429     1999   1883   1714      4    -93     51       C  
ATOM   6502  CD1 LEU A 429       3.703  35.225 -34.522  1.00 18.66           C  
ANISOU 6502  CD1 LEU A 429     2498   2383   2210     -7    -76     59       C  
ATOM   6503  CD2 LEU A 429       1.951  33.834 -35.699  1.00 17.37           C  
ANISOU 6503  CD2 LEU A 429     2331   2240   2030    -10    -78     31       C  
ATOM   6504  H   LEU A 429      -0.534  36.120 -32.956  1.00 16.54           H  
ATOM   6505  HA  LEU A 429      -0.122  33.628 -33.946  1.00 13.39           H  
ATOM   6506  HB2 LEU A 429       1.846  35.244 -32.715  1.00 17.02           H  
ATOM   6507  HB3 LEU A 429       2.071  33.713 -33.079  1.00 17.02           H  
ATOM   6508  HG  LEU A 429       1.813  35.754 -35.037  1.00 17.67           H  
ATOM   6509 HD11 LEU A 429       4.009  35.772 -35.263  1.00 22.39           H  
ATOM   6510 HD12 LEU A 429       3.841  35.696 -33.685  1.00 22.39           H  
ATOM   6511 HD13 LEU A 429       4.185  34.383 -34.511  1.00 22.39           H  
ATOM   6512 HD21 LEU A 429       2.433  34.026 -36.518  1.00 20.85           H  
ATOM   6513 HD22 LEU A 429       2.254  32.991 -35.327  1.00 20.85           H  
ATOM   6514 HD23 LEU A 429       0.999  33.794 -35.877  1.00 20.85           H  
ATOM   6515  N   PRO A 430      -0.170  32.474 -31.687  1.00 13.52           N  
ANISOU 6515  N   PRO A 430     1798   1709   1630     58    -77      4       N  
ATOM   6516  CA  PRO A 430      -0.239  31.957 -30.311  1.00 13.39           C  
ANISOU 6516  CA  PRO A 430     1768   1682   1638     73    -66     -2       C  
ATOM   6517  C   PRO A 430       0.941  32.455 -29.491  1.00 12.48           C  
ANISOU 6517  C   PRO A 430     1653   1554   1533     83    -58      7       C  
ATOM   6518  O   PRO A 430       2.056  32.580 -30.000  1.00 13.97           O  
ANISOU 6518  O   PRO A 430     1850   1744   1713     73    -48     11       O  
ATOM   6519  CB  PRO A 430      -0.180  30.434 -30.494  1.00 14.41           C  
ANISOU 6519  CB  PRO A 430     1896   1812   1769     62    -45    -20       C  
ATOM   6520  CG  PRO A 430      -0.573  30.193 -31.933  1.00 14.83           C  
ANISOU 6520  CG  PRO A 430     1958   1878   1797     42    -49    -28       C  
ATOM   6521  CD  PRO A 430      -0.059  31.393 -32.685  1.00 16.86           C  
ANISOU 6521  CD  PRO A 430     2226   2142   2037     38    -61    -12       C  
ATOM   6522  HA  PRO A 430      -1.076  32.205 -29.889  1.00 16.07           H  
ATOM   6523  HB2 PRO A 430       0.721  30.117 -30.324  1.00 17.30           H  
ATOM   6524  HB3 PRO A 430      -0.804  30.005 -29.888  1.00 17.30           H  
ATOM   6525  HG2 PRO A 430      -0.159  29.377 -32.256  1.00 17.79           H  
ATOM   6526  HG3 PRO A 430      -1.538  30.125 -32.005  1.00 17.79           H  
ATOM   6527  HD2 PRO A 430       0.863  31.264 -32.957  1.00 20.23           H  
ATOM   6528  HD3 PRO A 430      -0.611  31.578 -33.462  1.00 20.23           H  
ATOM   6529  N   HIS A 431       0.707  32.715 -28.205  1.00 12.74           N  
ANISOU 6529  N   HIS A 431     1677   1580   1583    100    -62      9       N  
ATOM   6530  CA  HIS A 431       1.789  33.163 -27.337  1.00 11.14           C  
ANISOU 6530  CA  HIS A 431     1474   1368   1390    106    -56     17       C  
ATOM   6531  C   HIS A 431       1.820  32.357 -26.045  1.00 13.34           C  
ANISOU 6531  C   HIS A 431     1738   1646   1686    117    -43     12       C  
ATOM   6532  O   HIS A 431       0.811  32.313 -25.321  1.00 13.82           O  
ANISOU 6532  O   HIS A 431     1789   1710   1753    127    -50      8       O  
ATOM   6533  CB  HIS A 431       1.651  34.654 -26.988  1.00 12.36           C  
ANISOU 6533  CB  HIS A 431     1637   1514   1543    115    -80     27       C  
ATOM   6534  CG  HIS A 431       1.687  35.561 -28.175  1.00 12.29           C  
ANISOU 6534  CG  HIS A 431     1648   1504   1519    104    -96     38       C  
ATOM   6535  ND1 HIS A 431       2.861  35.919 -28.802  1.00 12.42           N  
ANISOU 6535  ND1 HIS A 431     1675   1519   1523     84    -92     49       N  
ATOM   6536  CD2 HIS A 431       0.694  36.186 -28.848  1.00 12.92           C  
ANISOU 6536  CD2 HIS A 431     1736   1584   1590    108   -119     43       C  
ATOM   6537  CE1 HIS A 431       2.588  36.738 -29.802  1.00 13.44           C  
ANISOU 6537  CE1 HIS A 431     1822   1648   1638     74   -111     61       C  
ATOM   6538  NE2 HIS A 431       1.279  36.898 -29.863  1.00 12.16           N  
ANISOU 6538  NE2 HIS A 431     1659   1485   1477     90   -129     58       N  
ATOM   6539  H   HIS A 431      -0.059  32.639 -27.822  1.00 15.28           H  
ATOM   6540  HA  HIS A 431       2.619  33.011 -27.816  1.00 13.37           H  
ATOM   6541  HB2 HIS A 431       0.803  34.790 -26.537  1.00 14.83           H  
ATOM   6542  HB3 HIS A 431       2.383  34.905 -26.402  1.00 14.83           H  
ATOM   6543  HD2 HIS A 431      -0.216  36.142 -28.657  1.00 15.50           H  
ATOM   6544  HE1 HIS A 431       3.212  37.134 -30.366  1.00 16.13           H  
ATOM   6545  HE2 HIS A 431       0.861  37.372 -30.447  1.00 14.60           H  
ATOM   6546  N   PRO A 432       2.966  31.754 -25.689  1.00 11.03           N  
ANISOU 6546  N   PRO A 432     1441   1349   1399    116    -24     14       N  
ATOM   6547  CA  PRO A 432       3.089  31.129 -24.364  1.00 12.56           C  
ANISOU 6547  CA  PRO A 432     1623   1542   1609    126    -15     15       C  
ATOM   6548  C   PRO A 432       3.388  32.143 -23.270  1.00 14.03           C  
ANISOU 6548  C   PRO A 432     1805   1728   1798    135    -26     22       C  
ATOM   6549  O   PRO A 432       4.532  32.587 -23.120  1.00 13.68           O  
ANISOU 6549  O   PRO A 432     1762   1684   1752    132    -23     30       O  
ATOM   6550  CB  PRO A 432       4.253  30.150 -24.551  1.00 11.07           C  
ANISOU 6550  CB  PRO A 432     1432   1349   1424    125      6     14       C  
ATOM   6551  CG  PRO A 432       5.147  30.847 -25.547  1.00 10.01           C  
ANISOU 6551  CG  PRO A 432     1304   1222   1276    116      6     17       C  
ATOM   6552  CD  PRO A 432       4.187  31.559 -26.504  1.00 12.72           C  
ANISOU 6552  CD  PRO A 432     1660   1567   1606    106    -10     15       C  
ATOM   6553  HA  PRO A 432       2.282  30.639 -24.141  1.00 15.08           H  
ATOM   6554  HB2 PRO A 432       4.710  30.007 -23.708  1.00 13.28           H  
ATOM   6555  HB3 PRO A 432       3.929  29.305 -24.900  1.00 13.28           H  
ATOM   6556  HG2 PRO A 432       5.718  31.484 -25.090  1.00 12.01           H  
ATOM   6557  HG3 PRO A 432       5.688  30.195 -26.019  1.00 12.01           H  
ATOM   6558  HD2 PRO A 432       4.553  32.412 -26.786  1.00 15.27           H  
ATOM   6559  HD3 PRO A 432       4.000  31.006 -27.278  1.00 15.27           H  
ATOM   6560  N   MET A 433       2.368  32.520 -22.503  1.00 13.62           N  
ANISOU 6560  N   MET A 433     1748   1680   1748    145    -37     19       N  
ATOM   6561  CA  MET A 433       2.499  33.571 -21.502  1.00 10.61           C  
ANISOU 6561  CA  MET A 433     1366   1297   1367    155    -49     21       C  
ATOM   6562  C   MET A 433       2.956  32.978 -20.174  1.00 13.16           C  
ANISOU 6562  C   MET A 433     1676   1628   1697    159    -37     24       C  
ATOM   6563  O   MET A 433       2.426  31.958 -19.719  1.00 13.39           O  
ANISOU 6563  O   MET A 433     1693   1664   1730    160    -28     24       O  
ATOM   6564  CB  MET A 433       1.171  34.309 -21.330  1.00 12.42           C  
ANISOU 6564  CB  MET A 433     1596   1530   1594    169    -66     12       C  
ATOM   6565  CG  MET A 433       0.647  34.977 -22.598  1.00 16.61           C  
ANISOU 6565  CG  MET A 433     2139   2054   2116    168    -81     12       C  
ATOM   6566  SD  MET A 433       1.769  36.165 -23.361  1.00 17.36           S  
ANISOU 6566  SD  MET A 433     2261   2130   2205    156    -94     24       S  
ATOM   6567  CE  MET A 433       1.964  37.394 -22.061  1.00 16.77           C  
ANISOU 6567  CE  MET A 433     2194   2043   2134    171   -108     20       C  
ATOM   6568  H   MET A 433       1.581  32.175 -22.546  1.00 16.35           H  
ATOM   6569  HA  MET A 433       3.164  34.211 -21.799  1.00 12.73           H  
ATOM   6570  HB2 MET A 433       0.500  33.673 -21.036  1.00 14.91           H  
ATOM   6571  HB3 MET A 433       1.287  35.002 -20.661  1.00 14.91           H  
ATOM   6572  HG2 MET A 433       0.465  34.287 -23.255  1.00 19.93           H  
ATOM   6573  HG3 MET A 433      -0.171  35.451 -22.379  1.00 19.93           H  
ATOM   6574  HE1 MET A 433       2.536  38.108 -22.385  1.00 20.12           H  
ATOM   6575  HE2 MET A 433       1.092  37.750 -21.830  1.00 20.12           H  
ATOM   6576  HE3 MET A 433       2.366  36.973 -21.286  1.00 20.12           H  
ATOM   6577  N   HIS A 434       3.932  33.638 -19.553  1.00 12.72           N  
ANISOU 6577  N   HIS A 434     1622   1571   1640    158    -41     30       N  
ATOM   6578  CA  HIS A 434       4.631  33.127 -18.385  1.00 14.40           C  
ANISOU 6578  CA  HIS A 434     1822   1793   1857    159    -32     37       C  
ATOM   6579  C   HIS A 434       4.706  34.214 -17.324  1.00 12.95           C  
ANISOU 6579  C   HIS A 434     1640   1613   1666    163    -45     33       C  
ATOM   6580  O   HIS A 434       5.108  35.343 -17.622  1.00 12.60           O  
ANISOU 6580  O   HIS A 434     1611   1558   1617    157    -58     31       O  
ATOM   6581  CB  HIS A 434       6.047  32.662 -18.742  1.00 13.30           C  
ANISOU 6581  CB  HIS A 434     1679   1655   1720    151    -20     48       C  
ATOM   6582  CG  HIS A 434       6.895  32.366 -17.548  1.00 15.00           C  
ANISOU 6582  CG  HIS A 434     1880   1882   1937    153    -16     58       C  
ATOM   6583  ND1 HIS A 434       6.498  31.498 -16.553  1.00 14.12           N  
ANISOU 6583  ND1 HIS A 434     1757   1777   1830    160    -10     63       N  
ATOM   6584  CD2 HIS A 434       8.109  32.835 -17.177  1.00 13.16           C  
ANISOU 6584  CD2 HIS A 434     1642   1659   1700    145    -18     67       C  
ATOM   6585  CE1 HIS A 434       7.433  31.442 -15.624  1.00 15.23           C  
ANISOU 6585  CE1 HIS A 434     1887   1931   1970    160    -10     75       C  
ATOM   6586  NE2 HIS A 434       8.429  32.231 -15.985  1.00 13.00           N  
ANISOU 6586  NE2 HIS A 434     1606   1652   1682    151    -14     76       N  
ATOM   6587  H   HIS A 434       4.214  34.411 -19.803  1.00 15.27           H  
ATOM   6588  HA  HIS A 434       4.135  32.376 -18.024  1.00 17.28           H  
ATOM   6589  HB2 HIS A 434       5.985  31.852 -19.271  1.00 15.97           H  
ATOM   6590  HB3 HIS A 434       6.486  33.360 -19.253  1.00 15.97           H  
ATOM   6591  HD1 HIS A 434       5.757  31.062 -16.541  1.00 16.94           H  
ATOM   6592  HD2 HIS A 434       8.628  33.451 -17.641  1.00 15.80           H  
ATOM   6593  HE1 HIS A 434       7.396  30.933 -14.846  1.00 18.28           H  
ATOM   6594  N   LEU A 435       4.354  33.850 -16.090  1.00 11.61           N  
ANISOU 6594  N   LEU A 435     1457   1458   1495    170    -41     32       N  
ATOM   6595  CA  LEU A 435       4.389  34.730 -14.928  1.00 12.89           C  
ANISOU 6595  CA  LEU A 435     1620   1628   1649    174    -51     24       C  
ATOM   6596  C   LEU A 435       5.487  34.281 -13.970  1.00 13.83           C  
ANISOU 6596  C   LEU A 435     1727   1762   1766    166    -45     38       C  
ATOM   6597  O   LEU A 435       5.495  33.126 -13.531  1.00 14.64           O  
ANISOU 6597  O   LEU A 435     1815   1875   1872    167    -33     50       O  
ATOM   6598  CB  LEU A 435       3.033  34.712 -14.220  1.00 14.25           C  
ANISOU 6598  CB  LEU A 435     1782   1815   1816    188    -52     11       C  
ATOM   6599  CG  LEU A 435       2.938  35.568 -12.961  1.00 14.15           C  
ANISOU 6599  CG  LEU A 435     1770   1814   1791    196    -60     -2       C  
ATOM   6600  CD1 LEU A 435       3.250  37.033 -13.265  1.00 15.14           C  
ANISOU 6600  CD1 LEU A 435     1920   1917   1914    199    -78    -15       C  
ATOM   6601  CD2 LEU A 435       1.552  35.413 -12.342  1.00 13.28           C  
ANISOU 6601  CD2 LEU A 435     1645   1727   1673    211    -57    -16       C  
ATOM   6602  H   LEU A 435       4.080  33.058 -15.896  1.00 13.93           H  
ATOM   6603  HA  LEU A 435       4.597  35.633 -15.216  1.00 15.46           H  
ATOM   6604  HB2 LEU A 435       2.361  35.035 -14.840  1.00 17.09           H  
ATOM   6605  HB3 LEU A 435       2.836  33.798 -13.963  1.00 17.09           H  
ATOM   6606  HG  LEU A 435       3.598  35.270 -12.315  1.00 16.98           H  
ATOM   6607 HD11 LEU A 435       2.606  37.595 -12.807  1.00 18.16           H  
ATOM   6608 HD12 LEU A 435       4.146  37.236 -12.954  1.00 18.16           H  
ATOM   6609 HD13 LEU A 435       3.193  37.176 -14.223  1.00 18.16           H  
ATOM   6610 HD21 LEU A 435       1.476  36.011 -11.582  1.00 15.93           H  
ATOM   6611 HD22 LEU A 435       0.882  35.636 -13.007  1.00 15.93           H  
ATOM   6612 HD23 LEU A 435       1.437  34.494 -12.052  1.00 15.93           H  
ATOM   6613  N   HIS A 436       6.409  35.190 -13.651  1.00 11.85           N  
ANISOU 6613  N   HIS A 436     1483   1510   1508    156    -55     38       N  
ATOM   6614  CA  HIS A 436       7.371  34.957 -12.584  1.00 11.60           C  
ANISOU 6614  CA  HIS A 436     1439   1498   1470    148    -54     49       C  
ATOM   6615  C   HIS A 436       6.712  35.146 -11.211  1.00 13.15           C  
ANISOU 6615  C   HIS A 436     1629   1712   1654    155    -57     38       C  
ATOM   6616  O   HIS A 436       5.781  35.941 -11.058  1.00 12.37           O  
ANISOU 6616  O   HIS A 436     1542   1608   1550    165    -65     17       O  
ATOM   6617  CB  HIS A 436       8.552  35.935 -12.653  1.00 11.51           C  
ANISOU 6617  CB  HIS A 436     1436   1484   1452    130    -65     51       C  
ATOM   6618  CG  HIS A 436       9.439  35.815 -13.858  1.00 11.39           C  
ANISOU 6618  CG  HIS A 436     1421   1462   1444    119    -60     64       C  
ATOM   6619  ND1 HIS A 436      10.792  36.068 -13.781  1.00 14.99           N  
ANISOU 6619  ND1 HIS A 436     1869   1933   1894    100    -63     76       N  
ATOM   6620  CD2 HIS A 436       9.183  35.544 -15.160  1.00 11.10           C  
ANISOU 6620  CD2 HIS A 436     1390   1411   1415    121    -54     64       C  
ATOM   6621  CE1 HIS A 436      11.338  35.928 -14.975  1.00 16.00           C  
ANISOU 6621  CE1 HIS A 436     1996   2058   2026     92    -56     84       C  
ATOM   6622  NE2 HIS A 436      10.385  35.607 -15.831  1.00 13.20           N  
ANISOU 6622  NE2 HIS A 436     1652   1685   1680    105    -51     76       N  
ATOM   6623  H   HIS A 436       6.496  35.952 -14.040  1.00 14.22           H  
ATOM   6624  HA  HIS A 436       7.701  34.050 -12.683  1.00 13.92           H  
ATOM   6625  HB2 HIS A 436       8.198  36.838 -12.648  1.00 13.81           H  
ATOM   6626  HB3 HIS A 436       9.109  35.793 -11.872  1.00 13.81           H  
ATOM   6627  HD1 HIS A 436      11.216  36.284 -13.064  1.00 17.99           H  
ATOM   6628  HD2 HIS A 436       8.352  35.353 -15.532  1.00 13.32           H  
ATOM   6629  HE1 HIS A 436      12.239  36.036 -15.178  1.00 19.20           H  
ATOM   6630  N   GLY A 437       7.235  34.440 -10.200  1.00 11.00           N  
ANISOU 6630  N   GLY A 437     1340   1464   1376    151    -52     53       N  
ATOM   6631  CA  GLY A 437       6.884  34.684  -8.807  1.00 11.05           C  
ANISOU 6631  CA  GLY A 437     1340   1494   1364    152    -56     45       C  
ATOM   6632  C   GLY A 437       5.617  34.023  -8.306  1.00 12.89           C  
ANISOU 6632  C   GLY A 437     1562   1742   1593    162    -46     42       C  
ATOM   6633  O   GLY A 437       5.303  34.143  -7.108  1.00 14.40           O  
ANISOU 6633  O   GLY A 437     1745   1960   1765    162    -47     36       O  
ATOM   6634  H   GLY A 437       7.804  33.803 -10.304  1.00 13.20           H  
ATOM   6635  HA2 GLY A 437       7.614  34.371  -8.250  1.00 13.26           H  
ATOM   6636  HA3 GLY A 437       6.780  35.641  -8.683  1.00 13.26           H  
ATOM   6637  N   HIS A 438       4.873  33.349  -9.173  1.00 13.52           N  
ANISOU 6637  N   HIS A 438     1641   1810   1687    169    -38     45       N  
ATOM   6638  CA  HIS A 438       3.533  32.890  -8.867  1.00 11.31           C  
ANISOU 6638  CA  HIS A 438     1352   1546   1402    175    -31     39       C  
ATOM   6639  C   HIS A 438       3.174  31.769  -9.827  1.00 13.44           C  
ANISOU 6639  C   HIS A 438     1620   1800   1688    172    -21     53       C  
ATOM   6640  O   HIS A 438       3.612  31.770 -10.979  1.00 14.63           O  
ANISOU 6640  O   HIS A 438     1781   1925   1853    172    -22     54       O  
ATOM   6641  CB  HIS A 438       2.473  33.977  -9.067  1.00 12.25           C  
ANISOU 6641  CB  HIS A 438     1476   1664   1514    190    -38      9       C  
ATOM   6642  CG  HIS A 438       2.646  35.196  -8.226  1.00 12.87           C  
ANISOU 6642  CG  HIS A 438     1564   1751   1577    196    -48    -13       C  
ATOM   6643  ND1 HIS A 438       2.178  35.266  -6.934  1.00 19.58           N  
ANISOU 6643  ND1 HIS A 438     2400   2635   2405    199    -45    -23       N  
ATOM   6644  CD2 HIS A 438       3.177  36.410  -8.504  1.00 14.76           C  
ANISOU 6644  CD2 HIS A 438     1825   1966   1816    199    -62    -28       C  
ATOM   6645  CE1 HIS A 438       2.435  36.463  -6.440  1.00 21.92           C  
ANISOU 6645  CE1 HIS A 438     2711   2928   2689    206    -56    -47       C  
ATOM   6646  NE2 HIS A 438       3.032  37.181  -7.375  1.00 16.24           N  
ANISOU 6646  NE2 HIS A 438     2015   2171   1985    205    -68    -50       N  
ATOM   6647  H   HIS A 438       5.131  33.141  -9.967  1.00 16.22           H  
ATOM   6648  HA  HIS A 438       3.534  32.591  -7.944  1.00 13.58           H  
ATOM   6649  HB2 HIS A 438       2.496  34.260  -9.995  1.00 14.70           H  
ATOM   6650  HB3 HIS A 438       1.604  33.600  -8.857  1.00 14.70           H  
ATOM   6651  HD2 HIS A 438       3.567  36.673  -9.307  1.00 17.71           H  
ATOM   6652  HE1 HIS A 438       2.231  36.752  -5.580  1.00 26.30           H  
ATOM   6653  HE2 HIS A 438       3.288  37.998  -7.291  1.00 19.49           H  
ATOM   6654  N   ASP A 439       2.333  30.854  -9.367  1.00 12.33           N  
ANISOU 6654  N   ASP A 439     1466   1677   1543    167    -13     61       N  
ATOM   6655  CA  ASP A 439       1.423  30.176 -10.272  1.00 10.72           C  
ANISOU 6655  CA  ASP A 439     1262   1462   1349    163     -7     61       C  
ATOM   6656  C   ASP A 439       0.205  31.062 -10.468  1.00 13.01           C  
ANISOU 6656  C   ASP A 439     1546   1766   1630    174    -12     36       C  
ATOM   6657  O   ASP A 439      -0.237  31.751  -9.540  1.00 15.64           O  
ANISOU 6657  O   ASP A 439     1870   2126   1946    183    -14     22       O  
ATOM   6658  CB  ASP A 439       1.001  28.820  -9.726  1.00 12.29           C  
ANISOU 6658  CB  ASP A 439     1451   1673   1547    148      2     83       C  
ATOM   6659  CG  ASP A 439       2.148  27.841  -9.684  1.00 19.33           C  
ANISOU 6659  CG  ASP A 439     2350   2544   2451    143      5    109       C  
ATOM   6660  OD1 ASP A 439       2.906  27.765 -10.675  1.00 20.59           O  
ANISOU 6660  OD1 ASP A 439     2522   2675   2627    149      5    109       O  
ATOM   6661  OD2 ASP A 439       2.303  27.161  -8.654  1.00 17.71           O  
ANISOU 6661  OD2 ASP A 439     2137   2353   2238    134      7    131       O  
ATOM   6662  H   ASP A 439       2.272  30.610  -8.544  1.00 14.80           H  
ATOM   6663  HA  ASP A 439       1.857  30.010 -11.123  1.00 12.86           H  
ATOM   6664  HB2 ASP A 439       0.665  28.931  -8.823  1.00 14.75           H  
ATOM   6665  HB3 ASP A 439       0.308  28.450 -10.294  1.00 14.75           H  
ATOM   6666  N   PHE A 440      -0.322  31.062 -11.682  1.00 13.88           N  
ANISOU 6666  N   PHE A 440     1664   1861   1752    177    -14     28       N  
ATOM   6667  CA  PHE A 440      -1.612  31.687 -11.926  1.00 11.53           C  
ANISOU 6667  CA  PHE A 440     1355   1579   1446    189    -19      8       C  
ATOM   6668  C   PHE A 440      -2.674  30.615 -12.133  1.00 14.33           C  
ANISOU 6668  C   PHE A 440     1694   1951   1799    173    -11     16       C  
ATOM   6669  O   PHE A 440      -2.385  29.423 -12.288  1.00 14.90           O  
ANISOU 6669  O   PHE A 440     1771   2012   1880    153     -4     35       O  
ATOM   6670  CB  PHE A 440      -1.578  32.658 -13.122  1.00 13.17           C  
ANISOU 6670  CB  PHE A 440     1580   1761   1662    203    -31     -6       C  
ATOM   6671  CG  PHE A 440      -1.000  32.078 -14.388  1.00 14.27           C  
ANISOU 6671  CG  PHE A 440     1735   1871   1816    191    -30      6       C  
ATOM   6672  CD1 PHE A 440      -1.618  31.029 -15.048  1.00 15.26           C  
ANISOU 6672  CD1 PHE A 440     1855   1997   1946    177    -23     12       C  
ATOM   6673  CD2 PHE A 440       0.167  32.601 -14.926  1.00 18.58           C  
ANISOU 6673  CD2 PHE A 440     2300   2390   2368    191    -34      9       C  
ATOM   6674  CE1 PHE A 440      -1.068  30.503 -16.205  1.00 14.39           C  
ANISOU 6674  CE1 PHE A 440     1760   1860   1846    167    -21     18       C  
ATOM   6675  CE2 PHE A 440       0.713  32.082 -16.099  1.00 17.71           C  
ANISOU 6675  CE2 PHE A 440     2202   2260   2268    181    -31     17       C  
ATOM   6676  CZ  PHE A 440       0.097  31.035 -16.731  1.00 15.18           C  
ANISOU 6676  CZ  PHE A 440     1878   1939   1952    170    -24     20       C  
ATOM   6677  H   PHE A 440       0.047  30.709 -12.374  1.00 16.66           H  
ATOM   6678  HA  PHE A 440      -1.848  32.214 -11.147  1.00 13.83           H  
ATOM   6679  HB2 PHE A 440      -2.486  32.939 -13.317  1.00 15.80           H  
ATOM   6680  HB3 PHE A 440      -1.038  33.427 -12.880  1.00 15.80           H  
ATOM   6681  HD1 PHE A 440      -2.409  30.675 -14.712  1.00 18.31           H  
ATOM   6682  HD2 PHE A 440       0.591  33.308 -14.498  1.00 22.29           H  
ATOM   6683  HE1 PHE A 440      -1.484  29.789 -16.632  1.00 17.26           H  
ATOM   6684  HE2 PHE A 440       1.493  32.447 -16.452  1.00 21.26           H  
ATOM   6685  HZ  PHE A 440       0.461  30.682 -17.511  1.00 18.22           H  
ATOM   6686  N   TYR A 441      -3.920  31.080 -12.096  1.00 13.68           N  
ANISOU 6686  N   TYR A 441     1593   1898   1706    184    -14     -1       N  
ATOM   6687  CA  TYR A 441      -5.115  30.274 -12.293  1.00 13.29           C  
ANISOU 6687  CA  TYR A 441     1523   1874   1651    168     -9      3       C  
ATOM   6688  C   TYR A 441      -5.754  30.676 -13.613  1.00 12.18           C  
ANISOU 6688  C   TYR A 441     1384   1725   1517    177    -20     -9       C  
ATOM   6689  O   TYR A 441      -5.999  31.864 -13.851  1.00 14.94           O  
ANISOU 6689  O   TYR A 441     1736   2076   1866    205    -31    -27       O  
ATOM   6690  CB  TYR A 441      -6.115  30.495 -11.155  1.00 13.52           C  
ANISOU 6690  CB  TYR A 441     1521   1958   1658    173     -4     -6       C  
ATOM   6691  CG  TYR A 441      -5.592  30.182  -9.777  1.00 13.96           C  
ANISOU 6691  CG  TYR A 441     1572   2031   1701    163      5      5       C  
ATOM   6692  CD1 TYR A 441      -4.763  31.069  -9.101  1.00 12.37           C  
ANISOU 6692  CD1 TYR A 441     1382   1823   1495    182      1     -5       C  
ATOM   6693  CD2 TYR A 441      -5.940  29.004  -9.141  1.00 14.80           C  
ANISOU 6693  CD2 TYR A 441     1664   2161   1797    131     15     28       C  
ATOM   6694  CE1 TYR A 441      -4.281  30.773  -7.832  1.00 15.30           C  
ANISOU 6694  CE1 TYR A 441     1748   2214   1851    171      8      7       C  
ATOM   6695  CE2 TYR A 441      -5.489  28.714  -7.886  1.00 12.95           C  
ANISOU 6695  CE2 TYR A 441     1426   1945   1548    121     22     42       C  
ATOM   6696  CZ  TYR A 441      -4.649  29.590  -7.234  1.00 15.98           C  
ANISOU 6696  CZ  TYR A 441     1819   2326   1927    142     18     31       C  
ATOM   6697  OH  TYR A 441      -4.179  29.259  -5.982  1.00 18.95           O  
ANISOU 6697  OH  TYR A 441     2190   2724   2286    129     23     47       O  
ATOM   6698  H   TYR A 441      -4.104  31.907 -11.949  1.00 16.41           H  
ATOM   6699  HA  TYR A 441      -4.878  29.334 -12.321  1.00 15.94           H  
ATOM   6700  HB2 TYR A 441      -6.384  31.427 -11.159  1.00 16.22           H  
ATOM   6701  HB3 TYR A 441      -6.886  29.926 -11.309  1.00 16.22           H  
ATOM   6702  HD1 TYR A 441      -4.526  31.873  -9.505  1.00 14.84           H  
ATOM   6703  HD2 TYR A 441      -6.493  28.398  -9.578  1.00 17.76           H  
ATOM   6704  HE1 TYR A 441      -3.718  31.368  -7.392  1.00 18.36           H  
ATOM   6705  HE2 TYR A 441      -5.750  27.924  -7.470  1.00 15.54           H  
ATOM   6706  HH  TYR A 441      -3.365  29.453  -5.920  1.00 22.74           H  
ATOM   6707  N   VAL A 442      -6.040  29.696 -14.460  1.00 13.72           N  
ANISOU 6707  N   VAL A 442     1583   1912   1719    152    -18      1       N  
ATOM   6708  CA  VAL A 442      -6.636  29.963 -15.762  1.00 13.43           C  
ANISOU 6708  CA  VAL A 442     1548   1869   1685    156    -28     -8       C  
ATOM   6709  C   VAL A 442      -8.150  29.889 -15.586  1.00 16.47           C  
ANISOU 6709  C   VAL A 442     1897   2304   2055    153    -30    -14       C  
ATOM   6710  O   VAL A 442      -8.729  28.802 -15.502  1.00 15.94           O  
ANISOU 6710  O   VAL A 442     1818   2256   1983    120    -23     -4       O  
ATOM   6711  CB  VAL A 442      -6.126  28.992 -16.827  1.00 14.31           C  
ANISOU 6711  CB  VAL A 442     1682   1947   1809    131    -25      3       C  
ATOM   6712  CG1 VAL A 442      -6.682  29.397 -18.184  1.00 15.57           C  
ANISOU 6712  CG1 VAL A 442     1844   2104   1967    134    -38     -7       C  
ATOM   6713  CG2 VAL A 442      -4.601  28.970 -16.856  1.00 13.51           C  
ANISOU 6713  CG2 VAL A 442     1607   1805   1719    135    -21     10       C  
ATOM   6714  H   VAL A 442      -5.897  28.863 -14.301  1.00 16.47           H  
ATOM   6715  HA  VAL A 442      -6.409  30.864 -16.044  1.00 16.11           H  
ATOM   6716  HB  VAL A 442      -6.427  28.094 -16.617  1.00 17.17           H  
ATOM   6717 HG11 VAL A 442      -6.428  28.730 -18.841  1.00 18.68           H  
ATOM   6718 HG12 VAL A 442      -7.649  29.452 -18.125  1.00 18.68           H  
ATOM   6719 HG13 VAL A 442      -6.316  30.260 -18.430  1.00 18.68           H  
ATOM   6720 HG21 VAL A 442      -4.306  28.222 -17.398  1.00 16.21           H  
ATOM   6721 HG22 VAL A 442      -4.280  29.802 -17.238  1.00 16.21           H  
ATOM   6722 HG23 VAL A 442      -4.270  28.872 -15.949  1.00 16.21           H  
ATOM   6723  N   LEU A 443      -8.793  31.057 -15.499  1.00 13.11           N  
ANISOU 6723  N   LEU A 443     1456   1902   1623    187    -40    -32       N  
ATOM   6724  CA  LEU A 443     -10.230  31.091 -15.245  1.00 14.69           C  
ANISOU 6724  CA  LEU A 443     1616   2159   1807    191    -41    -41       C  
ATOM   6725  C   LEU A 443     -11.026  30.758 -16.495  1.00 16.90           C  
ANISOU 6725  C   LEU A 443     1887   2446   2087    177    -51    -39       C  
ATOM   6726  O   LEU A 443     -12.165  30.294 -16.391  1.00 16.99           O  
ANISOU 6726  O   LEU A 443     1864   2507   2086    161    -50    -39       O  
ATOM   6727  CB  LEU A 443     -10.646  32.457 -14.696  1.00 13.76           C  
ANISOU 6727  CB  LEU A 443     1483   2062   1682    239    -48    -64       C  
ATOM   6728  CG  LEU A 443      -9.899  32.896 -13.431  1.00 14.37           C  
ANISOU 6728  CG  LEU A 443     1569   2135   1755    253    -39    -70       C  
ATOM   6729  CD1 LEU A 443     -10.488  34.166 -12.854  1.00 16.96           C  
ANISOU 6729  CD1 LEU A 443     1881   2488   2073    301    -45    -98       C  
ATOM   6730  CD2 LEU A 443      -9.897  31.788 -12.394  1.00 17.70           C  
ANISOU 6730  CD2 LEU A 443     1975   2586   2165    218    -21    -55       C  
ATOM   6731  H   LEU A 443      -8.425  31.829 -15.583  1.00 15.73           H  
ATOM   6732  HA  LEU A 443     -10.451  30.439 -14.562  1.00 17.63           H  
ATOM   6733  HB2 LEU A 443     -10.481  33.126 -15.380  1.00 16.51           H  
ATOM   6734  HB3 LEU A 443     -11.592  32.427 -14.482  1.00 16.51           H  
ATOM   6735  HG  LEU A 443      -8.978  33.084 -13.672  1.00 17.24           H  
ATOM   6736 HD11 LEU A 443      -9.821  34.600 -12.298  1.00 20.35           H  
ATOM   6737 HD12 LEU A 443     -10.745  34.754 -13.581  1.00 20.35           H  
ATOM   6738 HD13 LEU A 443     -11.266  33.940 -12.321  1.00 20.35           H  
ATOM   6739 HD21 LEU A 443      -9.442  32.102 -11.597  1.00 21.24           H  
ATOM   6740 HD22 LEU A 443     -10.814  31.553 -12.180  1.00 21.24           H  
ATOM   6741 HD23 LEU A 443      -9.435  31.016 -12.757  1.00 21.24           H  
ATOM   6742  N   GLY A 444     -10.443  30.957 -17.664  1.00 14.38           N  
ANISOU 6742  N   GLY A 444     1597   2085   1780    179    -62    -38       N  
ATOM   6743  CA  GLY A 444     -11.117  30.611 -18.896  1.00 16.69           C  
ANISOU 6743  CA  GLY A 444     1885   2385   2070    162    -72    -36       C  
ATOM   6744  C   GLY A 444     -10.333  31.151 -20.061  1.00 14.69           C  
ANISOU 6744  C   GLY A 444     1668   2086   1827    172    -84    -36       C  
ATOM   6745  O   GLY A 444      -9.368  31.905 -19.899  1.00 16.47           O  
ANISOU 6745  O   GLY A 444     1918   2279   2062    194    -86    -37       O  
ATOM   6746  H   GLY A 444      -9.658  31.291 -17.770  1.00 17.25           H  
ATOM   6747  HA2 GLY A 444     -11.185  29.647 -18.979  1.00 20.02           H  
ATOM   6748  HA3 GLY A 444     -12.008  30.993 -18.907  1.00 20.02           H  
ATOM   6749  N   ARG A 445     -10.765  30.752 -21.252  1.00 14.29           N  
ANISOU 6749  N   ARG A 445     1618   2038   1773    153    -93    -33       N  
ATOM   6750  CA  ARG A 445     -10.135  31.229 -22.470  1.00 14.48           C  
ANISOU 6750  CA  ARG A 445     1673   2027   1801    158   -105    -32       C  
ATOM   6751  C   ARG A 445     -11.124  31.102 -23.610  1.00 14.05           C  
ANISOU 6751  C   ARG A 445     1606   1999   1735    146   -121    -32       C  
ATOM   6752  O   ARG A 445     -12.163  30.444 -23.502  1.00 14.23           O  
ANISOU 6752  O   ARG A 445     1598   2062   1748    126   -121    -33       O  
ATOM   6753  CB  ARG A 445      -8.844  30.476 -22.783  1.00 21.63           C  
ANISOU 6753  CB  ARG A 445     2614   2889   2716    133    -91    -26       C  
ATOM   6754  CG  ARG A 445      -8.998  29.066 -23.171  1.00 19.55           C  
ANISOU 6754  CG  ARG A 445     2354   2625   2450     92    -81    -24       C  
ATOM   6755  CD  ARG A 445      -7.622  28.481 -23.468  1.00 22.43           C  
ANISOU 6755  CD  ARG A 445     2753   2944   2826     80    -67    -21       C  
ATOM   6756  NE  ARG A 445      -7.793  27.107 -23.903  1.00 19.44           N  
ANISOU 6756  NE  ARG A 445     2383   2558   2446     43    -59    -22       N  
ATOM   6757  CZ  ARG A 445      -6.860  26.168 -23.867  1.00 16.63           C  
ANISOU 6757  CZ  ARG A 445     2052   2168   2100     29    -44    -20       C  
ATOM   6758  NH1 ARG A 445      -5.651  26.432 -23.394  1.00 16.45           N  
ANISOU 6758  NH1 ARG A 445     2042   2119   2088     49    -34    -16       N  
ATOM   6759  NH2 ARG A 445      -7.158  24.959 -24.312  1.00 18.24           N  
ANISOU 6759  NH2 ARG A 445     2266   2362   2302     -5    -40    -24       N  
ATOM   6760  H   ARG A 445     -11.419  30.208 -21.378  1.00 17.15           H  
ATOM   6761  HA  ARG A 445      -9.915  32.167 -22.356  1.00 17.37           H  
ATOM   6762  HB2 ARG A 445      -8.400  30.929 -23.517  1.00 25.96           H  
ATOM   6763  HB3 ARG A 445      -8.283  30.497 -21.992  1.00 25.96           H  
ATOM   6764  HG2 ARG A 445      -9.403  28.565 -22.445  1.00 23.46           H  
ATOM   6765  HG3 ARG A 445      -9.547  29.000 -23.967  1.00 23.46           H  
ATOM   6766  HD2 ARG A 445      -7.190  28.987 -24.174  1.00 26.92           H  
ATOM   6767  HD3 ARG A 445      -7.074  28.495 -22.667  1.00 26.92           H  
ATOM   6768  HE  ARG A 445      -8.564  26.885 -24.211  1.00 23.33           H  
ATOM   6769 HH11 ARG A 445      -5.464  27.220 -23.106  1.00 19.74           H  
ATOM   6770 HH12 ARG A 445      -5.053  25.814 -23.375  1.00 19.74           H  
ATOM   6771 HH21 ARG A 445      -7.944  24.795 -24.618  1.00 21.88           H  
ATOM   6772 HH22 ARG A 445      -6.564  24.337 -24.296  1.00 21.88           H  
ATOM   6773  N   SER A 446     -10.783  31.759 -24.704  1.00 16.18           N  
ANISOU 6773  N   SER A 446     1897   2247   2003    156   -136    -30       N  
ATOM   6774  CA  SER A 446     -11.613  31.741 -25.888  1.00 14.00           C  
ANISOU 6774  CA  SER A 446     1611   1994   1713    146   -154    -29       C  
ATOM   6775  C   SER A 446     -11.798  30.311 -26.393  1.00 16.35           C  
ANISOU 6775  C   SER A 446     1910   2299   2004     95   -144    -30       C  
ATOM   6776  O   SER A 446     -10.964  29.435 -26.134  1.00 15.78           O  
ANISOU 6776  O   SER A 446     1859   2197   1940     72   -125    -31       O  
ATOM   6777  CB  SER A 446     -10.969  32.633 -26.943  1.00 13.17           C  
ANISOU 6777  CB  SER A 446     1536   1859   1607    160   -170    -22       C  
ATOM   6778  OG  SER A 446      -9.610  32.291 -27.149  1.00 13.97           O  
ANISOU 6778  OG  SER A 446     1674   1918   1716    143   -154    -20       O  
ATOM   6779  H   SER A 446     -10.068  32.228 -24.789  1.00 19.41           H  
ATOM   6780  HA  SER A 446     -12.502  32.080 -25.697  1.00 16.80           H  
ATOM   6781  HB2 SER A 446     -11.450  32.526 -27.779  1.00 15.80           H  
ATOM   6782  HB3 SER A 446     -11.019  33.555 -26.648  1.00 15.80           H  
ATOM   6783  HG  SER A 446      -9.547  31.716 -27.759  1.00 16.76           H  
ATOM   6784  N   PRO A 447     -12.907  30.042 -27.081  1.00 18.55           N  
ANISOU 6784  N   PRO A 447     2165   2616   2266     77   -159    -31       N  
ATOM   6785  CA  PRO A 447     -13.171  28.678 -27.556  1.00 22.77           C  
ANISOU 6785  CA  PRO A 447     2703   3158   2792     24   -152    -35       C  
ATOM   6786  C   PRO A 447     -12.022  28.127 -28.384  1.00 20.86           C  
ANISOU 6786  C   PRO A 447     2506   2867   2552      3   -142    -38       C  
ATOM   6787  O   PRO A 447     -11.433  28.828 -29.213  1.00 18.64           O  
ANISOU 6787  O   PRO A 447     2246   2567   2268     19   -150    -37       O  
ATOM   6788  CB  PRO A 447     -14.442  28.835 -28.398  1.00 22.64           C  
ANISOU 6788  CB  PRO A 447     2656   3191   2756     15   -175    -34       C  
ATOM   6789  CG  PRO A 447     -15.143  30.033 -27.794  1.00 25.36           C  
ANISOU 6789  CG  PRO A 447     2965   3569   3102     66   -189    -31       C  
ATOM   6790  CD  PRO A 447     -14.024  30.963 -27.375  1.00 22.40           C  
ANISOU 6790  CD  PRO A 447     2620   3147   2743    106   -184    -29       C  
ATOM   6791  HA  PRO A 447     -13.338  28.090 -26.803  1.00 27.33           H  
ATOM   6792  HB2 PRO A 447     -14.210  28.997 -29.326  1.00 27.17           H  
ATOM   6793  HB3 PRO A 447     -14.989  28.037 -28.328  1.00 27.17           H  
ATOM   6794  HG2 PRO A 447     -15.714  30.452 -28.456  1.00 30.43           H  
ATOM   6795  HG3 PRO A 447     -15.671  29.757 -27.028  1.00 30.43           H  
ATOM   6796  HD2 PRO A 447     -13.791  31.569 -28.095  1.00 26.88           H  
ATOM   6797  HD3 PRO A 447     -14.272  31.467 -26.584  1.00 26.88           H  
ATOM   6798  N   ASP A 448     -11.721  26.846 -28.158  1.00 17.18           N  
ANISOU 6798  N   ASP A 448     2055   2382   2091    -33   -124    -44       N  
ATOM   6799  CA  ASP A 448     -10.639  26.189 -28.872  1.00 16.49           C  
ANISOU 6799  CA  ASP A 448     2008   2249   2006    -50   -111    -51       C  
ATOM   6800  C   ASP A 448     -10.895  26.247 -30.372  1.00 19.74           C  
ANISOU 6800  C   ASP A 448     2431   2672   2398    -67   -126    -59       C  
ATOM   6801  O   ASP A 448     -11.996  25.942 -30.841  1.00 24.32           O  
ANISOU 6801  O   ASP A 448     2992   3288   2961    -93   -140    -61       O  
ATOM   6802  CB  ASP A 448     -10.505  24.733 -28.438  1.00 22.57           C  
ANISOU 6802  CB  ASP A 448     2793   2998   2785    -86    -94    -56       C  
ATOM   6803  CG  ASP A 448      -9.891  24.569 -27.065  1.00 30.75           C  
ANISOU 6803  CG  ASP A 448     3829   4013   3840    -70    -77    -47       C  
ATOM   6804  OD1 ASP A 448      -9.600  25.574 -26.375  1.00 23.86           O  
ANISOU 6804  OD1 ASP A 448     2945   3147   2976    -33    -78    -39       O  
ATOM   6805  OD2 ASP A 448      -9.692  23.392 -26.694  1.00 34.38           O  
ANISOU 6805  OD2 ASP A 448     4305   4449   4308    -97    -65    -48       O  
ATOM   6806  H   ASP A 448     -12.131  26.339 -27.596  1.00 20.62           H  
ATOM   6807  HA  ASP A 448      -9.808  26.645 -28.666  1.00 19.78           H  
ATOM   6808  HB2 ASP A 448     -11.387  24.329 -28.419  1.00 27.09           H  
ATOM   6809  HB3 ASP A 448      -9.941  24.266 -29.074  1.00 27.09           H  
ATOM   6810  N   GLU A 449      -9.873  26.659 -31.118  1.00 16.59           N  
ANISOU 6810  N   GLU A 449     2060   2247   1997    -55   -123    -61       N  
ATOM   6811  CA  GLU A 449      -9.920  26.737 -32.567  1.00 17.88           C  
ANISOU 6811  CA  GLU A 449     2238   2419   2137    -71   -134    -67       C  
ATOM   6812  C   GLU A 449      -8.561  26.305 -33.097  1.00 18.97           C  
ANISOU 6812  C   GLU A 449     2413   2517   2276    -76   -114    -78       C  
ATOM   6813  O   GLU A 449      -7.563  26.368 -32.375  1.00 16.43           O  
ANISOU 6813  O   GLU A 449     2102   2167   1974    -55    -97    -75       O  
ATOM   6814  CB  GLU A 449     -10.165  28.155 -33.102  1.00 15.54           C  
ANISOU 6814  CB  GLU A 449     1931   2143   1829    -44   -158    -52       C  
ATOM   6815  CG  GLU A 449     -11.403  28.848 -32.648  1.00 24.52           C  
ANISOU 6815  CG  GLU A 449     3030   3321   2966    -24   -180    -42       C  
ATOM   6816  CD  GLU A 449     -12.656  28.292 -33.264  1.00 26.27           C  
ANISOU 6816  CD  GLU A 449     3229   3586   3166    -56   -196    -46       C  
ATOM   6817  OE1 GLU A 449     -12.591  27.420 -34.159  1.00 24.60           O  
ANISOU 6817  OE1 GLU A 449     3036   3372   2938    -96   -193    -59       O  
ATOM   6818  OE2 GLU A 449     -13.727  28.747 -32.834  1.00 25.00           O  
ANISOU 6818  OE2 GLU A 449     3029   3464   3004    -41   -213    -39       O  
ATOM   6819  H   GLU A 449      -9.117  26.906 -30.792  1.00 19.91           H  
ATOM   6820  HA  GLU A 449     -10.637  26.159 -32.871  1.00 21.45           H  
ATOM   6821  HB2 GLU A 449      -9.417  28.710 -32.832  1.00 18.64           H  
ATOM   6822  HB3 GLU A 449     -10.209  28.106 -34.070  1.00 18.64           H  
ATOM   6823  HG2 GLU A 449     -11.479  28.755 -31.685  1.00 29.43           H  
ATOM   6824  HG3 GLU A 449     -11.344  29.786 -32.887  1.00 29.43           H  
ATOM   6825  N   SER A 450      -8.492  25.939 -34.373  1.00 15.82           N  
ANISOU 6825  N   SER A 450     2034   2124   1856   -101   -117    -91       N  
ATOM   6826  CA  SER A 450      -7.192  25.941 -35.038  1.00 15.52           C  
ANISOU 6826  CA  SER A 450     2025   2061   1813    -96   -100    -99       C  
ATOM   6827  C   SER A 450      -6.716  27.386 -35.172  1.00 15.90           C  
ANISOU 6827  C   SER A 450     2069   2114   1857    -66   -111    -78       C  
ATOM   6828  O   SER A 450      -7.484  28.238 -35.637  1.00 15.91           O  
ANISOU 6828  O   SER A 450     2058   2144   1844    -63   -137    -65       O  
ATOM   6829  CB  SER A 450      -7.243  25.311 -36.424  1.00 17.43           C  
ANISOU 6829  CB  SER A 450     2287   2312   2026   -129   -101   -120       C  
ATOM   6830  OG  SER A 450      -6.022  25.563 -37.120  1.00 15.46           O  
ANISOU 6830  OG  SER A 450     2060   2050   1766   -120    -86   -125       O  
ATOM   6831  H   SER A 450      -9.157  25.694 -34.860  1.00 18.99           H  
ATOM   6832  HA  SER A 450      -6.575  25.416 -34.505  1.00 18.63           H  
ATOM   6833  HB2 SER A 450      -7.368  24.353 -36.335  1.00 20.92           H  
ATOM   6834  HB3 SER A 450      -7.980  25.696 -36.923  1.00 20.92           H  
ATOM   6835  HG  SER A 450      -6.095  26.256 -37.587  1.00 18.56           H  
ATOM   6836  N   PRO A 451      -5.467  27.709 -34.803  1.00 14.91           N  
ANISOU 6836  N   PRO A 451     1957   1964   1746    -46    -94    -74       N  
ATOM   6837  CA  PRO A 451      -4.991  29.089 -35.003  1.00 16.88           C  
ANISOU 6837  CA  PRO A 451     2208   2217   1990    -26   -106    -53       C  
ATOM   6838  C   PRO A 451      -4.898  29.472 -36.468  1.00 18.50           C  
ANISOU 6838  C   PRO A 451     2426   2441   2163    -43   -117    -52       C  
ATOM   6839  O   PRO A 451      -4.741  30.662 -36.772  1.00 19.31           O  
ANISOU 6839  O   PRO A 451     2531   2548   2256    -32   -134    -30       O  
ATOM   6840  CB  PRO A 451      -3.612  29.097 -34.316  1.00 18.63           C  
ANISOU 6840  CB  PRO A 451     2438   2409   2230    -10    -83    -52       C  
ATOM   6841  CG  PRO A 451      -3.176  27.688 -34.303  1.00 19.00           C  
ANISOU 6841  CG  PRO A 451     2496   2442   2283    -23    -58    -75       C  
ATOM   6842  CD  PRO A 451      -4.436  26.863 -34.170  1.00 16.33           C  
ANISOU 6842  CD  PRO A 451     2148   2112   1945    -41    -66    -85       C  
ATOM   6843  HA  PRO A 451      -5.561  29.722 -34.539  1.00 20.26           H  
ATOM   6844  HB2 PRO A 451      -2.994  29.645 -34.825  1.00 22.35           H  
ATOM   6845  HB3 PRO A 451      -3.696  29.441 -33.414  1.00 22.35           H  
ATOM   6846  HG2 PRO A 451      -2.717  27.480 -35.132  1.00 22.81           H  
ATOM   6847  HG3 PRO A 451      -2.585  27.536 -33.550  1.00 22.81           H  
ATOM   6848  HD2 PRO A 451      -4.347  26.019 -34.639  1.00 19.60           H  
ATOM   6849  HD3 PRO A 451      -4.647  26.704 -33.236  1.00 19.60           H  
ATOM   6850  N   ALA A 452      -5.004  28.508 -37.380  1.00 15.32           N  
ANISOU 6850  N   ALA A 452     2034   2047   1739    -72   -109    -73       N  
ATOM   6851  CA  ALA A 452      -5.022  28.788 -38.807  1.00 16.71           C  
ANISOU 6851  CA  ALA A 452     2222   2248   1879    -93   -120    -73       C  
ATOM   6852  C   ALA A 452      -6.426  29.002 -39.355  1.00 20.87           C  
ANISOU 6852  C   ALA A 452     2735   2808   2387   -106   -151    -66       C  
ATOM   6853  O   ALA A 452      -6.565  29.292 -40.547  1.00 18.87           O  
ANISOU 6853  O   ALA A 452     2489   2580   2099   -125   -165    -62       O  
ATOM   6854  CB  ALA A 452      -4.348  27.643 -39.571  1.00 19.26           C  
ANISOU 6854  CB  ALA A 452     2566   2567   2186   -116    -94   -104       C  
ATOM   6855  H   ALA A 452      -5.068  27.672 -37.189  1.00 18.38           H  
ATOM   6856  HA  ALA A 452      -4.515  29.599 -38.967  1.00 20.05           H  
ATOM   6857  HB1 ALA A 452      -4.478  27.780 -40.523  1.00 23.12           H  
ATOM   6858  HB2 ALA A 452      -3.400  27.640 -39.364  1.00 23.12           H  
ATOM   6859  HB3 ALA A 452      -4.749  26.803 -39.300  1.00 23.12           H  
ATOM   6860  N   SER A 453      -7.462  28.851 -38.518  1.00 14.68           N  
ANISOU 6860  N   SER A 453     1928   2030   1620    -99   -162    -63       N  
ATOM   6861  CA  SER A 453      -8.848  28.967 -38.956  1.00 16.63           C  
ANISOU 6861  CA  SER A 453     2154   2315   1851   -111   -192    -58       C  
ATOM   6862  C   SER A 453      -9.271  30.409 -39.196  1.00 16.59           C  
ANISOU 6862  C   SER A 453     2138   2328   1839    -86   -223    -27       C  
ATOM   6863  O   SER A 453     -10.278  30.644 -39.876  1.00 16.39           O  
ANISOU 6863  O   SER A 453     2097   2338   1791    -95   -251    -18       O  
ATOM   6864  CB  SER A 453      -9.785  28.362 -37.906  1.00 19.13           C  
ANISOU 6864  CB  SER A 453     2445   2637   2188   -111   -192    -64       C  
ATOM   6865  OG  SER A 453      -9.877  29.220 -36.776  1.00 18.48           O  
ANISOU 6865  OG  SER A 453     2343   2546   2131    -72   -197    -46       O  
ATOM   6866  H   SER A 453      -7.384  28.678 -37.679  1.00 17.62           H  
ATOM   6867  HA  SER A 453      -8.938  28.474 -39.787  1.00 19.96           H  
ATOM   6868  HB2 SER A 453     -10.667  28.250 -38.294  1.00 22.96           H  
ATOM   6869  HB3 SER A 453      -9.434  27.502 -37.625  1.00 22.96           H  
ATOM   6870  HG  SER A 453     -10.680  29.426 -36.637  1.00 22.17           H  
ATOM   6871  N   ASN A 454      -8.558  31.368 -38.608  1.00 17.27           N  
ANISOU 6871  N   ASN A 454     2230   2388   1943    -54   -222     -9       N  
ATOM   6872  CA  ASN A 454      -8.886  32.791 -38.693  1.00 14.25           C  
ANISOU 6872  CA  ASN A 454     1844   2010   1559    -24   -252     20       C  
ATOM   6873  C   ASN A 454     -10.227  33.135 -38.047  1.00 18.37           C  
ANISOU 6873  C   ASN A 454     2332   2555   2094      1   -275     27       C  
ATOM   6874  O   ASN A 454     -10.758  34.227 -38.270  1.00 21.55           O  
ANISOU 6874  O   ASN A 454     2729   2967   2493     27   -306     49       O  
ATOM   6875  CB  ASN A 454      -8.821  33.246 -40.151  1.00 15.80           C  
ANISOU 6875  CB  ASN A 454     2058   2227   1719    -44   -272     35       C  
ATOM   6876  CG  ASN A 454      -7.415  33.184 -40.689  1.00 17.78           C  
ANISOU 6876  CG  ASN A 454     2339   2459   1958    -63   -249     32       C  
ATOM   6877  OD1 ASN A 454      -6.471  33.534 -39.983  1.00 19.02           O  
ANISOU 6877  OD1 ASN A 454     2506   2584   2136    -46   -233     36       O  
ATOM   6878  ND2 ASN A 454      -7.256  32.699 -41.916  1.00 15.49           N  
ANISOU 6878  ND2 ASN A 454     2061   2193   1632    -97   -246     24       N  
ATOM   6879  H   ASN A 454      -7.855  31.212 -38.138  1.00 20.72           H  
ATOM   6880  HA  ASN A 454      -8.231  33.300 -38.190  1.00 17.10           H  
ATOM   6881  HB2 ASN A 454      -9.380  32.667 -40.692  1.00 18.96           H  
ATOM   6882  HB3 ASN A 454      -9.132  34.162 -40.215  1.00 18.96           H  
ATOM   6883 HD21 ASN A 454      -6.469  32.647 -42.259  1.00 18.59           H  
ATOM   6884 HD22 ASN A 454      -7.940  32.438 -42.367  1.00 18.59           H  
ATOM   6885  N   GLU A 455     -10.733  32.262 -37.171  1.00 17.64           N  
ANISOU 6885  N   GLU A 455     2217   2469   2017     -3   -261      9       N  
ATOM   6886  CA  GLU A 455     -11.942  32.525 -36.396  1.00 21.34           C  
ANISOU 6886  CA  GLU A 455     2648   2964   2498     22   -277     13       C  
ATOM   6887  C   GLU A 455     -11.611  33.431 -35.216  1.00 17.50           C  
ANISOU 6887  C   GLU A 455     2159   2450   2039     67   -274     20       C  
ATOM   6888  O   GLU A 455     -10.827  33.043 -34.342  1.00 21.17           O  
ANISOU 6888  O   GLU A 455     2634   2885   2523     68   -247     10       O  
ATOM   6889  CB  GLU A 455     -12.536  31.211 -35.887  1.00 22.59           C  
ANISOU 6889  CB  GLU A 455     2785   3141   2659     -7   -260     -8       C  
ATOM   6890  CG  GLU A 455     -12.926  30.236 -36.975  1.00 26.91           C  
ANISOU 6890  CG  GLU A 455     3335   3711   3177    -56   -263    -20       C  
ATOM   6891  CD  GLU A 455     -14.241  30.594 -37.596  1.00 83.62           C  
ANISOU 6891  CD  GLU A 455    10486  10948  10338    -58   -297    -10       C  
ATOM   6892  OE1 GLU A 455     -15.156  30.963 -36.831  1.00 36.79           O  
ANISOU 6892  OE1 GLU A 455     4517   5044   4419    -32   -309     -3       O  
ATOM   6893  OE2 GLU A 455     -14.351  30.521 -38.837  1.00 33.23           O  
ANISOU 6893  OE2 GLU A 455     4115   4585   3927    -84   -312     -8       O  
ATOM   6894  H   GLU A 455     -10.384  31.493 -37.006  1.00 21.17           H  
ATOM   6895  HA  GLU A 455     -12.590  32.971 -36.962  1.00 25.61           H  
ATOM   6896  HB2 GLU A 455     -11.880  30.774 -35.322  1.00 27.11           H  
ATOM   6897  HB3 GLU A 455     -13.335  31.412 -35.374  1.00 27.11           H  
ATOM   6898  HG2 GLU A 455     -12.249  30.244 -37.670  1.00 32.29           H  
ATOM   6899  HG3 GLU A 455     -13.001  29.346 -36.596  1.00 32.29           H  
ATOM   6900  N   ARG A 456     -12.201  34.629 -35.186  1.00 20.95           N  
ANISOU 6900  N   ARG A 456     2586   2896   2479    106   -303     38       N  
ATOM   6901  CA  ARG A 456     -11.923  35.605 -34.139  1.00 17.96           C  
ANISOU 6901  CA  ARG A 456     2210   2489   2125    152   -304     42       C  
ATOM   6902  C   ARG A 456     -12.831  35.389 -32.934  1.00 16.89           C  
ANISOU 6902  C   ARG A 456     2035   2379   2005    174   -299     30       C  
ATOM   6903  O   ARG A 456     -14.020  35.090 -33.082  1.00 17.51           O  
ANISOU 6903  O   ARG A 456     2076   2504   2072    173   -311     28       O  
ATOM   6904  CB  ARG A 456     -12.130  37.038 -34.640  1.00 18.08           C  
ANISOU 6904  CB  ARG A 456     2238   2495   2138    188   -339     66       C  
ATOM   6905  CG  ARG A 456     -11.329  37.443 -35.867  1.00 22.97           C  
ANISOU 6905  CG  ARG A 456     2896   3095   2738    166   -350     85       C  
ATOM   6906  CD  ARG A 456     -11.622  38.904 -36.228  1.00 25.59           C  
ANISOU 6906  CD  ARG A 456     3241   3412   3069    204   -388    111       C  
ATOM   6907  NE  ARG A 456     -10.871  39.352 -37.399  1.00 34.09           N  
ANISOU 6907  NE  ARG A 456     4355   4472   4124    179   -400    134       N  
ATOM   6908  CZ  ARG A 456      -9.632  39.835 -37.357  1.00 26.83           C  
ANISOU 6908  CZ  ARG A 456     3473   3511   3210    170   -391    144       C  
ATOM   6909  NH1 ARG A 456      -8.998  39.944 -36.203  1.00 19.09           N  
ANISOU 6909  NH1 ARG A 456     2499   2499   2256    184   -370    131       N  
ATOM   6910  NH2 ARG A 456      -9.027  40.218 -38.472  1.00 37.01           N  
ANISOU 6910  NH2 ARG A 456     4792   4794   4475    143   -402    166       N  
ATOM   6911  H   ARG A 456     -12.771  34.900 -35.771  1.00 25.15           H  
ATOM   6912  HA  ARG A 456     -10.998  35.491 -33.869  1.00 21.55           H  
ATOM   6913  HB2 ARG A 456     -13.068  37.148 -34.861  1.00 21.70           H  
ATOM   6914  HB3 ARG A 456     -11.885  37.646 -33.925  1.00 21.70           H  
ATOM   6915  HG2 ARG A 456     -10.381  37.353 -35.683  1.00 27.57           H  
ATOM   6916  HG3 ARG A 456     -11.577  36.882 -36.618  1.00 27.57           H  
ATOM   6917  HD2 ARG A 456     -12.567  39.000 -36.422  1.00 30.71           H  
ATOM   6918  HD3 ARG A 456     -11.378  39.471 -35.479  1.00 30.71           H  
ATOM   6919  HE  ARG A 456     -11.255  39.299 -38.166  1.00 40.90           H  
ATOM   6920 HH11 ARG A 456      -9.386  39.701 -35.475  1.00 22.91           H  
ATOM   6921 HH12 ARG A 456      -8.197  40.257 -36.180  1.00 22.91           H  
ATOM   6922 HH21 ARG A 456      -9.435  40.154 -39.226  1.00 44.41           H  
ATOM   6923 HH22 ARG A 456      -8.226  40.530 -38.441  1.00 44.41           H  
ATOM   6924  N   HIS A 457     -12.271  35.569 -31.741  1.00 18.92           N  
ANISOU 6924  N   HIS A 457     2296   2609   2283    194   -280     22       N  
ATOM   6925  CA  HIS A 457     -13.053  35.564 -30.511  1.00 18.00           C  
ANISOU 6925  CA  HIS A 457     2144   2517   2179    220   -275     11       C  
ATOM   6926  C   HIS A 457     -12.581  36.725 -29.651  1.00 18.68           C  
ANISOU 6926  C   HIS A 457     2245   2568   2284    266   -278     11       C  
ATOM   6927  O   HIS A 457     -11.458  36.703 -29.137  1.00 20.89           O  
ANISOU 6927  O   HIS A 457     2551   2810   2575    259   -260      8       O  
ATOM   6928  CB  HIS A 457     -12.909  34.247 -29.767  1.00 17.02           C  
ANISOU 6928  CB  HIS A 457     2007   2400   2059    186   -244     -4       C  
ATOM   6929  CG  HIS A 457     -13.422  33.068 -30.529  1.00 19.02           C  
ANISOU 6929  CG  HIS A 457     2249   2683   2295    139   -241     -7       C  
ATOM   6930  ND1 HIS A 457     -14.766  32.779 -30.633  1.00 21.32           N  
ANISOU 6930  ND1 HIS A 457     2498   3029   2573    133   -254     -9       N  
ATOM   6931  CD2 HIS A 457     -12.775  32.114 -31.237  1.00 22.87           C  
ANISOU 6931  CD2 HIS A 457     2762   3153   2774     95   -227    -11       C  
ATOM   6932  CE1 HIS A 457     -14.923  31.684 -31.356  1.00 25.00           C  
ANISOU 6932  CE1 HIS A 457     2966   3508   3024     82   -250    -13       C  
ATOM   6933  NE2 HIS A 457     -13.730  31.257 -31.730  1.00 23.66           N  
ANISOU 6933  NE2 HIS A 457     2839   3293   2858     60   -233    -16       N  
ATOM   6934  H   HIS A 457     -11.430  35.698 -31.619  1.00 22.70           H  
ATOM   6935  HA  HIS A 457     -13.990  35.695 -30.723  1.00 21.60           H  
ATOM   6936  HB2 HIS A 457     -11.969  34.094 -29.583  1.00 20.42           H  
ATOM   6937  HB3 HIS A 457     -13.405  34.302 -28.936  1.00 20.42           H  
ATOM   6938  HD1 HIS A 457     -15.403  33.239 -30.283  1.00 25.58           H  
ATOM   6939  HD2 HIS A 457     -11.856  32.049 -31.366  1.00 27.44           H  
ATOM   6940  HE1 HIS A 457     -15.735  31.282 -31.566  1.00 30.00           H  
ATOM   6941  HE2 HIS A 457     -13.576  30.557 -32.205  1.00 28.39           H  
ATOM   6942  N   VAL A 458     -13.438  37.727 -29.489  1.00 20.19           N  
ANISOU 6942  N   VAL A 458     2418   2774   2477    314   -303     13       N  
ATOM   6943  CA  VAL A 458     -13.164  38.878 -28.638  1.00 18.56           C  
ANISOU 6943  CA  VAL A 458     2227   2537   2289    362   -309      9       C  
ATOM   6944  C   VAL A 458     -14.052  38.765 -27.408  1.00 18.16           C  
ANISOU 6944  C   VAL A 458     2133   2525   2244    391   -299    -11       C  
ATOM   6945  O   VAL A 458     -15.274  38.615 -27.523  1.00 21.50           O  
ANISOU 6945  O   VAL A 458     2512   3001   2658    405   -310    -14       O  
ATOM   6946  CB  VAL A 458     -13.400  40.203 -29.383  1.00 19.06           C  
ANISOU 6946  CB  VAL A 458     2311   2580   2353    400   -347     25       C  
ATOM   6947  CG1 VAL A 458     -13.157  41.407 -28.458  1.00 24.17           C  
ANISOU 6947  CG1 VAL A 458     2977   3188   3018    451   -354     17       C  
ATOM   6948  CG2 VAL A 458     -12.482  40.286 -30.595  1.00 23.89           C  
ANISOU 6948  CG2 VAL A 458     2966   3159   2954    365   -355     47       C  
ATOM   6949  H   VAL A 458     -14.206  37.761 -29.874  1.00 24.22           H  
ATOM   6950  HA  VAL A 458     -12.238  38.863 -28.352  1.00 22.27           H  
ATOM   6951  HB  VAL A 458     -14.323  40.232 -29.680  1.00 22.88           H  
ATOM   6952 HG11 VAL A 458     -13.277  42.224 -28.966  1.00 29.00           H  
ATOM   6953 HG12 VAL A 458     -13.792  41.376 -27.726  1.00 29.00           H  
ATOM   6954 HG13 VAL A 458     -12.252  41.362 -28.113  1.00 29.00           H  
ATOM   6955 HG21 VAL A 458     -12.717  41.069 -31.116  1.00 28.67           H  
ATOM   6956 HG22 VAL A 458     -11.563  40.355 -30.291  1.00 28.67           H  
ATOM   6957 HG23 VAL A 458     -12.593  39.486 -31.131  1.00 28.67           H  
ATOM   6958  N   PHE A 459     -13.437  38.837 -26.238  1.00 16.14           N  
ANISOU 6958  N   PHE A 459     1885   2247   1999    399   -278    -24       N  
ATOM   6959  CA  PHE A 459     -14.165  38.638 -24.996  1.00 16.14           C  
ANISOU 6959  CA  PHE A 459     1844   2288   2001    420   -264    -44       C  
ATOM   6960  C   PHE A 459     -15.324  39.617 -24.884  1.00 17.93           C  
ANISOU 6960  C   PHE A 459     2043   2543   2228    481   -288    -51       C  
ATOM   6961  O   PHE A 459     -15.146  40.833 -24.994  1.00 21.97           O  
ANISOU 6961  O   PHE A 459     2582   3016   2748    524   -309    -51       O  
ATOM   6962  CB  PHE A 459     -13.206  38.797 -23.821  1.00 18.76           C  
ANISOU 6962  CB  PHE A 459     2197   2586   2344    424   -243    -55       C  
ATOM   6963  CG  PHE A 459     -13.846  38.592 -22.488  1.00 20.34           C  
ANISOU 6963  CG  PHE A 459     2358   2828   2541    442   -226    -75       C  
ATOM   6964  CD1 PHE A 459     -13.935  37.326 -21.942  1.00 26.49           C  
ANISOU 6964  CD1 PHE A 459     3112   3641   3313    401   -200    -76       C  
ATOM   6965  CD2 PHE A 459     -14.360  39.660 -21.775  1.00 30.18           C  
ANISOU 6965  CD2 PHE A 459     3595   4081   3792    500   -236    -93       C  
ATOM   6966  CE1 PHE A 459     -14.529  37.128 -20.710  1.00 22.52           C  
ANISOU 6966  CE1 PHE A 459     2572   3182   2804    413   -184    -92       C  
ATOM   6967  CE2 PHE A 459     -14.949  39.465 -20.541  1.00 24.82           C  
ANISOU 6967  CE2 PHE A 459     2877   3448   3106    516   -218   -114       C  
ATOM   6968  CZ  PHE A 459     -15.035  38.197 -20.012  1.00 19.03           C  
ANISOU 6968  CZ  PHE A 459     2116   2753   2363    470   -191   -111       C  
ATOM   6969  H   PHE A 459     -12.599  39.000 -26.134  1.00 19.36           H  
ATOM   6970  HA  PHE A 459     -14.538  37.743 -24.974  1.00 19.37           H  
ATOM   6971  HB2 PHE A 459     -12.493  38.146 -23.910  1.00 22.51           H  
ATOM   6972  HB3 PHE A 459     -12.840  39.695 -23.837  1.00 22.51           H  
ATOM   6973  HD1 PHE A 459     -13.592  36.599 -22.409  1.00 31.79           H  
ATOM   6974  HD2 PHE A 459     -14.308  40.518 -22.130  1.00 36.22           H  
ATOM   6975  HE1 PHE A 459     -14.587  36.271 -20.354  1.00 27.03           H  
ATOM   6976  HE2 PHE A 459     -15.288  40.190 -20.068  1.00 29.78           H  
ATOM   6977  HZ  PHE A 459     -15.435  38.065 -19.183  1.00 22.84           H  
ATOM   6978  N   ASP A 460     -16.511  39.072 -24.655  1.00 23.05           N  
ANISOU 6978  N   ASP A 460     2635   3259   2864    483   -284    -59       N  
ATOM   6979  CA  ASP A 460     -17.747  39.836 -24.480  1.00 25.15           C  
ANISOU 6979  CA  ASP A 460     2861   3568   3127    542   -303    -69       C  
ATOM   6980  C   ASP A 460     -18.225  39.562 -23.062  1.00 26.25           C  
ANISOU 6980  C   ASP A 460     2958   3753   3263    556   -278    -92       C  
ATOM   6981  O   ASP A 460     -18.654  38.429 -22.768  1.00 26.55           O  
ANISOU 6981  O   ASP A 460     2958   3841   3287    513   -258    -93       O  
ATOM   6982  CB  ASP A 460     -18.778  39.404 -25.522  1.00 31.83           C  
ANISOU 6982  CB  ASP A 460     3669   4468   3958    528   -322    -55       C  
ATOM   6983  CG  ASP A 460     -20.092  40.153 -25.407  1.00 32.41           C  
ANISOU 6983  CG  ASP A 460     3694   4594   4027    592   -343    -63       C  
ATOM   6984  OD1 ASP A 460     -20.262  40.937 -24.454  1.00 39.96           O  
ANISOU 6984  OD1 ASP A 460     4643   5548   4993    648   -340    -84       O  
ATOM   6985  OD2 ASP A 460     -20.965  39.955 -26.281  1.00 50.92           O  
ANISOU 6985  OD2 ASP A 460     6005   6984   6358    587   -363    -50       O  
ATOM   6986  H   ASP A 460     -16.635  38.223 -24.593  1.00 27.66           H  
ATOM   6987  HA  ASP A 460     -17.611  40.790 -24.594  1.00 30.18           H  
ATOM   6988  HB2 ASP A 460     -18.417  39.568 -26.407  1.00 38.20           H  
ATOM   6989  HB3 ASP A 460     -18.963  38.459 -25.409  1.00 38.20           H  
ATOM   6990  N   PRO A 461     -18.135  40.522 -22.139  1.00 38.81           N  
ANISOU 6990  N   PRO A 461     4557   5326   4863    610   -277   -113       N  
ATOM   6991  CA  PRO A 461     -18.422  40.190 -20.730  1.00 52.27           C  
ANISOU 6991  CA  PRO A 461     6227   7074   6560    616   -249   -136       C  
ATOM   6992  C   PRO A 461     -19.809  39.606 -20.528  1.00 51.51           C  
ANISOU 6992  C   PRO A 461     6057   7071   6445    616   -243   -142       C  
ATOM   6993  O   PRO A 461     -19.977  38.679 -19.725  1.00 50.28           O  
ANISOU 6993  O   PRO A 461     5870   6959   6276    579   -215   -146       O  
ATOM   6994  CB  PRO A 461     -18.243  41.534 -20.006  1.00 65.66           C  
ANISOU 6994  CB  PRO A 461     7945   8736   8268    684   -257   -160       C  
ATOM   6995  CG  PRO A 461     -18.372  42.573 -21.071  1.00 53.81           C  
ANISOU 6995  CG  PRO A 461     6472   7194   6778    725   -294   -150       C  
ATOM   6996  CD  PRO A 461     -17.865  41.957 -22.338  1.00 41.25           C  
ANISOU 6996  CD  PRO A 461     4906   5579   5187    669   -304   -117       C  
ATOM   6997  HA  PRO A 461     -17.761  39.565 -20.396  1.00 62.73           H  
ATOM   6998  HB2 PRO A 461     -18.934  41.640 -19.333  1.00 78.79           H  
ATOM   6999  HB3 PRO A 461     -17.367  41.570 -19.591  1.00 78.79           H  
ATOM   7000  HG2 PRO A 461     -19.303  42.827 -21.165  1.00 64.57           H  
ATOM   7001  HG3 PRO A 461     -17.839  43.348 -20.833  1.00 64.57           H  
ATOM   7002  HD2 PRO A 461     -18.350  42.298 -23.106  1.00 49.50           H  
ATOM   7003  HD3 PRO A 461     -16.915  42.120 -22.446  1.00 49.50           H  
ATOM   7004  N   ALA A 462     -20.809  40.108 -21.248  1.00 49.82           N  
ANISOU 7004  N   ALA A 462     5812   6890   6227    655   -269   -139       N  
ATOM   7005  CA  ALA A 462     -22.141  39.521 -21.182  1.00 50.62           C  
ANISOU 7005  CA  ALA A 462     5846   7077   6308    640   -261   -140       C  
ATOM   7006  C   ALA A 462     -22.120  38.073 -21.659  1.00 52.47           C  
ANISOU 7006  C   ALA A 462     6062   7346   6530    564   -253   -120       C  
ATOM   7007  O   ALA A 462     -22.519  37.154 -20.936  1.00 61.75           O  
ANISOU 7007  O   ALA A 462     7197   8575   7689    525   -229   -124       O  
ATOM   7008  CB  ALA A 462     -23.113  40.354 -22.020  1.00 57.75           C  
ANISOU 7008  CB  ALA A 462     6741   7989   7212    678   -287   -134       C  
ATOM   7009  H   ALA A 462     -20.744  40.783 -21.778  1.00 59.78           H  
ATOM   7010  HA  ALA A 462     -22.448  39.531 -20.262  1.00 60.74           H  
ATOM   7011  HB1 ALA A 462     -23.955  39.878 -22.092  1.00 69.30           H  
ATOM   7012  HB2 ALA A 462     -23.252  41.209 -21.585  1.00 69.30           H  
ATOM   7013  HB3 ALA A 462     -22.733  40.489 -22.903  1.00 69.30           H  
ATOM   7014  N   ARG A 463     -21.623  37.852 -22.874  1.00 34.32           N  
ANISOU 7014  N   ARG A 463     3801   5004   4236    530   -270    -99       N  
ATOM   7015  CA  ARG A 463     -21.760  36.564 -23.539  1.00 27.83           C  
ANISOU 7015  CA  ARG A 463     2969   4206   3400    455   -265    -82       C  
ATOM   7016  C   ARG A 463     -20.817  35.500 -22.988  1.00 45.66           C  
ANISOU 7016  C   ARG A 463     5256   6431   5661    393   -234    -79       C  
ATOM   7017  O   ARG A 463     -21.153  34.311 -23.036  1.00 46.27           O  
ANISOU 7017  O   ARG A 463     5313   6544   5725    332   -222    -72       O  
ATOM   7018  CB  ARG A 463     -21.525  36.764 -25.042  1.00 37.06           C  
ANISOU 7018  CB  ARG A 463     4170   5339   4570    445   -294    -62       C  
ATOM   7019  CG  ARG A 463     -21.593  35.513 -25.905  1.00 46.49           C  
ANISOU 7019  CG  ARG A 463     5363   6549   5750    368   -292    -48       C  
ATOM   7020  CD  ARG A 463     -20.955  35.770 -27.277  1.00 35.22           C  
ANISOU 7020  CD  ARG A 463     3986   5071   4326    357   -314    -32       C  
ATOM   7021  NE  ARG A 463     -19.519  36.010 -27.155  1.00 57.19           N  
ANISOU 7021  NE  ARG A 463     6833   7772   7126    355   -302    -31       N  
ATOM   7022  CZ  ARG A 463     -18.783  36.681 -28.037  1.00 45.76           C  
ANISOU 7022  CZ  ARG A 463     5433   6270   5684    366   -320    -19       C  
ATOM   7023  NH1 ARG A 463     -19.339  37.199 -29.124  1.00 46.33           N  
ANISOU 7023  NH1 ARG A 463     5499   6357   5746    382   -352     -5       N  
ATOM   7024  NH2 ARG A 463     -17.486  36.843 -27.822  1.00 33.77           N  
ANISOU 7024  NH2 ARG A 463     3966   4686   4180    360   -306    -19       N  
ATOM   7025  H   ARG A 463     -21.198  38.438 -23.339  1.00 41.19           H  
ATOM   7026  HA  ARG A 463     -22.659  36.227 -23.399  1.00 33.40           H  
ATOM   7027  HB2 ARG A 463     -22.198  37.378 -25.374  1.00 44.47           H  
ATOM   7028  HB3 ARG A 463     -20.640  37.145 -25.161  1.00 44.47           H  
ATOM   7029  HG2 ARG A 463     -21.112  34.792 -25.471  1.00 55.78           H  
ATOM   7030  HG3 ARG A 463     -22.520  35.261 -26.038  1.00 55.78           H  
ATOM   7031  HD2 ARG A 463     -21.090  34.995 -27.845  1.00 42.27           H  
ATOM   7032  HD3 ARG A 463     -21.363  36.552 -27.680  1.00 42.27           H  
ATOM   7033  HE  ARG A 463     -19.119  35.693 -26.463  1.00 68.63           H  
ATOM   7034 HH11 ARG A 463     -20.181  37.102 -29.264  1.00 55.59           H  
ATOM   7035 HH12 ARG A 463     -18.856  37.632 -29.689  1.00 55.59           H  
ATOM   7036 HH21 ARG A 463     -17.123  36.515 -27.115  1.00 40.53           H  
ATOM   7037 HH22 ARG A 463     -17.007  37.276 -28.389  1.00 40.53           H  
ATOM   7038  N   ASP A 464     -19.657  35.888 -22.457  1.00 35.51           N  
ANISOU 7038  N   ASP A 464     4020   5080   4392    406   -223    -84       N  
ATOM   7039  CA  ASP A 464     -18.580  34.938 -22.199  1.00 34.42           C  
ANISOU 7039  CA  ASP A 464     3919   4900   4259    350   -199    -77       C  
ATOM   7040  C   ASP A 464     -18.362  34.630 -20.720  1.00 36.66           C  
ANISOU 7040  C   ASP A 464     4191   5196   4541    346   -171    -88       C  
ATOM   7041  O   ASP A 464     -17.395  33.939 -20.386  1.00 33.82           O  
ANISOU 7041  O   ASP A 464     3864   4798   4188    309   -153    -81       O  
ATOM   7042  CB  ASP A 464     -17.268  35.445 -22.816  1.00 26.84           C  
ANISOU 7042  CB  ASP A 464     3024   3857   3316    355   -207    -70       C  
ATOM   7043  CG  ASP A 464     -17.298  35.450 -24.332  1.00 30.15           C  
ANISOU 7043  CG  ASP A 464     3461   4263   3732    340   -230    -55       C  
ATOM   7044  OD1 ASP A 464     -17.969  34.575 -24.918  1.00 38.74           O  
ANISOU 7044  OD1 ASP A 464     4523   5389   4805    300   -232    -49       O  
ATOM   7045  OD2 ASP A 464     -16.664  36.337 -24.940  1.00 24.49           O  
ANISOU 7045  OD2 ASP A 464     2783   3497   3024    365   -247    -50       O  
ATOM   7046  H   ASP A 464     -19.472  36.699 -22.239  1.00 42.61           H  
ATOM   7047  HA  ASP A 464     -18.827  34.104 -22.627  1.00 41.30           H  
ATOM   7048  HB2 ASP A 464     -17.107  36.353 -22.516  1.00 32.21           H  
ATOM   7049  HB3 ASP A 464     -16.541  34.869 -22.532  1.00 32.21           H  
ATOM   7050  N   ALA A 465     -19.240  35.085 -19.823  1.00 78.13           N  
ANISOU 7050  N   ALA A 465     9397  10506   9784    384   -167   -104       N  
ATOM   7051  CA  ALA A 465     -19.077  34.722 -18.417  1.00 48.44           C  
ANISOU 7051  CA  ALA A 465     5624   6766   6017    375   -139   -113       C  
ATOM   7052  C   ALA A 465     -19.106  33.209 -18.231  1.00 28.63           C  
ANISOU 7052  C   ALA A 465     3104   4278   3497    300   -121    -96       C  
ATOM   7053  O   ALA A 465     -18.370  32.661 -17.401  1.00 42.62           O  
ANISOU 7053  O   ALA A 465     4895   6028   5269    273   -100    -92       O  
ATOM   7054  CB  ALA A 465     -20.160  35.378 -17.563  1.00 33.22           C  
ANISOU 7054  CB  ALA A 465     3639   4909   4074    425   -136   -135       C  
ATOM   7055  H   ALA A 465     -19.915  35.589 -19.995  1.00 93.76           H  
ATOM   7056  HA  ALA A 465     -18.217  35.053 -18.115  1.00 58.13           H  
ATOM   7057  HB1 ALA A 465     -19.930  36.310 -17.423  1.00 39.87           H  
ATOM   7058  HB2 ALA A 465     -21.010  35.313 -18.026  1.00 39.87           H  
ATOM   7059  HB3 ALA A 465     -20.212  34.919 -16.710  1.00 39.87           H  
ATOM   7060  N   GLY A 466     -19.943  32.513 -19.001  1.00 46.51           N  
ANISOU 7060  N   GLY A 466     5339   6582   5749    263   -129    -86       N  
ATOM   7061  CA  GLY A 466     -20.029  31.072 -18.877  1.00 51.91           C  
ANISOU 7061  CA  GLY A 466     6018   7282   6423    189   -115    -70       C  
ATOM   7062  C   GLY A 466     -18.736  30.354 -19.185  1.00 34.93           C  
ANISOU 7062  C   GLY A 466     3930   5053   4290    150   -107    -57       C  
ATOM   7063  O   GLY A 466     -18.543  29.218 -18.738  1.00 49.47           O  
ANISOU 7063  O   GLY A 466     5778   6892   6127     96    -92    -45       O  
ATOM   7064  H   GLY A 466     -20.465  32.853 -19.594  1.00 55.81           H  
ATOM   7065  HA2 GLY A 466     -20.287  30.848 -17.969  1.00 62.29           H  
ATOM   7066  HA3 GLY A 466     -20.707  30.743 -19.488  1.00 62.29           H  
ATOM   7067  N   LEU A 467     -17.847  30.977 -19.951  1.00 24.94           N  
ANISOU 7067  N   LEU A 467     2711   3724   3042    175   -119    -58       N  
ATOM   7068  CA  LEU A 467     -16.566  30.345 -20.206  1.00 29.82           C  
ANISOU 7068  CA  LEU A 467     3384   4272   3675    144   -111    -48       C  
ATOM   7069  C   LEU A 467     -15.631  30.437 -19.009  1.00 25.58           C  
ANISOU 7069  C   LEU A 467     2866   3707   3146    155    -92    -50       C  
ATOM   7070  O   LEU A 467     -14.551  29.834 -19.047  1.00 35.36           O  
ANISOU 7070  O   LEU A 467     4145   4894   4396    131    -82    -40       O  
ATOM   7071  CB  LEU A 467     -15.891  30.963 -21.431  1.00 28.92           C  
ANISOU 7071  CB  LEU A 467     3310   4107   3573    162   -128    -48       C  
ATOM   7072  CG  LEU A 467     -16.505  30.616 -22.787  1.00 42.80           C  
ANISOU 7072  CG  LEU A 467     5063   5879   5322    137   -146    -44       C  
ATOM   7073  CD1 LEU A 467     -17.872  31.255 -22.943  1.00 43.59           C  
ANISOU 7073  CD1 LEU A 467     5109   6044   5407    166   -164    -49       C  
ATOM   7074  CD2 LEU A 467     -15.565  31.038 -23.913  1.00 35.54           C  
ANISOU 7074  CD2 LEU A 467     4191   4902   4412    145   -157    -40       C  
ATOM   7075  H   LEU A 467     -17.962  31.745 -20.322  1.00 29.93           H  
ATOM   7076  HA  LEU A 467     -16.718  29.408 -20.407  1.00 35.78           H  
ATOM   7077  HB2 LEU A 467     -15.926  31.928 -21.339  1.00 34.71           H  
ATOM   7078  HB3 LEU A 467     -14.968  30.665 -21.449  1.00 34.71           H  
ATOM   7079  HG  LEU A 467     -16.629  29.656 -22.845  1.00 51.37           H  
ATOM   7080 HD11 LEU A 467     -18.170  31.144 -23.860  1.00 52.30           H  
ATOM   7081 HD12 LEU A 467     -18.494  30.821 -22.338  1.00 52.30           H  
ATOM   7082 HD13 LEU A 467     -17.807  32.198 -22.729  1.00 52.30           H  
ATOM   7083 HD21 LEU A 467     -14.870  30.369 -24.012  1.00 42.65           H  
ATOM   7084 HD22 LEU A 467     -16.073  31.113 -24.737  1.00 42.65           H  
ATOM   7085 HD23 LEU A 467     -15.170  31.895 -23.690  1.00 42.65           H  
ATOM   7086  N   LEU A 468     -15.999  31.181 -17.965  1.00 25.64           N  
ANISOU 7086  N   LEU A 468     2846   3749   3146    193    -87    -62       N  
ATOM   7087  CA  LEU A 468     -15.116  31.389 -16.828  1.00 16.71           C  
ANISOU 7087  CA  LEU A 468     1734   2595   2020    206    -71    -65       C  
ATOM   7088  C   LEU A 468     -15.565  30.573 -15.625  1.00 20.44           C  
ANISOU 7088  C   LEU A 468     2174   3116   2475    176    -52    -59       C  
ATOM   7089  O   LEU A 468     -16.761  30.476 -15.333  1.00 25.66           O  
ANISOU 7089  O   LEU A 468     2786   3846   3118    173    -50    -63       O  
ATOM   7090  CB  LEU A 468     -15.036  32.860 -16.403  1.00 17.59           C  
ANISOU 7090  CB  LEU A 468     1846   2703   2135    270    -79    -86       C  
ATOM   7091  CG  LEU A 468     -14.664  33.888 -17.468  1.00 23.44           C  
ANISOU 7091  CG  LEU A 468     2617   3397   2891    306   -102    -91       C  
ATOM   7092  CD1 LEU A 468     -14.413  35.235 -16.815  1.00 27.56           C  
ANISOU 7092  CD1 LEU A 468     3150   3905   3417    363   -107   -111       C  
ATOM   7093  CD2 LEU A 468     -13.453  33.449 -18.261  1.00 19.58           C  
ANISOU 7093  CD2 LEU A 468     2178   2844   2417    275   -103    -75       C  
ATOM   7094  H   LEU A 468     -16.760  31.575 -17.898  1.00 30.77           H  
ATOM   7095  HA  LEU A 468     -14.233  31.094 -17.101  1.00 20.05           H  
ATOM   7096  HB2 LEU A 468     -15.906  33.116 -16.059  1.00 21.11           H  
ATOM   7097  HB3 LEU A 468     -14.369  32.929 -15.703  1.00 21.11           H  
ATOM   7098  HG  LEU A 468     -15.400  33.973 -18.094  1.00 28.12           H  
ATOM   7099 HD11 LEU A 468     -14.385  35.919 -17.503  1.00 33.07           H  
ATOM   7100 HD12 LEU A 468     -15.131  35.422 -16.191  1.00 33.07           H  
ATOM   7101 HD13 LEU A 468     -13.565  35.204 -16.345  1.00 33.07           H  
ATOM   7102 HD21 LEU A 468     -13.285  34.095 -18.965  1.00 23.50           H  
ATOM   7103 HD22 LEU A 468     -12.687  33.401 -17.667  1.00 23.50           H  
ATOM   7104 HD23 LEU A 468     -13.627  32.577 -18.647  1.00 23.50           H  
ATOM   7105  N   SER A 469     -14.594  30.020 -14.908  1.00 18.71           N  
ANISOU 7105  N   SER A 469     1982   2865   2262    154    -37    -48       N  
ATOM   7106  CA  SER A 469     -14.887  29.236 -13.723  1.00 19.70           C  
ANISOU 7106  CA  SER A 469     2084   3031   2369    122    -19    -37       C  
ATOM   7107  C   SER A 469     -13.755  29.392 -12.726  1.00 16.79           C  
ANISOU 7107  C   SER A 469     1742   2631   2005    132     -8    -35       C  
ATOM   7108  O   SER A 469     -12.581  29.373 -13.102  1.00 17.47           O  
ANISOU 7108  O   SER A 469     1873   2655   2112    133    -12    -28       O  
ATOM   7109  CB  SER A 469     -15.072  27.753 -14.057  1.00 20.11           C  
ANISOU 7109  CB  SER A 469     2141   3080   2420     56    -15    -13       C  
ATOM   7110  OG  SER A 469     -15.248  26.982 -12.881  1.00 21.37           O  
ANISOU 7110  OG  SER A 469     2284   3273   2563     22      1      3       O  
ATOM   7111  H   SER A 469     -13.756  30.086 -15.092  1.00 22.45           H  
ATOM   7112  HA  SER A 469     -15.704  29.569 -13.319  1.00 23.64           H  
ATOM   7113  HB2 SER A 469     -15.856  27.653 -14.619  1.00 24.13           H  
ATOM   7114  HB3 SER A 469     -14.285  27.436 -14.526  1.00 24.13           H  
ATOM   7115  HG  SER A 469     -15.310  27.487 -12.212  1.00 25.64           H  
ATOM   7116  N   GLY A 470     -14.116  29.513 -11.456  1.00 17.47           N  
ANISOU 7116  N   GLY A 470     1800   2768   2070    136      4    -39       N  
ATOM   7117  CA  GLY A 470     -13.142  29.535 -10.394  1.00 20.11           C  
ANISOU 7117  CA  GLY A 470     2155   3084   2403    138     15    -34       C  
ATOM   7118  C   GLY A 470     -12.984  28.216  -9.675  1.00 16.58           C  
ANISOU 7118  C   GLY A 470     1707   2646   1945     83     27     -4       C  
ATOM   7119  O   GLY A 470     -12.297  28.174  -8.649  1.00 16.22           O  
ANISOU 7119  O   GLY A 470     1672   2598   1893     82     36      3       O  
ATOM   7120  H   GLY A 470     -14.931  29.584 -11.191  1.00 20.96           H  
ATOM   7121  HA2 GLY A 470     -12.280  29.779 -10.764  1.00 24.14           H  
ATOM   7122  HA3 GLY A 470     -13.405  30.202  -9.740  1.00 24.14           H  
ATOM   7123  N   ALA A 471     -13.618  27.146 -10.160  1.00 15.11           N  
ANISOU 7123  N   ALA A 471     1512   2472   1758     37     27     15       N  
ATOM   7124  CA  ALA A 471     -13.649  25.862  -9.460  1.00 15.66           C  
ANISOU 7124  CA  ALA A 471     1581   2552   1816    -19     37     46       C  
ATOM   7125  C   ALA A 471     -12.419  25.051  -9.848  1.00 15.99           C  
ANISOU 7125  C   ALA A 471     1676   2515   1883    -39     34     68       C  
ATOM   7126  O   ALA A 471     -12.366  24.462 -10.929  1.00 19.42           O  
ANISOU 7126  O   ALA A 471     2132   2910   2335    -58     26     74       O  
ATOM   7127  CB  ALA A 471     -14.930  25.101  -9.783  1.00 21.35           C  
ANISOU 7127  CB  ALA A 471     2268   3322   2521    -64     38     56       C  
ATOM   7128  H   ALA A 471     -14.044  27.141 -10.907  1.00 18.14           H  
ATOM   7129  HA  ALA A 471     -13.613  26.031  -8.505  1.00 18.79           H  
ATOM   7130  HB1 ALA A 471     -14.907  24.241  -9.335  1.00 25.61           H  
ATOM   7131  HB2 ALA A 471     -15.690  25.617  -9.471  1.00 25.61           H  
ATOM   7132  HB3 ALA A 471     -14.988  24.973 -10.743  1.00 25.61           H  
ATOM   7133  N   ASN A 472     -11.431  25.021  -8.942  1.00 15.37           N  
ANISOU 7133  N   ASN A 472     1617   2417   1806    -32     39     80       N  
ATOM   7134  CA  ASN A 472     -10.129  24.383  -9.104  1.00 12.28           C  
ANISOU 7134  CA  ASN A 472     1272   1956   1438    -40     37    100       C  
ATOM   7135  C   ASN A 472      -9.648  24.524 -10.540  1.00 12.65           C  
ANISOU 7135  C   ASN A 472     1348   1946   1513    -24     27     88       C  
ATOM   7136  O   ASN A 472      -9.544  23.540 -11.290  1.00 15.15           O  
ANISOU 7136  O   ASN A 472     1688   2225   1844    -53     24    100       O  
ATOM   7137  CB  ASN A 472     -10.167  22.919  -8.698  1.00 14.98           C  
ANISOU 7137  CB  ASN A 472     1626   2288   1777    -93     40    136       C  
ATOM   7138  CG  ASN A 472      -8.791  22.383  -8.406  1.00 15.26           C  
ANISOU 7138  CG  ASN A 472     1701   2267   1831    -91     39    158       C  
ATOM   7139  OD1 ASN A 472      -7.881  23.143  -8.065  1.00 15.37           O  
ANISOU 7139  OD1 ASN A 472     1723   2269   1850    -54     39    149       O  
ATOM   7140  ND2 ASN A 472      -8.617  21.080  -8.569  1.00 14.65           N  
ANISOU 7140  ND2 ASN A 472     1650   2151   1765   -128     37    186       N  
ATOM   7141  H   ASN A 472     -11.501  25.392  -8.169  1.00 18.44           H  
ATOM   7142  HA  ASN A 472      -9.495  24.831  -8.522  1.00 14.74           H  
ATOM   7143  HB2 ASN A 472     -10.706  22.822  -7.898  1.00 17.98           H  
ATOM   7144  HB3 ASN A 472     -10.549  22.397  -9.421  1.00 17.98           H  
ATOM   7145 HD21 ASN A 472      -7.849  20.727  -8.415  1.00 17.58           H  
ATOM   7146 HD22 ASN A 472      -9.273  20.588  -8.829  1.00 17.58           H  
ATOM   7147  N   PRO A 473      -9.340  25.747 -10.942  1.00 13.04           N  
ANISOU 7147  N   PRO A 473     1399   1988   1568     21     22     62       N  
ATOM   7148  CA  PRO A 473      -8.834  25.985 -12.290  1.00 14.15           C  
ANISOU 7148  CA  PRO A 473     1566   2079   1731     36     12     52       C  
ATOM   7149  C   PRO A 473      -7.457  25.379 -12.497  1.00 14.10           C  
ANISOU 7149  C   PRO A 473     1599   2012   1746     32     14     67       C  
ATOM   7150  O   PRO A 473      -6.705  25.125 -11.553  1.00 13.98           O  
ANISOU 7150  O   PRO A 473     1591   1990   1730     31     19     82       O  
ATOM   7151  CB  PRO A 473      -8.750  27.518 -12.373  1.00 17.48           C  
ANISOU 7151  CB  PRO A 473     1981   2508   2151     83      6     26       C  
ATOM   7152  CG  PRO A 473      -9.520  28.038 -11.208  1.00 18.91           C  
ANISOU 7152  CG  PRO A 473     2126   2749   2308     95     11     16       C  
ATOM   7153  CD  PRO A 473      -9.401  26.984 -10.148  1.00 15.43           C  
ANISOU 7153  CD  PRO A 473     1681   2324   1856     59     23     42       C  
ATOM   7154  HA  PRO A 473      -9.455  25.637 -12.949  1.00 16.98           H  
ATOM   7155  HB2 PRO A 473      -7.822  27.796 -12.323  1.00 20.97           H  
ATOM   7156  HB3 PRO A 473      -9.143  27.820 -13.207  1.00 20.97           H  
ATOM   7157  HG2 PRO A 473      -9.134  28.876 -10.907  1.00 22.69           H  
ATOM   7158  HG3 PRO A 473     -10.447  28.172 -11.460  1.00 22.69           H  
ATOM   7159  HD2 PRO A 473      -8.593  27.104  -9.625  1.00 18.51           H  
ATOM   7160  HD3 PRO A 473     -10.177  26.986  -9.565  1.00 18.51           H  
ATOM   7161  N   VAL A 474      -7.103  25.221 -13.771  1.00 13.90           N  
ANISOU 7161  N   VAL A 474     1597   1946   1737     32      8     61       N  
ATOM   7162  CA  VAL A 474      -5.712  24.947 -14.098  1.00 12.61           C  
ANISOU 7162  CA  VAL A 474     1468   1731   1594     41     10     68       C  
ATOM   7163  C   VAL A 474      -4.822  25.957 -13.375  1.00 13.34           C  
ANISOU 7163  C   VAL A 474     1559   1825   1685     73     10     64       C  
ATOM   7164  O   VAL A 474      -5.072  27.167 -13.396  1.00 13.40           O  
ANISOU 7164  O   VAL A 474     1556   1851   1686     98      4     46       O  
ATOM   7165  CB  VAL A 474      -5.484  25.006 -15.617  1.00 14.43           C  
ANISOU 7165  CB  VAL A 474     1719   1929   1837     46      5     55       C  
ATOM   7166  CG1 VAL A 474      -4.003  24.822 -15.918  1.00 16.41           C  
ANISOU 7166  CG1 VAL A 474     1997   2133   2104     59      9     60       C  
ATOM   7167  CG2 VAL A 474      -6.283  23.946 -16.354  1.00 17.38           C  
ANISOU 7167  CG2 VAL A 474     2097   2297   2210     11      4     56       C  
ATOM   7168  H   VAL A 474      -7.635  25.267 -14.445  1.00 16.68           H  
ATOM   7169  HA  VAL A 474      -5.495  24.052 -13.794  1.00 15.13           H  
ATOM   7170  HB  VAL A 474      -5.784  25.872 -15.933  1.00 17.32           H  
ATOM   7171 HG11 VAL A 474      -3.870  24.851 -16.878  1.00 19.69           H  
ATOM   7172 HG12 VAL A 474      -3.504  25.537 -15.493  1.00 19.69           H  
ATOM   7173 HG13 VAL A 474      -3.714  23.964 -15.569  1.00 19.69           H  
ATOM   7174 HG21 VAL A 474      -6.179  24.079 -17.309  1.00 20.86           H  
ATOM   7175 HG22 VAL A 474      -5.951  23.070 -16.104  1.00 20.86           H  
ATOM   7176 HG23 VAL A 474      -7.218  24.029 -16.109  1.00 20.86           H  
ATOM   7177  N   ARG A 475      -3.771  25.461 -12.737  1.00 11.80           N  
ANISOU 7177  N   ARG A 475     1378   1609   1497     72     14     82       N  
ATOM   7178  CA  ARG A 475      -2.863  26.301 -11.965  1.00 10.52           C  
ANISOU 7178  CA  ARG A 475     1215   1451   1332     95     14     81       C  
ATOM   7179  C   ARG A 475      -1.447  25.941 -12.386  1.00 12.77           C  
ANISOU 7179  C   ARG A 475     1524   1694   1635    102     14     91       C  
ATOM   7180  O   ARG A 475      -1.027  24.795 -12.210  1.00 13.84           O  
ANISOU 7180  O   ARG A 475     1670   1809   1780     89     19    112       O  
ATOM   7181  CB  ARG A 475      -3.070  26.088 -10.464  1.00 12.91           C  
ANISOU 7181  CB  ARG A 475     1500   1789   1616     85     18     96       C  
ATOM   7182  CG  ARG A 475      -2.208  26.961  -9.604  1.00 14.53           C  
ANISOU 7182  CG  ARG A 475     1704   2004   1814    105     15     92       C  
ATOM   7183  CD  ARG A 475      -2.627  26.832  -8.159  1.00 17.93           C  
ANISOU 7183  CD  ARG A 475     2114   2478   2221     94     20    102       C  
ATOM   7184  NE  ARG A 475      -2.137  25.647  -7.453  1.00 14.46           N  
ANISOU 7184  NE  ARG A 475     1680   2032   1781     73     23    137       N  
ATOM   7185  CZ  ARG A 475      -2.911  24.709  -6.899  1.00 16.09           C  
ANISOU 7185  CZ  ARG A 475     1877   2260   1976     44     28    157       C  
ATOM   7186  NH1 ARG A 475      -4.236  24.766  -7.015  1.00 13.67           N  
ANISOU 7186  NH1 ARG A 475     1551   1988   1656     31     32    146       N  
ATOM   7187  NH2 ARG A 475      -2.351  23.708  -6.226  1.00 16.36           N  
ANISOU 7187  NH2 ARG A 475     1921   2283   2010     27     27    192       N  
ATOM   7188  H   ARG A 475      -3.561  24.628 -12.736  1.00 14.16           H  
ATOM   7189  HA  ARG A 475      -3.013  27.241 -12.152  1.00 12.63           H  
ATOM   7190  HB2 ARG A 475      -3.996  26.280 -10.248  1.00 15.49           H  
ATOM   7191  HB3 ARG A 475      -2.864  25.164 -10.250  1.00 15.49           H  
ATOM   7192  HG2 ARG A 475      -1.281  26.688  -9.685  1.00 17.44           H  
ATOM   7193  HG3 ARG A 475      -2.307  27.887  -9.875  1.00 17.44           H  
ATOM   7194  HD2 ARG A 475      -2.300  27.608  -7.677  1.00 21.52           H  
ATOM   7195  HD3 ARG A 475      -3.596  26.805  -8.124  1.00 21.52           H  
ATOM   7196  HE  ARG A 475      -1.285  25.547  -7.391  1.00 17.35           H  
ATOM   7197 HH11 ARG A 475      -4.603  25.410  -7.450  1.00 16.40           H  
ATOM   7198 HH12 ARG A 475      -4.726  24.157  -6.655  1.00 16.40           H  
ATOM   7199 HH21 ARG A 475      -1.495  23.667  -6.149  1.00 19.63           H  
ATOM   7200 HH22 ARG A 475      -2.845  23.102  -5.868  1.00 19.63           H  
ATOM   7201  N   ARG A 476      -0.721  26.894 -12.957  1.00 11.75           N  
ANISOU 7201  N   ARG A 476     1402   1551   1511    122     10     78       N  
ATOM   7202  CA  ARG A 476       0.610  26.615 -13.504  1.00 13.83           C  
ANISOU 7202  CA  ARG A 476     1683   1782   1790    130     12     85       C  
ATOM   7203  C   ARG A 476       1.288  27.954 -13.789  1.00 13.25           C  
ANISOU 7203  C   ARG A 476     1612   1708   1714    147      6     71       C  
ATOM   7204  O   ARG A 476       0.819  29.007 -13.340  1.00 13.64           O  
ANISOU 7204  O   ARG A 476     1653   1777   1751    155     -2     58       O  
ATOM   7205  CB  ARG A 476       0.516  25.701 -14.735  1.00 14.63           C  
ANISOU 7205  CB  ARG A 476     1801   1854   1905    121     17     83       C  
ATOM   7206  CG  ARG A 476      -0.101  26.333 -15.991  1.00 12.31           C  
ANISOU 7206  CG  ARG A 476     1511   1559   1609    122     12     62       C  
ATOM   7207  CD  ARG A 476      -0.313  25.322 -17.104  1.00 14.02           C  
ANISOU 7207  CD  ARG A 476     1743   1751   1834    107     16     58       C  
ATOM   7208  NE  ARG A 476       0.914  24.597 -17.399  1.00 13.51           N  
ANISOU 7208  NE  ARG A 476     1695   1656   1784    114     25     65       N  
ATOM   7209  CZ  ARG A 476       0.958  23.464 -18.086  1.00 12.05           C  
ANISOU 7209  CZ  ARG A 476     1528   1444   1608    105     31     63       C  
ATOM   7210  NH1 ARG A 476      -0.157  22.927 -18.565  1.00 14.91           N  
ANISOU 7210  NH1 ARG A 476     1895   1805   1967     83     29     56       N  
ATOM   7211  NH2 ARG A 476       2.122  22.862 -18.286  1.00 14.52           N  
ANISOU 7211  NH2 ARG A 476     1852   1730   1933    119     39     68       N  
ATOM   7212  H   ARG A 476      -0.975  27.711 -13.040  1.00 14.10           H  
ATOM   7213  HA  ARG A 476       1.144  26.158 -12.836  1.00 16.60           H  
ATOM   7214  HB2 ARG A 476       1.413  25.413 -14.969  1.00 17.56           H  
ATOM   7215  HB3 ARG A 476      -0.028  24.933 -14.503  1.00 17.56           H  
ATOM   7216  HG2 ARG A 476      -0.963  26.715 -15.763  1.00 14.78           H  
ATOM   7217  HG3 ARG A 476       0.492  27.025 -16.322  1.00 14.78           H  
ATOM   7218  HD2 ARG A 476      -0.989  24.682 -16.833  1.00 16.83           H  
ATOM   7219  HD3 ARG A 476      -0.597  25.784 -17.908  1.00 16.83           H  
ATOM   7220  HE  ARG A 476       1.656  24.923 -17.110  1.00 16.22           H  
ATOM   7221 HH11 ARG A 476      -0.913  23.314 -18.430  1.00 17.90           H  
ATOM   7222 HH12 ARG A 476      -0.123  22.192 -19.010  1.00 17.90           H  
ATOM   7223 HH21 ARG A 476       2.844  23.206 -17.971  1.00 17.42           H  
ATOM   7224 HH22 ARG A 476       2.155  22.127 -18.732  1.00 17.42           H  
ATOM   7225  N   ASP A 477       2.415  27.931 -14.506  1.00 11.70           N  
ANISOU 7225  N   ASP A 477     1428   1489   1529    153      8     74       N  
ATOM   7226  CA  ASP A 477       3.154  29.169 -14.690  1.00 11.39           C  
ANISOU 7226  CA  ASP A 477     1391   1451   1485    162      0     65       C  
ATOM   7227  C   ASP A 477       3.399  29.542 -16.147  1.00 11.38           C  
ANISOU 7227  C   ASP A 477     1404   1432   1489    162     -1     55       C  
ATOM   7228  O   ASP A 477       3.883  30.647 -16.396  1.00 11.79           O  
ANISOU 7228  O   ASP A 477     1460   1482   1536    165     -9     50       O  
ATOM   7229  CB  ASP A 477       4.490  29.165 -13.905  1.00 11.88           C  
ANISOU 7229  CB  ASP A 477     1448   1517   1548    165      1     80       C  
ATOM   7230  CG  ASP A 477       5.488  28.098 -14.346  1.00 14.74           C  
ANISOU 7230  CG  ASP A 477     1813   1863   1924    168     11     94       C  
ATOM   7231  OD1 ASP A 477       5.927  28.089 -15.518  1.00 13.39           O  
ANISOU 7231  OD1 ASP A 477     1651   1678   1760    170     15     87       O  
ATOM   7232  OD2 ASP A 477       5.897  27.302 -13.470  1.00 17.18           O  
ANISOU 7232  OD2 ASP A 477     2115   2176   2236    170     14    113       O  
ATOM   7233  H   ASP A 477       2.753  27.233 -14.879  1.00 14.04           H  
ATOM   7234  HA  ASP A 477       2.626  29.885 -14.305  1.00 13.67           H  
ATOM   7235  HB2 ASP A 477       4.917  30.028 -14.020  1.00 14.25           H  
ATOM   7236  HB3 ASP A 477       4.296  29.013 -12.967  1.00 14.25           H  
ATOM   7237  N   VAL A 478       3.030  28.690 -17.108  1.00 11.76           N  
ANISOU 7237  N   VAL A 478     1459   1467   1544    156      6     53       N  
ATOM   7238  CA  VAL A 478       2.975  29.043 -18.526  1.00 10.53           C  
ANISOU 7238  CA  VAL A 478     1314   1299   1386    154      4     42       C  
ATOM   7239  C   VAL A 478       1.654  28.525 -19.085  1.00  8.84           C  
ANISOU 7239  C   VAL A 478     1102   1087   1171    145      2     33       C  
ATOM   7240  O   VAL A 478       1.298  27.369 -18.843  1.00 12.71           O  
ANISOU 7240  O   VAL A 478     1590   1571   1666    136     10     38       O  
ATOM   7241  CB  VAL A 478       4.142  28.410 -19.319  1.00 10.70           C  
ANISOU 7241  CB  VAL A 478     1343   1307   1415    154     15     45       C  
ATOM   7242  CG1 VAL A 478       4.043  28.698 -20.820  1.00 10.47           C  
ANISOU 7242  CG1 VAL A 478     1327   1272   1380    148     15     33       C  
ATOM   7243  CG2 VAL A 478       5.481  28.873 -18.810  1.00 12.90           C  
ANISOU 7243  CG2 VAL A 478     1616   1593   1695    161     16     54       C  
ATOM   7244  H   VAL A 478       2.800  27.876 -16.954  1.00 14.12           H  
ATOM   7245  HA  VAL A 478       3.018  30.008 -18.617  1.00 12.63           H  
ATOM   7246  HB  VAL A 478       4.073  27.451 -19.187  1.00 12.84           H  
ATOM   7247 HG11 VAL A 478       4.663  28.121 -21.294  1.00 12.57           H  
ATOM   7248 HG12 VAL A 478       3.136  28.524 -21.117  1.00 12.57           H  
ATOM   7249 HG13 VAL A 478       4.271  29.627 -20.979  1.00 12.57           H  
ATOM   7250 HG21 VAL A 478       6.180  28.375 -19.263  1.00 15.49           H  
ATOM   7251 HG22 VAL A 478       5.578  29.820 -18.993  1.00 15.49           H  
ATOM   7252 HG23 VAL A 478       5.528  28.713 -17.854  1.00 15.49           H  
ATOM   7253  N   THR A 479       0.949  29.346 -19.868  1.00 12.59           N  
ANISOU 7253  N   THR A 479     1580   1566   1637    145     -9     22       N  
ATOM   7254  CA  THR A 479      -0.225  28.853 -20.589  1.00 12.86           C  
ANISOU 7254  CA  THR A 479     1613   1605   1668    134    -11     14       C  
ATOM   7255  C   THR A 479      -0.362  29.639 -21.884  1.00 14.90           C  
ANISOU 7255  C   THR A 479     1882   1861   1918    134    -21      7       C  
ATOM   7256  O   THR A 479       0.233  30.707 -22.049  1.00 13.38           O  
ANISOU 7256  O   THR A 479     1696   1665   1723    143    -29      8       O  
ATOM   7257  CB  THR A 479      -1.513  28.931 -19.743  1.00 13.69           C  
ANISOU 7257  CB  THR A 479     1699   1734   1767    134    -17     13       C  
ATOM   7258  OG1 THR A 479      -2.515  28.058 -20.299  1.00 13.09           O  
ANISOU 7258  OG1 THR A 479     1620   1664   1688    116    -16      9       O  
ATOM   7259  CG2 THR A 479      -2.077  30.338 -19.675  1.00 15.10           C  
ANISOU 7259  CG2 THR A 479     1872   1928   1938    152    -33      5       C  
ATOM   7260  H   THR A 479       1.128  30.177 -19.995  1.00 15.11           H  
ATOM   7261  HA  THR A 479      -0.094  27.919 -20.814  1.00 15.43           H  
ATOM   7262  HB  THR A 479      -1.292  28.660 -18.839  1.00 16.43           H  
ATOM   7263  HG1 THR A 479      -2.229  27.269 -20.320  1.00 15.70           H  
ATOM   7264 HG21 THR A 479      -2.956  30.324 -19.265  1.00 18.12           H  
ATOM   7265 HG22 THR A 479      -1.493  30.905 -19.148  1.00 18.12           H  
ATOM   7266 HG23 THR A 479      -2.153  30.709 -20.568  1.00 18.12           H  
ATOM   7267  N   MET A 480      -1.156  29.098 -22.811  1.00 12.98           N  
ANISOU 7267  N   MET A 480     1641   1621   1670    121    -23      0       N  
ATOM   7268  CA  MET A 480      -1.261  29.667 -24.148  1.00 10.64           C  
ANISOU 7268  CA  MET A 480     1356   1324   1363    117    -33     -6       C  
ATOM   7269  C   MET A 480      -2.324  30.759 -24.255  1.00 13.26           C  
ANISOU 7269  C   MET A 480     1679   1673   1687    128    -54     -7       C  
ATOM   7270  O   MET A 480      -3.469  30.594 -23.810  1.00 13.52           O  
ANISOU 7270  O   MET A 480     1693   1725   1717    129    -59    -10       O  
ATOM   7271  CB  MET A 480      -1.555  28.572 -25.181  1.00 11.54           C  
ANISOU 7271  CB  MET A 480     1478   1434   1472     96    -26    -14       C  
ATOM   7272  CG  MET A 480      -0.479  27.514 -25.315  1.00 12.66           C  
ANISOU 7272  CG  MET A 480     1632   1555   1622     92     -6    -17       C  
ATOM   7273  SD  MET A 480       1.154  28.155 -25.673  1.00 12.56           S  
ANISOU 7273  SD  MET A 480     1629   1535   1609    103      2    -13       S  
ATOM   7274  CE  MET A 480       0.869  29.019 -27.219  1.00 11.72           C  
ANISOU 7274  CE  MET A 480     1533   1441   1481     92    -11    -17       C  
ATOM   7275  H   MET A 480      -1.643  28.401 -22.685  1.00 15.57           H  
ATOM   7276  HA  MET A 480      -0.402  30.076 -24.339  1.00 12.77           H  
ATOM   7277  HB2 MET A 480      -2.375  28.122 -24.926  1.00 13.85           H  
ATOM   7278  HB3 MET A 480      -1.662  28.990 -26.050  1.00 13.85           H  
ATOM   7279  HG2 MET A 480      -0.424  27.022 -24.481  1.00 15.19           H  
ATOM   7280  HG3 MET A 480      -0.723  26.915 -26.038  1.00 15.19           H  
ATOM   7281  HE1 MET A 480       1.704  29.407 -27.523  1.00 14.07           H  
ATOM   7282  HE2 MET A 480       0.539  28.387 -27.877  1.00 14.07           H  
ATOM   7283  HE3 MET A 480       0.213  29.718 -27.074  1.00 14.07           H  
ATOM   7284  N   LEU A 481      -1.902  31.887 -24.840  1.00 13.02           N  
ANISOU 7284  N   LEU A 481     1661   1635   1650    136    -66     -3       N  
ATOM   7285  CA  LEU A 481      -2.795  32.919 -25.344  1.00 12.28           C  
ANISOU 7285  CA  LEU A 481     1567   1551   1549    147    -89     -3       C  
ATOM   7286  C   LEU A 481      -3.201  32.528 -26.756  1.00 14.07           C  
ANISOU 7286  C   LEU A 481     1799   1784   1762    129    -94     -5       C  
ATOM   7287  O   LEU A 481      -2.338  32.491 -27.649  1.00 13.50           O  
ANISOU 7287  O   LEU A 481     1745   1702   1682    116    -88     -2       O  
ATOM   7288  CB  LEU A 481      -2.099  34.269 -25.338  1.00 13.64           C  
ANISOU 7288  CB  LEU A 481     1756   1706   1720    160   -102      5       C  
ATOM   7289  CG  LEU A 481      -2.893  35.420 -25.949  1.00 13.91           C  
ANISOU 7289  CG  LEU A 481     1797   1740   1747    175   -129      8       C  
ATOM   7290  CD1 LEU A 481      -4.235  35.619 -25.247  1.00 14.41           C  
ANISOU 7290  CD1 LEU A 481     1838   1824   1814    199   -139     -1       C  
ATOM   7291  CD2 LEU A 481      -2.067  36.697 -25.879  1.00 15.59           C  
ANISOU 7291  CD2 LEU A 481     2033   1928   1961    182   -142     17       C  
ATOM   7292  H   LEU A 481      -1.072  32.079 -24.959  1.00 15.62           H  
ATOM   7293  HA  LEU A 481      -3.589  32.985 -24.790  1.00 14.74           H  
ATOM   7294  HB2 LEU A 481      -1.904  34.508 -24.419  1.00 16.37           H  
ATOM   7295  HB3 LEU A 481      -1.274  34.188 -25.842  1.00 16.37           H  
ATOM   7296  HG  LEU A 481      -3.087  35.210 -26.875  1.00 16.69           H  
ATOM   7297 HD11 LEU A 481      -4.556  36.516 -25.428  1.00 17.30           H  
ATOM   7298 HD12 LEU A 481      -4.868  34.966 -25.586  1.00 17.30           H  
ATOM   7299 HD13 LEU A 481      -4.113  35.497 -24.292  1.00 17.30           H  
ATOM   7300 HD21 LEU A 481      -2.601  37.437 -26.208  1.00 18.71           H  
ATOM   7301 HD22 LEU A 481      -1.811  36.857 -24.958  1.00 18.71           H  
ATOM   7302 HD23 LEU A 481      -1.275  36.591 -26.429  1.00 18.71           H  
ATOM   7303  N   PRO A 482      -4.460  32.185 -27.000  1.00 11.92           N  
ANISOU 7303  N   PRO A 482     1511   1534   1483    126   -102    -10       N  
ATOM   7304  CA  PRO A 482      -4.839  31.693 -28.329  1.00 11.29           C  
ANISOU 7304  CA  PRO A 482     1437   1464   1388    104   -106    -13       C  
ATOM   7305  C   PRO A 482      -4.744  32.767 -29.399  1.00 13.73           C  
ANISOU 7305  C   PRO A 482     1762   1772   1684    108   -126     -3       C  
ATOM   7306  O   PRO A 482      -5.023  33.946 -29.163  1.00 12.98           O  
ANISOU 7306  O   PRO A 482     1666   1675   1590    132   -146      5       O  
ATOM   7307  CB  PRO A 482      -6.296  31.241 -28.143  1.00 16.80           C  
ANISOU 7307  CB  PRO A 482     2109   2192   2082    100   -115    -18       C  
ATOM   7308  CG  PRO A 482      -6.435  30.994 -26.645  1.00 13.03           C  
ANISOU 7308  CG  PRO A 482     1614   1717   1618    111   -104    -20       C  
ATOM   7309  CD  PRO A 482      -5.559  32.046 -26.023  1.00 13.64           C  
ANISOU 7309  CD  PRO A 482     1702   1774   1705    137   -105    -14       C  
ATOM   7310  HA  PRO A 482      -4.279  30.940 -28.577  1.00 13.55           H  
ATOM   7311  HB2 PRO A 482      -6.900  31.939 -28.439  1.00 20.16           H  
ATOM   7312  HB3 PRO A 482      -6.457  30.427 -28.646  1.00 20.16           H  
ATOM   7313  HG2 PRO A 482      -7.360  31.102 -26.373  1.00 15.63           H  
ATOM   7314  HG3 PRO A 482      -6.125  30.103 -26.422  1.00 15.63           H  
ATOM   7315  HD2 PRO A 482      -6.040  32.883 -25.922  1.00 16.36           H  
ATOM   7316  HD3 PRO A 482      -5.221  31.751 -25.162  1.00 16.36           H  
ATOM   7317  N   ALA A 483      -4.382  32.334 -30.604  1.00 14.01           N  
ANISOU 7317  N   ALA A 483     1812   1809   1704     85   -123     -5       N  
ATOM   7318  CA  ALA A 483      -4.494  33.198 -31.765  1.00 14.63           C  
ANISOU 7318  CA  ALA A 483     1902   1893   1762     82   -144      6       C  
ATOM   7319  C   ALA A 483      -5.914  33.743 -31.857  1.00 11.47           C  
ANISOU 7319  C   ALA A 483     1484   1515   1358     97   -171     11       C  
ATOM   7320  O   ALA A 483      -6.890  33.010 -31.669  1.00 14.47           O  
ANISOU 7320  O   ALA A 483     1843   1918   1738     91   -170      1       O  
ATOM   7321  CB  ALA A 483      -4.143  32.440 -33.043  1.00 17.58           C  
ANISOU 7321  CB  ALA A 483     2289   2276   2116     51   -134     -1       C  
ATOM   7322  H   ALA A 483      -4.070  31.550 -30.771  1.00 16.82           H  
ATOM   7323  HA  ALA A 483      -3.867  33.933 -31.682  1.00 17.55           H  
ATOM   7324  HB1 ALA A 483      -4.118  33.065 -33.784  1.00 21.10           H  
ATOM   7325  HB2 ALA A 483      -3.275  32.021 -32.933  1.00 21.10           H  
ATOM   7326  HB3 ALA A 483      -4.818  31.762 -33.204  1.00 21.10           H  
ATOM   7327  N   PHE A 484      -6.009  35.046 -32.110  1.00 12.67           N  
ANISOU 7327  N   PHE A 484     1646   1660   1507    117   -196     27       N  
ATOM   7328  CA  PHE A 484      -7.274  35.751 -32.293  1.00 14.47           C  
ANISOU 7328  CA  PHE A 484     1859   1908   1730    139   -225     35       C  
ATOM   7329  C   PHE A 484      -8.217  35.574 -31.112  1.00 14.14           C  
ANISOU 7329  C   PHE A 484     1786   1883   1704    163   -224     23       C  
ATOM   7330  O   PHE A 484      -9.434  35.699 -31.262  1.00 15.28           O  
ANISOU 7330  O   PHE A 484     1905   2057   1842    176   -242     23       O  
ATOM   7331  CB  PHE A 484      -7.976  35.323 -33.588  1.00 16.55           C  
ANISOU 7331  CB  PHE A 484     2118   2202   1969    116   -238     37       C  
ATOM   7332  CG  PHE A 484      -7.214  35.671 -34.832  1.00 16.26           C  
ANISOU 7332  CG  PHE A 484     2111   2157   1911     95   -244     51       C  
ATOM   7333  CD1 PHE A 484      -7.103  36.990 -35.246  1.00 22.41           C  
ANISOU 7333  CD1 PHE A 484     2909   2922   2686    111   -271     75       C  
ATOM   7334  CD2 PHE A 484      -6.609  34.683 -35.594  1.00 23.13           C  
ANISOU 7334  CD2 PHE A 484     2990   3033   2764     58   -224     40       C  
ATOM   7335  CE1 PHE A 484      -6.396  37.314 -36.388  1.00 20.42           C  
ANISOU 7335  CE1 PHE A 484     2683   2666   2411     86   -277     91       C  
ATOM   7336  CE2 PHE A 484      -5.907  35.011 -36.743  1.00 18.45           C  
ANISOU 7336  CE2 PHE A 484     2422   2441   2149     36   -227     52       C  
ATOM   7337  CZ  PHE A 484      -5.796  36.326 -37.127  1.00 17.83           C  
ANISOU 7337  CZ  PHE A 484     2360   2351   2062     49   -254     79       C  
ATOM   7338  H   PHE A 484      -5.326  35.563 -32.182  1.00 15.20           H  
ATOM   7339  HA  PHE A 484      -7.065  36.696 -32.357  1.00 17.36           H  
ATOM   7340  HB2 PHE A 484      -8.097  34.360 -33.574  1.00 19.86           H  
ATOM   7341  HB3 PHE A 484      -8.839  35.764 -33.635  1.00 19.86           H  
ATOM   7342  HD1 PHE A 484      -7.508  37.664 -34.749  1.00 26.90           H  
ATOM   7343  HD2 PHE A 484      -6.675  33.793 -35.332  1.00 27.75           H  
ATOM   7344  HE1 PHE A 484      -6.328  38.202 -36.657  1.00 24.51           H  
ATOM   7345  HE2 PHE A 484      -5.511  34.342 -37.253  1.00 22.15           H  
ATOM   7346  HZ  PHE A 484      -5.313  36.547 -37.890  1.00 21.39           H  
ATOM   7347  N   GLY A 485      -7.675  35.351 -29.923  1.00 11.62           N  
ANISOU 7347  N   GLY A 485     1465   1549   1403    170   -203     14       N  
ATOM   7348  CA  GLY A 485      -8.497  35.042 -28.780  1.00 13.28           C  
ANISOU 7348  CA  GLY A 485     1644   1780   1623    187   -197      3       C  
ATOM   7349  C   GLY A 485      -8.029  35.725 -27.517  1.00 13.42           C  
ANISOU 7349  C   GLY A 485     1665   1777   1658    215   -192     -1       C  
ATOM   7350  O   GLY A 485      -7.513  36.850 -27.544  1.00 14.75           O  
ANISOU 7350  O   GLY A 485     1856   1918   1830    234   -206      7       O  
ATOM   7351  H   GLY A 485      -6.831  35.375 -29.758  1.00 13.95           H  
ATOM   7352  HA2 GLY A 485      -9.408  35.323 -28.957  1.00 15.94           H  
ATOM   7353  HA3 GLY A 485      -8.485  34.084 -28.629  1.00 15.94           H  
ATOM   7354  N   TRP A 486      -8.207  35.038 -26.395  1.00 12.03           N  
ANISOU 7354  N   TRP A 486     1468   1615   1489    214   -173    -11       N  
ATOM   7355  CA  TRP A 486      -8.020  35.666 -25.100  1.00 14.25           C  
ANISOU 7355  CA  TRP A 486     1745   1887   1781    242   -169    -18       C  
ATOM   7356  C   TRP A 486      -7.934  34.590 -24.032  1.00 15.96           C  
ANISOU 7356  C   TRP A 486     1944   2117   2002    226   -144    -24       C  
ATOM   7357  O   TRP A 486      -8.331  33.439 -24.241  1.00 14.07           O  
ANISOU 7357  O   TRP A 486     1690   1897   1758    198   -133    -25       O  
ATOM   7358  CB  TRP A 486      -9.161  36.650 -24.769  1.00 12.34           C  
ANISOU 7358  CB  TRP A 486     1484   1666   1539    284   -190    -24       C  
ATOM   7359  CG  TRP A 486     -10.541  36.038 -24.844  1.00 12.97           C  
ANISOU 7359  CG  TRP A 486     1522   1797   1610    283   -193    -29       C  
ATOM   7360  CD1 TRP A 486     -11.401  36.093 -25.907  1.00 13.44           C  
ANISOU 7360  CD1 TRP A 486     1569   1879   1657    282   -212    -23       C  
ATOM   7361  CD2 TRP A 486     -11.214  35.275 -23.829  1.00 18.20           C  
ANISOU 7361  CD2 TRP A 486     2149   2498   2270    277   -176    -39       C  
ATOM   7362  NE1 TRP A 486     -12.556  35.410 -25.619  1.00 15.38           N  
ANISOU 7362  NE1 TRP A 486     1772   2176   1894    275   -209    -30       N  
ATOM   7363  CE2 TRP A 486     -12.469  34.903 -24.350  1.00 14.15           C  
ANISOU 7363  CE2 TRP A 486     1600   2031   1744    271   -186    -39       C  
ATOM   7364  CE3 TRP A 486     -10.880  34.873 -22.533  1.00 14.68           C  
ANISOU 7364  CE3 TRP A 486     1694   2055   1828    274   -154    -46       C  
ATOM   7365  CZ2 TRP A 486     -13.387  34.144 -23.620  1.00 13.45           C  
ANISOU 7365  CZ2 TRP A 486     1471   1993   1648    259   -174    -46       C  
ATOM   7366  CZ3 TRP A 486     -11.799  34.124 -21.808  1.00 14.07           C  
ANISOU 7366  CZ3 TRP A 486     1578   2026   1743    263   -142    -52       C  
ATOM   7367  CH2 TRP A 486     -13.037  33.775 -22.353  1.00 14.57           C  
ANISOU 7367  CH2 TRP A 486     1606   2135   1793    255   -152    -51       C  
ATOM   7368  H   TRP A 486      -8.435  34.209 -26.361  1.00 14.44           H  
ATOM   7369  HA  TRP A 486      -7.182  36.154 -25.110  1.00 17.10           H  
ATOM   7370  HB2 TRP A 486      -9.034  36.981 -23.866  1.00 14.81           H  
ATOM   7371  HB3 TRP A 486      -9.130  37.386 -25.399  1.00 14.81           H  
ATOM   7372  HD1 TRP A 486     -11.228  36.531 -26.709  1.00 16.12           H  
ATOM   7373  HE1 TRP A 486     -13.225  35.315 -26.150  1.00 18.45           H  
ATOM   7374  HE3 TRP A 486     -10.058  35.103 -22.162  1.00 17.62           H  
ATOM   7375  HZ2 TRP A 486     -14.207  33.899 -23.983  1.00 16.15           H  
ATOM   7376  HZ3 TRP A 486     -11.586  33.851 -20.945  1.00 16.88           H  
ATOM   7377  HH2 TRP A 486     -13.635  33.280 -21.842  1.00 17.48           H  
ATOM   7378  N   VAL A 487      -7.405  34.990 -22.884  1.00 13.11           N  
ANISOU 7378  N   VAL A 487     1587   1746   1650    241   -136    -29       N  
ATOM   7379  CA  VAL A 487      -7.368  34.147 -21.695  1.00 11.85           C  
ANISOU 7379  CA  VAL A 487     1410   1602   1492    231   -115    -33       C  
ATOM   7380  C   VAL A 487      -7.521  35.060 -20.487  1.00 13.77           C  
ANISOU 7380  C   VAL A 487     1643   1851   1736    264   -118    -44       C  
ATOM   7381  O   VAL A 487      -7.047  36.200 -20.491  1.00 14.69           O  
ANISOU 7381  O   VAL A 487     1783   1942   1858    287   -131    -47       O  
ATOM   7382  CB  VAL A 487      -6.068  33.310 -21.657  1.00 16.83           C  
ANISOU 7382  CB  VAL A 487     2060   2205   2129    203    -97    -24       C  
ATOM   7383  CG1 VAL A 487      -4.856  34.214 -21.520  1.00 17.21           C  
ANISOU 7383  CG1 VAL A 487     2135   2221   2184    214   -100    -22       C  
ATOM   7384  CG2 VAL A 487      -6.131  32.261 -20.566  1.00 18.88           C  
ANISOU 7384  CG2 VAL A 487     2303   2481   2391    188    -78    -23       C  
ATOM   7385  H   VAL A 487      -7.053  35.766 -22.764  1.00 15.73           H  
ATOM   7386  HA  VAL A 487      -8.111  33.525 -21.689  1.00 14.23           H  
ATOM   7387  HB  VAL A 487      -5.973  32.831 -22.496  1.00 20.20           H  
ATOM   7388 HG11 VAL A 487      -4.083  33.766 -21.898  1.00 20.65           H  
ATOM   7389 HG12 VAL A 487      -5.024  35.042 -21.996  1.00 20.65           H  
ATOM   7390 HG13 VAL A 487      -4.704  34.398 -20.579  1.00 20.65           H  
ATOM   7391 HG21 VAL A 487      -5.434  31.604 -20.719  1.00 22.66           H  
ATOM   7392 HG22 VAL A 487      -5.998  32.690 -19.707  1.00 22.66           H  
ATOM   7393 HG23 VAL A 487      -7.001  31.831 -20.591  1.00 22.66           H  
ATOM   7394  N   VAL A 488      -8.224  34.572 -19.470  1.00 13.22           N  
ANISOU 7394  N   VAL A 488     1544   1819   1661    265   -106    -51       N  
ATOM   7395  CA  VAL A 488      -8.360  35.273 -18.198  1.00 11.23           C  
ANISOU 7395  CA  VAL A 488     1281   1580   1406    294   -104    -65       C  
ATOM   7396  C   VAL A 488      -7.547  34.507 -17.161  1.00 13.53           C  
ANISOU 7396  C   VAL A 488     1574   1870   1698    271    -84    -59       C  
ATOM   7397  O   VAL A 488      -7.743  33.297 -16.981  1.00 15.64           O  
ANISOU 7397  O   VAL A 488     1826   2155   1961    241    -70    -49       O  
ATOM   7398  CB  VAL A 488      -9.831  35.397 -17.757  1.00 14.76           C  
ANISOU 7398  CB  VAL A 488     1686   2080   1842    315   -106    -78       C  
ATOM   7399  CG1 VAL A 488      -9.907  35.964 -16.337  1.00 16.00           C  
ANISOU 7399  CG1 VAL A 488     1831   2255   1992    342    -99    -95       C  
ATOM   7400  CG2 VAL A 488     -10.636  36.271 -18.728  1.00 16.92           C  
ANISOU 7400  CG2 VAL A 488     1957   2357   2116    346   -130    -83       C  
ATOM   7401  H   VAL A 488      -8.640  33.820 -19.496  1.00 15.87           H  
ATOM   7402  HA  VAL A 488      -8.002  36.170 -18.287  1.00 13.47           H  
ATOM   7403  HB  VAL A 488     -10.229  34.513 -17.764  1.00 17.71           H  
ATOM   7404 HG11 VAL A 488      -9.281  36.700 -16.256  1.00 19.20           H  
ATOM   7405 HG12 VAL A 488     -10.810  36.279 -16.170  1.00 19.20           H  
ATOM   7406 HG13 VAL A 488      -9.679  35.265 -15.705  1.00 19.20           H  
ATOM   7407 HG21 VAL A 488     -11.555  35.961 -18.745  1.00 20.31           H  
ATOM   7408 HG22 VAL A 488     -10.603  37.192 -18.426  1.00 20.31           H  
ATOM   7409 HG23 VAL A 488     -10.246  36.200 -19.614  1.00 20.31           H  
ATOM   7410  N   LEU A 489      -6.634  35.213 -16.499  1.00 13.57           N  
ANISOU 7410  N   LEU A 489     1599   1851   1705    283    -84    -63       N  
ATOM   7411  CA  LEU A 489      -5.733  34.663 -15.503  1.00 13.02           C  
ANISOU 7411  CA  LEU A 489     1533   1779   1635    266    -68    -56       C  
ATOM   7412  C   LEU A 489      -5.976  35.365 -14.179  1.00 15.83           C  
ANISOU 7412  C   LEU A 489     1877   2157   1980    289    -67    -74       C  
ATOM   7413  O   LEU A 489      -6.406  36.521 -14.149  1.00 16.62           O  
ANISOU 7413  O   LEU A 489     1981   2255   2078    323    -80    -93       O  
ATOM   7414  CB  LEU A 489      -4.271  34.873 -15.884  1.00 14.16           C  
ANISOU 7414  CB  LEU A 489     1711   1880   1790    255    -71    -46       C  
ATOM   7415  CG  LEU A 489      -3.792  34.388 -17.246  1.00 13.46           C  
ANISOU 7415  CG  LEU A 489     1638   1766   1711    235    -72    -32       C  
ATOM   7416  CD1 LEU A 489      -2.330  34.728 -17.462  1.00 18.04           C  
ANISOU 7416  CD1 LEU A 489     2245   2313   2297    227    -73    -24       C  
ATOM   7417  CD2 LEU A 489      -4.043  32.895 -17.349  1.00 20.38           C  
ANISOU 7417  CD2 LEU A 489     2500   2655   2587    209    -57    -21       C  
ATOM   7418  H   LEU A 489      -6.517  36.056 -16.619  1.00 16.28           H  
ATOM   7419  HA  LEU A 489      -5.899  33.711 -15.416  1.00 15.62           H  
ATOM   7420  HB2 LEU A 489      -4.096  35.827 -15.855  1.00 16.99           H  
ATOM   7421  HB3 LEU A 489      -3.728  34.416 -15.223  1.00 16.99           H  
ATOM   7422  HG  LEU A 489      -4.283  34.834 -17.954  1.00 16.16           H  
ATOM   7423 HD11 LEU A 489      -2.043  34.361 -18.312  1.00 21.65           H  
ATOM   7424 HD12 LEU A 489      -2.228  35.692 -17.466  1.00 21.65           H  
ATOM   7425 HD13 LEU A 489      -1.807  34.342 -16.741  1.00 21.65           H  
ATOM   7426 HD21 LEU A 489      -3.615  32.557 -18.151  1.00 24.45           H  
ATOM   7427 HD22 LEU A 489      -3.672  32.458 -16.566  1.00 24.45           H  
ATOM   7428 HD23 LEU A 489      -4.999  32.737 -17.393  1.00 24.45           H  
ATOM   7429  N   ALA A 490      -5.684  34.680 -13.084  1.00 13.05           N  
ANISOU 7429  N   ALA A 490     1514   1825   1620    272    -52    -68       N  
ATOM   7430  CA  ALA A 490      -5.695  35.328 -11.785  1.00 13.36           C  
ANISOU 7430  CA  ALA A 490     1545   1885   1645    290    -49    -85       C  
ATOM   7431  C   ALA A 490      -4.513  34.828 -10.975  1.00 13.14           C  
ANISOU 7431  C   ALA A 490     1528   1849   1615    267    -40    -70       C  
ATOM   7432  O   ALA A 490      -4.069  33.691 -11.139  1.00 13.28           O  
ANISOU 7432  O   ALA A 490     1545   1861   1638    239    -31    -46       O  
ATOM   7433  CB  ALA A 490      -6.999  35.065 -11.018  1.00 14.49           C  
ANISOU 7433  CB  ALA A 490     1649   2087   1769    298    -39    -96       C  
ATOM   7434  H   ALA A 490      -5.478  33.845 -13.070  1.00 15.66           H  
ATOM   7435  HA  ALA A 490      -5.609  36.287 -11.904  1.00 16.03           H  
ATOM   7436  HB1 ALA A 490      -6.939  35.478 -10.142  1.00 17.39           H  
ATOM   7437  HB2 ALA A 490      -7.740  35.448 -11.514  1.00 17.39           H  
ATOM   7438  HB3 ALA A 490      -7.123  34.108 -10.924  1.00 17.39           H  
ATOM   7439  N   PHE A 491      -4.021  35.674 -10.077  1.00 13.01           N  
ANISOU 7439  N   PHE A 491     1521   1832   1589    281    -43    -85       N  
ATOM   7440  CA  PHE A 491      -3.030  35.214  -9.116  1.00 14.78           C  
ANISOU 7440  CA  PHE A 491     1749   2062   1807    260    -35    -71       C  
ATOM   7441  C   PHE A 491      -3.236  35.950  -7.800  1.00 13.46           C  
ANISOU 7441  C   PHE A 491     1574   1924   1617    275    -34    -95       C  
ATOM   7442  O   PHE A 491      -3.905  36.984  -7.737  1.00 13.22           O  
ANISOU 7442  O   PHE A 491     1545   1897   1581    306    -42   -125       O  
ATOM   7443  CB  PHE A 491      -1.600  35.359  -9.662  1.00 12.48           C  
ANISOU 7443  CB  PHE A 491     1485   1726   1530    247    -43    -57       C  
ATOM   7444  CG  PHE A 491      -1.160  36.765  -9.904  1.00 16.78           C  
ANISOU 7444  CG  PHE A 491     2058   2241   2079    264    -60    -76       C  
ATOM   7445  CD1 PHE A 491      -1.333  37.363 -11.143  1.00 16.16           C  
ANISOU 7445  CD1 PHE A 491     1997   2130   2014    274    -72    -80       C  
ATOM   7446  CD2 PHE A 491      -0.516  37.472  -8.906  1.00 17.40           C  
ANISOU 7446  CD2 PHE A 491     2146   2321   2144    264    -64    -88       C  
ATOM   7447  CE1 PHE A 491      -0.900  38.666 -11.371  1.00 16.98           C  
ANISOU 7447  CE1 PHE A 491     2131   2201   2121    286    -90    -94       C  
ATOM   7448  CE2 PHE A 491      -0.073  38.767  -9.129  1.00 20.87           C  
ANISOU 7448  CE2 PHE A 491     2616   2727   2587    274    -82   -106       C  
ATOM   7449  CZ  PHE A 491      -0.275  39.368 -10.361  1.00 21.01           C  
ANISOU 7449  CZ  PHE A 491     2653   2709   2620    285    -95   -108       C  
ATOM   7450  H   PHE A 491      -4.240  36.503 -10.007  1.00 15.61           H  
ATOM   7451  HA  PHE A 491      -3.161  34.271  -8.930  1.00 17.74           H  
ATOM   7452  HB2 PHE A 491      -0.985  34.968  -9.021  1.00 14.97           H  
ATOM   7453  HB3 PHE A 491      -1.544  34.887 -10.507  1.00 14.97           H  
ATOM   7454  HD1 PHE A 491      -1.743  36.888 -11.829  1.00 19.40           H  
ATOM   7455  HD2 PHE A 491      -0.378  37.075  -8.077  1.00 20.88           H  
ATOM   7456  HE1 PHE A 491      -1.032  39.063 -12.202  1.00 20.38           H  
ATOM   7457  HE2 PHE A 491       0.360  39.233  -8.451  1.00 25.05           H  
ATOM   7458  HZ  PHE A 491       0.010  40.241 -10.507  1.00 25.21           H  
ATOM   7459  N   ARG A 492      -2.693  35.366  -6.736  1.00 13.13           N  
ANISOU 7459  N   ARG A 492     1524   1905   1561    255    -25    -82       N  
ATOM   7460  CA  ARG A 492      -2.786  35.932  -5.398  1.00 16.77           C  
ANISOU 7460  CA  ARG A 492     1977   2399   1995    264    -22   -103       C  
ATOM   7461  C   ARG A 492      -1.577  36.815  -5.124  1.00 12.62           C  
ANISOU 7461  C   ARG A 492     1482   1844   1470    264    -35   -112       C  
ATOM   7462  O   ARG A 492      -0.442  36.432  -5.424  1.00 15.67           O  
ANISOU 7462  O   ARG A 492     1881   2205   1869    242    -39    -87       O  
ATOM   7463  CB  ARG A 492      -2.861  34.819  -4.350  1.00 17.94           C  
ANISOU 7463  CB  ARG A 492     2100   2593   2122    238     -7    -81       C  
ATOM   7464  CG  ARG A 492      -3.935  33.790  -4.626  1.00 33.10           C  
ANISOU 7464  CG  ARG A 492     3994   4542   4042    227      4    -65       C  
ATOM   7465  CD  ARG A 492      -4.284  32.970  -3.395  1.00 91.28           C  
ANISOU 7465  CD  ARG A 492    11335  11964  11382    204     18    -50       C  
ATOM   7466  NE  ARG A 492      -3.277  31.969  -3.054  1.00 66.85           N  
ANISOU 7466  NE  ARG A 492     8251   8859   8292    173     19    -11       N  
ATOM   7467  CZ  ARG A 492      -3.530  30.876  -2.338  1.00111.61           C  
ANISOU 7467  CZ  ARG A 492    13901  14560  13944    144     29     18       C  
ATOM   7468  NH1 ARG A 492      -4.760  30.631  -1.901  1.00 50.74           N  
ANISOU 7468  NH1 ARG A 492     6163   6903   6213    138     40     13       N  
ATOM   7469  NH2 ARG A 492      -2.557  30.023  -2.067  1.00 36.93           N  
ANISOU 7469  NH2 ARG A 492     4455   5085   4492    122     26     54       N  
ATOM   7470  H   ARG A 492      -2.257  34.625  -6.765  1.00 15.76           H  
ATOM   7471  HA  ARG A 492      -3.588  36.474  -5.327  1.00 20.12           H  
ATOM   7472  HB2 ARG A 492      -2.009  34.357  -4.325  1.00 21.53           H  
ATOM   7473  HB3 ARG A 492      -3.049  35.216  -3.485  1.00 21.53           H  
ATOM   7474  HG2 ARG A 492      -4.739  34.243  -4.924  1.00 39.72           H  
ATOM   7475  HG3 ARG A 492      -3.622  33.182  -5.314  1.00 39.72           H  
ATOM   7476  HD2 ARG A 492      -4.377  33.567  -2.637  1.00109.53           H  
ATOM   7477  HD3 ARG A 492      -5.121  32.505  -3.556  1.00109.53           H  
ATOM   7478  HE  ARG A 492      -2.473  32.093  -3.332  1.00 80.22           H  
ATOM   7479 HH11 ARG A 492      -5.397  31.180  -2.080  1.00 60.89           H  
ATOM   7480 HH12 ARG A 492      -4.919  29.923  -1.439  1.00 60.89           H  
ATOM   7481 HH21 ARG A 492      -1.761  30.174  -2.353  1.00 44.32           H  
ATOM   7482 HH22 ARG A 492      -2.721  29.317  -1.605  1.00 44.32           H  
ATOM   7483  N   ALA A 493      -1.821  37.997  -4.543  1.00 14.31           N  
ANISOU 7483  N   ALA A 493     1706   2062   1670    287    -42   -149       N  
ATOM   7484  CA  ALA A 493      -0.755  38.968  -4.261  1.00 16.62           C  
ANISOU 7484  CA  ALA A 493     2030   2324   1960    284    -57   -162       C  
ATOM   7485  C   ALA A 493      -0.107  38.611  -2.920  1.00 14.85           C  
ANISOU 7485  C   ALA A 493     1796   2137   1710    262    -51   -156       C  
ATOM   7486  O   ALA A 493      -0.226  39.308  -1.909  1.00 17.55           O  
ANISOU 7486  O   ALA A 493     2141   2500   2026    270    -52   -186       O  
ATOM   7487  CB  ALA A 493      -1.304  40.389  -4.270  1.00 17.47           C  
ANISOU 7487  CB  ALA A 493     2160   2413   2066    320    -69   -206       C  
ATOM   7488  H   ALA A 493      -2.602  38.261  -4.301  1.00 17.18           H  
ATOM   7489  HA  ALA A 493      -0.078  38.911  -4.953  1.00 19.94           H  
ATOM   7490  HB1 ALA A 493      -0.563  41.013  -4.323  1.00 20.97           H  
ATOM   7491  HB2 ALA A 493      -1.884  40.498  -5.040  1.00 20.97           H  
ATOM   7492  HB3 ALA A 493      -1.805  40.539  -3.454  1.00 20.97           H  
ATOM   7493  N   ASP A 494       0.595  37.479  -2.933  1.00 13.79           N  
ANISOU 7493  N   ASP A 494     1650   2009   1581    232    -45   -115       N  
ATOM   7494  CA  ASP A 494       1.165  36.886  -1.731  1.00 16.37           C  
ANISOU 7494  CA  ASP A 494     1962   2373   1883    210    -40    -98       C  
ATOM   7495  C   ASP A 494       2.686  36.957  -1.710  1.00 16.35           C  
ANISOU 7495  C   ASP A 494     1976   2350   1887    187    -52    -79       C  
ATOM   7496  O   ASP A 494       3.320  36.282  -0.894  1.00 15.63           O  
ANISOU 7496  O   ASP A 494     1871   2286   1780    167    -50    -54       O  
ATOM   7497  CB  ASP A 494       0.699  35.427  -1.613  1.00 23.06           C  
ANISOU 7497  CB  ASP A 494     2782   3250   2730    195    -24    -63       C  
ATOM   7498  CG  ASP A 494       1.131  34.572  -2.799  1.00 19.88           C  
ANISOU 7498  CG  ASP A 494     2384   2810   2360    186    -24    -30       C  
ATOM   7499  OD1 ASP A 494       1.968  35.032  -3.601  1.00 17.95           O  
ANISOU 7499  OD1 ASP A 494     2160   2525   2136    187    -35    -30       O  
ATOM   7500  OD2 ASP A 494       0.640  33.429  -2.931  1.00 25.83           O  
ANISOU 7500  OD2 ASP A 494     3121   3575   3118    175    -14     -5       O  
ATOM   7501  H   ASP A 494       0.756  37.027  -3.646  1.00 16.55           H  
ATOM   7502  HA  ASP A 494       0.844  37.373  -0.956  1.00 19.64           H  
ATOM   7503  HB2 ASP A 494       1.078  35.038  -0.809  1.00 27.67           H  
ATOM   7504  HB3 ASP A 494      -0.270  35.408  -1.566  1.00 27.67           H  
ATOM   7505  N   ASN A 495       3.291  37.767  -2.572  1.00 14.47           N  
ANISOU 7505  N   ASN A 495     1763   2066   1667    190    -65    -87       N  
ATOM   7506  CA  ASN A 495       4.733  37.701  -2.812  1.00 14.21           C  
ANISOU 7506  CA  ASN A 495     1739   2015   1643    166    -75    -64       C  
ATOM   7507  C   ASN A 495       5.240  39.044  -3.301  1.00 19.30           C  
ANISOU 7507  C   ASN A 495     2417   2622   2295    165    -93    -87       C  
ATOM   7508  O   ASN A 495       5.396  39.273  -4.507  1.00 16.99           O  
ANISOU 7508  O   ASN A 495     2138   2291   2025    167    -98    -81       O  
ATOM   7509  CB  ASN A 495       5.043  36.590  -3.814  1.00 13.03           C  
ANISOU 7509  CB  ASN A 495     1579   1851   1520    161    -68    -27       C  
ATOM   7510  CG  ASN A 495       6.504  36.237  -3.861  1.00 15.67           C  
ANISOU 7510  CG  ASN A 495     1911   2183   1860    140    -73      2       C  
ATOM   7511  OD1 ASN A 495       7.312  36.715  -3.056  1.00 14.69           O  
ANISOU 7511  OD1 ASN A 495     1789   2075   1718    125    -83     -1       O  
ATOM   7512  ND2 ASN A 495       6.859  35.386  -4.813  1.00 15.45           N  
ANISOU 7512  ND2 ASN A 495     1877   2137   1855    139    -67     28       N  
ATOM   7513  H   ASN A 495       2.886  38.368  -3.035  1.00 17.36           H  
ATOM   7514  HA  ASN A 495       5.192  37.517  -1.977  1.00 17.05           H  
ATOM   7515  HB2 ASN A 495       4.551  35.793  -3.564  1.00 15.63           H  
ATOM   7516  HB3 ASN A 495       4.777  36.881  -4.700  1.00 15.63           H  
ATOM   7517 HD21 ASN A 495       7.681  35.146  -4.891  1.00 18.53           H  
ATOM   7518 HD22 ASN A 495       6.266  35.074  -5.353  1.00 18.53           H  
ATOM   7519  N   PRO A 496       5.522  39.964  -2.380  1.00 15.01           N  
ANISOU 7519  N   PRO A 496     1888   2087   1728    159   -104   -113       N  
ATOM   7520  CA  PRO A 496       6.025  41.284  -2.784  1.00 15.08           C  
ANISOU 7520  CA  PRO A 496     1933   2054   1742    153   -123   -135       C  
ATOM   7521  C   PRO A 496       7.258  41.135  -3.656  1.00 15.17           C  
ANISOU 7521  C   PRO A 496     1949   2044   1771    126   -131   -104       C  
ATOM   7522  O   PRO A 496       8.153  40.342  -3.367  1.00 16.04           O  
ANISOU 7522  O   PRO A 496     2037   2181   1878    106   -127    -73       O  
ATOM   7523  CB  PRO A 496       6.329  41.970  -1.445  1.00 15.94           C  
ANISOU 7523  CB  PRO A 496     2052   2186   1819    142   -132   -162       C  
ATOM   7524  CG  PRO A 496       5.381  41.289  -0.475  1.00 19.56           C  
ANISOU 7524  CG  PRO A 496     2482   2694   2256    159   -114   -169       C  
ATOM   7525  CD  PRO A 496       5.402  39.851  -0.913  1.00 15.89           C  
ANISOU 7525  CD  PRO A 496     1985   2246   1806    154    -99   -124       C  
ATOM   7526  HA  PRO A 496       5.349  41.796  -3.255  1.00 18.09           H  
ATOM   7527  HB2 PRO A 496       7.255  41.824  -1.195  1.00 19.13           H  
ATOM   7528  HB3 PRO A 496       6.148  42.922  -1.506  1.00 19.13           H  
ATOM   7529  HG2 PRO A 496       5.705  41.385   0.435  1.00 23.47           H  
ATOM   7530  HG3 PRO A 496       4.492  41.668  -0.552  1.00 23.47           H  
ATOM   7531  HD2 PRO A 496       6.164  39.383  -0.536  1.00 19.07           H  
ATOM   7532  HD3 PRO A 496       4.580  39.400  -0.665  1.00 19.07           H  
ATOM   7533  N   GLY A 497       7.284  41.884  -4.754  1.00 13.99           N  
ANISOU 7533  N   GLY A 497     1827   1849   1641    128   -142   -109       N  
ATOM   7534  CA  GLY A 497       8.355  41.744  -5.704  1.00 15.49           C  
ANISOU 7534  CA  GLY A 497     2018   2022   1846    103   -146    -80       C  
ATOM   7535  C   GLY A 497       8.036  42.411  -7.018  1.00 14.35           C  
ANISOU 7535  C   GLY A 497     1901   1831   1722    110   -155    -84       C  
ATOM   7536  O   GLY A 497       6.884  42.807  -7.251  1.00 13.06           O  
ANISOU 7536  O   GLY A 497     1752   1648   1564    140   -156   -106       O  
ATOM   7537  H   GLY A 497       6.693  42.474  -4.961  1.00 16.79           H  
ATOM   7538  HA2 GLY A 497       9.161  42.145  -5.343  1.00 18.59           H  
ATOM   7539  HA3 GLY A 497       8.518  40.802  -5.869  1.00 18.59           H  
ATOM   7540  N   ALA A 498       9.051  42.615  -7.841  1.00 13.34           N  
ANISOU 7540  N   ALA A 498     1780   1686   1601     82   -162    -64       N  
ATOM   7541  CA  ALA A 498       8.885  42.987  -9.239  1.00 13.70           C  
ANISOU 7541  CA  ALA A 498     1847   1695   1665     84   -167    -56       C  
ATOM   7542  C   ALA A 498       8.927  41.699 -10.059  1.00 12.62           C  
ANISOU 7542  C   ALA A 498     1679   1576   1542     90   -147    -29       C  
ATOM   7543  O   ALA A 498       9.958  41.018 -10.095  1.00 13.66           O  
ANISOU 7543  O   ALA A 498     1787   1731   1672     70   -139     -5       O  
ATOM   7544  CB  ALA A 498       9.980  43.963  -9.663  1.00 14.26           C  
ANISOU 7544  CB  ALA A 498     1944   1743   1733     45   -187    -49       C  
ATOM   7545  H   ALA A 498       9.875  42.541  -7.606  1.00 16.00           H  
ATOM   7546  HA  ALA A 498       8.031  43.424  -9.380  1.00 16.44           H  
ATOM   7547  HB1 ALA A 498       9.874  44.167 -10.605  1.00 17.12           H  
ATOM   7548  HB2 ALA A 498       9.900  44.775  -9.138  1.00 17.12           H  
ATOM   7549  HB3 ALA A 498      10.846  43.553  -9.509  1.00 17.12           H  
ATOM   7550  N   TRP A 499       7.808  41.362 -10.712  1.00 13.42           N  
ANISOU 7550  N   TRP A 499     1779   1666   1655    118   -140    -33       N  
ATOM   7551  CA  TRP A 499       7.649  40.082 -11.399  1.00 13.39           C  
ANISOU 7551  CA  TRP A 499     1749   1677   1663    125   -121    -13       C  
ATOM   7552  C   TRP A 499       7.364  40.278 -12.881  1.00 12.76           C  
ANISOU 7552  C   TRP A 499     1684   1569   1595    127   -123     -7       C  
ATOM   7553  O   TRP A 499       6.331  40.842 -13.256  1.00 13.87           O  
ANISOU 7553  O   TRP A 499     1842   1689   1740    147   -132    -22       O  
ATOM   7554  CB  TRP A 499       6.516  39.258 -10.776  1.00 12.65           C  
ANISOU 7554  CB  TRP A 499     1634   1603   1568    151   -107    -21       C  
ATOM   7555  CG  TRP A 499       6.665  39.065  -9.296  1.00 11.36           C  
ANISOU 7555  CG  TRP A 499     1457   1471   1388    150   -104    -26       C  
ATOM   7556  CD1 TRP A 499       5.897  39.612  -8.299  1.00 11.71           C  
ANISOU 7556  CD1 TRP A 499     1506   1525   1419    164   -108    -52       C  
ATOM   7557  CD2 TRP A 499       7.662  38.279  -8.647  1.00 11.65           C  
ANISOU 7557  CD2 TRP A 499     1472   1536   1420    133    -97     -4       C  
ATOM   7558  NE1 TRP A 499       6.363  39.206  -7.068  1.00 14.19           N  
ANISOU 7558  NE1 TRP A 499     1802   1872   1715    154   -104    -48       N  
ATOM   7559  CE2 TRP A 499       7.447  38.387  -7.257  1.00 14.52           C  
ANISOU 7559  CE2 TRP A 499     1829   1926   1764    135    -99    -17       C  
ATOM   7560  CE3 TRP A 499       8.718  37.487  -9.110  1.00 13.16           C  
ANISOU 7560  CE3 TRP A 499     1647   1735   1619    119    -90     24       C  
ATOM   7561  CZ2 TRP A 499       8.248  37.724  -6.328  1.00 16.02           C  
ANISOU 7561  CZ2 TRP A 499     1997   2149   1942    121    -95      2       C  
ATOM   7562  CZ3 TRP A 499       9.511  36.834  -8.189  1.00 15.90           C  
ANISOU 7562  CZ3 TRP A 499     1972   2113   1957    110    -87     41       C  
ATOM   7563  CH2 TRP A 499       9.270  36.952  -6.815  1.00 13.42           C  
ANISOU 7563  CH2 TRP A 499     1653   1824   1624    110    -91     32       C  
ATOM   7564  H   TRP A 499       7.117  41.872 -10.769  1.00 16.11           H  
ATOM   7565  HA  TRP A 499       8.492  39.609 -11.320  1.00 16.07           H  
ATOM   7566  HB2 TRP A 499       5.674  39.714 -10.933  1.00 15.17           H  
ATOM   7567  HB3 TRP A 499       6.500  38.382 -11.191  1.00 15.17           H  
ATOM   7568  HD1 TRP A 499       5.168  40.174  -8.434  1.00 14.05           H  
ATOM   7569  HE1 TRP A 499       6.031  39.429  -6.307  1.00 17.02           H  
ATOM   7570  HE3 TRP A 499       8.883  37.402 -10.021  1.00 15.79           H  
ATOM   7571  HZ2 TRP A 499       8.095  37.803  -5.414  1.00 19.23           H  
ATOM   7572  HZ3 TRP A 499      10.217  36.306  -8.486  1.00 19.08           H  
ATOM   7573  HH2 TRP A 499       9.817  36.495  -6.218  1.00 16.11           H  
ATOM   7574  N   LEU A 500       8.255  39.777 -13.717  1.00 13.80           N  
ANISOU 7574  N   LEU A 500     1807   1706   1732    108   -116     15       N  
ATOM   7575  CA  LEU A 500       8.031  39.815 -15.148  1.00 12.40           C  
ANISOU 7575  CA  LEU A 500     1640   1510   1561    107   -116     23       C  
ATOM   7576  C   LEU A 500       6.872  38.911 -15.539  1.00 14.54           C  
ANISOU 7576  C   LEU A 500     1898   1785   1841    132   -104     19       C  
ATOM   7577  O   LEU A 500       6.714  37.806 -15.016  1.00 13.51           O  
ANISOU 7577  O   LEU A 500     1743   1676   1713    141    -88     22       O  
ATOM   7578  CB  LEU A 500       9.298  39.375 -15.855  1.00 12.09           C  
ANISOU 7578  CB  LEU A 500     1588   1484   1521     82   -107     44       C  
ATOM   7579  CG  LEU A 500       9.394  39.644 -17.344  1.00 15.94           C  
ANISOU 7579  CG  LEU A 500     2090   1957   2010     70   -109     54       C  
ATOM   7580  CD1 LEU A 500       9.276  41.122 -17.596  1.00 19.83           C  
ANISOU 7580  CD1 LEU A 500     2620   2419   2498     57   -134     50       C  
ATOM   7581  CD2 LEU A 500      10.724  39.083 -17.830  1.00 16.52           C  
ANISOU 7581  CD2 LEU A 500     2142   2056   2079     49    -95     73       C  
ATOM   7582  H   LEU A 500       8.996  39.409 -13.482  1.00 16.56           H  
ATOM   7583  HA  LEU A 500       7.806  40.716 -15.427  1.00 14.88           H  
ATOM   7584  HB2 LEU A 500      10.045  39.832 -15.437  1.00 14.50           H  
ATOM   7585  HB3 LEU A 500       9.387  38.417 -15.735  1.00 14.50           H  
ATOM   7586  HG  LEU A 500       8.678  39.217 -17.839  1.00 19.13           H  
ATOM   7587 HD11 LEU A 500       9.633  41.322 -18.475  1.00 23.80           H  
ATOM   7588 HD12 LEU A 500       8.341  41.376 -17.553  1.00 23.80           H  
ATOM   7589 HD13 LEU A 500       9.780  41.599 -16.918  1.00 23.80           H  
ATOM   7590 HD21 LEU A 500      10.850  39.331 -18.759  1.00 19.82           H  
ATOM   7591 HD22 LEU A 500      11.439  39.454 -17.289  1.00 19.82           H  
ATOM   7592 HD23 LEU A 500      10.710  38.117 -17.743  1.00 19.82           H  
ATOM   7593  N   PHE A 501       6.071  39.387 -16.481  1.00 13.63           N  
ANISOU 7593  N   PHE A 501     1801   1649   1730    142   -113     14       N  
ATOM   7594  CA  PHE A 501       5.013  38.613 -17.116  1.00 10.28           C  
ANISOU 7594  CA  PHE A 501     1365   1228   1311    159   -104     12       C  
ATOM   7595  C   PHE A 501       5.229  38.803 -18.604  1.00  9.40           C  
ANISOU 7595  C   PHE A 501     1268   1104   1200    146   -108     23       C  
ATOM   7596  O   PHE A 501       5.135  39.931 -19.097  1.00 13.18           O  
ANISOU 7596  O   PHE A 501     1772   1558   1675    143   -127     23       O  
ATOM   7597  CB  PHE A 501       3.635  39.114 -16.693  1.00 12.28           C  
ANISOU 7597  CB  PHE A 501     1622   1478   1564    187   -114     -8       C  
ATOM   7598  CG  PHE A 501       2.491  38.419 -17.370  1.00 13.76           C  
ANISOU 7598  CG  PHE A 501     1797   1674   1756    201   -108     -9       C  
ATOM   7599  CD1 PHE A 501       2.277  37.062 -17.209  1.00 12.50           C  
ANISOU 7599  CD1 PHE A 501     1613   1538   1600    198    -89     -4       C  
ATOM   7600  CD2 PHE A 501       1.586  39.140 -18.128  1.00 18.01           C  
ANISOU 7600  CD2 PHE A 501     2350   2198   2296    216   -124    -16       C  
ATOM   7601  CE1 PHE A 501       1.195  36.439 -17.812  1.00 13.17           C  
ANISOU 7601  CE1 PHE A 501     1687   1632   1686    206    -85     -6       C  
ATOM   7602  CE2 PHE A 501       0.509  38.513 -18.735  1.00 17.66           C  
ANISOU 7602  CE2 PHE A 501     2291   2168   2253    227   -121    -17       C  
ATOM   7603  CZ  PHE A 501       0.319  37.165 -18.575  1.00 14.28           C  
ANISOU 7603  CZ  PHE A 501     1838   1763   1826    219   -101    -13       C  
ATOM   7604  H   PHE A 501       6.125  40.191 -16.783  1.00 16.36           H  
ATOM   7605  HA  PHE A 501       5.056  37.673 -16.880  1.00 12.33           H  
ATOM   7606  HB2 PHE A 501       3.536  38.980 -15.737  1.00 14.73           H  
ATOM   7607  HB3 PHE A 501       3.571  40.059 -16.903  1.00 14.73           H  
ATOM   7608  HD1 PHE A 501       2.866  36.562 -16.690  1.00 15.00           H  
ATOM   7609  HD2 PHE A 501       1.702  40.057 -18.232  1.00 21.62           H  
ATOM   7610  HE1 PHE A 501       1.064  35.525 -17.698  1.00 15.81           H  
ATOM   7611  HE2 PHE A 501      -0.086  39.008 -19.250  1.00 21.20           H  
ATOM   7612  HZ  PHE A 501      -0.403  36.745 -18.984  1.00 17.14           H  
ATOM   7613  N   HIS A 502       5.524  37.724 -19.322  1.00 13.03           N  
ANISOU 7613  N   HIS A 502     1713   1576   1662    138    -91     33       N  
ATOM   7614  CA  HIS A 502       5.962  37.901 -20.699  1.00 12.76           C  
ANISOU 7614  CA  HIS A 502     1691   1536   1623    121    -92     44       C  
ATOM   7615  C   HIS A 502       5.649  36.685 -21.556  1.00 14.54           C  
ANISOU 7615  C   HIS A 502     1902   1772   1850    124    -75     44       C  
ATOM   7616  O   HIS A 502       5.363  35.598 -21.053  1.00 12.08           O  
ANISOU 7616  O   HIS A 502     1573   1472   1546    134    -60     40       O  
ATOM   7617  CB  HIS A 502       7.464  38.216 -20.718  1.00 10.63           C  
ANISOU 7617  CB  HIS A 502     1421   1272   1346     95    -90     57       C  
ATOM   7618  CG  HIS A 502       8.334  37.088 -20.252  1.00 16.04           C  
ANISOU 7618  CG  HIS A 502     2079   1982   2035     94    -68     62       C  
ATOM   7619  ND1 HIS A 502       8.929  36.202 -21.125  1.00 13.26           N  
ANISOU 7619  ND1 HIS A 502     1713   1643   1681     89    -50     68       N  
ATOM   7620  CD2 HIS A 502       8.702  36.693 -19.008  1.00 13.30           C  
ANISOU 7620  CD2 HIS A 502     1714   1647   1691    100    -62     62       C  
ATOM   7621  CE1 HIS A 502       9.644  35.326 -20.442  1.00 18.89           C  
ANISOU 7621  CE1 HIS A 502     2404   2375   2401     95    -35     72       C  
ATOM   7622  NE2 HIS A 502       9.513  35.593 -19.155  1.00 14.66           N  
ANISOU 7622  NE2 HIS A 502     1864   1839   1867    101    -43     70       N  
ATOM   7623  H   HIS A 502       5.480  36.911 -19.044  1.00 15.64           H  
ATOM   7624  HA  HIS A 502       5.459  38.626 -21.102  1.00 15.32           H  
ATOM   7625  HB2 HIS A 502       7.724  38.433 -21.627  1.00 12.76           H  
ATOM   7626  HB3 HIS A 502       7.629  38.975 -20.136  1.00 12.76           H  
ATOM   7627  HD1 HIS A 502       8.847  36.218 -21.981  1.00 15.91           H  
ATOM   7628  HD2 HIS A 502       8.453  37.092 -18.206  1.00 15.96           H  
ATOM   7629  HE1 HIS A 502      10.153  34.638 -20.806  1.00 22.67           H  
ATOM   7630  N   CYS A 503       5.668  36.892 -22.871  1.00 12.86           N  
ANISOU 7630  N   CYS A 503     1701   1555   1629    112    -78     50       N  
ATOM   7631  CA  CYS A 503       5.654  35.761 -23.788  1.00 12.50           C  
ANISOU 7631  CA  CYS A 503     1647   1522   1582    108    -60     49       C  
ATOM   7632  C   CYS A 503       7.009  35.078 -23.709  1.00 12.37           C  
ANISOU 7632  C   CYS A 503     1615   1520   1565     99    -40     54       C  
ATOM   7633  O   CYS A 503       8.046  35.749 -23.744  1.00 13.67           O  
ANISOU 7633  O   CYS A 503     1782   1690   1723     82    -43     65       O  
ATOM   7634  CB  CYS A 503       5.383  36.204 -25.216  1.00 13.02           C  
ANISOU 7634  CB  CYS A 503     1728   1584   1634     96    -69     53       C  
ATOM   7635  SG  CYS A 503       5.523  34.838 -26.383  1.00 14.48           S  
ANISOU 7635  SG  CYS A 503     1904   1786   1812     88    -46     47       S  
ATOM   7636  H   CYS A 503       5.689  37.663 -23.250  1.00 15.43           H  
ATOM   7637  HA  CYS A 503       4.945  35.146 -23.543  1.00 15.00           H  
ATOM   7638  HB2 CYS A 503       4.484  36.562 -25.273  1.00 15.62           H  
ATOM   7639  HB3 CYS A 503       6.028  36.885 -25.466  1.00 15.62           H  
ATOM   7640  N   HIS A 504       7.009  33.753 -23.619  1.00 11.94           N  
ANISOU 7640  N   HIS A 504     1545   1472   1518    109    -21     48       N  
ATOM   7641  CA  HIS A 504       8.258  33.018 -23.508  1.00 14.35           C  
ANISOU 7641  CA  HIS A 504     1834   1792   1826    109     -2     52       C  
ATOM   7642  C   HIS A 504       8.909  32.701 -24.853  1.00 13.09           C  
ANISOU 7642  C   HIS A 504     1674   1644   1654     98     12     51       C  
ATOM   7643  O   HIS A 504       9.998  32.119 -24.870  1.00 14.35           O  
ANISOU 7643  O   HIS A 504     1818   1820   1814    102     29     52       O  
ATOM   7644  CB  HIS A 504       8.048  31.734 -22.713  1.00 12.67           C  
ANISOU 7644  CB  HIS A 504     1610   1577   1629    127     11     48       C  
ATOM   7645  CG  HIS A 504       9.203  31.403 -21.828  1.00 13.08           C  
ANISOU 7645  CG  HIS A 504     1643   1641   1686    134     20     58       C  
ATOM   7646  ND1 HIS A 504      10.465  31.160 -22.325  1.00 14.12           N  
ANISOU 7646  ND1 HIS A 504     1762   1789   1814    132     33     63       N  
ATOM   7647  CD2 HIS A 504       9.307  31.329 -20.480  1.00 16.27           C  
ANISOU 7647  CD2 HIS A 504     2036   2047   2097    142     16     66       C  
ATOM   7648  CE1 HIS A 504      11.290  30.909 -21.324  1.00 19.07           C  
ANISOU 7648  CE1 HIS A 504     2371   2429   2448    140     36     73       C  
ATOM   7649  NE2 HIS A 504      10.613  31.009 -20.192  1.00 16.02           N  
ANISOU 7649  NE2 HIS A 504     1986   2033   2067    145     25     76       N  
ATOM   7650  H   HIS A 504       6.302  33.263 -23.622  1.00 14.33           H  
ATOM   7651  HA  HIS A 504       8.886  33.570 -23.015  1.00 17.22           H  
ATOM   7652  HB2 HIS A 504       7.261  31.834 -22.154  1.00 15.21           H  
ATOM   7653  HB3 HIS A 504       7.924  30.997 -23.331  1.00 15.21           H  
ATOM   7654  HD1 HIS A 504      10.682  31.169 -23.157  1.00 16.94           H  
ATOM   7655  HD2 HIS A 504       8.623  31.468 -19.864  1.00 19.52           H  
ATOM   7656  HE1 HIS A 504      12.192  30.699 -21.402  1.00 22.89           H  
ATOM   7657  N   ILE A 505       8.312  33.096 -25.975  1.00 13.27           N  
ANISOU 7657  N   ILE A 505     1714   1664   1665     87      5     48       N  
ATOM   7658  CA  ILE A 505       9.040  33.045 -27.239  1.00 12.91           C  
ANISOU 7658  CA  ILE A 505     1669   1637   1601     71     16     48       C  
ATOM   7659  C   ILE A 505      10.118  34.120 -27.184  1.00 13.82           C  
ANISOU 7659  C   ILE A 505     1781   1766   1704     51     10     65       C  
ATOM   7660  O   ILE A 505       9.811  35.313 -27.072  1.00 13.53           O  
ANISOU 7660  O   ILE A 505     1761   1716   1663     37    -13     76       O  
ATOM   7661  CB  ILE A 505       8.102  33.241 -28.439  1.00 13.33           C  
ANISOU 7661  CB  ILE A 505     1739   1685   1639     61      7     42       C  
ATOM   7662  CG1 ILE A 505       7.098  32.081 -28.536  1.00 15.62           C  
ANISOU 7662  CG1 ILE A 505     2031   1966   1939     76     14     25       C  
ATOM   7663  CG2 ILE A 505       8.930  33.418 -29.719  1.00 14.68           C  
ANISOU 7663  CG2 ILE A 505     1911   1881   1785     40     17     46       C  
ATOM   7664  CD1 ILE A 505       5.930  32.341 -29.510  1.00 15.06           C  
ANISOU 7664  CD1 ILE A 505     1976   1892   1854     66      0     21       C  
ATOM   7665  H   ILE A 505       7.506  33.391 -26.030  1.00 15.93           H  
ATOM   7666  HA  ILE A 505       9.457  32.176 -27.346  1.00 15.50           H  
ATOM   7667  HB  ILE A 505       7.579  34.048 -28.315  1.00 15.99           H  
ATOM   7668 HG12 ILE A 505       7.567  31.289 -28.843  1.00 18.75           H  
ATOM   7669 HG13 ILE A 505       6.720  31.923 -27.657  1.00 18.75           H  
ATOM   7670 HG21 ILE A 505       8.342  33.355 -30.487  1.00 17.61           H  
ATOM   7671 HG22 ILE A 505       9.359  34.288 -29.700  1.00 17.61           H  
ATOM   7672 HG23 ILE A 505       9.602  32.719 -29.759  1.00 17.61           H  
ATOM   7673 HD11 ILE A 505       5.256  31.654 -29.384  1.00 18.07           H  
ATOM   7674 HD12 ILE A 505       5.551  33.214 -29.323  1.00 18.07           H  
ATOM   7675 HD13 ILE A 505       6.265  32.313 -30.420  1.00 18.07           H  
ATOM   7676  N   ALA A 506      11.389  33.702 -27.231  1.00 13.45           N  
ANISOU 7676  N   ALA A 506     1712   1745   1653     48     29     67       N  
ATOM   7677  CA  ALA A 506      12.496  34.637 -27.040  1.00 13.43           C  
ANISOU 7677  CA  ALA A 506     1701   1761   1640     25     24     84       C  
ATOM   7678  C   ALA A 506      12.416  35.830 -27.990  1.00 13.39           C  
ANISOU 7678  C   ALA A 506     1719   1757   1613     -9      7     97       C  
ATOM   7679  O   ALA A 506      12.698  36.966 -27.590  1.00 14.43           O  
ANISOU 7679  O   ALA A 506     1861   1882   1741    -31    -12    113       O  
ATOM   7680  CB  ALA A 506      13.831  33.908 -27.221  1.00 21.60           C  
ANISOU 7680  CB  ALA A 506     2704   2833   2668     28     49     83       C  
ATOM   7681  H   ALA A 506      11.635  32.890 -27.372  1.00 16.14           H  
ATOM   7682  HA  ALA A 506      12.449  34.980 -26.133  1.00 16.11           H  
ATOM   7683  HB1 ALA A 506      14.554  34.549 -27.138  1.00 25.91           H  
ATOM   7684  HB2 ALA A 506      13.913  33.225 -26.538  1.00 25.91           H  
ATOM   7685  HB3 ALA A 506      13.850  33.500 -28.101  1.00 25.91           H  
ATOM   7686  N   TRP A 507      12.032  35.595 -29.250  1.00 14.45           N  
ANISOU 7686  N   TRP A 507     1862   1897   1731    -15     13     92       N  
ATOM   7687  CA  TRP A 507      11.955  36.685 -30.215  1.00 14.15           C  
ANISOU 7687  CA  TRP A 507     1846   1860   1669    -48     -4    108       C  
ATOM   7688  C   TRP A 507      10.915  37.732 -29.823  1.00 15.09           C  
ANISOU 7688  C   TRP A 507     1996   1940   1798    -49    -37    117       C  
ATOM   7689  O   TRP A 507      11.073  38.916 -30.150  1.00 14.57           O  
ANISOU 7689  O   TRP A 507     1951   1865   1718    -77    -58    138       O  
ATOM   7690  CB  TRP A 507      11.616  36.149 -31.609  1.00 13.94           C  
ANISOU 7690  CB  TRP A 507     1824   1851   1623    -53      8    100       C  
ATOM   7691  CG  TRP A 507      12.183  34.801 -31.956  1.00 12.80           C  
ANISOU 7691  CG  TRP A 507     1653   1733   1476    -36     42     78       C  
ATOM   7692  CD1 TRP A 507      11.530  33.793 -32.602  1.00 13.78           C  
ANISOU 7692  CD1 TRP A 507     1782   1856   1599    -19     54     56       C  
ATOM   7693  CD2 TRP A 507      13.511  34.321 -31.705  1.00 13.15           C  
ANISOU 7693  CD2 TRP A 507     1667   1812   1519    -32     66     76       C  
ATOM   7694  NE1 TRP A 507      12.360  32.722 -32.777  1.00 15.79           N  
ANISOU 7694  NE1 TRP A 507     2013   2135   1852     -3     85     37       N  
ATOM   7695  CE2 TRP A 507      13.579  33.013 -32.228  1.00 16.11           C  
ANISOU 7695  CE2 TRP A 507     2030   2199   1894     -8     93     50       C  
ATOM   7696  CE3 TRP A 507      14.644  34.859 -31.085  1.00 14.89           C  
ANISOU 7696  CE3 TRP A 507     1867   2053   1738    -46     66     92       C  
ATOM   7697  CZ2 TRP A 507      14.716  32.233 -32.139  1.00 16.66           C  
ANISOU 7697  CZ2 TRP A 507     2068   2300   1963      9    120     40       C  
ATOM   7698  CZ3 TRP A 507      15.781  34.074 -31.003  1.00 15.85           C  
ANISOU 7698  CZ3 TRP A 507     1953   2212   1859    -32     94     84       C  
ATOM   7699  CH2 TRP A 507      15.805  32.775 -31.525  1.00 15.15           C  
ANISOU 7699  CH2 TRP A 507     1852   2133   1771     -2    120     58       C  
ATOM   7700  H   TRP A 507      11.815  34.825 -29.565  1.00 17.34           H  
ATOM   7701  HA  TRP A 507      12.827  37.109 -30.246  1.00 16.98           H  
ATOM   7702  HB2 TRP A 507      10.651  36.080 -31.680  1.00 16.73           H  
ATOM   7703  HB3 TRP A 507      11.953  36.778 -32.266  1.00 16.73           H  
ATOM   7704  HD1 TRP A 507      10.645  33.829 -32.885  1.00 16.54           H  
ATOM   7705  HE1 TRP A 507      12.151  31.985 -33.168  1.00 18.95           H  
ATOM   7706  HE3 TRP A 507      14.633  35.721 -30.737  1.00 17.87           H  
ATOM   7707  HZ2 TRP A 507      14.737  31.370 -32.484  1.00 19.99           H  
ATOM   7708  HZ3 TRP A 507      16.542  34.415 -30.593  1.00 19.03           H  
ATOM   7709  HH2 TRP A 507      16.582  32.271 -31.452  1.00 18.18           H  
ATOM   7710  N   HIS A 508       9.840  37.316 -29.147  1.00 14.83           N  
ANISOU 7710  N   HIS A 508     1965   1882   1786    -18    -43    103       N  
ATOM   7711  CA  HIS A 508       8.735  38.212 -28.827  1.00 13.78           C  
ANISOU 7711  CA  HIS A 508     1859   1717   1662    -10    -72    107       C  
ATOM   7712  C   HIS A 508       9.042  39.058 -27.601  1.00 13.32           C  
ANISOU 7712  C   HIS A 508     1806   1639   1615    -10    -87    112       C  
ATOM   7713  O   HIS A 508       8.848  40.277 -27.620  1.00 13.42           O  
ANISOU 7713  O   HIS A 508     1847   1629   1625    -22   -113    124       O  
ATOM   7714  CB  HIS A 508       7.464  37.387 -28.630  1.00 11.31           C  
ANISOU 7714  CB  HIS A 508     1541   1394   1363     21    -70     88       C  
ATOM   7715  CG  HIS A 508       6.994  36.715 -29.882  1.00 13.14           C  
ANISOU 7715  CG  HIS A 508     1773   1640   1580     18    -61     82       C  
ATOM   7716  ND1 HIS A 508       5.869  35.918 -29.928  1.00 12.82           N  
ANISOU 7716  ND1 HIS A 508     1728   1595   1547     36    -60     66       N  
ATOM   7717  CD2 HIS A 508       7.493  36.736 -31.141  1.00 14.61           C  
ANISOU 7717  CD2 HIS A 508     1964   1847   1742     -6    -55     88       C  
ATOM   7718  CE1 HIS A 508       5.700  35.472 -31.162  1.00 14.72           C  
ANISOU 7718  CE1 HIS A 508     1972   1852   1770     24    -53     62       C  
ATOM   7719  NE2 HIS A 508       6.669  35.958 -31.919  1.00 15.84           N  
ANISOU 7719  NE2 HIS A 508     2119   2008   1890      0    -50     75       N  
ATOM   7720  H   HIS A 508       9.727  36.512 -28.862  1.00 17.79           H  
ATOM   7721  HA  HIS A 508       8.587  38.825 -29.565  1.00 16.54           H  
ATOM   7722  HB2 HIS A 508       7.636  36.698 -27.970  1.00 13.58           H  
ATOM   7723  HB3 HIS A 508       6.754  37.972 -28.322  1.00 13.58           H  
ATOM   7724  HD2 HIS A 508       8.252  37.191 -31.426  1.00 17.54           H  
ATOM   7725  HE1 HIS A 508       5.016  34.912 -31.449  1.00 17.67           H  
ATOM   7726  HE2 HIS A 508       6.768  35.812 -32.761  1.00 19.00           H  
ATOM   7727  N   VAL A 509       9.551  38.445 -26.532  1.00 13.00           N  
ANISOU 7727  N   VAL A 509     1743   1608   1588      3    -72    104       N  
ATOM   7728  CA  VAL A 509       9.915  39.255 -25.377  1.00 10.99           C  
ANISOU 7728  CA  VAL A 509     1494   1340   1340     -2    -86    107       C  
ATOM   7729  C   VAL A 509      11.112  40.149 -25.713  1.00 11.98           C  
ANISOU 7729  C   VAL A 509     1627   1476   1450    -42    -94    127       C  
ATOM   7730  O   VAL A 509      11.152  41.314 -25.303  1.00 14.62           O  
ANISOU 7730  O   VAL A 509     1986   1786   1783    -58   -118    134       O  
ATOM   7731  CB  VAL A 509      10.135  38.382 -24.125  1.00 14.44           C  
ANISOU 7731  CB  VAL A 509     1905   1789   1792     20    -71     96       C  
ATOM   7732  CG1 VAL A 509      11.240  37.379 -24.272  1.00 14.63           C  
ANISOU 7732  CG1 VAL A 509     1898   1846   1814     16    -45     99       C  
ATOM   7733  CG2 VAL A 509      10.383  39.271 -22.933  1.00 15.69           C  
ANISOU 7733  CG2 VAL A 509     2072   1934   1954     14    -88     98       C  
ATOM   7734  H   VAL A 509       9.688  37.600 -26.454  1.00 15.60           H  
ATOM   7735  HA  VAL A 509       9.172  39.840 -25.163  1.00 13.19           H  
ATOM   7736  HB  VAL A 509       9.328  37.860 -23.992  1.00 17.33           H  
ATOM   7737 HG11 VAL A 509      11.247  36.800 -23.494  1.00 17.55           H  
ATOM   7738 HG12 VAL A 509      11.087  36.855 -25.074  1.00 17.55           H  
ATOM   7739 HG13 VAL A 509      12.086  37.849 -24.341  1.00 17.55           H  
ATOM   7740 HG21 VAL A 509      10.671  38.724 -22.185  1.00 18.82           H  
ATOM   7741 HG22 VAL A 509      11.074  39.914 -23.157  1.00 18.82           H  
ATOM   7742 HG23 VAL A 509       9.562  39.734 -22.708  1.00 18.82           H  
ATOM   7743  N   SER A 510      12.072  39.651 -26.502  1.00 14.32           N  
ANISOU 7743  N   SER A 510     1903   1807   1730    -61    -73    135       N  
ATOM   7744  CA  SER A 510      13.124  40.517 -27.033  1.00 15.28           C  
ANISOU 7744  CA  SER A 510     2031   1945   1832   -106    -80    156       C  
ATOM   7745  C   SER A 510      12.538  41.738 -27.725  1.00 13.53           C  
ANISOU 7745  C   SER A 510     1851   1691   1600   -128   -109    171       C  
ATOM   7746  O   SER A 510      13.052  42.858 -27.591  1.00 14.66           O  
ANISOU 7746  O   SER A 510     2016   1821   1735   -162   -129    188       O  
ATOM   7747  CB  SER A 510      13.985  39.734 -28.027  1.00 18.20           C  
ANISOU 7747  CB  SER A 510     2372   2362   2183   -118    -52    159       C  
ATOM   7748  OG  SER A 510      14.809  40.589 -28.801  1.00 23.82           O  
ANISOU 7748  OG  SER A 510     3090   3093   2869   -166    -58    182       O  
ATOM   7749  H   SER A 510      12.135  38.827 -26.741  1.00 17.18           H  
ATOM   7750  HA  SER A 510      13.682  40.814 -26.297  1.00 18.34           H  
ATOM   7751  HB2 SER A 510      14.551  39.120 -27.533  1.00 21.84           H  
ATOM   7752  HB3 SER A 510      13.401  39.240 -28.623  1.00 21.84           H  
ATOM   7753  HG  SER A 510      15.556  40.682 -28.429  1.00 28.59           H  
ATOM   7754  N   GLY A 511      11.485  41.524 -28.507  1.00 15.15           N  
ANISOU 7754  N   GLY A 511     2070   1883   1804   -110   -113    166       N  
ATOM   7755  CA  GLY A 511      10.839  42.549 -29.286  1.00 15.12           C  
ANISOU 7755  CA  GLY A 511     2104   1850   1791   -124   -141    182       C  
ATOM   7756  C   GLY A 511       9.789  43.372 -28.585  1.00 15.82           C  
ANISOU 7756  C   GLY A 511     2224   1890   1899   -100   -171    177       C  
ATOM   7757  O   GLY A 511       9.121  44.170 -29.250  1.00 17.17           O  
ANISOU 7757  O   GLY A 511     2427   2034   2064   -102   -196    190       O  
ATOM   7758  H   GLY A 511      11.117  40.753 -28.601  1.00 18.18           H  
ATOM   7759  HA2 GLY A 511      11.520  43.162 -29.604  1.00 18.14           H  
ATOM   7760  HA3 GLY A 511      10.413  42.127 -30.048  1.00 18.14           H  
ATOM   7761  N   GLY A 512       9.593  43.194 -27.281  1.00 12.72           N  
ANISOU 7761  N   GLY A 512     1822   1486   1526    -73   -169    158       N  
ATOM   7762  CA  GLY A 512       8.739  44.078 -26.508  1.00 12.93           C  
ANISOU 7762  CA  GLY A 512     1877   1468   1568    -50   -196    150       C  
ATOM   7763  C   GLY A 512       7.586  43.423 -25.768  1.00 14.40           C  
ANISOU 7763  C   GLY A 512     2048   1651   1773     -1   -190    125       C  
ATOM   7764  O   GLY A 512       6.891  44.123 -25.016  1.00 14.38           O  
ANISOU 7764  O   GLY A 512     2064   1617   1782     22   -210    113       O  
ATOM   7765  H   GLY A 512       9.949  42.560 -26.822  1.00 15.27           H  
ATOM   7766  HA2 GLY A 512       9.288  44.530 -25.847  1.00 15.52           H  
ATOM   7767  HA3 GLY A 512       8.360  44.739 -27.108  1.00 15.52           H  
ATOM   7768  N   LEU A 513       7.360  42.113 -25.884  1.00 14.00           N  
ANISOU 7768  N   LEU A 513     1964   1630   1724     14   -164    114       N  
ATOM   7769  CA  LEU A 513       6.138  41.496 -25.364  1.00 11.44           C  
ANISOU 7769  CA  LEU A 513     1627   1306   1415     54   -160     94       C  
ATOM   7770  C   LEU A 513       6.290  41.100 -23.898  1.00 13.33           C  
ANISOU 7770  C   LEU A 513     1847   1551   1667     70   -149     78       C  
ATOM   7771  O   LEU A 513       6.590  39.951 -23.563  1.00 13.76           O  
ANISOU 7771  O   LEU A 513     1874   1631   1726     74   -125     72       O  
ATOM   7772  CB  LEU A 513       5.756  40.287 -26.217  1.00 13.39           C  
ANISOU 7772  CB  LEU A 513     1852   1577   1657     59   -141     90       C  
ATOM   7773  CG  LEU A 513       4.249  40.046 -26.348  1.00 11.26           C  
ANISOU 7773  CG  LEU A 513     1581   1304   1395     89   -149     79       C  
ATOM   7774  CD1 LEU A 513       3.989  38.940 -27.364  1.00 14.53           C  
ANISOU 7774  CD1 LEU A 513     1980   1742   1800     83   -132     76       C  
ATOM   7775  CD2 LEU A 513       3.625  39.719 -24.993  1.00 13.60           C  
ANISOU 7775  CD2 LEU A 513     1861   1601   1707    118   -145     60       C  
ATOM   7776  H   LEU A 513       7.901  41.561 -26.261  1.00 16.80           H  
ATOM   7777  HA  LEU A 513       5.443  42.172 -25.397  1.00 13.73           H  
ATOM   7778  HB2 LEU A 513       6.111  40.417 -27.110  1.00 16.06           H  
ATOM   7779  HB3 LEU A 513       6.145  39.494 -25.817  1.00 16.06           H  
ATOM   7780  HG  LEU A 513       3.820  40.856 -26.667  1.00 13.52           H  
ATOM   7781 HD11 LEU A 513       3.032  38.804 -27.445  1.00 17.44           H  
ATOM   7782 HD12 LEU A 513       4.359  39.205 -28.221  1.00 17.44           H  
ATOM   7783 HD13 LEU A 513       4.414  38.124 -27.058  1.00 17.44           H  
ATOM   7784 HD21 LEU A 513       3.707  40.492 -24.413  1.00 16.32           H  
ATOM   7785 HD22 LEU A 513       2.689  39.500 -25.121  1.00 16.32           H  
ATOM   7786 HD23 LEU A 513       4.092  38.963 -24.604  1.00 16.32           H  
ATOM   7787  N   GLY A 514       6.017  42.050 -23.004  1.00 13.93           N  
ANISOU 7787  N   GLY A 514     1942   1603   1749     81   -168     70       N  
ATOM   7788  CA  GLY A 514       6.072  41.790 -21.578  1.00 14.71           C  
ANISOU 7788  CA  GLY A 514     2025   1709   1856     96   -161     54       C  
ATOM   7789  C   GLY A 514       5.602  42.995 -20.796  1.00 14.67           C  
ANISOU 7789  C   GLY A 514     2047   1673   1854    111   -185     42       C  
ATOM   7790  O   GLY A 514       5.492  44.102 -21.326  1.00 12.89           O  
ANISOU 7790  O   GLY A 514     1856   1416   1628    105   -209     48       O  
ATOM   7791  H   GLY A 514       5.796  42.857 -23.203  1.00 16.72           H  
ATOM   7792  HA2 GLY A 514       5.503  41.036 -21.360  1.00 17.66           H  
ATOM   7793  HA3 GLY A 514       6.983  41.585 -21.317  1.00 17.66           H  
ATOM   7794  N   VAL A 515       5.318  42.756 -19.513  1.00 13.00           N  
ANISOU 7794  N   VAL A 515     1821   1472   1648    130   -178     23       N  
ATOM   7795  CA  VAL A 515       5.065  43.805 -18.533  1.00 11.24           C  
ANISOU 7795  CA  VAL A 515     1620   1224   1425    144   -197      4       C  
ATOM   7796  C   VAL A 515       5.735  43.385 -17.231  1.00 12.94           C  
ANISOU 7796  C   VAL A 515     1817   1464   1637    136   -183     -4       C  
ATOM   7797  O   VAL A 515       6.144  42.234 -17.062  1.00 12.52           O  
ANISOU 7797  O   VAL A 515     1731   1444   1583    129   -161      5       O  
ATOM   7798  CB  VAL A 515       3.569  44.068 -18.262  1.00 12.70           C  
ANISOU 7798  CB  VAL A 515     1807   1401   1616    189   -206    -17       C  
ATOM   7799  CG1 VAL A 515       2.821  44.489 -19.531  1.00 13.64           C  
ANISOU 7799  CG1 VAL A 515     1943   1499   1739    201   -222     -7       C  
ATOM   7800  CG2 VAL A 515       2.905  42.837 -17.648  1.00 16.37           C  
ANISOU 7800  CG2 VAL A 515     2231   1907   2083    209   -182    -27       C  
ATOM   7801  H   VAL A 515       5.265  41.965 -19.181  1.00 15.60           H  
ATOM   7802  HA  VAL A 515       5.452  44.629 -18.867  1.00 13.48           H  
ATOM   7803  HB  VAL A 515       3.513  44.802 -17.631  1.00 15.24           H  
ATOM   7804 HG11 VAL A 515       1.923  44.767 -19.290  1.00 16.36           H  
ATOM   7805 HG12 VAL A 515       3.295  45.225 -19.947  1.00 16.36           H  
ATOM   7806 HG13 VAL A 515       2.782  43.734 -20.139  1.00 16.36           H  
ATOM   7807 HG21 VAL A 515       2.832  42.148 -18.326  1.00 19.65           H  
ATOM   7808 HG22 VAL A 515       3.450  42.520 -16.911  1.00 19.65           H  
ATOM   7809 HG23 VAL A 515       2.023  43.081 -17.327  1.00 19.65           H  
ATOM   7810  N   VAL A 516       5.771  44.313 -16.281  1.00 13.20           N  
ANISOU 7810  N   VAL A 516     1870   1478   1666    140   -198    -22       N  
ATOM   7811  CA  VAL A 516       6.316  44.057 -14.954  1.00 11.35           C  
ANISOU 7811  CA  VAL A 516     1621   1268   1425    132   -190    -32       C  
ATOM   7812  C   VAL A 516       5.202  44.285 -13.947  1.00 12.77           C  
ANISOU 7812  C   VAL A 516     1800   1450   1604    171   -192    -62       C  
ATOM   7813  O   VAL A 516       4.735  45.417 -13.772  1.00 14.80           O  
ANISOU 7813  O   VAL A 516     2090   1673   1861    187   -212    -82       O  
ATOM   7814  CB  VAL A 516       7.519  44.948 -14.621  1.00 12.83           C  
ANISOU 7814  CB  VAL A 516     1832   1440   1603     94   -205    -28       C  
ATOM   7815  CG1 VAL A 516       8.018  44.632 -13.184  1.00 16.20           C  
ANISOU 7815  CG1 VAL A 516     2239   1898   2019     88   -197    -39       C  
ATOM   7816  CG2 VAL A 516       8.624  44.741 -15.610  1.00 14.86           C  
ANISOU 7816  CG2 VAL A 516     2084   1704   1858     55   -202      2       C  
ATOM   7817  H   VAL A 516       5.477  45.115 -16.386  1.00 15.84           H  
ATOM   7818  HA  VAL A 516       6.598  43.130 -14.916  1.00 13.62           H  
ATOM   7819  HB  VAL A 516       7.248  45.878 -14.666  1.00 15.40           H  
ATOM   7820 HG11 VAL A 516       8.841  45.119 -13.022  1.00 19.44           H  
ATOM   7821 HG12 VAL A 516       7.340  44.907 -12.546  1.00 19.44           H  
ATOM   7822 HG13 VAL A 516       8.177  43.678 -13.107  1.00 19.44           H  
ATOM   7823 HG21 VAL A 516       8.341  45.079 -16.474  1.00 17.83           H  
ATOM   7824 HG22 VAL A 516       9.411  45.220 -15.308  1.00 17.83           H  
ATOM   7825 HG23 VAL A 516       8.817  43.793 -15.673  1.00 17.83           H  
ATOM   7826  N   TYR A 517       4.774  43.223 -13.283  1.00 13.31           N  
ANISOU 7826  N   TYR A 517     1831   1556   1669    185   -171    -66       N  
ATOM   7827  CA  TYR A 517       3.882  43.385 -12.151  1.00 13.55           C  
ANISOU 7827  CA  TYR A 517     1854   1600   1692    215   -169    -95       C  
ATOM   7828  C   TYR A 517       4.710  43.830 -10.954  1.00 14.58           C  
ANISOU 7828  C   TYR A 517     1994   1738   1809    197   -174   -106       C  
ATOM   7829  O   TYR A 517       5.612  43.109 -10.510  1.00 15.62           O  
ANISOU 7829  O   TYR A 517     2104   1897   1934    172   -162    -90       O  
ATOM   7830  CB  TYR A 517       3.159  42.088 -11.845  1.00 15.45           C  
ANISOU 7830  CB  TYR A 517     2054   1883   1932    230   -146    -91       C  
ATOM   7831  CG  TYR A 517       2.093  41.700 -12.829  1.00 14.98           C  
ANISOU 7831  CG  TYR A 517     1985   1823   1883    250   -143    -87       C  
ATOM   7832  CD1 TYR A 517       0.977  42.499 -13.033  1.00 16.91           C  
ANISOU 7832  CD1 TYR A 517     2241   2053   2130    285   -156   -108       C  
ATOM   7833  CD2 TYR A 517       2.174  40.502 -13.518  1.00 15.67           C  
ANISOU 7833  CD2 TYR A 517     2051   1927   1977    238   -127    -64       C  
ATOM   7834  CE1 TYR A 517      -0.027  42.118 -13.916  1.00 14.14           C  
ANISOU 7834  CE1 TYR A 517     1877   1709   1787    302   -155   -103       C  
ATOM   7835  CE2 TYR A 517       1.177  40.108 -14.401  1.00 15.69           C  
ANISOU 7835  CE2 TYR A 517     2044   1932   1986    252   -125    -62       C  
ATOM   7836  CZ  TYR A 517       0.081  40.922 -14.605  1.00 13.23           C  
ANISOU 7836  CZ  TYR A 517     1741   1611   1676    283   -139    -80       C  
ATOM   7837  OH  TYR A 517      -0.912  40.518 -15.473  1.00 17.00           O  
ANISOU 7837  OH  TYR A 517     2205   2097   2158    296   -139    -76       O  
ATOM   7838  H   TYR A 517       4.984  42.410 -13.467  1.00 15.97           H  
ATOM   7839  HA  TYR A 517       3.210  44.055 -12.351  1.00 16.25           H  
ATOM   7840  HB2 TYR A 517       3.811  41.370 -11.827  1.00 18.53           H  
ATOM   7841  HB3 TYR A 517       2.734  42.172 -10.976  1.00 18.53           H  
ATOM   7842  HD1 TYR A 517       0.899  43.302 -12.572  1.00 20.29           H  
ATOM   7843  HD2 TYR A 517       2.911  39.951 -13.388  1.00 18.81           H  
ATOM   7844  HE1 TYR A 517      -0.768  42.665 -14.044  1.00 16.97           H  
ATOM   7845  HE2 TYR A 517       1.247  39.298 -14.853  1.00 18.83           H  
ATOM   7846  HH  TYR A 517      -1.526  41.091 -15.494  1.00 20.40           H  
ATOM   7847  N   LEU A 518       4.425  45.021 -10.450  1.00 14.74           N  
ANISOU 7847  N   LEU A 518     2046   1732   1824    210   -192   -135       N  
ATOM   7848  CA  LEU A 518       5.118  45.563  -9.287  1.00 15.41           C  
ANISOU 7848  CA  LEU A 518     2143   1820   1892    193   -199   -152       C  
ATOM   7849  C   LEU A 518       4.184  45.325  -8.109  1.00 13.04           C  
ANISOU 7849  C   LEU A 518     1823   1553   1578    225   -187   -182       C  
ATOM   7850  O   LEU A 518       3.238  46.085  -7.875  1.00 14.70           O  
ANISOU 7850  O   LEU A 518     2050   1747   1787    261   -195   -214       O  
ATOM   7851  CB  LEU A 518       5.466  47.029  -9.472  1.00 15.90           C  
ANISOU 7851  CB  LEU A 518     2258   1827   1955    183   -227   -167       C  
ATOM   7852  CG  LEU A 518       6.236  47.665  -8.314  1.00 18.28           C  
ANISOU 7852  CG  LEU A 518     2579   2130   2238    158   -238   -187       C  
ATOM   7853  CD1 LEU A 518       7.441  46.828  -7.943  1.00 18.29           C  
ANISOU 7853  CD1 LEU A 518     2548   2174   2228    116   -226   -160       C  
ATOM   7854  CD2 LEU A 518       6.649  49.085  -8.672  1.00 19.32           C  
ANISOU 7854  CD2 LEU A 518     2768   2200   2373    140   -268   -198       C  
ATOM   7855  H   LEU A 518       3.822  45.544 -10.770  1.00 17.69           H  
ATOM   7856  HA  LEU A 518       5.958  45.101  -9.139  1.00 18.49           H  
ATOM   7857  HB2 LEU A 518       6.015  47.115 -10.267  1.00 19.08           H  
ATOM   7858  HB3 LEU A 518       4.642  47.528  -9.581  1.00 19.08           H  
ATOM   7859  HG  LEU A 518       5.660  47.706  -7.534  1.00 21.94           H  
ATOM   7860 HD11 LEU A 518       8.116  47.403  -7.550  1.00 21.95           H  
ATOM   7861 HD12 LEU A 518       7.170  46.151  -7.303  1.00 21.95           H  
ATOM   7862 HD13 LEU A 518       7.791  46.406  -8.743  1.00 21.95           H  
ATOM   7863 HD21 LEU A 518       7.287  49.403  -8.015  1.00 23.18           H  
ATOM   7864 HD22 LEU A 518       7.054  49.083  -9.554  1.00 23.18           H  
ATOM   7865 HD23 LEU A 518       5.862  49.652  -8.671  1.00 23.18           H  
ATOM   7866  N   GLU A 519       4.465  44.256  -7.380  1.00 14.61           N  
ANISOU 7866  N   GLU A 519     1984   1801   1765    213   -168   -168       N  
ATOM   7867  CA  GLU A 519       3.566  43.710  -6.380  1.00 13.29           C  
ANISOU 7867  CA  GLU A 519     1788   1678   1583    237   -151   -186       C  
ATOM   7868  C   GLU A 519       4.004  44.182  -5.001  1.00 11.85           C  
ANISOU 7868  C   GLU A 519     1613   1515   1375    226   -155   -209       C  
ATOM   7869  O   GLU A 519       5.117  43.877  -4.555  1.00 14.13           O  
ANISOU 7869  O   GLU A 519     1895   1819   1654    190   -156   -191       O  
ATOM   7870  CB  GLU A 519       3.563  42.188  -6.464  1.00 13.98           C  
ANISOU 7870  CB  GLU A 519     1833   1805   1673    227   -130   -153       C  
ATOM   7871  CG  GLU A 519       2.676  41.512  -5.461  1.00 13.80           C  
ANISOU 7871  CG  GLU A 519     1779   1832   1633    243   -112   -163       C  
ATOM   7872  CD  GLU A 519       2.683  40.019  -5.650  1.00 18.58           C  
ANISOU 7872  CD  GLU A 519     2351   2465   2244    231    -94   -127       C  
ATOM   7873  OE1 GLU A 519       3.116  39.580  -6.738  1.00 17.78           O  
ANISOU 7873  OE1 GLU A 519     2252   2342   2163    220    -94   -102       O  
ATOM   7874  OE2 GLU A 519       2.265  39.293  -4.725  1.00 21.57           O  
ANISOU 7874  OE2 GLU A 519     2702   2887   2606    230    -80   -124       O  
ATOM   7875  H   GLU A 519       5.199  43.814  -7.452  1.00 17.53           H  
ATOM   7876  HA  GLU A 519       2.663  44.034  -6.527  1.00 15.94           H  
ATOM   7877  HB2 GLU A 519       3.258  41.928  -7.347  1.00 16.77           H  
ATOM   7878  HB3 GLU A 519       4.467  41.869  -6.318  1.00 16.77           H  
ATOM   7879  HG2 GLU A 519       2.993  41.709  -4.565  1.00 16.56           H  
ATOM   7880  HG3 GLU A 519       1.766  41.831  -5.568  1.00 16.56           H  
ATOM   7881  N   ARG A 520       3.134  44.944  -4.344  1.00 13.67           N  
ANISOU 7881  N   ARG A 520     1856   1745   1593    258   -159   -251       N  
ATOM   7882  CA  ARG A 520       3.305  45.335  -2.949  1.00 13.45           C  
ANISOU 7882  CA  ARG A 520     1832   1743   1536    253   -159   -281       C  
ATOM   7883  C   ARG A 520       4.678  45.961  -2.716  1.00 19.22           C  
ANISOU 7883  C   ARG A 520     2592   2451   2260    211   -178   -278       C  
ATOM   7884  O   ARG A 520       5.480  45.508  -1.896  1.00 16.55           O  
ANISOU 7884  O   ARG A 520     2238   2150   1902    180   -174   -266       O  
ATOM   7885  CB  ARG A 520       3.081  44.133  -2.029  1.00 16.36           C  
ANISOU 7885  CB  ARG A 520     2154   2180   1884    248   -136   -268       C  
ATOM   7886  CG  ARG A 520       1.678  43.565  -2.150  1.00 15.09           C  
ANISOU 7886  CG  ARG A 520     1962   2047   1725    284   -118   -273       C  
ATOM   7887  CD  ARG A 520       1.537  42.221  -1.496  1.00 15.98           C  
ANISOU 7887  CD  ARG A 520     2031   2220   1822    270    -96   -247       C  
ATOM   7888  NE  ARG A 520       1.881  42.270  -0.081  1.00 17.33           N  
ANISOU 7888  NE  ARG A 520     2194   2432   1957    255    -93   -261       N  
ATOM   7889  CZ  ARG A 520       1.894  41.215   0.725  1.00 20.43           C  
ANISOU 7889  CZ  ARG A 520     2553   2880   2329    237    -78   -238       C  
ATOM   7890  NH1 ARG A 520       1.544  40.024   0.262  1.00 20.21           N  
ANISOU 7890  NH1 ARG A 520     2497   2867   2314    232    -64   -201       N  
ATOM   7891  NH2 ARG A 520       2.242  41.355   1.996  1.00 18.52           N  
ANISOU 7891  NH2 ARG A 520     2309   2677   2052    222    -78   -251       N  
ATOM   7892  H   ARG A 520       2.414  45.255  -4.697  1.00 16.40           H  
ATOM   7893  HA  ARG A 520       2.644  46.012  -2.736  1.00 16.14           H  
ATOM   7894  HB2 ARG A 520       3.711  43.433  -2.263  1.00 19.63           H  
ATOM   7895  HB3 ARG A 520       3.217  44.408  -1.109  1.00 19.63           H  
ATOM   7896  HG2 ARG A 520       1.053  44.172  -1.724  1.00 18.11           H  
ATOM   7897  HG3 ARG A 520       1.457  43.466  -3.089  1.00 18.11           H  
ATOM   7898  HD2 ARG A 520       0.618  41.922  -1.576  1.00 19.18           H  
ATOM   7899  HD3 ARG A 520       2.131  41.590  -1.932  1.00 19.18           H  
ATOM   7900  HE  ARG A 520       2.090  43.034   0.255  1.00 20.79           H  
ATOM   7901 HH11 ARG A 520       1.308  39.935  -0.560  1.00 24.25           H  
ATOM   7902 HH12 ARG A 520       1.552  39.340   0.783  1.00 24.25           H  
ATOM   7903 HH21 ARG A 520       2.459  42.130   2.300  1.00 22.23           H  
ATOM   7904 HH22 ARG A 520       2.250  40.671   2.518  1.00 22.23           H  
ATOM   7905  N   ALA A 521       4.933  47.034  -3.465  1.00 16.18           N  
ANISOU 7905  N   ALA A 521     2252   2006   1891    208   -200   -287       N  
ATOM   7906  CA  ALA A 521       6.266  47.616  -3.492  1.00 18.62           C  
ANISOU 7906  CA  ALA A 521     2589   2290   2196    161   -220   -277       C  
ATOM   7907  C   ALA A 521       6.709  48.057  -2.107  1.00 15.71           C  
ANISOU 7907  C   ALA A 521     2230   1944   1796    142   -226   -306       C  
ATOM   7908  O   ALA A 521       7.876  47.879  -1.737  1.00 18.67           O  
ANISOU 7908  O   ALA A 521     2598   2338   2157     97   -231   -287       O  
ATOM   7909  CB  ALA A 521       6.302  48.799  -4.456  1.00 18.59           C  
ANISOU 7909  CB  ALA A 521     2638   2214   2212    161   -244   -285       C  
ATOM   7910  H   ALA A 521       4.357  47.439  -3.960  1.00 19.42           H  
ATOM   7911  HA  ALA A 521       6.889  46.943  -3.810  1.00 22.35           H  
ATOM   7912  HB1 ALA A 521       7.224  48.980  -4.699  1.00 22.31           H  
ATOM   7913  HB2 ALA A 521       5.788  48.577  -5.247  1.00 22.31           H  
ATOM   7914  HB3 ALA A 521       5.918  49.575  -4.018  1.00 22.31           H  
ATOM   7915  N   ASP A 522       5.792  48.635  -1.324  1.00 18.10           N  
ANISOU 7915  N   ASP A 522     2547   2248   2084    179   -225   -355       N  
ATOM   7916  CA  ASP A 522       6.162  49.090   0.010  1.00 15.84           C  
ANISOU 7916  CA  ASP A 522     2272   1984   1762    162   -230   -388       C  
ATOM   7917  C   ASP A 522       6.561  47.916   0.888  1.00 17.45           C  
ANISOU 7917  C   ASP A 522     2426   2264   1943    140   -212   -363       C  
ATOM   7918  O   ASP A 522       7.507  48.015   1.677  1.00 19.50           O  
ANISOU 7918  O   ASP A 522     2687   2546   2178    100   -221   -362       O  
ATOM   7919  CB  ASP A 522       5.012  49.850   0.669  1.00 18.68           C  
ANISOU 7919  CB  ASP A 522     2652   2336   2109    212   -229   -448       C  
ATOM   7920  CG  ASP A 522       4.763  51.204   0.046  1.00 37.17           C  
ANISOU 7920  CG  ASP A 522     5054   4597   4470    233   -254   -479       C  
ATOM   7921  OD1 ASP A 522       5.681  51.753  -0.600  1.00 34.74           O  
ANISOU 7921  OD1 ASP A 522     4782   4240   4177    194   -276   -460       O  
ATOM   7922  OD2 ASP A 522       3.642  51.727   0.223  1.00 46.34           O  
ANISOU 7922  OD2 ASP A 522     6229   5746   5633    288   -251   -522       O  
ATOM   7923  H   ASP A 522       4.970  48.771  -1.537  1.00 21.72           H  
ATOM   7924  HA  ASP A 522       6.912  49.699  -0.077  1.00 19.01           H  
ATOM   7925  HB2 ASP A 522       4.199  49.328   0.583  1.00 22.42           H  
ATOM   7926  HB3 ASP A 522       5.221  49.986   1.607  1.00 22.42           H  
ATOM   7927  N   ASP A 523       5.828  46.802   0.784  1.00 16.22           N  
ANISOU 7927  N   ASP A 523     2225   2148   1792    164   -188   -342       N  
ATOM   7928  CA  ASP A 523       6.191  45.604   1.533  1.00 14.75           C  
ANISOU 7928  CA  ASP A 523     1992   2027   1585    143   -172   -311       C  
ATOM   7929  C   ASP A 523       7.534  45.059   1.059  1.00 18.92           C  
ANISOU 7929  C   ASP A 523     2509   2555   2125     99   -179   -261       C  
ATOM   7930  O   ASP A 523       8.339  44.590   1.872  1.00 18.97           O  
ANISOU 7930  O   ASP A 523     2494   2604   2108     69   -180   -243       O  
ATOM   7931  CB  ASP A 523       5.117  44.529   1.388  1.00 17.44           C  
ANISOU 7931  CB  ASP A 523     2292   2402   1932    174   -147   -295       C  
ATOM   7932  CG  ASP A 523       3.828  44.855   2.128  1.00 22.67           C  
ANISOU 7932  CG  ASP A 523     2951   3091   2573    213   -135   -340       C  
ATOM   7933  OD1 ASP A 523       3.816  45.697   3.054  1.00 22.00           O  
ANISOU 7933  OD1 ASP A 523     2886   3012   2460    216   -142   -384       O  
ATOM   7934  OD2 ASP A 523       2.812  44.220   1.784  1.00 21.47           O  
ANISOU 7934  OD2 ASP A 523     2770   2956   2430    241   -117   -333       O  
ATOM   7935  H   ASP A 523       5.127  46.716   0.294  1.00 19.47           H  
ATOM   7936  HA  ASP A 523       6.255  45.838   2.472  1.00 17.70           H  
ATOM   7937  HB2 ASP A 523       4.901  44.425   0.448  1.00 20.93           H  
ATOM   7938  HB3 ASP A 523       5.459  43.694   1.744  1.00 20.93           H  
ATOM   7939  N   LEU A 524       7.781  45.088  -0.255  1.00 17.21           N  
ANISOU 7939  N   LEU A 524     2302   2296   1942     97   -184   -238       N  
ATOM   7940  CA  LEU A 524       9.066  44.637  -0.782  1.00 16.08           C  
ANISOU 7940  CA  LEU A 524     2147   2154   1809     59   -190   -194       C  
ATOM   7941  C   LEU A 524      10.211  45.437  -0.174  1.00 17.79           C  
ANISOU 7941  C   LEU A 524     2384   2371   2004     16   -212   -203       C  
ATOM   7942  O   LEU A 524      11.188  44.868   0.327  1.00 18.71           O  
ANISOU 7942  O   LEU A 524     2473   2529   2106    -15   -213   -176       O  
ATOM   7943  CB  LEU A 524       9.083  44.754  -2.307  1.00 17.62           C  
ANISOU 7943  CB  LEU A 524     2355   2301   2038     63   -193   -176       C  
ATOM   7944  CG  LEU A 524      10.430  44.475  -2.971  1.00 18.31           C  
ANISOU 7944  CG  LEU A 524     2432   2389   2135     24   -199   -137       C  
ATOM   7945  CD1 LEU A 524      10.874  43.043  -2.815  1.00 16.53           C  
ANISOU 7945  CD1 LEU A 524     2158   2212   1910     21   -182    -97       C  
ATOM   7946  CD2 LEU A 524      10.330  44.809  -4.454  1.00 23.94           C  
ANISOU 7946  CD2 LEU A 524     3166   3055   2877     28   -203   -126       C  
ATOM   7947  H   LEU A 524       7.228  45.361  -0.854  1.00 20.65           H  
ATOM   7948  HA  LEU A 524       9.186  43.703  -0.551  1.00 19.30           H  
ATOM   7949  HB2 LEU A 524       8.444  44.120  -2.669  1.00 21.14           H  
ATOM   7950  HB3 LEU A 524       8.824  45.658  -2.546  1.00 21.14           H  
ATOM   7951  HG  LEU A 524      11.098  45.026  -2.536  1.00 21.97           H  
ATOM   7952 HD11 LEU A 524      11.822  42.984  -3.013  1.00 19.83           H  
ATOM   7953 HD12 LEU A 524      10.708  42.758  -1.903  1.00 19.83           H  
ATOM   7954 HD13 LEU A 524      10.373  42.488  -3.432  1.00 19.83           H  
ATOM   7955 HD21 LEU A 524       9.700  44.203  -4.873  1.00 28.73           H  
ATOM   7956 HD22 LEU A 524      10.023  45.724  -4.551  1.00 28.73           H  
ATOM   7957 HD23 LEU A 524      11.206  44.710  -4.859  1.00 28.73           H  
ATOM   7958  N   ARG A 525      10.111  46.766  -0.225  1.00 17.63           N  
ANISOU 7958  N   ARG A 525     2412   2304   1982     12   -231   -241       N  
ATOM   7959  CA  ARG A 525      11.149  47.613   0.343  1.00 17.89           C  
ANISOU 7959  CA  ARG A 525     2471   2333   1994    -34   -254   -253       C  
ATOM   7960  C   ARG A 525      11.384  47.273   1.808  1.00 21.73           C  
ANISOU 7960  C   ARG A 525     2934   2880   2442    -47   -251   -264       C  
ATOM   7961  O   ARG A 525      12.529  47.243   2.271  1.00 19.49           O  
ANISOU 7961  O   ARG A 525     2641   2626   2140    -92   -263   -247       O  
ATOM   7962  CB  ARG A 525      10.763  49.084   0.182  1.00 21.56           C  
ANISOU 7962  CB  ARG A 525     2998   2733   2462    -28   -275   -299       C  
ATOM   7963  CG  ARG A 525      11.870  50.060   0.560  1.00 27.79           C  
ANISOU 7963  CG  ARG A 525     3822   3504   3232    -84   -302   -311       C  
ATOM   7964  CD  ARG A 525      11.454  51.529   0.413  1.00 25.65           C  
ANISOU 7964  CD  ARG A 525     3621   3159   2967    -77   -325   -357       C  
ATOM   7965  NE  ARG A 525      10.159  51.715  -0.236  1.00 73.62           N  
ANISOU 7965  NE  ARG A 525     9712   9193   9067    -16   -317   -375       N  
ATOM   7966  CZ  ARG A 525       9.023  51.983   0.405  1.00 96.12           C  
ANISOU 7966  CZ  ARG A 525    12572  12041  11908     35   -309   -422       C  
ATOM   7967  NH1 ARG A 525       8.997  52.100   1.727  1.00 68.09           N  
ANISOU 7967  NH1 ARG A 525     9021   8528   8323     32   -307   -458       N  
ATOM   7968  NH2 ARG A 525       7.903  52.136  -0.285  1.00 69.67           N  
ANISOU 7968  NH2 ARG A 525     9232   8657   8582     89   -304   -433       N  
ATOM   7969  H   ARG A 525       9.457  47.198  -0.581  1.00 21.15           H  
ATOM   7970  HA  ARG A 525      11.980  47.468  -0.136  1.00 21.47           H  
ATOM   7971  HB2 ARG A 525      10.531  49.245  -0.746  1.00 25.88           H  
ATOM   7972  HB3 ARG A 525       9.999  49.269   0.751  1.00 25.88           H  
ATOM   7973  HG2 ARG A 525      12.118  49.912   1.486  1.00 33.34           H  
ATOM   7974  HG3 ARG A 525      12.634  49.908  -0.017  1.00 33.34           H  
ATOM   7975  HD2 ARG A 525      11.402  51.929   1.295  1.00 30.79           H  
ATOM   7976  HD3 ARG A 525      12.120  51.990  -0.121  1.00 30.79           H  
ATOM   7977  HE  ARG A 525      10.128  51.646  -1.092  1.00 88.34           H  
ATOM   7978 HH11 ARG A 525       9.721  52.002   2.181  1.00 81.71           H  
ATOM   7979 HH12 ARG A 525       8.257  52.273   2.129  1.00 81.71           H  
ATOM   7980 HH21 ARG A 525       7.913  52.063  -1.142  1.00 83.60           H  
ATOM   7981 HH22 ARG A 525       7.166  52.309   0.124  1.00 83.60           H  
ATOM   7982  N   GLY A 526      10.314  46.996   2.551  1.00 18.73           N  
ANISOU 7982  N   GLY A 526     2543   2526   2046    -10   -235   -289       N  
ATOM   7983  CA  GLY A 526      10.454  46.718   3.968  1.00 21.09           C  
ANISOU 7983  CA  GLY A 526     2823   2885   2304    -22   -232   -301       C  
ATOM   7984  C   GLY A 526      11.040  45.357   4.281  1.00 20.60           C  
ANISOU 7984  C   GLY A 526     2707   2884   2235    -38   -220   -248       C  
ATOM   7985  O   GLY A 526      11.601  45.169   5.366  1.00 24.87           O  
ANISOU 7985  O   GLY A 526     3233   3476   2742    -64   -225   -245       O  
ATOM   7986  H   GLY A 526       9.505  46.965   2.259  1.00 22.47           H  
ATOM   7987  HA2 GLY A 526      11.031  47.389   4.363  1.00 25.30           H  
ATOM   7988  HA3 GLY A 526       9.579  46.769   4.385  1.00 25.30           H  
ATOM   7989  N   ALA A 527      10.932  44.408   3.352  1.00 20.09           N  
ANISOU 7989  N   ALA A 527     2616   2815   2203    -22   -206   -207       N  
ATOM   7990  CA  ALA A 527      11.359  43.037   3.583  1.00 23.61           C  
ANISOU 7990  CA  ALA A 527     3014   3310   2646    -28   -194   -157       C  
ATOM   7991  C   ALA A 527      12.766  42.744   3.084  1.00 25.08           C  
ANISOU 7991  C   ALA A 527     3185   3500   2845    -62   -206   -115       C  
ATOM   7992  O   ALA A 527      13.369  41.757   3.520  1.00 25.86           O  
ANISOU 7992  O   ALA A 527     3246   3644   2934    -71   -203    -76       O  
ATOM   7993  CB  ALA A 527      10.386  42.065   2.902  1.00 22.08           C  
ANISOU 7993  CB  ALA A 527     2800   3110   2479     10   -171   -138       C  
ATOM   7994  H   ALA A 527      10.608  44.540   2.566  1.00 24.11           H  
ATOM   7995  HA  ALA A 527      11.345  42.868   4.538  1.00 28.33           H  
ATOM   7996  HB1 ALA A 527      10.759  41.170   2.935  1.00 26.49           H  
ATOM   7997  HB2 ALA A 527       9.537  42.087   3.371  1.00 26.49           H  
ATOM   7998  HB3 ALA A 527      10.262  42.338   1.979  1.00 26.49           H  
ATOM   7999  N   VAL A 528      13.305  43.564   2.188  1.00 17.20           N  
ANISOU 7999  N   VAL A 528     2213   2458   1865    -79   -220   -120       N  
ATOM   8000  CA  VAL A 528      14.590  43.252   1.575  1.00 19.49           C  
ANISOU 8000  CA  VAL A 528     2482   2756   2167   -109   -227    -80       C  
ATOM   8001  C   VAL A 528      15.685  43.372   2.628  1.00 16.36           C  
ANISOU 8001  C   VAL A 528     2070   2408   1736   -150   -245    -72       C  
ATOM   8002  O   VAL A 528      15.840  44.418   3.267  1.00 18.59           O  
ANISOU 8002  O   VAL A 528     2383   2686   1993   -176   -262   -107       O  
ATOM   8003  CB  VAL A 528      14.853  44.168   0.375  1.00 17.62           C  
ANISOU 8003  CB  VAL A 528     2279   2464   1953   -123   -238    -87       C  
ATOM   8004  CG1 VAL A 528      16.308  44.091  -0.079  1.00 20.33           C  
ANISOU 8004  CG1 VAL A 528     2602   2825   2299   -164   -249    -52       C  
ATOM   8005  CG2 VAL A 528      13.962  43.768  -0.797  1.00 18.79           C  
ANISOU 8005  CG2 VAL A 528     2430   2574   2135    -84   -221    -81       C  
ATOM   8006  H   VAL A 528      12.951  44.301   1.921  1.00 20.64           H  
ATOM   8007  HA  VAL A 528      14.582  42.335   1.259  1.00 23.39           H  
ATOM   8008  HB  VAL A 528      14.658  45.077   0.650  1.00 21.15           H  
ATOM   8009 HG11 VAL A 528      16.406  44.579  -0.911  1.00 24.40           H  
ATOM   8010 HG12 VAL A 528      16.873  44.485   0.604  1.00 24.40           H  
ATOM   8011 HG13 VAL A 528      16.549  43.160  -0.211  1.00 24.40           H  
ATOM   8012 HG21 VAL A 528      14.127  44.371  -1.539  1.00 22.54           H  
ATOM   8013 HG22 VAL A 528      14.172  42.858  -1.058  1.00 22.54           H  
ATOM   8014 HG23 VAL A 528      13.034  43.828  -0.523  1.00 22.54           H  
ATOM   8015  N   SER A 529      16.452  42.301   2.809  1.00 17.86           N  
ANISOU 8015  N   SER A 529     2215   2646   1926   -154   -241    -27       N  
ATOM   8016  CA  SER A 529      17.475  42.275   3.841  1.00 16.82           C  
ANISOU 8016  CA  SER A 529     2061   2570   1760   -190   -258    -14       C  
ATOM   8017  C   SER A 529      18.655  43.175   3.474  1.00 13.93           C  
ANISOU 8017  C   SER A 529     1704   2199   1390   -239   -280    -13       C  
ATOM   8018  O   SER A 529      18.882  43.508   2.310  1.00 15.76           O  
ANISOU 8018  O   SER A 529     1947   2392   1648   -244   -280     -8       O  
ATOM   8019  CB  SER A 529      17.980  40.848   4.059  1.00 17.79           C  
ANISOU 8019  CB  SER A 529     2132   2742   1887   -176   -249     39       C  
ATOM   8020  OG  SER A 529      18.746  40.413   2.951  1.00 17.10           O  
ANISOU 8020  OG  SER A 529     2022   2646   1829   -175   -246     72       O  
ATOM   8021  H   SER A 529      16.400  41.577   2.348  1.00 21.43           H  
ATOM   8022  HA  SER A 529      17.088  42.601   4.669  1.00 20.19           H  
ATOM   8023  HB2 SER A 529      18.534  40.827   4.855  1.00 21.35           H  
ATOM   8024  HB3 SER A 529      17.219  40.257   4.169  1.00 21.35           H  
ATOM   8025  HG  SER A 529      18.699  39.577   2.879  1.00 20.52           H  
ATOM   8026  N  AASP A 530      19.408  43.582   4.494  0.63 16.85           N  
ANISOU 8026  N  AASP A 530     2069   2611   1723   -279   -301    -18       N  
ATOM   8027  N  BASP A 530      19.415  43.573   4.504  0.37 16.48           N  
ANISOU 8027  N  BASP A 530     2021   2565   1676   -279   -301    -18       N  
ATOM   8028  CA AASP A 530      20.620  44.337   4.216  0.63 16.23           C  
ANISOU 8028  CA AASP A 530     1992   2538   1637   -332   -323    -13       C  
ATOM   8029  CA BASP A 530      20.660  44.316   4.297  0.37 31.27           C  
ANISOU 8029  CA BASP A 530     3894   4447   3539   -334   -324    -12       C  
ATOM   8030  C  AASP A 530      21.520  43.573   3.251  0.63 14.80           C  
ANISOU 8030  C  AASP A 530     1766   2375   1481   -331   -316     37       C  
ATOM   8031  C  BASP A 530      21.579  43.585   3.327  0.37 22.02           C  
ANISOU 8031  C  BASP A 530     2680   3294   2394   -334   -318     37       C  
ATOM   8032  O  AASP A 530      22.086  44.161   2.323  0.63 16.57           O  
ANISOU 8032  O  AASP A 530     2000   2576   1719   -358   -323     40       O  
ATOM   8033  O  BASP A 530      22.207  44.209   2.464  0.37 15.04           O  
ANISOU 8033  O  BASP A 530     1805   2390   1521   -364   -326     40       O  
ATOM   8034  CB AASP A 530      21.366  44.650   5.508  0.63 26.19           C  
ANISOU 8034  CB AASP A 530     3242   3856   2852   -376   -346    -18       C  
ATOM   8035  CB BASP A 530      21.342  44.526   5.658  0.37 11.68           C  
ANISOU 8035  CB BASP A 530     1401   2026   1012   -373   -345    -16       C  
ATOM   8036  CG AASP A 530      20.595  45.586   6.416  0.63 28.65           C  
ANISOU 8036  CG AASP A 530     3603   4147   3134   -384   -355    -75       C  
ATOM   8037  CG BASP A 530      22.558  45.473   5.619  0.37 23.75           C  
ANISOU 8037  CG BASP A 530     2935   3566   2522   -440   -374    -18       C  
ATOM   8038  OD1AASP A 530      19.632  46.233   5.946  0.63 24.95           O  
ANISOU 8038  OD1AASP A 530     3182   3616   2684   -362   -347   -113       O  
ATOM   8039  OD1BASP A 530      22.961  46.009   4.570  0.37 19.03           O  
ANISOU 8039  OD1BASP A 530     2351   2933   1946   -461   -378    -14       O  
ATOM   8040  OD2AASP A 530      20.965  45.676   7.605  0.63 22.13           O  
ANISOU 8040  OD2AASP A 530     2769   3373   2268   -411   -369    -82       O  
ATOM   8041  OD2BASP A 530      23.129  45.686   6.701  0.37 18.35           O  
ANISOU 8041  OD2BASP A 530     2241   2932   1798   -476   -393    -23       O  
ATOM   8042  H  AASP A 530      19.245  43.439   5.326  0.63 20.22           H  
ATOM   8043  H  BASP A 530      19.233  43.425   5.331  0.37 19.78           H  
ATOM   8044  HA AASP A 530      20.377  45.184   3.810  0.63 19.48           H  
ATOM   8045  HA BASP A 530      20.470  45.187   3.913  0.37 37.52           H  
ATOM   8046  HB2AASP A 530      21.521  43.824   5.992  0.63 31.43           H  
ATOM   8047  HB2BASP A 530      20.695  44.904   6.274  0.37 14.02           H  
ATOM   8048  HB3AASP A 530      22.212  45.072   5.291  0.63 31.43           H  
ATOM   8049  HB3BASP A 530      21.649  43.666   5.987  0.37 14.02           H  
ATOM   8050  N   ALA A 531      21.654  42.256   3.444  1.00 17.04           N  
ANISOU 8050  N   ALA A 531     2003   2701   1772   -299   -303     76       N  
ATOM   8051  CA  ALA A 531      22.511  41.465   2.561  1.00 14.03           C  
ANISOU 8051  CA  ALA A 531     1578   2339   1415   -290   -295    120       C  
ATOM   8052  C   ALA A 531      22.013  41.491   1.116  1.00 16.03           C  
ANISOU 8052  C   ALA A 531     1849   2534   1706   -267   -277    116       C  
ATOM   8053  O   ALA A 531      22.803  41.675   0.186  1.00 16.72           O  
ANISOU 8053  O   ALA A 531     1925   2622   1806   -286   -278    131       O  
ATOM   8054  CB  ALA A 531      22.606  40.021   3.066  1.00 20.25           C  
ANISOU 8054  CB  ALA A 531     2319   3171   2206   -252   -285    159       C  
ATOM   8055  H  AALA A 531      21.268  41.805   4.066  0.63 20.45           H  
ATOM   8056  H  BALA A 531      21.222  41.789   4.023  0.37 20.45           H  
ATOM   8057  HA  ALA A 531      23.399  41.854   2.578  1.00 16.84           H  
ATOM   8058  HB1 ALA A 531      23.130  39.501   2.438  1.00 24.31           H  
ATOM   8059  HB2 ALA A 531      23.034  40.019   3.936  1.00 24.31           H  
ATOM   8060  HB3 ALA A 531      21.712  39.652   3.137  1.00 24.31           H  
ATOM   8061  N   ASP A 532      20.708  41.294   0.897  1.00 14.04           N  
ANISOU 8061  N   ASP A 532     1625   2237   1471   -227   -260     96       N  
ATOM   8062  CA  ASP A 532      20.203  41.330  -0.474  1.00 17.42           C  
ANISOU 8062  CA  ASP A 532     2072   2613   1934   -206   -245     93       C  
ATOM   8063  C   ASP A 532      20.415  42.707  -1.105  1.00 14.72           C  
ANISOU 8063  C   ASP A 532     1769   2232   1590   -246   -260     69       C  
ATOM   8064  O   ASP A 532      20.787  42.810  -2.280  1.00 15.32           O  
ANISOU 8064  O   ASP A 532     1844   2291   1686   -253   -255     82       O  
ATOM   8065  CB  ASP A 532      18.721  40.949  -0.523  1.00 15.41           C  
ANISOU 8065  CB  ASP A 532     1840   2322   1694   -160   -227     74       C  
ATOM   8066  CG  ASP A 532      18.490  39.430  -0.520  1.00 15.33           C  
ANISOU 8066  CG  ASP A 532     1793   2332   1699   -119   -207    106       C  
ATOM   8067  OD1 ASP A 532      19.473  38.653  -0.582  1.00 17.65           O  
ANISOU 8067  OD1 ASP A 532     2047   2663   1997   -119   -206    142       O  
ATOM   8068  OD2 ASP A 532      17.314  39.014  -0.447  1.00 19.42           O  
ANISOU 8068  OD2 ASP A 532     2323   2830   2226    -87   -193     95       O  
ATOM   8069  H   ASP A 532      20.116  41.142   1.502  1.00 16.84           H  
ATOM   8070  HA  ASP A 532      20.692  40.672  -0.992  1.00 20.91           H  
ATOM   8071  HB2 ASP A 532      18.274  41.320   0.253  1.00 18.50           H  
ATOM   8072  HB3 ASP A 532      18.330  41.309  -1.335  1.00 18.50           H  
ATOM   8073  N   ALA A 533      20.165  43.778  -0.346  1.00 16.75           N  
ANISOU 8073  N   ALA A 533     2066   2475   1825   -272   -278     34       N  
ATOM   8074  CA  ALA A 533      20.373  45.130  -0.861  1.00 16.17           C  
ANISOU 8074  CA  ALA A 533     2036   2357   1749   -312   -296     11       C  
ATOM   8075  C   ALA A 533      21.846  45.397  -1.151  1.00 18.11           C  
ANISOU 8075  C   ALA A 533     2257   2639   1984   -367   -311     38       C  
ATOM   8076  O   ALA A 533      22.193  45.989  -2.184  1.00 18.45           O  
ANISOU 8076  O   ALA A 533     2317   2654   2039   -394   -316     44       O  
ATOM   8077  CB  ALA A 533      19.835  46.143   0.151  1.00 19.05           C  
ANISOU 8077  CB  ALA A 533     2448   2701   2090   -326   -314    -35       C  
ATOM   8078  H   ALA A 533      19.876  43.750   0.464  1.00 20.11           H  
ATOM   8079  HA  ALA A 533      19.886  45.232  -1.694  1.00 19.40           H  
ATOM   8080  HB1 ALA A 533      20.079  47.036  -0.136  1.00 22.86           H  
ATOM   8081  HB2 ALA A 533      18.870  46.061   0.197  1.00 22.86           H  
ATOM   8082  HB3 ALA A 533      20.225  45.957   1.020  1.00 22.86           H  
ATOM   8083  N   ASP A 534      22.726  44.976  -0.243  1.00 13.80           N  
ANISOU 8083  N   ASP A 534     1670   2160   1414   -388   -320     57       N  
ATOM   8084  CA  ASP A 534      24.159  45.105  -0.475  1.00 16.70           C  
ANISOU 8084  CA  ASP A 534     2002   2574   1770   -437   -333     86       C  
ATOM   8085  C   ASP A 534      24.567  44.399  -1.765  1.00 15.62           C  
ANISOU 8085  C   ASP A 534     1830   2444   1660   -418   -313    120       C  
ATOM   8086  O   ASP A 534      25.340  44.936  -2.566  1.00 16.03           O  
ANISOU 8086  O   ASP A 534     1879   2500   1713   -460   -320    132       O  
ATOM   8087  CB  ASP A 534      24.943  44.509   0.696  1.00 15.42           C  
ANISOU 8087  CB  ASP A 534     1790   2488   1579   -448   -343    106       C  
ATOM   8088  CG  ASP A 534      25.083  45.445   1.891  1.00 17.76           C  
ANISOU 8088  CG  ASP A 534     2115   2795   1837   -494   -370     76       C  
ATOM   8089  OD1 ASP A 534      24.523  46.560   1.915  1.00 20.97           O  
ANISOU 8089  OD1 ASP A 534     2583   3146   2239   -515   -381     35       O  
ATOM   8090  OD2 ASP A 534      25.780  45.023   2.833  1.00 19.18           O  
ANISOU 8090  OD2 ASP A 534     2254   3042   1991   -509   -381     93       O  
ATOM   8091  H   ASP A 534      22.521  44.614   0.510  1.00 16.56           H  
ATOM   8092  HA  ASP A 534      24.371  46.049  -0.544  1.00 20.04           H  
ATOM   8093  HB2 ASP A 534      24.487  43.709   1.001  1.00 18.50           H  
ATOM   8094  HB3 ASP A 534      25.836  44.286   0.391  1.00 18.50           H  
ATOM   8095  N   ASP A 535      24.098  43.163  -1.957  1.00 15.85           N  
ANISOU 8095  N   ASP A 535     1831   2481   1712   -359   -289    136       N  
ATOM   8096  CA  ASP A 535      24.522  42.392  -3.123  1.00 18.42           C  
ANISOU 8096  CA  ASP A 535     2121   2817   2061   -337   -269    166       C  
ATOM   8097  C   ASP A 535      23.968  42.998  -4.405  1.00 16.78           C  
ANISOU 8097  C   ASP A 535     1953   2548   1873   -339   -261    152       C  
ATOM   8098  O   ASP A 535      24.670  43.066  -5.422  1.00 17.18           O  
ANISOU 8098  O   ASP A 535     1987   2611   1930   -358   -256    171       O  
ATOM   8099  CB  ASP A 535      24.088  40.934  -2.966  1.00 15.40           C  
ANISOU 8099  CB  ASP A 535     1707   2448   1697   -273   -247    184       C  
ATOM   8100  CG  ASP A 535      24.831  40.222  -1.848  1.00 21.24           C  
ANISOU 8100  CG  ASP A 535     2399   3253   2417   -270   -256    208       C  
ATOM   8101  OD1 ASP A 535      25.928  40.694  -1.491  1.00 20.40           O  
ANISOU 8101  OD1 ASP A 535     2269   3195   2288   -315   -274    219       O  
ATOM   8102  OD2 ASP A 535      24.334  39.192  -1.340  1.00 23.53           O  
ANISOU 8102  OD2 ASP A 535     2676   3549   2715   -225   -245    219       O  
ATOM   8103  H   ASP A 535      23.546  42.755  -1.438  1.00 19.02           H  
ATOM   8104  HA  ASP A 535      25.489  42.406  -3.185  1.00 22.11           H  
ATOM   8105  HB2 ASP A 535      23.140  40.906  -2.762  1.00 18.48           H  
ATOM   8106  HB3 ASP A 535      24.264  40.460  -3.793  1.00 18.48           H  
ATOM   8107  N   LEU A 536      22.713  43.457  -4.373  1.00 16.06           N  
ANISOU 8107  N   LEU A 536     1916   2397   1791   -320   -261    121       N  
ATOM   8108  CA  LEU A 536      22.145  44.179  -5.506  1.00 16.47           C  
ANISOU 8108  CA  LEU A 536     2010   2388   1858   -324   -259    108       C  
ATOM   8109  C   LEU A 536      23.025  45.361  -5.890  1.00 19.24           C  
ANISOU 8109  C   LEU A 536     2381   2736   2195   -391   -281    110       C  
ATOM   8110  O   LEU A 536      23.406  45.527  -7.055  1.00 17.87           O  
ANISOU 8110  O   LEU A 536     2205   2556   2029   -409   -276    126       O  
ATOM   8111  CB  LEU A 536      20.736  44.677  -5.163  1.00 15.20           C  
ANISOU 8111  CB  LEU A 536     1903   2168   1703   -297   -262     71       C  
ATOM   8112  CG  LEU A 536      20.063  45.576  -6.211  1.00 17.23           C  
ANISOU 8112  CG  LEU A 536     2212   2358   1976   -300   -266     55       C  
ATOM   8113  CD1 LEU A 536      19.611  44.736  -7.396  1.00 19.43           C  
ANISOU 8113  CD1 LEU A 536     2474   2626   2280   -261   -242     72       C  
ATOM   8114  CD2 LEU A 536      18.895  46.330  -5.582  1.00 20.59           C  
ANISOU 8114  CD2 LEU A 536     2690   2734   2400   -281   -277     14       C  
ATOM   8115  H   LEU A 536      22.174  43.364  -3.709  1.00 19.28           H  
ATOM   8116  HA  LEU A 536      22.083  43.572  -6.260  1.00 19.76           H  
ATOM   8117  HB2 LEU A 536      20.165  43.903  -5.039  1.00 18.24           H  
ATOM   8118  HB3 LEU A 536      20.789  45.187  -4.339  1.00 18.24           H  
ATOM   8119  HG  LEU A 536      20.693  46.236  -6.539  1.00 20.67           H  
ATOM   8120 HD11 LEU A 536      19.063  45.283  -7.980  1.00 23.31           H  
ATOM   8121 HD12 LEU A 536      20.393  44.421  -7.876  1.00 23.31           H  
ATOM   8122 HD13 LEU A 536      19.096  43.981  -7.071  1.00 23.31           H  
ATOM   8123 HD21 LEU A 536      18.646  47.066  -6.162  1.00 24.71           H  
ATOM   8124 HD22 LEU A 536      18.146  45.722  -5.479  1.00 24.71           H  
ATOM   8125 HD23 LEU A 536      19.168  46.669  -4.716  1.00 24.71           H  
ATOM   8126  N   ASP A 537      23.350  46.198  -4.901  1.00 17.31           N  
ANISOU 8126  N   ASP A 537     2156   2496   1924   -433   -306     93       N  
ATOM   8127  CA  ASP A 537      24.087  47.425  -5.164  1.00 18.63           C  
ANISOU 8127  CA  ASP A 537     2351   2651   2076   -504   -331     91       C  
ATOM   8128  C   ASP A 537      25.490  47.131  -5.673  1.00 18.64           C  
ANISOU 8128  C   ASP A 537     2297   2718   2068   -544   -329    130       C  
ATOM   8129  O   ASP A 537      25.982  47.814  -6.580  1.00 18.58           O  
ANISOU 8129  O   ASP A 537     2303   2699   2058   -590   -336    141       O  
ATOM   8130  CB  ASP A 537      24.139  48.275  -3.894  1.00 19.77           C  
ANISOU 8130  CB  ASP A 537     2527   2791   2193   -539   -358     62       C  
ATOM   8131  CG  ASP A 537      22.796  48.897  -3.548  1.00 32.30           C  
ANISOU 8131  CG  ASP A 537     4178   4305   3787   -508   -363     18       C  
ATOM   8132  OD1 ASP A 537      21.854  48.825  -4.369  1.00 34.05           O  
ANISOU 8132  OD1 ASP A 537     4424   4477   4035   -466   -349     12       O  
ATOM   8133  OD2 ASP A 537      22.687  49.461  -2.440  1.00 41.61           O  
ANISOU 8133  OD2 ASP A 537     5383   5481   4945   -524   -380    -12       O  
ATOM   8134  H   ASP A 537      23.156  46.077  -4.072  1.00 20.77           H  
ATOM   8135  HA  ASP A 537      23.625  47.932  -5.850  1.00 22.35           H  
ATOM   8136  HB2 ASP A 537      24.410  47.715  -3.150  1.00 23.72           H  
ATOM   8137  HB3 ASP A 537      24.779  48.993  -4.019  1.00 23.72           H  
ATOM   8138  N   ARG A 538      26.146  46.111  -5.117  1.00 16.74           N  
ANISOU 8138  N   ARG A 538     1992   2548   1820   -526   -320    152       N  
ATOM   8139  CA  ARG A 538      27.521  45.832  -5.514  1.00 16.34           C  
ANISOU 8139  CA  ARG A 538     1882   2569   1758   -561   -318    187       C  
ATOM   8140  C   ARG A 538      27.569  45.324  -6.946  1.00 19.28           C  
ANISOU 8140  C   ARG A 538     2235   2939   2152   -538   -293    206       C  
ATOM   8141  O   ARG A 538      28.394  45.773  -7.752  1.00 17.20           O  
ANISOU 8141  O   ARG A 538     1957   2698   1879   -585   -296    224       O  
ATOM   8142  CB  ARG A 538      28.154  44.809  -4.573  1.00 19.60           C  
ANISOU 8142  CB  ARG A 538     2231   3058   2161   -538   -315    206       C  
ATOM   8143  CG  ARG A 538      29.624  44.538  -4.883  1.00 20.84           C  
ANISOU 8143  CG  ARG A 538     2319   3296   2303   -570   -316    241       C  
ATOM   8144  CD  ARG A 538      30.147  43.349  -4.087  1.00 21.29           C  
ANISOU 8144  CD  ARG A 538     2310   3422   2356   -530   -310    264       C  
ATOM   8145  NE  ARG A 538      29.842  43.523  -2.674  1.00 24.13           N  
ANISOU 8145  NE  ARG A 538     2687   3784   2697   -536   -330    249       N  
ATOM   8146  CZ  ARG A 538      28.927  42.835  -1.994  1.00 19.32           C  
ANISOU 8146  CZ  ARG A 538     2090   3154   2098   -481   -322    239       C  
ATOM   8147  NH1 ARG A 538      28.743  43.120  -0.716  1.00 21.02           N  
ANISOU 8147  NH1 ARG A 538     2320   3378   2288   -496   -341    224       N  
ATOM   8148  NH2 ARG A 538      28.217  41.870  -2.570  1.00 19.90           N  
ANISOU 8148  NH2 ARG A 538     2160   3198   2202   -415   -294    244       N  
ATOM   8149  H   ARG A 538      25.826  45.579  -4.523  1.00 20.09           H  
ATOM   8150  HA  ARG A 538      28.034  46.652  -5.451  1.00 19.61           H  
ATOM   8151  HB2 ARG A 538      28.096  45.140  -3.664  1.00 23.53           H  
ATOM   8152  HB3 ARG A 538      27.673  43.970  -4.652  1.00 23.53           H  
ATOM   8153  HG2 ARG A 538      29.723  44.342  -5.827  1.00 25.01           H  
ATOM   8154  HG3 ARG A 538      30.151  45.318  -4.649  1.00 25.01           H  
ATOM   8155  HD2 ARG A 538      29.722  42.535  -4.400  1.00 25.54           H  
ATOM   8156  HD3 ARG A 538      31.108  43.283  -4.193  1.00 25.54           H  
ATOM   8157  HE  ARG A 538      30.290  44.118  -2.244  1.00 28.96           H  
ATOM   8158 HH11 ARG A 538      29.210  43.737  -0.341  1.00 25.22           H  
ATOM   8159 HH12 ARG A 538      28.156  42.687  -0.259  1.00 25.22           H  
ATOM   8160 HH21 ARG A 538      28.345  41.678  -3.399  1.00 23.88           H  
ATOM   8161 HH22 ARG A 538      27.630  41.437  -2.114  1.00 23.88           H  
ATOM   8162  N   LEU A 539      26.691  44.370  -7.272  1.00 17.91           N  
ANISOU 8162  N   LEU A 539     2059   2742   2005   -467   -268    203       N  
ATOM   8163  CA  LEU A 539      26.671  43.821  -8.618  1.00 18.79           C  
ANISOU 8163  CA  LEU A 539     2154   2850   2136   -442   -243    218       C  
ATOM   8164  C   LEU A 539      26.287  44.897  -9.617  1.00 15.64           C  
ANISOU 8164  C   LEU A 539     1809   2395   1739   -478   -250    209       C  
ATOM   8165  O   LEU A 539      26.856  44.967 -10.711  1.00 15.75           O  
ANISOU 8165  O   LEU A 539     1806   2427   1750   -500   -241    227       O  
ATOM   8166  CB  LEU A 539      25.708  42.640  -8.710  1.00 16.66           C  
ANISOU 8166  CB  LEU A 539     1880   2559   1893   -365   -218    213       C  
ATOM   8167  CG  LEU A 539      25.706  41.900 -10.052  1.00 22.31           C  
ANISOU 8167  CG  LEU A 539     2574   3275   2626   -333   -191    226       C  
ATOM   8168  CD1 LEU A 539      27.064  41.279 -10.349  1.00 24.93           C  
ANISOU 8168  CD1 LEU A 539     2838   3685   2950   -339   -180    254       C  
ATOM   8169  CD2 LEU A 539      24.631  40.823 -10.046  1.00 19.47           C  
ANISOU 8169  CD2 LEU A 539     2220   2885   2292   -263   -171    217       C  
ATOM   8170  H   LEU A 539      26.108  44.030  -6.738  1.00 21.49           H  
ATOM   8171  HA  LEU A 539      27.555  43.488  -8.836  1.00 22.55           H  
ATOM   8172  HB2 LEU A 539      25.947  41.998  -8.024  1.00 19.99           H  
ATOM   8173  HB3 LEU A 539      24.808  42.968  -8.558  1.00 19.99           H  
ATOM   8174  HG  LEU A 539      25.516  42.538 -10.757  1.00 26.77           H  
ATOM   8175 HD11 LEU A 539      27.017  40.324 -10.188  1.00 29.92           H  
ATOM   8176 HD12 LEU A 539      27.292  41.448 -11.277  1.00 29.92           H  
ATOM   8177 HD13 LEU A 539      27.729  41.681  -9.767  1.00 29.92           H  
ATOM   8178 HD21 LEU A 539      24.515  40.488 -10.949  1.00 23.36           H  
ATOM   8179 HD22 LEU A 539      24.908  40.103  -9.459  1.00 23.36           H  
ATOM   8180 HD23 LEU A 539      23.800  41.209  -9.727  1.00 23.36           H  
ATOM   8181  N   CYS A 540      25.342  45.767  -9.255  1.00 14.57           N  
ANISOU 8181  N   CYS A 540     1739   2193   1606   -483   -268    181       N  
ATOM   8182  CA  CYS A 540      24.967  46.836 -10.173  1.00 16.97           C  
ANISOU 8182  CA  CYS A 540     2098   2437   1912   -515   -279    174       C  
ATOM   8183  C   CYS A 540      26.114  47.820 -10.367  1.00 16.97           C  
ANISOU 8183  C   CYS A 540     2100   2460   1887   -599   -301    190       C  
ATOM   8184  O   CYS A 540      26.343  48.304 -11.482  1.00 18.08           O  
ANISOU 8184  O   CYS A 540     2255   2589   2026   -632   -301    206       O  
ATOM   8185  CB  CYS A 540      23.707  47.541  -9.679  1.00 20.19           C  
ANISOU 8185  CB  CYS A 540     2574   2768   2329   -496   -294    139       C  
ATOM   8186  SG  CYS A 540      22.197  46.604 -10.054  1.00 18.14           S  
ANISOU 8186  SG  CYS A 540     2322   2470   2100   -408   -268    125       S  
ATOM   8187  H   CYS A 540      24.916  45.760  -8.507  1.00 17.49           H  
ATOM   8188  HA  CYS A 540      24.760  46.451 -11.039  1.00 20.36           H  
ATOM   8189  HB2 CYS A 540      23.763  47.652  -8.717  1.00 24.23           H  
ATOM   8190  HB3 CYS A 540      23.639  48.408 -10.109  1.00 24.23           H  
ATOM   8191  N   ALA A 541      26.858  48.127  -9.307  1.00 16.52           N  
ANISOU 8191  N   ALA A 541     2028   2440   1807   -639   -320    189       N  
ATOM   8192  CA  ALA A 541      28.036  48.964  -9.492  1.00 17.39           C  
ANISOU 8192  CA  ALA A 541     2131   2584   1891   -724   -340    207       C  
ATOM   8193  C   ALA A 541      29.041  48.285 -10.418  1.00 19.68           C  
ANISOU 8193  C   ALA A 541     2353   2949   2178   -733   -318    243       C  
ATOM   8194  O   ALA A 541      29.636  48.937 -11.284  1.00 20.18           O  
ANISOU 8194  O   ALA A 541     2420   3019   2228   -791   -324    262       O  
ATOM   8195  CB  ALA A 541      28.672  49.291  -8.142  1.00 22.32           C  
ANISOU 8195  CB  ALA A 541     2745   3245   2491   -763   -364    199       C  
ATOM   8196  H   ALA A 541      26.709  47.874  -8.499  1.00 19.82           H  
ATOM   8197  HA  ALA A 541      27.769  49.803  -9.899  1.00 20.86           H  
ATOM   8198  HB1 ALA A 541      29.556  49.660  -8.291  1.00 26.78           H  
ATOM   8199  HB2 ALA A 541      28.116  49.939  -7.681  1.00 26.78           H  
ATOM   8200  HB3 ALA A 541      28.736  48.478  -7.618  1.00 26.78           H  
ATOM   8201  N   ASP A 542      29.244  46.972 -10.249  1.00 20.14           N  
ANISOU 8201  N   ASP A 542     2347   3062   2245   -675   -292    254       N  
ATOM   8202  CA  ASP A 542      30.194  46.252 -11.091  1.00 16.89           C  
ANISOU 8202  CA  ASP A 542     1865   2723   1828   -673   -269    283       C  
ATOM   8203  C   ASP A 542      29.736  46.237 -12.546  1.00 18.06           C  
ANISOU 8203  C   ASP A 542     2034   2838   1990   -660   -250    288       C  
ATOM   8204  O   ASP A 542      30.545  46.427 -13.463  1.00 19.22           O  
ANISOU 8204  O   ASP A 542     2153   3027   2122   -701   -243    310       O  
ATOM   8205  CB  ASP A 542      30.379  44.817 -10.580  1.00 19.18           C  
ANISOU 8205  CB  ASP A 542     2091   3065   2129   -603   -248    290       C  
ATOM   8206  CG  ASP A 542      31.051  44.748  -9.206  1.00 22.67           C  
ANISOU 8206  CG  ASP A 542     2501   3560   2554   -620   -267    294       C  
ATOM   8207  OD1 ASP A 542      31.757  45.702  -8.819  1.00 30.79           O  
ANISOU 8207  OD1 ASP A 542     3533   4610   3554   -694   -293    298       O  
ATOM   8208  OD2 ASP A 542      30.873  43.723  -8.510  1.00 24.74           O  
ANISOU 8208  OD2 ASP A 542     2733   3842   2827   -560   -258    295       O  
ATOM   8209  H   ASP A 542      28.848  46.483  -9.662  1.00 24.17           H  
ATOM   8210  HA  ASP A 542      31.052  46.702 -11.043  1.00 20.26           H  
ATOM   8211  HB2 ASP A 542      29.508  44.395 -10.508  1.00 23.01           H  
ATOM   8212  HB3 ASP A 542      30.933  44.328 -11.208  1.00 23.01           H  
ATOM   8213  N   TRP A 543      28.440  45.997 -12.774  1.00 15.40           N  
ANISOU 8213  N   TRP A 543     1741   2430   1679   -605   -241    267       N  
ATOM   8214  CA  TRP A 543      27.904  46.006 -14.127  1.00 14.81           C  
ANISOU 8214  CA  TRP A 543     1690   2322   1616   -593   -225    270       C  
ATOM   8215  C   TRP A 543      28.038  47.388 -14.751  1.00 16.62           C  
ANISOU 8215  C   TRP A 543     1970   2516   1830   -667   -248    278       C  
ATOM   8216  O   TRP A 543      28.436  47.522 -15.913  1.00 20.58           O  
ANISOU 8216  O   TRP A 543     2462   3037   2322   -695   -238    297       O  
ATOM   8217  CB  TRP A 543      26.436  45.568 -14.128  1.00 15.27           C  
ANISOU 8217  CB  TRP A 543     1788   2312   1703   -524   -216    246       C  
ATOM   8218  CG  TRP A 543      25.859  45.684 -15.487  1.00 14.03           C  
ANISOU 8218  CG  TRP A 543     1659   2118   1554   -516   -204    249       C  
ATOM   8219  CD1 TRP A 543      24.987  46.632 -15.936  1.00 18.67           C  
ANISOU 8219  CD1 TRP A 543     2315   2633   2147   -531   -221    240       C  
ATOM   8220  CD2 TRP A 543      26.163  44.853 -16.611  1.00 16.25           C  
ANISOU 8220  CD2 TRP A 543     1899   2438   1837   -495   -174    263       C  
ATOM   8221  NE1 TRP A 543      24.720  46.437 -17.272  1.00 17.15           N  
ANISOU 8221  NE1 TRP A 543     2125   2433   1958   -522   -205    250       N  
ATOM   8222  CE2 TRP A 543      25.432  45.351 -17.712  1.00 15.85           C  
ANISOU 8222  CE2 TRP A 543     1895   2336   1789   -501   -175    262       C  
ATOM   8223  CE3 TRP A 543      26.983  43.734 -16.793  1.00 18.49           C  
ANISOU 8223  CE3 TRP A 543     2112   2794   2118   -468   -148    275       C  
ATOM   8224  CZ2 TRP A 543      25.479  44.752 -18.978  1.00 19.18           C  
ANISOU 8224  CZ2 TRP A 543     2296   2781   2211   -485   -149    272       C  
ATOM   8225  CZ3 TRP A 543      27.051  43.153 -18.057  1.00 18.45           C  
ANISOU 8225  CZ3 TRP A 543     2087   2808   2114   -449   -121    282       C  
ATOM   8226  CH2 TRP A 543      26.300  43.663 -19.133  1.00 16.64           C  
ANISOU 8226  CH2 TRP A 543     1906   2531   1886   -460   -121    280       C  
ATOM   8227  H   TRP A 543      27.857  45.828 -12.165  1.00 18.48           H  
ATOM   8228  HA  TRP A 543      28.405  45.370 -14.662  1.00 17.78           H  
ATOM   8229  HB2 TRP A 543      26.374  44.642 -13.843  1.00 18.33           H  
ATOM   8230  HB3 TRP A 543      25.929  46.134 -13.526  1.00 18.33           H  
ATOM   8231  HD1 TRP A 543      24.625  47.312 -15.415  1.00 22.41           H  
ATOM   8232  HE1 TRP A 543      24.193  46.918 -17.752  1.00 20.58           H  
ATOM   8233  HE3 TRP A 543      27.473  43.385 -16.084  1.00 22.18           H  
ATOM   8234  HZ2 TRP A 543      24.973  45.079 -19.686  1.00 23.02           H  
ATOM   8235  HZ3 TRP A 543      27.601  42.416 -18.192  1.00 22.14           H  
ATOM   8236  HH2 TRP A 543      26.362  43.254 -19.966  1.00 19.97           H  
ATOM   8237  N   ARG A 544      27.721  48.434 -13.991  1.00 16.96           N  
ANISOU 8237  N   ARG A 544     2069   2507   1867   -702   -280    262       N  
ATOM   8238  CA  ARG A 544      27.754  49.768 -14.574  1.00 18.71           C  
ANISOU 8238  CA  ARG A 544     2350   2683   2078   -771   -305    269       C  
ATOM   8239  C   ARG A 544      29.171  50.201 -14.914  1.00 23.53           C  
ANISOU 8239  C   ARG A 544     2923   3361   2657   -854   -312    300       C  
ATOM   8240  O   ARG A 544      29.365  50.965 -15.866  1.00 25.83           O  
ANISOU 8240  O   ARG A 544     3243   3635   2937   -908   -321    318       O  
ATOM   8241  CB  ARG A 544      27.074  50.759 -13.637  1.00 24.93           C  
ANISOU 8241  CB  ARG A 544     3209   3396   2869   -783   -338    240       C  
ATOM   8242  CG  ARG A 544      25.566  50.555 -13.645  1.00 26.06           C  
ANISOU 8242  CG  ARG A 544     3396   3465   3040   -708   -332    213       C  
ATOM   8243  CD  ARG A 544      24.811  51.707 -13.062  1.00 48.96           C  
ANISOU 8243  CD  ARG A 544     6376   6282   5945   -720   -364    185       C  
ATOM   8244  NE  ARG A 544      25.042  51.781 -11.629  1.00 35.86           N  
ANISOU 8244  NE  ARG A 544     4711   4638   4274   -726   -377    163       N  
ATOM   8245  CZ  ARG A 544      24.169  51.410 -10.698  1.00 50.46           C  
ANISOU 8245  CZ  ARG A 544     6569   6468   6136   -667   -373    132       C  
ATOM   8246  NH1 ARG A 544      22.974  50.941 -11.014  1.00 35.80           N  
ANISOU 8246  NH1 ARG A 544     4726   4573   4303   -597   -357    118       N  
ATOM   8247  NH2 ARG A 544      24.497  51.530  -9.429  1.00 31.76           N  
ANISOU 8247  NH2 ARG A 544     4194   4122   3751   -682   -386    114       N  
ATOM   8248  H   ARG A 544      27.492  48.401 -13.163  1.00 20.35           H  
ATOM   8249  HA  ARG A 544      27.253  49.767 -15.405  1.00 22.45           H  
ATOM   8250  HB2 ARG A 544      27.400  50.624 -12.733  1.00 29.92           H  
ATOM   8251  HB3 ARG A 544      27.266  51.664 -13.927  1.00 29.92           H  
ATOM   8252  HG2 ARG A 544      25.269  50.438 -14.561  1.00 31.27           H  
ATOM   8253  HG3 ARG A 544      25.352  49.765 -13.123  1.00 31.27           H  
ATOM   8254  HD2 ARG A 544      25.113  52.534 -13.469  1.00 58.75           H  
ATOM   8255  HD3 ARG A 544      23.862  51.587 -13.218  1.00 58.75           H  
ATOM   8256  HE  ARG A 544      25.800  52.088 -11.364  1.00 43.03           H  
ATOM   8257 HH11 ARG A 544      22.744  50.869 -11.840  1.00 42.96           H  
ATOM   8258 HH12 ARG A 544      22.426  50.708 -10.394  1.00 42.96           H  
ATOM   8259 HH21 ARG A 544      25.268  51.844  -9.212  1.00 38.11           H  
ATOM   8260 HH22 ARG A 544      23.941  51.294  -8.817  1.00 38.11           H  
ATOM   8261  N   ARG A 545      30.166  49.708 -14.170  1.00 22.01           N  
ANISOU 8261  N   ARG A 545     2665   3248   2449   -866   -308    308       N  
ATOM   8262  CA  ARG A 545      31.565  49.964 -14.502  1.00 23.10           C  
ANISOU 8262  CA  ARG A 545     2753   3468   2556   -940   -311    338       C  
ATOM   8263  C   ARG A 545      31.971  49.191 -15.746  1.00 28.61           C  
ANISOU 8263  C   ARG A 545     3395   4223   3252   -920   -276    361       C  
ATOM   8264  O   ARG A 545      32.746  49.688 -16.572  1.00 24.72           O  
ANISOU 8264  O   ARG A 545     2889   3770   2736   -986   -276    386       O  
ATOM   8265  CB  ARG A 545      32.451  49.583 -13.310  1.00 23.70           C  
ANISOU 8265  CB  ARG A 545     2771   3618   2618   -949   -318    340       C  
ATOM   8266  CG  ARG A 545      33.939  49.885 -13.475  1.00 43.40           C  
ANISOU 8266  CG  ARG A 545     5207   6206   5077  -1030   -324    370       C  
ATOM   8267  CD  ARG A 545      34.742  49.480 -12.225  1.00 46.77           C  
ANISOU 8267  CD  ARG A 545     5575   6707   5490  -1033   -333    372       C  
ATOM   8268  NE  ARG A 545      33.953  49.637 -11.004  1.00 36.80           N  
ANISOU 8268  NE  ARG A 545     4361   5384   4239  -1006   -353    341       N  
ATOM   8269  CZ  ARG A 545      33.507  48.633 -10.247  1.00 57.05           C  
ANISOU 8269  CZ  ARG A 545     6901   7954   6820   -926   -340    327       C  
ATOM   8270  NH1 ARG A 545      33.782  47.371 -10.548  1.00 51.34           N  
ANISOU 8270  NH1 ARG A 545     6108   7290   6108   -862   -308    342       N  
ATOM   8271  NH2 ARG A 545      32.786  48.898  -9.170  1.00 45.99           N  
ANISOU 8271  NH2 ARG A 545     5548   6502   5425   -911   -358    299       N  
ATOM   8272  H   ARG A 545      30.058  49.222 -13.469  1.00 26.41           H  
ATOM   8273  HA  ARG A 545      31.690  50.909 -14.680  1.00 27.72           H  
ATOM   8274  HB2 ARG A 545      32.142  50.073 -12.531  1.00 28.44           H  
ATOM   8275  HB3 ARG A 545      32.365  48.629 -13.158  1.00 28.44           H  
ATOM   8276  HG2 ARG A 545      34.284  49.389 -14.233  1.00 52.08           H  
ATOM   8277  HG3 ARG A 545      34.059  50.837 -13.619  1.00 52.08           H  
ATOM   8278  HD2 ARG A 545      35.005  48.549 -12.300  1.00 56.13           H  
ATOM   8279  HD3 ARG A 545      35.529  50.042 -12.153  1.00 56.13           H  
ATOM   8280  HE  ARG A 545      33.761  50.438 -10.755  1.00 44.16           H  
ATOM   8281 HH11 ARG A 545      34.256  47.188 -11.242  1.00 61.60           H  
ATOM   8282 HH12 ARG A 545      33.487  46.736 -10.049  1.00 61.60           H  
ATOM   8283 HH21 ARG A 545      32.608  49.714  -8.962  1.00 55.19           H  
ATOM   8284 HH22 ARG A 545      32.495  48.256  -8.678  1.00 55.19           H  
ATOM   8285  N   TYR A 546      31.425  47.986 -15.916  1.00 21.43           N  
ANISOU 8285  N   TYR A 546     2458   3317   2366   -831   -245    350       N  
ATOM   8286  CA  TYR A 546      31.775  47.180 -17.075  1.00 26.48           C  
ANISOU 8286  CA  TYR A 546     3047   4010   3004   -805   -210    365       C  
ATOM   8287  C   TYR A 546      31.119  47.703 -18.354  1.00 29.35           C  
ANISOU 8287  C   TYR A 546     3462   4320   3369   -820   -207    369       C  
ATOM   8288  O   TYR A 546      31.747  47.724 -19.421  1.00 22.69           O  
ANISOU 8288  O   TYR A 546     2590   3526   2506   -853   -192    391       O  
ATOM   8289  CB  TYR A 546      31.374  45.711 -16.851  1.00 23.14           C  
ANISOU 8289  CB  TYR A 546     2584   3601   2607   -706   -181    350       C  
ATOM   8290  CG  TYR A 546      31.520  45.004 -18.159  1.00 21.81           C  
ANISOU 8290  CG  TYR A 546     2382   3467   2439   -678   -146    359       C  
ATOM   8291  CD1 TYR A 546      32.779  44.682 -18.636  1.00 19.77           C  
ANISOU 8291  CD1 TYR A 546     2049   3306   2156   -701   -128    379       C  
ATOM   8292  CD2 TYR A 546      30.424  44.751 -18.975  1.00 21.68           C  
ANISOU 8292  CD2 TYR A 546     2408   3390   2442   -636   -133    345       C  
ATOM   8293  CE1 TYR A 546      32.950  44.100 -19.877  1.00 19.86           C  
ANISOU 8293  CE1 TYR A 546     2030   3353   2162   -679    -96    384       C  
ATOM   8294  CE2 TYR A 546      30.583  44.165 -20.226  1.00 23.53           C  
ANISOU 8294  CE2 TYR A 546     2613   3657   2670   -617   -102    351       C  
ATOM   8295  CZ  TYR A 546      31.851  43.832 -20.668  1.00 23.74           C  
ANISOU 8295  CZ  TYR A 546     2568   3781   2673   -637    -82    369       C  
ATOM   8296  OH  TYR A 546      32.019  43.252 -21.910  1.00 25.97           O  
ANISOU 8296  OH  TYR A 546     2821   4099   2946   -618    -50    370       O  
ATOM   8297  H   TYR A 546      30.858  47.620 -15.384  1.00 25.71           H  
ATOM   8298  HA  TYR A 546      32.738  47.225 -17.184  1.00 31.78           H  
ATOM   8299  HB2 TYR A 546      31.958  45.299 -16.195  1.00 27.77           H  
ATOM   8300  HB3 TYR A 546      30.451  45.655 -16.556  1.00 27.77           H  
ATOM   8301  HD1 TYR A 546      33.524  44.862 -18.110  1.00 23.72           H  
ATOM   8302  HD2 TYR A 546      29.571  44.977 -18.680  1.00 26.02           H  
ATOM   8303  HE1 TYR A 546      33.804  43.889 -20.179  1.00 23.83           H  
ATOM   8304  HE2 TYR A 546      29.842  43.997 -20.762  1.00 28.23           H  
ATOM   8305  HH  TYR A 546      31.393  43.480 -22.421  1.00 31.16           H  
ATOM   8306  N   TRP A 547      29.850  48.102 -18.273  1.00 21.35           N  
ANISOU 8306  N   TRP A 547     2524   3210   2378   -794   -221    349       N  
ATOM   8307  CA  TRP A 547      29.056  48.267 -19.484  1.00 20.59           C  
ANISOU 8307  CA  TRP A 547     2469   3065   2288   -783   -214    351       C  
ATOM   8308  C   TRP A 547      29.678  49.214 -20.500  1.00 26.42           C  
ANISOU 8308  C   TRP A 547     3222   3818   2998   -867   -224    381       C  
ATOM   8309  O   TRP A 547      29.667  48.877 -21.696  1.00 22.83           O  
ANISOU 8309  O   TRP A 547     2753   3386   2536   -860   -201    393       O  
ATOM   8310  CB  TRP A 547      27.640  48.726 -19.111  1.00 26.12           C  
ANISOU 8310  CB  TRP A 547     3249   3662   3016   -749   -234    327       C  
ATOM   8311  CG  TRP A 547      26.736  48.972 -20.282  1.00 24.10           C  
ANISOU 8311  CG  TRP A 547     3038   3351   2766   -736   -231    330       C  
ATOM   8312  CD1 TRP A 547      26.088  50.133 -20.587  1.00 26.09           C  
ANISOU 8312  CD1 TRP A 547     3368   3526   3021   -768   -261    332       C  
ATOM   8313  CD2 TRP A 547      26.381  48.035 -21.309  1.00 23.36           C  
ANISOU 8313  CD2 TRP A 547     2919   3276   2679   -688   -199    330       C  
ATOM   8314  NE1 TRP A 547      25.343  49.976 -21.733  1.00 23.44           N  
ANISOU 8314  NE1 TRP A 547     3052   3162   2690   -742   -250    337       N  
ATOM   8315  CE2 TRP A 547      25.507  48.697 -22.197  1.00 22.30           C  
ANISOU 8315  CE2 TRP A 547     2847   3078   2548   -695   -212    335       C  
ATOM   8316  CE3 TRP A 547      26.711  46.699 -21.557  1.00 21.24           C  
ANISOU 8316  CE3 TRP A 547     2584   3071   2414   -638   -162    327       C  
ATOM   8317  CZ2 TRP A 547      24.975  48.073 -23.321  1.00 25.62           C  
ANISOU 8317  CZ2 TRP A 547     3261   3501   2972   -659   -189    336       C  
ATOM   8318  CZ3 TRP A 547      26.180  46.083 -22.662  1.00 20.20           C  
ANISOU 8318  CZ3 TRP A 547     2450   2937   2286   -601   -139    325       C  
ATOM   8319  CH2 TRP A 547      25.326  46.770 -23.537  1.00 23.59           C  
ANISOU 8319  CH2 TRP A 547     2940   3307   2716   -614   -152    329       C  
ATOM   8320  H   TRP A 547      29.432  48.282 -17.543  1.00 25.62           H  
ATOM   8321  HA  TRP A 547      28.996  47.397 -19.910  1.00 24.70           H  
ATOM   8322  HB2 TRP A 547      27.228  48.041 -18.562  1.00 31.35           H  
ATOM   8323  HB3 TRP A 547      27.706  49.555 -18.613  1.00 31.35           H  
ATOM   8324  HD1 TRP A 547      26.142  50.919 -20.092  1.00 31.31           H  
ATOM   8325  HE1 TRP A 547      24.853  50.581 -22.099  1.00 28.12           H  
ATOM   8326  HE3 TRP A 547      27.280  46.238 -20.984  1.00 25.48           H  
ATOM   8327  HZ2 TRP A 547      24.404  48.524 -23.901  1.00 30.74           H  
ATOM   8328  HZ3 TRP A 547      26.390  45.193 -22.834  1.00 24.24           H  
ATOM   8329  HH2 TRP A 547      24.989  46.327 -24.283  1.00 28.31           H  
ATOM   8330  N   PRO A 548      30.218  50.377 -20.129  1.00 24.29           N  
ANISOU 8330  N   PRO A 548     2982   3538   2708   -950   -256    394       N  
ATOM   8331  CA  PRO A 548      30.776  51.270 -21.159  1.00 26.96           C  
ANISOU 8331  CA  PRO A 548     3337   3889   3018  -1035   -266    427       C  
ATOM   8332  C   PRO A 548      31.952  50.668 -21.908  1.00 26.63           C  
ANISOU 8332  C   PRO A 548     3210   3960   2947  -1059   -236    452       C  
ATOM   8333  O   PRO A 548      32.286  51.154 -22.995  1.00 31.33           O  
ANISOU 8333  O   PRO A 548     3812   4575   3518  -1116   -234    479       O  
ATOM   8334  CB  PRO A 548      31.186  52.519 -20.362  1.00 31.52           C  
ANISOU 8334  CB  PRO A 548     3958   4435   3582  -1117   -309    432       C  
ATOM   8335  CG  PRO A 548      30.363  52.459 -19.115  1.00 33.67           C  
ANISOU 8335  CG  PRO A 548     4266   4645   3883  -1062   -324    396       C  
ATOM   8336  CD  PRO A 548      30.259  50.995 -18.790  1.00 26.76           C  
ANISOU 8336  CD  PRO A 548     3323   3820   3024   -973   -288    380       C  
ATOM   8337  HA  PRO A 548      30.087  51.516 -21.796  1.00 32.35           H  
ATOM   8338  HB2 PRO A 548      32.133  52.485 -20.156  1.00 37.82           H  
ATOM   8339  HB3 PRO A 548      30.986  53.319 -20.873  1.00 37.82           H  
ATOM   8340  HG2 PRO A 548      30.808  52.942 -18.401  1.00 40.41           H  
ATOM   8341  HG3 PRO A 548      29.486  52.841 -19.279  1.00 40.41           H  
ATOM   8342  HD2 PRO A 548      31.034  50.693 -18.290  1.00 32.11           H  
ATOM   8343  HD3 PRO A 548      29.449  50.805 -18.293  1.00 32.11           H  
ATOM   8344  N   THR A 549      32.582  49.620 -21.380  1.00 24.98           N  
ANISOU 8344  N   THR A 549     2922   3830   2740  -1017   -211    444       N  
ATOM   8345  CA  THR A 549      33.669  48.949 -22.082  1.00 28.32           C  
ANISOU 8345  CA  THR A 549     3258   4364   3137  -1026   -178    462       C  
ATOM   8346  C   THR A 549      33.181  47.850 -23.018  1.00 31.31           C  
ANISOU 8346  C   THR A 549     3614   4755   3529   -948   -138    451       C  
ATOM   8347  O   THR A 549      33.997  47.252 -23.730  1.00 27.21           O  
ANISOU 8347  O   THR A 549     3025   4325   2988   -947   -107    461       O  
ATOM   8348  CB  THR A 549      34.670  48.351 -21.081  1.00 27.38           C  
ANISOU 8348  CB  THR A 549     3062   4330   3013  -1016   -172    461       C  
ATOM   8349  OG1 THR A 549      34.095  47.214 -20.424  1.00 24.51           O  
ANISOU 8349  OG1 THR A 549     2681   3950   2683   -915   -156    434       O  
ATOM   8350  CG2 THR A 549      35.069  49.392 -20.051  1.00 31.54           C  
ANISOU 8350  CG2 THR A 549     3617   4838   3527  -1085   -213    466       C  
ATOM   8351  H   THR A 549      32.394  49.279 -20.613  1.00 29.98           H  
ATOM   8352  HA  THR A 549      34.139  49.612 -22.611  1.00 33.98           H  
ATOM   8353  HB  THR A 549      35.466  48.065 -21.555  1.00 32.86           H  
ATOM   8354  HG1 THR A 549      34.264  46.515 -20.858  1.00 29.42           H  
ATOM   8355 HG21 THR A 549      35.649  48.993 -19.384  1.00 37.84           H  
ATOM   8356 HG22 THR A 549      35.541  50.122 -20.482  1.00 37.84           H  
ATOM   8357 HG23 THR A 549      34.279  49.744 -19.611  1.00 37.84           H  
ATOM   8358  N   ASN A 550      31.881  47.578 -23.046  1.00 26.61           N  
ANISOU 8358  N   ASN A 550     3072   4074   2965   -884   -138    428       N  
ATOM   8359  CA  ASN A 550      31.374  46.500 -23.881  1.00 25.54           C  
ANISOU 8359  CA  ASN A 550     2916   3945   2841   -810   -103    414       C  
ATOM   8360  C   ASN A 550      31.426  46.901 -25.352  1.00 22.14           C  
ANISOU 8360  C   ASN A 550     2499   3529   2384   -853    -93    433       C  
ATOM   8361  O   ASN A 550      31.033  48.016 -25.705  1.00 25.25           O  
ANISOU 8361  O   ASN A 550     2957   3867   2769   -910   -121    449       O  
ATOM   8362  CB  ASN A 550      29.941  46.151 -23.498  1.00 21.41           C  
ANISOU 8362  CB  ASN A 550     2448   3329   2357   -738   -108    386       C  
ATOM   8363  CG  ASN A 550      29.509  44.829 -24.072  1.00 23.11           C  
ANISOU 8363  CG  ASN A 550     2634   3559   2589   -657    -71    367       C  
ATOM   8364  OD1 ASN A 550      30.088  43.794 -23.750  1.00 30.90           O  
ANISOU 8364  OD1 ASN A 550     3557   4603   3579   -613    -47    359       O  
ATOM   8365  ND2 ASN A 550      28.494  44.848 -24.928  1.00 27.50           N  
ANISOU 8365  ND2 ASN A 550     3236   4061   3152   -637    -68    360       N  
ATOM   8366  H   ASN A 550      31.278  47.996 -22.597  1.00 31.93           H  
ATOM   8367  HA  ASN A 550      31.926  45.712 -23.753  1.00 30.64           H  
ATOM   8368  HB2 ASN A 550      29.872  46.098 -22.532  1.00 25.69           H  
ATOM   8369  HB3 ASN A 550      29.345  46.837 -23.836  1.00 25.69           H  
ATOM   8370 HD21 ASN A 550      28.215  44.115 -25.280  1.00 33.00           H  
ATOM   8371 HD22 ASN A 550      28.116  45.594 -25.130  1.00 33.00           H  
ATOM   8372  N   PRO A 551      31.872  46.009 -26.242  1.00 22.39           N  
ANISOU 8372  N   PRO A 551     2473   3632   2402   -825    -54    432       N  
ATOM   8373  CA  PRO A 551      31.962  46.386 -27.661  1.00 28.96           C  
ANISOU 8373  CA  PRO A 551     3314   4488   3203   -870    -43    452       C  
ATOM   8374  C   PRO A 551      30.635  46.370 -28.399  1.00 25.77           C  
ANISOU 8374  C   PRO A 551     2975   4003   2814   -835    -45    441       C  
ATOM   8375  O   PRO A 551      30.587  46.842 -29.542  1.00 29.02           O  
ANISOU 8375  O   PRO A 551     3406   4421   3198   -878    -43    460       O  
ATOM   8376  CB  PRO A 551      32.930  45.345 -28.246  1.00 39.98           C  
ANISOU 8376  CB  PRO A 551     4619   5993   4576   -843      2    448       C  
ATOM   8377  CG  PRO A 551      32.873  44.188 -27.321  1.00 33.88           C  
ANISOU 8377  CG  PRO A 551     3809   5227   3839   -756     17    419       C  
ATOM   8378  CD  PRO A 551      32.462  44.685 -25.968  1.00 26.82           C  
ANISOU 8378  CD  PRO A 551     2955   4265   2970   -758    -20    416       C  
ATOM   8379  HA  PRO A 551      32.359  47.267 -27.742  1.00 34.76           H  
ATOM   8380  HB2 PRO A 551      32.639  45.091 -29.136  1.00 47.97           H  
ATOM   8381  HB3 PRO A 551      33.826  45.715 -28.283  1.00 47.97           H  
ATOM   8382  HG2 PRO A 551      32.224  43.548 -27.654  1.00 40.66           H  
ATOM   8383  HG3 PRO A 551      33.751  43.777 -27.274  1.00 40.66           H  
ATOM   8384  HD2 PRO A 551      31.806  44.092 -25.569  1.00 32.18           H  
ATOM   8385  HD3 PRO A 551      33.233  44.766 -25.384  1.00 32.18           H  
ATOM   8386  N   TYR A 552      29.562  45.881 -27.783  1.00 24.03           N  
ANISOU 8386  N   TYR A 552     2787   3711   2634   -763    -50    413       N  
ATOM   8387  CA  TYR A 552      28.300  45.723 -28.481  1.00 26.02           C  
ANISOU 8387  CA  TYR A 552     3090   3897   2901   -723    -49    400       C  
ATOM   8388  C   TYR A 552      27.180  46.489 -27.790  1.00 30.35           C  
ANISOU 8388  C   TYR A 552     3715   4340   3477   -717    -87    394       C  
ATOM   8389  O   TYR A 552      27.160  46.606 -26.561  1.00 26.07           O  
ANISOU 8389  O   TYR A 552     3178   3774   2956   -706   -104    384       O  
ATOM   8390  CB  TYR A 552      27.897  44.242 -28.562  1.00 28.71           C  
ANISOU 8390  CB  TYR A 552     3396   4250   3262   -632    -14    368       C  
ATOM   8391  CG  TYR A 552      28.928  43.334 -29.194  1.00 27.59           C  
ANISOU 8391  CG  TYR A 552     3178   4208   3098   -620     27    365       C  
ATOM   8392  CD1 TYR A 552      29.290  43.485 -30.521  1.00 31.17           C  
ANISOU 8392  CD1 TYR A 552     3619   4710   3513   -657     44    379       C  
ATOM   8393  CD2 TYR A 552      29.519  42.308 -28.466  1.00 26.24           C  
ANISOU 8393  CD2 TYR A 552     2947   4082   2941   -567     48    348       C  
ATOM   8394  CE1 TYR A 552      30.224  42.656 -31.099  1.00 27.05           C  
ANISOU 8394  CE1 TYR A 552     3026   4282   2969   -641     84    372       C  
ATOM   8395  CE2 TYR A 552      30.450  41.472 -29.037  1.00 26.43           C  
ANISOU 8395  CE2 TYR A 552     2900   4195   2945   -548     85    343       C  
ATOM   8396  CZ  TYR A 552      30.793  41.646 -30.353  1.00 28.28           C  
ANISOU 8396  CZ  TYR A 552     3123   4479   3143   -584    104    353       C  
ATOM   8397  OH  TYR A 552      31.721  40.809 -30.921  1.00 36.64           O  
ANISOU 8397  OH  TYR A 552     4110   5630   4180   -561    143    343       O  
ATOM   8398  H   TYR A 552      29.546  45.634 -26.959  1.00 28.84           H  
ATOM   8399  HA  TYR A 552      28.399  46.078 -29.378  1.00 31.23           H  
ATOM   8400  HB2 TYR A 552      27.736  43.917 -27.662  1.00 34.45           H  
ATOM   8401  HB3 TYR A 552      27.086  44.172 -29.090  1.00 34.45           H  
ATOM   8402  HD1 TYR A 552      28.896  44.157 -31.030  1.00 37.40           H  
ATOM   8403  HD2 TYR A 552      29.281  42.185 -27.575  1.00 31.49           H  
ATOM   8404  HE1 TYR A 552      30.469  42.776 -31.988  1.00 32.46           H  
ATOM   8405  HE2 TYR A 552      30.844  40.795 -28.535  1.00 31.71           H  
ATOM   8406  HH  TYR A 552      31.687  40.053 -30.557  1.00 43.97           H  
ATOM   8407  N   PRO A 553      26.218  46.994 -28.552  1.00 25.59           N  
ANISOU 8407  N   PRO A 553     3171   3677   2875   -721   -102    400       N  
ATOM   8408  CA  PRO A 553      25.065  47.655 -27.939  1.00 28.02           C  
ANISOU 8408  CA  PRO A 553     3549   3886   3211   -704   -136    390       C  
ATOM   8409  C   PRO A 553      24.061  46.642 -27.414  1.00 23.07           C  
ANISOU 8409  C   PRO A 553     2918   3226   2619   -614   -123    355       C  
ATOM   8410  O   PRO A 553      24.087  45.457 -27.749  1.00 25.20           O  
ANISOU 8410  O   PRO A 553     3145   3538   2893   -566    -89    339       O  
ATOM   8411  CB  PRO A 553      24.477  48.474 -29.094  1.00 39.97           C  
ANISOU 8411  CB  PRO A 553     5119   5360   4710   -738   -154    413       C  
ATOM   8412  CG  PRO A 553      24.794  47.662 -30.295  1.00 32.92           C  
ANISOU 8412  CG  PRO A 553     4182   4535   3793   -730   -118    416       C  
ATOM   8413  CD  PRO A 553      26.155  47.045 -30.028  1.00 28.42           C  
ANISOU 8413  CD  PRO A 553     3534   4059   3205   -744    -89    416       C  
ATOM   8414  HA  PRO A 553      25.336  48.251 -27.223  1.00 33.62           H  
ATOM   8415  HB2 PRO A 553      23.519  48.575 -28.980  1.00 47.97           H  
ATOM   8416  HB3 PRO A 553      24.899  49.346 -29.137  1.00 47.97           H  
ATOM   8417  HG2 PRO A 553      24.121  46.972 -30.410  1.00 39.51           H  
ATOM   8418  HG3 PRO A 553      24.822  48.232 -31.078  1.00 39.51           H  
ATOM   8419  HD2 PRO A 553      26.212  46.155 -30.408  1.00 34.10           H  
ATOM   8420  HD3 PRO A 553      26.863  47.604 -30.385  1.00 34.10           H  
ATOM   8421  N   LYS A 554      23.188  47.130 -26.542  1.00 26.29           N  
ANISOU 8421  N   LYS A 554     3375   3561   3054   -593   -150    341       N  
ATOM   8422  CA  LYS A 554      21.992  46.385 -26.178  1.00 20.42           C  
ANISOU 8422  CA  LYS A 554     2642   2776   2342   -517   -144    312       C  
ATOM   8423  C   LYS A 554      21.065  46.385 -27.384  1.00 24.72           C  
ANISOU 8423  C   LYS A 554     3217   3292   2884   -502   -143    315       C  
ATOM   8424  O   LYS A 554      20.741  47.450 -27.918  1.00 25.08           O  
ANISOU 8424  O   LYS A 554     3313   3297   2920   -539   -170    335       O  
ATOM   8425  CB  LYS A 554      21.330  47.024 -24.969  1.00 20.01           C  
ANISOU 8425  CB  LYS A 554     2633   2659   2314   -503   -173    297       C  
ATOM   8426  CG  LYS A 554      20.027  46.384 -24.549  1.00 24.22           C  
ANISOU 8426  CG  LYS A 554     3178   3149   2876   -430   -169    268       C  
ATOM   8427  CD  LYS A 554      19.685  46.847 -23.153  1.00 23.98           C  
ANISOU 8427  CD  LYS A 554     3171   3078   2863   -418   -191    251       C  
ATOM   8428  CE  LYS A 554      18.280  46.500 -22.775  1.00 22.87           C  
ANISOU 8428  CE  LYS A 554     3052   2890   2748   -354   -193    225       C  
ATOM   8429  NZ  LYS A 554      17.310  47.415 -23.425  1.00 22.67           N  
ANISOU 8429  NZ  LYS A 554     3085   2803   2726   -355   -218    229       N  
ATOM   8430  H   LYS A 554      23.265  47.890 -26.146  1.00 31.55           H  
ATOM   8431  HA  LYS A 554      22.206  45.471 -25.937  1.00 24.51           H  
ATOM   8432  HB2 LYS A 554      21.940  46.965 -24.217  1.00 24.02           H  
ATOM   8433  HB3 LYS A 554      21.146  47.954 -25.174  1.00 24.02           H  
ATOM   8434  HG2 LYS A 554      19.317  46.650 -25.153  1.00 29.07           H  
ATOM   8435  HG3 LYS A 554      20.117  45.418 -24.548  1.00 29.07           H  
ATOM   8436  HD2 LYS A 554      20.284  46.421 -22.520  1.00 28.78           H  
ATOM   8437  HD3 LYS A 554      19.783  47.811 -23.104  1.00 28.78           H  
ATOM   8438  HE2 LYS A 554      18.084  45.594 -23.058  1.00 27.44           H  
ATOM   8439  HE3 LYS A 554      18.176  46.577 -21.813  1.00 27.44           H  
ATOM   8440  HZ1 LYS A 554      16.501  47.305 -23.070  1.00 27.20           H  
ATOM   8441  HZ2 LYS A 554      17.563  48.260 -23.310  1.00 27.20           H  
ATOM   8442  HZ3 LYS A 554      17.267  47.244 -24.298  1.00 27.20           H  
ATOM   8443  N   SER A 555      20.663  45.204 -27.844  1.00 22.33           N  
ANISOU 8443  N   SER A 555     2885   3011   2587   -451   -114    298       N  
ATOM   8444  CA  SER A 555      20.012  45.084 -29.140  1.00 34.65           C  
ANISOU 8444  CA  SER A 555     4464   4565   4137   -445   -108    303       C  
ATOM   8445  C   SER A 555      18.491  45.079 -29.069  1.00 21.44           C  
ANISOU 8445  C   SER A 555     2832   2826   2489   -397   -124    287       C  
ATOM   8446  O   SER A 555      17.838  45.153 -30.119  1.00 22.22           O  
ANISOU 8446  O   SER A 555     2953   2912   2578   -396   -127    293       O  
ATOM   8447  CB  SER A 555      20.476  43.796 -29.838  1.00 38.46           C  
ANISOU 8447  CB  SER A 555     4892   5113   4607   -421    -66    292       C  
ATOM   8448  OG  SER A 555      20.065  42.657 -29.097  1.00 52.15           O  
ANISOU 8448  OG  SER A 555     6602   6842   6370   -356    -49    262       O  
ATOM   8449  H   SER A 555      20.757  44.461 -27.422  1.00 26.79           H  
ATOM   8450  HA  SER A 555      20.275  45.845 -29.682  1.00 41.58           H  
ATOM   8451  HB2 SER A 555      20.085  43.756 -30.724  1.00 46.15           H  
ATOM   8452  HB3 SER A 555      21.444  43.801 -29.902  1.00 46.15           H  
ATOM   8453  HG  SER A 555      19.370  42.833 -28.660  1.00 62.58           H  
ATOM   8454  N   ASP A 556      17.914  44.978 -27.877  1.00 16.25           N  
ANISOU 8454  N   ASP A 556     2184   2132   1861   -359   -133    266       N  
ATOM   8455  CA  ASP A 556      16.494  44.680 -27.763  1.00 15.36           C  
ANISOU 8455  CA  ASP A 556     2093   1971   1770   -306   -140    246       C  
ATOM   8456  C   ASP A 556      16.012  45.087 -26.372  1.00 17.58           C  
ANISOU 8456  C   ASP A 556     2394   2210   2076   -284   -159    230       C  
ATOM   8457  O   ASP A 556      16.628  45.933 -25.714  1.00 19.04           O  
ANISOU 8457  O   ASP A 556     2592   2384   2257   -318   -177    238       O  
ATOM   8458  CB  ASP A 556      16.244  43.187 -28.051  1.00 17.80           C  
ANISOU 8458  CB  ASP A 556     2363   2314   2086   -260   -105    226       C  
ATOM   8459  CG  ASP A 556      16.984  42.275 -27.085  1.00 22.09           C  
ANISOU 8459  CG  ASP A 556     2860   2892   2640   -240    -83    212       C  
ATOM   8460  OD1 ASP A 556      17.507  42.789 -26.075  1.00 18.77           O  
ANISOU 8460  OD1 ASP A 556     2439   2469   2224   -256    -95    216       O  
ATOM   8461  OD2 ASP A 556      17.049  41.050 -27.336  1.00 23.52           O  
ANISOU 8461  OD2 ASP A 556     3008   3103   2824   -208    -54    198       O  
ATOM   8462  H   ASP A 556      18.322  45.077 -27.127  1.00 19.51           H  
ATOM   8463  HA  ASP A 556      16.022  45.218 -28.417  1.00 18.43           H  
ATOM   8464  HB2 ASP A 556      15.295  43.003 -27.972  1.00 21.36           H  
ATOM   8465  HB3 ASP A 556      16.547  42.982 -28.950  1.00 21.36           H  
ATOM   8466  N   SER A 557      14.908  44.482 -25.926  1.00 16.11           N  
ANISOU 8466  N   SER A 557     2208   2000   1912   -229   -156    207       N  
ATOM   8467  CA  SER A 557      14.330  44.835 -24.636  1.00 15.90           C  
ANISOU 8467  CA  SER A 557     2199   1937   1906   -204   -172    189       C  
ATOM   8468  C   SER A 557      15.295  44.584 -23.489  1.00 17.27           C  
ANISOU 8468  C   SER A 557     2343   2139   2081   -213   -163    184       C  
ATOM   8469  O   SER A 557      15.176  45.208 -22.429  1.00 17.09           O  
ANISOU 8469  O   SER A 557     2339   2090   2066   -213   -182    174       O  
ATOM   8470  CB  SER A 557      13.060  44.025 -24.397  1.00 14.28           C  
ANISOU 8470  CB  SER A 557     1987   1717   1720   -146   -163    166       C  
ATOM   8471  OG  SER A 557      13.387  42.655 -24.230  1.00 15.91           O  
ANISOU 8471  OG  SER A 557     2148   1965   1930   -125   -132    157       O  
ATOM   8472  H   SER A 557      14.478  43.868 -26.348  1.00 19.33           H  
ATOM   8473  HA  SER A 557      14.111  45.780 -24.654  1.00 19.08           H  
ATOM   8474  HB2 SER A 557      12.620  44.349 -23.595  1.00 17.13           H  
ATOM   8475  HB3 SER A 557      12.470  44.123 -25.160  1.00 17.13           H  
ATOM   8476  HG  SER A 557      12.777  42.173 -24.548  1.00 19.09           H  
ATOM   8477  N   GLY A 558      16.228  43.652 -23.670  1.00 15.93           N  
ANISOU 8477  N   GLY A 558     2126   2024   1902   -218   -136    189       N  
ATOM   8478  CA  GLY A 558      17.093  43.194 -22.612  1.00 15.73           C  
ANISOU 8478  CA  GLY A 558     2064   2033   1879   -218   -126    186       C  
ATOM   8479  C   GLY A 558      16.630  41.918 -21.939  1.00 16.53           C  
ANISOU 8479  C   GLY A 558     2137   2144   1999   -165   -106    167       C  
ATOM   8480  O   GLY A 558      17.362  41.386 -21.095  1.00 16.14           O  
ANISOU 8480  O   GLY A 558     2054   2128   1952   -160    -96    167       O  
ATOM   8481  H   GLY A 558      16.375  43.264 -24.423  1.00 19.11           H  
ATOM   8482  HA2 GLY A 558      17.978  43.035 -22.977  1.00 18.87           H  
ATOM   8483  HA3 GLY A 558      17.151  43.885 -21.933  1.00 18.87           H  
ATOM   8484  N   LEU A 559      15.453  41.410 -22.302  1.00 15.03           N  
ANISOU 8484  N   LEU A 559     1959   1930   1822   -127   -100    154       N  
ATOM   8485  CA  LEU A 559      14.842  40.280 -21.611  1.00 15.30           C  
ANISOU 8485  CA  LEU A 559     1974   1966   1875    -80    -85    138       C  
ATOM   8486  C   LEU A 559      14.649  39.084 -22.526  1.00 18.87           C  
ANISOU 8486  C   LEU A 559     2406   2434   2329    -57    -60    134       C  
ATOM   8487  O   LEU A 559      14.459  37.982 -22.009  1.00 21.46           O  
ANISOU 8487  O   LEU A 559     2713   2771   2671    -24    -44    124       O  
ATOM   8488  CB  LEU A 559      13.492  40.687 -21.020  1.00 19.64           C  
ANISOU 8488  CB  LEU A 559     2554   2472   2437    -56   -102    121       C  
ATOM   8489  CG  LEU A 559      13.597  41.882 -20.078  1.00 17.56           C  
ANISOU 8489  CG  LEU A 559     2314   2186   2170    -74   -128    119       C  
ATOM   8490  CD1 LEU A 559      12.241  42.515 -19.869  1.00 19.07           C  
ANISOU 8490  CD1 LEU A 559     2542   2333   2372    -50   -146    102       C  
ATOM   8491  CD2 LEU A 559      14.216  41.440 -18.767  1.00 17.94           C  
ANISOU 8491  CD2 LEU A 559     2336   2260   2220    -70   -122    115       C  
ATOM   8492  OXT LEU A 559      14.693  39.203 -23.753  1.00 19.84           O  
ANISOU 8492  OXT LEU A 559     2536   2562   2440    -72    -55    140       O  
ATOM   8493  H   LEU A 559      14.981  41.708 -22.957  1.00 18.04           H  
ATOM   8494  HA  LEU A 559      15.436  40.009 -20.893  1.00 18.36           H  
ATOM   8495  HB2 LEU A 559      12.891  40.926 -21.743  1.00 23.57           H  
ATOM   8496  HB3 LEU A 559      13.129  39.940 -20.520  1.00 23.57           H  
ATOM   8497  HG  LEU A 559      14.169  42.562 -20.467  1.00 21.07           H  
ATOM   8498 HD11 LEU A 559      12.358  43.374 -19.434  1.00 22.89           H  
ATOM   8499 HD12 LEU A 559      11.814  42.637 -20.731  1.00 22.89           H  
ATOM   8500 HD13 LEU A 559      11.703  41.932 -19.312  1.00 22.89           H  
ATOM   8501 HD21 LEU A 559      14.516  42.223 -18.280  1.00 21.53           H  
ATOM   8502 HD22 LEU A 559      13.549  40.963 -18.248  1.00 21.53           H  
ATOM   8503 HD23 LEU A 559      14.969  40.858 -18.954  1.00 21.53           H  
TER    8504      LEU A 559                                                      
HETATM 8505  C1  NAG B   1      30.547  23.215 -12.987  1.00 23.38           C  
ANISOU 8505  C1  NAG B   1     2263   3587   3035    543     54    351       C  
HETATM 8506  C2  NAG B   1      30.508  22.250 -11.826  1.00 30.94           C  
ANISOU 8506  C2  NAG B   1     3236   4509   4009    576     33    375       C  
HETATM 8507  C3  NAG B   1      31.390  22.737 -10.675  1.00 27.22           C  
ANISOU 8507  C3  NAG B   1     2727   4099   3516    550      7    405       C  
HETATM 8508  C4  NAG B   1      32.803  23.047 -11.146  1.00 27.04           C  
ANISOU 8508  C4  NAG B   1     2649   4152   3475    547     16    400       C  
HETATM 8509  C5  NAG B   1      32.732  24.035 -12.300  1.00 31.88           C  
ANISOU 8509  C5  NAG B   1     3249   4792   4070    508     36    377       C  
HETATM 8510  C6  NAG B   1      34.078  24.349 -12.906  1.00 32.96           C  
ANISOU 8510  C6  NAG B   1     3333   5005   4186    500     48    370       C  
HETATM 8511  C7  NAG B   1      28.483  20.924 -11.438  1.00 32.84           C  
ANISOU 8511  C7  NAG B   1     3572   4613   4292    612     28    377       C  
HETATM 8512  C8  NAG B   1      27.087  20.936 -10.898  1.00 33.28           C  
ANISOU 8512  C8  NAG B   1     3684   4608   4353    585     18    382       C  
HETATM 8513  N2  NAG B   1      29.142  22.082 -11.368  1.00 27.31           N  
ANISOU 8513  N2  NAG B   1     2829   3985   3564    571     24    382       N  
HETATM 8514  O3  NAG B   1      31.418  21.734  -9.664  1.00 33.62           O  
ANISOU 8514  O3  NAG B   1     3553   4880   4343    585    -11    429       O  
HETATM 8515  O4  NAG B   1      33.543  23.629 -10.077  1.00 35.77           O  
ANISOU 8515  O4  NAG B   1     3721   5314   4556    513     -9    428       O  
HETATM 8516  O5  NAG B   1      31.921  23.488 -13.349  1.00 27.35           O  
ANISOU 8516  O5  NAG B   1     2712   4163   3518    539     61    349       O  
HETATM 8517  O6  NAG B   1      33.959  25.327 -13.931  1.00 41.47           O  
ANISOU 8517  O6  NAG B   1     4403   6109   5244    454     65    352       O  
HETATM 8518  O7  NAG B   1      28.992  19.914 -11.911  1.00 30.56           O  
ANISOU 8518  O7  NAG B   1     3283   4305   4021    660     39    365       O  
HETATM 8519  H2  NAG B   1      30.868  21.394 -12.128  1.00 37.13           H  
HETATM 8520  H3  NAG B   1      31.009  23.560 -10.313  1.00 32.66           H  
HETATM 8521  H4  NAG B   1      33.250  22.229 -11.436  1.00 32.45           H  
HETATM 8522  H5  NAG B   1      32.331  24.866 -11.982  1.00 38.25           H  
HETATM 8523  H61 NAG B   1      34.458  23.534 -13.284  1.00 39.56           H  
HETATM 8524  H62 NAG B   1      34.672  24.686 -12.209  1.00 39.56           H  
HETATM 8525  H81 NAG B   1      26.705  20.040 -10.964  1.00 39.93           H  
HETATM 8526  H82 NAG B   1      26.543  21.560 -11.415  1.00 39.93           H  
HETATM 8527  H83 NAG B   1      27.102  21.215  -9.963  1.00 39.93           H  
HETATM 8528  HN2 NAG B   1      28.711  22.804 -11.015  1.00 32.77           H  
HETATM 8529  HO3 NAG B   1      32.143  21.838  -9.163  1.00 40.35           H  
HETATM 8530  HO6 NAG B   1      34.387  26.065 -13.686  1.00 49.76           H  
HETATM 8531  C1  NAG B   2      34.877  23.055 -10.027  1.00 31.43           C  
ANISOU 8531  C1  NAG B   2     3128   4809   4005    548     -8    434       C  
HETATM 8532  C2  NAG B   2      35.785  23.956  -9.201  1.00 21.43           C  
ANISOU 8532  C2  NAG B   2     1820   3620   2705    498    -29    457       C  
HETATM 8533  C3  NAG B   2      37.200  23.390  -9.192  1.00 48.25           C  
ANISOU 8533  C3  NAG B   2     5166   7068   6097    535    -28    464       C  
HETATM 8534  C4  NAG B   2      37.215  21.901  -8.863  1.00 41.90           C  
ANISOU 8534  C4  NAG B   2     4377   6215   5326    611    -31    471       C  
HETATM 8535  C5  NAG B   2      36.095  21.108  -9.543  1.00 53.17           C  
ANISOU 8535  C5  NAG B   2     5859   7556   6789    650    -14    449       C  
HETATM 8536  C6  NAG B   2      35.905  19.734  -8.934  1.00 40.12           C  
ANISOU 8536  C6  NAG B   2     4233   5843   5168    710    -26    463       C  
HETATM 8537  C7  NAG B   2      35.014  26.284  -9.214  1.00 31.83           C  
ANISOU 8537  C7  NAG B   2     3145   4969   3979    373    -42    452       C  
HETATM 8538  C8  NAG B   2      35.150  27.630  -9.857  1.00 35.81           C  
ANISOU 8538  C8  NAG B   2     3634   5515   4456    304    -38    440       C  
HETATM 8539  N2  NAG B   2      35.787  25.316  -9.714  1.00 28.92           N  
ANISOU 8539  N2  NAG B   2     2754   4609   3624    430    -25    447       N  
HETATM 8540  O3  NAG B   2      37.978  24.095  -8.227  1.00 38.96           O  
ANISOU 8540  O3  NAG B   2     3955   5958   4890    491    -51    490       O  
HETATM 8541  O4  NAG B   2      38.446  21.359  -9.343  1.00 40.79           O  
ANISOU 8541  O4  NAG B   2     4192   6118   5188    653    -19    465       O  
HETATM 8542  O5  NAG B   2      34.833  21.776  -9.435  1.00 39.39           O  
ANISOU 8542  O5  NAG B   2     4154   5772   5039    606    -17    447       O  
HETATM 8543  O6  NAG B   2      34.853  19.014  -9.565  1.00 55.37           O  
ANISOU 8543  O6  NAG B   2     6217   7691   7128    740    -12    442       O  
HETATM 8544  O7  NAG B   2      34.240  26.082  -8.285  1.00 35.01           O  
ANISOU 8544  O7  NAG B   2     3579   5333   4390    375    -59    465       O  
HETATM 8545  H2  NAG B   2      35.451  23.973  -8.284  1.00 25.72           H  
HETATM 8546  H3  NAG B   2      37.578  23.510 -10.084  1.00 57.89           H  
HETATM 8547  H4  NAG B   2      37.099  21.815  -7.898  1.00 50.27           H  
HETATM 8548  H5  NAG B   2      36.313  21.032 -10.492  1.00 63.81           H  
HETATM 8549  H61 NAG B   2      35.696  19.834  -7.986  1.00 48.15           H  
HETATM 8550  H62 NAG B   2      36.734  19.228  -9.027  1.00 48.15           H  
HETATM 8551  H81 NAG B   2      34.514  28.250  -9.453  1.00 42.97           H  
HETATM 8552  H82 NAG B   2      34.968  27.555 -10.813  1.00 42.97           H  
HETATM 8553  H83 NAG B   2      36.058  27.964  -9.724  1.00 42.97           H  
HETATM 8554  HN2 NAG B   2      36.341  25.517 -10.409  1.00 34.70           H  
HETATM 8555  HO3 NAG B   2      38.622  24.546  -8.639  1.00 46.75           H  
HETATM 8556  HO6 NAG B   2      34.286  18.718  -8.949  1.00 66.44           H  
HETATM 8557  C1  BMA B   3      39.480  21.252  -8.342  1.00 37.48           C  
ANISOU 8557  C1  BMA B   3     3733   5753   4756    658    -42    495       C  
HETATM 8558  C2  BMA B   3      40.481  20.167  -8.803  1.00 78.73           C  
ANISOU 8558  C2  BMA B   3     8926  10990   9999    731    -31    487       C  
HETATM 8559  C3  BMA B   3      41.665  20.086  -7.835  1.00 42.71           C  
ANISOU 8559  C3  BMA B   3     4314   6493   5421    737    -53    519       C  
HETATM 8560  C4  BMA B   3      42.233  21.477  -7.500  1.00 50.35           C  
ANISOU 8560  C4  BMA B   3     5244   7545   6343    659    -62    531       C  
HETATM 8561  C5  BMA B   3      41.114  22.446  -7.084  1.00 61.74           C  
ANISOU 8561  C5  BMA B   3     6728   8960   7771    590    -72    534       C  
HETATM 8562  C6  BMA B   3      41.620  23.867  -6.814  1.00 35.23           C  
ANISOU 8562  C6  BMA B   3     3340   5678   4369    507    -82    543       C  
HETATM 8563  O2  BMA B   3      41.015  20.492 -10.083  1.00 40.76           O  
ANISOU 8563  O2  BMA B   3     4088   6220   5180    729     -2    458       O  
HETATM 8564  O3  BMA B   3      42.708  19.234  -8.345  1.00 44.17           O  
ANISOU 8564  O3  BMA B   3     4461   6703   5620    802    -42    510       O  
HETATM 8565  O4  BMA B   3      43.175  21.363  -6.432  1.00 52.25           O  
ANISOU 8565  O4  BMA B   3     5446   7839   6569    662    -86    563       O  
HETATM 8566  O5  BMA B   3      40.150  22.490  -8.156  1.00 33.32           O  
ANISOU 8566  O5  BMA B   3     3166   5305   4188    592    -48    504       O  
HETATM 8567  O6  BMA B   3      40.514  24.655  -6.383  1.00 50.87           O  
ANISOU 8567  O6  BMA B   3     5363   7624   6342    452    -94    544       O  
HETATM 8568  H2  BMA B   3      39.960  19.197  -8.832  1.00 94.48           H  
HETATM 8569  H3  BMA B   3      41.332  19.632  -6.892  1.00 51.25           H  
HETATM 8570  H4  BMA B   3      42.687  21.880  -8.420  1.00 60.42           H  
HETATM 8571  H5  BMA B   3      40.630  22.085  -6.161  1.00 74.09           H  
HETATM 8572  H61 BMA B   3      42.063  24.261  -7.742  1.00 42.28           H  
HETATM 8573  H62 BMA B   3      42.407  23.817  -6.047  1.00 42.28           H  
HETATM 8574  HO2 BMA B   3      40.975  19.676 -10.605  1.00 48.91           H  
HETATM 8575  HO3 BMA B   3      42.376  18.328  -8.238  1.00 53.01           H  
HETATM 8576  HO4 BMA B   3      42.746  21.778  -5.667  1.00 62.70           H  
HETATM 8577  C1  MAN B   4      40.972  25.938  -5.893  1.00 52.60           C  
ANISOU 8577  C1  MAN B   4     5560   7907   6520    372   -110    554       C  
HETATM 8578  C2  MAN B   4      39.742  26.665  -5.272  1.00 72.18           C  
ANISOU 8578  C2  MAN B   4     8088  10344   8994    321   -125    554       C  
HETATM 8579  C3  MAN B   4      38.753  27.116  -6.353  1.00 35.72           C  
ANISOU 8579  C3  MAN B   4     3504   5680   4387    304   -106    526       C  
HETATM 8580  C4  MAN B   4      39.462  27.821  -7.514  1.00114.22           C  
ANISOU 8580  C4  MAN B   4    13415  15673  14311    272    -87    509       C  
HETATM 8581  C5  MAN B   4      40.662  27.006  -8.023  1.00 92.73           C  
ANISOU 8581  C5  MAN B   4    10646  12994  11594    326    -71    510       C  
HETATM 8582  C6  MAN B   4      41.486  27.771  -9.059  1.00 85.20           C  
ANISOU 8582  C6  MAN B   4     9655  12103  10613    287    -54    497       C  
HETATM 8583  O2  MAN B   4      40.140  27.858  -4.593  1.00 78.91           O  
ANISOU 8583  O2  MAN B   4     8926  11250   9807    244   -146    564       O  
HETATM 8584  O3  MAN B   4      37.756  27.992  -5.810  1.00 65.82           O  
ANISOU 8584  O3  MAN B   4     7354   9467   8189    248   -122    525       O  
HETATM 8585  O4  MAN B   4      38.531  27.999  -8.579  1.00 38.58           O  
ANISOU 8585  O4  MAN B   4     3867   6047   4747    270    -66    484       O  
HETATM 8586  O5  MAN B   4      41.547  26.705  -6.931  1.00 58.08           O  
ANISOU 8586  O5  MAN B   4     6226   8649   7194    337    -92    537       O  
HETATM 8587  O6  MAN B   4      41.926  28.995  -8.463  1.00 70.57           O  
ANISOU 8587  O6  MAN B   4     7789  10304   8722    205    -75    511       O  
HETATM 8588  H2  MAN B   4      39.237  25.966  -4.592  1.00 86.62           H  
HETATM 8589  H3  MAN B   4      38.247  26.229  -6.750  1.00 42.86           H  
HETATM 8590  H4  MAN B   4      39.867  28.774  -7.134  1.00137.07           H  
HETATM 8591  H5  MAN B   4      40.289  26.072  -8.462  1.00111.28           H  
HETATM 8592  H61 MAN B   4      40.855  27.955  -9.942  1.00102.23           H  
HETATM 8593  H62 MAN B   4      42.337  27.141  -9.363  1.00102.23           H  
HETATM 8594  HO2 MAN B   4      39.620  27.948  -3.784  1.00 94.70           H  
HETATM 8595  HO4 MAN B   4      37.657  27.977  -8.159  1.00 46.30           H  
HETATM 8596  HO6 MAN B   4      42.022  29.645  -9.171  1.00 84.69           H  
HETATM 8597  C1  MAN B   5      36.457  27.363  -5.794  1.00 61.74           C  
ANISOU 8597  C1  MAN B   5     6886   8871   7703    284   -118    518       C  
HETATM 8598  C2  MAN B   5      35.430  28.494  -5.947  1.00115.09           C  
ANISOU 8598  C2  MAN B   5    13675  15605  14448    223   -123    503       C  
HETATM 8599  C3  MAN B   5      35.326  29.343  -4.663  1.00 97.70           C  
ANISOU 8599  C3  MAN B   5    11480  13424  12216    164   -155    516       C  
HETATM 8600  C4  MAN B   5      35.668  28.654  -3.318  1.00102.89           C  
ANISOU 8600  C4  MAN B   5    12131  14093  12868    187   -175    543       C  
HETATM 8601  C5  MAN B   5      36.547  27.408  -3.432  1.00 93.85           C  
ANISOU 8601  C5  MAN B   5    10956  12960  11743    256   -164    558       C  
HETATM 8602  C6  MAN B   5      36.333  26.473  -2.231  1.00100.04           C  
ANISOU 8602  C6  MAN B   5    11754  13720  12534    292   -181    584       C  
HETATM 8603  O2  MAN B   5      34.116  27.980  -6.226  1.00 63.17           O  
ANISOU 8603  O2  MAN B   5     7146   8956   7902    255   -114    493       O  
HETATM 8604  O3  MAN B   5      33.979  29.880  -4.559  1.00 70.38           O  
ANISOU 8604  O3  MAN B   5     8066   9916   8760    137   -162    503       O  
HETATM 8605  O4  MAN B   5      36.386  29.589  -2.462  1.00 72.01           O  
ANISOU 8605  O4  MAN B   5     8199  10242   8919    125   -198    553       O  
HETATM 8606  O5  MAN B   5      36.229  26.668  -4.599  1.00 73.40           O  
ANISOU 8606  O5  MAN B   5     8376  10326   9185    309   -137    541       O  
HETATM 8607  O6  MAN B   5      34.899  26.364  -1.971  1.00 36.27           O  
ANISOU 8607  O6  MAN B   5     3730   5578   4471    292   -184    579       O  
HETATM 8608  H2  MAN B   5      35.759  29.153  -6.761  1.00138.11           H  
HETATM 8609  H3  MAN B   5      36.089  30.122  -4.767  1.00117.24           H  
HETATM 8610  H4  MAN B   5      34.691  28.312  -2.936  1.00123.46           H  
HETATM 8611  H5  MAN B   5      37.598  27.719  -3.502  1.00112.62           H  
HETATM 8612  H61 MAN B   5      36.868  26.894  -1.365  1.00120.04           H  
HETATM 8613  H62 MAN B   5      36.774  25.494  -2.471  1.00120.04           H  
HETATM 8614  HO2 MAN B   5      33.646  28.607  -6.789  1.00 75.81           H  
HETATM 8615  HO3 MAN B   5      33.392  29.107  -4.579  1.00 84.46           H  
HETATM 8616  HO4 MAN B   5      36.632  29.078  -1.676  1.00 86.41           H  
HETATM 8617  HO6 MAN B   5      34.680  26.997  -1.275  1.00 43.52           H  
HETATM 8618  C1  NAG C   1      26.692  38.924 -26.569  1.00 17.82           C  
ANISOU 8618  C1  NAG C   1     1913   2856   2000   -304     70    256       C  
HETATM 8619  C2  NAG C   1      26.573  40.302 -27.177  1.00 16.30           C  
ANISOU 8619  C2  NAG C   1     1761   2649   1783   -378     48    278       C  
HETATM 8620  C3  NAG C   1      26.189  40.195 -28.658  1.00 19.17           C  
ANISOU 8620  C3  NAG C   1     2140   3017   2127   -382     65    274       C  
HETATM 8621  C4  NAG C   1      27.174  39.303 -29.395  1.00 18.87           C  
ANISOU 8621  C4  NAG C   1     2038   3063   2069   -365    104    267       C  
HETATM 8622  C5  NAG C   1      27.325  37.966 -28.669  1.00 19.55           C  
ANISOU 8622  C5  NAG C   1     2087   3159   2184   -288    124    243       C  
HETATM 8623  C6  NAG C   1      28.372  37.060 -29.281  1.00 21.49           C  
ANISOU 8623  C6  NAG C   1     2267   3488   2412   -262    163    233       C  
HETATM 8624  C7  NAG C   1      25.975  42.093 -25.613  1.00 20.14           C  
ANISOU 8624  C7  NAG C   1     2320   3047   2284   -435    -15    294       C  
HETATM 8625  C8  NAG C   1      24.856  42.881 -25.010  1.00 20.64           C  
ANISOU 8625  C8  NAG C   1     2450   3025   2367   -437    -48    289       C  
HETATM 8626  N2  NAG C   1      25.617  41.132 -26.468  1.00 18.55           N  
ANISOU 8626  N2  NAG C   1     2106   2855   2086   -390     13    280       N  
HETATM 8627  O3  NAG C   1      26.136  41.512 -29.197  1.00 21.22           O  
ANISOU 8627  O3  NAG C   1     2438   3263   2363   -454     42    300       O  
HETATM 8628  O4  NAG C   1      26.671  38.910 -30.666  1.00 19.72           O  
ANISOU 8628  O4  NAG C   1     2160   3171   2163   -352    124    254       O  
HETATM 8629  O5  NAG C   1      27.677  38.165 -27.297  1.00 16.21           O  
ANISOU 8629  O5  NAG C   1     1651   2731   1778   -289    105    253       O  
HETATM 8630  O6  NAG C   1      29.620  37.719 -29.446  1.00 25.36           O  
ANISOU 8630  O6  NAG C   1     2712   4058   2868   -319    165    257       O  
HETATM 8631  O7  NAG C   1      27.146  42.307 -25.326  1.00 23.87           O  
ANISOU 8631  O7  NAG C   1     2752   3581   2739   -471    -14    310       O  
HETATM 8632  H2  NAG C   1      27.450  40.726 -27.110  1.00 19.56           H  
HETATM 8633  H3  NAG C   1      25.307  39.789 -28.760  1.00 23.00           H  
HETATM 8634  H4  NAG C   1      28.003  39.813 -29.462  1.00 22.65           H  
HETATM 8635  H5  NAG C   1      26.463  37.507 -28.693  1.00 23.46           H  
HETATM 8636  H61 NAG C   1      28.057  36.757 -30.154  1.00 25.79           H  
HETATM 8637  H62 NAG C   1      28.498  36.285 -28.701  1.00 25.79           H  
HETATM 8638  H81 NAG C   1      25.168  43.318 -24.195  1.00 24.77           H  
HETATM 8639  H82 NAG C   1      24.116  42.282 -24.796  1.00 24.77           H  
HETATM 8640  H83 NAG C   1      24.554  43.556 -25.647  1.00 24.77           H  
HETATM 8641  HN2 NAG C   1      24.728  40.991 -26.615  1.00 22.26           H  
HETATM 8642  HO3 NAG C   1      26.329  41.486 -30.063  1.00 25.47           H  
HETATM 8643  HO6 NAG C   1      29.555  38.553 -29.148  1.00 30.44           H  
HETATM 8644  C1  NAG C   2      27.112  39.702 -31.756  1.00 17.73           C  
ANISOU 8644  C1  NAG C   2     1908   2959   1868   -416    126    276       C  
HETATM 8645  C2  NAG C   2      26.816  38.902 -33.019  1.00 20.13           C  
ANISOU 8645  C2  NAG C   2     2208   3285   2156   -387    157    254       C  
HETATM 8646  C3  NAG C   2      27.134  39.733 -34.261  1.00 21.17           C  
ANISOU 8646  C3  NAG C   2     2346   3458   2240   -456    158    278       C  
HETATM 8647  C4  NAG C   2      26.471  41.102 -34.194  1.00 27.49           C  
ANISOU 8647  C4  NAG C   2     3210   4195   3039   -515    115    309       C  
HETATM 8648  C5  NAG C   2      26.808  41.776 -32.869  1.00 25.67           C  
ANISOU 8648  C5  NAG C   2     2984   3941   2829   -536     87    325       C  
HETATM 8649  C6  NAG C   2      26.125  43.110 -32.669  1.00 35.17           C  
ANISOU 8649  C6  NAG C   2     4254   5071   4036   -586     43    350       C  
HETATM 8650  C7  NAG C   2      27.032  36.449 -32.799  1.00 22.24           C  
ANISOU 8650  C7  NAG C   2     2415   3580   2457   -257    210    195       C  
HETATM 8651  C8  NAG C   2      27.976  35.289 -32.868  1.00 23.43           C  
ANISOU 8651  C8  NAG C   2     2501   3794   2605   -205    248    172       C  
HETATM 8652  N2  NAG C   2      27.568  37.654 -33.039  1.00 21.65           N  
ANISOU 8652  N2  NAG C   2     2339   3536   2351   -332    195    228       N  
HETATM 8653  O3  NAG C   2      26.670  39.018 -35.399  1.00 26.95           O  
ANISOU 8653  O3  NAG C   2     3083   4201   2957   -428    184    255       O  
HETATM 8654  O4  NAG C   2      26.947  41.918 -35.257  1.00 28.79           O  
ANISOU 8654  O4  NAG C   2     3378   4405   3156   -587    115    338       O  
HETATM 8655  O5  NAG C   2      26.405  40.924 -31.790  1.00 24.07           O  
ANISOU 8655  O5  NAG C   2     2773   3702   2669   -466     90    298       O  
HETATM 8656  O6  NAG C   2      24.708  43.009 -32.696  1.00 36.16           O  
ANISOU 8656  O6  NAG C   2     4434   5115   4188   -544     28    335       O  
HETATM 8657  O7  NAG C   2      25.847  36.303 -32.523  1.00 22.59           O  
ANISOU 8657  O7  NAG C   2     2507   3546   2528   -232    194    184       O  
HETATM 8658  H2  NAG C   2      25.863  38.694 -33.028  1.00 24.16           H  
HETATM 8659  H3  NAG C   2      28.099  39.872 -34.321  1.00 25.40           H  
HETATM 8660  H4  NAG C   2      25.504  40.998 -34.271  1.00 32.99           H  
HETATM 8661  H5  NAG C   2      27.772  41.923 -32.823  1.00 30.81           H  
HETATM 8662  H61 NAG C   2      26.409  43.718 -33.377  1.00 42.20           H  
HETATM 8663  H62 NAG C   2      26.397  43.476 -31.806  1.00 42.20           H  
HETATM 8664  H81 NAG C   2      27.532  34.487 -32.533  1.00 28.11           H  
HETATM 8665  H82 NAG C   2      28.763  35.477 -32.321  1.00 28.11           H  
HETATM 8666  H83 NAG C   2      28.250  35.146 -33.794  1.00 28.11           H  
HETATM 8667  HN2 NAG C   2      28.459  37.696 -33.226  1.00 25.98           H  
HETATM 8668  HO3 NAG C   2      25.807  39.187 -35.523  1.00 32.34           H  
HETATM 8669  HO4 NAG C   2      26.404  41.841 -35.956  1.00 34.55           H  
HETATM 8670  HO6 NAG C   2      24.457  42.564 -33.422  1.00 43.39           H  
HETATM 8671  C1  NAG D   1      18.829  13.048 -19.583  1.00 23.50           C  
ANISOU 8671  C1  NAG D   1     2940   2706   3282    694    156     87       C  
HETATM 8672  C2  NAG D   1      18.318  11.765 -18.915  1.00 21.81           C  
ANISOU 8672  C2  NAG D   1     2775   2415   3098    710    139    106       C  
HETATM 8673  C3  NAG D   1      18.628  11.798 -17.407  1.00 21.78           C  
ANISOU 8673  C3  NAG D   1     2751   2425   3101    715    115    161       C  
HETATM 8674  C4  NAG D   1      20.077  12.173 -17.135  1.00 23.39           C  
ANISOU 8674  C4  NAG D   1     2895   2692   3301    759    118    175       C  
HETATM 8675  C5  NAG D   1      20.495  13.400 -17.941  1.00 27.86           C  
ANISOU 8675  C5  NAG D   1     3419   3329   3838    738    137    148       C  
HETATM 8676  C6  NAG D   1      21.972  13.693 -17.828  1.00 25.58           C  
ANISOU 8676  C6  NAG D   1     3069   3106   3545    780    142    157       C  
HETATM 8677  C7  NAG D   1      16.316  10.440 -19.524  1.00 25.72           C  
ANISOU 8677  C7  NAG D   1     3374   2789   3611    666    133     79       C  
HETATM 8678  C8  NAG D   1      14.816  10.441 -19.590  1.00 20.84           C  
ANISOU 8678  C8  NAG D   1     2795   2138   2984    602    125     76       C  
HETATM 8679  N2  NAG D   1      16.885  11.584 -19.112  1.00 20.13           N  
ANISOU 8679  N2  NAG D   1     2611   2155   2883    659    133     97       N  
HETATM 8680  O3  NAG D   1      18.343  10.525 -16.834  1.00 22.13           O  
ANISOU 8680  O3  NAG D   1     2838   2396   3172    738     99    182       O  
HETATM 8681  O4  NAG D   1      20.239  12.546 -15.769  1.00 23.34           O  
ANISOU 8681  O4  NAG D   1     2865   2714   3290    746     95    223       O  
HETATM 8682  O5  NAG D   1      20.214  13.196 -19.329  1.00 25.43           O  
ANISOU 8682  O5  NAG D   1     3134   3001   3527    740    160     99       O  
HETATM 8683  O6  NAG D   1      22.738  12.574 -18.255  1.00 30.76           O  
ANISOU 8683  O6  NAG D   1     3728   3738   4220    835    148    137       O  
HETATM 8684  O7  NAG D   1      16.979   9.463 -19.862  1.00 25.49           O  
ANISOU 8684  O7  NAG D   1     3361   2722   3603    723    140     64       O  
HETATM 8685  H2  NAG D   1      18.787  11.014 -19.325  1.00 26.17           H  
HETATM 8686  H3  NAG D   1      18.056  12.476 -17.000  1.00 26.14           H  
HETATM 8687  H4  NAG D   1      20.621  11.398 -17.370  1.00 28.07           H  
HETATM 8688  H5  NAG D   1      19.987  14.174 -17.632  1.00 33.43           H  
HETATM 8689  H61 NAG D   1      22.190  13.897 -16.899  1.00 30.70           H  
HETATM 8690  H62 NAG D   1      22.191  14.464 -18.385  1.00 30.70           H  
HETATM 8691  H81 NAG D   1      14.531  10.656 -20.498  1.00 25.00           H  
HETATM 8692  H82 NAG D   1      14.464  11.109 -18.972  1.00 25.00           H  
HETATM 8693  H83 NAG D   1      14.479   9.559 -19.342  1.00 25.00           H  
HETATM 8694  HN2 NAG D   1      16.339  12.295 -18.944  1.00 24.16           H  
HETATM 8695  HO3 NAG D   1      17.517  10.282 -17.048  1.00 26.55           H  
HETATM 8696  HO6 NAG D   1      22.739  12.537 -19.142  1.00 36.91           H  
HETATM 8697  C1  NAG D   2      20.247  11.487 -14.806  1.00 22.95           C  
ANISOU 8697  C1  NAG D   2     2839   2618   3263    768     72    258       C  
HETATM 8698  C2  NAG D   2      21.204  11.931 -13.722  1.00 28.14           C  
ANISOU 8698  C2  NAG D   2     3445   3337   3909    775     55    296       C  
HETATM 8699  C3  NAG D   2      21.256  10.898 -12.606  1.00 28.27           C  
ANISOU 8699  C3  NAG D   2     3484   3314   3943    789     26    334       C  
HETATM 8700  C4  NAG D   2      19.850  10.616 -12.100  1.00 31.02           C  
ANISOU 8700  C4  NAG D   2     3884   3609   4295    748     16    357       C  
HETATM 8701  C5  NAG D   2      18.905  10.305 -13.260  1.00 21.40           C  
ANISOU 8701  C5  NAG D   2     2711   2333   3086    738     36    317       C  
HETATM 8702  C6  NAG D   2      17.458  10.240 -12.827  1.00 27.85           C  
ANISOU 8702  C6  NAG D   2     3571   3114   3898    679     26    332       C  
HETATM 8703  C7  NAG D   2      23.047  13.406 -14.362  1.00 52.99           C  
ANISOU 8703  C7  NAG D   2     6493   6616   7026    792     75    274       C  
HETATM 8704  C8  NAG D   2      24.431  13.484 -14.928  1.00 32.34           C  
ANISOU 8704  C8  NAG D   2     3828   4054   4405    826     87    254       C  
HETATM 8705  N2  NAG D   2      22.530  12.179 -14.253  1.00 27.09           N  
ANISOU 8705  N2  NAG D   2     3262   3259   3770    809     66    275       N  
HETATM 8706  O3  NAG D   2      22.072  11.400 -11.555  1.00 34.25           O  
ANISOU 8706  O3  NAG D   2     4194   4134   4685    789      8    369       O  
HETATM 8707  O4  NAG D   2      19.864   9.485 -11.240  1.00 25.60           O  
ANISOU 8707  O4  NAG D   2     3227   2876   3625    762    -10    390       O  
HETATM 8708  O5  NAG D   2      18.982  11.321 -14.270  1.00 24.36           O  
ANISOU 8708  O5  NAG D   2     3060   2754   3442    724     60    277       O  
HETATM 8709  O6  NAG D   2      17.069  11.429 -12.154  1.00 25.02           O  
ANISOU 8709  O6  NAG D   2     3182   2816   3509    627     21    347       O  
HETATM 8710  O7  NAG D   2      22.423  14.411 -14.021  1.00 28.94           O  
ANISOU 8710  O7  NAG D   2     3440   3594   3962    749     74    288       O  
HETATM 8711  H2  NAG D   2      20.864  12.765 -13.345  1.00 33.76           H  
HETATM 8712  H3  NAG D   2      21.644  10.066 -12.939  1.00 33.92           H  
HETATM 8713  H4  NAG D   2      19.534  11.406 -11.622  1.00 37.23           H  
HETATM 8714  H5  NAG D   2      19.173   9.455 -13.658  1.00 25.68           H  
HETATM 8715  H61 NAG D   2      17.338   9.479 -12.228  1.00 33.42           H  
HETATM 8716  H62 NAG D   2      16.895  10.119 -13.615  1.00 33.42           H  
HETATM 8717  H81 NAG D   2      24.610  14.396 -15.226  1.00 38.80           H  
HETATM 8718  H82 NAG D   2      24.507  12.873 -15.686  1.00 38.80           H  
HETATM 8719  H83 NAG D   2      25.078  13.233 -14.242  1.00 38.80           H  
HETATM 8720  HN2 NAG D   2      23.033  11.468 -14.523  1.00 32.50           H  
HETATM 8721  HO3 NAG D   2      21.581  11.500 -10.821  1.00 41.10           H  
HETATM 8722  HO6 NAG D   2      17.676  12.062 -12.295  1.00 30.03           H  
HETATM 8723  C1  BMA D   3      19.798   9.927  -9.887  1.00 25.46           C  
ANISOU 8723  C1  BMA D   3     3189   2895   3590    735    -31    439       C  
HETATM 8724  C2  BMA D   3      19.409   8.710  -9.133  1.00 26.16           C  
ANISOU 8724  C2  BMA D   3     3325   2921   3695    736    -56    472       C  
HETATM 8725  C3  BMA D   3      19.300   9.056  -7.662  1.00 42.21           C  
ANISOU 8725  C3  BMA D   3     5341   4993   5706    706    -79    526       C  
HETATM 8726  C4  BMA D   3      20.505   9.819  -7.106  1.00 68.31           C  
ANISOU 8726  C4  BMA D   3     8582   8380   8992    722    -85    537       C  
HETATM 8727  C5  BMA D   3      21.173  10.806  -8.087  1.00 56.61           C  
ANISOU 8727  C5  BMA D   3     7055   6951   7502    735    -60    495       C  
HETATM 8728  C6  BMA D   3      22.701  10.919  -7.780  1.00 81.72           C  
ANISOU 8728  C6  BMA D   3    10183  10190  10679    772    -69    501       C  
HETATM 8729  O2  BMA D   3      20.412   7.719  -9.284  1.00 40.58           O  
ANISOU 8729  O2  BMA D   3     5153   4721   5544    791    -67    466       O  
HETATM 8730  O3  BMA D   3      19.151   7.854  -6.912  1.00 41.37           O  
ANISOU 8730  O3  BMA D   3     5275   4832   5613    712   -105    561       O  
HETATM 8731  O4  BMA D   3      20.077  10.592  -5.956  1.00 77.86           O  
ANISOU 8731  O4  BMA D   3     9774   9638  10172    677    -97    574       O  
HETATM 8732  O5  BMA D   3      21.054  10.398  -9.466  1.00 37.99           O  
ANISOU 8732  O5  BMA D   3     4720   4549   5165    758    -38    448       O  
HETATM 8733  O6  BMA D   3      23.093  12.278  -7.674  1.00 59.38           O  
ANISOU 8733  O6  BMA D   3     7301   7440   7821    747    -61    498       O  
HETATM 8734  H2  BMA D   3      18.441   8.325  -9.488  1.00 31.39           H  
HETATM 8735  H3  BMA D   3      18.427   9.706  -7.515  1.00 50.66           H  
HETATM 8736  H4  BMA D   3      21.259   9.040  -6.911  1.00 81.97           H  
HETATM 8737  H5  BMA D   3      20.648  11.771  -8.000  1.00 67.93           H  
HETATM 8738  H61 BMA D   3      23.244  10.412  -8.592  1.00 98.07           H  
HETATM 8739  H62 BMA D   3      22.894  10.376  -6.842  1.00 98.07           H  
HETATM 8740  HO2 BMA D   3      20.076   7.098  -9.949  1.00 48.69           H  
HETATM 8741  HO4 BMA D   3      19.454  10.020  -5.480  1.00 93.44           H  
HETATM 8742  HO6 BMA D   3      22.340  12.822  -7.933  1.00 71.26           H  
HETATM 8743  C1  MAN D   4      17.761   7.543  -6.694  1.00 45.20           C  
ANISOU 8743  C1  MAN D   4     5808   5269   6096    664   -107    579       C  
HETATM 8744  C2  MAN D   4      17.675   6.718  -5.401  1.00 73.83           C  
ANISOU 8744  C2  MAN D   4     9458   8874   9718    653   -140    634       C  
HETATM 8745  C3  MAN D   4      18.331   5.359  -5.617  1.00 54.08           C  
ANISOU 8745  C3  MAN D   4     6993   6307   7249    703   -158    632       C  
HETATM 8746  C4  MAN D   4      17.704   4.650  -6.837  1.00 42.97           C  
ANISOU 8746  C4  MAN D   4     5638   4820   5868    707   -145    591       C  
HETATM 8747  C5  MAN D   4      17.864   5.554  -8.064  1.00 40.35           C  
ANISOU 8747  C5  MAN D   4     5273   4522   5537    718   -110    536       C  
HETATM 8748  C6  MAN D   4      17.228   4.985  -9.320  1.00 46.45           C  
ANISOU 8748  C6  MAN D   4     6092   5225   6330    717    -94    491       C  
HETATM 8749  O2  MAN D   4      16.330   6.398  -5.093  1.00 42.74           O  
ANISOU 8749  O2  MAN D   4     5566   4898   5777    599   -143    657       O  
HETATM 8750  O3  MAN D   4      18.229   4.540  -4.465  1.00 69.17           O  
ANISOU 8750  O3  MAN D   4     8934   8193   9156    694   -190    684       O  
HETATM 8751  O4  MAN D   4      18.337   3.409  -7.082  1.00 58.11           O  
ANISOU 8751  O4  MAN D   4     7587   6674   7818    756   -164    584       O  
HETATM 8752  O5  MAN D   4      17.221   6.811  -7.780  1.00 37.53           O  
ANISOU 8752  O5  MAN D   4     4886   4225   5150    670    -96    544       O  
HETATM 8753  O6  MAN D   4      17.649   5.775 -10.437  1.00 72.44           O  
ANISOU 8753  O6  MAN D   4     9349   8556   9619    737    -64    440       O  
HETATM 8754  H2  MAN D   4      18.163   7.274  -4.590  1.00 88.59           H  
HETATM 8755  H3  MAN D   4      19.401   5.495  -5.806  1.00 64.90           H  
HETATM 8756  H4  MAN D   4      16.630   4.499  -6.636  1.00 51.56           H  
HETATM 8757  H5  MAN D   4      18.932   5.706  -8.267  1.00 48.42           H  
HETATM 8758  H61 MAN D   4      16.134   5.009  -9.198  1.00 55.74           H  
HETATM 8759  H62 MAN D   4      17.544   3.935  -9.425  1.00 55.74           H  
HETATM 8760  HO3 MAN D   4      18.434   5.124  -3.716  1.00 83.01           H  
HETATM 8761  HO4 MAN D   4      17.696   2.892  -7.595  1.00 69.73           H  
HETATM 8762  HO6 MAN D   4      18.574   6.014 -10.292  1.00 86.93           H  
HETATM 8763  C1  MAN D   5      15.706   7.425  -4.301  1.00 33.02           C  
ANISOU 8763  C1  MAN D   5     4304   3729   4512    548   -140    682       C  
HETATM 8764  C2  MAN D   5      14.405   6.796  -3.800  1.00 39.40           C  
ANISOU 8764  C2  MAN D   5     5160   4494   5315    492   -150    715       C  
HETATM 8765  C3  MAN D   5      13.523   6.494  -5.009  1.00 41.11           C  
ANISOU 8765  C3  MAN D   5     5416   4650   5554    477   -130    679       C  
HETATM 8766  C4  MAN D   5      13.243   7.789  -5.797  1.00 35.50           C  
ANISOU 8766  C4  MAN D   5     4669   3996   4824    457   -103    621       C  
HETATM 8767  C5  MAN D   5      14.564   8.477  -6.195  1.00 37.02           C  
ANISOU 8767  C5  MAN D   5     4813   4233   5020    514    -94    599       C  
HETATM 8768  C6  MAN D   5      14.332   9.884  -6.754  1.00 38.68           C  
ANISOU 8768  C6  MAN D   5     4985   4506   5206    487    -72    552       C  
HETATM 8769  O2  MAN D   5      13.681   7.723  -3.006  1.00 38.18           O  
ANISOU 8769  O2  MAN D   5     4978   4404   5125    436   -148    736       O  
HETATM 8770  O3  MAN D   5      12.317   5.863  -4.608  1.00 33.48           O  
ANISOU 8770  O3  MAN D   5     4493   3645   4581    418   -140    704       O  
HETATM 8771  O4  MAN D   5      12.485   7.509  -6.986  1.00 28.79           O  
ANISOU 8771  O4  MAN D   5     3854   3097   3988    441    -87    576       O  
HETATM 8772  O5  MAN D   5      15.435   8.615  -5.032  1.00 35.79           O  
ANISOU 8772  O5  MAN D   5     4623   4122   4853    535   -114    646       O  
HETATM 8773  O6  MAN D   5      15.555  10.375  -7.292  1.00 51.60           O  
ANISOU 8773  O6  MAN D   5     6582   6175   6848    537    -63    530       O  
HETATM 8774  H2  MAN D   5      14.609   5.879  -3.231  1.00 47.28           H  
HETATM 8775  H3  MAN D   5      14.025   5.795  -5.686  1.00 49.33           H  
HETATM 8776  H4  MAN D   5      12.693   8.466  -5.122  1.00 42.60           H  
HETATM 8777  H5  MAN D   5      15.071   7.855  -6.944  1.00 44.42           H  
HETATM 8778  H61 MAN D   5      13.967  10.525  -5.937  1.00 46.42           H  
HETATM 8779  H62 MAN D   5      13.550   9.824  -7.526  1.00 46.42           H  
HETATM 8780  HO3 MAN D   5      12.442   4.921  -4.808  1.00 40.17           H  
HETATM 8781  HO4 MAN D   5      11.602   7.873  -6.817  1.00 34.55           H  
HETATM 8782  HO6 MAN D   5      15.581  11.328  -7.133  1.00 61.92           H  
HETATM 8783  C1  MAN D   6      13.465   7.195  -1.680  1.00 66.38           C  
ANISOU 8783  C1  MAN D   6     8562   7982   8678    408   -173    793       C  
HETATM 8784  C2  MAN D   6      12.333   8.038  -1.034  1.00 67.00           C  
ANISOU 8784  C2  MAN D   6     8623   8119   8715    336   -167    799       C  
HETATM 8785  C3  MAN D   6      12.834   9.453  -0.710  1.00 60.55           C  
ANISOU 8785  C3  MAN D   6     7745   7393   7867    338   -158    778       C  
HETATM 8786  C4  MAN D   6      14.149   9.418   0.096  1.00 46.95           C  
ANISOU 8786  C4  MAN D   6     5993   5702   6142    382   -179    818       C  
HETATM 8787  C5  MAN D   6      15.191   8.562  -0.646  1.00 58.77           C  
ANISOU 8787  C5  MAN D   6     7507   7144   7679    446   -182    801       C  
HETATM 8788  C6  MAN D   6      16.469   8.379   0.161  1.00 65.04           C  
ANISOU 8788  C6  MAN D   6     8276   7972   8466    482   -203    823       C  
HETATM 8789  O2  MAN D   6      11.909   7.489   0.217  1.00 34.70           O  
ANISOU 8789  O2  MAN D   6     4547   4034   4603    300   -188    860       O  
HETATM 8790  O3  MAN D   6      11.845  10.204  -0.013  1.00 42.08           O  
ANISOU 8790  O3  MAN D   6     5392   5111   5487    276   -153    778       O  
HETATM 8791  O4  MAN D   6      14.657  10.750   0.256  1.00 54.90           O  
ANISOU 8791  O4  MAN D   6     6947   6789   7123    381   -171    792       O  
HETATM 8792  O5  MAN D   6      14.658   7.230  -0.914  1.00 39.14           O  
ANISOU 8792  O5  MAN D   6     5082   4571   5217    444   -190    812       O  
HETATM 8793  O6  MAN D   6      16.285   7.255   1.015  1.00 82.64           O  
ANISOU 8793  O6  MAN D   6    10544  10163  10693    472   -228    867       O  
HETATM 8794  H2  MAN D   6      11.494   8.089  -1.741  1.00 80.40           H  
HETATM 8795  H3  MAN D   6      13.037   9.980  -1.648  1.00 72.66           H  
HETATM 8796  H4  MAN D   6      13.948   8.945   1.072  1.00 56.34           H  
HETATM 8797  H5  MAN D   6      15.421   9.051  -1.601  1.00 70.53           H  
HETATM 8798  H61 MAN D   6      16.658   9.300   0.735  1.00 78.05           H  
HETATM 8799  H62 MAN D   6      17.307   8.226  -0.537  1.00 78.05           H  
HETATM 8800  HO2 MAN D   6      12.665   7.452   0.816  1.00 41.64           H  
HETATM 8801  HO3 MAN D   6      12.221  11.093   0.088  1.00 50.50           H  
HETATM 8802  HO4 MAN D   6      13.890  11.286   0.511  1.00 65.88           H  
HETATM 8803  HO6 MAN D   6      15.622   6.684   0.606  1.00 99.17           H  
HETATM 8804  C1  NAG E   1      19.846   2.015 -26.279  1.00 34.66           C  
ANISOU 8804  C1  NAG E   1     4693   3591   4883    987    214   -271       C  
HETATM 8805  C2  NAG E   1      20.542   1.319 -27.428  1.00 33.97           C  
ANISOU 8805  C2  NAG E   1     4608   3498   4803   1031    240   -333       C  
HETATM 8806  C3  NAG E   1      20.445  -0.193 -27.252  1.00 34.44           C  
ANISOU 8806  C3  NAG E   1     4721   3459   4906   1054    224   -340       C  
HETATM 8807  C4  NAG E   1      20.921  -0.613 -25.869  1.00 46.14           C  
ANISOU 8807  C4  NAG E   1     6191   4918   6423   1082    194   -280       C  
HETATM 8808  C5  NAG E   1      20.320   0.257 -24.767  1.00 36.55           C  
ANISOU 8808  C5  NAG E   1     4965   3728   5194   1036    172   -218       C  
HETATM 8809  C6  NAG E   1      20.995   0.048 -23.431  1.00 35.43           C  
ANISOU 8809  C6  NAG E   1     4796   3587   5077   1067    145   -160       C  
HETATM 8810  C7  NAG E   1      20.621   2.529 -29.566  1.00 33.98           C  
ANISOU 8810  C7  NAG E   1     4576   3600   4735   1010    297   -415       C  
HETATM 8811  C8  NAG E   1      19.898   2.830 -30.847  1.00 41.27           C  
ANISOU 8811  C8  NAG E   1     5526   4534   5623    971    318   -467       C  
HETATM 8812  N2  NAG E   1      19.983   1.722 -28.709  1.00 28.52           N  
ANISOU 8812  N2  NAG E   1     3932   2826   4077    999    265   -385       N  
HETATM 8813  O3  NAG E   1      21.248  -0.813 -28.252  1.00 46.78           O  
ANISOU 8813  O3  NAG E   1     6277   5021   6475   1104    251   -396       O  
HETATM 8814  O4  NAG E   1      20.468  -1.935 -25.591  1.00 38.21           O  
ANISOU 8814  O4  NAG E   1     5250   3811   5457   1084    174   -276       O  
HETATM 8815  O5  NAG E   1      20.456   1.649 -25.076  1.00 31.11           O  
ANISOU 8815  O5  NAG E   1     4226   3131   4464   1018    191   -222       O  
HETATM 8816  O6  NAG E   1      20.107   0.306 -22.353  1.00 43.46           O  
ANISOU 8816  O6  NAG E   1     5835   4586   6093   1018    117   -104       O  
HETATM 8817  O7  NAG E   1      21.729   2.996 -29.320  1.00 59.40           O  
ANISOU 8817  O7  NAG E   1     7734   6885   7952   1046    307   -400       O  
HETATM 8818  H2  NAG E   1      21.484   1.571 -27.414  1.00 40.77           H  
HETATM 8819  H3  NAG E   1      19.515  -0.471 -27.352  1.00 41.33           H  
HETATM 8820  H4  NAG E   1      21.894  -0.538 -25.867  1.00 55.37           H  
HETATM 8821  H5  NAG E   1      19.368   0.053 -24.698  1.00 43.86           H  
HETATM 8822  H61 NAG E   1      21.762   0.648 -23.363  1.00 42.51           H  
HETATM 8823  H62 NAG E   1      21.307  -0.875 -23.372  1.00 42.51           H  
HETATM 8824  H81 NAG E   1      19.487   2.014 -31.188  1.00 49.53           H  
HETATM 8825  H82 NAG E   1      20.532   3.175 -31.505  1.00 49.53           H  
HETATM 8826  H83 NAG E   1      19.206   3.498 -30.681  1.00 49.53           H  
HETATM 8827  HN2 NAG E   1      19.158   1.410 -28.940  1.00 34.22           H  
HETATM 8828  HO3 NAG E   1      21.207  -0.337 -29.001  1.00 56.13           H  
HETATM 8829  HO6 NAG E   1      19.410  -0.240 -22.407  1.00 52.16           H  
HETATM 8830  C1  NAG E   2      21.496  -2.908 -25.733  1.00 45.34           C  
ANISOU 8830  C1  NAG E   2     6147   4686   6394   1153    180   -294       C  
HETATM 8831  C2  NAG E   2      21.046  -4.154 -24.978  1.00 29.24           C  
ANISOU 8831  C2  NAG E   2     4168   2542   4398   1152    148   -263       C  
HETATM 8832  C3  NAG E   2      22.018  -5.308 -25.216  1.00 52.59           C  
ANISOU 8832  C3  NAG E   2     7131   5456   7396   1226    155   -287       C  
HETATM 8833  C4  NAG E   2      22.298  -5.506 -26.698  1.00 65.72           C  
ANISOU 8833  C4  NAG E   2     8798   7128   9046   1249    192   -367       C  
HETATM 8834  C5  NAG E   2      22.671  -4.182 -27.353  1.00 57.46           C  
ANISOU 8834  C5  NAG E   2     7689   6191   7951   1241    222   -390       C  
HETATM 8835  C6  NAG E   2      22.792  -4.281 -28.856  1.00 51.17           C  
ANISOU 8835  C6  NAG E   2     6899   5410   7134   1251    260   -468       C  
HETATM 8836  C7  NAG E   2      19.762  -3.863 -22.892  1.00 42.21           C  
ANISOU 8836  C7  NAG E   2     5839   4151   6046   1072     92   -150       C  
HETATM 8837  C8  NAG E   2      19.847  -3.572 -21.423  1.00 43.28           C  
ANISOU 8837  C8  NAG E   2     5952   4303   6188   1064     62    -75       C  
HETATM 8838  N2  NAG E   2      20.926  -3.883 -23.552  1.00 38.76           N  
ANISOU 8838  N2  NAG E   2     5361   3753   5612   1136    116   -189       N  
HETATM 8839  O3  NAG E   2      21.451  -6.499 -24.678  1.00 46.83           O  
ANISOU 8839  O3  NAG E   2     6468   4621   6705   1216    128   -264       O  
HETATM 8840  O4  NAG E   2      23.396  -6.402 -26.836  1.00 67.86           O  
ANISOU 8840  O4  NAG E   2     9059   7375   9350   1327    201   -386       O  
HETATM 8841  O5  NAG E   2      21.655  -3.208 -27.089  1.00 35.68           O  
ANISOU 8841  O5  NAG E   2     4935   3461   5161   1170    211   -365       O  
HETATM 8842  O6  NAG E   2      22.993  -3.002 -29.442  1.00 67.97           O  
ANISOU 8842  O6  NAG E   2     8974   7639   9214   1233    285   -483       O  
HETATM 8843  O7  NAG E   2      18.691  -4.069 -23.452  1.00 41.95           O  
ANISOU 8843  O7  NAG E   2     5858   4076   6004   1022     95   -174       O  
HETATM 8844  H2  NAG E   2      20.174  -4.418 -25.327  1.00 35.08           H  
HETATM 8845  H3  NAG E   2      22.861  -5.101 -24.769  1.00 63.11           H  
HETATM 8846  H4  NAG E   2      21.503  -5.863 -27.138  1.00 78.87           H  
HETATM 8847  H5  NAG E   2      23.518  -3.871 -26.981  1.00 68.95           H  
HETATM 8848  H61 NAG E   2      21.974  -4.673 -29.217  1.00 61.41           H  
HETATM 8849  H62 NAG E   2      23.547  -4.857 -29.078  1.00 61.41           H  
HETATM 8850  H81 NAG E   2      19.686  -2.622 -21.270  1.00 51.93           H  
HETATM 8851  H82 NAG E   2      20.735  -3.809 -21.095  1.00 51.93           H  
HETATM 8852  H83 NAG E   2      19.174  -4.097 -20.949  1.00 51.93           H  
HETATM 8853  HN2 NAG E   2      21.690  -3.717 -23.082  1.00 46.51           H  
HETATM 8854  HO3 NAG E   2      20.896  -6.857 -25.272  1.00 56.20           H  
HETATM 8855  HO6 NAG E   2      22.620  -2.984 -30.248  1.00 81.56           H  
HETATM 8856  C1  BMA E   3      23.126  -7.453 -27.783  1.00 98.78           C  
ANISOU 8856  C1  BMA E   3    13034  11216  13282   1338    215   -445       C  
HETATM 8857  C2  BMA E   3      24.449  -7.702 -28.548  1.00108.47           C  
ANISOU 8857  C2  BMA E   3    14219  12481  14514   1417    249   -493       C  
HETATM 8858  C3  BMA E   3      24.332  -8.934 -29.438  1.00 82.49           C  
ANISOU 8858  C3  BMA E   3    10989   9106  11246   1442    263   -554       C  
HETATM 8859  C4  BMA E   3      23.774 -10.125 -28.656  1.00 66.98           C  
ANISOU 8859  C4  BMA E   3     9096   7025   9330   1437    228   -521       C  
HETATM 8860  C5  BMA E   3      22.434  -9.750 -28.001  1.00108.06           C  
ANISOU 8860  C5  BMA E   3    14335  12203  14520   1348    197   -474       C  
HETATM 8861  C6  BMA E   3      21.837 -10.896 -27.180  1.00 82.17           C  
ANISOU 8861  C6  BMA E   3    11125   8811  11285   1334    162   -434       C  
HETATM 8862  O2  BMA E   3      25.513  -7.954 -27.639  1.00 87.88           O  
ANISOU 8862  O2  BMA E   3    11571   9884  11937   1480    235   -450       O  
HETATM 8863  O3  BMA E   3      25.583  -9.281 -30.032  1.00 75.67           O  
ANISOU 8863  O3  BMA E   3    10089   8270  10391   1522    293   -595       O  
HETATM 8864  O4  BMA E   3      23.581 -11.214 -29.536  1.00 80.47           O  
ANISOU 8864  O4  BMA E   3    10865   8654  11056   1452    241   -581       O  
HETATM 8865  O5  BMA E   3      22.654  -8.629 -27.126  1.00108.10           O  
ANISOU 8865  O5  BMA E   3    14278  12288  14506   1335    186   -417       O  
HETATM 8866  O6  BMA E   3      22.418 -10.882 -25.882  1.00 72.82           O  
ANISOU 8866  O6  BMA E   3     9908   7633  10125   1364    136   -363       O  
HETATM 8867  H2  BMA E   3      24.664  -6.818 -29.169  1.00130.17           H  
HETATM 8868  H3  BMA E   3      23.653  -8.723 -30.274  1.00 98.98           H  
HETATM 8869  H4  BMA E   3      24.481 -10.370 -27.847  1.00 80.38           H  
HETATM 8870  H5  BMA E   3      21.708  -9.469 -28.782  1.00129.67           H  
HETATM 8871  H61 BMA E   3      22.046 -11.841 -27.706  1.00 98.60           H  
HETATM 8872  H62 BMA E   3      20.746 -10.757 -27.137  1.00 98.60           H  
HETATM 8873  HO2 BMA E   3      25.103  -8.334 -26.846  1.00105.46           H  
HETATM 8874  HO3 BMA E   3      25.600  -8.818 -30.886  1.00 90.80           H  
HETATM 8875  HO4 BMA E   3      23.618 -10.834 -30.427  1.00 96.57           H  
HETATM 8876  HO6 BMA E   3      21.976 -11.559 -25.355  1.00 87.38           H  
HETATM 8877  C1  NAG F   1       8.636   9.215 -35.387  1.00 19.47           C  
ANISOU 8877  C1  NAG F   1     2919   1924   2555    320    260   -493       C  
HETATM 8878  C2  NAG F   1       7.791   9.333 -36.669  1.00 21.66           C  
ANISOU 8878  C2  NAG F   1     3217   2221   2792    268    260   -530       C  
HETATM 8879  C3  NAG F   1       8.293   8.360 -37.734  1.00 23.87           C  
ANISOU 8879  C3  NAG F   1     3535   2473   3060    297    282   -596       C  
HETATM 8880  C4  NAG F   1       9.789   8.544 -37.953  1.00 20.71           C  
ANISOU 8880  C4  NAG F   1     3101   2110   2658    365    312   -611       C  
HETATM 8881  C5  NAG F   1      10.511   8.431 -36.611  1.00 20.91           C  
ANISOU 8881  C5  NAG F   1     3106   2112   2728    413    308   -569       C  
HETATM 8882  C6  NAG F   1      12.007   8.629 -36.701  1.00 21.38           C  
ANISOU 8882  C6  NAG F   1     3124   2214   2787    480    336   -578       C  
HETATM 8883  C7  NAG F   1       5.487  10.106 -36.314  1.00 25.55           C  
ANISOU 8883  C7  NAG F   1     3710   2731   3268    158    214   -484       C  
HETATM 8884  C8  NAG F   1       4.075   9.697 -36.023  1.00 31.10           C  
ANISOU 8884  C8  NAG F   1     4440   3403   3976     99    188   -473       C  
HETATM 8885  N2  NAG F   1       6.380   9.114 -36.397  1.00 22.75           N  
ANISOU 8885  N2  NAG F   1     3382   2329   2932    207    232   -516       N  
HETATM 8886  O3  NAG F   1       7.558   8.595 -38.928  1.00 24.55           O  
ANISOU 8886  O3  NAG F   1     3635   2591   3104    247    281   -629       O  
HETATM 8887  O4  NAG F   1      10.305   7.537 -38.815  1.00 23.82           O  
ANISOU 8887  O4  NAG F   1     3532   2473   3046    402    334   -675       O  
HETATM 8888  O5  NAG F   1      10.001   9.413 -35.700  1.00 18.16           O  
ANISOU 8888  O5  NAG F   1     2723   1793   2384    377    287   -508       O  
HETATM 8889  O6  NAG F   1      12.355   9.853 -37.331  1.00 22.59           O  
ANISOU 8889  O6  NAG F   1     3228   2456   2900    463    349   -572       O  
HETATM 8890  O7  NAG F   1       5.801  11.280 -36.486  1.00 27.16           O  
ANISOU 8890  O7  NAG F   1     3868   2999   3452    160    219   -466       O  
HETATM 8891  H2  NAG F   1       7.900  10.239 -37.016  1.00 25.99           H  
HETATM 8892  H3  NAG F   1       8.148   7.438 -37.450  1.00 28.64           H  
HETATM 8893  H4  NAG F   1       9.940   9.418 -38.359  1.00 24.85           H  
HETATM 8894  H5  NAG F   1      10.347   7.543 -36.241  1.00 25.09           H  
HETATM 8895  H61 NAG F   1      12.392   7.891 -37.212  1.00 25.66           H  
HETATM 8896  H62 NAG F   1      12.380   8.622 -35.799  1.00 25.66           H  
HETATM 8897  H81 NAG F   1       3.497  10.483 -36.047  1.00 37.33           H  
HETATM 8898  H82 NAG F   1       4.032   9.288 -35.138  1.00 37.33           H  
HETATM 8899  H83 NAG F   1       3.778   9.054 -36.694  1.00 37.33           H  
HETATM 8900  HN2 NAG F   1       6.089   8.258 -36.278  1.00 27.29           H  
HETATM 8901  HO3 NAG F   1       6.762   8.206 -38.867  1.00 29.47           H  
HETATM 8902  HO6 NAG F   1      11.656  10.161 -37.785  1.00 27.11           H  
HETATM 8903  C1  NAG F   2      10.520   8.054 -40.140  1.00 26.27           C  
ANISOU 8903  C1  NAG F   2     3826   2850   3306    389    355   -713       C  
HETATM 8904  C2  NAG F   2      11.566   7.174 -40.834  1.00 25.38           C  
ANISOU 8904  C2  NAG F   2     3730   2723   3190    454    387   -776       C  
HETATM 8905  C3  NAG F   2      11.750   7.601 -42.293  1.00 40.53           C  
ANISOU 8905  C3  NAG F   2     5637   4712   5049    438    411   -822       C  
HETATM 8906  C4  NAG F   2      10.413   7.705 -43.011  1.00 47.63           C  
ANISOU 8906  C4  NAG F   2     6570   5611   5917    360    391   -834       C  
HETATM 8907  C5  NAG F   2       9.482   8.610 -42.215  1.00 32.35           C  
ANISOU 8907  C5  NAG F   2     4612   3688   3991    305    358   -766       C  
HETATM 8908  C6  NAG F   2       8.113   8.777 -42.830  1.00 34.08           C  
ANISOU 8908  C6  NAG F   2     4857   3913   4180    228    335   -771       C  
HETATM 8909  C7  NAG F   2      13.435   6.192 -39.549  1.00 31.26           C  
ANISOU 8909  C7  NAG F   2     4450   3421   4005    583    403   -765       C  
HETATM 8910  C8  NAG F   2      14.755   6.470 -38.894  1.00 30.84           C  
ANISOU 8910  C8  NAG F   2     4338   3407   3974    645    416   -737       C  
HETATM 8911  N2  NAG F   2      12.841   7.240 -40.131  1.00 28.80           N  
ANISOU 8911  N2  NAG F   2     4123   3171   3650    525    403   -756       N  
HETATM 8912  O3  NAG F   2      12.590   6.656 -42.947  1.00 40.99           O  
ANISOU 8912  O3  NAG F   2     5714   4756   5106    496    438   -885       O  
HETATM 8913  O4  NAG F   2      10.592   8.288 -44.296  1.00 47.22           O  
ANISOU 8913  O4  NAG F   2     6500   5636   5807    340    410   -866       O  
HETATM 8914  O5  NAG F   2       9.306   8.060 -40.903  1.00 27.06           O  
ANISOU 8914  O5  NAG F   2     3958   2949   3376    321    340   -732       O  
HETATM 8915  O6  NAG F   2       7.582   7.552 -43.314  1.00 31.63           O  
ANISOU 8915  O6  NAG F   2     4610   3538   3870    215    332   -823       O  
HETATM 8916  O7  NAG F   2      12.935   5.072 -39.555  1.00 32.51           O  
ANISOU 8916  O7  NAG F   2     4656   3506   4188    575    386   -786       O  
HETATM 8917  H2  NAG F   2      11.240   6.254 -40.828  1.00 30.46           H  
HETATM 8918  H3  NAG F   2      12.171   8.482 -42.313  1.00 48.63           H  
HETATM 8919  H4  NAG F   2      10.029   6.812 -43.105  1.00 57.16           H  
HETATM 8920  H5  NAG F   2       9.883   9.497 -42.141  1.00 38.82           H  
HETATM 8921  H61 NAG F   2       8.177   9.407 -43.573  1.00 40.90           H  
HETATM 8922  H62 NAG F   2       7.507   9.138 -42.156  1.00 40.90           H  
HETATM 8923  H81 NAG F   2      14.829   5.944 -38.075  1.00 37.01           H  
HETATM 8924  H82 NAG F   2      14.817   7.419 -38.678  1.00 37.01           H  
HETATM 8925  H83 NAG F   2      15.478   6.226 -39.503  1.00 37.01           H  
HETATM 8926  HN2 NAG F   2      13.260   8.048 -40.084  1.00 34.56           H  
HETATM 8927  HO3 NAG F   2      12.397   5.839 -42.659  1.00 49.19           H  
HETATM 8928  HO6 NAG F   2       7.425   7.007 -42.630  1.00 37.95           H  
HETATM 8929  C1  BMA F   3      10.392   7.294 -45.313  1.00 64.69           C  
ANISOU 8929  C1  BMA F   3     8766   7818   7996    338    422   -938       C  
HETATM 8930  C2  BMA F   3       9.980   8.024 -46.604  1.00 67.92           C  
ANISOU 8930  C2  BMA F   3     9164   8306   8339    283    426   -957       C  
HETATM 8931  C3  BMA F   3       9.862   7.033 -47.764  1.00 95.76           C  
ANISOU 8931  C3  BMA F   3    12732  11817  11834    284    429  -1024       C  
HETATM 8932  C4  BMA F   3      11.095   6.131 -47.860  1.00 72.95           C  
ANISOU 8932  C4  BMA F   3     9844   8912   8962    370    448  -1060       C  
HETATM 8933  C5  BMA F   3      11.440   5.519 -46.486  1.00 87.06           C  
ANISOU 8933  C5  BMA F   3    11632  10624  10824    418    438  -1037       C  
HETATM 8934  C6  BMA F   3      12.744   4.726 -46.520  1.00 60.58           C  
ANISOU 8934  C6  BMA F   3     8256   7266   7495    502    457  -1075       C  
HETATM 8935  O2  BMA F   3      10.977   8.964 -46.943  1.00 52.68           O  
ANISOU 8935  O2  BMA F   3     7174   6463   6379    306    451   -944       O  
HETATM 8936  O3  BMA F   3       9.637   7.683 -49.023  1.00 58.24           O  
ANISOU 8936  O3  BMA F   3     7969   7144   7016    240    436  -1041       O  
HETATM 8937  O4  BMA F   3      10.837   5.088 -48.793  1.00101.76           O  
ANISOU 8937  O4  BMA F   3    13539  12532  12592    370    439  -1118       O  
HETATM 8938  O5  BMA F   3      11.580   6.571 -45.512  1.00 46.45           O  
ANISOU 8938  O5  BMA F   3     6448   5503   5696    414    444   -976       O  
HETATM 8939  O6  BMA F   3      13.803   5.616 -46.860  1.00 82.27           O  
ANISOU 8939  O6  BMA F   3    10955  10103  10201    536    488  -1056       O  
HETATM 8940  H2  BMA F   3       9.005   8.515 -46.460  1.00 81.51           H  
HETATM 8941  H3  BMA F   3       8.981   6.398 -47.598  1.00114.91           H  
HETATM 8942  H4  BMA F   3      11.953   6.756 -48.155  1.00 87.54           H  
HETATM 8943  H5  BMA F   3      10.618   4.854 -46.172  1.00104.48           H  
HETATM 8944  H61 BMA F   3      12.640   3.918 -47.260  1.00 72.70           H  
HETATM 8945  H62 BMA F   3      12.899   4.271 -45.529  1.00 72.70           H  
HETATM 8946  HO2 BMA F   3      11.251   8.749 -47.849  1.00 63.22           H  
HETATM 8947  HO3 BMA F   3       8.684   7.601 -49.189  1.00 69.89           H  
HETATM 8948  HO4 BMA F   3      10.343   5.506 -49.515  1.00122.11           H  
HETATM 8949  HO6 BMA F   3      13.644   6.450 -46.400  1.00 98.73           H  
HETATM 8950 CU    CU A 601       4.766  35.522 -28.285  1.00 15.50          CU  
ANISOU 8950 CU    CU A 601     2161   1929   1801    -24   -112    131      CU  
HETATM 8951 CU    CU A 602      10.088  32.381 -15.088  1.00 19.28          CU  
ANISOU 8951 CU    CU A 602     2274   2476   2576    122   -192    -28      CU  
HETATM 8952 CU    CU A 603      10.964  35.212 -17.710  1.00 19.56          CU  
ANISOU 8952 CU    CU A 603     2409   3171   1853   -156      6    203      CU  
HETATM 8953 CU    CU A 604      11.553  30.664 -18.366  1.00 20.88          CU  
ANISOU 8953 CU    CU A 604     2223   3641   2071   -245    -81    155      CU  
HETATM 8954 CA    CA A 605      25.861  47.013   4.146  1.00 17.87          CA  
ANISOU 8954 CA    CA A 605     2296   2440   2053    323   -265    367      CA  
HETATM 8955 CA    CA A 606      -1.015  46.147 -35.561  0.58 20.01          CA  
ANISOU 8955 CA    CA A 606     2967   2515   2122     79   -820    -29      CA  
HETATM 8956  C1  NAG A 626      -2.502  51.041 -19.846  1.00 20.09           C  
ANISOU 8956  C1  NAG A 626     2934   2097   2603    453   -390    -84       C  
HETATM 8957  C2  NAG A 626      -2.546  51.025 -18.328  1.00 19.29           C  
ANISOU 8957  C2  NAG A 626     2820   2010   2499    473   -373   -125       C  
HETATM 8958  C3  NAG A 626      -3.238  52.283 -17.811  1.00 41.88           C  
ANISOU 8958  C3  NAG A 626     5717   4825   5370    530   -400   -157       C  
HETATM 8959  C4  NAG A 626      -2.555  53.526 -18.367  1.00 47.87           C  
ANISOU 8959  C4  NAG A 626     6548   5505   6136    511   -436   -140       C  
HETATM 8960  C5  NAG A 626      -2.453  53.461 -19.889  1.00 66.29           C  
ANISOU 8960  C5  NAG A 626     8890   7826   8470    486   -452    -92       C  
HETATM 8961  C6  NAG A 626      -1.620  54.584 -20.467  1.00 45.41           C  
ANISOU 8961  C6  NAG A 626     6316   5108   5830    451   -485    -68       C  
HETATM 8962  C7  NAG A 626      -2.573  48.887 -17.123  1.00 28.02           C  
ANISOU 8962  C7  NAG A 626     3832   3225   3588    454   -312   -141       C  
HETATM 8963  C8  NAG A 626      -3.399  47.707 -16.698  1.00 24.57           C  
ANISOU 8963  C8  NAG A 626     3336   2855   3145    469   -284   -151       C  
HETATM 8964  N2  NAG A 626      -3.208  49.826 -17.836  1.00 21.21           N  
ANISOU 8964  N2  NAG A 626     2999   2323   2735    487   -342   -138       N  
HETATM 8965  O3  NAG A 626      -3.179  52.310 -16.389  1.00 33.51           O  
ANISOU 8965  O3  NAG A 626     4649   3780   4303    544   -384   -198       O  
HETATM 8966  O4  NAG A 626      -3.281  54.699 -18.013  1.00 45.36           O  
ANISOU 8966  O4  NAG A 626     6266   5138   5829    569   -463   -169       O  
HETATM 8967  O5  NAG A 626      -1.828  52.235 -20.296  1.00 29.75           O  
ANISOU 8967  O5  NAG A 626     4221   3251   3830    434   -422    -68       O  
HETATM 8968  O6  NAG A 626      -1.444  54.439 -21.870  1.00 44.72           O  
ANISOU 8968  O6  NAG A 626     6234   5020   5738    420   -496    -21       O  
HETATM 8969  O7  NAG A 626      -1.387  48.990 -16.824  1.00 37.75           O  
ANISOU 8969  O7  NAG A 626     5086   4442   4816    411   -309   -134       O  
HETATM 8970  H2  NAG A 626      -1.630  51.027 -17.990  1.00 23.15           H  
HETATM 8971  H3  NAG A 626      -4.171  52.266 -18.096  1.00 50.25           H  
HETATM 8972  H4  NAG A 626      -1.658  53.572 -17.984  1.00 57.44           H  
HETATM 8973  H5  NAG A 626      -3.352  53.492 -20.266  1.00 79.54           H  
HETATM 8974  H61 NAG A 626      -0.744  54.585 -20.035  1.00 54.49           H  
HETATM 8975  H62 NAG A 626      -2.065  55.434 -20.289  1.00 54.49           H  
HETATM 8976  H81 NAG A 626      -2.809  46.983 -16.411  1.00 29.48           H  
HETATM 8977  H82 NAG A 626      -3.944  47.404 -17.448  1.00 29.48           H  
HETATM 8978  H83 NAG A 626      -3.979  47.966 -15.957  1.00 29.48           H  
HETATM 8979  HN2 NAG A 626      -4.093  49.708 -18.022  1.00 25.45           H  
HETATM 8980  HO3 NAG A 626      -3.881  51.879 -16.056  1.00 40.21           H  
HETATM 8981  HO4 NAG A 626      -2.748  55.256 -17.573  1.00 54.43           H  
HETATM 8982  HO6 NAG A 626      -0.601  54.216 -22.041  1.00 53.67           H  
HETATM 8983  C1  NAG A 627      14.804  58.639 -10.628  1.00 39.56           C  
ANISOU 8983  C1  NAG A 627     5780   4366   4885   -380   -532   -126       C  
HETATM 8984  C2  NAG A 627      16.120  59.412 -10.511  1.00 86.13           C  
ANISOU 8984  C2  NAG A 627    11709  10255  10763   -476   -558   -110       C  
HETATM 8985  C3  NAG A 627      16.302  60.347 -11.704  1.00 41.32           C  
ANISOU 8985  C3  NAG A 627     6092   4511   5095   -518   -588    -76       C  
HETATM 8986  C4  NAG A 627      16.159  59.578 -13.012  1.00 44.43           C  
ANISOU 8986  C4  NAG A 627     6443   4938   5500   -503   -566    -30       C  
HETATM 8987  C5  NAG A 627      14.820  58.848 -13.028  1.00 70.27           C  
ANISOU 8987  C5  NAG A 627     9689   8218   8794   -404   -542    -51       C  
HETATM 8988  C6  NAG A 627      14.598  58.009 -14.265  1.00 36.57           C  
ANISOU 8988  C6  NAG A 627     5377   3984   4534   -386   -520    -12       C  
HETATM 8989  C7  NAG A 627      17.089  59.958  -8.321  1.00 47.00           C  
ANISOU 8989  C7  NAG A 627     6767   5322   5768   -535   -576   -166       C  
HETATM 8990  C8  NAG A 627      16.977  60.816  -7.097  1.00 55.77           C  
ANISOU 8990  C8  NAG A 627     7933   6393   6866   -540   -599   -222       C  
HETATM 8991  N2  NAG A 627      16.162  60.158  -9.263  1.00 42.16           N  
ANISOU 8991  N2  NAG A 627     6182   4655   5180   -486   -578   -158       N  
HETATM 8992  O3  NAG A 627      17.587  60.954 -11.636  1.00 72.95           O  
ANISOU 8992  O3  NAG A 627    10118   8521   9080   -616   -609    -56       O  
HETATM 8993  O4  NAG A 627      16.254  60.469 -14.117  1.00 60.57           O  
ANISOU 8993  O4  NAG A 627     8544   6920   7549   -540   -594      2       O  
HETATM 8994  O5  NAG A 627      14.747  57.964 -11.899  1.00 70.11           O  
ANISOU 8994  O5  NAG A 627     9614   8260   8765   -373   -515    -81       O  
HETATM 8995  O6  NAG A 627      15.537  56.948 -14.371  1.00 39.34           O  
ANISOU 8995  O6  NAG A 627     5654   4423   4869   -419   -490     16       O  
HETATM 8996  O7  NAG A 627      17.981  59.125  -8.452  1.00 54.63           O  
ANISOU 8996  O7  NAG A 627     7668   6369   6721   -571   -557   -131       O  
HETATM 8997  H2  NAG A 627      16.856  58.771 -10.524  1.00103.36           H  
HETATM 8998  H3  NAG A 627      15.617  61.042 -11.670  1.00 49.58           H  
HETATM 8999  H4  NAG A 627      16.877  58.921 -13.093  1.00 53.31           H  
HETATM 9000  H5  NAG A 627      14.100  59.505 -12.971  1.00 84.33           H  
HETATM 9001  H61 NAG A 627      14.679  58.581 -15.052  1.00 43.89           H  
HETATM 9002  H62 NAG A 627      13.699  57.633 -14.235  1.00 43.89           H  
HETATM 9003  H81 NAG A 627      17.366  60.347  -6.334  1.00 66.93           H  
HETATM 9004  H82 NAG A 627      16.036  61.005  -6.917  1.00 66.93           H  
HETATM 9005  H83 NAG A 627      17.455  61.654  -7.242  1.00 66.93           H  
HETATM 9006  HN2 NAG A 627      15.526  60.795  -9.117  1.00 50.59           H  
HETATM 9007  HO3 NAG A 627      17.984  60.898 -12.428  1.00 87.54           H  
HETATM 9008  HO4 NAG A 627      17.086  60.466 -14.429  1.00 72.68           H  
HETATM 9009  HO6 NAG A 627      16.294  57.182 -13.972  1.00 47.20           H  
HETATM 9010  O1  2PE A 628      28.369  51.148 -28.890  1.00 53.88           O  
ANISOU 9010  O1  2PE A 628     6843   7256   6372  -1028   -196    511       O  
HETATM 9011  C2  2PE A 628      28.632  49.804 -28.592  1.00 51.61           C  
ANISOU 9011  C2  2PE A 628     6482   7032   6095   -960   -157    484       C  
HETATM 9012  C3  2PE A 628      29.011  49.665 -27.117  1.00 48.89           C  
ANISOU 9012  C3  2PE A 628     6116   6690   5770   -946   -166    466       C  
HETATM 9013  O4  2PE A 628      28.023  50.252 -26.317  1.00 47.08           O  
ANISOU 9013  O4  2PE A 628     5956   6362   5571   -925   -199    450       O  
HETATM 9014  C5  2PE A 628      27.799  49.610 -25.093  1.00 46.84           C  
ANISOU 9014  C5  2PE A 628     5906   6323   5569   -865   -195    419       C  
HETATM 9015  C6  2PE A 628      28.277  50.511 -23.955  1.00 48.62           C  
ANISOU 9015  C6  2PE A 628     6152   6528   5792   -918   -228    422       C  
HETATM 9016  O7  2PE A 628      27.886  51.827 -24.223  1.00 52.79           O  
ANISOU 9016  O7  2PE A 628     6760   6983   6316   -973   -265    437       O  
HETATM 9017  C8  2PE A 628      27.380  52.523 -23.120  1.00 51.45           C  
ANISOU 9017  C8  2PE A 628     6645   6739   6166   -971   -299    417       C  
HETATM 9018  C9  2PE A 628      27.458  54.025 -23.392  1.00 55.56           C  
ANISOU 9018  C9  2PE A 628     7239   7199   6672  -1054   -340    441       C  
HETATM 9019  O10 2PE A 628      26.612  54.349 -24.459  1.00 60.70           O  
ANISOU 9019  O10 2PE A 628     7940   7796   7328  -1043   -347    454       O  
HETATM 9020  HO1 2PE A 628      27.789  51.193 -29.510  1.00 64.66           H  
HETATM 9021  H21 2PE A 628      27.840  49.274 -28.772  1.00 61.93           H  
HETATM 9022  H22 2PE A 628      29.364  49.489 -29.144  1.00 61.93           H  
HETATM 9023  H31 2PE A 628      29.091  48.724 -26.893  1.00 58.67           H  
HETATM 9024  H32 2PE A 628      29.860  50.108 -26.959  1.00 58.67           H  
HETATM 9025  H51 2PE A 628      26.851  49.433 -24.990  1.00 56.21           H  
HETATM 9026  H52 2PE A 628      28.288  48.773 -25.072  1.00 56.21           H  
HETATM 9027  H61 2PE A 628      29.243  50.465 -23.889  1.00 58.34           H  
HETATM 9028  H62 2PE A 628      27.881  50.218 -23.120  1.00 58.34           H  
HETATM 9029  H81 2PE A 628      27.904  52.308 -22.333  1.00 61.74           H  
HETATM 9030  H82 2PE A 628      26.455  52.268 -22.973  1.00 61.74           H  
HETATM 9031  H91 2PE A 628      28.370  54.265 -23.618  1.00 66.67           H  
HETATM 9032  H92 2PE A 628      27.182  54.512 -22.600  1.00 66.67           H  
HETATM 9033  O    OH A 629      11.444  33.242 -18.423  1.00 34.80           O  
ANISOU 9033  O    OH A 629     4361   4432   4430    118     -7     90       O  
HETATM 9034  O   HOH A 701      23.553  45.657   8.326  0.63 23.15           O  
HETATM 9035  O   HOH A 702      24.609  24.634 -21.099  1.00 34.45           O  
HETATM 9036  O   HOH A 703      23.763  48.031   4.436  1.00 33.16           O  
HETATM 9037  O   HOH A 704      25.858  34.067  -0.055  1.00 48.87           O  
HETATM 9038  O   HOH A 705      22.341  44.667   9.117  0.37 15.72           O  
HETATM 9039  O   HOH A 706      12.080  11.697  -8.077  1.00 40.28           O  
HETATM 9040  O   HOH A 707      21.366   6.517 -32.461  1.00 26.69           O  
HETATM 9041  O   HOH A 708      16.661  53.790  -9.964  1.00 36.70           O  
HETATM 9042  O   HOH A 709      33.733  25.252 -22.353  1.00 29.40           O  
HETATM 9043  O   HOH A 710       8.437  51.600  -2.639  1.00 52.34           O  
HETATM 9044  O   HOH A 711      16.720  55.881  -7.847  1.00 44.81           O  
HETATM 9045  O   HOH A 712       0.564  26.275  -6.902  1.00 15.44           O  
HETATM 9046  O   HOH A 713      22.002  47.313   2.677  1.00 24.95           O  
HETATM 9047  O   HOH A 714      33.696  51.992 -16.717  1.00 38.99           O  
HETATM 9048  O   HOH A 715      16.074  10.674  -9.730  1.00 23.47           O  
HETATM 9049  O   HOH A 716      -4.070  25.974   2.855  1.00 40.80           O  
HETATM 9050  O   HOH A 717       3.540  52.996 -34.215  1.00 48.93           O  
HETATM 9051  O   HOH A 718      34.240  42.211 -22.479  1.00 35.32           O  
HETATM 9052  O   HOH A 719      22.099  38.156  -1.864  1.00 30.18           O  
HETATM 9053  O   HOH A 720      11.205  31.456  -0.045  1.00 34.12           O  
HETATM 9054  O   HOH A 721      20.112  40.152 -29.379  1.00 32.11           O  
HETATM 9055  O   HOH A 722     -15.719  29.811 -34.659  1.00 46.16           O  
HETATM 9056  O   HOH A 723       2.821  -2.244 -28.820  1.00 52.60           O  
HETATM 9057  O   HOH A 724      17.778  38.493  -9.235  1.00 14.72           O  
HETATM 9058  O   HOH A 725      30.881  37.798 -31.650  1.00 43.09           O  
HETATM 9059  O   HOH A 726      22.289   5.070 -27.957  1.00 39.28           O  
HETATM 9060  O   HOH A 727       4.247  53.615 -41.238  1.00 48.73           O  
HETATM 9061  O   HOH A 728      -3.319  14.113 -36.906  1.00 38.05           O  
HETATM 9062  O   HOH A 729      24.582  35.229 -30.004  1.00 22.98           O  
HETATM 9063  O   HOH A 730      19.781  26.859 -41.185  1.00 39.64           O  
HETATM 9064  O   HOH A 731      10.944   9.633  -7.462  1.00 24.38           O  
HETATM 9065  O   HOH A 732      34.530  22.047 -34.219  1.00 40.13           O  
HETATM 9066  O   HOH A 733      16.810  14.529  -3.925  1.00 42.68           O  
HETATM 9067  O   HOH A 734      15.980  53.232 -16.063  1.00 28.90           O  
HETATM 9068  O   HOH A 735      10.047  27.189  -4.191  1.00 28.03           O  
HETATM 9069  O   HOH A 736      25.245  20.549 -34.391  1.00 23.42           O  
HETATM 9070  O   HOH A 737       0.331  18.004   5.582  1.00 25.78           O  
HETATM 9071  O   HOH A 738       2.052  18.776  -1.126  1.00 17.87           O  
HETATM 9072  O   HOH A 739       9.374  50.872 -25.488  1.00 25.77           O  
HETATM 9073  O   HOH A 740      30.207  30.761  -3.813  1.00 26.01           O  
HETATM 9074  O   HOH A 741       4.470  25.927 -11.602  1.00 18.29           O  
HETATM 9075  O   HOH A 742      19.675  28.699 -37.903  1.00 21.84           O  
HETATM 9076  O   HOH A 743      -8.761  28.314 -26.899  1.00 20.42           O  
HETATM 9077  O   HOH A 744      23.874  43.175 -28.957  1.00 32.96           O  
HETATM 9078  O   HOH A 745      10.869   3.676 -40.271  1.00 38.69           O  
HETATM 9079  O   HOH A 746      24.400  13.165 -31.070  1.00 38.82           O  
HETATM 9080  O   HOH A 747       9.236   0.184 -40.710  1.00 48.30           O  
HETATM 9081  O   HOH A 748      -8.620  29.905  -2.900  1.00 27.61           O  
HETATM 9082  O   HOH A 749      -0.588  24.930   7.866  1.00 31.86           O  
HETATM 9083  O   HOH A 750      19.227  42.815 -33.300  1.00 29.05           O  
HETATM 9084  O   HOH A 751      -9.846  30.881 -29.458  1.00 18.59           O  
HETATM 9085  O   HOH A 752      -2.255  28.548   0.070  1.00 31.84           O  
HETATM 9086  O   HOH A 753      -0.233   6.026 -19.197  1.00 35.27           O  
HETATM 9087  O   HOH A 754      15.801   7.841 -10.454  1.00 27.08           O  
HETATM 9088  O   HOH A 755      24.187   3.879 -29.119  1.00 49.72           O  
HETATM 9089  O   HOH A 756     -10.102  16.930 -15.730  1.00 22.57           O  
HETATM 9090  O   HOH A 757       8.622   0.095 -32.935  1.00 33.57           O  
HETATM 9091  O   HOH A 758      18.292   6.733 -38.337  1.00 39.58           O  
HETATM 9092  O   HOH A 759      22.858  40.195 -26.760  1.00 21.95           O  
HETATM 9093  O   HOH A 760      -4.686  43.538  -9.743  1.00 22.24           O  
HETATM 9094  O   HOH A 761      17.389  24.952 -25.095  1.00 20.68           O  
HETATM 9095  O   HOH A 762       0.208   1.443  -4.828  1.00 39.26           O  
HETATM 9096  O   HOH A 763      35.485  34.652 -11.050  1.00 30.10           O  
HETATM 9097  O   HOH A 764      20.465  37.641 -38.646  1.00 27.82           O  
HETATM 9098  O   HOH A 765      -7.122  18.856 -30.745  1.00 38.52           O  
HETATM 9099  O   HOH A 766      -1.934  30.500  -5.387  1.00 24.86           O  
HETATM 9100  O   HOH A 767      -0.767  20.593 -22.820  1.00 12.48           O  
HETATM 9101  O   HOH A 768      29.578  41.735  -7.357  1.00 39.41           O  
HETATM 9102  O   HOH A 769     -12.997  42.414 -24.796  1.00 32.15           O  
HETATM 9103  O   HOH A 770      31.067  26.150 -19.392  1.00 25.08           O  
HETATM 9104  O   HOH A 771       0.922  44.950   3.483  1.00 43.74           O  
HETATM 9105  O   HOH A 772      16.705  42.551 -39.367  1.00 33.51           O  
HETATM 9106  O   HOH A 773      -7.114  31.738 -36.318  1.00 27.44           O  
HETATM 9107  O   HOH A 774     -12.762  27.874 -23.695  1.00 33.69           O  
HETATM 9108  O   HOH A 775      26.600  28.676 -37.004  1.00 26.63           O  
HETATM 9109  O   HOH A 776      24.359  29.660 -30.751  1.00 20.84           O  
HETATM 9110  O   HOH A 777      -4.448  23.703 -36.083  1.00 24.14           O  
HETATM 9111  O   HOH A 778      25.782  16.344 -39.840  1.00 30.38           O  
HETATM 9112  O   HOH A 779       6.233  31.854 -33.210  1.00 17.95           O  
HETATM 9113  O   HOH A 780      14.736  37.137 -25.414  1.00 17.53           O  
HETATM 9114  O   HOH A 781      25.701  46.273   6.423  1.00 16.00           O  
HETATM 9115  O   HOH A 782       7.947   2.836 -32.597  1.00 23.15           O  
HETATM 9116  O   HOH A 783      29.618  37.043 -24.718  1.00 21.23           O  
HETATM 9117  O   HOH A 784      23.963  13.158 -10.929  1.00 45.58           O  
HETATM 9118  O   HOH A 785      -1.852  21.983 -38.379  1.00 25.97           O  
HETATM 9119  O   HOH A 786      -4.899  47.437 -12.047  1.00 35.23           O  
HETATM 9120  O   HOH A 787      31.321  37.793 -27.261  1.00 24.53           O  
HETATM 9121  O   HOH A 788       7.580  14.413  -6.796  1.00 17.29           O  
HETATM 9122  O   HOH A 789     -15.246  30.420  -6.930  1.00 30.87           O  
HETATM 9123  O   HOH A 790      -8.869  26.172 -15.902  1.00 19.01           O  
HETATM 9124  O   HOH A 791      -8.784  42.547  -7.713  1.00 38.94           O  
HETATM 9125  O   HOH A 792       2.118   8.690 -26.072  1.00 24.69           O  
HETATM 9126  O   HOH A 793       8.088  29.420 -38.839  1.00 22.05           O  
HETATM 9127  O   HOH A 794       9.930  33.377 -10.186  1.00 20.36           O  
HETATM 9128  O   HOH A 795      17.516   0.399 -29.417  1.00 30.75           O  
HETATM 9129  O   HOH A 796      20.602   6.081 -29.595  1.00 35.34           O  
HETATM 9130  O   HOH A 797      25.278  38.469   1.053  1.00 23.18           O  
HETATM 9131  O   HOH A 798      -2.733  24.141 -19.214  1.00 14.10           O  
HETATM 9132  O   HOH A 799     -16.528  34.509 -29.606  1.00 36.36           O  
HETATM 9133  O   HOH A 800     -10.368  43.053  -4.390  1.00 23.43           O  
HETATM 9134  O   HOH A 801      19.328  41.284  -6.793  1.00 18.02           O  
HETATM 9135  O   HOH A 802       9.607  27.627 -35.880  1.00 18.87           O  
HETATM 9136  O   HOH A 803      33.028  45.413 -13.445  1.00 33.16           O  
HETATM 9137  O   HOH A 804       6.988  49.088 -41.080  1.00 32.03           O  
HETATM 9138  O   HOH A 805       6.776  52.963 -23.929  1.00 34.62           O  
HETATM 9139  O   HOH A 806      21.546  -0.227 -30.856  1.00 39.62           O  
HETATM 9140  O   HOH A 807      14.345   2.111 -16.589  1.00 38.76           O  
HETATM 9141  O   HOH A 808      23.458  16.890 -14.027  1.00 28.78           O  
HETATM 9142  O   HOH A 809      -5.801  46.466 -28.590  1.00 36.18           O  
HETATM 9143  O   HOH A 810       7.697  44.145   4.446  1.00 31.19           O  
HETATM 9144  O   HOH A 811      34.533  31.671 -22.408  1.00 25.15           O  
HETATM 9145  O   HOH A 812      17.542  34.119  -0.332  1.00 20.19           O  
HETATM 9146  O   HOH A 813     -12.602  23.258  -5.989  1.00 15.23           O  
HETATM 9147  O   HOH A 814      14.039  10.257 -39.395  1.00 36.29           O  
HETATM 9148  O   HOH A 815      13.107  52.034 -20.741  1.00 30.13           O  
HETATM 9149  O   HOH A 816     -12.542  24.905 -13.584  1.00 26.47           O  
HETATM 9150  O   HOH A 817      19.135  26.903 -26.247  1.00 22.50           O  
HETATM 9151  O   HOH A 818      -5.397  45.050  -5.673  1.00 28.48           O  
HETATM 9152  O   HOH A 819      -1.243  32.761  -7.248  1.00 17.88           O  
HETATM 9153  O   HOH A 820       9.787  38.223  -2.992  1.00 19.99           O  
HETATM 9154  O   HOH A 821       4.954   4.397   2.857  1.00 35.18           O  
HETATM 9155  O   HOH A 822       2.580  11.745   5.988  1.00 40.85           O  
HETATM 9156  O   HOH A 823       2.353  30.940  -2.425  1.00 35.53           O  
HETATM 9157  O   HOH A 824      27.105  41.411   0.836  1.00 22.97           O  
HETATM 9158  O   HOH A 825      -0.419  38.000 -31.815  1.00 12.42           O  
HETATM 9159  O   HOH A 826      -9.112  38.716 -28.678  1.00 24.73           O  
HETATM 9160  O   HOH A 827      -4.554  29.785 -42.290  1.00 22.25           O  
HETATM 9161  O   HOH A 828      -2.579  46.004 -33.671  1.00 22.46           O  
HETATM 9162  O   HOH A 829      25.038  50.319  -6.981  1.00 41.36           O  
HETATM 9163  O   HOH A 830       6.946  16.397 -40.908  1.00 39.58           O  
HETATM 9164  O   HOH A 831      37.013  30.242  -8.593  1.00 48.08           O  
HETATM 9165  O   HOH A 832      14.462  41.516   5.987  1.00 43.14           O  
HETATM 9166  O   HOH A 833       4.720   8.816 -31.717  1.00 22.27           O  
HETATM 9167  O   HOH A 834      15.152  23.772   5.340  1.00 34.50           O  
HETATM 9168  O   HOH A 835      -5.434  35.461  -1.349  1.00 33.88           O  
HETATM 9169  O   HOH A 836      16.576  36.532   0.359  1.00 26.55           O  
HETATM 9170  O   HOH A 837      20.480  37.158  -5.954  1.00 38.16           O  
HETATM 9171  O   HOH A 838      36.068  28.688 -24.385  1.00 47.97           O  
HETATM 9172  O   HOH A 839      -4.651  38.312   4.744  1.00 24.99           O  
HETATM 9173  O   HOH A 840      17.418  21.282 -23.460  1.00 23.99           O  
HETATM 9174  O   HOH A 841      14.480  37.300 -44.008  1.00 33.88           O  
HETATM 9175  O   HOH A 842       6.417  19.020 -11.495  1.00 16.25           O  
HETATM 9176  O   HOH A 843      12.155  16.768   2.409  1.00 25.70           O  
HETATM 9177  O   HOH A 844      30.564  53.384 -15.571  1.00 46.65           O  
HETATM 9178  O   HOH A 845      16.341  19.097 -43.289  1.00 33.62           O  
HETATM 9179  O   HOH A 846       1.994  50.715 -17.185  1.00 47.94           O  
HETATM 9180  O   HOH A 847      -0.728  22.456   4.535  1.00 20.07           O  
HETATM 9181  O   HOH A 848      -3.647  46.070  -9.912  1.00 19.92           O  
HETATM 9182  O   HOH A 849       1.099  29.112 -41.064  1.00 31.08           O  
HETATM 9183  O   HOH A 850      19.127  56.682  -8.077  1.00 40.54           O  
HETATM 9184  O   HOH A 851       6.391  -5.660 -21.356  1.00 44.35           O  
HETATM 9185  O   HOH A 852       6.996  48.453 -36.297  1.00 17.59           O  
HETATM 9186  O   HOH A 853      19.087  20.407 -39.947  1.00 25.21           O  
HETATM 9187  O   HOH A 854      14.209  46.479   4.280  1.00 36.38           O  
HETATM 9188  O   HOH A 855       4.090  13.833 -31.631  1.00 19.61           O  
HETATM 9189  O   HOH A 856      -4.978  12.462  -7.255  1.00 18.95           O  
HETATM 9190  O   HOH A 857      18.901  23.251 -41.518  1.00 31.04           O  
HETATM 9191  O   HOH A 858      -1.458  43.805 -35.454  1.00 15.57           O  
HETATM 9192  O   HOH A 859      -7.296  22.428 -25.804  1.00 28.71           O  
HETATM 9193  O   HOH A 860       8.945  38.020 -36.095  1.00 21.31           O  
HETATM 9194  O   HOH A 861      36.458  33.132 -13.516  1.00 32.56           O  
HETATM 9195  O   HOH A 862      23.724  36.350 -26.425  1.00 21.56           O  
HETATM 9196  O   HOH A 863      -3.529  20.172 -25.840  1.00 15.92           O  
HETATM 9197  O   HOH A 864       1.827   4.283 -20.174  1.00 28.32           O  
HETATM 9198  O   HOH A 865      15.510  15.138 -33.544  1.00 27.13           O  
HETATM 9199  O   HOH A 866      26.159  31.251 -37.893  1.00 37.68           O  
HETATM 9200  O   HOH A 867      18.233  34.495 -22.500  1.00 16.42           O  
HETATM 9201  O   HOH A 868       5.500  23.586   7.319  1.00 32.63           O  
HETATM 9202  O   HOH A 869     -17.201  39.776 -29.087  1.00 52.23           O  
HETATM 9203  O   HOH A 870      -3.904  10.990  -9.229  1.00 19.07           O  
HETATM 9204  O   HOH A 871       9.564  16.004  -8.006  1.00 16.91           O  
HETATM 9205  O   HOH A 872      12.605  47.794 -40.451  1.00 37.96           O  
HETATM 9206  O   HOH A 873     -10.917  26.154 -35.922  1.00 22.96           O  
HETATM 9207  O   HOH A 874      14.735  39.916 -41.255  1.00 25.05           O  
HETATM 9208  O   HOH A 875      32.705  43.921  -6.477  1.00 25.62           O  
HETATM 9209  O   HOH A 876       0.215  48.383 -31.321  1.00 24.68           O  
HETATM 9210  O   HOH A 877      -5.551  36.359 -41.022  1.00 28.42           O  
HETATM 9211  O   HOH A 878       3.275  24.831 -34.535  1.00 14.62           O  
HETATM 9212  O   HOH A 879       6.387  31.300 -11.686  1.00 19.30           O  
HETATM 9213  O   HOH A 880      19.963  19.668 -16.610  1.00 18.80           O  
HETATM 9214  O   HOH A 881     -11.347  23.234 -24.509  1.00 41.70           O  
HETATM 9215  O   HOH A 882       3.807  31.485 -32.028  1.00 16.46           O  
HETATM 9216  O   HOH A 883       4.838   8.403 -39.256  1.00 40.06           O  
HETATM 9217  O   HOH A 884      -5.578  45.290 -31.159  1.00 20.27           O  
HETATM 9218  O   HOH A 885      -4.559  28.686 -22.026  1.00 16.38           O  
HETATM 9219  O   HOH A 886      14.081  13.071 -40.141  1.00 28.31           O  
HETATM 9220  O   HOH A 887      -2.825  34.862  -0.435  1.00 29.12           O  
HETATM 9221  O   HOH A 888      14.940  13.449 -42.541  1.00 29.86           O  
HETATM 9222  O   HOH A 889      15.563  39.845   1.506  1.00 20.34           O  
HETATM 9223  O   HOH A 890      -2.541  22.624 -12.966  1.00 16.38           O  
HETATM 9224  O   HOH A 891      19.538  15.134 -14.661  1.00 23.69           O  
HETATM 9225  O   HOH A 892       4.091  25.363  -7.578  1.00 16.48           O  
HETATM 9226  O   HOH A 893       1.282  20.144 -38.977  1.00 43.98           O  
HETATM 9227  O   HOH A 894     -16.684  29.707 -10.475  1.00 34.60           O  
HETATM 9228  O   HOH A 895       5.426  19.069 -14.734  1.00 15.98           O  
HETATM 9229  O   HOH A 896       0.898  33.144  -5.723  1.00 23.48           O  
HETATM 9230  O   HOH A 897      24.004  18.069 -10.852  1.00 28.23           O  
HETATM 9231  O   HOH A 898      -1.325  41.867 -37.478  1.00 16.25           O  
HETATM 9232  O   HOH A 899      -2.427   3.616  -9.413  1.00 44.55           O  
HETATM 9233  O   HOH A 900      -7.130  30.438 -32.645  1.00 25.68           O  
HETATM 9234  O   HOH A 901     -10.602  39.475 -26.380  1.00 17.77           O  
HETATM 9235  O   HOH A 902      -5.920  16.537 -13.941  1.00 17.76           O  
HETATM 9236  O   HOH A 903      -2.117  16.632   3.748  1.00 24.69           O  
HETATM 9237  O   HOH A 904      -5.908  21.409 -28.212  1.00 23.20           O  
HETATM 9238  O   HOH A 905      -4.950  43.519   1.602  1.00 42.05           O  
HETATM 9239  O   HOH A 906      11.438  -6.237 -16.060  1.00 42.71           O  
HETATM 9240  O   HOH A 907      12.310  34.196 -41.134  1.00 27.32           O  
HETATM 9241  O   HOH A 908      32.631  23.645  -7.463  1.00 48.26           O  
HETATM 9242  O   HOH A 909      -4.152  32.572 -38.816  1.00 25.98           O  
HETATM 9243  O   HOH A 910      28.492  18.019 -29.391  1.00 48.11           O  
HETATM 9244  O   HOH A 911      12.719  31.276  -2.198  1.00 21.25           O  
HETATM 9245  O   HOH A 912       9.040  18.643 -37.972  1.00 23.77           O  
HETATM 9246  O   HOH A 913      26.690  26.581 -38.664  1.00 31.62           O  
HETATM 9247  O   HOH A 914      22.226   8.747 -27.262  1.00 46.53           O  
HETATM 9248  O   HOH A 915      11.768  47.042 -26.821  1.00 27.30           O  
HETATM 9249  O   HOH A 916      -6.445  43.566 -12.025  1.00 20.91           O  
HETATM 9250  O   HOH A 917      -3.184   8.200  -6.826  1.00 42.57           O  
HETATM 9251  O   HOH A 918      -7.378  10.846 -11.894  1.00 28.96           O  
HETATM 9252  O   HOH A 919      -8.185  13.011 -14.965  1.00 27.85           O  
HETATM 9253  O   HOH A 920       3.808  33.179  -4.972  1.00 22.34           O  
HETATM 9254  O   HOH A 921      14.897  12.324  -2.101  1.00 36.03           O  
HETATM 9255  O   HOH A 922       0.198  18.614  -4.516  1.00 18.12           O  
HETATM 9256  O   HOH A 923     -12.462  28.903 -40.080  1.00 17.97           O  
HETATM 9257  O   HOH A 924     -15.216  27.030 -34.989  1.00 49.15           O  
HETATM 9258  O   HOH A 925      11.968  30.315 -34.396  1.00 14.18           O  
HETATM 9259  O   HOH A 926      -2.911  16.076 -24.100  1.00 17.50           O  
HETATM 9260  O   HOH A 927       2.088  -4.527 -27.413  1.00 46.53           O  
HETATM 9261  O   HOH A 928      11.167  53.773 -21.858  1.00 30.50           O  
HETATM 9262  O   HOH A 929      13.689  -2.291 -32.783  1.00 47.92           O  
HETATM 9263  O   HOH A 930     -12.927  27.098  -1.403  1.00 30.46           O  
HETATM 9264  O   HOH A 931      -4.319  46.917 -22.872  1.00 21.95           O  
HETATM 9265  O   HOH A 932      27.239  31.270   0.893  1.00 33.55           O  
HETATM 9266  O   HOH A 933      18.462  11.094 -39.722  1.00 33.85           O  
HETATM 9267  O   HOH A 934      19.523  23.061 -24.310  1.00 29.68           O  
HETATM 9268  O   HOH A 935     -16.314  42.774 -26.615  1.00 47.70           O  
HETATM 9269  O   HOH A 936      17.159  13.965 -13.656  1.00 20.10           O  
HETATM 9270  O   HOH A 937      14.954  48.596   2.008  1.00 43.57           O  
HETATM 9271  O   HOH A 938     -14.514  33.214 -39.548  1.00 27.58           O  
HETATM 9272  O   HOH A 939       7.246  35.894 -34.649  1.00 33.08           O  
HETATM 9273  O   HOH A 940      20.468  40.848  -4.242  1.00 24.97           O  
HETATM 9274  O   HOH A 941      20.974  29.162 -31.417  1.00 20.23           O  
HETATM 9275  O   HOH A 942      -6.060  43.080  -7.339  1.00 35.00           O  
HETATM 9276  O   HOH A 943      19.453  32.792 -39.458  1.00 40.92           O  
HETATM 9277  O   HOH A 944      31.430  47.466  -6.675  1.00 37.05           O  
HETATM 9278  O   HOH A 945     -15.012  35.100 -26.921  1.00 24.94           O  
HETATM 9279  O   HOH A 946       3.948  12.704 -38.023  1.00 30.77           O  
HETATM 9280  O   HOH A 947      13.502  32.278 -10.174  1.00 12.76           O  
HETATM 9281  O   HOH A 948       7.235  10.817  -5.421  1.00 18.42           O  
HETATM 9282  O   HOH A 949      20.974  42.469 -26.437  1.00 22.39           O  
HETATM 9283  O   HOH A 950       6.565  34.392 -36.649  1.00 20.14           O  
HETATM 9284  O   HOH A 951      -0.784  40.150 -33.660  1.00 14.12           O  
HETATM 9285  O   HOH A 952      -0.818  46.754 -26.866  1.00 16.67           O  
HETATM 9286  O   HOH A 953      15.070  12.595 -36.341  1.00 27.34           O  
HETATM 9287  O   HOH A 954      33.107  36.753 -30.795  1.00 43.39           O  
HETATM 9288  O   HOH A 955      29.739  51.729 -10.960  1.00 26.89           O  
HETATM 9289  O   HOH A 956     -11.331  27.368 -14.628  1.00 24.59           O  
HETATM 9290  O   HOH A 957      -3.255  12.901   2.645  1.00 27.94           O  
HETATM 9291  O   HOH A 958      22.721  17.512  -4.667  1.00 43.06           O  
HETATM 9292  O   HOH A 959      -9.661  32.525 -31.686  1.00 23.41           O  
HETATM 9293  O   HOH A 960      -9.372  22.825 -14.007  1.00 22.73           O  
HETATM 9294  O   HOH A 961      10.552  10.586  -4.655  1.00 23.20           O  
HETATM 9295  O   HOH A 962      27.086  46.786  -1.359  1.00 18.93           O  
HETATM 9296  O   HOH A 963       3.265  48.016  -5.813  1.00 18.40           O  
HETATM 9297  O   HOH A 964      -6.494  25.527  -8.774  1.00 15.41           O  
HETATM 9298  O   HOH A 965      13.761   6.108  -9.073  1.00 24.58           O  
HETATM 9299  O   HOH A 966      22.351  43.268  -9.273  1.00 19.96           O  
HETATM 9300  O   HOH A 967      14.006  42.093 -31.047  1.00 23.49           O  
HETATM 9301  O   HOH A 968       2.514  14.395  -8.908  1.00 15.43           O  
HETATM 9302  O   HOH A 969      17.081  16.929   2.010  1.00 33.27           O  
HETATM 9303  O   HOH A 970      20.718  41.009 -32.345  1.00 31.59           O  
HETATM 9304  O   HOH A 971      -4.729  13.141  -3.150  1.00 30.27           O  
HETATM 9305  O   HOH A 972      -6.090  28.445 -31.144  1.00 19.63           O  
HETATM 9306  O   HOH A 973      17.042  12.268 -30.081  1.00 19.95           O  
HETATM 9307  O   HOH A 974      10.746  39.173 -12.158  1.00 13.19           O  
HETATM 9308  O   HOH A 975      -6.971  15.236  -5.323  1.00 19.77           O  
HETATM 9309  O   HOH A 976      -6.258  44.696   0.245  1.00 37.40           O  
HETATM 9310  O   HOH A 977      33.819  38.242 -28.284  1.00 38.67           O  
HETATM 9311  O   HOH A 978      17.207  24.608   4.538  1.00 30.56           O  
HETATM 9312  O   HOH A 979       4.448  52.710 -27.965  1.00 40.54           O  
HETATM 9313  O   HOH A 980       5.251  18.386  -8.857  1.00 16.48           O  
HETATM 9314  O   HOH A 981       0.600  10.994   4.500  1.00 37.11           O  
HETATM 9315  O   HOH A 982      19.052  23.223 -28.340  1.00 21.27           O  
HETATM 9316  O   HOH A 983      18.180  10.821 -22.572  1.00 25.30           O  
HETATM 9317  O   HOH A 984      23.112  37.580  -4.274  1.00 39.69           O  
HETATM 9318  O   HOH A 985       0.039   8.984  -5.303  1.00 19.13           O  
HETATM 9319  O   HOH A 986      23.394  26.113 -28.898  1.00 23.49           O  
HETATM 9320  O   HOH A 987      -2.537  34.917 -38.180  1.00 19.40           O  
HETATM 9321  O   HOH A 988       9.175  -1.008  -7.385  1.00 37.38           O  
HETATM 9322  O   HOH A 989       1.625  52.242 -29.107  1.00 36.88           O  
HETATM 9323  O   HOH A 990      20.968  53.045  -6.550  1.00 54.43           O  
HETATM 9324  O   HOH A 991      -8.061  21.926 -29.616  1.00 30.23           O  
HETATM 9325  O   HOH A 992       6.758  28.930 -36.100  1.00 32.43           O  
HETATM 9326  O   HOH A 993      12.788  39.888 -32.219  1.00 17.29           O  
HETATM 9327  O   HOH A 994      27.858  11.087 -35.909  1.00 42.92           O  
HETATM 9328  O   HOH A 995      15.221  35.228 -21.873  1.00 27.73           O  
HETATM 9329  O   HOH A 996      12.878  40.028  -0.218  1.00 29.78           O  
HETATM 9330  O   HOH A 997      34.317  37.069  -9.214  1.00 41.02           O  
HETATM 9331  O   HOH A 998       9.290  53.170  -6.596  1.00 38.63           O  
HETATM 9332  O   HOH A 999      26.838  48.165   2.455  1.00 25.74           O  
HETATM 9333  O   HOH A1000     -13.832  35.343 -37.436  1.00 29.35           O  
HETATM 9334  O   HOH A1001      10.409   3.184 -37.888  1.00 28.54           O  
HETATM 9335  O   HOH A1002      16.700   6.397 -13.467  1.00 40.92           O  
HETATM 9336  O   HOH A1003      17.659  19.065 -25.419  1.00 18.99           O  
HETATM 9337  O   HOH A1004       7.466  16.388 -36.999  1.00 22.82           O  
HETATM 9338  O   HOH A1005      27.302  42.622 -22.470  1.00 21.86           O  
HETATM 9339  O   HOH A1006      11.143  44.926 -31.772  1.00 36.03           O  
HETATM 9340  O   HOH A1007     -14.719  25.538 -30.002  1.00 39.53           O  
HETATM 9341  O   HOH A1008      -2.048  45.219   2.360  1.00 32.70           O  
HETATM 9342  O   HOH A1009      27.040  27.765  -4.053  1.00 21.08           O  
HETATM 9343  O   HOH A1010      22.963  48.497   0.459  1.00 41.83           O  
HETATM 9344  O   HOH A1011      24.117  32.074 -39.226  1.00 41.40           O  
HETATM 9345  O   HOH A1012      13.075  45.602 -28.485  1.00 29.71           O  
HETATM 9346  O   HOH A1013      -3.164  12.056 -30.161  1.00 23.27           O  
HETATM 9347  O   HOH A1014      30.940  19.915 -14.745  1.00 35.33           O  
HETATM 9348  O   HOH A1015      19.875  26.740 -30.767  1.00 19.98           O  
HETATM 9349  O   HOH A1016      -4.936  25.043  -0.628  1.00 36.12           O  
HETATM 9350  O   HOH A1017      -7.752  21.306 -35.824  1.00 37.70           O  
HETATM 9351  O   HOH A1018      10.295  41.243 -32.616  1.00 18.78           O  
HETATM 9352  O   HOH A1019      20.063  37.826 -27.678  1.00 23.11           O  
HETATM 9353  O   HOH A1020       8.507  12.911 -35.538  1.00 21.78           O  
HETATM 9354  O   HOH A1021      -9.960  39.824 -33.475  1.00 17.54           O  
HETATM 9355  O   HOH A1022       5.070  22.221  -5.794  1.00 16.53           O  
HETATM 9356  O   HOH A1023       2.309   7.362 -32.683  1.00 31.05           O  
HETATM 9357  O   HOH A1024       0.044  22.389 -31.881  1.00 15.88           O  
HETATM 9358  O   HOH A1025      -0.720  16.942 -35.436  1.00 36.73           O  
HETATM 9359  O   HOH A1026      -1.852  18.490 -24.373  1.00 14.00           O  
HETATM 9360  O   HOH A1027      31.405  39.704  -9.826  1.00 34.57           O  
HETATM 9361  O   HOH A1028      -8.303  26.309 -18.470  1.00 29.07           O  
HETATM 9362  O   HOH A1029     -10.868  46.945 -20.726  1.00 31.37           O  
HETATM 9363  O   HOH A1030      29.306  22.042 -40.173  1.00 28.20           O  
HETATM 9364  O   HOH A1031      -4.990  12.194 -25.774  1.00 30.40           O  
HETATM 9365  O   HOH A1032      10.661  -3.031 -31.556  1.00 38.19           O  
HETATM 9366  O   HOH A1033       9.074  38.874 -33.304  1.00 19.93           O  
HETATM 9367  O   HOH A1034       5.877   1.774 -39.730  1.00 41.46           O  
HETATM 9368  O   HOH A1035       6.129  26.500   1.910  1.00 38.25           O  
HETATM 9369  O   HOH A1036      20.940  48.631 -20.381  1.00 22.22           O  
HETATM 9370  O   HOH A1037      18.016  50.164 -24.144  1.00 49.08           O  
HETATM 9371  O   HOH A1038      33.731  21.141 -30.795  1.00 38.79           O  
HETATM 9372  O   HOH A1039      22.264   7.338 -39.175  1.00 40.53           O  
HETATM 9373  O   HOH A1040      32.725  23.526 -16.167  1.00 37.08           O  
HETATM 9374  O   HOH A1041       0.780  48.957 -18.797  1.00 31.83           O  
HETATM 9375  O   HOH A1042      23.687  48.301 -19.286  1.00 21.59           O  
HETATM 9376  O   HOH A1043       5.047  17.643 -37.527  1.00 19.30           O  
HETATM 9377  O   HOH A1044       2.933  22.846 -32.533  1.00 14.32           O  
HETATM 9378  O   HOH A1045       5.234  27.450  -2.658  1.00 36.64           O  
HETATM 9379  O   HOH A1046      32.041  19.537 -29.405  1.00 41.80           O  
HETATM 9380  O   HOH A1047      11.018  11.886   2.255  1.00 38.42           O  
HETATM 9381  O   HOH A1048      -8.659  31.015 -34.787  1.00 22.91           O  
HETATM 9382  O   HOH A1049      15.064  58.532  -5.392  1.00 47.66           O  
HETATM 9383  O   HOH A1050       9.093  30.088  -2.863  1.00 21.74           O  
HETATM 9384  O   HOH A1051      26.108  37.205  -4.506  1.00 25.69           O  
HETATM 9385  O   HOH A1052      23.784  39.449  -6.254  1.00 30.65           O  
HETATM 9386  O   HOH A1053      -9.953  27.647  -2.002  1.00 16.75           O  
HETATM 9387  O   HOH A1054       7.992  20.785 -39.081  1.00 21.60           O  
HETATM 9388  O   HOH A1055      -1.382  20.214  -6.184  1.00 15.13           O  
HETATM 9389  O   HOH A1056      -7.338   9.733 -17.319  1.00 28.03           O  
HETATM 9390  O   HOH A1057     -12.713  28.534 -21.033  1.00 24.25           O  
HETATM 9391  O   HOH A1058      11.536  42.751 -44.021  1.00 40.96           O  
HETATM 9392  O   HOH A1059      21.906  38.065 -25.533  1.00 24.19           O  
HETATM 9393  O   HOH A1060     -12.700  27.506 -17.247  1.00 31.04           O  
HETATM 9394  O   HOH A1061      11.766  29.714  -4.495  1.00 23.61           O  
HETATM 9395  O   HOH A1062      26.943  51.961 -17.258  1.00 28.99           O  
HETATM 9396  O   HOH A1063      23.383  50.063 -26.141  1.00 29.04           O  
HETATM 9397  O   HOH A1064      27.170  52.820  -9.509  1.00 44.30           O  
HETATM 9398  O   HOH A1065      26.267  29.869 -33.806  1.00 24.56           O  
HETATM 9399  O   HOH A1066     -17.083  33.012  -6.430  1.00 49.89           O  
HETATM 9400  O   HOH A1067      36.463  28.930 -28.629  1.00 35.18           O  
HETATM 9401  O   HOH A1068      20.571   9.094 -24.523  1.00 41.19           O  
HETATM 9402  O   HOH A1069      16.343  10.799 -38.197  1.00 32.85           O  
HETATM 9403  O   HOH A1070      22.925  21.228 -42.322  1.00 26.94           O  
HETATM 9404  O   HOH A1071       9.785  16.515   7.465  0.65 31.15           O  
HETATM 9405  O   HOH A1072       0.355  46.721  -0.879  1.00 30.14           O  
HETATM 9406  O   HOH A1073       6.749  51.277 -27.239  1.00 18.18           O  
HETATM 9407  O   HOH A1074      28.830  22.323  -7.965  1.00 20.90           O  
HETATM 9408  O   HOH A1075     -13.394  25.194 -26.305  1.00 28.02           O  
HETATM 9409  O   HOH A1076       2.628  48.401 -20.539  1.00 23.04           O  
HETATM 9410  O   HOH A1077      11.906  33.937 -23.449  1.00 32.63           O  
HETATM 9411  O   HOH A1078      10.821  46.577 -29.795  1.00 39.22           O  
HETATM 9412  O   HOH A1079      -3.874  46.816  -7.095  1.00 25.58           O  
HETATM 9413  O   HOH A1080       4.958  15.665  -8.217  1.00 17.37           O  
HETATM 9414  O   HOH A1081       3.960  50.623  -6.197  1.00 35.09           O  
HETATM 9415  O   HOH A1082      15.834  46.864 -37.950  1.00 36.47           O  
HETATM 9416  O   HOH A1083       0.853   6.633  -4.253  1.00 23.81           O  
HETATM 9417  O   HOH A1084      35.893  24.418 -30.712  1.00 47.87           O  
HETATM 9418  O   HOH A1085      14.746  39.238  -2.010  1.00 16.40           O  
HETATM 9419  O   HOH A1086     -16.124  25.842  -6.538  1.00 26.16           O  
HETATM 9420  O   HOH A1087      -8.180  42.469 -10.311  1.00 24.68           O  
HETATM 9421  O   HOH A1088      13.142  26.527 -43.443  1.00 38.36           O  
HETATM 9422  O   HOH A1089      20.340  43.357   9.460  1.00 34.98           O  
HETATM 9423  O   HOH A1090      10.304  12.936  -6.330  1.00 17.73           O  
HETATM 9424  O   HOH A1091       6.967  -0.137  -2.463  1.00 23.60           O  
HETATM 9425  O   HOH A1092       2.007  30.767  -6.340  1.00 19.58           O  
HETATM 9426  O   HOH A1093     -17.366  44.900 -18.717  1.00 44.77           O  
HETATM 9427  O   HOH A1094       9.218  31.746 -12.716  1.00 11.76           O  
HETATM 9428  O   HOH A1095      -4.695  32.564 -43.573  1.00 29.61           O  
HETATM 9429  O   HOH A1096      10.605  59.725  -7.927  1.00 42.55           O  
HETATM 9430  O   HOH A1097     -13.811  38.506  -7.278  1.00 36.07           O  
HETATM 9431  O   HOH A1098      28.257  45.608   0.993  1.00 26.93           O  
HETATM 9432  O   HOH A1099      -8.159  28.634 -29.534  1.00 21.08           O  
HETATM 9433  O   HOH A1100      22.024  41.135  -7.604  1.00 22.08           O  
HETATM 9434  O   HOH A1101      16.710  12.856 -33.998  1.00 30.65           O  
HETATM 9435  O   HOH A1102     -16.228  37.520 -30.739  1.00 32.69           O  
HETATM 9436  O   HOH A1103      -1.386   5.793 -27.321  1.00 38.39           O  
HETATM 9437  O   HOH A1104       2.981  49.479  -2.255  1.00 27.23           O  
HETATM 9438  O   HOH A1105      36.766  34.342 -19.926  1.00 43.21           O  
HETATM 9439  O   HOH A1106       0.379  47.459 -36.903  1.00 20.55           O  
HETATM 9440  O   HOH A1107     -10.837  42.704 -11.494  1.00 24.67           O  
HETATM 9441  O   HOH A1108      -8.573  38.873 -31.362  1.00 27.54           O  
HETATM 9442  O   HOH A1109      17.461  27.083 -29.037  1.00 18.74           O  
HETATM 9443  O   HOH A1110      -9.476  15.176 -11.517  1.00 24.30           O  
HETATM 9444  O   HOH A1111     -11.569  44.380 -27.090  1.00 34.28           O  
HETATM 9445  O   HOH A1112      -8.968  36.686 -38.867  1.00 28.84           O  
HETATM 9446  O   HOH A1113      -3.657  29.321 -30.536  1.00 20.11           O  
HETATM 9447  O   HOH A1114      19.303  47.871   3.329  1.00 39.66           O  
HETATM 9448  O   HOH A1115     -10.929  25.955 -23.594  1.00 41.32           O  
HETATM 9449  O   HOH A1116      -4.855  26.290 -19.265  1.00 27.70           O  
HETATM 9450  O   HOH A1117      26.464  19.655 -25.216  1.00 36.30           O  
HETATM 9451  O   HOH A1118      20.319   4.486 -34.460  1.00 35.94           O  
HETATM 9452  O   HOH A1119      14.338  15.287   2.532  1.00 36.60           O  
HETATM 9453  O   HOH A1120      23.582  39.355 -35.754  1.00 33.88           O  
HETATM 9454  O   HOH A1121       3.603  51.200 -20.482  1.00 32.11           O  
HETATM 9455  O   HOH A1122       2.916  47.275  -0.285  1.00 21.84           O  
HETATM 9456  O   HOH A1123       5.200  31.606 -35.904  1.00 21.04           O  
HETATM 9457  O   HOH A1124      -0.762  48.008 -33.917  1.00 39.71           O  
HETATM 9458  O   HOH A1125      33.218  25.643 -17.968  1.00 34.99           O  
HETATM 9459  O   HOH A1126      22.933  48.821   7.002  1.00 34.57           O  
HETATM 9460  O   HOH A1127      -3.463  49.507  -6.520  1.00 48.90           O  
HETATM 9461  O   HOH A1128       0.842   5.312 -31.423  1.00 42.25           O  
HETATM 9462  O   HOH A1129      12.670  34.075 -21.240  1.00 29.86           O  
HETATM 9463  O   HOH A1130      20.722  -6.513 -30.647  1.00 39.19           O  
HETATM 9464  O   HOH A1131      20.794  22.734   9.917  1.00 33.82           O  
HETATM 9465  O   HOH A1132       5.907  52.183 -16.605  1.00 23.27           O  
HETATM 9466  O   HOH A1133     -10.866  24.259 -15.819  1.00 32.71           O  
HETATM 9467  O   HOH A1134      -0.148   2.165 -23.120  1.00 41.70           O  
HETATM 9468  O   HOH A1135      25.681  48.723  -0.154  1.00 23.57           O  
HETATM 9469  O   HOH A1136      24.167  20.042  -3.535  1.00 37.99           O  
HETATM 9470  O   HOH A1137      18.714  42.458   7.436  1.00 14.83           O  
HETATM 9471  O   HOH A1138       9.503  40.564  -0.430  1.00 29.77           O  
HETATM 9472  O   HOH A1139      -5.801  18.636 -28.440  1.00 36.17           O  
HETATM 9473  O   HOH A1140      26.658  11.501 -44.313  1.00 48.07           O  
HETATM 9474  O   HOH A1141     -17.903  37.860 -17.340  1.00 41.66           O  
HETATM 9475  O   HOH A1142       0.278  43.234 -39.461  1.00 14.22           O  
HETATM 9476  O   HOH A1143     -10.840  50.478 -14.347  1.00 41.23           O  
HETATM 9477  O   HOH A1144      14.666  34.859 -24.184  1.00 35.14           O  
HETATM 9478  O   HOH A1145      20.715  25.608 -28.116  1.00 24.61           O  
HETATM 9479  O   HOH A1146     -10.992  16.665 -10.110  1.00 32.65           O  
HETATM 9480  O   HOH A1147      -0.207  49.786 -35.427  1.00 34.48           O  
HETATM 9481  O   HOH A1148       5.955  52.366  -6.858  1.00 50.08           O  
HETATM 9482  O   HOH A1149      28.427  48.186  -3.426  1.00 25.52           O  
HETATM 9483  O   HOH A1150      17.352  30.020 -38.698  1.00 32.52           O  
HETATM 9484  O   HOH A1151      -3.471  10.763  -1.419  1.00 28.22           O  
HETATM 9485  O   HOH A1152      -2.924  48.238 -27.185  1.00 36.05           O  
HETATM 9486  O   HOH A1153     -16.183  28.226  -7.920  1.00 35.30           O  
HETATM 9487  O   HOH A1154      13.154  11.202  -3.761  1.00 33.99           O  
HETATM 9488  O   HOH A1155       3.885  52.285 -18.109  1.00 39.84           O  
HETATM 9489  O   HOH A1156      -1.145  45.634 -38.324  1.00 28.91           O  
HETATM 9490  O   HOH A1157      -1.723  11.245   0.917  1.00 41.63           O  
HETATM 9491  O   HOH A1158      12.970  12.700   2.815  1.00 41.72           O  
HETATM 9492  O   HOH A1159      -6.307  27.845  -0.132  1.00 40.85           O  
HETATM 9493  O   HOH A1160      -9.010  45.215   1.367  1.00 38.39           O  
HETATM 9494  O   HOH A1161      -2.484   9.890  -4.536  1.00 27.57           O  
HETATM 9495  O   HOH A1162      40.237  22.986  -3.102  1.00 42.63           O  
HETATM 9496  O   HOH A1163       7.129  50.540 -34.493  1.00 26.29           O  
HETATM 9497  O   HOH A1164      -0.064   9.686   2.018  1.00 42.11           O  
HETATM 9498  O   HOH A1165      29.578  23.230  -5.492  1.00 48.00           O  
HETATM 9499  O   HOH A1166      13.100  59.872  -6.666  1.00 47.79           O  
HETATM 9500  O   HOH A1167     -13.076  48.338 -20.350  1.00 46.30           O  
HETATM 9501  O   HOH A1168      36.436  30.362 -12.483  1.00 41.05           O  
HETATM 9502  O   HOH A1169      -4.790  35.262 -43.197  1.00 32.23           O  
HETATM 9503  O   HOH A1170      17.191  11.011  -2.574  1.00 43.02           O  
HETATM 9504  O   HOH A1171     -12.402  41.108 -33.785  1.00 35.10           O  
HETATM 9505  O   HOH A1172      19.964  34.582   1.097  1.00 29.06           O  
HETATM 9506  O   HOH A1173      -6.202  20.419 -25.101  1.00 22.93           O  
HETATM 9507  O   HOH A1174      16.158  47.736 -34.831  1.00 53.46           O  
HETATM 9508  O   HOH A1175      -4.185  32.752   1.281  1.00 33.13           O  
HETATM 9509  O   HOH A1176      -2.727  24.049   5.187  1.00 39.74           O  
HETATM 9510  O   HOH A1177      -5.866  46.971  -1.532  1.00 43.87           O  
HETATM 9511  O   HOH A1178      11.380  49.907 -27.287  1.00 30.28           O  
HETATM 9512  O   HOH A1179      19.199  39.270 -40.399  1.00 33.37           O  
HETATM 9513  O   HOH A1180       8.772  48.210 -42.848  1.00 42.05           O  
HETATM 9514  O   HOH A1181      13.422  44.633 -31.073  1.00 27.10           O  
HETATM 9515  O   HOH A1182     -10.353  27.197 -19.631  1.00 51.27           O  
HETATM 9516  O   HOH A1183       6.232  29.281  -2.841  1.00 41.47           O  
HETATM 9517  O   HOH A1184      -7.280  46.481  -4.072  1.00 40.43           O  
HETATM 9518  O   HOH A1185       6.829  25.593   7.954  1.00 42.78           O  
HETATM 9519  O   HOH A1186      16.315  31.868   0.974  1.00 26.21           O  
HETATM 9520  O   HOH A1187      -3.017  12.439  -5.257  1.00 21.40           O  
HETATM 9521  O   HOH A1188      15.161  38.200   3.608  1.00 42.25           O  
HETATM 9522  O   HOH A1189       7.492  21.389 -41.892  1.00 44.41           O  
HETATM 9523  O   HOH A1190      31.146  33.171  -4.457  1.00 38.91           O  
HETATM 9524  O   HOH A1191      26.620  18.156 -41.544  1.00 35.70           O  
HETATM 9525  O   HOH A1192      -9.540  12.583 -10.743  1.00 41.81           O  
HETATM 9526  O   HOH A1193      24.582  50.503 -17.027  1.00 34.47           O  
HETATM 9527  O   HOH A1194      18.653  20.028 -42.465  1.00 34.43           O  
HETATM 9528  O   HOH A1195      -8.581  15.474 -14.048  1.00 22.00           O  
HETATM 9529  O   HOH A1196      -0.077  34.562 -39.452  1.00 36.15           O  
HETATM 9530  O   HOH A1197      -5.306  15.179 -24.820  1.00 32.44           O  
HETATM 9531  O   HOH A1198      -5.843   9.148  -9.747  1.00 28.11           O  
HETATM 9532  O   HOH A1199      -3.264  20.090 -40.750  1.00 36.07           O  
HETATM 9533  O   HOH A1200       0.139  17.910 -39.700  1.00 36.93           O  
HETATM 9534  O   HOH A1201      16.384  15.568   4.211  1.00 47.31           O  
HETATM 9535  O   HOH A1202      18.206  30.987   2.780  1.00 31.69           O  
HETATM 9536  O   HOH A1203      19.336  21.332 -26.463  1.00 25.10           O  
HETATM 9537  O   HOH A1204      12.165  16.174   5.140  1.00 47.19           O  
HETATM 9538  O   HOH A1205      -6.813  10.993  -6.055  1.00 43.32           O  
HETATM 9539  O   HOH A1206      -8.649  48.400 -21.692  1.00 38.92           O  
HETATM 9540  O   HOH A1207      20.940  50.288 -22.400  1.00 38.05           O  
HETATM 9541  O   HOH A1208      22.938  38.801 -38.389  1.00 30.23           O  
HETATM 9542  O   HOH A1209      -7.017  12.872  -4.088  1.00 36.67           O  
HETATM 9543  O   HOH A1210     -14.996  26.701 -24.963  1.00 29.57           O  
HETATM 9544  O   HOH A1211       5.230  53.754 -14.246  1.00 41.59           O  
HETATM 9545  O   HOH A1212      -2.414   9.755 -30.973  1.00 31.26           O  
HETATM 9546  O   HOH A1213      26.879  53.500 -19.426  1.00 39.58           O  
HETATM 9547  O   HOH A1214      12.235  24.163 -44.319  1.00 41.37           O  
HETATM 9548  O   HOH A1215      13.684  31.816   1.864  1.00 47.06           O  
HETATM 9549  O   HOH A1216       8.392  39.348   1.678  1.00 31.71           O  
HETATM 9550  O   HOH A1217      -9.163  12.254 -17.264  1.00 42.41           O  
HETATM 9551  O   HOH A1218      -2.313  31.628 -40.570  1.00 27.65           O  
HETATM 9552  O   HOH A1219      -2.548  33.773 -42.419  1.00 25.37           O  
HETATM 9553  O   HOH A1220       8.346  50.922 -29.608  1.00 32.50           O  
HETATM 9554  O   HOH A1221       5.669  19.526 -39.516  1.00 26.40           O  
HETATM 9555  O   HOH A1222       3.330  15.418 -38.387  1.00 29.55           O  
HETATM 9556  O   HOH A1223      16.505  40.823   7.454  1.00 28.55           O  
HETATM 9557  O   HOH A1224       4.228  15.805 -41.060  1.00 39.73           O  
HETATM 9558  O   HOH A1225      10.434  49.239 -29.802  1.00 36.91           O  
HETATM 9559  O   HOH A1226      -5.787   6.950 -11.167  1.00 42.23           O  
CONECT   25  136                                                                
CONECT  136   25                                                                
CONECT  931 8505                                                                
CONECT 1360 8618                                                                
CONECT 1434 8951                                                                
CONECT 1472 8953                                                                
CONECT 1492 1516                                                                
CONECT 1509 1510 1511 1519                                                      
CONECT 1510 1509 1513                                                           
CONECT 1511 1509 1512                                                           
CONECT 1512 1511 1513 1520                                                      
CONECT 1513 1510 1512 1514                                                      
CONECT 1514 1513 1515 1521 1522                                                 
CONECT 1515 1514 1516 1517 1523                                                 
CONECT 1516 1492 1515 1524                                                      
CONECT 1517 1515 1518 1525                                                      
CONECT 1518 1517                                                                
CONECT 1519 1509                                                                
CONECT 1520 1512                                                                
CONECT 1521 1514                                                                
CONECT 1522 1514                                                                
CONECT 1523 1515                                                                
CONECT 1524 1516                                                                
CONECT 1525 1517                                                                
CONECT 1738 8186                                                                
CONECT 2140 8953                                                                
CONECT 2168 8952                                                                
CONECT 3068 8671                                                                
CONECT 3269 8804                                                                
CONECT 4438 8877                                                                
CONECT 4558 5014                                                                
CONECT 5014 4558                                                                
CONECT 5491 8955                                                                
CONECT 5706 8956                                                                
CONECT 6011 8983                                                                
CONECT 6535 8950                                                                
CONECT 6586 8951                                                                
CONECT 6622 8952                                                                
CONECT 7622 8952                                                                
CONECT 7635 8950                                                                
CONECT 7649 8953                                                                
CONECT 7716 8950                                                                
CONECT 8039 8954                                                                
CONECT 8089 8954                                                                
CONECT 8090 8954                                                                
CONECT 8186 1738                                                                
CONECT 8505  931 8506 8516                                                      
CONECT 8506 8505 8507 8513 8519                                                 
CONECT 8507 8506 8508 8514 8520                                                 
CONECT 8508 8507 8509 8515 8521                                                 
CONECT 8509 8508 8510 8516 8522                                                 
CONECT 8510 8509 8517 8523 8524                                                 
CONECT 8511 8512 8513 8518                                                      
CONECT 8512 8511 8525 8526 8527                                                 
CONECT 8513 8506 8511 8528                                                      
CONECT 8514 8507 8529                                                           
CONECT 8515 8508 8531                                                           
CONECT 8516 8505 8509                                                           
CONECT 8517 8510 8530                                                           
CONECT 8518 8511                                                                
CONECT 8519 8506                                                                
CONECT 8520 8507                                                                
CONECT 8521 8508                                                                
CONECT 8522 8509                                                                
CONECT 8523 8510                                                                
CONECT 8524 8510                                                                
CONECT 8525 8512                                                                
CONECT 8526 8512                                                                
CONECT 8527 8512                                                                
CONECT 8528 8513                                                                
CONECT 8529 8514                                                                
CONECT 8530 8517                                                                
CONECT 8531 8515 8532 8542                                                      
CONECT 8532 8531 8533 8539 8545                                                 
CONECT 8533 8532 8534 8540 8546                                                 
CONECT 8534 8533 8535 8541 8547                                                 
CONECT 8535 8534 8536 8542 8548                                                 
CONECT 8536 8535 8543 8549 8550                                                 
CONECT 8537 8538 8539 8544                                                      
CONECT 8538 8537 8551 8552 8553                                                 
CONECT 8539 8532 8537 8554                                                      
CONECT 8540 8533 8555                                                           
CONECT 8541 8534 8557                                                           
CONECT 8542 8531 8535                                                           
CONECT 8543 8536 8556                                                           
CONECT 8544 8537                                                                
CONECT 8545 8532                                                                
CONECT 8546 8533                                                                
CONECT 8547 8534                                                                
CONECT 8548 8535                                                                
CONECT 8549 8536                                                                
CONECT 8550 8536                                                                
CONECT 8551 8538                                                                
CONECT 8552 8538                                                                
CONECT 8553 8538                                                                
CONECT 8554 8539                                                                
CONECT 8555 8540                                                                
CONECT 8556 8543                                                                
CONECT 8557 8541 8558 8566                                                      
CONECT 8558 8557 8559 8563 8568                                                 
CONECT 8559 8558 8560 8564 8569                                                 
CONECT 8560 8559 8561 8565 8570                                                 
CONECT 8561 8560 8562 8566 8571                                                 
CONECT 8562 8561 8567 8572 8573                                                 
CONECT 8563 8558 8574                                                           
CONECT 8564 8559 8575                                                           
CONECT 8565 8560 8576                                                           
CONECT 8566 8557 8561                                                           
CONECT 8567 8562 8577                                                           
CONECT 8568 8558                                                                
CONECT 8569 8559                                                                
CONECT 8570 8560                                                                
CONECT 8571 8561                                                                
CONECT 8572 8562                                                                
CONECT 8573 8562                                                                
CONECT 8574 8563                                                                
CONECT 8575 8564                                                                
CONECT 8576 8565                                                                
CONECT 8577 8567 8578 8586                                                      
CONECT 8578 8577 8579 8583 8588                                                 
CONECT 8579 8578 8580 8584 8589                                                 
CONECT 8580 8579 8581 8585 8590                                                 
CONECT 8581 8580 8582 8586 8591                                                 
CONECT 8582 8581 8587 8592 8593                                                 
CONECT 8583 8578 8594                                                           
CONECT 8584 8579 8597                                                           
CONECT 8585 8580 8595                                                           
CONECT 8586 8577 8581                                                           
CONECT 8587 8582 8596                                                           
CONECT 8588 8578                                                                
CONECT 8589 8579                                                                
CONECT 8590 8580                                                                
CONECT 8591 8581                                                                
CONECT 8592 8582                                                                
CONECT 8593 8582                                                                
CONECT 8594 8583                                                                
CONECT 8595 8585                                                                
CONECT 8596 8587                                                                
CONECT 8597 8584 8598 8606                                                      
CONECT 8598 8597 8599 8603 8608                                                 
CONECT 8599 8598 8600 8604 8609                                                 
CONECT 8600 8599 8601 8605 8610                                                 
CONECT 8601 8600 8602 8606 8611                                                 
CONECT 8602 8601 8607 8612 8613                                                 
CONECT 8603 8598 8614                                                           
CONECT 8604 8599 8615                                                           
CONECT 8605 8600 8616                                                           
CONECT 8606 8597 8601                                                           
CONECT 8607 8602 8617                                                           
CONECT 8608 8598                                                                
CONECT 8609 8599                                                                
CONECT 8610 8600                                                                
CONECT 8611 8601                                                                
CONECT 8612 8602                                                                
CONECT 8613 8602                                                                
CONECT 8614 8603                                                                
CONECT 8615 8604                                                                
CONECT 8616 8605                                                                
CONECT 8617 8607                                                                
CONECT 8618 1360 8619 8629                                                      
CONECT 8619 8618 8620 8626 8632                                                 
CONECT 8620 8619 8621 8627 8633                                                 
CONECT 8621 8620 8622 8628 8634                                                 
CONECT 8622 8621 8623 8629 8635                                                 
CONECT 8623 8622 8630 8636 8637                                                 
CONECT 8624 8625 8626 8631                                                      
CONECT 8625 8624 8638 8639 8640                                                 
CONECT 8626 8619 8624 8641                                                      
CONECT 8627 8620 8642                                                           
CONECT 8628 8621 8644                                                           
CONECT 8629 8618 8622                                                           
CONECT 8630 8623 8643                                                           
CONECT 8631 8624                                                                
CONECT 8632 8619                                                                
CONECT 8633 8620                                                                
CONECT 8634 8621                                                                
CONECT 8635 8622                                                                
CONECT 8636 8623                                                                
CONECT 8637 8623                                                                
CONECT 8638 8625                                                                
CONECT 8639 8625                                                                
CONECT 8640 8625                                                                
CONECT 8641 8626                                                                
CONECT 8642 8627                                                                
CONECT 8643 8630                                                                
CONECT 8644 8628 8645 8655                                                      
CONECT 8645 8644 8646 8652 8658                                                 
CONECT 8646 8645 8647 8653 8659                                                 
CONECT 8647 8646 8648 8654 8660                                                 
CONECT 8648 8647 8649 8655 8661                                                 
CONECT 8649 8648 8656 8662 8663                                                 
CONECT 8650 8651 8652 8657                                                      
CONECT 8651 8650 8664 8665 8666                                                 
CONECT 8652 8645 8650 8667                                                      
CONECT 8653 8646 8668                                                           
CONECT 8654 8647 8669                                                           
CONECT 8655 8644 8648                                                           
CONECT 8656 8649 8670                                                           
CONECT 8657 8650                                                                
CONECT 8658 8645                                                                
CONECT 8659 8646                                                                
CONECT 8660 8647                                                                
CONECT 8661 8648                                                                
CONECT 8662 8649                                                                
CONECT 8663 8649                                                                
CONECT 8664 8651                                                                
CONECT 8665 8651                                                                
CONECT 8666 8651                                                                
CONECT 8667 8652                                                                
CONECT 8668 8653                                                                
CONECT 8669 8654                                                                
CONECT 8670 8656                                                                
CONECT 8671 3068 8672 8682                                                      
CONECT 8672 8671 8673 8679 8685                                                 
CONECT 8673 8672 8674 8680 8686                                                 
CONECT 8674 8673 8675 8681 8687                                                 
CONECT 8675 8674 8676 8682 8688                                                 
CONECT 8676 8675 8683 8689 8690                                                 
CONECT 8677 8678 8679 8684                                                      
CONECT 8678 8677 8691 8692 8693                                                 
CONECT 8679 8672 8677 8694                                                      
CONECT 8680 8673 8695                                                           
CONECT 8681 8674 8697                                                           
CONECT 8682 8671 8675                                                           
CONECT 8683 8676 8696                                                           
CONECT 8684 8677                                                                
CONECT 8685 8672                                                                
CONECT 8686 8673                                                                
CONECT 8687 8674                                                                
CONECT 8688 8675                                                                
CONECT 8689 8676                                                                
CONECT 8690 8676                                                                
CONECT 8691 8678                                                                
CONECT 8692 8678                                                                
CONECT 8693 8678                                                                
CONECT 8694 8679                                                                
CONECT 8695 8680                                                                
CONECT 8696 8683                                                                
CONECT 8697 8681 8698 8708                                                      
CONECT 8698 8697 8699 8705 8711                                                 
CONECT 8699 8698 8700 8706 8712                                                 
CONECT 8700 8699 8701 8707 8713                                                 
CONECT 8701 8700 8702 8708 8714                                                 
CONECT 8702 8701 8709 8715 8716                                                 
CONECT 8703 8704 8705 8710                                                      
CONECT 8704 8703 8717 8718 8719                                                 
CONECT 8705 8698 8703 8720                                                      
CONECT 8706 8699 8721                                                           
CONECT 8707 8700 8723                                                           
CONECT 8708 8697 8701                                                           
CONECT 8709 8702 8722                                                           
CONECT 8710 8703                                                                
CONECT 8711 8698                                                                
CONECT 8712 8699                                                                
CONECT 8713 8700                                                                
CONECT 8714 8701                                                                
CONECT 8715 8702                                                                
CONECT 8716 8702                                                                
CONECT 8717 8704                                                                
CONECT 8718 8704                                                                
CONECT 8719 8704                                                                
CONECT 8720 8705                                                                
CONECT 8721 8706                                                                
CONECT 8722 8709                                                                
CONECT 8723 8707 8724 8732                                                      
CONECT 8724 8723 8725 8729 8734                                                 
CONECT 8725 8724 8726 8730 8735                                                 
CONECT 8726 8725 8727 8731 8736                                                 
CONECT 8727 8726 8728 8732 8737                                                 
CONECT 8728 8727 8733 8738 8739                                                 
CONECT 8729 8724 8740                                                           
CONECT 8730 8725 8743                                                           
CONECT 8731 8726 8741                                                           
CONECT 8732 8723 8727                                                           
CONECT 8733 8728 8742                                                           
CONECT 8734 8724                                                                
CONECT 8735 8725                                                                
CONECT 8736 8726                                                                
CONECT 8737 8727                                                                
CONECT 8738 8728                                                                
CONECT 8739 8728                                                                
CONECT 8740 8729                                                                
CONECT 8741 8731                                                                
CONECT 8742 8733                                                                
CONECT 8743 8730 8744 8752                                                      
CONECT 8744 8743 8745 8749 8754                                                 
CONECT 8745 8744 8746 8750 8755                                                 
CONECT 8746 8745 8747 8751 8756                                                 
CONECT 8747 8746 8748 8752 8757                                                 
CONECT 8748 8747 8753 8758 8759                                                 
CONECT 8749 8744 8763                                                           
CONECT 8750 8745 8760                                                           
CONECT 8751 8746 8761                                                           
CONECT 8752 8743 8747                                                           
CONECT 8753 8748 8762                                                           
CONECT 8754 8744                                                                
CONECT 8755 8745                                                                
CONECT 8756 8746                                                                
CONECT 8757 8747                                                                
CONECT 8758 8748                                                                
CONECT 8759 8748                                                                
CONECT 8760 8750                                                                
CONECT 8761 8751                                                                
CONECT 8762 8753                                                                
CONECT 8763 8749 8764 8772                                                      
CONECT 8764 8763 8765 8769 8774                                                 
CONECT 8765 8764 8766 8770 8775                                                 
CONECT 8766 8765 8767 8771 8776                                                 
CONECT 8767 8766 8768 8772 8777                                                 
CONECT 8768 8767 8773 8778 8779                                                 
CONECT 8769 8764 8783                                                           
CONECT 8770 8765 8780                                                           
CONECT 8771 8766 8781                                                           
CONECT 8772 8763 8767                                                           
CONECT 8773 8768 8782                                                           
CONECT 8774 8764                                                                
CONECT 8775 8765                                                                
CONECT 8776 8766                                                                
CONECT 8777 8767                                                                
CONECT 8778 8768                                                                
CONECT 8779 8768                                                                
CONECT 8780 8770                                                                
CONECT 8781 8771                                                                
CONECT 8782 8773                                                                
CONECT 8783 8769 8784 8792                                                      
CONECT 8784 8783 8785 8789 8794                                                 
CONECT 8785 8784 8786 8790 8795                                                 
CONECT 8786 8785 8787 8791 8796                                                 
CONECT 8787 8786 8788 8792 8797                                                 
CONECT 8788 8787 8793 8798 8799                                                 
CONECT 8789 8784 8800                                                           
CONECT 8790 8785 8801                                                           
CONECT 8791 8786 8802                                                           
CONECT 8792 8783 8787                                                           
CONECT 8793 8788 8803                                                           
CONECT 8794 8784                                                                
CONECT 8795 8785                                                                
CONECT 8796 8786                                                                
CONECT 8797 8787                                                                
CONECT 8798 8788                                                                
CONECT 8799 8788                                                                
CONECT 8800 8789                                                                
CONECT 8801 8790                                                                
CONECT 8802 8791                                                                
CONECT 8803 8793                                                                
CONECT 8804 3269 8805 8815                                                      
CONECT 8805 8804 8806 8812 8818                                                 
CONECT 8806 8805 8807 8813 8819                                                 
CONECT 8807 8806 8808 8814 8820                                                 
CONECT 8808 8807 8809 8815 8821                                                 
CONECT 8809 8808 8816 8822 8823                                                 
CONECT 8810 8811 8812 8817                                                      
CONECT 8811 8810 8824 8825 8826                                                 
CONECT 8812 8805 8810 8827                                                      
CONECT 8813 8806 8828                                                           
CONECT 8814 8807 8830                                                           
CONECT 8815 8804 8808                                                           
CONECT 8816 8809 8829                                                           
CONECT 8817 8810                                                                
CONECT 8818 8805                                                                
CONECT 8819 8806                                                                
CONECT 8820 8807                                                                
CONECT 8821 8808                                                                
CONECT 8822 8809                                                                
CONECT 8823 8809                                                                
CONECT 8824 8811                                                                
CONECT 8825 8811                                                                
CONECT 8826 8811                                                                
CONECT 8827 8812                                                                
CONECT 8828 8813                                                                
CONECT 8829 8816                                                                
CONECT 8830 8814 8831 8841                                                      
CONECT 8831 8830 8832 8838 8844                                                 
CONECT 8832 8831 8833 8839 8845                                                 
CONECT 8833 8832 8834 8840 8846                                                 
CONECT 8834 8833 8835 8841 8847                                                 
CONECT 8835 8834 8842 8848 8849                                                 
CONECT 8836 8837 8838 8843                                                      
CONECT 8837 8836 8850 8851 8852                                                 
CONECT 8838 8831 8836 8853                                                      
CONECT 8839 8832 8854                                                           
CONECT 8840 8833 8856                                                           
CONECT 8841 8830 8834                                                           
CONECT 8842 8835 8855                                                           
CONECT 8843 8836                                                                
CONECT 8844 8831                                                                
CONECT 8845 8832                                                                
CONECT 8846 8833                                                                
CONECT 8847 8834                                                                
CONECT 8848 8835                                                                
CONECT 8849 8835                                                                
CONECT 8850 8837                                                                
CONECT 8851 8837                                                                
CONECT 8852 8837                                                                
CONECT 8853 8838                                                                
CONECT 8854 8839                                                                
CONECT 8855 8842                                                                
CONECT 8856 8840 8857 8865                                                      
CONECT 8857 8856 8858 8862 8867                                                 
CONECT 8858 8857 8859 8863 8868                                                 
CONECT 8859 8858 8860 8864 8869                                                 
CONECT 8860 8859 8861 8865 8870                                                 
CONECT 8861 8860 8866 8871 8872                                                 
CONECT 8862 8857 8873                                                           
CONECT 8863 8858 8874                                                           
CONECT 8864 8859 8875                                                           
CONECT 8865 8856 8860                                                           
CONECT 8866 8861 8876                                                           
CONECT 8867 8857                                                                
CONECT 8868 8858                                                                
CONECT 8869 8859                                                                
CONECT 8870 8860                                                                
CONECT 8871 8861                                                                
CONECT 8872 8861                                                                
CONECT 8873 8862                                                                
CONECT 8874 8863                                                                
CONECT 8875 8864                                                                
CONECT 8876 8866                                                                
CONECT 8877 4438 8878 8888                                                      
CONECT 8878 8877 8879 8885 8891                                                 
CONECT 8879 8878 8880 8886 8892                                                 
CONECT 8880 8879 8881 8887 8893                                                 
CONECT 8881 8880 8882 8888 8894                                                 
CONECT 8882 8881 8889 8895 8896                                                 
CONECT 8883 8884 8885 8890                                                      
CONECT 8884 8883 8897 8898 8899                                                 
CONECT 8885 8878 8883 8900                                                      
CONECT 8886 8879 8901                                                           
CONECT 8887 8880 8903                                                           
CONECT 8888 8877 8881                                                           
CONECT 8889 8882 8902                                                           
CONECT 8890 8883                                                                
CONECT 8891 8878                                                                
CONECT 8892 8879                                                                
CONECT 8893 8880                                                                
CONECT 8894 8881                                                                
CONECT 8895 8882                                                                
CONECT 8896 8882                                                                
CONECT 8897 8884                                                                
CONECT 8898 8884                                                                
CONECT 8899 8884                                                                
CONECT 8900 8885                                                                
CONECT 8901 8886                                                                
CONECT 8902 8889                                                                
CONECT 8903 8887 8904 8914                                                      
CONECT 8904 8903 8905 8911 8917                                                 
CONECT 8905 8904 8906 8912 8918                                                 
CONECT 8906 8905 8907 8913 8919                                                 
CONECT 8907 8906 8908 8914 8920                                                 
CONECT 8908 8907 8915 8921 8922                                                 
CONECT 8909 8910 8911 8916                                                      
CONECT 8910 8909 8923 8924 8925                                                 
CONECT 8911 8904 8909 8926                                                      
CONECT 8912 8905 8927                                                           
CONECT 8913 8906 8929                                                           
CONECT 8914 8903 8907                                                           
CONECT 8915 8908 8928                                                           
CONECT 8916 8909                                                                
CONECT 8917 8904                                                                
CONECT 8918 8905                                                                
CONECT 8919 8906                                                                
CONECT 8920 8907                                                                
CONECT 8921 8908                                                                
CONECT 8922 8908                                                                
CONECT 8923 8910                                                                
CONECT 8924 8910                                                                
CONECT 8925 8910                                                                
CONECT 8926 8911                                                                
CONECT 8927 8912                                                                
CONECT 8928 8915                                                                
CONECT 8929 8913 8930 8938                                                      
CONECT 8930 8929 8931 8935 8940                                                 
CONECT 8931 8930 8932 8936 8941                                                 
CONECT 8932 8931 8933 8937 8942                                                 
CONECT 8933 8932 8934 8938 8943                                                 
CONECT 8934 8933 8939 8944 8945                                                 
CONECT 8935 8930 8946                                                           
CONECT 8936 8931 8947                                                           
CONECT 8937 8932 8948                                                           
CONECT 8938 8929 8933                                                           
CONECT 8939 8934 8949                                                           
CONECT 8940 8930                                                                
CONECT 8941 8931                                                                
CONECT 8942 8932                                                                
CONECT 8943 8933                                                                
CONECT 8944 8934                                                                
CONECT 8945 8934                                                                
CONECT 8946 8935                                                                
CONECT 8947 8936                                                                
CONECT 8948 8937                                                                
CONECT 8949 8939                                                                
CONECT 8950 6535 7635 7716                                                      
CONECT 8951 1434 6586 9427                                                      
CONECT 8952 2168 6622 7622 9033                                                 
CONECT 8953 1472 2140 7649 9033                                                 
CONECT 8954 8039 8089 8090 9036                                                 
CONECT 8954 9114 9332                                                           
CONECT 8955 5491 9161 9191 9439                                                 
CONECT 8955 9457 9489                                                           
CONECT 8956 5706 8957 8967                                                      
CONECT 8957 8956 8958 8964 8970                                                 
CONECT 8958 8957 8959 8965 8971                                                 
CONECT 8959 8958 8960 8966 8972                                                 
CONECT 8960 8959 8961 8967 8973                                                 
CONECT 8961 8960 8968 8974 8975                                                 
CONECT 8962 8963 8964 8969                                                      
CONECT 8963 8962 8976 8977 8978                                                 
CONECT 8964 8957 8962 8979                                                      
CONECT 8965 8958 8980                                                           
CONECT 8966 8959 8981                                                           
CONECT 8967 8956 8960                                                           
CONECT 8968 8961 8982                                                           
CONECT 8969 8962                                                                
CONECT 8970 8957                                                                
CONECT 8971 8958                                                                
CONECT 8972 8959                                                                
CONECT 8973 8960                                                                
CONECT 8974 8961                                                                
CONECT 8975 8961                                                                
CONECT 8976 8963                                                                
CONECT 8977 8963                                                                
CONECT 8978 8963                                                                
CONECT 8979 8964                                                                
CONECT 8980 8965                                                                
CONECT 8981 8966                                                                
CONECT 8982 8968                                                                
CONECT 8983 6011 8984 8994                                                      
CONECT 8984 8983 8985 8991 8997                                                 
CONECT 8985 8984 8986 8992 8998                                                 
CONECT 8986 8985 8987 8993 8999                                                 
CONECT 8987 8986 8988 8994 9000                                                 
CONECT 8988 8987 8995 9001 9002                                                 
CONECT 8989 8990 8991 8996                                                      
CONECT 8990 8989 9003 9004 9005                                                 
CONECT 8991 8984 8989 9006                                                      
CONECT 8992 8985 9007                                                           
CONECT 8993 8986 9008                                                           
CONECT 8994 8983 8987                                                           
CONECT 8995 8988 9009                                                           
CONECT 8996 8989                                                                
CONECT 8997 8984                                                                
CONECT 8998 8985                                                                
CONECT 8999 8986                                                                
CONECT 9000 8987                                                                
CONECT 9001 8988                                                                
CONECT 9002 8988                                                                
CONECT 9003 8990                                                                
CONECT 9004 8990                                                                
CONECT 9005 8990                                                                
CONECT 9006 8991                                                                
CONECT 9007 8992                                                                
CONECT 9008 8993                                                                
CONECT 9009 8995                                                                
CONECT 9010 9011 9020                                                           
CONECT 9011 9010 9012 9021 9022                                                 
CONECT 9012 9011 9013 9023 9024                                                 
CONECT 9013 9012 9014                                                           
CONECT 9014 9013 9015 9025 9026                                                 
CONECT 9015 9014 9016 9027 9028                                                 
CONECT 9016 9015 9017                                                           
CONECT 9017 9016 9018 9029 9030                                                 
CONECT 9018 9017 9019 9031 9032                                                 
CONECT 9019 9018                                                                
CONECT 9020 9010                                                                
CONECT 9021 9011                                                                
CONECT 9022 9011                                                                
CONECT 9023 9012                                                                
CONECT 9024 9012                                                                
CONECT 9025 9014                                                                
CONECT 9026 9014                                                                
CONECT 9027 9015                                                                
CONECT 9028 9015                                                                
CONECT 9029 9017                                                                
CONECT 9030 9017                                                                
CONECT 9031 9018                                                                
CONECT 9032 9018                                                                
CONECT 9033 8952 8953                                                           
CONECT 9036 8954                                                                
CONECT 9114 8954                                                                
CONECT 9161 8955                                                                
CONECT 9191 8955                                                                
CONECT 9332 8954                                                                
CONECT 9427 8951                                                                
CONECT 9439 8955                                                                
CONECT 9457 8955                                                                
CONECT 9489 8955                                                                
MASTER      363    0   30   13   32    0    0    6 5131    1  586   43          
END                                                                             



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: April 25th, 2023.