CNRS Nantes University UFIP UFIP
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***  OXIDOREDUCTASE 07-MAR-20 6M4J  ***

elNémo ID: 22082920040676049

Job options:

ID        	=	 22082920040676049
JOBID     	=	 OXIDOREDUCTASE 07-MAR-20 6M4J
USERID    	=	 martin
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                          07-MAR-20   6M4J              
TITLE     SSPA IN COMPLEX WITH CYSTEINE                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SSPA COMPLEX PROTEIN;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: VIBRIO CYCLITROPHICUS;                          
SOURCE   3 ORGANISM_TAXID: 47951;                                               
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CYSTEINE DESULFHYDRASE, OXIDOREDUCTASE                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.LIU,H.GAO                                                           
REVDAT   2   13-MAY-20 6M4J    1       JRNL                                     
REVDAT   1   22-APR-20 6M4J    0                                                
JRNL        AUTH   L.LIU,S.JIANG,M.XING,C.CHEN,C.LAI,N.LI,G.LIU,D.WU,H.GAO,     
JRNL        AUTH 2 L.HONG,P.TAN,S.CHEN,Z.DENG,G.WU,L.WANG                       
JRNL        TITL   STRUCTURAL ANALYSIS OF AN L-CYSTEINE DESULFURASE FROM AN SSP 
JRNL        TITL 2 DNA PHOSPHOROTHIOATION SYSTEM.                               
JRNL        REF    MBIO                          V.  11       2020              
JRNL        REFN                   ESSN 2150-7511                               
JRNL        PMID   32345643                                                     
JRNL        DOI    10.1128/MBIO.00488-20                                        
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 114.54                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 68787                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.167                           
REMARK   3   R VALUE            (WORKING SET) : 0.166                           
REMARK   3   FREE R VALUE                     : 0.190                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3655                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4640                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.09                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2070                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 248                          
REMARK   3   BIN FREE R VALUE                    : 0.2380                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5297                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 44                                      
REMARK   3   SOLVENT ATOMS            : 863                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.16                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.42000                                             
REMARK   3    B22 (A**2) : -1.42000                                             
REMARK   3    B33 (A**2) : 2.13000                                              
REMARK   3    B12 (A**2) : -0.71000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.219         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.106         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.071         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.106         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.953                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5556 ; 0.012 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7573 ; 1.765 ; 1.962       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   728 ; 6.871 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   244 ;37.282 ;24.918       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   924 ;17.076 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    25 ;20.600 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   859 ; 0.144 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4239 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  5556 ; 1.973 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):    57 ;30.401 ; 5.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  6236 ;16.977 ; 5.000       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : NULL                            
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 0                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT THERMAL      1   NULL (A**2):    537 ; 3.240 ; 0.500         
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 6M4J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-MAR-20.                  
REMARK 100 THE DEPOSITION ID IS D_1300016070.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-APR-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 173                                
REMARK 200  PH                             : 6.5-7.5                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9789                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 2M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 72776                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 115.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 12.50                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 5.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.84                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 3VAX                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.05                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8M AMMONIUM CITRATE, PH 7.0, VAPOR     
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 287.15K                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/2                                            
REMARK 290       6555   X-Y,X,Z+1/2                                             
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z                                              
REMARK 290      10555   -Y,-X,-Z+1/2                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/2                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
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       76.31800            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       76.31800            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       76.31800            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       76.31800            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       76.31800            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       76.31800            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   2  0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       76.31800            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 921  LIES ON A SPECIAL POSITION.                          
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     MET A     1                                                      
REMARK 465     MET B     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     THR A   2    OG1  CG2                                            
REMARK 470     GLN A 261    CG   CD   OE1  NE2                                  
REMARK 470     THR B   2    OG1  CG2                                            
REMARK 470     SER B 256    OG                                                  
REMARK 470     GLU B 257    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 261    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   CB   ASN B   293     O    HOH B   503              1.69            
REMARK 500   CB   CYS B    68     O    HOH B   784              1.74            
REMARK 500   O    HOH A   798     O    HOH A   883              1.77            
REMARK 500   O    HOH B   771     O    HOH B   828              1.78            
REMARK 500   O    HOH B   504     O    HOH B   513              1.78            
REMARK 500   O    HOH B   551     O    HOH B   840              1.85            
REMARK 500   O    HOH A   729     O    HOH A   846              1.85            
REMARK 500   OD1  ASN A    44     O    HOH A   501              1.90            
REMARK 500   O    HOH A   615     O    HOH A   802              1.91            
REMARK 500   O    HOH A   874     O    HOH A   899              1.96            
REMARK 500   SG   CYS B    68     O    HOH B   784              1.96            
REMARK 500   O    HOH B   512     O    HOH B   673              1.97            
REMARK 500   O    HOH A   511     O    HOH A   784              2.01            
REMARK 500   O    HOH A   617     O    HOH A   862              2.01            
REMARK 500   O    HOH B   773     O    HOH B   860              2.04            
REMARK 500   O    HOH A   875     O    HOH A   887              2.05            
REMARK 500   O    HOH A   637     O    HOH A   852              2.06            
REMARK 500   O    HOH B   793     O    HOH B   832              2.07            
REMARK 500   O    HOH B   508     O    HOH B   814              2.08            
REMARK 500   O    HOH B   526     O    HOH B   792              2.10            
REMARK 500   O    GLN B   310     O    HOH B   501              2.10            
REMARK 500   O    HOH B   735     O    HOH B   887              2.12            
REMARK 500   CB   GLU B   159     CE   MET B   190              2.15            
REMARK 500   O    HOH A   508     O    HOH A   887              2.17            
REMARK 500   OD2  ASP B    55     O    HOH B   502              2.18            
REMARK 500   O    HOH B   523     O    HOH B   695              2.18            
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 B   784     O    HOH B   784    12555     1.79            
REMARK 500   O    HOH A   536     O    HOH A   772     8555     2.09            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ASP A  55   CB    ASP A  55   CG     -0.145                       
REMARK 500    GLU B  19   CG    GLU B  19   CD     -0.108                       
REMARK 500    ASP B  55   CB    ASP B  55   CG     -0.140                       
REMARK 500    SER B 259   CB    SER B 259   OG     -0.116                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A  55   CB  -  CG  -  OD2 ANGL. DEV. = -14.0 DEGREES          
REMARK 500    THR A 144   CB  -  CA  -  C   ANGL. DEV. = -17.7 DEGREES          
REMARK 500    ASP A 184   CB  -  CG  -  OD2 ANGL. DEV. =  -8.8 DEGREES          
REMARK 500    SER A 259   N   -  CA  -  C   ANGL. DEV. = -26.6 DEGREES          
REMARK 500    MET A 317   CG  -  SD  -  CE  ANGL. DEV. = -10.1 DEGREES          
REMARK 500    GLU B  19   OE1 -  CD  -  OE2 ANGL. DEV. =  14.3 DEGREES          
REMARK 500    GLU B  19   CG  -  CD  -  OE1 ANGL. DEV. = -12.0 DEGREES          
REMARK 500    ASP B  55   OD1 -  CG  -  OD2 ANGL. DEV. =  13.2 DEGREES          
REMARK 500    ASP B  55   CB  -  CG  -  OD2 ANGL. DEV. =  -7.9 DEGREES          
REMARK 500    ARG B 336   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    ARG B 336   NE  -  CZ  -  NH2 ANGL. DEV. =   3.8 DEGREES          
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    GLN A  25      -61.02    -91.10                                   
REMARK 500    LYS A  89     -142.56     59.74                                   
REMARK 500    CYS A 181      -36.45     76.17                                   
REMARK 500    ALA A 260     -135.03      4.14                                   
REMARK 500    THR A 263       13.96    -69.75                                   
REMARK 500    PHE A 265      -63.67     52.70                                   
REMARK 500    LYS B  89     -143.82     58.35                                   
REMARK 500    CYS B 181      -33.75     76.81                                   
REMARK 500    SER B 256      149.71    174.11                                   
REMARK 500    GLU B 257      -97.26    -71.59                                   
REMARK 500    ALA B 258      104.31     64.82                                   
REMARK 500    PHE B 265      -56.68     26.80                                   
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 ALA A  258     SER A  259                  -59.95                    
REMARK 500 SER A  259     ALA A  260                 -123.45                    
REMARK 500 THR B  263     GLU B  264                 -143.23                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 919        DISTANCE =  6.02 ANGSTROMS                       
REMARK 525    HOH A 920        DISTANCE =  6.02 ANGSTROMS                       
REMARK 525    HOH A 921        DISTANCE =  6.04 ANGSTROMS                       
REMARK 525    HOH A 922        DISTANCE =  6.05 ANGSTROMS                       
REMARK 525    HOH A 923        DISTANCE =  6.26 ANGSTROMS                       
REMARK 525    HOH A 924        DISTANCE =  6.34 ANGSTROMS                       
REMARK 525    HOH A 925        DISTANCE =  6.73 ANGSTROMS                       
REMARK 525    HOH A 926        DISTANCE =  7.03 ANGSTROMS                       
REMARK 525    HOH A 927        DISTANCE =  7.26 ANGSTROMS                       
REMARK 525    HOH A 928        DISTANCE =  7.59 ANGSTROMS                       
REMARK 525    HOH B 932        DISTANCE =  6.16 ANGSTROMS                       
REMARK 525    HOH B 933        DISTANCE =  6.23 ANGSTROMS                       
REMARK 525    HOH B 934        DISTANCE =  6.25 ANGSTROMS                       
REMARK 525    HOH B 935        DISTANCE =  9.22 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PLP A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CYS A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CYS B 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PLP B 401 and LYS B    
REMARK 800  201                                                                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE SEQUENCE HAS BEEN DEPOSITED TO NCBI WITH ACCESSION CODE WP_      
REMARK 999 016789103.1. AND C314S MUTATION WAS INTRODUCED.                      
DBREF  6M4J A    1   348  PDB    6M4J     6M4J             1    348             
DBREF  6M4J B    1   348  PDB    6M4J     6M4J             1    348             
SEQRES   1 A  348  MET THR LYS TYR PHE ASP TYR ALA ALA SER THR PRO VAL          
SEQRES   2 A  348  ALA LYS GLY VAL LEU GLU SER MET LYS PRO TRP GLN SER          
SEQRES   3 A  348  ASP SER PHE ALA ASN PRO SER ALA ALA HIS ILE GLU ALA          
SEQRES   4 A  348  GLU LYS ALA LEU ASN ALA ILE LYS GLN ALA ARG GLU ILE          
SEQRES   5 A  348  ILE ALA ASP THR LEU GLY ALA MET PRO SER GLU ILE VAL          
SEQRES   6 A  348  PHE THR CYS GLY ALA SER GLU SER ASN ASN LEU ALA ILE          
SEQRES   7 A  348  LYS GLY LEU ALA PHE LYS ARG LEU GLU GLU LYS GLY HIS          
SEQRES   8 A  348  LEU ILE THR SER SER ILE GLU HIS LYS CYS VAL LEU ASN          
SEQRES   9 A  348  THR CYS GLY PHE LEU GLU SER ILE GLY PHE ASP VAL THR          
SEQRES  10 A  348  TYR LEU THR PRO LYS ALA SER GLY LEU ILE SER ALA GLN          
SEQRES  11 A  348  GLN VAL GLU GLU ALA ILE ARG PRO ASN THR PHE LEU ILE          
SEQRES  12 A  348  THR ILE HIS HIS VAL ASN ASN GLU LEU GLY THR VAL GLN          
SEQRES  13 A  348  PRO ILE GLU ASP ILE GLY ASN VAL ALA PHE GLU HIS ASP          
SEQRES  14 A  348  ILE PRO PHE HIS THR ASP ALA ALA GLN SER PHE CYS LYS          
SEQRES  15 A  348  LEU ASP ILE ASP VAL ASP ASP MET ASN ILE ASP MET LEU          
SEQRES  16 A  348  SER LEU SER GLY HIS LYS VAL TYR GLY PRO LYS GLY ILE          
SEQRES  17 A  348  GLY ALA LEU TYR VAL ARG ASP ALA ARG ASN SER GLU LEU          
SEQRES  18 A  348  VAL PRO LEU ILE HIS GLY GLY GLY GLN GLU LEU GLY LEU          
SEQRES  19 A  348  ARG GLY GLY THR SER PRO THR PRO LEU ILE VAL GLY LEU          
SEQRES  20 A  348  GLY VAL ALA VAL GLU HIS PHE PRO SER GLU ALA SER ALA          
SEQRES  21 A  348  GLN GLN THR GLU PHE GLU LYS ILE ILE ASN GLU TYR SER          
SEQRES  22 A  348  PHE SER ARG ASN SER GLY ASP ASN ALA LEU SER THR THR          
SEQRES  23 A  348  TRP ASN VAL THR PHE GLU ASN ASP ASP GLU VAL LYS ARG          
SEQRES  24 A  348  PHE THR SER GLU ARG ASN TRP LEU ILE SER GLN GLY SER          
SEQRES  25 A  348  ALA SER ASN ALA MET SER ASN THR PRO SER HIS VAL LEU          
SEQRES  26 A  348  THR ALA ILE GLY LEU SER GLU ALA GLU ALA ARG ARG THR          
SEQRES  27 A  348  TYR ARG ILE SER LEU PRO PRO TYR LYS VAL                      
SEQRES   1 B  348  MET THR LYS TYR PHE ASP TYR ALA ALA SER THR PRO VAL          
SEQRES   2 B  348  ALA LYS GLY VAL LEU GLU SER MET LYS PRO TRP GLN SER          
SEQRES   3 B  348  ASP SER PHE ALA ASN PRO SER ALA ALA HIS ILE GLU ALA          
SEQRES   4 B  348  GLU LYS ALA LEU ASN ALA ILE LYS GLN ALA ARG GLU ILE          
SEQRES   5 B  348  ILE ALA ASP THR LEU GLY ALA MET PRO SER GLU ILE VAL          
SEQRES   6 B  348  PHE THR CYS GLY ALA SER GLU SER ASN ASN LEU ALA ILE          
SEQRES   7 B  348  LYS GLY LEU ALA PHE LYS ARG LEU GLU GLU LYS GLY HIS          
SEQRES   8 B  348  LEU ILE THR SER SER ILE GLU HIS LYS CYS VAL LEU ASN          
SEQRES   9 B  348  THR CYS GLY PHE LEU GLU SER ILE GLY PHE ASP VAL THR          
SEQRES  10 B  348  TYR LEU THR PRO LYS ALA SER GLY LEU ILE SER ALA GLN          
SEQRES  11 B  348  GLN VAL GLU GLU ALA ILE ARG PRO ASN THR PHE LEU ILE          
SEQRES  12 B  348  THR ILE HIS HIS VAL ASN ASN GLU LEU GLY THR VAL GLN          
SEQRES  13 B  348  PRO ILE GLU ASP ILE GLY ASN VAL ALA PHE GLU HIS ASP          
SEQRES  14 B  348  ILE PRO PHE HIS THR ASP ALA ALA GLN SER PHE CYS LYS          
SEQRES  15 B  348  LEU ASP ILE ASP VAL ASP ASP MET ASN ILE ASP MET LEU          
SEQRES  16 B  348  SER LEU SER GLY HIS LYS VAL TYR GLY PRO LYS GLY ILE          
SEQRES  17 B  348  GLY ALA LEU TYR VAL ARG ASP ALA ARG ASN SER GLU LEU          
SEQRES  18 B  348  VAL PRO LEU ILE HIS GLY GLY GLY GLN GLU LEU GLY LEU          
SEQRES  19 B  348  ARG GLY GLY THR SER PRO THR PRO LEU ILE VAL GLY LEU          
SEQRES  20 B  348  GLY VAL ALA VAL GLU HIS PHE PRO SER GLU ALA SER ALA          
SEQRES  21 B  348  GLN GLN THR GLU PHE GLU LYS ILE ILE ASN GLU TYR SER          
SEQRES  22 B  348  PHE SER ARG ASN SER GLY ASP ASN ALA LEU SER THR THR          
SEQRES  23 B  348  TRP ASN VAL THR PHE GLU ASN ASP ASP GLU VAL LYS ARG          
SEQRES  24 B  348  PHE THR SER GLU ARG ASN TRP LEU ILE SER GLN GLY SER          
SEQRES  25 B  348  ALA SER ASN ALA MET SER ASN THR PRO SER HIS VAL LEU          
SEQRES  26 B  348  THR ALA ILE GLY LEU SER GLU ALA GLU ALA ARG ARG THR          
SEQRES  27 B  348  TYR ARG ILE SER LEU PRO PRO TYR LYS VAL                      
HET    PLP  A 401      15                                                       
HET    CYS  A 402       7                                                       
HET    PLP  B 401      15                                                       
HET    CYS  B 402       7                                                       
HETNAM     PLP PYRIDOXAL-5'-PHOSPHATE                                           
HETNAM     CYS CYSTEINE                                                         
HETSYN     PLP VITAMIN B6 PHOSPHATE                                             
FORMUL   3  PLP    2(C8 H10 N O6 P)                                             
FORMUL   4  CYS    2(C3 H7 N O2 S)                                              
FORMUL   7  HOH   *863(H2 O)                                                    
HELIX    1 AA1 ALA A   14  LYS A   22  1                                   9    
HELIX    2 AA2 PRO A   23  GLN A   25  5                                   3    
HELIX    3 AA3 HIS A   36  GLY A   58  1                                  23    
HELIX    4 AA4 MET A   60  SER A   62  5                                   3    
HELIX    5 AA5 GLY A   69  PHE A   83  1                                  15    
HELIX    6 AA6 HIS A   99  ILE A  112  1                                  14    
HELIX    7 AA7 SER A  128  ILE A  136  1                                   9    
HELIX    8 AA8 PRO A  157  ASP A  169  1                                  13    
HELIX    9 AA9 HIS A  200  VAL A  202  5                                   3    
HELIX   10 AB1 ASP A  215  SER A  219  5                                   5    
HELIX   11 AB2 GLN A  230  LEU A  234  5                                   5    
HELIX   12 AB3 PRO A  240  HIS A  253  1                                  14    
HELIX   13 AB4 ALA A  260  GLU A  264  5                                   5    
HELIX   14 AB5 ILE A  268  TYR A  272  5                                   5    
HELIX   15 AB6 ASN A  293  ARG A  304  1                                  12    
HELIX   16 AB7 SER A  312  ASN A  319  1                                   8    
HELIX   17 AB8 SER A  322  ILE A  328  1                                   7    
HELIX   18 AB9 SER A  331  ARG A  337  1                                   7    
HELIX   19 AC1 ALA B   14  LYS B   22  1                                   9    
HELIX   20 AC2 PRO B   23  GLN B   25  5                                   3    
HELIX   21 AC3 HIS B   36  GLY B   58  1                                  23    
HELIX   22 AC4 MET B   60  SER B   62  5                                   3    
HELIX   23 AC5 GLY B   69  PHE B   83  1                                  15    
HELIX   24 AC6 HIS B   99  ILE B  112  1                                  14    
HELIX   25 AC7 SER B  128  ILE B  136  1                                   9    
HELIX   26 AC8 PRO B  157  HIS B  168  1                                  12    
HELIX   27 AC9 HIS B  200  VAL B  202  5                                   3    
HELIX   28 AD1 ASP B  215  SER B  219  5                                   5    
HELIX   29 AD2 GLN B  230  LEU B  234  5                                   5    
HELIX   30 AD3 PRO B  240  HIS B  253  1                                  14    
HELIX   31 AD4 ILE B  268  TYR B  272  5                                   5    
HELIX   32 AD5 ASN B  293  ARG B  304  1                                  12    
HELIX   33 AD6 SER B  312  ASN B  319  1                                   8    
HELIX   34 AD7 SER B  322  ILE B  328  1                                   7    
HELIX   35 AD8 SER B  331  ARG B  337  1                                   7    
SHEET    1 AA1 7 ILE A  64  THR A  67  0                                        
SHEET    2 AA1 7 GLY A 209  VAL A 213 -1  O  GLY A 209   N  THR A  67           
SHEET    3 AA1 7 MET A 194  SER A 198 -1  N  LEU A 195   O  TYR A 212           
SHEET    4 AA1 7 PHE A 172  ASP A 175  1  N  THR A 174   O  SER A 196           
SHEET    5 AA1 7 THR A 140  THR A 144  1  N  ILE A 143   O  HIS A 173           
SHEET    6 AA1 7 HIS A  91  SER A  95  1  N  ILE A  93   O  THR A 144           
SHEET    7 AA1 7 ASP A 115  LEU A 119  1  O  LEU A 119   N  THR A  94           
SHEET    1 AA2 3 PHE A 274  ASN A 277  0                                        
SHEET    2 AA2 3 THR A 286  PHE A 291 -1  O  THR A 290   N  SER A 275           
SHEET    3 AA2 3 THR A 338  SER A 342 -1  O  ILE A 341   N  TRP A 287           
SHEET    1 AA3 7 ILE B  64  THR B  67  0                                        
SHEET    2 AA3 7 GLY B 209  VAL B 213 -1  O  GLY B 209   N  THR B  67           
SHEET    3 AA3 7 MET B 194  SER B 198 -1  N  LEU B 195   O  TYR B 212           
SHEET    4 AA3 7 PHE B 172  ASP B 175  1  N  THR B 174   O  SER B 196           
SHEET    5 AA3 7 THR B 140  THR B 144  1  N  ILE B 143   O  HIS B 173           
SHEET    6 AA3 7 HIS B  91  SER B  95  1  N  ILE B  93   O  THR B 144           
SHEET    7 AA3 7 ASP B 115  LEU B 119  1  O  LEU B 119   N  THR B  94           
SHEET    1 AA4 3 PHE B 274  ASN B 277  0                                        
SHEET    2 AA4 3 THR B 286  PHE B 291 -1  O  THR B 290   N  SER B 275           
SHEET    3 AA4 3 THR B 338  SER B 342 -1  O  ILE B 341   N  TRP B 287           
SSBOND   1 CYS A   68    CYS A   68                          1555   8555  1.90  
LINK         NZ  LYS A 201                 C4A PLP A 401     1555   1555  1.74  
LINK         NZ  LYS B 201                 C4A PLP B 401     1555   1555  1.73  
CISPEP   1 THR A    2    LYS A    3          0        -7.58                     
CISPEP   2 THR A    2    LYS A    3          0        -8.04                     
CISPEP   3 GLU A  264    PHE A  265          0        19.89                     
CISPEP   4 THR B    2    LYS B    3          0        -7.76                     
CISPEP   5 SER B  256    GLU B  257          0        -9.19                     
CISPEP   6 GLU B  264    PHE B  265          0        25.41                     
SITE     1 AC1 18 GLY A  69  ALA A  70  SER A  71  HIS A  99                    
SITE     2 AC1 18 ASN A 150  ASP A 175  ALA A 177  GLN A 178                    
SITE     3 AC1 18 SER A 198  HIS A 200  LYS A 201  GLY A 237                    
SITE     4 AC1 18 THR A 238  HOH A 505  HOH A 601  HOH A 724                    
SITE     5 AC1 18 HOH A 725  HOH A 789                                          
SITE     1 AC2 13 ALA A   9  SER A  33  HIS A  99  ASN A 150                    
SITE     2 AC2 13 ARG A 340  HOH A 505  HOH A 536  HOH A 729                    
SITE     3 AC2 13 HOH A 744  HOH A 750  HOH A 772  HOH A 779                    
SITE     4 AC2 13 HOH A 811                                                     
SITE     1 AC3 12 ALA B   9  SER B  33  HIS B  99  ASN B 150                    
SITE     2 AC3 12 SER B 312  ARG B 340  HOH B 508  HOH B 547                    
SITE     3 AC3 12 HOH B 746  HOH B 755  HOH B 760  HOH B 814                    
SITE     1 AC4 22 ALA B   8  ALA B   9  THR B  11  GLY B  69                    
SITE     2 AC4 22 ALA B  70  SER B  71  HIS B  99  ASN B 150                    
SITE     3 AC4 22 ASP B 175  ALA B 177  GLN B 178  SER B 198                    
SITE     4 AC4 22 GLY B 199  HIS B 200  VAL B 202  TYR B 203                    
SITE     5 AC4 22 GLY B 237  THR B 238  HOH B 547  HOH B 548                    
SITE     6 AC4 22 HOH B 577  HOH B 638                                          
CRYST1  132.264  132.264  152.636  90.00  90.00 120.00 P 63 2 2     24          
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      0.007561  0.004365  0.000000        0.00000                         
SCALE2      0.000000  0.008730  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006552        0.00000                         
MTRIX1   1  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2   1  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3   1  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1   2  0.870800  0.491563  0.008509       -0.05609    1                    
MTRIX2   2 -0.491635  0.870707  0.012785       -0.02877    1                    
MTRIX3   2 -0.001124 -0.015316  0.999882      -38.62826    1                    
ATOM      1  N   THR A   2     -64.972  -9.422 -19.736  0.50 32.37           N  
ANISOU    1  N   THR A   2     4550   5311   2438    -69  -1103     54       N  
ATOM      2  CA  THR A   2     -65.622  -9.475 -21.070  0.50 30.66           C  
ANISOU    2  CA  THR A   2     4601   4948   2098     21   -827    232       C  
ATOM      3  C   THR A   2     -64.644  -9.708 -22.219  0.50 32.09           C  
ANISOU    3  C   THR A   2     4561   5133   2496     98   -604    323       C  
ATOM      4  O   THR A   2     -64.587  -8.915 -23.171  0.50 35.92           O  
ANISOU    4  O   THR A   2     5275   5680   2692    311   -316    637       O  
ATOM      5  CB  THR A   2     -66.437  -8.210 -21.309  0.50 34.80           C  
ANISOU    5  CB  THR A   2     5027   5094   3099    158   -984    235       C  
ATOM      6  N   LYS A   3     -63.846 -10.761 -22.110  1.00 27.93           N  
ANISOU    6  N   LYS A   3     4220   5157   1234     26   -353     79       N  
ATOM      7  CA ALYS A   3     -63.797 -11.530 -20.901  0.50 25.73           C  
ANISOU    7  CA ALYS A   3     3871   4300   1602    -81   -793     25       C  
ATOM      8  CA BLYS A   3     -63.775 -11.542 -20.899  0.50 25.69           C  
ANISOU    8  CA BLYS A   3     3855   4305   1600   -113   -770     19       C  
ATOM      9  C   LYS A   3     -62.351 -11.584 -20.419  1.00 23.27           C  
ANISOU    9  C   LYS A   3     3620   3978   1242    -74   -417   -104       C  
ATOM     10  O   LYS A   3     -61.398 -11.797 -21.163  1.00 22.31           O  
ANISOU   10  O   LYS A   3     3436   3639   1401   -230   -343   -114       O  
ATOM     11  CB ALYS A   3     -64.413 -12.925 -21.096  0.50 29.12           C  
ANISOU   11  CB ALYS A   3     4357   4371   2333   -225   -437     39       C  
ATOM     12  CB BLYS A   3     -64.269 -12.964 -21.118  0.50 28.31           C  
ANISOU   12  CB BLYS A   3     4307   4349   2099   -238   -377     83       C  
ATOM     13  CG ALYS A   3     -64.979 -13.568 -19.830  0.50 28.16           C  
ANISOU   13  CG ALYS A   3     4248   4728   1722   -298   -417   -535       C  
ATOM     14  CG BLYS A   3     -64.876 -13.631 -19.888  0.50 28.06           C  
ANISOU   14  CG BLYS A   3     4302   4839   1518   -267   -356   -339       C  
ATOM     15  CD ALYS A   3     -65.993 -12.676 -19.125  0.50 29.18           C  
ANISOU   15  CD ALYS A   3     4165   4545   2375    -87   -757   -604       C  
ATOM     16  CD BLYS A   3     -65.922 -12.730 -19.241  0.50 29.50           C  
ANISOU   16  CD BLYS A   3     4350   4944   1915    -40   -451   -231       C  
ATOM     17  CE ALYS A   3     -65.573 -12.453 -17.679  0.50 26.74           C  
ANISOU   17  CE ALYS A   3     4057   3991   2111   -492   -160   -752       C  
ATOM     18  CE BLYS A   3     -66.897 -13.514 -18.378  0.50 29.80           C  
ANISOU   18  CE BLYS A   3     4418   5348   1553    -32   -243   -336       C  
ATOM     19  NZ ALYS A   3     -64.944 -11.124 -17.448  0.50 20.41           N  
ANISOU   19  NZ ALYS A   3     3292   3926    537   -181   -612   -729       N  
ATOM     20  NZ BLYS A   3     -67.930 -14.192 -19.208  0.50 31.83           N  
ANISOU   20  NZ BLYS A   3     4784   5241   2069   -208   -376   -541       N  
ATOM     21  N   TYR A   4     -62.238 -11.506 -19.121  1.00 21.93           N  
ANISOU   21  N   TYR A   4     3247   3811   1271   -331   -454   -226       N  
ATOM     22  CA  TYR A   4     -60.935 -11.368 -18.493  1.00 19.12           C  
ANISOU   22  CA  TYR A   4     3017   3251    997   -179   -228   -349       C  
ATOM     23  C   TYR A   4     -60.303 -12.721 -18.261  1.00 18.84           C  
ANISOU   23  C   TYR A   4     3088   3141    930   -321    -53   -151       C  
ATOM     24  O   TYR A   4     -60.836 -13.536 -17.528  1.00 19.93           O  
ANISOU   24  O   TYR A   4     3221   3327   1022   -476   -146    -43       O  
ATOM     25  CB  TYR A   4     -61.131 -10.646 -17.156  1.00 18.74           C  
ANISOU   25  CB  TYR A   4     2777   3238   1104   -319   -193   -465       C  
ATOM     26  CG  TYR A   4     -59.893 -10.225 -16.385  1.00 17.14           C  
ANISOU   26  CG  TYR A   4     2618   3077    816   -291    -62   -284       C  
ATOM     27  CD1 TYR A   4     -59.285 -11.079 -15.481  1.00 16.99           C  
ANISOU   27  CD1 TYR A   4     2744   3036    675   -356     39   -223       C  
ATOM     28  CD2 TYR A   4     -59.376  -8.961 -16.532  1.00 17.54           C  
ANISOU   28  CD2 TYR A   4     2578   3012   1072   -266    -96   -319       C  
ATOM     29  CE1 TYR A   4     -58.174 -10.684 -14.790  1.00 16.57           C  
ANISOU   29  CE1 TYR A   4     2757   2782    755   -277    -61   -147       C  
ATOM     30  CE2 TYR A   4     -58.269  -8.566 -15.831  1.00 15.51           C  
ANISOU   30  CE2 TYR A   4     2514   3120    259   -111     -6   -134       C  
ATOM     31  CZ  TYR A   4     -57.670  -9.433 -14.964  1.00 16.05           C  
ANISOU   31  CZ  TYR A   4     2572   2767    759   -231     10     27       C  
ATOM     32  OH  TYR A   4     -56.577  -9.039 -14.233  1.00 15.89           O  
ANISOU   32  OH  TYR A   4     2616   2571    848    -64   -156    138       O  
ATOM     33  N   PHE A   5     -59.150 -12.933 -18.869  1.00 18.54           N  
ANISOU   33  N   PHE A   5     3125   3047    872   -171    -36   -226       N  
ATOM     34  CA  PHE A   5     -58.391 -14.159 -18.679  1.00 17.47           C  
ANISOU   34  CA  PHE A   5     3105   2811    721   -410   -174    -83       C  
ATOM     35  C   PHE A   5     -56.949 -13.810 -18.312  1.00 16.95           C  
ANISOU   35  C   PHE A   5     3026   2615    798   -295   -125    -73       C  
ATOM     36  O   PHE A   5     -55.996 -14.369 -18.853  1.00 17.18           O  
ANISOU   36  O   PHE A   5     3235   2888    405   -310      8   -110       O  
ATOM     37  CB  PHE A   5     -58.400 -14.969 -19.973  1.00 19.03           C  
ANISOU   37  CB  PHE A   5     3314   2944    972   -470    -77   -323       C  
ATOM     38  CG  PHE A   5     -59.658 -15.748 -20.207  1.00 19.15           C  
ANISOU   38  CG  PHE A   5     3299   3087    887   -567    -21   -113       C  
ATOM     39  CD1 PHE A   5     -59.725 -17.071 -19.850  1.00 21.90           C  
ANISOU   39  CD1 PHE A   5     3506   3144   1670   -604   -198   -111       C  
ATOM     40  CD2 PHE A   5     -60.757 -15.162 -20.809  1.00 20.43           C  
ANISOU   40  CD2 PHE A   5     3542   3379    838   -456   -134   -170       C  
ATOM     41  CE1 PHE A   5     -60.880 -17.786 -20.072  1.00 22.65           C  
ANISOU   41  CE1 PHE A   5     3688   3209   1706   -707   -287   -147       C  
ATOM     42  CE2 PHE A   5     -61.910 -15.875 -21.043  1.00 20.78           C  
ANISOU   42  CE2 PHE A   5     3742   3511    640   -513   -439   -184       C  
ATOM     43  CZ  PHE A   5     -61.972 -17.201 -20.682  1.00 20.93           C  
ANISOU   43  CZ  PHE A   5     3845   3499    607   -781   -445   -318       C  
ATOM     44  N   ASP A   6     -56.791 -12.858 -17.405  1.00 15.79           N  
ANISOU   44  N   ASP A   6     2880   2630    489   -296    -76      0       N  
ATOM     45  CA  ASP A   6     -55.471 -12.371 -17.044  1.00 16.28           C  
ANISOU   45  CA  ASP A   6     2839   2618    729   -242    -29     29       C  
ATOM     46  C   ASP A   6     -55.298 -12.405 -15.538  1.00 15.77           C  
ANISOU   46  C   ASP A   6     2886   2360    744   -180    -85   -104       C  
ATOM     47  O   ASP A   6     -54.738 -11.483 -14.961  1.00 14.90           O  
ANISOU   47  O   ASP A   6     2736   2458    464   -216     81   -103       O  
ATOM     48  CB  ASP A   6     -55.319 -10.943 -17.542  1.00 16.07           C  
ANISOU   48  CB  ASP A   6     2873   2567    665   -156   -130      7       C  
ATOM     49  CG  ASP A   6     -53.882 -10.573 -17.826  1.00 16.53           C  
ANISOU   49  CG  ASP A   6     3003   2420    858   -196    -60    141       C  
ATOM     50  OD1 ASP A   6     -53.536  -9.430 -17.866  1.00 15.96           O  
ANISOU   50  OD1 ASP A   6     2988   2320    755   -122   -280     84       O  
ATOM     51  OD2 ASP A   6     -53.027 -11.393 -17.977  1.00 16.74           O  
ANISOU   51  OD2 ASP A   6     3196   2258    904   -104   -193    110       O  
ATOM     52  N   TYR A   7     -55.807 -13.458 -14.904  1.00 15.78           N  
ANISOU   52  N   TYR A   7     2773   2505    715   -234    -45    -40       N  
ATOM     53  CA  TYR A   7     -55.724 -13.569 -13.461  1.00 15.58           C  
ANISOU   53  CA  TYR A   7     2799   2403    715   -346    -68   -126       C  
ATOM     54  C   TYR A   7     -54.297 -13.662 -12.923  1.00 15.80           C  
ANISOU   54  C   TYR A   7     2814   2429    759   -220    -84   -116       C  
ATOM     55  O   TYR A   7     -54.092 -13.302 -11.788  1.00 15.85           O  
ANISOU   55  O   TYR A   7     2886   2390    744   -178     19   -154       O  
ATOM     56  CB  TYR A   7     -56.607 -14.719 -12.905  1.00 16.81           C  
ANISOU   56  CB  TYR A   7     2946   2609    830   -451    -66     11       C  
ATOM     57  CG  TYR A   7     -58.077 -14.556 -13.192  1.00 17.94           C  
ANISOU   57  CG  TYR A   7     2933   2911    970   -506      4   -141       C  
ATOM     58  CD1 TYR A   7     -58.635 -15.065 -14.358  1.00 19.09           C  
ANISOU   58  CD1 TYR A   7     3122   3101   1028   -461   -201    -97       C  
ATOM     59  CD2 TYR A   7     -58.908 -13.866 -12.318  1.00 18.13           C  
ANISOU   59  CD2 TYR A   7     2933   2766   1189   -434     18    -62       C  
ATOM     60  CE1 TYR A   7     -59.967 -14.902 -14.646  1.00 19.66           C  
ANISOU   60  CE1 TYR A   7     3068   3132   1267   -595      1     33       C  
ATOM     61  CE2 TYR A   7     -60.254 -13.698 -12.610  1.00 20.36           C  
ANISOU   61  CE2 TYR A   7     3007   3196   1533   -429   -174    -95       C  
ATOM     62  CZ  TYR A   7     -60.775 -14.222 -13.777  1.00 21.14           C  
ANISOU   62  CZ  TYR A   7     3335   3137   1559   -550    -50   -232       C  
ATOM     63  OH  TYR A   7     -62.116 -14.035 -14.082  1.00 24.43           O  
ANISOU   63  OH  TYR A   7     3444   3483   2352   -438   -127   -377       O  
ATOM     64  N   ALA A   8     -53.317 -14.099 -13.705  1.00 14.92           N  
ANISOU   64  N   ALA A   8     2946   2197    524   -265     -5    -88       N  
ATOM     65  CA  ALA A   8     -51.970 -14.191 -13.201  1.00 15.54           C  
ANISOU   65  CA  ALA A   8     2929   2294    678   -218    -54   -151       C  
ATOM     66  C   ALA A   8     -51.406 -12.806 -12.998  1.00 15.28           C  
ANISOU   66  C   ALA A   8     2985   2177    642   -144     64    -25       C  
ATOM     67  O   ALA A   8     -50.443 -12.635 -12.262  1.00 16.48           O  
ANISOU   67  O   ALA A   8     2983   2302    975   -272     26    -89       O  
ATOM     68  CB  ALA A   8     -51.098 -14.962 -14.161  1.00 16.16           C  
ANISOU   68  CB  ALA A   8     3094   2324    722   -167    -42   -176       C  
ATOM     69  N   ALA A   9     -52.015 -11.826 -13.658  1.00 14.66           N  
ANISOU   69  N   ALA A   9     2879   2103    586   -120     99   -127       N  
ATOM     70  CA  ALA A   9     -51.604 -10.424 -13.503  1.00 14.27           C  
ANISOU   70  CA  ALA A   9     2814   2071    537   -169    190    114       C  
ATOM     71  C   ALA A   9     -52.284  -9.712 -12.343  1.00 14.52           C  
ANISOU   71  C   ALA A   9     2670   2194    649   -139     77    -55       C  
ATOM     72  O   ALA A   9     -51.632  -8.948 -11.631  1.00 14.70           O  
ANISOU   72  O   ALA A   9     2748   2298    537   -270    182   -113       O  
ATOM     73  CB  ALA A   9     -51.825  -9.635 -14.787  1.00 14.94           C  
ANISOU   73  CB  ALA A   9     2982   2089    603   -185     18    133       C  
ATOM     74  N   SER A  10     -53.583  -9.938 -12.165  1.00 15.03           N  
ANISOU   74  N   SER A  10     2604   2424    681    -73    143   -105       N  
ATOM     75  CA  SER A  10     -54.269  -9.492 -10.954  1.00 15.48           C  
ANISOU   75  CA  SER A  10     2727   2429    725   -120    173   -225       C  
ATOM     76  C   SER A  10     -55.631 -10.115 -10.851  1.00 15.91           C  
ANISOU   76  C   SER A  10     2740   2550    753   -178     29   -239       C  
ATOM     77  O   SER A  10     -56.173 -10.610 -11.841  1.00 15.01           O  
ANISOU   77  O   SER A  10     2661   2440    601   -116     24    -70       O  
ATOM     78  CB  SER A  10     -54.410  -7.977 -10.907  1.00 15.48           C  
ANISOU   78  CB  SER A  10     2781   2405    696    -66    250   -177       C  
ATOM     79  OG  SER A  10     -54.832  -7.596  -9.602  1.00 14.83           O  
ANISOU   79  OG  SER A  10     2779   2260    594   -107     96   -187       O  
ATOM     80  N   THR A  11     -56.198 -10.060  -9.660  1.00 16.14           N  
ANISOU   80  N   THR A  11     2699   2646    785   -124    100    -11       N  
ATOM     81  CA  THR A  11     -57.443 -10.732  -9.428  1.00 15.73           C  
ANISOU   81  CA  THR A  11     2798   2358    817   -110     25     13       C  
ATOM     82  C   THR A  11     -58.427  -9.792  -8.813  1.00 16.36           C  
ANISOU   82  C   THR A  11     2820   2536    857   -166    274     32       C  
ATOM     83  O   THR A  11     -58.070  -8.755  -8.278  1.00 15.55           O  
ANISOU   83  O   THR A  11     2846   2650    412   -250    227    150       O  
ATOM     84  CB  THR A  11     -57.278 -11.925  -8.482  1.00 15.77           C  
ANISOU   84  CB  THR A  11     2884   2389    718   -125    -80    -64       C  
ATOM     85  OG1 THR A  11     -56.729 -11.470  -7.247  1.00 15.06           O  
ANISOU   85  OG1 THR A  11     2593   2473    655    -85    -79     60       O  
ATOM     86  CG2 THR A  11     -56.332 -12.903  -9.099  1.00 16.29           C  
ANISOU   86  CG2 THR A  11     2770   2508    911    -37   -105     51       C  
ATOM     87  N   PRO A  12     -59.701 -10.156  -8.885  1.00 16.74           N  
ANISOU   87  N   PRO A  12     2867   2584    906   -157    153     41       N  
ATOM     88  CA  PRO A  12     -60.754  -9.309  -8.344  1.00 16.11           C  
ANISOU   88  CA  PRO A  12     2793   2569    759   -113     31    144       C  
ATOM     89  C   PRO A  12     -60.952  -9.484  -6.844  1.00 16.24           C  
ANISOU   89  C   PRO A  12     2837   2572    759   -232     97     47       C  
ATOM     90  O   PRO A  12     -61.021 -10.602  -6.352  1.00 17.26           O  
ANISOU   90  O   PRO A  12     3065   2584    909    -72     88     90       O  
ATOM     91  CB  PRO A  12     -61.998  -9.810  -9.069  1.00 16.67           C  
ANISOU   91  CB  PRO A  12     2862   2557    911   -299     27    341       C  
ATOM     92  CG  PRO A  12     -61.711 -11.251  -9.372  1.00 16.70           C  
ANISOU   92  CG  PRO A  12     2882   2631    830   -160     58    133       C  
ATOM     93  CD  PRO A  12     -60.214 -11.421  -9.446  1.00 16.59           C  
ANISOU   93  CD  PRO A  12     2793   2728    782   -283    -18    127       C  
ATOM     94  N   VAL A  13     -61.106  -8.387  -6.123  1.00 16.08           N  
ANISOU   94  N   VAL A  13     2776   2640    693    -63      2     18       N  
ATOM     95  CA  VAL A  13     -61.267  -8.476  -4.676  1.00 16.30           C  
ANISOU   95  CA  VAL A  13     2909   2501    781   -183    195    305       C  
ATOM     96  C   VAL A  13     -62.580  -9.157  -4.310  1.00 17.10           C  
ANISOU   96  C   VAL A  13     2802   2725    967   -181     86    224       C  
ATOM     97  O   VAL A  13     -63.637  -8.731  -4.769  1.00 16.76           O  
ANISOU   97  O   VAL A  13     2770   2895    701   -306     -2    131       O  
ATOM     98  CB  VAL A  13     -61.276  -7.079  -4.074  1.00 16.23           C  
ANISOU   98  CB  VAL A  13     2702   2645    818    -99    309    166       C  
ATOM     99  CG1 VAL A  13     -61.495  -7.143  -2.585  1.00 17.83           C  
ANISOU   99  CG1 VAL A  13     3064   2926    781   -230    187     85       C  
ATOM    100  CG2 VAL A  13     -59.956  -6.385  -4.356  1.00 16.81           C  
ANISOU  100  CG2 VAL A  13     2684   2853    847   -243    -26    161       C  
ATOM    101  N   ALA A  14     -62.505 -10.184  -3.462  1.00 16.07           N  
ANISOU  101  N   ALA A  14     2891   2574    639   -216    161     52       N  
ATOM    102  CA  ALA A  14     -63.664 -10.982  -3.071  1.00 17.95           C  
ANISOU  102  CA  ALA A  14     2918   2880   1022   -287     59    264       C  
ATOM    103  C   ALA A  14     -64.635 -10.108  -2.289  1.00 19.05           C  
ANISOU  103  C   ALA A  14     2825   3079   1333   -333    125    191       C  
ATOM    104  O   ALA A  14     -64.226  -9.153  -1.655  1.00 17.61           O  
ANISOU  104  O   ALA A  14     2747   3222    721   -182    247    171       O  
ATOM    105  CB  ALA A  14     -63.217 -12.174  -2.230  1.00 18.93           C  
ANISOU  105  CB  ALA A  14     2882   2867   1444   -216     95    405       C  
ATOM    106  N   LYS A  15     -65.923 -10.418  -2.328  1.00 19.72           N  
ANISOU  106  N   LYS A  15     2751   3290   1449   -233     89    208       N  
ATOM    107  CA  LYS A  15     -66.919  -9.601  -1.641  1.00 20.53           C  
ANISOU  107  CA  LYS A  15     2986   3613   1200   -138    175    235       C  
ATOM    108  C   LYS A  15     -66.651  -9.501  -0.153  1.00 19.71           C  
ANISOU  108  C   LYS A  15     2966   3328   1195    -75    323    103       C  
ATOM    109  O   LYS A  15     -66.803  -8.433   0.417  1.00 18.66           O  
ANISOU  109  O   LYS A  15     3096   3252    741   -209    180    241       O  
ATOM    110  CB  LYS A  15     -68.332 -10.143  -1.899  1.00 22.32           C  
ANISOU  110  CB  LYS A  15     3023   4033   1422   -288    275    245       C  
ATOM    111  CG  LYS A  15     -69.443  -9.662  -0.951  1.00 23.78           C  
ANISOU  111  CG  LYS A  15     3299   4073   1661    182    207    139       C  
ATOM    112  CD  LYS A  15     -69.910  -8.229  -1.174  1.00 23.22           C  
ANISOU  112  CD  LYS A  15     3377   4190   1255     23    -41    593       C  
ATOM    113  CE  LYS A  15     -71.229  -7.982  -0.463  1.00 26.42           C  
ANISOU  113  CE  LYS A  15     3278   4592   2166    450   -127    198       C  
ATOM    114  NZ  LYS A  15     -71.455  -6.520  -0.339  1.00 28.88           N  
ANISOU  114  NZ  LYS A  15     3843   4621   2506     77   -722     80       N  
ATOM    115  N   GLY A  16     -66.262 -10.621   0.447  1.00 19.22           N  
ANISOU  115  N   GLY A  16     2948   3355    998    -86    243    178       N  
ATOM    116  CA  GLY A  16     -65.954 -10.658   1.872  1.00 19.00           C  
ANISOU  116  CA  GLY A  16     2862   3318   1038   -414    196    161       C  
ATOM    117  C   GLY A  16     -64.759  -9.792   2.227  1.00 17.89           C  
ANISOU  117  C   GLY A  16     2781   3251    764   -160    129     48       C  
ATOM    118  O   GLY A  16     -64.721  -9.199   3.304  1.00 17.99           O  
ANISOU  118  O   GLY A  16     2934   3111    788   -194    192     72       O  
ATOM    119  N   VAL A  17     -63.789  -9.717   1.318  1.00 17.81           N  
ANISOU  119  N   VAL A  17     2720   3074    972   -257    207    369       N  
ATOM    120  CA  VAL A  17     -62.607  -8.884   1.495  1.00 17.61           C  
ANISOU  120  CA  VAL A  17     2652   3025   1012   -151    138    264       C  
ATOM    121  C   VAL A  17     -62.998  -7.411   1.482  1.00 17.86           C  
ANISOU  121  C   VAL A  17     2763   3098    923    -84    103    157       C  
ATOM    122  O   VAL A  17     -62.657  -6.664   2.388  1.00 17.01           O  
ANISOU  122  O   VAL A  17     2837   3067    557    -46    203    276       O  
ATOM    123  CB  VAL A  17     -61.555  -9.174   0.406  1.00 17.15           C  
ANISOU  123  CB  VAL A  17     2766   2859    890   -173    120    197       C  
ATOM    124  CG1 VAL A  17     -60.379  -8.203   0.506  1.00 16.81           C  
ANISOU  124  CG1 VAL A  17     2771   2865    748   -183    196    249       C  
ATOM    125  CG2 VAL A  17     -61.088 -10.624   0.495  1.00 17.43           C  
ANISOU  125  CG2 VAL A  17     2718   2820   1082   -176    145     12       C  
ATOM    126  N   LEU A  18     -63.751  -7.004   0.472  1.00 17.88           N  
ANISOU  126  N   LEU A  18     2725   3213    856   -162    161    274       N  
ATOM    127  CA  LEU A  18     -64.225  -5.642   0.445  1.00 19.08           C  
ANISOU  127  CA  LEU A  18     2987   3370    893     -1    157    263       C  
ATOM    128  C   LEU A  18     -64.996  -5.229   1.681  1.00 18.59           C  
ANISOU  128  C   LEU A  18     3053   3359    649   -201     30    164       C  
ATOM    129  O   LEU A  18     -64.749  -4.165   2.219  1.00 17.94           O  
ANISOU  129  O   LEU A  18     2833   3284    697   -232    100    242       O  
ATOM    130  CB  LEU A  18     -65.094  -5.392  -0.775  1.00 21.16           C  
ANISOU  130  CB  LEU A  18     3327   3876    835    -63     13    222       C  
ATOM    131  CG  LEU A  18     -64.716  -4.145  -1.584  1.00 26.52           C  
ANISOU  131  CG  LEU A  18     4131   3943   2002   -165   -750    707       C  
ATOM    132  CD1 LEU A  18     -65.879  -3.674  -2.461  1.00 28.70           C  
ANISOU  132  CD1 LEU A  18     4906   4375   1624    138   -964    933       C  
ATOM    133  CD2 LEU A  18     -64.139  -2.959  -0.810  1.00 29.23           C  
ANISOU  133  CD2 LEU A  18     4548   3866   2689     93   -110     47       C  
ATOM    134  N   GLU A  19     -65.953  -6.044   2.090  1.00 18.04           N  
ANISOU  134  N   GLU A  19     2851   3318    683   -200    -33     86       N  
ATOM    135  CA  GLU A  19     -66.715  -5.772   3.283  1.00 18.56           C  
ANISOU  135  CA  GLU A  19     2879   3368    804   -143     60     97       C  
ATOM    136  C   GLU A  19     -65.837  -5.596   4.502  1.00 18.17           C  
ANISOU  136  C   GLU A  19     2924   3151    827      5     35     42       C  
ATOM    137  O   GLU A  19     -66.028  -4.683   5.300  1.00 18.21           O  
ANISOU  137  O   GLU A  19     3073   3074    770   -144     45     18       O  
ATOM    138  CB  GLU A  19     -67.734  -6.886   3.513  1.00 20.21           C  
ANISOU  138  CB  GLU A  19     3052   3420   1207   -254    119    167       C  
ATOM    139  CG  GLU A  19     -68.924  -6.833   2.564  1.00 22.74           C  
ANISOU  139  CG  GLU A  19     3275   4138   1226    -23     24    282       C  
ATOM    140  CD  GLU A  19     -69.569  -5.497   2.604  1.00 24.03           C  
ANISOU  140  CD  GLU A  19     3558   4211   1358    -68    -77    423       C  
ATOM    141  OE1 GLU A  19     -69.715  -4.968   3.700  1.00 25.82           O  
ANISOU  141  OE1 GLU A  19     3663   4419   1727    -65    121    187       O  
ATOM    142  OE2 GLU A  19     -69.949  -5.024   1.534  1.00 24.07           O  
ANISOU  142  OE2 GLU A  19     3245   4276   1623    -68     74    763       O  
ATOM    143  N   SER A  20     -64.849  -6.472   4.645  1.00 16.82           N  
ANISOU  143  N   SER A  20     2778   3030    581    -81     37    -35       N  
ATOM    144  CA  SER A  20     -64.002  -6.449   5.834  1.00 16.97           C  
ANISOU  144  CA  SER A  20     2640   3050    757    -94    -36     81       C  
ATOM    145  C   SER A  20     -63.133  -5.210   5.909  1.00 17.18           C  
ANISOU  145  C   SER A  20     2794   3033    698    -81    157    -14       C  
ATOM    146  O   SER A  20     -62.729  -4.805   7.006  1.00 16.35           O  
ANISOU  146  O   SER A  20     2492   2902    817   -160    106    -51       O  
ATOM    147  CB  SER A  20     -63.133  -7.703   5.922  1.00 17.43           C  
ANISOU  147  CB  SER A  20     2717   3045    859    -57    207    -33       C  
ATOM    148  OG  SER A  20     -61.999  -7.630   5.064  1.00 16.91           O  
ANISOU  148  OG  SER A  20     2584   2889    951    -37    103     26       O  
ATOM    149  N   MET A  21     -62.826  -4.625   4.753  1.00 17.13           N  
ANISOU  149  N   MET A  21     2701   2945    861   -147    127    112       N  
ATOM    150  CA  MET A  21     -62.059  -3.386   4.718  1.00 16.79           C  
ANISOU  150  CA  MET A  21     2753   2902    723    -89    143     86       C  
ATOM    151  C   MET A  21     -62.854  -2.185   5.160  1.00 17.71           C  
ANISOU  151  C   MET A  21     2728   3016    981   -103    115    -24       C  
ATOM    152  O   MET A  21     -62.269  -1.229   5.651  1.00 18.10           O  
ANISOU  152  O   MET A  21     2855   2901   1121   -102    181    -51       O  
ATOM    153  CB  MET A  21     -61.454  -3.137   3.337  1.00 17.55           C  
ANISOU  153  CB  MET A  21     2811   2971    883   -108    337     49       C  
ATOM    154  CG  MET A  21     -60.374  -4.142   3.013  1.00 20.06           C  
ANISOU  154  CG  MET A  21     3060   3327   1232    266    126     73       C  
ATOM    155  SD  MET A  21     -59.498  -3.750   1.493  1.00 29.45           S  
ANISOU  155  SD  MET A  21     3953   5163   2071    674   1029    449       S  
ATOM    156  CE  MET A  21     -60.749  -4.256   0.345  1.00 24.66           C  
ANISOU  156  CE  MET A  21     4117   3939   1311    429    876    122       C  
ATOM    157  N   LYS A  22     -64.166  -2.237   4.992  1.00 17.57           N  
ANISOU  157  N   LYS A  22     2621   3043   1011   -175    205     17       N  
ATOM    158  CA  LYS A  22     -64.986  -1.046   5.135  1.00 18.23           C  
ANISOU  158  CA  LYS A  22     2780   2877   1267   -218     61   -111       C  
ATOM    159  C   LYS A  22     -64.950  -0.347   6.498  1.00 18.81           C  
ANISOU  159  C   LYS A  22     2906   2990   1250   -148    165   -137       C  
ATOM    160  O   LYS A  22     -64.869   0.867   6.545  1.00 19.39           O  
ANISOU  160  O   LYS A  22     2932   2967   1467    -62    218    -60       O  
ATOM    161  CB  LYS A  22     -66.434  -1.347   4.765  1.00 18.72           C  
ANISOU  161  CB  LYS A  22     2757   3094   1258   -421     68    -22       C  
ATOM    162  CG  LYS A  22     -66.721  -1.382   3.269  1.00 21.23           C  
ANISOU  162  CG  LYS A  22     3156   3641   1269   -586     72    281       C  
ATOM    163  CD  LYS A  22     -68.124  -1.940   2.926  1.00 23.70           C  
ANISOU  163  CD  LYS A  22     3219   4134   1651   -522   -375     76       C  
ATOM    164  CE  LYS A  22     -68.311  -1.931   1.419  1.00 26.76           C  
ANISOU  164  CE  LYS A  22     3894   4561   1710   -303   -436    396       C  
ATOM    165  NZ  LYS A  22     -69.646  -2.411   0.960  1.00 30.37           N  
ANISOU  165  NZ  LYS A  22     4012   4871   2656   -414   -568   -197       N  
ATOM    166  N   PRO A  23     -65.020  -1.101   7.601  1.00 17.83           N  
ANISOU  166  N   PRO A  23     2704   3046   1023   -164    344   -253       N  
ATOM    167  CA  PRO A  23     -65.070  -0.387   8.876  1.00 18.40           C  
ANISOU  167  CA  PRO A  23     2863   3111   1015   -219    234   -243       C  
ATOM    168  C   PRO A  23     -63.782   0.333   9.244  1.00 17.77           C  
ANISOU  168  C   PRO A  23     2830   3074    845   -131    299   -117       C  
ATOM    169  O   PRO A  23     -63.785   1.121  10.184  1.00 19.20           O  
ANISOU  169  O   PRO A  23     2808   3226   1261    -58    221   -427       O  
ATOM    170  CB  PRO A  23     -65.356  -1.489   9.904  1.00 17.86           C  
ANISOU  170  CB  PRO A  23     2870   3297    616   -116    445   -293       C  
ATOM    171  CG  PRO A  23     -65.086  -2.776   9.210  1.00 19.44           C  
ANISOU  171  CG  PRO A  23     3376   3104    906    -25    221   -179       C  
ATOM    172  CD  PRO A  23     -65.275  -2.542   7.745  1.00 18.32           C  
ANISOU  172  CD  PRO A  23     2947   3084    929   -208    217    -61       C  
ATOM    173  N   TRP A  24     -62.705   0.088   8.505  1.00 16.80           N  
ANISOU  173  N   TRP A  24     2626   2898    856    -11    184     13       N  
ATOM    174  CA  TRP A  24     -61.405   0.667   8.831  1.00 16.49           C  
ANISOU  174  CA  TRP A  24     2706   2670    887     59    163     10       C  
ATOM    175  C   TRP A  24     -61.048   1.830   7.974  1.00 17.31           C  
ANISOU  175  C   TRP A  24     2619   2760   1195     65    200    162       C  
ATOM    176  O   TRP A  24     -59.912   2.301   8.010  1.00 17.28           O  
ANISOU  176  O   TRP A  24     2721   2623   1220     42    -78    165       O  
ATOM    177  CB  TRP A  24     -60.312  -0.383   8.722  1.00 15.75           C  
ANISOU  177  CB  TRP A  24     2590   2598    795     53    129     98       C  
ATOM    178  CG  TRP A  24     -60.593  -1.582   9.576  1.00 16.90           C  
ANISOU  178  CG  TRP A  24     2790   2631    999   -118    187     98       C  
ATOM    179  CD1 TRP A  24     -61.078  -2.820   9.164  1.00 16.89           C  
ANISOU  179  CD1 TRP A  24     2949   2532    937     20    177     43       C  
ATOM    180  CD2 TRP A  24     -60.479  -1.673  11.033  1.00 17.22           C  
ANISOU  180  CD2 TRP A  24     2823   2699   1020    115     14    141       C  
ATOM    181  NE1 TRP A  24     -61.234  -3.660  10.238  1.00 17.99           N  
ANISOU  181  NE1 TRP A  24     2979   2938    918    -86    139    175       N  
ATOM    182  CE2 TRP A  24     -60.894  -3.031  11.391  1.00 17.86           C  
ANISOU  182  CE2 TRP A  24     2981   2787   1016    -51     87    126       C  
ATOM    183  CE3 TRP A  24     -60.065  -0.805  12.041  1.00 16.90           C  
ANISOU  183  CE3 TRP A  24     2817   2757    845    253    103    134       C  
ATOM    184  CZ2 TRP A  24     -60.892  -3.476  12.705  1.00 19.41           C  
ANISOU  184  CZ2 TRP A  24     3339   3093    942     86      8     76       C  
ATOM    185  CZ3 TRP A  24     -60.070  -1.264  13.365  1.00 17.21           C  
ANISOU  185  CZ3 TRP A  24     3061   2627    850    274    190    135       C  
ATOM    186  CH2 TRP A  24     -60.475  -2.564  13.686  1.00 18.74           C  
ANISOU  186  CH2 TRP A  24     3129   2752   1238    -37    198     64       C  
ATOM    187  N   GLN A  25     -62.030   2.318   7.230  1.00 17.15           N  
ANISOU  187  N   GLN A  25     2716   2829    969   -137     20     70       N  
ATOM    188  CA  GLN A  25     -61.844   3.478   6.389  1.00 17.75           C  
ANISOU  188  CA  GLN A  25     2855   2955    933    -84   -116    156       C  
ATOM    189  C   GLN A  25     -62.195   4.760   7.136  1.00 18.69           C  
ANISOU  189  C   GLN A  25     2839   2932   1328    -16    -65    199       C  
ATOM    190  O   GLN A  25     -61.348   5.620   7.321  1.00 17.46           O  
ANISOU  190  O   GLN A  25     2862   2931    838    -80     75    272       O  
ATOM    191  CB  GLN A  25     -62.652   3.332   5.095  1.00 18.13           C  
ANISOU  191  CB  GLN A  25     2755   2916   1215    -61   -307    175       C  
ATOM    192  CG  GLN A  25     -62.455   2.004   4.350  1.00 18.84           C  
ANISOU  192  CG  GLN A  25     2951   3078   1126    -64    -98     66       C  
ATOM    193  CD  GLN A  25     -61.159   1.907   3.555  1.00 20.28           C  
ANISOU  193  CD  GLN A  25     2987   3441   1275   -157    -61   -231       C  
ATOM    194  OE1 GLN A  25     -60.928   0.911   2.866  1.00 23.13           O  
ANISOU  194  OE1 GLN A  25     3468   3362   1958    250    -40   -243       O  
ATOM    195  NE2 GLN A  25     -60.313   2.929   3.641  1.00 19.79           N  
ANISOU  195  NE2 GLN A  25     3252   3030   1237    -52    263    -10       N  
ATOM    196  N   SER A  26     -63.444   4.874   7.569  1.00 20.36           N  
ANISOU  196  N   SER A  26     2863   3228   1643     50    -12    155       N  
ATOM    197  CA  SER A  26     -63.883   6.057   8.297  1.00 20.39           C  
ANISOU  197  CA  SER A  26     3011   3407   1330    137    169    251       C  
ATOM    198  C   SER A  26     -64.485   5.761   9.672  1.00 21.13           C  
ANISOU  198  C   SER A  26     2979   3598   1448     20    332     46       C  
ATOM    199  O   SER A  26     -64.478   6.631  10.540  1.00 22.72           O  
ANISOU  199  O   SER A  26     3044   3964   1625    193    499   -186       O  
ATOM    200  CB  SER A  26     -64.863   6.889   7.459  1.00 22.02           C  
ANISOU  200  CB  SER A  26     3216   3505   1642    215     50    308       C  
ATOM    201  OG  SER A  26     -65.973   6.105   7.094  1.00 27.51           O  
ANISOU  201  OG  SER A  26     3404   4363   2683   -103   -163     31       O  
ATOM    202  N   ASP A  27     -65.004   4.555   9.904  1.00 20.77           N  
ANISOU  202  N   ASP A  27     3020   3570   1300      2    340     92       N  
ATOM    203  CA  ASP A  27     -65.564   4.213  11.234  1.00 21.68           C  
ANISOU  203  CA  ASP A  27     3156   3684   1397    -99    406    122       C  
ATOM    204  C   ASP A  27     -64.509   4.151  12.354  1.00 21.28           C  
ANISOU  204  C   ASP A  27     3062   3705   1317     25    485     30       C  
ATOM    205  O   ASP A  27     -64.711   4.700  13.437  1.00 22.49           O  
ANISOU  205  O   ASP A  27     3229   3869   1446    332    618     -7       O  
ATOM    206  CB  ASP A  27     -66.339   2.898  11.200  1.00 22.15           C  
ANISOU  206  CB  ASP A  27     3091   3868   1457   -252    513    214       C  
ATOM    207  CG  ASP A  27     -67.620   2.983  10.392  1.00 25.89           C  
ANISOU  207  CG  ASP A  27     3515   4224   2096   -216     51    353       C  
ATOM    208  OD1 ASP A  27     -68.057   4.098  10.021  1.00 28.81           O  
ANISOU  208  OD1 ASP A  27     3421   4353   3171    336    147     77       O  
ATOM    209  OD2 ASP A  27     -68.197   1.909  10.130  1.00 28.44           O  
ANISOU  209  OD2 ASP A  27     3901   4434   2469   -306    -95    -80       O  
ATOM    210  N   SER A  28     -63.402   3.461  12.083  1.00 19.50           N  
ANISOU  210  N   SER A  28     3043   3227   1138     24    299    154       N  
ATOM    211  CA  SER A  28     -62.299   3.316  13.023  1.00 19.25           C  
ANISOU  211  CA  SER A  28     2945   3120   1246     20    316    -26       C  
ATOM    212  C   SER A  28     -61.024   3.450  12.227  1.00 18.85           C  
ANISOU  212  C   SER A  28     2885   2889   1385     50    292   -104       C  
ATOM    213  O   SER A  28     -60.724   2.589  11.426  1.00 18.80           O  
ANISOU  213  O   SER A  28     2863   2872   1408      6    277    -88       O  
ATOM    214  CB  SER A  28     -62.369   1.944  13.685  1.00 19.77           C  
ANISOU  214  CB  SER A  28     3044   3109   1358    260    135     38       C  
ATOM    215  OG  SER A  28     -61.299   1.744  14.591  1.00 19.80           O  
ANISOU  215  OG  SER A  28     2899   3266   1356    249    211   -214       O  
ATOM    216  N   PHE A  29     -60.300   4.538  12.396  1.00 16.13           N  
ANISOU  216  N   PHE A  29     2798   2634    696    141    120     95       N  
ATOM    217  CA  PHE A  29     -59.278   4.836  11.422  1.00 15.74           C  
ANISOU  217  CA  PHE A  29     2690   2541    748    219    132    -17       C  
ATOM    218  C   PHE A  29     -57.969   5.209  12.089  1.00 16.41           C  
ANISOU  218  C   PHE A  29     2724   2728    781    148    115    278       C  
ATOM    219  O   PHE A  29     -57.132   5.873  11.478  1.00 15.26           O  
ANISOU  219  O   PHE A  29     2795   2565    435    113    -89    253       O  
ATOM    220  CB  PHE A  29     -59.768   5.990  10.551  1.00 15.76           C  
ANISOU  220  CB  PHE A  29     2788   2505    693    165    104    -28       C  
ATOM    221  CG  PHE A  29     -60.233   7.175  11.347  1.00 15.39           C  
ANISOU  221  CG  PHE A  29     2781   2585    480    199     62    -34       C  
ATOM    222  CD1 PHE A  29     -61.538   7.263  11.825  1.00 16.74           C  
ANISOU  222  CD1 PHE A  29     2743   2791    824    296      0     20       C  
ATOM    223  CD2 PHE A  29     -59.350   8.193  11.643  1.00 14.90           C  
ANISOU  223  CD2 PHE A  29     2616   2629    416    250   -157     52       C  
ATOM    224  CE1 PHE A  29     -61.943   8.347  12.595  1.00 17.50           C  
ANISOU  224  CE1 PHE A  29     2910   2617   1119    490   -140     39       C  
ATOM    225  CE2 PHE A  29     -59.753   9.286  12.387  1.00 18.63           C  
ANISOU  225  CE2 PHE A  29     2658   2976   1444    563   -168   -339       C  
ATOM    226  CZ  PHE A  29     -61.050   9.365  12.867  1.00 17.59           C  
ANISOU  226  CZ  PHE A  29     2657   3180    847    341   -220   -116       C  
ATOM    227  N   ALA A  30     -57.769   4.795  13.339  1.00 15.99           N  
ANISOU  227  N   ALA A  30     2604   2786    684    220     -3     83       N  
ATOM    228  CA  ALA A  30     -56.558   5.200  14.075  1.00 15.34           C  
ANISOU  228  CA  ALA A  30     2518   2610    700    161    137    160       C  
ATOM    229  C   ALA A  30     -55.252   4.711  13.434  1.00 14.13           C  
ANISOU  229  C   ALA A  30     2586   2415    364    109    106     84       C  
ATOM    230  O   ALA A  30     -55.242   3.720  12.708  1.00 14.36           O  
ANISOU  230  O   ALA A  30     2587   2369    497    230    265     29       O  
ATOM    231  CB  ALA A  30     -56.630   4.711  15.515  1.00 15.84           C  
ANISOU  231  CB  ALA A  30     2775   2645    598    -23    132     27       C  
ATOM    232  N   ASN A  31     -54.148   5.396  13.726  1.00 14.42           N  
ANISOU  232  N   ASN A  31     2596   2283    599     97    226    152       N  
ATOM    233  CA  ASN A  31     -52.834   4.860  13.408  1.00 15.03           C  
ANISOU  233  CA  ASN A  31     2611   2404    693    102    165     -4       C  
ATOM    234  C   ASN A  31     -52.576   3.740  14.400  1.00 15.52           C  
ANISOU  234  C   ASN A  31     2879   2294    722     76      0    -79       C  
ATOM    235  O   ASN A  31     -52.608   3.967  15.592  1.00 16.93           O  
ANISOU  235  O   ASN A  31     3129   2538    763     44    221   -157       O  
ATOM    236  CB  ASN A  31     -51.759   5.948  13.551  1.00 15.11           C  
ANISOU  236  CB  ASN A  31     2759   2483    498     14    199     29       C  
ATOM    237  CG  ASN A  31     -50.399   5.511  13.020  1.00 15.93           C  
ANISOU  237  CG  ASN A  31     2749   2568    734    131    117     87       C  
ATOM    238  OD1 ASN A  31     -49.968   4.376  13.224  1.00 16.59           O  
ANISOU  238  OD1 ASN A  31     2892   2617    792     93    222    150       O  
ATOM    239  ND2 ASN A  31     -49.717   6.424  12.319  1.00 15.93           N  
ANISOU  239  ND2 ASN A  31     2828   2320    902    141    202    -98       N  
ATOM    240  N   PRO A  32     -52.321   2.520  13.928  1.00 14.97           N  
ANISOU  240  N   PRO A  32     2766   2283    637     60     48    -80       N  
ATOM    241  CA  PRO A  32     -52.162   1.428  14.867  1.00 15.64           C  
ANISOU  241  CA  PRO A  32     2992   2346    603     79    -27    -70       C  
ATOM    242  C   PRO A  32     -50.994   1.618  15.831  1.00 16.58           C  
ANISOU  242  C   PRO A  32     2961   2564    771     94    -71    -31       C  
ATOM    243  O   PRO A  32     -50.902   0.909  16.818  1.00 17.08           O  
ANISOU  243  O   PRO A  32     3060   2608    820      6    -51     45       O  
ATOM    244  CB  PRO A  32     -51.932   0.225  13.962  1.00 15.05           C  
ANISOU  244  CB  PRO A  32     2832   2335    550    122   -220    -60       C  
ATOM    245  CG  PRO A  32     -52.676   0.585  12.710  1.00 14.87           C  
ANISOU  245  CG  PRO A  32     2967   2145    538    151   -126    121       C  
ATOM    246  CD  PRO A  32     -52.337   2.047  12.541  1.00 15.02           C  
ANISOU  246  CD  PRO A  32     2935   2106    664    105     38    -85       C  
ATOM    247  N   SER A  33     -50.111   2.567  15.560  1.00 16.47           N  
ANISOU  247  N   SER A  33     2990   2585    682     51    158   -162       N  
ATOM    248  CA  SER A  33     -49.050   2.810  16.507  1.00 17.60           C  
ANISOU  248  CA  SER A  33     2957   2725   1004     90     82   -152       C  
ATOM    249  C   SER A  33     -49.468   3.604  17.737  1.00 18.04           C  
ANISOU  249  C   SER A  33     3060   2938    854     49      1   -156       C  
ATOM    250  O   SER A  33     -48.643   3.774  18.618  1.00 18.59           O  
ANISOU  250  O   SER A  33     3228   3096    736    260   -135    -31       O  
ATOM    251  CB  SER A  33     -47.892   3.542  15.852  1.00 17.85           C  
ANISOU  251  CB  SER A  33     2917   2728   1136    224    214    -73       C  
ATOM    252  OG  SER A  33     -48.216   4.909  15.756  1.00 20.63           O  
ANISOU  252  OG  SER A  33     3617   2835   1385    210    418     29       O  
ATOM    253  N   ALA A  34     -50.693   4.114  17.799  1.00 16.97           N  
ANISOU  253  N   ALA A  34     3089   2510    847     84    137   -100       N  
ATOM    254  CA  ALA A  34     -51.036   5.095  18.817  1.00 18.27           C  
ANISOU  254  CA  ALA A  34     3313   2690    937    230     55   -209       C  
ATOM    255  C   ALA A  34     -51.306   4.367  20.106  1.00 20.21           C  
ANISOU  255  C   ALA A  34     3504   2962   1210     96     68     37       C  
ATOM    256  O   ALA A  34     -51.439   3.170  20.107  1.00 19.24           O  
ANISOU  256  O   ALA A  34     3336   2941   1032     30   -279    148       O  
ATOM    257  CB  ALA A  34     -52.262   5.869  18.396  1.00 18.72           C  
ANISOU  257  CB  ALA A  34     3228   2847   1037    209    133   -137       C  
ATOM    258  N   ALA A  35     -51.400   5.070  21.213  1.00 20.75           N  
ANISOU  258  N   ALA A  35     3570   3455    858     84    213    144       N  
ATOM    259  CA  ALA A  35     -51.483   4.345  22.441  1.00 20.54           C  
ANISOU  259  CA  ALA A  35     3280   3720    803    137    -76    208       C  
ATOM    260  C   ALA A  35     -52.915   4.115  22.949  1.00 20.82           C  
ANISOU  260  C   ALA A  35     3520   3625    765     64    142    176       C  
ATOM    261  O   ALA A  35     -53.095   3.578  24.039  1.00 26.81           O  
ANISOU  261  O   ALA A  35     4009   4598   1577    124    509   1078       O  
ATOM    262  CB  ALA A  35     -50.623   5.039  23.479  1.00 21.24           C  
ANISOU  262  CB  ALA A  35     3577   4043    449     52    189     -6       C  
ATOM    263  N   HIS A  36     -53.931   4.476  22.178  1.00 17.77           N  
ANISOU  263  N   HIS A  36     3239   2923    587     -3    349    235       N  
ATOM    264  CA  HIS A  36     -55.289   4.519  22.706  1.00 17.82           C  
ANISOU  264  CA  HIS A  36     3330   2894    547    101    381    334       C  
ATOM    265  C   HIS A  36     -56.116   3.407  22.142  1.00 18.39           C  
ANISOU  265  C   HIS A  36     3076   2914    996    146    320    313       C  
ATOM    266  O   HIS A  36     -55.603   2.584  21.390  1.00 18.53           O  
ANISOU  266  O   HIS A  36     3406   3058    576    -89    431    260       O  
ATOM    267  CB  HIS A  36     -55.916   5.885  22.467  1.00 18.15           C  
ANISOU  267  CB  HIS A  36     3176   2938    780    147    460    212       C  
ATOM    268  CG  HIS A  36     -55.780   6.370  21.060  1.00 17.99           C  
ANISOU  268  CG  HIS A  36     3306   2845    684     88    312     85       C  
ATOM    269  ND1 HIS A  36     -56.409   5.777  20.028  1.00 16.98           N  
ANISOU  269  ND1 HIS A  36     2800   2935    717    138    233    194       N  
ATOM    270  CD2 HIS A  36     -55.048   7.425  20.527  1.00 17.86           C  
ANISOU  270  CD2 HIS A  36     3210   2794    782    165    393     70       C  
ATOM    271  CE1 HIS A  36     -56.102   6.430  18.889  1.00 17.28           C  
ANISOU  271  CE1 HIS A  36     3105   2807    650    106    333     22       C  
ATOM    272  NE2 HIS A  36     -55.262   7.431  19.195  1.00 17.23           N  
ANISOU  272  NE2 HIS A  36     3220   2548    777    157    416    155       N  
ATOM    273  N   ILE A  37     -57.388   3.350  22.523  1.00 18.21           N  
ANISOU  273  N   ILE A  37     3135   3028    752    -30    337    258       N  
ATOM    274  CA  ILE A  37     -58.233   2.188  22.233  1.00 19.18           C  
ANISOU  274  CA  ILE A  37     3381   3139    764    -92    270    121       C  
ATOM    275  C   ILE A  37     -58.500   1.965  20.743  1.00 18.64           C  
ANISOU  275  C   ILE A  37     3181   3161    741    -47    324    156       C  
ATOM    276  O   ILE A  37     -58.720   0.847  20.315  1.00 18.57           O  
ANISOU  276  O   ILE A  37     3104   3122    829    189    385     71       O  
ATOM    277  CB  ILE A  37     -59.574   2.267  23.018  1.00 21.32           C  
ANISOU  277  CB  ILE A  37     3290   3395   1415    -28    346    262       C  
ATOM    278  CG1 ILE A  37     -60.398   0.992  22.892  1.00 23.85           C  
ANISOU  278  CG1 ILE A  37     3775   3439   1847   -150    204    129       C  
ATOM    279  CG2 ILE A  37     -60.465   3.374  22.509  1.00 22.11           C  
ANISOU  279  CG2 ILE A  37     3362   3568   1468    167    546    253       C  
ATOM    280  CD1 ILE A  37     -59.773  -0.181  23.578  1.00 27.45           C  
ANISOU  280  CD1 ILE A  37     4452   3797   2180     74     67    297       C  
ATOM    281  N   GLU A  38     -58.539   3.033  19.962  1.00 18.20           N  
ANISOU  281  N   GLU A  38     2998   3099    816     33    301    111       N  
ATOM    282  CA  GLU A  38     -58.820   2.833  18.558  1.00 18.14           C  
ANISOU  282  CA  GLU A  38     2905   3172    813     73    333     33       C  
ATOM    283  C   GLU A  38     -57.644   2.150  17.883  1.00 17.14           C  
ANISOU  283  C   GLU A  38     2960   2735    815     90    248     89       C  
ATOM    284  O   GLU A  38     -57.838   1.313  16.999  1.00 17.28           O  
ANISOU  284  O   GLU A  38     3108   2903    551    -39    204    168       O  
ATOM    285  CB  GLU A  38     -59.222   4.126  17.861  1.00 18.20           C  
ANISOU  285  CB  GLU A  38     2887   3181    845    327    329   -139       C  
ATOM    286  CG  GLU A  38     -60.627   4.613  18.208  1.00 20.56           C  
ANISOU  286  CG  GLU A  38     2965   3607   1237    384    598   -229       C  
ATOM    287  CD  GLU A  38     -61.721   3.610  17.878  1.00 22.58           C  
ANISOU  287  CD  GLU A  38     3169   3987   1421    388    286   -531       C  
ATOM    288  OE1 GLU A  38     -62.502   3.267  18.788  1.00 25.75           O  
ANISOU  288  OE1 GLU A  38     3247   4233   2301    185    569   -166       O  
ATOM    289  OE2 GLU A  38     -61.797   3.149  16.727  1.00 24.75           O  
ANISOU  289  OE2 GLU A  38     3338   4290   1776    324    393  -1041       O  
ATOM    290  N   ALA A  39     -56.426   2.469  18.326  1.00 16.03           N  
ANISOU  290  N   ALA A  39     2906   2742    440    -93    412     99       N  
ATOM    291  CA  ALA A  39     -55.245   1.774  17.804  1.00 17.76           C  
ANISOU  291  CA  ALA A  39     2898   2785   1064     30    277     74       C  
ATOM    292  C   ALA A  39     -55.255   0.321  18.267  1.00 17.92           C  
ANISOU  292  C   ALA A  39     3073   2818    917     46    479     17       C  
ATOM    293  O   ALA A  39     -54.887  -0.581  17.513  1.00 17.82           O  
ANISOU  293  O   ALA A  39     3059   2752    958    168    299    -19       O  
ATOM    294  CB  ALA A  39     -53.963   2.461  18.238  1.00 18.20           C  
ANISOU  294  CB  ALA A  39     3171   2790    954    -40    193    -79       C  
ATOM    295  N   GLU A  40     -55.724   0.101  19.495  1.00 18.28           N  
ANISOU  295  N   GLU A  40     3336   2834    775    -92    309     88       N  
ATOM    296  CA  GLU A  40     -55.866  -1.240  20.041  1.00 19.28           C  
ANISOU  296  CA  GLU A  40     3481   3017    825    -65    234    208       C  
ATOM    297  C   GLU A  40     -56.762  -2.135  19.175  1.00 18.27           C  
ANISOU  297  C   GLU A  40     3300   2907    735     75    330    157       C  
ATOM    298  O   GLU A  40     -56.426  -3.293  18.904  1.00 19.45           O  
ANISOU  298  O   GLU A  40     3470   3044    875    136    191    131       O  
ATOM    299  CB  GLU A  40     -56.387  -1.179  21.481  1.00 22.37           C  
ANISOU  299  CB  GLU A  40     3965   3606    927     -7    476    270       C  
ATOM    300  CG  GLU A  40     -55.874  -2.369  22.275  1.00 27.83           C  
ANISOU  300  CG  GLU A  40     4794   4157   1622    370    338    527       C  
ATOM    301  CD  GLU A  40     -56.187  -2.309  23.746  1.00 34.70           C  
ANISOU  301  CD  GLU A  40     6224   5424   1535   -177    378   1064       C  
ATOM    302  OE1 GLU A  40     -56.766  -3.288  24.262  1.00 40.16           O  
ANISOU  302  OE1 GLU A  40     6517   5631   3108   -341   1291    879       O  
ATOM    303  OE2 GLU A  40     -55.833  -1.304  24.394  1.00 41.88           O  
ANISOU  303  OE2 GLU A  40     7711   6060   2139   -163    795    231       O  
ATOM    304  N   LYS A  41     -57.892  -1.598  18.751  1.00 17.75           N  
ANISOU  304  N   LYS A  41     3201   2966    575     44    325     39       N  
ATOM    305  CA  LYS A  41     -58.806  -2.325  17.892  1.00 17.70           C  
ANISOU  305  CA  LYS A  41     2978   2860    884     92    400    -67       C  
ATOM    306  C   LYS A  41     -58.186  -2.667  16.543  1.00 17.07           C  
ANISOU  306  C   LYS A  41     3002   2744    739    107    304     38       C  
ATOM    307  O   LYS A  41     -58.297  -3.789  16.082  1.00 17.21           O  
ANISOU  307  O   LYS A  41     2955   2678    903    121    132     70       O  
ATOM    308  CB  LYS A  41     -60.069  -1.510  17.703  1.00 18.75           C  
ANISOU  308  CB  LYS A  41     2824   3184   1117    169    738    -72       C  
ATOM    309  CG  LYS A  41     -60.840  -1.350  19.006  1.00 20.98           C  
ANISOU  309  CG  LYS A  41     2884   3631   1454    394    948   -376       C  
ATOM    310  CD  LYS A  41     -62.245  -0.856  18.760  1.00 28.01           C  
ANISOU  310  CD  LYS A  41     3145   4695   2802    713    511   -508       C  
ATOM    311  CE  LYS A  41     -62.252   0.626  18.469  1.00 26.22           C  
ANISOU  311  CE  LYS A  41     2734   4689   2537   1235    784   -556       C  
ATOM    312  NZ  LYS A  41     -63.477   1.217  19.054  1.00 31.75           N  
ANISOU  312  NZ  LYS A  41     3551   5136   3376   2071    881   -923       N  
ATOM    313  N   ALA A  42     -57.540  -1.696  15.915  1.00 16.63           N  
ANISOU  313  N   ALA A  42     2920   2679    718    110    352      0       N  
ATOM    314  CA  ALA A  42     -56.811  -1.962  14.674  1.00 17.08           C  
ANISOU  314  CA  ALA A  42     2878   2674    935    117    522      0       C  
ATOM    315  C   ALA A  42     -55.764  -3.055  14.858  1.00 17.14           C  
ANISOU  315  C   ALA A  42     3040   2709    764    120    181     74       C  
ATOM    316  O   ALA A  42     -55.674  -3.994  14.055  1.00 17.12           O  
ANISOU  316  O   ALA A  42     3121   2665    717     71    131    119       O  
ATOM    317  CB  ALA A  42     -56.172  -0.685  14.159  1.00 16.95           C  
ANISOU  317  CB  ALA A  42     3012   2607    819    136    316    128       C  
ATOM    318  N   LEU A  43     -55.003  -2.946  15.946  1.00 17.34           N  
ANISOU  318  N   LEU A  43     3033   2812    741    132    243   -139       N  
ATOM    319  CA  LEU A  43     -53.954  -3.900  16.242  1.00 16.84           C  
ANISOU  319  CA  LEU A  43     2969   2971    459     34     34     26       C  
ATOM    320  C   LEU A  43     -54.441  -5.303  16.421  1.00 18.25           C  
ANISOU  320  C   LEU A  43     3146   2936    850    136    140     72       C  
ATOM    321  O   LEU A  43     -53.788  -6.218  16.010  1.00 17.62           O  
ANISOU  321  O   LEU A  43     3180   2936    577    144     29      0       O  
ATOM    322  CB  LEU A  43     -53.147  -3.498  17.469  1.00 18.71           C  
ANISOU  322  CB  LEU A  43     3112   3038    956    -94   -192   -258       C  
ATOM    323  CG  LEU A  43     -52.102  -2.407  17.245  1.00 17.98           C  
ANISOU  323  CG  LEU A  43     2857   3051    923      2   -122   -295       C  
ATOM    324  CD1 LEU A  43     -51.515  -1.964  18.581  1.00 19.43           C  
ANISOU  324  CD1 LEU A  43     3411   3169    800   -211      1   -346       C  
ATOM    325  CD2 LEU A  43     -50.979  -2.759  16.265  1.00 17.94           C  
ANISOU  325  CD2 LEU A  43     2959   2975    882    108    -68   -137       C  
ATOM    326  N   ASN A  44     -55.587  -5.454  17.017  1.00 19.09           N  
ANISOU  326  N   ASN A  44     3135   2958   1158     56    166     86       N  
ATOM    327  CA AASN A  44     -56.176  -6.744  17.183  0.50 18.78           C  
ANISOU  327  CA AASN A  44     3313   2927    894     77     93    181       C  
ATOM    328  CA BASN A  44     -56.142  -6.767  17.210  0.50 18.54           C  
ANISOU  328  CA BASN A  44     3259   2981    805     79    180    213       C  
ATOM    329  C   ASN A  44     -56.616  -7.361  15.863  1.00 18.70           C  
ANISOU  329  C   ASN A  44     3290   2889    924     66     62    190       C  
ATOM    330  O   ASN A  44     -56.507  -8.538  15.656  1.00 19.67           O  
ANISOU  330  O   ASN A  44     3509   2925   1039     43    116     94       O  
ATOM    331  CB AASN A  44     -57.358  -6.601  18.093  0.50 20.16           C  
ANISOU  331  CB AASN A  44     3307   3075   1277    223    188    153       C  
ATOM    332  CB BASN A  44     -57.286  -6.691  18.237  0.50 18.66           C  
ANISOU  332  CB BASN A  44     3225   2836   1026    115    267    305       C  
ATOM    333  CG AASN A  44     -57.739  -7.893  18.634  0.50 22.43           C  
ANISOU  333  CG AASN A  44     3648   3278   1594    -24    130    264       C  
ATOM    334  CG BASN A  44     -56.797  -6.427  19.633  0.50 18.86           C  
ANISOU  334  CG BASN A  44     3282   2920    963    -36    352    343       C  
ATOM    335  OD1AASN A  44     -56.973  -8.464  19.423  0.50 25.86           O  
ANISOU  335  OD1AASN A  44     4246   3733   1845    436    -36    324       O  
ATOM    336  OD1BASN A  44     -55.682  -6.779  19.946  0.50 19.73           O  
ANISOU  336  OD1BASN A  44     3341   3174    981     40    338    428       O  
ATOM    337  ND2AASN A  44     -58.897  -8.394  18.228  0.50 25.03           N  
ANISOU  337  ND2AASN A  44     3697   3632   2178     11    -12    -10       N  
ATOM    338  ND2BASN A  44     -57.643  -5.861  20.484  0.50 20.61           N  
ANISOU  338  ND2BASN A  44     3600   2953   1275     23    588    329       N  
ATOM    339  N   ALA A  45     -57.179  -6.535  14.999  1.00 17.51           N  
ANISOU  339  N   ALA A  45     3043   2885    723    -36    156    204       N  
ATOM    340  CA  ALA A  45     -57.594  -6.980  13.671  1.00 17.16           C  
ANISOU  340  CA  ALA A  45     3008   2726    786    -57     52    217       C  
ATOM    341  C   ALA A  45     -56.378  -7.358  12.823  1.00 16.94           C  
ANISOU  341  C   ALA A  45     2984   2700    750      2    -86     98       C  
ATOM    342  O   ALA A  45     -56.414  -8.337  12.069  1.00 17.46           O  
ANISOU  342  O   ALA A  45     3175   2743    716    -29     14     66       O  
ATOM    343  CB  ALA A  45     -58.419  -5.895  12.996  1.00 16.97           C  
ANISOU  343  CB  ALA A  45     3017   2847    584     34    161    167       C  
ATOM    344  N   ILE A  46     -55.288  -6.607  12.979  1.00 15.98           N  
ANISOU  344  N   ILE A  46     2927   2629    515     25    189    216       N  
ATOM    345  CA  ILE A  46     -54.035  -6.889  12.272  1.00 15.75           C  
ANISOU  345  CA  ILE A  46     2773   2509    700    -60    125    230       C  
ATOM    346  C   ILE A  46     -53.466  -8.233  12.744  1.00 16.59           C  
ANISOU  346  C   ILE A  46     3050   2525    729     68     60    103       C  
ATOM    347  O   ILE A  46     -53.061  -9.074  11.936  1.00 16.45           O  
ANISOU  347  O   ILE A  46     2985   2622    640      1     94     46       O  
ATOM    348  CB  ILE A  46     -53.012  -5.735  12.463  1.00 15.16           C  
ANISOU  348  CB  ILE A  46     2695   2309    753     73    111    166       C  
ATOM    349  CG1 ILE A  46     -53.470  -4.502  11.677  1.00 14.39           C  
ANISOU  349  CG1 ILE A  46     2635   2198    633     78    183     62       C  
ATOM    350  CG2 ILE A  46     -51.594  -6.160  12.070  1.00 15.48           C  
ANISOU  350  CG2 ILE A  46     2750   2338    795      2    276    119       C  
ATOM    351  CD1 ILE A  46     -52.720  -3.213  11.973  1.00 14.76           C  
ANISOU  351  CD1 ILE A  46     2624   2203    781     64    260    188       C  
ATOM    352  N   LYS A  47     -53.472  -8.434  14.059  1.00 16.60           N  
ANISOU  352  N   LYS A  47     2984   2618    704    -22    141     50       N  
ATOM    353  CA  LYS A  47     -53.044  -9.698  14.641  1.00 17.73           C  
ANISOU  353  CA  LYS A  47     3290   2685    760     54     31    115       C  
ATOM    354  C   LYS A  47     -53.804 -10.882  14.042  1.00 18.58           C  
ANISOU  354  C   LYS A  47     3317   2616   1126     25     36    108       C  
ATOM    355  O   LYS A  47     -53.218 -11.899  13.771  1.00 17.87           O  
ANISOU  355  O   LYS A  47     3077   2728    982     37     57     76       O  
ATOM    356  CB  LYS A  47     -53.249  -9.663  16.162  1.00 18.98           C  
ANISOU  356  CB  LYS A  47     3369   3062    777     89     30    -43       C  
ATOM    357  CG  LYS A  47     -52.581 -10.808  16.907  1.00 23.99           C  
ANISOU  357  CG  LYS A  47     4086   3495   1531    159   -227    445       C  
ATOM    358  CD  LYS A  47     -52.753 -10.678  18.404  1.00 30.13           C  
ANISOU  358  CD  LYS A  47     5003   4729   1716     49    107     30       C  
ATOM    359  CE  LYS A  47     -54.147 -11.112  18.777  1.00 33.06           C  
ANISOU  359  CE  LYS A  47     5084   4904   2570    214    483    138       C  
ATOM    360  NZ  LYS A  47     -54.361 -11.039  20.238  1.00 39.25           N  
ANISOU  360  NZ  LYS A  47     7108   5287   2517    638    110    -97       N  
ATOM    361  N   GLN A  48     -55.110 -10.758  13.866  1.00 17.80           N  
ANISOU  361  N   GLN A  48     3288   2595    877     92    -45     54       N  
ATOM    362  CA  GLN A  48     -55.856 -11.883  13.331  1.00 18.48           C  
ANISOU  362  CA  GLN A  48     3350   2564   1108     40    113     10       C  
ATOM    363  C   GLN A  48     -55.402 -12.227  11.911  1.00 17.97           C  
ANISOU  363  C   GLN A  48     3237   2539   1051    -10    105    109       C  
ATOM    364  O   GLN A  48     -55.281 -13.398  11.572  1.00 17.93           O  
ANISOU  364  O   GLN A  48     3237   2524   1049    -43    132    161       O  
ATOM    365  CB  GLN A  48     -57.367 -11.663  13.362  1.00 21.38           C  
ANISOU  365  CB  GLN A  48     3402   3132   1588      9      4    338       C  
ATOM    366  CG  GLN A  48     -58.077 -12.781  12.604  1.00 27.67           C  
ANISOU  366  CG  GLN A  48     4197   3873   2442   -168   -298   -232       C  
ATOM    367  CD  GLN A  48     -59.529 -12.985  12.947  1.00 33.75           C  
ANISOU  367  CD  GLN A  48     4570   5364   2887   -324     15    501       C  
ATOM    368  OE1 GLN A  48     -60.377 -12.814  12.084  1.00 43.72           O  
ANISOU  368  OE1 GLN A  48     5717   6537   4354   -357  -1520     -5       O  
ATOM    369  NE2 GLN A  48     -59.824 -13.402  14.180  1.00 39.59           N  
ANISOU  369  NE2 GLN A  48     6383   5754   2904    120   -555   1326       N  
ATOM    370  N   ALA A  49     -55.162 -11.213  11.090  1.00 16.51           N  
ANISOU  370  N   ALA A  49     3094   2439    737      4   -120      6       N  
ATOM    371  CA  ALA A  49     -54.732 -11.449   9.718  1.00 16.00           C  
ANISOU  371  CA  ALA A  49     3003   2185    891    -30    182    173       C  
ATOM    372  C   ALA A  49     -53.333 -12.082   9.676  1.00 16.35           C  
ANISOU  372  C   ALA A  49     2852   2486    872   -132     38    108       C  
ATOM    373  O   ALA A  49     -53.069 -13.041   8.935  1.00 16.66           O  
ANISOU  373  O   ALA A  49     2997   2472    858   -100     14    135       O  
ATOM    374  CB  ALA A  49     -54.751 -10.138   8.953  1.00 14.70           C  
ANISOU  374  CB  ALA A  49     2835   2293    457    -61     31    134       C  
ATOM    375  N   ARG A  50     -52.437 -11.533  10.486  1.00 16.04           N  
ANISOU  375  N   ARG A  50     2914   2520    660    -59     19    111       N  
ATOM    376  CA  ARG A  50     -51.082 -12.065  10.609  1.00 16.39           C  
ANISOU  376  CA  ARG A  50     2915   2522    789    -39    -75    -81       C  
ATOM    377  C   ARG A  50     -51.107 -13.574  10.978  1.00 16.54           C  
ANISOU  377  C   ARG A  50     2796   2607    881    -33     74    127       C  
ATOM    378  O   ARG A  50     -50.364 -14.379  10.419  1.00 16.82           O  
ANISOU  378  O   ARG A  50     2992   2646    751     34    104     93       O  
ATOM    379  CB  ARG A  50     -50.332 -11.243  11.658  1.00 15.87           C  
ANISOU  379  CB  ARG A  50     2815   2550    664   -118    -34     62       C  
ATOM    380  CG  ARG A  50     -48.835 -11.307  11.559  1.00 15.51           C  
ANISOU  380  CG  ARG A  50     2801   2489    599    -45   -130     10       C  
ATOM    381  CD  ARG A  50     -48.177 -10.599  12.740  1.00 16.18           C  
ANISOU  381  CD  ARG A  50     3022   2200    924   -218    -52   -173       C  
ATOM    382  NE  ARG A  50     -48.389  -9.147  12.769  1.00 15.34           N  
ANISOU  382  NE  ARG A  50     2782   2173    873   -142   -138    162       N  
ATOM    383  CZ  ARG A  50     -47.750  -8.270  11.994  1.00 14.73           C  
ANISOU  383  CZ  ARG A  50     2625   2204    767     67     31    114       C  
ATOM    384  NH1 ARG A  50     -46.866  -8.685  11.088  1.00 14.01           N  
ANISOU  384  NH1 ARG A  50     2624   2133    567     67    -89     90       N  
ATOM    385  NH2 ARG A  50     -48.001  -6.969  12.116  1.00 14.31           N  
ANISOU  385  NH2 ARG A  50     2576   2226    633     45    121    -77       N  
ATOM    386  N   GLU A  51     -51.990 -13.944  11.900  1.00 16.27           N  
ANISOU  386  N   GLU A  51     2779   2614    790    -21     78     34       N  
ATOM    387  CA  GLU A  51     -52.123 -15.337  12.328  1.00 16.22           C  
ANISOU  387  CA  GLU A  51     2904   2611    647   -100     43     57       C  
ATOM    388  C   GLU A  51     -52.658 -16.242  11.228  1.00 16.05           C  
ANISOU  388  C   GLU A  51     2853   2619    624    -83     63     44       C  
ATOM    389  O   GLU A  51     -52.210 -17.379  11.070  1.00 17.31           O  
ANISOU  389  O   GLU A  51     3084   2549    941   -106    141    126       O  
ATOM    390  CB  GLU A  51     -53.024 -15.441  13.555  1.00 17.60           C  
ANISOU  390  CB  GLU A  51     3008   2890    790   -129    189   -113       C  
ATOM    391  CG  GLU A  51     -52.305 -15.069  14.835  1.00 20.32           C  
ANISOU  391  CG  GLU A  51     3416   3476    827   -118   -143    173       C  
ATOM    392  CD  GLU A  51     -53.216 -14.954  16.042  1.00 23.13           C  
ANISOU  392  CD  GLU A  51     3787   3942   1059   -204     76   -138       C  
ATOM    393  OE1 GLU A  51     -54.450 -15.126  15.917  1.00 25.46           O  
ANISOU  393  OE1 GLU A  51     3642   4346   1685   -240    575    734       O  
ATOM    394  OE2 GLU A  51     -52.682 -14.677  17.132  1.00 27.73           O  
ANISOU  394  OE2 GLU A  51     4965   4596    973      9   -255    -95       O  
ATOM    395  N   ILE A  52     -53.638 -15.750  10.483  1.00 15.81           N  
ANISOU  395  N   ILE A  52     2826   2687    491    -58    126     97       N  
ATOM    396  CA  ILE A  52     -54.174 -16.494   9.355  1.00 17.09           C  
ANISOU  396  CA  ILE A  52     3089   2787    618     34    -68     12       C  
ATOM    397  C   ILE A  52     -53.061 -16.800   8.344  1.00 16.71           C  
ANISOU  397  C   ILE A  52     2929   2599    820    -20    -76     58       C  
ATOM    398  O   ILE A  52     -52.932 -17.931   7.882  1.00 17.60           O  
ANISOU  398  O   ILE A  52     3135   2607    944     10    -78     74       O  
ATOM    399  CB  ILE A  52     -55.352 -15.735   8.701  1.00 17.74           C  
ANISOU  399  CB  ILE A  52     3103   2923    712     96   -176   -142       C  
ATOM    400  CG1 ILE A  52     -56.607 -15.806   9.598  1.00 20.65           C  
ANISOU  400  CG1 ILE A  52     3407   3185   1251     72    200   -159       C  
ATOM    401  CG2 ILE A  52     -55.672 -16.275   7.319  1.00 17.85           C  
ANISOU  401  CG2 ILE A  52     3210   2837    732     55      6   -263       C  
ATOM    402  CD1 ILE A  52     -57.649 -14.754   9.272  1.00 22.15           C  
ANISOU  402  CD1 ILE A  52     3576   3639   1199    307    244   -158       C  
ATOM    403  N   ILE A  53     -52.255 -15.798   8.002  1.00 15.76           N  
ANISOU  403  N   ILE A  53     2792   2582    612     19   -172     90       N  
ATOM    404  CA  ILE A  53     -51.137 -15.953   7.045  1.00 15.35           C  
ANISOU  404  CA  ILE A  53     2862   2536    434   -114   -195    108       C  
ATOM    405  C   ILE A  53     -50.071 -16.899   7.585  1.00 16.04           C  
ANISOU  405  C   ILE A  53     2863   2490    739    -12    -66    -41       C  
ATOM    406  O   ILE A  53     -49.643 -17.838   6.897  1.00 16.35           O  
ANISOU  406  O   ILE A  53     3079   2453    679   -150      4   -121       O  
ATOM    407  CB  ILE A  53     -50.505 -14.597   6.676  1.00 15.72           C  
ANISOU  407  CB  ILE A  53     2716   2554    701    -49   -207    120       C  
ATOM    408  CG1 ILE A  53     -51.499 -13.754   5.869  1.00 15.40           C  
ANISOU  408  CG1 ILE A  53     3047   2053    751    -35    -84    257       C  
ATOM    409  CG2 ILE A  53     -49.216 -14.782   5.877  1.00 16.42           C  
ANISOU  409  CG2 ILE A  53     2971   2659    608    -25    -68    -97       C  
ATOM    410  CD1 ILE A  53     -51.276 -12.270   6.031  1.00 16.12           C  
ANISOU  410  CD1 ILE A  53     2999   2187    939    -49    252   -128       C  
ATOM    411  N   ALA A  54     -49.668 -16.672   8.831  1.00 16.10           N  
ANISOU  411  N   ALA A  54     2916   2586    615    -86      7    122       N  
ATOM    412  CA  ALA A  54     -48.717 -17.565   9.470  1.00 16.66           C  
ANISOU  412  CA  ALA A  54     2988   2530    811     74   -113   -162       C  
ATOM    413  C   ALA A  54     -49.176 -19.019   9.428  1.00 17.44           C  
ANISOU  413  C   ALA A  54     3133   2620    871    -49      5    -42       C  
ATOM    414  O   ALA A  54     -48.437 -19.910   8.984  1.00 17.51           O  
ANISOU  414  O   ALA A  54     3290   2656    707      7      7     -2       O  
ATOM    415  CB  ALA A  54     -48.467 -17.132  10.903  1.00 16.47           C  
ANISOU  415  CB  ALA A  54     3147   2477    633     -4     20     57       C  
ATOM    416  N   ASP A  55     -50.425 -19.247   9.838  1.00 17.25           N  
ANISOU  416  N   ASP A  55     3150   2648    754   -200   -100     37       N  
ATOM    417  CA AASP A  55     -51.026 -20.591   9.821  0.50 18.32           C  
ANISOU  417  CA AASP A  55     3249   2567   1144   -112    -37    -61       C  
ATOM    418  CA BASP A  55     -50.953 -20.589   9.816  0.50 17.89           C  
ANISOU  418  CA BASP A  55     3156   2579   1060   -101     51     24       C  
ATOM    419  C   ASP A  55     -50.920 -21.258   8.437  1.00 18.07           C  
ANISOU  419  C   ASP A  55     3372   2509    984    -66    123    110       C  
ATOM    420  O   ASP A  55     -50.632 -22.450   8.364  1.00 18.17           O  
ANISOU  420  O   ASP A  55     3363   2451   1089   -134    130    215       O  
ATOM    421  CB AASP A  55     -52.537 -20.554  10.131  0.50 20.91           C  
ANISOU  421  CB AASP A  55     3349   2853   1742    -89    243     47       C  
ATOM    422  CB BASP A  55     -52.367 -20.611  10.374  0.50 18.24           C  
ANISOU  422  CB BASP A  55     3491   2775    661    -53    476     20       C  
ATOM    423  CG AASP A  55     -52.870 -20.495  11.457  0.50 21.71           C  
ANISOU  423  CG AASP A  55     3647   2908   1693   -135     85    263       C  
ATOM    424  CG BASP A  55     -53.001 -21.937  10.222  0.50 20.87           C  
ANISOU  424  CG BASP A  55     3734   2759   1435   -132    632    165       C  
ATOM    425  OD1AASP A  55     -52.059 -20.674  12.324  0.50 20.81           O  
ANISOU  425  OD1AASP A  55     3860   2584   1463   -168    119    215       O  
ATOM    426  OD1BASP A  55     -52.888 -22.702  11.181  0.50 24.94           O  
ANISOU  426  OD1BASP A  55     4338   3084   2054   -235    603    647       O  
ATOM    427  OD2AASP A  55     -54.050 -20.493  11.461  0.50 26.91           O  
ANISOU  427  OD2AASP A  55     3726   3570   2927   -205    346    396       O  
ATOM    428  OD2BASP A  55     -53.561 -22.212   9.156  0.50 24.94           O  
ANISOU  428  OD2BASP A  55     4079   3147   2249   -231   -104    151       O  
ATOM    429  N   THR A  56     -51.234 -20.494   7.394  1.00 17.93           N  
ANISOU  429  N   THR A  56     3256   2641    916   -105     39     92       N  
ATOM    430  CA  THR A  56     -51.240 -21.089   6.130  1.00 18.34           C  
ANISOU  430  CA  THR A  56     3303   2661   1004   -109    142    -34       C  
ATOM    431  C   THR A  56     -49.858 -21.492   5.656  1.00 17.08           C  
ANISOU  431  C   THR A  56     3272   2550    665   -142    139     50       C  
ATOM    432  O   THR A  56     -49.769 -22.440   4.920  1.00 17.81           O  
ANISOU  432  O   THR A  56     3221   2400   1143   -211     16    -39       O  
ATOM    433  CB  THR A  56     -52.168 -20.439   5.085  1.00 20.63           C  
ANISOU  433  CB  THR A  56     3623   2784   1430    172    179    167       C  
ATOM    434  OG1 THR A  56     -51.502 -20.135   3.851  1.00 25.63           O  
ANISOU  434  OG1 THR A  56     4114   3564   2060    -96    678    467       O  
ATOM    435  CG2 THR A  56     -53.002 -19.361   5.584  1.00 15.91           C  
ANISOU  435  CG2 THR A  56     3554   2222    267   -269    104    -54       C  
ATOM    436  N   LEU A  57     -48.798 -20.844   6.155  1.00 17.12           N  
ANISOU  436  N   LEU A  57     3128   2437    939    -37     43    141       N  
ATOM    437  CA  LEU A  57     -47.422 -21.168   5.761  1.00 15.88           C  
ANISOU  437  CA  LEU A  57     3091   2353    587   -188     71    104       C  
ATOM    438  C   LEU A  57     -46.696 -22.082   6.742  1.00 16.95           C  
ANISOU  438  C   LEU A  57     3226   2341    873    -58     51    155       C  
ATOM    439  O   LEU A  57     -45.547 -22.444   6.528  1.00 18.45           O  
ANISOU  439  O   LEU A  57     3372   2658    979    116    120    170       O  
ATOM    440  CB  LEU A  57     -46.614 -19.878   5.612  1.00 15.21           C  
ANISOU  440  CB  LEU A  57     3015   2292    470   -158    -25     42       C  
ATOM    441  CG  LEU A  57     -47.064 -18.869   4.540  1.00 15.00           C  
ANISOU  441  CG  LEU A  57     2984   2058    656   -117   -123    -59       C  
ATOM    442  CD1 LEU A  57     -46.226 -17.597   4.606  1.00 14.66           C  
ANISOU  442  CD1 LEU A  57     2848   1994    728    -41    -59    -18       C  
ATOM    443  CD2 LEU A  57     -46.992 -19.510   3.154  1.00 15.91           C  
ANISOU  443  CD2 LEU A  57     2961   2323    762   -165    109   -223       C  
ATOM    444  N   GLY A  58     -47.360 -22.443   7.825  1.00 17.17           N  
ANISOU  444  N   GLY A  58     3275   2409    837   -104     61    144       N  
ATOM    445  CA  GLY A  58     -46.698 -23.181   8.895  1.00 18.35           C  
ANISOU  445  CA  GLY A  58     3447   2600    923     24      1    188       C  
ATOM    446  C   GLY A  58     -45.645 -22.356   9.606  1.00 18.22           C  
ANISOU  446  C   GLY A  58     3232   2638   1051     63    148    172       C  
ATOM    447  O   GLY A  58     -44.660 -22.898  10.081  1.00 19.36           O  
ANISOU  447  O   GLY A  58     3477   2810   1065    124    -67    266       O  
ATOM    448  N   ALA A  59     -45.861 -21.042   9.665  1.00 18.52           N  
ANISOU  448  N   ALA A  59     3331   2569   1136    -65    220     82       N  
ATOM    449  CA  ALA A  59     -44.970 -20.108  10.347  1.00 17.53           C  
ANISOU  449  CA  ALA A  59     3187   2691    783     33    108    135       C  
ATOM    450  C   ALA A  59     -45.560 -19.625  11.658  1.00 18.23           C  
ANISOU  450  C   ALA A  59     3358   2720    846    215    187    203       C  
ATOM    451  O   ALA A  59     -46.725 -19.883  11.966  1.00 18.64           O  
ANISOU  451  O   ALA A  59     3338   2836    905     93     97    252       O  
ATOM    452  CB  ALA A  59     -44.698 -18.910   9.448  1.00 16.10           C  
ANISOU  452  CB  ALA A  59     3010   2553    554     63    136     -4       C  
ATOM    453  N   MET A  60     -44.739 -18.904  12.402  1.00 19.03           N  
ANISOU  453  N   MET A  60     3355   2967    908    284     87    141       N  
ATOM    454  CA  MET A  60     -45.196 -18.164  13.547  1.00 19.40           C  
ANISOU  454  CA  MET A  60     3527   2757   1086    381   -118     -5       C  
ATOM    455  C   MET A  60     -45.638 -16.747  13.168  1.00 17.63           C  
ANISOU  455  C   MET A  60     3111   2636    949    193    221     24       C  
ATOM    456  O   MET A  60     -45.099 -16.177  12.229  1.00 17.09           O  
ANISOU  456  O   MET A  60     3106   2643    742    167     -7     80       O  
ATOM    457  CB  MET A  60     -44.110 -18.178  14.625  1.00 21.31           C  
ANISOU  457  CB  MET A  60     3782   3243   1069    310   -198     74       C  
ATOM    458  CG  MET A  60     -43.867 -19.556  15.244  1.00 26.64           C  
ANISOU  458  CG  MET A  60     4780   3777   1563    737   -526    502       C  
ATOM    459  SD  MET A  60     -45.312 -20.215  16.086  1.00 38.25           S  
ANISOU  459  SD  MET A  60     6283   4860   3387   -290   -392    840       S  
ATOM    460  CE  MET A  60     -45.778 -21.631  15.075  1.00 29.58           C  
ANISOU  460  CE  MET A  60     4550   4368   2320    830    -48    675       C  
ATOM    461  N   PRO A  61     -46.654 -16.219  13.861  1.00 17.51           N  
ANISOU  461  N   PRO A  61     3130   2534    989    223    225      9       N  
ATOM    462  CA  PRO A  61     -47.155 -14.897  13.486  1.00 16.34           C  
ANISOU  462  CA  PRO A  61     2954   2470    781    218    315   -103       C  
ATOM    463  C   PRO A  61     -46.065 -13.823  13.359  1.00 16.41           C  
ANISOU  463  C   PRO A  61     3009   2553    672    167    168     -2       C  
ATOM    464  O   PRO A  61     -46.079 -13.031  12.398  1.00 16.78           O  
ANISOU  464  O   PRO A  61     3069   2436    869    113     70     83       O  
ATOM    465  CB  PRO A  61     -48.125 -14.569  14.625  1.00 17.32           C  
ANISOU  465  CB  PRO A  61     2921   2519   1141    260    514    -64       C  
ATOM    466  CG  PRO A  61     -48.621 -15.904  15.062  1.00 18.48           C  
ANISOU  466  CG  PRO A  61     3183   2634   1202    337    528    222       C  
ATOM    467  CD  PRO A  61     -47.436 -16.825  14.959  1.00 18.61           C  
ANISOU  467  CD  PRO A  61     3172   2797   1102    373    409     40       C  
ATOM    468  N   SER A  62     -45.130 -13.793  14.307  1.00 16.34           N  
ANISOU  468  N   SER A  62     2977   2578    651    233    171     -5       N  
ATOM    469  CA  SER A  62     -44.079 -12.778  14.304  1.00 16.66           C  
ANISOU  469  CA  SER A  62     2986   2641    700    120    110    -93       C  
ATOM    470  C   SER A  62     -43.162 -12.850  13.074  1.00 16.30           C  
ANISOU  470  C   SER A  62     3043   2389    761    112    166     73       C  
ATOM    471  O   SER A  62     -42.494 -11.874  12.748  1.00 16.46           O  
ANISOU  471  O   SER A  62     3062   2509    683    -67    137    -20       O  
ATOM    472  CB  SER A  62     -43.248 -12.860  15.585  1.00 18.29           C  
ANISOU  472  CB  SER A  62     3211   3127    608     49     92   -103       C  
ATOM    473  OG  SER A  62     -42.388 -13.969  15.520  1.00 19.39           O  
ANISOU  473  OG  SER A  62     3416   3338    612    272    250    485       O  
ATOM    474  N   GLU A  63     -43.153 -13.999  12.395  1.00 15.99           N  
ANISOU  474  N   GLU A  63     3068   2489    517    130     52     47       N  
ATOM    475  CA  GLU A  63     -42.344 -14.209  11.195  1.00 15.28           C  
ANISOU  475  CA  GLU A  63     2789   2367    648    267     60    159       C  
ATOM    476  C   GLU A  63     -42.982 -13.672   9.908  1.00 15.11           C  
ANISOU  476  C   GLU A  63     2754   2349    637    193    -13     81       C  
ATOM    477  O   GLU A  63     -42.360 -13.751   8.842  1.00 14.38           O  
ANISOU  477  O   GLU A  63     2678   2246    539    219   -125     20       O  
ATOM    478  CB  GLU A  63     -42.014 -15.687  11.037  1.00 15.78           C  
ANISOU  478  CB  GLU A  63     2852   2373    769    239    -18    202       C  
ATOM    479  CG  GLU A  63     -41.276 -16.235  12.244  1.00 16.51           C  
ANISOU  479  CG  GLU A  63     2949   2539    784    304     -7    273       C  
ATOM    480  CD  GLU A  63     -41.014 -17.718  12.140  1.00 18.11           C  
ANISOU  480  CD  GLU A  63     3053   2630   1198    346    108    102       C  
ATOM    481  OE1 GLU A  63     -39.852 -18.121  12.350  1.00 19.49           O  
ANISOU  481  OE1 GLU A  63     3205   2961   1238    385   -293    228       O  
ATOM    482  OE2 GLU A  63     -41.968 -18.476  11.853  1.00 17.69           O  
ANISOU  482  OE2 GLU A  63     3318   2605    797    149    -10    195       O  
ATOM    483  N   ILE A  64     -44.198 -13.134  10.011  1.00 14.17           N  
ANISOU  483  N   ILE A  64     2768   2165    448    163    -81    103       N  
ATOM    484  CA  ILE A  64     -44.856 -12.469   8.877  1.00 14.37           C  
ANISOU  484  CA  ILE A  64     2775   2095    587    178   -143    118       C  
ATOM    485  C   ILE A  64     -44.617 -10.949   8.913  1.00 14.30           C  
ANISOU  485  C   ILE A  64     2747   2103    581    137    -28     88       C  
ATOM    486  O   ILE A  64     -45.041 -10.266   9.851  1.00 14.59           O  
ANISOU  486  O   ILE A  64     2742   2171    630     75    123     87       O  
ATOM    487  CB  ILE A  64     -46.371 -12.805   8.821  1.00 14.01           C  
ANISOU  487  CB  ILE A  64     2795   2136    392    141   -191     69       C  
ATOM    488  CG1 ILE A  64     -46.593 -14.335   8.842  1.00 15.08           C  
ANISOU  488  CG1 ILE A  64     3074   2184    471    124   -134    -29       C  
ATOM    489  CG2 ILE A  64     -47.051 -12.121   7.624  1.00 14.67           C  
ANISOU  489  CG2 ILE A  64     2825   2021    726    169   -229    271       C  
ATOM    490  CD1 ILE A  64     -45.882 -15.138   7.753  1.00 15.48           C  
ANISOU  490  CD1 ILE A  64     2859   2205    818    244     44     -7       C  
ATOM    491  N   VAL A  65     -43.901 -10.444   7.906  1.00 14.06           N  
ANISOU  491  N   VAL A  65     2635   2112    593     84    -58     34       N  
ATOM    492  CA  VAL A  65     -43.630  -9.018   7.772  1.00 13.76           C  
ANISOU  492  CA  VAL A  65     2621   2105    501     74     40     95       C  
ATOM    493  C   VAL A  65     -44.544  -8.461   6.680  1.00 13.93           C  
ANISOU  493  C   VAL A  65     2536   2048    706    154     -7     22       C  
ATOM    494  O   VAL A  65     -44.426  -8.869   5.511  1.00 13.47           O  
ANISOU  494  O   VAL A  65     2519   1909    688    186     54     85       O  
ATOM    495  CB  VAL A  65     -42.136  -8.763   7.421  1.00 13.39           C  
ANISOU  495  CB  VAL A  65     2493   1918    676    203   -146    146       C  
ATOM    496  CG1 VAL A  65     -41.850  -7.278   7.194  1.00 13.41           C  
ANISOU  496  CG1 VAL A  65     2542   1949    603    131   -105    174       C  
ATOM    497  CG2 VAL A  65     -41.217  -9.324   8.511  1.00 14.18           C  
ANISOU  497  CG2 VAL A  65     2754   2171    461    190   -185    122       C  
ATOM    498  N   PHE A  66     -45.441  -7.535   7.018  1.00 13.20           N  
ANISOU  498  N   PHE A  66     2365   2023    626     61     86     58       N  
ATOM    499  CA  PHE A  66     -46.262  -6.930   5.974  1.00 13.71           C  
ANISOU  499  CA  PHE A  66     2399   2156    652    197    169    115       C  
ATOM    500  C   PHE A  66     -45.480  -5.975   5.074  1.00 13.81           C  
ANISOU  500  C   PHE A  66     2437   2095    713    121     63    108       C  
ATOM    501  O   PHE A  66     -44.570  -5.279   5.529  1.00 13.54           O  
ANISOU  501  O   PHE A  66     2447   2140    554    212     42    -55       O  
ATOM    502  CB  PHE A  66     -47.501  -6.256   6.553  1.00 14.09           C  
ANISOU  502  CB  PHE A  66     2415   2120    819    152    211     37       C  
ATOM    503  CG  PHE A  66     -48.485  -7.224   7.125  1.00 14.71           C  
ANISOU  503  CG  PHE A  66     2526   2294    766    -26    193    -15       C  
ATOM    504  CD1 PHE A  66     -48.706  -7.279   8.492  1.00 14.80           C  
ANISOU  504  CD1 PHE A  66     2528   2361    735    -32     47    144       C  
ATOM    505  CD2 PHE A  66     -49.174  -8.106   6.303  1.00 15.54           C  
ANISOU  505  CD2 PHE A  66     2499   2367   1035   -186     84     40       C  
ATOM    506  CE1 PHE A  66     -49.615  -8.190   9.028  1.00 14.92           C  
ANISOU  506  CE1 PHE A  66     2576   2368    723    -76    104     78       C  
ATOM    507  CE2 PHE A  66     -50.082  -9.011   6.830  1.00 15.10           C  
ANISOU  507  CE2 PHE A  66     2580   2377    780    -89    185    198       C  
ATOM    508  CZ  PHE A  66     -50.301  -9.064   8.198  1.00 14.95           C  
ANISOU  508  CZ  PHE A  66     2548   2405    726    -55     65     65       C  
ATOM    509  N   THR A  67     -45.826  -5.982   3.790  1.00 14.01           N  
ANISOU  509  N   THR A  67     2477   2142    702    107     61    154       N  
ATOM    510  CA  THR A  67     -45.209  -5.106   2.795  1.00 13.62           C  
ANISOU  510  CA  THR A  67     2420   2137    617    162      0    142       C  
ATOM    511  C   THR A  67     -46.300  -4.679   1.865  1.00 14.11           C  
ANISOU  511  C   THR A  67     2515   2158    687    169    -20    225       C  
ATOM    512  O   THR A  67     -47.488  -5.021   2.083  1.00 14.05           O  
ANISOU  512  O   THR A  67     2439   2198    700    191    -99    291       O  
ATOM    513  CB  THR A  67     -44.193  -5.881   1.949  1.00 13.38           C  
ANISOU  513  CB  THR A  67     2464   2156    462    155    -66     62       C  
ATOM    514  OG1 THR A  67     -44.900  -6.904   1.233  1.00 13.28           O  
ANISOU  514  OG1 THR A  67     2417   2055    573    111    -14    148       O  
ATOM    515  CG2 THR A  67     -43.082  -6.527   2.828  1.00 13.74           C  
ANISOU  515  CG2 THR A  67     2383   2197    641    233     44    131       C  
ATOM    516  N   CYS A  68     -45.917  -3.927   0.828  1.00 14.04           N  
ANISOU  516  N   CYS A  68     2730   2063    541    182    -75    147       N  
ATOM    517  CA ACYS A  68     -46.967  -3.778  -0.084  0.50 14.76           C  
ANISOU  517  CA ACYS A  68     2606   2184    817     99   -136     95       C  
ATOM    518  CA BCYS A  68     -46.809  -3.564  -0.306  0.50 14.73           C  
ANISOU  518  CA BCYS A  68     2598   2188    809    151   -183    174       C  
ATOM    519  C   CYS A  68     -47.185  -4.709  -1.233  1.00 14.64           C  
ANISOU  519  C   CYS A  68     2694   2285    582     83    -52    151       C  
ATOM    520  O   CYS A  68     -48.070  -4.485  -2.038  1.00 15.33           O  
ANISOU  520  O   CYS A  68     2546   2464    814    119      5    197       O  
ATOM    521  CB ACYS A  68     -47.019  -2.415  -0.656  0.50 15.96           C  
ANISOU  521  CB ACYS A  68     2838   2223   1001    130   -122    158       C  
ATOM    522  CB BCYS A  68     -46.243  -2.437  -1.199  0.50 15.92           C  
ANISOU  522  CB BCYS A  68     2842   2442    764    114    -11    235       C  
ATOM    523  SG ACYS A  68     -45.708  -2.119  -1.834  0.50 19.39           S  
ANISOU  523  SG ACYS A  68     3442   2790   1132    -26    250    -91       S  
ATOM    524  SG BCYS A  68     -46.010  -0.876  -0.367  0.50 18.32           S  
ANISOU  524  SG BCYS A  68     3220   2690   1048     25   -387     67       S  
ATOM    525  N   GLY A  69     -46.441  -5.759  -1.258  1.00 14.00           N  
ANISOU  525  N   GLY A  69     2636   2207    473     73   -126    152       N  
ATOM    526  CA  GLY A  69     -46.586  -6.698  -2.337  1.00 14.89           C  
ANISOU  526  CA  GLY A  69     2686   2325    647    105    -93     17       C  
ATOM    527  C   GLY A  69     -45.330  -7.514  -2.511  1.00 14.13           C  
ANISOU  527  C   GLY A  69     2670   2052    643     14    -16     24       C  
ATOM    528  O   GLY A  69     -44.337  -7.319  -1.793  1.00 14.59           O  
ANISOU  528  O   GLY A  69     2646   2197    700    -61    -37    -79       O  
ATOM    529  N   ALA A  70     -45.360  -8.449  -3.462  1.00 14.09           N  
ANISOU  529  N   ALA A  70     2714   2203    434     15    -30     28       N  
ATOM    530  CA  ALA A  70     -44.232  -9.345  -3.664  1.00 14.76           C  
ANISOU  530  CA  ALA A  70     2746   2091    769    -27     46    -55       C  
ATOM    531  C   ALA A  70     -42.999  -8.597  -4.176  1.00 14.92           C  
ANISOU  531  C   ALA A  70     2641   2177    849     -9    -19    -47       C  
ATOM    532  O   ALA A  70     -41.878  -9.020  -3.902  1.00 14.40           O  
ANISOU  532  O   ALA A  70     2591   2163    718    -24     65    -56       O  
ATOM    533  CB  ALA A  70     -44.605 -10.500  -4.591  1.00 15.18           C  
ANISOU  533  CB  ALA A  70     2855   2102    811     11     22    -94       C  
ATOM    534  N   SER A  71     -43.188  -7.495  -4.912  1.00 14.62           N  
ANISOU  534  N   SER A  71     2781   2066    706   -151    -79   -156       N  
ATOM    535  CA  SER A  71     -42.039  -6.683  -5.348  1.00 14.59           C  
ANISOU  535  CA  SER A  71     2747   2125    669   -112    -74   -139       C  
ATOM    536  C   SER A  71     -41.268  -6.113  -4.155  1.00 13.79           C  
ANISOU  536  C   SER A  71     2565   2062    612    -49    -25    -96       C  
ATOM    537  O   SER A  71     -40.049  -6.292  -4.052  1.00 13.93           O  
ANISOU  537  O   SER A  71     2554   2164    573    -41    119   -124       O  
ATOM    538  CB  SER A  71     -42.451  -5.545  -6.284  1.00 15.33           C  
ANISOU  538  CB  SER A  71     2913   2247    663    -83     28    -29       C  
ATOM    539  OG  SER A  71     -43.070  -6.042  -7.451  1.00 16.99           O  
ANISOU  539  OG  SER A  71     3037   2607    809   -271    -75    -74       O  
ATOM    540  N   GLU A  72     -41.962  -5.422  -3.254  1.00 13.63           N  
ANISOU  540  N   GLU A  72     2582   1986    607    -49    -17    -79       N  
ATOM    541  CA  GLU A  72     -41.297  -4.928  -2.061  1.00 13.70           C  
ANISOU  541  CA  GLU A  72     2512   2106    586     77    -46   -111       C  
ATOM    542  C   GLU A  72     -40.704  -6.082  -1.242  1.00 13.66           C  
ANISOU  542  C   GLU A  72     2439   2063    686     96      4   -114       C  
ATOM    543  O   GLU A  72     -39.558  -5.994  -0.764  1.00 14.33           O  
ANISOU  543  O   GLU A  72     2502   2177    764      5    -48    -14       O  
ATOM    544  CB  GLU A  72     -42.235  -4.079  -1.201  1.00 14.02           C  
ANISOU  544  CB  GLU A  72     2466   2165    692    134   -154   -235       C  
ATOM    545  CG  GLU A  72     -41.539  -3.632   0.079  1.00 13.56           C  
ANISOU  545  CG  GLU A  72     2375   2118    657    140   -210    -62       C  
ATOM    546  CD  GLU A  72     -42.425  -2.929   1.081  1.00 14.60           C  
ANISOU  546  CD  GLU A  72     2475   2279    791    125    -65    -56       C  
ATOM    547  OE1 GLU A  72     -41.955  -2.785   2.225  1.00 15.43           O  
ANISOU  547  OE1 GLU A  72     2739   2380    743    147    -65    -99       O  
ATOM    548  OE2 GLU A  72     -43.543  -2.508   0.749  1.00 13.89           O  
ANISOU  548  OE2 GLU A  72     2535   2251    491    141   -113     79       O  
ATOM    549  N   SER A  73     -41.454  -7.180  -1.132  1.00 13.68           N  
ANISOU  549  N   SER A  73     2466   2061    669    123     30    -26       N  
ATOM    550  CA  SER A  73     -40.968  -8.367  -0.417  1.00 13.76           C  
ANISOU  550  CA  SER A  73     2460   2062    705     73    116     24       C  
ATOM    551  C   SER A  73     -39.693  -8.944  -1.012  1.00 14.31           C  
ANISOU  551  C   SER A  73     2467   2229    739     99     53    -64       C  
ATOM    552  O   SER A  73     -38.758  -9.227  -0.267  1.00 13.44           O  
ANISOU  552  O   SER A  73     2519   2115    470     92    158    -66       O  
ATOM    553  CB  SER A  73     -42.032  -9.455  -0.347  1.00 14.21           C  
ANISOU  553  CB  SER A  73     2481   2114    802     69    127     55       C  
ATOM    554  OG  SER A  73     -43.134  -8.998   0.399  1.00 14.24           O  
ANISOU  554  OG  SER A  73     2597   2351    461    130     81     74       O  
ATOM    555  N   ASN A  74     -39.643  -9.092  -2.337  1.00 14.76           N  
ANISOU  555  N   ASN A  74     2568   2317    722     21    158      6       N  
ATOM    556  CA  ASN A  74     -38.438  -9.572  -3.003  1.00 14.85           C  
ANISOU  556  CA  ASN A  74     2478   2420    743     24     75    -73       C  
ATOM    557  C   ASN A  74     -37.253  -8.650  -2.746  1.00 14.05           C  
ANISOU  557  C   ASN A  74     2467   2258    610     61     45   -104       C  
ATOM    558  O   ASN A  74     -36.146  -9.100  -2.512  1.00 14.81           O  
ANISOU  558  O   ASN A  74     2555   2312    759    108    -29     15       O  
ATOM    559  CB  ASN A  74     -38.664  -9.671  -4.518  1.00 14.81           C  
ANISOU  559  CB  ASN A  74     2512   2402    711    -10    154   -128       C  
ATOM    560  CG  ASN A  74     -39.583 -10.812  -4.917  1.00 15.16           C  
ANISOU  560  CG  ASN A  74     2666   2391    702    -24    103    -24       C  
ATOM    561  OD1 ASN A  74     -40.115 -10.834  -6.042  1.00 17.08           O  
ANISOU  561  OD1 ASN A  74     2902   2764    824     84    -69    -40       O  
ATOM    562  ND2 ASN A  74     -39.771 -11.773  -4.020  1.00 13.12           N  
ANISOU  562  ND2 ASN A  74     2437   2170    375    246    -95   -151       N  
ATOM    563  N   ASN A  75     -37.504  -7.353  -2.804  1.00 13.99           N  
ANISOU  563  N   ASN A  75     2481   2271    561     38     93    -10       N  
ATOM    564  CA  ASN A  75     -36.471  -6.365  -2.560  1.00 14.10           C  
ANISOU  564  CA  ASN A  75     2491   2251    616     33     74     60       C  
ATOM    565  C   ASN A  75     -35.922  -6.468  -1.134  1.00 14.30           C  
ANISOU  565  C   ASN A  75     2454   2262    715    130    -10    151       C  
ATOM    566  O   ASN A  75     -34.712  -6.444  -0.943  1.00 14.07           O  
ANISOU  566  O   ASN A  75     2491   2213    640     75     52    130       O  
ATOM    567  CB  ASN A  75     -36.997  -4.964  -2.855  1.00 14.05           C  
ANISOU  567  CB  ASN A  75     2484   2241    612     43    109     56       C  
ATOM    568  CG  ASN A  75     -36.885  -4.591  -4.327  1.00 14.40           C  
ANISOU  568  CG  ASN A  75     2550   2270    651   -151     10    150       C  
ATOM    569  OD1 ASN A  75     -37.678  -5.025  -5.172  1.00 16.04           O  
ANISOU  569  OD1 ASN A  75     2816   2441    835   -213     25   -172       O  
ATOM    570  ND2 ASN A  75     -35.916  -3.759  -4.630  1.00 12.28           N  
ANISOU  570  ND2 ASN A  75     2206   2188    271    -12     15    185       N  
ATOM    571  N   LEU A  76     -36.809  -6.607  -0.149  1.00 14.20           N  
ANISOU  571  N   LEU A  76     2516   2239    639    183     18     59       N  
ATOM    572  CA  LEU A  76     -36.397  -6.749   1.258  1.00 13.85           C  
ANISOU  572  CA  LEU A  76     2317   2285    660    117     -6      7       C  
ATOM    573  C   LEU A  76     -35.568  -8.014   1.474  1.00 14.12           C  
ANISOU  573  C   LEU A  76     2474   2232    656     60      2    141       C  
ATOM    574  O   LEU A  76     -34.502  -7.957   2.083  1.00 14.40           O  
ANISOU  574  O   LEU A  76     2609   2354    507    167    -62     65       O  
ATOM    575  CB  LEU A  76     -37.607  -6.734   2.189  1.00 14.17           C  
ANISOU  575  CB  LEU A  76     2380   2331    673     99     70    117       C  
ATOM    576  CG  LEU A  76     -37.295  -6.972   3.683  1.00 14.45           C  
ANISOU  576  CG  LEU A  76     2324   2542    623    -69     89      0       C  
ATOM    577  CD1 LEU A  76     -36.295  -5.964   4.239  1.00 15.22           C  
ANISOU  577  CD1 LEU A  76     2613   2689    480   -100    -68    -19       C  
ATOM    578  CD2 LEU A  76     -38.585  -6.931   4.484  1.00 14.24           C  
ANISOU  578  CD2 LEU A  76     2505   2377    528    258    223     82       C  
ATOM    579  N   ALA A  77     -36.048  -9.142   0.959  1.00 14.79           N  
ANISOU  579  N   ALA A  77     2602   2238    779    118      7     14       N  
ATOM    580  CA  ALA A  77     -35.311 -10.399   1.074  1.00 14.80           C  
ANISOU  580  CA  ALA A  77     2648   2251    722    146     47    -46       C  
ATOM    581  C   ALA A  77     -33.891 -10.302   0.528  1.00 15.41           C  
ANISOU  581  C   ALA A  77     2636   2476    743     89    -19    210       C  
ATOM    582  O   ALA A  77     -32.958 -10.762   1.174  1.00 14.71           O  
ANISOU  582  O   ALA A  77     2796   2518    274     58    -36     82       O  
ATOM    583  CB  ALA A  77     -36.059 -11.539   0.397  1.00 14.35           C  
ANISOU  583  CB  ALA A  77     2673   2142    637    227      6    -53       C  
ATOM    584  N   ILE A  78     -33.741  -9.693  -0.649  1.00 14.88           N  
ANISOU  584  N   ILE A  78     2474   2484    693     94     11    171       N  
ATOM    585  CA  ILE A  78     -32.465  -9.654  -1.355  1.00 14.84           C  
ANISOU  585  CA  ILE A  78     2412   2508    716     50    -77     86       C  
ATOM    586  C   ILE A  78     -31.530  -8.562  -0.816  1.00 15.18           C  
ANISOU  586  C   ILE A  78     2573   2463    729     -2    -18    110       C  
ATOM    587  O   ILE A  78     -30.384  -8.841  -0.409  1.00 15.59           O  
ANISOU  587  O   ILE A  78     2631   2527    765     66    -37    135       O  
ATOM    588  CB  ILE A  78     -32.705  -9.525  -2.879  1.00 14.42           C  
ANISOU  588  CB  ILE A  78     2455   2333    692     95     53    161       C  
ATOM    589  CG1 ILE A  78     -33.412 -10.798  -3.364  1.00 14.80           C  
ANISOU  589  CG1 ILE A  78     2376   2523    721    106   -154     36       C  
ATOM    590  CG2 ILE A  78     -31.392  -9.300  -3.606  1.00 14.84           C  
ANISOU  590  CG2 ILE A  78     2486   2465    687     18     13    100       C  
ATOM    591  CD1 ILE A  78     -33.966 -10.738  -4.778  1.00 15.73           C  
ANISOU  591  CD1 ILE A  78     2575   2658    744     88   -211    -21       C  
ATOM    592  N   LYS A  79     -32.015  -7.324  -0.824  1.00 15.20           N  
ANISOU  592  N   LYS A  79     2713   2439    624     66     19    105       N  
ATOM    593  CA  LYS A  79     -31.230  -6.180  -0.352  1.00 15.73           C  
ANISOU  593  CA  LYS A  79     2699   2501    776     79   -196     79       C  
ATOM    594  C   LYS A  79     -30.994  -6.240   1.152  1.00 16.09           C  
ANISOU  594  C   LYS A  79     2827   2536    748    164    -53    274       C  
ATOM    595  O   LYS A  79     -29.971  -5.761   1.644  1.00 18.11           O  
ANISOU  595  O   LYS A  79     2934   3009    936     71   -156    184       O  
ATOM    596  CB  LYS A  79     -31.905  -4.860  -0.727  1.00 16.88           C  
ANISOU  596  CB  LYS A  79     2899   2648    865    164   -209    327       C  
ATOM    597  CG  LYS A  79     -31.944  -4.605  -2.225  1.00 16.00           C  
ANISOU  597  CG  LYS A  79     2724   2596    760    179   -118     55       C  
ATOM    598  CD  LYS A  79     -32.886  -3.460  -2.553  1.00 16.71           C  
ANISOU  598  CD  LYS A  79     2938   2652    757    244   -131    199       C  
ATOM    599  CE  LYS A  79     -32.835  -3.132  -4.028  1.00 16.17           C  
ANISOU  599  CE  LYS A  79     2779   2597    765    308    -12    204       C  
ATOM    600  NZ  LYS A  79     -33.557  -1.865  -4.307  1.00 15.58           N  
ANISOU  600  NZ  LYS A  79     2934   2460    524    117    104    486       N  
ATOM    601  N   GLY A  80     -31.934  -6.844   1.874  1.00 15.53           N  
ANISOU  601  N   GLY A  80     2645   2533    720    259    -47    129       N  
ATOM    602  CA  GLY A  80     -31.808  -6.987   3.326  1.00 16.20           C  
ANISOU  602  CA  GLY A  80     2690   2722    743     90   -103    196       C  
ATOM    603  C   GLY A  80     -30.564  -7.774   3.698  1.00 17.73           C  
ANISOU  603  C   GLY A  80     2818   2800   1118    249   -106     69       C  
ATOM    604  O   GLY A  80     -29.948  -7.506   4.734  1.00 17.22           O  
ANISOU  604  O   GLY A  80     2798   2883    860    308     45    177       O  
ATOM    605  N   LEU A  81     -30.196  -8.756   2.867  1.00 16.53           N  
ANISOU  605  N   LEU A  81     2850   2670    759    -55     11    167       N  
ATOM    606  CA  LEU A  81     -28.984  -9.547   3.110  1.00 18.12           C  
ANISOU  606  CA  LEU A  81     2865   2839   1179     96     26    140       C  
ATOM    607  C   LEU A  81     -27.779  -8.862   2.492  1.00 18.53           C  
ANISOU  607  C   LEU A  81     2985   3162    893    133    117    188       C  
ATOM    608  O   LEU A  81     -26.696  -8.815   3.078  1.00 20.54           O  
ANISOU  608  O   LEU A  81     2887   3518   1399     23     87    114       O  
ATOM    609  CB  LEU A  81     -29.112 -10.969   2.567  1.00 18.08           C  
ANISOU  609  CB  LEU A  81     3095   3035    738     63     30     26       C  
ATOM    610  CG  LEU A  81     -30.048 -11.900   3.346  1.00 18.16           C  
ANISOU  610  CG  LEU A  81     3228   2762    909   -116   -322     56       C  
ATOM    611  CD1 LEU A  81     -30.062 -13.293   2.727  1.00 18.44           C  
ANISOU  611  CD1 LEU A  81     3039   2854   1112     52     -9   -169       C  
ATOM    612  CD2 LEU A  81     -29.661 -11.969   4.818  1.00 19.17           C  
ANISOU  612  CD2 LEU A  81     3289   3146    847    -77   -178    185       C  
ATOM    613  N   ALA A  82     -27.972  -8.352   1.285  1.00 18.85           N  
ANISOU  613  N   ALA A  82     3173   2998    991    118    254    314       N  
ATOM    614  CA  ALA A  82     -26.878  -7.760   0.551  1.00 19.02           C  
ANISOU  614  CA  ALA A  82     2940   3250   1035     29    116    175       C  
ATOM    615  C   ALA A  82     -26.365  -6.549   1.273  1.00 20.65           C  
ANISOU  615  C   ALA A  82     3071   3383   1390     67     57    -57       C  
ATOM    616  O   ALA A  82     -25.197  -6.287   1.233  1.00 20.43           O  
ANISOU  616  O   ALA A  82     3086   3434   1240    -32     92   -113       O  
ATOM    617  CB  ALA A  82     -27.288  -7.370  -0.853  1.00 17.76           C  
ANISOU  617  CB  ALA A  82     2842   3005    900    -10    423    279       C  
ATOM    618  N   PHE A  83     -27.249  -5.755   1.849  1.00 20.85           N  
ANISOU  618  N   PHE A  83     3096   3401   1425     34    188    -42       N  
ATOM    619  CA  PHE A  83     -26.773  -4.493   2.379  1.00 21.80           C  
ANISOU  619  CA  PHE A  83     3270   3435   1576     14    154    -97       C  
ATOM    620  C   PHE A  83     -26.003  -4.691   3.682  1.00 23.26           C  
ANISOU  620  C   PHE A  83     3230   3760   1848      7     24    -37       C  
ATOM    621  O   PHE A  83     -25.501  -3.737   4.247  1.00 24.38           O  
ANISOU  621  O   PHE A  83     3492   4054   1717     -1    196   -390       O  
ATOM    622  CB  PHE A  83     -27.892  -3.439   2.528  1.00 21.61           C  
ANISOU  622  CB  PHE A  83     3267   3499   1444     31     81   -491       C  
ATOM    623  CG  PHE A  83     -28.487  -2.931   1.223  1.00 23.03           C  
ANISOU  623  CG  PHE A  83     3628   3533   1589     67    465    212       C  
ATOM    624  CD1 PHE A  83     -29.626  -2.128   1.236  1.00 25.38           C  
ANISOU  624  CD1 PHE A  83     4130   3339   2172    190    161    256       C  
ATOM    625  CD2 PHE A  83     -27.936  -3.264  -0.001  1.00 22.00           C  
ANISOU  625  CD2 PHE A  83     3510   3370   1478   -138    -43   -439       C  
ATOM    626  CE1 PHE A  83     -30.180  -1.661   0.058  1.00 25.83           C  
ANISOU  626  CE1 PHE A  83     3931   3647   2234    143     41     78       C  
ATOM    627  CE2 PHE A  83     -28.478  -2.797  -1.177  1.00 24.28           C  
ANISOU  627  CE2 PHE A  83     3779   3498   1947    178     39    186       C  
ATOM    628  CZ  PHE A  83     -29.607  -1.998  -1.156  1.00 25.57           C  
ANISOU  628  CZ  PHE A  83     4020   3460   2233    223    -12    -42       C  
ATOM    629  N   LYS A  84     -25.942  -5.918   4.183  1.00 22.75           N  
ANISOU  629  N   LYS A  84     3075   3934   1632    149     40    103       N  
ATOM    630  CA ALYS A  84     -24.985  -6.153   5.241  0.50 24.14           C  
ANISOU  630  CA ALYS A  84     3131   4291   1749     63    -52     47       C  
ATOM    631  CA BLYS A  84     -25.009  -6.322   5.226  0.50 23.27           C  
ANISOU  631  CA BLYS A  84     3162   4066   1611     14    -12    136       C  
ATOM    632  C   LYS A  84     -23.583  -6.540   4.755  1.00 24.08           C  
ANISOU  632  C   LYS A  84     3227   4230   1692    172    -17    -79       C  
ATOM    633  O   LYS A  84     -22.684  -6.754   5.578  1.00 26.41           O  
ANISOU  633  O   LYS A  84     3231   4423   2380    277   -263   -106       O  
ATOM    634  CB ALYS A  84     -25.506  -7.208   6.189  0.50 26.19           C  
ANISOU  634  CB ALYS A  84     3408   4441   2100    100    -26    298       C  
ATOM    635  CB BLYS A  84     -25.459  -7.642   5.850  0.50 22.43           C  
ANISOU  635  CB BLYS A  84     2936   4063   1522    148   -203    240       C  
ATOM    636  CG ALYS A  84     -25.121  -6.950   7.620  0.50 28.21           C  
ANISOU  636  CG ALYS A  84     3512   4896   2310     74   -293    183       C  
ATOM    637  CG BLYS A  84     -26.856  -7.619   6.425  0.50 21.97           C  
ANISOU  637  CG BLYS A  84     3061   3919   1367    168    -49    227       C  
ATOM    638  CD ALYS A  84     -26.260  -6.304   8.392  0.50 29.15           C  
ANISOU  638  CD ALYS A  84     3578   4919   2577    169    -73    424       C  
ATOM    639  CD BLYS A  84     -27.011  -8.708   7.466  0.50 23.73           C  
ANISOU  639  CD BLYS A  84     3291   3988   1737     69    -98    395       C  
ATOM    640  CE ALYS A  84     -25.803  -5.875   9.776  0.50 31.53           C  
ANISOU  640  CE ALYS A  84     3385   5132   3464   -392   -810      8       C  
ATOM    641  CE BLYS A  84     -27.697  -9.933   6.904  0.50 22.96           C  
ANISOU  641  CE BLYS A  84     3392   3902   1427     94     17    369       C  
ATOM    642  NZ ALYS A  84     -24.670  -4.912   9.704  0.50 32.72           N  
ANISOU  642  NZ ALYS A  84     3599   5388   3443   -483    291   1029       N  
ATOM    643  NZ BLYS A  84     -26.987 -11.185   7.277  0.50 24.79           N  
ANISOU  643  NZ BLYS A  84     3197   4712   1507    443   -528    756       N  
ATOM    644  N   ARG A  85     -23.414  -6.604   3.440  1.00 23.22           N  
ANISOU  644  N   ARG A  85     3190   3924   1708     -6    168    -66       N  
ATOM    645  CA  ARG A  85     -22.200  -7.051   2.790  1.00 23.58           C  
ANISOU  645  CA  ARG A  85     3268   3810   1878    207    121   -101       C  
ATOM    646  C   ARG A  85     -21.582  -6.012   1.865  1.00 23.79           C  
ANISOU  646  C   ARG A  85     3201   3643   2195    130    245   -138       C  
ATOM    647  O   ARG A  85     -20.941  -6.372   0.893  1.00 23.47           O  
ANISOU  647  O   ARG A  85     3418   3608   1889    114     70   -270       O  
ATOM    648  CB  ARG A  85     -22.555  -8.223   1.892  1.00 23.72           C  
ANISOU  648  CB  ARG A  85     3170   3655   2188    151    121   -110       C  
ATOM    649  CG  ARG A  85     -22.922  -9.464   2.623  1.00 25.67           C  
ANISOU  649  CG  ARG A  85     3729   4007   2016     81     79     21       C  
ATOM    650  CD  ARG A  85     -22.663 -10.595   1.663  1.00 29.02           C  
ANISOU  650  CD  ARG A  85     4626   4197   2202   -193   -129   -266       C  
ATOM    651  NE  ARG A  85     -22.516 -11.777   2.435  1.00 32.53           N  
ANISOU  651  NE  ARG A  85     4810   4129   3420   -186   -323   -102       N  
ATOM    652  CZ  ARG A  85     -21.496 -12.612   2.372  1.00 32.84           C  
ANISOU  652  CZ  ARG A  85     5006   4246   3224      6     24   -394       C  
ATOM    653  NH1 ARG A  85     -20.493 -12.459   1.524  1.00 30.39           N  
ANISOU  653  NH1 ARG A  85     5346   4304   1895   -191   -355    177       N  
ATOM    654  NH2 ARG A  85     -21.517 -13.644   3.168  1.00 36.65           N  
ANISOU  654  NH2 ARG A  85     6253   5234   2437   -206   -394    -21       N  
ATOM    655  N   LEU A  86     -21.792  -4.734   2.113  1.00 22.83           N  
ANISOU  655  N   LEU A  86     3118   3560   1997    101     19   -215       N  
ATOM    656  CA  LEU A  86     -21.411  -3.763   1.105  1.00 24.83           C  
ANISOU  656  CA  LEU A  86     3579   3481   2374      1    310   -173       C  
ATOM    657  C   LEU A  86     -19.909  -3.749   0.830  1.00 27.32           C  
ANISOU  657  C   LEU A  86     3628   3899   2854    -23    237   -445       C  
ATOM    658  O   LEU A  86     -19.467  -3.333  -0.218  1.00 28.44           O  
ANISOU  658  O   LEU A  86     3596   4125   3085   -188    287   -242       O  
ATOM    659  CB  LEU A  86     -21.914  -2.397   1.514  1.00 24.92           C  
ANISOU  659  CB  LEU A  86     3450   3444   2574    -57    305   -201       C  
ATOM    660  CG  LEU A  86     -23.441  -2.303   1.558  1.00 23.11           C  
ANISOU  660  CG  LEU A  86     3420   3326   2035   -134    383   -228       C  
ATOM    661  CD1 LEU A  86     -23.839  -0.926   2.056  1.00 24.20           C  
ANISOU  661  CD1 LEU A  86     3688   3540   1965    116    134   -421       C  
ATOM    662  CD2 LEU A  86     -24.018  -2.546   0.177  1.00 24.19           C  
ANISOU  662  CD2 LEU A  86     3221   3795   2173   -229    226   -150       C  
ATOM    663  N   GLU A  87     -19.144  -4.161   1.827  1.00 26.96           N  
ANISOU  663  N   GLU A  87     3698   3793   2751    292    448   -572       N  
ATOM    664  CA  GLU A  87     -17.710  -4.197   1.690  1.00 28.43           C  
ANISOU  664  CA  GLU A  87     3711   3938   3153    113     13   -563       C  
ATOM    665  C   GLU A  87     -17.172  -5.482   1.065  1.00 27.38           C  
ANISOU  665  C   GLU A  87     3762   4003   2639     61     13   -577       C  
ATOM    666  O   GLU A  87     -16.438  -5.436   0.085  1.00 29.98           O  
ANISOU  666  O   GLU A  87     3455   4672   3263     65    316   -573       O  
ATOM    667  CB  GLU A  87     -17.077  -3.988   3.032  1.00 31.30           C  
ANISOU  667  CB  GLU A  87     4256   4370   3265    161    -35  -1190       C  
ATOM    668  CG  GLU A  87     -17.217  -2.559   3.519  1.00 38.43           C  
ANISOU  668  CG  GLU A  87     5244   4673   4684    389   -372  -1712       C  
ATOM    669  CD  GLU A  87     -16.577  -2.336   4.868  1.00 52.31           C  
ANISOU  669  CD  GLU A  87     7413   7049   5413    628  -1459  -2071       C  
ATOM    670  OE1 GLU A  87     -15.372  -2.636   5.016  1.00 56.27           O  
ANISOU  670  OE1 GLU A  87     7630   7568   6179   1215  -1272  -2214       O  
ATOM    671  OE2 GLU A  87     -17.276  -1.842   5.779  1.00 63.79           O  
ANISOU  671  OE2 GLU A  87     8303   8498   7435   1158   -408  -2741       O  
ATOM    672  N   GLU A  88     -17.563  -6.630   1.592  1.00 25.32           N  
ANISOU  672  N   GLU A  88     3746   3848   2027    -60   -435   -760       N  
ATOM    673  CA  GLU A  88     -17.020  -7.883   1.090  1.00 27.37           C  
ANISOU  673  CA  GLU A  88     4074   3977   2346    179   -168   -595       C  
ATOM    674  C   GLU A  88     -17.771  -8.405  -0.144  1.00 25.96           C  
ANISOU  674  C   GLU A  88     3576   3999   2288     48    -35   -437       C  
ATOM    675  O   GLU A  88     -17.270  -9.276  -0.850  1.00 28.03           O  
ANISOU  675  O   GLU A  88     3719   4192   2737    290     70   -517       O  
ATOM    676  CB  GLU A  88     -17.079  -8.912   2.197  1.00 29.87           C  
ANISOU  676  CB  GLU A  88     4405   4520   2423    183   -427   -301       C  
ATOM    677  CG  GLU A  88     -18.506  -9.298   2.489  1.00 32.24           C  
ANISOU  677  CG  GLU A  88     4505   4943   2800    235   -181   -215       C  
ATOM    678  CD  GLU A  88     -18.667 -10.199   3.671  1.00 37.19           C  
ANISOU  678  CD  GLU A  88     5695   5545   2889    437    198   -103       C  
ATOM    679  OE1 GLU A  88     -18.114 -11.317   3.648  1.00 44.24           O  
ANISOU  679  OE1 GLU A  88     6681   5633   4494    635   -406   -130       O  
ATOM    680  OE2 GLU A  88     -19.392  -9.793   4.590  1.00 39.17           O  
ANISOU  680  OE2 GLU A  88     6336   5736   2811    586     74   -721       O  
ATOM    681  N   LYS A  89     -18.965  -7.863  -0.403  1.00 23.72           N  
ANISOU  681  N   LYS A  89     3537   3709   1764     49      5   -360       N  
ATOM    682  CA  LYS A  89     -19.828  -8.273  -1.538  1.00 22.74           C  
ANISOU  682  CA  LYS A  89     3525   3519   1594     24    101   -313       C  
ATOM    683  C   LYS A  89     -20.219  -9.761  -1.478  1.00 23.34           C  
ANISOU  683  C   LYS A  89     3526   3583   1758    -60    184   -163       C  
ATOM    684  O   LYS A  89     -20.439 -10.235  -0.386  1.00 24.84           O  
ANISOU  684  O   LYS A  89     3912   3824   1701      7    -38    -51       O  
ATOM    685  CB  LYS A  89     -19.226  -7.870  -2.889  1.00 23.65           C  
ANISOU  685  CB  LYS A  89     3562   3725   1697   -157    111   -191       C  
ATOM    686  CG  LYS A  89     -18.644  -6.458  -2.957  1.00 26.20           C  
ANISOU  686  CG  LYS A  89     3743   3811   2400   -217     78   -321       C  
ATOM    687  CD  LYS A  89     -19.706  -5.369  -2.894  1.00 27.75           C  
ANISOU  687  CD  LYS A  89     3755   3851   2938   -241     21     -3       C  
ATOM    688  CE  LYS A  89     -19.057  -3.997  -2.888  1.00 31.16           C  
ANISOU  688  CE  LYS A  89     3654   4385   3800   -728   -382   -475       C  
ATOM    689  NZ  LYS A  89     -17.673  -4.099  -2.364  1.00 32.41           N  
ANISOU  689  NZ  LYS A  89     3569   4842   3903   -381   -121   -157       N  
ATOM    690  N   GLY A  90     -20.302 -10.487  -2.597  1.00 22.75           N  
ANISOU  690  N   GLY A  90     3258   3671   1716    -72   -143   -196       N  
ATOM    691  CA  GLY A  90     -20.623 -11.915  -2.554  1.00 22.62           C  
ANISOU  691  CA  GLY A  90     3352   3561   1680     62   -124    -15       C  
ATOM    692  C   GLY A  90     -21.464 -12.276  -3.751  1.00 20.38           C  
ANISOU  692  C   GLY A  90     3247   3174   1319    163    129    -80       C  
ATOM    693  O   GLY A  90     -21.645 -11.466  -4.634  1.00 20.86           O  
ANISOU  693  O   GLY A  90     3241   3215   1469    -38    283    113       O  
ATOM    694  N   HIS A  91     -21.989 -13.489  -3.745  1.00 20.35           N  
ANISOU  694  N   HIS A  91     3149   3185   1396    100    179   -113       N  
ATOM    695  CA  HIS A  91     -22.616 -14.095  -4.875  1.00 19.28           C  
ANISOU  695  CA  HIS A  91     3041   3039   1242    186    221    -40       C  
ATOM    696  C   HIS A  91     -24.006 -14.479  -4.496  1.00 19.19           C  
ANISOU  696  C   HIS A  91     3072   3068   1150    133    232    -91       C  
ATOM    697  O   HIS A  91     -24.247 -14.916  -3.385  1.00 18.20           O  
ANISOU  697  O   HIS A  91     3002   2781   1129    118    185   -155       O  
ATOM    698  CB  HIS A  91     -21.777 -15.310  -5.215  1.00 19.71           C  
ANISOU  698  CB  HIS A  91     3244   2976   1266    257    230     22       C  
ATOM    699  CG  HIS A  91     -22.316 -16.148  -6.303  1.00 20.10           C  
ANISOU  699  CG  HIS A  91     3259   3098   1281    140    358    -53       C  
ATOM    700  ND1 HIS A  91     -22.724 -17.395  -6.093  1.00 20.88           N  
ANISOU  700  ND1 HIS A  91     3296   3094   1542    204    400    -92       N  
ATOM    701  CD2 HIS A  91     -22.465 -15.905  -7.656  1.00 20.21           C  
ANISOU  701  CD2 HIS A  91     3180   3247   1249    200    426    -82       C  
ATOM    702  CE1 HIS A  91     -23.138 -17.920  -7.244  1.00 20.85           C  
ANISOU  702  CE1 HIS A  91     3353   3061   1508    271    472   -130       C  
ATOM    703  NE2 HIS A  91     -22.975 -17.007  -8.199  1.00 20.79           N  
ANISOU  703  NE2 HIS A  91     3423   3079   1394    341    543   -179       N  
ATOM    704  N   LEU A  92     -24.915 -14.349  -5.461  1.00 18.41           N  
ANISOU  704  N   LEU A  92     2956   2878   1159    115    274    -98       N  
ATOM    705  CA ALEU A  92     -26.299 -14.725  -5.300  0.50 18.47           C  
ANISOU  705  CA ALEU A  92     2999   2825   1194     38    199   -108       C  
ATOM    706  CA BLEU A  92     -26.307 -14.734  -5.321  0.50 18.24           C  
ANISOU  706  CA BLEU A  92     2976   2837   1116     65    195    -75       C  
ATOM    707  C   LEU A  92     -26.648 -15.692  -6.435  1.00 18.17           C  
ANISOU  707  C   LEU A  92     3133   2852    917     71    231     -5       C  
ATOM    708  O   LEU A  92     -26.182 -15.523  -7.538  1.00 18.23           O  
ANISOU  708  O   LEU A  92     3019   2850   1055     82    336     -7       O  
ATOM    709  CB ALEU A  92     -27.131 -13.450  -5.417  0.50 19.05           C  
ANISOU  709  CB ALEU A  92     3125   2807   1306     95    314    -77       C  
ATOM    710  CB BLEU A  92     -27.218 -13.529  -5.514  0.50 18.37           C  
ANISOU  710  CB BLEU A  92     2962   2850   1168     95    293    -16       C  
ATOM    711  CG ALEU A  92     -28.609 -13.625  -5.742  0.50 20.02           C  
ANISOU  711  CG ALEU A  92     3106   2894   1607     98    382    -98       C  
ATOM    712  CG BLEU A  92     -27.182 -12.399  -4.497  0.50 18.25           C  
ANISOU  712  CG BLEU A  92     2889   2930   1113    178    217    -22       C  
ATOM    713  CD1ALEU A  92     -29.263 -12.270  -5.985  0.50 24.55           C  
ANISOU  713  CD1ALEU A  92     3450   3304   2573    348    171    314       C  
ATOM    714  CD1BLEU A  92     -26.040 -11.431  -4.785  0.50 18.09           C  
ANISOU  714  CD1BLEU A  92     2956   2987    930    109    344   -140       C  
ATOM    715  CD2ALEU A  92     -28.810 -14.516  -6.949  0.50 20.69           C  
ANISOU  715  CD2ALEU A  92     3218   3145   1498    -48    148    -36       C  
ATOM    716  CD2BLEU A  92     -28.523 -11.682  -4.443  0.50 18.55           C  
ANISOU  716  CD2BLEU A  92     2903   2883   1259    170    317   -214       C  
ATOM    717  N   ILE A  93     -27.494 -16.667  -6.164  1.00 17.79           N  
ANISOU  717  N   ILE A  93     2976   2815    966     37    203   -171       N  
ATOM    718  CA  ILE A  93     -27.997 -17.533  -7.218  1.00 16.75           C  
ANISOU  718  CA  ILE A  93     2930   2531    901    203     29     34       C  
ATOM    719  C   ILE A  93     -29.483 -17.255  -7.405  1.00 16.91           C  
ANISOU  719  C   ILE A  93     2970   2615    839    175     77     58       C  
ATOM    720  O   ILE A  93     -30.257 -17.298  -6.456  1.00 17.22           O  
ANISOU  720  O   ILE A  93     2854   2703    984    225    121     63       O  
ATOM    721  CB  ILE A  93     -27.799 -19.019  -6.873  1.00 17.23           C  
ANISOU  721  CB  ILE A  93     2964   2473   1109     69     42     73       C  
ATOM    722  CG1 ILE A  93     -26.310 -19.354  -6.798  1.00 17.41           C  
ANISOU  722  CG1 ILE A  93     2988   2543   1081    278    394     92       C  
ATOM    723  CG2 ILE A  93     -28.481 -19.933  -7.895  1.00 16.34           C  
ANISOU  723  CG2 ILE A  93     3190   2401    617    164    200    111       C  
ATOM    724  CD1 ILE A  93     -26.021 -20.716  -6.171  1.00 17.80           C  
ANISOU  724  CD1 ILE A  93     3118   2626   1018    461    400    112       C  
ATOM    725  N   THR A  94     -29.878 -16.976  -8.642  1.00 15.83           N  
ANISOU  725  N   THR A  94     2960   2386    667     98    247    -57       N  
ATOM    726  CA  THR A  94     -31.297 -16.874  -9.008  1.00 16.52           C  
ANISOU  726  CA  THR A  94     3047   2466    763     44    129    -15       C  
ATOM    727  C   THR A  94     -31.542 -17.532 -10.383  1.00 17.14           C  
ANISOU  727  C   THR A  94     3021   2622    870    181    203   -204       C  
ATOM    728  O   THR A  94     -30.653 -18.245 -10.902  1.00 16.45           O  
ANISOU  728  O   THR A  94     3042   2551    656    205    186   -250       O  
ATOM    729  CB  THR A  94     -31.820 -15.417  -8.928  1.00 16.77           C  
ANISOU  729  CB  THR A  94     3084   2528    759    103    237   -109       C  
ATOM    730  OG1 THR A  94     -33.246 -15.410  -9.013  1.00 16.57           O  
ANISOU  730  OG1 THR A  94     3016   2545    731     -4    215    -69       O  
ATOM    731  CG2 THR A  94     -31.248 -14.547 -10.035  1.00 16.22           C  
ANISOU  731  CG2 THR A  94     3089   2488    582     23    160   -177       C  
ATOM    732  N   SER A  95     -32.729 -17.340 -10.955  1.00 17.27           N  
ANISOU  732  N   SER A  95     3152   2618    791     35     73   -181       N  
ATOM    733  CA  SER A  95     -32.973 -17.817 -12.324  1.00 16.37           C  
ANISOU  733  CA  SER A  95     3057   2493    667    132    186    -68       C  
ATOM    734  C   SER A  95     -33.131 -16.673 -13.309  1.00 16.77           C  
ANISOU  734  C   SER A  95     3148   2452    771    185    361    -92       C  
ATOM    735  O   SER A  95     -33.472 -15.562 -12.925  1.00 16.77           O  
ANISOU  735  O   SER A  95     3383   2433    554    123    146   -188       O  
ATOM    736  CB  SER A  95     -34.179 -18.771 -12.403  1.00 16.77           C  
ANISOU  736  CB  SER A  95     3032   2624    714    136    193   -128       C  
ATOM    737  OG  SER A  95     -35.427 -18.090 -12.357  1.00 16.37           O  
ANISOU  737  OG  SER A  95     3143   2468    608    280    285    -14       O  
ATOM    738  N   SER A  96     -32.902 -16.963 -14.586  1.00 17.20           N  
ANISOU  738  N   SER A  96     3357   2510    664    188    221      3       N  
ATOM    739  CA  SER A  96     -33.104 -15.961 -15.636  1.00 17.64           C  
ANISOU  739  CA  SER A  96     3430   2633    639    248    392     43       C  
ATOM    740  C   SER A  96     -34.588 -15.723 -15.982  1.00 17.49           C  
ANISOU  740  C   SER A  96     3368   2642    635    165    325    -40       C  
ATOM    741  O   SER A  96     -34.903 -14.873 -16.805  1.00 18.82           O  
ANISOU  741  O   SER A  96     3414   2871    866    248    428    138       O  
ATOM    742  CB  SER A  96     -32.336 -16.357 -16.898  1.00 18.43           C  
ANISOU  742  CB  SER A  96     3440   2877    686    264    345   -156       C  
ATOM    743  OG  SER A  96     -32.973 -17.462 -17.500  1.00 18.76           O  
ANISOU  743  OG  SER A  96     3594   2721    813    405    283   -131       O  
ATOM    744  N   ILE A  97     -35.499 -16.473 -15.370  1.00 16.87           N  
ANISOU  744  N   ILE A  97     3205   2617    585    146    275   -237       N  
ATOM    745  CA  ILE A  97     -36.918 -16.322 -15.676  1.00 17.06           C  
ANISOU  745  CA  ILE A  97     3161   2406    912    134    367   -135       C  
ATOM    746  C   ILE A  97     -37.737 -15.834 -14.494  1.00 16.66           C  
ANISOU  746  C   ILE A  97     3189   2447    693    196    204   -125       C  
ATOM    747  O   ILE A  97     -38.966 -15.924 -14.501  1.00 17.70           O  
ANISOU  747  O   ILE A  97     3341   2586    795   -102    167   -303       O  
ATOM    748  CB  ILE A  97     -37.543 -17.602 -16.274  1.00 17.63           C  
ANISOU  748  CB  ILE A  97     3444   2541    711     96    282   -221       C  
ATOM    749  CG1 ILE A  97     -37.259 -18.841 -15.405  1.00 17.44           C  
ANISOU  749  CG1 ILE A  97     3217   2521    889     46    332   -111       C  
ATOM    750  CG2 ILE A  97     -37.028 -17.809 -17.684  1.00 16.92           C  
ANISOU  750  CG2 ILE A  97     3169   2456    803    243    415    -46       C  
ATOM    751  CD1 ILE A  97     -38.171 -20.019 -15.698  1.00 19.05           C  
ANISOU  751  CD1 ILE A  97     3423   2396   1416     86    281    -75       C  
ATOM    752  N   GLU A  98     -37.051 -15.302 -13.486  1.00 16.45           N  
ANISOU  752  N   GLU A  98     3196   2361    694    193    138      5       N  
ATOM    753  CA  GLU A  98     -37.718 -14.619 -12.368  1.00 15.93           C  
ANISOU  753  CA  GLU A  98     3018   2298    736    182    114     -1       C  
ATOM    754  C   GLU A  98     -38.581 -13.436 -12.856  1.00 16.02           C  
ANISOU  754  C   GLU A  98     2818   2601    669    234    -11    -15       C  
ATOM    755  O   GLU A  98     -38.405 -12.931 -13.968  1.00 16.34           O  
ANISOU  755  O   GLU A  98     2968   2537    703    113    210    -88       O  
ATOM    756  CB  GLU A  98     -36.685 -14.072 -11.370  1.00 15.62           C  
ANISOU  756  CB  GLU A  98     3001   2335    599    244     77     23       C  
ATOM    757  CG  GLU A  98     -35.829 -15.094 -10.634  1.00 16.38           C  
ANISOU  757  CG  GLU A  98     3099   2301    822    279    256    170       C  
ATOM    758  CD  GLU A  98     -36.650 -16.072  -9.819  1.00 15.88           C  
ANISOU  758  CD  GLU A  98     2888   2206    939    206    176     73       C  
ATOM    759  OE1 GLU A  98     -36.380 -17.278  -9.931  1.00 16.27           O  
ANISOU  759  OE1 GLU A  98     2984   2219    977    264    160     32       O  
ATOM    760  OE2 GLU A  98     -37.549 -15.652  -9.063  1.00 15.06           O  
ANISOU  760  OE2 GLU A  98     3179   2054    490    263    169     46       O  
ATOM    761  N   HIS A  99     -39.503 -12.979 -12.022  1.00 15.41           N  
ANISOU  761  N   HIS A  99     2840   2375    640    232    -32    -50       N  
ATOM    762  CA  HIS A  99     -40.215 -11.742 -12.285  1.00 15.87           C  
ANISOU  762  CA  HIS A  99     2673   2482    871    232    230    101       C  
ATOM    763  C   HIS A  99     -39.204 -10.645 -12.429  1.00 16.23           C  
ANISOU  763  C   HIS A  99     2816   2566    785    132    145    137       C  
ATOM    764  O   HIS A  99     -38.135 -10.703 -11.817  1.00 16.16           O  
ANISOU  764  O   HIS A  99     2825   2407    909     54    102     89       O  
ATOM    765  CB  HIS A  99     -41.141 -11.440 -11.111  1.00 16.37           C  
ANISOU  765  CB  HIS A  99     3064   2452    703    168    277    -75       C  
ATOM    766  CG  HIS A  99     -42.036 -10.253 -11.338  1.00 16.91           C  
ANISOU  766  CG  HIS A  99     2945   2643    836    141     -4    108       C  
ATOM    767  ND1 HIS A  99     -43.310 -10.377 -11.734  1.00 18.68           N  
ANISOU  767  ND1 HIS A  99     2949   2968   1180    189    102    239       N  
ATOM    768  CD2 HIS A  99     -41.782  -8.889 -11.246  1.00 16.93           C  
ANISOU  768  CD2 HIS A  99     2857   2613    961    166    -64     35       C  
ATOM    769  CE1 HIS A  99     -43.859  -9.155 -11.854  1.00 18.34           C  
ANISOU  769  CE1 HIS A  99     2846   2857   1263    198     36     90       C  
ATOM    770  NE2 HIS A  99     -42.919  -8.247 -11.560  1.00 19.50           N  
ANISOU  770  NE2 HIS A  99     3030   2841   1536    346   -162    -51       N  
ATOM    771  N   LYS A 100     -39.519  -9.621 -13.216  1.00 17.16           N  
ANISOU  771  N   LYS A 100     2972   2393   1152    129    149    151       N  
ATOM    772  CA  LYS A 100     -38.537  -8.571 -13.466  1.00 17.43           C  
ANISOU  772  CA  LYS A 100     2960   2583   1078      3    -15     14       C  
ATOM    773  C   LYS A 100     -38.071  -7.831 -12.207  1.00 16.98           C  
ANISOU  773  C   LYS A 100     2895   2560    996    -20     89     41       C  
ATOM    774  O   LYS A 100     -36.971  -7.314 -12.191  1.00 17.03           O  
ANISOU  774  O   LYS A 100     2870   2625    973    -18    -32    -12       O  
ATOM    775  CB  LYS A 100     -39.026  -7.584 -14.538  1.00 18.68           C  
ANISOU  775  CB  LYS A 100     3494   2455   1149    117    146     54       C  
ATOM    776  CG  LYS A 100     -38.945  -8.104 -15.970  1.00 21.57           C  
ANISOU  776  CG  LYS A 100     3959   2897   1338    211    189   -238       C  
ATOM    777  CD  LYS A 100     -37.617  -7.786 -16.646  1.00 24.54           C  
ANISOU  777  CD  LYS A 100     4164   3454   1706    281    519   -358       C  
ATOM    778  CE  LYS A 100     -37.653  -8.112 -18.134  1.00 26.64           C  
ANISOU  778  CE  LYS A 100     4460   3934   1728    185    147   -384       C  
ATOM    779  NZ  LYS A 100     -36.265  -8.264 -18.645  1.00 32.84           N  
ANISOU  779  NZ  LYS A 100     4735   4527   3215    270    569   -365       N  
ATOM    780  N   CYS A 101     -38.891  -7.777 -11.163  1.00 16.60           N  
ANISOU  780  N   CYS A 101     2750   2534   1024     92     47    -22       N  
ATOM    781  CA  CYS A 101     -38.436  -7.138  -9.931  1.00 16.20           C  
ANISOU  781  CA  CYS A 101     2694   2397   1063     95    120    -78       C  
ATOM    782  C   CYS A 101     -37.203  -7.819  -9.348  1.00 16.05           C  
ANISOU  782  C   CYS A 101     2716   2386    994     -9    125     87       C  
ATOM    783  O   CYS A 101     -36.294  -7.140  -8.889  1.00 16.65           O  
ANISOU  783  O   CYS A 101     2911   2480    933      2     47    -22       O  
ATOM    784  CB  CYS A 101     -39.547  -6.992  -8.882  1.00 16.84           C  
ANISOU  784  CB  CYS A 101     2614   2499   1285      2    186   -178       C  
ATOM    785  SG  CYS A 101     -40.253  -8.528  -8.249  1.00 18.26           S  
ANISOU  785  SG  CYS A 101     3207   2773    957    -76    259    126       S  
ATOM    786  N   VAL A 102     -37.151  -9.146  -9.409  1.00 16.07           N  
ANISOU  786  N   VAL A 102     2674   2400   1032    113    154    -10       N  
ATOM    787  CA  VAL A 102     -35.989  -9.881  -8.910  1.00 15.72           C  
ANISOU  787  CA  VAL A 102     2682   2303    986     80    174    -47       C  
ATOM    788  C   VAL A 102     -34.792  -9.667  -9.837  1.00 16.02           C  
ANISOU  788  C   VAL A 102     2740   2569    779     35    120    -74       C  
ATOM    789  O   VAL A 102     -33.676  -9.441  -9.372  1.00 15.27           O  
ANISOU  789  O   VAL A 102     2626   2559    616    120    213   -101       O  
ATOM    790  CB  VAL A 102     -36.278 -11.394  -8.779  1.00 15.44           C  
ANISOU  790  CB  VAL A 102     2587   2366    912     45    186    112       C  
ATOM    791  CG1 VAL A 102     -35.012 -12.169  -8.413  1.00 14.44           C  
ANISOU  791  CG1 VAL A 102     2574   2388    523     72    167    -28       C  
ATOM    792  CG2 VAL A 102     -37.388 -11.632  -7.765  1.00 15.88           C  
ANISOU  792  CG2 VAL A 102     2738   2560    734     45    288   -171       C  
ATOM    793  N   LEU A 103     -35.028  -9.737 -11.144  1.00 15.69           N  
ANISOU  793  N   LEU A 103     2720   2455    786     42     30     40       N  
ATOM    794  CA  LEU A 103     -33.945  -9.538 -12.110  1.00 16.17           C  
ANISOU  794  CA  LEU A 103     2877   2588    677     24     64    -49       C  
ATOM    795  C   LEU A 103     -33.329  -8.150 -11.958  1.00 15.68           C  
ANISOU  795  C   LEU A 103     2841   2647    469     -6    129   -104       C  
ATOM    796  O   LEU A 103     -32.099  -7.994 -11.970  1.00 16.83           O  
ANISOU  796  O   LEU A 103     2911   2642    840    -10    218    -59       O  
ATOM    797  CB  LEU A 103     -34.436  -9.784 -13.551  1.00 16.35           C  
ANISOU  797  CB  LEU A 103     2970   2546    696     25     61   -149       C  
ATOM    798  CG  LEU A 103     -34.898 -11.213 -13.862  1.00 16.60           C  
ANISOU  798  CG  LEU A 103     2953   2494    857    152    -69   -226       C  
ATOM    799  CD1 LEU A 103     -35.443 -11.332 -15.286  1.00 17.00           C  
ANISOU  799  CD1 LEU A 103     3123   2756    579     78    207    -85       C  
ATOM    800  CD2 LEU A 103     -33.783 -12.221 -13.617  1.00 17.24           C  
ANISOU  800  CD2 LEU A 103     3100   2721    728    263    -54     80       C  
ATOM    801  N   ASN A 104     -34.187  -7.154 -11.772  1.00 15.90           N  
ANISOU  801  N   ASN A 104     2886   2573    581     -6     86   -177       N  
ATOM    802  CA  ASN A 104     -33.721  -5.780 -11.677  1.00 16.68           C  
ANISOU  802  CA  ASN A 104     2770   2648    917    -15    -65   -195       C  
ATOM    803  C   ASN A 104     -33.050  -5.459 -10.347  1.00 17.00           C  
ANISOU  803  C   ASN A 104     2931   2681    847    -15    -88   -143       C  
ATOM    804  O   ASN A 104     -32.051  -4.732 -10.337  1.00 17.56           O  
ANISOU  804  O   ASN A 104     3018   2832    822    -88    -21   -232       O  
ATOM    805  CB  ASN A 104     -34.832  -4.798 -12.038  1.00 16.40           C  
ANISOU  805  CB  ASN A 104     2721   2680    829    -40   -150     30       C  
ATOM    806  CG  ASN A 104     -35.162  -4.837 -13.520  1.00 18.83           C  
ANISOU  806  CG  ASN A 104     2844   3449    861     42   -173   -106       C  
ATOM    807  OD1 ASN A 104     -34.315  -5.198 -14.348  1.00 20.95           O  
ANISOU  807  OD1 ASN A 104     3377   3634    948    -52    235     50       O  
ATOM    808  ND2 ASN A 104     -36.398  -4.496 -13.863  1.00 18.08           N  
ANISOU  808  ND2 ASN A 104     2963   2699   1205    198   -264    155       N  
ATOM    809  N   THR A 105     -33.533  -6.024  -9.248  1.00 16.80           N  
ANISOU  809  N   THR A 105     2829   2564    989    -37    -23   -117       N  
ATOM    810  CA  THR A 105     -32.766  -5.850  -8.010  1.00 17.70           C  
ANISOU  810  CA  THR A 105     2923   2756   1045    124   -135   -266       C  
ATOM    811  C   THR A 105     -31.398  -6.533  -8.035  1.00 17.24           C  
ANISOU  811  C   THR A 105     2939   2530   1082     52    -20    -77       C  
ATOM    812  O   THR A 105     -30.412  -5.972  -7.553  1.00 17.35           O  
ANISOU  812  O   THR A 105     2977   2690    925     37     49   -232       O  
ATOM    813  CB  THR A 105     -33.557  -6.072  -6.686  1.00 19.27           C  
ANISOU  813  CB  THR A 105     3039   2864   1419   -134    -59    358       C  
ATOM    814  OG1 THR A 105     -32.942  -7.064  -5.841  1.00 23.35           O  
ANISOU  814  OG1 THR A 105     3457   3011   2404    290     30    606       O  
ATOM    815  CG2 THR A 105     -34.999  -6.303  -6.896  1.00 14.54           C  
ANISOU  815  CG2 THR A 105     3029   1922    571   -306   -117    177       C  
ATOM    816  N   CYS A 106     -31.318  -7.715  -8.640  1.00 16.17           N  
ANISOU  816  N   CYS A 106     2760   2720    662     71     86   -123       N  
ATOM    817  CA  CYS A 106     -30.036  -8.393  -8.795  1.00 16.97           C  
ANISOU  817  CA  CYS A 106     2850   2610    985     52    340   -221       C  
ATOM    818  C   CYS A 106     -29.099  -7.632  -9.746  1.00 16.97           C  
ANISOU  818  C   CYS A 106     2868   2604    976     53    180    -43       C  
ATOM    819  O   CYS A 106     -27.881  -7.595  -9.537  1.00 17.07           O  
ANISOU  819  O   CYS A 106     2906   2637    941     45     93   -283       O  
ATOM    820  CB  CYS A 106     -30.254  -9.825  -9.287  1.00 16.45           C  
ANISOU  820  CB  CYS A 106     2740   2500   1007     79    250    -90       C  
ATOM    821  SG  CYS A 106     -30.969 -10.928  -8.045  1.00 19.68           S  
ANISOU  821  SG  CYS A 106     3555   2859   1061    -70    259    135       S  
ATOM    822  N   GLY A 107     -29.671  -7.027 -10.787  1.00 16.79           N  
ANISOU  822  N   GLY A 107     2954   2686    736     -7    157   -150       N  
ATOM    823  CA  GLY A 107     -28.907  -6.195 -11.710  1.00 17.67           C  
ANISOU  823  CA  GLY A 107     3078   2806    826    -76    133    -56       C  
ATOM    824  C   GLY A 107     -28.275  -5.020 -10.991  1.00 18.22           C  
ANISOU  824  C   GLY A 107     3061   2807   1051     34     97    -97       C  
ATOM    825  O   GLY A 107     -27.122  -4.677 -11.229  1.00 18.99           O  
ANISOU  825  O   GLY A 107     3161   2970   1081    -33     44     88       O  
ATOM    826  N   PHE A 108     -29.038  -4.411 -10.092  1.00 17.40           N  
ANISOU  826  N   PHE A 108     3119   2664    826    118   -102   -107       N  
ATOM    827  CA  PHE A 108     -28.527  -3.333  -9.270  1.00 18.21           C  
ANISOU  827  CA  PHE A 108     3229   2891    799     25     16   -234       C  
ATOM    828  C   PHE A 108     -27.374  -3.795  -8.370  1.00 17.99           C  
ANISOU  828  C   PHE A 108     3067   2747   1019     44    112   -182       C  
ATOM    829  O   PHE A 108     -26.347  -3.124  -8.245  1.00 19.03           O  
ANISOU  829  O   PHE A 108     3183   2769   1278    -17     72   -167       O  
ATOM    830  CB  PHE A 108     -29.641  -2.729  -8.417  1.00 17.80           C  
ANISOU  830  CB  PHE A 108     3111   2851    799    -41    -25   -223       C  
ATOM    831  CG  PHE A 108     -29.115  -1.818  -7.353  1.00 19.76           C  
ANISOU  831  CG  PHE A 108     3447   2990   1069    -55     89   -533       C  
ATOM    832  CD1 PHE A 108     -28.526  -0.615  -7.709  1.00 20.65           C  
ANISOU  832  CD1 PHE A 108     3677   2621   1545     67   -146   -624       C  
ATOM    833  CD2 PHE A 108     -29.122  -2.197  -6.021  1.00 20.98           C  
ANISOU  833  CD2 PHE A 108     3519   3235   1215    156    -24   -249       C  
ATOM    834  CE1 PHE A 108     -27.992   0.226  -6.751  1.00 21.39           C  
ANISOU  834  CE1 PHE A 108     3861   2834   1430    -39   -169   -580       C  
ATOM    835  CE2 PHE A 108     -28.591  -1.359  -5.056  1.00 21.68           C  
ANISOU  835  CE2 PHE A 108     3721   2943   1572    287   -224   -304       C  
ATOM    836  CZ  PHE A 108     -28.022  -0.148  -5.422  1.00 22.52           C  
ANISOU  836  CZ  PHE A 108     3847   3153   1556     67   -186   -374       C  
ATOM    837  N   LEU A 109     -27.571  -4.926  -7.707  1.00 17.53           N  
ANISOU  837  N   LEU A 109     2903   2704   1050     85    127   -179       N  
ATOM    838  CA  LEU A 109     -26.507  -5.495  -6.907  1.00 17.19           C  
ANISOU  838  CA  LEU A 109     2789   2591   1151     11    174   -151       C  
ATOM    839  C   LEU A 109     -25.230  -5.698  -7.725  1.00 18.20           C  
ANISOU  839  C   LEU A 109     2960   2751   1201    -63    323    -82       C  
ATOM    840  O   LEU A 109     -24.147  -5.382  -7.254  1.00 19.32           O  
ANISOU  840  O   LEU A 109     3055   2929   1353   -145    265    -57       O  
ATOM    841  CB  LEU A 109     -26.950  -6.801  -6.246  1.00 16.50           C  
ANISOU  841  CB  LEU A 109     2668   2699    901    -56    401   -229       C  
ATOM    842  CG  LEU A 109     -28.070  -6.692  -5.201  1.00 16.19           C  
ANISOU  842  CG  LEU A 109     2608   2692    848   -194    351   -241       C  
ATOM    843  CD1 LEU A 109     -28.276  -8.047  -4.536  1.00 17.93           C  
ANISOU  843  CD1 LEU A 109     2657   2804   1349   -126    450     -8       C  
ATOM    844  CD2 LEU A 109     -27.777  -5.611  -4.160  1.00 16.34           C  
ANISOU  844  CD2 LEU A 109     2582   2783    844   -214    513   -305       C  
ATOM    845  N   GLU A 110     -25.352  -6.184  -8.961  1.00 18.21           N  
ANISOU  845  N   GLU A 110     2980   2803   1137     74    217    -28       N  
ATOM    846  CA  GLU A 110     -24.174  -6.312  -9.830  1.00 18.41           C  
ANISOU  846  CA  GLU A 110     3050   2747   1198     -3    313    -28       C  
ATOM    847  C   GLU A 110     -23.487  -4.971 -10.037  1.00 19.72           C  
ANISOU  847  C   GLU A 110     3175   2828   1488    -71    236    -33       C  
ATOM    848  O   GLU A 110     -22.258  -4.897 -10.054  1.00 20.47           O  
ANISOU  848  O   GLU A 110     3180   3177   1419   -161     74     60       O  
ATOM    849  CB  GLU A 110     -24.523  -6.928 -11.185  1.00 18.72           C  
ANISOU  849  CB  GLU A 110     3152   2745   1216     37    264    -58       C  
ATOM    850  CG  GLU A 110     -24.811  -8.416 -11.124  1.00 19.48           C  
ANISOU  850  CG  GLU A 110     3351   2718   1333    143    296   -255       C  
ATOM    851  CD  GLU A 110     -25.207  -8.976 -12.467  1.00 19.36           C  
ANISOU  851  CD  GLU A 110     3513   2810   1029    159    442    -37       C  
ATOM    852  OE1 GLU A 110     -24.355  -9.606 -13.109  1.00 23.58           O  
ANISOU  852  OE1 GLU A 110     3816   3761   1380    225    861   -402       O  
ATOM    853  OE2 GLU A 110     -26.367  -8.777 -12.886  1.00 19.68           O  
ANISOU  853  OE2 GLU A 110     3548   2848   1080    -56    318     41       O  
ATOM    854  N   SER A 111     -24.292  -3.919 -10.154  1.00 19.09           N  
ANISOU  854  N   SER A 111     3285   2747   1220      9    321    -75       N  
ATOM    855  CA  SER A 111     -23.792  -2.577 -10.439  1.00 20.23           C  
ANISOU  855  CA  SER A 111     3225   2880   1580   -140    224     59       C  
ATOM    856  C   SER A 111     -23.012  -1.982  -9.270  1.00 21.16           C  
ANISOU  856  C   SER A 111     3466   3049   1522   -238    241     51       C  
ATOM    857  O   SER A 111     -22.255  -1.028  -9.457  1.00 22.79           O  
ANISOU  857  O   SER A 111     3682   3230   1746   -472    -20     23       O  
ATOM    858  CB  SER A 111     -24.938  -1.647 -10.851  1.00 20.43           C  
ANISOU  858  CB  SER A 111     3370   2795   1597    -37    204     66       C  
ATOM    859  OG  SER A 111     -25.561  -1.065  -9.716  1.00 21.51           O  
ANISOU  859  OG  SER A 111     3677   2838   1657   -197    245   -101       O  
ATOM    860  N   ILE A 112     -23.205  -2.537  -8.072  1.00 21.29           N  
ANISOU  860  N   ILE A 112     3428   3011   1648   -168    215    139       N  
ATOM    861  CA  ILE A 112     -22.441  -2.107  -6.906  1.00 22.13           C  
ANISOU  861  CA  ILE A 112     3487   3140   1780   -151    249   -183       C  
ATOM    862  C   ILE A 112     -21.453  -3.187  -6.459  1.00 22.52           C  
ANISOU  862  C   ILE A 112     3450   3230   1874   -169    327   -168       C  
ATOM    863  O   ILE A 112     -20.963  -3.163  -5.336  1.00 23.86           O  
ANISOU  863  O   ILE A 112     3499   3585   1979   -184    266    -37       O  
ATOM    864  CB  ILE A 112     -23.324  -1.618  -5.726  1.00 21.09           C  
ANISOU  864  CB  ILE A 112     3079   3065   1868   -253    250    -73       C  
ATOM    865  CG1 ILE A 112     -24.316  -2.693  -5.285  1.00 19.48           C  
ANISOU  865  CG1 ILE A 112     3097   2712   1592   -136    131    -98       C  
ATOM    866  CG2 ILE A 112     -24.043  -0.313  -6.063  1.00 21.65           C  
ANISOU  866  CG2 ILE A 112     3366   2922   1937   -289     38   -143       C  
ATOM    867  CD1 ILE A 112     -24.951  -2.398  -3.946  1.00 21.92           C  
ANISOU  867  CD1 ILE A 112     3491   3161   1673    -42    230   -201       C  
ATOM    868  N   GLY A 113     -21.169  -4.133  -7.350  1.00 22.08           N  
ANISOU  868  N   GLY A 113     3342   3092   1953   -228    296   -166       N  
ATOM    869  CA  GLY A 113     -20.064  -5.061  -7.160  1.00 22.10           C  
ANISOU  869  CA  GLY A 113     3286   3222   1887   -283    236     11       C  
ATOM    870  C   GLY A 113     -20.380  -6.490  -6.762  1.00 21.43           C  
ANISOU  870  C   GLY A 113     3136   3225   1780   -159    263    -39       C  
ATOM    871  O   GLY A 113     -19.459  -7.279  -6.550  1.00 22.53           O  
ANISOU  871  O   GLY A 113     3173   3479   1907   -105     62    -37       O  
ATOM    872  N   PHE A 114     -21.663  -6.830  -6.653  1.00 20.65           N  
ANISOU  872  N   PHE A 114     3207   3167   1472   -256    533    -61       N  
ATOM    873  CA  PHE A 114     -22.080  -8.199  -6.337  1.00 19.22           C  
ANISOU  873  CA  PHE A 114     2965   3030   1308      3    552   -135       C  
ATOM    874  C   PHE A 114     -22.025  -9.079  -7.590  1.00 20.11           C  
ANISOU  874  C   PHE A 114     3313   2959   1369     -3    343   -160       C  
ATOM    875  O   PHE A 114     -22.157  -8.570  -8.706  1.00 21.72           O  
ANISOU  875  O   PHE A 114     3646   3318   1286     -8    386   -117       O  
ATOM    876  CB  PHE A 114     -23.491  -8.205  -5.708  1.00 18.24           C  
ANISOU  876  CB  PHE A 114     2962   3035    932   -103    516   -107       C  
ATOM    877  CG  PHE A 114     -23.539  -7.634  -4.307  1.00 18.21           C  
ANISOU  877  CG  PHE A 114     2904   3012   1001   -201    364   -205       C  
ATOM    878  CD1 PHE A 114     -23.558  -8.476  -3.186  1.00 19.70           C  
ANISOU  878  CD1 PHE A 114     3121   3248   1115     72    388    -28       C  
ATOM    879  CD2 PHE A 114     -23.574  -6.257  -4.102  1.00 20.00           C  
ANISOU  879  CD2 PHE A 114     3222   3009   1368    -63    333   -298       C  
ATOM    880  CE1 PHE A 114     -23.589  -7.952  -1.897  1.00 19.17           C  
ANISOU  880  CE1 PHE A 114     3068   3116   1099     71    419     16       C  
ATOM    881  CE2 PHE A 114     -23.618  -5.729  -2.818  1.00 19.22           C  
ANISOU  881  CE2 PHE A 114     2862   3287   1154     39    585   -102       C  
ATOM    882  CZ  PHE A 114     -23.617  -6.577  -1.723  1.00 19.87           C  
ANISOU  882  CZ  PHE A 114     2906   3081   1560   -132    495     14       C  
ATOM    883  N   ASP A 115     -21.787 -10.383  -7.401  1.00 19.78           N  
ANISOU  883  N   ASP A 115     3053   2992   1468     52    338    -91       N  
ATOM    884  CA  ASP A 115     -21.865 -11.359  -8.497  1.00 20.01           C  
ANISOU  884  CA  ASP A 115     3072   3104   1425    114    283   -135       C  
ATOM    885  C   ASP A 115     -23.171 -12.143  -8.448  1.00 18.79           C  
ANISOU  885  C   ASP A 115     3152   2953   1033    106    264    -69       C  
ATOM    886  O   ASP A 115     -23.625 -12.539  -7.366  1.00 18.27           O  
ANISOU  886  O   ASP A 115     3025   2849   1067    146    250    -69       O  
ATOM    887  CB  ASP A 115     -20.685 -12.334  -8.459  1.00 21.32           C  
ANISOU  887  CB  ASP A 115     3149   3303   1648    218    377    -18       C  
ATOM    888  CG  ASP A 115     -19.347 -11.640  -8.354  1.00 22.97           C  
ANISOU  888  CG  ASP A 115     3419   3504   1801    -19    315    -88       C  
ATOM    889  OD1 ASP A 115     -19.019 -10.801  -9.218  1.00 24.21           O  
ANISOU  889  OD1 ASP A 115     3330   3378   2487   -105    490     91       O  
ATOM    890  OD2 ASP A 115     -18.611 -11.959  -7.405  1.00 26.42           O  
ANISOU  890  OD2 ASP A 115     3406   4149   2481    322     24    -52       O  
ATOM    891  N   VAL A 116     -23.780 -12.371  -9.609  1.00 18.49           N  
ANISOU  891  N   VAL A 116     2999   2976   1048    108    274   -188       N  
ATOM    892  CA  VAL A 116     -25.048 -13.088  -9.672  1.00 18.00           C  
ANISOU  892  CA  VAL A 116     3141   2623   1074    107    269    -33       C  
ATOM    893  C   VAL A 116     -24.983 -14.104 -10.800  1.00 18.35           C  
ANISOU  893  C   VAL A 116     3212   2760    997     85    398    -72       C  
ATOM    894  O   VAL A 116     -24.523 -13.780 -11.888  1.00 19.50           O  
ANISOU  894  O   VAL A 116     3372   3099    935    187    436    -20       O  
ATOM    895  CB  VAL A 116     -26.249 -12.140  -9.950  1.00 17.48           C  
ANISOU  895  CB  VAL A 116     3034   2588   1017    143    504   -161       C  
ATOM    896  CG1 VAL A 116     -27.548 -12.909  -9.889  1.00 17.44           C  
ANISOU  896  CG1 VAL A 116     3039   2594    990    105    268    -84       C  
ATOM    897  CG2 VAL A 116     -26.317 -11.021  -8.919  1.00 17.93           C  
ANISOU  897  CG2 VAL A 116     3216   2456   1139    -32    369   -181       C  
ATOM    898  N   THR A 117     -25.491 -15.314 -10.561  1.00 17.99           N  
ANISOU  898  N   THR A 117     3259   2759    817    140    350      0       N  
ATOM    899  CA  THR A 117     -25.687 -16.328 -11.601  1.00 19.65           C  
ANISOU  899  CA  THR A 117     3311   2843   1311    115    292   -305       C  
ATOM    900  C   THR A 117     -27.180 -16.418 -11.947  1.00 18.77           C  
ANISOU  900  C   THR A 117     3265   2794   1072    233    447    -84       C  
ATOM    901  O   THR A 117     -27.947 -16.549 -11.032  1.00 18.33           O  
ANISOU  901  O   THR A 117     3370   2671    922    135    338     49       O  
ATOM    902  CB  THR A 117     -25.204 -17.676 -11.040  1.00 19.89           C  
ANISOU  902  CB  THR A 117     3339   2881   1337     71    177   -309       C  
ATOM    903  OG1 THR A 117     -23.787 -17.611 -10.782  1.00 20.19           O  
ANISOU  903  OG1 THR A 117     3303   3104   1264    411    176   -255       O  
ATOM    904  CG2 THR A 117     -25.511 -18.828 -11.986  1.00 20.78           C  
ANISOU  904  CG2 THR A 117     3636   2743   1514    336    349   -444       C  
ATOM    905  N   TYR A 118     -27.522 -16.191 -13.172  1.00 18.97           N  
ANISOU  905  N   TYR A 118     3295   2747   1166    172    235    -32       N  
ATOM    906  CA  TYR A 118     -28.890 -16.365 -13.511  1.00 17.11           C  
ANISOU  906  CA  TYR A 118     3102   2469    928    181    508    238       C  
ATOM    907  C   TYR A 118     -29.020 -17.712 -14.191  1.00 17.89           C  
ANISOU  907  C   TYR A 118     3295   2719    783    176    280     29       C  
ATOM    908  O   TYR A 118     -28.726 -17.846 -15.389  1.00 19.14           O  
ANISOU  908  O   TYR A 118     3455   2834    981    270    758    133       O  
ATOM    909  CB  TYR A 118     -29.292 -15.253 -14.441  1.00 17.61           C  
ANISOU  909  CB  TYR A 118     3308   2532    849    198    317    196       C  
ATOM    910  CG  TYR A 118     -29.108 -13.869 -13.861  1.00 18.53           C  
ANISOU  910  CG  TYR A 118     3304   2440   1293    188    369    239       C  
ATOM    911  CD1 TYR A 118     -30.165 -13.214 -13.234  1.00 17.66           C  
ANISOU  911  CD1 TYR A 118     3400   2418    891    152    299     84       C  
ATOM    912  CD2 TYR A 118     -27.891 -13.197 -13.963  1.00 18.31           C  
ANISOU  912  CD2 TYR A 118     3276   2760    922     55    268    105       C  
ATOM    913  CE1 TYR A 118     -30.014 -11.939 -12.713  1.00 17.45           C  
ANISOU  913  CE1 TYR A 118     3264   2549    816     23    300    -39       C  
ATOM    914  CE2 TYR A 118     -27.737 -11.909 -13.451  1.00 17.48           C  
ANISOU  914  CE2 TYR A 118     3180   2735    725    189    362    109       C  
ATOM    915  CZ  TYR A 118     -28.807 -11.289 -12.819  1.00 17.27           C  
ANISOU  915  CZ  TYR A 118     3138   2602    820    126    283    -44       C  
ATOM    916  OH  TYR A 118     -28.709 -10.015 -12.282  1.00 18.37           O  
ANISOU  916  OH  TYR A 118     3294   2677   1006    -45    465   -172       O  
ATOM    917  N   LEU A 119     -29.492 -18.712 -13.452  1.00 17.74           N  
ANISOU  917  N   LEU A 119     3178   2706    854    153    179     26       N  
ATOM    918  CA  LEU A 119     -29.654 -20.067 -13.986  1.00 17.40           C  
ANISOU  918  CA  LEU A 119     3162   2785    663    330    221   -145       C  
ATOM    919  C   LEU A 119     -30.648 -20.109 -15.149  1.00 18.49           C  
ANISOU  919  C   LEU A 119     3269   2994    762    261    150   -122       C  
ATOM    920  O   LEU A 119     -31.745 -19.542 -15.077  1.00 18.34           O  
ANISOU  920  O   LEU A 119     3337   2809    819    256    108   -189       O  
ATOM    921  CB  LEU A 119     -30.074 -21.026 -12.872  1.00 17.88           C  
ANISOU  921  CB  LEU A 119     2921   2878    994    262    235     35       C  
ATOM    922  CG  LEU A 119     -29.078 -21.199 -11.722  1.00 17.76           C  
ANISOU  922  CG  LEU A 119     3108   2853    785    366    243    -85       C  
ATOM    923  CD1 LEU A 119     -29.716 -21.969 -10.576  1.00 17.74           C  
ANISOU  923  CD1 LEU A 119     3247   2683    809    338    197    -80       C  
ATOM    924  CD2 LEU A 119     -27.798 -21.899 -12.167  1.00 18.82           C  
ANISOU  924  CD2 LEU A 119     3104   2904   1140    555   -231   -516       C  
ATOM    925  N   THR A 120     -30.277 -20.795 -16.225  1.00 19.34           N  
ANISOU  925  N   THR A 120     3401   3081    863    199    238   -230       N  
ATOM    926  CA  THR A 120     -31.159 -20.904 -17.408  1.00 20.29           C  
ANISOU  926  CA  THR A 120     3512   3282    914    361    115   -174       C  
ATOM    927  C   THR A 120     -32.078 -22.134 -17.335  1.00 21.02           C  
ANISOU  927  C   THR A 120     3637   3336   1012    266    172   -178       C  
ATOM    928  O   THR A 120     -31.615 -23.142 -16.900  1.00 22.40           O  
ANISOU  928  O   THR A 120     3775   3515   1218    322     85    -66       O  
ATOM    929  CB  THR A 120     -30.343 -20.970 -18.703  1.00 22.58           C  
ANISOU  929  CB  THR A 120     3602   3658   1316    220    439   -110       C  
ATOM    930  OG1 THR A 120     -29.625 -22.208 -18.749  1.00 30.10           O  
ANISOU  930  OG1 THR A 120     4535   4169   2732    634    447   -607       O  
ATOM    931  CG2 THR A 120     -29.351 -19.819 -18.759  1.00 21.19           C  
ANISOU  931  CG2 THR A 120     3486   3775    791    125    433    -14       C  
ATOM    932  N   PRO A 121     -33.364 -21.982 -17.605  1.00 20.28           N  
ANISOU  932  N   PRO A 121     3600   3196    910    289    176   -135       N  
ATOM    933  CA  PRO A 121     -34.322 -23.075 -17.438  1.00 20.20           C  
ANISOU  933  CA  PRO A 121     3915   2941    817    237     38   -117       C  
ATOM    934  C   PRO A 121     -34.119 -24.181 -18.473  1.00 21.48           C  
ANISOU  934  C   PRO A 121     3564   3070   1528    143    263   -477       C  
ATOM    935  O   PRO A 121     -33.364 -23.992 -19.425  1.00 22.23           O  
ANISOU  935  O   PRO A 121     3991   3188   1264    195    264   -410       O  
ATOM    936  CB  PRO A 121     -35.653 -22.376 -17.665  1.00 20.23           C  
ANISOU  936  CB  PRO A 121     3813   2729   1142    223    118     13       C  
ATOM    937  CG  PRO A 121     -35.315 -21.204 -18.543  1.00 20.06           C  
ANISOU  937  CG  PRO A 121     3645   2908   1067    188    207     66       C  
ATOM    938  CD  PRO A 121     -33.987 -20.740 -18.072  1.00 20.85           C  
ANISOU  938  CD  PRO A 121     3827   2937   1156    182     91   -280       C  
ATOM    939  N   LYS A 122     -34.810 -25.304 -18.331  1.00 21.06           N  
ANISOU  939  N   LYS A 122     4382   2583   1036    234    186   -196       N  
ATOM    940  CA  LYS A 122     -34.871 -26.227 -19.440  1.00 21.89           C  
ANISOU  940  CA  LYS A 122     4128   2986   1202    134    181   -472       C  
ATOM    941  C   LYS A 122     -35.989 -25.747 -20.332  1.00 20.84           C  
ANISOU  941  C   LYS A 122     4268   2790    859     65    222   -494       C  
ATOM    942  O   LYS A 122     -36.646 -24.773 -19.996  1.00 20.74           O  
ANISOU  942  O   LYS A 122     4266   2691    920     64    229   -239       O  
ATOM    943  CB  LYS A 122     -35.101 -27.627 -18.926  1.00 25.30           C  
ANISOU  943  CB  LYS A 122     4408   2913   2290     65     -3   -358       C  
ATOM    944  CG  LYS A 122     -33.826 -28.212 -18.349  1.00 30.30           C  
ANISOU  944  CG  LYS A 122     4524   3640   3346    262     17     16       C  
ATOM    945  CD  LYS A 122     -34.060 -29.497 -17.562  1.00 37.68           C  
ANISOU  945  CD  LYS A 122     5745   3985   4586   -196     77    419       C  
ATOM    946  CE  LYS A 122     -34.105 -30.740 -18.450  1.00 45.55           C  
ANISOU  946  CE  LYS A 122     6596   4967   5742    675    631   -605       C  
ATOM    947  NZ  LYS A 122     -33.204 -30.610 -19.630  1.00 50.23           N  
ANISOU  947  NZ  LYS A 122     6564   6322   6197    338    705     73       N  
ATOM    948  N   ALA A 123     -36.173 -26.379 -21.488  1.00 21.81           N  
ANISOU  948  N   ALA A 123     4384   2625   1275      2    -24   -758       N  
ATOM    949  CA  ALA A 123     -37.261 -26.012 -22.377  1.00 20.84           C  
ANISOU  949  CA  ALA A 123     4392   2628    895    -75    215   -557       C  
ATOM    950  C   ALA A 123     -38.608 -26.144 -21.683  1.00 21.89           C  
ANISOU  950  C   ALA A 123     4259   2900   1157   -146    100   -432       C  
ATOM    951  O   ALA A 123     -39.587 -25.506 -22.062  1.00 23.24           O  
ANISOU  951  O   ALA A 123     4597   3001   1230      5    236   -265       O  
ATOM    952  CB  ALA A 123     -37.225 -26.865 -23.633  1.00 23.16           C  
ANISOU  952  CB  ALA A 123     4605   2844   1348    -37    116   -968       C  
ATOM    953  N   SER A 124     -38.651 -26.974 -20.651  1.00 22.40           N  
ANISOU  953  N   SER A 124     4439   3038   1033     21     34   -408       N  
ATOM    954  CA  SER A 124     -39.869 -27.147 -19.857  1.00 21.59           C  
ANISOU  954  CA  SER A 124     4274   2568   1359   -152     24   -449       C  
ATOM    955  C   SER A 124     -40.191 -25.948 -18.957  1.00 21.06           C  
ANISOU  955  C   SER A 124     4083   2605   1312    142     -8   -337       C  
ATOM    956  O   SER A 124     -41.305 -25.839 -18.426  1.00 21.29           O  
ANISOU  956  O   SER A 124     4157   2819   1111     -4     56    -86       O  
ATOM    957  CB  SER A 124     -39.725 -28.380 -18.975  1.00 22.63           C  
ANISOU  957  CB  SER A 124     4580   2982   1033    223    -77   -283       C  
ATOM    958  OG  SER A 124     -38.601 -28.245 -18.117  1.00 23.41           O  
ANISOU  958  OG  SER A 124     4606   2663   1625   -126   -212   -262       O  
ATOM    959  N   GLY A 125     -39.198 -25.076 -18.772  1.00 19.71           N  
ANISOU  959  N   GLY A 125     4210   2297    981    100    -63   -144       N  
ATOM    960  CA  GLY A 125     -39.302 -23.957 -17.832  1.00 19.43           C  
ANISOU  960  CA  GLY A 125     4035   2512    833    301     38   -179       C  
ATOM    961  C   GLY A 125     -38.695 -24.276 -16.480  1.00 19.45           C  
ANISOU  961  C   GLY A 125     4158   2440    790     63    137     33       C  
ATOM    962  O   GLY A 125     -38.566 -23.403 -15.613  1.00 19.24           O  
ANISOU  962  O   GLY A 125     4068   2442    799    143     95     38       O  
ATOM    963  N   LEU A 126     -38.313 -25.536 -16.303  1.00 20.23           N  
ANISOU  963  N   LEU A 126     4289   2594    800    291     45    -24       N  
ATOM    964  CA  LEU A 126     -37.823 -26.015 -15.025  1.00 20.53           C  
ANISOU  964  CA  LEU A 126     4182   2458   1159    186   -215    152       C  
ATOM    965  C   LEU A 126     -36.400 -25.569 -14.705  1.00 20.98           C  
ANISOU  965  C   LEU A 126     4096   2694   1181    155    151      6       C  
ATOM    966  O   LEU A 126     -35.501 -25.579 -15.572  1.00 20.08           O  
ANISOU  966  O   LEU A 126     4034   2488   1105    173    147   -210       O  
ATOM    967  CB  LEU A 126     -37.899 -27.542 -14.991  1.00 21.95           C  
ANISOU  967  CB  LEU A 126     4898   2403   1036    432     14      5       C  
ATOM    968  CG  LEU A 126     -38.893 -28.339 -14.142  1.00 26.73           C  
ANISOU  968  CG  LEU A 126     4689   2643   2821    -89     -5      9       C  
ATOM    969  CD1 LEU A 126     -40.292 -27.756 -13.992  1.00 28.52           C  
ANISOU  969  CD1 LEU A 126     4868   2990   2976    263   -250    340       C  
ATOM    970  CD2 LEU A 126     -38.972 -29.770 -14.651  1.00 25.91           C  
ANISOU  970  CD2 LEU A 126     5425   3419   1000   -239   -101   -847       C  
ATOM    971  N   ILE A 127     -36.218 -25.174 -13.445  1.00 20.11           N  
ANISOU  971  N   ILE A 127     3876   2543   1219    236    107    -24       N  
ATOM    972  CA  ILE A 127     -34.906 -24.990 -12.841  1.00 20.04           C  
ANISOU  972  CA  ILE A 127     3913   2714    988    411     58    -50       C  
ATOM    973  C   ILE A 127     -34.676 -26.181 -11.914  1.00 21.59           C  
ANISOU  973  C   ILE A 127     3924   2966   1313    447      6    230       C  
ATOM    974  O   ILE A 127     -35.568 -26.572 -11.160  1.00 24.94           O  
ANISOU  974  O   ILE A 127     4114   3475   1884    488    323    451       O  
ATOM    975  CB  ILE A 127     -34.820 -23.686 -12.019  1.00 20.63           C  
ANISOU  975  CB  ILE A 127     3867   2719   1250    194    -21    -89       C  
ATOM    976  CG1 ILE A 127     -35.014 -22.441 -12.900  1.00 19.28           C  
ANISOU  976  CG1 ILE A 127     3703   2742    879     95     77   -225       C  
ATOM    977  CG2 ILE A 127     -33.520 -23.651 -11.214  1.00 22.05           C  
ANISOU  977  CG2 ILE A 127     3913   2817   1648    153   -133   -269       C  
ATOM    978  CD1 ILE A 127     -33.955 -22.253 -13.964  1.00 19.12           C  
ANISOU  978  CD1 ILE A 127     3797   2767    698    141     81   -176       C  
ATOM    979  N   SER A 128     -33.486 -26.762 -11.965  1.00 21.27           N  
ANISOU  979  N   SER A 128     4020   2650   1411    479    203     68       N  
ATOM    980  CA  SER A 128     -33.184 -27.941 -11.154  1.00 21.64           C  
ANISOU  980  CA  SER A 128     4248   2971   1002    653    -32     56       C  
ATOM    981  C   SER A 128     -32.380 -27.570  -9.910  1.00 20.41           C  
ANISOU  981  C   SER A 128     4052   2661   1041    656     93    -78       C  
ATOM    982  O   SER A 128     -31.624 -26.595  -9.913  1.00 20.78           O  
ANISOU  982  O   SER A 128     3833   2754   1307    651    167     29       O  
ATOM    983  CB  SER A 128     -32.442 -29.004 -11.988  1.00 22.45           C  
ANISOU  983  CB  SER A 128     4188   2783   1558    590     82    -26       C  
ATOM    984  OG  SER A 128     -31.060 -28.705 -12.122  1.00 24.51           O  
ANISOU  984  OG  SER A 128     4143   3158   2009    715    262   -109       O  
ATOM    985  N   ALA A 129     -32.548 -28.360  -8.856  1.00 20.48           N  
ANISOU  985  N   ALA A 129     4042   2853    886    569    -18    -94       N  
ATOM    986  CA  ALA A 129     -31.731 -28.229  -7.648  1.00 19.88           C  
ANISOU  986  CA  ALA A 129     3981   2772    798    646      1     59       C  
ATOM    987  C   ALA A 129     -30.237 -28.505  -7.940  1.00 19.73           C  
ANISOU  987  C   ALA A 129     4037   2692    766    587    138     44       C  
ATOM    988  O   ALA A 129     -29.341 -27.890  -7.354  1.00 20.47           O  
ANISOU  988  O   ALA A 129     3973   2846    959    694    181   -188       O  
ATOM    989  CB  ALA A 129     -32.265 -29.160  -6.566  1.00 19.59           C  
ANISOU  989  CB  ALA A 129     3787   2686    971    495    137    -71       C  
ATOM    990  N   GLN A 130     -29.975 -29.403  -8.890  1.00 21.21           N  
ANISOU  990  N   GLN A 130     4238   2728   1091    636    281    -77       N  
ATOM    991  CA  GLN A 130     -28.625 -29.749  -9.261  1.00 23.00           C  
ANISOU  991  CA  GLN A 130     4364   2903   1470    666    346   -419       C  
ATOM    992  C   GLN A 130     -27.895 -28.564  -9.859  1.00 22.62           C  
ANISOU  992  C   GLN A 130     4143   3108   1342    751    262   -229       C  
ATOM    993  O   GLN A 130     -26.712 -28.389  -9.643  1.00 22.31           O  
ANISOU  993  O   GLN A 130     4069   3035   1372    692    256   -233       O  
ATOM    994  CB  GLN A 130     -28.623 -30.909 -10.258  1.00 25.19           C  
ANISOU  994  CB  GLN A 130     4866   2890   1814    811   -167   -542       C  
ATOM    995  CG  GLN A 130     -27.279 -31.584 -10.378  1.00 28.29           C  
ANISOU  995  CG  GLN A 130     4824   3512   2411    757    271   -392       C  
ATOM    996  CD  GLN A 130     -26.945 -32.311  -9.100  1.00 32.21           C  
ANISOU  996  CD  GLN A 130     5754   3748   2734    931   -431   -434       C  
ATOM    997  OE1 GLN A 130     -26.175 -31.839  -8.281  1.00 33.99           O  
ANISOU  997  OE1 GLN A 130     5465   4113   3334    827   -524   -518       O  
ATOM    998  NE2 GLN A 130     -27.578 -33.457  -8.900  1.00 36.52           N  
ANISOU  998  NE2 GLN A 130     6122   4450   3304    668    -35    427       N  
ATOM    999  N   GLN A 131     -28.597 -27.768 -10.656  1.00 21.75           N  
ANISOU  999  N   GLN A 131     3973   2727   1562    722    440   -271       N  
ATOM   1000  CA  GLN A 131     -27.944 -26.588 -11.171  1.00 22.12           C  
ANISOU 1000  CA  GLN A 131     4284   2853   1264    582    444   -224       C  
ATOM   1001  C   GLN A 131     -27.648 -25.559 -10.104  1.00 19.95           C  
ANISOU 1001  C   GLN A 131     3542   3013   1025    637    276   -113       C  
ATOM   1002  O   GLN A 131     -26.639 -24.903 -10.179  1.00 19.87           O  
ANISOU 1002  O   GLN A 131     3600   2858   1092    663    341     -4       O  
ATOM   1003  CB  GLN A 131     -28.578 -25.988 -12.426  1.00 25.02           C  
ANISOU 1003  CB  GLN A 131     4058   3147   2300    649    -75    162       C  
ATOM   1004  CG  GLN A 131     -30.042 -25.647 -12.422  1.00 24.87           C  
ANISOU 1004  CG  GLN A 131     4072   3387   1991    491   -220    186       C  
ATOM   1005  CD  GLN A 131     -30.572 -25.410 -13.841  1.00 26.75           C  
ANISOU 1005  CD  GLN A 131     4514   4250   1397   -241    134    -65       C  
ATOM   1006  OE1 GLN A 131     -31.632 -25.907 -14.180  1.00 24.74           O  
ANISOU 1006  OE1 GLN A 131     4255   3515   1628    370   -351    245       O  
ATOM   1007  NE2 GLN A 131     -29.842 -24.645 -14.670  1.00 23.70           N  
ANISOU 1007  NE2 GLN A 131     3574   3814   1615    424    177   -155       N  
ATOM   1008  N   VAL A 132     -28.517 -25.452  -9.109  1.00 18.99           N  
ANISOU 1008  N   VAL A 132     3506   2832    875    765    180   -210       N  
ATOM   1009  CA  VAL A 132     -28.269 -24.591  -7.958  1.00 18.48           C  
ANISOU 1009  CA  VAL A 132     3526   2785    708    679    292    -90       C  
ATOM   1010  C   VAL A 132     -26.994 -25.065  -7.268  1.00 19.35           C  
ANISOU 1010  C   VAL A 132     3495   2881    974    662    309   -210       C  
ATOM   1011  O   VAL A 132     -26.097 -24.277  -6.969  1.00 20.21           O  
ANISOU 1011  O   VAL A 132     3442   3102   1132    524    252    -48       O  
ATOM   1012  CB  VAL A 132     -29.462 -24.603  -6.964  1.00 18.38           C  
ANISOU 1012  CB  VAL A 132     3398   2833    751    701    244   -199       C  
ATOM   1013  CG1 VAL A 132     -29.085 -23.910  -5.653  1.00 18.64           C  
ANISOU 1013  CG1 VAL A 132     3454   2942    684    451    303   -110       C  
ATOM   1014  CG2 VAL A 132     -30.688 -23.925  -7.571  1.00 19.62           C  
ANISOU 1014  CG2 VAL A 132     3506   3001    947    595      0   -266       C  
ATOM   1015  N   GLU A 133     -26.920 -26.366  -7.041  1.00 20.02           N  
ANISOU 1015  N   GLU A 133     3621   2912   1071    753    402     -8       N  
ATOM   1016  CA  GLU A 133     -25.797 -26.943  -6.350  1.00 21.13           C  
ANISOU 1016  CA  GLU A 133     3661   3124   1242    707    315     30       C  
ATOM   1017  C   GLU A 133     -24.516 -26.662  -7.108  1.00 21.29           C  
ANISOU 1017  C   GLU A 133     3700   3174   1213    781    327    -11       C  
ATOM   1018  O   GLU A 133     -23.535 -26.299  -6.512  1.00 22.36           O  
ANISOU 1018  O   GLU A 133     3762   3179   1554    744    325    -21       O  
ATOM   1019  CB  GLU A 133     -26.008 -28.437  -6.249  1.00 23.10           C  
ANISOU 1019  CB  GLU A 133     3931   3203   1642    754    294     51       C  
ATOM   1020  CG  GLU A 133     -24.783 -29.206  -5.838  1.00 24.12           C  
ANISOU 1020  CG  GLU A 133     3845   3308   2010    679    260     88       C  
ATOM   1021  CD  GLU A 133     -24.675 -29.266  -4.336  1.00 27.80           C  
ANISOU 1021  CD  GLU A 133     4400   4122   2039    490    300    111       C  
ATOM   1022  OE1 GLU A 133     -25.633 -29.748  -3.692  1.00 32.75           O  
ANISOU 1022  OE1 GLU A 133     4439   4763   3239    634    922     35       O  
ATOM   1023  OE2 GLU A 133     -23.647 -28.825  -3.791  1.00 30.28           O  
ANISOU 1023  OE2 GLU A 133     4581   3998   2925    294    205    -30       O  
ATOM   1024  N   GLU A 134     -24.532 -26.786  -8.422  1.00 20.80           N  
ANISOU 1024  N   GLU A 134     3747   2954   1201    713    502    -18       N  
ATOM   1025  CA  GLU A 134     -23.326 -26.542  -9.186  1.00 22.28           C  
ANISOU 1025  CA  GLU A 134     3815   3193   1458    831    623    -82       C  
ATOM   1026  C   GLU A 134     -22.895 -25.072  -9.254  1.00 22.49           C  
ANISOU 1026  C   GLU A 134     3618   3318   1607    666    558     -9       C  
ATOM   1027  O   GLU A 134     -21.729 -24.782  -9.518  1.00 24.16           O  
ANISOU 1027  O   GLU A 134     3455   3708   2014   1084    646     32       O  
ATOM   1028  CB  GLU A 134     -23.489 -27.152 -10.578  1.00 23.57           C  
ANISOU 1028  CB  GLU A 134     3854   3496   1605    884    311   -189       C  
ATOM   1029  CG  GLU A 134     -23.317 -28.662 -10.561  1.00 27.22           C  
ANISOU 1029  CG  GLU A 134     4585   3560   2197    981    718   -283       C  
ATOM   1030  CD  GLU A 134     -23.712 -29.352 -11.855  1.00 30.77           C  
ANISOU 1030  CD  GLU A 134     5180   4100   2409    780    126   -153       C  
ATOM   1031  OE1 GLU A 134     -23.876 -28.680 -12.896  1.00 35.84           O  
ANISOU 1031  OE1 GLU A 134     6296   5219   2101    920    -41    -83       O  
ATOM   1032  OE2 GLU A 134     -23.854 -30.590 -11.829  1.00 33.92           O  
ANISOU 1032  OE2 GLU A 134     5167   3927   3794   1487    712   -756       O  
ATOM   1033  N   ALA A 135     -23.824 -24.150  -8.994  1.00 20.89           N  
ANISOU 1033  N   ALA A 135     3637   3178   1122    655    705    111       N  
ATOM   1034  CA  ALA A 135     -23.521 -22.717  -9.062  1.00 20.61           C  
ANISOU 1034  CA  ALA A 135     3479   3166   1186    637    496    -22       C  
ATOM   1035  C   ALA A 135     -22.969 -22.152  -7.751  1.00 20.78           C  
ANISOU 1035  C   ALA A 135     3467   3230   1198    438    416    168       C  
ATOM   1036  O   ALA A 135     -22.462 -21.027  -7.709  1.00 21.17           O  
ANISOU 1036  O   ALA A 135     3354   3274   1415    471    413     28       O  
ATOM   1037  CB  ALA A 135     -24.744 -21.919  -9.518  1.00 19.88           C  
ANISOU 1037  CB  ALA A 135     3367   3093   1093    605    355   -190       C  
ATOM   1038  N   ILE A 136     -23.039 -22.944  -6.689  1.00 20.49           N  
ANISOU 1038  N   ILE A 136     3540   3286    957    478    436     40       N  
ATOM   1039  CA  ILE A 136     -22.618 -22.482  -5.373  1.00 20.03           C  
ANISOU 1039  CA  ILE A 136     3279   3285   1043    362    457     53       C  
ATOM   1040  C   ILE A 136     -21.123 -22.167  -5.314  1.00 21.75           C  
ANISOU 1040  C   ILE A 136     3342   3408   1513    335    305    -23       C  
ATOM   1041  O   ILE A 136     -20.281 -22.926  -5.814  1.00 21.81           O  
ANISOU 1041  O   ILE A 136     3360   3427   1497    421    368    147       O  
ATOM   1042  CB  ILE A 136     -23.012 -23.489  -4.270  1.00 20.18           C  
ANISOU 1042  CB  ILE A 136     3359   3353    953    331    507      0       C  
ATOM   1043  CG1 ILE A 136     -24.539 -23.533  -4.109  1.00 20.65           C  
ANISOU 1043  CG1 ILE A 136     3306   3311   1228    439    280    204       C  
ATOM   1044  CG2 ILE A 136     -22.328 -23.157  -2.944  1.00 21.74           C  
ANISOU 1044  CG2 ILE A 136     3358   3606   1295    360    234    -22       C  
ATOM   1045  CD1 ILE A 136     -25.026 -24.705  -3.278  1.00 21.40           C  
ANISOU 1045  CD1 ILE A 136     3491   3369   1270    306    434    145       C  
ATOM   1046  N   ARG A 137     -20.816 -21.041  -4.679  1.00 21.59           N  
ANISOU 1046  N   ARG A 137     3276   3413   1515    483    440   -167       N  
ATOM   1047  CA  ARG A 137     -19.456 -20.563  -4.506  1.00 23.10           C  
ANISOU 1047  CA  ARG A 137     3382   3432   1961    421    277   -319       C  
ATOM   1048  C   ARG A 137     -19.193 -20.339  -3.025  1.00 24.12           C  
ANISOU 1048  C   ARG A 137     3456   3708   2000    440     -5   -119       C  
ATOM   1049  O   ARG A 137     -20.131 -20.310  -2.250  1.00 24.08           O  
ANISOU 1049  O   ARG A 137     3437   3740   1971    322    -51   -125       O  
ATOM   1050  CB  ARG A 137     -19.273 -19.277  -5.306  1.00 24.02           C  
ANISOU 1050  CB  ARG A 137     3358   3585   2183    572    576   -141       C  
ATOM   1051  CG  ARG A 137     -19.020 -19.596  -6.770  1.00 27.95           C  
ANISOU 1051  CG  ARG A 137     4184   4502   1930    210     59   -116       C  
ATOM   1052  CD  ARG A 137     -19.776 -18.728  -7.759  1.00 27.66           C  
ANISOU 1052  CD  ARG A 137     3815   3508   3184    581    335   -185       C  
ATOM   1053  NE  ARG A 137     -19.257 -17.387  -7.902  1.00 30.32           N  
ANISOU 1053  NE  ARG A 137     4060   3882   3577    198    689    303       N  
ATOM   1054  CZ  ARG A 137     -19.311 -16.671  -9.021  1.00 29.39           C  
ANISOU 1054  CZ  ARG A 137     4242   4355   2568    212    740   -213       C  
ATOM   1055  NH1 ARG A 137     -18.840 -15.450  -8.996  1.00 30.03           N  
ANISOU 1055  NH1 ARG A 137     4183   4300   2924    184    503    283       N  
ATOM   1056  NH2 ARG A 137     -19.810 -17.153 -10.157  1.00 31.28           N  
ANISOU 1056  NH2 ARG A 137     3878   4378   3628     35    220   -511       N  
ATOM   1057  N   PRO A 138     -17.918 -20.244  -2.622  1.00 24.91           N  
ANISOU 1057  N   PRO A 138     3410   3550   2504    580    -88   -158       N  
ATOM   1058  CA  PRO A 138     -17.583 -19.967  -1.223  1.00 26.59           C  
ANISOU 1058  CA  PRO A 138     3361   4025   2714    662   -317   -374       C  
ATOM   1059  C   PRO A 138     -18.278 -18.724  -0.635  1.00 24.65           C  
ANISOU 1059  C   PRO A 138     3362   3563   2439    472   -318   -119       C  
ATOM   1060  O   PRO A 138     -18.603 -18.708   0.558  1.00 26.49           O  
ANISOU 1060  O   PRO A 138     3768   3954   2342    352   -532     44       O  
ATOM   1061  CB  PRO A 138     -16.062 -19.795  -1.273  1.00 27.21           C  
ANISOU 1061  CB  PRO A 138     3307   4309   2723    689   -233   -500       C  
ATOM   1062  CG  PRO A 138     -15.652 -20.734  -2.356  1.00 27.22           C  
ANISOU 1062  CG  PRO A 138     3322   4377   2640    558   -305   -505       C  
ATOM   1063  CD  PRO A 138     -16.721 -20.585  -3.408  1.00 25.97           C  
ANISOU 1063  CD  PRO A 138     3316   3906   2644    745   -229   -215       C  
ATOM   1064  N   ASN A 139     -18.521 -17.711  -1.469  1.00 23.45           N  
ANISOU 1064  N   ASN A 139     3078   3606   2223    358   -139    -65       N  
ATOM   1065  CA  ASN A 139     -19.194 -16.483  -1.035  1.00 24.05           C  
ANISOU 1065  CA  ASN A 139     3315   3427   2396    333   -145    -18       C  
ATOM   1066  C   ASN A 139     -20.658 -16.326  -1.478  1.00 22.19           C  
ANISOU 1066  C   ASN A 139     3204   3284   1942    223      5     -7       C  
ATOM   1067  O   ASN A 139     -21.168 -15.214  -1.523  1.00 21.21           O  
ANISOU 1067  O   ASN A 139     3127   3300   1629    308     31   -126       O  
ATOM   1068  CB  ASN A 139     -18.384 -15.245  -1.437  1.00 24.04           C  
ANISOU 1068  CB  ASN A 139     3405   3443   2284    283    -34    -19       C  
ATOM   1069  CG  ASN A 139     -18.281 -15.051  -2.949  1.00 24.46           C  
ANISOU 1069  CG  ASN A 139     3550   3374   2367    196    -42    199       C  
ATOM   1070  OD1 ASN A 139     -17.868 -13.983  -3.405  1.00 29.61           O  
ANISOU 1070  OD1 ASN A 139     4271   3823   3153    -20    241    704       O  
ATOM   1071  ND2 ASN A 139     -18.639 -16.073  -3.732  1.00 24.78           N  
ANISOU 1071  ND2 ASN A 139     3402   3693   2319    361   -279      0       N  
ATOM   1072  N   THR A 140     -21.320 -17.431  -1.811  1.00 21.06           N  
ANISOU 1072  N   THR A 140     3065   3310   1626    230     11     23       N  
ATOM   1073  CA  THR A 140     -22.759 -17.421  -2.072  1.00 19.59           C  
ANISOU 1073  CA  THR A 140     2968   3178   1296    123    250   -166       C  
ATOM   1074  C   THR A 140     -23.522 -17.184  -0.773  1.00 19.15           C  
ANISOU 1074  C   THR A 140     3091   3026   1159    201    183   -109       C  
ATOM   1075  O   THR A 140     -23.344 -17.905   0.206  1.00 19.90           O  
ANISOU 1075  O   THR A 140     3185   3325   1049    266    225    -46       O  
ATOM   1076  CB  THR A 140     -23.207 -18.736  -2.749  1.00 19.93           C  
ANISOU 1076  CB  THR A 140     2957   3093   1522    178    336   -212       C  
ATOM   1077  OG1 THR A 140     -22.442 -18.930  -3.944  1.00 20.95           O  
ANISOU 1077  OG1 THR A 140     3222   3348   1390    257    327    -65       O  
ATOM   1078  CG2 THR A 140     -24.704 -18.709  -3.107  1.00 17.41           C  
ANISOU 1078  CG2 THR A 140     2975   2823    815    141    284   -238       C  
ATOM   1079  N   PHE A 141     -24.356 -16.158  -0.759  1.00 19.62           N  
ANISOU 1079  N   PHE A 141     2877   3354   1220    316    230    -94       N  
ATOM   1080  CA  PHE A 141     -25.045 -15.795   0.468  1.00 19.19           C  
ANISOU 1080  CA  PHE A 141     3041   3005   1243    193    321    -79       C  
ATOM   1081  C   PHE A 141     -26.564 -15.769   0.349  1.00 17.50           C  
ANISOU 1081  C   PHE A 141     2976   2719    953    306     86    -90       C  
ATOM   1082  O   PHE A 141     -27.250 -15.477   1.332  1.00 17.92           O  
ANISOU 1082  O   PHE A 141     2927   2906    976    338    144      6       O  
ATOM   1083  CB  PHE A 141     -24.524 -14.455   0.989  1.00 20.76           C  
ANISOU 1083  CB  PHE A 141     3316   3137   1433    135    -51   -125       C  
ATOM   1084  CG  PHE A 141     -24.993 -13.264   0.192  1.00 21.39           C  
ANISOU 1084  CG  PHE A 141     3510   2896   1718    150    196   -158       C  
ATOM   1085  CD1 PHE A 141     -26.150 -12.575   0.544  1.00 22.09           C  
ANISOU 1085  CD1 PHE A 141     3470   3016   1906    333    -42    -46       C  
ATOM   1086  CD2 PHE A 141     -24.262 -12.818  -0.894  1.00 22.30           C  
ANISOU 1086  CD2 PHE A 141     3497   3281   1694    227    103     25       C  
ATOM   1087  CE1 PHE A 141     -26.566 -11.468  -0.188  1.00 21.57           C  
ANISOU 1087  CE1 PHE A 141     3409   3340   1445    147    215    250       C  
ATOM   1088  CE2 PHE A 141     -24.670 -11.713  -1.628  1.00 21.83           C  
ANISOU 1088  CE2 PHE A 141     3287   3302   1704    179    285     78       C  
ATOM   1089  CZ  PHE A 141     -25.821 -11.034  -1.269  1.00 21.82           C  
ANISOU 1089  CZ  PHE A 141     3362   3287   1641    286    385    152       C  
ATOM   1090  N   LEU A 142     -27.085 -16.044  -0.844  1.00 16.97           N  
ANISOU 1090  N   LEU A 142     2879   2727    842    182    229    -20       N  
ATOM   1091  CA  LEU A 142     -28.520 -16.193  -1.054  1.00 16.23           C  
ANISOU 1091  CA  LEU A 142     2794   2601    771    382    142    -59       C  
ATOM   1092  C   LEU A 142     -28.804 -16.983  -2.320  1.00 16.27           C  
ANISOU 1092  C   LEU A 142     2816   2542    823    288      2    -22       C  
ATOM   1093  O   LEU A 142     -28.153 -16.791  -3.357  1.00 18.45           O  
ANISOU 1093  O   LEU A 142     3084   2882   1045    107    179     58       O  
ATOM   1094  CB  LEU A 142     -29.237 -14.834  -1.127  1.00 16.64           C  
ANISOU 1094  CB  LEU A 142     2912   2506    901    287    105     95       C  
ATOM   1095  CG  LEU A 142     -30.762 -14.774  -1.334  1.00 16.16           C  
ANISOU 1095  CG  LEU A 142     2881   2437    819    318    152    147       C  
ATOM   1096  CD1 LEU A 142     -31.538 -15.429  -0.196  1.00 15.56           C  
ANISOU 1096  CD1 LEU A 142     2670   2391    850    336     90    152       C  
ATOM   1097  CD2 LEU A 142     -31.217 -13.335  -1.516  1.00 16.47           C  
ANISOU 1097  CD2 LEU A 142     2772   2489    997    356     56    215       C  
ATOM   1098  N   ILE A 143     -29.781 -17.878  -2.200  1.00 15.47           N  
ANISOU 1098  N   ILE A 143     2713   2342    822    418     39    -72       N  
ATOM   1099  CA  ILE A 143     -30.451 -18.545  -3.321  1.00 16.19           C  
ANISOU 1099  CA  ILE A 143     2888   2392    872    183    -56     65       C  
ATOM   1100  C   ILE A 143     -31.919 -18.079  -3.324  1.00 16.49           C  
ANISOU 1100  C   ILE A 143     2891   2414    960    246     10     67       C  
ATOM   1101  O   ILE A 143     -32.647 -18.262  -2.328  1.00 16.28           O  
ANISOU 1101  O   ILE A 143     2867   2525    792    197   -101     28       O  
ATOM   1102  CB  ILE A 143     -30.380 -20.097  -3.216  1.00 16.39           C  
ANISOU 1102  CB  ILE A 143     2943   2359    924    306    -15   -166       C  
ATOM   1103  CG1 ILE A 143     -28.925 -20.604  -3.273  1.00 16.53           C  
ANISOU 1103  CG1 ILE A 143     2954   2453    872    310    -87    124       C  
ATOM   1104  CG2 ILE A 143     -31.214 -20.749  -4.324  1.00 16.95           C  
ANISOU 1104  CG2 ILE A 143     3136   2506    798    245   -167     10       C  
ATOM   1105  CD1 ILE A 143     -28.685 -21.876  -2.469  1.00 16.91           C  
ANISOU 1105  CD1 ILE A 143     3005   2311   1107    391    -96     57       C  
ATOM   1106  N   THR A 144     -32.318 -17.405  -4.411  1.00 17.19           N  
ANISOU 1106  N   THR A 144     2995   2549    986    144   -144    101       N  
ATOM   1107  CA  THR A 144     -33.720 -17.009  -4.630  1.00 16.20           C  
ANISOU 1107  CA  THR A 144     2840   2644    671     -7    -84    137       C  
ATOM   1108  C   THR A 144     -34.245 -17.652  -5.889  1.00 15.94           C  
ANISOU 1108  C   THR A 144     2892   2352    810     53     51   -109       C  
ATOM   1109  O   THR A 144     -33.810 -17.313  -6.985  1.00 16.42           O  
ANISOU 1109  O   THR A 144     3031   2283    925     40     27    203       O  
ATOM   1110  CB  THR A 144     -33.958 -15.573  -5.138  1.00 17.81           C  
ANISOU 1110  CB  THR A 144     2926   2427   1413    139    -66   -147       C  
ATOM   1111  OG1 THR A 144     -32.798 -14.729  -5.129  1.00 21.07           O  
ANISOU 1111  OG1 THR A 144     3447   2676   1880   -242   -378   -484       O  
ATOM   1112  CG2 THR A 144     -35.188 -14.973  -4.623  1.00 13.77           C  
ANISOU 1112  CG2 THR A 144     2979   1994    257     -8     99    -14       C  
ATOM   1113  N   ILE A 145     -35.253 -18.495  -5.757  1.00 15.26           N  
ANISOU 1113  N   ILE A 145     2786   2306    704     65   -120     -4       N  
ATOM   1114  CA  ILE A 145     -35.873 -19.102  -6.937  1.00 15.47           C  
ANISOU 1114  CA  ILE A 145     2833   2355    688     95   -125    -45       C  
ATOM   1115  C   ILE A 145     -37.383 -19.074  -6.736  1.00 15.70           C  
ANISOU 1115  C   ILE A 145     2843   2354    766    171   -110    -54       C  
ATOM   1116  O   ILE A 145     -37.870 -19.442  -5.669  1.00 16.71           O  
ANISOU 1116  O   ILE A 145     3065   2484    797     74    -24   -123       O  
ATOM   1117  CB  ILE A 145     -35.411 -20.570  -7.118  1.00 15.83           C  
ANISOU 1117  CB  ILE A 145     2887   2369    757     99     68    -62       C  
ATOM   1118  CG1 ILE A 145     -33.880 -20.678  -7.268  1.00 15.80           C  
ANISOU 1118  CG1 ILE A 145     2888   2468    645     62      8    107       C  
ATOM   1119  CG2 ILE A 145     -36.144 -21.231  -8.277  1.00 17.27           C  
ANISOU 1119  CG2 ILE A 145     3030   2566    964     12    -23   -144       C  
ATOM   1120  CD1 ILE A 145     -33.354 -20.180  -8.598  1.00 16.77           C  
ANISOU 1120  CD1 ILE A 145     3119   2393    858   -112    328      0       C  
ATOM   1121  N   HIS A 146     -38.119 -18.641  -7.757  1.00 15.53           N  
ANISOU 1121  N   HIS A 146     2918   2281    701    143    -79    -52       N  
ATOM   1122  CA  HIS A 146     -39.569 -18.513  -7.701  1.00 14.77           C  
ANISOU 1122  CA  HIS A 146     2865   2230    515    181     14   -109       C  
ATOM   1123  C   HIS A 146     -40.199 -19.879  -7.587  1.00 15.57           C  
ANISOU 1123  C   HIS A 146     2877   2292    744    142      4     15       C  
ATOM   1124  O   HIS A 146     -39.633 -20.869  -8.072  1.00 15.39           O  
ANISOU 1124  O   HIS A 146     2847   2429    570    166    -19   -112       O  
ATOM   1125  CB  HIS A 146     -40.058 -17.805  -8.966  1.00 15.46           C  
ANISOU 1125  CB  HIS A 146     2950   2322    599    298     34    -49       C  
ATOM   1126  CG  HIS A 146     -39.728 -18.550 -10.258  1.00 16.46           C  
ANISOU 1126  CG  HIS A 146     3057   2454    740    267     37   -219       C  
ATOM   1127  ND1 HIS A 146     -40.645 -19.275 -10.937  1.00 17.56           N  
ANISOU 1127  ND1 HIS A 146     3184   2577    909    170    141   -279       N  
ATOM   1128  CD2 HIS A 146     -38.543 -18.655 -10.981  1.00 15.44           C  
ANISOU 1128  CD2 HIS A 146     3027   2259    579    163     51    -91       C  
ATOM   1129  CE1 HIS A 146     -40.077 -19.815 -12.032  1.00 15.46           C  
ANISOU 1129  CE1 HIS A 146     3216   2333    325     51   -176    -79       C  
ATOM   1130  NE2 HIS A 146     -38.791 -19.445 -12.058  1.00 16.30           N  
ANISOU 1130  NE2 HIS A 146     3237   2469    484    162    -18    -98       N  
ATOM   1131  N   HIS A 147     -41.372 -19.948  -6.965  1.00 15.19           N  
ANISOU 1131  N   HIS A 147     2879   2391    500     56    -30    176       N  
ATOM   1132  CA  HIS A 147     -42.077 -21.222  -6.767  1.00 15.41           C  
ANISOU 1132  CA  HIS A 147     2957   2277    620    131     68    170       C  
ATOM   1133  C   HIS A 147     -42.890 -21.571  -7.972  1.00 16.74           C  
ANISOU 1133  C   HIS A 147     3110   2371    877    186    -93    -71       C  
ATOM   1134  O   HIS A 147     -42.724 -22.640  -8.563  1.00 17.21           O  
ANISOU 1134  O   HIS A 147     3404   2479    653    118    -76   -106       O  
ATOM   1135  CB  HIS A 147     -42.949 -21.126  -5.519  1.00 15.64           C  
ANISOU 1135  CB  HIS A 147     3050   2251    642     45    124     65       C  
ATOM   1136  CG  HIS A 147     -43.623 -22.430  -5.110  1.00 16.37           C  
ANISOU 1136  CG  HIS A 147     3162   2310    746     21     70    164       C  
ATOM   1137  ND1 HIS A 147     -44.459 -22.507  -4.041  1.00 17.32           N  
ANISOU 1137  ND1 HIS A 147     3296   2346    936    -47    237     40       N  
ATOM   1138  CD2 HIS A 147     -43.578 -23.712  -5.661  1.00 16.12           C  
ANISOU 1138  CD2 HIS A 147     3137   2273    713    -77     10    180       C  
ATOM   1139  CE1 HIS A 147     -44.910 -23.773  -3.909  1.00 17.17           C  
ANISOU 1139  CE1 HIS A 147     3282   2275    964    -36    123     72       C  
ATOM   1140  NE2 HIS A 147     -44.374 -24.511  -4.895  1.00 16.64           N  
ANISOU 1140  NE2 HIS A 147     3179   2577    563     56    159    310       N  
ATOM   1141  N   VAL A 148     -43.781 -20.668  -8.351  1.00 15.88           N  
ANISOU 1141  N   VAL A 148     3054   2347    630     98   -179     22       N  
ATOM   1142  CA  VAL A 148     -44.539 -20.838  -9.580  1.00 16.45           C  
ANISOU 1142  CA  VAL A 148     3239   2351    658     19   -218   -148       C  
ATOM   1143  C   VAL A 148     -44.272 -19.664 -10.516  1.00 16.48           C  
ANISOU 1143  C   VAL A 148     3217   2392    652     94   -141   -141       C  
ATOM   1144  O   VAL A 148     -44.391 -18.502 -10.118  1.00 15.93           O  
ANISOU 1144  O   VAL A 148     3107   2262    683    165   -147     56       O  
ATOM   1145  CB  VAL A 148     -46.042 -20.992  -9.290  1.00 16.05           C  
ANISOU 1145  CB  VAL A 148     3272   2187    638     83   -121     20       C  
ATOM   1146  CG1 VAL A 148     -46.884 -20.848 -10.557  1.00 17.78           C  
ANISOU 1146  CG1 VAL A 148     3457   2480    816     47   -307    -72       C  
ATOM   1147  CG2 VAL A 148     -46.318 -22.330  -8.609  1.00 16.43           C  
ANISOU 1147  CG2 VAL A 148     3446   2140    656     76    -74    -61       C  
ATOM   1148  N   ASN A 149     -43.923 -19.971 -11.767  1.00 17.20           N  
ANISOU 1148  N   ASN A 149     3174   2642    716    167     49    -17       N  
ATOM   1149  CA  ASN A 149     -43.617 -18.929 -12.743  1.00 16.48           C  
ANISOU 1149  CA  ASN A 149     3223   2588    449    200    -44   -109       C  
ATOM   1150  C   ASN A 149     -44.858 -18.157 -13.191  1.00 16.54           C  
ANISOU 1150  C   ASN A 149     3223   2464    594    130    -41    -64       C  
ATOM   1151  O   ASN A 149     -45.858 -18.765 -13.558  1.00 16.68           O  
ANISOU 1151  O   ASN A 149     3404   2418    514     22   -182    -63       O  
ATOM   1152  CB  ASN A 149     -42.945 -19.534 -13.965  1.00 16.89           C  
ANISOU 1152  CB  ASN A 149     3285   2558    576    134    128    -82       C  
ATOM   1153  CG  ASN A 149     -42.295 -18.478 -14.830  1.00 17.46           C  
ANISOU 1153  CG  ASN A 149     3173   2644    814     84    -13     58       C  
ATOM   1154  OD1 ASN A 149     -41.161 -18.062 -14.571  1.00 19.29           O  
ANISOU 1154  OD1 ASN A 149     3277   2881   1168     15     40   -367       O  
ATOM   1155  ND2 ASN A 149     -43.005 -18.029 -15.850  1.00 15.18           N  
ANISOU 1155  ND2 ASN A 149     3228   2122    417     74     77   -164       N  
ATOM   1156  N   ASN A 150     -44.794 -16.829 -13.177  1.00 16.77           N  
ANISOU 1156  N   ASN A 150     3370   2478    524    115   -125   -165       N  
ATOM   1157  CA  ASN A 150     -45.972 -16.052 -13.525  1.00 18.24           C  
ANISOU 1157  CA  ASN A 150     3435   2709    787    130   -338    -15       C  
ATOM   1158  C   ASN A 150     -46.381 -16.082 -14.986  1.00 17.75           C  
ANISOU 1158  C   ASN A 150     3413   2663    669   -100   -135     -9       C  
ATOM   1159  O   ASN A 150     -47.536 -15.838 -15.268  1.00 17.36           O  
ANISOU 1159  O   ASN A 150     3496   2662    435    -23    -33    202       O  
ATOM   1160  CB  ASN A 150     -45.857 -14.591 -13.076  1.00 18.83           C  
ANISOU 1160  CB  ASN A 150     3517   2835    801   -160   -379    -78       C  
ATOM   1161  CG  ASN A 150     -44.614 -13.931 -13.601  1.00 20.23           C  
ANISOU 1161  CG  ASN A 150     3520   2942   1223    -99   -194     74       C  
ATOM   1162  OD1 ASN A 150     -43.523 -14.450 -13.404  1.00 20.96           O  
ANISOU 1162  OD1 ASN A 150     3593   3090   1279     33     56     76       O  
ATOM   1163  ND2 ASN A 150     -44.764 -12.781 -14.271  1.00 19.92           N  
ANISOU 1163  ND2 ASN A 150     3370   2819   1377   -156   -376    -13       N  
ATOM   1164  N   GLU A 151     -45.455 -16.344 -15.905  1.00 17.91           N  
ANISOU 1164  N   GLU A 151     3462   2660    682     53   -173     28       N  
ATOM   1165  CA  GLU A 151     -45.832 -16.440 -17.321  1.00 17.29           C  
ANISOU 1165  CA  GLU A 151     3501   2414    655   -113   -154     96       C  
ATOM   1166  C   GLU A 151     -46.270 -17.835 -17.752  1.00 17.22           C  
ANISOU 1166  C   GLU A 151     3393   2437    712     17   -117    -34       C  
ATOM   1167  O   GLU A 151     -47.243 -17.982 -18.501  1.00 17.91           O  
ANISOU 1167  O   GLU A 151     3605   2580    616     47   -253    -88       O  
ATOM   1168  CB  GLU A 151     -44.712 -15.921 -18.213  1.00 17.02           C  
ANISOU 1168  CB  GLU A 151     3481   2398    586   -105   -130    -68       C  
ATOM   1169  CG  GLU A 151     -44.416 -14.470 -17.909  1.00 18.38           C  
ANISOU 1169  CG  GLU A 151     3512   2482    989   -385   -386    110       C  
ATOM   1170  CD  GLU A 151     -43.542 -13.816 -18.960  1.00 19.70           C  
ANISOU 1170  CD  GLU A 151     3581   3097    805   -438   -319     85       C  
ATOM   1171  OE1 GLU A 151     -42.830 -12.846 -18.613  1.00 21.53           O  
ANISOU 1171  OE1 GLU A 151     4115   2964   1101   -601   -155    129       O  
ATOM   1172  OE2 GLU A 151     -43.553 -14.277 -20.120  1.00 19.12           O  
ANISOU 1172  OE2 GLU A 151     3821   2595    848   -295   -242    142       O  
ATOM   1173  N   LEU A 152     -45.574 -18.857 -17.263  1.00 17.02           N  
ANISOU 1173  N   LEU A 152     3484   2299    682     49    -30    -46       N  
ATOM   1174  CA  LEU A 152     -45.760 -20.236 -17.753  1.00 17.16           C  
ANISOU 1174  CA  LEU A 152     3488   2344    685    110    -11    -95       C  
ATOM   1175  C   LEU A 152     -46.598 -21.106 -16.842  1.00 18.01           C  
ANISOU 1175  C   LEU A 152     3641   2447    754    -12   -118    -10       C  
ATOM   1176  O   LEU A 152     -47.217 -22.074 -17.288  1.00 20.28           O  
ANISOU 1176  O   LEU A 152     3849   2799   1057   -163   -227   -276       O  
ATOM   1177  CB  LEU A 152     -44.407 -20.919 -17.937  1.00 17.26           C  
ANISOU 1177  CB  LEU A 152     3560   2436    562    108    115   -185       C  
ATOM   1178  CG  LEU A 152     -43.401 -20.314 -18.913  1.00 17.55           C  
ANISOU 1178  CG  LEU A 152     3506   2422    737    110     28     50       C  
ATOM   1179  CD1 LEU A 152     -42.040 -20.972 -18.763  1.00 18.90           C  
ANISOU 1179  CD1 LEU A 152     3494   2766    919    193    200     66       C  
ATOM   1180  CD2 LEU A 152     -43.893 -20.464 -20.346  1.00 18.41           C  
ANISOU 1180  CD2 LEU A 152     3654   2709    629    -40    123    107       C  
ATOM   1181  N   GLY A 153     -46.593 -20.785 -15.556  1.00 18.06           N  
ANISOU 1181  N   GLY A 153     3634   2435    790    104     28   -113       N  
ATOM   1182  CA  GLY A 153     -47.302 -21.605 -14.590  1.00 18.60           C  
ANISOU 1182  CA  GLY A 153     3805   2412    850     61     43    -54       C  
ATOM   1183  C   GLY A 153     -46.446 -22.701 -13.994  1.00 19.05           C  
ANISOU 1183  C   GLY A 153     3719   2715    802    103   -129    -89       C  
ATOM   1184  O   GLY A 153     -46.921 -23.458 -13.134  1.00 20.31           O  
ANISOU 1184  O   GLY A 153     4013   2596   1106     15     33   -102       O  
ATOM   1185  N   THR A 154     -45.181 -22.758 -14.410  1.00 17.82           N  
ANISOU 1185  N   THR A 154     3686   2501    583     11   -198    -43       N  
ATOM   1186  CA  THR A 154     -44.255 -23.829 -14.050  1.00 18.50           C  
ANISOU 1186  CA  THR A 154     3677   2631    719    127   -230   -290       C  
ATOM   1187  C   THR A 154     -44.092 -23.918 -12.549  1.00 18.77           C  
ANISOU 1187  C   THR A 154     3784   2603    741     91   -216    -42       C  
ATOM   1188  O   THR A 154     -43.785 -22.923 -11.895  1.00 17.97           O  
ANISOU 1188  O   THR A 154     3622   2609    594      9   -155      0       O  
ATOM   1189  CB  THR A 154     -42.874 -23.524 -14.651  1.00 19.05           C  
ANISOU 1189  CB  THR A 154     3705   2811    721    259   -134   -152       C  
ATOM   1190  OG1 THR A 154     -43.043 -23.135 -16.015  1.00 19.12           O  
ANISOU 1190  OG1 THR A 154     3698   2854    711    137    -36    -77       O  
ATOM   1191  CG2 THR A 154     -41.939 -24.727 -14.558  1.00 19.45           C  
ANISOU 1191  CG2 THR A 154     3783   2736    871    225    -96   -119       C  
ATOM   1192  N   VAL A 155     -44.316 -25.113 -12.014  1.00 19.30           N  
ANISOU 1192  N   VAL A 155     3918   2700    712    111   -172     18       N  
ATOM   1193  CA  VAL A 155     -44.075 -25.374 -10.602  1.00 18.55           C  
ANISOU 1193  CA  VAL A 155     3689   2575    781    204   -181    164       C  
ATOM   1194  C   VAL A 155     -42.642 -25.839 -10.428  1.00 17.30           C  
ANISOU 1194  C   VAL A 155     3626   2425    522    123    -38     65       C  
ATOM   1195  O   VAL A 155     -42.270 -26.921 -10.885  1.00 19.16           O  
ANISOU 1195  O   VAL A 155     3917   2444    917    154   -119    -85       O  
ATOM   1196  CB  VAL A 155     -45.043 -26.423 -10.027  1.00 18.70           C  
ANISOU 1196  CB  VAL A 155     3758   2562    784    122   -171     48       C  
ATOM   1197  CG1 VAL A 155     -44.826 -26.558  -8.529  1.00 19.49           C  
ANISOU 1197  CG1 VAL A 155     3770   2786    847    221   -272    188       C  
ATOM   1198  CG2 VAL A 155     -46.480 -26.022 -10.302  1.00 18.95           C  
ANISOU 1198  CG2 VAL A 155     3716   2637    846     41   -244     56       C  
ATOM   1199  N   GLN A 156     -41.844 -25.003  -9.774  1.00 16.73           N  
ANISOU 1199  N   GLN A 156     3568   2372    413    147    -74     96       N  
ATOM   1200  CA  GLN A 156     -40.429 -25.279  -9.554  1.00 16.27           C  
ANISOU 1200  CA  GLN A 156     3570   2113    499    327     87    -51       C  
ATOM   1201  C   GLN A 156     -40.195 -26.211  -8.350  1.00 17.28           C  
ANISOU 1201  C   GLN A 156     3581   2344    639    383   -188     51       C  
ATOM   1202  O   GLN A 156     -41.010 -26.250  -7.419  1.00 18.25           O  
ANISOU 1202  O   GLN A 156     3397   2576    959    278    -72    154       O  
ATOM   1203  CB  GLN A 156     -39.643 -23.968  -9.373  1.00 16.59           C  
ANISOU 1203  CB  GLN A 156     3402   2283    616    182     91    151       C  
ATOM   1204  CG  GLN A 156     -39.747 -22.982 -10.536  1.00 17.28           C  
ANISOU 1204  CG  GLN A 156     3629   2391    546    354     10    112       C  
ATOM   1205  CD  GLN A 156     -39.131 -23.501 -11.835  1.00 17.39           C  
ANISOU 1205  CD  GLN A 156     3539   2406    659    255     63     36       C  
ATOM   1206  OE1 GLN A 156     -38.489 -24.564 -11.873  1.00 17.09           O  
ANISOU 1206  OE1 GLN A 156     3554   2440    498    304     67    112       O  
ATOM   1207  NE2 GLN A 156     -39.344 -22.760 -12.916  1.00 17.52           N  
ANISOU 1207  NE2 GLN A 156     3674   2577    405    105     29    -56       N  
ATOM   1208  N   PRO A 157     -39.079 -26.965  -8.363  1.00 17.69           N  
ANISOU 1208  N   PRO A 157     3564   2555    603    399   -157     -8       N  
ATOM   1209  CA  PRO A 157     -38.838 -27.926  -7.291  1.00 17.96           C  
ANISOU 1209  CA  PRO A 157     3657   2330    836    429   -433    -35       C  
ATOM   1210  C   PRO A 157     -38.248 -27.254  -6.041  1.00 17.92           C  
ANISOU 1210  C   PRO A 157     3544   2506    758    273   -226    -78       C  
ATOM   1211  O   PRO A 157     -37.083 -27.457  -5.692  1.00 18.28           O  
ANISOU 1211  O   PRO A 157     3625   2465    855    481   -234   -139       O  
ATOM   1212  CB  PRO A 157     -37.864 -28.928  -7.934  1.00 18.75           C  
ANISOU 1212  CB  PRO A 157     3632   2817    674    498   -288     38       C  
ATOM   1213  CG  PRO A 157     -37.114 -28.131  -8.942  1.00 18.38           C  
ANISOU 1213  CG  PRO A 157     3759   2560    663    674   -122    -67       C  
ATOM   1214  CD  PRO A 157     -38.003 -26.988  -9.374  1.00 18.01           C  
ANISOU 1214  CD  PRO A 157     3524   2439    877    529    -96    -57       C  
ATOM   1215  N   ILE A 158     -39.057 -26.457  -5.368  1.00 17.95           N  
ANISOU 1215  N   ILE A 158     3570   2411    835    366   -275    -25       N  
ATOM   1216  CA  ILE A 158     -38.525 -25.678  -4.261  1.00 17.86           C  
ANISOU 1216  CA  ILE A 158     3684   2381    719    292   -155    -15       C  
ATOM   1217  C   ILE A 158     -38.034 -26.563  -3.117  1.00 18.69           C  
ANISOU 1217  C   ILE A 158     3681   2489    928    292   -195    119       C  
ATOM   1218  O   ILE A 158     -37.097 -26.213  -2.419  1.00 19.01           O  
ANISOU 1218  O   ILE A 158     3593   2719    910    186    -32    100       O  
ATOM   1219  CB  ILE A 158     -39.502 -24.585  -3.768  1.00 18.05           C  
ANISOU 1219  CB  ILE A 158     3404   2478    974    369    -80    280       C  
ATOM   1220  CG1 ILE A 158     -40.857 -25.165  -3.369  1.00 18.89           C  
ANISOU 1220  CG1 ILE A 158     3426   2808    940    355     99    108       C  
ATOM   1221  CG2 ILE A 158     -39.657 -23.480  -4.812  1.00 16.59           C  
ANISOU 1221  CG2 ILE A 158     3291   2435    575    290     87     89       C  
ATOM   1222  CD1 ILE A 158     -41.676 -24.218  -2.500  1.00 20.47           C  
ANISOU 1222  CD1 ILE A 158     3720   2768   1290    380     52   -143       C  
ATOM   1223  N   GLU A 159     -38.671 -27.708  -2.915  1.00 18.61           N  
ANISOU 1223  N   GLU A 159     3627   2587    854    258   -311    231       N  
ATOM   1224  CA  GLU A 159     -38.223 -28.564  -1.833  1.00 19.17           C  
ANISOU 1224  CA  GLU A 159     3789   2542    950    265   -188    363       C  
ATOM   1225  C   GLU A 159     -36.805 -29.078  -2.070  1.00 19.11           C  
ANISOU 1225  C   GLU A 159     3890   2540    828    249   -138    214       C  
ATOM   1226  O   GLU A 159     -35.987 -29.060  -1.179  1.00 19.05           O  
ANISOU 1226  O   GLU A 159     3561   2577   1097    299   -107    -53       O  
ATOM   1227  CB  GLU A 159     -39.165 -29.735  -1.588  1.00 21.75           C  
ANISOU 1227  CB  GLU A 159     3932   2913   1418     20   -366    461       C  
ATOM   1228  CG  GLU A 159     -38.704 -30.572  -0.418  1.00 23.32           C  
ANISOU 1228  CG  GLU A 159     4196   3114   1550     47   -340    654       C  
ATOM   1229  CD  GLU A 159     -39.697 -31.640   0.027  1.00 28.18           C  
ANISOU 1229  CD  GLU A 159     4607   3944   2153   -384   -382   1055       C  
ATOM   1230  OE1 GLU A 159     -39.409 -32.314   1.018  1.00 27.44           O  
ANISOU 1230  OE1 GLU A 159     4435   3630   2358   -462   -208   1198       O  
ATOM   1231  OE2 GLU A 159     -40.775 -31.807  -0.558  1.00 33.54           O  
ANISOU 1231  OE2 GLU A 159     4460   4656   3624   -823   -400   1030       O  
ATOM   1232  N   ASP A 160     -36.531 -29.510  -3.290  1.00 20.28           N  
ANISOU 1232  N   ASP A 160     3846   2854   1004    232    -68     10       N  
ATOM   1233  CA  ASP A 160     -35.200 -29.982  -3.648  1.00 20.53           C  
ANISOU 1233  CA  ASP A 160     3917   2898    983    212    -20   -471       C  
ATOM   1234  C   ASP A 160     -34.157 -28.866  -3.623  1.00 18.08           C  
ANISOU 1234  C   ASP A 160     3713   2510    646    407      5   -196       C  
ATOM   1235  O   ASP A 160     -33.025 -29.067  -3.167  1.00 18.30           O  
ANISOU 1235  O   ASP A 160     3682   2556    712    515     67    -98       O  
ATOM   1236  CB  ASP A 160     -35.219 -30.624  -5.034  1.00 22.68           C  
ANISOU 1236  CB  ASP A 160     4321   3167   1129    229     -6   -669       C  
ATOM   1237  CG  ASP A 160     -35.906 -31.972  -5.046  1.00 28.11           C  
ANISOU 1237  CG  ASP A 160     5089   3390   2199    -80      7   -921       C  
ATOM   1238  OD1 ASP A 160     -36.337 -32.378  -6.136  1.00 32.47           O  
ANISOU 1238  OD1 ASP A 160     4935   4141   3259   -176   -936  -1290       O  
ATOM   1239  OD2 ASP A 160     -36.022 -32.611  -3.977  1.00 31.37           O  
ANISOU 1239  OD2 ASP A 160     5224   3364   3331     25   -284     11       O  
ATOM   1240  N   ILE A 161     -34.547 -27.690  -4.114  1.00 17.22           N  
ANISOU 1240  N   ILE A 161     3703   2409    431    292   -124   -260       N  
ATOM   1241  CA  ILE A 161     -33.679 -26.506  -4.057  1.00 17.67           C  
ANISOU 1241  CA  ILE A 161     3574   2414    723    327   -190    -67       C  
ATOM   1242  C   ILE A 161     -33.420 -26.114  -2.594  1.00 17.05           C  
ANISOU 1242  C   ILE A 161     3431   2380    666    282    -99     -8       C  
ATOM   1243  O   ILE A 161     -32.285 -25.816  -2.219  1.00 17.47           O  
ANISOU 1243  O   ILE A 161     3334   2466    836    213     -7     90       O  
ATOM   1244  CB  ILE A 161     -34.251 -25.306  -4.852  1.00 16.76           C  
ANISOU 1244  CB  ILE A 161     3371   2311    685    314   -221   -159       C  
ATOM   1245  CG1 ILE A 161     -34.374 -25.658  -6.343  1.00 17.19           C  
ANISOU 1245  CG1 ILE A 161     3496   2340    691    621   -178   -213       C  
ATOM   1246  CG2 ILE A 161     -33.361 -24.076  -4.689  1.00 15.84           C  
ANISOU 1246  CG2 ILE A 161     3266   2334    417    314   -277   -240       C  
ATOM   1247  CD1 ILE A 161     -35.430 -24.860  -7.088  1.00 17.39           C  
ANISOU 1247  CD1 ILE A 161     3616   2283    705    459   -441   -221       C  
ATOM   1248  N   GLY A 162     -34.471 -26.139  -1.773  1.00 17.27           N  
ANISOU 1248  N   GLY A 162     3394   2491    676    261   -108     95       N  
ATOM   1249  CA  GLY A 162     -34.332 -25.811  -0.344  1.00 17.17           C  
ANISOU 1249  CA  GLY A 162     3240   2536    746    211   -133    -57       C  
ATOM   1250  C   GLY A 162     -33.409 -26.786   0.366  1.00 16.78           C  
ANISOU 1250  C   GLY A 162     3349   2354    673    229     19    -15       C  
ATOM   1251  O   GLY A 162     -32.682 -26.411   1.298  1.00 16.84           O  
ANISOU 1251  O   GLY A 162     3157   2501    740    407    -78     77       O  
ATOM   1252  N   ASN A 163     -33.420 -28.037  -0.093  1.00 15.93           N  
ANISOU 1252  N   ASN A 163     3351   2349    352    233     54     24       N  
ATOM   1253  CA  ASN A 163     -32.552 -29.082   0.448  1.00 16.99           C  
ANISOU 1253  CA  ASN A 163     3499   2361    595    376     62    -66       C  
ATOM   1254  C   ASN A 163     -31.086 -28.775   0.183  1.00 17.84           C  
ANISOU 1254  C   ASN A 163     3546   2476    755    242     94     42       C  
ATOM   1255  O   ASN A 163     -30.239 -28.873   1.078  1.00 17.83           O  
ANISOU 1255  O   ASN A 163     3568   2393    812    352     53    -92       O  
ATOM   1256  CB  ASN A 163     -32.936 -30.466  -0.111  1.00 18.33           C  
ANISOU 1256  CB  ASN A 163     3799   2381    781    325    -45    -64       C  
ATOM   1257  CG  ASN A 163     -34.207 -31.027   0.524  1.00 21.05           C  
ANISOU 1257  CG  ASN A 163     4031   2913   1054    168    -21    -55       C  
ATOM   1258  OD1 ASN A 163     -34.614 -30.611   1.616  1.00 20.99           O  
ANISOU 1258  OD1 ASN A 163     4370   3054    552    319    106    598       O  
ATOM   1259  ND2 ASN A 163     -34.830 -31.997  -0.158  1.00 22.65           N  
ANISOU 1259  ND2 ASN A 163     4258   2761   1587    234   -402    -53       N  
ATOM   1260  N   VAL A 164     -30.801 -28.372  -1.054  1.00 17.55           N  
ANISOU 1260  N   VAL A 164     3371   2514    782    332     54    116       N  
ATOM   1261  CA  VAL A 164     -29.461 -27.944  -1.431  1.00 17.64           C  
ANISOU 1261  CA  VAL A 164     3499   2444    759    237    134     42       C  
ATOM   1262  C   VAL A 164     -29.017 -26.740  -0.577  1.00 17.01           C  
ANISOU 1262  C   VAL A 164     3367   2306    790    343    112     87       C  
ATOM   1263  O   VAL A 164     -27.911 -26.727  -0.032  1.00 17.20           O  
ANISOU 1263  O   VAL A 164     3293   2347    893    275    191      7       O  
ATOM   1264  CB  VAL A 164     -29.386 -27.582  -2.933  1.00 18.30           C  
ANISOU 1264  CB  VAL A 164     3519   2669    762    274    301     14       C  
ATOM   1265  CG1 VAL A 164     -28.045 -26.944  -3.262  1.00 18.66           C  
ANISOU 1265  CG1 VAL A 164     3485   2775    828    316    297     15       C  
ATOM   1266  CG2 VAL A 164     -29.644 -28.811  -3.803  1.00 18.87           C  
ANISOU 1266  CG2 VAL A 164     3775   2973    421    332    390   -159       C  
ATOM   1267  N   ALA A 165     -29.876 -25.732  -0.457  1.00 15.83           N  
ANISOU 1267  N   ALA A 165     3223   2288    502    253    133    111       N  
ATOM   1268  CA  ALA A 165     -29.536 -24.550   0.342  1.00 15.82           C  
ANISOU 1268  CA  ALA A 165     3099   2215    695    392     48     32       C  
ATOM   1269  C   ALA A 165     -29.299 -24.918   1.815  1.00 16.73           C  
ANISOU 1269  C   ALA A 165     3232   2399    723    335     48    114       C  
ATOM   1270  O   ALA A 165     -28.389 -24.383   2.459  1.00 16.78           O  
ANISOU 1270  O   ALA A 165     3213   2425    737    289    122    156       O  
ATOM   1271  CB  ALA A 165     -30.628 -23.503   0.222  1.00 15.82           C  
ANISOU 1271  CB  ALA A 165     3117   2105    787    331     44     52       C  
ATOM   1272  N   PHE A 166     -30.109 -25.830   2.339  1.00 15.65           N  
ANISOU 1272  N   PHE A 166     3001   2308    634    377     49     39       N  
ATOM   1273  CA  PHE A 166     -29.945 -26.317   3.709  1.00 17.01           C  
ANISOU 1273  CA  PHE A 166     3234   2462    766    384    109    258       C  
ATOM   1274  C   PHE A 166     -28.604 -27.025   3.896  1.00 17.26           C  
ANISOU 1274  C   PHE A 166     3245   2566    744    398     87    157       C  
ATOM   1275  O   PHE A 166     -27.946 -26.849   4.916  1.00 18.17           O  
ANISOU 1275  O   PHE A 166     3238   2742    922    372      0     67       O  
ATOM   1276  CB  PHE A 166     -31.096 -27.266   4.051  1.00 16.87           C  
ANISOU 1276  CB  PHE A 166     3340   2344    725    339    142    138       C  
ATOM   1277  CG  PHE A 166     -31.004 -27.891   5.411  1.00 17.47           C  
ANISOU 1277  CG  PHE A 166     3316   2498    824    384    164    269       C  
ATOM   1278  CD1 PHE A 166     -31.581 -27.259   6.501  1.00 17.70           C  
ANISOU 1278  CD1 PHE A 166     3533   2536    656    190    129    206       C  
ATOM   1279  CD2 PHE A 166     -30.399 -29.135   5.598  1.00 18.21           C  
ANISOU 1279  CD2 PHE A 166     3522   2510    886    318     23    366       C  
ATOM   1280  CE1 PHE A 166     -31.542 -27.846   7.750  1.00 18.16           C  
ANISOU 1280  CE1 PHE A 166     3538   2598    763    380   -157    305       C  
ATOM   1281  CE2 PHE A 166     -30.344 -29.723   6.853  1.00 17.56           C  
ANISOU 1281  CE2 PHE A 166     3338   2526    807    326    -69    271       C  
ATOM   1282  CZ  PHE A 166     -30.922 -29.077   7.927  1.00 17.29           C  
ANISOU 1282  CZ  PHE A 166     3513   2384    672    177    -50    298       C  
ATOM   1283  N   GLU A 167     -28.200 -27.807   2.896  1.00 16.77           N  
ANISOU 1283  N   GLU A 167     3147   2328    896    314    120    134       N  
ATOM   1284  CA  GLU A 167     -26.973 -28.596   2.972  1.00 18.49           C  
ANISOU 1284  CA  GLU A 167     3267   2511   1247    373      0    120       C  
ATOM   1285  C   GLU A 167     -25.718 -27.721   2.966  1.00 18.87           C  
ANISOU 1285  C   GLU A 167     3166   2651   1351    359     15    269       C  
ATOM   1286  O   GLU A 167     -24.691 -28.098   3.514  1.00 20.07           O  
ANISOU 1286  O   GLU A 167     3306   2998   1319    303   -279    173       O  
ATOM   1287  CB  GLU A 167     -26.956 -29.670   1.874  1.00 20.58           C  
ANISOU 1287  CB  GLU A 167     3777   2431   1611    326    121    -30       C  
ATOM   1288  CG  GLU A 167     -27.966 -30.787   2.133  1.00 21.53           C  
ANISOU 1288  CG  GLU A 167     3945   2667   1566    123    -38    -22       C  
ATOM   1289  CD  GLU A 167     -28.365 -31.577   0.894  1.00 22.44           C  
ANISOU 1289  CD  GLU A 167     4321   2697   1506     62      8    -43       C  
ATOM   1290  OE1 GLU A 167     -27.716 -31.446  -0.163  1.00 26.63           O  
ANISOU 1290  OE1 GLU A 167     4438   3470   2210     51    550     13       O  
ATOM   1291  OE2 GLU A 167     -29.344 -32.340   0.993  1.00 21.86           O  
ANISOU 1291  OE2 GLU A 167     4308   2593   1402     86   -153   -197       O  
ATOM   1292  N   HIS A 168     -25.847 -26.527   2.403  1.00 18.20           N  
ANISOU 1292  N   HIS A 168     3332   2493   1090    338    161    119       N  
ATOM   1293  CA  HIS A 168     -24.798 -25.535   2.447  1.00 18.30           C  
ANISOU 1293  CA  HIS A 168     3217   2643   1090    327    175    120       C  
ATOM   1294  C   HIS A 168     -24.971 -24.386   3.434  1.00 18.75           C  
ANISOU 1294  C   HIS A 168     3290   2771   1063    392    -95     13       C  
ATOM   1295  O   HIS A 168     -24.112 -23.506   3.489  1.00 19.49           O  
ANISOU 1295  O   HIS A 168     3203   3063   1139    310    115    224       O  
ATOM   1296  CB  HIS A 168     -24.597 -24.958   1.051  1.00 18.96           C  
ANISOU 1296  CB  HIS A 168     3307   2828   1068    370     54    185       C  
ATOM   1297  CG  HIS A 168     -24.108 -25.948   0.049  1.00 21.57           C  
ANISOU 1297  CG  HIS A 168     3626   3090   1477    355    222    -65       C  
ATOM   1298  ND1 HIS A 168     -22.831 -25.985  -0.358  1.00 24.34           N  
ANISOU 1298  ND1 HIS A 168     3706   3512   2027    429    206   -113       N  
ATOM   1299  CD2 HIS A 168     -24.773 -26.952  -0.641  1.00 20.97           C  
ANISOU 1299  CD2 HIS A 168     3458   3054   1453    319    332      0       C  
ATOM   1300  CE1 HIS A 168     -22.685 -26.950  -1.275  1.00 25.14           C  
ANISOU 1300  CE1 HIS A 168     3666   3789   2095    665    463   -217       C  
ATOM   1301  NE2 HIS A 168     -23.871 -27.547  -1.440  1.00 24.81           N  
ANISOU 1301  NE2 HIS A 168     3736   3845   1845    542    564   -144       N  
ATOM   1302  N   ASP A 169     -26.046 -24.349   4.225  1.00 18.32           N  
ANISOU 1302  N   ASP A 169     3230   2705   1025    344   -133    144       N  
ATOM   1303  CA  ASP A 169     -26.270 -23.208   5.151  1.00 18.61           C  
ANISOU 1303  CA  ASP A 169     3432   2701    937    399   -223    124       C  
ATOM   1304  C   ASP A 169     -26.234 -21.843   4.452  1.00 17.72           C  
ANISOU 1304  C   ASP A 169     3221   2781    730    321     72    210       C  
ATOM   1305  O   ASP A 169     -25.654 -20.844   4.889  1.00 19.42           O  
ANISOU 1305  O   ASP A 169     3330   2972   1073    256    -93     55       O  
ATOM   1306  CB  ASP A 169     -25.330 -23.235   6.338  1.00 17.82           C  
ANISOU 1306  CB  ASP A 169     3215   2833    721    512      8    467       C  
ATOM   1307  CG  ASP A 169     -25.846 -22.387   7.491  1.00 20.49           C  
ANISOU 1307  CG  ASP A 169     3656   3167    961    261   -242    -90       C  
ATOM   1308  OD1 ASP A 169     -27.069 -22.126   7.535  1.00 20.37           O  
ANISOU 1308  OD1 ASP A 169     3774   2869   1095    325    233    296       O  
ATOM   1309  OD2 ASP A 169     -25.038 -21.953   8.325  1.00 21.78           O  
ANISOU 1309  OD2 ASP A 169     3847   3624    805    390   -376   -117       O  
ATOM   1310  N   ILE A 170     -26.862 -21.866   3.290  1.00 16.46           N  
ANISOU 1310  N   ILE A 170     2939   2533    780    395    115    120       N  
ATOM   1311  CA  ILE A 170     -27.180 -20.673   2.484  1.00 16.07           C  
ANISOU 1311  CA  ILE A 170     2820   2534    751    487    109     34       C  
ATOM   1312  C   ILE A 170     -28.675 -20.324   2.573  1.00 15.89           C  
ANISOU 1312  C   ILE A 170     2797   2399    839    382    146     17       C  
ATOM   1313  O   ILE A 170     -29.538 -21.184   2.311  1.00 15.90           O  
ANISOU 1313  O   ILE A 170     2847   2478    714    381      0     13       O  
ATOM   1314  CB  ILE A 170     -26.808 -20.884   0.991  1.00 16.81           C  
ANISOU 1314  CB  ILE A 170     2869   2717    799    378    304    160       C  
ATOM   1315  CG1 ILE A 170     -25.296 -21.083   0.831  1.00 16.86           C  
ANISOU 1315  CG1 ILE A 170     2851   2693    862    488    288      0       C  
ATOM   1316  CG2 ILE A 170     -27.283 -19.712   0.124  1.00 16.86           C  
ANISOU 1316  CG2 ILE A 170     2823   2653    928    381    221    134       C  
ATOM   1317  CD1 ILE A 170     -24.899 -21.728  -0.481  1.00 17.39           C  
ANISOU 1317  CD1 ILE A 170     2908   2930    767    346    417     43       C  
ATOM   1318  N   PRO A 171     -28.991 -19.053   2.910  1.00 15.83           N  
ANISOU 1318  N   PRO A 171     2692   2392    929    376     24    -11       N  
ATOM   1319  CA  PRO A 171     -30.390 -18.624   2.944  1.00 15.30           C  
ANISOU 1319  CA  PRO A 171     2663   2293    856    338   -107     86       C  
ATOM   1320  C   PRO A 171     -31.139 -18.903   1.623  1.00 14.89           C  
ANISOU 1320  C   PRO A 171     2589   2311    756    319     39      7       C  
ATOM   1321  O   PRO A 171     -30.591 -18.689   0.512  1.00 15.50           O  
ANISOU 1321  O   PRO A 171     2853   2258    778    395     64    226       O  
ATOM   1322  CB  PRO A 171     -30.285 -17.122   3.253  1.00 15.61           C  
ANISOU 1322  CB  PRO A 171     2643   2319    969    400    -89    -30       C  
ATOM   1323  CG  PRO A 171     -29.032 -17.021   4.054  1.00 15.86           C  
ANISOU 1323  CG  PRO A 171     2520   2351   1153    351    -63   -178       C  
ATOM   1324  CD  PRO A 171     -28.088 -17.982   3.372  1.00 15.91           C  
ANISOU 1324  CD  PRO A 171     2735   2258   1049    346    213     18       C  
ATOM   1325  N   PHE A 172     -32.355 -19.426   1.771  1.00 14.21           N  
ANISOU 1325  N   PHE A 172     2636   2136    626    254    -63     87       N  
ATOM   1326  CA  PHE A 172     -33.220 -19.747   0.646  1.00 13.98           C  
ANISOU 1326  CA  PHE A 172     2641   2155    516    262     -6    131       C  
ATOM   1327  C   PHE A 172     -34.490 -18.919   0.689  1.00 14.51           C  
ANISOU 1327  C   PHE A 172     2694   2139    677    311     59     78       C  
ATOM   1328  O   PHE A 172     -35.302 -19.042   1.609  1.00 14.59           O  
ANISOU 1328  O   PHE A 172     2640   2213    687    247     24    164       O  
ATOM   1329  CB  PHE A 172     -33.581 -21.231   0.661  1.00 14.68           C  
ANISOU 1329  CB  PHE A 172     2835   2103    636    403     88    -12       C  
ATOM   1330  CG  PHE A 172     -34.566 -21.635  -0.412  1.00 15.18           C  
ANISOU 1330  CG  PHE A 172     2814   2206    746    311    115    -50       C  
ATOM   1331  CD1 PHE A 172     -34.458 -21.120  -1.710  1.00 15.64           C  
ANISOU 1331  CD1 PHE A 172     2931   2302    707    306    -65    -19       C  
ATOM   1332  CD2 PHE A 172     -35.581 -22.559  -0.146  1.00 15.83           C  
ANISOU 1332  CD2 PHE A 172     2933   2298    782    270    153    -52       C  
ATOM   1333  CE1 PHE A 172     -35.345 -21.497  -2.710  1.00 16.42           C  
ANISOU 1333  CE1 PHE A 172     2759   2267   1211    217   -112   -213       C  
ATOM   1334  CE2 PHE A 172     -36.472 -22.940  -1.145  1.00 17.20           C  
ANISOU 1334  CE2 PHE A 172     3087   2539    910    258    -32     16       C  
ATOM   1335  CZ  PHE A 172     -36.353 -22.399  -2.422  1.00 17.93           C  
ANISOU 1335  CZ  PHE A 172     3174   2562   1076    126    189    130       C  
ATOM   1336  N   HIS A 173     -34.653 -18.087  -0.328  1.00 14.87           N  
ANISOU 1336  N   HIS A 173     2774   2173    701    326     29    108       N  
ATOM   1337  CA  HIS A 173     -35.861 -17.313  -0.515  1.00 14.14           C  
ANISOU 1337  CA  HIS A 173     2534   2100    736    181    -42    -77       C  
ATOM   1338  C   HIS A 173     -36.630 -17.806  -1.719  1.00 14.68           C  
ANISOU 1338  C   HIS A 173     2678   2228    669    173    -82    -18       C  
ATOM   1339  O   HIS A 173     -36.038 -18.212  -2.731  1.00 15.25           O  
ANISOU 1339  O   HIS A 173     2881   2127    785    160    -27   -129       O  
ATOM   1340  CB  HIS A 173     -35.488 -15.852  -0.685  1.00 14.29           C  
ANISOU 1340  CB  HIS A 173     2562   2092    773    193     21    -24       C  
ATOM   1341  CG  HIS A 173     -36.612 -15.002  -1.200  1.00 15.04           C  
ANISOU 1341  CG  HIS A 173     2719   2246    749    212    -34    135       C  
ATOM   1342  ND1 HIS A 173     -36.733 -14.674  -2.508  1.00 14.92           N  
ANISOU 1342  ND1 HIS A 173     2714   2224    727    235     26    120       N  
ATOM   1343  CD2 HIS A 173     -37.699 -14.436  -0.549  1.00 15.01           C  
ANISOU 1343  CD2 HIS A 173     2772   2132    798    170    -26     -4       C  
ATOM   1344  CE1 HIS A 173     -37.839 -13.925  -2.679  1.00 14.62           C  
ANISOU 1344  CE1 HIS A 173     2630   2233    692    160     59     85       C  
ATOM   1345  NE2 HIS A 173     -38.435 -13.783  -1.483  1.00 14.78           N  
ANISOU 1345  NE2 HIS A 173     2776   2218    620    150     11    -49       N  
ATOM   1346  N   THR A 174     -37.954 -17.769  -1.635  1.00 14.39           N  
ANISOU 1346  N   THR A 174     2657   2127    683    106   -106   -114       N  
ATOM   1347  CA  THR A 174     -38.778 -18.080  -2.802  1.00 14.33           C  
ANISOU 1347  CA  THR A 174     2650   2174    619    127   -103    -24       C  
ATOM   1348  C   THR A 174     -39.859 -17.024  -3.057  1.00 14.62           C  
ANISOU 1348  C   THR A 174     2698   2171    683    160    119     24       C  
ATOM   1349  O   THR A 174     -40.597 -16.638  -2.142  1.00 14.15           O  
ANISOU 1349  O   THR A 174     2747   2064    563    121    105      0       O  
ATOM   1350  CB  THR A 174     -39.346 -19.528  -2.759  1.00 14.84           C  
ANISOU 1350  CB  THR A 174     2766   2310    561    -60     15   -181       C  
ATOM   1351  OG1 THR A 174     -40.068 -19.791  -3.970  1.00 15.02           O  
ANISOU 1351  OG1 THR A 174     2785   2358    565    144   -116     69       O  
ATOM   1352  CG2 THR A 174     -40.271 -19.760  -1.574  1.00 15.88           C  
ANISOU 1352  CG2 THR A 174     2860   2272    902     20    233     64       C  
ATOM   1353  N   ASP A 175     -39.913 -16.544  -4.301  1.00 14.34           N  
ANISOU 1353  N   ASP A 175     2666   2156    626    133     88    -40       N  
ATOM   1354  CA  ASP A 175     -41.008 -15.712  -4.748  1.00 14.20           C  
ANISOU 1354  CA  ASP A 175     2680   2122    593     85    117     39       C  
ATOM   1355  C   ASP A 175     -42.237 -16.592  -4.982  1.00 14.74           C  
ANISOU 1355  C   ASP A 175     2555   2342    702    104     90     50       C  
ATOM   1356  O   ASP A 175     -42.330 -17.297  -5.998  1.00 15.39           O  
ANISOU 1356  O   ASP A 175     2841   2378    630    126    200     97       O  
ATOM   1357  CB  ASP A 175     -40.603 -14.962  -6.018  1.00 14.93           C  
ANISOU 1357  CB  ASP A 175     2746   2322    602    202    150    132       C  
ATOM   1358  CG  ASP A 175     -41.664 -13.989  -6.483  1.00 14.03           C  
ANISOU 1358  CG  ASP A 175     2633   2121    577    121    197    -18       C  
ATOM   1359  OD1 ASP A 175     -41.353 -13.136  -7.340  1.00 15.38           O  
ANISOU 1359  OD1 ASP A 175     2850   2493    500     85     82    170       O  
ATOM   1360  OD2 ASP A 175     -42.808 -14.063  -5.998  1.00 14.33           O  
ANISOU 1360  OD2 ASP A 175     2702   2250    491     63    273     47       O  
ATOM   1361  N   ALA A 176     -43.171 -16.547  -4.027  1.00 14.52           N  
ANISOU 1361  N   ALA A 176     2628   2332    554     80     53     55       N  
ATOM   1362  CA  ALA A 176     -44.370 -17.388  -4.049  1.00 14.76           C  
ANISOU 1362  CA  ALA A 176     2791   2190    625     20    144    188       C  
ATOM   1363  C   ALA A 176     -45.618 -16.590  -4.432  1.00 14.02           C  
ANISOU 1363  C   ALA A 176     2785   2026    515     -9     94    -15       C  
ATOM   1364  O   ALA A 176     -46.733 -16.956  -4.080  1.00 13.58           O  
ANISOU 1364  O   ALA A 176     2790   2007    361   -111     20   -149       O  
ATOM   1365  CB  ALA A 176     -44.569 -18.073  -2.690  1.00 14.71           C  
ANISOU 1365  CB  ALA A 176     2866   2109    612    -20     83    153       C  
ATOM   1366  N   ALA A 177     -45.444 -15.498  -5.168  1.00 14.32           N  
ANISOU 1366  N   ALA A 177     2782   2135    522     76     67    103       N  
ATOM   1367  CA  ALA A 177     -46.598 -14.678  -5.509  1.00 14.12           C  
ANISOU 1367  CA  ALA A 177     2590   2017    758    -56     77     59       C  
ATOM   1368  C   ALA A 177     -47.660 -15.464  -6.263  1.00 14.71           C  
ANISOU 1368  C   ALA A 177     2870   2042    676    -50    -25    -97       C  
ATOM   1369  O   ALA A 177     -48.848 -15.223  -6.082  1.00 15.05           O  
ANISOU 1369  O   ALA A 177     2851   2163    702    -99   -143   -166       O  
ATOM   1370  CB  ALA A 177     -46.186 -13.451  -6.298  1.00 14.24           C  
ANISOU 1370  CB  ALA A 177     2561   1985    862     94    -40    174       C  
ATOM   1371  N   GLN A 178     -47.231 -16.411  -7.089  1.00 14.77           N  
ANISOU 1371  N   GLN A 178     3061   1948    600   -159     41    -21       N  
ATOM   1372  CA  GLN A 178     -48.181 -17.207  -7.869  1.00 15.45           C  
ANISOU 1372  CA  GLN A 178     3077   2157    634   -187     88   -156       C  
ATOM   1373  C   GLN A 178     -48.583 -18.532  -7.227  1.00 15.75           C  
ANISOU 1373  C   GLN A 178     3124   2144    715    -77     35   -119       C  
ATOM   1374  O   GLN A 178     -49.484 -19.221  -7.720  1.00 17.63           O  
ANISOU 1374  O   GLN A 178     3283   2338   1078   -340      9    -41       O  
ATOM   1375  CB  GLN A 178     -47.624 -17.512  -9.261  1.00 15.64           C  
ANISOU 1375  CB  GLN A 178     3175   2082    683   -125     41   -330       C  
ATOM   1376  CG  GLN A 178     -47.397 -16.308 -10.144  1.00 16.74           C  
ANISOU 1376  CG  GLN A 178     3192   2407    758    -47    -55    -46       C  
ATOM   1377  CD  GLN A 178     -48.677 -15.741 -10.746  1.00 17.24           C  
ANISOU 1377  CD  GLN A 178     3212   2454    881   -110   -190   -249       C  
ATOM   1378  OE1 GLN A 178     -49.594 -16.473 -11.128  1.00 19.18           O  
ANISOU 1378  OE1 GLN A 178     3249   2587   1451   -326   -127    -30       O  
ATOM   1379  NE2 GLN A 178     -48.726 -14.431 -10.865  1.00 16.64           N  
ANISOU 1379  NE2 GLN A 178     3027   2391    901   -104    -98   -251       N  
ATOM   1380  N   SER A 179     -47.915 -18.903  -6.143  1.00 15.40           N  
ANISOU 1380  N   SER A 179     3061   2105    684    -27    116    -64       N  
ATOM   1381  CA  SER A 179     -48.179 -20.204  -5.525  1.00 15.62           C  
ANISOU 1381  CA  SER A 179     3018   2132    784    -78    150    -55       C  
ATOM   1382  C   SER A 179     -48.918 -20.107  -4.204  1.00 15.77           C  
ANISOU 1382  C   SER A 179     3032   2253    705   -109     85   -115       C  
ATOM   1383  O   SER A 179     -49.640 -21.031  -3.826  1.00 17.03           O  
ANISOU 1383  O   SER A 179     3203   2348    918   -154     69     19       O  
ATOM   1384  CB  SER A 179     -46.879 -20.946  -5.293  1.00 15.79           C  
ANISOU 1384  CB  SER A 179     3042   2262    694    -68     -1    -81       C  
ATOM   1385  OG  SER A 179     -46.049 -20.214  -4.411  1.00 14.77           O  
ANISOU 1385  OG  SER A 179     3010   2111    488      6    102   -141       O  
ATOM   1386  N   PHE A 180     -48.717 -18.998  -3.496  1.00 15.34           N  
ANISOU 1386  N   PHE A 180     2959   2181    687     -4    146   -100       N  
ATOM   1387  CA  PHE A 180     -49.369 -18.776  -2.206  1.00 15.38           C  
ANISOU 1387  CA  PHE A 180     2881   2190    770   -116    217   -159       C  
ATOM   1388  C   PHE A 180     -50.881 -19.023  -2.334  1.00 15.92           C  
ANISOU 1388  C   PHE A 180     2997   2279    771   -290    145      0       C  
ATOM   1389  O   PHE A 180     -51.528 -18.498  -3.248  1.00 16.93           O  
ANISOU 1389  O   PHE A 180     3175   2502    755   -314     31     -3       O  
ATOM   1390  CB  PHE A 180     -49.069 -17.351  -1.699  1.00 15.08           C  
ANISOU 1390  CB  PHE A 180     2934   2158    637    -36    134   -118       C  
ATOM   1391  CG  PHE A 180     -49.681 -17.032  -0.357  1.00 15.60           C  
ANISOU 1391  CG  PHE A 180     2869   2325    730     26    162   -205       C  
ATOM   1392  CD1 PHE A 180     -50.580 -15.977  -0.225  1.00 14.94           C  
ANISOU 1392  CD1 PHE A 180     2856   2123    697    -71    127   -248       C  
ATOM   1393  CD2 PHE A 180     -49.362 -17.784   0.774  1.00 15.50           C  
ANISOU 1393  CD2 PHE A 180     3032   2217    639   -175     38   -261       C  
ATOM   1394  CE1 PHE A 180     -51.145 -15.667   1.006  1.00 15.62           C  
ANISOU 1394  CE1 PHE A 180     2875   2245    812    -78    313   -151       C  
ATOM   1395  CE2 PHE A 180     -49.928 -17.480   2.007  1.00 16.02           C  
ANISOU 1395  CE2 PHE A 180     2788   2313    984    -14    480     59       C  
ATOM   1396  CZ  PHE A 180     -50.816 -16.418   2.127  1.00 16.40           C  
ANISOU 1396  CZ  PHE A 180     2959   2334    936     38    364    -49       C  
ATOM   1397  N   CYS A 181     -51.413 -19.845  -1.420  1.00 15.28           N  
ANISOU 1397  N   CYS A 181     2982   2280    543   -226    146    -87       N  
ATOM   1398  CA  CYS A 181     -52.839 -20.272  -1.365  1.00 16.12           C  
ANISOU 1398  CA  CYS A 181     3132   2313    680   -413    143    -28       C  
ATOM   1399  C   CYS A 181     -53.246 -21.334  -2.393  1.00 16.59           C  
ANISOU 1399  C   CYS A 181     3236   2330    737   -369    115    -58       C  
ATOM   1400  O   CYS A 181     -54.064 -22.166  -2.091  1.00 18.49           O  
ANISOU 1400  O   CYS A 181     3500   2562    963   -530     73    111       O  
ATOM   1401  CB  CYS A 181     -53.818 -19.084  -1.411  1.00 16.92           C  
ANISOU 1401  CB  CYS A 181     3134   2418    874   -363    -21    -57       C  
ATOM   1402  SG  CYS A 181     -53.811 -18.053   0.073  1.00 18.61           S  
ANISOU 1402  SG  CYS A 181     3363   2853    854   -233    217   -186       S  
ATOM   1403  N   LYS A 182     -52.693 -21.267  -3.603  1.00 16.60           N  
ANISOU 1403  N   LYS A 182     3269   2344    692   -345     51     40       N  
ATOM   1404  CA  LYS A 182     -52.916 -22.296  -4.626  1.00 17.09           C  
ANISOU 1404  CA  LYS A 182     3505   2199    787   -390    315     57       C  
ATOM   1405  C   LYS A 182     -52.321 -23.652  -4.267  1.00 18.72           C  
ANISOU 1405  C   LYS A 182     3346   2490   1274   -181     62    116       C  
ATOM   1406  O   LYS A 182     -52.945 -24.715  -4.497  1.00 21.26           O  
ANISOU 1406  O   LYS A 182     3566   2762   1748   -391    -75    -34       O  
ATOM   1407  CB  LYS A 182     -52.278 -21.894  -5.937  1.00 18.06           C  
ANISOU 1407  CB  LYS A 182     3514   2597    748   -262    350     56       C  
ATOM   1408  CG  LYS A 182     -52.966 -20.800  -6.705  1.00 19.37           C  
ANISOU 1408  CG  LYS A 182     3738   2720    901   -100    467    177       C  
ATOM   1409  CD  LYS A 182     -52.464 -20.987  -8.127  1.00 20.18           C  
ANISOU 1409  CD  LYS A 182     4004   2830    830   -152    375     89       C  
ATOM   1410  CE  LYS A 182     -52.660 -19.819  -9.076  1.00 20.33           C  
ANISOU 1410  CE  LYS A 182     3975   2779    968   -457     70    119       C  
ATOM   1411  NZ  LYS A 182     -52.023 -18.543  -8.643  1.00 21.48           N  
ANISOU 1411  NZ  LYS A 182     3821   3007   1333   -523   -185    -29       N  
ATOM   1412  N   LEU A 183     -51.090 -23.613  -3.745  1.00 17.59           N  
ANISOU 1412  N   LEU A 183     3196   2403   1083   -194    234     70       N  
ATOM   1413  CA  LEU A 183     -50.336 -24.808  -3.422  1.00 18.55           C  
ANISOU 1413  CA  LEU A 183     3290   2497   1259   -105     89     38       C  
ATOM   1414  C   LEU A 183     -50.043 -24.797  -1.950  1.00 20.13           C  
ANISOU 1414  C   LEU A 183     3763   2570   1315    -60     -1    131       C  
ATOM   1415  O   LEU A 183     -49.785 -23.772  -1.376  1.00 20.70           O  
ANISOU 1415  O   LEU A 183     3802   2610   1452    -71    -88    113       O  
ATOM   1416  CB  LEU A 183     -49.010 -24.814  -4.168  1.00 18.27           C  
ANISOU 1416  CB  LEU A 183     3212   2673   1056    -40     13     32       C  
ATOM   1417  CG  LEU A 183     -49.104 -24.916  -5.692  1.00 19.75           C  
ANISOU 1417  CG  LEU A 183     3430   3011   1062   -112    250    -83       C  
ATOM   1418  CD1 LEU A 183     -47.687 -24.976  -6.267  1.00 19.57           C  
ANISOU 1418  CD1 LEU A 183     3369   2829   1237    151    264     89       C  
ATOM   1419  CD2 LEU A 183     -49.942 -26.122  -6.106  1.00 21.85           C  
ANISOU 1419  CD2 LEU A 183     3312   3254   1733   -132     75   -280       C  
ATOM   1420  N   ASP A 184     -50.122 -25.947  -1.320  1.00 21.25           N  
ANISOU 1420  N   ASP A 184     3981   2718   1374   -115     -3    217       N  
ATOM   1421  CA AASP A 184     -49.849 -26.002   0.110  0.50 21.05           C  
ANISOU 1421  CA AASP A 184     4040   2496   1462    -52   -212    211       C  
ATOM   1422  CA BASP A 184     -49.802 -26.023   0.126  0.50 21.06           C  
ANISOU 1422  CA BASP A 184     4025   2506   1471    -71   -203    220       C  
ATOM   1423  C   ASP A 184     -48.361 -25.754   0.409  1.00 21.82           C  
ANISOU 1423  C   ASP A 184     4045   2639   1607    -45   -155    110       C  
ATOM   1424  O   ASP A 184     -47.560 -26.414  -0.154  1.00 22.91           O  
ANISOU 1424  O   ASP A 184     4338   2684   1681    -97   -127   -145       O  
ATOM   1425  CB AASP A 184     -50.299 -27.348   0.617  0.50 23.16           C  
ANISOU 1425  CB AASP A 184     4335   2637   1824   -149   -131    349       C  
ATOM   1426  CB BASP A 184     -50.051 -27.422   0.624  0.50 22.39           C  
ANISOU 1426  CB BASP A 184     4329   2622   1555   -104   -198    364       C  
ATOM   1427  CG AASP A 184     -50.116 -27.460   1.988  0.50 24.23           C  
ANISOU 1427  CG AASP A 184     4673   2659   1874   -257   -237    321       C  
ATOM   1428  CG BASP A 184     -51.463 -27.681   0.837  0.50 25.92           C  
ANISOU 1428  CG BASP A 184     4338   3131   2376   -170   -385    527       C  
ATOM   1429  OD1AASP A 184     -50.574 -26.575   2.722  0.50 25.77           O  
ANISOU 1429  OD1AASP A 184     4812   3340   1639   -412     46     69       O  
ATOM   1430  OD1BASP A 184     -52.239 -26.707   0.854  0.50 28.57           O  
ANISOU 1430  OD1BASP A 184     4492   3450   2910     22   -109    -11       O  
ATOM   1431  OD2AASP A 184     -49.608 -28.504   2.236  0.50 26.97           O  
ANISOU 1431  OD2AASP A 184     4700   3456   2088    287   -516    641       O  
ATOM   1432  OD2BASP A 184     -51.775 -28.856   1.012  0.50 30.15           O  
ANISOU 1432  OD2BASP A 184     4851   3299   3305   -504   -160    404       O  
ATOM   1433  N   ILE A 185     -48.049 -24.795   1.264  1.00 20.10           N  
ANISOU 1433  N   ILE A 185     3769   2786   1080    -91   -175    238       N  
ATOM   1434  CA  ILE A 185     -46.652 -24.444   1.510  1.00 18.40           C  
ANISOU 1434  CA  ILE A 185     3706   2459    823   -104     -3    174       C  
ATOM   1435  C   ILE A 185     -46.426 -24.564   3.011  1.00 18.34           C  
ANISOU 1435  C   ILE A 185     3610   2510    847     21    -22    302       C  
ATOM   1436  O   ILE A 185     -47.158 -23.959   3.788  1.00 18.91           O  
ANISOU 1436  O   ILE A 185     3592   2660    931    -49     25    119       O  
ATOM   1437  CB  ILE A 185     -46.313 -23.004   1.015  1.00 17.99           C  
ANISOU 1437  CB  ILE A 185     3395   2564    875    -84    -97    406       C  
ATOM   1438  CG1 ILE A 185     -46.387 -22.937  -0.520  1.00 17.02           C  
ANISOU 1438  CG1 ILE A 185     3506   2125    834    -19      1    144       C  
ATOM   1439  CG2 ILE A 185     -44.923 -22.556   1.501  1.00 17.75           C  
ANISOU 1439  CG2 ILE A 185     3483   2587    674   -107   -122    185       C  
ATOM   1440  CD1 ILE A 185     -46.440 -21.501  -1.091  1.00 17.39           C  
ANISOU 1440  CD1 ILE A 185     3378   2147   1080    -55     29    244       C  
ATOM   1441  N   ASP A 186     -45.473 -25.400   3.399  1.00 18.62           N  
ANISOU 1441  N   ASP A 186     3581   2595    896     93    -44    106       N  
ATOM   1442  CA  ASP A 186     -45.011 -25.447   4.785  1.00 19.12           C  
ANISOU 1442  CA  ASP A 186     3592   2698    975    -18   -188     37       C  
ATOM   1443  C   ASP A 186     -43.538 -25.070   4.835  1.00 19.05           C  
ANISOU 1443  C   ASP A 186     3590   2659    989     44     -6    -68       C  
ATOM   1444  O   ASP A 186     -42.654 -25.737   4.295  1.00 18.41           O  
ANISOU 1444  O   ASP A 186     3551   2620    822    147    -91     19       O  
ATOM   1445  CB  ASP A 186     -45.254 -26.804   5.427  1.00 20.21           C  
ANISOU 1445  CB  ASP A 186     3802   2926    950    -50    -12    222       C  
ATOM   1446  CG  ASP A 186     -44.930 -26.799   6.904  1.00 21.27           C  
ANISOU 1446  CG  ASP A 186     3888   3246    947     14     24    267       C  
ATOM   1447  OD1 ASP A 186     -43.741 -26.825   7.272  1.00 21.25           O  
ANISOU 1447  OD1 ASP A 186     3784   3156   1132   -118    105    165       O  
ATOM   1448  OD2 ASP A 186     -45.864 -26.742   7.713  1.00 26.27           O  
ANISOU 1448  OD2 ASP A 186     4256   3757   1966    255    617    245       O  
ATOM   1449  N   VAL A 187     -43.298 -23.972   5.508  1.00 18.13           N  
ANISOU 1449  N   VAL A 187     3613   2374    901    -37      0    160       N  
ATOM   1450  CA  VAL A 187     -42.019 -23.335   5.540  1.00 17.17           C  
ANISOU 1450  CA  VAL A 187     3574   2312    635     85    100    106       C  
ATOM   1451  C   VAL A 187     -40.904 -24.244   6.118  1.00 17.95           C  
ANISOU 1451  C   VAL A 187     3472   2511    835     28     26    107       C  
ATOM   1452  O   VAL A 187     -39.760 -24.219   5.663  1.00 17.42           O  
ANISOU 1452  O   VAL A 187     3492   2342    785    103    111    206       O  
ATOM   1453  CB  VAL A 187     -42.296 -21.985   6.241  1.00 18.93           C  
ANISOU 1453  CB  VAL A 187     3836   2105   1251     27   -141     79       C  
ATOM   1454  CG1 VAL A 187     -41.663 -21.815   7.611  1.00 19.35           C  
ANISOU 1454  CG1 VAL A 187     3674   2530   1146    183    -18    -12       C  
ATOM   1455  CG2 VAL A 187     -42.199 -20.825   5.274  1.00 18.25           C  
ANISOU 1455  CG2 VAL A 187     3601   2369    962    175    216     91       C  
ATOM   1456  N   ASP A 188     -41.246 -25.082   7.085  1.00 18.09           N  
ANISOU 1456  N   ASP A 188     3539   2422    911     30    274     66       N  
ATOM   1457  CA  ASP A 188     -40.252 -25.997   7.637  1.00 18.70           C  
ANISOU 1457  CA  ASP A 188     3634   2677    793     46    252    273       C  
ATOM   1458  C   ASP A 188     -39.991 -27.205   6.753  1.00 19.07           C  
ANISOU 1458  C   ASP A 188     3577   2681    987    185    147    214       C  
ATOM   1459  O   ASP A 188     -38.839 -27.628   6.596  1.00 19.91           O  
ANISOU 1459  O   ASP A 188     3598   2731   1236    275    197    124       O  
ATOM   1460  CB  ASP A 188     -40.672 -26.449   9.032  1.00 20.00           C  
ANISOU 1460  CB  ASP A 188     3777   2976    844    -44    375    289       C  
ATOM   1461  CG  ASP A 188     -40.688 -25.309  10.014  1.00 21.87           C  
ANISOU 1461  CG  ASP A 188     4343   3061    906   -193    467    246       C  
ATOM   1462  OD1 ASP A 188     -39.932 -24.342   9.795  1.00 25.21           O  
ANISOU 1462  OD1 ASP A 188     4420   3313   1845   -463     65     92       O  
ATOM   1463  OD2 ASP A 188     -41.449 -25.370  10.993  1.00 27.46           O  
ANISOU 1463  OD2 ASP A 188     4485   4183   1764   -238   1059    240       O  
ATOM   1464  N   ASP A 189     -41.059 -27.748   6.170  1.00 20.15           N  
ANISOU 1464  N   ASP A 189     3821   2764   1068    177     25      1       N  
ATOM   1465  CA  ASP A 189     -40.964 -28.887   5.260  1.00 19.81           C  
ANISOU 1465  CA  ASP A 189     3775   2549   1203    209     79    108       C  
ATOM   1466  C   ASP A 189     -40.151 -28.540   4.034  1.00 20.02           C  
ANISOU 1466  C   ASP A 189     3691   2675   1241    268     52    112       C  
ATOM   1467  O   ASP A 189     -39.399 -29.378   3.540  1.00 20.87           O  
ANISOU 1467  O   ASP A 189     3796   2586   1545    298     72     73       O  
ATOM   1468  CB  ASP A 189     -42.350 -29.347   4.828  1.00 21.31           C  
ANISOU 1468  CB  ASP A 189     3905   3023   1167    113     20     37       C  
ATOM   1469  CG  ASP A 189     -43.144 -29.971   5.965  1.00 25.30           C  
ANISOU 1469  CG  ASP A 189     4242   3529   1843   -286    280    189       C  
ATOM   1470  OD1 ASP A 189     -42.627 -30.100   7.101  1.00 27.64           O  
ANISOU 1470  OD1 ASP A 189     4832   3668   2000    -63     88    399       O  
ATOM   1471  OD2 ASP A 189     -44.303 -30.353   5.717  1.00 29.86           O  
ANISOU 1471  OD2 ASP A 189     4197   4288   2859    -94    221    -12       O  
ATOM   1472  N   MET A 190     -40.262 -27.295   3.575  1.00 18.72           N  
ANISOU 1472  N   MET A 190     3544   2565   1001    187     33     21       N  
ATOM   1473  CA AMET A 190     -39.552 -26.896   2.368  0.50 18.94           C  
ANISOU 1473  CA AMET A 190     3565   2593   1035    230     40     78       C  
ATOM   1474  CA BMET A 190     -39.554 -26.830   2.385  0.50 18.13           C  
ANISOU 1474  CA BMET A 190     3514   2437    938    296    -21     46       C  
ATOM   1475  C   MET A 190     -38.213 -26.180   2.641  1.00 18.63           C  
ANISOU 1475  C   MET A 190     3515   2454   1110    338    -26    149       C  
ATOM   1476  O   MET A 190     -37.566 -25.659   1.738  1.00 18.81           O  
ANISOU 1476  O   MET A 190     3448   2459   1238    306     59     76       O  
ATOM   1477  CB AMET A 190     -40.504 -26.149   1.426  0.50 19.99           C  
ANISOU 1477  CB AMET A 190     3583   2743   1269    379     38    106       C  
ATOM   1478  CB BMET A 190     -40.424 -25.845   1.638  0.50 17.81           C  
ANISOU 1478  CB BMET A 190     3294   2399   1074    306     14    -22       C  
ATOM   1479  CG AMET A 190     -41.429 -27.083   0.668  0.50 22.85           C  
ANISOU 1479  CG AMET A 190     3778   3229   1676     29   -177    193       C  
ATOM   1480  CG BMET A 190     -41.752 -26.423   1.219  0.50 17.70           C  
ANISOU 1480  CG BMET A 190     3354   2499    870    341    -83   -268       C  
ATOM   1481  SD AMET A 190     -42.855 -26.140   0.116  0.50 26.66           S  
ANISOU 1481  SD AMET A 190     3896   3717   2516    544    218    111       S  
ATOM   1482  SD BMET A 190     -41.544 -27.552  -0.153  0.50 17.37           S  
ANISOU 1482  SD BMET A 190     3295   2509    794    222     61   -190       S  
ATOM   1483  CE AMET A 190     -42.935 -24.968   1.420  0.50 22.67           C  
ANISOU 1483  CE AMET A 190     3683   3098   1833     98    -60    585       C  
ATOM   1484  CE BMET A 190     -42.001 -29.098   0.626  0.50 18.51           C  
ANISOU 1484  CE BMET A 190     3621   2625    784     85   -230    -56       C  
ATOM   1485  N   ASN A 191     -37.810 -26.161   3.899  1.00 18.66           N  
ANISOU 1485  N   ASN A 191     3570   2357   1162    367    -88     47       N  
ATOM   1486  CA  ASN A 191     -36.637 -25.446   4.366  1.00 18.44           C  
ANISOU 1486  CA  ASN A 191     3491   2370   1143    329     14    155       C  
ATOM   1487  C   ASN A 191     -36.485 -24.018   3.873  1.00 17.55           C  
ANISOU 1487  C   ASN A 191     3229   2354   1082    289    -15    139       C  
ATOM   1488  O   ASN A 191     -35.383 -23.577   3.521  1.00 18.26           O  
ANISOU 1488  O   ASN A 191     3246   2522   1169    338     32    117       O  
ATOM   1489  CB  ASN A 191     -35.362 -26.262   4.112  1.00 19.31           C  
ANISOU 1489  CB  ASN A 191     3559   2479   1300    418    -38    358       C  
ATOM   1490  CG  ASN A 191     -35.463 -27.665   4.658  1.00 21.50           C  
ANISOU 1490  CG  ASN A 191     4132   2370   1664    280    -10    195       C  
ATOM   1491  OD1 ASN A 191     -35.660 -27.869   5.867  1.00 21.91           O  
ANISOU 1491  OD1 ASN A 191     3775   2935   1613    541     97     54       O  
ATOM   1492  ND2 ASN A 191     -35.307 -28.652   3.775  1.00 23.34           N  
ANISOU 1492  ND2 ASN A 191     4328   2674   1865    460     92     -2       N  
ATOM   1493  N   ILE A 192     -37.598 -23.297   3.887  1.00 17.24           N  
ANISOU 1493  N   ILE A 192     3228   2172   1150    252     65    143       N  
ATOM   1494  CA  ILE A 192     -37.632 -21.915   3.457  1.00 15.49           C  
ANISOU 1494  CA  ILE A 192     2971   2105    810    222     46     25       C  
ATOM   1495  C   ILE A 192     -37.203 -20.959   4.580  1.00 16.09           C  
ANISOU 1495  C   ILE A 192     3031   2254    827    149    -34     10       C  
ATOM   1496  O   ILE A 192     -37.673 -21.048   5.714  1.00 17.70           O  
ANISOU 1496  O   ILE A 192     3418   2395    909    234    112    257       O  
ATOM   1497  CB  ILE A 192     -39.042 -21.518   2.974  1.00 15.72           C  
ANISOU 1497  CB  ILE A 192     3107   2122    744    208   -143     94       C  
ATOM   1498  CG1 ILE A 192     -39.420 -22.324   1.730  1.00 16.34           C  
ANISOU 1498  CG1 ILE A 192     3087   2125    995    197   -178    -28       C  
ATOM   1499  CG2 ILE A 192     -39.103 -20.035   2.656  1.00 15.09           C  
ANISOU 1499  CG2 ILE A 192     2901   2095    736    162    -24    121       C  
ATOM   1500  CD1 ILE A 192     -40.881 -22.180   1.310  1.00 16.84           C  
ANISOU 1500  CD1 ILE A 192     3053   2294   1051     78   -261    119       C  
ATOM   1501  N   ASP A 193     -36.335 -20.017   4.226  1.00 14.62           N  
ANISOU 1501  N   ASP A 193     2908   2269    376    210    -34    119       N  
ATOM   1502  CA  ASP A 193     -35.934 -18.940   5.131  1.00 15.37           C  
ANISOU 1502  CA  ASP A 193     2891   2047    901    257    -44    -21       C  
ATOM   1503  C   ASP A 193     -36.752 -17.672   4.914  1.00 14.94           C  
ANISOU 1503  C   ASP A 193     2799   2155    721    267    -97     33       C  
ATOM   1504  O   ASP A 193     -37.154 -17.011   5.878  1.00 15.16           O  
ANISOU 1504  O   ASP A 193     2913   2154    692    178     -8    -14       O  
ATOM   1505  CB  ASP A 193     -34.453 -18.653   4.951  1.00 15.33           C  
ANISOU 1505  CB  ASP A 193     2871   2246    706    267     29    -44       C  
ATOM   1506  CG  ASP A 193     -33.600 -19.854   5.276  1.00 16.78           C  
ANISOU 1506  CG  ASP A 193     2958   2458    958    399    152    126       C  
ATOM   1507  OD1 ASP A 193     -32.958 -20.425   4.355  1.00 15.90           O  
ANISOU 1507  OD1 ASP A 193     2901   2632    506    138    -26     75       O  
ATOM   1508  OD2 ASP A 193     -33.596 -20.246   6.461  1.00 19.01           O  
ANISOU 1508  OD2 ASP A 193     3338   3074    811    541     -8      7       O  
ATOM   1509  N   MET A 194     -37.010 -17.334   3.656  1.00 14.42           N  
ANISOU 1509  N   MET A 194     2637   2179    659    138     20     55       N  
ATOM   1510  CA  MET A 194     -37.875 -16.200   3.354  1.00 14.57           C  
ANISOU 1510  CA  MET A 194     2643   2229    664    153   -148      8       C  
ATOM   1511  C   MET A 194     -38.781 -16.505   2.174  1.00 14.11           C  
ANISOU 1511  C   MET A 194     2562   2150    647    160    -88      6       C  
ATOM   1512  O   MET A 194     -38.408 -17.254   1.274  1.00 14.63           O  
ANISOU 1512  O   MET A 194     2865   2182    509    218   -189      5       O  
ATOM   1513  CB  MET A 194     -37.056 -14.950   3.046  1.00 14.59           C  
ANISOU 1513  CB  MET A 194     2680   2185    677    125   -163   -210       C  
ATOM   1514  CG  MET A 194     -36.098 -14.537   4.162  1.00 15.60           C  
ANISOU 1514  CG  MET A 194     2674   2548    702    -21   -132   -198       C  
ATOM   1515  SD  MET A 194     -35.152 -13.025   3.831  1.00 15.86           S  
ANISOU 1515  SD  MET A 194     2773   2502    751     50     62   -239       S  
ATOM   1516  CE  MET A 194     -33.837 -13.638   2.772  1.00 14.23           C  
ANISOU 1516  CE  MET A 194     2744   2400    260    194   -133    -44       C  
ATOM   1517  N   LEU A 195     -39.981 -15.939   2.208  1.00 13.98           N  
ANISOU 1517  N   LEU A 195     2536   2055    720    164   -172    135       N  
ATOM   1518  CA  LEU A 195     -40.991 -16.173   1.170  1.00 13.28           C  
ANISOU 1518  CA  LEU A 195     2653   1876    516    -41    -36    -79       C  
ATOM   1519  C   LEU A 195     -41.822 -14.920   0.883  1.00 13.98           C  
ANISOU 1519  C   LEU A 195     2650   2019    641     58     62     66       C  
ATOM   1520  O   LEU A 195     -42.351 -14.279   1.801  1.00 13.79           O  
ANISOU 1520  O   LEU A 195     2746   2008    485     19     82    159       O  
ATOM   1521  CB  LEU A 195     -41.885 -17.343   1.580  1.00 13.48           C  
ANISOU 1521  CB  LEU A 195     2574   1982    563    -30    102    -55       C  
ATOM   1522  CG  LEU A 195     -43.116 -17.647   0.717  1.00 13.69           C  
ANISOU 1522  CG  LEU A 195     2577   1894    730    -65     49     13       C  
ATOM   1523  CD1 LEU A 195     -43.439 -19.136   0.814  1.00 14.81           C  
ANISOU 1523  CD1 LEU A 195     2861   1859    905    -34     37     16       C  
ATOM   1524  CD2 LEU A 195     -44.333 -16.802   1.109  1.00 14.53           C  
ANISOU 1524  CD2 LEU A 195     2680   2078    763     30     89   -202       C  
ATOM   1525  N   SER A 196     -41.921 -14.560  -0.398  1.00 14.02           N  
ANISOU 1525  N   SER A 196     2711   1956    658     23    -11     70       N  
ATOM   1526  CA  SER A 196     -42.718 -13.405  -0.800  1.00 13.74           C  
ANISOU 1526  CA  SER A 196     2563   2003    653    -20    134    156       C  
ATOM   1527  C   SER A 196     -44.111 -13.783  -1.264  1.00 14.06           C  
ANISOU 1527  C   SER A 196     2606   1992    743    -23     92     24       C  
ATOM   1528  O   SER A 196     -44.291 -14.784  -1.975  1.00 14.20           O  
ANISOU 1528  O   SER A 196     2731   2244    421    -29   -110    -22       O  
ATOM   1529  CB  SER A 196     -42.042 -12.662  -1.950  1.00 12.96           C  
ANISOU 1529  CB  SER A 196     2451   2024    446     82     72    139       C  
ATOM   1530  OG  SER A 196     -40.782 -12.167  -1.557  1.00 14.30           O  
ANISOU 1530  OG  SER A 196     2584   2157    692    -59     58     12       O  
ATOM   1531  N   LEU A 197     -45.089 -12.964  -0.890  1.00 13.41           N  
ANISOU 1531  N   LEU A 197     2553   2173    369     -4    103    117       N  
ATOM   1532  CA  LEU A 197     -46.454 -13.139  -1.390  1.00 14.05           C  
ANISOU 1532  CA  LEU A 197     2624   2220    494     70     -4    157       C  
ATOM   1533  C   LEU A 197     -47.113 -11.782  -1.695  1.00 14.44           C  
ANISOU 1533  C   LEU A 197     2654   2150    682     36     62     81       C  
ATOM   1534  O   LEU A 197     -46.676 -10.747  -1.176  1.00 13.88           O  
ANISOU 1534  O   LEU A 197     2702   2175    396     82    -53     78       O  
ATOM   1535  CB  LEU A 197     -47.296 -13.986  -0.413  1.00 14.57           C  
ANISOU 1535  CB  LEU A 197     2677   2175    682    -73    133    -33       C  
ATOM   1536  CG  LEU A 197     -47.522 -13.440   1.009  1.00 13.73           C  
ANISOU 1536  CG  LEU A 197     2542   2022    650     70    107     42       C  
ATOM   1537  CD1 LEU A 197     -48.821 -12.643   1.120  1.00 13.54           C  
ANISOU 1537  CD1 LEU A 197     2582   1958    604    104    101    228       C  
ATOM   1538  CD2 LEU A 197     -47.517 -14.589   2.015  1.00 14.67           C  
ANISOU 1538  CD2 LEU A 197     2829   2073    672   -123    123     94       C  
ATOM   1539  N   SER A 198     -48.153 -11.817  -2.532  1.00 15.20           N  
ANISOU 1539  N   SER A 198     2563   2381    830    138     14    207       N  
ATOM   1540  CA  SER A 198     -48.848 -10.623  -3.026  1.00 14.97           C  
ANISOU 1540  CA  SER A 198     2630   2275    782     44    127    269       C  
ATOM   1541  C   SER A 198     -50.370 -10.746  -2.841  1.00 14.84           C  
ANISOU 1541  C   SER A 198     2622   2195    819     70     93    150       C  
ATOM   1542  O   SER A 198     -50.964 -11.721  -3.299  1.00 14.99           O  
ANISOU 1542  O   SER A 198     2677   2305    712    -41     84    170       O  
ATOM   1543  CB  SER A 198     -48.526 -10.438  -4.513  1.00 16.02           C  
ANISOU 1543  CB  SER A 198     2936   2493    656    102     24     48       C  
ATOM   1544  OG  SER A 198     -49.216  -9.332  -5.048  1.00 16.41           O  
ANISOU 1544  OG  SER A 198     3155   2388    690    222    265    -11       O  
ATOM   1545  N   GLY A 199     -50.994  -9.759  -2.190  1.00 14.11           N  
ANISOU 1545  N   GLY A 199     2504   2343    512     63      0     58       N  
ATOM   1546  CA  GLY A 199     -52.444  -9.799  -1.913  1.00 14.12           C  
ANISOU 1546  CA  GLY A 199     2504   2385    475    -16     18    -66       C  
ATOM   1547  C   GLY A 199     -53.335  -9.851  -3.143  1.00 14.50           C  
ANISOU 1547  C   GLY A 199     2551   2208    748    -77   -172     59       C  
ATOM   1548  O   GLY A 199     -54.304 -10.601  -3.186  1.00 14.40           O  
ANISOU 1548  O   GLY A 199     2531   2258    681    -98    -13     76       O  
ATOM   1549  N   HIS A 200     -52.995  -9.085  -4.169  1.00 14.54           N  
ANISOU 1549  N   HIS A 200     2648   2283    591    -56    -78    -25       N  
ATOM   1550  CA  HIS A 200     -53.913  -8.974  -5.291  1.00 15.29           C  
ANISOU 1550  CA  HIS A 200     2744   2311    751   -202   -203     73       C  
ATOM   1551  C   HIS A 200     -53.814 -10.140  -6.248  1.00 15.47           C  
ANISOU 1551  C   HIS A 200     2739   2385    752   -142    -82     41       C  
ATOM   1552  O   HIS A 200     -54.480 -10.152  -7.279  1.00 16.63           O  
ANISOU 1552  O   HIS A 200     2999   2475    844   -105   -218    130       O  
ATOM   1553  CB  HIS A 200     -53.761  -7.628  -5.996  1.00 15.38           C  
ANISOU 1553  CB  HIS A 200     2745   2333    766    -81   -123    112       C  
ATOM   1554  CG  HIS A 200     -52.484  -7.503  -6.784  1.00 15.60           C  
ANISOU 1554  CG  HIS A 200     2784   2445    694   -201   -124    142       C  
ATOM   1555  ND1 HIS A 200     -52.440  -7.661  -8.121  1.00 15.33           N  
ANISOU 1555  ND1 HIS A 200     2690   2361    770   -190     -6   -174       N  
ATOM   1556  CD2 HIS A 200     -51.170  -7.261  -6.369  1.00 16.09           C  
ANISOU 1556  CD2 HIS A 200     2714   2514    882   -182    -35    120       C  
ATOM   1557  CE1 HIS A 200     -51.166  -7.516  -8.542  1.00 15.74           C  
ANISOU 1557  CE1 HIS A 200     2662   2494    824   -210    -84     23       C  
ATOM   1558  NE2 HIS A 200     -50.392  -7.276  -7.471  1.00 15.84           N  
ANISOU 1558  NE2 HIS A 200     2753   2514    752     13   -127     -8       N  
ATOM   1559  N   LYS A 201     -53.002 -11.138  -5.914  1.00 14.62           N  
ANISOU 1559  N   LYS A 201     2586   2321    646   -227    -19    114       N  
ATOM   1560  CA  LYS A 201     -52.944 -12.382  -6.688  1.00 14.95           C  
ANISOU 1560  CA  LYS A 201     2626   2485    568   -154     27     37       C  
ATOM   1561  C   LYS A 201     -53.865 -13.468  -6.112  1.00 15.32           C  
ANISOU 1561  C   LYS A 201     2685   2396    737   -140     29    100       C  
ATOM   1562  O   LYS A 201     -54.059 -14.525  -6.742  1.00 15.59           O  
ANISOU 1562  O   LYS A 201     2745   2616    560   -180   -146     60       O  
ATOM   1563  CB  LYS A 201     -51.498 -12.908  -6.767  1.00 15.51           C  
ANISOU 1563  CB  LYS A 201     2719   2434    737    -45    -94    131       C  
ATOM   1564  CG  LYS A 201     -50.497 -11.927  -7.356  1.00 16.11           C  
ANISOU 1564  CG  LYS A 201     2760   2557    803   -131    -34     -7       C  
ATOM   1565  CD  LYS A 201     -50.810 -11.674  -8.822  1.00 16.80           C  
ANISOU 1565  CD  LYS A 201     2981   2629    772   -155    269    323       C  
ATOM   1566  CE  LYS A 201     -49.834 -10.689  -9.428  1.00 17.61           C  
ANISOU 1566  CE  LYS A 201     2685   2333   1672   -197    142     43       C  
ATOM   1567  NZ  LYS A 201     -48.475 -11.277  -9.477  1.00 17.11           N  
ANISOU 1567  NZ  LYS A 201     2788   2245   1466   -162    185    117       N  
ATOM   1568  N   VAL A 202     -54.429 -13.199  -4.925  1.00 14.79           N  
ANISOU 1568  N   VAL A 202     2549   2424    643   -181    -90     75       N  
ATOM   1569  CA  VAL A 202     -55.266 -14.165  -4.187  1.00 14.83           C  
ANISOU 1569  CA  VAL A 202     2613   2319    703   -174    -45     93       C  
ATOM   1570  C   VAL A 202     -56.641 -13.576  -3.806  1.00 14.84           C  
ANISOU 1570  C   VAL A 202     2664   2236    739   -150    -40     89       C  
ATOM   1571  O   VAL A 202     -57.242 -13.926  -2.780  1.00 15.65           O  
ANISOU 1571  O   VAL A 202     2743   2404    798   -169    -79    318       O  
ATOM   1572  CB  VAL A 202     -54.525 -14.763  -2.955  1.00 14.61           C  
ANISOU 1572  CB  VAL A 202     2646   2233    673   -186    -99    -18       C  
ATOM   1573  CG1 VAL A 202     -53.380 -15.665  -3.394  1.00 15.31           C  
ANISOU 1573  CG1 VAL A 202     2767   2065    984   -302    -20   -230       C  
ATOM   1574  CG2 VAL A 202     -54.017 -13.682  -1.999  1.00 14.66           C  
ANISOU 1574  CG2 VAL A 202     2630   2298    642   -248     12    -53       C  
ATOM   1575  N   TYR A 203     -57.133 -12.684  -4.671  1.00 15.47           N  
ANISOU 1575  N   TYR A 203     2780   2342    756   -186   -119    164       N  
ATOM   1576  CA  TYR A 203     -58.428 -12.010  -4.507  1.00 15.29           C  
ANISOU 1576  CA  TYR A 203     2777   2240    792   -235    -41    103       C  
ATOM   1577  C   TYR A 203     -58.432 -11.028  -3.333  1.00 15.16           C  
ANISOU 1577  C   TYR A 203     2776   2286    698   -253    -34    131       C  
ATOM   1578  O   TYR A 203     -59.493 -10.665  -2.797  1.00 15.59           O  
ANISOU 1578  O   TYR A 203     2702   2434    786   -169   -114     50       O  
ATOM   1579  CB  TYR A 203     -59.598 -13.007  -4.403  1.00 15.65           C  
ANISOU 1579  CB  TYR A 203     2947   2237    762   -313    -51     70       C  
ATOM   1580  CG  TYR A 203     -59.708 -14.077  -5.489  1.00 15.73           C  
ANISOU 1580  CG  TYR A 203     2932   2276    766   -227   -101     14       C  
ATOM   1581  CD1 TYR A 203     -60.289 -13.806  -6.732  1.00 15.98           C  
ANISOU 1581  CD1 TYR A 203     2903   2442    725   -269    -44     40       C  
ATOM   1582  CD2 TYR A 203     -59.279 -15.372  -5.244  1.00 15.57           C  
ANISOU 1582  CD2 TYR A 203     2919   2272    724   -358   -216     75       C  
ATOM   1583  CE1 TYR A 203     -60.419 -14.800  -7.689  1.00 16.90           C  
ANISOU 1583  CE1 TYR A 203     2927   2573    920   -368     88   -133       C  
ATOM   1584  CE2 TYR A 203     -59.387 -16.357  -6.198  1.00 17.20           C  
ANISOU 1584  CE2 TYR A 203     3105   2641    789   -294   -142   -152       C  
ATOM   1585  CZ  TYR A 203     -59.954 -16.079  -7.407  1.00 16.36           C  
ANISOU 1585  CZ  TYR A 203     2991   2666    557   -426    156     59       C  
ATOM   1586  OH  TYR A 203     -60.060 -17.130  -8.277  1.00 17.74           O  
ANISOU 1586  OH  TYR A 203     3284   2543    913   -266     15    -21       O  
ATOM   1587  N   GLY A 204     -57.225 -10.623  -2.939  1.00 15.18           N  
ANISOU 1587  N   GLY A 204     2810   2176    779   -320     -1     49       N  
ATOM   1588  CA  GLY A 204     -57.030  -9.563  -1.945  1.00 15.06           C  
ANISOU 1588  CA  GLY A 204     2812   2335    573   -254   -162     78       C  
ATOM   1589  C   GLY A 204     -56.903  -8.189  -2.585  1.00 15.24           C  
ANISOU 1589  C   GLY A 204     2747   2318    723   -128    -38     98       C  
ATOM   1590  O   GLY A 204     -56.845  -8.063  -3.823  1.00 15.47           O  
ANISOU 1590  O   GLY A 204     2677   2543    655   -165   -142   -109       O  
ATOM   1591  N   PRO A 205     -56.831  -7.142  -1.754  1.00 15.02           N  
ANISOU 1591  N   PRO A 205     2632   2436    639    -68     47      4       N  
ATOM   1592  CA  PRO A 205     -56.668  -5.824  -2.325  1.00 15.62           C  
ANISOU 1592  CA  PRO A 205     2754   2406    774   -142    137    -67       C  
ATOM   1593  C   PRO A 205     -55.259  -5.587  -2.846  1.00 14.83           C  
ANISOU 1593  C   PRO A 205     2587   2195    851    -26    -26    135       C  
ATOM   1594  O   PRO A 205     -54.298  -6.261  -2.444  1.00 13.85           O  
ANISOU 1594  O   PRO A 205     2682   2257    322    -74   -151    188       O  
ATOM   1595  CB  PRO A 205     -56.986  -4.882  -1.162  1.00 15.40           C  
ANISOU 1595  CB  PRO A 205     2816   2521    513    -78    187     92       C  
ATOM   1596  CG  PRO A 205     -56.659  -5.664   0.050  1.00 14.22           C  
ANISOU 1596  CG  PRO A 205     2604   2247    552     93   -146   -158       C  
ATOM   1597  CD  PRO A 205     -56.878  -7.112  -0.281  1.00 15.05           C  
ANISOU 1597  CD  PRO A 205     2749   2321    648   -161    -28    -50       C  
ATOM   1598  N   LYS A 206     -55.160  -4.634  -3.765  1.00 14.96           N  
ANISOU 1598  N   LYS A 206     2611   2407    663    -77   -142    191       N  
ATOM   1599  CA  LYS A 206     -53.869  -4.124  -4.197  1.00 14.06           C  
ANISOU 1599  CA  LYS A 206     2602   2101    636    -79   -219    203       C  
ATOM   1600  C   LYS A 206     -53.232  -3.281  -3.087  1.00 14.22           C  
ANISOU 1600  C   LYS A 206     2440   2276    686    -56   -187    112       C  
ATOM   1601  O   LYS A 206     -53.928  -2.725  -2.214  1.00 15.22           O  
ANISOU 1601  O   LYS A 206     2550   2295    938     -6   -166    -57       O  
ATOM   1602  CB  LYS A 206     -54.007  -3.309  -5.496  1.00 13.04           C  
ANISOU 1602  CB  LYS A 206     2643   1796    515     36   -178     14       C  
ATOM   1603  CG  LYS A 206     -54.226  -4.184  -6.725  1.00 13.28           C  
ANISOU 1603  CG  LYS A 206     2603   1818    624     16   -301    -40       C  
ATOM   1604  CD  LYS A 206     -54.420  -3.362  -7.996  1.00 13.45           C  
ANISOU 1604  CD  LYS A 206     2651   1957    499    100   -306    -96       C  
ATOM   1605  CE  LYS A 206     -54.787  -4.265  -9.180  1.00 14.03           C  
ANISOU 1605  CE  LYS A 206     2528   2130    672    -62   -138   -280       C  
ATOM   1606  NZ  LYS A 206     -56.158  -4.859  -9.055  1.00 14.67           N  
ANISOU 1606  NZ  LYS A 206     2382   2489    702     83     25   -269       N  
ATOM   1607  N   GLY A 207     -51.903  -3.198  -3.133  1.00 13.92           N  
ANISOU 1607  N   GLY A 207     2408   2186    694    -26   -224    134       N  
ATOM   1608  CA  GLY A 207     -51.123  -2.444  -2.161  1.00 13.58           C  
ANISOU 1608  CA  GLY A 207     2488   2051    619    -66    -80     74       C  
ATOM   1609  C   GLY A 207     -50.759  -3.180  -0.889  1.00 13.82           C  
ANISOU 1609  C   GLY A 207     2466   2029    753      1   -204    100       C  
ATOM   1610  O   GLY A 207     -50.279  -2.555   0.052  1.00 14.01           O  
ANISOU 1610  O   GLY A 207     2562   2142    617     42   -104     -4       O  
ATOM   1611  N   ILE A 208     -50.929  -4.503  -0.860  1.00 13.29           N  
ANISOU 1611  N   ILE A 208     2536   2028    484    -50   -162     87       N  
ATOM   1612  CA  ILE A 208     -50.496  -5.266   0.306  1.00 13.82           C  
ANISOU 1612  CA  ILE A 208     2398   2070    782     34   -237    223       C  
ATOM   1613  C   ILE A 208     -49.846  -6.594  -0.068  1.00 14.13           C  
ANISOU 1613  C   ILE A 208     2509   2157    700     44   -193    153       C  
ATOM   1614  O   ILE A 208     -50.239  -7.223  -1.021  1.00 13.88           O  
ANISOU 1614  O   ILE A 208     2479   2165    628     13   -184    176       O  
ATOM   1615  CB  ILE A 208     -51.684  -5.481   1.260  1.00 13.65           C  
ANISOU 1615  CB  ILE A 208     2482   2014    690     10   -213    255       C  
ATOM   1616  CG1 ILE A 208     -51.212  -5.960   2.634  1.00 14.41           C  
ANISOU 1616  CG1 ILE A 208     2523   2269    680    -17   -258    231       C  
ATOM   1617  CG2 ILE A 208     -52.724  -6.399   0.643  1.00 14.06           C  
ANISOU 1617  CG2 ILE A 208     2459   2245    635    -85   -121    217       C  
ATOM   1618  CD1 ILE A 208     -50.566  -4.858   3.442  1.00 14.38           C  
ANISOU 1618  CD1 ILE A 208     2482   2463    516      9   -171    127       C  
ATOM   1619  N   GLY A 209     -48.846  -7.015   0.681  1.00 13.81           N  
ANISOU 1619  N   GLY A 209     2487   2124    633     23   -158    198       N  
ATOM   1620  CA  GLY A 209     -48.351  -8.372   0.540  1.00 13.79           C  
ANISOU 1620  CA  GLY A 209     2512   2139    587     72    -42    230       C  
ATOM   1621  C   GLY A 209     -47.617  -8.692   1.821  1.00 13.57           C  
ANISOU 1621  C   GLY A 209     2467   2050    637     75    -88    143       C  
ATOM   1622  O   GLY A 209     -47.831  -8.037   2.846  1.00 13.44           O  
ANISOU 1622  O   GLY A 209     2421   2235    451     20    -25    232       O  
ATOM   1623  N   ALA A 210     -46.755  -9.697   1.776  1.00 13.38           N  
ANISOU 1623  N   ALA A 210     2561   2044    479     75     22    245       N  
ATOM   1624  CA  ALA A 210     -45.973 -10.046   2.948  1.00 12.79           C  
ANISOU 1624  CA  ALA A 210     2424   1900    536     61     -5    163       C  
ATOM   1625  C   ALA A 210     -44.650 -10.710   2.595  1.00 13.51           C  
ANISOU 1625  C   ALA A 210     2496   2056    579     47    120    145       C  
ATOM   1626  O   ALA A 210     -44.457 -11.175   1.468  1.00 13.74           O  
ANISOU 1626  O   ALA A 210     2641   1915    665    140     33     28       O  
ATOM   1627  CB  ALA A 210     -46.794 -10.940   3.877  1.00 13.47           C  
ANISOU 1627  CB  ALA A 210     2596   2023    497     63     72    210       C  
ATOM   1628  N   LEU A 211     -43.725 -10.704   3.551  1.00 13.31           N  
ANISOU 1628  N   LEU A 211     2499   1903    655     76     64    102       N  
ATOM   1629  CA  LEU A 211     -42.505 -11.485   3.469  1.00 13.99           C  
ANISOU 1629  CA  LEU A 211     2544   1986    786    112     65     98       C  
ATOM   1630  C   LEU A 211     -42.431 -12.326   4.738  1.00 13.84           C  
ANISOU 1630  C   LEU A 211     2661   1881    714    105    107     20       C  
ATOM   1631  O   LEU A 211     -42.370 -11.775   5.844  1.00 13.77           O  
ANISOU 1631  O   LEU A 211     2599   1957    674    181     31     47       O  
ATOM   1632  CB  LEU A 211     -41.264 -10.588   3.379  1.00 13.49           C  
ANISOU 1632  CB  LEU A 211     2502   1964    659    120    223    -42       C  
ATOM   1633  CG  LEU A 211     -39.929 -11.337   3.229  1.00 13.32           C  
ANISOU 1633  CG  LEU A 211     2447   1917    697     69    127   -109       C  
ATOM   1634  CD1 LEU A 211     -39.809 -12.068   1.885  1.00 13.63           C  
ANISOU 1634  CD1 LEU A 211     2643   1831    704    113    118   -103       C  
ATOM   1635  CD2 LEU A 211     -38.759 -10.385   3.449  1.00 13.57           C  
ANISOU 1635  CD2 LEU A 211     2420   2162    574     14    -38   -177       C  
ATOM   1636  N   TYR A 212     -42.482 -13.649   4.575  1.00 13.69           N  
ANISOU 1636  N   TYR A 212     2730   1828    643    181    220    137       N  
ATOM   1637  CA  TYR A 212     -42.098 -14.573   5.651  1.00 13.66           C  
ANISOU 1637  CA  TYR A 212     2587   1914    686    182      9     86       C  
ATOM   1638  C   TYR A 212     -40.590 -14.452   5.902  1.00 14.14           C  
ANISOU 1638  C   TYR A 212     2614   2060    697    205     54     36       C  
ATOM   1639  O   TYR A 212     -39.795 -14.533   4.962  1.00 14.02           O  
ANISOU 1639  O   TYR A 212     2697   2051    576    178     60     24       O  
ATOM   1640  CB  TYR A 212     -42.457 -16.025   5.298  1.00 14.12           C  
ANISOU 1640  CB  TYR A 212     2828   1919    618    118     94     76       C  
ATOM   1641  CG  TYR A 212     -41.702 -17.030   6.130  1.00 14.28           C  
ANISOU 1641  CG  TYR A 212     2717   2012    696    135    -61    -60       C  
ATOM   1642  CD1 TYR A 212     -42.069 -17.264   7.436  1.00 15.16           C  
ANISOU 1642  CD1 TYR A 212     2766   2152    841     75     25    207       C  
ATOM   1643  CD2 TYR A 212     -40.608 -17.722   5.609  1.00 14.99           C  
ANISOU 1643  CD2 TYR A 212     2640   2134    919    152    -87    -19       C  
ATOM   1644  CE1 TYR A 212     -41.378 -18.175   8.209  1.00 16.08           C  
ANISOU 1644  CE1 TYR A 212     3080   2273    756    306     60    146       C  
ATOM   1645  CE2 TYR A 212     -39.913 -18.647   6.362  1.00 15.48           C  
ANISOU 1645  CE2 TYR A 212     3066   2007    808     81    -46    116       C  
ATOM   1646  CZ  TYR A 212     -40.307 -18.862   7.666  1.00 16.04           C  
ANISOU 1646  CZ  TYR A 212     3053   2224    815    251     -2     72       C  
ATOM   1647  OH  TYR A 212     -39.641 -19.769   8.427  1.00 17.59           O  
ANISOU 1647  OH  TYR A 212     3325   2336   1019    380   -134    129       O  
ATOM   1648  N   VAL A 213     -40.199 -14.260   7.157  1.00 13.97           N  
ANISOU 1648  N   VAL A 213     2633   2003    669    243     34     54       N  
ATOM   1649  CA  VAL A 213     -38.790 -14.218   7.532  1.00 14.45           C  
ANISOU 1649  CA  VAL A 213     2653   2082    754    301    125    157       C  
ATOM   1650  C   VAL A 213     -38.624 -15.131   8.728  1.00 14.75           C  
ANISOU 1650  C   VAL A 213     2757   2131    716    305     36    132       C  
ATOM   1651  O   VAL A 213     -39.092 -14.833   9.832  1.00 15.54           O  
ANISOU 1651  O   VAL A 213     2964   2265    673    257     75    117       O  
ATOM   1652  CB  VAL A 213     -38.350 -12.793   7.929  1.00 14.75           C  
ANISOU 1652  CB  VAL A 213     2833   2195    574    113   -134    230       C  
ATOM   1653  CG1 VAL A 213     -36.885 -12.760   8.374  1.00 16.14           C  
ANISOU 1653  CG1 VAL A 213     2745   2522    865    336     70    143       C  
ATOM   1654  CG2 VAL A 213     -38.588 -11.826   6.779  1.00 14.24           C  
ANISOU 1654  CG2 VAL A 213     2658   1950    802    222     -8    253       C  
ATOM   1655  N   ARG A 214     -37.951 -16.249   8.506  1.00 15.43           N  
ANISOU 1655  N   ARG A 214     2890   2045    928    320   -118    226       N  
ATOM   1656  CA  ARG A 214     -37.683 -17.167   9.606  1.00 15.53           C  
ANISOU 1656  CA  ARG A 214     3055   2240    604    327      2    169       C  
ATOM   1657  C   ARG A 214     -36.946 -16.432  10.724  1.00 16.44           C  
ANISOU 1657  C   ARG A 214     3067   2472    704    283     12     71       C  
ATOM   1658  O   ARG A 214     -35.953 -15.741  10.481  1.00 17.70           O  
ANISOU 1658  O   ARG A 214     3180   2577    968    288    101     78       O  
ATOM   1659  CB  ARG A 214     -36.860 -18.361   9.122  1.00 15.68           C  
ANISOU 1659  CB  ARG A 214     3093   2112    752    291   -167     77       C  
ATOM   1660  CG  ARG A 214     -36.713 -19.446  10.187  1.00 17.21           C  
ANISOU 1660  CG  ARG A 214     3312   2254    973    337   -193    211       C  
ATOM   1661  CD  ARG A 214     -35.898 -20.633   9.680  1.00 19.02           C  
ANISOU 1661  CD  ARG A 214     3663   2537   1027    574   -368    -81       C  
ATOM   1662  NE  ARG A 214     -36.562 -21.420   8.631  1.00 20.22           N  
ANISOU 1662  NE  ARG A 214     3807   2682   1193     23   -301     34       N  
ATOM   1663  CZ  ARG A 214     -37.468 -22.372   8.848  1.00 21.76           C  
ANISOU 1663  CZ  ARG A 214     4127   3097   1041   -191    -67    -40       C  
ATOM   1664  NH1 ARG A 214     -37.852 -22.683  10.084  1.00 24.44           N  
ANISOU 1664  NH1 ARG A 214     4473   3438   1374   -255    184    255       N  
ATOM   1665  NH2 ARG A 214     -37.993 -23.033   7.820  1.00 21.70           N  
ANISOU 1665  NH2 ARG A 214     3761   2893   1591    -92   -287   -129       N  
ATOM   1666  N   ASP A 215     -37.430 -16.608  11.955  1.00 16.89           N  
ANISOU 1666  N   ASP A 215     3115   2594    708    401     38     58       N  
ATOM   1667  CA  ASP A 215     -36.795 -16.029  13.145  1.00 17.08           C  
ANISOU 1667  CA  ASP A 215     3124   2741    623    266    235    -59       C  
ATOM   1668  C   ASP A 215     -36.700 -14.509  12.996  1.00 17.99           C  
ANISOU 1668  C   ASP A 215     3140   2757    937    260     12     55       C  
ATOM   1669  O   ASP A 215     -35.679 -13.902  13.326  1.00 18.67           O  
ANISOU 1669  O   ASP A 215     3133   2941   1017    346   -313    124       O  
ATOM   1670  CB  ASP A 215     -35.401 -16.657  13.394  1.00 19.07           C  
ANISOU 1670  CB  ASP A 215     3474   2902    868    485   -123   -108       C  
ATOM   1671  CG  ASP A 215     -34.828 -16.351  14.778  1.00 21.77           C  
ANISOU 1671  CG  ASP A 215     3789   3408   1073    109   -308   -176       C  
ATOM   1672  OD1 ASP A 215     -35.605 -16.137  15.721  1.00 23.88           O  
ANISOU 1672  OD1 ASP A 215     4459   3679    934    212    -53     84       O  
ATOM   1673  OD2 ASP A 215     -33.588 -16.375  14.922  1.00 25.21           O  
ANISOU 1673  OD2 ASP A 215     3908   3807   1861    286   -582   -142       O  
ATOM   1674  N   ALA A 216     -37.766 -13.890  12.494  1.00 16.57           N  
ANISOU 1674  N   ALA A 216     3069   2700    527    273    -52   -127       N  
ATOM   1675  CA  ALA A 216     -37.778 -12.445  12.262  1.00 17.14           C  
ANISOU 1675  CA  ALA A 216     3179   2758    574    194    -50     16       C  
ATOM   1676  C   ALA A 216     -37.345 -11.626  13.491  1.00 18.99           C  
ANISOU 1676  C   ALA A 216     3497   2970    746     26   -229    -60       C  
ATOM   1677  O   ALA A 216     -36.664 -10.617  13.349  1.00 19.39           O  
ANISOU 1677  O   ALA A 216     3613   3170    582   -142   -237     -1       O  
ATOM   1678  CB  ALA A 216     -39.150 -11.996  11.777  1.00 15.80           C  
ANISOU 1678  CB  ALA A 216     3176   2462    364    245    -89     78       C  
ATOM   1679  N   ARG A 217     -37.693 -12.106  14.684  1.00 19.71           N  
ANISOU 1679  N   ARG A 217     3643   3082    763    113     74   -217       N  
ATOM   1680  CA AARG A 217     -37.393 -11.358  15.888  0.50 20.03           C  
ANISOU 1680  CA AARG A 217     3736   3170    703    -49    -87    -86       C  
ATOM   1681  CA BARG A 217     -37.414 -11.411  15.927  0.50 20.69           C  
ANISOU 1681  CA BARG A 217     3782   3310    766    -59    -71   -181       C  
ATOM   1682  C   ARG A 217     -35.895 -11.172  16.038  1.00 22.01           C  
ANISOU 1682  C   ARG A 217     3754   3362   1245    -35    -16   -161       C  
ATOM   1683  O   ARG A 217     -35.483 -10.181  16.566  1.00 22.79           O  
ANISOU 1683  O   ARG A 217     3948   3533   1178     -7    -42   -373       O  
ATOM   1684  CB AARG A 217     -37.963 -12.027  17.132  0.50 20.77           C  
ANISOU 1684  CB AARG A 217     3660   3519    711    -78    276   -328       C  
ATOM   1685  CB BARG A 217     -37.907 -12.264  17.101  0.50 23.08           C  
ANISOU 1685  CB BARG A 217     4017   3788    963   -215    362   -187       C  
ATOM   1686  CG AARG A 217     -39.425 -11.710  17.411  0.50 20.87           C  
ANISOU 1686  CG AARG A 217     3535   3504    888    -22     14    372       C  
ATOM   1687  CG BARG A 217     -38.484 -11.532  18.303  0.50 26.69           C  
ANISOU 1687  CG BARG A 217     4445   4186   1509     25    756   -369       C  
ATOM   1688  CD AARG A 217     -39.902 -12.574  18.569  0.50 23.69           C  
ANISOU 1688  CD AARG A 217     3633   4057   1308    112    499    684       C  
ATOM   1689  CD BARG A 217     -37.850 -12.115  19.547  0.50 27.87           C  
ANISOU 1689  CD BARG A 217     4499   4666   1421     41   1121     23       C  
ATOM   1690  NE AARG A 217     -41.310 -12.369  18.893  0.50 22.32           N  
ANISOU 1690  NE AARG A 217     3283   3861   1335    268   -403    615       N  
ATOM   1691  NE BARG A 217     -38.120 -13.547  19.648  0.50 28.02           N  
ANISOU 1691  NE BARG A 217     4687   4813   1144     78   1910    589       N  
ATOM   1692  CZ AARG A 217     -42.197 -13.347  19.006  0.50 22.43           C  
ANISOU 1692  CZ AARG A 217     3343   3798   1380    207   -430    277       C  
ATOM   1693  CZ BARG A 217     -37.293 -14.431  20.192  0.50 26.49           C  
ANISOU 1693  CZ BARG A 217     4128   4893   1042    -69   1721    310       C  
ATOM   1694  NH1AARG A 217     -41.816 -14.597  18.811  0.50 26.17           N  
ANISOU 1694  NH1AARG A 217     3912   3946   2085    403   -433    120       N  
ATOM   1695  NH1BARG A 217     -36.123 -14.042  20.677  0.50 26.83           N  
ANISOU 1695  NH1BARG A 217     4737   4896    558   -317   1159     77       N  
ATOM   1696  NH2AARG A 217     -43.459 -13.079  19.308  0.50 18.50           N  
ANISOU 1696  NH2AARG A 217     3395   3077    554    237   -362    157       N  
ATOM   1697  NH2BARG A 217     -37.637 -15.711  20.238  0.50 29.21           N  
ANISOU 1697  NH2BARG A 217     4941   4847   1310    -25   1942     78       N  
ATOM   1698  N   ASN A 218     -35.090 -12.115  15.580  1.00 20.15           N  
ANISOU 1698  N   ASN A 218     3706   3257    692      0    -40   -123       N  
ATOM   1699  CA  ASN A 218     -33.642 -12.049  15.728  1.00 21.36           C  
ANISOU 1699  CA  ASN A 218     3752   3480    884    -52   -161     23       C  
ATOM   1700  C   ASN A 218     -32.943 -11.805  14.394  1.00 21.11           C  
ANISOU 1700  C   ASN A 218     3364   3746    908     -7   -226     26       C  
ATOM   1701  O   ASN A 218     -31.713 -11.925  14.283  1.00 23.86           O  
ANISOU 1701  O   ASN A 218     3385   4126   1552    435   -560    105       O  
ATOM   1702  CB  ASN A 218     -33.172 -13.349  16.373  1.00 22.76           C  
ANISOU 1702  CB  ASN A 218     4004   3691    953     14    -12    225       C  
ATOM   1703  CG  ASN A 218     -33.757 -13.546  17.756  1.00 24.59           C  
ANISOU 1703  CG  ASN A 218     4454   3906    981    -42    233   -150       C  
ATOM   1704  OD1 ASN A 218     -34.520 -14.476  17.993  1.00 26.93           O  
ANISOU 1704  OD1 ASN A 218     4530   4299   1402    -76    525    146       O  
ATOM   1705  ND2 ASN A 218     -33.423 -12.652  18.666  1.00 25.71           N  
ANISOU 1705  ND2 ASN A 218     5033   3865    869     33   -121    -78       N  
ATOM   1706  N   SER A 219     -33.723 -11.447  13.381  1.00 20.82           N  
ANISOU 1706  N   SER A 219     3682   3541    687    187   -140    109       N  
ATOM   1707  CA  SER A 219     -33.177 -11.243  12.045  1.00 21.33           C  
ANISOU 1707  CA  SER A 219     3520   3802    780   -102   -106    131       C  
ATOM   1708  C   SER A 219     -32.255 -10.031  11.963  1.00 23.07           C  
ANISOU 1708  C   SER A 219     3572   3906   1286   -106   -314    110       C  
ATOM   1709  O   SER A 219     -32.552  -8.954  12.485  1.00 24.11           O  
ANISOU 1709  O   SER A 219     3979   3972   1207   -178   -301     37       O  
ATOM   1710  CB  SER A 219     -34.305 -11.111  11.019  1.00 21.06           C  
ANISOU 1710  CB  SER A 219     3587   3650    763     21   -134    439       C  
ATOM   1711  OG  SER A 219     -33.823 -10.461   9.856  1.00 22.58           O  
ANISOU 1711  OG  SER A 219     3497   4048   1033   -188    154    453       O  
ATOM   1712  N   GLU A 220     -31.136 -10.206  11.279  1.00 23.18           N  
ANISOU 1712  N   GLU A 220     3390   3924   1491    -96   -396    201       N  
ATOM   1713  CA  GLU A 220     -30.233  -9.102  11.040  1.00 24.65           C  
ANISOU 1713  CA  GLU A 220     3644   3974   1747   -215   -503    438       C  
ATOM   1714  C   GLU A 220     -30.448  -8.464   9.675  1.00 22.76           C  
ANISOU 1714  C   GLU A 220     3422   3769   1457     32   -291    128       C  
ATOM   1715  O   GLU A 220     -29.610  -7.698   9.227  1.00 22.85           O  
ANISOU 1715  O   GLU A 220     3279   3947   1453     70   -407    329       O  
ATOM   1716  CB  GLU A 220     -28.806  -9.581  11.133  1.00 27.86           C  
ANISOU 1716  CB  GLU A 220     3763   4264   2557    -43   -906    247       C  
ATOM   1717  CG  GLU A 220     -28.416 -10.122  12.495  1.00 28.48           C  
ANISOU 1717  CG  GLU A 220     3559   4495   2766     75  -1162    243       C  
ATOM   1718  CD  GLU A 220     -26.909 -10.323  12.583  1.00 31.51           C  
ANISOU 1718  CD  GLU A 220     3448   1958   6563   -775  -2380  -1594       C  
ATOM   1719  OE1 GLU A 220     -26.178  -9.355  12.873  1.00 38.76           O  
ANISOU 1719  OE1 GLU A 220     3546   2962   8217  -1566  -1966  -2550       O  
ATOM   1720  OE2 GLU A 220     -26.450 -11.454  12.324  1.00 43.49           O  
ANISOU 1720  OE2 GLU A 220     5531   3816   7175   1957  -1025   -820       O  
ATOM   1721  N   LEU A 221     -31.582  -8.751   9.036  1.00 22.17           N  
ANISOU 1721  N   LEU A 221     3611   3620   1190    -39   -302     99       N  
ATOM   1722  CA  LEU A 221     -31.887  -8.163   7.735  1.00 20.29           C  
ANISOU 1722  CA  LEU A 221     3180   3478   1050     -9    -74     13       C  
ATOM   1723  C   LEU A 221     -31.860  -6.667   7.863  1.00 19.73           C  
ANISOU 1723  C   LEU A 221     3037   3383   1073    209     39    107       C  
ATOM   1724  O   LEU A 221     -32.365  -6.134   8.838  1.00 20.53           O  
ANISOU 1724  O   LEU A 221     3510   3289   1002    107     67     48       O  
ATOM   1725  CB  LEU A 221     -33.295  -8.519   7.303  1.00 21.41           C  
ANISOU 1725  CB  LEU A 221     3065   3786   1281    -61    143     24       C  
ATOM   1726  CG  LEU A 221     -33.651  -9.805   6.564  1.00 22.44           C  
ANISOU 1726  CG  LEU A 221     2831   3969   1727     38    718   -459       C  
ATOM   1727  CD1 LEU A 221     -35.148  -9.761   6.296  1.00 20.87           C  
ANISOU 1727  CD1 LEU A 221     2944   3691   1293    231    420   -374       C  
ATOM   1728  CD2 LEU A 221     -32.883 -10.033   5.260  1.00 18.04           C  
ANISOU 1728  CD2 LEU A 221     2987   2950    914     16    225      7       C  
ATOM   1729  N   VAL A 222     -31.280  -5.986   6.883  1.00 18.94           N  
ANISOU 1729  N   VAL A 222     3099   3130    967    279    -65    124       N  
ATOM   1730  CA  VAL A 222     -31.315  -4.530   6.829  1.00 19.29           C  
ANISOU 1730  CA  VAL A 222     2889   3142   1295    139   -146    187       C  
ATOM   1731  C   VAL A 222     -32.695  -4.103   6.296  1.00 18.20           C  
ANISOU 1731  C   VAL A 222     2831   3008   1076    227    -71    -43       C  
ATOM   1732  O   VAL A 222     -33.073  -4.492   5.187  1.00 18.75           O  
ANISOU 1732  O   VAL A 222     2972   3123   1028    237    -24    -70       O  
ATOM   1733  CB  VAL A 222     -30.181  -3.963   5.932  1.00 19.67           C  
ANISOU 1733  CB  VAL A 222     2964   3201   1305    157    -21     17       C  
ATOM   1734  CG1 VAL A 222     -30.331  -2.457   5.793  1.00 20.08           C  
ANISOU 1734  CG1 VAL A 222     2991   3162   1473    -29    -17    208       C  
ATOM   1735  CG2 VAL A 222     -28.819  -4.299   6.508  1.00 21.41           C  
ANISOU 1735  CG2 VAL A 222     2864   3522   1747    243     10    -33       C  
ATOM   1736  N   PRO A 223     -33.458  -3.329   7.092  1.00 16.47           N  
ANISOU 1736  N   PRO A 223     2719   2740    799     69    -94     66       N  
ATOM   1737  CA  PRO A 223     -34.767  -2.844   6.662  1.00 16.07           C  
ANISOU 1737  CA  PRO A 223     2616   2677    812    216    194    125       C  
ATOM   1738  C   PRO A 223     -34.668  -2.070   5.342  1.00 16.74           C  
ANISOU 1738  C   PRO A 223     2908   2733    719     84    -20     80       C  
ATOM   1739  O   PRO A 223     -33.720  -1.299   5.142  1.00 17.81           O  
ANISOU 1739  O   PRO A 223     2900   3009    858    -17     72   -265       O  
ATOM   1740  CB  PRO A 223     -35.186  -1.922   7.811  1.00 15.51           C  
ANISOU 1740  CB  PRO A 223     2672   2539    682    114   -198    -12       C  
ATOM   1741  CG  PRO A 223     -34.485  -2.498   9.003  1.00 15.94           C  
ANISOU 1741  CG  PRO A 223     2707   2507    842    160   -182    128       C  
ATOM   1742  CD  PRO A 223     -33.142  -2.910   8.471  1.00 16.50           C  
ANISOU 1742  CD  PRO A 223     2803   2630    835    244   -104      6       C  
ATOM   1743  N   LEU A 224     -35.608  -2.331   4.436  1.00 16.69           N  
ANISOU 1743  N   LEU A 224     2828   2688    825     87    -28     24       N  
ATOM   1744  CA  LEU A 224     -35.728  -1.586   3.182  1.00 16.97           C  
ANISOU 1744  CA  LEU A 224     3052   2539    854     36   -188    -14       C  
ATOM   1745  C   LEU A 224     -36.359  -0.226   3.492  1.00 16.76           C  
ANISOU 1745  C   LEU A 224     2887   2451   1028   -120   -110    -83       C  
ATOM   1746  O   LEU A 224     -35.874   0.821   3.046  1.00 16.82           O  
ANISOU 1746  O   LEU A 224     2688   2738    963   -220   -143    128       O  
ATOM   1747  CB  LEU A 224     -36.584  -2.379   2.175  1.00 18.05           C  
ANISOU 1747  CB  LEU A 224     3148   2748    962    -86   -192   -138       C  
ATOM   1748  CG  LEU A 224     -36.523  -2.063   0.677  1.00 17.65           C  
ANISOU 1748  CG  LEU A 224     2738   2877   1091     82   -179    160       C  
ATOM   1749  CD1 LEU A 224     -35.216  -2.551   0.068  1.00 19.30           C  
ANISOU 1749  CD1 LEU A 224     3045   3257   1028    305     66     94       C  
ATOM   1750  CD2 LEU A 224     -37.728  -2.664  -0.029  1.00 17.22           C  
ANISOU 1750  CD2 LEU A 224     3050   2807    684    112   -310   -114       C  
ATOM   1751  N   ILE A 225     -37.442  -0.250   4.264  1.00 16.25           N  
ANISOU 1751  N   ILE A 225     3016   2452    703     -5    -70      7       N  
ATOM   1752  CA  ILE A 225     -38.063   0.977   4.748  1.00 15.33           C  
ANISOU 1752  CA  ILE A 225     2840   2290    692   -171   -138    -53       C  
ATOM   1753  C   ILE A 225     -37.800   1.091   6.252  1.00 15.42           C  
ANISOU 1753  C   ILE A 225     2822   2367    669    -46    -58    -84       C  
ATOM   1754  O   ILE A 225     -38.368   0.338   7.036  1.00 15.67           O  
ANISOU 1754  O   ILE A 225     3085   2261    606     62     50    -61       O  
ATOM   1755  CB  ILE A 225     -39.577   0.987   4.444  1.00 15.71           C  
ANISOU 1755  CB  ILE A 225     2868   2363    739     36   -209     18       C  
ATOM   1756  CG1 ILE A 225     -39.802   0.815   2.933  1.00 17.51           C  
ANISOU 1756  CG1 ILE A 225     3001   2758    894   -287   -513   -221       C  
ATOM   1757  CG2 ILE A 225     -40.242   2.273   4.942  1.00 15.59           C  
ANISOU 1757  CG2 ILE A 225     2858   2403    661    -52   -124   -139       C  
ATOM   1758  CD1 ILE A 225     -41.230   0.471   2.575  1.00 19.01           C  
ANISOU 1758  CD1 ILE A 225     2949   3089   1184   -200   -474    -62       C  
ATOM   1759  N   HIS A 226     -36.913   2.000   6.641  1.00 15.07           N  
ANISOU 1759  N   HIS A 226     2775   2287    664     35   -186    -65       N  
ATOM   1760  CA  HIS A 226     -36.735   2.299   8.064  1.00 15.47           C  
ANISOU 1760  CA  HIS A 226     2778   2429    668     23    -90   -142       C  
ATOM   1761  C   HIS A 226     -37.890   3.130   8.529  1.00 16.00           C  
ANISOU 1761  C   HIS A 226     2956   2571    549     74     28    -37       C  
ATOM   1762  O   HIS A 226     -38.353   4.012   7.815  1.00 16.35           O  
ANISOU 1762  O   HIS A 226     2963   2499    748     72     -2      7       O  
ATOM   1763  CB  HIS A 226     -35.413   3.010   8.312  1.00 15.31           C  
ANISOU 1763  CB  HIS A 226     2814   2464    540     55    -93   -138       C  
ATOM   1764  CG  HIS A 226     -34.224   2.105   8.221  1.00 16.03           C  
ANISOU 1764  CG  HIS A 226     2794   2547    747    115   -288      5       C  
ATOM   1765  ND1 HIS A 226     -33.672   1.517   9.302  1.00 18.52           N  
ANISOU 1765  ND1 HIS A 226     3041   2737   1255    536   -388    224       N  
ATOM   1766  CD2 HIS A 226     -33.500   1.676   7.125  1.00 15.58           C  
ANISOU 1766  CD2 HIS A 226     2749   2412    758     37   -138    192       C  
ATOM   1767  CE1 HIS A 226     -32.638   0.751   8.903  1.00 15.27           C  
ANISOU 1767  CE1 HIS A 226     2583   2376    843     91   -342      8       C  
ATOM   1768  NE2 HIS A 226     -32.541   0.850   7.570  1.00 17.49           N  
ANISOU 1768  NE2 HIS A 226     2949   2755    939     22   -237    315       N  
ATOM   1769  N   GLY A 227     -38.393   2.864   9.730  1.00 16.19           N  
ANISOU 1769  N   GLY A 227     3040   2454    657    -24    131    -13       N  
ATOM   1770  CA  GLY A 227     -39.584   3.563  10.158  1.00 17.04           C  
ANISOU 1770  CA  GLY A 227     3115   2636    722      9    198   -127       C  
ATOM   1771  C   GLY A 227     -39.620   3.743  11.647  1.00 18.08           C  
ANISOU 1771  C   GLY A 227     3342   2766    759     14    275   -248       C  
ATOM   1772  O   GLY A 227     -38.578   3.820  12.290  1.00 20.37           O  
ANISOU 1772  O   GLY A 227     3697   3130    911   -277     75    -97       O  
ATOM   1773  N   GLY A 228     -40.835   3.765  12.187  1.00 17.96           N  
ANISOU 1773  N   GLY A 228     3439   2462    922   -138    424   -209       N  
ATOM   1774  CA  GLY A 228     -41.079   3.992  13.603  1.00 18.62           C  
ANISOU 1774  CA  GLY A 228     3483   2774    817    -66    213   -118       C  
ATOM   1775  C   GLY A 228     -41.076   2.777  14.518  1.00 18.12           C  
ANISOU 1775  C   GLY A 228     3477   2571    836    -46    209   -243       C  
ATOM   1776  O   GLY A 228     -41.248   2.940  15.714  1.00 19.81           O  
ANISOU 1776  O   GLY A 228     3738   2924    866     -7    447   -169       O  
ATOM   1777  N   GLY A 229     -40.838   1.586  13.968  1.00 17.44           N  
ANISOU 1777  N   GLY A 229     3116   2407   1104    -28    142   -110       N  
ATOM   1778  CA  GLY A 229     -40.780   0.351  14.750  1.00 17.50           C  
ANISOU 1778  CA  GLY A 229     3238   2375   1035    103    -49   -124       C  
ATOM   1779  C   GLY A 229     -41.744  -0.720  14.280  1.00 16.07           C  
ANISOU 1779  C   GLY A 229     3087   2397    621    118     26    -53       C  
ATOM   1780  O   GLY A 229     -41.754  -1.829  14.808  1.00 16.02           O  
ANISOU 1780  O   GLY A 229     3212   2387    487    158   -130    -91       O  
ATOM   1781  N   GLN A 230     -42.562  -0.391  13.287  1.00 15.39           N  
ANISOU 1781  N   GLN A 230     2836   2269    741    133     39   -116       N  
ATOM   1782  CA  GLN A 230     -43.491  -1.356  12.716  1.00 15.22           C  
ANISOU 1782  CA  GLN A 230     2811   2246    723    180   -120     16       C  
ATOM   1783  C   GLN A 230     -42.769  -2.599  12.218  1.00 14.32           C  
ANISOU 1783  C   GLN A 230     2721   2192    527     82    -69     42       C  
ATOM   1784  O   GLN A 230     -41.614  -2.544  11.779  1.00 14.40           O  
ANISOU 1784  O   GLN A 230     2785   2213    471     91     67    -28       O  
ATOM   1785  CB  GLN A 230     -44.302  -0.744  11.565  1.00 15.26           C  
ANISOU 1785  CB  GLN A 230     2795   2225    776    137    -62    152       C  
ATOM   1786  CG  GLN A 230     -45.270   0.345  12.012  1.00 15.60           C  
ANISOU 1786  CG  GLN A 230     2678   2315    934     65    -40     33       C  
ATOM   1787  CD  GLN A 230     -44.686   1.749  11.934  1.00 16.89           C  
ANISOU 1787  CD  GLN A 230     2868   2363   1186     20   -165     17       C  
ATOM   1788  OE1 GLN A 230     -43.475   1.934  11.808  1.00 17.70           O  
ANISOU 1788  OE1 GLN A 230     2941   2450   1332    -58      0      1       O  
ATOM   1789  NE2 GLN A 230     -45.549   2.747  12.024  1.00 16.15           N  
ANISOU 1789  NE2 GLN A 230     2896   2358    880     12   -208   -103       N  
ATOM   1790  N   GLU A 231     -43.477  -3.720  12.301  1.00 14.37           N  
ANISOU 1790  N   GLU A 231     2639   2214    606     71    -75     44       N  
ATOM   1791  CA  GLU A 231     -43.022  -5.017  11.770  1.00 14.58           C  
ANISOU 1791  CA  GLU A 231     2661   2205    672     40   -109     -3       C  
ATOM   1792  C   GLU A 231     -41.685  -5.431  12.383  1.00 15.23           C  
ANISOU 1792  C   GLU A 231     2704   2392    690     93    -82    -12       C  
ATOM   1793  O   GLU A 231     -40.761  -5.818  11.682  1.00 15.06           O  
ANISOU 1793  O   GLU A 231     2810   2293    618    114    -84    -59       O  
ATOM   1794  CB  GLU A 231     -42.981  -5.020  10.223  1.00 14.95           C  
ANISOU 1794  CB  GLU A 231     2566   2435    679    143   -109    -16       C  
ATOM   1795  CG  GLU A 231     -44.289  -4.603   9.570  1.00 14.86           C  
ANISOU 1795  CG  GLU A 231     2472   2414    759    134    -16     30       C  
ATOM   1796  CD  GLU A 231     -45.434  -5.516   9.963  1.00 15.45           C  
ANISOU 1796  CD  GLU A 231     2768   2262    839     44     92    -16       C  
ATOM   1797  OE1 GLU A 231     -46.424  -5.034  10.558  1.00 17.14           O  
ANISOU 1797  OE1 GLU A 231     2728   2624   1158    188     61    -94       O  
ATOM   1798  OE2 GLU A 231     -45.329  -6.725   9.690  1.00 14.45           O  
ANISOU 1798  OE2 GLU A 231     2774   2186    528     82    105    150       O  
ATOM   1799  N   LEU A 232     -41.596  -5.305  13.708  1.00 15.31           N  
ANISOU 1799  N   LEU A 232     2736   2399    683    -89    -68    -30       N  
ATOM   1800  CA  LEU A 232     -40.403  -5.698  14.473  1.00 15.54           C  
ANISOU 1800  CA  LEU A 232     2917   2203    783     83   -123      1       C  
ATOM   1801  C   LEU A 232     -39.192  -4.873  14.067  1.00 15.96           C  
ANISOU 1801  C   LEU A 232     2903   2397    761     84    -27     84       C  
ATOM   1802  O   LEU A 232     -38.047  -5.301  14.233  1.00 17.88           O  
ANISOU 1802  O   LEU A 232     2938   2632   1224     28   -129    416       O  
ATOM   1803  CB  LEU A 232     -40.103  -7.198  14.323  1.00 16.74           C  
ANISOU 1803  CB  LEU A 232     3120   2246    991    160    -25    138       C  
ATOM   1804  CG  LEU A 232     -41.220  -8.220  14.571  1.00 17.92           C  
ANISOU 1804  CG  LEU A 232     3214   2460   1134    -52   -124    -83       C  
ATOM   1805  CD1 LEU A 232     -40.713  -9.629  14.271  1.00 20.01           C  
ANISOU 1805  CD1 LEU A 232     3622   2599   1380    186    -93     37       C  
ATOM   1806  CD2 LEU A 232     -41.794  -8.180  15.986  1.00 19.74           C  
ANISOU 1806  CD2 LEU A 232     3779   2757    961     -3   -187    283       C  
ATOM   1807  N   GLY A 233     -39.453  -3.687  13.529  1.00 14.62           N  
ANISOU 1807  N   GLY A 233     2892   2229    432     10   -116   -112       N  
ATOM   1808  CA  GLY A 233     -38.393  -2.794  13.068  1.00 16.51           C  
ANISOU 1808  CA  GLY A 233     2967   2531    776   -107     -2    -59       C  
ATOM   1809  C   GLY A 233     -37.887  -3.147  11.680  1.00 15.25           C  
ANISOU 1809  C   GLY A 233     2854   2201    737    107    -80     31       C  
ATOM   1810  O   GLY A 233     -36.980  -2.491  11.159  1.00 16.53           O  
ANISOU 1810  O   GLY A 233     2984   2302    992    -13     32   -122       O  
ATOM   1811  N   LEU A 234     -38.459  -4.192  11.081  1.00 14.71           N  
ANISOU 1811  N   LEU A 234     2859   2079    652    186    -49     81       N  
ATOM   1812  CA  LEU A 234     -38.014  -4.637   9.738  1.00 14.34           C  
ANISOU 1812  CA  LEU A 234     2731   2049    667    145      4    120       C  
ATOM   1813  C   LEU A 234     -38.649  -3.904   8.553  1.00 14.08           C  
ANISOU 1813  C   LEU A 234     2517   2113    716     96    -71     83       C  
ATOM   1814  O   LEU A 234     -38.085  -3.905   7.451  1.00 15.04           O  
ANISOU 1814  O   LEU A 234     2723   2280    711     95    -24    104       O  
ATOM   1815  CB  LEU A 234     -38.203  -6.146   9.557  1.00 14.67           C  
ANISOU 1815  CB  LEU A 234     2822   2077    672    208    -53     36       C  
ATOM   1816  CG  LEU A 234     -37.428  -7.028  10.536  1.00 15.88           C  
ANISOU 1816  CG  LEU A 234     2813   2140   1079    257    -72    241       C  
ATOM   1817  CD1 LEU A 234     -37.973  -8.446  10.494  1.00 16.14           C  
ANISOU 1817  CD1 LEU A 234     2955   2250    924    143     72   -222       C  
ATOM   1818  CD2 LEU A 234     -35.930  -7.000  10.239  1.00 19.33           C  
ANISOU 1818  CD2 LEU A 234     2989   2659   1695    365    263    278       C  
ATOM   1819  N   ARG A 235     -39.818  -3.302   8.771  1.00 14.86           N  
ANISOU 1819  N   ARG A 235     2584   2339    722    216   -179     85       N  
ATOM   1820  CA  ARG A 235     -40.577  -2.662   7.685  1.00 13.91           C  
ANISOU 1820  CA  ARG A 235     2577   2157    550    141    -50    127       C  
ATOM   1821  C   ARG A 235     -41.418  -1.499   8.203  1.00 14.18           C  
ANISOU 1821  C   ARG A 235     2594   2266    527    160   -141     43       C  
ATOM   1822  O   ARG A 235     -42.468  -1.703   8.843  1.00 14.52           O  
ANISOU 1822  O   ARG A 235     2667   2204    644    110    -22     66       O  
ATOM   1823  CB  ARG A 235     -41.460  -3.694   6.966  1.00 15.08           C  
ANISOU 1823  CB  ARG A 235     2686   2320    723    108   -182     64       C  
ATOM   1824  CG  ARG A 235     -41.963  -3.262   5.596  1.00 14.76           C  
ANISOU 1824  CG  ARG A 235     2485   2392    728    247    -75    101       C  
ATOM   1825  CD  ARG A 235     -43.152  -2.327   5.710  1.00 15.23           C  
ANISOU 1825  CD  ARG A 235     2645   2313    827    325   -269    107       C  
ATOM   1826  NE  ARG A 235     -43.685  -2.014   4.393  1.00 13.94           N  
ANISOU 1826  NE  ARG A 235     2408   2204    684     87   -171     16       N  
ATOM   1827  CZ  ARG A 235     -44.855  -1.425   4.176  1.00 14.48           C  
ANISOU 1827  CZ  ARG A 235     2434   2376    689    245    -20     -8       C  
ATOM   1828  NH1 ARG A 235     -45.618  -1.059   5.205  1.00 14.91           N  
ANISOU 1828  NH1 ARG A 235     2572   2646    445     64     29    141       N  
ATOM   1829  NH2 ARG A 235     -45.261  -1.182   2.925  1.00 15.55           N  
ANISOU 1829  NH2 ARG A 235     2929   2246    730    254     -5    270       N  
ATOM   1830  N   GLY A 236     -40.942  -0.285   7.925  1.00 14.50           N  
ANISOU 1830  N   GLY A 236     2591   2253    663    132    -61      3       N  
ATOM   1831  CA  GLY A 236     -41.588   0.936   8.395  1.00 14.84           C  
ANISOU 1831  CA  GLY A 236     2855   2145    638     32    -88   -103       C  
ATOM   1832  C   GLY A 236     -42.777   1.401   7.585  1.00 15.32           C  
ANISOU 1832  C   GLY A 236     2662   2289    870    156      1   -211       C  
ATOM   1833  O   GLY A 236     -43.061   0.861   6.516  1.00 15.59           O  
ANISOU 1833  O   GLY A 236     2842   2268    811     87    -83   -124       O  
ATOM   1834  N   GLY A 237     -43.458   2.428   8.094  1.00 15.96           N  
ANISOU 1834  N   GLY A 237     2767   2215   1080     83    123   -298       N  
ATOM   1835  CA  GLY A 237     -44.687   2.946   7.485  1.00 16.19           C  
ANISOU 1835  CA  GLY A 237     2722   2527    898     72    191   -158       C  
ATOM   1836  C   GLY A 237     -45.900   2.568   8.315  1.00 15.75           C  
ANISOU 1836  C   GLY A 237     2727   2412    843     40     78     47       C  
ATOM   1837  O   GLY A 237     -45.966   1.456   8.844  1.00 14.84           O  
ANISOU 1837  O   GLY A 237     2854   2310    475    -27     36    -91       O  
ATOM   1838  N   THR A 238     -46.878   3.460   8.429  1.00 14.19           N  
ANISOU 1838  N   THR A 238     2698   2378    315     -4    -14   -241       N  
ATOM   1839  CA  THR A 238     -48.032   3.067   9.241  1.00 16.59           C  
ANISOU 1839  CA  THR A 238     2878   2692    734   -165    191   -104       C  
ATOM   1840  C   THR A 238     -48.809   1.903   8.660  1.00 15.81           C  
ANISOU 1840  C   THR A 238     2777   2430    800    -29    -65    139       C  
ATOM   1841  O   THR A 238     -49.055   1.822   7.456  1.00 15.76           O  
ANISOU 1841  O   THR A 238     2819   2388    779    -35     55    -29       O  
ATOM   1842  CB  THR A 238     -48.900   4.216   9.849  1.00 19.09           C  
ANISOU 1842  CB  THR A 238     3035   2584   1633     81    -60     12       C  
ATOM   1843  OG1 THR A 238     -50.297   4.133   9.513  1.00 20.08           O  
ANISOU 1843  OG1 THR A 238     3344   3065   1219    143   -748   -189       O  
ATOM   1844  CG2 THR A 238     -48.338   5.581   9.662  1.00 14.00           C  
ANISOU 1844  CG2 THR A 238     2527   2424    367    303    273    451       C  
ATOM   1845  N   SER A 239     -49.105   0.959   9.548  1.00 15.35           N  
ANISOU 1845  N   SER A 239     2555   2382    894   -111     95     72       N  
ATOM   1846  CA  SER A 239     -49.771  -0.277   9.177  1.00 15.02           C  
ANISOU 1846  CA  SER A 239     2482   2352    870   -112   -152    234       C  
ATOM   1847  C   SER A 239     -51.108   0.053   8.540  1.00 14.94           C  
ANISOU 1847  C   SER A 239     2461   2543    670     99    -44    107       C  
ATOM   1848  O   SER A 239     -51.950   0.713   9.155  1.00 15.63           O  
ANISOU 1848  O   SER A 239     2755   2336    846    113    -62    -17       O  
ATOM   1849  CB  SER A 239     -49.978  -1.155  10.407  1.00 15.13           C  
ANISOU 1849  CB  SER A 239     2500   2492    756     30    -70    227       C  
ATOM   1850  OG  SER A 239     -48.732  -1.438  11.009  1.00 16.04           O  
ANISOU 1850  OG  SER A 239     2643   2732    716   -116   -270    126       O  
ATOM   1851  N   PRO A 240     -51.315  -0.389   7.292  1.00 14.45           N  
ANISOU 1851  N   PRO A 240     2251   2460    776    -19      4    -46       N  
ATOM   1852  CA  PRO A 240     -52.583  -0.047   6.629  1.00 14.22           C  
ANISOU 1852  CA  PRO A 240     2190   2514    697     29    144   -108       C  
ATOM   1853  C   PRO A 240     -53.701  -1.030   6.971  1.00 14.32           C  
ANISOU 1853  C   PRO A 240     2353   2416    670     12    136    -19       C  
ATOM   1854  O   PRO A 240     -53.945  -1.991   6.229  1.00 14.20           O  
ANISOU 1854  O   PRO A 240     2343   2276    774    -36    112      8       O  
ATOM   1855  CB  PRO A 240     -52.215  -0.119   5.147  1.00 14.10           C  
ANISOU 1855  CB  PRO A 240     2330   2342    685    153    160      0       C  
ATOM   1856  CG  PRO A 240     -51.143  -1.167   5.090  1.00 13.47           C  
ANISOU 1856  CG  PRO A 240     1855   2648    613     53    -84    143       C  
ATOM   1857  CD  PRO A 240     -50.339  -0.986   6.358  1.00 13.84           C  
ANISOU 1857  CD  PRO A 240     2240   2400    618    -71   -117   -133       C  
ATOM   1858  N   THR A 241     -54.404  -0.761   8.067  1.00 14.93           N  
ANISOU 1858  N   THR A 241     2445   2277    950    129    362     26       N  
ATOM   1859  CA  THR A 241     -55.246  -1.787   8.652  1.00 15.56           C  
ANISOU 1859  CA  THR A 241     2633   2278   1000   -185     -8     24       C  
ATOM   1860  C   THR A 241     -56.284  -2.356   7.697  1.00 14.95           C  
ANISOU 1860  C   THR A 241     2507   2225    945     48    -51     -3       C  
ATOM   1861  O   THR A 241     -56.408  -3.544   7.635  1.00 13.78           O  
ANISOU 1861  O   THR A 241     2512   2209    512     48    -61     -6       O  
ATOM   1862  CB  THR A 241     -55.687  -1.483  10.114  1.00 17.78           C  
ANISOU 1862  CB  THR A 241     2777   2485   1494      0    514   -253       C  
ATOM   1863  OG1 THR A 241     -57.034  -1.918  10.427  1.00 20.84           O  
ANISOU 1863  OG1 THR A 241     2650   3212   2054     -7    208   -173       O  
ATOM   1864  CG2 THR A 241     -55.381  -0.078  10.526  1.00 12.42           C  
ANISOU 1864  CG2 THR A 241     2328   2019    372    250    463    220       C  
ATOM   1865  N   PRO A 242     -56.949  -1.523   6.892  1.00 14.40           N  
ANISOU 1865  N   PRO A 242     2526   2313    631    -18     60     50       N  
ATOM   1866  CA  PRO A 242     -57.919  -2.116   5.960  1.00 14.77           C  
ANISOU 1866  CA  PRO A 242     2593   2297    719    104    -61      0       C  
ATOM   1867  C   PRO A 242     -57.298  -3.148   5.007  1.00 14.21           C  
ANISOU 1867  C   PRO A 242     2467   2189    740     79    142    203       C  
ATOM   1868  O   PRO A 242     -57.864  -4.232   4.800  1.00 14.08           O  
ANISOU 1868  O   PRO A 242     2424   2282    644      3    173    160       O  
ATOM   1869  CB  PRO A 242     -58.456  -0.909   5.171  1.00 14.80           C  
ANISOU 1869  CB  PRO A 242     2612   2394    616    118     24    101       C  
ATOM   1870  CG  PRO A 242     -58.024   0.312   5.932  1.00 16.13           C  
ANISOU 1870  CG  PRO A 242     2695   2375   1058     47      2     70       C  
ATOM   1871  CD  PRO A 242     -56.788  -0.078   6.705  1.00 14.79           C  
ANISOU 1871  CD  PRO A 242     2542   2333    744     13    122     62       C  
ATOM   1872  N   LEU A 243     -56.132  -2.824   4.447  1.00 13.92           N  
ANISOU 1872  N   LEU A 243     2319   2221    749    113     29    110       N  
ATOM   1873  CA  LEU A 243     -55.418  -3.730   3.517  1.00 13.69           C  
ANISOU 1873  CA  LEU A 243     2313   2226    662     35     23    111       C  
ATOM   1874  C   LEU A 243     -54.957  -5.031   4.194  1.00 14.19           C  
ANISOU 1874  C   LEU A 243     2506   2189    697    -13    -93     88       C  
ATOM   1875  O   LEU A 243     -55.063  -6.134   3.630  1.00 13.76           O  
ANISOU 1875  O   LEU A 243     2514   2186    527    -33    -68    143       O  
ATOM   1876  CB  LEU A 243     -54.220  -3.009   2.896  1.00 13.92           C  
ANISOU 1876  CB  LEU A 243     2362   2298    629      7     36    194       C  
ATOM   1877  CG  LEU A 243     -54.567  -1.757   2.089  1.00 13.80           C  
ANISOU 1877  CG  LEU A 243     2364   2115    762      0    -36     86       C  
ATOM   1878  CD1 LEU A 243     -53.287  -1.043   1.693  1.00 14.10           C  
ANISOU 1878  CD1 LEU A 243     2324   2270    761     15    -64    152       C  
ATOM   1879  CD2 LEU A 243     -55.396  -2.100   0.854  1.00 15.58           C  
ANISOU 1879  CD2 LEU A 243     2463   2703    753     -6   -148    194       C  
ATOM   1880  N   ILE A 244     -54.467  -4.900   5.424  1.00 14.06           N  
ANISOU 1880  N   ILE A 244     2462   2277    603    -49     -1    130       N  
ATOM   1881  CA  ILE A 244     -54.035  -6.060   6.189  1.00 14.18           C  
ANISOU 1881  CA  ILE A 244     2372   2234    780   -159   -139    159       C  
ATOM   1882  C   ILE A 244     -55.229  -6.979   6.515  1.00 13.87           C  
ANISOU 1882  C   ILE A 244     2373   2197    699   -148     13     -9       C  
ATOM   1883  O   ILE A 244     -55.176  -8.195   6.279  1.00 13.10           O  
ANISOU 1883  O   ILE A 244     2462   2122    390    -33    124     99       O  
ATOM   1884  CB  ILE A 244     -53.305  -5.615   7.476  1.00 14.01           C  
ANISOU 1884  CB  ILE A 244     2424   2205    692   -176    -66    110       C  
ATOM   1885  CG1 ILE A 244     -51.906  -5.061   7.160  1.00 14.12           C  
ANISOU 1885  CG1 ILE A 244     2429   2218    716   -199    -82    -61       C  
ATOM   1886  CG2 ILE A 244     -53.121  -6.785   8.420  1.00 14.89           C  
ANISOU 1886  CG2 ILE A 244     2499   2323    835    -65     73    249       C  
ATOM   1887  CD1 ILE A 244     -51.330  -4.184   8.262  1.00 14.15           C  
ANISOU 1887  CD1 ILE A 244     2518   2376    482   -197    -95     -2       C  
ATOM   1888  N   VAL A 245     -56.305  -6.386   7.035  1.00 13.12           N  
ANISOU 1888  N   VAL A 245     2405   2232    344    -62    -30     51       N  
ATOM   1889  CA  VAL A 245     -57.539  -7.130   7.323  1.00 13.85           C  
ANISOU 1889  CA  VAL A 245     2395   2269    598    -81     -4    -23       C  
ATOM   1890  C   VAL A 245     -58.061  -7.845   6.062  1.00 14.14           C  
ANISOU 1890  C   VAL A 245     2556   2178    636   -105     -8    -20       C  
ATOM   1891  O   VAL A 245     -58.389  -9.030   6.099  1.00 14.32           O  
ANISOU 1891  O   VAL A 245     2525   2173    743    -53    146    -44       O  
ATOM   1892  CB  VAL A 245     -58.608  -6.210   7.983  1.00 14.02           C  
ANISOU 1892  CB  VAL A 245     2432   2201    690    -64     55     32       C  
ATOM   1893  CG1 VAL A 245     -59.968  -6.885   8.075  1.00 15.28           C  
ANISOU 1893  CG1 VAL A 245     2529   2454    821   -206    103     -4       C  
ATOM   1894  CG2 VAL A 245     -58.160  -5.788   9.380  1.00 15.00           C  
ANISOU 1894  CG2 VAL A 245     2619   2365    716      2     -2    -45       C  
ATOM   1895  N   GLY A 246     -58.088  -7.136   4.941  1.00 14.33           N  
ANISOU 1895  N   GLY A 246     2508   2327    609    -60    118      9       N  
ATOM   1896  CA  GLY A 246     -58.590  -7.704   3.700  1.00 14.73           C  
ANISOU 1896  CA  GLY A 246     2626   2270    699    -33    -73     52       C  
ATOM   1897  C   GLY A 246     -57.743  -8.870   3.240  1.00 14.13           C  
ANISOU 1897  C   GLY A 246     2543   2337    487    -76     -8     10       C  
ATOM   1898  O   GLY A 246     -58.276  -9.851   2.721  1.00 14.60           O  
ANISOU 1898  O   GLY A 246     2744   2386    414   -142    102    -48       O  
ATOM   1899  N   LEU A 247     -56.430  -8.769   3.439  1.00 14.35           N  
ANISOU 1899  N   LEU A 247     2469   2263    720    -25    127     61       N  
ATOM   1900  CA  LEU A 247     -55.538  -9.850   3.052  1.00 13.83           C  
ANISOU 1900  CA  LEU A 247     2382   2290    583   -161    150    -69       C  
ATOM   1901  C   LEU A 247     -55.826 -11.116   3.863  1.00 14.88           C  
ANISOU 1901  C   LEU A 247     2623   2284    744    -92    163     -3       C  
ATOM   1902  O   LEU A 247     -55.866 -12.221   3.311  1.00 14.61           O  
ANISOU 1902  O   LEU A 247     2614   2307    630   -167    187    -18       O  
ATOM   1903  CB  LEU A 247     -54.074  -9.428   3.188  1.00 14.92           C  
ANISOU 1903  CB  LEU A 247     2238   2598    830     41    194    -28       C  
ATOM   1904  CG  LEU A 247     -53.039 -10.498   2.823  1.00 14.76           C  
ANISOU 1904  CG  LEU A 247     2298   2420    889    -80    146   -180       C  
ATOM   1905  CD1 LEU A 247     -53.241 -11.067   1.416  1.00 14.86           C  
ANISOU 1905  CD1 LEU A 247     2295   2469    882    129    305   -256       C  
ATOM   1906  CD2 LEU A 247     -51.643  -9.907   2.975  1.00 15.63           C  
ANISOU 1906  CD2 LEU A 247     2234   2446   1256    -11      3    -83       C  
ATOM   1907  N   GLY A 248     -56.055 -10.954   5.163  1.00 14.86           N  
ANISOU 1907  N   GLY A 248     2614   2278    754   -181    152   -106       N  
ATOM   1908  CA  GLY A 248     -56.416 -12.103   5.991  1.00 15.06           C  
ANISOU 1908  CA  GLY A 248     2715   2452    552    -77    234      0       C  
ATOM   1909  C   GLY A 248     -57.687 -12.788   5.513  1.00 15.55           C  
ANISOU 1909  C   GLY A 248     2748   2475    682    -86    163    -31       C  
ATOM   1910  O   GLY A 248     -57.769 -14.022   5.488  1.00 16.69           O  
ANISOU 1910  O   GLY A 248     2947   2419    972     73    135    131       O  
ATOM   1911  N   VAL A 249     -58.682 -11.983   5.141  1.00 14.17           N  
ANISOU 1911  N   VAL A 249     2666   2420    298    -22    309   -115       N  
ATOM   1912  CA  VAL A 249     -59.981 -12.502   4.717  1.00 15.58           C  
ANISOU 1912  CA  VAL A 249     2584   2606    728    -29    347    -66       C  
ATOM   1913  C   VAL A 249     -59.836 -13.249   3.397  1.00 15.68           C  
ANISOU 1913  C   VAL A 249     2711   2579    666    -98    249    -26       C  
ATOM   1914  O   VAL A 249     -60.470 -14.286   3.192  1.00 16.34           O  
ANISOU 1914  O   VAL A 249     2990   2553    664   -148    400    -19       O  
ATOM   1915  CB  VAL A 249     -61.012 -11.361   4.608  1.00 15.45           C  
ANISOU 1915  CB  VAL A 249     2596   2513    759    -51    298   -200       C  
ATOM   1916  CG1 VAL A 249     -62.336 -11.840   4.029  1.00 16.10           C  
ANISOU 1916  CG1 VAL A 249     2625   2884    608   -119    274   -118       C  
ATOM   1917  CG2 VAL A 249     -61.242 -10.772   5.993  1.00 15.22           C  
ANISOU 1917  CG2 VAL A 249     2407   2686    688   -117    116   -233       C  
ATOM   1918  N   ALA A 250     -58.992 -12.715   2.516  1.00 14.64           N  
ANISOU 1918  N   ALA A 250     2512   2435    615   -110     79    -26       N  
ATOM   1919  CA  ALA A 250     -58.723 -13.346   1.224  1.00 15.24           C  
ANISOU 1919  CA  ALA A 250     2641   2425    724    -72    423     19       C  
ATOM   1920  C   ALA A 250     -58.126 -14.736   1.400  1.00 15.74           C  
ANISOU 1920  C   ALA A 250     2732   2472    773   -120    245     72       C  
ATOM   1921  O   ALA A 250     -58.552 -15.682   0.755  1.00 16.56           O  
ANISOU 1921  O   ALA A 250     3060   2473    756   -225    314     19       O  
ATOM   1922  CB  ALA A 250     -57.803 -12.475   0.370  1.00 14.79           C  
ANISOU 1922  CB  ALA A 250     2721   2296    601   -223    169      7       C  
ATOM   1923  N   VAL A 251     -57.145 -14.843   2.297  1.00 14.92           N  
ANISOU 1923  N   VAL A 251     2758   2547    363    -98    381     37       N  
ATOM   1924  CA  VAL A 251     -56.461 -16.105   2.567  1.00 17.11           C  
ANISOU 1924  CA  VAL A 251     2876   2565   1058   -145    106     68       C  
ATOM   1925  C   VAL A 251     -57.462 -17.094   3.165  1.00 17.39           C  
ANISOU 1925  C   VAL A 251     3127   2744    734   -105    425     86       C  
ATOM   1926  O   VAL A 251     -57.540 -18.257   2.742  1.00 18.05           O  
ANISOU 1926  O   VAL A 251     3172   2630   1054   -272    394    265       O  
ATOM   1927  CB  VAL A 251     -55.243 -15.879   3.491  1.00 17.02           C  
ANISOU 1927  CB  VAL A 251     2964   2628    873   -197    117     65       C  
ATOM   1928  CG1 VAL A 251     -54.655 -17.202   3.944  1.00 16.96           C  
ANISOU 1928  CG1 VAL A 251     3230   2583    631   -122    279      4       C  
ATOM   1929  CG2 VAL A 251     -54.176 -15.045   2.786  1.00 17.31           C  
ANISOU 1929  CG2 VAL A 251     3156   2866    552   -149    428     68       C  
ATOM   1930  N   GLU A 252     -58.254 -16.607   4.115  1.00 17.31           N  
ANISOU 1930  N   GLU A 252     3123   2712    742   -127    378     44       N  
ATOM   1931  CA  GLU A 252     -59.179 -17.476   4.807  1.00 19.85           C  
ANISOU 1931  CA  GLU A 252     3448   2949   1144   -222    837    -91       C  
ATOM   1932  C   GLU A 252     -60.229 -18.075   3.897  1.00 20.88           C  
ANISOU 1932  C   GLU A 252     3498   3016   1416   -206    580    153       C  
ATOM   1933  O   GLU A 252     -60.596 -19.231   4.076  1.00 23.49           O  
ANISOU 1933  O   GLU A 252     3956   3140   1828   -319    838    453       O  
ATOM   1934  CB  GLU A 252     -59.860 -16.793   6.000  1.00 22.91           C  
ANISOU 1934  CB  GLU A 252     3727   3589   1389   -166   1206   -145       C  
ATOM   1935  CG  GLU A 252     -60.357 -17.812   7.028  1.00 28.48           C  
ANISOU 1935  CG  GLU A 252     4881   4078   1859   -148   1142    396       C  
ATOM   1936  CD  GLU A 252     -60.448 -17.239   8.417  1.00 32.33           C  
ANISOU 1936  CD  GLU A 252     5192   4879   2210    442    731   -208       C  
ATOM   1937  OE1 GLU A 252     -60.942 -16.112   8.533  1.00 34.66           O  
ANISOU 1937  OE1 GLU A 252     4744   5443   2981    857   1342   -453       O  
ATOM   1938  OE2 GLU A 252     -60.018 -17.907   9.378  1.00 39.45           O  
ANISOU 1938  OE2 GLU A 252     5606   5796   3584     76    152    855       O  
ATOM   1939  N   HIS A 253     -60.722 -17.287   2.946  1.00 19.57           N  
ANISOU 1939  N   HIS A 253     3335   3065   1034   -349    760    168       N  
ATOM   1940  CA  HIS A 253     -61.802 -17.725   2.061  1.00 21.14           C  
ANISOU 1940  CA  HIS A 253     3588   3169   1274   -273    639   -148       C  
ATOM   1941  C   HIS A 253     -61.362 -18.029   0.644  1.00 20.69           C  
ANISOU 1941  C   HIS A 253     3516   3161   1185   -257    644     81       C  
ATOM   1942  O   HIS A 253     -62.166 -17.927  -0.295  1.00 24.03           O  
ANISOU 1942  O   HIS A 253     3714   3601   1813   -228    227   -199       O  
ATOM   1943  CB  HIS A 253     -62.936 -16.694   2.072  1.00 23.86           C  
ANISOU 1943  CB  HIS A 253     3589   3553   1922    -95    484    -94       C  
ATOM   1944  CG  HIS A 253     -63.515 -16.440   3.444  1.00 25.20           C  
ANISOU 1944  CG  HIS A 253     3812   3549   2211   -411    851   -330       C  
ATOM   1945  ND1 HIS A 253     -64.387 -17.284   4.024  1.00 29.25           N  
ANISOU 1945  ND1 HIS A 253     4209   4234   2669   -972   1069   -467       N  
ATOM   1946  CD2 HIS A 253     -63.318 -15.394   4.346  1.00 24.52           C  
ANISOU 1946  CD2 HIS A 253     3611   3433   2270   -553    727   -282       C  
ATOM   1947  CE1 HIS A 253     -64.738 -16.806   5.237  1.00 30.37           C  
ANISOU 1947  CE1 HIS A 253     4089   4420   3026   -851   1548   -549       C  
ATOM   1948  NE2 HIS A 253     -64.085 -15.647   5.432  1.00 31.39           N  
ANISOU 1948  NE2 HIS A 253     4337   4397   3190  -1045   1392      2       N  
ATOM   1949  N   PHE A 254     -60.101 -18.440   0.475  1.00 19.49           N  
ANISOU 1949  N   PHE A 254     3435   2776   1192   -394    471    -68       N  
ATOM   1950  CA  PHE A 254     -59.522 -18.683  -0.855  1.00 18.57           C  
ANISOU 1950  CA  PHE A 254     3065   2794   1196   -400    408      7       C  
ATOM   1951  C   PHE A 254     -60.258 -19.839  -1.515  1.00 19.72           C  
ANISOU 1951  C   PHE A 254     3408   2759   1326   -428    286    -18       C  
ATOM   1952  O   PHE A 254     -60.550 -20.818  -0.877  1.00 20.72           O  
ANISOU 1952  O   PHE A 254     3645   2638   1588   -332    297      1       O  
ATOM   1953  CB  PHE A 254     -58.026 -18.999  -0.752  1.00 18.72           C  
ANISOU 1953  CB  PHE A 254     3108   2897   1108   -349    358     14       C  
ATOM   1954  CG  PHE A 254     -57.317 -19.039  -2.075  1.00 17.43           C  
ANISOU 1954  CG  PHE A 254     3092   2646    885   -515    122    -27       C  
ATOM   1955  CD1 PHE A 254     -56.962 -20.247  -2.625  1.00 17.89           C  
ANISOU 1955  CD1 PHE A 254     3245   2630    920   -320    -48    101       C  
ATOM   1956  CD2 PHE A 254     -56.997 -17.871  -2.751  1.00 16.47           C  
ANISOU 1956  CD2 PHE A 254     2985   2594    678   -382   -140     23       C  
ATOM   1957  CE1 PHE A 254     -56.314 -20.306  -3.834  1.00 18.16           C  
ANISOU 1957  CE1 PHE A 254     3316   2535   1049   -436     62     31       C  
ATOM   1958  CE2 PHE A 254     -56.345 -17.920  -3.969  1.00 17.52           C  
ANISOU 1958  CE2 PHE A 254     3108   2643    904   -421     26   -187       C  
ATOM   1959  CZ  PHE A 254     -56.010 -19.143  -4.516  1.00 17.98           C  
ANISOU 1959  CZ  PHE A 254     3343   2502    984   -347     -2     16       C  
ATOM   1960  N   PRO A 255     -60.594 -19.720  -2.791  1.00 20.07           N  
ANISOU 1960  N   PRO A 255     3342   2851   1432   -563    144    177       N  
ATOM   1961  CA  PRO A 255     -61.487 -20.684  -3.394  1.00 21.21           C  
ANISOU 1961  CA  PRO A 255     3745   2737   1576   -697    248     77       C  
ATOM   1962  C   PRO A 255     -60.923 -22.080  -3.393  1.00 22.24           C  
ANISOU 1962  C   PRO A 255     3879   2905   1666   -638    137    365       C  
ATOM   1963  O   PRO A 255     -59.738 -22.289  -3.621  1.00 21.90           O  
ANISOU 1963  O   PRO A 255     3879   2906   1534   -550    -22    165       O  
ATOM   1964  CB  PRO A 255     -61.608 -20.199  -4.828  1.00 21.51           C  
ANISOU 1964  CB  PRO A 255     3563   2875   1734   -560     11    293       C  
ATOM   1965  CG  PRO A 255     -61.365 -18.748  -4.744  1.00 19.29           C  
ANISOU 1965  CG  PRO A 255     3479   2811   1036   -427      1     22       C  
ATOM   1966  CD  PRO A 255     -60.325 -18.591  -3.675  1.00 19.28           C  
ANISOU 1966  CD  PRO A 255     3326   2848   1152   -461    -20    183       C  
ATOM   1967  N   SER A 256     -61.820 -23.018  -3.133  1.00 24.19           N  
ANISOU 1967  N   SER A 256     4183   2974   2032   -816    217    360       N  
ATOM   1968  CA  SER A 256     -61.461 -24.395  -2.976  1.00 25.91           C  
ANISOU 1968  CA  SER A 256     4616   3075   2153   -803    146    449       C  
ATOM   1969  C   SER A 256     -61.695 -25.183  -4.237  1.00 27.81           C  
ANISOU 1969  C   SER A 256     4968   3295   2303   -902    -33    428       C  
ATOM   1970  O   SER A 256     -61.263 -26.269  -4.317  1.00 30.92           O  
ANISOU 1970  O   SER A 256     5024   3649   3073   -517   -198    418       O  
ATOM   1971  CB  SER A 256     -62.285 -25.012  -1.840  1.00 26.89           C  
ANISOU 1971  CB  SER A 256     4751   3197   2267   -801    114    706       C  
ATOM   1972  OG  SER A 256     -63.675 -25.042  -2.156  1.00 35.32           O  
ANISOU 1972  OG  SER A 256     4987   4372   4059  -1512   -174    850       O  
ATOM   1973  N   GLU A 257     -62.396 -24.664  -5.217  1.00 27.57           N  
ANISOU 1973  N   GLU A 257     4605   3585   2285   -864    -40    258       N  
ATOM   1974  CA  GLU A 257     -62.743 -25.531  -6.380  1.00 28.46           C  
ANISOU 1974  CA  GLU A 257     5033   3680   2098   -904    -57    370       C  
ATOM   1975  C   GLU A 257     -62.506 -24.834  -7.681  1.00 27.03           C  
ANISOU 1975  C   GLU A 257     4616   3699   1956   -965    -35    133       C  
ATOM   1976  O   GLU A 257     -62.519 -23.644  -7.648  1.00 26.90           O  
ANISOU 1976  O   GLU A 257     4245   3721   2252   -886    -41    338       O  
ATOM   1977  CB  GLU A 257     -64.217 -25.849  -6.320  1.00 31.35           C  
ANISOU 1977  CB  GLU A 257     5093   4169   2647  -1138   -245    722       C  
ATOM   1978  CG  GLU A 257     -64.574 -26.781  -5.187  1.00 34.80           C  
ANISOU 1978  CG  GLU A 257     5916   4725   2581  -1574      8    738       C  
ATOM   1979  CD  GLU A 257     -66.069 -26.952  -4.994  1.00 44.65           C  
ANISOU 1979  CD  GLU A 257     5844   6261   4858  -1347   -500    544       C  
ATOM   1980  OE1 GLU A 257     -66.816 -26.860  -5.995  1.00 46.02           O  
ANISOU 1980  OE1 GLU A 257     6698   6723   4062  -1571   -395   -240       O  
ATOM   1981  OE2 GLU A 257     -66.501 -27.198  -3.841  1.00 51.85           O  
ANISOU 1981  OE2 GLU A 257     7756   6840   5103   -871    157    489       O  
ATOM   1982  N   ALA A 258     -62.286 -25.498  -8.816  1.00 26.52           N  
ANISOU 1982  N   ALA A 258     4372   3651   2052   -942    -63     73       N  
ATOM   1983  CA  ALA A 258     -61.968 -24.696  -9.976  1.00 27.28           C  
ANISOU 1983  CA  ALA A 258     4417   3736   2210   -930     -4    107       C  
ATOM   1984  C   ALA A 258     -63.145 -23.895 -10.476  1.00 27.62           C  
ANISOU 1984  C   ALA A 258     4585   4233   1676   -859     59    273       C  
ATOM   1985  O   ALA A 258     -64.278 -24.164 -10.137  1.00 28.79           O  
ANISOU 1985  O   ALA A 258     4379   4096   2462  -1017   -526     11       O  
ATOM   1986  CB  ALA A 258     -61.493 -25.570 -11.104  1.00 28.12           C  
ANISOU 1986  CB  ALA A 258     4587   3831   2264   -804     31    142       C  
ATOM   1987  N   SER A 259     -62.912 -22.872 -11.293  1.00 28.82           N  
ANISOU 1987  N   SER A 259     4649   4037   2264  -1065     83    298       N  
ATOM   1988  CA  SER A 259     -62.118 -21.607 -11.153  1.00 28.27           C  
ANISOU 1988  CA  SER A 259     4183   4282   2275   -874    -43     54       C  
ATOM   1989  C   SER A 259     -63.280 -20.979 -11.736  1.00 31.69           C  
ANISOU 1989  C   SER A 259     4711   5154   2175   -589   -275    409       C  
ATOM   1990  O   SER A 259     -63.252 -20.452 -12.792  1.00 27.44           O  
ANISOU 1990  O   SER A 259     4101   3908   2418   -957   -786    483       O  
ATOM   1991  CB  SER A 259     -61.034 -21.361 -12.171  1.00 24.05           C  
ANISOU 1991  CB  SER A 259     4232   3411   1493   -853   -197    135       C  
ATOM   1992  OG  SER A 259     -59.977 -22.249 -11.944  1.00 31.07           O  
ANISOU 1992  OG  SER A 259     4282   4627   2894   -652     83    171       O  
ATOM   1993  N   ALA A 260     -64.302 -21.095 -10.926  1.00 35.40           N  
ANISOU 1993  N   ALA A 260     4136   5702   3613  -1069   -105    149       N  
ATOM   1994  CA  ALA A 260     -65.575 -21.689 -11.232  1.00 35.13           C  
ANISOU 1994  CA  ALA A 260     5309   4417   3618  -1408   -696   -399       C  
ATOM   1995  C   ALA A 260     -65.674 -22.302 -12.592  1.00 31.92           C  
ANISOU 1995  C   ALA A 260     4842   4631   2656  -1238   -417    412       C  
ATOM   1996  O   ALA A 260     -64.795 -22.989 -13.157  1.00 29.55           O  
ANISOU 1996  O   ALA A 260     4264   4426   2535  -1567   -689    505       O  
ATOM   1997  CB  ALA A 260     -66.717 -20.696 -11.019  1.00 35.42           C  
ANISOU 1997  CB  ALA A 260     4862   5094   3499  -1202   -626     -7       C  
ATOM   1998  N   GLN A 261     -66.820 -21.926 -13.112  1.00 31.99           N  
ANISOU 1998  N   GLN A 261     4841   4764   2547   -983   -207    406       N  
ATOM   1999  CA  GLN A 261     -67.312 -22.295 -14.369  1.00 31.36           C  
ANISOU 1999  CA  GLN A 261     4607   4449   2857  -1476   -471    241       C  
ATOM   2000  C   GLN A 261     -66.369 -21.741 -15.411  1.00 30.83           C  
ANISOU 2000  C   GLN A 261     4784   4291   2640  -1241   -346    143       C  
ATOM   2001  O   GLN A 261     -66.234 -22.325 -16.469  1.00 30.77           O  
ANISOU 2001  O   GLN A 261     4587   4301   2803  -1466   -577   -117       O  
ATOM   2002  CB  GLN A 261     -68.687 -21.682 -14.520  1.00 34.63           C  
ANISOU 2002  CB  GLN A 261     5032   4754   3369   -862    -47     74       C  
ATOM   2003  N   GLN A 262     -65.695 -20.635 -15.140  1.00 27.59           N  
ANISOU 2003  N   GLN A 262     4166   4086   2231  -1048   -449    376       N  
ATOM   2004  CA  GLN A 262     -64.901 -20.031 -16.204  1.00 27.46           C  
ANISOU 2004  CA  GLN A 262     4152   4031   2251  -1000   -373    240       C  
ATOM   2005  C   GLN A 262     -63.872 -21.008 -16.728  1.00 29.36           C  
ANISOU 2005  C   GLN A 262     4468   4218   2468   -909   -239    283       C  
ATOM   2006  O   GLN A 262     -63.651 -21.075 -17.944  1.00 28.30           O  
ANISOU 2006  O   GLN A 262     4402   4133   2218   -957   -912    155       O  
ATOM   2007  CB  GLN A 262     -64.211 -18.722 -15.819  1.00 25.49           C  
ANISOU 2007  CB  GLN A 262     3893   3809   1983   -899     -1    318       C  
ATOM   2008  CG  GLN A 262     -63.513 -18.035 -17.015  1.00 22.95           C  
ANISOU 2008  CG  GLN A 262     3976   3562   1181   -975   -363    -66       C  
ATOM   2009  CD  GLN A 262     -62.925 -16.705 -16.653  1.00 22.87           C  
ANISOU 2009  CD  GLN A 262     3806   3495   1388   -879    192   -218       C  
ATOM   2010  OE1 GLN A 262     -63.172 -16.183 -15.574  1.00 23.68           O  
ANISOU 2010  OE1 GLN A 262     3867   3553   1575   -654    127   -460       O  
ATOM   2011  NE2 GLN A 262     -62.156 -16.141 -17.556  1.00 21.64           N  
ANISOU 2011  NE2 GLN A 262     3604   3354   1265   -820     74   -188       N  
ATOM   2012  N   THR A 263     -63.291 -21.813 -15.860  1.00 28.41           N  
ANISOU 2012  N   THR A 263     4406   4312   2074  -1153   -400    204       N  
ATOM   2013  CA  THR A 263     -62.133 -22.552 -16.271  1.00 30.55           C  
ANISOU 2013  CA  THR A 263     4634   4414   2559   -857   -728    140       C  
ATOM   2014  C   THR A 263     -62.570 -23.624 -17.286  1.00 34.55           C  
ANISOU 2014  C   THR A 263     5159   4687   3280   -803   -922   -229       C  
ATOM   2015  O   THR A 263     -61.856 -24.459 -17.750  1.00 32.76           O  
ANISOU 2015  O   THR A 263     5182   4058   3207  -1120   -819    -59       O  
ATOM   2016  CB  THR A 263     -61.304 -22.962 -15.040  1.00 29.76           C  
ANISOU 2016  CB  THR A 263     4733   4447   2126   -655   -367    121       C  
ATOM   2017  OG1 THR A 263     -60.562 -24.145 -15.309  1.00 36.34           O  
ANISOU 2017  OG1 THR A 263     5690   4588   3527   -536    176   -248       O  
ATOM   2018  CG2 THR A 263     -62.201 -23.182 -13.829  1.00 33.29           C  
ANISOU 2018  CG2 THR A 263     4959   4905   2784   -799    -17    193       C  
ATOM   2019  N   GLU A 264     -63.779 -23.464 -17.771  1.00 38.07           N  
ANISOU 2019  N   GLU A 264     5006   5399   4058  -1284   -851   -464       N  
ATOM   2020  CA  GLU A 264     -64.219 -24.229 -18.958  1.00 36.35           C  
ANISOU 2020  CA  GLU A 264     5371   5110   3331  -1167   -814     60       C  
ATOM   2021  C   GLU A 264     -64.725 -23.301 -20.088  1.00 37.35           C  
ANISOU 2021  C   GLU A 264     4973   5239   3979   -940   -836    342       C  
ATOM   2022  O   GLU A 264     -65.930 -23.199 -20.267  1.00 39.46           O  
ANISOU 2022  O   GLU A 264     4862   5588   4542  -2380  -1672   -563       O  
ATOM   2023  CB  GLU A 264     -65.277 -25.178 -18.519  1.00 35.98           C  
ANISOU 2023  CB  GLU A 264     4566   5339   3765  -1366  -1432    -18       C  
ATOM   2024  CG  GLU A 264     -65.353 -24.957 -17.022  1.00 39.32           C  
ANISOU 2024  CG  GLU A 264     5684   5190   4066  -1217   -428    -67       C  
ATOM   2025  CD  GLU A 264     -65.751 -26.084 -16.200  1.00 40.66           C  
ANISOU 2025  CD  GLU A 264     5569   5330   4547  -1270   -441    169       C  
ATOM   2026  OE1 GLU A 264     -65.060 -26.422 -15.220  1.00 40.12           O  
ANISOU 2026  OE1 GLU A 264     5012   5277   4954  -1978   -730    123       O  
ATOM   2027  OE2 GLU A 264     -66.828 -26.461 -16.535  1.00 48.89           O  
ANISOU 2027  OE2 GLU A 264     5832   6595   6145  -1666   -735     74       O  
ATOM   2028  N   PHE A 265     -63.875 -22.538 -20.793  1.00 36.08           N  
ANISOU 2028  N   PHE A 265     5068   4936   3705   -807   -340     24       N  
ATOM   2029  CA  PHE A 265     -62.403 -22.573 -21.043  1.00 30.40           C  
ANISOU 2029  CA  PHE A 265     4757   4218   2573  -1244  -1108   -375       C  
ATOM   2030  C   PHE A 265     -61.736 -23.811 -21.548  1.00 31.51           C  
ANISOU 2030  C   PHE A 265     4775   4468   2730  -1391   -314   -134       C  
ATOM   2031  O   PHE A 265     -61.142 -23.807 -22.645  1.00 31.88           O  
ANISOU 2031  O   PHE A 265     5016   4704   2389  -1227   -555   -290       O  
ATOM   2032  CB  PHE A 265     -61.431 -21.826 -20.105  1.00 27.63           C  
ANISOU 2032  CB  PHE A 265     4269   3728   2500  -1177   -773   -249       C  
ATOM   2033  CG  PHE A 265     -59.995 -21.898 -20.596  1.00 27.19           C  
ANISOU 2033  CG  PHE A 265     4490   3565   2276  -1090   -582      2       C  
ATOM   2034  CD1 PHE A 265     -59.546 -21.077 -21.627  1.00 26.42           C  
ANISOU 2034  CD1 PHE A 265     4304   3850   1881   -861   -403   -135       C  
ATOM   2035  CD2 PHE A 265     -59.122 -22.837 -20.081  1.00 27.48           C  
ANISOU 2035  CD2 PHE A 265     4292   3711   2436  -1114   -641   -235       C  
ATOM   2036  CE1 PHE A 265     -58.250 -21.168 -22.101  1.00 24.35           C  
ANISOU 2036  CE1 PHE A 265     4216   3650   1385   -792   -779   -343       C  
ATOM   2037  CE2 PHE A 265     -57.813 -22.934 -20.550  1.00 25.90           C  
ANISOU 2037  CE2 PHE A 265     4552   3515   1771   -802   -336    -54       C  
ATOM   2038  CZ  PHE A 265     -57.374 -22.092 -21.565  1.00 25.44           C  
ANISOU 2038  CZ  PHE A 265     4534   3304   1828   -777   -428    -60       C  
ATOM   2039  N   GLU A 266     -61.786 -24.846 -20.743  1.00 32.76           N  
ANISOU 2039  N   GLU A 266     5037   4537   2870  -1798   -606    -69       N  
ATOM   2040  CA  GLU A 266     -61.154 -26.065 -21.121  1.00 24.39           C  
ANISOU 2040  CA  GLU A 266     3898   4487    879  -2595   -792   -403       C  
ATOM   2041  C   GLU A 266     -61.845 -26.694 -22.335  1.00 25.18           C  
ANISOU 2041  C   GLU A 266     4163   4210   1194  -3065   -413   -527       C  
ATOM   2042  O   GLU A 266     -61.209 -27.418 -23.072  1.00 37.52           O  
ANISOU 2042  O   GLU A 266     5899   5138   3218  -1600    115   -992       O  
ATOM   2043  CB  GLU A 266     -61.114 -27.011 -19.930  1.00 30.81           C  
ANISOU 2043  CB  GLU A 266     5590   4528   1586  -1705   -920    -86       C  
ATOM   2044  CG  GLU A 266     -60.003 -26.693 -18.920  1.00 31.85           C  
ANISOU 2044  CG  GLU A 266     4895   4845   2360  -1548   -770   -611       C  
ATOM   2045  CD  GLU A 266     -60.112 -27.424 -17.594  1.00 37.39           C  
ANISOU 2045  CD  GLU A 266     5930   5191   3083  -1013  -1286    178       C  
ATOM   2046  OE1 GLU A 266     -61.165 -28.031 -17.317  1.00 45.36           O  
ANISOU 2046  OE1 GLU A 266     6626   5999   4608  -1638   -961     36       O  
ATOM   2047  OE2 GLU A 266     -59.152 -27.321 -16.800  1.00 37.27           O  
ANISOU 2047  OE2 GLU A 266     5766   5395   3000    -67  -1293    810       O  
ATOM   2048  N   LYS A 267     -63.124 -26.386 -22.560  1.00 28.37           N  
ANISOU 2048  N   LYS A 267     3771   6385    621  -3718   -332   -302       N  
ATOM   2049  CA  LYS A 267     -63.857 -26.882 -23.731  1.00 29.28           C  
ANISOU 2049  CA  LYS A 267     4684   5963    475  -4358    278   -584       C  
ATOM   2050  C   LYS A 267     -63.751 -25.934 -24.945  1.00 32.50           C  
ANISOU 2050  C   LYS A 267     5310   5051   1986  -2284   -264    141       C  
ATOM   2051  O   LYS A 267     -64.166 -26.245 -26.078  1.00 43.33           O  
ANISOU 2051  O   LYS A 267     7551   6380   2529  -1498   -822   -925       O  
ATOM   2052  CB  LYS A 267     -65.323 -27.061 -23.349  0.50 27.71           C  
ANISOU 2052  CB  LYS A 267     4075   4763   1689  -3159   -120   -347       C  
ATOM   2053  CG  LYS A 267     -65.589 -28.177 -22.353  0.20 24.70           C  
ANISOU 2053  CG  LYS A 267     3586   4287   1512  -2962   -464   -559       C  
ATOM   2054  CD  LYS A 267     -67.020 -28.133 -21.838  0.20 24.53           C  
ANISOU 2054  CD  LYS A 267     3612   3994   1714  -2573   -405   -345       C  
ATOM   2055  CE  LYS A 267     -67.258 -29.195 -20.777  0.10 23.48           C  
ANISOU 2055  CE  LYS A 267     3105   3798   2018  -2563   -341   -308       C  
ATOM   2056  NZ  LYS A 267     -68.594 -29.049 -20.138  0.10 23.00           N  
ANISOU 2056  NZ  LYS A 267     3032   3767   1938  -2508   -445   -445       N  
ATOM   2057  N   ILE A 268     -63.299 -24.709 -24.708  1.00 34.49           N  
ANISOU 2057  N   ILE A 268     5027   5191   2887  -2113   -321   -426       N  
ATOM   2058  CA  ILE A 268     -63.081 -23.755 -25.808  1.00 33.57           C  
ANISOU 2058  CA  ILE A 268     5472   5360   1920  -1317   -594   -621       C  
ATOM   2059  C   ILE A 268     -61.713 -23.952 -26.486  1.00 33.80           C  
ANISOU 2059  C   ILE A 268     5376   5230   2234  -1053   -828   -726       C  
ATOM   2060  O   ILE A 268     -61.626 -24.065 -27.708  1.00 35.39           O  
ANISOU 2060  O   ILE A 268     5984   5234   2228  -1006   -615   -581       O  
ATOM   2061  CB  ILE A 268     -63.333 -22.286 -25.377  1.00 35.59           C  
ANISOU 2061  CB  ILE A 268     5667   5183   2673  -1074   -315   -442       C  
ATOM   2062  CG1 ILE A 268     -64.842 -22.039 -25.265  1.00 37.71           C  
ANISOU 2062  CG1 ILE A 268     5726   5440   3162  -1180    -79   -555       C  
ATOM   2063  CG2 ILE A 268     -62.830 -21.385 -26.447  1.00 31.17           C  
ANISOU 2063  CG2 ILE A 268     5259   4635   1947   -640   -334   -888       C  
ATOM   2064  CD1 ILE A 268     -65.232 -20.738 -24.613  1.00 39.93           C  
ANISOU 2064  CD1 ILE A 268     6124   5259   3789   -654    377   -120       C  
ATOM   2065  N   ILE A 269     -60.676 -24.051 -25.661  1.00 33.30           N  
ANISOU 2065  N   ILE A 269     5359   5256   2038   -895   -735   -609       N  
ATOM   2066  CA  ILE A 269     -59.298 -23.886 -26.080  1.00 30.97           C  
ANISOU 2066  CA  ILE A 269     5145   4821   1800   -840   -995   -582       C  
ATOM   2067  C   ILE A 269     -58.889 -24.942 -27.118  1.00 32.70           C  
ANISOU 2067  C   ILE A 269     5354   4880   2189  -1001   -708   -725       C  
ATOM   2068  O   ILE A 269     -58.041 -24.700 -27.963  1.00 32.19           O  
ANISOU 2068  O   ILE A 269     5574   4719   1936   -903   -593   -825       O  
ATOM   2069  CB  ILE A 269     -58.358 -23.827 -24.844  1.00 30.36           C  
ANISOU 2069  CB  ILE A 269     4952   4558   2023   -929  -1034   -389       C  
ATOM   2070  CG1 ILE A 269     -57.006 -23.242 -25.226  1.00 30.43           C  
ANISOU 2070  CG1 ILE A 269     4796   4400   2363   -607   -691   -611       C  
ATOM   2071  CG2 ILE A 269     -58.221 -25.167 -24.143  1.00 32.26           C  
ANISOU 2071  CG2 ILE A 269     5299   4493   2465   -822   -870   -347       C  
ATOM   2072  CD1 ILE A 269     -57.156 -21.874 -25.845  1.00 28.92           C  
ANISOU 2072  CD1 ILE A 269     4670   4460   1857   -884   -651   -586       C  
ATOM   2073  N   ASN A 270     -59.519 -26.111 -27.026  1.00 35.33           N  
ANISOU 2073  N   ASN A 270     5635   4869   2918  -1051   -952   -792       N  
ATOM   2074  CA  ASN A 270     -59.242 -27.244 -27.903  1.00 37.29           C  
ANISOU 2074  CA  ASN A 270     6080   4812   3275   -731   -224   -580       C  
ATOM   2075  C   ASN A 270     -59.830 -27.120 -29.308  1.00 37.94           C  
ANISOU 2075  C   ASN A 270     5908   5235   3269   -922   -370   -678       C  
ATOM   2076  O   ASN A 270     -59.464 -27.883 -30.211  1.00 41.31           O  
ANISOU 2076  O   ASN A 270     6429   5154   4112  -1383   -232  -1226       O  
ATOM   2077  CB  ASN A 270     -59.660 -28.558 -27.226  1.00 40.81           C  
ANISOU 2077  CB  ASN A 270     5982   5576   3945   -771   -159    174       C  
ATOM   2078  CG  ASN A 270     -58.610 -29.063 -26.258  1.00 42.71           C  
ANISOU 2078  CG  ASN A 270     6327   5680   4221   -795     68   1109       C  
ATOM   2079  OD1 ASN A 270     -57.502 -28.524 -26.205  1.00 44.11           O  
ANISOU 2079  OD1 ASN A 270     6306   5926   4525   -802   -234   -103       O  
ATOM   2080  ND2 ASN A 270     -58.949 -30.087 -25.483  1.00 50.17           N  
ANISOU 2080  ND2 ASN A 270     7409   6505   5147     99    -90   2501       N  
ATOM   2081  N   GLU A 271     -60.723 -26.149 -29.503  1.00 37.60           N  
ANISOU 2081  N   GLU A 271     6109   5151   3026   -881   -460   -686       N  
ATOM   2082  CA  GLU A 271     -61.153 -25.786 -30.850  1.00 34.15           C  
ANISOU 2082  CA  GLU A 271     5608   5221   2145  -1372    -99  -1260       C  
ATOM   2083  C   GLU A 271     -60.022 -25.082 -31.617  1.00 33.86           C  
ANISOU 2083  C   GLU A 271     5449   4956   2459  -1259   -572   -352       C  
ATOM   2084  O   GLU A 271     -60.178 -24.697 -32.792  1.00 33.67           O  
ANISOU 2084  O   GLU A 271     5445   5456   1891  -1567   -522   -942       O  
ATOM   2085  CB  GLU A 271     -62.364 -24.883 -30.799  1.00 35.55           C  
ANISOU 2085  CB  GLU A 271     6144   4966   2394  -1084   -460  -1497       C  
ATOM   2086  CG  GLU A 271     -63.700 -25.535 -30.495  1.00 42.01           C  
ANISOU 2086  CG  GLU A 271     6550   5496   3914  -1215   -101   -876       C  
ATOM   2087  CD  GLU A 271     -64.742 -24.490 -30.100  1.00 42.41           C  
ANISOU 2087  CD  GLU A 271     7491   6539   2080   -544   -410  -1553       C  
ATOM   2088  OE1 GLU A 271     -65.460 -24.690 -29.082  1.00 48.72           O  
ANISOU 2088  OE1 GLU A 271     7618   6995   3895   -948    413   -789       O  
ATOM   2089  OE2 GLU A 271     -64.824 -23.387 -30.761  1.00 51.37           O  
ANISOU 2089  OE2 GLU A 271     7848   6498   5172    220   -487   -883       O  
ATOM   2090  N   TYR A 272     -58.882 -24.912 -30.938  1.00 31.52           N  
ANISOU 2090  N   TYR A 272     5419   4632   1923  -1144   -346   -880       N  
ATOM   2091  CA  TYR A 272     -57.746 -24.233 -31.549  1.00 30.72           C  
ANISOU 2091  CA  TYR A 272     5364   4052   2255  -1050   -341   -849       C  
ATOM   2092  C   TYR A 272     -56.494 -25.114 -31.564  1.00 30.31           C  
ANISOU 2092  C   TYR A 272     5373   4273   1870   -933   -430   -487       C  
ATOM   2093  O   TYR A 272     -56.359 -26.023 -30.774  1.00 31.06           O  
ANISOU 2093  O   TYR A 272     5444   4299   2057   -995   -723   -455       O  
ATOM   2094  CB  TYR A 272     -57.493 -22.885 -30.856  1.00 27.82           C  
ANISOU 2094  CB  TYR A 272     4995   3950   1622  -1127   -539   -596       C  
ATOM   2095  CG  TYR A 272     -58.695 -21.958 -30.905  1.00 30.01           C  
ANISOU 2095  CG  TYR A 272     5202   3990   2210  -1008   -316   -725       C  
ATOM   2096  CD1 TYR A 272     -58.933 -21.154 -32.011  1.00 30.01           C  
ANISOU 2096  CD1 TYR A 272     5471   3976   1954  -1010   -516   -881       C  
ATOM   2097  CD2 TYR A 272     -59.604 -21.900 -29.844  1.00 28.22           C  
ANISOU 2097  CD2 TYR A 272     5392   3976   1352  -1104   -609   -801       C  
ATOM   2098  CE1 TYR A 272     -60.041 -20.315 -32.065  1.00 33.63           C  
ANISOU 2098  CE1 TYR A 272     5445   4955   2376   -693   -584   -841       C  
ATOM   2099  CE2 TYR A 272     -60.720 -21.060 -29.895  1.00 32.40           C  
ANISOU 2099  CE2 TYR A 272     5660   4193   2458   -753   -330   -497       C  
ATOM   2100  CZ  TYR A 272     -60.928 -20.267 -30.999  1.00 31.46           C  
ANISOU 2100  CZ  TYR A 272     5602   4427   1923   -604   -695   -819       C  
ATOM   2101  OH  TYR A 272     -62.012 -19.426 -31.043  1.00 34.84           O  
ANISOU 2101  OH  TYR A 272     5367   4903   2968   -524   -495  -1130       O  
ATOM   2102  N   SER A 273     -55.571 -24.828 -32.471  1.00 30.08           N  
ANISOU 2102  N   SER A 273     5200   4114   2114   -791   -291   -675       N  
ATOM   2103  CA ASER A 273     -54.333 -25.589 -32.599  0.50 29.09           C  
ANISOU 2103  CA ASER A 273     5337   3944   1771   -734   -444   -467       C  
ATOM   2104  CA BSER A 273     -54.361 -25.589 -32.617  0.50 28.80           C  
ANISOU 2104  CA BSER A 273     5329   3921   1691   -746   -381   -481       C  
ATOM   2105  C   SER A 273     -53.168 -24.884 -31.975  1.00 27.95           C  
ANISOU 2105  C   SER A 273     5334   3760   1526   -645   -403   -430       C  
ATOM   2106  O   SER A 273     -52.777 -23.801 -32.362  1.00 26.33           O  
ANISOU 2106  O   SER A 273     5097   3513   1391   -558   -292   -545       O  
ATOM   2107  CB ASER A 273     -53.959 -25.858 -34.038  0.50 30.06           C  
ANISOU 2107  CB ASER A 273     5425   4118   1878   -873   -332   -671       C  
ATOM   2108  CB BSER A 273     -54.116 -25.822 -34.089  0.50 29.63           C  
ANISOU 2108  CB BSER A 273     5354   4094   1810   -823   -166   -663       C  
ATOM   2109  OG ASER A 273     -54.960 -26.555 -34.633  0.50 32.44           O  
ANISOU 2109  OG ASER A 273     5548   4532   2246   -818   -734   -713       O  
ATOM   2110  OG BSER A 273     -52.875 -26.427 -34.279  0.50 29.38           O  
ANISOU 2110  OG BSER A 273     5449   4174   1541   -692    -73   -857       O  
ATOM   2111  N   PHE A 274     -52.644 -25.524 -30.958  1.00 28.11           N  
ANISOU 2111  N   PHE A 274     5389   3728   1564   -441   -326   -471       N  
ATOM   2112  CA  PHE A 274     -51.611 -24.910 -30.132  1.00 25.90           C  
ANISOU 2112  CA  PHE A 274     5244   3327   1269   -108   -276   -608       C  
ATOM   2113  C   PHE A 274     -50.689 -25.923 -29.436  1.00 26.29           C  
ANISOU 2113  C   PHE A 274     5377   3111   1500   -151   -313   -663       C  
ATOM   2114  O   PHE A 274     -51.009 -27.110 -29.337  1.00 27.63           O  
ANISOU 2114  O   PHE A 274     5844   3092   1560   -227   -248   -644       O  
ATOM   2115  CB  PHE A 274     -52.265 -24.001 -29.070  1.00 25.91           C  
ANISOU 2115  CB  PHE A 274     5148   3475   1219   -238    -46   -586       C  
ATOM   2116  CG  PHE A 274     -53.101 -24.747 -28.042  1.00 27.21           C  
ANISOU 2116  CG  PHE A 274     5221   3679   1436   -287   -115   -336       C  
ATOM   2117  CD1 PHE A 274     -52.539 -25.199 -26.845  1.00 25.50           C  
ANISOU 2117  CD1 PHE A 274     4892   3270   1524   -202   -149   -466       C  
ATOM   2118  CD2 PHE A 274     -54.457 -25.002 -28.282  1.00 28.88           C  
ANISOU 2118  CD2 PHE A 274     5281   3801   1890   -614   -133   -610       C  
ATOM   2119  CE1 PHE A 274     -53.313 -25.870 -25.909  1.00 26.04           C  
ANISOU 2119  CE1 PHE A 274     4728   3364   1802   -326   -271   -164       C  
ATOM   2120  CE2 PHE A 274     -55.233 -25.673 -27.350  1.00 30.16           C  
ANISOU 2120  CE2 PHE A 274     5355   4396   1706   -660   -122   -497       C  
ATOM   2121  CZ  PHE A 274     -54.661 -26.102 -26.158  1.00 30.66           C  
ANISOU 2121  CZ  PHE A 274     4993   4156   2497   -675   -570   -194       C  
ATOM   2122  N   SER A 275     -49.566 -25.416 -28.926  1.00 26.50           N  
ANISOU 2122  N   SER A 275     5057   3605   1407      0   -302   -399       N  
ATOM   2123  CA  SER A 275     -48.654 -26.157 -28.063  1.00 26.78           C  
ANISOU 2123  CA  SER A 275     5344   3370   1460     97   -522   -771       C  
ATOM   2124  C   SER A 275     -48.603 -25.443 -26.713  1.00 25.07           C  
ANISOU 2124  C   SER A 275     5257   3021   1246   -214   -158   -480       C  
ATOM   2125  O   SER A 275     -48.451 -24.228 -26.679  1.00 24.36           O  
ANISOU 2125  O   SER A 275     5056   3051   1148   -166   -224   -425       O  
ATOM   2126  CB  SER A 275     -47.266 -26.140 -28.690  1.00 30.64           C  
ANISOU 2126  CB  SER A 275     5545   4278   1817     91   -353   -411       C  
ATOM   2127  OG  SER A 275     -46.430 -27.107 -28.087  1.00 39.29           O  
ANISOU 2127  OG  SER A 275     6763   4394   3770    407   -477    192       O  
ATOM   2128  N   ARG A 276     -48.746 -26.176 -25.612  1.00 24.73           N  
ANISOU 2128  N   ARG A 276     5345   3053    995   -183   -208   -675       N  
ATOM   2129  CA  ARG A 276     -48.697 -25.537 -24.316  1.00 23.11           C  
ANISOU 2129  CA  ARG A 276     4801   2846   1131   -154    -45   -765       C  
ATOM   2130  C   ARG A 276     -47.286 -25.568 -23.765  1.00 23.02           C  
ANISOU 2130  C   ARG A 276     4767   2689   1288   -198     36   -445       C  
ATOM   2131  O   ARG A 276     -46.695 -26.634 -23.587  1.00 25.85           O  
ANISOU 2131  O   ARG A 276     5019   2910   1890     37    -74   -461       O  
ATOM   2132  CB  ARG A 276     -49.683 -26.162 -23.336  1.00 24.32           C  
ANISOU 2132  CB  ARG A 276     4959   3194   1084   -260     -2   -667       C  
ATOM   2133  CG  ARG A 276     -49.664 -25.485 -21.979  1.00 23.84           C  
ANISOU 2133  CG  ARG A 276     4824   3106   1127   -304    -74   -686       C  
ATOM   2134  CD  ARG A 276     -50.575 -26.213 -21.028  1.00 24.90           C  
ANISOU 2134  CD  ARG A 276     4958   3424   1079   -426   -234   -532       C  
ATOM   2135  NE  ARG A 276     -50.716 -25.494 -19.772  1.00 22.72           N  
ANISOU 2135  NE  ARG A 276     4500   3064   1067   -347   -118   -378       N  
ATOM   2136  CZ  ARG A 276     -51.413 -25.951 -18.739  1.00 23.78           C  
ANISOU 2136  CZ  ARG A 276     4489   3025   1521   -451     42   -233       C  
ATOM   2137  NH1 ARG A 276     -52.051 -27.108 -18.834  1.00 28.45           N  
ANISOU 2137  NH1 ARG A 276     5028   3005   2774   -605    174    -20       N  
ATOM   2138  NH2 ARG A 276     -51.508 -25.240 -17.626  1.00 23.04           N  
ANISOU 2138  NH2 ARG A 276     4169   3327   1255   -321   -108   -123       N  
ATOM   2139  N   ASN A 277     -46.754 -24.385 -23.497  1.00 21.44           N  
ANISOU 2139  N   ASN A 277     4403   2785    955   -315    131   -215       N  
ATOM   2140  CA  ASN A 277     -45.444 -24.259 -22.882  1.00 19.87           C  
ANISOU 2140  CA  ASN A 277     4270   2543    736   -127    208   -141       C  
ATOM   2141  C   ASN A 277     -45.469 -24.636 -21.405  1.00 20.77           C  
ANISOU 2141  C   ASN A 277     4440   2672    777   -142   -259    -37       C  
ATOM   2142  O   ASN A 277     -46.414 -24.304 -20.680  1.00 22.05           O  
ANISOU 2142  O   ASN A 277     4581   2895    899   -190     14     27       O  
ATOM   2143  CB  ASN A 277     -44.898 -22.860 -23.127  1.00 19.73           C  
ANISOU 2143  CB  ASN A 277     4156   2555    784    -88     44      9       C  
ATOM   2144  CG  ASN A 277     -44.820 -22.538 -24.610  1.00 19.73           C  
ANISOU 2144  CG  ASN A 277     4356   2319    819   -379     52     55       C  
ATOM   2145  OD1 ASN A 277     -44.236 -23.293 -25.389  1.00 21.40           O  
ANISOU 2145  OD1 ASN A 277     4442   2755    931   -168     33    -14       O  
ATOM   2146  ND2 ASN A 277     -45.435 -21.441 -25.013  1.00 20.63           N  
ANISOU 2146  ND2 ASN A 277     4116   2573   1146   -159     29    -70       N  
ATOM   2147  N   SER A 278     -44.440 -25.368 -20.980  1.00 21.00           N  
ANISOU 2147  N   SER A 278     4467   2507   1005   -157   -195     60       N  
ATOM   2148  CA  SER A 278     -44.418 -25.989 -19.651  1.00 21.00           C  
ANISOU 2148  CA  SER A 278     4489   2632    857    -59    -71    -59       C  
ATOM   2149  C   SER A 278     -45.655 -26.877 -19.430  1.00 23.38           C  
ANISOU 2149  C   SER A 278     4766   2881   1233   -355   -210   -345       C  
ATOM   2150  O   SER A 278     -46.169 -26.977 -18.309  1.00 24.86           O  
ANISOU 2150  O   SER A 278     4840   3236   1367   -364   -152     79       O  
ATOM   2151  CB  SER A 278     -44.345 -24.930 -18.549  1.00 21.55           C  
ANISOU 2151  CB  SER A 278     4453   2713   1021     16    -32   -172       C  
ATOM   2152  OG  SER A 278     -43.795 -25.499 -17.380  1.00 24.08           O  
ANISOU 2152  OG  SER A 278     4533   3491   1126     80   -369   -254       O  
ATOM   2153  N   GLY A 279     -46.131 -27.521 -20.496  1.00 23.70           N  
ANISOU 2153  N   GLY A 279     4860   3129   1013   -318   -305   -220       N  
ATOM   2154  CA  GLY A 279     -47.402 -28.278 -20.449  1.00 26.54           C  
ANISOU 2154  CA  GLY A 279     5151   3214   1719   -566   -304   -174       C  
ATOM   2155  C   GLY A 279     -47.541 -29.444 -19.473  1.00 28.54           C  
ANISOU 2155  C   GLY A 279     5448   3828   1564   -277   -497    226       C  
ATOM   2156  O   GLY A 279     -48.659 -29.822 -19.092  1.00 33.81           O  
ANISOU 2156  O   GLY A 279     5640   4263   2942   -191    -81    408       O  
ATOM   2157  N   ASP A 280     -46.414 -30.037 -19.085  1.00 26.12           N  
ANISOU 2157  N   ASP A 280     5567   3392    962   -164   -514   -260       N  
ATOM   2158  CA  ASP A 280     -46.408 -31.117 -18.100  1.00 28.28           C  
ANISOU 2158  CA  ASP A 280     6077   3333   1333    -58   -579   -134       C  
ATOM   2159  C   ASP A 280     -46.053 -30.642 -16.698  1.00 26.32           C  
ANISOU 2159  C   ASP A 280     5608   3022   1371   -248   -371   -241       C  
ATOM   2160  O   ASP A 280     -46.047 -31.441 -15.758  1.00 29.42           O  
ANISOU 2160  O   ASP A 280     6010   3365   1800   -513   -511    138       O  
ATOM   2161  CB  ASP A 280     -45.413 -32.201 -18.519  1.00 30.89           C  
ANISOU 2161  CB  ASP A 280     6183   3474   2078     25   -125    -91       C  
ATOM   2162  CG  ASP A 280     -45.661 -32.706 -19.927  1.00 34.18           C  
ANISOU 2162  CG  ASP A 280     6191   4469   2325   -216   -285   -391       C  
ATOM   2163  OD1 ASP A 280     -46.830 -32.975 -20.284  1.00 36.09           O  
ANISOU 2163  OD1 ASP A 280     6509   4370   2831   -421   -811     -1       O  
ATOM   2164  OD2 ASP A 280     -44.680 -32.833 -20.680  1.00 39.95           O  
ANISOU 2164  OD2 ASP A 280     6867   4924   3388    -66    506   -456       O  
ATOM   2165  N   ASN A 281     -45.752 -29.354 -16.559  1.00 25.28           N  
ANISOU 2165  N   ASN A 281     5466   2863   1274    -17   -349   -164       N  
ATOM   2166  CA  ASN A 281     -45.176 -28.818 -15.322  1.00 24.68           C  
ANISOU 2166  CA  ASN A 281     5241   2943   1191     12   -177   -248       C  
ATOM   2167  C   ASN A 281     -45.904 -27.570 -14.820  1.00 23.95           C  
ANISOU 2167  C   ASN A 281     4949   2849   1300    -27   -173   -141       C  
ATOM   2168  O   ASN A 281     -45.555 -27.004 -13.770  1.00 25.02           O  
ANISOU 2168  O   ASN A 281     4957   2861   1685    126   -419   -370       O  
ATOM   2169  CB  ASN A 281     -43.693 -28.495 -15.536  1.00 27.45           C  
ANISOU 2169  CB  ASN A 281     5166   3214   2046    121   -463   -218       C  
ATOM   2170  CG  ASN A 281     -42.830 -29.736 -15.658  1.00 27.41           C  
ANISOU 2170  CG  ASN A 281     5553   3129   1730     86   -358   -249       C  
ATOM   2171  OD1 ASN A 281     -42.394 -30.105 -16.753  1.00 27.94           O  
ANISOU 2171  OD1 ASN A 281     5645   2968   2003    205     85   -135       O  
ATOM   2172  ND2 ASN A 281     -42.576 -30.387 -14.536  1.00 27.30           N  
ANISOU 2172  ND2 ASN A 281     5429   3005   1937   -307   -309     68       N  
ATOM   2173  N   ALA A 282     -46.929 -27.160 -15.562  1.00 23.31           N  
ANISOU 2173  N   ALA A 282     4698   2792   1366      5     69    -89       N  
ATOM   2174  CA  ALA A 282     -47.689 -25.953 -15.238  1.00 21.58           C  
ANISOU 2174  CA  ALA A 282     4456   2709   1032    -36     80     74       C  
ATOM   2175  C   ALA A 282     -48.972 -26.234 -14.441  1.00 23.05           C  
ANISOU 2175  C   ALA A 282     4272   2838   1649   -212    119   -210       C  
ATOM   2176  O   ALA A 282     -49.623 -27.273 -14.616  1.00 23.36           O  
ANISOU 2176  O   ALA A 282     4332   2831   1711   -238    226   -417       O  
ATOM   2177  CB  ALA A 282     -48.001 -25.174 -16.517  1.00 21.30           C  
ANISOU 2177  CB  ALA A 282     4249   2724   1116    -41   -153     53       C  
ATOM   2178  N   LEU A 283     -49.305 -25.301 -13.547  1.00 23.83           N  
ANISOU 2178  N   LEU A 283     4315   3173   1563   -109    274   -216       N  
ATOM   2179  CA  LEU A 283     -50.605 -25.259 -12.869  1.00 24.33           C  
ANISOU 2179  CA  LEU A 283     4102   3592   1547   -115     62   -200       C  
ATOM   2180  C   LEU A 283     -51.764 -25.205 -13.850  1.00 22.76           C  
ANISOU 2180  C   LEU A 283     3917   3138   1592   -183     89    -55       C  
ATOM   2181  O   LEU A 283     -51.633 -24.609 -14.930  1.00 23.25           O  
ANISOU 2181  O   LEU A 283     4050   2982   1802   -376    156     77       O  
ATOM   2182  CB  LEU A 283     -50.671 -24.039 -11.949  1.00 26.47           C  
ANISOU 2182  CB  LEU A 283     4333   3796   1926     13    139   -406       C  
ATOM   2183  CG  LEU A 283     -49.726 -24.095 -10.757  1.00 25.81           C  
ANISOU 2183  CG  LEU A 283     4285   3616   1903    177    192   -466       C  
ATOM   2184  CD1 LEU A 283     -50.136 -23.086  -9.702  1.00 26.30           C  
ANISOU 2184  CD1 LEU A 283     4438   3944   1608     92    125   -579       C  
ATOM   2185  CD2 LEU A 283     -49.723 -25.499 -10.174  1.00 29.64           C  
ANISOU 2185  CD2 LEU A 283     4539   3861   2860   -225    337     42       C  
ATOM   2186  N   SER A 284     -52.903 -25.791 -13.451  1.00 22.89           N  
ANISOU 2186  N   SER A 284     4117   2918   1660   -218    101    140       N  
ATOM   2187  CA  SER A 284     -54.096 -25.883 -14.298  1.00 23.80           C  
ANISOU 2187  CA  SER A 284     4024   2965   2053   -246    -28     43       C  
ATOM   2188  C   SER A 284     -54.696 -24.519 -14.633  1.00 22.40           C  
ANISOU 2188  C   SER A 284     3908   2959   1641   -340   -154     45       C  
ATOM   2189  O   SER A 284     -55.513 -24.396 -15.544  1.00 23.42           O  
ANISOU 2189  O   SER A 284     4373   3291   1232   -300   -109    238       O  
ATOM   2190  CB  SER A 284     -55.171 -26.769 -13.637  1.00 25.98           C  
ANISOU 2190  CB  SER A 284     4521   3486   1861   -446    146    247       C  
ATOM   2191  OG  SER A 284     -55.816 -26.115 -12.566  1.00 29.01           O  
ANISOU 2191  OG  SER A 284     4832   3658   2529   -191    281   -111       O  
ATOM   2192  N   THR A 285     -54.300 -23.498 -13.881  1.00 22.17           N  
ANISOU 2192  N   THR A 285     3977   2911   1535   -266     71    -58       N  
ATOM   2193  CA  THR A 285     -54.878 -22.174 -14.050  1.00 20.03           C  
ANISOU 2193  CA  THR A 285     3794   2985    831   -260     60     58       C  
ATOM   2194  C   THR A 285     -54.036 -21.202 -14.886  1.00 20.27           C  
ANISOU 2194  C   THR A 285     3517   3048   1136   -313    -53     74       C  
ATOM   2195  O   THR A 285     -54.490 -20.093 -15.189  1.00 19.48           O  
ANISOU 2195  O   THR A 285     3520   2871   1009   -470    -49    127       O  
ATOM   2196  CB  THR A 285     -55.263 -21.544 -12.693  1.00 19.46           C  
ANISOU 2196  CB  THR A 285     3470   3229    693   -403   -172    -48       C  
ATOM   2197  OG1 THR A 285     -54.134 -21.590 -11.807  1.00 19.44           O  
ANISOU 2197  OG1 THR A 285     3611   3172    603   -278   -211    335       O  
ATOM   2198  CG2 THR A 285     -56.476 -22.299 -12.047  1.00 21.75           C  
ANISOU 2198  CG2 THR A 285     3671   3276   1315   -542      3    -49       C  
ATOM   2199  N   THR A 286     -52.817 -21.584 -15.260  1.00 19.44           N  
ANISOU 2199  N   THR A 286     3564   2919    901   -322     48    -61       N  
ATOM   2200  CA  THR A 286     -52.150 -20.820 -16.330  1.00 19.67           C  
ANISOU 2200  CA  THR A 286     3701   2739   1031   -238    -10    108       C  
ATOM   2201  C   THR A 286     -51.738 -21.613 -17.548  1.00 19.47           C  
ANISOU 2201  C   THR A 286     3591   2930    877   -287     96    214       C  
ATOM   2202  O   THR A 286     -50.984 -22.559 -17.470  1.00 21.04           O  
ANISOU 2202  O   THR A 286     3786   3023   1182   -130    180    165       O  
ATOM   2203  CB  THR A 286     -51.092 -19.748 -15.904  1.00 22.87           C  
ANISOU 2203  CB  THR A 286     3781   3619   1289   -570    171   -128       C  
ATOM   2204  OG1 THR A 286     -49.843 -19.873 -16.624  1.00 25.56           O  
ANISOU 2204  OG1 THR A 286     3745   3936   2028    134    177   -695       O  
ATOM   2205  CG2 THR A 286     -50.878 -19.686 -14.443  1.00 17.00           C  
ANISOU 2205  CG2 THR A 286     2855   2418   1185   -317    117    459       C  
ATOM   2206  N   TRP A 287     -52.269 -21.186 -18.687  1.00 19.77           N  
ANISOU 2206  N   TRP A 287     3755   2934    821   -275     25     85       N  
ATOM   2207  CA  TRP A 287     -52.052 -21.848 -19.963  1.00 19.20           C  
ANISOU 2207  CA  TRP A 287     3757   2677    861   -157    -15    113       C  
ATOM   2208  C   TRP A 287     -51.256 -20.907 -20.825  1.00 18.06           C  
ANISOU 2208  C   TRP A 287     3592   2471    797   -227    -20   -122       C  
ATOM   2209  O   TRP A 287     -51.818 -19.965 -21.398  1.00 18.62           O  
ANISOU 2209  O   TRP A 287     3633   2479    960   -291     30     82       O  
ATOM   2210  CB  TRP A 287     -53.402 -22.162 -20.609  1.00 20.39           C  
ANISOU 2210  CB  TRP A 287     3904   2624   1217   -383    -67    -98       C  
ATOM   2211  CG  TRP A 287     -54.125 -23.359 -20.016  1.00 20.89           C  
ANISOU 2211  CG  TRP A 287     4125   2874    935   -471    -97     32       C  
ATOM   2212  CD1 TRP A 287     -54.577 -23.532 -18.707  1.00 21.39           C  
ANISOU 2212  CD1 TRP A 287     4035   2993   1097   -456     41    135       C  
ATOM   2213  CD2 TRP A 287     -54.487 -24.590 -20.706  1.00 22.81           C  
ANISOU 2213  CD2 TRP A 287     4406   2735   1525   -498   -104    -53       C  
ATOM   2214  NE1 TRP A 287     -55.181 -24.756 -18.558  1.00 22.25           N  
ANISOU 2214  NE1 TRP A 287     4316   2978   1160   -547   -187     62       N  
ATOM   2215  CE2 TRP A 287     -55.156 -25.442 -19.719  1.00 23.31           C  
ANISOU 2215  CE2 TRP A 287     4585   2835   1437   -587    -70   -135       C  
ATOM   2216  CE3 TRP A 287     -54.335 -25.054 -22.001  1.00 25.39           C  
ANISOU 2216  CE3 TRP A 287     4856   3279   1512   -800   -189   -207       C  
ATOM   2217  CZ2 TRP A 287     -55.641 -26.699 -20.040  1.00 25.59           C  
ANISOU 2217  CZ2 TRP A 287     4982   2815   1923   -587   -281   -259       C  
ATOM   2218  CZ3 TRP A 287     -54.833 -26.319 -22.317  1.00 28.24           C  
ANISOU 2218  CZ3 TRP A 287     5166   3363   2201  -1146   -171      2       C  
ATOM   2219  CH2 TRP A 287     -55.465 -27.125 -21.357  1.00 27.96           C  
ANISOU 2219  CH2 TRP A 287     5495   3533   1594   -798   -176    124       C  
ATOM   2220  N   ASN A 288     -49.939 -21.112 -20.878  1.00 18.05           N  
ANISOU 2220  N   ASN A 288     3547   2470    839   -351    -97    -82       N  
ATOM   2221  CA  ASN A 288     -49.076 -20.349 -21.774  1.00 17.97           C  
ANISOU 2221  CA  ASN A 288     3629   2289    909   -337    -35   -146       C  
ATOM   2222  C   ASN A 288     -48.975 -21.182 -23.032  1.00 18.97           C  
ANISOU 2222  C   ASN A 288     3883   2452    871   -259    -60   -157       C  
ATOM   2223  O   ASN A 288     -48.403 -22.274 -23.027  1.00 19.08           O  
ANISOU 2223  O   ASN A 288     3941   2474    831   -271    -55   -264       O  
ATOM   2224  CB  ASN A 288     -47.699 -20.091 -21.149  1.00 17.68           C  
ANISOU 2224  CB  ASN A 288     3508   2267    941   -284    108   -164       C  
ATOM   2225  CG  ASN A 288     -46.859 -19.124 -21.970  1.00 18.24           C  
ANISOU 2225  CG  ASN A 288     3730   2029   1168   -161    112     30       C  
ATOM   2226  OD1 ASN A 288     -46.345 -19.485 -23.028  1.00 19.57           O  
ANISOU 2226  OD1 ASN A 288     3965   2584    886   -330    -14     30       O  
ATOM   2227  ND2 ASN A 288     -46.718 -17.892 -21.487  1.00 16.94           N  
ANISOU 2227  ND2 ASN A 288     3412   2335    688   -137   -101   -274       N  
ATOM   2228  N   VAL A 289     -49.587 -20.678 -24.095  1.00 18.55           N  
ANISOU 2228  N   VAL A 289     3971   2418    659   -310     -3   -254       N  
ATOM   2229  CA  VAL A 289     -49.756 -21.456 -25.322  1.00 18.65           C  
ANISOU 2229  CA  VAL A 289     4061   2371    654   -409   -124   -189       C  
ATOM   2230  C   VAL A 289     -49.222 -20.773 -26.579  1.00 19.22           C  
ANISOU 2230  C   VAL A 289     4050   2610    642   -304    -88   -125       C  
ATOM   2231  O   VAL A 289     -49.412 -19.583 -26.794  1.00 19.56           O  
ANISOU 2231  O   VAL A 289     4156   2653    621   -215    -23    -16       O  
ATOM   2232  CB  VAL A 289     -51.229 -21.843 -25.564  1.00 19.14           C  
ANISOU 2232  CB  VAL A 289     4063   2473    736   -462    -30    -95       C  
ATOM   2233  CG1 VAL A 289     -51.782 -22.698 -24.424  1.00 19.02           C  
ANISOU 2233  CG1 VAL A 289     3829   2446    950   -411     12      4       C  
ATOM   2234  CG2 VAL A 289     -52.100 -20.611 -25.790  1.00 19.69           C  
ANISOU 2234  CG2 VAL A 289     3968   2618    894   -455   -103    120       C  
ATOM   2235  N   THR A 290     -48.546 -21.557 -27.404  1.00 20.73           N  
ANISOU 2235  N   THR A 290     4157   2869    850   -222    114    -95       N  
ATOM   2236  CA  THR A 290     -48.036 -21.084 -28.678  1.00 20.78           C  
ANISOU 2236  CA  THR A 290     4063   3048    783   -240    138   -182       C  
ATOM   2237  C   THR A 290     -48.919 -21.661 -29.776  1.00 21.71           C  
ANISOU 2237  C   THR A 290     4385   3024    839   -158    -57   -205       C  
ATOM   2238  O   THR A 290     -48.924 -22.861 -29.994  1.00 22.76           O  
ANISOU 2238  O   THR A 290     4719   3042    884   -129   -154   -313       O  
ATOM   2239  CB  THR A 290     -46.592 -21.572 -28.883  1.00 20.16           C  
ANISOU 2239  CB  THR A 290     4056   2931    673   -237    175     98       C  
ATOM   2240  OG1 THR A 290     -45.773 -21.089 -27.820  1.00 21.69           O  
ANISOU 2240  OG1 THR A 290     4350   2760   1130   -151   -147    -37       O  
ATOM   2241  CG2 THR A 290     -46.005 -21.059 -30.211  1.00 20.46           C  
ANISOU 2241  CG2 THR A 290     4151   3030    590   -341    134     45       C  
ATOM   2242  N   PHE A 291     -49.687 -20.813 -30.444  1.00 20.36           N  
ANISOU 2242  N   PHE A 291     4501   2980    253   -347    -14    -31       N  
ATOM   2243  CA  PHE A 291     -50.477 -21.278 -31.568  1.00 22.84           C  
ANISOU 2243  CA  PHE A 291     4416   3306    954   -389   -340   -246       C  
ATOM   2244  C   PHE A 291     -49.565 -21.592 -32.744  1.00 24.15           C  
ANISOU 2244  C   PHE A 291     4971   3444    759   -295   -230   -273       C  
ATOM   2245  O   PHE A 291     -48.449 -21.052 -32.865  1.00 26.77           O  
ANISOU 2245  O   PHE A 291     4966   3818   1387   -264    -57   -171       O  
ATOM   2246  CB  PHE A 291     -51.546 -20.239 -31.956  1.00 22.35           C  
ANISOU 2246  CB  PHE A 291     4474   3350    667   -361   -250     -9       C  
ATOM   2247  CG  PHE A 291     -52.521 -19.911 -30.840  1.00 22.22           C  
ANISOU 2247  CG  PHE A 291     4635   3070    736   -394   -191    -59       C  
ATOM   2248  CD1 PHE A 291     -52.269 -18.848 -29.969  1.00 21.98           C  
ANISOU 2248  CD1 PHE A 291     4646   2988    715   -333   -270      7       C  
ATOM   2249  CD2 PHE A 291     -53.675 -20.679 -30.647  1.00 22.21           C  
ANISOU 2249  CD2 PHE A 291     4704   2950    782   -446   -247   -187       C  
ATOM   2250  CE1 PHE A 291     -53.140 -18.556 -28.934  1.00 22.59           C  
ANISOU 2250  CE1 PHE A 291     4410   3172    999   -466   -292    -93       C  
ATOM   2251  CE2 PHE A 291     -54.550 -20.392 -29.602  1.00 22.96           C  
ANISOU 2251  CE2 PHE A 291     4627   3116    977   -594    -71    -81       C  
ATOM   2252  CZ  PHE A 291     -54.277 -19.330 -28.747  1.00 21.80           C  
ANISOU 2252  CZ  PHE A 291     4522   3101    657   -495   -181     14       C  
ATOM   2253  N   GLU A 292     -50.123 -22.483 -33.560  1.00 24.31           N  
ANISOU 2253  N   GLU A 292     5151   3544    540   -223    -63   -244       N  
ATOM   2254  CA  GLU A 292     -49.472 -23.171 -34.645  1.00 26.10           C  
ANISOU 2254  CA  GLU A 292     5244   3474   1196   -216     -4   -746       C  
ATOM   2255  C   GLU A 292     -48.943 -22.241 -35.694  1.00 25.97           C  
ANISOU 2255  C   GLU A 292     5115   4026    725   -400   -153   -623       C  
ATOM   2256  O   GLU A 292     -47.852 -22.432 -36.174  1.00 29.11           O  
ANISOU 2256  O   GLU A 292     5145   4574   1340    -11   -103   -628       O  
ATOM   2257  CB  GLU A 292     -50.439 -24.143 -35.295  1.00 27.76           C  
ANISOU 2257  CB  GLU A 292     5074   3874   1599   -708    398   -504       C  
ATOM   2258  CG  GLU A 292     -49.801 -24.985 -36.393  1.00 32.36           C  
ANISOU 2258  CG  GLU A 292     5668   4492   2135   -336    327  -1019       C  
ATOM   2259  CD  GLU A 292     -50.747 -25.879 -37.149  1.00 36.38           C  
ANISOU 2259  CD  GLU A 292     6247   4859   2715   -735    928  -1761       C  
ATOM   2260  OE1 GLU A 292     -51.937 -26.011 -36.783  1.00 38.55           O  
ANISOU 2260  OE1 GLU A 292     6470   5161   3017  -1156    922   -654       O  
ATOM   2261  OE2 GLU A 292     -50.249 -26.473 -38.114  1.00 43.73           O  
ANISOU 2261  OE2 GLU A 292     7351   6435   2827   -537   1801  -1698       O  
ATOM   2262  N   ASN A 293     -49.690 -21.223 -36.056  1.00 26.95           N  
ANISOU 2262  N   ASN A 293     5016   4085   1139   -367   -306   -649       N  
ATOM   2263  CA  ASN A 293     -49.154 -20.345 -37.098  1.00 27.60           C  
ANISOU 2263  CA  ASN A 293     5248   3979   1259   -654    -14   -881       C  
ATOM   2264  C   ASN A 293     -49.791 -18.957 -37.003  1.00 28.32           C  
ANISOU 2264  C   ASN A 293     5066   4079   1614   -524   -236   -519       C  
ATOM   2265  O   ASN A 293     -50.699 -18.872 -36.251  1.00 26.69           O  
ANISOU 2265  O   ASN A 293     5026   3941   1171   -705   -489   -363       O  
ATOM   2266  CB  ASN A 293     -49.323 -20.977 -38.472  1.00 28.29           C  
ANISOU 2266  CB  ASN A 293     5315   4083   1349   -577   -320   -940       C  
ATOM   2267  CG  ASN A 293     -50.728 -21.500 -38.745  1.00 28.35           C  
ANISOU 2267  CG  ASN A 293     5280   4107   1382   -627   -160   -621       C  
ATOM   2268  OD1 ASN A 293     -50.811 -22.581 -39.367  1.00 35.32           O  
ANISOU 2268  OD1 ASN A 293     6390   4603   2425   -660   -132  -1252       O  
ATOM   2269  ND2 ASN A 293     -51.814 -20.751 -38.361  1.00 26.17           N  
ANISOU 2269  ND2 ASN A 293     4894   3908   1138   -928    -86   -395       N  
ATOM   2270  N   ASP A 294     -49.442 -17.921 -37.769  1.00 27.37           N  
ANISOU 2270  N   ASP A 294     4893   4033   1473   -808   -413   -583       N  
ATOM   2271  CA  ASP A 294     -50.092 -16.642 -37.550  1.00 28.04           C  
ANISOU 2271  CA  ASP A 294     4761   3975   1917   -905   -352   -415       C  
ATOM   2272  C   ASP A 294     -51.572 -16.648 -37.915  1.00 28.15           C  
ANISOU 2272  C   ASP A 294     4937   4116   1643   -703   -497   -274       C  
ATOM   2273  O   ASP A 294     -52.330 -15.827 -37.409  1.00 28.40           O  
ANISOU 2273  O   ASP A 294     5084   4259   1445   -461   -547   -111       O  
ATOM   2274  CB  ASP A 294     -49.339 -15.550 -38.285  1.00 28.49           C  
ANISOU 2274  CB  ASP A 294     5180   4041   1603   -543   -289    152       C  
ATOM   2275  CG  ASP A 294     -47.953 -15.305 -37.701  1.00 29.80           C  
ANISOU 2275  CG  ASP A 294     5171   4136   2014   -569   -432    538       C  
ATOM   2276  OD1 ASP A 294     -47.704 -15.669 -36.526  1.00 29.83           O  
ANISOU 2276  OD1 ASP A 294     5637   3955   1740   -513   -449    108       O  
ATOM   2277  OD2 ASP A 294     -47.102 -14.738 -38.414  1.00 32.96           O  
ANISOU 2277  OD2 ASP A 294     5327   3983   3211   -917   -360    877       O  
ATOM   2278  N   ASP A 295     -51.997 -17.584 -38.772  1.00 28.73           N  
ANISOU 2278  N   ASP A 295     4809   4571   1535   -961   -244   -425       N  
ATOM   2279  CA  ASP A 295     -53.406 -17.654 -39.189  1.00 27.50           C  
ANISOU 2279  CA  ASP A 295     4996   4721    732   -863   -427   -182       C  
ATOM   2280  C   ASP A 295     -54.298 -18.144 -38.053  1.00 26.75           C  
ANISOU 2280  C   ASP A 295     4696   4246   1221   -867   -394   -141       C  
ATOM   2281  O   ASP A 295     -55.427 -17.655 -37.889  1.00 27.74           O  
ANISOU 2281  O   ASP A 295     4755   4396   1388   -614   -948   -109       O  
ATOM   2282  CB  ASP A 295     -53.590 -18.528 -40.441  1.00 28.63           C  
ANISOU 2282  CB  ASP A 295     5147   4828    903   -724   -393   -364       C  
ATOM   2283  CG  ASP A 295     -53.177 -17.816 -41.729  1.00 32.57           C  
ANISOU 2283  CG  ASP A 295     5994   5083   1297   -643    218   -207       C  
ATOM   2284  OD1 ASP A 295     -53.220 -16.566 -41.814  1.00 35.36           O  
ANISOU 2284  OD1 ASP A 295     6344   5176   1914   -552      9     92       O  
ATOM   2285  OD2 ASP A 295     -52.814 -18.529 -42.680  1.00 39.13           O  
ANISOU 2285  OD2 ASP A 295     7018   6071   1776   -142    879   -423       O  
ATOM   2286  N   GLU A 296     -53.770 -19.085 -37.271  1.00 25.12           N  
ANISOU 2286  N   GLU A 296     4663   4184    694   -872   -359   -276       N  
ATOM   2287  CA  GLU A 296     -54.475 -19.621 -36.122  1.00 26.29           C  
ANISOU 2287  CA  GLU A 296     4800   4022   1164   -720      0   -200       C  
ATOM   2288  C   GLU A 296     -54.616 -18.546 -35.035  1.00 26.48           C  
ANISOU 2288  C   GLU A 296     4940   4111   1008   -784   -594   -292       C  
ATOM   2289  O   GLU A 296     -55.649 -18.442 -34.388  1.00 27.42           O  
ANISOU 2289  O   GLU A 296     5131   4009   1279   -839   -395   -217       O  
ATOM   2290  CB  GLU A 296     -53.754 -20.857 -35.583  1.00 26.05           C  
ANISOU 2290  CB  GLU A 296     4946   3696   1254   -949     65   -193       C  
ATOM   2291  CG  GLU A 296     -54.589 -21.689 -34.619  1.00 27.05           C  
ANISOU 2291  CG  GLU A 296     5085   3747   1446  -1048    108   -168       C  
ATOM   2292  CD  GLU A 296     -55.858 -22.245 -35.255  1.00 31.77           C  
ANISOU 2292  CD  GLU A 296     5213   4894   1964   -971   -240   -346       C  
ATOM   2293  OE1 GLU A 296     -56.651 -22.878 -34.526  1.00 32.04           O  
ANISOU 2293  OE1 GLU A 296     5149   4168   2857  -1120   -240   -628       O  
ATOM   2294  OE2 GLU A 296     -56.068 -22.044 -36.467  1.00 36.06           O  
ANISOU 2294  OE2 GLU A 296     6302   5434   1965   -968   -515   -444       O  
ATOM   2295  N   VAL A 297     -53.577 -17.741 -34.864  1.00 25.08           N  
ANISOU 2295  N   VAL A 297     4819   3702   1009   -731   -636     33       N  
ATOM   2296  CA  VAL A 297     -53.621 -16.634 -33.918  1.00 26.61           C  
ANISOU 2296  CA  VAL A 297     4870   3841   1397   -619   -722   -201       C  
ATOM   2297  C   VAL A 297     -54.745 -15.670 -34.286  1.00 27.65           C  
ANISOU 2297  C   VAL A 297     5123   4094   1288   -451   -850    -14       C  
ATOM   2298  O   VAL A 297     -55.492 -15.207 -33.417  1.00 28.92           O  
ANISOU 2298  O   VAL A 297     5090   4366   1532   -528   -685    129       O  
ATOM   2299  CB  VAL A 297     -52.277 -15.869 -33.870  1.00 27.30           C  
ANISOU 2299  CB  VAL A 297     4884   3686   1802   -688   -879   -224       C  
ATOM   2300  CG1 VAL A 297     -52.397 -14.596 -33.036  1.00 26.35           C  
ANISOU 2300  CG1 VAL A 297     5010   3331   1670   -313   -615    212       C  
ATOM   2301  CG2 VAL A 297     -51.191 -16.748 -33.279  1.00 26.00           C  
ANISOU 2301  CG2 VAL A 297     4698   3537   1642   -607   -427   -144       C  
ATOM   2302  N   LYS A 298     -54.838 -15.361 -35.580  1.00 26.78           N  
ANISOU 2302  N   LYS A 298     4871   4068   1236   -763   -898    -89       N  
ATOM   2303  CA  LYS A 298     -55.817 -14.402 -36.084  1.00 29.53           C  
ANISOU 2303  CA  LYS A 298     5023   4261   1936   -455   -821     12       C  
ATOM   2304  C   LYS A 298     -57.241 -14.889 -35.846  1.00 29.57           C  
ANISOU 2304  C   LYS A 298     5163   4300   1772   -416   -796     92       C  
ATOM   2305  O   LYS A 298     -58.100 -14.100 -35.456  1.00 30.47           O  
ANISOU 2305  O   LYS A 298     5302   4575   1697   -187   -729     34       O  
ATOM   2306  CB  LYS A 298     -55.585 -14.089 -37.559  1.00 30.03           C  
ANISOU 2306  CB  LYS A 298     4924   4208   2276   -407   -420    540       C  
ATOM   2307  CG  LYS A 298     -54.407 -13.148 -37.795  1.00 37.51           C  
ANISOU 2307  CG  LYS A 298     4886   4572   4792   -388   -220   1037       C  
ATOM   2308  CD  LYS A 298     -54.427 -12.533 -39.186  1.00 38.37           C  
ANISOU 2308  CD  LYS A 298     3904   4155   6519  -1505   1079   2832       C  
ATOM   2309  CE  LYS A 298     -53.233 -11.613 -39.406  1.00 41.72           C  
ANISOU 2309  CE  LYS A 298     3460   3990   8399  -1071   1527   2962       C  
ATOM   2310  NZ  LYS A 298     -53.241 -10.931 -40.734  1.00 55.07           N  
ANISOU 2310  NZ  LYS A 298     6525   5436   8962   -918    912   3842       N  
ATOM   2311  N   ARG A 299     -57.459 -16.183 -36.082  1.00 29.39           N  
ANISOU 2311  N   ARG A 299     5105   4379   1681   -593   -930    175       N  
ATOM   2312  CA  ARG A 299     -58.729 -16.861 -35.824  1.00 29.39           C  
ANISOU 2312  CA  ARG A 299     5260   4359   1548   -590   -523   -199       C  
ATOM   2313  C   ARG A 299     -59.084 -16.763 -34.338  1.00 29.53           C  
ANISOU 2313  C   ARG A 299     5270   4575   1373   -426   -937   -311       C  
ATOM   2314  O   ARG A 299     -60.169 -16.313 -33.990  1.00 31.30           O  
ANISOU 2314  O   ARG A 299     5071   5235   1584   -482   -965   -107       O  
ATOM   2315  CB  ARG A 299     -58.627 -18.330 -36.276  1.00 30.55           C  
ANISOU 2315  CB  ARG A 299     5365   4385   1854   -565   -571   -205       C  
ATOM   2316  CG  ARG A 299     -59.899 -19.162 -36.178  1.00 34.38           C  
ANISOU 2316  CG  ARG A 299     5567   4953   2543   -800   -456   -614       C  
ATOM   2317  CD  ARG A 299     -59.592 -20.662 -36.191  1.00 39.60           C  
ANISOU 2317  CD  ARG A 299     5913   4976   4155   -976   -601   -819       C  
ATOM   2318  NE  ARG A 299     -60.724 -21.479 -35.739  1.00 41.40           N  
ANISOU 2318  NE  ARG A 299     6668   4697   4365  -1159   -753   -628       N  
ATOM   2319  CZ  ARG A 299     -60.610 -22.672 -35.155  1.00 39.49           C  
ANISOU 2319  CZ  ARG A 299     6141   5037   3825   -782   -940   -539       C  
ATOM   2320  NH1 ARG A 299     -59.416 -23.204 -34.929  1.00 38.24           N  
ANISOU 2320  NH1 ARG A 299     5830   5105   3593   -870   -726   -840       N  
ATOM   2321  NH2 ARG A 299     -61.693 -23.335 -34.773  1.00 48.20           N  
ANISOU 2321  NH2 ARG A 299     5968   7032   5314   -691   -226   -416       N  
ATOM   2322  N   PHE A 300     -58.144 -17.145 -33.474  1.00 27.46           N  
ANISOU 2322  N   PHE A 300     5356   4254    823   -521   -645     40       N  
ATOM   2323  CA  PHE A 300     -58.355 -17.122 -32.022  1.00 27.18           C  
ANISOU 2323  CA  PHE A 300     5180   4269    878   -576   -539   -442       C  
ATOM   2324  C   PHE A 300     -58.705 -15.740 -31.500  1.00 28.01           C  
ANISOU 2324  C   PHE A 300     5218   4150   1274   -524   -687   -466       C  
ATOM   2325  O   PHE A 300     -59.643 -15.589 -30.733  1.00 30.29           O  
ANISOU 2325  O   PHE A 300     5211   4425   1871   -434   -496   -331       O  
ATOM   2326  CB  PHE A 300     -57.135 -17.692 -31.288  1.00 26.75           C  
ANISOU 2326  CB  PHE A 300     5235   3988    939   -479   -460   -270       C  
ATOM   2327  CG  PHE A 300     -57.156 -17.479 -29.789  1.00 26.31           C  
ANISOU 2327  CG  PHE A 300     5054   4001    939   -444   -447   -270       C  
ATOM   2328  CD1 PHE A 300     -57.996 -18.232 -28.972  1.00 26.78           C  
ANISOU 2328  CD1 PHE A 300     4797   3826   1552   -601   -417   -456       C  
ATOM   2329  CD2 PHE A 300     -56.319 -16.537 -29.196  1.00 27.57           C  
ANISOU 2329  CD2 PHE A 300     4907   4099   1468   -480   -369   -472       C  
ATOM   2330  CE1 PHE A 300     -58.007 -18.052 -27.588  1.00 26.31           C  
ANISOU 2330  CE1 PHE A 300     4624   3919   1452   -634   -151    -35       C  
ATOM   2331  CE2 PHE A 300     -56.327 -16.345 -27.817  1.00 25.81           C  
ANISOU 2331  CE2 PHE A 300     4487   3973   1343   -370   -380    -26       C  
ATOM   2332  CZ  PHE A 300     -57.175 -17.100 -27.012  1.00 27.97           C  
ANISOU 2332  CZ  PHE A 300     4765   3925   1936   -646   -229    -97       C  
ATOM   2333  N   THR A 301     -57.965 -14.725 -31.926  1.00 28.69           N  
ANISOU 2333  N   THR A 301     5220   4212   1466   -358   -499     71       N  
ATOM   2334  CA  THR A 301     -58.176 -13.378 -31.381  1.00 30.20           C  
ANISOU 2334  CA  THR A 301     4941   4382   2149   -302   -465   -254       C  
ATOM   2335  C   THR A 301     -59.440 -12.708 -31.916  1.00 30.89           C  
ANISOU 2335  C   THR A 301     5328   4595   1814   -338   -863    -86       C  
ATOM   2336  O   THR A 301     -60.085 -11.940 -31.200  1.00 33.34           O  
ANISOU 2336  O   THR A 301     5278   5096   2292    -91   -727    -79       O  
ATOM   2337  CB  THR A 301     -56.967 -12.437 -31.580  1.00 30.91           C  
ANISOU 2337  CB  THR A 301     4879   4326   2539   -291   -694   -124       C  
ATOM   2338  OG1 THR A 301     -56.707 -12.265 -32.979  1.00 33.42           O  
ANISOU 2338  OG1 THR A 301     5554   4486   2655   -199   -493    -44       O  
ATOM   2339  CG2 THR A 301     -55.721 -12.981 -30.868  1.00 29.82           C  
ANISOU 2339  CG2 THR A 301     5056   3734   2540   -150   -687   -185       C  
ATOM   2340  N   SER A 302     -59.796 -12.994 -33.164  1.00 30.90           N  
ANISOU 2340  N   SER A 302     5259   4558   1924   -445   -928   -220       N  
ATOM   2341  CA  SER A 302     -61.028 -12.452 -33.733  1.00 33.42           C  
ANISOU 2341  CA  SER A 302     5307   5471   1919   -125   -673    -21       C  
ATOM   2342  C   SER A 302     -62.279 -13.114 -33.156  1.00 35.20           C  
ANISOU 2342  C   SER A 302     5382   5158   2831   -213   -616   -156       C  
ATOM   2343  O   SER A 302     -63.307 -12.455 -33.001  1.00 35.08           O  
ANISOU 2343  O   SER A 302     5510   5451   2369    -24   -208   -379       O  
ATOM   2344  CB  SER A 302     -61.037 -12.558 -35.258  1.00 35.40           C  
ANISOU 2344  CB  SER A 302     5918   5547   1984   -252  -1110   -499       C  
ATOM   2345  OG  SER A 302     -61.273 -13.886 -35.673  1.00 38.24           O  
ANISOU 2345  OG  SER A 302     6117   5344   3067   -299   -799   -296       O  
ATOM   2346  N   GLU A 303     -62.198 -14.410 -32.860  1.00 32.39           N  
ANISOU 2346  N   GLU A 303     5223   4973   2110   -252   -799   -461       N  
ATOM   2347  CA  GLU A 303     -63.346 -15.123 -32.314  1.00 32.46           C  
ANISOU 2347  CA  GLU A 303     5393   5193   1745   -516   -999   -620       C  
ATOM   2348  C   GLU A 303     -63.524 -14.887 -30.823  1.00 31.57           C  
ANISOU 2348  C   GLU A 303     4819   5346   1829   -357   -827   -570       C  
ATOM   2349  O   GLU A 303     -64.645 -14.880 -30.335  1.00 32.68           O  
ANISOU 2349  O   GLU A 303     4821   5468   2126   -523   -753   -599       O  
ATOM   2350  CB  GLU A 303     -63.251 -16.616 -32.595  1.00 33.89           C  
ANISOU 2350  CB  GLU A 303     5486   5436   1952   -287   -486   -969       C  
ATOM   2351  CG  GLU A 303     -63.426 -16.963 -34.068  1.00 35.72           C  
ANISOU 2351  CG  GLU A 303     5147   6279   2143   -572  -1459   -988       C  
ATOM   2352  CD  GLU A 303     -63.346 -18.448 -34.361  1.00 38.84           C  
ANISOU 2352  CD  GLU A 303     6018   6632   2106   -374  -1337  -1670       C  
ATOM   2353  OE1 GLU A 303     -62.927 -19.226 -33.477  1.00 36.12           O  
ANISOU 2353  OE1 GLU A 303     5931   5753   2037   -544   -847  -1859       O  
ATOM   2354  OE2 GLU A 303     -63.690 -18.833 -35.501  1.00 41.82           O  
ANISOU 2354  OE2 GLU A 303     7160   6537   2192  -1159  -1023  -1944       O  
ATOM   2355  N   ARG A 304     -62.420 -14.683 -30.112  1.00 29.40           N  
ANISOU 2355  N   ARG A 304     4886   4756   1527   -404   -913   -491       N  
ATOM   2356  CA  ARG A 304     -62.436 -14.555 -28.651  1.00 29.07           C  
ANISOU 2356  CA  ARG A 304     4667   4822   1556   -291   -614   -364       C  
ATOM   2357  C   ARG A 304     -61.905 -13.200 -28.214  1.00 30.67           C  
ANISOU 2357  C   ARG A 304     4837   5014   1802   -302  -1024   -695       C  
ATOM   2358  O   ARG A 304     -60.740 -12.867 -28.430  1.00 33.28           O  
ANISOU 2358  O   ARG A 304     4859   5419   2364   -381  -1293   -699       O  
ATOM   2359  CB  ARG A 304     -61.600 -15.660 -28.000  1.00 27.79           C  
ANISOU 2359  CB  ARG A 304     4757   4500   1300   -468   -666   -453       C  
ATOM   2360  CG  ARG A 304     -61.830 -17.045 -28.569  1.00 30.21           C  
ANISOU 2360  CG  ARG A 304     4833   4564   2081   -614   -551   -631       C  
ATOM   2361  CD  ARG A 304     -63.117 -17.616 -28.056  1.00 28.80           C  
ANISOU 2361  CD  ARG A 304     4862   4164   1915   -596   -527   -800       C  
ATOM   2362  NE  ARG A 304     -63.451 -18.861 -28.738  1.00 32.46           N  
ANISOU 2362  NE  ARG A 304     5069   4416   2848   -497   -923  -1178       N  
ATOM   2363  CZ  ARG A 304     -64.645 -19.438 -28.679  1.00 34.14           C  
ANISOU 2363  CZ  ARG A 304     5119   4316   3536   -526  -1025  -1290       C  
ATOM   2364  NH1 ARG A 304     -65.651 -18.903 -27.993  1.00 37.88           N  
ANISOU 2364  NH1 ARG A 304     5131   5206   4056   -305   -850  -1245       N  
ATOM   2365  NH2 ARG A 304     -64.827 -20.550 -29.328  1.00 37.02           N  
ANISOU 2365  NH2 ARG A 304     5507   4295   4262   -522   -636  -1451       N  
ATOM   2366  N   ASN A 305     -62.765 -12.394 -27.628  1.00 31.97           N  
ANISOU 2366  N   ASN A 305     4613   5254   2278   -223  -1054   -739       N  
ATOM   2367  CA  ASN A 305     -62.325 -11.110 -27.186  1.00 32.16           C  
ANISOU 2367  CA  ASN A 305     4857   5016   2344     27  -1834   -413       C  
ATOM   2368  C   ASN A 305     -61.800 -11.195 -25.756  1.00 28.09           C  
ANISOU 2368  C   ASN A 305     4301   4344   2026    -75  -1326   -198       C  
ATOM   2369  O   ASN A 305     -62.284 -10.495 -24.889  1.00 31.76           O  
ANISOU 2369  O   ASN A 305     4666   5093   2309    245  -1060   -227       O  
ATOM   2370  CB  ASN A 305     -63.489 -10.145 -27.288  1.00 36.00           C  
ANISOU 2370  CB  ASN A 305     4977   5359   3340    277  -1699    -12       C  
ATOM   2371  CG  ASN A 305     -63.061  -8.699 -27.178  1.00 38.93           C  
ANISOU 2371  CG  ASN A 305     4944   5509   4335    127  -1765    321       C  
ATOM   2372  OD1 ASN A 305     -61.872  -8.397 -27.037  1.00 41.57           O  
ANISOU 2372  OD1 ASN A 305     4823   6003   4967    140  -1306     86       O  
ATOM   2373  ND2 ASN A 305     -64.033  -7.787 -27.237  1.00 42.85           N  
ANISOU 2373  ND2 ASN A 305     4782   6312   5184    476  -1021   -413       N  
ATOM   2374  N   TRP A 306     -60.802 -12.041 -25.512  1.00 24.95           N  
ANISOU 2374  N   TRP A 306     4191   3848   1441   -332  -1267   -138       N  
ATOM   2375  CA  TRP A 306     -60.258 -12.212 -24.157  1.00 21.80           C  
ANISOU 2375  CA  TRP A 306     3706   3385   1192   -189   -878   -213       C  
ATOM   2376  C   TRP A 306     -59.170 -11.251 -23.798  1.00 22.05           C  
ANISOU 2376  C   TRP A 306     3591   3366   1421   -306   -286    -97       C  
ATOM   2377  O   TRP A 306     -58.304 -10.952 -24.635  1.00 22.09           O  
ANISOU 2377  O   TRP A 306     3669   3520   1203   -330   -291   -126       O  
ATOM   2378  CB  TRP A 306     -59.709 -13.612 -23.999  1.00 22.12           C  
ANISOU 2378  CB  TRP A 306     3569   3372   1463   -300   -650   -106       C  
ATOM   2379  CG  TRP A 306     -60.746 -14.674 -24.198  1.00 22.56           C  
ANISOU 2379  CG  TRP A 306     3953   3325   1294   -405   -712   -176       C  
ATOM   2380  CD1 TRP A 306     -62.113 -14.507 -24.382  1.00 23.32           C  
ANISOU 2380  CD1 TRP A 306     3903   3473   1483   -421   -575   -202       C  
ATOM   2381  CD2 TRP A 306     -60.532 -16.114 -24.200  1.00 22.77           C  
ANISOU 2381  CD2 TRP A 306     3898   3387   1366   -398   -429   -109       C  
ATOM   2382  NE1 TRP A 306     -62.737 -15.720 -24.509  1.00 23.54           N  
ANISOU 2382  NE1 TRP A 306     4332   3407   1203   -398   -573   -201       N  
ATOM   2383  CE2 TRP A 306     -61.843 -16.721 -24.423  1.00 22.83           C  
ANISOU 2383  CE2 TRP A 306     4076   3340   1256   -531   -451   -149       C  
ATOM   2384  CE3 TRP A 306     -59.420 -16.934 -24.072  1.00 23.12           C  
ANISOU 2384  CE3 TRP A 306     3905   3333   1546   -418   -203     46       C  
ATOM   2385  CZ2 TRP A 306     -62.013 -18.080 -24.490  1.00 24.67           C  
ANISOU 2385  CZ2 TRP A 306     4251   3403   1719   -372   -296   -353       C  
ATOM   2386  CZ3 TRP A 306     -59.603 -18.319 -24.150  1.00 23.14           C  
ANISOU 2386  CZ3 TRP A 306     4001   3466   1323   -642   -459   -194       C  
ATOM   2387  CH2 TRP A 306     -60.874 -18.877 -24.342  1.00 22.89           C  
ANISOU 2387  CH2 TRP A 306     3926   3523   1247   -572   -426   -422       C  
ATOM   2388  N   LEU A 307     -59.176 -10.777 -22.551  1.00 22.37           N  
ANISOU 2388  N   LEU A 307     3622   3491   1384   -202   -579   -155       N  
ATOM   2389  CA  LEU A 307     -58.059  -9.985 -22.074  1.00 20.92           C  
ANISOU 2389  CA  LEU A 307     3230   3205   1512    -31   -233   -223       C  
ATOM   2390  C   LEU A 307     -57.048 -10.937 -21.501  1.00 19.28           C  
ANISOU 2390  C   LEU A 307     3414   2754   1154   -187    -60    -26       C  
ATOM   2391  O   LEU A 307     -57.297 -11.640 -20.498  1.00 18.85           O  
ANISOU 2391  O   LEU A 307     3375   2850    937   -191   -149   -123       O  
ATOM   2392  CB  LEU A 307     -58.506  -8.987 -21.025  1.00 21.03           C  
ANISOU 2392  CB  LEU A 307     3423   3380   1186      1   -145   -172       C  
ATOM   2393  CG  LEU A 307     -59.794  -8.296 -21.457  1.00 21.55           C  
ANISOU 2393  CG  LEU A 307     3316   3603   1268     -7    -26    -18       C  
ATOM   2394  CD1 LEU A 307     -60.380  -7.530 -20.288  1.00 22.49           C  
ANISOU 2394  CD1 LEU A 307     3483   3587   1474    273   -248   -202       C  
ATOM   2395  CD2 LEU A 307     -59.560  -7.380 -22.650  1.00 22.30           C  
ANISOU 2395  CD2 LEU A 307     3574   3647   1250    -20     34    -26       C  
ATOM   2396  N   ILE A 308     -55.907 -10.962 -22.174  1.00 17.41           N  
ANISOU 2396  N   ILE A 308     3333   2483    797   -194   -324     -2       N  
ATOM   2397  CA  ILE A 308     -54.838 -11.907 -21.893  1.00 17.83           C  
ANISOU 2397  CA  ILE A 308     3369   2350   1056   -206    -37   -147       C  
ATOM   2398  C   ILE A 308     -53.498 -11.189 -21.910  1.00 18.20           C  
ANISOU 2398  C   ILE A 308     3413   2345   1154   -174   -314   -168       C  
ATOM   2399  O   ILE A 308     -53.426  -9.959 -21.869  1.00 18.19           O  
ANISOU 2399  O   ILE A 308     3294   2289   1325   -351    -68   -215       O  
ATOM   2400  CB  ILE A 308     -54.825 -13.117 -22.869  1.00 17.23           C  
ANISOU 2400  CB  ILE A 308     3443   2294    808   -324   -192    -17       C  
ATOM   2401  CG1 ILE A 308     -54.775 -12.671 -24.341  1.00 18.64           C  
ANISOU 2401  CG1 ILE A 308     3793   2547    742   -213   -137   -106       C  
ATOM   2402  CG2 ILE A 308     -56.009 -14.030 -22.579  1.00 17.28           C  
ANISOU 2402  CG2 ILE A 308     3361   2550    651   -389   -251    -89       C  
ATOM   2403  CD1 ILE A 308     -54.988 -13.794 -25.337  1.00 18.89           C  
ANISOU 2403  CD1 ILE A 308     3989   2574    610   -184   -449      2       C  
ATOM   2404  N   SER A 309     -52.420 -11.947 -21.966  1.00 17.05           N  
ANISOU 2404  N   SER A 309     3419   2527    530    -79   -558   -283       N  
ATOM   2405  CA  SER A 309     -51.113 -11.317 -21.802  1.00 18.60           C  
ANISOU 2405  CA  SER A 309     3514   2646    904   -217   -294   -115       C  
ATOM   2406  C   SER A 309     -50.050 -11.894 -22.716  1.00 18.80           C  
ANISOU 2406  C   SER A 309     3634   2514    995   -248   -266     -7       C  
ATOM   2407  O   SER A 309     -50.092 -13.059 -23.045  1.00 18.28           O  
ANISOU 2407  O   SER A 309     3519   2517    908     37   -127    -17       O  
ATOM   2408  CB  SER A 309     -50.670 -11.462 -20.343  1.00 18.46           C  
ANISOU 2408  CB  SER A 309     3476   2610    926    -18   -310     48       C  
ATOM   2409  OG  SER A 309     -49.315 -11.121 -20.236  1.00 18.95           O  
ANISOU 2409  OG  SER A 309     3612   2611    975   -110     62     85       O  
ATOM   2410  N   GLN A 310     -49.056 -11.127 -23.150  1.00 18.10           N  
ANISOU 2410  N   GLN A 310     3652   2550    673   -133   -300    420       N  
ATOM   2411  CA  GLN A 310     -48.014 -11.759 -23.965  1.00 19.13           C  
ANISOU 2411  CA  GLN A 310     3899   2572    798    -46   -381    376       C  
ATOM   2412  C   GLN A 310     -46.644 -11.758 -23.330  1.00 21.65           C  
ANISOU 2412  C   GLN A 310     3771   2833   1621   -124   -308      8       C  
ATOM   2413  O   GLN A 310     -45.813 -12.572 -23.686  1.00 25.21           O  
ANISOU 2413  O   GLN A 310     4369   3323   1884    220   -131     60       O  
ATOM   2414  CB  GLN A 310     -47.928 -11.199 -25.398  1.00 19.75           C  
ANISOU 2414  CB  GLN A 310     3978   2805    719   -314     82    236       C  
ATOM   2415  CG  GLN A 310     -48.857 -11.882 -26.381  1.00 20.30           C  
ANISOU 2415  CG  GLN A 310     4223   2796    691   -217     42     54       C  
ATOM   2416  CD  GLN A 310     -48.466 -11.645 -27.823  1.00 20.36           C  
ANISOU 2416  CD  GLN A 310     4499   2405    832   -245     97    437       C  
ATOM   2417  OE1 GLN A 310     -48.508 -10.530 -28.324  1.00 19.14           O  
ANISOU 2417  OE1 GLN A 310     4363   2043    865   -458    -24     89       O  
ATOM   2418  NE2 GLN A 310     -48.105 -12.710 -28.503  1.00 21.02           N  
ANISOU 2418  NE2 GLN A 310     4264   2686   1034   -202   -119    123       N  
ATOM   2419  N   GLY A 311     -46.378 -10.874 -22.400  1.00 21.03           N  
ANISOU 2419  N   GLY A 311     3562   2881   1545     17   -354    -15       N  
ATOM   2420  CA  GLY A 311     -45.097 -10.954 -21.773  1.00 18.63           C  
ANISOU 2420  CA  GLY A 311     3747   2716    613     83   -295      7       C  
ATOM   2421  C   GLY A 311     -45.056  -9.738 -20.908  1.00 18.99           C  
ANISOU 2421  C   GLY A 311     3560   2457   1196    177   -423     73       C  
ATOM   2422  O   GLY A 311     -46.048  -9.052 -20.808  1.00 20.14           O  
ANISOU 2422  O   GLY A 311     3751   2322   1577    281   -138     65       O  
ATOM   2423  N   SER A 312     -43.902  -9.471 -20.300  1.00 18.29           N  
ANISOU 2423  N   SER A 312     3702   2599    648   -200   -260   -180       N  
ATOM   2424  CA  SER A 312     -43.693  -8.349 -19.375  1.00 17.99           C  
ANISOU 2424  CA  SER A 312     3540   2523    770    -78    -78   -197       C  
ATOM   2425  C   SER A 312     -43.829  -7.009 -20.067  1.00 18.44           C  
ANISOU 2425  C   SER A 312     3713   2362    931    -56    -59   -368       C  
ATOM   2426  O   SER A 312     -43.620  -6.887 -21.293  1.00 19.65           O  
ANISOU 2426  O   SER A 312     3670   2819    976   -181    -61    -61       O  
ATOM   2427  CB  SER A 312     -42.302  -8.418 -18.732  1.00 18.22           C  
ANISOU 2427  CB  SER A 312     3513   2638    770    -70     31   -156       C  
ATOM   2428  OG  SER A 312     -41.308  -7.930 -19.634  1.00 19.61           O  
ANISOU 2428  OG  SER A 312     3687   2576   1186   -279    180   -315       O  
ATOM   2429  N   ALA A 313     -44.105  -5.988 -19.243  1.00 17.21           N  
ANISOU 2429  N   ALA A 313     3598   2299    641     74   -161   -163       N  
ATOM   2430  CA  ALA A 313     -44.179  -4.570 -19.684  1.00 16.90           C  
ANISOU 2430  CA  ALA A 313     3644   1902    872   -212    -96   -664       C  
ATOM   2431  C   ALA A 313     -42.868  -4.029 -20.249  1.00 18.71           C  
ANISOU 2431  C   ALA A 313     3663   2358   1085   -175    -76   -366       C  
ATOM   2432  O   ALA A 313     -42.868  -3.197 -21.171  1.00 20.40           O  
ANISOU 2432  O   ALA A 313     3999   2931    820    -18    -21   -236       O  
ATOM   2433  CB  ALA A 313     -44.654  -3.661 -18.553  1.00 16.42           C  
ANISOU 2433  CB  ALA A 313     3385   2099    754    112     91   -372       C  
ATOM   2434  N   SER A 314     -41.759  -4.448 -19.660  1.00 18.28           N  
ANISOU 2434  N   SER A 314     3748   2541    656    -66    -48   -389       N  
ATOM   2435  CA  SER A 314     -40.499  -4.008 -20.194  1.00 19.65           C  
ANISOU 2435  CA  SER A 314     3672   2822    971   -118     45   -514       C  
ATOM   2436  C   SER A 314     -40.232  -4.610 -21.541  1.00 18.84           C  
ANISOU 2436  C   SER A 314     3810   2675    672   -102   -113   -237       C  
ATOM   2437  O   SER A 314     -39.701  -3.927 -22.362  1.00 20.00           O  
ANISOU 2437  O   SER A 314     3766   2801   1030   -155    136   -250       O  
ATOM   2438  CB  SER A 314     -39.334  -4.245 -19.259  1.00 22.46           C  
ANISOU 2438  CB  SER A 314     4320   2956   1256   -240   -458   -307       C  
ATOM   2439  OG  SER A 314     -39.390  -5.534 -18.743  1.00 26.58           O  
ANISOU 2439  OG  SER A 314     4476   3305   2317    -68     12    104       O  
ATOM   2440  N   ASN A 315     -40.580  -5.872 -21.749  1.00 18.21           N  
ANISOU 2440  N   ASN A 315     3704   2561    652    -24     16   -138       N  
ATOM   2441  CA  ASN A 315     -40.474  -6.413 -23.078  1.00 18.75           C  
ANISOU 2441  CA  ASN A 315     3802   2598    722    -59    -55   -241       C  
ATOM   2442  C   ASN A 315     -41.396  -5.712 -24.055  1.00 19.67           C  
ANISOU 2442  C   ASN A 315     3911   2775    786    -61    -44    -62       C  
ATOM   2443  O   ASN A 315     -41.015  -5.505 -25.206  1.00 19.91           O  
ANISOU 2443  O   ASN A 315     4010   2675    879   -156     39    -59       O  
ATOM   2444  CB  ASN A 315     -40.602  -7.932 -23.078  1.00 18.95           C  
ANISOU 2444  CB  ASN A 315     3683   2602    914    -44     27   -136       C  
ATOM   2445  CG  ASN A 315     -39.370  -8.584 -22.487  1.00 18.83           C  
ANISOU 2445  CG  ASN A 315     3590   2766    799    -97    185     87       C  
ATOM   2446  OD1 ASN A 315     -38.255  -8.468 -23.026  1.00 20.45           O  
ANISOU 2446  OD1 ASN A 315     3708   2808   1252   -333    407    259       O  
ATOM   2447  ND2 ASN A 315     -39.547  -9.232 -21.362  1.00 15.91           N  
ANISOU 2447  ND2 ASN A 315     3033   2335    674    -12    167   -110       N  
ATOM   2448  N   ALA A 316     -42.575  -5.307 -23.611  1.00 20.03           N  
ANISOU 2448  N   ALA A 316     3777   2920    913    -43   -166    -88       N  
ATOM   2449  CA  ALA A 316     -43.414  -4.580 -24.544  1.00 20.14           C  
ANISOU 2449  CA  ALA A 316     3713   2955    983    -21    -78    -60       C  
ATOM   2450  C   ALA A 316     -42.744  -3.269 -24.942  1.00 20.35           C  
ANISOU 2450  C   ALA A 316     3972   2920    840    -54    -39    -94       C  
ATOM   2451  O   ALA A 316     -42.763  -2.903 -26.108  1.00 21.14           O  
ANISOU 2451  O   ALA A 316     4041   3083    906     33   -282     10       O  
ATOM   2452  CB  ALA A 316     -44.793  -4.341 -23.978  1.00 20.25           C  
ANISOU 2452  CB  ALA A 316     3685   3123    883   -193     11   -197       C  
ATOM   2453  N   MET A 317     -42.130  -2.583 -23.976  1.00 21.65           N  
ANISOU 2453  N   MET A 317     3978   3094   1153   -128   -158   -185       N  
ATOM   2454  CA  MET A 317     -41.479  -1.335 -24.217  1.00 21.96           C  
ANISOU 2454  CA  MET A 317     4091   3117   1136   -141   -160   -194       C  
ATOM   2455  C   MET A 317     -40.252  -1.419 -25.094  1.00 21.40           C  
ANISOU 2455  C   MET A 317     3994   3019   1117   -107   -169   -152       C  
ATOM   2456  O   MET A 317     -39.940  -0.489 -25.827  1.00 22.50           O  
ANISOU 2456  O   MET A 317     4293   2969   1287   -128   -322    -75       O  
ATOM   2457  CB  MET A 317     -41.032  -0.867 -22.877  1.00 23.31           C  
ANISOU 2457  CB  MET A 317     4240   3418   1197   -273   -296   -178       C  
ATOM   2458  CG  MET A 317     -41.168   0.527 -22.510  1.00 31.75           C  
ANISOU 2458  CG  MET A 317     5601   3845   2616    642   -110   -596       C  
ATOM   2459  SD  MET A 317     -42.789   1.212 -22.736  1.00 46.54           S  
ANISOU 2459  SD  MET A 317     5990   6835   4856    735   -756    179       S  
ATOM   2460  CE  MET A 317     -42.210   2.159 -24.051  1.00 31.06           C  
ANISOU 2460  CE  MET A 317     4978   4242   2581   1079   -856  -1318       C  
ATOM   2461  N   SER A 318     -39.517  -2.511 -24.973  1.00 19.48           N  
ANISOU 2461  N   SER A 318     3816   2822    762   -219   -288   -176       N  
ATOM   2462  CA  SER A 318     -38.348  -2.721 -25.814  1.00 19.80           C  
ANISOU 2462  CA  SER A 318     3780   2812    930   -194   -250   -221       C  
ATOM   2463  C   SER A 318     -38.707  -3.405 -27.132  1.00 19.88           C  
ANISOU 2463  C   SER A 318     3882   2765    907   -188   -187   -227       C  
ATOM   2464  O   SER A 318     -37.822  -3.663 -27.948  1.00 21.79           O  
ANISOU 2464  O   SER A 318     3961   3117   1200   -195    -90   -423       O  
ATOM   2465  CB  SER A 318     -37.300  -3.546 -25.070  1.00 21.10           C  
ANISOU 2465  CB  SER A 318     3775   2811   1431    -78   -236    -76       C  
ATOM   2466  OG  SER A 318     -37.801  -4.841 -24.766  1.00 22.65           O  
ANISOU 2466  OG  SER A 318     4180   3052   1374   -273     23     91       O  
ATOM   2467  N   ASN A 319     -39.993  -3.689 -27.346  1.00 19.09           N  
ANISOU 2467  N   ASN A 319     3847   2642    764   -152   -209     91       N  
ATOM   2468  CA  ASN A 319     -40.429  -4.363 -28.564  1.00 18.83           C  
ANISOU 2468  CA  ASN A 319     3968   2521    663   -239    -22    131       C  
ATOM   2469  C   ASN A 319     -39.678  -5.676 -28.759  1.00 19.44           C  
ANISOU 2469  C   ASN A 319     3961   2624    798   -241     64     -8       C  
ATOM   2470  O   ASN A 319     -39.159  -5.949 -29.848  1.00 19.56           O  
ANISOU 2470  O   ASN A 319     4117   2492    822   -284    113    -16       O  
ATOM   2471  CB  ASN A 319     -40.216  -3.441 -29.770  1.00 19.36           C  
ANISOU 2471  CB  ASN A 319     3919   2436    998   -288     20    314       C  
ATOM   2472  CG  ASN A 319     -41.157  -3.745 -30.923  1.00 20.20           C  
ANISOU 2472  CG  ASN A 319     4226   2443   1003   -497    -15    435       C  
ATOM   2473  OD1 ASN A 319     -41.073  -3.131 -32.004  1.00 22.91           O  
ANISOU 2473  OD1 ASN A 319     4552   2985   1166   -242   -196    756       O  
ATOM   2474  ND2 ASN A 319     -42.056  -4.689 -30.711  1.00 17.75           N  
ANISOU 2474  ND2 ASN A 319     4313   2124    305   -520     89    -39       N  
ATOM   2475  N   THR A 320     -39.608  -6.469 -27.691  1.00 18.79           N  
ANISOU 2475  N   THR A 320     3719   2631    789   -260    134     21       N  
ATOM   2476  CA  THR A 320     -38.938  -7.770 -27.711  1.00 18.55           C  
ANISOU 2476  CA  THR A 320     3703   2657    685   -256    265    -92       C  
ATOM   2477  C   THR A 320     -39.819  -8.848 -27.075  1.00 19.47           C  
ANISOU 2477  C   THR A 320     3868   2580    947   -313    212    -47       C  
ATOM   2478  O   THR A 320     -40.748  -8.536 -26.339  1.00 19.49           O  
ANISOU 2478  O   THR A 320     3957   2695    754   -276    203    -88       O  
ATOM   2479  CB  THR A 320     -37.572  -7.693 -27.003  1.00 19.28           C  
ANISOU 2479  CB  THR A 320     3808   2688    830   -324     78   -160       C  
ATOM   2480  OG1 THR A 320     -37.762  -7.304 -25.641  1.00 20.10           O  
ANISOU 2480  OG1 THR A 320     3969   2812    855   -359    194   -150       O  
ATOM   2481  CG2 THR A 320     -36.704  -6.634 -27.660  1.00 20.70           C  
ANISOU 2481  CG2 THR A 320     3862   3077    923   -310    301    -59       C  
ATOM   2482  N   PRO A 321     -39.555 -10.109 -27.413  1.00 19.36           N  
ANISOU 2482  N   PRO A 321     3821   2636    897   -432    277    -61       N  
ATOM   2483  CA  PRO A 321     -40.357 -11.192 -26.866  1.00 19.07           C  
ANISOU 2483  CA  PRO A 321     4008   2409    828   -330    146     18       C  
ATOM   2484  C   PRO A 321     -40.177 -11.245 -25.361  1.00 18.69           C  
ANISOU 2484  C   PRO A 321     3846   2448    806   -275    222     51       C  
ATOM   2485  O   PRO A 321     -39.220 -10.686 -24.843  1.00 18.99           O  
ANISOU 2485  O   PRO A 321     3921   2565    730   -299    173     15       O  
ATOM   2486  CB  PRO A 321     -39.746 -12.441 -27.481  1.00 20.36           C  
ANISOU 2486  CB  PRO A 321     4065   2755    915   -353    517   -168       C  
ATOM   2487  CG  PRO A 321     -38.895 -11.993 -28.614  1.00 20.78           C  
ANISOU 2487  CG  PRO A 321     4088   2617   1189   -504    481    100       C  
ATOM   2488  CD  PRO A 321     -38.574 -10.548 -28.418  1.00 19.92           C  
ANISOU 2488  CD  PRO A 321     3870   2541   1155   -242    262   -219       C  
ATOM   2489  N   SER A 322     -41.083 -11.936 -24.684  1.00 19.11           N  
ANISOU 2489  N   SER A 322     3857   2566    837   -231    113    323       N  
ATOM   2490  CA  SER A 322     -40.964 -12.247 -23.267  1.00 18.00           C  
ANISOU 2490  CA  SER A 322     3476   2631    732   -102    -94     15       C  
ATOM   2491  C   SER A 322     -39.592 -12.785 -22.926  1.00 17.96           C  
ANISOU 2491  C   SER A 322     3503   2575    746    -14     -5     36       C  
ATOM   2492  O   SER A 322     -39.075 -13.632 -23.633  1.00 17.90           O  
ANISOU 2492  O   SER A 322     3660   2387    755    -11   -150    -24       O  
ATOM   2493  CB  SER A 322     -41.951 -13.353 -22.951  1.00 17.92           C  
ANISOU 2493  CB  SER A 322     3558   2588    662   -112   -238    171       C  
ATOM   2494  OG  SER A 322     -41.638 -14.029 -21.762  1.00 18.23           O  
ANISOU 2494  OG  SER A 322     3506   2708    710     44   -189    248       O  
ATOM   2495  N   HIS A 323     -39.006 -12.300 -21.843  1.00 18.26           N  
ANISOU 2495  N   HIS A 323     3394   2599    944    -58   -178     52       N  
ATOM   2496  CA  HIS A 323     -37.725 -12.836 -21.428  1.00 17.70           C  
ANISOU 2496  CA  HIS A 323     3280   2478    966     22    -77    -19       C  
ATOM   2497  C   HIS A 323     -37.881 -14.271 -21.065  1.00 17.67           C  
ANISOU 2497  C   HIS A 323     3378   2499    836    -24   -116     -7       C  
ATOM   2498  O   HIS A 323     -36.939 -15.031 -21.189  1.00 19.54           O  
ANISOU 2498  O   HIS A 323     3621   2522   1282     87      0    164       O  
ATOM   2499  CB  HIS A 323     -37.100 -12.034 -20.279  1.00 17.19           C  
ANISOU 2499  CB  HIS A 323     3251   2590    689      6    145    -18       C  
ATOM   2500  CG  HIS A 323     -37.834 -12.143 -18.955  1.00 17.20           C  
ANISOU 2500  CG  HIS A 323     3236   2517    782     31    214     22       C  
ATOM   2501  ND1 HIS A 323     -39.071 -11.620 -18.755  1.00 17.18           N  
ANISOU 2501  ND1 HIS A 323     3066   2762    698    -93     78    -35       N  
ATOM   2502  CD2 HIS A 323     -37.438 -12.696 -17.746  1.00 17.03           C  
ANISOU 2502  CD2 HIS A 323     3146   2599    725     46    137    -73       C  
ATOM   2503  CE1 HIS A 323     -39.462 -11.865 -17.490  1.00 17.31           C  
ANISOU 2503  CE1 HIS A 323     3169   2655    752    -16     91     97       C  
ATOM   2504  NE2 HIS A 323     -38.454 -12.511 -16.864  1.00 16.81           N  
ANISOU 2504  NE2 HIS A 323     3090   2665    631    115     55    -92       N  
ATOM   2505  N   VAL A 324     -39.067 -14.641 -20.592  1.00 16.72           N  
ANISOU 2505  N   VAL A 324     3394   2397    561    -41   -188   -106       N  
ATOM   2506  CA  VAL A 324     -39.310 -16.001 -20.149  1.00 17.32           C  
ANISOU 2506  CA  VAL A 324     3429   2346    806    -40   -175   -170       C  
ATOM   2507  C   VAL A 324     -39.339 -16.911 -21.371  1.00 17.64           C  
ANISOU 2507  C   VAL A 324     3515   2433    754    174    -92   -176       C  
ATOM   2508  O   VAL A 324     -38.652 -17.944 -21.419  1.00 18.57           O  
ANISOU 2508  O   VAL A 324     3683   2356   1014    177    151    -23       O  
ATOM   2509  CB  VAL A 324     -40.619 -16.095 -19.341  1.00 17.17           C  
ANISOU 2509  CB  VAL A 324     3526   2257    740   -125    -96   -206       C  
ATOM   2510  CG1 VAL A 324     -40.967 -17.545 -19.082  1.00 16.99           C  
ANISOU 2510  CG1 VAL A 324     3421   2223    811    -23     76   -305       C  
ATOM   2511  CG2 VAL A 324     -40.464 -15.363 -18.016  1.00 17.12           C  
ANISOU 2511  CG2 VAL A 324     3425   2466    612    -88   -256   -116       C  
ATOM   2512  N   LEU A 325     -40.116 -16.501 -22.368  1.00 18.07           N  
ANISOU 2512  N   LEU A 325     3532   2595    739      0   -116    -33       N  
ATOM   2513  CA  LEU A 325     -40.234 -17.297 -23.588  1.00 18.24           C  
ANISOU 2513  CA  LEU A 325     3691   2613    625    179   -146     41       C  
ATOM   2514  C   LEU A 325     -38.893 -17.502 -24.294  1.00 19.55           C  
ANISOU 2514  C   LEU A 325     3798   2504   1126    241     16    110       C  
ATOM   2515  O   LEU A 325     -38.612 -18.605 -24.785  1.00 19.10           O  
ANISOU 2515  O   LEU A 325     3893   2679    684    136    106   -102       O  
ATOM   2516  CB  LEU A 325     -41.258 -16.680 -24.546  1.00 18.11           C  
ANISOU 2516  CB  LEU A 325     3611   2666    601    124   -106    130       C  
ATOM   2517  CG  LEU A 325     -42.710 -16.544 -24.061  1.00 18.82           C  
ANISOU 2517  CG  LEU A 325     3626   2681    843     48    -77    273       C  
ATOM   2518  CD1 LEU A 325     -43.595 -16.038 -25.195  1.00 20.07           C  
ANISOU 2518  CD1 LEU A 325     3754   2851   1017     40   -328    106       C  
ATOM   2519  CD2 LEU A 325     -43.264 -17.842 -23.479  1.00 18.79           C  
ANISOU 2519  CD2 LEU A 325     3589   2525   1024    -69     18     -2       C  
ATOM   2520  N   THR A 326     -38.055 -16.461 -24.360  1.00 20.17           N  
ANISOU 2520  N   THR A 326     3807   2773   1083    120     -4    -91       N  
ATOM   2521  CA  THR A 326     -36.766 -16.652 -25.047  1.00 20.68           C  
ANISOU 2521  CA  THR A 326     3941   2894   1021    176    196    439       C  
ATOM   2522  C   THR A 326     -35.799 -17.511 -24.228  1.00 19.37           C  
ANISOU 2522  C   THR A 326     3731   2840    787    228    144     69       C  
ATOM   2523  O   THR A 326     -35.016 -18.277 -24.798  1.00 21.85           O  
ANISOU 2523  O   THR A 326     3848   3063   1389    250    510    -11       O  
ATOM   2524  CB  THR A 326     -36.065 -15.359 -25.523  1.00 22.67           C  
ANISOU 2524  CB  THR A 326     4420   2582   1613    247     76    309       C  
ATOM   2525  OG1 THR A 326     -35.158 -14.894 -24.529  1.00 30.67           O  
ANISOU 2525  OG1 THR A 326     5056   3787   2808   -147   -374     44       O  
ATOM   2526  CG2 THR A 326     -37.047 -14.280 -25.900  1.00 17.98           C  
ANISOU 2526  CG2 THR A 326     3767   2154    911    -35    408    -55       C  
ATOM   2527  N   ALA A 327     -35.880 -17.408 -22.903  1.00 18.33           N  
ANISOU 2527  N   ALA A 327     3663   2516    783    122     55     10       N  
ATOM   2528  CA  ALA A 327     -35.047 -18.231 -22.025  1.00 18.56           C  
ANISOU 2528  CA  ALA A 327     3705   2590    755    193    108     47       C  
ATOM   2529  C   ALA A 327     -35.342 -19.719 -22.195  1.00 19.40           C  
ANISOU 2529  C   ALA A 327     3915   2548    906    301     69    -77       C  
ATOM   2530  O   ALA A 327     -34.431 -20.551 -22.105  1.00 19.30           O  
ANISOU 2530  O   ALA A 327     3750   2673    909    300    139    -70       O  
ATOM   2531  CB  ALA A 327     -35.250 -17.826 -20.583  1.00 19.12           C  
ANISOU 2531  CB  ALA A 327     3760   2741    763    179    -84    -89       C  
ATOM   2532  N   ILE A 328     -36.615 -20.048 -22.437  1.00 19.58           N  
ANISOU 2532  N   ILE A 328     3909   2628    901    205    337   -144       N  
ATOM   2533  CA  ILE A 328     -37.017 -21.452 -22.605  1.00 19.36           C  
ANISOU 2533  CA  ILE A 328     3944   2528    883    402    274   -241       C  
ATOM   2534  C   ILE A 328     -36.742 -21.940 -24.015  1.00 20.58           C  
ANISOU 2534  C   ILE A 328     4185   2723    909    319    483   -206       C  
ATOM   2535  O   ILE A 328     -36.890 -23.128 -24.324  1.00 22.72           O  
ANISOU 2535  O   ILE A 328     4256   2857   1517     46    443   -431       O  
ATOM   2536  CB  ILE A 328     -38.472 -21.781 -22.174  1.00 19.60           C  
ANISOU 2536  CB  ILE A 328     4034   2632    779    338    201   -203       C  
ATOM   2537  CG1 ILE A 328     -39.535 -21.025 -22.978  1.00 20.07           C  
ANISOU 2537  CG1 ILE A 328     3783   2852    991    272    109   -259       C  
ATOM   2538  CG2 ILE A 328     -38.651 -21.596 -20.670  1.00 19.34           C  
ANISOU 2538  CG2 ILE A 328     3953   2615    778    251    325    -97       C  
ATOM   2539  CD1 ILE A 328     -40.920 -21.583 -22.741  1.00 21.93           C  
ANISOU 2539  CD1 ILE A 328     4106   2676   1548    -60    364   -606       C  
ATOM   2540  N   GLY A 329     -36.327 -21.021 -24.873  1.00 19.72           N  
ANISOU 2540  N   GLY A 329     3938   2743    809    364    358   -187       N  
ATOM   2541  CA  GLY A 329     -35.838 -21.410 -26.184  1.00 21.92           C  
ANISOU 2541  CA  GLY A 329     4144   3068   1115    381    658   -425       C  
ATOM   2542  C   GLY A 329     -36.775 -21.211 -27.356  1.00 20.37           C  
ANISOU 2542  C   GLY A 329     4341   2554    842    104    647   -958       C  
ATOM   2543  O   GLY A 329     -36.515 -21.736 -28.446  1.00 22.95           O  
ANISOU 2543  O   GLY A 329     4648   3059   1013    504    790  -1139       O  
ATOM   2544  N   LEU A 330     -37.847 -20.440 -27.161  1.00 20.81           N  
ANISOU 2544  N   LEU A 330     3962   3027    917    140    467   -147       N  
ATOM   2545  CA  LEU A 330     -38.754 -20.112 -28.263  1.00 21.61           C  
ANISOU 2545  CA  LEU A 330     4164   3073    973    -96    263   -233       C  
ATOM   2546  C   LEU A 330     -38.119 -19.066 -29.163  1.00 21.73           C  
ANISOU 2546  C   LEU A 330     4409   3039    806   -127    159   -230       C  
ATOM   2547  O   LEU A 330     -37.387 -18.199 -28.684  1.00 20.75           O  
ANISOU 2547  O   LEU A 330     4096   2963    822   -173    435    -70       O  
ATOM   2548  CB  LEU A 330     -40.110 -19.609 -27.754  1.00 21.10           C  
ANISOU 2548  CB  LEU A 330     4332   3020    666    -77    445   -400       C  
ATOM   2549  CG  LEU A 330     -40.995 -20.573 -26.955  1.00 23.81           C  
ANISOU 2549  CG  LEU A 330     3923   3174   1949   -427    477   -483       C  
ATOM   2550  CD1 LEU A 330     -42.425 -20.063 -26.906  1.00 23.21           C  
ANISOU 2550  CD1 LEU A 330     3925   2983   1908   -339    164   -237       C  
ATOM   2551  CD2 LEU A 330     -40.957 -21.975 -27.541  1.00 25.35           C  
ANISOU 2551  CD2 LEU A 330     4270   3015   2345    -67    439   -316       C  
ATOM   2552  N   SER A 331     -38.391 -19.162 -30.463  1.00 21.42           N  
ANISOU 2552  N   SER A 331     4608   2831    698     11    383   -176       N  
ATOM   2553  CA  SER A 331     -37.900 -18.172 -31.407  1.00 21.55           C  
ANISOU 2553  CA  SER A 331     4628   2820    739     23     63    -12       C  
ATOM   2554  C   SER A 331     -38.796 -16.962 -31.272  1.00 20.74           C  
ANISOU 2554  C   SER A 331     4315   2839    725   -145    156    -16       C  
ATOM   2555  O   SER A 331     -39.859 -17.041 -30.672  1.00 21.42           O  
ANISOU 2555  O   SER A 331     4387   2916    834    -34    184   -105       O  
ATOM   2556  CB  SER A 331     -37.936 -18.702 -32.843  1.00 21.92           C  
ANISOU 2556  CB  SER A 331     4603   2840    884   -290    200   -198       C  
ATOM   2557  OG  SER A 331     -39.270 -18.975 -33.244  1.00 21.50           O  
ANISOU 2557  OG  SER A 331     4601   3096    471   -106    -40    -50       O  
ATOM   2558  N   GLU A 332     -38.363 -15.857 -31.849  1.00 21.62           N  
ANISOU 2558  N   GLU A 332     4390   2761   1062    -59    214    -19       N  
ATOM   2559  CA  GLU A 332     -39.110 -14.622 -31.833  1.00 20.80           C  
ANISOU 2559  CA  GLU A 332     4148   2596   1158   -295    233   -166       C  
ATOM   2560  C   GLU A 332     -40.437 -14.814 -32.548  1.00 20.91           C  
ANISOU 2560  C   GLU A 332     4373   2918    653   -296    140     12       C  
ATOM   2561  O   GLU A 332     -41.458 -14.305 -32.106  1.00 20.79           O  
ANISOU 2561  O   GLU A 332     4262   2995    641   -294    -45    113       O  
ATOM   2562  CB  GLU A 332     -38.298 -13.520 -32.523  1.00 21.31           C  
ANISOU 2562  CB  GLU A 332     4288   2922    884   -312    153    134       C  
ATOM   2563  CG  GLU A 332     -36.985 -13.136 -31.831  1.00 23.48           C  
ANISOU 2563  CG  GLU A 332     4387   3215   1317   -491    120    -59       C  
ATOM   2564  CD  GLU A 332     -35.790 -13.995 -32.251  1.00 24.67           C  
ANISOU 2564  CD  GLU A 332     4440   3539   1393   -140   -192    -97       C  
ATOM   2565  OE1 GLU A 332     -35.970 -14.995 -32.984  1.00 25.06           O  
ANISOU 2565  OE1 GLU A 332     4476   3137   1906    -83    306    -86       O  
ATOM   2566  OE2 GLU A 332     -34.659 -13.685 -31.838  1.00 27.90           O  
ANISOU 2566  OE2 GLU A 332     4485   3885   2229   -350   -240    112       O  
ATOM   2567  N   ALA A 333     -40.413 -15.538 -33.662  1.00 20.39           N  
ANISOU 2567  N   ALA A 333     4267   2594    884   -223    214    -36       N  
ATOM   2568  CA  ALA A 333     -41.646 -15.829 -34.383  1.00 20.94           C  
ANISOU 2568  CA  ALA A 333     4407   2815    733   -383    177     27       C  
ATOM   2569  C   ALA A 333     -42.610 -16.660 -33.539  1.00 21.18           C  
ANISOU 2569  C   ALA A 333     4309   2887    850   -270    238     41       C  
ATOM   2570  O   ALA A 333     -43.814 -16.414 -33.520  1.00 20.06           O  
ANISOU 2570  O   ALA A 333     4238   2850    530   -321    166    -70       O  
ATOM   2571  CB  ALA A 333     -41.361 -16.510 -35.721  1.00 21.58           C  
ANISOU 2571  CB  ALA A 333     4496   3019    682   -226     98     49       C  
ATOM   2572  N   GLU A 334     -42.079 -17.651 -32.843  1.00 19.83           N  
ANISOU 2572  N   GLU A 334     4276   2608    649   -298    263   -104       N  
ATOM   2573  CA  GLU A 334     -42.903 -18.422 -31.943  1.00 20.02           C  
ANISOU 2573  CA  GLU A 334     4248   2662    693   -160    329    -28       C  
ATOM   2574  C   GLU A 334     -43.440 -17.528 -30.823  1.00 19.55           C  
ANISOU 2574  C   GLU A 334     4203   2708    515   -205    211    -32       C  
ATOM   2575  O   GLU A 334     -44.612 -17.571 -30.496  1.00 19.50           O  
ANISOU 2575  O   GLU A 334     4164   2645    598   -286     93   -128       O  
ATOM   2576  CB  GLU A 334     -42.117 -19.599 -31.371  1.00 21.33           C  
ANISOU 2576  CB  GLU A 334     4370   2633   1099    -18    330   -134       C  
ATOM   2577  CG  GLU A 334     -41.899 -20.752 -32.338  1.00 22.05           C  
ANISOU 2577  CG  GLU A 334     4669   2700   1007    104    391    -92       C  
ATOM   2578  CD  GLU A 334     -40.992 -21.835 -31.790  1.00 24.15           C  
ANISOU 2578  CD  GLU A 334     4890   2876   1411    321    161   -222       C  
ATOM   2579  OE1 GLU A 334     -40.008 -21.520 -31.088  1.00 24.00           O  
ANISOU 2579  OE1 GLU A 334     4952   3101   1066    219    323   -411       O  
ATOM   2580  OE2 GLU A 334     -41.257 -23.017 -32.078  1.00 32.51           O  
ANISOU 2580  OE2 GLU A 334     5810   3330   3211   -393   -416   -614       O  
ATOM   2581  N   ALA A 335     -42.587 -16.680 -30.267  1.00 20.96           N  
ANISOU 2581  N   ALA A 335     4374   2715    874   -380    216     -7       N  
ATOM   2582  CA  ALA A 335     -43.020 -15.801 -29.199  1.00 21.12           C  
ANISOU 2582  CA  ALA A 335     4239   2743   1043   -289    207    -48       C  
ATOM   2583  C   ALA A 335     -44.182 -14.925 -29.650  1.00 21.29           C  
ANISOU 2583  C   ALA A 335     4234   2969    886   -373     89    -67       C  
ATOM   2584  O   ALA A 335     -45.086 -14.644 -28.873  1.00 21.55           O  
ANISOU 2584  O   ALA A 335     4295   2986    905   -261     76     -3       O  
ATOM   2585  CB  ALA A 335     -41.856 -14.954 -28.732  1.00 21.27           C  
ANISOU 2585  CB  ALA A 335     4444   2627   1011   -376    141   -140       C  
ATOM   2586  N   ARG A 336     -44.168 -14.508 -30.912  1.00 21.78           N  
ANISOU 2586  N   ARG A 336     4375   2951    947   -439    -25    -10       N  
ATOM   2587  CA  ARG A 336     -45.250 -13.701 -31.452  1.00 21.64           C  
ANISOU 2587  CA  ARG A 336     4456   2938    827   -396    134    268       C  
ATOM   2588  C   ARG A 336     -46.604 -14.388 -31.356  1.00 21.49           C  
ANISOU 2588  C   ARG A 336     4451   2944    767   -299    242     60       C  
ATOM   2589  O   ARG A 336     -47.615 -13.727 -31.190  1.00 21.38           O  
ANISOU 2589  O   ARG A 336     4348   3152    621   -327    155     91       O  
ATOM   2590  CB  ARG A 336     -44.959 -13.305 -32.917  1.00 23.82           C  
ANISOU 2590  CB  ARG A 336     4667   3385    998   -449    449    383       C  
ATOM   2591  CG  ARG A 336     -43.736 -12.401 -33.084  1.00 25.18           C  
ANISOU 2591  CG  ARG A 336     4873   3240   1455   -557    466    596       C  
ATOM   2592  CD  ARG A 336     -43.689 -11.761 -34.463  1.00 30.10           C  
ANISOU 2592  CD  ARG A 336     5403   4207   1827   -625     60   1203       C  
ATOM   2593  NE  ARG A 336     -45.031 -11.837 -34.995  1.00 36.87           N  
ANISOU 2593  NE  ARG A 336     5981   4699   3328   -595   -681    785       N  
ATOM   2594  CZ  ARG A 336     -45.414 -12.615 -35.997  1.00 29.99           C  
ANISOU 2594  CZ  ARG A 336     5995   3853   1546    229   -170   1402       C  
ATOM   2595  NH1 ARG A 336     -46.684 -12.623 -36.321  1.00 33.11           N  
ANISOU 2595  NH1 ARG A 336     5627   4071   2881   -418    206   1027       N  
ATOM   2596  NH2 ARG A 336     -44.552 -13.357 -36.687  1.00 33.33           N  
ANISOU 2596  NH2 ARG A 336     5506   3748   3407    150    600   1913       N  
ATOM   2597  N   ARG A 337     -46.619 -15.708 -31.475  1.00 20.54           N  
ANISOU 2597  N   ARG A 337     4318   2887    599   -477    193    -24       N  
ATOM   2598  CA  ARG A 337     -47.861 -16.447 -31.436  1.00 21.03           C  
ANISOU 2598  CA  ARG A 337     4272   3063    654   -469    139    -89       C  
ATOM   2599  C   ARG A 337     -48.156 -16.984 -30.052  1.00 20.48           C  
ANISOU 2599  C   ARG A 337     4211   2809    760   -414    118     39       C  
ATOM   2600  O   ARG A 337     -48.974 -17.876 -29.923  1.00 19.04           O  
ANISOU 2600  O   ARG A 337     4066   2726    442   -377   -112    -99       O  
ATOM   2601  CB  ARG A 337     -47.798 -17.645 -32.386  1.00 23.31           C  
ANISOU 2601  CB  ARG A 337     4633   3195   1029   -583    127   -310       C  
ATOM   2602  CG  ARG A 337     -47.038 -17.393 -33.655  1.00 24.46           C  
ANISOU 2602  CG  ARG A 337     4836   3586    871   -530    183   -668       C  
ATOM   2603  CD  ARG A 337     -47.369 -18.450 -34.657  1.00 26.64           C  
ANISOU 2603  CD  ARG A 337     5170   3527   1422   -389   -272   -780       C  
ATOM   2604  NE  ARG A 337     -46.772 -19.741 -34.366  1.00 26.29           N  
ANISOU 2604  NE  ARG A 337     5064   3610   1312   -326     34   -598       N  
ATOM   2605  CZ  ARG A 337     -45.542 -20.082 -34.726  1.00 25.15           C  
ANISOU 2605  CZ  ARG A 337     5047   3105   1402   -376     64   -414       C  
ATOM   2606  NH1 ARG A 337     -44.759 -19.231 -35.387  1.00 22.39           N  
ANISOU 2606  NH1 ARG A 337     4351   2949   1205   -103      9   -424       N  
ATOM   2607  NH2 ARG A 337     -45.103 -21.296 -34.438  1.00 25.02           N  
ANISOU 2607  NH2 ARG A 337     5273   2829   1402   -724   -392   -583       N  
ATOM   2608  N   THR A 338     -47.493 -16.473 -29.024  1.00 19.82           N  
ANISOU 2608  N   THR A 338     4120   2711    697   -347     40    108       N  
ATOM   2609  CA  THR A 338     -47.621 -17.066 -27.708  1.00 18.99           C  
ANISOU 2609  CA  THR A 338     3849   2645    719   -323    247     74       C  
ATOM   2610  C   THR A 338     -48.351 -16.161 -26.737  1.00 18.66           C  
ANISOU 2610  C   THR A 338     3905   2536    646   -290     55     33       C  
ATOM   2611  O   THR A 338     -48.019 -14.989 -26.647  1.00 19.33           O  
ANISOU 2611  O   THR A 338     4053   2502    787   -225    152     99       O  
ATOM   2612  CB  THR A 338     -46.232 -17.391 -27.174  1.00 19.26           C  
ANISOU 2612  CB  THR A 338     4055   2637    622   -216     44    119       C  
ATOM   2613  OG1 THR A 338     -45.624 -18.326 -28.067  1.00 19.29           O  
ANISOU 2613  OG1 THR A 338     4124   2601    604   -189    102    222       O  
ATOM   2614  CG2 THR A 338     -46.335 -18.022 -25.814  1.00 18.03           C  
ANISOU 2614  CG2 THR A 338     3863   2286    701   -317     16    113       C  
ATOM   2615  N   TYR A 339     -49.332 -16.721 -26.026  1.00 18.02           N  
ANISOU 2615  N   TYR A 339     3776   2557    514   -277     16     66       N  
ATOM   2616  CA  TYR A 339     -50.187 -15.989 -25.102  1.00 18.24           C  
ANISOU 2616  CA  TYR A 339     3706   2431    791   -133    -24    121       C  
ATOM   2617  C   TYR A 339     -50.317 -16.711 -23.777  1.00 17.93           C  
ANISOU 2617  C   TYR A 339     3720   2249    843   -238    -40    117       C  
ATOM   2618  O   TYR A 339     -50.418 -17.935 -23.735  1.00 17.28           O  
ANISOU 2618  O   TYR A 339     3729   2216    619   -317   -192   -139       O  
ATOM   2619  CB  TYR A 339     -51.576 -15.818 -25.721  1.00 19.24           C  
ANISOU 2619  CB  TYR A 339     3752   2594    965   -117    -48    215       C  
ATOM   2620  CG  TYR A 339     -51.540 -14.947 -26.944  1.00 20.02           C  
ANISOU 2620  CG  TYR A 339     4037   2618    951   -210    -41    207       C  
ATOM   2621  CD1 TYR A 339     -51.830 -13.585 -26.860  1.00 21.16           C  
ANISOU 2621  CD1 TYR A 339     4148   2631   1260   -132     21    157       C  
ATOM   2622  CD2 TYR A 339     -51.194 -15.480 -28.190  1.00 19.84           C  
ANISOU 2622  CD2 TYR A 339     3952   2769    817   -399    -68    241       C  
ATOM   2623  CE1 TYR A 339     -51.764 -12.769 -27.979  1.00 22.21           C  
ANISOU 2623  CE1 TYR A 339     4397   2773   1267   -389    -67    221       C  
ATOM   2624  CE2 TYR A 339     -51.134 -14.671 -29.313  1.00 21.37           C  
ANISOU 2624  CE2 TYR A 339     4474   2637   1006   -331   -198    326       C  
ATOM   2625  CZ  TYR A 339     -51.425 -13.319 -29.201  1.00 21.66           C  
ANISOU 2625  CZ  TYR A 339     4497   2568   1165   -406    -11    438       C  
ATOM   2626  OH  TYR A 339     -51.385 -12.521 -30.319  1.00 24.09           O  
ANISOU 2626  OH  TYR A 339     4977   3147   1029   -523   -482    580       O  
ATOM   2627  N   ARG A 340     -50.298 -15.947 -22.694  1.00 17.86           N  
ANISOU 2627  N   ARG A 340     3639   2413    730   -353   -154    122       N  
ATOM   2628  CA  ARG A 340     -50.663 -16.471 -21.397  1.00 17.40           C  
ANISOU 2628  CA  ARG A 340     3426   2450    733   -277   -186    147       C  
ATOM   2629  C   ARG A 340     -52.152 -16.233 -21.161  1.00 17.65           C  
ANISOU 2629  C   ARG A 340     3478   2431    794   -343    -44    -66       C  
ATOM   2630  O   ARG A 340     -52.612 -15.096 -21.077  1.00 18.20           O  
ANISOU 2630  O   ARG A 340     3490   2503    921   -208   -230    123       O  
ATOM   2631  CB  ARG A 340     -49.825 -15.835 -20.280  1.00 17.12           C  
ANISOU 2631  CB  ARG A 340     3494   2336    675   -173   -139     44       C  
ATOM   2632  CG  ARG A 340     -50.136 -16.416 -18.901  1.00 16.68           C  
ANISOU 2632  CG  ARG A 340     3288   2408    639   -201   -111      0       C  
ATOM   2633  CD  ARG A 340     -49.531 -15.606 -17.771  1.00 17.42           C  
ANISOU 2633  CD  ARG A 340     3493   2327    796   -121   -172    -90       C  
ATOM   2634  NE  ARG A 340     -50.115 -14.270 -17.706  1.00 17.00           N  
ANISOU 2634  NE  ARG A 340     3630   2261    566   -153   -157    170       N  
ATOM   2635  CZ  ARG A 340     -49.557 -13.247 -17.074  1.00 16.24           C  
ANISOU 2635  CZ  ARG A 340     3277   2402    491    -45    -52     44       C  
ATOM   2636  NH1 ARG A 340     -48.405 -13.421 -16.423  1.00 15.75           N  
ANISOU 2636  NH1 ARG A 340     3131   2584    270     -9     97   -180       N  
ATOM   2637  NH2 ARG A 340     -50.148 -12.051 -17.090  1.00 16.80           N  
ANISOU 2637  NH2 ARG A 340     3284   2341    757   -112    257    -61       N  
ATOM   2638  N   ILE A 341     -52.899 -17.327 -21.078  1.00 17.80           N  
ANISOU 2638  N   ILE A 341     3473   2589    702   -452   -106   -137       N  
ATOM   2639  CA  ILE A 341     -54.309 -17.298 -20.744  1.00 17.91           C  
ANISOU 2639  CA  ILE A 341     3472   2633    697   -396      2     28       C  
ATOM   2640  C   ILE A 341     -54.387 -17.849 -19.323  1.00 17.82           C  
ANISOU 2640  C   ILE A 341     3555   2514    700   -408    -34     -3       C  
ATOM   2641  O   ILE A 341     -54.022 -18.998 -19.090  1.00 17.15           O  
ANISOU 2641  O   ILE A 341     3523   2636    355   -307    -48     79       O  
ATOM   2642  CB  ILE A 341     -55.119 -18.208 -21.696  1.00 17.86           C  
ANISOU 2642  CB  ILE A 341     3456   2556    771   -430    145    -89       C  
ATOM   2643  CG1 ILE A 341     -54.844 -17.849 -23.164  1.00 18.16           C  
ANISOU 2643  CG1 ILE A 341     3666   2466    767   -492     41    -39       C  
ATOM   2644  CG2 ILE A 341     -56.606 -18.133 -21.384  1.00 18.58           C  
ANISOU 2644  CG2 ILE A 341     3391   2790    876   -507    -93   -207       C  
ATOM   2645  CD1 ILE A 341     -55.126 -18.965 -24.148  1.00 20.82           C  
ANISOU 2645  CD1 ILE A 341     3834   3156    921   -665    -13   -443       C  
ATOM   2646  N   SER A 342     -54.842 -17.031 -18.378  1.00 17.12           N  
ANISOU 2646  N   SER A 342     3160   2670    675   -412     15     17       N  
ATOM   2647  CA  SER A 342     -54.894 -17.455 -16.975  1.00 17.20           C  
ANISOU 2647  CA  SER A 342     3216   2631    686   -436   -125     34       C  
ATOM   2648  C   SER A 342     -56.293 -17.385 -16.365  1.00 18.06           C  
ANISOU 2648  C   SER A 342     3268   2847    745   -440    -84      4       C  
ATOM   2649  O   SER A 342     -57.134 -16.601 -16.806  1.00 18.12           O  
ANISOU 2649  O   SER A 342     3399   2724    761   -401    -37     21       O  
ATOM   2650  CB  SER A 342     -53.863 -16.703 -16.133  1.00 16.68           C  
ANISOU 2650  CB  SER A 342     3119   2461    756   -288   -127    -21       C  
ATOM   2651  OG  SER A 342     -53.993 -15.313 -16.261  1.00 15.59           O  
ANISOU 2651  OG  SER A 342     2996   2439    486   -343   -163   -201       O  
ATOM   2652  N   LEU A 343     -56.532 -18.234 -15.369  1.00 17.69           N  
ANISOU 2652  N   LEU A 343     3285   2731    703   -529   -103    -67       N  
ATOM   2653  CA  LEU A 343     -57.871 -18.528 -14.881  1.00 18.23           C  
ANISOU 2653  CA  LEU A 343     3246   2882    796   -405      9   -221       C  
ATOM   2654  C   LEU A 343     -58.019 -18.243 -13.389  1.00 18.24           C  
ANISOU 2654  C   LEU A 343     3223   2996    709   -417    -72    -63       C  
ATOM   2655  O   LEU A 343     -57.023 -18.086 -12.704  1.00 18.02           O  
ANISOU 2655  O   LEU A 343     3219   2752    875   -494     -5   -163       O  
ATOM   2656  CB  LEU A 343     -58.159 -19.998 -15.136  1.00 18.51           C  
ANISOU 2656  CB  LEU A 343     3307   2961    764   -517   -230   -203       C  
ATOM   2657  CG  LEU A 343     -58.328 -20.478 -16.583  1.00 20.17           C  
ANISOU 2657  CG  LEU A 343     3501   3275    888   -413   -163   -470       C  
ATOM   2658  CD1 LEU A 343     -59.544 -19.861 -17.263  1.00 22.81           C  
ANISOU 2658  CD1 LEU A 343     3859   3462   1347   -540   -591    -96       C  
ATOM   2659  CD2 LEU A 343     -57.089 -20.355 -17.465  1.00 21.33           C  
ANISOU 2659  CD2 LEU A 343     3752   3131   1221   -505     48   -117       C  
ATOM   2660  N   PRO A 344     -59.258 -18.160 -12.888  1.00 18.37           N  
ANISOU 2660  N   PRO A 344     3115   3099    762   -539   -151   -146       N  
ATOM   2661  CA  PRO A 344     -59.415 -17.848 -11.474  1.00 18.11           C  
ANISOU 2661  CA  PRO A 344     3237   2876    767   -576   -118   -153       C  
ATOM   2662  C   PRO A 344     -58.687 -18.865 -10.597  1.00 18.79           C  
ANISOU 2662  C   PRO A 344     3394   2830    915   -492   -170   -155       C  
ATOM   2663  O   PRO A 344     -58.953 -20.038 -10.704  1.00 19.09           O  
ANISOU 2663  O   PRO A 344     3602   2807    844   -531   -131   -300       O  
ATOM   2664  CB  PRO A 344     -60.919 -17.956 -11.274  1.00 19.45           C  
ANISOU 2664  CB  PRO A 344     3225   3195    969   -576   -113    -52       C  
ATOM   2665  CG  PRO A 344     -61.479 -17.573 -12.615  1.00 19.90           C  
ANISOU 2665  CG  PRO A 344     3260   3346    955   -411    -82   -166       C  
ATOM   2666  CD  PRO A 344     -60.551 -18.175 -13.602  1.00 18.39           C  
ANISOU 2666  CD  PRO A 344     3184   3142    659   -541   -217   -175       C  
ATOM   2667  N   PRO A 345     -57.773 -18.380  -9.735  1.00 17.55           N  
ANISOU 2667  N   PRO A 345     3149   2727    791   -439    -33    -20       N  
ATOM   2668  CA  PRO A 345     -56.985 -19.247  -8.884  1.00 17.26           C  
ANISOU 2668  CA  PRO A 345     3346   2798    413   -455    -59    -52       C  
ATOM   2669  C   PRO A 345     -57.845 -19.977  -7.876  1.00 18.38           C  
ANISOU 2669  C   PRO A 345     3459   2753    771   -505     57     30       C  
ATOM   2670  O   PRO A 345     -58.878 -19.470  -7.457  1.00 19.21           O  
ANISOU 2670  O   PRO A 345     3459   2901    936   -424     59     29       O  
ATOM   2671  CB  PRO A 345     -56.085 -18.276  -8.133  1.00 17.68           C  
ANISOU 2671  CB  PRO A 345     3262   2537    916   -546     44    145       C  
ATOM   2672  CG  PRO A 345     -55.976 -17.072  -8.996  1.00 17.08           C  
ANISOU 2672  CG  PRO A 345     3125   2760    604   -313   -146    261       C  
ATOM   2673  CD  PRO A 345     -57.306 -16.983  -9.694  1.00 16.99           C  
ANISOU 2673  CD  PRO A 345     3033   2760    659   -484   -219    -61       C  
ATOM   2674  N   TYR A 346     -57.432 -21.165  -7.493  1.00 19.16           N  
ANISOU 2674  N   TYR A 346     3553   2695   1029   -526    191     85       N  
ATOM   2675  CA  TYR A 346     -58.165 -21.895  -6.468  1.00 20.58           C  
ANISOU 2675  CA  TYR A 346     3727   2850   1243   -608    200    265       C  
ATOM   2676  C   TYR A 346     -57.198 -22.872  -5.863  1.00 21.10           C  
ANISOU 2676  C   TYR A 346     3765   2875   1375   -520     62    101       C  
ATOM   2677  O   TYR A 346     -56.117 -23.091  -6.382  1.00 20.58           O  
ANISOU 2677  O   TYR A 346     3787   2854   1177   -549    -40     88       O  
ATOM   2678  CB  TYR A 346     -59.357 -22.636  -7.046  1.00 22.06           C  
ANISOU 2678  CB  TYR A 346     3916   2985   1480   -653    103      1       C  
ATOM   2679  CG  TYR A 346     -58.997 -23.761  -7.972  1.00 22.52           C  
ANISOU 2679  CG  TYR A 346     4009   3106   1441   -770    -16   -171       C  
ATOM   2680  CD1 TYR A 346     -58.760 -23.522  -9.323  1.00 23.22           C  
ANISOU 2680  CD1 TYR A 346     4116   3234   1473   -666   -140     30       C  
ATOM   2681  CD2 TYR A 346     -58.916 -25.071  -7.494  1.00 24.58           C  
ANISOU 2681  CD2 TYR A 346     4166   3176   1997   -791   -216    -24       C  
ATOM   2682  CE1 TYR A 346     -58.421 -24.554 -10.167  1.00 26.53           C  
ANISOU 2682  CE1 TYR A 346     4636   3404   2040   -701    143   -257       C  
ATOM   2683  CE2 TYR A 346     -58.607 -26.103  -8.340  1.00 26.72           C  
ANISOU 2683  CE2 TYR A 346     4303   3486   2362   -675    -51   -243       C  
ATOM   2684  CZ  TYR A 346     -58.318 -25.849  -9.672  1.00 27.93           C  
ANISOU 2684  CZ  TYR A 346     4799   3441   2371   -443   -120   -275       C  
ATOM   2685  OH  TYR A 346     -57.985 -26.820 -10.582  1.00 30.46           O  
ANISOU 2685  OH  TYR A 346     5422   3852   2298   -392   -186   -471       O  
ATOM   2686  N   LYS A 347     -57.595 -23.499  -4.772  1.00 20.94           N  
ANISOU 2686  N   LYS A 347     3936   2715   1303   -578   -135    163       N  
ATOM   2687  CA  LYS A 347     -56.706 -24.442  -4.139  1.00 22.38           C  
ANISOU 2687  CA  LYS A 347     3885   3102   1517   -425   -104     94       C  
ATOM   2688  C   LYS A 347     -56.728 -25.753  -4.834  1.00 25.69           C  
ANISOU 2688  C   LYS A 347     4462   3205   2092   -465    -61     86       C  
ATOM   2689  O   LYS A 347     -57.719 -26.538  -4.698  1.00 26.29           O  
ANISOU 2689  O   LYS A 347     4594   3082   2311   -700   -591    -31       O  
ATOM   2690  CB  LYS A 347     -57.023 -24.645  -2.655  1.00 23.97           C  
ANISOU 2690  CB  LYS A 347     4365   3163   1578   -436    -92    538       C  
ATOM   2691  CG  LYS A 347     -55.919 -25.404  -1.939  1.00 26.66           C  
ANISOU 2691  CG  LYS A 347     4386   3394   2349   -246   -239    313       C  
ATOM   2692  CD  LYS A 347     -56.379 -25.840  -0.560  1.00 32.06           C  
ANISOU 2692  CD  LYS A 347     5403   4400   2379   -136   -273    671       C  
ATOM   2693  CE  LYS A 347     -55.194 -26.260   0.289  1.00 36.48           C  
ANISOU 2693  CE  LYS A 347     5344   4421   4096     63   -983     -9       C  
ATOM   2694  NZ  LYS A 347     -54.388 -27.304  -0.399  1.00 37.74           N  
ANISOU 2694  NZ  LYS A 347     5564   4320   4456    479   -910    586       N  
ATOM   2695  N   VAL A 348     -55.638 -25.982  -5.576  1.00 26.51           N  
ANISOU 2695  N   VAL A 348     4325   3399   2348   -284   -184    183       N  
ATOM   2696  CA  VAL A 348     -55.195 -27.317  -5.945  1.00 32.35           C  
ANISOU 2696  CA  VAL A 348     4889   3823   3578   -369    -93   -439       C  
ATOM   2697  C   VAL A 348     -55.057 -27.531  -7.425  1.00 37.03           C  
ANISOU 2697  C   VAL A 348     5288   5218   3563    -96     83   -175       C  
ATOM   2698  O   VAL A 348     -53.963 -27.513  -7.845  1.00 42.29           O  
ANISOU 2698  O   VAL A 348     5208   5928   4931   -169    376    -56       O  
ATOM   2699  CB  VAL A 348     -56.001 -28.507  -5.307  1.00 34.17           C  
ANISOU 2699  CB  VAL A 348     5779   3655   3546   -480   -163   -217       C  
ATOM   2700  CG1 VAL A 348     -56.291 -29.671  -6.277  1.00 34.23           C  
ANISOU 2700  CG1 VAL A 348     5571   3447   3986    -79   -294   -330       C  
ATOM   2701  CG2 VAL A 348     -55.194 -28.979  -4.162  1.00 35.58           C  
ANISOU 2701  CG2 VAL A 348     5269   3735   4513    186   -456   -423       C  
ATOM   2702  OXT VAL A 348     -56.018 -27.717  -8.184  1.00 42.69           O  
ANISOU 2702  OXT VAL A 348     5789   5731   4700   -483   -360     25       O  
TER    2703      VAL A 348                                                      
ATOM   2704  N   THR B   2     -53.655 -40.746  15.922  0.30 27.66           N  
ANISOU 2704  N   THR B   2     4651   4198   1659    -90   -199   -338       N  
ATOM   2705  CA  THR B   2     -52.353 -40.706  16.589  0.30 26.93           C  
ANISOU 2705  CA  THR B   2     4471   3958   1802    -85   -119   -204       C  
ATOM   2706  C   THR B   2     -51.369 -40.243  15.549  0.30 27.10           C  
ANISOU 2706  C   THR B   2     4270   4174   1852    -79   -149   -253       C  
ATOM   2707  O   THR B   2     -51.728 -39.479  14.664  0.30 28.70           O  
ANISOU 2707  O   THR B   2     4093   4530   2280    113   -111      9       O  
ATOM   2708  CB  THR B   2     -51.980 -42.092  17.064  0.30 27.73           C  
ANISOU 2708  CB  THR B   2     4663   3837   2035   -123    -84   -328       C  
ATOM   2709  N   LYS B   3     -50.151 -40.741  15.645  1.00 25.18           N  
ANISOU 2709  N   LYS B   3     4357   4046   1164   -112   -232    -74       N  
ATOM   2710  CA  LYS B   3     -49.755 -41.546  16.792  1.00 23.64           C  
ANISOU 2710  CA  LYS B   3     4338   3564   1079   -145   -586   -472       C  
ATOM   2711  C   LYS B   3     -48.566 -40.868  17.408  1.00 21.10           C  
ANISOU 2711  C   LYS B   3     3690   3307   1018    -77   -114   -323       C  
ATOM   2712  O   LYS B   3     -47.653 -40.458  16.722  1.00 19.80           O  
ANISOU 2712  O   LYS B   3     3599   3260    663    148   -191   -362       O  
ATOM   2713  CB  LYS B   3     -49.428 -42.992  16.413  1.00 27.29           C  
ANISOU 2713  CB  LYS B   3     4598   3503   2267    -22    -48   -180       C  
ATOM   2714  CG  LYS B   3     -49.777 -43.997  17.518  1.00 30.29           C  
ANISOU 2714  CG  LYS B   3     5148   4200   2159   -309   -152      2       C  
ATOM   2715  CD  LYS B   3     -49.638 -45.452  17.053  1.00 37.20           C  
ANISOU 2715  CD  LYS B   3     6105   4153   3874     46     64     15       C  
ATOM   2716  CE  LYS B   3     -49.491 -46.431  18.221  1.00 36.95           C  
ANISOU 2716  CE  LYS B   3     5747   4689   3601    154   -295    -72       C  
ATOM   2717  NZ  LYS B   3     -49.003 -47.798  17.842  1.00 39.83           N  
ANISOU 2717  NZ  LYS B   3     6355   4508   4268     71   -784   -202       N  
ATOM   2718  N   TYR B   4     -48.583 -40.747  18.721  1.00 19.93           N  
ANISOU 2718  N   TYR B   4     3600   2913   1058   -109    102   -592       N  
ATOM   2719  CA  TYR B   4     -47.554 -39.978  19.402  1.00 19.10           C  
ANISOU 2719  CA  TYR B   4     3241   3068    946     45    134   -582       C  
ATOM   2720  C   TYR B   4     -46.331 -40.840  19.620  1.00 18.42           C  
ANISOU 2720  C   TYR B   4     3415   2692    891     32    133   -421       C  
ATOM   2721  O   TYR B   4     -46.398 -41.855  20.290  1.00 18.94           O  
ANISOU 2721  O   TYR B   4     3444   2791    961   -105    129   -395       O  
ATOM   2722  CB  TYR B   4     -48.098 -39.500  20.739  1.00 18.46           C  
ANISOU 2722  CB  TYR B   4     3378   2723    910   -127    248   -458       C  
ATOM   2723  CG  TYR B   4     -47.200 -38.586  21.516  1.00 17.71           C  
ANISOU 2723  CG  TYR B   4     3349   2729    649   -107    251   -392       C  
ATOM   2724  CD1 TYR B   4     -47.324 -37.215  21.404  1.00 18.33           C  
ANISOU 2724  CD1 TYR B   4     3359   2660    944   -476    268   -291       C  
ATOM   2725  CD2 TYR B   4     -46.256 -39.091  22.386  1.00 18.16           C  
ANISOU 2725  CD2 TYR B   4     3171   2713   1013   -187    225   -235       C  
ATOM   2726  CE1 TYR B   4     -46.531 -36.364  22.139  1.00 16.03           C  
ANISOU 2726  CE1 TYR B   4     2974   2747    370   -256    353   -261       C  
ATOM   2727  CE2 TYR B   4     -45.453 -38.245  23.126  1.00 16.66           C  
ANISOU 2727  CE2 TYR B   4     3075   2622    630    -37    226   -185       C  
ATOM   2728  CZ  TYR B   4     -45.585 -36.883  22.987  1.00 17.07           C  
ANISOU 2728  CZ  TYR B   4     3101   2607    777   -158    186   -253       C  
ATOM   2729  OH  TYR B   4     -44.797 -36.027  23.728  1.00 16.96           O  
ANISOU 2729  OH  TYR B   4     2937   2769    737    -66    -86    -47       O  
ATOM   2730  N   PHE B   5     -45.209 -40.431  19.062  1.00 17.25           N  
ANISOU 2730  N   PHE B   5     3335   2611    604     87     37   -379       N  
ATOM   2731  CA  PHE B   5     -44.015 -41.201  19.207  1.00 18.45           C  
ANISOU 2731  CA  PHE B   5     3322   2575   1112    144    250   -856       C  
ATOM   2732  C   PHE B   5     -42.942 -40.225  19.645  1.00 17.50           C  
ANISOU 2732  C   PHE B   5     3250   2430    969    170    158   -357       C  
ATOM   2733  O   PHE B   5     -41.824 -40.262  19.147  1.00 16.41           O  
ANISOU 2733  O   PHE B   5     3286   2512    437    149     81   -246       O  
ATOM   2734  CB  PHE B   5     -43.646 -41.857  17.866  1.00 17.80           C  
ANISOU 2734  CB  PHE B   5     3343   2661    759     91    356   -480       C  
ATOM   2735  CG  PHE B   5     -44.337 -43.162  17.602  1.00 18.52           C  
ANISOU 2735  CG  PHE B   5     3429   2711    896     91    317   -507       C  
ATOM   2736  CD1 PHE B   5     -43.769 -44.334  18.021  1.00 21.42           C  
ANISOU 2736  CD1 PHE B   5     3660   2896   1581     12     52   -214       C  
ATOM   2737  CD2 PHE B   5     -45.535 -43.222  16.914  1.00 19.42           C  
ANISOU 2737  CD2 PHE B   5     3653   2975    751    112    132   -480       C  
ATOM   2738  CE1 PHE B   5     -44.382 -45.546  17.771  1.00 23.17           C  
ANISOU 2738  CE1 PHE B   5     4041   2904   1855     36    -66   -392       C  
ATOM   2739  CE2 PHE B   5     -46.153 -44.430  16.669  1.00 21.13           C  
ANISOU 2739  CE2 PHE B   5     3976   2922   1128     86     89   -387       C  
ATOM   2740  CZ  PHE B   5     -45.573 -45.599  17.091  1.00 22.50           C  
ANISOU 2740  CZ  PHE B   5     4013   2999   1534     91     -1   -350       C  
ATOM   2741  N   ASP B   6     -43.284 -39.319  20.556  1.00 15.82           N  
ANISOU 2741  N   ASP B   6     3197   2396    414     31    109   -151       N  
ATOM   2742  CA  ASP B   6     -42.339 -38.272  20.900  1.00 16.49           C  
ANISOU 2742  CA  ASP B   6     3044   2507    712     79    103   -103       C  
ATOM   2743  C   ASP B   6     -42.174 -38.202  22.407  1.00 16.59           C  
ANISOU 2743  C   ASP B   6     3095   2480    726    185    126   -117       C  
ATOM   2744  O   ASP B   6     -42.204 -37.128  22.982  1.00 16.00           O  
ANISOU 2744  O   ASP B   6     3076   2574    429     65    198    -71       O  
ATOM   2745  CB  ASP B   6     -42.818 -36.936  20.328  1.00 16.74           C  
ANISOU 2745  CB  ASP B   6     2941   2478    939     93     85   -195       C  
ATOM   2746  CG  ASP B   6     -41.715 -35.903  20.234  1.00 17.24           C  
ANISOU 2746  CG  ASP B   6     2990   2460   1099    150     41    -53       C  
ATOM   2747  OD1 ASP B   6     -40.555 -36.178  20.151  1.00 15.91           O  
ANISOU 2747  OD1 ASP B   6     2994   2433    619    349    212     17       O  
ATOM   2748  OD2 ASP B   6     -41.970 -34.743  20.247  1.00 16.15           O  
ANISOU 2748  OD2 ASP B   6     2920   2456    759    169    -76   -114       O  
ATOM   2749  N   TYR B   7     -42.029 -39.364  23.032  1.00 16.71           N  
ANISOU 2749  N   TYR B   7     3155   2523    667    168    114    -35       N  
ATOM   2750  CA  TYR B   7     -41.900 -39.424  24.477  1.00 15.95           C  
ANISOU 2750  CA  TYR B   7     3121   2259    677    139     70   -126       C  
ATOM   2751  C   TYR B   7     -40.574 -38.883  25.052  1.00 17.00           C  
ANISOU 2751  C   TYR B   7     3081   2584    793    188    -13      9       C  
ATOM   2752  O   TYR B   7     -40.581 -38.538  26.219  1.00 17.53           O  
ANISOU 2752  O   TYR B   7     3235   2643    784     27     49     45       O  
ATOM   2753  CB  TYR B   7     -42.241 -40.827  25.039  1.00 15.60           C  
ANISOU 2753  CB  TYR B   7     3093   2416    417     41     33   -102       C  
ATOM   2754  CG  TYR B   7     -43.630 -41.359  24.730  1.00 17.32           C  
ANISOU 2754  CG  TYR B   7     3206   2558    816   -106    152   -161       C  
ATOM   2755  CD1 TYR B   7     -44.675 -41.196  25.634  1.00 18.25           C  
ANISOU 2755  CD1 TYR B   7     3030   2674   1231    -59    189   -184       C  
ATOM   2756  CD2 TYR B   7     -43.892 -42.023  23.535  1.00 17.59           C  
ANISOU 2756  CD2 TYR B   7     3344   2447    890    -91     85   -178       C  
ATOM   2757  CE1 TYR B   7     -45.939 -41.672  25.353  1.00 19.12           C  
ANISOU 2757  CE1 TYR B   7     3208   2790   1266   -199     -4   -200       C  
ATOM   2758  CE2 TYR B   7     -45.155 -42.498  23.244  1.00 17.99           C  
ANISOU 2758  CE2 TYR B   7     3392   2516    928   -153     44   -122       C  
ATOM   2759  CZ  TYR B   7     -46.168 -42.322  24.159  1.00 19.11           C  
ANISOU 2759  CZ  TYR B   7     3266   2747   1246   -139     74   -204       C  
ATOM   2760  OH  TYR B   7     -47.409 -42.818  23.864  1.00 22.64           O  
ANISOU 2760  OH  TYR B   7     3452   3174   1976   -301   -228    -24       O  
ATOM   2761  N   ALA B   8     -39.481 -38.774  24.290  1.00 16.92           N  
ANISOU 2761  N   ALA B   8     3091   2445    891    188    119    168       N  
ATOM   2762  CA  ALA B   8     -38.258 -38.181  24.814  1.00 16.58           C  
ANISOU 2762  CA  ALA B   8     3151   2544    601    240     -9    -92       C  
ATOM   2763  C   ALA B   8     -38.478 -36.698  25.044  1.00 16.37           C  
ANISOU 2763  C   ALA B   8     3064   2554    598    261      3    -36       C  
ATOM   2764  O   ALA B   8     -37.723 -36.085  25.783  1.00 16.55           O  
ANISOU 2764  O   ALA B   8     3135   2558    593    152     -5    -49       O  
ATOM   2765  CB  ALA B   8     -37.100 -38.396  23.850  1.00 16.72           C  
ANISOU 2765  CB  ALA B   8     3151   2635    566    224     50    -43       C  
ATOM   2766  N   ALA B   9     -39.494 -36.124  24.398  1.00 15.85           N  
ANISOU 2766  N   ALA B   9     2800   2549    670    319    247   -129       N  
ATOM   2767  CA  ALA B   9     -39.843 -34.701  24.570  1.00 15.38           C  
ANISOU 2767  CA  ALA B   9     2810   2420    612    265    204    -43       C  
ATOM   2768  C   ALA B   9     -40.828 -34.426  25.722  1.00 15.66           C  
ANISOU 2768  C   ALA B   9     2848   2534    566    107    193   -158       C  
ATOM   2769  O   ALA B   9     -40.656 -33.461  26.462  1.00 15.55           O  
ANISOU 2769  O   ALA B   9     3046   2520    342    283    104   -124       O  
ATOM   2770  CB  ALA B   9     -40.371 -34.115  23.268  1.00 15.00           C  
ANISOU 2770  CB  ALA B   9     2748   2298    652    229    159    -60       C  
ATOM   2771  N   SER B  10     -41.865 -35.244  25.840  1.00 15.35           N  
ANISOU 2771  N   SER B  10     2719   2553    559    108    142    -82       N  
ATOM   2772  CA  SER B  10     -42.695 -35.244  27.022  1.00 15.07           C  
ANISOU 2772  CA  SER B  10     2734   2451    540    140    116   -192       C  
ATOM   2773  C   SER B  10     -43.523 -36.501  27.080  1.00 15.92           C  
ANISOU 2773  C   SER B  10     2743   2492    812     68    215   -187       C  
ATOM   2774  O   SER B  10     -43.756 -37.155  26.061  1.00 16.95           O  
ANISOU 2774  O   SER B  10     3085   2630    725     57     87   -126       O  
ATOM   2775  CB  SER B  10     -43.630 -34.044  27.088  1.00 16.28           C  
ANISOU 2775  CB  SER B  10     2874   2454    858    202    405   -174       C  
ATOM   2776  OG  SER B  10     -44.073 -33.916  28.430  1.00 15.75           O  
ANISOU 2776  OG  SER B  10     2804   2432    745    171    219   -200       O  
ATOM   2777  N   THR B  11     -43.990 -36.810  28.287  1.00 15.35           N  
ANISOU 2777  N   THR B  11     2870   2367    593     91    -38   -210       N  
ATOM   2778  CA  THR B  11     -44.798 -37.999  28.563  1.00 15.73           C  
ANISOU 2778  CA  THR B  11     2960   2464    550     83    115   -165       C  
ATOM   2779  C   THR B  11     -46.133 -37.621  29.184  1.00 15.91           C  
ANISOU 2779  C   THR B  11     2971   2532    542     16    149   -147       C  
ATOM   2780  O   THR B  11     -46.278 -36.537  29.724  1.00 16.30           O  
ANISOU 2780  O   THR B  11     2939   2536    717    178    254   -166       O  
ATOM   2781  CB  THR B  11     -44.085 -38.937  29.558  1.00 15.88           C  
ANISOU 2781  CB  THR B  11     2950   2381    701     94      1   -261       C  
ATOM   2782  OG1 THR B  11     -43.780 -38.217  30.757  1.00 15.54           O  
ANISOU 2782  OG1 THR B  11     2887   2454    564    210    162   -281       O  
ATOM   2783  CG2 THR B  11     -42.804 -39.460  28.963  1.00 16.12           C  
ANISOU 2783  CG2 THR B  11     3038   2467    618    130    101   -195       C  
ATOM   2784  N   PRO B  12     -47.112 -38.511  29.090  1.00 15.81           N  
ANISOU 2784  N   PRO B  12     3170   2339    497     -6    168   -110       N  
ATOM   2785  CA  PRO B  12     -48.422 -38.263  29.694  1.00 17.02           C  
ANISOU 2785  CA  PRO B  12     2976   2648    843      6     33    -18       C  
ATOM   2786  C   PRO B  12     -48.410 -38.513  31.194  1.00 18.15           C  
ANISOU 2786  C   PRO B  12     3356   2721    818      6     89    -60       C  
ATOM   2787  O   PRO B  12     -47.766 -39.448  31.640  1.00 17.94           O  
ANISOU 2787  O   PRO B  12     3351   2631    832     53    193   -131       O  
ATOM   2788  CB  PRO B  12     -49.309 -39.300  29.013  1.00 17.76           C  
ANISOU 2788  CB  PRO B  12     3246   2630    872     17    231   -340       C  
ATOM   2789  CG  PRO B  12     -48.379 -40.417  28.654  1.00 17.32           C  
ANISOU 2789  CG  PRO B  12     3089   2561    930     70    157    -99       C  
ATOM   2790  CD  PRO B  12     -47.039 -39.799  28.383  1.00 15.48           C  
ANISOU 2790  CD  PRO B  12     3160   2315    406    -44     62    -94       C  
ATOM   2791  N   VAL B  13     -49.121 -37.701  31.964  1.00 18.87           N  
ANISOU 2791  N   VAL B  13     3486   2892    792    -12    238     40       N  
ATOM   2792  CA  VAL B  13     -49.229 -37.959  33.386  1.00 19.05           C  
ANISOU 2792  CA  VAL B  13     3527   2978    733    152     14     -3       C  
ATOM   2793  C   VAL B  13     -49.998 -39.255  33.628  1.00 21.22           C  
ANISOU 2793  C   VAL B  13     3832   3281    950   -194    -10     26       C  
ATOM   2794  O   VAL B  13     -51.072 -39.446  33.071  1.00 22.33           O  
ANISOU 2794  O   VAL B  13     4084   3360   1039   -261   -141   -221       O  
ATOM   2795  CB  VAL B  13     -49.982 -36.812  34.066  1.00 19.25           C  
ANISOU 2795  CB  VAL B  13     3682   2871    760    -65     98   -145       C  
ATOM   2796  CG1 VAL B  13     -50.205 -37.111  35.535  1.00 21.05           C  
ANISOU 2796  CG1 VAL B  13     3919   3285    792   -203     13     -1       C  
ATOM   2797  CG2 VAL B  13     -49.211 -35.521  33.887  1.00 18.18           C  
ANISOU 2797  CG2 VAL B  13     3310   2682    914    162    -49   -107       C  
ATOM   2798  N   ALA B  14     -49.463 -40.120  34.487  1.00 21.64           N  
ANISOU 2798  N   ALA B  14     4042   3305    873   -200    135    107       N  
ATOM   2799  CA  ALA B  14     -50.100 -41.394  34.827  1.00 25.83           C  
ANISOU 2799  CA  ALA B  14     4665   3405   1742   -566   -203   -101       C  
ATOM   2800  C   ALA B  14     -51.387 -41.156  35.629  1.00 27.67           C  
ANISOU 2800  C   ALA B  14     4445   3943   2124   -560    -89     92       C  
ATOM   2801  O   ALA B  14     -51.505 -40.134  36.300  1.00 28.14           O  
ANISOU 2801  O   ALA B  14     4927   4367   1398   -621   -392   -174       O  
ATOM   2802  CB  ALA B  14     -49.116 -42.242  35.605  1.00 28.23           C  
ANISOU 2802  CB  ALA B  14     4752   3765   2206   -349   -194    142       C  
ATOM   2803  N   LYS B  15     -52.334 -42.077  35.524  1.00 28.38           N  
ANISOU 2803  N   LYS B  15     4743   4071   1969   -703   -216    191       N  
ATOM   2804  CA  LYS B  15     -53.659 -41.854  36.118  1.00 33.30           C  
ANISOU 2804  CA  LYS B  15     4561   5584   2504   -860   -232    133       C  
ATOM   2805  C   LYS B  15     -53.646 -41.690  37.644  1.00 32.51           C  
ANISOU 2805  C   LYS B  15     4926   5022   2401   -594   -430    386       C  
ATOM   2806  O   LYS B  15     -54.313 -40.859  38.231  1.00 35.59           O  
ANISOU 2806  O   LYS B  15     5724   4994   2803   -733   -408   -263       O  
ATOM   2807  CB  LYS B  15     -54.647 -42.953  35.748  1.00 36.53           C  
ANISOU 2807  CB  LYS B  15     5207   5315   3358   -782   -775     22       C  
ATOM   2808  CG  LYS B  15     -56.052 -42.589  36.255  1.00 40.35           C  
ANISOU 2808  CG  LYS B  15     5245   6101   3983   -661   -631    421       C  
ATOM   2809  CD  LYS B  15     -56.379 -41.122  35.943  1.00 46.72           C  
ANISOU 2809  CD  LYS B  15     6055   6319   5378    188   -676    254       C  
ATOM   2810  CE  LYS B  15     -57.870 -40.880  35.689  1.00 51.97           C  
ANISOU 2810  CE  LYS B  15     6285   6748   6710    896   -785    300       C  
ATOM   2811  NZ  LYS B  15     -58.064 -39.613  34.946  1.00 58.36           N  
ANISOU 2811  NZ  LYS B  15     7648   6780   7744   1695   -435    477       N  
ATOM   2812  N   GLY B  16     -52.779 -42.496  38.242  1.00 30.61           N  
ANISOU 2812  N   GLY B  16     4966   5025   1637   -975   -771    289       N  
ATOM   2813  CA  GLY B  16     -52.446 -42.401  39.681  1.00 28.87           C  
ANISOU 2813  CA  GLY B  16     5423   4270   1276   -760    -20   -112       C  
ATOM   2814  C   GLY B  16     -51.735 -41.117  40.113  1.00 29.68           C  
ANISOU 2814  C   GLY B  16     5126   4418   1731   -742     59   -414       C  
ATOM   2815  O   GLY B  16     -52.019 -40.600  41.215  1.00 29.30           O  
ANISOU 2815  O   GLY B  16     5217   4534   1381   -642    145   -153       O  
ATOM   2816  N   VAL B  17     -50.894 -40.575  39.232  1.00 28.72           N  
ANISOU 2816  N   VAL B  17     5246   4294   1372   -473    -62     26       N  
ATOM   2817  CA  VAL B  17     -50.244 -39.281  39.466  1.00 28.69           C  
ANISOU 2817  CA  VAL B  17     4840   4161   1897   -493    -36    177       C  
ATOM   2818  C   VAL B  17     -51.267 -38.148  39.514  1.00 29.51           C  
ANISOU 2818  C   VAL B  17     4938   4361   1912   -336   -366   -611       C  
ATOM   2819  O   VAL B  17     -51.290 -37.375  40.485  1.00 28.96           O  
ANISOU 2819  O   VAL B  17     4629   4614   1758   -535   -316   -664       O  
ATOM   2820  CB  VAL B  17     -49.163 -38.977  38.400  1.00 25.53           C  
ANISOU 2820  CB  VAL B  17     4518   3707   1474   -224   -157    -99       C  
ATOM   2821  CG1 VAL B  17     -48.604 -37.561  38.545  1.00 25.09           C  
ANISOU 2821  CG1 VAL B  17     4494   3605   1431   -200   -132   -376       C  
ATOM   2822  CG2 VAL B  17     -48.059 -40.012  38.456  1.00 23.58           C  
ANISOU 2822  CG2 VAL B  17     4601   3324   1033   -276      4    -29       C  
ATOM   2823  N   LEU B  18     -52.144 -38.060  38.503  1.00 29.76           N  
ANISOU 2823  N   LEU B  18     5083   4346   1876   -800   -520   -516       N  
ATOM   2824  CA  LEU B  18     -53.191 -37.026  38.491  1.00 32.66           C  
ANISOU 2824  CA  LEU B  18     5117   5002   2290   -506  -1124   -538       C  
ATOM   2825  C   LEU B  18     -54.075 -37.062  39.751  1.00 32.53           C  
ANISOU 2825  C   LEU B  18     4934   4574   2851   -608   -797   -442       C  
ATOM   2826  O   LEU B  18     -54.403 -36.071  40.349  1.00 33.18           O  
ANISOU 2826  O   LEU B  18     4791   4925   2890   -413   -585   -538       O  
ATOM   2827  CB  LEU B  18     -54.075 -37.165  37.250  1.00 32.76           C  
ANISOU 2827  CB  LEU B  18     5843   5129   1475   -625   -811   -614       C  
ATOM   2828  CG  LEU B  18     -54.153 -35.985  36.294  1.00 34.79           C  
ANISOU 2828  CG  LEU B  18     5962   5357   1897   -315   -621   -260       C  
ATOM   2829  CD1 LEU B  18     -55.241 -36.261  35.262  1.00 34.51           C  
ANISOU 2829  CD1 LEU B  18     6019   5657   1436   -134   -573   -180       C  
ATOM   2830  CD2 LEU B  18     -54.406 -34.646  36.972  1.00 36.29           C  
ANISOU 2830  CD2 LEU B  18     6181   5803   1804   -568   -843   -758       C  
ATOM   2831  N   GLU B  19     -54.449 -38.260  40.129  1.00 31.21           N  
ANISOU 2831  N   GLU B  19     4850   4912   2094   -694   -788   -594       N  
ATOM   2832  CA  GLU B  19     -55.279 -38.498  41.306  1.00 31.94           C  
ANISOU 2832  CA  GLU B  19     4483   4951   2701   -873   -561   -521       C  
ATOM   2833  C   GLU B  19     -54.663 -38.158  42.601  1.00 28.97           C  
ANISOU 2833  C   GLU B  19     4154   4397   2454   -683   -225   -571       C  
ATOM   2834  O   GLU B  19     -55.319 -37.675  43.498  1.00 28.51           O  
ANISOU 2834  O   GLU B  19     4095   4556   2179   -665   -222   -377       O  
ATOM   2835  CB  GLU B  19     -55.817 -39.921  41.283  1.00 35.43           C  
ANISOU 2835  CB  GLU B  19     5324   4856   3282   -731   -519   -644       C  
ATOM   2836  CG  GLU B  19     -57.246 -39.724  40.610  1.00 40.42           C  
ANISOU 2836  CG  GLU B  19     5261   5539   4555  -1110   -668   -573       C  
ATOM   2837  CD  GLU B  19     -57.927 -40.809  40.027  0.20 40.87           C  
ANISOU 2837  CD  GLU B  19     5811   5102   4613  -1292    112   -627       C  
ATOM   2838  OE1 GLU B  19     -58.944 -40.986  40.708  0.20 42.14           O  
ANISOU 2838  OE1 GLU B  19     6204   5293   4512  -1079    417   -423       O  
ATOM   2839  OE2 GLU B  19     -57.483 -41.178  38.927  0.20 41.04           O  
ANISOU 2839  OE2 GLU B  19     5738   5637   4217   -611   -226   -238       O  
ATOM   2840  N   SER B  20     -53.398 -38.461  42.705  1.00 28.24           N  
ANISOU 2840  N   SER B  20     4260   4183   2286   -635   -240   -745       N  
ATOM   2841  CA  SER B  20     -52.605 -38.035  43.866  1.00 26.92           C  
ANISOU 2841  CA  SER B  20     4017   4362   1847   -456     15   -698       C  
ATOM   2842  C   SER B  20     -52.444 -36.503  44.025  1.00 25.37           C  
ANISOU 2842  C   SER B  20     3823   4162   1654   -291     13   -686       C  
ATOM   2843  O   SER B  20     -52.294 -36.053  45.154  1.00 23.92           O  
ANISOU 2843  O   SER B  20     3614   3994   1477   -237    -49   -495       O  
ATOM   2844  CB  SER B  20     -51.258 -38.760  43.912  1.00 27.91           C  
ANISOU 2844  CB  SER B  20     4348   4329   1925   -162    292   -411       C  
ATOM   2845  OG  SER B  20     -50.332 -38.165  43.016  1.00 29.86           O  
ANISOU 2845  OG  SER B  20     4574   4398   2371   -365    351   -387       O  
ATOM   2846  N   MET B  21     -52.463 -35.732  42.930  1.00 25.57           N  
ANISOU 2846  N   MET B  21     3670   4416   1628   -529   -243   -508       N  
ATOM   2847  CA  MET B  21     -52.357 -34.272  42.939  1.00 25.29           C  
ANISOU 2847  CA  MET B  21     3641   4169   1797   -279     38   -640       C  
ATOM   2848  C   MET B  21     -53.651 -33.618  43.395  1.00 25.22           C  
ANISOU 2848  C   MET B  21     3499   3723   2357   -438    170   -353       C  
ATOM   2849  O   MET B  21     -53.651 -32.504  43.873  1.00 24.07           O  
ANISOU 2849  O   MET B  21     3496   3873   1777   -284    -34   -564       O  
ATOM   2850  CB  MET B  21     -51.996 -33.753  41.535  1.00 24.46           C  
ANISOU 2850  CB  MET B  21     3347   4166   1780   -214    142   -560       C  
ATOM   2851  CG  MET B  21     -50.624 -34.162  41.064  1.00 26.42           C  
ANISOU 2851  CG  MET B  21     3336   4336   2364    -61    163   -347       C  
ATOM   2852  SD  MET B  21     -50.199 -33.706  39.386  1.00 32.08           S  
ANISOU 2852  SD  MET B  21     4179   5519   2490    200    594     12       S  
ATOM   2853  CE  MET B  21     -50.224 -31.923  39.433  1.00 30.67           C  
ANISOU 2853  CE  MET B  21     3616   5154   2884    337    485   -718       C  
ATOM   2854  N   LYS B  22     -54.752 -34.341  43.280  1.00 24.10           N  
ANISOU 2854  N   LYS B  22     3723   3833   1599   -598    -78   -417       N  
ATOM   2855  CA  LYS B  22     -56.089 -33.768  43.414  1.00 26.77           C  
ANISOU 2855  CA  LYS B  22     3833   4019   2317   -494    -70   -374       C  
ATOM   2856  C   LYS B  22     -56.402 -33.130  44.754  1.00 25.35           C  
ANISOU 2856  C   LYS B  22     3571   3865   2194   -395    124   -133       C  
ATOM   2857  O   LYS B  22     -56.914 -32.028  44.817  1.00 25.64           O  
ANISOU 2857  O   LYS B  22     3697   3952   2091   -241      2   -258       O  
ATOM   2858  CB  LYS B  22     -57.154 -34.827  43.124  1.00 29.97           C  
ANISOU 2858  CB  LYS B  22     3953   4393   3041   -783     73   -352       C  
ATOM   2859  CG  LYS B  22     -57.657 -34.872  41.692  1.00 35.25           C  
ANISOU 2859  CG  LYS B  22     4682   5350   3358   -510   -356    109       C  
ATOM   2860  CD  LYS B  22     -59.167 -35.019  41.719  1.00 38.66           C  
ANISOU 2860  CD  LYS B  22     4607   5707   4375     23    -77    387       C  
ATOM   2861  CE  LYS B  22     -59.701 -34.214  42.892  1.00 40.74           C  
ANISOU 2861  CE  LYS B  22     4954   5771   4751     13    238    134       C  
ATOM   2862  NZ  LYS B  22     -61.184 -34.330  43.033  1.00 45.44           N  
ANISOU 2862  NZ  LYS B  22     4970   6273   6021   -707   -199   -104       N  
ATOM   2863  N   PRO B  23     -56.089 -33.815  45.847  1.00 23.83           N  
ANISOU 2863  N   PRO B  23     3355   3788   1910   -385    197   -426       N  
ATOM   2864  CA  PRO B  23     -56.466 -33.238  47.137  1.00 23.69           C  
ANISOU 2864  CA  PRO B  23     3501   3709   1788   -517     82   -410       C  
ATOM   2865  C   PRO B  23     -55.700 -31.973  47.513  1.00 22.10           C  
ANISOU 2865  C   PRO B  23     3418   3495   1481   -408    137   -245       C  
ATOM   2866  O   PRO B  23     -56.078 -31.294  48.452  1.00 23.85           O  
ANISOU 2866  O   PRO B  23     3397   3699   1963   -246    381   -416       O  
ATOM   2867  CB  PRO B  23     -56.164 -34.355  48.137  1.00 25.22           C  
ANISOU 2867  CB  PRO B  23     3737   4035   1808   -274    584   -176       C  
ATOM   2868  CG  PRO B  23     -55.333 -35.346  47.414  1.00 25.88           C  
ANISOU 2868  CG  PRO B  23     3782   4156   1894    112    168   -185       C  
ATOM   2869  CD  PRO B  23     -55.609 -35.192  45.957  1.00 24.34           C  
ANISOU 2869  CD  PRO B  23     3532   3906   1810   -206    112   -481       C  
ATOM   2870  N   TRP B  24     -54.644 -31.658  46.775  1.00 20.99           N  
ANISOU 2870  N   TRP B  24     3363   3423   1190   -251    157   -298       N  
ATOM   2871  CA  TRP B  24     -53.780 -30.522  47.082  1.00 20.32           C  
ANISOU 2871  CA  TRP B  24     3103   3328   1289   -159    268   -221       C  
ATOM   2872  C   TRP B  24     -54.049 -29.321  46.241  1.00 20.25           C  
ANISOU 2872  C   TRP B  24     3163   3464   1066   -202    185    -35       C  
ATOM   2873  O   TRP B  24     -53.300 -28.354  46.284  1.00 20.84           O  
ANISOU 2873  O   TRP B  24     3114   3640   1162   -298    114    113       O  
ATOM   2874  CB  TRP B  24     -52.321 -30.919  46.935  1.00 20.09           C  
ANISOU 2874  CB  TRP B  24     3075   3355   1200   -203     41   -215       C  
ATOM   2875  CG  TRP B  24     -51.982 -32.104  47.796  1.00 20.96           C  
ANISOU 2875  CG  TRP B  24     3217   3375   1371    -82    239   -291       C  
ATOM   2876  CD1 TRP B  24     -51.810 -33.420  47.390  1.00 21.60           C  
ANISOU 2876  CD1 TRP B  24     3310   3534   1363   -166     71   -407       C  
ATOM   2877  CD2 TRP B  24     -51.819 -32.127  49.256  1.00 20.50           C  
ANISOU 2877  CD2 TRP B  24     3092   3306   1390     31    149   -408       C  
ATOM   2878  NE1 TRP B  24     -51.527 -34.234  48.463  1.00 21.50           N  
ANISOU 2878  NE1 TRP B  24     3398   3432   1336   -227    104   -472       N  
ATOM   2879  CE2 TRP B  24     -51.553 -33.520  49.616  1.00 19.98           C  
ANISOU 2879  CE2 TRP B  24     3259   3414    917   -109    303   -154       C  
ATOM   2880  CE3 TRP B  24     -51.894 -31.173  50.260  1.00 20.49           C  
ANISOU 2880  CE3 TRP B  24     3151   3594   1039   -168    178   -404       C  
ATOM   2881  CZ2 TRP B  24     -51.341 -33.909  50.932  1.00 20.10           C  
ANISOU 2881  CZ2 TRP B  24     3498   3012   1127    196   -130   -165       C  
ATOM   2882  CZ3 TRP B  24     -51.686 -31.576  51.571  1.00 20.60           C  
ANISOU 2882  CZ3 TRP B  24     3381   3082   1362    224    193    -20       C  
ATOM   2883  CH2 TRP B  24     -51.415 -32.907  51.905  1.00 20.28           C  
ANISOU 2883  CH2 TRP B  24     3605   3118    980    135      0   -157       C  
ATOM   2884  N   GLN B  25     -55.123 -29.376  45.470  1.00 20.68           N  
ANISOU 2884  N   GLN B  25     3217   3226   1414   -324      8    -88       N  
ATOM   2885  CA  GLN B  25     -55.526 -28.271  44.619  1.00 20.53           C  
ANISOU 2885  CA  GLN B  25     3277   3593    929   -250    -61     16       C  
ATOM   2886  C   GLN B  25     -56.472 -27.344  45.343  1.00 20.95           C  
ANISOU 2886  C   GLN B  25     3471   3569    919   -115    -56   -137       C  
ATOM   2887  O   GLN B  25     -56.164 -26.170  45.529  1.00 20.19           O  
ANISOU 2887  O   GLN B  25     3450   3522    697   -221     70    148       O  
ATOM   2888  CB  GLN B  25     -56.161 -28.801  43.325  1.00 21.46           C  
ANISOU 2888  CB  GLN B  25     3487   3484   1182   -146    -78   -361       C  
ATOM   2889  CG  GLN B  25     -55.319 -29.829  42.574  1.00 21.74           C  
ANISOU 2889  CG  GLN B  25     3371   3553   1336   -122   -105   -280       C  
ATOM   2890  CD  GLN B  25     -54.195 -29.221  41.746  1.00 23.51           C  
ANISOU 2890  CD  GLN B  25     3736   3476   1717     19    184   -257       C  
ATOM   2891  OE1 GLN B  25     -53.527 -29.931  40.993  1.00 26.89           O  
ANISOU 2891  OE1 GLN B  25     3743   4255   2218    247     62   -647       O  
ATOM   2892  NE2 GLN B  25     -53.971 -27.915  41.881  1.00 21.17           N  
ANISOU 2892  NE2 GLN B  25     3466   3489   1087    -85    665   -385       N  
ATOM   2893  N   SER B  26     -57.583 -27.886  45.795  1.00 22.78           N  
ANISOU 2893  N   SER B  26     3619   3748   1288   -322     66   -174       N  
ATOM   2894  CA ASER B  26     -58.616 -27.094  46.439  0.50 23.78           C  
ANISOU 2894  CA ASER B  26     3651   3854   1527    -96     20   -104       C  
ATOM   2895  CA BSER B  26     -58.505 -27.038  46.502  0.50 23.85           C  
ANISOU 2895  CA BSER B  26     3723   3830   1509   -105     58    -93       C  
ATOM   2896  C   SER B  26     -58.916 -27.535  47.872  1.00 24.05           C  
ANISOU 2896  C   SER B  26     3652   3860   1624   -213    229   -111       C  
ATOM   2897  O   SER B  26     -59.410 -26.756  48.637  1.00 27.01           O  
ANISOU 2897  O   SER B  26     3862   4160   2241     -2    221   -462       O  
ATOM   2898  CB ASER B  26     -59.941 -27.168  45.669  0.50 23.85           C  
ANISOU 2898  CB ASER B  26     3659   3815   1587   -215     12   -272       C  
ATOM   2899  CB BSER B  26     -59.758 -26.800  45.687  0.50 25.29           C  
ANISOU 2899  CB BSER B  26     3814   3958   1836   -239   -127    -76       C  
ATOM   2900  OG ASER B  26     -59.779 -27.363  44.288  0.50 23.11           O  
ANISOU 2900  OG ASER B  26     3412   3714   1652    186     49   -468       O  
ATOM   2901  OG BSER B  26     -60.434 -28.014  45.490  0.50 26.52           O  
ANISOU 2901  OG BSER B  26     4219   3755   2101   -278     70    266       O  
ATOM   2902  N   ASP B  27     -58.759 -28.829  48.159  1.00 24.71           N  
ANISOU 2902  N   ASP B  27     3769   3799   1820   -217    123   -117       N  
ATOM   2903  CA  ASP B  27     -59.109 -29.390  49.489  1.00 25.24           C  
ANISOU 2903  CA  ASP B  27     3839   4039   1710   -131    173   -191       C  
ATOM   2904  C   ASP B  27     -58.152 -28.947  50.593  1.00 24.16           C  
ANISOU 2904  C   ASP B  27     3285   4010   1884   -195    445   -368       C  
ATOM   2905  O   ASP B  27     -58.592 -28.533  51.663  1.00 25.36           O  
ANISOU 2905  O   ASP B  27     3585   4205   1845   -307    517   -432       O  
ATOM   2906  CB  ASP B  27     -59.178 -30.915  49.455  1.00 25.78           C  
ANISOU 2906  CB  ASP B  27     3844   4010   1940   -345    252   -234       C  
ATOM   2907  CG  ASP B  27     -60.348 -31.435  48.626  1.00 30.27           C  
ANISOU 2907  CG  ASP B  27     3988   4587   2924    -99   -316   -321       C  
ATOM   2908  OD1 ASP B  27     -61.290 -30.667  48.343  1.00 31.86           O  
ANISOU 2908  OD1 ASP B  27     4034   4837   3235      0    -72     86       O  
ATOM   2909  OD2 ASP B  27     -60.337 -32.626  48.256  1.00 32.40           O  
ANISOU 2909  OD2 ASP B  27     4813   4768   2729   -225    -49   -577       O  
ATOM   2910  N   SER B  28     -56.849 -29.078  50.341  1.00 21.14           N  
ANISOU 2910  N   SER B  28     3239   3455   1336     84    232   -156       N  
ATOM   2911  CA  SER B  28     -55.810 -28.653  51.273  1.00 20.97           C  
ANISOU 2911  CA  SER B  28     3266   3238   1460   -167    290   -242       C  
ATOM   2912  C   SER B  28     -54.764 -27.889  50.489  1.00 21.53           C  
ANISOU 2912  C   SER B  28     3219   3214   1746     27    443   -167       C  
ATOM   2913  O   SER B  28     -54.052 -28.477  49.723  1.00 20.96           O  
ANISOU 2913  O   SER B  28     3040   2970   1954   -222    459   -185       O  
ATOM   2914  CB  SER B  28     -55.186 -29.882  51.920  1.00 20.62           C  
ANISOU 2914  CB  SER B  28     3122   3098   1613   -176    313   -337       C  
ATOM   2915  OG  SER B  28     -54.131 -29.534  52.788  1.00 21.12           O  
ANISOU 2915  OG  SER B  28     3209   3380   1434   -194    299    -68       O  
ATOM   2916  N   PHE B  29     -54.666 -26.584  50.644  1.00 18.24           N  
ANISOU 2916  N   PHE B  29     2969   3156    805    -10    228   -204       N  
ATOM   2917  CA  PHE B  29     -53.936 -25.825  49.650  1.00 17.39           C  
ANISOU 2917  CA  PHE B  29     2686   2962    959    131    194   -207       C  
ATOM   2918  C   PHE B  29     -52.975 -24.844  50.308  1.00 17.05           C  
ANISOU 2918  C   PHE B  29     2893   2781    804    131     60     37       C  
ATOM   2919  O   PHE B  29     -52.602 -23.834  49.706  1.00 17.58           O  
ANISOU 2919  O   PHE B  29     2829   3053    796    -53    265     96       O  
ATOM   2920  CB  PHE B  29     -54.960 -25.054  48.803  1.00 17.02           C  
ANISOU 2920  CB  PHE B  29     2839   2847    779    235    168   -294       C  
ATOM   2921  CG  PHE B  29     -55.933 -24.257  49.640  1.00 17.15           C  
ANISOU 2921  CG  PHE B  29     2916   3272    328    293    252   -261       C  
ATOM   2922  CD1 PHE B  29     -57.097 -24.832  50.149  1.00 19.03           C  
ANISOU 2922  CD1 PHE B  29     2867   3249   1112     94    -32   -188       C  
ATOM   2923  CD2 PHE B  29     -55.656 -22.942  49.960  1.00 18.02           C  
ANISOU 2923  CD2 PHE B  29     2990   3323    533    153     24   -397       C  
ATOM   2924  CE1 PHE B  29     -57.953 -24.106  50.965  1.00 19.35           C  
ANISOU 2924  CE1 PHE B  29     2851   3826    674    225   -108   -302       C  
ATOM   2925  CE2 PHE B  29     -56.523 -22.209  50.752  1.00 19.91           C  
ANISOU 2925  CE2 PHE B  29     2813   4047    703    339     95   -471       C  
ATOM   2926  CZ  PHE B  29     -57.673 -22.791  51.247  1.00 19.90           C  
ANISOU 2926  CZ  PHE B  29     2994   3830    734     61   -200   -402       C  
ATOM   2927  N   ALA B  30     -52.585 -25.108  51.551  1.00 16.01           N  
ANISOU 2927  N   ALA B  30     2807   2598    677     76    131   -154       N  
ATOM   2928  CA  ALA B  30     -51.738 -24.151  52.285  1.00 16.03           C  
ANISOU 2928  CA  ALA B  30     2760   2650    679     38     34     30       C  
ATOM   2929  C   ALA B  30     -50.374 -23.906  51.639  1.00 15.81           C  
ANISOU 2929  C   ALA B  30     2869   2563    574     79    100   -143       C  
ATOM   2930  O   ALA B  30     -49.865 -24.747  50.908  1.00 15.63           O  
ANISOU 2930  O   ALA B  30     2709   2763    464    142    306    -51       O  
ATOM   2931  CB  ALA B  30     -51.544 -24.616  53.721  1.00 16.31           C  
ANISOU 2931  CB  ALA B  30     2834   2761    600    132    205    -26       C  
ATOM   2932  N   ASN B  31     -49.760 -22.763  51.936  1.00 15.61           N  
ANISOU 2932  N   ASN B  31     2935   2604    390    -48    158     46       N  
ATOM   2933  CA  ASN B  31     -48.358 -22.573  51.602  1.00 16.28           C  
ANISOU 2933  CA  ASN B  31     2883   2631    672    127     10   -149       C  
ATOM   2934  C   ASN B  31     -47.555 -23.416  52.578  1.00 16.56           C  
ANISOU 2934  C   ASN B  31     2931   2618    740    240    104   -111       C  
ATOM   2935  O   ASN B  31     -47.695 -23.247  53.777  1.00 16.70           O  
ANISOU 2935  O   ASN B  31     2908   2666    771    186    138   -198       O  
ATOM   2936  CB  ASN B  31     -47.980 -21.108  51.761  1.00 16.26           C  
ANISOU 2936  CB  ASN B  31     2991   2640    544     28     89    -12       C  
ATOM   2937  CG  ASN B  31     -46.615 -20.801  51.202  1.00 16.99           C  
ANISOU 2937  CG  ASN B  31     2944   2657    852    168     68     -8       C  
ATOM   2938  OD1 ASN B  31     -45.664 -21.571  51.382  1.00 18.08           O  
ANISOU 2938  OD1 ASN B  31     3113   2943    813    263    -92     80       O  
ATOM   2939  ND2 ASN B  31     -46.504 -19.664  50.527  1.00 17.10           N  
ANISOU 2939  ND2 ASN B  31     2991   2549    955     50    146    -72       N  
ATOM   2940  N   PRO B  32     -46.692 -24.315  52.096  1.00 16.07           N  
ANISOU 2940  N   PRO B  32     2934   2557    615    224     85    -80       N  
ATOM   2941  CA  PRO B  32     -46.017 -25.220  53.015  1.00 16.18           C  
ANISOU 2941  CA  PRO B  32     2890   2661    595    331    -37   -234       C  
ATOM   2942  C   PRO B  32     -45.073 -24.522  53.967  1.00 16.79           C  
ANISOU 2942  C   PRO B  32     2979   2803    595    178     55   -302       C  
ATOM   2943  O   PRO B  32     -44.639 -25.135  54.922  1.00 18.83           O  
ANISOU 2943  O   PRO B  32     3196   2997    961    347   -107   -152       O  
ATOM   2944  CB  PRO B  32     -45.242 -26.150  52.079  1.00 15.52           C  
ANISOU 2944  CB  PRO B  32     2778   2605    512    242   -122   -293       C  
ATOM   2945  CG  PRO B  32     -46.125 -26.202  50.879  1.00 15.14           C  
ANISOU 2945  CG  PRO B  32     2872   2562    318    260    -25   -190       C  
ATOM   2946  CD  PRO B  32     -46.527 -24.759  50.708  1.00 16.12           C  
ANISOU 2946  CD  PRO B  32     2969   2469    684    161    -49   -237       C  
ATOM   2947  N   SER B  33     -44.762 -23.253  53.733  1.00 16.68           N  
ANISOU 2947  N   SER B  33     2851   2745    742    245    242   -430       N  
ATOM   2948  CA  SER B  33     -43.925 -22.524  54.685  1.00 17.25           C  
ANISOU 2948  CA  SER B  33     2707   2886    960    157     55   -200       C  
ATOM   2949  C   SER B  33     -44.664 -22.017  55.929  1.00 17.94           C  
ANISOU 2949  C   SER B  33     2894   2928    991     84    145   -253       C  
ATOM   2950  O   SER B  33     -44.027 -21.455  56.812  1.00 18.78           O  
ANISOU 2950  O   SER B  33     2997   3378    761    278    -16   -247       O  
ATOM   2951  CB  SER B  33     -43.260 -21.325  54.009  1.00 18.86           C  
ANISOU 2951  CB  SER B  33     2872   2821   1473    232    146    -81       C  
ATOM   2952  OG  SER B  33     -44.188 -20.252  53.869  1.00 19.55           O  
ANISOU 2952  OG  SER B  33     3142   2796   1488    267     83   -245       O  
ATOM   2953  N   ALA B  34     -45.986 -22.182  55.987  1.00 17.58           N  
ANISOU 2953  N   ALA B  34     2802   2904    973    282     92   -260       N  
ATOM   2954  CA  ALA B  34     -46.825 -21.557  56.994  1.00 17.92           C  
ANISOU 2954  CA  ALA B  34     2993   3131    682    185    121   -318       C  
ATOM   2955  C   ALA B  34     -46.681 -22.318  58.282  1.00 19.68           C  
ANISOU 2955  C   ALA B  34     3234   3206   1037    238     16    -71       C  
ATOM   2956  O   ALA B  34     -46.206 -23.439  58.297  1.00 19.98           O  
ANISOU 2956  O   ALA B  34     3167   3369   1052    383   -312   -130       O  
ATOM   2957  CB  ALA B  34     -48.269 -21.548  56.541  1.00 17.35           C  
ANISOU 2957  CB  ALA B  34     2965   2875    751     48    210   -163       C  
ATOM   2958  N   ALA B  35     -47.091 -21.701  59.373  1.00 19.28           N  
ANISOU 2958  N   ALA B  35     3206   3474    644    -68    127     96       N  
ATOM   2959  CA  ALA B  35     -46.827 -22.284  60.681  1.00 21.56           C  
ANISOU 2959  CA  ALA B  35     3586   3723    883    -23     21    358       C  
ATOM   2960  C   ALA B  35     -47.897 -23.232  61.220  1.00 21.52           C  
ANISOU 2960  C   ALA B  35     3619   3748    807    -63    231    137       C  
ATOM   2961  O   ALA B  35     -47.731 -23.773  62.319  1.00 27.46           O  
ANISOU 2961  O   ALA B  35     4415   4951   1067   -189    227    688       O  
ATOM   2962  CB  ALA B  35     -46.554 -21.182  61.686  1.00 22.80           C  
ANISOU 2962  CB  ALA B  35     3721   4006    933   -139     -9    191       C  
ATOM   2963  N   HIS B  36     -48.955 -23.463  60.451  1.00 19.28           N  
ANISOU 2963  N   HIS B  36     3255   3263    807    272    331    116       N  
ATOM   2964  CA  HIS B  36     -50.147 -24.155  60.933  1.00 19.50           C  
ANISOU 2964  CA  HIS B  36     3465   3050    891    136    319     79       C  
ATOM   2965  C   HIS B  36     -50.347 -25.523  60.343  1.00 19.74           C  
ANISOU 2965  C   HIS B  36     3534   3144    822    118    317     24       C  
ATOM   2966  O   HIS B  36     -49.547 -25.978  59.532  1.00 19.92           O  
ANISOU 2966  O   HIS B  36     3479   3256    834    198    341    145       O  
ATOM   2967  CB  HIS B  36     -51.364 -23.289  60.695  1.00 19.76           C  
ANISOU 2967  CB  HIS B  36     3431   3341    736    198    319     92       C  
ATOM   2968  CG  HIS B  36     -51.480 -22.796  59.296  1.00 19.15           C  
ANISOU 2968  CG  HIS B  36     3550   2973    753    157    -25    -31       C  
ATOM   2969  ND1 HIS B  36     -51.749 -23.612  58.268  1.00 18.20           N  
ANISOU 2969  ND1 HIS B  36     3307   2964    643    240    119    -67       N  
ATOM   2970  CD2 HIS B  36     -51.366 -21.516  58.766  1.00 18.98           C  
ANISOU 2970  CD2 HIS B  36     3469   2986    754     55      2    -59       C  
ATOM   2971  CE1 HIS B  36     -51.814 -22.897  57.132  1.00 16.95           C  
ANISOU 2971  CE1 HIS B  36     2989   2700    751     31    223    -58       C  
ATOM   2972  NE2 HIS B  36     -51.582 -21.612  57.436  1.00 18.25           N  
ANISOU 2972  NE2 HIS B  36     3251   2859    822     -5    -51   -353       N  
ATOM   2973  N   ILE B  37     -51.402 -26.193  60.785  1.00 20.06           N  
ANISOU 2973  N   ILE B  37     3508   3040   1074     66    214    -17       N  
ATOM   2974  CA  ILE B  37     -51.614 -27.593  60.483  1.00 19.76           C  
ANISOU 2974  CA  ILE B  37     3605   2984    916     92    264     -8       C  
ATOM   2975  C   ILE B  37     -51.755 -27.905  58.987  1.00 19.65           C  
ANISOU 2975  C   ILE B  37     3523   3097    845    169    481     58       C  
ATOM   2976  O   ILE B  37     -51.355 -28.970  58.565  1.00 19.33           O  
ANISOU 2976  O   ILE B  37     3514   3024    806    197    518     94       O  
ATOM   2977  CB  ILE B  37     -52.803 -28.164  61.303  1.00 21.05           C  
ANISOU 2977  CB  ILE B  37     3803   3305    890     27    338     40       C  
ATOM   2978  CG1 ILE B  37     -52.862 -29.686  61.206  1.00 24.25           C  
ANISOU 2978  CG1 ILE B  37     4119   3346   1749    -30    313    255       C  
ATOM   2979  CG2 ILE B  37     -54.138 -27.584  60.859  1.00 21.60           C  
ANISOU 2979  CG2 ILE B  37     3776   3115   1315    188    479     36       C  
ATOM   2980  CD1 ILE B  37     -51.661 -30.364  61.810  1.00 26.36           C  
ANISOU 2980  CD1 ILE B  37     4283   4095   1634    354    364     74       C  
ATOM   2981  N   GLU B  38     -52.352 -27.016  58.201  1.00 18.76           N  
ANISOU 2981  N   GLU B  38     3268   3083    775     93    473     46       N  
ATOM   2982  CA  GLU B  38     -52.511 -27.314  56.780  1.00 18.69           C  
ANISOU 2982  CA  GLU B  38     3094   3092    913     33    284   -179       C  
ATOM   2983  C   GLU B  38     -51.151 -27.331  56.092  1.00 18.10           C  
ANISOU 2983  C   GLU B  38     3199   2907    770    177    304   -152       C  
ATOM   2984  O   GLU B  38     -50.930 -28.153  55.211  1.00 18.04           O  
ANISOU 2984  O   GLU B  38     3293   2903    655    246    492    -52       O  
ATOM   2985  CB  GLU B  38     -53.513 -26.373  56.097  1.00 19.70           C  
ANISOU 2985  CB  GLU B  38     3018   3032   1434     72    377    -63       C  
ATOM   2986  CG  GLU B  38     -54.962 -26.642  56.490  1.00 20.91           C  
ANISOU 2986  CG  GLU B  38     2895   3203   1844    -83    277   -446       C  
ATOM   2987  CD  GLU B  38     -55.426 -28.037  56.101  1.00 22.17           C  
ANISOU 2987  CD  GLU B  38     3529   3292   1603   -155    667   -573       C  
ATOM   2988  OE1 GLU B  38     -55.939 -28.749  56.970  1.00 26.59           O  
ANISOU 2988  OE1 GLU B  38     3790   3948   2362   -514    711      2       O  
ATOM   2989  OE2 GLU B  38     -55.282 -28.430  54.931  1.00 23.01           O  
ANISOU 2989  OE2 GLU B  38     3501   3316   1926   -237    725  -1067       O  
ATOM   2990  N   ALA B  39     -50.229 -26.464  56.523  1.00 16.80           N  
ANISOU 2990  N   ALA B  39     3171   2836    373    118    367     46       N  
ATOM   2991  CA  ALA B  39     -48.863 -26.485  55.990  1.00 18.11           C  
ANISOU 2991  CA  ALA B  39     3076   2939    865     76    297     19       C  
ATOM   2992  C   ALA B  39     -48.168 -27.770  56.426  1.00 18.93           C  
ANISOU 2992  C   ALA B  39     3339   2939    913    194    577      7       C  
ATOM   2993  O   ALA B  39     -47.427 -28.376  55.652  1.00 18.47           O  
ANISOU 2993  O   ALA B  39     3299   3031    685     43    530    -68       O  
ATOM   2994  CB  ALA B  39     -48.065 -25.257  56.425  1.00 17.75           C  
ANISOU 2994  CB  ALA B  39     2973   2929    841    209    286   -211       C  
ATOM   2995  N   GLU B  40     -48.423 -28.194  57.660  1.00 19.74           N  
ANISOU 2995  N   GLU B  40     3615   2911    974    137    370    211       N  
ATOM   2996  CA  GLU B  40     -47.850 -29.419  58.160  1.00 19.52           C  
ANISOU 2996  CA  GLU B  40     3656   2926    834    120    449    174       C  
ATOM   2997  C   GLU B  40     -48.291 -30.635  57.326  1.00 18.65           C  
ANISOU 2997  C   GLU B  40     3494   2905    687    121    468    209       C  
ATOM   2998  O   GLU B  40     -47.470 -31.488  57.043  1.00 19.73           O  
ANISOU 2998  O   GLU B  40     3617   3162    715    247    434     15       O  
ATOM   2999  CB  GLU B  40     -48.205 -29.590  59.650  1.00 22.24           C  
ANISOU 2999  CB  GLU B  40     4073   3549    828    150    431    309       C  
ATOM   3000  CG  GLU B  40     -47.333 -30.579  60.399  1.00 27.92           C  
ANISOU 3000  CG  GLU B  40     4802   4515   1290    510    101    595       C  
ATOM   3001  CD  GLU B  40     -47.694 -30.650  61.872  1.00 32.58           C  
ANISOU 3001  CD  GLU B  40     5830   5490   1059    404   -275    667       C  
ATOM   3002  OE1 GLU B  40     -47.737 -31.772  62.401  1.00 37.85           O  
ANISOU 3002  OE1 GLU B  40     6651   5761   1967    726    278   1073       O  
ATOM   3003  OE2 GLU B  40     -47.995 -29.599  62.488  1.00 38.21           O  
ANISOU 3003  OE2 GLU B  40     6900   6085   1530    321     48     63       O  
ATOM   3004  N   LYS B  41     -49.565 -30.714  56.939  1.00 18.02           N  
ANISOU 3004  N   LYS B  41     3368   2976    502    143    540    104       N  
ATOM   3005  CA  LYS B  41     -50.043 -31.797  56.073  1.00 19.06           C  
ANISOU 3005  CA  LYS B  41     3319   2962    958     30    701   -126       C  
ATOM   3006  C   LYS B  41     -49.324 -31.802  54.722  1.00 18.52           C  
ANISOU 3006  C   LYS B  41     3342   2902    790     39    559     -5       C  
ATOM   3007  O   LYS B  41     -48.841 -32.841  54.271  1.00 19.59           O  
ANISOU 3007  O   LYS B  41     3526   2806   1110     78    324    -23       O  
ATOM   3008  CB  LYS B  41     -51.556 -31.688  55.873  1.00 20.18           C  
ANISOU 3008  CB  LYS B  41     3307   3096   1263     68    688    -42       C  
ATOM   3009  CG  LYS B  41     -52.360 -31.934  57.149  1.00 21.97           C  
ANISOU 3009  CG  LYS B  41     3425   3338   1583   -153   1036   -386       C  
ATOM   3010  CD  LYS B  41     -53.846 -31.668  56.930  1.00 27.79           C  
ANISOU 3010  CD  LYS B  41     3534   3991   3034   -147    726   -368       C  
ATOM   3011  CE  LYS B  41     -54.620 -31.739  58.239  1.00 34.21           C  
ANISOU 3011  CE  LYS B  41     4592   5138   3268   -277   1156   -462       C  
ATOM   3012  NZ  LYS B  41     -56.062 -32.045  58.005  1.00 42.38           N  
ANISOU 3012  NZ  LYS B  41     4860   6290   4952   -375    591   -675       N  
ATOM   3013  N   ALA B  42     -49.249 -30.639  54.084  1.00 17.85           N  
ANISOU 3013  N   ALA B  42     3280   2812    689    173    351    -67       N  
ATOM   3014  CA  ALA B  42     -48.511 -30.507  52.817  1.00 18.52           C  
ANISOU 3014  CA  ALA B  42     3246   2816    973    183    563    103       C  
ATOM   3015  C   ALA B  42     -47.051 -30.940  52.975  1.00 17.93           C  
ANISOU 3015  C   ALA B  42     3359   2682    769    120    263    -95       C  
ATOM   3016  O   ALA B  42     -46.521 -31.683  52.153  1.00 17.95           O  
ANISOU 3016  O   ALA B  42     3347   2771    701     99    247   -162       O  
ATOM   3017  CB  ALA B  42     -48.580 -29.075  52.295  1.00 17.28           C  
ANISOU 3017  CB  ALA B  42     3099   2776    690     31    537     70       C  
ATOM   3018  N   LEU B  43     -46.422 -30.484  54.056  1.00 17.73           N  
ANISOU 3018  N   LEU B  43     3339   2721    674     95    323    -93       N  
ATOM   3019  CA  LEU B  43     -45.022 -30.777  54.354  1.00 18.28           C  
ANISOU 3019  CA  LEU B  43     3396   2777    770    -30    144   -212       C  
ATOM   3020  C   LEU B  43     -44.766 -32.270  54.526  1.00 19.01           C  
ANISOU 3020  C   LEU B  43     3375   2876    972     62    162   -196       C  
ATOM   3021  O   LEU B  43     -43.741 -32.765  54.083  1.00 18.38           O  
ANISOU 3021  O   LEU B  43     3578   2754    650     33    248   -228       O  
ATOM   3022  CB  LEU B  43     -44.595 -30.001  55.603  1.00 19.70           C  
ANISOU 3022  CB  LEU B  43     3359   3454    671     15    184   -390       C  
ATOM   3023  CG  LEU B  43     -43.308 -29.187  55.618  1.00 22.76           C  
ANISOU 3023  CG  LEU B  43     3992   3958    697   -518    353   -404       C  
ATOM   3024  CD1 LEU B  43     -43.068 -28.385  54.344  1.00 20.55           C  
ANISOU 3024  CD1 LEU B  43     3683   3289    832    -48   -334   -192       C  
ATOM   3025  CD2 LEU B  43     -43.351 -28.252  56.822  1.00 21.79           C  
ANISOU 3025  CD2 LEU B  43     3850   3182   1246   -336    367   -445       C  
ATOM   3026  N   ASN B  44     -45.702 -32.986  55.148  1.00 18.99           N  
ANISOU 3026  N   ASN B  44     3543   2754    915    166    209    -63       N  
ATOM   3027  CA  ASN B  44     -45.609 -34.439  55.264  1.00 19.62           C  
ANISOU 3027  CA  ASN B  44     3817   2848    787    134    280     51       C  
ATOM   3028  C   ASN B  44     -45.705 -35.151  53.911  1.00 19.36           C  
ANISOU 3028  C   ASN B  44     3633   2790    932    196    152    -61       C  
ATOM   3029  O   ASN B  44     -44.982 -36.110  53.672  1.00 20.10           O  
ANISOU 3029  O   ASN B  44     3755   2787   1092    231    292     46       O  
ATOM   3030  CB  ASN B  44     -46.672 -34.964  56.252  1.00 21.78           C  
ANISOU 3030  CB  ASN B  44     3648   3348   1277    155    528     50       C  
ATOM   3031  CG  ASN B  44     -46.335 -34.641  57.673  1.00 26.32           C  
ANISOU 3031  CG  ASN B  44     4304   4347   1347    523    319    -59       C  
ATOM   3032  OD1 ASN B  44     -45.182 -34.765  58.038  1.00 30.13           O  
ANISOU 3032  OD1 ASN B  44     4435   4776   2237    345   -114    273       O  
ATOM   3033  ND2 ASN B  44     -47.328 -34.277  58.494  1.00 29.60           N  
ANISOU 3033  ND2 ASN B  44     4620   4351   2275    652    953     76       N  
ATOM   3034  N   ALA B  45     -46.571 -34.648  53.036  1.00 19.00           N  
ANISOU 3034  N   ALA B  45     3655   2856    705     39     94    -73       N  
ATOM   3035  CA  ALA B  45     -46.734 -35.212  51.709  1.00 18.18           C  
ANISOU 3035  CA  ALA B  45     3371   2792    742    178    242   -175       C  
ATOM   3036  C   ALA B  45     -45.500 -34.929  50.859  1.00 17.98           C  
ANISOU 3036  C   ALA B  45     3384   2766    678    111    165    -44       C  
ATOM   3037  O   ALA B  45     -45.067 -35.783  50.092  1.00 19.16           O  
ANISOU 3037  O   ALA B  45     3580   2736    962    170    212   -100       O  
ATOM   3038  CB  ALA B  45     -47.977 -34.651  51.062  1.00 18.01           C  
ANISOU 3038  CB  ALA B  45     3359   2842    640    195    254   -138       C  
ATOM   3039  N   ILE B  46     -44.921 -33.741  51.028  1.00 17.92           N  
ANISOU 3039  N   ILE B  46     3413   2659    736    174    224     89       N  
ATOM   3040  CA  ILE B  46     -43.702 -33.354  50.318  1.00 17.86           C  
ANISOU 3040  CA  ILE B  46     3228   2489   1068    123     99     39       C  
ATOM   3041  C   ILE B  46     -42.551 -34.240  50.770  1.00 17.44           C  
ANISOU 3041  C   ILE B  46     3363   2482    779    281    248    -55       C  
ATOM   3042  O   ILE B  46     -41.784 -34.751  49.961  1.00 18.00           O  
ANISOU 3042  O   ILE B  46     3446   2619    772    265    403    104       O  
ATOM   3043  CB  ILE B  46     -43.381 -31.854  50.533  1.00 16.73           C  
ANISOU 3043  CB  ILE B  46     2972   2381   1002    244     99     23       C  
ATOM   3044  CG1 ILE B  46     -44.385 -31.002  49.754  1.00 15.94           C  
ANISOU 3044  CG1 ILE B  46     2923   2178    953    180    117    -39       C  
ATOM   3045  CG2 ILE B  46     -41.933 -31.521  50.148  1.00 15.53           C  
ANISOU 3045  CG2 ILE B  46     2978   2239    680    339    216    -97       C  
ATOM   3046  CD1 ILE B  46     -44.344 -29.515  50.075  1.00 17.06           C  
ANISOU 3046  CD1 ILE B  46     3084   2156   1241    218    -29    -33       C  
ATOM   3047  N   LYS B  47     -42.464 -34.446  52.073  1.00 18.02           N  
ANISOU 3047  N   LYS B  47     3319   2740    786    198    339     52       N  
ATOM   3048  CA  LYS B  47     -41.467 -35.326  52.651  1.00 18.41           C  
ANISOU 3048  CA  LYS B  47     3621   2665    706    308    281    -42       C  
ATOM   3049  C   LYS B  47     -41.512 -36.730  52.068  1.00 18.51           C  
ANISOU 3049  C   LYS B  47     3591   2689    752    255    205    -44       C  
ATOM   3050  O   LYS B  47     -40.468 -37.306  51.818  1.00 17.88           O  
ANISOU 3050  O   LYS B  47     3658   2492    643    275    251     -6       O  
ATOM   3051  CB  LYS B  47     -41.637 -35.411  54.175  1.00 20.25           C  
ANISOU 3051  CB  LYS B  47     4011   2994    688    249    204     29       C  
ATOM   3052  CG  LYS B  47     -40.441 -36.043  54.880  1.00 22.71           C  
ANISOU 3052  CG  LYS B  47     3911   3286   1428    456     86   -360       C  
ATOM   3053  CD  LYS B  47     -40.478 -35.851  56.392  1.00 27.26           C  
ANISOU 3053  CD  LYS B  47     4841   4183   1332    293   -145   -122       C  
ATOM   3054  CE  LYS B  47     -41.443 -36.812  57.063  1.00 35.36           C  
ANISOU 3054  CE  LYS B  47     5400   4607   3427   -455     72   -403       C  
ATOM   3055  NZ  LYS B  47     -41.080 -38.233  56.801  1.00 36.28           N  
ANISOU 3055  NZ  LYS B  47     5798   5050   2937    108    463   -603       N  
ATOM   3056  N   GLN B  48     -42.706 -37.279  51.871  1.00 18.30           N  
ANISOU 3056  N   GLN B  48     3660   2567    725    156    455     20       N  
ATOM   3057  CA  GLN B  48     -42.835 -38.633  51.308  1.00 19.01           C  
ANISOU 3057  CA  GLN B  48     3792   2566    862     25    398    -13       C  
ATOM   3058  C   GLN B  48     -42.224 -38.676  49.904  1.00 18.53           C  
ANISOU 3058  C   GLN B  48     3603   2592    845    133    338    115       C  
ATOM   3059  O   GLN B  48     -41.473 -39.597  49.578  1.00 18.56           O  
ANISOU 3059  O   GLN B  48     3678   2680    692    237    252    164       O  
ATOM   3060  CB  GLN B  48     -44.287 -39.088  51.326  1.00 21.41           C  
ANISOU 3060  CB  GLN B  48     3795   3119   1220     68    526     66       C  
ATOM   3061  CG  GLN B  48     -44.560 -40.176  50.328  1.00 27.16           C  
ANISOU 3061  CG  GLN B  48     4575   3490   2253   -380     30   -300       C  
ATOM   3062  CD  GLN B  48     -45.584 -41.178  50.701  1.00 34.74           C  
ANISOU 3062  CD  GLN B  48     5597   4854   2748  -1206    574     88       C  
ATOM   3063  OE1 GLN B  48     -46.105 -41.819  49.805  1.00 39.08           O  
ANISOU 3063  OE1 GLN B  48     5341   5549   3958   -969   -576   -176       O  
ATOM   3064  NE2 GLN B  48     -45.859 -41.371  51.990  1.00 36.07           N  
ANISOU 3064  NE2 GLN B  48     5644   5277   2783   -720    550    395       N  
ATOM   3065  N   ALA B  49     -42.528 -37.666  49.091  1.00 18.29           N  
ANISOU 3065  N   ALA B  49     3574   2529    843    175    357     48       N  
ATOM   3066  CA  ALA B  49     -42.045 -37.615  47.714  1.00 17.67           C  
ANISOU 3066  CA  ALA B  49     3426   2483    803    153    274    172       C  
ATOM   3067  C   ALA B  49     -40.528 -37.441  47.662  1.00 16.92           C  
ANISOU 3067  C   ALA B  49     3368   2369    691    218    213     15       C  
ATOM   3068  O   ALA B  49     -39.829 -38.114  46.911  1.00 16.18           O  
ANISOU 3068  O   ALA B  49     3369   2396    382    312    207    181       O  
ATOM   3069  CB  ALA B  49     -42.739 -36.494  46.962  1.00 16.99           C  
ANISOU 3069  CB  ALA B  49     3446   2324    681    233    427     47       C  
ATOM   3070  N   ARG B  50     -40.027 -36.529  48.479  1.00 17.06           N  
ANISOU 3070  N   ARG B  50     3379   2346    756    229    231    -32       N  
ATOM   3071  CA  ARG B  50     -38.598 -36.310  48.607  1.00 16.80           C  
ANISOU 3071  CA  ARG B  50     3373   2432    578    149    138    -35       C  
ATOM   3072  C   ARG B  50     -37.882 -37.619  48.960  1.00 17.18           C  
ANISOU 3072  C   ARG B  50     3364   2444    719    127    246     52       C  
ATOM   3073  O   ARG B  50     -36.826 -37.936  48.392  1.00 17.09           O  
ANISOU 3073  O   ARG B  50     3424   2570    496    202    160    139       O  
ATOM   3074  CB  ARG B  50     -38.348 -35.235  49.669  1.00 16.77           C  
ANISOU 3074  CB  ARG B  50     3353   2320    698     24    166    -25       C  
ATOM   3075  CG  ARG B  50     -36.995 -34.546  49.557  1.00 16.47           C  
ANISOU 3075  CG  ARG B  50     3201   2257    800    169    187    -44       C  
ATOM   3076  CD  ARG B  50     -36.749 -33.620  50.734  1.00 16.87           C  
ANISOU 3076  CD  ARG B  50     3370   2433    607    260    305    -58       C  
ATOM   3077  NE  ARG B  50     -37.661 -32.477  50.788  1.00 16.58           N  
ANISOU 3077  NE  ARG B  50     3235   2387    675    194    180     12       N  
ATOM   3078  CZ  ARG B  50     -37.537 -31.375  50.058  1.00 15.42           C  
ANISOU 3078  CZ  ARG B  50     2954   2337    567    212    196    -95       C  
ATOM   3079  NH1 ARG B  50     -36.552 -31.268  49.174  1.00 15.45           N  
ANISOU 3079  NH1 ARG B  50     2722   2234    915    165    210   -127       N  
ATOM   3080  NH2 ARG B  50     -38.414 -30.379  50.194  1.00 16.68           N  
ANISOU 3080  NH2 ARG B  50     2827   2564    947    226    215   -223       N  
ATOM   3081  N   GLU B  51     -38.456 -38.385  49.890  1.00 17.73           N  
ANISOU 3081  N   GLU B  51     3645   2469    623    130    224     90       N  
ATOM   3082  CA  GLU B  51     -37.872 -39.662  50.297  1.00 18.18           C  
ANISOU 3082  CA  GLU B  51     3821   2535    550    232    258     77       C  
ATOM   3083  C   GLU B  51     -37.879 -40.693  49.191  1.00 17.52           C  
ANISOU 3083  C   GLU B  51     3544   2553    559    244    148     75       C  
ATOM   3084  O   GLU B  51     -36.916 -41.408  49.023  1.00 18.30           O  
ANISOU 3084  O   GLU B  51     3515   2746    690    271     71    117       O  
ATOM   3085  CB  GLU B  51     -38.601 -40.218  51.516  1.00 19.58           C  
ANISOU 3085  CB  GLU B  51     3908   2830    698    116    415     57       C  
ATOM   3086  CG  GLU B  51     -38.138 -39.538  52.787  1.00 21.97           C  
ANISOU 3086  CG  GLU B  51     4425   3118    803    140    332   -125       C  
ATOM   3087  CD  GLU B  51     -38.952 -39.890  54.017  1.00 25.92           C  
ANISOU 3087  CD  GLU B  51     5074   3901    870   -147    468     69       C  
ATOM   3088  OE1 GLU B  51     -39.952 -40.641  53.932  1.00 28.79           O  
ANISOU 3088  OE1 GLU B  51     5134   4537   1267   -268    343    319       O  
ATOM   3089  OE2 GLU B  51     -38.577 -39.398  55.094  1.00 27.65           O  
ANISOU 3089  OE2 GLU B  51     5497   4196    814    228    440   -109       O  
ATOM   3090  N   ILE B  52     -38.975 -40.765  48.449  1.00 17.06           N  
ANISOU 3090  N   ILE B  52     3487   2422    573    150    205     -2       N  
ATOM   3091  CA  ILE B  52     -39.069 -41.666  47.303  1.00 17.31           C  
ANISOU 3091  CA  ILE B  52     3392   2650    531    251    190    -87       C  
ATOM   3092  C   ILE B  52     -37.945 -41.366  46.301  1.00 16.92           C  
ANISOU 3092  C   ILE B  52     3249   2419    760    293    135     54       C  
ATOM   3093  O   ILE B  52     -37.265 -42.286  45.862  1.00 18.27           O  
ANISOU 3093  O   ILE B  52     3394   2550    994    408    218     48       O  
ATOM   3094  CB  ILE B  52     -40.465 -41.582  46.637  1.00 17.69           C  
ANISOU 3094  CB  ILE B  52     3270   2780    670    119    266   -252       C  
ATOM   3095  CG1 ILE B  52     -41.524 -42.263  47.514  1.00 19.06           C  
ANISOU 3095  CG1 ILE B  52     3371   2771   1099    -28    298   -130       C  
ATOM   3096  CG2 ILE B  52     -40.456 -42.220  45.248  1.00 17.46           C  
ANISOU 3096  CG2 ILE B  52     3274   2687    671    153    390   -226       C  
ATOM   3097  CD1 ILE B  52     -42.965 -41.854  47.226  1.00 22.31           C  
ANISOU 3097  CD1 ILE B  52     3552   3194   1728    202    161    -90       C  
ATOM   3098  N   ILE B  53     -37.751 -40.090  45.959  1.00 16.29           N  
ANISOU 3098  N   ILE B  53     3247   2445    497    155     70      2       N  
ATOM   3099  CA  ILE B  53     -36.714 -39.669  44.996  1.00 16.56           C  
ANISOU 3099  CA  ILE B  53     3217   2293    781    325    263     -4       C  
ATOM   3100  C   ILE B  53     -35.320 -39.974  45.542  1.00 17.00           C  
ANISOU 3100  C   ILE B  53     3263   2351    843    252    123   -213       C  
ATOM   3101  O   ILE B  53     -34.485 -40.583  44.849  1.00 17.65           O  
ANISOU 3101  O   ILE B  53     3340   2614    753    344    294    -21       O  
ATOM   3102  CB  ILE B  53     -36.846 -38.169  44.624  1.00 16.59           C  
ANISOU 3102  CB  ILE B  53     3224   2319    761    275    281     36       C  
ATOM   3103  CG1 ILE B  53     -38.142 -37.925  43.851  1.00 16.02           C  
ANISOU 3103  CG1 ILE B  53     3137   2401    547    309    490    193       C  
ATOM   3104  CG2 ILE B  53     -35.618 -37.661  43.855  1.00 16.43           C  
ANISOU 3104  CG2 ILE B  53     3062   2302    877    227    168    -47       C  
ATOM   3105  CD1 ILE B  53     -38.654 -36.515  44.013  1.00 17.19           C  
ANISOU 3105  CD1 ILE B  53     3114   2449    965    279    489   -149       C  
ATOM   3106  N   ALA B  54     -35.077 -39.575  46.794  1.00 16.77           N  
ANISOU 3106  N   ALA B  54     3389   2429    554    425     74    229       N  
ATOM   3107  CA  ALA B  54     -33.792 -39.855  47.434  1.00 17.33           C  
ANISOU 3107  CA  ALA B  54     3247   2495    843    371     21   -228       C  
ATOM   3108  C   ALA B  54     -33.471 -41.339  47.382  1.00 17.97           C  
ANISOU 3108  C   ALA B  54     3463   2520    841    366     87    -76       C  
ATOM   3109  O   ALA B  54     -32.396 -41.762  46.950  1.00 17.82           O  
ANISOU 3109  O   ALA B  54     3512   2506    749    393     38    -59       O  
ATOM   3110  CB  ALA B  54     -33.790 -39.373  48.874  1.00 17.39           C  
ANISOU 3110  CB  ALA B  54     3362   2608    636    404    -50     68       C  
ATOM   3111  N   ASP B  55     -34.427 -42.137  47.798  1.00 17.96           N  
ANISOU 3111  N   ASP B  55     3510   2526    788    438     91    110       N  
ATOM   3112  CA AASP B  55     -34.221 -43.582  47.835  0.50 18.87           C  
ANISOU 3112  CA AASP B  55     3625   2518   1023    343    125   -139       C  
ATOM   3113  CA BASP B  55     -34.234 -43.606  47.816  0.50 18.67           C  
ANISOU 3113  CA BASP B  55     3553   2510   1029    349    165   -119       C  
ATOM   3114  C   ASP B  55     -33.906 -44.181  46.453  1.00 19.61           C  
ANISOU 3114  C   ASP B  55     3694   2742   1015    452    183   -108       C  
ATOM   3115  O   ASP B  55     -33.045 -45.027  46.338  1.00 20.27           O  
ANISOU 3115  O   ASP B  55     3761   2691   1247    429    353      0       O  
ATOM   3116  CB AASP B  55     -35.399 -44.247  48.503  0.50 20.39           C  
ANISOU 3116  CB AASP B  55     3738   2959   1048    342    241    -31       C  
ATOM   3117  CB BASP B  55     -35.478 -44.307  48.326  0.50 20.05           C  
ANISOU 3117  CB BASP B  55     3572   2578   1464    412    265      3       C  
ATOM   3118  CG AASP B  55     -35.342 -45.616  48.410  0.50 24.73           C  
ANISOU 3118  CG AASP B  55     4273   3091   2031    287    332   -381       C  
ATOM   3119  CG BASP B  55     -35.684 -44.117  49.810  0.50 21.35           C  
ANISOU 3119  CG BASP B  55     3687   2903   1519    473    346    -84       C  
ATOM   3120  OD1AASP B  55     -35.322 -46.192  49.541  0.50 31.63           O  
ANISOU 3120  OD1AASP B  55     5142   3967   2907    303    -19    548       O  
ATOM   3121  OD1BASP B  55     -34.753 -43.682  50.514  0.50 21.35           O  
ANISOU 3121  OD1BASP B  55     3711   3205   1193    615    156    293       O  
ATOM   3122  OD2AASP B  55     -35.329 -45.968  47.219  0.50 27.19           O  
ANISOU 3122  OD2AASP B  55     4521   3724   2085    241     69   -456       O  
ATOM   3123  OD2BASP B  55     -36.790 -44.406  50.287  0.50 20.63           O  
ANISOU 3123  OD2BASP B  55     4241   2924    672    213    584    225       O  
ATOM   3124  N   THR B  56     -34.575 -43.708  45.425  1.00 18.24           N  
ANISOU 3124  N   THR B  56     3561   2570    798    362    286   -164       N  
ATOM   3125  CA  THR B  56     -34.238 -44.245  44.122  1.00 18.65           C  
ANISOU 3125  CA  THR B  56     3456   2702    928    386    287   -303       C  
ATOM   3126  C   THR B  56     -32.815 -43.886  43.638  1.00 17.96           C  
ANISOU 3126  C   THR B  56     3571   2700    552    299    279     17       C  
ATOM   3127  O   THR B  56     -32.221 -44.663  42.933  1.00 18.71           O  
ANISOU 3127  O   THR B  56     3467   2873    767    357    259    -87       O  
ATOM   3128  CB  THR B  56     -35.366 -44.196  43.029  1.00 21.46           C  
ANISOU 3128  CB  THR B  56     3490   3331   1332    552    160     17       C  
ATOM   3129  OG1 THR B  56     -34.949 -43.588  41.786  1.00 23.71           O  
ANISOU 3129  OG1 THR B  56     3714   2982   2313    186     71    799       O  
ATOM   3130  CG2 THR B  56     -36.598 -43.559  43.496  1.00 16.26           C  
ANISOU 3130  CG2 THR B  56     3639   2184    352    529     59    -78       C  
ATOM   3131  N   LEU B  57     -32.257 -42.776  44.120  1.00 18.47           N  
ANISOU 3131  N   LEU B  57     3452   2643    922    346    184    132       N  
ATOM   3132  CA  LEU B  57     -30.892 -42.368  43.730  1.00 17.19           C  
ANISOU 3132  CA  LEU B  57     3432   2389    708    358    139    200       C  
ATOM   3133  C   LEU B  57     -29.787 -42.803  44.697  1.00 17.98           C  
ANISOU 3133  C   LEU B  57     3516   2543    773    385    -13    -47       C  
ATOM   3134  O   LEU B  57     -28.596 -42.523  44.470  1.00 18.35           O  
ANISOU 3134  O   LEU B  57     3535   2637    800    485    -11    126       O  
ATOM   3135  CB  LEU B  57     -30.812 -40.847  43.553  1.00 17.01           C  
ANISOU 3135  CB  LEU B  57     3293   2380    787    425    153     57       C  
ATOM   3136  CG  LEU B  57     -31.716 -40.188  42.509  1.00 16.01           C  
ANISOU 3136  CG  LEU B  57     3211   2179    693    260    182     46       C  
ATOM   3137  CD1 LEU B  57     -31.588 -38.660  42.589  1.00 15.37           C  
ANISOU 3137  CD1 LEU B  57     3081   2132    625    390    202    250       C  
ATOM   3138  CD2 LEU B  57     -31.357 -40.693  41.116  1.00 18.01           C  
ANISOU 3138  CD2 LEU B  57     3394   2545    901    370    251   -243       C  
ATOM   3139  N   GLY B  58     -30.186 -43.440  45.798  1.00 18.51           N  
ANISOU 3139  N   GLY B  58     3462   2492   1078    336     79    138       N  
ATOM   3140  CA  GLY B  58     -29.251 -43.766  46.860  1.00 19.21           C  
ANISOU 3140  CA  GLY B  58     3668   2638    992    506     50     81       C  
ATOM   3141  C   GLY B  58     -28.724 -42.522  47.563  1.00 19.90           C  
ANISOU 3141  C   GLY B  58     3443   2725   1392    450     -2    146       C  
ATOM   3142  O   GLY B  58     -27.596 -42.509  48.051  1.00 20.92           O  
ANISOU 3142  O   GLY B  58     3467   3062   1418    491   -109    101       O  
ATOM   3143  N   ALA B  59     -29.554 -41.480  47.610  1.00 18.10           N  
ANISOU 3143  N   ALA B  59     3531   2489    855    408    306     62       N  
ATOM   3144  CA  ALA B  59     -29.237 -40.231  48.286  1.00 17.58           C  
ANISOU 3144  CA  ALA B  59     3386   2520    772    302    231    168       C  
ATOM   3145  C   ALA B  59     -30.002 -40.114  49.599  1.00 19.09           C  
ANISOU 3145  C   ALA B  59     3573   2907    771    357    268    100       C  
ATOM   3146  O   ALA B  59     -30.892 -40.923  49.901  1.00 19.27           O  
ANISOU 3146  O   ALA B  59     3728   2749    841    205    -72    182       O  
ATOM   3147  CB  ALA B  59     -29.592 -39.056  47.393  1.00 17.33           C  
ANISOU 3147  CB  ALA B  59     3275   2553    754    362    106    110       C  
ATOM   3148  N   MET B  60     -29.636 -39.094  50.376  1.00 18.94           N  
ANISOU 3148  N   MET B  60     3458   2821    917    456    128    185       N  
ATOM   3149  CA  MET B  60     -30.379 -38.697  51.573  1.00 19.73           C  
ANISOU 3149  CA  MET B  60     3550   3112    834    465     30     44       C  
ATOM   3150  C   MET B  60     -31.471 -37.688  51.186  1.00 18.48           C  
ANISOU 3150  C   MET B  60     3356   2809    857    261    251    161       C  
ATOM   3151  O   MET B  60     -31.261 -36.887  50.288  1.00 17.49           O  
ANISOU 3151  O   MET B  60     3202   2709    734    345    136    120       O  
ATOM   3152  CB  MET B  60     -29.436 -38.071  52.611  1.00 20.81           C  
ANISOU 3152  CB  MET B  60     3699   3292    914    373    -23     -5       C  
ATOM   3153  CG  MET B  60     -28.369 -39.005  53.162  1.00 25.30           C  
ANISOU 3153  CG  MET B  60     4011   4370   1230    928   -133     -1       C  
ATOM   3154  SD  MET B  60     -29.105 -40.377  54.096  1.00 37.13           S  
ANISOU 3154  SD  MET B  60     6031   3843   4232   1033   -374    663       S  
ATOM   3155  CE  MET B  60     -28.794 -41.680  52.931  1.00 30.87           C  
ANISOU 3155  CE  MET B  60     4449   4705   2574    657   -173    610       C  
ATOM   3156  N   PRO B  61     -32.642 -37.724  51.847  1.00 18.63           N  
ANISOU 3156  N   PRO B  61     3277   2806    994    254    257    168       N  
ATOM   3157  CA  PRO B  61     -33.729 -36.801  51.466  1.00 17.44           C  
ANISOU 3157  CA  PRO B  61     3120   2750    757    230    341    103       C  
ATOM   3158  C   PRO B  61     -33.317 -35.325  51.375  1.00 17.03           C  
ANISOU 3158  C   PRO B  61     3115   2798    554    215    228     91       C  
ATOM   3159  O   PRO B  61     -33.718 -34.630  50.449  1.00 16.57           O  
ANISOU 3159  O   PRO B  61     2931   2714    650    303    185     18       O  
ATOM   3160  CB  PRO B  61     -34.759 -37.013  52.576  1.00 18.42           C  
ANISOU 3160  CB  PRO B  61     3519   2784    695    269    519    141       C  
ATOM   3161  CG  PRO B  61     -34.543 -38.428  52.992  1.00 16.87           C  
ANISOU 3161  CG  PRO B  61     3254   2782    372    307    347    111       C  
ATOM   3162  CD  PRO B  61     -33.060 -38.652  52.913  1.00 18.32           C  
ANISOU 3162  CD  PRO B  61     3246   2960    754    203    268     72       C  
ATOM   3163  N   SER B  62     -32.513 -34.860  52.327  1.00 17.07           N  
ANISOU 3163  N   SER B  62     3083   2784    617    185    244     55       N  
ATOM   3164  CA  SER B  62     -32.088 -33.466  52.353  1.00 17.57           C  
ANISOU 3164  CA  SER B  62     3166   2884    625     54    101     53       C  
ATOM   3165  C   SER B  62     -31.240 -33.068  51.142  1.00 16.80           C  
ANISOU 3165  C   SER B  62     2909   2861    613    166     28     41       C  
ATOM   3166  O   SER B  62     -31.126 -31.895  50.838  1.00 16.64           O  
ANISOU 3166  O   SER B  62     3181   2865    274    228     57   -127       O  
ATOM   3167  CB  SER B  62     -31.331 -33.154  53.649  1.00 20.22           C  
ANISOU 3167  CB  SER B  62     3469   3317    896    -19   -121   -118       C  
ATOM   3168  OG  SER B  62     -30.032 -33.699  53.603  1.00 21.55           O  
ANISOU 3168  OG  SER B  62     3472   4013    701     33     19    175       O  
ATOM   3169  N   GLU B  63     -30.658 -34.054  50.459  1.00 16.74           N  
ANISOU 3169  N   GLU B  63     2833   2976    552    329    149    259       N  
ATOM   3170  CA  GLU B  63     -29.850 -33.828  49.256  1.00 15.35           C  
ANISOU 3170  CA  GLU B  63     2543   2746    543    363     54    127       C  
ATOM   3171  C   GLU B  63     -30.675 -33.658  47.973  1.00 15.51           C  
ANISOU 3171  C   GLU B  63     2571   2699    620    374    -21     46       C  
ATOM   3172  O   GLU B  63     -30.097 -33.397  46.917  1.00 16.01           O  
ANISOU 3172  O   GLU B  63     2850   2702    530    233   -114    143       O  
ATOM   3173  CB  GLU B  63     -28.830 -34.950  49.089  1.00 15.56           C  
ANISOU 3173  CB  GLU B  63     2567   2728    615    413    -92    182       C  
ATOM   3174  CG  GLU B  63     -27.919 -35.103  50.300  1.00 16.96           C  
ANISOU 3174  CG  GLU B  63     2669   2928    846    354   -298    123       C  
ATOM   3175  CD  GLU B  63     -26.958 -36.262  50.182  1.00 18.08           C  
ANISOU 3175  CD  GLU B  63     2987   2850   1033    429     -1    166       C  
ATOM   3176  OE1 GLU B  63     -25.744 -36.028  50.381  1.00 19.74           O  
ANISOU 3176  OE1 GLU B  63     3119   2968   1411    589   -407    306       O  
ATOM   3177  OE2 GLU B  63     -27.412 -37.396  49.897  1.00 18.75           O  
ANISOU 3177  OE2 GLU B  63     3296   2839    987    559    -23    -89       O  
ATOM   3178  N   ILE B  64     -32.002 -33.790  48.071  1.00 15.34           N  
ANISOU 3178  N   ILE B  64     2533   2640    655    354   -133     79       N  
ATOM   3179  CA  ILE B  64     -32.920 -33.531  46.940  1.00 14.91           C  
ANISOU 3179  CA  ILE B  64     2618   2393    654    403   -157     72       C  
ATOM   3180  C   ILE B  64     -33.468 -32.097  47.008  1.00 14.80           C  
ANISOU 3180  C   ILE B  64     2474   2411    736    375     10     -8       C  
ATOM   3181  O   ILE B  64     -34.179 -31.730  47.941  1.00 15.60           O  
ANISOU 3181  O   ILE B  64     2710   2664    549    266    -16   -157       O  
ATOM   3182  CB  ILE B  64     -34.073 -34.573  46.876  1.00 14.64           C  
ANISOU 3182  CB  ILE B  64     2574   2403    584    451    -40     -7       C  
ATOM   3183  CG1 ILE B  64     -33.519 -36.005  46.866  1.00 14.25           C  
ANISOU 3183  CG1 ILE B  64     2635   2362    417    426     43    -59       C  
ATOM   3184  CG2 ILE B  64     -35.004 -34.320  45.695  1.00 15.60           C  
ANISOU 3184  CG2 ILE B  64     2419   2494   1011    424   -271     -3       C  
ATOM   3185  CD1 ILE B  64     -32.503 -36.341  45.772  1.00 14.78           C  
ANISOU 3185  CD1 ILE B  64     2846   2510    260    446    128     54       C  
ATOM   3186  N   VAL B  65     -33.103 -31.292  46.011  1.00 14.57           N  
ANISOU 3186  N   VAL B  65     2481   2445    609    379      2    -53       N  
ATOM   3187  CA  VAL B  65     -33.566 -29.904  45.888  1.00 14.12           C  
ANISOU 3187  CA  VAL B  65     2422   2379    563    293      8    -75       C  
ATOM   3188  C   VAL B  65     -34.632 -29.853  44.792  1.00 14.27           C  
ANISOU 3188  C   VAL B  65     2391   2391    640    287      8    -15       C  
ATOM   3189  O   VAL B  65     -34.327 -30.142  43.628  1.00 14.25           O  
ANISOU 3189  O   VAL B  65     2364   2365    683    361    -73   -166       O  
ATOM   3190  CB  VAL B  65     -32.386 -28.940  45.566  1.00 13.97           C  
ANISOU 3190  CB  VAL B  65     2327   2310    669    349   -166    -56       C  
ATOM   3191  CG1 VAL B  65     -32.867 -27.504  45.357  1.00 14.40           C  
ANISOU 3191  CG1 VAL B  65     2454   2317    699    363   -301     67       C  
ATOM   3192  CG2 VAL B  65     -31.315 -28.997  46.657  1.00 14.28           C  
ANISOU 3192  CG2 VAL B  65     2500   2291    631    170   -253     -1       C  
ATOM   3193  N   PHE B  66     -35.870 -29.503  45.133  1.00 13.82           N  
ANISOU 3193  N   PHE B  66     2309   2240    700    260    -38     34       N  
ATOM   3194  CA  PHE B  66     -36.886 -29.378  44.095  1.00 14.01           C  
ANISOU 3194  CA  PHE B  66     2442   2330    551    213    -13     66       C  
ATOM   3195  C   PHE B  66     -36.678 -28.147  43.218  1.00 14.45           C  
ANISOU 3195  C   PHE B  66     2562   2233    693    168   -133     46       C  
ATOM   3196  O   PHE B  66     -36.222 -27.098  43.682  1.00 13.90           O  
ANISOU 3196  O   PHE B  66     2593   2212    476    236   -111      2       O  
ATOM   3197  CB  PHE B  66     -38.294 -29.408  44.679  1.00 13.32           C  
ANISOU 3197  CB  PHE B  66     2425   2250    386    204    -12    -28       C  
ATOM   3198  CG  PHE B  66     -38.679 -30.746  45.218  1.00 14.94           C  
ANISOU 3198  CG  PHE B  66     2790   2173    713    183    109   -133       C  
ATOM   3199  CD1 PHE B  66     -38.855 -30.928  46.579  1.00 15.39           C  
ANISOU 3199  CD1 PHE B  66     2830   2285    731    174     43     38       C  
ATOM   3200  CD2 PHE B  66     -38.836 -31.845  44.372  1.00 15.78           C  
ANISOU 3200  CD2 PHE B  66     2958   2108    927    138     22   -143       C  
ATOM   3201  CE1 PHE B  66     -39.215 -32.177  47.084  1.00 16.34           C  
ANISOU 3201  CE1 PHE B  66     3081   2267    857    118    160    -41       C  
ATOM   3202  CE2 PHE B  66     -39.190 -33.094  44.874  1.00 16.66           C  
ANISOU 3202  CE2 PHE B  66     3337   2213    777    182    112    -16       C  
ATOM   3203  CZ  PHE B  66     -39.370 -33.267  46.239  1.00 16.79           C  
ANISOU 3203  CZ  PHE B  66     3157   2448    771    169    206   -124       C  
ATOM   3204  N   THR B  67     -36.987 -28.311  41.936  1.00 14.31           N  
ANISOU 3204  N   THR B  67     2483   2263    691    188    -79    -55       N  
ATOM   3205  CA  THR B  67     -36.893 -27.239  40.949  1.00 15.00           C  
ANISOU 3205  CA  THR B  67     2559   2416    722    143    -76     25       C  
ATOM   3206  C   THR B  67     -38.095 -27.417  40.035  1.00 15.48           C  
ANISOU 3206  C   THR B  67     2660   2553    668    154   -124    -75       C  
ATOM   3207  O   THR B  67     -38.936 -28.288  40.266  1.00 15.47           O  
ANISOU 3207  O   THR B  67     2735   2520    621    108   -222   -117       O  
ATOM   3208  CB  THR B  67     -35.629 -27.396  40.092  1.00 14.69           C  
ANISOU 3208  CB  THR B  67     2549   2299    734    126    -55     21       C  
ATOM   3209  OG1 THR B  67     -35.742 -28.625  39.366  1.00 14.89           O  
ANISOU 3209  OG1 THR B  67     2714   2367    575    114    -87      4       O  
ATOM   3210  CG2 THR B  67     -34.344 -27.416  40.964  1.00 15.41           C  
ANISOU 3210  CG2 THR B  67     2582   2516    757     71    -85     -7       C  
ATOM   3211  N   CYS B  68     -38.184 -26.634  38.972  1.00 16.26           N  
ANISOU 3211  N   CYS B  68     2807   2527    844    314   -146    -31       N  
ATOM   3212  CA  CYS B  68     -39.301 -26.883  38.067  1.00 17.15           C  
ANISOU 3212  CA  CYS B  68     3024   2769    721    290   -241   -134       C  
ATOM   3213  C   CYS B  68     -38.959 -27.800  36.904  1.00 15.71           C  
ANISOU 3213  C   CYS B  68     2816   2417    735    181    -51     32       C  
ATOM   3214  O   CYS B  68     -39.798 -28.044  36.049  1.00 16.34           O  
ANISOU 3214  O   CYS B  68     2827   2716    664    104      0     72       O  
ATOM   3215  CB  CYS B  68     -39.934 -25.596  37.587  1.00 20.96           C  
ANISOU 3215  CB  CYS B  68     3615   2823   1526    423   -409   -186       C  
ATOM   3216  SG  CYS B  68     -38.862 -24.639  36.548  1.00 31.42           S  
ANISOU 3216  SG  CYS B  68     5086   4193   2660     22   -103    508       S  
ATOM   3217  N   GLY B  69     -37.741 -28.318  36.887  1.00 14.72           N  
ANISOU 3217  N   GLY B  69     2818   2251    524    178     20    -24       N  
ATOM   3218  CA  GLY B  69     -37.321 -29.225  35.820  1.00 15.09           C  
ANISOU 3218  CA  GLY B  69     2724   2442    568    264     39    -69       C  
ATOM   3219  C   GLY B  69     -35.824 -29.306  35.641  1.00 14.57           C  
ANISOU 3219  C   GLY B  69     2724   2224    586    283     34    -14       C  
ATOM   3220  O   GLY B  69     -35.056 -28.650  36.358  1.00 15.10           O  
ANISOU 3220  O   GLY B  69     2788   2309    638    153     90    -15       O  
ATOM   3221  N   ALA B  70     -35.400 -30.118  34.680  1.00 14.41           N  
ANISOU 3221  N   ALA B  70     2627   2330    518    333     67     28       N  
ATOM   3222  CA  ALA B  70     -33.976 -30.336  34.465  1.00 14.09           C  
ANISOU 3222  CA  ALA B  70     2618   2166    566    185    104    -50       C  
ATOM   3223  C   ALA B  70     -33.263 -29.078  33.965  1.00 14.37           C  
ANISOU 3223  C   ALA B  70     2722   2121    616    173     -2    -30       C  
ATOM   3224  O   ALA B  70     -32.083 -28.898  34.237  1.00 14.44           O  
ANISOU 3224  O   ALA B  70     2677   2244    565    211     64      6       O  
ATOM   3225  CB  ALA B  70     -33.739 -31.515  33.527  1.00 13.65           C  
ANISOU 3225  CB  ALA B  70     2628   2062    495    222     14     13       C  
ATOM   3226  N   SER B  71     -33.967 -28.206  33.236  1.00 14.34           N  
ANISOU 3226  N   SER B  71     2737   2034    678    251    -16   -149       N  
ATOM   3227  CA  SER B  71     -33.372 -26.926  32.811  1.00 15.22           C  
ANISOU 3227  CA  SER B  71     2935   2176    672    106   -118    -51       C  
ATOM   3228  C   SER B  71     -32.986 -26.063  34.012  1.00 14.45           C  
ANISOU 3228  C   SER B  71     2610   2224    655    236    -53   -110       C  
ATOM   3229  O   SER B  71     -31.842 -25.621  34.110  1.00 14.53           O  
ANISOU 3229  O   SER B  71     2710   2143    664     74    -38   -160       O  
ATOM   3230  CB  SER B  71     -34.302 -26.133  31.886  1.00 16.56           C  
ANISOU 3230  CB  SER B  71     3078   2303    910    181   -199     33       C  
ATOM   3231  OG  SER B  71     -34.582 -26.848  30.701  1.00 17.93           O  
ANISOU 3231  OG  SER B  71     3419   2659    734    277   -223     40       O  
ATOM   3232  N   GLU B  72     -33.924 -25.827  34.921  1.00 14.27           N  
ANISOU 3232  N   GLU B  72     2642   2222    556    170     22     25       N  
ATOM   3233  CA  GLU B  72     -33.605 -25.072  36.119  1.00 14.31           C  
ANISOU 3233  CA  GLU B  72     2517   2270    649    127     45    -77       C  
ATOM   3234  C   GLU B  72     -32.513 -25.792  36.918  1.00 14.70           C  
ANISOU 3234  C   GLU B  72     2656   2233    693    147      2    -91       C  
ATOM   3235  O   GLU B  72     -31.558 -25.156  37.398  1.00 14.06           O  
ANISOU 3235  O   GLU B  72     2630   2159    552    189     -3     -4       O  
ATOM   3236  CB  GLU B  72     -34.851 -24.829  36.973  1.00 14.50           C  
ANISOU 3236  CB  GLU B  72     2573   2382    552    149     17   -154       C  
ATOM   3237  CG  GLU B  72     -34.462 -24.087  38.242  1.00 15.13           C  
ANISOU 3237  CG  GLU B  72     2778   2416    555     22     71   -176       C  
ATOM   3238  CD  GLU B  72     -35.565 -23.942  39.266  1.00 15.58           C  
ANISOU 3238  CD  GLU B  72     2615   2533    771     16     21   -289       C  
ATOM   3239  OE1 GLU B  72     -35.211 -23.619  40.419  1.00 15.73           O  
ANISOU 3239  OE1 GLU B  72     2859   2473    643    122     17   -143       O  
ATOM   3240  OE2 GLU B  72     -36.758 -24.120  38.943  1.00 15.58           O  
ANISOU 3240  OE2 GLU B  72     2529   2650    739     78    144    -15       O  
ATOM   3241  N   SER B  73     -32.620 -27.119  37.010  1.00 14.62           N  
ANISOU 3241  N   SER B  73     2716   2226    612    261      2    -75       N  
ATOM   3242  CA  SER B  73     -31.601 -27.917  37.708  1.00 14.26           C  
ANISOU 3242  CA  SER B  73     2594   2277    545    227     95    -99       C  
ATOM   3243  C   SER B  73     -30.191 -27.772  37.117  1.00 14.88           C  
ANISOU 3243  C   SER B  73     2507   2411    733    197      7   -115       C  
ATOM   3244  O   SER B  73     -29.234 -27.559  37.859  1.00 14.54           O  
ANISOU 3244  O   SER B  73     2667   2302    553    218    -14    -51       O  
ATOM   3245  CB  SER B  73     -31.993 -29.390  37.764  1.00 14.96           C  
ANISOU 3245  CB  SER B  73     2691   2276    717    278    168     35       C  
ATOM   3246  OG  SER B  73     -33.178 -29.566  38.515  1.00 14.18           O  
ANISOU 3246  OG  SER B  73     2628   2299    459    234     -1     58       O  
ATOM   3247  N   ASN B  74     -30.070 -27.856  35.795  1.00 14.78           N  
ANISOU 3247  N   ASN B  74     2670   2238    705    261     24     58       N  
ATOM   3248  CA  ASN B  74     -28.787 -27.673  35.142  1.00 14.53           C  
ANISOU 3248  CA  ASN B  74     2608   2237    673    137    -58     82       C  
ATOM   3249  C   ASN B  74     -28.222 -26.285  35.409  1.00 14.61           C  
ANISOU 3249  C   ASN B  74     2600   2293    658    156    -39    -13       C  
ATOM   3250  O   ASN B  74     -27.031 -26.125  35.643  1.00 14.92           O  
ANISOU 3250  O   ASN B  74     2602   2378    686    181   -145     81       O  
ATOM   3251  CB  ASN B  74     -28.933 -27.867  33.625  1.00 14.85           C  
ANISOU 3251  CB  ASN B  74     2637   2289    713    144     -5   -134       C  
ATOM   3252  CG  ASN B  74     -29.169 -29.317  33.220  1.00 14.76           C  
ANISOU 3252  CG  ASN B  74     2703   2257    648    160    -13     58       C  
ATOM   3253  OD1 ASN B  74     -29.617 -29.592  32.096  1.00 17.97           O  
ANISOU 3253  OD1 ASN B  74     3147   2845    835     30   -228   -109       O  
ATOM   3254  ND2 ASN B  74     -28.852 -30.246  34.103  1.00 12.50           N  
ANISOU 3254  ND2 ASN B  74     2399   2050    297    153    125   -123       N  
ATOM   3255  N   ASN B  75     -29.089 -25.283  35.357  1.00 14.24           N  
ANISOU 3255  N   ASN B  75     2586   2268    555    124     50     83       N  
ATOM   3256  CA  ASN B  75     -28.682 -23.912  35.604  1.00 14.90           C  
ANISOU 3256  CA  ASN B  75     2620   2320    720    106    -71    -37       C  
ATOM   3257  C   ASN B  75     -28.146 -23.743  37.020  1.00 15.18           C  
ANISOU 3257  C   ASN B  75     2478   2513    776    117   -164    133       C  
ATOM   3258  O   ASN B  75     -27.106 -23.123  37.210  1.00 14.77           O  
ANISOU 3258  O   ASN B  75     2532   2518    561     58   -142     64       O  
ATOM   3259  CB  ASN B  75     -29.835 -22.951  35.318  1.00 14.58           C  
ANISOU 3259  CB  ASN B  75     2550   2350    638     85    -29     -6       C  
ATOM   3260  CG  ASN B  75     -29.927 -22.557  33.842  1.00 14.38           C  
ANISOU 3260  CG  ASN B  75     2675   2118    669    109    -67      1       C  
ATOM   3261  OD1 ASN B  75     -30.399 -23.324  33.003  1.00 16.09           O  
ANISOU 3261  OD1 ASN B  75     2808   2449    853    129     -4   -281       O  
ATOM   3262  ND2 ASN B  75     -29.499 -21.352  33.532  1.00 12.27           N  
ANISOU 3262  ND2 ASN B  75     2389   2014    259    271   -103     31       N  
ATOM   3263  N   LEU B  76     -28.845 -24.315  38.001  1.00 14.84           N  
ANISOU 3263  N   LEU B  76     2543   2359    734    229   -106    123       N  
ATOM   3264  CA  LEU B  76     -28.406 -24.252  39.406  1.00 15.16           C  
ANISOU 3264  CA  LEU B  76     2511   2491    755    120    -90     54       C  
ATOM   3265  C   LEU B  76     -27.058 -24.945  39.608  1.00 15.10           C  
ANISOU 3265  C   LEU B  76     2605   2312    816    155   -115     64       C  
ATOM   3266  O   LEU B  76     -26.157 -24.387  40.225  1.00 15.39           O  
ANISOU 3266  O   LEU B  76     2672   2482    693    184    -94    -57       O  
ATOM   3267  CB  LEU B  76     -29.460 -24.849  40.346  1.00 14.87           C  
ANISOU 3267  CB  LEU B  76     2616   2243    790    171    -38    118       C  
ATOM   3268  CG  LEU B  76     -29.074 -24.918  41.833  1.00 14.92           C  
ANISOU 3268  CG  LEU B  76     2634   2292    742    -68     27    -51       C  
ATOM   3269  CD1 LEU B  76     -28.694 -23.545  42.399  1.00 14.85           C  
ANISOU 3269  CD1 LEU B  76     2801   2324    517     60     15   -127       C  
ATOM   3270  CD2 LEU B  76     -30.201 -25.529  42.662  1.00 13.99           C  
ANISOU 3270  CD2 LEU B  76     2753   1925    636    100     68     51       C  
ATOM   3271  N   ALA B  77     -26.920 -26.157  39.080  1.00 14.82           N  
ANISOU 3271  N   ALA B  77     2571   2302    755    174     40     77       N  
ATOM   3272  CA  ALA B  77     -25.656 -26.891  39.194  1.00 14.92           C  
ANISOU 3272  CA  ALA B  77     2601   2307    757    243     27    -39       C  
ATOM   3273  C   ALA B  77     -24.470 -26.092  38.647  1.00 15.34           C  
ANISOU 3273  C   ALA B  77     2589   2497    742    156   -157    115       C  
ATOM   3274  O   ALA B  77     -23.425 -26.038  39.296  1.00 15.33           O  
ANISOU 3274  O   ALA B  77     2812   2614    397     81   -184    -74       O  
ATOM   3275  CB  ALA B  77     -25.744 -28.243  38.492  1.00 15.06           C  
ANISOU 3275  CB  ALA B  77     2609   2292    820    241   -142    -45       C  
ATOM   3276  N   ILE B  78     -24.646 -25.477  37.478  1.00 15.27           N  
ANISOU 3276  N   ILE B  78     2630   2395    777     35   -153    156       N  
ATOM   3277  CA  ILE B  78     -23.559 -24.808  36.783  1.00 15.06           C  
ANISOU 3277  CA  ILE B  78     2456   2542    721    183   -102     97       C  
ATOM   3278  C   ILE B  78     -23.293 -23.401  37.328  1.00 15.47           C  
ANISOU 3278  C   ILE B  78     2635   2611    630    159   -181     80       C  
ATOM   3279  O   ILE B  78     -22.168 -23.084  37.738  1.00 15.72           O  
ANISOU 3279  O   ILE B  78     2609   2717    648    172   -157     52       O  
ATOM   3280  CB  ILE B  78     -23.832 -24.790  35.270  1.00 15.91           C  
ANISOU 3280  CB  ILE B  78     2796   2544    703     90    -56    167       C  
ATOM   3281  CG1 ILE B  78     -23.828 -26.236  34.756  1.00 15.83           C  
ANISOU 3281  CG1 ILE B  78     2782   2584    647    110   -239     53       C  
ATOM   3282  CG2 ILE B  78     -22.809 -23.922  34.549  1.00 16.11           C  
ANISOU 3282  CG2 ILE B  78     2697   2644    780     91    -91    229       C  
ATOM   3283  CD1 ILE B  78     -24.350 -26.412  33.333  1.00 16.04           C  
ANISOU 3283  CD1 ILE B  78     2850   2711    531    297    -34    -96       C  
ATOM   3284  N   LYS B  79     -24.328 -22.563  37.329  1.00 14.88           N  
ANISOU 3284  N   LYS B  79     2589   2618    444    180     87     44       N  
ATOM   3285  CA  LYS B  79     -24.204 -21.186  37.810  1.00 16.15           C  
ANISOU 3285  CA  LYS B  79     2668   2683    784    175    -61    -35       C  
ATOM   3286  C   LYS B  79     -23.979 -21.138  39.319  1.00 16.84           C  
ANISOU 3286  C   LYS B  79     2683   2912    801    200   -113    -55       C  
ATOM   3287  O   LYS B  79     -23.327 -20.225  39.822  1.00 18.13           O  
ANISOU 3287  O   LYS B  79     2933   3005    950     80    -93   -166       O  
ATOM   3288  CB  LYS B  79     -25.441 -20.366  37.441  1.00 17.38           C  
ANISOU 3288  CB  LYS B  79     2798   2969    835    229   -355     40       C  
ATOM   3289  CG  LYS B  79     -25.604 -20.151  35.947  1.00 16.06           C  
ANISOU 3289  CG  LYS B  79     2560   2835    705    197    -14   -152       C  
ATOM   3290  CD  LYS B  79     -26.988 -19.621  35.642  1.00 15.79           C  
ANISOU 3290  CD  LYS B  79     2650   2544    804    170   -202   -244       C  
ATOM   3291  CE  LYS B  79     -27.131 -19.301  34.172  1.00 16.41           C  
ANISOU 3291  CE  LYS B  79     2757   2486    991    269   -371     83       C  
ATOM   3292  NZ  LYS B  79     -28.390 -18.553  33.911  1.00 15.24           N  
ANISOU 3292  NZ  LYS B  79     2935   2230    624    307   -370     21       N  
ATOM   3293  N   GLY B  80     -24.495 -22.135  40.034  1.00 16.30           N  
ANISOU 3293  N   GLY B  80     2644   2779    769    264   -108    -93       N  
ATOM   3294  CA  GLY B  80     -24.322 -22.205  41.486  1.00 16.90           C  
ANISOU 3294  CA  GLY B  80     2711   2896    813    316   -246    -27       C  
ATOM   3295  C   GLY B  80     -22.857 -22.280  41.863  1.00 17.18           C  
ANISOU 3295  C   GLY B  80     2639   3102    787    100   -102   -181       C  
ATOM   3296  O   GLY B  80     -22.447 -21.753  42.896  1.00 17.85           O  
ANISOU 3296  O   GLY B  80     2640   3160    980     76    -52   -420       O  
ATOM   3297  N   LEU B  81     -22.075 -22.948  41.023  1.00 16.91           N  
ANISOU 3297  N   LEU B  81     2665   2756   1003    144    -19    -76       N  
ATOM   3298  CA  LEU B  81     -20.648 -22.987  41.203  1.00 17.11           C  
ANISOU 3298  CA  LEU B  81     2706   2809    982     90   -204   -201       C  
ATOM   3299  C   LEU B  81     -19.943 -21.797  40.576  1.00 18.30           C  
ANISOU 3299  C   LEU B  81     2922   3125    903     43   -127     27       C  
ATOM   3300  O   LEU B  81     -19.056 -21.228  41.198  1.00 20.31           O  
ANISOU 3300  O   LEU B  81     3116   3277   1323   -231   -122    -77       O  
ATOM   3301  CB  LEU B  81     -20.085 -24.298  40.669  1.00 16.75           C  
ANISOU 3301  CB  LEU B  81     2654   2837    870    134   -210   -225       C  
ATOM   3302  CG  LEU B  81     -20.429 -25.537  41.499  1.00 17.26           C  
ANISOU 3302  CG  LEU B  81     2893   2833    829    208   -208   -223       C  
ATOM   3303  CD1 LEU B  81     -19.754 -26.737  40.847  1.00 17.46           C  
ANISOU 3303  CD1 LEU B  81     2658   2860   1115    239    -90   -203       C  
ATOM   3304  CD2 LEU B  81     -19.994 -25.386  42.962  1.00 18.70           C  
ANISOU 3304  CD2 LEU B  81     3032   3289    783    110   -153   -126       C  
ATOM   3305  N   ALA B  82     -20.369 -21.396  39.383  1.00 17.31           N  
ANISOU 3305  N   ALA B  82     2793   2923    860     -6   -174    -92       N  
ATOM   3306  CA  ALA B  82     -19.692 -20.334  38.659  1.00 19.28           C  
ANISOU 3306  CA  ALA B  82     3023   3071   1230    -45   -111     76       C  
ATOM   3307  C   ALA B  82     -19.772 -19.008  39.346  1.00 20.21           C  
ANISOU 3307  C   ALA B  82     3199   3275   1202     23    178     26       C  
ATOM   3308  O   ALA B  82     -18.903 -18.189  39.157  1.00 21.08           O  
ANISOU 3308  O   ALA B  82     3083   3199   1725    -31   -100   -178       O  
ATOM   3309  CB  ALA B  82     -20.255 -20.179  37.259  1.00 18.90           C  
ANISOU 3309  CB  ALA B  82     2899   3138   1142    120     33    121       C  
ATOM   3310  N   PHE B  83     -20.866 -18.773  40.067  1.00 20.35           N  
ANISOU 3310  N   PHE B  83     3207   3313   1210     32    131   -104       N  
ATOM   3311  CA  PHE B  83     -21.189 -17.436  40.583  1.00 21.47           C  
ANISOU 3311  CA  PHE B  83     3157   3326   1674     65    116   -145       C  
ATOM   3312  C   PHE B  83     -20.460 -17.145  41.893  1.00 22.47           C  
ANISOU 3312  C   PHE B  83     3379   3514   1644    -28    118   -177       C  
ATOM   3313  O   PHE B  83     -20.611 -16.079  42.469  1.00 25.42           O  
ANISOU 3313  O   PHE B  83     3847   3959   1850    -87    355   -584       O  
ATOM   3314  CB  PHE B  83     -22.704 -17.209  40.744  1.00 20.88           C  
ANISOU 3314  CB  PHE B  83     3193   3191   1546    150    100   -228       C  
ATOM   3315  CG  PHE B  83     -23.459 -16.991  39.442  1.00 21.96           C  
ANISOU 3315  CG  PHE B  83     3267   3629   1448    340    344    141       C  
ATOM   3316  CD1 PHE B  83     -22.825 -17.025  38.216  1.00 20.68           C  
ANISOU 3316  CD1 PHE B  83     3325   3242   1288    352    191   -244       C  
ATOM   3317  CD2 PHE B  83     -24.835 -16.812  39.463  1.00 24.54           C  
ANISOU 3317  CD2 PHE B  83     3375   3735   2212    368   -137    120       C  
ATOM   3318  CE1 PHE B  83     -23.538 -16.842  37.045  1.00 22.95           C  
ANISOU 3318  CE1 PHE B  83     3235   3844   1640    327      0   -270       C  
ATOM   3319  CE2 PHE B  83     -25.555 -16.629  38.299  1.00 24.59           C  
ANISOU 3319  CE2 PHE B  83     3574   3905   1861    -56      4    -47       C  
ATOM   3320  CZ  PHE B  83     -24.903 -16.642  37.078  1.00 23.72           C  
ANISOU 3320  CZ  PHE B  83     3333   3729   1948    535     14   -186       C  
ATOM   3321  N   LYS B  84     -19.753 -18.156  42.402  1.00 20.85           N  
ANISOU 3321  N   LYS B  84     3122   3572   1228   -181     54   -138       N  
ATOM   3322  CA  LYS B  84     -18.819 -18.042  43.529  1.00 23.84           C  
ANISOU 3322  CA  LYS B  84     3447   3892   1717   -276   -335    -71       C  
ATOM   3323  C   LYS B  84     -17.431 -17.671  43.042  1.00 24.62           C  
ANISOU 3323  C   LYS B  84     3493   4078   1783   -275   -176   -256       C  
ATOM   3324  O   LYS B  84     -16.532 -17.420  43.842  1.00 27.05           O  
ANISOU 3324  O   LYS B  84     3856   4472   1948   -533   -284   -558       O  
ATOM   3325  CB  LYS B  84     -18.658 -19.390  44.251  1.00 25.16           C  
ANISOU 3325  CB  LYS B  84     3587   4164   1808    -87   -174    171       C  
ATOM   3326  CG  LYS B  84     -19.888 -19.925  44.956  0.50 24.65           C  
ANISOU 3326  CG  LYS B  84     3478   3697   2190   -160   -249     26       C  
ATOM   3327  CD  LYS B  84     -19.923 -21.450  44.956  0.50 23.75           C  
ANISOU 3327  CD  LYS B  84     3455   3698   1871   -102    -89    -51       C  
ATOM   3328  CE  LYS B  84     -18.787 -22.031  45.792  0.50 24.75           C  
ANISOU 3328  CE  LYS B  84     3716   3762   1925   -157   -146    356       C  
ATOM   3329  NZ  LYS B  84     -18.765 -23.522  45.797  0.50 25.39           N  
ANISOU 3329  NZ  LYS B  84     4003   3836   1808    -40   -175   -175       N  
ATOM   3330  N   ARG B  85     -17.251 -17.695  41.722  1.00 23.11           N  
ANISOU 3330  N   ARG B  85     3401   3585   1793   -304    -32   -109       N  
ATOM   3331  CA  ARG B  85     -15.945 -17.539  41.104  1.00 24.44           C  
ANISOU 3331  CA  ARG B  85     3518   3729   2037   -250     61   -380       C  
ATOM   3332  C   ARG B  85     -15.923 -16.391  40.127  1.00 24.06           C  
ANISOU 3332  C   ARG B  85     3407   3616   2119   -379    117   -386       C  
ATOM   3333  O   ARG B  85     -15.244 -16.467  39.116  1.00 24.20           O  
ANISOU 3333  O   ARG B  85     3539   3595   2059   -302     37   -608       O  
ATOM   3334  CB  ARG B  85     -15.597 -18.795  40.314  1.00 26.25           C  
ANISOU 3334  CB  ARG B  85     3748   3736   2489   -150     79   -406       C  
ATOM   3335  CG  ARG B  85     -15.386 -20.009  41.178  1.00 27.40           C  
ANISOU 3335  CG  ARG B  85     4065   3674   2668    -14     52   -493       C  
ATOM   3336  CD  ARG B  85     -15.102 -21.205  40.311  1.00 25.51           C  
ANISOU 3336  CD  ARG B  85     4051   3898   1743     43    193   -335       C  
ATOM   3337  NE  ARG B  85     -13.776 -21.099  39.741  1.00 25.69           N  
ANISOU 3337  NE  ARG B  85     4025   3831   1903    -49     12   -312       N  
ATOM   3338  CZ  ARG B  85     -12.724 -21.752  40.209  1.00 27.31           C  
ANISOU 3338  CZ  ARG B  85     4172   3890   2315    157     81   -419       C  
ATOM   3339  NH1 ARG B  85     -12.848 -22.561  41.249  1.00 29.15           N  
ANISOU 3339  NH1 ARG B  85     5120   3800   2153    165    132   -481       N  
ATOM   3340  NH2 ARG B  85     -11.552 -21.589  39.630  1.00 28.19           N  
ANISOU 3340  NH2 ARG B  85     4000   4184   2526     -1     21   -650       N  
ATOM   3341  N   LEU B  86     -16.691 -15.350  40.401  1.00 23.00           N  
ANISOU 3341  N   LEU B  86     3158   3563   2018   -378     22   -146       N  
ATOM   3342  CA  LEU B  86     -16.838 -14.314  39.408  1.00 24.62           C  
ANISOU 3342  CA  LEU B  86     3474   3542   2335   -132    339    -68       C  
ATOM   3343  C   LEU B  86     -15.555 -13.562  39.155  1.00 27.51           C  
ANISOU 3343  C   LEU B  86     3602   3987   2862   -364    436   -438       C  
ATOM   3344  O   LEU B  86     -15.337 -13.104  38.054  1.00 29.53           O  
ANISOU 3344  O   LEU B  86     4045   3919   3256   -656    497   -180       O  
ATOM   3345  CB  LEU B  86     -17.956 -13.351  39.764  1.00 25.50           C  
ANISOU 3345  CB  LEU B  86     3447   3791   2449   -149    389   -372       C  
ATOM   3346  CG  LEU B  86     -19.365 -13.958  39.693  1.00 22.88           C  
ANISOU 3346  CG  LEU B  86     3378   3552   1763    -59    517   -176       C  
ATOM   3347  CD1 LEU B  86     -20.405 -12.934  40.119  1.00 23.81           C  
ANISOU 3347  CD1 LEU B  86     3409   3449   2186     37    363    -23       C  
ATOM   3348  CD2 LEU B  86     -19.700 -14.522  38.313  1.00 22.78           C  
ANISOU 3348  CD2 LEU B  86     3391   3582   1679     81    406    -24       C  
ATOM   3349  N   GLU B  87     -14.733 -13.381  40.171  1.00 26.38           N  
ANISOU 3349  N   GLU B  87     3555   3862   2604   -270    609   -660       N  
ATOM   3350  CA  GLU B  87     -13.437 -12.751  39.950  1.00 29.92           C  
ANISOU 3350  CA  GLU B  87     3661   4221   3485   -455    396   -456       C  
ATOM   3351  C   GLU B  87     -12.365 -13.626  39.295  1.00 28.05           C  
ANISOU 3351  C   GLU B  87     3702   4063   2890   -477    176   -495       C  
ATOM   3352  O   GLU B  87     -11.722 -13.207  38.341  1.00 28.65           O  
ANISOU 3352  O   GLU B  87     3924   4302   2658   -370     91   -506       O  
ATOM   3353  CB  GLU B  87     -12.907 -12.214  41.254  1.00 33.68           C  
ANISOU 3353  CB  GLU B  87     4178   5028   3591   -760    381   -678       C  
ATOM   3354  CG  GLU B  87     -13.744 -11.091  41.817  1.00 38.76           C  
ANISOU 3354  CG  GLU B  87     4121   5698   4907   -440    680   -713       C  
ATOM   3355  CD  GLU B  87     -13.312 -10.725  43.215  1.00 50.90           C  
ANISOU 3355  CD  GLU B  87     5076   7946   6315   -732   -553  -2029       C  
ATOM   3356  OE1 GLU B  87     -12.120 -10.407  43.409  1.00 54.53           O  
ANISOU 3356  OE1 GLU B  87     5339   7805   7573  -1624    -56  -1475       O  
ATOM   3357  OE2 GLU B  87     -14.162 -10.766  44.127  1.00 60.67           O  
ANISOU 3357  OE2 GLU B  87     5464   9786   7802   -664    252  -1392       O  
ATOM   3358  N   GLU B  88     -12.172 -14.839  39.793  1.00 27.14           N  
ANISOU 3358  N   GLU B  88     3674   3964   2674   -289    150   -751       N  
ATOM   3359  CA  GLU B  88     -11.081 -15.672  39.304  1.00 26.54           C  
ANISOU 3359  CA  GLU B  88     3810   3781   2492   -224    -63   -794       C  
ATOM   3360  C   GLU B  88     -11.488 -16.457  38.068  1.00 25.46           C  
ANISOU 3360  C   GLU B  88     3688   3647   2336   -167    221   -761       C  
ATOM   3361  O   GLU B  88     -10.637 -16.950  37.333  1.00 24.85           O  
ANISOU 3361  O   GLU B  88     3690   3507   2242   -280    144   -903       O  
ATOM   3362  CB  GLU B  88     -10.631 -16.636  40.389  1.00 30.23           C  
ANISOU 3362  CB  GLU B  88     4255   4418   2812   -308   -148   -326       C  
ATOM   3363  CG  GLU B  88     -11.625 -17.742  40.639  1.00 30.50           C  
ANISOU 3363  CG  GLU B  88     4353   4365   2868   -347   -276   -475       C  
ATOM   3364  CD  GLU B  88     -11.259 -18.603  41.826  1.00 34.83           C  
ANISOU 3364  CD  GLU B  88     5072   4770   3392   -161      4     27       C  
ATOM   3365  OE1 GLU B  88     -10.089 -19.030  41.935  1.00 41.58           O  
ANISOU 3365  OE1 GLU B  88     4896   5832   5069   -369   -197   -390       O  
ATOM   3366  OE2 GLU B  88     -12.151 -18.874  42.654  1.00 36.44           O  
ANISOU 3366  OE2 GLU B  88     5090   5033   3724   -554    139   -258       O  
ATOM   3367  N   LYS B  89     -12.795 -16.590  37.881  1.00 25.07           N  
ANISOU 3367  N   LYS B  89     3704   3412   2410   -171     59   -886       N  
ATOM   3368  CA  LYS B  89     -13.343 -17.406  36.829  1.00 24.07           C  
ANISOU 3368  CA  LYS B  89     3754   3499   1891    105    158   -751       C  
ATOM   3369  C   LYS B  89     -12.883 -18.854  36.935  1.00 23.61           C  
ANISOU 3369  C   LYS B  89     3795   3385   1790     26    143   -775       C  
ATOM   3370  O   LYS B  89     -12.739 -19.374  38.019  1.00 24.10           O  
ANISOU 3370  O   LYS B  89     3896   3596   1665     64    216   -711       O  
ATOM   3371  CB  LYS B  89     -13.021 -16.766  35.494  1.00 26.53           C  
ANISOU 3371  CB  LYS B  89     3964   3891   2225     59    162   -466       C  
ATOM   3372  CG  LYS B  89     -14.000 -15.650  35.238  1.00 28.25           C  
ANISOU 3372  CG  LYS B  89     4120   3886   2725    -74   -134   -171       C  
ATOM   3373  CD  LYS B  89     -13.338 -14.367  34.834  1.00 29.83           C  
ANISOU 3373  CD  LYS B  89     4413   3817   3103   -363   -118   -549       C  
ATOM   3374  CE  LYS B  89     -14.331 -13.243  35.061  1.00 32.06           C  
ANISOU 3374  CE  LYS B  89     4508   4479   3191     40   -184   -862       C  
ATOM   3375  NZ  LYS B  89     -13.708 -12.186  35.896  1.00 33.05           N  
ANISOU 3375  NZ  LYS B  89     4845   3770   3940   -476    -53   -409       N  
ATOM   3376  N   GLY B  90     -12.660 -19.486  35.784  1.00 21.71           N  
ANISOU 3376  N   GLY B  90     3475   3413   1358     65     24   -429       N  
ATOM   3377  CA  GLY B  90     -12.400 -20.924  35.735  1.00 23.14           C  
ANISOU 3377  CA  GLY B  90     3535   3425   1832    118     34   -559       C  
ATOM   3378  C   GLY B  90     -12.846 -21.636  34.474  1.00 20.42           C  
ANISOU 3378  C   GLY B  90     3247   3314   1196    219    190    -68       C  
ATOM   3379  O   GLY B  90     -13.345 -21.027  33.530  1.00 20.72           O  
ANISOU 3379  O   GLY B  90     3046   3524   1300    202    -82   -120       O  
ATOM   3380  N   HIS B  91     -12.679 -22.948  34.485  1.00 20.27           N  
ANISOU 3380  N   HIS B  91     3194   3198   1306    107    246   -146       N  
ATOM   3381  CA  HIS B  91     -12.849 -23.774  33.315  1.00 19.46           C  
ANISOU 3381  CA  HIS B  91     2918   3320   1154     67    150    -74       C  
ATOM   3382  C   HIS B  91     -13.817 -24.859  33.645  1.00 19.42           C  
ANISOU 3382  C   HIS B  91     2960   3163   1256    117     95    -10       C  
ATOM   3383  O   HIS B  91     -13.789 -25.416  34.740  1.00 19.53           O  
ANISOU 3383  O   HIS B  91     2901   3372   1144    142    144    -74       O  
ATOM   3384  CB  HIS B  91     -11.499 -24.345  32.926  1.00 19.53           C  
ANISOU 3384  CB  HIS B  91     2854   3421   1145     79    118    -50       C  
ATOM   3385  CG  HIS B  91     -11.562 -25.356  31.829  1.00 19.91           C  
ANISOU 3385  CG  HIS B  91     2768   3553   1241     85    274   -130       C  
ATOM   3386  ND1 HIS B  91     -11.323 -26.661  32.036  1.00 21.11           N  
ANISOU 3386  ND1 HIS B  91     2933   3694   1393    197     83      0       N  
ATOM   3387  CD2 HIS B  91     -11.846 -25.214  30.481  1.00 20.39           C  
ANISOU 3387  CD2 HIS B  91     2853   3538   1354    116    176    139       C  
ATOM   3388  CE1 HIS B  91     -11.439 -27.320  30.875  1.00 21.78           C  
ANISOU 3388  CE1 HIS B  91     3063   3649   1560    183    187    -92       C  
ATOM   3389  NE2 HIS B  91     -11.759 -26.430  29.923  1.00 21.47           N  
ANISOU 3389  NE2 HIS B  91     3003   3781   1372     98    229    -34       N  
ATOM   3390  N   LEU B  92     -14.666 -25.183  32.682  1.00 18.52           N  
ANISOU 3390  N   LEU B  92     2741   3105   1189    140    205    -25       N  
ATOM   3391  CA ALEU B  92     -15.726 -26.183  32.853  0.50 17.82           C  
ANISOU 3391  CA ALEU B  92     2676   2954   1141    224    187    -35       C  
ATOM   3392  CA BLEU B  92     -15.670 -26.187  32.898  0.50 18.31           C  
ANISOU 3392  CA BLEU B  92     2798   2973   1186    172    219    -64       C  
ATOM   3393  C   LEU B  92     -15.579 -27.163  31.735  1.00 17.65           C  
ANISOU 3393  C   LEU B  92     2702   2911   1092    256    156      7       C  
ATOM   3394  O   LEU B  92     -15.200 -26.758  30.672  1.00 19.05           O  
ANISOU 3394  O   LEU B  92     2911   3121   1206    182    252     53       O  
ATOM   3395  CB ALEU B  92     -17.113 -25.566  32.703  0.50 17.41           C  
ANISOU 3395  CB ALEU B  92     2657   2906   1053    194     51    -26       C  
ATOM   3396  CB BLEU B  92     -16.993 -25.457  32.946  0.50 19.21           C  
ANISOU 3396  CB BLEU B  92     2892   3123   1284    291    215     25       C  
ATOM   3397  CG ALEU B  92     -17.577 -24.573  33.755  0.50 17.79           C  
ANISOU 3397  CG ALEU B  92     2714   2873   1170    309    213     49       C  
ATOM   3398  CG BLEU B  92     -18.321 -25.954  32.422  0.50 19.55           C  
ANISOU 3398  CG BLEU B  92     3042   3018   1367    219    191    -11       C  
ATOM   3399  CD1ALEU B  92     -17.065 -23.174  33.447  0.50 17.74           C  
ANISOU 3399  CD1ALEU B  92     2782   2977    978    140    192    -39       C  
ATOM   3400  CD1BLEU B  92     -18.976 -24.801  31.685  0.50 21.91           C  
ANISOU 3400  CD1BLEU B  92     3242   3217   1864    302    176    227       C  
ATOM   3401  CD2ALEU B  92     -19.093 -24.599  33.898  0.50 17.77           C  
ANISOU 3401  CD2ALEU B  92     2667   2806   1278    424    182     66       C  
ATOM   3402  CD2BLEU B  92     -18.167 -27.138  31.510  0.50 19.44           C  
ANISOU 3402  CD2BLEU B  92     3017   3065   1304    178    173    -42       C  
ATOM   3403  N   ILE B  93     -15.803 -28.444  31.977  1.00 17.23           N  
ANISOU 3403  N   ILE B  93     2728   2904    914    271    160     44       N  
ATOM   3404  CA  ILE B  93     -15.809 -29.455  30.913  1.00 16.82           C  
ANISOU 3404  CA  ILE B  93     2616   2968    807    262     87      3       C  
ATOM   3405  C   ILE B  93     -17.234 -29.947  30.715  1.00 16.90           C  
ANISOU 3405  C   ILE B  93     2682   2938    800    293     62     -6       C  
ATOM   3406  O   ILE B  93     -17.893 -30.371  31.674  1.00 16.97           O  
ANISOU 3406  O   ILE B  93     2663   2985    797    258    141   -180       O  
ATOM   3407  CB  ILE B  93     -14.904 -30.661  31.259  1.00 16.65           C  
ANISOU 3407  CB  ILE B  93     2639   2938    748    263   -108   -152       C  
ATOM   3408  CG1 ILE B  93     -13.446 -30.223  31.348  1.00 17.21           C  
ANISOU 3408  CG1 ILE B  93     2622   2979    936    167    -36   -130       C  
ATOM   3409  CG2 ILE B  93     -15.031 -31.763  30.206  1.00 16.20           C  
ANISOU 3409  CG2 ILE B  93     2494   2982    680    366    176   -202       C  
ATOM   3410  CD1 ILE B  93     -12.536 -31.265  31.970  1.00 18.89           C  
ANISOU 3410  CD1 ILE B  93     2789   3126   1261    258   -133    -26       C  
ATOM   3411  N   THR B  94     -17.704 -29.897  29.472  1.00 16.53           N  
ANISOU 3411  N   THR B  94     2549   2969    761    242    145    -23       N  
ATOM   3412  CA  THR B  94     -18.981 -30.499  29.108  1.00 16.75           C  
ANISOU 3412  CA  THR B  94     2732   2928    705    255    -32    -72       C  
ATOM   3413  C   THR B  94     -18.860 -31.189  27.735  1.00 16.70           C  
ANISOU 3413  C   THR B  94     2757   2888    699    350     89    -37       C  
ATOM   3414  O   THR B  94     -17.744 -31.365  27.212  1.00 17.37           O  
ANISOU 3414  O   THR B  94     2756   3096    746    452    106     14       O  
ATOM   3415  CB  THR B  94     -20.159 -29.486  29.199  1.00 16.55           C  
ANISOU 3415  CB  THR B  94     2770   2692    826    202     29      4       C  
ATOM   3416  OG1 THR B  94     -21.409 -30.184  29.126  1.00 16.19           O  
ANISOU 3416  OG1 THR B  94     2655   2824    672    270    221     69       O  
ATOM   3417  CG2 THR B  94     -20.092 -28.436  28.087  1.00 16.56           C  
ANISOU 3417  CG2 THR B  94     2835   2922    535    227    213     -3       C  
ATOM   3418  N   SER B  95     -19.985 -31.617  27.169  1.00 16.31           N  
ANISOU 3418  N   SER B  95     2713   2784    699    310    163    -16       N  
ATOM   3419  CA  SER B  95     -19.958 -32.151  25.803  1.00 16.74           C  
ANISOU 3419  CA  SER B  95     2745   2907    707    353     82    -67       C  
ATOM   3420  C   SER B  95     -20.670 -31.225  24.827  1.00 17.31           C  
ANISOU 3420  C   SER B  95     2882   2948    747    486    310     48       C  
ATOM   3421  O   SER B  95     -21.518 -30.417  25.219  1.00 15.89           O  
ANISOU 3421  O   SER B  95     2607   2983    446    391    115    -25       O  
ATOM   3422  CB  SER B  95     -20.525 -33.583  25.716  1.00 17.33           C  
ANISOU 3422  CB  SER B  95     2804   2896    883    356    232     27       C  
ATOM   3423  OG  SER B  95     -21.946 -33.608  25.771  1.00 17.68           O  
ANISOU 3423  OG  SER B  95     2836   2836   1042    338     -8    -60       O  
ATOM   3424  N   SER B  96     -20.328 -31.353  23.548  1.00 17.57           N  
ANISOU 3424  N   SER B  96     2974   3053    646    418    160     72       N  
ATOM   3425  CA  SER B  96     -20.999 -30.564  22.518  1.00 17.29           C  
ANISOU 3425  CA  SER B  96     2811   3095    664    364    212    110       C  
ATOM   3426  C   SER B  96     -22.400 -31.093  22.170  1.00 16.83           C  
ANISOU 3426  C   SER B  96     2887   3057    448    303    156    129       C  
ATOM   3427  O   SER B  96     -23.101 -30.484  21.378  1.00 17.89           O  
ANISOU 3427  O   SER B  96     2891   3130    774    448    159    205       O  
ATOM   3428  CB  SER B  96     -20.138 -30.510  21.268  1.00 18.48           C  
ANISOU 3428  CB  SER B  96     3121   3231    669    274    324    -21       C  
ATOM   3429  OG  SER B  96     -20.103 -31.790  20.680  1.00 17.85           O  
ANISOU 3429  OG  SER B  96     2854   3260    667    337    325     24       O  
ATOM   3430  N   ILE B  97     -22.814 -32.207  22.770  1.00 15.93           N  
ANISOU 3430  N   ILE B  97     2578   2925    547    374     78     77       N  
ATOM   3431  CA  ILE B  97     -24.119 -32.791  22.477  1.00 16.20           C  
ANISOU 3431  CA  ILE B  97     2666   2807    679    322    220      5       C  
ATOM   3432  C   ILE B  97     -25.085 -32.758  23.655  1.00 15.76           C  
ANISOU 3432  C   ILE B  97     2454   2791    743    369    153    -52       C  
ATOM   3433  O   ILE B  97     -26.104 -33.438  23.649  1.00 14.89           O  
ANISOU 3433  O   ILE B  97     2636   2721    298    298    274   -147       O  
ATOM   3434  CB  ILE B  97     -24.020 -34.209  21.887  1.00 16.09           C  
ANISOU 3434  CB  ILE B  97     2734   2636    743    324    320    145       C  
ATOM   3435  CG1 ILE B  97     -23.157 -35.147  22.744  1.00 17.39           C  
ANISOU 3435  CG1 ILE B  97     2950   2696    959    322    140    142       C  
ATOM   3436  CG2 ILE B  97     -23.434 -34.126  20.495  1.00 17.14           C  
ANISOU 3436  CG2 ILE B  97     2826   2864    822    385    446      2       C  
ATOM   3437  CD1 ILE B  97     -23.370 -36.621  22.443  1.00 18.91           C  
ANISOU 3437  CD1 ILE B  97     3203   2755   1226    517     82    -87       C  
ATOM   3438  N   GLU B  98     -24.762 -31.952  24.658  1.00 15.70           N  
ANISOU 3438  N   GLU B  98     2567   2818    578    380     96     18       N  
ATOM   3439  CA  GLU B  98     -25.681 -31.696  25.772  1.00 15.01           C  
ANISOU 3439  CA  GLU B  98     2435   2553    713    352    104     38       C  
ATOM   3440  C   GLU B  98     -27.008 -31.085  25.293  1.00 14.98           C  
ANISOU 3440  C   GLU B  98     2405   2562    722    316    103    -89       C  
ATOM   3441  O   GLU B  98     -27.097 -30.543  24.192  1.00 16.25           O  
ANISOU 3441  O   GLU B  98     2708   2678    786    361     15    -18       O  
ATOM   3442  CB  GLU B  98     -25.050 -30.729  26.779  1.00 15.50           C  
ANISOU 3442  CB  GLU B  98     2569   2650    667    337     33     10       C  
ATOM   3443  CG  GLU B  98     -23.802 -31.205  27.506  1.00 15.74           C  
ANISOU 3443  CG  GLU B  98     2463   2723    795    451    193     84       C  
ATOM   3444  CD  GLU B  98     -24.018 -32.471  28.299  1.00 16.01           C  
ANISOU 3444  CD  GLU B  98     2454   2736    891    447     85    113       C  
ATOM   3445  OE1 GLU B  98     -23.191 -33.397  28.167  1.00 16.88           O  
ANISOU 3445  OE1 GLU B  98     2786   2769    857    566     29    -38       O  
ATOM   3446  OE2 GLU B  98     -24.997 -32.541  29.069  1.00 15.75           O  
ANISOU 3446  OE2 GLU B  98     2767   2744    471    406    165    129       O  
ATOM   3447  N   HIS B  99     -28.038 -31.144  26.129  1.00 15.62           N  
ANISOU 3447  N   HIS B  99     2225   2744    963    267     53    -27       N  
ATOM   3448  CA  HIS B  99     -29.269 -30.408  25.865  1.00 15.10           C  
ANISOU 3448  CA  HIS B  99     2372   2559    807    383    112     66       C  
ATOM   3449  C   HIS B  99     -28.928 -28.956  25.736  1.00 15.52           C  
ANISOU 3449  C   HIS B  99     2367   2622    905    321    148    126       C  
ATOM   3450  O   HIS B  99     -27.972 -28.482  26.343  1.00 15.23           O  
ANISOU 3450  O   HIS B  99     2494   2487    804    331    132     51       O  
ATOM   3451  CB  HIS B  99     -30.243 -30.620  27.018  1.00 16.34           C  
ANISOU 3451  CB  HIS B  99     2496   2743    967    417    231    258       C  
ATOM   3452  CG  HIS B  99     -31.616 -30.019  26.791  1.00 16.89           C  
ANISOU 3452  CG  HIS B  99     2527   2854   1035    369     35    193       C  
ATOM   3453  ND1 HIS B  99     -32.671 -30.748  26.402  1.00 19.43           N  
ANISOU 3453  ND1 HIS B  99     2834   3140   1405    179    -97    164       N  
ATOM   3454  CD2 HIS B  99     -32.066 -28.713  26.908  1.00 16.93           C  
ANISOU 3454  CD2 HIS B  99     2666   2798    966    369     51     88       C  
ATOM   3455  CE1 HIS B  99     -33.749 -29.953  26.300  1.00 18.10           C  
ANISOU 3455  CE1 HIS B  99     2891   2869   1114    251    191     80       C  
ATOM   3456  NE2 HIS B  99     -33.372 -28.706  26.598  1.00 19.16           N  
ANISOU 3456  NE2 HIS B  99     2592   3248   1439    238    128   -284       N  
ATOM   3457  N   LYS B 100     -29.726 -28.222  24.975  1.00 16.29           N  
ANISOU 3457  N   LYS B 100     2617   2574    997    333     43    147       N  
ATOM   3458  CA  LYS B 100     -29.393 -26.839  24.704  1.00 16.34           C  
ANISOU 3458  CA  LYS B 100     2783   2614    809    235    133    154       C  
ATOM   3459  C   LYS B 100     -29.326 -25.964  25.963  1.00 16.52           C  
ANISOU 3459  C   LYS B 100     2736   2653    887    325    136     73       C  
ATOM   3460  O   LYS B 100     -28.620 -24.987  25.983  1.00 16.58           O  
ANISOU 3460  O   LYS B 100     2825   2660    812    272    121    -15       O  
ATOM   3461  CB  LYS B 100     -30.336 -26.256  23.645  1.00 17.34           C  
ANISOU 3461  CB  LYS B 100     2965   2749    875    400     -7    -40       C  
ATOM   3462  CG  LYS B 100     -30.000 -26.690  22.220  1.00 19.54           C  
ANISOU 3462  CG  LYS B 100     3489   3072    862    320     91    -25       C  
ATOM   3463  CD  LYS B 100     -28.950 -25.784  21.625  1.00 21.63           C  
ANISOU 3463  CD  LYS B 100     3617   3290   1309    283    213     37       C  
ATOM   3464  CE  LYS B 100     -28.631 -26.196  20.203  1.00 22.63           C  
ANISOU 3464  CE  LYS B 100     3867   3171   1560    330    344   -230       C  
ATOM   3465  NZ  LYS B 100     -27.459 -25.413  19.749  1.00 30.02           N  
ANISOU 3465  NZ  LYS B 100     4751   4369   2284   -331    622     60       N  
ATOM   3466  N   CYS B 101     -30.075 -26.317  26.997  1.00 15.76           N  
ANISOU 3466  N   CYS B 101     2654   2561    772    505     57    126       N  
ATOM   3467  CA  CYS B 101     -29.998 -25.531  28.216  1.00 16.79           C  
ANISOU 3467  CA  CYS B 101     2768   2690    920    330    186    -40       C  
ATOM   3468  C   CYS B 101     -28.588 -25.515  28.799  1.00 16.15           C  
ANISOU 3468  C   CYS B 101     2700   2487    947    239    271     22       C  
ATOM   3469  O   CYS B 101     -28.131 -24.474  29.262  1.00 17.63           O  
ANISOU 3469  O   CYS B 101     3015   2626   1055    198    170   -122       O  
ATOM   3470  CB  CYS B 101     -31.033 -25.966  29.262  1.00 17.65           C  
ANISOU 3470  CB  CYS B 101     2954   2680   1073    269    315    -40       C  
ATOM   3471  SG  CYS B 101     -30.900 -27.656  29.886  1.00 18.08           S  
ANISOU 3471  SG  CYS B 101     3106   2877    885    396    202    110       S  
ATOM   3472  N   VAL B 102     -27.890 -26.647  28.752  1.00 15.33           N  
ANISOU 3472  N   VAL B 102     2443   2543    836    225    260     44       N  
ATOM   3473  CA  VAL B 102     -26.513 -26.717  29.244  1.00 15.96           C  
ANISOU 3473  CA  VAL B 102     2556   2562    945    319    117    147       C  
ATOM   3474  C   VAL B 102     -25.576 -25.925  28.330  1.00 16.00           C  
ANISOU 3474  C   VAL B 102     2578   2738    761    287    260    -47       C  
ATOM   3475  O   VAL B 102     -24.720 -25.177  28.799  1.00 16.54           O  
ANISOU 3475  O   VAL B 102     2593   2804    886    212    219     85       O  
ATOM   3476  CB  VAL B 102     -26.017 -28.177  29.353  1.00 15.96           C  
ANISOU 3476  CB  VAL B 102     2427   2517   1119    293    249      6       C  
ATOM   3477  CG1 VAL B 102     -24.533 -28.226  29.712  1.00 17.15           C  
ANISOU 3477  CG1 VAL B 102     2507   2833   1177    315      4    -12       C  
ATOM   3478  CG2 VAL B 102     -26.853 -28.951  30.361  1.00 16.36           C  
ANISOU 3478  CG2 VAL B 102     2582   2811    821    227    314   -125       C  
ATOM   3479  N   LEU B 103     -25.751 -26.086  27.021  1.00 16.38           N  
ANISOU 3479  N   LEU B 103     2786   2645    792    261    114    -19       N  
ATOM   3480  CA  LEU B 103     -24.897 -25.382  26.073  1.00 16.30           C  
ANISOU 3480  CA  LEU B 103     2776   2647    768    144    195   -204       C  
ATOM   3481  C   LEU B 103     -25.054 -23.867  26.209  1.00 16.70           C  
ANISOU 3481  C   LEU B 103     2892   2646    805    235    235    -18       C  
ATOM   3482  O   LEU B 103     -24.059 -23.124  26.195  1.00 17.03           O  
ANISOU 3482  O   LEU B 103     2915   2662    891    228    306     37       O  
ATOM   3483  CB  LEU B 103     -25.181 -25.844  24.640  1.00 16.30           C  
ANISOU 3483  CB  LEU B 103     2754   2669    767    126    199   -214       C  
ATOM   3484  CG  LEU B 103     -24.892 -27.320  24.344  1.00 16.34           C  
ANISOU 3484  CG  LEU B 103     2677   2654    875    155    -37   -202       C  
ATOM   3485  CD1 LEU B 103     -25.289 -27.662  22.914  1.00 16.55           C  
ANISOU 3485  CD1 LEU B 103     2851   2736    700    210    123   -146       C  
ATOM   3486  CD2 LEU B 103     -23.433 -27.668  24.600  1.00 16.85           C  
ANISOU 3486  CD2 LEU B 103     2653   3070    676    126    -75    -56       C  
ATOM   3487  N   ASN B 104     -26.297 -23.428  26.393  1.00 15.22           N  
ANISOU 3487  N   ASN B 104     2948   2515    318    292    299     40       N  
ATOM   3488  CA  ASN B 104     -26.569 -22.004  26.504  1.00 16.82           C  
ANISOU 3488  CA  ASN B 104     3035   2580    773    269    221     -3       C  
ATOM   3489  C   ASN B 104     -26.131 -21.400  27.830  1.00 16.90           C  
ANISOU 3489  C   ASN B 104     2929   2642    851    202    157    -44       C  
ATOM   3490  O   ASN B 104     -25.620 -20.274  27.847  1.00 17.22           O  
ANISOU 3490  O   ASN B 104     3018   2552    971    298    311    118       O  
ATOM   3491  CB  ASN B 104     -28.023 -21.691  26.162  1.00 17.26           C  
ANISOU 3491  CB  ASN B 104     2999   2806    750    141     73     -8       C  
ATOM   3492  CG  ASN B 104     -28.309 -21.880  24.691  1.00 18.66           C  
ANISOU 3492  CG  ASN B 104     3226   3084    778    112     37    -64       C  
ATOM   3493  OD1 ASN B 104     -27.402 -21.762  23.856  1.00 21.85           O  
ANISOU 3493  OD1 ASN B 104     3390   3521   1388    261    400     57       O  
ATOM   3494  ND2 ASN B 104     -29.554 -22.202  24.362  1.00 19.93           N  
ANISOU 3494  ND2 ASN B 104     3337   3278    956     10    -28    -59       N  
ATOM   3495  N   THR B 105     -26.268 -22.134  28.941  1.00 16.55           N  
ANISOU 3495  N   THR B 105     2885   2369   1032    278    120     41       N  
ATOM   3496  CA  THR B 105     -25.680 -21.576  30.188  1.00 18.26           C  
ANISOU 3496  CA  THR B 105     2855   2829   1250    211    -84   -104       C  
ATOM   3497  C   THR B 105     -24.152 -21.509  30.133  1.00 18.41           C  
ANISOU 3497  C   THR B 105     2873   2649   1472    377    -17    -57       C  
ATOM   3498  O   THR B 105     -23.553 -20.548  30.606  1.00 19.00           O  
ANISOU 3498  O   THR B 105     2982   2855   1382    237     28   -134       O  
ATOM   3499  CB  THR B 105     -26.179 -22.167  31.540  1.00 19.34           C  
ANISOU 3499  CB  THR B 105     2776   2638   1934     25      0    386       C  
ATOM   3500  OG1 THR B 105     -25.120 -22.807  32.276  1.00 24.45           O  
ANISOU 3500  OG1 THR B 105     3420   3188   2682    339   -346    757       O  
ATOM   3501  CG2 THR B 105     -27.425 -23.001  31.405  1.00 13.07           C  
ANISOU 3501  CG2 THR B 105     2896   1790    277    118    -82    -32       C  
ATOM   3502  N   CYS B 106     -23.525 -22.516  29.537  1.00 17.98           N  
ANISOU 3502  N   CYS B 106     2810   2814   1206    296    231      0       N  
ATOM   3503  CA  CYS B 106     -22.078 -22.485  29.359  1.00 17.25           C  
ANISOU 3503  CA  CYS B 106     2832   2709   1011    341    291    -75       C  
ATOM   3504  C   CYS B 106     -21.642 -21.359  28.417  1.00 17.65           C  
ANISOU 3504  C   CYS B 106     2762   2743   1199    342    181     22       C  
ATOM   3505  O   CYS B 106     -20.604 -20.723  28.636  1.00 17.91           O  
ANISOU 3505  O   CYS B 106     2950   2789   1066    265     32    -25       O  
ATOM   3506  CB  CYS B 106     -21.572 -23.839  28.857  1.00 17.92           C  
ANISOU 3506  CB  CYS B 106     2955   2717   1134    325    260   -108       C  
ATOM   3507  SG  CYS B 106     -21.641 -25.161  30.083  1.00 19.61           S  
ANISOU 3507  SG  CYS B 106     3244   3221    986    229    171    107       S  
ATOM   3508  N   GLY B 107     -22.442 -21.109  27.381  1.00 17.30           N  
ANISOU 3508  N   GLY B 107     3026   2659    888    218    235    -10       N  
ATOM   3509  CA  GLY B 107     -22.183 -20.000  26.461  1.00 17.99           C  
ANISOU 3509  CA  GLY B 107     3103   2774    955    187    238     71       C  
ATOM   3510  C   GLY B 107     -22.218 -18.669  27.194  1.00 18.51           C  
ANISOU 3510  C   GLY B 107     3036   2942   1054    163    297   -101       C  
ATOM   3511  O   GLY B 107     -21.372 -17.796  26.980  1.00 19.26           O  
ANISOU 3511  O   GLY B 107     3171   2951   1193    152    347    179       O  
ATOM   3512  N   PHE B 108     -23.187 -18.526  28.092  1.00 17.63           N  
ANISOU 3512  N   PHE B 108     2895   2864    939    195    185    112       N  
ATOM   3513  CA  PHE B 108     -23.275 -17.335  28.920  1.00 18.17           C  
ANISOU 3513  CA  PHE B 108     2973   2976    952    220    308     -5       C  
ATOM   3514  C   PHE B 108     -22.040 -17.174  29.824  1.00 18.95           C  
ANISOU 3514  C   PHE B 108     2978   2963   1256    179    210     -5       C  
ATOM   3515  O   PHE B 108     -21.469 -16.095  29.959  1.00 20.18           O  
ANISOU 3515  O   PHE B 108     3123   3022   1521    126    -75   -139       O  
ATOM   3516  CB  PHE B 108     -24.534 -17.369  29.782  1.00 18.90           C  
ANISOU 3516  CB  PHE B 108     2936   2955   1287     49    332    -65       C  
ATOM   3517  CG  PHE B 108     -24.525 -16.325  30.845  1.00 19.76           C  
ANISOU 3517  CG  PHE B 108     3214   2868   1424    198    278   -105       C  
ATOM   3518  CD1 PHE B 108     -24.601 -14.987  30.497  1.00 19.82           C  
ANISOU 3518  CD1 PHE B 108     3158   2746   1624    254     87   -287       C  
ATOM   3519  CD2 PHE B 108     -24.356 -16.670  32.182  1.00 20.37           C  
ANISOU 3519  CD2 PHE B 108     3134   3242   1361    224    161   -215       C  
ATOM   3520  CE1 PHE B 108     -24.553 -14.008  31.470  1.00 21.09           C  
ANISOU 3520  CE1 PHE B 108     3387   3061   1564    383    130   -411       C  
ATOM   3521  CE2 PHE B 108     -24.304 -15.692  33.159  1.00 21.94           C  
ANISOU 3521  CE2 PHE B 108     3367   3214   1752    468    414   -429       C  
ATOM   3522  CZ  PHE B 108     -24.400 -14.358  32.801  1.00 21.87           C  
ANISOU 3522  CZ  PHE B 108     3375   3325   1608    245    231   -215       C  
ATOM   3523  N   LEU B 109     -21.647 -18.259  30.472  1.00 19.10           N  
ANISOU 3523  N   LEU B 109     2814   2960   1482    216    206     19       N  
ATOM   3524  CA  LEU B 109     -20.442 -18.228  31.286  1.00 18.84           C  
ANISOU 3524  CA  LEU B 109     2847   2968   1341    140    146    -58       C  
ATOM   3525  C   LEU B 109     -19.227 -17.777  30.474  1.00 19.04           C  
ANISOU 3525  C   LEU B 109     3074   2922   1235    162    276    -33       C  
ATOM   3526  O   LEU B 109     -18.434 -16.978  30.964  1.00 20.12           O  
ANISOU 3526  O   LEU B 109     3054   3084   1505     49    223     23       O  
ATOM   3527  CB  LEU B 109     -20.196 -19.581  31.956  1.00 19.41           C  
ANISOU 3527  CB  LEU B 109     2889   2904   1581    163    348    -61       C  
ATOM   3528  CG  LEU B 109     -21.228 -20.016  33.005  1.00 18.26           C  
ANISOU 3528  CG  LEU B 109     2550   2864   1522     -2    138   -180       C  
ATOM   3529  CD1 LEU B 109     -20.762 -21.304  33.662  1.00 19.39           C  
ANISOU 3529  CD1 LEU B 109     2722   2973   1672     19    178    -28       C  
ATOM   3530  CD2 LEU B 109     -21.469 -18.930  34.054  1.00 19.55           C  
ANISOU 3530  CD2 LEU B 109     2722   3304   1403     69     70   -298       C  
ATOM   3531  N   GLU B 110     -19.098 -18.246  29.229  1.00 18.70           N  
ANISOU 3531  N   GLU B 110     3069   2888   1147    196    327    106       N  
ATOM   3532  CA  GLU B 110     -18.000 -17.782  28.371  1.00 19.26           C  
ANISOU 3532  CA  GLU B 110     3080   2978   1258     72    407    -87       C  
ATOM   3533  C   GLU B 110     -18.057 -16.281  28.176  1.00 20.86           C  
ANISOU 3533  C   GLU B 110     3212   3081   1633    147    233     89       C  
ATOM   3534  O   GLU B 110     -17.016 -15.619  28.173  1.00 22.89           O  
ANISOU 3534  O   GLU B 110     3488   3178   2031   -156    280     92       O  
ATOM   3535  CB  GLU B 110     -17.999 -18.478  27.013  1.00 19.21           C  
ANISOU 3535  CB  GLU B 110     3198   2964   1136     87    366     32       C  
ATOM   3536  CG  GLU B 110     -17.523 -19.913  27.065  1.00 19.47           C  
ANISOU 3536  CG  GLU B 110     3254   3067   1077    213    384     79       C  
ATOM   3537  CD  GLU B 110     -17.591 -20.586  25.719  1.00 20.30           C  
ANISOU 3537  CD  GLU B 110     3470   2992   1251    208    398    -57       C  
ATOM   3538  OE1 GLU B 110     -16.535 -20.711  25.090  1.00 23.23           O  
ANISOU 3538  OE1 GLU B 110     3675   3648   1503    258    706     98       O  
ATOM   3539  OE2 GLU B 110     -18.695 -20.983  25.298  1.00 22.34           O  
ANISOU 3539  OE2 GLU B 110     3605   3212   1669     74    270    400       O  
ATOM   3540  N   SER B 111     -19.279 -15.768  28.054  1.00 20.18           N  
ANISOU 3540  N   SER B 111     3224   2978   1465    184    132    104       N  
ATOM   3541  CA  SER B 111     -19.495 -14.356  27.777  1.00 21.36           C  
ANISOU 3541  CA  SER B 111     3279   3034   1802    262    192    158       C  
ATOM   3542  C   SER B 111     -19.101 -13.469  28.965  1.00 21.84           C  
ANISOU 3542  C   SER B 111     3439   2909   1950    161    144    117       C  
ATOM   3543  O   SER B 111     -18.901 -12.262  28.797  1.00 23.93           O  
ANISOU 3543  O   SER B 111     3759   3009   2323     -6    178    344       O  
ATOM   3544  CB  SER B 111     -20.951 -14.105  27.371  1.00 21.00           C  
ANISOU 3544  CB  SER B 111     3401   2996   1582    236    -27    383       C  
ATOM   3545  OG  SER B 111     -21.779 -13.917  28.511  1.00 21.43           O  
ANISOU 3545  OG  SER B 111     3308   2936   1896    411     83    287       O  
ATOM   3546  N   ILE B 112     -19.009 -14.058  30.160  1.00 21.58           N  
ANISOU 3546  N   ILE B 112     3340   2982   1875    131     64     62       N  
ATOM   3547  CA  ILE B 112     -18.556 -13.320  31.352  1.00 21.61           C  
ANISOU 3547  CA  ILE B 112     3400   2952   1858    150    178    -38       C  
ATOM   3548  C   ILE B 112     -17.166 -13.786  31.813  1.00 22.41           C  
ANISOU 3548  C   ILE B 112     3376   3146   1993    146    207    -62       C  
ATOM   3549  O   ILE B 112     -16.753 -13.556  32.961  1.00 24.54           O  
ANISOU 3549  O   ILE B 112     3607   3565   2149   -107     99   -133       O  
ATOM   3550  CB  ILE B 112     -19.574 -13.337  32.528  1.00 21.38           C  
ANISOU 3550  CB  ILE B 112     3257   2782   2085     93    260    -23       C  
ATOM   3551  CG1 ILE B 112     -19.916 -14.765  32.958  1.00 21.24           C  
ANISOU 3551  CG1 ILE B 112     3353   2727   1987    245    324    -17       C  
ATOM   3552  CG2 ILE B 112     -20.840 -12.548  32.192  1.00 22.43           C  
ANISOU 3552  CG2 ILE B 112     3569   2952   1999    235     52     51       C  
ATOM   3553  CD1 ILE B 112     -20.621 -14.828  34.299  1.00 21.06           C  
ANISOU 3553  CD1 ILE B 112     3388   2979   1632    164    -18     38       C  
ATOM   3554  N   GLY B 113     -16.454 -14.452  30.905  1.00 22.19           N  
ANISOU 3554  N   GLY B 113     3321   3026   2082    209    324    130       N  
ATOM   3555  CA  GLY B 113     -15.032 -14.713  31.095  1.00 22.28           C  
ANISOU 3555  CA  GLY B 113     3242   3234   1990    -68    313    -58       C  
ATOM   3556  C   GLY B 113     -14.598 -16.108  31.494  1.00 22.69           C  
ANISOU 3556  C   GLY B 113     3417   3234   1969    -81    230     -1       C  
ATOM   3557  O   GLY B 113     -13.403 -16.336  31.739  1.00 23.62           O  
ANISOU 3557  O   GLY B 113     3449   3615   1910   -256    262   -115       O  
ATOM   3558  N   PHE B 114     -15.556 -17.025  31.576  1.00 21.31           N  
ANISOU 3558  N   PHE B 114     3148   3278   1668     -4    328     54       N  
ATOM   3559  CA  PHE B 114     -15.256 -18.423  31.866  1.00 20.46           C  
ANISOU 3559  CA  PHE B 114     3189   3288   1293    -24    411    140       C  
ATOM   3560  C   PHE B 114     -14.772 -19.139  30.598  1.00 20.57           C  
ANISOU 3560  C   PHE B 114     2950   3293   1573     72    316    -48       C  
ATOM   3561  O   PHE B 114     -15.125 -18.740  29.484  1.00 21.85           O  
ANISOU 3561  O   PHE B 114     3338   3508   1454   -101    539    207       O  
ATOM   3562  CB  PHE B 114     -16.484 -19.126  32.496  1.00 19.68           C  
ANISOU 3562  CB  PHE B 114     2944   3211   1321     14    424   -202       C  
ATOM   3563  CG  PHE B 114     -16.807 -18.659  33.907  1.00 19.61           C  
ANISOU 3563  CG  PHE B 114     3217   3111   1120      3    301    -41       C  
ATOM   3564  CD1 PHE B 114     -16.398 -19.394  35.027  1.00 19.59           C  
ANISOU 3564  CD1 PHE B 114     3308   2872   1260     32    255    -51       C  
ATOM   3565  CD2 PHE B 114     -17.520 -17.483  34.122  1.00 21.24           C  
ANISOU 3565  CD2 PHE B 114     3334   3121   1612     90    209    -96       C  
ATOM   3566  CE1 PHE B 114     -16.689 -18.959  36.327  1.00 19.88           C  
ANISOU 3566  CE1 PHE B 114     3321   3067   1165     45     48    -96       C  
ATOM   3567  CE2 PHE B 114     -17.817 -17.053  35.419  1.00 20.60           C  
ANISOU 3567  CE2 PHE B 114     3539   2848   1437    -20    176     81       C  
ATOM   3568  CZ  PHE B 114     -17.389 -17.782  36.521  1.00 19.81           C  
ANISOU 3568  CZ  PHE B 114     3249   2806   1472   -129    -93    -55       C  
ATOM   3569  N   ASP B 115     -13.935 -20.166  30.775  1.00 20.28           N  
ANISOU 3569  N   ASP B 115     2706   3156   1843    -44    289    -76       N  
ATOM   3570  CA  ASP B 115     -13.514 -21.037  29.666  1.00 20.13           C  
ANISOU 3570  CA  ASP B 115     2819   3342   1487     27    477    169       C  
ATOM   3571  C   ASP B 115     -14.268 -22.366  29.703  1.00 19.26           C  
ANISOU 3571  C   ASP B 115     2807   3137   1372    213    317    256       C  
ATOM   3572  O   ASP B 115     -14.472 -22.942  30.785  1.00 18.97           O  
ANISOU 3572  O   ASP B 115     2878   3121   1209    118    277    110       O  
ATOM   3573  CB  ASP B 115     -12.010 -21.321  29.720  1.00 22.51           C  
ANISOU 3573  CB  ASP B 115     2882   3608   2060    133    397     55       C  
ATOM   3574  CG  ASP B 115     -11.173 -20.066  29.878  1.00 24.80           C  
ANISOU 3574  CG  ASP B 115     3204   3698   2521     14    263    209       C  
ATOM   3575  OD1 ASP B 115     -11.285 -19.147  29.040  1.00 26.09           O  
ANISOU 3575  OD1 ASP B 115     3256   4005   2652   -288    936    560       O  
ATOM   3576  OD2 ASP B 115     -10.370 -20.015  30.832  1.00 28.07           O  
ANISOU 3576  OD2 ASP B 115     3359   4476   2831   -291     87   -129       O  
ATOM   3577  N   VAL B 116     -14.683 -22.850  28.534  1.00 19.11           N  
ANISOU 3577  N   VAL B 116     2788   3088   1385    150    577    105       N  
ATOM   3578  CA  VAL B 116     -15.436 -24.098  28.459  1.00 20.05           C  
ANISOU 3578  CA  VAL B 116     3041   3047   1527    156    466     37       C  
ATOM   3579  C   VAL B 116     -14.879 -24.959  27.346  1.00 19.39           C  
ANISOU 3579  C   VAL B 116     3039   3021   1306    172    455    198       C  
ATOM   3580  O   VAL B 116     -14.625 -24.464  26.255  1.00 18.92           O  
ANISOU 3580  O   VAL B 116     2997   3095   1095    270    466     67       O  
ATOM   3581  CB  VAL B 116     -16.945 -23.877  28.191  1.00 18.77           C  
ANISOU 3581  CB  VAL B 116     3042   2905   1183    213    419    126       C  
ATOM   3582  CG1 VAL B 116     -17.695 -25.201  28.232  1.00 18.99           C  
ANISOU 3582  CG1 VAL B 116     2984   2975   1255    186    269   -123       C  
ATOM   3583  CG2 VAL B 116     -17.559 -22.949  29.230  1.00 18.56           C  
ANISOU 3583  CG2 VAL B 116     3059   2914   1076    232    550    237       C  
ATOM   3584  N   THR B 117     -14.713 -26.247  27.629  1.00 17.28           N  
ANISOU 3584  N   THR B 117     2557   3047    960    197    330    209       N  
ATOM   3585  CA  THR B 117     -14.360 -27.233  26.623  1.00 19.10           C  
ANISOU 3585  CA  THR B 117     2865   3181   1210    228    219    -51       C  
ATOM   3586  C   THR B 117     -15.631 -28.010  26.303  1.00 19.19           C  
ANISOU 3586  C   THR B 117     2970   3227   1093    181    262    139       C  
ATOM   3587  O   THR B 117     -16.251 -28.543  27.216  1.00 18.74           O  
ANISOU 3587  O   THR B 117     3046   3235    838    215    227     43       O  
ATOM   3588  CB  THR B 117     -13.302 -28.199  27.183  1.00 20.08           C  
ANISOU 3588  CB  THR B 117     2894   3103   1631    299    382   -115       C  
ATOM   3589  OG1 THR B 117     -12.064 -27.500  27.339  1.00 22.16           O  
ANISOU 3589  OG1 THR B 117     2922   3484   2011    214    174   -172       O  
ATOM   3590  CG2 THR B 117     -13.102 -29.396  26.248  1.00 20.43           C  
ANISOU 3590  CG2 THR B 117     3035   3310   1415    369    390   -136       C  
ATOM   3591  N   TYR B 118     -16.042 -28.040  25.037  1.00 18.40           N  
ANISOU 3591  N   TYR B 118     2837   3146   1006    329    333     58       N  
ATOM   3592  CA  TYR B 118     -17.165 -28.861  24.610  1.00 17.22           C  
ANISOU 3592  CA  TYR B 118     2937   2921    682    357    168    136       C  
ATOM   3593  C   TYR B 118     -16.619 -30.107  23.904  1.00 18.51           C  
ANISOU 3593  C   TYR B 118     3144   3081    808    530     87     45       C  
ATOM   3594  O   TYR B 118     -16.281 -30.068  22.706  1.00 20.42           O  
ANISOU 3594  O   TYR B 118     3246   3501   1009    408    439    226       O  
ATOM   3595  CB  TYR B 118     -18.070 -28.061  23.662  1.00 17.92           C  
ANISOU 3595  CB  TYR B 118     2979   2932    896    408    125    212       C  
ATOM   3596  CG  TYR B 118     -18.597 -26.767  24.245  1.00 18.17           C  
ANISOU 3596  CG  TYR B 118     2891   3099    912    329    413     72       C  
ATOM   3597  CD1 TYR B 118     -19.833 -26.729  24.896  1.00 17.62           C  
ANISOU 3597  CD1 TYR B 118     2532   3085   1076    384     87    -55       C  
ATOM   3598  CD2 TYR B 118     -17.865 -25.579  24.156  1.00 18.46           C  
ANISOU 3598  CD2 TYR B 118     3010   3007    994    333    415     43       C  
ATOM   3599  CE1 TYR B 118     -20.331 -25.548  25.428  1.00 16.52           C  
ANISOU 3599  CE1 TYR B 118     2742   3049    486    284    269     21       C  
ATOM   3600  CE2 TYR B 118     -18.358 -24.383  24.688  1.00 19.41           C  
ANISOU 3600  CE2 TYR B 118     3108   3013   1251    300    616     61       C  
ATOM   3601  CZ  TYR B 118     -19.596 -24.379  25.326  1.00 17.71           C  
ANISOU 3601  CZ  TYR B 118     2774   2856   1097    415    220     57       C  
ATOM   3602  OH  TYR B 118     -20.127 -23.228  25.882  1.00 18.55           O  
ANISOU 3602  OH  TYR B 118     3095   3037    914    415    454    -45       O  
ATOM   3603  N   LEU B 119     -16.534 -31.208  24.648  1.00 18.65           N  
ANISOU 3603  N   LEU B 119     3052   2939   1092    468    160     40       N  
ATOM   3604  CA  LEU B 119     -15.982 -32.460  24.119  1.00 18.24           C  
ANISOU 3604  CA  LEU B 119     3214   3024    692    415    188   -106       C  
ATOM   3605  C   LEU B 119     -16.809 -32.992  22.964  1.00 18.57           C  
ANISOU 3605  C   LEU B 119     3048   3347    658    414    263    -87       C  
ATOM   3606  O   LEU B 119     -18.040 -33.030  23.027  1.00 18.37           O  
ANISOU 3606  O   LEU B 119     3028   3277    673    467    314    -64       O  
ATOM   3607  CB  LEU B 119     -15.882 -33.499  25.238  1.00 18.58           C  
ANISOU 3607  CB  LEU B 119     3046   3085    926    470    218     54       C  
ATOM   3608  CG  LEU B 119     -14.923 -33.165  26.379  1.00 18.79           C  
ANISOU 3608  CG  LEU B 119     3097   3183    859    469    301   -115       C  
ATOM   3609  CD1 LEU B 119     -15.098 -34.155  27.528  1.00 18.63           C  
ANISOU 3609  CD1 LEU B 119     2975   3245    857    563    296    -27       C  
ATOM   3610  CD2 LEU B 119     -13.471 -33.144  25.915  1.00 20.62           C  
ANISOU 3610  CD2 LEU B 119     3125   3530   1177    296    339   -349       C  
ATOM   3611  N   THR B 120     -16.149 -33.439  21.906  1.00 19.04           N  
ANISOU 3611  N   THR B 120     3065   3418    752    566    160   -311       N  
ATOM   3612  CA ATHR B 120     -16.860 -33.955  20.731  0.50 19.37           C  
ANISOU 3612  CA ATHR B 120     3064   3487    805    406     94   -209       C  
ATOM   3613  CA BTHR B 120     -16.921 -33.977  20.779  0.50 19.55           C  
ANISOU 3613  CA BTHR B 120     3114   3492    821    415    184   -346       C  
ATOM   3614  C   THR B 120     -17.023 -35.484  20.805  1.00 20.68           C  
ANISOU 3614  C   THR B 120     3171   3572   1114    329    140   -209       C  
ATOM   3615  O   THR B 120     -16.101 -36.147  21.197  1.00 21.53           O  
ANISOU 3615  O   THR B 120     3471   3515   1193    466    129    -98       O  
ATOM   3616  CB ATHR B 120     -16.148 -33.588  19.426  0.50 19.93           C  
ANISOU 3616  CB ATHR B 120     2940   3672    959    261    201   -323       C  
ATOM   3617  CB BTHR B 120     -16.572 -33.369  19.403  0.50 21.17           C  
ANISOU 3617  CB BTHR B 120     3537   3559    946    294    307   -308       C  
ATOM   3618  OG1ATHR B 120     -14.912 -34.295  19.354  0.50 21.67           O  
ANISOU 3618  OG1ATHR B 120     2912   3879   1441    302    -86   -177       O  
ATOM   3619  OG1BTHR B 120     -16.374 -34.388  18.413  0.50 20.66           O  
ANISOU 3619  OG1BTHR B 120     3471   3691    686    385    553   -200       O  
ATOM   3620  CG2ATHR B 120     -15.874 -32.108  19.358  0.50 20.16           C  
ANISOU 3620  CG2ATHR B 120     3130   3770    760     78    309     75       C  
ATOM   3621  CG2BTHR B 120     -15.353 -32.469  19.465  0.50 20.78           C  
ANISOU 3621  CG2BTHR B 120     3338   3905    652    274    299    -21       C  
ATOM   3622  N   PRO B 121     -18.217 -35.977  20.556  1.00 19.31           N  
ANISOU 3622  N   PRO B 121     3118   3369    849    356    133    -60       N  
ATOM   3623  CA  PRO B 121     -18.509 -37.395  20.725  1.00 19.77           C  
ANISOU 3623  CA  PRO B 121     3342   3282    886    484    233    -73       C  
ATOM   3624  C   PRO B 121     -17.801 -38.241  19.671  1.00 20.58           C  
ANISOU 3624  C   PRO B 121     3278   3120   1422    357    452   -204       C  
ATOM   3625  O   PRO B 121     -17.256 -37.696  18.710  1.00 21.60           O  
ANISOU 3625  O   PRO B 121     3462   3519   1224    523    488   -149       O  
ATOM   3626  CB  PRO B 121     -20.019 -37.444  20.517  1.00 20.40           C  
ANISOU 3626  CB  PRO B 121     3338   3277   1135    520    259      8       C  
ATOM   3627  CG  PRO B 121     -20.314 -36.251  19.671  1.00 20.05           C  
ANISOU 3627  CG  PRO B 121     3218   3039   1358    515    308    -49       C  
ATOM   3628  CD  PRO B 121     -19.399 -35.198  20.161  1.00 19.41           C  
ANISOU 3628  CD  PRO B 121     2995   3292   1086    461    356   -147       C  
ATOM   3629  N   LYS B 122     -17.814 -39.563  19.827  1.00 21.25           N  
ANISOU 3629  N   LYS B 122     3640   3128   1304    626    260   -148       N  
ATOM   3630  CA  LYS B 122     -17.422 -40.430  18.723  1.00 20.47           C  
ANISOU 3630  CA  LYS B 122     3349   3173   1254    663    372    -83       C  
ATOM   3631  C   LYS B 122     -18.628 -40.519  17.798  1.00 19.68           C  
ANISOU 3631  C   LYS B 122     3587   2893    995    753    274   -123       C  
ATOM   3632  O   LYS B 122     -19.670 -39.969  18.128  1.00 18.67           O  
ANISOU 3632  O   LYS B 122     3475   2936    680    660    251    -44       O  
ATOM   3633  CB  LYS B 122     -17.023 -41.814  19.240  1.00 23.83           C  
ANISOU 3633  CB  LYS B 122     3718   3440   1894    872     33     78       C  
ATOM   3634  CG  LYS B 122     -15.683 -41.854  19.988  1.00 26.42           C  
ANISOU 3634  CG  LYS B 122     4002   3864   2172    866   -318    -43       C  
ATOM   3635  CD  LYS B 122     -15.215 -43.284  20.320  1.00 30.12           C  
ANISOU 3635  CD  LYS B 122     4641   4272   2531   1309   -318    157       C  
ATOM   3636  CE  LYS B 122     -16.213 -44.075  21.168  0.20 29.83           C  
ANISOU 3636  CE  LYS B 122     4321   4756   2256   1312    117   -399       C  
ATOM   3637  NZ  LYS B 122     -15.839 -45.472  21.579  0.20 30.29           N  
ANISOU 3637  NZ  LYS B 122     4243   4704   2559   1320    366   -484       N  
ATOM   3638  N   ALA B 123     -18.484 -41.159  16.636  1.00 20.40           N  
ANISOU 3638  N   ALA B 123     3577   3238    933    824    334   -134       N  
ATOM   3639  CA  ALA B 123     -19.610 -41.343  15.719  1.00 19.67           C  
ANISOU 3639  CA  ALA B 123     3684   3118    669    678    397   -289       C  
ATOM   3640  C   ALA B 123     -20.744 -42.107  16.388  1.00 19.06           C  
ANISOU 3640  C   ALA B 123     3442   2955    844    757    193   -427       C  
ATOM   3641  O   ALA B 123     -21.901 -42.013  15.975  1.00 19.56           O  
ANISOU 3641  O   ALA B 123     3581   3194    656    883    119   -222       O  
ATOM   3642  CB  ALA B 123     -19.161 -42.058  14.445  1.00 19.85           C  
ANISOU 3642  CB  ALA B 123     3827   2865    848    927     80   -500       C  
ATOM   3643  N   SER B 124     -20.399 -42.861  17.424  1.00 19.49           N  
ANISOU 3643  N   SER B 124     3367   3152    884    808    272   -273       N  
ATOM   3644  CA  SER B 124     -21.377 -43.625  18.194  1.00 19.90           C  
ANISOU 3644  CA  SER B 124     3425   2905   1229    791    109   -174       C  
ATOM   3645  C   SER B 124     -22.246 -42.743  19.102  1.00 20.56           C  
ANISOU 3645  C   SER B 124     3360   3085   1366    682    227   -268       C  
ATOM   3646  O   SER B 124     -23.284 -43.195  19.609  1.00 20.70           O  
ANISOU 3646  O   SER B 124     3204   3320   1340    601     21   -332       O  
ATOM   3647  CB  SER B 124     -20.634 -44.629  19.072  1.00 20.99           C  
ANISOU 3647  CB  SER B 124     3632   3113   1230    846     24    -52       C  
ATOM   3648  OG  SER B 124     -19.734 -43.964  19.956  1.00 21.81           O  
ANISOU 3648  OG  SER B 124     3786   3148   1352    935    -64   -193       O  
ATOM   3649  N   GLY B 125     -21.795 -41.507  19.329  1.00 19.77           N  
ANISOU 3649  N   GLY B 125     3355   3024   1133    712    103   -358       N  
ATOM   3650  CA  GLY B 125     -22.432 -40.599  20.286  1.00 19.52           C  
ANISOU 3650  CA  GLY B 125     3175   3186   1054    803    129   -256       C  
ATOM   3651  C   GLY B 125     -21.753 -40.605  21.640  1.00 19.26           C  
ANISOU 3651  C   GLY B 125     3203   3050   1065    790    134   -210       C  
ATOM   3652  O   GLY B 125     -22.064 -39.785  22.505  1.00 17.73           O  
ANISOU 3652  O   GLY B 125     3307   2653    774    681    -49    -14       O  
ATOM   3653  N   LEU B 126     -20.803 -41.518  21.808  1.00 18.70           N  
ANISOU 3653  N   LEU B 126     3285   2914    905    734     -7    -76       N  
ATOM   3654  CA  LEU B 126     -20.132 -41.691  23.080  1.00 19.55           C  
ANISOU 3654  CA  LEU B 126     3298   3131    997    912    -32    -72       C  
ATOM   3655  C   LEU B 126     -19.111 -40.604  23.405  1.00 19.52           C  
ANISOU 3655  C   LEU B 126     3279   3217    920    821    -33   -143       C  
ATOM   3656  O   LEU B 126     -18.331 -40.156  22.539  1.00 20.43           O  
ANISOU 3656  O   LEU B 126     3379   3123   1259    628     17    -80       O  
ATOM   3657  CB  LEU B 126     -19.450 -43.055  23.110  1.00 21.52           C  
ANISOU 3657  CB  LEU B 126     3611   3487   1077   1347    153     78       C  
ATOM   3658  CG  LEU B 126     -19.933 -44.263  23.912  1.00 26.12           C  
ANISOU 3658  CG  LEU B 126     3873   3294   2754    957    264      0       C  
ATOM   3659  CD1 LEU B 126     -21.441 -44.426  24.078  1.00 28.15           C  
ANISOU 3659  CD1 LEU B 126     3704   3823   3169    972   -345      9       C  
ATOM   3660  CD2 LEU B 126     -19.311 -45.544  23.370  1.00 25.55           C  
ANISOU 3660  CD2 LEU B 126     4457   3783   1468    957    444   -517       C  
ATOM   3661  N   ILE B 127     -19.148 -40.173  24.667  1.00 19.01           N  
ANISOU 3661  N   ILE B 127     3184   3121    915    724     18    -84       N  
ATOM   3662  CA  ILE B 127     -18.090 -39.369  25.271  1.00 20.05           C  
ANISOU 3662  CA  ILE B 127     3313   3444    858    639   -174    -68       C  
ATOM   3663  C   ILE B 127     -17.298 -40.299  26.190  1.00 21.77           C  
ANISOU 3663  C   ILE B 127     3195   3654   1420    757   -119    129       C  
ATOM   3664  O   ILE B 127     -17.886 -41.085  26.935  1.00 24.87           O  
ANISOU 3664  O   ILE B 127     3503   3867   2075    485   -108    416       O  
ATOM   3665  CB  ILE B 127     -18.657 -38.194  26.100  1.00 20.58           C  
ANISOU 3665  CB  ILE B 127     3155   3442   1221    733   -166    -75       C  
ATOM   3666  CG1 ILE B 127     -19.412 -37.184  25.210  1.00 20.78           C  
ANISOU 3666  CG1 ILE B 127     3396   3218   1281    618     33     90       C  
ATOM   3667  CG2 ILE B 127     -17.551 -37.537  26.915  1.00 22.48           C  
ANISOU 3667  CG2 ILE B 127     3436   3585   1518    625   -271   -223       C  
ATOM   3668  CD1 ILE B 127     -18.560 -36.496  24.166  1.00 20.17           C  
ANISOU 3668  CD1 ILE B 127     3391   3228   1044    451    -37   -166       C  
ATOM   3669  N   SER B 128     -15.977 -40.213  26.144  1.00 20.01           N  
ANISOU 3669  N   SER B 128     3077   3425   1099    869     26   -325       N  
ATOM   3670  CA  SER B 128     -15.132 -41.088  26.950  1.00 20.70           C  
ANISOU 3670  CA  SER B 128     3184   3678   1000    807    105    -83       C  
ATOM   3671  C   SER B 128     -14.612 -40.372  28.193  1.00 20.73           C  
ANISOU 3671  C   SER B 128     3235   3662    979    851    116    -40       C  
ATOM   3672  O   SER B 128     -14.443 -39.148  28.192  1.00 21.15           O  
ANISOU 3672  O   SER B 128     3260   3719   1056    656    108   -171       O  
ATOM   3673  CB  SER B 128     -13.962 -41.640  26.116  1.00 21.94           C  
ANISOU 3673  CB  SER B 128     3378   3582   1373    931    226   -324       C  
ATOM   3674  OG  SER B 128     -12.917 -40.684  25.968  1.00 23.60           O  
ANISOU 3674  OG  SER B 128     3290   3954   1722    897    298   -303       O  
ATOM   3675  N   ALA B 129     -14.366 -41.145  29.250  1.00 19.96           N  
ANISOU 3675  N   ALA B 129     3302   3692    589    768    268   -257       N  
ATOM   3676  CA  ALA B 129     -13.727 -40.621  30.457  1.00 20.53           C  
ANISOU 3676  CA  ALA B 129     3281   3704    815    486   -178    218       C  
ATOM   3677  C   ALA B 129     -12.304 -40.121  30.161  1.00 20.96           C  
ANISOU 3677  C   ALA B 129     3177   3761   1026    742    166     77       C  
ATOM   3678  O   ALA B 129     -11.849 -39.136  30.745  1.00 21.64           O  
ANISOU 3678  O   ALA B 129     3395   3783   1041    611    194    100       O  
ATOM   3679  CB  ALA B 129     -13.724 -41.672  31.560  1.00 19.90           C  
ANISOU 3679  CB  ALA B 129     3371   3599    591    635   -224     34       C  
ATOM   3680  N   GLN B 130     -11.615 -40.781  29.232  1.00 21.71           N  
ANISOU 3680  N   GLN B 130     3360   3863   1025    792    293    159       N  
ATOM   3681  CA  GLN B 130     -10.259 -40.371  28.869  1.00 23.87           C  
ANISOU 3681  CA  GLN B 130     3487   3950   1633    677    602    -27       C  
ATOM   3682  C   GLN B 130     -10.230 -38.970  28.250  1.00 22.82           C  
ANISOU 3682  C   GLN B 130     3327   4020   1321    709    487     52       C  
ATOM   3683  O   GLN B 130      -9.314 -38.194  28.458  1.00 22.28           O  
ANISOU 3683  O   GLN B 130     3473   3907   1082    654    466      9       O  
ATOM   3684  CB  GLN B 130      -9.610 -41.394  27.942  1.00 25.74           C  
ANISOU 3684  CB  GLN B 130     3378   4154   2248    742    609   -322       C  
ATOM   3685  CG  GLN B 130      -8.192 -41.044  27.551  1.00 26.82           C  
ANISOU 3685  CG  GLN B 130     3521   4397   2270    665    726   -170       C  
ATOM   3686  CD  GLN B 130      -7.226 -41.094  28.731  1.00 29.77           C  
ANISOU 3686  CD  GLN B 130     3943   5047   2320    646    588    147       C  
ATOM   3687  OE1 GLN B 130      -7.455 -41.746  29.728  1.00 34.46           O  
ANISOU 3687  OE1 GLN B 130     4750   5122   3218    485    895    732       O  
ATOM   3688  NE2 GLN B 130      -6.162 -40.363  28.623  1.00 31.24           N  
ANISOU 3688  NE2 GLN B 130     4347   4784   2736    437    579    314       N  
ATOM   3689  N   GLN B 131     -11.231 -38.631  27.464  1.00 21.81           N  
ANISOU 3689  N   GLN B 131     3007   3839   1438    684    678    -67       N  
ATOM   3690  CA  GLN B 131     -11.210 -37.275  26.931  1.00 23.34           C  
ANISOU 3690  CA  GLN B 131     3623   3863   1379    689    691    -20       C  
ATOM   3691  C   GLN B 131     -11.562 -36.220  27.975  1.00 21.88           C  
ANISOU 3691  C   GLN B 131     3233   3738   1340    620    521     38       C  
ATOM   3692  O   GLN B 131     -11.102 -35.086  27.863  1.00 22.32           O  
ANISOU 3692  O   GLN B 131     3455   3709   1314    625    573   -182       O  
ATOM   3693  CB  GLN B 131     -11.992 -37.118  25.634  1.00 27.26           C  
ANISOU 3693  CB  GLN B 131     3539   4294   2525    615    -50    301       C  
ATOM   3694  CG  GLN B 131     -13.466 -37.420  25.703  1.00 26.90           C  
ANISOU 3694  CG  GLN B 131     3697   4343   2180    361   -268    -56       C  
ATOM   3695  CD  GLN B 131     -14.069 -37.563  24.322  1.00 27.35           C  
ANISOU 3695  CD  GLN B 131     4478   4259   1652   -119    219   -479       C  
ATOM   3696  OE1 GLN B 131     -14.864 -38.465  24.053  1.00 25.21           O  
ANISOU 3696  OE1 GLN B 131     3687   4017   1873    349   -388   -126       O  
ATOM   3697  NE2 GLN B 131     -13.693 -36.655  23.433  1.00 25.81           N  
ANISOU 3697  NE2 GLN B 131     3712   4646   1446     76    456   -445       N  
ATOM   3698  N   VAL B 132     -12.339 -36.606  28.991  1.00 20.63           N  
ANISOU 3698  N   VAL B 132     3223   3575   1040    633    393    -78       N  
ATOM   3699  CA  VAL B 132     -12.563 -35.750  30.164  1.00 19.74           C  
ANISOU 3699  CA  VAL B 132     3046   3536    915    635    464     46       C  
ATOM   3700  C   VAL B 132     -11.223 -35.522  30.864  1.00 20.97           C  
ANISOU 3700  C   VAL B 132     3241   3724   1000    625    391   -250       C  
ATOM   3701  O   VAL B 132     -10.841 -34.393  31.156  1.00 21.95           O  
ANISOU 3701  O   VAL B 132     3342   3807   1188    407    248    -26       O  
ATOM   3702  CB  VAL B 132     -13.596 -36.355  31.153  1.00 19.85           C  
ANISOU 3702  CB  VAL B 132     2841   3783    917    528    350    -11       C  
ATOM   3703  CG1 VAL B 132     -13.609 -35.600  32.488  1.00 20.15           C  
ANISOU 3703  CG1 VAL B 132     3036   3362   1255    442    219   -205       C  
ATOM   3704  CG2 VAL B 132     -14.991 -36.380  30.529  1.00 18.81           C  
ANISOU 3704  CG2 VAL B 132     2928   3623    596    590    240   -153       C  
ATOM   3705  N   GLU B 133     -10.498 -36.608  31.092  1.00 21.56           N  
ANISOU 3705  N   GLU B 133     3173   3917   1102    607    296     56       N  
ATOM   3706  CA  GLU B 133      -9.219 -36.553  31.777  1.00 23.03           C  
ANISOU 3706  CA  GLU B 133     3393   3929   1427    575     66    -15       C  
ATOM   3707  C   GLU B 133      -8.237 -35.656  31.039  1.00 22.58           C  
ANISOU 3707  C   GLU B 133     3297   4097   1182    600    183   -108       C  
ATOM   3708  O   GLU B 133      -7.567 -34.845  31.656  1.00 23.24           O  
ANISOU 3708  O   GLU B 133     3450   4057   1323    668    326   -250       O  
ATOM   3709  CB  GLU B 133      -8.677 -37.969  31.874  1.00 25.23           C  
ANISOU 3709  CB  GLU B 133     3599   4072   1913    700    -41     60       C  
ATOM   3710  CG  GLU B 133      -7.248 -38.071  32.325  1.00 27.78           C  
ANISOU 3710  CG  GLU B 133     3619   4523   2413    508   -131     37       C  
ATOM   3711  CD  GLU B 133      -7.170 -38.090  33.820  1.00 29.13           C  
ANISOU 3711  CD  GLU B 133     3928   4692   2446    340   -342     20       C  
ATOM   3712  OE1 GLU B 133      -7.854 -38.923  34.440  1.00 32.32           O  
ANISOU 3712  OE1 GLU B 133     3842   5350   3086     72   -138    116       O  
ATOM   3713  OE2 GLU B 133      -6.418 -37.270  34.359  1.00 32.31           O  
ANISOU 3713  OE2 GLU B 133     4494   4837   2945    150   -439   -146       O  
ATOM   3714  N   GLU B 134      -8.190 -35.771  29.711  1.00 22.80           N  
ANISOU 3714  N   GLU B 134     3379   4091   1192    769    452    -33       N  
ATOM   3715  CA  GLU B 134      -7.279 -34.965  28.903  1.00 24.10           C  
ANISOU 3715  CA  GLU B 134     3568   3952   1636    573    309    104       C  
ATOM   3716  C   GLU B 134      -7.638 -33.477  28.851  1.00 23.30           C  
ANISOU 3716  C   GLU B 134     3422   3801   1627    375    367    -53       C  
ATOM   3717  O   GLU B 134      -6.763 -32.642  28.604  1.00 24.87           O  
ANISOU 3717  O   GLU B 134     3474   4194   1779    173    331     -6       O  
ATOM   3718  CB  GLU B 134      -7.141 -35.559  27.492  1.00 24.80           C  
ANISOU 3718  CB  GLU B 134     3546   4169   1708    483    515      7       C  
ATOM   3719  CG  GLU B 134      -6.237 -36.773  27.481  1.00 28.66           C  
ANISOU 3719  CG  GLU B 134     4276   4392   2220    784    597    -57       C  
ATOM   3720  CD  GLU B 134      -6.236 -37.540  26.172  1.00 31.94           C  
ANISOU 3720  CD  GLU B 134     4958   4668   2510    801    212   -339       C  
ATOM   3721  OE1 GLU B 134      -6.707 -37.014  25.148  1.00 36.82           O  
ANISOU 3721  OE1 GLU B 134     6329   5281   2379   1072    148   -227       O  
ATOM   3722  OE2 GLU B 134      -5.738 -38.685  26.166  1.00 32.78           O  
ANISOU 3722  OE2 GLU B 134     4527   4900   3026    872    624   -381       O  
ATOM   3723  N   ALA B 135      -8.905 -33.148  29.100  1.00 22.24           N  
ANISOU 3723  N   ALA B 135     3430   3784   1235    405    474   -163       N  
ATOM   3724  CA  ALA B 135      -9.367 -31.756  29.043  1.00 21.09           C  
ANISOU 3724  CA  ALA B 135     3212   3642   1157    291    -32   -204       C  
ATOM   3725  C   ALA B 135      -9.158 -31.003  30.364  1.00 20.73           C  
ANISOU 3725  C   ALA B 135     3081   3682   1112    278     56   -186       C  
ATOM   3726  O   ALA B 135      -9.265 -29.785  30.402  1.00 23.31           O  
ANISOU 3726  O   ALA B 135     3371   3697   1789    344    -53   -204       O  
ATOM   3727  CB  ALA B 135     -10.831 -31.681  28.598  1.00 20.33           C  
ANISOU 3727  CB  ALA B 135     2973   3654   1097    340    253   -137       C  
ATOM   3728  N   ILE B 136      -8.821 -31.726  31.433  1.00 21.23           N  
ANISOU 3728  N   ILE B 136     3152   3882   1030    333    263    -96       N  
ATOM   3729  CA  ILE B 136      -8.680 -31.124  32.757  1.00 20.41           C  
ANISOU 3729  CA  ILE B 136     2914   3739   1099    251    112    -79       C  
ATOM   3730  C   ILE B 136      -7.529 -30.117  32.815  1.00 22.22           C  
ANISOU 3730  C   ILE B 136     2734   4060   1647    254     88   -145       C  
ATOM   3731  O   ILE B 136      -6.428 -30.368  32.316  1.00 24.64           O  
ANISOU 3731  O   ILE B 136     2909   4506   1944    409    375   -110       O  
ATOM   3732  CB  ILE B 136      -8.522 -32.204  33.856  1.00 21.56           C  
ANISOU 3732  CB  ILE B 136     3120   3766   1303    177      6     67       C  
ATOM   3733  CG1 ILE B 136      -9.828 -32.992  34.022  1.00 20.86           C  
ANISOU 3733  CG1 ILE B 136     2988   3598   1337    361   -161    173       C  
ATOM   3734  CG2 ILE B 136      -8.085 -31.589  35.178  1.00 20.76           C  
ANISOU 3734  CG2 ILE B 136     3022   3406   1460    334    161   -143       C  
ATOM   3735  CD1 ILE B 136      -9.675 -34.260  34.845  1.00 20.87           C  
ANISOU 3735  CD1 ILE B 136     3543   3530    856    190   -225     14       C  
ATOM   3736  N   ARG B 137      -7.796 -28.973  33.436  1.00 21.32           N  
ANISOU 3736  N   ARG B 137     2836   4072   1191    271    -11    -70       N  
ATOM   3737  CA  ARG B 137      -6.785 -27.942  33.632  1.00 24.25           C  
ANISOU 3737  CA  ARG B 137     3013   4287   1911    107    234    116       C  
ATOM   3738  C   ARG B 137      -6.712 -27.604  35.106  1.00 24.81           C  
ANISOU 3738  C   ARG B 137     2826   4650   1950    291   -124      7       C  
ATOM   3739  O   ARG B 137      -7.563 -28.018  35.863  1.00 24.24           O  
ANISOU 3739  O   ARG B 137     2967   4600   1644    315   -125    -22       O  
ATOM   3740  CB  ARG B 137      -7.140 -26.704  32.821  1.00 24.75           C  
ANISOU 3740  CB  ARG B 137     2935   4211   2256    298     90     53       C  
ATOM   3741  CG  ARG B 137      -8.002 -27.049  31.630  1.00 26.01           C  
ANISOU 3741  CG  ARG B 137     3204   4428   2251    249      7    -30       C  
ATOM   3742  CD  ARG B 137      -7.581 -26.436  30.320  1.00 28.05           C  
ANISOU 3742  CD  ARG B 137     3429   4164   3064     -4    515    262       C  
ATOM   3743  NE  ARG B 137      -8.054 -25.073  30.178  1.00 30.33           N  
ANISOU 3743  NE  ARG B 137     3717   4594   3211    586   -144    438       N  
ATOM   3744  CZ  ARG B 137      -8.656 -24.567  29.105  1.00 28.66           C  
ANISOU 3744  CZ  ARG B 137     3926   5068   1894    214    168    -80       C  
ATOM   3745  NH1 ARG B 137      -9.019 -23.302  29.138  1.00 29.29           N  
ANISOU 3745  NH1 ARG B 137     3816   4945   2366    242     57    294       N  
ATOM   3746  NH2 ARG B 137      -8.891 -25.283  28.007  1.00 30.48           N  
ANISOU 3746  NH2 ARG B 137     3739   4549   3291    -64    253   -836       N  
ATOM   3747  N   PRO B 138      -5.666 -26.888  35.521  1.00 26.72           N  
ANISOU 3747  N   PRO B 138     2766   4706   2678    375    -27   -117       N  
ATOM   3748  CA  PRO B 138      -5.522 -26.514  36.928  1.00 28.23           C  
ANISOU 3748  CA  PRO B 138     2996   5148   2579    273     39     21       C  
ATOM   3749  C   PRO B 138      -6.743 -25.777  37.510  1.00 26.42           C  
ANISOU 3749  C   PRO B 138     3220   4717   2098    298     37     54       C  
ATOM   3750  O   PRO B 138      -7.047 -25.941  38.701  1.00 26.05           O  
ANISOU 3750  O   PRO B 138     3239   4758   1899    333   -269     15       O  
ATOM   3751  CB  PRO B 138      -4.287 -25.614  36.915  1.00 29.84           C  
ANISOU 3751  CB  PRO B 138     3050   5402   2883    154    156   -149       C  
ATOM   3752  CG  PRO B 138      -3.488 -26.097  35.748  1.00 28.90           C  
ANISOU 3752  CG  PRO B 138     2968   4958   3051    306   -139   -661       C  
ATOM   3753  CD  PRO B 138      -4.484 -26.532  34.719  1.00 27.55           C  
ANISOU 3753  CD  PRO B 138     2599   5147   2719    431   -128     18       C  
ATOM   3754  N   ASN B 139      -7.440 -24.997  36.677  1.00 26.00           N  
ANISOU 3754  N   ASN B 139     3098   4882   1896    241     32    -28       N  
ATOM   3755  CA  ASN B 139      -8.632 -24.259  37.102  1.00 25.44           C  
ANISOU 3755  CA  ASN B 139     3158   4444   2062    350   -198      2       C  
ATOM   3756  C   ASN B 139      -9.985 -24.837  36.654  1.00 22.80           C  
ANISOU 3756  C   ASN B 139     3275   3874   1514    257     19     49       C  
ATOM   3757  O   ASN B 139     -10.992 -24.112  36.619  1.00 22.59           O  
ANISOU 3757  O   ASN B 139     3179   3862   1542    203    150    161       O  
ATOM   3758  CB  ASN B 139      -8.523 -22.775  36.722  1.00 28.28           C  
ANISOU 3758  CB  ASN B 139     3701   4559   2485     75    111     19       C  
ATOM   3759  CG  ASN B 139      -8.535 -22.534  35.222  1.00 27.69           C  
ANISOU 3759  CG  ASN B 139     3521   4415   2581     27   -113    109       C  
ATOM   3760  OD1 ASN B 139      -8.697 -21.396  34.783  1.00 32.06           O  
ANISOU 3760  OD1 ASN B 139     3813   4831   3537    179   -277    583       O  
ATOM   3761  ND2 ASN B 139      -8.359 -23.589  34.430  1.00 27.20           N  
ANISOU 3761  ND2 ASN B 139     3334   4719   2282    124     54     32       N  
ATOM   3762  N   THR B 140     -10.021 -26.130  36.332  1.00 21.60           N  
ANISOU 3762  N   THR B 140     3023   3898   1284    177    -18    -92       N  
ATOM   3763  CA  THR B 140     -11.295 -26.816  36.062  1.00 20.74           C  
ANISOU 3763  CA  THR B 140     2896   3608   1374    239    292    -45       C  
ATOM   3764  C   THR B 140     -12.083 -26.986  37.356  1.00 19.31           C  
ANISOU 3764  C   THR B 140     2816   3455   1065    196     49   -176       C  
ATOM   3765  O   THR B 140     -11.574 -27.542  38.329  1.00 19.90           O  
ANISOU 3765  O   THR B 140     2851   3619   1091    340     33   -204       O  
ATOM   3766  CB  THR B 140     -11.057 -28.177  35.383  1.00 20.35           C  
ANISOU 3766  CB  THR B 140     2890   3659   1181    165    116   -126       C  
ATOM   3767  OG1 THR B 140     -10.278 -27.972  34.200  1.00 20.24           O  
ANISOU 3767  OG1 THR B 140     2908   3693   1088     99     28     27       O  
ATOM   3768  CG2 THR B 140     -12.379 -28.883  35.035  1.00 18.53           C  
ANISOU 3768  CG2 THR B 140     2782   3438    821    372     56   -185       C  
ATOM   3769  N   PHE B 141     -13.319 -26.491  37.369  1.00 18.74           N  
ANISOU 3769  N   PHE B 141     2960   3222    936    336    110   -174       N  
ATOM   3770  CA  PHE B 141     -14.108 -26.521  38.589  1.00 19.09           C  
ANISOU 3770  CA  PHE B 141     3026   3226   1001    214    166   -114       C  
ATOM   3771  C   PHE B 141     -15.438 -27.248  38.468  1.00 18.53           C  
ANISOU 3771  C   PHE B 141     2746   3266   1027    441    -32   -146       C  
ATOM   3772  O   PHE B 141     -16.154 -27.355  39.455  1.00 19.28           O  
ANISOU 3772  O   PHE B 141     2804   3474   1047    341    -32   -112       O  
ATOM   3773  CB  PHE B 141     -14.322 -25.108  39.131  1.00 20.62           C  
ANISOU 3773  CB  PHE B 141     3408   3242   1182    313     -4   -112       C  
ATOM   3774  CG  PHE B 141     -15.305 -24.291  38.343  1.00 20.50           C  
ANISOU 3774  CG  PHE B 141     3250   3195   1341    395    235   -102       C  
ATOM   3775  CD1 PHE B 141     -16.653 -24.267  38.683  1.00 20.41           C  
ANISOU 3775  CD1 PHE B 141     3016   3075   1664    313   -127    -65       C  
ATOM   3776  CD2 PHE B 141     -14.877 -23.530  37.264  1.00 21.60           C  
ANISOU 3776  CD2 PHE B 141     3365   3391   1449    335    226     43       C  
ATOM   3777  CE1 PHE B 141     -17.560 -23.507  37.957  1.00 20.01           C  
ANISOU 3777  CE1 PHE B 141     3262   3051   1287    160   -119     87       C  
ATOM   3778  CE2 PHE B 141     -15.776 -22.764  36.539  1.00 21.64           C  
ANISOU 3778  CE2 PHE B 141     3183   3314   1723    231    344    142       C  
ATOM   3779  CZ  PHE B 141     -17.115 -22.749  36.884  1.00 21.33           C  
ANISOU 3779  CZ  PHE B 141     3082   3214   1808    333    290    240       C  
ATOM   3780  N   LEU B 142     -15.759 -27.737  37.270  1.00 17.47           N  
ANISOU 3780  N   LEU B 142     2714   2927    997    294      5    -36       N  
ATOM   3781  CA  LEU B 142     -16.933 -28.580  37.073  1.00 16.50           C  
ANISOU 3781  CA  LEU B 142     2593   2860    815    440    -35   -170       C  
ATOM   3782  C   LEU B 142     -16.787 -29.411  35.815  1.00 16.28           C  
ANISOU 3782  C   LEU B 142     2611   2791    782    297      8   -129       C  
ATOM   3783  O   LEU B 142     -16.321 -28.911  34.778  1.00 17.20           O  
ANISOU 3783  O   LEU B 142     2830   2899    806    254    -11    -65       O  
ATOM   3784  CB  LEU B 142     -18.226 -27.745  37.001  1.00 16.83           C  
ANISOU 3784  CB  LEU B 142     2561   2812   1021    440    -86    194       C  
ATOM   3785  CG  LEU B 142     -19.580 -28.443  36.772  1.00 16.85           C  
ANISOU 3785  CG  LEU B 142     2720   2815    864    346    -96    139       C  
ATOM   3786  CD1 LEU B 142     -19.920 -29.400  37.906  1.00 16.83           C  
ANISOU 3786  CD1 LEU B 142     2632   2584   1178    312    -46    180       C  
ATOM   3787  CD2 LEU B 142     -20.692 -27.426  36.566  1.00 16.63           C  
ANISOU 3787  CD2 LEU B 142     2574   2726   1018    261   -244    -55       C  
ATOM   3788  N   ILE B 143     -17.188 -30.676  35.932  1.00 15.75           N  
ANISOU 3788  N   ILE B 143     2536   2708    740    337   -106   -187       N  
ATOM   3789  CA  ILE B 143     -17.425 -31.571  34.795  1.00 15.55           C  
ANISOU 3789  CA  ILE B 143     2467   2715    725    300     45   -218       C  
ATOM   3790  C   ILE B 143     -18.920 -31.894  34.787  1.00 16.05           C  
ANISOU 3790  C   ILE B 143     2568   2735    795    249      8   -111       C  
ATOM   3791  O   ILE B 143     -19.459 -32.411  35.777  1.00 16.09           O  
ANISOU 3791  O   ILE B 143     2685   2714    713    247    -51    -59       O  
ATOM   3792  CB  ILE B 143     -16.606 -32.890  34.898  1.00 15.94           C  
ANISOU 3792  CB  ILE B 143     2513   2758    783    315    -61   -194       C  
ATOM   3793  CG1 ILE B 143     -15.095 -32.616  34.861  1.00 16.55           C  
ANISOU 3793  CG1 ILE B 143     2499   2901    886    305   -211   -113       C  
ATOM   3794  CG2 ILE B 143     -16.985 -33.857  33.771  1.00 17.18           C  
ANISOU 3794  CG2 ILE B 143     2691   3007    827    339   -185   -318       C  
ATOM   3795  CD1 ILE B 143     -14.268 -33.616  35.658  1.00 18.29           C  
ANISOU 3795  CD1 ILE B 143     2671   3154   1121    408   -233    129       C  
ATOM   3796  N   THR B 144     -19.594 -31.518  33.695  1.00 16.40           N  
ANISOU 3796  N   THR B 144     2540   2913    777    337     57   -109       N  
ATOM   3797  CA  THR B 144     -20.997 -31.860  33.483  1.00 15.38           C  
ANISOU 3797  CA  THR B 144     2658   2785    400     80    -95     96       C  
ATOM   3798  C   THR B 144     -21.164 -32.685  32.227  1.00 15.61           C  
ANISOU 3798  C   THR B 144     2672   2580    677    378     56   -112       C  
ATOM   3799  O   THR B 144     -20.999 -32.163  31.132  1.00 16.42           O  
ANISOU 3799  O   THR B 144     2717   2868    652    348     42    -16       O  
ATOM   3800  CB  THR B 144     -21.914 -30.706  33.027  1.00 17.67           C  
ANISOU 3800  CB  THR B 144     2651   2722   1338    335    116   -405       C  
ATOM   3801  OG1 THR B 144     -21.326 -29.385  33.016  1.00 22.96           O  
ANISOU 3801  OG1 THR B 144     3643   2669   2411    232   -163   -687       O  
ATOM   3802  CG2 THR B 144     -23.292 -30.838  33.502  1.00 13.68           C  
ANISOU 3802  CG2 THR B 144     2628   2301    267    287     99   -133       C  
ATOM   3803  N   ILE B 145     -21.595 -33.925  32.362  1.00 15.25           N  
ANISOU 3803  N   ILE B 145     2569   2647    578    271    -50      0       N  
ATOM   3804  CA  ILE B 145     -21.839 -34.762  31.181  1.00 15.66           C  
ANISOU 3804  CA  ILE B 145     2595   2587    766    323   -112   -120       C  
ATOM   3805  C   ILE B 145     -23.164 -35.482  31.366  1.00 15.65           C  
ANISOU 3805  C   ILE B 145     2634   2634    678    337    -40   -149       C  
ATOM   3806  O   ILE B 145     -23.406 -36.049  32.424  1.00 16.18           O  
ANISOU 3806  O   ILE B 145     2789   2612    746    309      0   -107       O  
ATOM   3807  CB  ILE B 145     -20.708 -35.800  30.968  1.00 15.48           C  
ANISOU 3807  CB  ILE B 145     2507   2743    631    321   -124   -203       C  
ATOM   3808  CG1 ILE B 145     -19.331 -35.126  30.809  1.00 15.22           C  
ANISOU 3808  CG1 ILE B 145     2590   2639    553    305     71   -130       C  
ATOM   3809  CG2 ILE B 145     -21.033 -36.735  29.799  1.00 15.49           C  
ANISOU 3809  CG2 ILE B 145     2458   2655    769    353     51   -303       C  
ATOM   3810  CD1 ILE B 145     -19.111 -34.415  29.488  1.00 16.58           C  
ANISOU 3810  CD1 ILE B 145     2865   2728    705    238    118      2       C  
ATOM   3811  N   HIS B 146     -24.018 -35.459  30.341  1.00 15.51           N  
ANISOU 3811  N   HIS B 146     2546   2621    723    450    -18    -29       N  
ATOM   3812  CA  HIS B 146     -25.350 -36.060  30.390  1.00 15.27           C  
ANISOU 3812  CA  HIS B 146     2571   2449    779    409    -64   -159       C  
ATOM   3813  C   HIS B 146     -25.239 -37.561  30.502  1.00 15.09           C  
ANISOU 3813  C   HIS B 146     2645   2474    613    338    -60    -31       C  
ATOM   3814  O   HIS B 146     -24.264 -38.144  30.037  1.00 15.79           O  
ANISOU 3814  O   HIS B 146     2772   2536    691    419    -85   -109       O  
ATOM   3815  CB  HIS B 146     -26.124 -35.670  29.129  1.00 15.31           C  
ANISOU 3815  CB  HIS B 146     2578   2624    612    427    134    -46       C  
ATOM   3816  CG  HIS B 146     -25.473 -36.155  27.839  1.00 16.00           C  
ANISOU 3816  CG  HIS B 146     2786   2760    534    514      6   -179       C  
ATOM   3817  ND1 HIS B 146     -25.913 -37.236  27.162  1.00 17.01           N  
ANISOU 3817  ND1 HIS B 146     2951   2709    799    481     86   -115       N  
ATOM   3818  CD2 HIS B 146     -24.374 -35.672  27.130  1.00 14.91           C  
ANISOU 3818  CD2 HIS B 146     2691   2493    479    479    -43    -51       C  
ATOM   3819  CE1 HIS B 146     -25.142 -37.429  26.069  1.00 15.73           C  
ANISOU 3819  CE1 HIS B 146     2831   2538    606    573    -78   -201       C  
ATOM   3820  NE2 HIS B 146     -24.201 -36.477  26.052  1.00 17.21           N  
ANISOU 3820  NE2 HIS B 146     2955   2580   1005    590    138   -374       N  
ATOM   3821  N   HIS B 147     -26.230 -38.193  31.126  1.00 14.37           N  
ANISOU 3821  N   HIS B 147     2692   2363    404    371   -152     18       N  
ATOM   3822  CA  HIS B 147     -26.237 -39.646  31.318  1.00 14.69           C  
ANISOU 3822  CA  HIS B 147     2632   2351    596    263     15    113       C  
ATOM   3823  C   HIS B 147     -26.779 -40.343  30.103  1.00 15.54           C  
ANISOU 3823  C   HIS B 147     2709   2509    685    314     -4      2       C  
ATOM   3824  O   HIS B 147     -26.107 -41.190  29.509  1.00 16.30           O  
ANISOU 3824  O   HIS B 147     3002   2596    594    530   -146    -41       O  
ATOM   3825  CB  HIS B 147     -27.032 -39.990  32.577  1.00 14.45           C  
ANISOU 3825  CB  HIS B 147     2703   2283    501    347      7     36       C  
ATOM   3826  CG  HIS B 147     -26.984 -41.462  32.978  1.00 15.75           C  
ANISOU 3826  CG  HIS B 147     2989   2353    643    208    111     95       C  
ATOM   3827  ND1 HIS B 147     -27.698 -41.944  34.019  1.00 16.18           N  
ANISOU 3827  ND1 HIS B 147     2912   2664    572    310     67    200       N  
ATOM   3828  CD2 HIS B 147     -26.305 -42.553  32.434  1.00 16.34           C  
ANISOU 3828  CD2 HIS B 147     3043   2538    627    250    119    -44       C  
ATOM   3829  CE1 HIS B 147     -27.484 -43.268  34.142  1.00 16.58           C  
ANISOU 3829  CE1 HIS B 147     3165   2656    476    302    -44     91       C  
ATOM   3830  NE2 HIS B 147     -26.622 -43.641  33.179  1.00 16.37           N  
ANISOU 3830  NE2 HIS B 147     3244   2709    266    362   -163     86       N  
ATOM   3831  N   VAL B 148     -27.996 -39.988  29.710  1.00 15.16           N  
ANISOU 3831  N   VAL B 148     2745   2408    606    287   -147     56       N  
ATOM   3832  CA  VAL B 148     -28.558 -40.491  28.458  1.00 16.13           C  
ANISOU 3832  CA  VAL B 148     3063   2404    661    368   -184    -61       C  
ATOM   3833  C   VAL B 148     -28.895 -39.323  27.533  1.00 16.20           C  
ANISOU 3833  C   VAL B 148     2993   2597    564    507    -73    -10       C  
ATOM   3834  O   VAL B 148     -29.558 -38.368  27.936  1.00 15.05           O  
ANISOU 3834  O   VAL B 148     2771   2477    469    482    -75    170       O  
ATOM   3835  CB  VAL B 148     -29.800 -41.363  28.718  1.00 16.62           C  
ANISOU 3835  CB  VAL B 148     3064   2507    740    316   -376   -133       C  
ATOM   3836  CG1 VAL B 148     -30.605 -41.620  27.439  1.00 16.09           C  
ANISOU 3836  CG1 VAL B 148     3110   2426    574    192   -232   -116       C  
ATOM   3837  CG2 VAL B 148     -29.398 -42.670  29.377  1.00 16.99           C  
ANISOU 3837  CG2 VAL B 148     3225   2403    826    254      8    -91       C  
ATOM   3838  N   ASN B 149     -28.437 -39.408  26.285  1.00 16.18           N  
ANISOU 3838  N   ASN B 149     2910   2557    677    364     82     24       N  
ATOM   3839  CA  ASN B 149     -28.667 -38.342  25.317  1.00 15.84           C  
ANISOU 3839  CA  ASN B 149     2890   2610    519    466    108    -36       C  
ATOM   3840  C   ASN B 149     -30.124 -38.245  24.863  1.00 16.27           C  
ANISOU 3840  C   ASN B 149     2949   2681    551    424     76   -130       C  
ATOM   3841  O   ASN B 149     -30.710 -39.260  24.484  1.00 16.55           O  
ANISOU 3841  O   ASN B 149     3140   2566    580    427    -13    -55       O  
ATOM   3842  CB  ASN B 149     -27.776 -38.538  24.101  1.00 16.33           C  
ANISOU 3842  CB  ASN B 149     2959   2615    629    450    226     55       C  
ATOM   3843  CG  ASN B 149     -27.710 -37.296  23.246  1.00 17.08           C  
ANISOU 3843  CG  ASN B 149     3030   2660    800    391     95    112       C  
ATOM   3844  OD1 ASN B 149     -26.930 -36.382  23.528  1.00 19.97           O  
ANISOU 3844  OD1 ASN B 149     3131   3094   1362    199    222     89       O  
ATOM   3845  ND2 ASN B 149     -28.543 -37.229  22.233  1.00 15.78           N  
ANISOU 3845  ND2 ASN B 149     3052   2566    378    324    269    -50       N  
ATOM   3846  N   ASN B 150     -30.709 -37.042  24.880  1.00 16.59           N  
ANISOU 3846  N   ASN B 150     3000   2706    595    480    -53    -41       N  
ATOM   3847  CA  ASN B 150     -32.133 -36.911  24.523  1.00 18.01           C  
ANISOU 3847  CA  ASN B 150     3098   2862    883    389   -269   -253       C  
ATOM   3848  C   ASN B 150     -32.479 -37.130  23.058  1.00 17.35           C  
ANISOU 3848  C   ASN B 150     3166   2730    695    264    -46    -12       C  
ATOM   3849  O   ASN B 150     -33.614 -37.476  22.768  1.00 17.36           O  
ANISOU 3849  O   ASN B 150     3007   2961    625    310    149     35       O  
ATOM   3850  CB  ASN B 150     -32.752 -35.586  24.986  1.00 19.25           C  
ANISOU 3850  CB  ASN B 150     3483   2852    977    342    -54   -320       C  
ATOM   3851  CG  ASN B 150     -32.010 -34.394  24.450  1.00 20.85           C  
ANISOU 3851  CG  ASN B 150     3426   2817   1679    315    -17   -226       C  
ATOM   3852  OD1 ASN B 150     -30.805 -34.298  24.644  1.00 22.58           O  
ANISOU 3852  OD1 ASN B 150     3450   3200   1928    498   -129    -15       O  
ATOM   3853  ND2 ASN B 150     -32.717 -33.478  23.773  1.00 21.84           N  
ANISOU 3853  ND2 ASN B 150     3458   3421   1418    319   -286   -108       N  
ATOM   3854  N   GLU B 151     -31.525 -36.929  22.151  1.00 17.24           N  
ANISOU 3854  N   GLU B 151     3035   2722    792    278    -43   -180       N  
ATOM   3855  CA  GLU B 151     -31.805 -37.169  20.744  1.00 17.00           C  
ANISOU 3855  CA  GLU B 151     3210   2536    711    229     39    -51       C  
ATOM   3856  C   GLU B 151     -31.507 -38.602  20.297  1.00 16.15           C  
ANISOU 3856  C   GLU B 151     2907   2550    677    321    135     -8       C  
ATOM   3857  O   GLU B 151     -32.282 -39.185  19.532  1.00 16.00           O  
ANISOU 3857  O   GLU B 151     3032   2582    465    381    164    -94       O  
ATOM   3858  CB  GLU B 151     -31.077 -36.148  19.871  1.00 16.68           C  
ANISOU 3858  CB  GLU B 151     3238   2600    498    216    179   -160       C  
ATOM   3859  CG  GLU B 151     -31.569 -34.746  20.148  1.00 19.21           C  
ANISOU 3859  CG  GLU B 151     3632   2564   1103    348      2    126       C  
ATOM   3860  CD  GLU B 151     -31.068 -33.738  19.132  1.00 19.15           C  
ANISOU 3860  CD  GLU B 151     3499   2928    847    -58   -288     91       C  
ATOM   3861  OE1 GLU B 151     -30.915 -32.550  19.494  1.00 22.30           O  
ANISOU 3861  OE1 GLU B 151     4232   2878   1361    195    -41     78       O  
ATOM   3862  OE2 GLU B 151     -30.807 -34.141  17.978  1.00 19.64           O  
ANISOU 3862  OE2 GLU B 151     3514   3186    762    251   -139    360       O  
ATOM   3863  N   LEU B 152     -30.396 -39.165  20.784  1.00 15.82           N  
ANISOU 3863  N   LEU B 152     3020   2529    461    427    126    -52       N  
ATOM   3864  CA  LEU B 152     -29.880 -40.456  20.292  1.00 16.15           C  
ANISOU 3864  CA  LEU B 152     2908   2500    728    384    140    -60       C  
ATOM   3865  C   LEU B 152     -30.196 -41.630  21.186  1.00 17.06           C  
ANISOU 3865  C   LEU B 152     3149   2515    816    488     69     10       C  
ATOM   3866  O   LEU B 152     -30.267 -42.767  20.720  1.00 18.22           O  
ANISOU 3866  O   LEU B 152     3538   2548    834    255     38    -31       O  
ATOM   3867  CB  LEU B 152     -28.359 -40.400  20.135  1.00 16.84           C  
ANISOU 3867  CB  LEU B 152     2968   2580    849    396    234   -108       C  
ATOM   3868  CG  LEU B 152     -27.764 -39.384  19.164  1.00 16.56           C  
ANISOU 3868  CG  LEU B 152     2967   2537    785    230    153   -193       C  
ATOM   3869  CD1 LEU B 152     -26.259 -39.290  19.370  1.00 17.45           C  
ANISOU 3869  CD1 LEU B 152     2921   2648   1058    484     98    104       C  
ATOM   3870  CD2 LEU B 152     -28.107 -39.767  17.726  1.00 17.57           C  
ANISOU 3870  CD2 LEU B 152     3177   2852    645    232    158     12       C  
ATOM   3871  N   GLY B 153     -30.364 -41.358  22.473  1.00 17.01           N  
ANISOU 3871  N   GLY B 153     3151   2491    820    497    119     31       N  
ATOM   3872  CA  GLY B 153     -30.585 -42.433  23.418  1.00 17.19           C  
ANISOU 3872  CA  GLY B 153     3068   2622    841    339    199     55       C  
ATOM   3873  C   GLY B 153     -29.312 -42.994  24.015  1.00 17.49           C  
ANISOU 3873  C   GLY B 153     3204   2685    754    403     55    -33       C  
ATOM   3874  O   GLY B 153     -29.360 -43.902  24.854  1.00 17.12           O  
ANISOU 3874  O   GLY B 153     3247   2829    428    496    172    -99       O  
ATOM   3875  N   THR B 154     -28.177 -42.426  23.615  1.00 17.48           N  
ANISOU 3875  N   THR B 154     3113   2588    940    394     47    -96       N  
ATOM   3876  CA  THR B 154     -26.847 -42.915  23.988  1.00 17.63           C  
ANISOU 3876  CA  THR B 154     3275   2660    760    691     58     13       C  
ATOM   3877  C   THR B 154     -26.661 -42.939  25.490  1.00 17.91           C  
ANISOU 3877  C   THR B 154     3374   2633    795    575    -53    -54       C  
ATOM   3878  O   THR B 154     -26.874 -41.928  26.151  1.00 17.20           O  
ANISOU 3878  O   THR B 154     3306   2551    679    496    -24     87       O  
ATOM   3879  CB  THR B 154     -25.782 -41.989  23.394  1.00 17.99           C  
ANISOU 3879  CB  THR B 154     3031   2934    871    582   -153     13       C  
ATOM   3880  OG1 THR B 154     -26.117 -41.730  22.027  1.00 18.92           O  
ANISOU 3880  OG1 THR B 154     3399   3022    768    507      2     94       O  
ATOM   3881  CG2 THR B 154     -24.387 -42.604  23.478  1.00 18.67           C  
ANISOU 3881  CG2 THR B 154     3115   2976   1000    752    -51   -228       C  
ATOM   3882  N   VAL B 155     -26.272 -44.096  26.016  1.00 17.15           N  
ANISOU 3882  N   VAL B 155     3107   2776    633    459    -27    204       N  
ATOM   3883  CA  VAL B 155     -25.933 -44.221  27.431  1.00 16.81           C  
ANISOU 3883  CA  VAL B 155     3083   2585    719    512   -227     64       C  
ATOM   3884  C   VAL B 155     -24.453 -43.913  27.637  1.00 16.73           C  
ANISOU 3884  C   VAL B 155     3092   2667    595    572   -206     40       C  
ATOM   3885  O   VAL B 155     -23.582 -44.645  27.165  1.00 19.33           O  
ANISOU 3885  O   VAL B 155     3345   2895   1103    820   -160     11       O  
ATOM   3886  CB  VAL B 155     -26.266 -45.623  27.976  1.00 17.45           C  
ANISOU 3886  CB  VAL B 155     3260   2622    746    536   -244    147       C  
ATOM   3887  CG1 VAL B 155     -25.950 -45.708  29.474  1.00 18.13           C  
ANISOU 3887  CG1 VAL B 155     3167   2924    797    573   -298    240       C  
ATOM   3888  CG2 VAL B 155     -27.729 -45.955  27.700  1.00 17.72           C  
ANISOU 3888  CG2 VAL B 155     3293   2773    665    380    -35   -140       C  
ATOM   3889  N   GLN B 156     -24.179 -42.810  28.326  1.00 16.24           N  
ANISOU 3889  N   GLN B 156     2918   2624    626    604    -69     41       N  
ATOM   3890  CA  GLN B 156     -22.801 -42.354  28.560  1.00 15.88           C  
ANISOU 3890  CA  GLN B 156     2792   2619    620    748      7    -82       C  
ATOM   3891  C   GLN B 156     -22.130 -43.062  29.749  1.00 17.26           C  
ANISOU 3891  C   GLN B 156     2903   2744    910    782    -76    103       C  
ATOM   3892  O   GLN B 156     -22.819 -43.514  30.664  1.00 18.22           O  
ANISOU 3892  O   GLN B 156     3075   3000    844    598   -114     87       O  
ATOM   3893  CB  GLN B 156     -22.757 -40.832  28.747  1.00 16.13           C  
ANISOU 3893  CB  GLN B 156     2859   2576    692    631     -3    102       C  
ATOM   3894  CG  GLN B 156     -23.322 -40.028  27.571  1.00 16.30           C  
ANISOU 3894  CG  GLN B 156     2766   2859    567    736    -26     25       C  
ATOM   3895  CD  GLN B 156     -22.525 -40.179  26.276  1.00 17.82           C  
ANISOU 3895  CD  GLN B 156     2898   3045    827    882    144   -208       C  
ATOM   3896  OE1 GLN B 156     -21.429 -40.740  26.256  1.00 18.05           O  
ANISOU 3896  OE1 GLN B 156     2886   2933   1036    846     59     26       O  
ATOM   3897  NE2 GLN B 156     -23.075 -39.647  25.185  1.00 18.36           N  
ANISOU 3897  NE2 GLN B 156     3251   2955    767    839     83   -195       N  
ATOM   3898  N   PRO B 157     -20.782 -43.149  29.744  1.00 16.95           N  
ANISOU 3898  N   PRO B 157     2860   2664    913    650   -206     58       N  
ATOM   3899  CA  PRO B 157     -20.089 -43.867  30.821  1.00 18.15           C  
ANISOU 3899  CA  PRO B 157     2874   2986   1034    856   -401    -93       C  
ATOM   3900  C   PRO B 157     -19.902 -42.998  32.081  1.00 17.93           C  
ANISOU 3900  C   PRO B 157     2956   3004    851    670   -153     24       C  
ATOM   3901  O   PRO B 157     -18.779 -42.599  32.423  1.00 16.57           O  
ANISOU 3901  O   PRO B 157     3005   2786    503    721   -276     -7       O  
ATOM   3902  CB  PRO B 157     -18.755 -44.250  30.171  1.00 18.86           C  
ANISOU 3902  CB  PRO B 157     2982   2993   1188    740   -170     -8       C  
ATOM   3903  CG  PRO B 157     -18.502 -43.190  29.154  1.00 19.23           C  
ANISOU 3903  CG  PRO B 157     2889   2980   1438    881   -150    172       C  
ATOM   3904  CD  PRO B 157     -19.838 -42.632  28.731  1.00 17.99           C  
ANISOU 3904  CD  PRO B 157     2615   2906   1314    605   -122     -4       C  
ATOM   3905  N   ILE B 158     -21.001 -42.723  32.782  1.00 17.60           N  
ANISOU 3905  N   ILE B 158     2959   3056    671    672   -257   -128       N  
ATOM   3906  CA  ILE B 158     -20.947 -41.788  33.904  1.00 18.07           C  
ANISOU 3906  CA  ILE B 158     3019   3002    842    717   -221   -205       C  
ATOM   3907  C   ILE B 158     -20.085 -42.303  35.050  1.00 18.78           C  
ANISOU 3907  C   ILE B 158     3212   3103    819    833   -172    -77       C  
ATOM   3908  O   ILE B 158     -19.447 -41.530  35.724  1.00 18.99           O  
ANISOU 3908  O   ILE B 158     3193   3178    842    696   -129     61       O  
ATOM   3909  CB  ILE B 158     -22.339 -41.311  34.372  1.00 18.59           C  
ANISOU 3909  CB  ILE B 158     3089   3065    907    664    -94      0       C  
ATOM   3910  CG1 ILE B 158     -23.224 -42.489  34.774  1.00 19.78           C  
ANISOU 3910  CG1 ILE B 158     3238   3170   1107    556    138   -171       C  
ATOM   3911  CG2 ILE B 158     -22.997 -40.461  33.282  1.00 17.60           C  
ANISOU 3911  CG2 ILE B 158     2983   2794    908    572   -122    -96       C  
ATOM   3912  CD1 ILE B 158     -24.433 -42.084  35.593  1.00 20.89           C  
ANISOU 3912  CD1 ILE B 158     3511   3447    979    351    383   -249       C  
ATOM   3913  N   GLU B 159     -20.057 -43.610  35.259  1.00 18.84           N  
ANISOU 3913  N   GLU B 159     3053   3209    896    846   -462     83       N  
ATOM   3914  CA  GLU B 159     -19.181 -44.138  36.288  1.00 21.61           C  
ANISOU 3914  CA  GLU B 159     3263   3580   1368    904   -691    344       C  
ATOM   3915  C   GLU B 159     -17.708 -43.875  36.016  1.00 19.89           C  
ANISOU 3915  C   GLU B 159     3261   3249   1045    890   -412    224       C  
ATOM   3916  O   GLU B 159     -17.020 -43.390  36.876  1.00 19.86           O  
ANISOU 3916  O   GLU B 159     3421   3277    847    802   -293    207       O  
ATOM   3917  CB  GLU B 159     -19.407 -45.629  36.516  1.00 16.97           C  
ANISOU 3917  CB  GLU B 159     2207   3397    841   1724   -530    380       C  
ATOM   3918  CG  GLU B 159     -18.482 -46.223  37.584  1.00 16.90           C  
ANISOU 3918  CG  GLU B 159     1910   3522    987   1591   -275    604       C  
ATOM   3919  CD  GLU B 159     -19.073 -47.422  38.303  1.00 16.78           C  
ANISOU 3919  CD  GLU B 159     2544   2713   1117   1908   -316    580       C  
ATOM   3920  OE1 GLU B 159     -18.329 -48.108  39.013  1.00 19.76           O  
ANISOU 3920  OE1 GLU B 159     2799   2906   1802   1924   -471    713       O  
ATOM   3921  OE2 GLU B 159     -20.278 -47.692  38.151  1.00 31.25           O  
ANISOU 3921  OE2 GLU B 159     3385   4779   3706    423   -574    577       O  
ATOM   3922  N   ASP B 160     -17.247 -44.120  34.794  1.00 20.97           N  
ANISOU 3922  N   ASP B 160     3583   3230   1152    895   -343     52       N  
ATOM   3923  CA  ASP B 160     -15.853 -43.876  34.426  1.00 21.33           C  
ANISOU 3923  CA  ASP B 160     3635   3290   1180    653   -361   -100       C  
ATOM   3924  C   ASP B 160     -15.512 -42.393  34.490  1.00 18.92           C  
ANISOU 3924  C   ASP B 160     3299   3167    721    748   -232     62       C  
ATOM   3925  O   ASP B 160     -14.432 -42.013  34.952  1.00 19.20           O  
ANISOU 3925  O   ASP B 160     3234   3157    901    689   -203    190       O  
ATOM   3926  CB  ASP B 160     -15.580 -44.407  33.017  1.00 22.82           C  
ANISOU 3926  CB  ASP B 160     4136   3260   1273    732   -244   -137       C  
ATOM   3927  CG  ASP B 160     -15.525 -45.919  32.962  1.00 28.35           C  
ANISOU 3927  CG  ASP B 160     4623   3331   2815    881   -445   -711       C  
ATOM   3928  OD1 ASP B 160     -15.677 -46.463  31.852  1.00 31.81           O  
ANISOU 3928  OD1 ASP B 160     4953   3679   3452    998   -382  -1341       O  
ATOM   3929  OD2 ASP B 160     -15.326 -46.566  34.016  1.00 31.47           O  
ANISOU 3929  OD2 ASP B 160     5077   3453   3424    714   -295    -99       O  
ATOM   3930  N   ILE B 161     -16.441 -41.558  34.019  1.00 18.04           N  
ANISOU 3930  N   ILE B 161     3268   3018    568    684   -217    -42       N  
ATOM   3931  CA  ILE B 161     -16.280 -40.104  34.099  1.00 18.32           C  
ANISOU 3931  CA  ILE B 161     3189   2990    780    803   -221    -89       C  
ATOM   3932  C   ILE B 161     -16.240 -39.652  35.564  1.00 18.58           C  
ANISOU 3932  C   ILE B 161     3129   3169    759    689   -227    -61       C  
ATOM   3933  O   ILE B 161     -15.404 -38.832  35.937  1.00 18.21           O  
ANISOU 3933  O   ILE B 161     3169   3085    663    580    -19     11       O  
ATOM   3934  CB  ILE B 161     -17.365 -39.332  33.306  1.00 17.76           C  
ANISOU 3934  CB  ILE B 161     3100   2901    747    651   -324   -131       C  
ATOM   3935  CG1 ILE B 161     -17.297 -39.689  31.810  1.00 18.53           C  
ANISOU 3935  CG1 ILE B 161     3068   3280    691    573   -319    -73       C  
ATOM   3936  CG2 ILE B 161     -17.178 -37.824  33.474  1.00 17.51           C  
ANISOU 3936  CG2 ILE B 161     3062   2871    719    721   -232   -240       C  
ATOM   3937  CD1 ILE B 161     -18.616 -39.511  31.070  1.00 18.32           C  
ANISOU 3937  CD1 ILE B 161     2954   3067    937    612   -289      3       C  
ATOM   3938  N   GLY B 162     -17.125 -40.218  36.383  1.00 18.77           N  
ANISOU 3938  N   GLY B 162     3312   3164    656    721   -215      6       N  
ATOM   3939  CA  GLY B 162     -17.171 -39.891  37.809  1.00 18.27           C  
ANISOU 3939  CA  GLY B 162     3215   3033    693    742   -108    -51       C  
ATOM   3940  C   GLY B 162     -15.865 -40.269  38.486  1.00 19.12           C  
ANISOU 3940  C   GLY B 162     3223   3114    929    703   -145    -63       C  
ATOM   3941  O   GLY B 162     -15.410 -39.577  39.408  1.00 18.84           O  
ANISOU 3941  O   GLY B 162     2975   3341    841    637   -147      0       O  
ATOM   3942  N   ASN B 163     -15.258 -41.361  38.016  1.00 18.78           N  
ANISOU 3942  N   ASN B 163     3145   3075    913    708   -134     59       N  
ATOM   3943  CA  ASN B 163     -13.985 -41.840  38.556  1.00 19.36           C  
ANISOU 3943  CA  ASN B 163     3062   3257   1034    676   -150    -78       C  
ATOM   3944  C   ASN B 163     -12.879 -40.836  38.275  1.00 19.03           C  
ANISOU 3944  C   ASN B 163     3259   3158    812    676      0     24       C  
ATOM   3945  O   ASN B 163     -12.091 -40.501  39.159  1.00 18.66           O  
ANISOU 3945  O   ASN B 163     3099   3154    836    732    112    -63       O  
ATOM   3946  CB  ASN B 163     -13.618 -43.207  37.968  1.00 20.25           C  
ANISOU 3946  CB  ASN B 163     3444   3111   1138    678   -365     24       C  
ATOM   3947  CG  ASN B 163     -14.430 -44.350  38.569  1.00 21.55           C  
ANISOU 3947  CG  ASN B 163     3649   3538   1001    549   -473    185       C  
ATOM   3948  OD1 ASN B 163     -14.995 -44.221  39.655  1.00 22.21           O  
ANISOU 3948  OD1 ASN B 163     3628   3700   1107    888   -437    365       O  
ATOM   3949  ND2 ASN B 163     -14.483 -45.486  37.858  1.00 22.06           N  
ANISOU 3949  ND2 ASN B 163     3397   3438   1544    797   -629      4       N  
ATOM   3950  N   VAL B 164     -12.851 -40.340  37.043  1.00 18.47           N  
ANISOU 3950  N   VAL B 164     3028   3129    860    730    -15     76       N  
ATOM   3951  CA  VAL B 164     -11.905 -39.302  36.664  1.00 18.70           C  
ANISOU 3951  CA  VAL B 164     3196   3166    741    686    107    111       C  
ATOM   3952  C   VAL B 164     -12.109 -38.037  37.507  1.00 18.25           C  
ANISOU 3952  C   VAL B 164     2945   3226    762    681     45     98       C  
ATOM   3953  O   VAL B 164     -11.152 -37.475  38.041  1.00 18.67           O  
ANISOU 3953  O   VAL B 164     3136   3131    826    593    190   -200       O  
ATOM   3954  CB  VAL B 164     -12.026 -38.955  35.167  1.00 18.96           C  
ANISOU 3954  CB  VAL B 164     3182   3292    728    527     96     89       C  
ATOM   3955  CG1 VAL B 164     -11.170 -37.741  34.837  1.00 20.32           C  
ANISOU 3955  CG1 VAL B 164     3276   3393   1051    491    238     83       C  
ATOM   3956  CG2 VAL B 164     -11.605 -40.146  34.322  1.00 18.16           C  
ANISOU 3956  CG2 VAL B 164     3212   3411    275    466    204    101       C  
ATOM   3957  N   ALA B 165     -13.354 -37.595  37.640  1.00 18.67           N  
ANISOU 3957  N   ALA B 165     2964   3219    908    738     -3     46       N  
ATOM   3958  CA  ALA B 165     -13.646 -36.397  38.443  1.00 17.39           C  
ANISOU 3958  CA  ALA B 165     2599   3136    870    744    -56     93       C  
ATOM   3959  C   ALA B 165     -13.244 -36.598  39.906  1.00 18.62           C  
ANISOU 3959  C   ALA B 165     3000   3244    828    675    -53     16       C  
ATOM   3960  O   ALA B 165     -12.722 -35.676  40.537  1.00 19.23           O  
ANISOU 3960  O   ALA B 165     2919   3487    898    611   -294     60       O  
ATOM   3961  CB  ALA B 165     -15.112 -36.024  38.330  1.00 17.16           C  
ANISOU 3961  CB  ALA B 165     2497   3125    897    566     29    133       C  
ATOM   3962  N   PHE B 166     -13.478 -37.793  40.433  1.00 18.44           N  
ANISOU 3962  N   PHE B 166     2925   3212    869    769   -119    182       N  
ATOM   3963  CA  PHE B 166     -13.086 -38.132  41.803  1.00 19.18           C  
ANISOU 3963  CA  PHE B 166     3238   3271    779    754   -204    -57       C  
ATOM   3964  C   PHE B 166     -11.573 -38.075  41.970  1.00 20.10           C  
ANISOU 3964  C   PHE B 166     3254   3492    892    683    -71     12       C  
ATOM   3965  O   PHE B 166     -11.075 -37.603  42.993  1.00 20.61           O  
ANISOU 3965  O   PHE B 166     3380   3517    934    596    -19      4       O  
ATOM   3966  CB  PHE B 166     -13.597 -39.529  42.160  1.00 19.89           C  
ANISOU 3966  CB  PHE B 166     3336   3382    837    734    -17    195       C  
ATOM   3967  CG  PHE B 166     -13.176 -40.016  43.521  1.00 19.48           C  
ANISOU 3967  CG  PHE B 166     3309   3376    715    785    -36    -43       C  
ATOM   3968  CD1 PHE B 166     -13.951 -39.731  44.633  1.00 20.46           C  
ANISOU 3968  CD1 PHE B 166     3628   3452    693    738     65    -63       C  
ATOM   3969  CD2 PHE B 166     -12.026 -40.790  43.693  1.00 19.69           C  
ANISOU 3969  CD2 PHE B 166     3353   3245    882    692   -293    229       C  
ATOM   3970  CE1 PHE B 166     -13.582 -40.188  45.889  1.00 22.51           C  
ANISOU 3970  CE1 PHE B 166     3945   3670    936   1037    203    356       C  
ATOM   3971  CE2 PHE B 166     -11.650 -41.249  44.948  1.00 20.65           C  
ANISOU 3971  CE2 PHE B 166     3569   3509    767   1010   -182    124       C  
ATOM   3972  CZ  PHE B 166     -12.432 -40.948  46.050  1.00 21.26           C  
ANISOU 3972  CZ  PHE B 166     3870   3644    564    902     22    528       C  
ATOM   3973  N   GLU B 167     -10.839 -38.553  40.962  1.00 19.76           N  
ANISOU 3973  N   GLU B 167     3098   3487    921    737    -64    102       N  
ATOM   3974  CA  GLU B 167      -9.365 -38.619  41.022  1.00 19.96           C  
ANISOU 3974  CA  GLU B 167     3104   3410   1070    602   -123      1       C  
ATOM   3975  C   GLU B 167      -8.707 -37.237  41.018  1.00 20.92           C  
ANISOU 3975  C   GLU B 167     3394   3362   1190    618   -247      4       C  
ATOM   3976  O   GLU B 167      -7.619 -37.052  41.564  1.00 22.02           O  
ANISOU 3976  O   GLU B 167     3116   3722   1527    795   -144    -20       O  
ATOM   3977  CB  GLU B 167      -8.817 -39.547  39.927  1.00 22.04           C  
ANISOU 3977  CB  GLU B 167     3624   3189   1559    614      4   -190       C  
ATOM   3978  CG  GLU B 167      -9.128 -41.018  40.196  1.00 23.13           C  
ANISOU 3978  CG  GLU B 167     4212   3175   1402    643   -176    -96       C  
ATOM   3979  CD  GLU B 167      -9.076 -41.905  38.957  1.00 23.94           C  
ANISOU 3979  CD  GLU B 167     4310   3595   1191    388   -187   -143       C  
ATOM   3980  OE1 GLU B 167      -8.594 -41.464  37.892  1.00 28.93           O  
ANISOU 3980  OE1 GLU B 167     4625   4186   2182    144    542    270       O  
ATOM   3981  OE2 GLU B 167      -9.531 -43.061  39.048  1.00 25.24           O  
ANISOU 3981  OE2 GLU B 167     4312   3531   1745    399     27    110       O  
ATOM   3982  N   HIS B 168      -9.422 -36.254  40.479  1.00 19.75           N  
ANISOU 3982  N   HIS B 168     3269   3297    935    658   -126    -96       N  
ATOM   3983  CA  HIS B 168      -8.996 -34.858  40.525  1.00 20.26           C  
ANISOU 3983  CA  HIS B 168     3357   3304   1035    635    -97    -15       C  
ATOM   3984  C   HIS B 168      -9.710 -33.942  41.504  1.00 21.32           C  
ANISOU 3984  C   HIS B 168     3478   3532   1090    590     38    -84       C  
ATOM   3985  O   HIS B 168      -9.442 -32.745  41.523  1.00 21.93           O  
ANISOU 3985  O   HIS B 168     3458   3544   1330    523     18   -102       O  
ATOM   3986  CB  HIS B 168      -9.121 -34.255  39.139  1.00 20.39           C  
ANISOU 3986  CB  HIS B 168     3338   3320   1089    549    -78     62       C  
ATOM   3987  CG  HIS B 168      -8.245 -34.906  38.123  1.00 21.98           C  
ANISOU 3987  CG  HIS B 168     3645   3633   1072    472    144     53       C  
ATOM   3988  ND1 HIS B 168      -7.087 -34.366  37.730  1.00 25.66           N  
ANISOU 3988  ND1 HIS B 168     3627   4162   1959    256    115   -311       N  
ATOM   3989  CD2 HIS B 168      -8.382 -36.102  37.429  1.00 22.49           C  
ANISOU 3989  CD2 HIS B 168     3609   3672   1263    360   -114      0       C  
ATOM   3990  CE1 HIS B 168      -6.514 -35.160  36.811  1.00 24.37           C  
ANISOU 3990  CE1 HIS B 168     3562   4153   1541     77     28   -281       C  
ATOM   3991  NE2 HIS B 168      -7.305 -36.227  36.634  1.00 23.35           N  
ANISOU 3991  NE2 HIS B 168     3554   3926   1392    193   -145   -201       N  
ATOM   3992  N   ASP B 169     -10.632 -34.446  42.321  1.00 20.13           N  
ANISOU 3992  N   ASP B 169     3083   3412   1152    638   -200    124       N  
ATOM   3993  CA  ASP B 169     -11.417 -33.575  43.231  1.00 20.93           C  
ANISOU 3993  CA  ASP B 169     3406   3571    974    623   -142     62       C  
ATOM   3994  C   ASP B 169     -12.093 -32.396  42.541  1.00 19.57           C  
ANISOU 3994  C   ASP B 169     3186   3556    692    551   -112     74       C  
ATOM   3995  O   ASP B 169     -12.090 -31.257  43.000  1.00 20.93           O  
ANISOU 3995  O   ASP B 169     3370   3432   1151    347   -259     93       O  
ATOM   3996  CB  ASP B 169     -10.612 -33.108  44.429  1.00 22.21           C  
ANISOU 3996  CB  ASP B 169     3475   3820   1143    549   -312     93       C  
ATOM   3997  CG  ASP B 169     -11.498 -32.687  45.590  1.00 23.49           C  
ANISOU 3997  CG  ASP B 169     3625   4122   1175    266   -100    147       C  
ATOM   3998  OD1 ASP B 169     -12.689 -33.079  45.624  1.00 25.06           O  
ANISOU 3998  OD1 ASP B 169     3400   4467   1654    534   -172    122       O  
ATOM   3999  OD2 ASP B 169     -11.001 -31.966  46.465  1.00 24.43           O  
ANISOU 3999  OD2 ASP B 169     3795   4153   1334    571      9   -275       O  
ATOM   4000  N   ILE B 170     -12.664 -32.728  41.394  1.00 18.19           N  
ANISOU 4000  N   ILE B 170     2873   3186    852    514   -163     43       N  
ATOM   4001  CA  ILE B 170     -13.528 -31.852  40.593  1.00 17.96           C  
ANISOU 4001  CA  ILE B 170     2548   3337    938    383   -225     28       C  
ATOM   4002  C   ILE B 170     -14.999 -32.295  40.677  1.00 16.94           C  
ANISOU 4002  C   ILE B 170     2596   3126    715    377    -53     79       C  
ATOM   4003  O   ILE B 170     -15.316 -33.469  40.410  1.00 17.39           O  
ANISOU 4003  O   ILE B 170     2631   3246    729    348   -222    -88       O  
ATOM   4004  CB  ILE B 170     -13.108 -31.841  39.095  1.00 18.47           C  
ANISOU 4004  CB  ILE B 170     2724   3339    952    338   -163    187       C  
ATOM   4005  CG1 ILE B 170     -11.698 -31.264  38.941  1.00 19.46           C  
ANISOU 4005  CG1 ILE B 170     2836   3293   1266    287     81     43       C  
ATOM   4006  CG2 ILE B 170     -14.104 -31.051  38.229  1.00 18.15           C  
ANISOU 4006  CG2 ILE B 170     2672   3161   1063    408   -140     63       C  
ATOM   4007  CD1 ILE B 170     -11.042 -31.620  37.618  1.00 19.78           C  
ANISOU 4007  CD1 ILE B 170     2972   3395   1148    573    -28     77       C  
ATOM   4008  N   PRO B 171     -15.904 -31.351  41.021  1.00 16.75           N  
ANISOU 4008  N   PRO B 171     2578   3079    705    330   -143     32       N  
ATOM   4009  CA  PRO B 171     -17.328 -31.670  41.045  1.00 16.99           C  
ANISOU 4009  CA  PRO B 171     2560   3042    852    355   -225    -78       C  
ATOM   4010  C   PRO B 171     -17.829 -32.266  39.719  1.00 16.45           C  
ANISOU 4010  C   PRO B 171     2599   2910    741    304    -11   -106       C  
ATOM   4011  O   PRO B 171     -17.475 -31.801  38.612  1.00 16.72           O  
ANISOU 4011  O   PRO B 171     2732   2915    704    384   -237     74       O  
ATOM   4012  CB  PRO B 171     -17.985 -30.314  41.347  1.00 17.09           C  
ANISOU 4012  CB  PRO B 171     2656   3068    768    381   -122   -191       C  
ATOM   4013  CG  PRO B 171     -16.953 -29.599  42.150  1.00 18.36           C  
ANISOU 4013  CG  PRO B 171     2569   3384   1020    203    -76   -150       C  
ATOM   4014  CD  PRO B 171     -15.652 -29.972  41.489  1.00 17.70           C  
ANISOU 4014  CD  PRO B 171     2745   3110    867    383    -40    -39       C  
ATOM   4015  N   PHE B 172     -18.620 -33.325  39.855  1.00 16.18           N  
ANISOU 4015  N   PHE B 172     2632   2841    672    307      5   -183       N  
ATOM   4016  CA  PHE B 172     -19.210 -34.014  38.718  1.00 16.05           C  
ANISOU 4016  CA  PHE B 172     2530   2925    641    408   -286     32       C  
ATOM   4017  C   PHE B 172     -20.726 -33.922  38.758  1.00 15.87           C  
ANISOU 4017  C   PHE B 172     2577   2724    728    328   -131    165       C  
ATOM   4018  O   PHE B 172     -21.373 -34.441  39.673  1.00 14.72           O  
ANISOU 4018  O   PHE B 172     2467   2676    449    363   -240    107       O  
ATOM   4019  CB  PHE B 172     -18.783 -35.482  38.718  1.00 16.61           C  
ANISOU 4019  CB  PHE B 172     2841   2863    606    324    -64     18       C  
ATOM   4020  CG  PHE B 172     -19.443 -36.318  37.647  1.00 16.61           C  
ANISOU 4020  CG  PHE B 172     2712   2904    695    418   -123     13       C  
ATOM   4021  CD1 PHE B 172     -19.627 -35.816  36.366  1.00 16.79           C  
ANISOU 4021  CD1 PHE B 172     2721   2922    736    406   -138     79       C  
ATOM   4022  CD2 PHE B 172     -19.848 -37.625  37.912  1.00 16.70           C  
ANISOU 4022  CD2 PHE B 172     2811   2888    646    486      0     69       C  
ATOM   4023  CE1 PHE B 172     -20.220 -36.591  35.380  1.00 19.12           C  
ANISOU 4023  CE1 PHE B 172     3210   2784   1270    246   -244    -95       C  
ATOM   4024  CE2 PHE B 172     -20.440 -38.407  36.932  1.00 18.20           C  
ANISOU 4024  CE2 PHE B 172     3002   3072    838    458    -79    -59       C  
ATOM   4025  CZ  PHE B 172     -20.635 -37.884  35.664  1.00 18.05           C  
ANISOU 4025  CZ  PHE B 172     3174   2803    878    382   -112    -60       C  
ATOM   4026  N   HIS B 173     -21.277 -33.268  37.741  1.00 14.87           N  
ANISOU 4026  N   HIS B 173     2465   2603    582    342   -198    -43       N  
ATOM   4027  CA  HIS B 173     -22.715 -33.180  37.560  1.00 14.69           C  
ANISOU 4027  CA  HIS B 173     2457   2328    794    280   -125    -51       C  
ATOM   4028  C   HIS B 173     -23.137 -33.988  36.363  1.00 14.59           C  
ANISOU 4028  C   HIS B 173     2469   2443    630    322   -201     47       C  
ATOM   4029  O   HIS B 173     -22.425 -34.053  35.369  1.00 16.20           O  
ANISOU 4029  O   HIS B 173     2654   2697    802    342    -41    -53       O  
ATOM   4030  CB  HIS B 173     -23.119 -31.726  37.390  1.00 14.57           C  
ANISOU 4030  CB  HIS B 173     2497   2408    632    358   -143     27       C  
ATOM   4031  CG  HIS B 173     -24.523 -31.538  36.884  1.00 15.24           C  
ANISOU 4031  CG  HIS B 173     2475   2574    738    270   -117     -9       C  
ATOM   4032  ND1 HIS B 173     -24.792 -31.293  35.591  1.00 15.08           N  
ANISOU 4032  ND1 HIS B 173     2471   2472    784    422   -132     45       N  
ATOM   4033  CD2 HIS B 173     -25.742 -31.582  37.541  1.00 14.98           C  
ANISOU 4033  CD2 HIS B 173     2489   2414    786    316   -109    -27       C  
ATOM   4034  CE1 HIS B 173     -26.117 -31.185  35.424  1.00 14.41           C  
ANISOU 4034  CE1 HIS B 173     2393   2379    700    258     32     35       C  
ATOM   4035  NE2 HIS B 173     -26.702 -31.369  36.621  1.00 14.13           N  
ANISOU 4035  NE2 HIS B 173     2578   2227    562    241    -62     45       N  
ATOM   4036  N   THR B 174     -24.305 -34.612  36.441  1.00 14.62           N  
ANISOU 4036  N   THR B 174     2535   2232    785    300   -218    -68       N  
ATOM   4037  CA  THR B 174     -24.870 -35.287  35.270  1.00 13.92           C  
ANISOU 4037  CA  THR B 174     2494   2268    523    350   -103     27       C  
ATOM   4038  C   THR B 174     -26.332 -34.900  35.023  1.00 14.66           C  
ANISOU 4038  C   THR B 174     2465   2380    722    248    -51    172       C  
ATOM   4039  O   THR B 174     -27.163 -34.929  35.941  1.00 14.64           O  
ANISOU 4039  O   THR B 174     2716   2342    504    360    -33     70       O  
ATOM   4040  CB  THR B 174     -24.653 -36.825  35.310  1.00 15.37           C  
ANISOU 4040  CB  THR B 174     2830   2240    766    210    -54   -105       C  
ATOM   4041  OG1 THR B 174     -25.172 -37.412  34.112  1.00 16.27           O  
ANISOU 4041  OG1 THR B 174     2812   2602    767    285   -155    -74       O  
ATOM   4042  CG2 THR B 174     -25.325 -37.484  36.496  1.00 15.15           C  
ANISOU 4042  CG2 THR B 174     2792   2235    727    359    -97     20       C  
ATOM   4043  N   ASP B 175     -26.626 -34.506  33.784  1.00 13.93           N  
ANISOU 4043  N   ASP B 175     2477   2199    616    311     13     32       N  
ATOM   4044  CA  ASP B 175     -27.998 -34.309  33.348  1.00 13.31           C  
ANISOU 4044  CA  ASP B 175     2420   2103    531    236    103    143       C  
ATOM   4045  C   ASP B 175     -28.621 -35.687  33.099  1.00 13.96           C  
ANISOU 4045  C   ASP B 175     2495   2194    612    237      0     58       C  
ATOM   4046  O   ASP B 175     -28.357 -36.331  32.077  1.00 15.04           O  
ANISOU 4046  O   ASP B 175     2640   2386    686    306     75    -13       O  
ATOM   4047  CB  ASP B 175     -28.025 -33.435  32.088  1.00 14.28           C  
ANISOU 4047  CB  ASP B 175     2560   2295    570    212     28    241       C  
ATOM   4048  CG  ASP B 175     -29.433 -33.097  31.634  1.00 14.53           C  
ANISOU 4048  CG  ASP B 175     2544   2213    764    264    123    132       C  
ATOM   4049  OD1 ASP B 175     -29.581 -32.210  30.771  1.00 14.96           O  
ANISOU 4049  OD1 ASP B 175     2582   2367    731    297    -72    170       O  
ATOM   4050  OD2 ASP B 175     -30.393 -33.723  32.130  1.00 14.96           O  
ANISOU 4050  OD2 ASP B 175     2572   2458    653    152     -5    150       O  
ATOM   4051  N   ALA B 176     -29.449 -36.129  34.050  1.00 14.00           N  
ANISOU 4051  N   ALA B 176     2569   2109    638    211     20     71       N  
ATOM   4052  CA  ALA B 176     -30.096 -37.440  34.010  1.00 14.10           C  
ANISOU 4052  CA  ALA B 176     2609   2109    639    234     15    187       C  
ATOM   4053  C   ALA B 176     -31.591 -37.355  33.631  1.00 13.97           C  
ANISOU 4053  C   ALA B 176     2603   2137    568    299     68     49       C  
ATOM   4054  O   ALA B 176     -32.378 -38.236  33.969  1.00 14.84           O  
ANISOU 4054  O   ALA B 176     2816   2140    683    216     69    168       O  
ATOM   4055  CB  ALA B 176     -29.914 -38.141  35.360  1.00 14.17           C  
ANISOU 4055  CB  ALA B 176     2748   2018    617    267    -35    121       C  
ATOM   4056  N   ALA B 177     -31.991 -36.296  32.927  1.00 13.37           N  
ANISOU 4056  N   ALA B 177     2567   2159    352    292     40     37       N  
ATOM   4057  CA  ALA B 177     -33.405 -36.147  32.581  1.00 14.85           C  
ANISOU 4057  CA  ALA B 177     2574   2175    892    296    -18     37       C  
ATOM   4058  C   ALA B 177     -33.935 -37.344  31.797  1.00 15.19           C  
ANISOU 4058  C   ALA B 177     2706   2322    740    250    -52     -7       C  
ATOM   4059  O   ALA B 177     -35.094 -37.715  31.961  1.00 15.59           O  
ANISOU 4059  O   ALA B 177     2773   2609    541     61     -7   -230       O  
ATOM   4060  CB  ALA B 177     -33.650 -34.862  31.816  1.00 14.49           C  
ANISOU 4060  CB  ALA B 177     2508   2170    826    214     -8     73       C  
ATOM   4061  N   GLN B 178     -33.090 -37.956  30.968  1.00 14.69           N  
ANISOU 4061  N   GLN B 178     2789   2202    589    321    -88    135       N  
ATOM   4062  CA  GLN B 178     -33.518 -39.100  30.148  1.00 15.65           C  
ANISOU 4062  CA  GLN B 178     2998   2297    649    242     40     13       C  
ATOM   4063  C   GLN B 178     -33.226 -40.462  30.773  1.00 16.35           C  
ANISOU 4063  C   GLN B 178     3100   2300    810    294    -94    -57       C  
ATOM   4064  O   GLN B 178     -33.690 -41.484  30.271  1.00 18.00           O  
ANISOU 4064  O   GLN B 178     3481   2417    940     14     48    -94       O  
ATOM   4065  CB  GLN B 178     -32.886 -39.063  28.751  1.00 15.99           C  
ANISOU 4065  CB  GLN B 178     3016   2468    591    356    -27     -9       C  
ATOM   4066  CG  GLN B 178     -33.283 -37.877  27.888  1.00 15.54           C  
ANISOU 4066  CG  GLN B 178     2889   2460    555    331    -45    -28       C  
ATOM   4067  CD  GLN B 178     -34.672 -37.999  27.270  1.00 16.35           C  
ANISOU 4067  CD  GLN B 178     2937   2703    573    279    -22   -239       C  
ATOM   4068  OE1 GLN B 178     -35.113 -39.086  26.882  1.00 16.37           O  
ANISOU 4068  OE1 GLN B 178     3157   2521    543    238   -137     62       O  
ATOM   4069  NE2 GLN B 178     -35.364 -36.869  27.158  1.00 17.51           N  
ANISOU 4069  NE2 GLN B 178     2938   2719    995    285    -22   -167       N  
ATOM   4070  N   SER B 179     -32.459 -40.482  31.862  1.00 15.41           N  
ANISOU 4070  N   SER B 179     3055   2191    606    177     55     -3       N  
ATOM   4071  CA  SER B 179     -32.047 -41.746  32.475  1.00 15.36           C  
ANISOU 4071  CA  SER B 179     2924   2182    729    265    178    -58       C  
ATOM   4072  C   SER B 179     -32.753 -42.042  33.788  1.00 15.95           C  
ANISOU 4072  C   SER B 179     3106   2271    680    193    198    -94       C  
ATOM   4073  O   SER B 179     -32.915 -43.207  34.161  1.00 15.59           O  
ANISOU 4073  O   SER B 179     3140   2189    594    279    249   -312       O  
ATOM   4074  CB  SER B 179     -30.543 -41.757  32.719  1.00 15.50           C  
ANISOU 4074  CB  SER B 179     2914   2299    674    195    126   -141       C  
ATOM   4075  OG  SER B 179     -30.178 -40.723  33.619  1.00 15.56           O  
ANISOU 4075  OG  SER B 179     3035   2314    563    232     95   -100       O  
ATOM   4076  N   PHE B 180     -33.142 -40.989  34.500  1.00 15.09           N  
ANISOU 4076  N   PHE B 180     2928   2219    584    258    196     30       N  
ATOM   4077  CA  PHE B 180     -33.828 -41.139  35.783  1.00 15.28           C  
ANISOU 4077  CA  PHE B 180     2901   2208    696    251    322    -56       C  
ATOM   4078  C   PHE B 180     -35.014 -42.091  35.638  1.00 15.28           C  
ANISOU 4078  C   PHE B 180     3087   2057    661    193    226   -148       C  
ATOM   4079  O   PHE B 180     -35.828 -41.934  34.721  1.00 15.84           O  
ANISOU 4079  O   PHE B 180     3005   2216    796    112    149   -256       O  
ATOM   4080  CB  PHE B 180     -34.263 -39.765  36.307  1.00 15.11           C  
ANISOU 4080  CB  PHE B 180     2920   2143    675    175    231    -84       C  
ATOM   4081  CG  PHE B 180     -34.944 -39.808  37.645  1.00 15.40           C  
ANISOU 4081  CG  PHE B 180     2877   2290    684     84    227   -127       C  
ATOM   4082  CD1 PHE B 180     -36.230 -39.303  37.794  1.00 15.64           C  
ANISOU 4082  CD1 PHE B 180     2938   2224    777    168    313    -50       C  
ATOM   4083  CD2 PHE B 180     -34.297 -40.341  38.761  1.00 16.40           C  
ANISOU 4083  CD2 PHE B 180     3145   2375    710    204    205   -115       C  
ATOM   4084  CE1 PHE B 180     -36.869 -39.318  39.036  1.00 16.10           C  
ANISOU 4084  CE1 PHE B 180     3070   2335    712    -65    264    -93       C  
ATOM   4085  CE2 PHE B 180     -34.926 -40.363  39.999  1.00 16.16           C  
ANISOU 4085  CE2 PHE B 180     2975   2402    762     62    212     11       C  
ATOM   4086  CZ  PHE B 180     -36.216 -39.855  40.137  1.00 15.95           C  
ANISOU 4086  CZ  PHE B 180     2926   2461    671    -35    348    -78       C  
ATOM   4087  N   CYS B 181     -35.072 -43.087  36.531  1.00 15.82           N  
ANISOU 4087  N   CYS B 181     3152   2266    590     27    150    -75       N  
ATOM   4088  CA  CYS B 181     -36.093 -44.158  36.566  1.00 15.34           C  
ANISOU 4088  CA  CYS B 181     3190   2113    524     74    288   -141       C  
ATOM   4089  C   CYS B 181     -35.906 -45.266  35.524  1.00 16.44           C  
ANISOU 4089  C   CYS B 181     3436   2140    669    162    156   -196       C  
ATOM   4090  O   CYS B 181     -36.232 -46.431  35.788  1.00 17.33           O  
ANISOU 4090  O   CYS B 181     3548   2211    823      2    209   -275       O  
ATOM   4091  CB  CYS B 181     -37.523 -43.606  36.513  1.00 16.07           C  
ANISOU 4091  CB  CYS B 181     3196   2240    670     30    199   -265       C  
ATOM   4092  SG  CYS B 181     -38.006 -42.691  37.990  1.00 17.09           S  
ANISOU 4092  SG  CYS B 181     3476   2285    731     25    319   -288       S  
ATOM   4093  N   LYS B 182     -35.395 -44.907  34.347  1.00 16.91           N  
ANISOU 4093  N   LYS B 182     3361   2329    732    182    283   -224       N  
ATOM   4094  CA  LYS B 182     -35.111 -45.885  33.285  1.00 16.36           C  
ANISOU 4094  CA  LYS B 182     3440   2091    684    148    250    -98       C  
ATOM   4095  C   LYS B 182     -33.938 -46.801  33.634  1.00 17.14           C  
ANISOU 4095  C   LYS B 182     3441   2368    701    243    146   -322       C  
ATOM   4096  O   LYS B 182     -33.974 -47.994  33.358  1.00 18.52           O  
ANISOU 4096  O   LYS B 182     3567   2400   1067     85     54   -297       O  
ATOM   4097  CB  LYS B 182     -34.838 -45.180  31.940  1.00 17.16           C  
ANISOU 4097  CB  LYS B 182     3548   2242    730    144    255    -13       C  
ATOM   4098  CG  LYS B 182     -36.054 -44.485  31.335  1.00 20.06           C  
ANISOU 4098  CG  LYS B 182     3436   2579   1606    242    126    -84       C  
ATOM   4099  CD  LYS B 182     -36.141 -44.660  29.811  1.00 24.29           C  
ANISOU 4099  CD  LYS B 182     4392   3179   1657    172    290   -172       C  
ATOM   4100  CE  LYS B 182     -35.655 -43.493  28.965  1.00 22.53           C  
ANISOU 4100  CE  LYS B 182     4004   3139   1417    230    753   -444       C  
ATOM   4101  NZ  LYS B 182     -36.382 -42.211  29.209  1.00 22.17           N  
ANISOU 4101  NZ  LYS B 182     3576   2947   1900    326    -26    132       N  
ATOM   4102  N   LEU B 183     -32.893 -46.223  34.225  1.00 18.31           N  
ANISOU 4102  N   LEU B 183     3418   2457   1080    208     35   -224       N  
ATOM   4103  CA  LEU B 183     -31.649 -46.924  34.571  1.00 17.37           C  
ANISOU 4103  CA  LEU B 183     3387   2425    788    231    103   -232       C  
ATOM   4104  C   LEU B 183     -31.394 -46.800  36.065  1.00 18.82           C  
ANISOU 4104  C   LEU B 183     3586   2717    844    256    -64   -321       C  
ATOM   4105  O   LEU B 183     -31.723 -45.772  36.641  1.00 18.72           O  
ANISOU 4105  O   LEU B 183     3585   2496   1032    279    -92   -222       O  
ATOM   4106  CB  LEU B 183     -30.460 -46.298  33.823  1.00 17.87           C  
ANISOU 4106  CB  LEU B 183     3388   2590    809    208    169   -360       C  
ATOM   4107  CG  LEU B 183     -30.465 -46.448  32.294  1.00 18.21           C  
ANISOU 4107  CG  LEU B 183     3521   2637    757     58    340   -115       C  
ATOM   4108  CD1 LEU B 183     -29.306 -45.722  31.670  1.00 18.12           C  
ANISOU 4108  CD1 LEU B 183     3244   2823    816    161    204    -55       C  
ATOM   4109  CD2 LEU B 183     -30.428 -47.914  31.912  1.00 17.36           C  
ANISOU 4109  CD2 LEU B 183     3323   2771    499     82    394   -295       C  
ATOM   4110  N   ASP B 184     -30.777 -47.797  36.684  1.00 20.52           N  
ANISOU 4110  N   ASP B 184     4003   2646   1147    205    -66   -107       N  
ATOM   4111  CA  ASP B 184     -30.368 -47.599  38.052  1.00 21.31           C  
ANISOU 4111  CA  ASP B 184     4147   2654   1293    267   -324   -255       C  
ATOM   4112  C   ASP B 184     -29.297 -46.550  38.195  1.00 21.11           C  
ANISOU 4112  C   ASP B 184     3767   2825   1428    341   -150   -396       C  
ATOM   4113  O   ASP B 184     -28.304 -46.620  37.517  1.00 23.29           O  
ANISOU 4113  O   ASP B 184     4002   3296   1550    569    -75   -659       O  
ATOM   4114  CB  ASP B 184     -29.830 -48.894  38.586  1.00 23.45           C  
ANISOU 4114  CB  ASP B 184     4439   2833   1635    520   -240   -180       C  
ATOM   4115  CG  ASP B 184     -30.895 -49.776  39.054  1.00 30.28           C  
ANISOU 4115  CG  ASP B 184     5022   3111   3370    337     42    157       C  
ATOM   4116  OD1 ASP B 184     -32.028 -49.316  39.333  1.00 33.06           O  
ANISOU 4116  OD1 ASP B 184     5120   3720   3720    402    -45   -111       O  
ATOM   4117  OD2 ASP B 184     -30.573 -50.937  39.129  1.00 36.13           O  
ANISOU 4117  OD2 ASP B 184     6032   3156   4538    511    135   -433       O  
ATOM   4118  N   ILE B 185     -29.504 -45.614  39.109  1.00 19.45           N  
ANISOU 4118  N   ILE B 185     3657   2890    842    348   -175   -196       N  
ATOM   4119  CA  ILE B 185     -28.483 -44.636  39.405  1.00 18.43           C  
ANISOU 4119  CA  ILE B 185     3502   2776    725    395   -115    -64       C  
ATOM   4120  C   ILE B 185     -28.279 -44.710  40.909  1.00 18.22           C  
ANISOU 4120  C   ILE B 185     3516   2653    754    585   -174    -42       C  
ATOM   4121  O   ILE B 185     -29.246 -44.557  41.696  1.00 18.83           O  
ANISOU 4121  O   ILE B 185     3653   2875    625    427    -66     20       O  
ATOM   4122  CB  ILE B 185     -28.926 -43.214  38.994  1.00 18.31           C  
ANISOU 4122  CB  ILE B 185     3532   2717    704    371    -91     14       C  
ATOM   4123  CG1 ILE B 185     -29.154 -43.132  37.472  1.00 18.47           C  
ANISOU 4123  CG1 ILE B 185     3422   2836    758    494   -274    -21       C  
ATOM   4124  CG2 ILE B 185     -27.881 -42.207  39.447  1.00 18.19           C  
ANISOU 4124  CG2 ILE B 185     3571   2841    498    345   -123    -73       C  
ATOM   4125  CD1 ILE B 185     -29.935 -41.939  36.967  1.00 17.97           C  
ANISOU 4125  CD1 ILE B 185     3172   2677    977    318    -46    188       C  
ATOM   4126  N   ASP B 186     -27.028 -44.962  41.303  1.00 19.11           N  
ANISOU 4126  N   ASP B 186     3490   3004    766    604   -171    -71       N  
ATOM   4127  CA  ASP B 186     -26.627 -44.821  42.690  1.00 19.90           C  
ANISOU 4127  CA  ASP B 186     3640   3048    873    507   -320    -98       C  
ATOM   4128  C   ASP B 186     -25.528 -43.782  42.765  1.00 19.82           C  
ANISOU 4128  C   ASP B 186     3535   2901   1092    656   -192    -54       C  
ATOM   4129  O   ASP B 186     -24.419 -43.928  42.223  1.00 19.82           O  
ANISOU 4129  O   ASP B 186     3585   3099    844    587    -95     78       O  
ATOM   4130  CB  ASP B 186     -26.186 -46.140  43.309  1.00 21.79           C  
ANISOU 4130  CB  ASP B 186     4100   3153   1024    557   -219    124       C  
ATOM   4131  CG  ASP B 186     -25.927 -46.012  44.794  1.00 23.22           C  
ANISOU 4131  CG  ASP B 186     4203   3512   1107    504   -507    319       C  
ATOM   4132  OD1 ASP B 186     -24.880 -45.461  45.174  1.00 24.63           O  
ANISOU 4132  OD1 ASP B 186     4282   3606   1469    409   -370    186       O  
ATOM   4133  OD2 ASP B 186     -26.779 -46.431  45.595  1.00 28.09           O  
ANISOU 4133  OD2 ASP B 186     4563   4379   1732    303   -138    339       O  
ATOM   4134  N   VAL B 187     -25.867 -42.724  43.466  1.00 19.24           N  
ANISOU 4134  N   VAL B 187     3484   2947    878    530   -438   -120       N  
ATOM   4135  CA  VAL B 187     -25.069 -41.544  43.529  1.00 19.89           C  
ANISOU 4135  CA  VAL B 187     3449   2962   1145    610     22    -68       C  
ATOM   4136  C   VAL B 187     -23.650 -41.805  44.110  1.00 19.52           C  
ANISOU 4136  C   VAL B 187     3652   2963    803    593    -70     57       C  
ATOM   4137  O   VAL B 187     -22.655 -41.222  43.664  1.00 19.00           O  
ANISOU 4137  O   VAL B 187     3557   2881    779    645      0    101       O  
ATOM   4138  CB  VAL B 187     -25.977 -40.517  44.243  1.00 21.55           C  
ANISOU 4138  CB  VAL B 187     3626   2909   1651    916   -277   -151       C  
ATOM   4139  CG1 VAL B 187     -25.503 -40.073  45.618  1.00 22.06           C  
ANISOU 4139  CG1 VAL B 187     3716   3162   1502    607    -41   -176       C  
ATOM   4140  CG2 VAL B 187     -26.467 -39.452  43.274  1.00 18.47           C  
ANISOU 4140  CG2 VAL B 187     3213   2807    995    559    325    -42       C  
ATOM   4141  N   ASP B 188     -23.546 -42.720  45.062  1.00 19.85           N  
ANISOU 4141  N   ASP B 188     3643   2798   1100    742    120    182       N  
ATOM   4142  CA  ASP B 188     -22.240 -43.038  45.634  1.00 20.50           C  
ANISOU 4142  CA  ASP B 188     3692   3209    887    553     29    403       C  
ATOM   4143  C   ASP B 188     -21.407 -43.952  44.738  1.00 20.60           C  
ANISOU 4143  C   ASP B 188     3742   3070   1013    750   -182    373       C  
ATOM   4144  O   ASP B 188     -20.199 -43.747  44.586  1.00 20.57           O  
ANISOU 4144  O   ASP B 188     3823   3150    840    775    -78    460       O  
ATOM   4145  CB  ASP B 188     -22.397 -43.654  47.019  1.00 21.12           C  
ANISOU 4145  CB  ASP B 188     4112   3079    831    784    129    307       C  
ATOM   4146  CG  ASP B 188     -22.945 -42.665  48.025  1.00 23.54           C  
ANISOU 4146  CG  ASP B 188     4588   3323   1030    771    277    154       C  
ATOM   4147  OD1 ASP B 188     -22.783 -41.448  47.813  1.00 27.27           O  
ANISOU 4147  OD1 ASP B 188     4987   3428   1946    378    263    -14       O  
ATOM   4148  OD2 ASP B 188     -23.569 -43.102  49.002  1.00 27.30           O  
ANISOU 4148  OD2 ASP B 188     4694   4161   1516    428    600    117       O  
ATOM   4149  N   ASP B 189     -22.053 -44.953  44.154  1.00 21.19           N  
ANISOU 4149  N   ASP B 189     3906   3179    964    629    -83    221       N  
ATOM   4150  CA  ASP B 189     -21.389 -45.885  43.259  1.00 21.80           C  
ANISOU 4150  CA  ASP B 189     3830   3461    992    739     48    265       C  
ATOM   4151  C   ASP B 189     -20.838 -45.142  42.051  1.00 20.86           C  
ANISOU 4151  C   ASP B 189     3663   3295    965    779      0    200       C  
ATOM   4152  O   ASP B 189     -19.784 -45.477  41.521  1.00 22.16           O  
ANISOU 4152  O   ASP B 189     3454   3415   1549    748    -24    257       O  
ATOM   4153  CB  ASP B 189     -22.374 -46.959  42.800  1.00 23.89           C  
ANISOU 4153  CB  ASP B 189     4150   3486   1440    698     49     45       C  
ATOM   4154  CG  ASP B 189     -22.741 -47.940  43.909  1.00 27.30           C  
ANISOU 4154  CG  ASP B 189     4682   3816   1874    291   -110    254       C  
ATOM   4155  OD1 ASP B 189     -22.158 -47.860  45.012  1.00 28.75           O  
ANISOU 4155  OD1 ASP B 189     4739   4267   1916    518   -204    413       O  
ATOM   4156  OD2 ASP B 189     -23.636 -48.777  43.675  1.00 30.33           O  
ANISOU 4156  OD2 ASP B 189     4485   4025   3015    403   -203   -177       O  
ATOM   4157  N   MET B 190     -21.562 -44.132  41.594  1.00 20.57           N  
ANISOU 4157  N   MET B 190     3540   3137   1137    756     31    119       N  
ATOM   4158  CA AMET B 190     -21.104 -43.355  40.453  0.50 20.21           C  
ANISOU 4158  CA AMET B 190     3509   3204    963    637   -103     35       C  
ATOM   4159  CA BMET B 190     -21.093 -43.366  40.438  0.50 20.19           C  
ANISOU 4159  CA BMET B 190     3497   3208    966    645   -143     63       C  
ATOM   4160  C   MET B 190     -20.265 -42.137  40.758  1.00 19.65           C  
ANISOU 4160  C   MET B 190     3363   3075   1026    732      3      8       C  
ATOM   4161  O   MET B 190     -19.901 -41.380  39.866  1.00 19.16           O  
ANISOU 4161  O   MET B 190     3298   3143    839    767     78   -105       O  
ATOM   4162  CB AMET B 190     -22.298 -42.981  39.589  0.50 20.04           C  
ANISOU 4162  CB AMET B 190     3333   3141   1138    643    -25    -32       C  
ATOM   4163  CB BMET B 190     -22.270 -42.940  39.579  0.50 20.29           C  
ANISOU 4163  CB BMET B 190     3374   3163   1171    700    -86     33       C  
ATOM   4164  CG AMET B 190     -22.993 -44.259  39.127  0.50 20.81           C  
ANISOU 4164  CG AMET B 190     3464   3328   1116    643    -44   -299       C  
ATOM   4165  CG BMET B 190     -23.156 -44.104  39.178  0.50 20.41           C  
ANISOU 4165  CG BMET B 190     3250   3413   1089    762   -232   -189       C  
ATOM   4166  SD AMET B 190     -24.619 -44.161  38.423  0.50 20.45           S  
ANISOU 4166  SD AMET B 190     3366   3564    839    529    171   -467       S  
ATOM   4167  SD BMET B 190     -22.452 -45.122  37.866  0.50 21.34           S  
ANISOU 4167  SD BMET B 190     3473   3569   1065   1160   -227    -60       S  
ATOM   4168  CE AMET B 190     -24.638 -45.512  37.250  0.50 22.82           C  
ANISOU 4168  CE AMET B 190     3984   3429   1255    477     31   -581       C  
ATOM   4169  CE BMET B 190     -20.690 -44.997  38.120  0.50 22.67           C  
ANISOU 4169  CE BMET B 190     3551   3570   1492    914   -378    125       C  
ATOM   4170  N   ASN B 191     -20.024 -41.895  42.026  1.00 19.70           N  
ANISOU 4170  N   ASN B 191     3422   3017   1044    841   -131     68       N  
ATOM   4171  CA  ASN B 191     -19.298 -40.716  42.435  1.00 19.64           C  
ANISOU 4171  CA  ASN B 191     3222   3080   1159    796    -41    132       C  
ATOM   4172  C   ASN B 191     -19.912 -39.424  41.913  1.00 18.86           C  
ANISOU 4172  C   ASN B 191     3104   2890   1171    670    -56     14       C  
ATOM   4173  O   ASN B 191     -19.198 -38.540  41.486  1.00 20.00           O  
ANISOU 4173  O   ASN B 191     3319   3196   1081    645    -22    181       O  
ATOM   4174  CB  ASN B 191     -17.839 -40.808  42.003  1.00 20.47           C  
ANISOU 4174  CB  ASN B 191     3244   3208   1323    771    -33     11       C  
ATOM   4175  CG  ASN B 191     -17.086 -41.896  42.740  1.00 21.24           C  
ANISOU 4175  CG  ASN B 191     3273   3357   1439    892     10     10       C  
ATOM   4176  OD1 ASN B 191     -17.307 -42.138  43.926  1.00 22.93           O  
ANISOU 4176  OD1 ASN B 191     3248   3858   1604    846    224    249       O  
ATOM   4177  ND2 ASN B 191     -16.164 -42.543  42.050  1.00 20.81           N  
ANISOU 4177  ND2 ASN B 191     3469   3379   1057    659     70   -281       N  
ATOM   4178  N   ILE B 192     -21.235 -39.339  41.929  1.00 17.85           N  
ANISOU 4178  N   ILE B 192     3053   2719   1010    736   -109    -30       N  
ATOM   4179  CA  ILE B 192     -21.947 -38.138  41.494  1.00 16.03           C  
ANISOU 4179  CA  ILE B 192     2882   2511    698    595     -4   -128       C  
ATOM   4180  C   ILE B 192     -22.049 -37.101  42.615  1.00 15.80           C  
ANISOU 4180  C   ILE B 192     2786   2453    763    593    -64   -123       C  
ATOM   4181  O   ILE B 192     -22.408 -37.427  43.746  1.00 17.18           O  
ANISOU 4181  O   ILE B 192     3016   2740    769    686    -98     13       O  
ATOM   4182  CB  ILE B 192     -23.370 -38.489  41.005  1.00 15.55           C  
ANISOU 4182  CB  ILE B 192     2822   2508    577    625     51    -44       C  
ATOM   4183  CG1 ILE B 192     -23.288 -39.411  39.785  1.00 16.54           C  
ANISOU 4183  CG1 ILE B 192     2870   2604    809    517     46   -228       C  
ATOM   4184  CG2 ILE B 192     -24.159 -37.222  40.688  1.00 16.28           C  
ANISOU 4184  CG2 ILE B 192     2744   2560    879    573    -49     48       C  
ATOM   4185  CD1 ILE B 192     -24.591 -39.977  39.282  1.00 16.67           C  
ANISOU 4185  CD1 ILE B 192     2861   2736    734    353    167   -135       C  
ATOM   4186  N   ASP B 193     -21.755 -35.851  42.270  1.00 15.51           N  
ANISOU 4186  N   ASP B 193     2718   2535    637    534   -128    -50       N  
ATOM   4187  CA  ASP B 193     -21.945 -34.721  43.185  1.00 14.80           C  
ANISOU 4187  CA  ASP B 193     2527   2543    554    499   -228    -55       C  
ATOM   4188  C   ASP B 193     -23.278 -34.017  42.974  1.00 15.23           C  
ANISOU 4188  C   ASP B 193     2563   2564    656    525   -103    -11       C  
ATOM   4189  O   ASP B 193     -23.939 -33.638  43.935  1.00 14.95           O  
ANISOU 4189  O   ASP B 193     2688   2587    402    468   -138     53       O  
ATOM   4190  CB  ASP B 193     -20.793 -33.740  43.037  1.00 15.37           C  
ANISOU 4190  CB  ASP B 193     2698   2666    474    432   -133    118       C  
ATOM   4191  CG  ASP B 193     -19.460 -34.381  43.348  1.00 17.05           C  
ANISOU 4191  CG  ASP B 193     2654   2987    838    398   -208    264       C  
ATOM   4192  OD1 ASP B 193     -18.628 -34.532  42.427  1.00 18.47           O  
ANISOU 4192  OD1 ASP B 193     3178   3210    630    380   -120     97       O  
ATOM   4193  OD2 ASP B 193     -19.257 -34.762  44.519  1.00 18.55           O  
ANISOU 4193  OD2 ASP B 193     3138   3095    814    446   -361    177       O  
ATOM   4194  N   MET B 194     -23.676 -33.838  41.719  1.00 14.81           N  
ANISOU 4194  N   MET B 194     2551   2500    575    385    -19    -22       N  
ATOM   4195  CA  MET B 194     -24.989 -33.269  41.417  1.00 14.71           C  
ANISOU 4195  CA  MET B 194     2623   2355    610    371   -146    -97       C  
ATOM   4196  C   MET B 194     -25.635 -33.976  40.237  1.00 14.90           C  
ANISOU 4196  C   MET B 194     2562   2484    615    300   -122    -80       C  
ATOM   4197  O   MET B 194     -24.947 -34.443  39.334  1.00 14.79           O  
ANISOU 4197  O   MET B 194     2713   2430    475    362   -185    -79       O  
ATOM   4198  CB  MET B 194     -24.903 -31.764  41.122  1.00 14.95           C  
ANISOU 4198  CB  MET B 194     2729   2407    541    267    -23    -95       C  
ATOM   4199  CG  MET B 194     -24.273 -30.924  42.236  1.00 16.39           C  
ANISOU 4199  CG  MET B 194     2943   2638    646    171   -193   -107       C  
ATOM   4200  SD  MET B 194     -24.219 -29.136  41.944  1.00 16.27           S  
ANISOU 4200  SD  MET B 194     3070   2693    419    293     -9   -260       S  
ATOM   4201  CE  MET B 194     -22.784 -28.992  40.866  1.00 17.22           C  
ANISOU 4201  CE  MET B 194     3013   2742    789    241     54    192       C  
ATOM   4202  N   LEU B 195     -26.965 -34.042  40.258  1.00 14.34           N  
ANISOU 4202  N   LEU B 195     2579   2307    561    274   -133     16       N  
ATOM   4203  CA  LEU B 195     -27.735 -34.738  39.223  1.00 14.46           C  
ANISOU 4203  CA  LEU B 195     2674   2111    706    256   -143    -52       C  
ATOM   4204  C   LEU B 195     -29.079 -34.053  38.946  1.00 14.38           C  
ANISOU 4204  C   LEU B 195     2646   2157    661    297     -6    -25       C  
ATOM   4205  O   LEU B 195     -29.848 -33.775  39.866  1.00 14.35           O  
ANISOU 4205  O   LEU B 195     2705   2260    484    340    -26    122       O  
ATOM   4206  CB  LEU B 195     -27.926 -36.215  39.605  1.00 14.24           C  
ANISOU 4206  CB  LEU B 195     2628   2137    644    273    -43     78       C  
ATOM   4207  CG  LEU B 195     -28.844 -37.089  38.743  1.00 14.21           C  
ANISOU 4207  CG  LEU B 195     2724   1958    715    328     -2     10       C  
ATOM   4208  CD1 LEU B 195     -28.364 -38.538  38.839  1.00 14.48           C  
ANISOU 4208  CD1 LEU B 195     2895   2021    585    445     39    105       C  
ATOM   4209  CD2 LEU B 195     -30.316 -36.960  39.137  1.00 14.23           C  
ANISOU 4209  CD2 LEU B 195     2730   2210    465    256     66     15       C  
ATOM   4210  N   SER B 196     -29.352 -33.771  37.675  1.00 14.51           N  
ANISOU 4210  N   SER B 196     2709   2158    646    247     84     59       N  
ATOM   4211  CA  SER B 196     -30.618 -33.162  37.282  1.00 14.20           C  
ANISOU 4211  CA  SER B 196     2610   2203    581    195    133     60       C  
ATOM   4212  C   SER B 196     -31.662 -34.169  36.805  1.00 14.05           C  
ANISOU 4212  C   SER B 196     2602   2145    589    225     94     40       C  
ATOM   4213  O   SER B 196     -31.330 -35.127  36.106  1.00 14.12           O  
ANISOU 4213  O   SER B 196     2679   2126    557    267     62     63       O  
ATOM   4214  CB  SER B 196     -30.389 -32.169  36.154  1.00 14.34           C  
ANISOU 4214  CB  SER B 196     2723   2179    547    152     68     47       C  
ATOM   4215  OG  SER B 196     -29.534 -31.112  36.538  1.00 14.27           O  
ANISOU 4215  OG  SER B 196     2587   2316    516    186     78    -85       O  
ATOM   4216  N   LEU B 197     -32.920 -33.945  37.177  1.00 13.13           N  
ANISOU 4216  N   LEU B 197     2582   2152    255    239     56    -21       N  
ATOM   4217  CA  LEU B 197     -34.026 -34.767  36.672  1.00 14.00           C  
ANISOU 4217  CA  LEU B 197     2471   2281    564    183    193     50       C  
ATOM   4218  C   LEU B 197     -35.268 -33.913  36.388  1.00 14.23           C  
ANISOU 4218  C   LEU B 197     2529   2233    641    174     75    -19       C  
ATOM   4219  O   LEU B 197     -35.403 -32.801  36.906  1.00 14.43           O  
ANISOU 4219  O   LEU B 197     2621   2225    635    247     -1    -27       O  
ATOM   4220  CB  LEU B 197     -34.334 -35.943  37.626  1.00 14.68           C  
ANISOU 4220  CB  LEU B 197     2713   2166    698    149    271    -27       C  
ATOM   4221  CG  LEU B 197     -34.807 -35.596  39.048  1.00 14.57           C  
ANISOU 4221  CG  LEU B 197     2535   2304    695    225    223    -60       C  
ATOM   4222  CD1 LEU B 197     -36.332 -35.538  39.146  1.00 14.60           C  
ANISOU 4222  CD1 LEU B 197     2563   2260    723    253    213    -23       C  
ATOM   4223  CD2 LEU B 197     -34.234 -36.615  40.035  1.00 14.54           C  
ANISOU 4223  CD2 LEU B 197     2872   2151    501    252    166   -262       C  
ATOM   4224  N   SER B 198     -36.159 -34.452  35.550  1.00 14.69           N  
ANISOU 4224  N   SER B 198     2390   2406    782    156     54     -4       N  
ATOM   4225  CA  SER B 198     -37.354 -33.756  35.073  1.00 14.83           C  
ANISOU 4225  CA  SER B 198     2522   2420    692    142    -58    143       C  
ATOM   4226  C   SER B 198     -38.612 -34.627  35.251  1.00 14.83           C  
ANISOU 4226  C   SER B 198     2520   2346    769    162   -110     97       C  
ATOM   4227  O   SER B 198     -38.656 -35.761  34.775  1.00 15.05           O  
ANISOU 4227  O   SER B 198     2648   2398    670    184    142     54       O  
ATOM   4228  CB  SER B 198     -37.173 -33.413  33.593  1.00 15.82           C  
ANISOU 4228  CB  SER B 198     2720   2604    686    217     72     84       C  
ATOM   4229  OG  SER B 198     -38.324 -32.788  33.068  1.00 16.76           O  
ANISOU 4229  OG  SER B 198     2954   2511    901    266     27    314       O  
ATOM   4230  N   GLY B 199     -39.621 -34.092  35.934  1.00 14.61           N  
ANISOU 4230  N   GLY B 199     2633   2424    493    101    -95      2       N  
ATOM   4231  CA  GLY B 199     -40.872 -34.813  36.182  1.00 15.18           C  
ANISOU 4231  CA  GLY B 199     2791   2470    504      9     42     16       C  
ATOM   4232  C   GLY B 199     -41.624 -35.270  34.943  1.00 15.42           C  
ANISOU 4232  C   GLY B 199     2757   2328    772     26   -103    -17       C  
ATOM   4233  O   GLY B 199     -42.107 -36.399  34.882  1.00 15.82           O  
ANISOU 4233  O   GLY B 199     2786   2368    856      4     23    -85       O  
ATOM   4234  N   HIS B 200     -41.698 -34.420  33.931  1.00 14.67           N  
ANISOU 4234  N   HIS B 200     2683   2342    547     55     -7   -104       N  
ATOM   4235  CA  HIS B 200     -42.553 -34.756  32.797  1.00 15.22           C  
ANISOU 4235  CA  HIS B 200     2776   2306    697    111   -107   -152       C  
ATOM   4236  C   HIS B 200     -41.894 -35.703  31.825  1.00 15.34           C  
ANISOU 4236  C   HIS B 200     2785   2424    619    167     -3    -45       C  
ATOM   4237  O   HIS B 200     -42.470 -36.018  30.789  1.00 15.49           O  
ANISOU 4237  O   HIS B 200     2830   2310    745    193    -98   -125       O  
ATOM   4238  CB  HIS B 200     -43.088 -33.508  32.108  1.00 15.46           C  
ANISOU 4238  CB  HIS B 200     2737   2373    761     48    -71     11       C  
ATOM   4239  CG  HIS B 200     -42.044 -32.750  31.338  1.00 15.76           C  
ANISOU 4239  CG  HIS B 200     2785   2495    708    105     32     81       C  
ATOM   4240  ND1 HIS B 200     -41.919 -32.842  29.998  1.00 16.16           N  
ANISOU 4240  ND1 HIS B 200     2910   2485    744      4    113    -13       N  
ATOM   4241  CD2 HIS B 200     -41.032 -31.900  31.769  1.00 15.26           C  
ANISOU 4241  CD2 HIS B 200     2904   2228    665      1    160    231       C  
ATOM   4242  CE1 HIS B 200     -40.885 -32.085  29.589  1.00 16.63           C  
ANISOU 4242  CE1 HIS B 200     2894   2642    781      2    166     51       C  
ATOM   4243  NE2 HIS B 200     -40.341 -31.505  30.673  1.00 16.50           N  
ANISOU 4243  NE2 HIS B 200     2897   2667    703   -148    245     89       N  
ATOM   4244  N   LYS B 201     -40.696 -36.180  32.154  1.00 14.32           N  
ANISOU 4244  N   LYS B 201     2741   2315    385    120    -75     23       N  
ATOM   4245  CA  LYS B 201     -40.053 -37.228  31.366  1.00 15.38           C  
ANISOU 4245  CA  LYS B 201     2842   2453    548    111     -1    -71       C  
ATOM   4246  C   LYS B 201     -40.325 -38.632  31.921  1.00 16.04           C  
ANISOU 4246  C   LYS B 201     2879   2503    710     82     49     19       C  
ATOM   4247  O   LYS B 201     -39.984 -39.629  31.277  1.00 16.84           O  
ANISOU 4247  O   LYS B 201     3078   2382    935     40    -26     15       O  
ATOM   4248  CB  LYS B 201     -38.543 -36.993  31.284  1.00 16.47           C  
ANISOU 4248  CB  LYS B 201     2844   2564    850    188     45    -16       C  
ATOM   4249  CG  LYS B 201     -38.145 -35.646  30.703  1.00 17.76           C  
ANISOU 4249  CG  LYS B 201     3094   2691    960     48    148      1       C  
ATOM   4250  CD  LYS B 201     -38.547 -35.554  29.247  1.00 18.25           C  
ANISOU 4250  CD  LYS B 201     3195   2690   1050     34    -21    136       C  
ATOM   4251  CE  LYS B 201     -38.195 -34.206  28.656  1.00 17.79           C  
ANISOU 4251  CE  LYS B 201     2821   2572   1365    -29     -2    -90       C  
ATOM   4252  NZ  LYS B 201     -36.728 -34.031  28.608  1.00 18.11           N  
ANISOU 4252  NZ  LYS B 201     2888   2463   1528     89    221     68       N  
ATOM   4253  N   VAL B 202     -40.943 -38.690  33.105  1.00 15.57           N  
ANISOU 4253  N   VAL B 202     2777   2342    794     57    122   -171       N  
ATOM   4254  CA  VAL B 202     -41.213 -39.949  33.824  1.00 15.68           C  
ANISOU 4254  CA  VAL B 202     2793   2493    671     69     60      1       C  
ATOM   4255  C   VAL B 202     -42.697 -40.118  34.190  1.00 14.67           C  
ANISOU 4255  C   VAL B 202     2805   2189    578     30     87   -253       C  
ATOM   4256  O   VAL B 202     -43.043 -40.745  35.194  1.00 15.82           O  
ANISOU 4256  O   VAL B 202     2999   2366    646      8    103   -126       O  
ATOM   4257  CB  VAL B 202     -40.281 -40.139  35.062  1.00 14.78           C  
ANISOU 4257  CB  VAL B 202     2710   2322    581      1     75   -299       C  
ATOM   4258  CG1 VAL B 202     -38.839 -40.354  34.620  1.00 14.90           C  
ANISOU 4258  CG1 VAL B 202     2798   2364    500     99    150   -245       C  
ATOM   4259  CG2 VAL B 202     -40.382 -38.966  36.044  1.00 14.12           C  
ANISOU 4259  CG2 VAL B 202     2768   2321    275     34    132   -142       C  
ATOM   4260  N   TYR B 203     -43.560 -39.567  33.334  1.00 15.47           N  
ANISOU 4260  N   TYR B 203     2966   2229    683     33     66    -94       N  
ATOM   4261  CA  TYR B 203     -45.020 -39.617  33.499  1.00 15.51           C  
ANISOU 4261  CA  TYR B 203     2950   2132    808    103     60   -258       C  
ATOM   4262  C   TYR B 203     -45.508 -38.801  34.700  1.00 15.62           C  
ANISOU 4262  C   TYR B 203     3106   2181    645     18    137   -143       C  
ATOM   4263  O   TYR B 203     -46.616 -39.023  35.228  1.00 16.79           O  
ANISOU 4263  O   TYR B 203     3242   2503    633     24    220   -107       O  
ATOM   4264  CB  TYR B 203     -45.551 -41.058  33.575  1.00 15.69           C  
ANISOU 4264  CB  TYR B 203     3160   2154    645     56    217      8       C  
ATOM   4265  CG  TYR B 203     -45.121 -42.014  32.470  1.00 16.20           C  
ANISOU 4265  CG  TYR B 203     3262   2187    705      3     47   -161       C  
ATOM   4266  CD1 TYR B 203     -45.766 -42.024  31.223  1.00 15.94           C  
ANISOU 4266  CD1 TYR B 203     3163   2344    550     20    227     27       C  
ATOM   4267  CD2 TYR B 203     -44.116 -42.965  32.701  1.00 17.07           C  
ANISOU 4267  CD2 TYR B 203     3274   2304    908     61     34   -141       C  
ATOM   4268  CE1 TYR B 203     -45.392 -42.933  30.240  1.00 17.47           C  
ANISOU 4268  CE1 TYR B 203     3520   2130    987     90    217   -130       C  
ATOM   4269  CE2 TYR B 203     -43.737 -43.860  31.722  1.00 17.57           C  
ANISOU 4269  CE2 TYR B 203     3451   2514    709    -63    150   -132       C  
ATOM   4270  CZ  TYR B 203     -44.365 -43.840  30.504  1.00 16.32           C  
ANISOU 4270  CZ  TYR B 203     3382   2142    676    -52    172     12       C  
ATOM   4271  OH  TYR B 203     -43.949 -44.771  29.586  1.00 17.17           O  
ANISOU 4271  OH  TYR B 203     3410   2188    924   -156    170   -210       O  
ATOM   4272  N   GLY B 204     -44.648 -37.869  35.121  1.00 15.21           N  
ANISOU 4272  N   GLY B 204     3041   2119    619    111    112   -256       N  
ATOM   4273  CA  GLY B 204     -44.995 -36.863  36.122  1.00 14.91           C  
ANISOU 4273  CA  GLY B 204     3116   2131    416     54    151   -159       C  
ATOM   4274  C   GLY B 204     -45.565 -35.610  35.476  1.00 15.61           C  
ANISOU 4274  C   GLY B 204     2919   2288    722    188     36   -182       C  
ATOM   4275  O   GLY B 204     -45.553 -35.452  34.244  1.00 16.24           O  
ANISOU 4275  O   GLY B 204     2950   2482    737     43     83    -87       O  
ATOM   4276  N   PRO B 205     -46.055 -34.685  36.301  1.00 16.11           N  
ANISOU 4276  N   PRO B 205     3022   2361    736     83     49   -298       N  
ATOM   4277  CA  PRO B 205     -46.555 -33.448  35.731  1.00 16.15           C  
ANISOU 4277  CA  PRO B 205     2917   2420    796    112    273   -215       C  
ATOM   4278  C   PRO B 205     -45.429 -32.543  35.264  1.00 15.66           C  
ANISOU 4278  C   PRO B 205     2804   2300    844    162     84    -51       C  
ATOM   4279  O   PRO B 205     -44.267 -32.668  35.695  1.00 15.71           O  
ANISOU 4279  O   PRO B 205     2768   2495    706    235    106   -118       O  
ATOM   4280  CB  PRO B 205     -47.314 -32.809  36.892  1.00 16.61           C  
ANISOU 4280  CB  PRO B 205     2828   2673    809    221    272   -216       C  
ATOM   4281  CG  PRO B 205     -46.623 -33.332  38.102  1.00 16.50           C  
ANISOU 4281  CG  PRO B 205     2991   2507    770    249    192   -333       C  
ATOM   4282  CD  PRO B 205     -46.194 -34.727  37.764  1.00 16.64           C  
ANISOU 4282  CD  PRO B 205     3180   2353    788    159    292   -180       C  
ATOM   4283  N   LYS B 206     -45.795 -31.642  34.364  1.00 14.91           N  
ANISOU 4283  N   LYS B 206     2870   2320    472     72     20   -183       N  
ATOM   4284  CA  LYS B 206     -44.900 -30.577  33.947  1.00 14.80           C  
ANISOU 4284  CA  LYS B 206     2801   2217    603    112    -13   -106       C  
ATOM   4285  C   LYS B 206     -44.744 -29.553  35.065  1.00 14.68           C  
ANISOU 4285  C   LYS B 206     2706   2108    763     53     13   -125       C  
ATOM   4286  O   LYS B 206     -45.627 -29.406  35.935  1.00 16.07           O  
ANISOU 4286  O   LYS B 206     2875   2566    666     -7     77   -148       O  
ATOM   4287  CB  LYS B 206     -45.396 -29.912  32.649  1.00 15.44           C  
ANISOU 4287  CB  LYS B 206     2945   2291    630    118    -55    -98       C  
ATOM   4288  CG  LYS B 206     -45.257 -30.796  31.412  1.00 15.90           C  
ANISOU 4288  CG  LYS B 206     3060   2275    705    137   -183   -173       C  
ATOM   4289  CD  LYS B 206     -45.902 -30.179  30.171  1.00 15.38           C  
ANISOU 4289  CD  LYS B 206     2914   2313    616     96   -186   -279       C  
ATOM   4290  CE  LYS B 206     -45.763 -31.102  28.962  1.00 15.00           C  
ANISOU 4290  CE  LYS B 206     2856   2127    713     24     -5   -249       C  
ATOM   4291  NZ  LYS B 206     -46.606 -32.331  29.065  1.00 15.98           N  
ANISOU 4291  NZ  LYS B 206     2947   2380    743   -219   -191   -258       N  
ATOM   4292  N   GLY B 207     -43.610 -28.861  35.034  1.00 14.54           N  
ANISOU 4292  N   GLY B 207     2640   2141    741     51   -135     32       N  
ATOM   4293  CA  GLY B 207     -43.329 -27.806  35.985  1.00 14.29           C  
ANISOU 4293  CA  GLY B 207     2639   2220    569     70   -123     47       C  
ATOM   4294  C   GLY B 207     -42.660 -28.277  37.263  1.00 14.76           C  
ANISOU 4294  C   GLY B 207     2726   2209    671    150   -251    -10       C  
ATOM   4295  O   GLY B 207     -42.562 -27.505  38.217  1.00 15.58           O  
ANISOU 4295  O   GLY B 207     2934   2296    687    290    -95   -122       O  
ATOM   4296  N   ILE B 208     -42.175 -29.519  37.285  1.00 13.68           N  
ANISOU 4296  N   ILE B 208     2670   2134    391    143   -121     13       N  
ATOM   4297  CA  ILE B 208     -41.441 -30.012  38.459  1.00 14.98           C  
ANISOU 4297  CA  ILE B 208     2626   2359    703    241   -300     55       C  
ATOM   4298  C   ILE B 208     -40.201 -30.807  38.065  1.00 14.69           C  
ANISOU 4298  C   ILE B 208     2683   2367    530    181   -186     63       C  
ATOM   4299  O   ILE B 208     -40.202 -31.509  37.086  1.00 15.28           O  
ANISOU 4299  O   ILE B 208     2819   2298    687    134   -281    -35       O  
ATOM   4300  CB  ILE B 208     -42.377 -30.844  39.389  1.00 15.17           C  
ANISOU 4300  CB  ILE B 208     2721   2318    724    178   -271      6       C  
ATOM   4301  CG1 ILE B 208     -41.767 -31.038  40.782  1.00 15.13           C  
ANISOU 4301  CG1 ILE B 208     2772   2316    659    133   -186     30       C  
ATOM   4302  CG2 ILE B 208     -42.776 -32.179  38.764  1.00 16.25           C  
ANISOU 4302  CG2 ILE B 208     2855   2367    952    150   -155    -99       C  
ATOM   4303  CD1 ILE B 208     -41.590 -29.739  41.541  1.00 15.45           C  
ANISOU 4303  CD1 ILE B 208     2805   2514    548     11   -127    -65       C  
ATOM   4304  N   GLY B 209     -39.129 -30.679  38.820  1.00 14.52           N  
ANISOU 4304  N   GLY B 209     2519   2378    619    185   -101    -64       N  
ATOM   4305  CA  GLY B 209     -38.014 -31.584  38.652  1.00 15.01           C  
ANISOU 4305  CA  GLY B 209     2676   2342    684    298   -184    -71       C  
ATOM   4306  C   GLY B 209     -37.216 -31.524  39.929  1.00 14.82           C  
ANISOU 4306  C   GLY B 209     2525   2352    754    297   -165   -141       C  
ATOM   4307  O   GLY B 209     -37.723 -31.075  40.966  1.00 14.36           O  
ANISOU 4307  O   GLY B 209     2618   2311    524     75   -160      3       O  
ATOM   4308  N   ALA B 210     -35.969 -31.968  39.869  1.00 14.69           N  
ANISOU 4308  N   ALA B 210     2432   2469    681    201   -204    -30       N  
ATOM   4309  CA  ALA B 210     -35.112 -31.906  41.047  1.00 13.83           C  
ANISOU 4309  CA  ALA B 210     2445   2264    545    150   -110     -4       C  
ATOM   4310  C   ALA B 210     -33.638 -31.817  40.688  1.00 14.22           C  
ANISOU 4310  C   ALA B 210     2480   2334    588    259    -49    -13       C  
ATOM   4311  O   ALA B 210     -33.249 -32.112  39.556  1.00 14.77           O  
ANISOU 4311  O   ALA B 210     2615   2323    674    363     13   -121       O  
ATOM   4312  CB  ALA B 210     -35.377 -33.106  41.962  1.00 13.92           C  
ANISOU 4312  CB  ALA B 210     2519   2211    559    249   -292     34       C  
ATOM   4313  N   LEU B 211     -32.828 -31.364  41.649  1.00 13.75           N  
ANISOU 4313  N   LEU B 211     2511   2288    426    280     71   -117       N  
ATOM   4314  CA  LEU B 211     -31.376 -31.439  41.562  1.00 14.09           C  
ANISOU 4314  CA  LEU B 211     2527   2166    661    338      0    -50       C  
ATOM   4315  C   LEU B 211     -30.873 -32.140  42.813  1.00 14.43           C  
ANISOU 4315  C   LEU B 211     2638   2144    698    403     29      0       C  
ATOM   4316  O   LEU B 211     -31.100 -31.639  43.925  1.00 14.92           O  
ANISOU 4316  O   LEU B 211     2640   2274    753    421     20    -81       O  
ATOM   4317  CB  LEU B 211     -30.725 -30.045  41.469  1.00 13.51           C  
ANISOU 4317  CB  LEU B 211     2540   2143    450    316    173      2       C  
ATOM   4318  CG  LEU B 211     -29.193 -30.020  41.329  1.00 14.03           C  
ANISOU 4318  CG  LEU B 211     2534   2135    659    449     57    -78       C  
ATOM   4319  CD1 LEU B 211     -28.733 -30.579  39.975  1.00 14.51           C  
ANISOU 4319  CD1 LEU B 211     2621   2290    600    362     83    -58       C  
ATOM   4320  CD2 LEU B 211     -28.652 -28.616  41.556  1.00 14.75           C  
ANISOU 4320  CD2 LEU B 211     2618   2288    698    193   -166     24       C  
ATOM   4321  N   TYR B 212     -30.266 -33.314  42.640  1.00 13.17           N  
ANISOU 4321  N   TYR B 212     2389   2161    454    443    103     74       N  
ATOM   4322  CA  TYR B 212     -29.472 -33.940  43.707  1.00 14.50           C  
ANISOU 4322  CA  TYR B 212     2527   2241    741    562   -134    -40       C  
ATOM   4323  C   TYR B 212     -28.222 -33.088  43.956  1.00 14.98           C  
ANISOU 4323  C   TYR B 212     2632   2326    732    418     41    -39       C  
ATOM   4324  O   TYR B 212     -27.494 -32.757  43.015  1.00 14.67           O  
ANISOU 4324  O   TYR B 212     2701   2300    571    450    -31     31       O  
ATOM   4325  CB  TYR B 212     -29.070 -35.384  43.341  1.00 14.60           C  
ANISOU 4325  CB  TYR B 212     2703   2126    716    551    -58     74       C  
ATOM   4326  CG  TYR B 212     -27.901 -35.902  44.171  1.00 15.62           C  
ANISOU 4326  CG  TYR B 212     2684   2479    770    590    -14    164       C  
ATOM   4327  CD1 TYR B 212     -28.097 -36.300  45.487  1.00 15.41           C  
ANISOU 4327  CD1 TYR B 212     2761   2350    741    629   -107    126       C  
ATOM   4328  CD2 TYR B 212     -26.608 -35.966  43.644  1.00 15.47           C  
ANISOU 4328  CD2 TYR B 212     2650   2496    728    463    -83     38       C  
ATOM   4329  CE1 TYR B 212     -27.045 -36.773  46.251  1.00 15.53           C  
ANISOU 4329  CE1 TYR B 212     2804   2537    558    604   -160      3       C  
ATOM   4330  CE2 TYR B 212     -25.543 -36.440  44.396  1.00 16.13           C  
ANISOU 4330  CE2 TYR B 212     2809   2522    797    633    -76     34       C  
ATOM   4331  CZ  TYR B 212     -25.772 -36.829  45.700  1.00 16.62           C  
ANISOU 4331  CZ  TYR B 212     2810   2751    751    636   -119      0       C  
ATOM   4332  OH  TYR B 212     -24.743 -37.302  46.469  1.00 18.66           O  
ANISOU 4332  OH  TYR B 212     3037   2970   1080    785   -249    105       O  
ATOM   4333  N   VAL B 213     -27.975 -32.737  45.219  1.00 14.86           N  
ANISOU 4333  N   VAL B 213     2601   2382    660    426   -128    178       N  
ATOM   4334  CA  VAL B 213     -26.764 -32.017  45.614  1.00 15.21           C  
ANISOU 4334  CA  VAL B 213     2719   2452    605    321     21    120       C  
ATOM   4335  C   VAL B 213     -26.166 -32.754  46.802  1.00 15.62           C  
ANISOU 4335  C   VAL B 213     2674   2582    677    404   -145     14       C  
ATOM   4336  O   VAL B 213     -26.730 -32.748  47.896  1.00 16.58           O  
ANISOU 4336  O   VAL B 213     3017   2649    631    291    -91     62       O  
ATOM   4337  CB  VAL B 213     -27.074 -30.560  46.012  1.00 16.16           C  
ANISOU 4337  CB  VAL B 213     2979   2462    695    198   -157     72       C  
ATOM   4338  CG1 VAL B 213     -25.812 -29.814  46.438  1.00 17.98           C  
ANISOU 4338  CG1 VAL B 213     3074   2847    907    148   -329    102       C  
ATOM   4339  CG2 VAL B 213     -27.758 -29.829  44.870  1.00 15.77           C  
ANISOU 4339  CG2 VAL B 213     2697   2411    882    289   -111     74       C  
ATOM   4340  N   ARG B 214     -25.027 -33.402  46.583  1.00 15.64           N  
ANISOU 4340  N   ARG B 214     2802   2417    720    571   -268      3       N  
ATOM   4341  CA  ARG B 214     -24.328 -34.083  47.673  1.00 16.40           C  
ANISOU 4341  CA  ARG B 214     2918   2753    558    632   -199     45       C  
ATOM   4342  C   ARG B 214     -24.061 -33.089  48.798  1.00 17.34           C  
ANISOU 4342  C   ARG B 214     3016   2831    741    368    -84    -46       C  
ATOM   4343  O   ARG B 214     -23.564 -31.978  48.558  1.00 17.61           O  
ANISOU 4343  O   ARG B 214     3194   2672    824    355    -39   -285       O  
ATOM   4344  CB  ARG B 214     -23.018 -34.713  47.186  1.00 16.77           C  
ANISOU 4344  CB  ARG B 214     2855   2785    728    711   -353     93       C  
ATOM   4345  CG  ARG B 214     -22.353 -35.584  48.256  1.00 17.28           C  
ANISOU 4345  CG  ARG B 214     2933   2673    958    964   -275    103       C  
ATOM   4346  CD  ARG B 214     -21.056 -36.230  47.766  1.00 18.12           C  
ANISOU 4346  CD  ARG B 214     3136   2735   1011   1002   -147    -63       C  
ATOM   4347  NE  ARG B 214     -21.258 -37.229  46.707  1.00 19.01           N  
ANISOU 4347  NE  ARG B 214     3496   2755    970    719    -94    -42       N  
ATOM   4348  CZ  ARG B 214     -21.578 -38.509  46.905  1.00 20.85           C  
ANISOU 4348  CZ  ARG B 214     4005   2939    975    518     81     69       C  
ATOM   4349  NH1 ARG B 214     -21.767 -38.978  48.138  1.00 24.67           N  
ANISOU 4349  NH1 ARG B 214     4608   3445   1319    678    135    593       N  
ATOM   4350  NH2 ARG B 214     -21.724 -39.329  45.864  1.00 21.32           N  
ANISOU 4350  NH2 ARG B 214     3777   2864   1457    625   -167   -211       N  
ATOM   4351  N   ASP B 215     -24.409 -33.487  50.023  1.00 17.44           N  
ANISOU 4351  N   ASP B 215     3017   2886    722    487   -109      1       N  
ATOM   4352  CA  ASP B 215     -24.173 -32.646  51.197  1.00 18.21           C  
ANISOU 4352  CA  ASP B 215     3292   3008    616    293   -261     79       C  
ATOM   4353  C   ASP B 215     -24.839 -31.272  51.053  1.00 18.69           C  
ANISOU 4353  C   ASP B 215     3172   3016    913    317    -34    -74       C  
ATOM   4354  O   ASP B 215     -24.250 -30.241  51.370  1.00 19.38           O  
ANISOU 4354  O   ASP B 215     3496   3060    805    271    -58   -102       O  
ATOM   4355  CB  ASP B 215     -22.651 -32.510  51.453  1.00 19.51           C  
ANISOU 4355  CB  ASP B 215     3300   3263    849    314    -55   -270       C  
ATOM   4356  CG  ASP B 215     -22.320 -31.997  52.840  1.00 21.69           C  
ANISOU 4356  CG  ASP B 215     4077   3366    798    141   -248   -118       C  
ATOM   4357  OD1 ASP B 215     -23.135 -32.167  53.769  1.00 23.02           O  
ANISOU 4357  OD1 ASP B 215     4404   3448    892    153    -45   -236       O  
ATOM   4358  OD2 ASP B 215     -21.213 -31.448  52.999  1.00 24.31           O  
ANISOU 4358  OD2 ASP B 215     4137   3794   1306    138   -347   -376       O  
ATOM   4359  N   ALA B 216     -26.074 -31.261  50.553  1.00 18.09           N  
ANISOU 4359  N   ALA B 216     3216   2964    690    329   -143    -79       N  
ATOM   4360  CA  ALA B 216     -26.800 -30.012  50.325  1.00 17.93           C  
ANISOU 4360  CA  ALA B 216     3222   2976    612    278   -232    128       C  
ATOM   4361  C   ALA B 216     -26.849 -29.107  51.552  1.00 20.00           C  
ANISOU 4361  C   ALA B 216     3614   3062    922    276    -61    -60       C  
ATOM   4362  O   ALA B 216     -26.765 -27.890  51.427  1.00 21.04           O  
ANISOU 4362  O   ALA B 216     3964   3054    973    513     22   -206       O  
ATOM   4363  CB  ALA B 216     -28.207 -30.285  49.826  1.00 17.19           C  
ANISOU 4363  CB  ALA B 216     3181   2736    612    306   -202     44       C  
ATOM   4364  N   ARG B 217     -26.957 -29.703  52.737  1.00 19.69           N  
ANISOU 4364  N   ARG B 217     3594   3184    700    464   -155   -201       N  
ATOM   4365  CA  ARG B 217     -27.007 -28.932  53.991  1.00 20.77           C  
ANISOU 4365  CA  ARG B 217     3958   3265    668    342   -176   -171       C  
ATOM   4366  C   ARG B 217     -25.816 -27.992  54.205  1.00 21.23           C  
ANISOU 4366  C   ARG B 217     4015   3363    688    277   -270    -80       C  
ATOM   4367  O   ARG B 217     -25.956 -26.946  54.844  1.00 22.94           O  
ANISOU 4367  O   ARG B 217     4191   3528    995    383   -106   -205       O  
ATOM   4368  CB  ARG B 217     -27.120 -29.865  55.187  1.00 23.25           C  
ANISOU 4368  CB  ARG B 217     4206   3950    677     84   -241    107       C  
ATOM   4369  CG  ARG B 217     -28.482 -30.492  55.371  1.00 26.28           C  
ANISOU 4369  CG  ARG B 217     4080   4610   1295     94   -274    -70       C  
ATOM   4370  CD  ARG B 217     -28.572 -30.881  56.821  1.00 31.76           C  
ANISOU 4370  CD  ARG B 217     5034   5025   2006   -332    289   1086       C  
ATOM   4371  NE  ARG B 217     -29.828 -31.556  57.127  1.00 29.13           N  
ANISOU 4371  NE  ARG B 217     4620   4650   1795   -306     13    -96       N  
ATOM   4372  CZ  ARG B 217     -30.026 -32.860  56.984  1.00 29.31           C  
ANISOU 4372  CZ  ARG B 217     4642   4802   1693   -467    -90  -1198       C  
ATOM   4373  NH1 ARG B 217     -29.045 -33.629  56.535  1.00 35.02           N  
ANISOU 4373  NH1 ARG B 217     4737   5256   3312    447   -232   -167       N  
ATOM   4374  NH2 ARG B 217     -31.203 -33.397  57.284  1.00 29.62           N  
ANISOU 4374  NH2 ARG B 217     4620   4601   2032    -81    -12   -503       N  
ATOM   4375  N   ASN B 218     -24.663 -28.374  53.659  1.00 19.90           N  
ANISOU 4375  N   ASN B 218     3934   3350    277    327   -297    -32       N  
ATOM   4376  CA  ASN B 218     -23.414 -27.632  53.789  1.00 21.86           C  
ANISOU 4376  CA  ASN B 218     4165   3516    622    173   -162     17       C  
ATOM   4377  C   ASN B 218     -22.932 -27.070  52.448  1.00 21.83           C  
ANISOU 4377  C   ASN B 218     3840   3706    749     30   -201     74       C  
ATOM   4378  O   ASN B 218     -21.802 -26.591  52.330  1.00 22.99           O  
ANISOU 4378  O   ASN B 218     3684   3981   1066    -66   -579   -311       O  
ATOM   4379  CB  ASN B 218     -22.352 -28.545  54.420  1.00 22.72           C  
ANISOU 4379  CB  ASN B 218     4167   3577    886    279   -138     47       C  
ATOM   4380  CG  ASN B 218     -22.749 -29.003  55.805  1.00 23.63           C  
ANISOU 4380  CG  ASN B 218     4501   3474   1000    214   -140    236       C  
ATOM   4381  OD1 ASN B 218     -22.974 -30.192  56.046  1.00 26.87           O  
ANISOU 4381  OD1 ASN B 218     4693   3511   2002    236   -155    520       O  
ATOM   4382  ND2 ASN B 218     -22.888 -28.053  56.713  1.00 24.29           N  
ANISOU 4382  ND2 ASN B 218     4814   3191   1225    328    -42    206       N  
ATOM   4383  N   SER B 219     -23.803 -27.123  51.447  1.00 21.71           N  
ANISOU 4383  N   SER B 219     3933   3542    772    234   -303    -35       N  
ATOM   4384  CA  SER B 219     -23.438 -26.680  50.122  1.00 22.99           C  
ANISOU 4384  CA  SER B 219     4064   3718    950    123   -370    242       C  
ATOM   4385  C   SER B 219     -23.207 -25.183  50.046  1.00 24.22           C  
ANISOU 4385  C   SER B 219     3887   3844   1470      0   -392    -22       C  
ATOM   4386  O   SER B 219     -23.956 -24.380  50.604  1.00 24.29           O  
ANISOU 4386  O   SER B 219     4055   3578   1594    -39   -595   -240       O  
ATOM   4387  CB  SER B 219     -24.501 -27.088  49.106  1.00 23.69           C  
ANISOU 4387  CB  SER B 219     4056   3784   1161     -6   -383    216       C  
ATOM   4388  OG  SER B 219     -24.380 -26.280  47.949  1.00 23.25           O  
ANISOU 4388  OG  SER B 219     3912   3675   1244   -120   -397    185       O  
ATOM   4389  N   GLU B 220     -22.171 -24.810  49.314  1.00 24.80           N  
ANISOU 4389  N   GLU B 220     3933   4019   1471   -199   -444     56       N  
ATOM   4390  CA  GLU B 220     -21.859 -23.408  49.112  1.00 26.83           C  
ANISOU 4390  CA  GLU B 220     4189   3926   2076    121   -690    -18       C  
ATOM   4391  C   GLU B 220     -22.388 -22.906  47.780  1.00 24.20           C  
ANISOU 4391  C   GLU B 220     3669   3543   1981    -56   -457     -1       C  
ATOM   4392  O   GLU B 220     -21.999 -21.840  47.333  1.00 25.42           O  
ANISOU 4392  O   GLU B 220     3886   3784   1986   -235   -433     19       O  
ATOM   4393  CB  GLU B 220     -20.360 -23.172  49.196  1.00 31.48           C  
ANISOU 4393  CB  GLU B 220     4239   4491   3232    126   -507   -158       C  
ATOM   4394  CG  GLU B 220     -19.857 -23.200  50.620  1.00 36.68           C  
ANISOU 4394  CG  GLU B 220     5627   5178   3131    945   -520   -311       C  
ATOM   4395  CD  GLU B 220     -18.435 -22.808  50.691  1.00 47.96           C  
ANISOU 4395  CD  GLU B 220     4311   7032   6880   3751    965  -2987       C  
ATOM   4396  OE1 GLU B 220     -18.219 -21.633  50.998  1.00 59.08           O  
ANISOU 4396  OE1 GLU B 220     7575   7241   7629   1698   -574  -1786       O  
ATOM   4397  OE2 GLU B 220     -17.552 -23.650  50.438  1.00 52.63           O  
ANISOU 4397  OE2 GLU B 220     5499   6598   7900   4564    925  -2846       O  
ATOM   4398  N   LEU B 221     -23.248 -23.687  47.144  1.00 21.62           N  
ANISOU 4398  N   LEU B 221     3533   3383   1296    173   -498     73       N  
ATOM   4399  CA ALEU B 221     -23.846 -23.285  45.881  0.50 20.51           C  
ANISOU 4399  CA ALEU B 221     3413   3158   1222     65   -276    242       C  
ATOM   4400  CA BLEU B 221     -23.855 -23.283  45.880  0.50 19.78           C  
ANISOU 4400  CA BLEU B 221     3236   3147   1132     21   -183    203       C  
ATOM   4401  C   LEU B 221     -24.549 -21.944  46.025  1.00 19.36           C  
ANISOU 4401  C   LEU B 221     3167   3230    958     62   -154     61       C  
ATOM   4402  O   LEU B 221     -25.266 -21.715  46.993  1.00 20.95           O  
ANISOU 4402  O   LEU B 221     3332   3507   1119    187    -39     -5       O  
ATOM   4403  CB ALEU B 221     -24.865 -24.326  45.406  0.50 21.59           C  
ANISOU 4403  CB ALEU B 221     3401   3479   1322      4   -404    151       C  
ATOM   4404  CB BLEU B 221     -24.902 -24.294  45.414  0.50 19.19           C  
ANISOU 4404  CB BLEU B 221     3031   3225   1034    114   -118     61       C  
ATOM   4405  CG ALEU B 221     -24.468 -25.478  44.486  0.50 23.00           C  
ANISOU 4405  CG ALEU B 221     3685   3438   1614    -75   -341     61       C  
ATOM   4406  CG BLEU B 221     -24.538 -25.603  44.718  0.50 18.38           C  
ANISOU 4406  CG BLEU B 221     2726   3355    901     85    321     75       C  
ATOM   4407  CD1ALEU B 221     -23.178 -26.141  44.926  0.50 26.48           C  
ANISOU 4407  CD1ALEU B 221     3966   3923   2171    136   -590    141       C  
ATOM   4408  CD1BLEU B 221     -25.803 -26.423  44.512  0.50 17.91           C  
ANISOU 4408  CD1BLEU B 221     2875   3172    755     59    247    -13       C  
ATOM   4409  CD2ALEU B 221     -25.594 -26.492  44.407  0.50 20.94           C  
ANISOU 4409  CD2ALEU B 221     3417   3455   1083     -1    -36     39       C  
ATOM   4410  CD2BLEU B 221     -23.801 -25.384  43.400  0.50 16.74           C  
ANISOU 4410  CD2BLEU B 221     2794   2888    675     77    144     31       C  
ATOM   4411  N   VAL B 222     -24.354 -21.073  45.039  1.00 18.81           N  
ANISOU 4411  N   VAL B 222     2918   3037   1193    186   -208    136       N  
ATOM   4412  CA  VAL B 222     -25.102 -19.820  44.975  1.00 18.90           C  
ANISOU 4412  CA  VAL B 222     2952   2989   1238     94   -164     71       C  
ATOM   4413  C   VAL B 222     -26.509 -20.120  44.447  1.00 17.28           C  
ANISOU 4413  C   VAL B 222     2834   2925    803    203    -59      2       C  
ATOM   4414  O   VAL B 222     -26.649 -20.661  43.346  1.00 17.92           O  
ANISOU 4414  O   VAL B 222     2968   2959    881     98     30    -89       O  
ATOM   4415  CB  VAL B 222     -24.407 -18.784  44.073  1.00 19.15           C  
ANISOU 4415  CB  VAL B 222     3134   2990   1149    186    -97      2       C  
ATOM   4416  CG1 VAL B 222     -25.279 -17.546  43.918  1.00 19.10           C  
ANISOU 4416  CG1 VAL B 222     3280   2930   1043    183   -289    208       C  
ATOM   4417  CG2 VAL B 222     -23.067 -18.405  44.674  1.00 21.82           C  
ANISOU 4417  CG2 VAL B 222     3182   3452   1656     27   -139   -229       C  
ATOM   4418  N   PRO B 223     -27.552 -19.808  45.245  1.00 16.82           N  
ANISOU 4418  N   PRO B 223     2818   2828    743    251    -93    -50       N  
ATOM   4419  CA  PRO B 223     -28.933 -20.051  44.821  1.00 16.22           C  
ANISOU 4419  CA  PRO B 223     2780   2791    590    246     16   -153       C  
ATOM   4420  C   PRO B 223     -29.228 -19.349  43.490  1.00 16.62           C  
ANISOU 4420  C   PRO B 223     2928   2662    724    150   -142   -109       C  
ATOM   4421  O   PRO B 223     -28.777 -18.214  43.276  1.00 16.42           O  
ANISOU 4421  O   PRO B 223     2779   2826    630     38     99    -99       O  
ATOM   4422  CB  PRO B 223     -29.761 -19.456  45.977  1.00 15.54           C  
ANISOU 4422  CB  PRO B 223     2655   2541    706    328    -65   -209       C  
ATOM   4423  CG  PRO B 223     -28.863 -19.603  47.173  1.00 16.49           C  
ANISOU 4423  CG  PRO B 223     2640   2837    786    327   -106   -155       C  
ATOM   4424  CD  PRO B 223     -27.482 -19.301  46.631  1.00 17.13           C  
ANISOU 4424  CD  PRO B 223     2768   2880    857    145    -46   -212       C  
ATOM   4425  N   LEU B 224     -29.929 -20.045  42.597  1.00 16.22           N  
ANISOU 4425  N   LEU B 224     2905   2639    619    258    -80   -198       N  
ATOM   4426  CA  LEU B 224     -30.408 -19.454  41.345  1.00 15.94           C  
ANISOU 4426  CA  LEU B 224     2701   2638    717    127   -119   -110       C  
ATOM   4427  C   LEU B 224     -31.642 -18.583  41.665  1.00 15.77           C  
ANISOU 4427  C   LEU B 224     2777   2419    793     62   -124   -320       C  
ATOM   4428  O   LEU B 224     -31.741 -17.428  41.223  1.00 16.98           O  
ANISOU 4428  O   LEU B 224     3043   2559    849    113   -151   -179       O  
ATOM   4429  CB  LEU B 224     -30.746 -20.564  40.342  1.00 16.97           C  
ANISOU 4429  CB  LEU B 224     2945   2695    805     39     50   -245       C  
ATOM   4430  CG  LEU B 224     -30.860 -20.237  38.847  1.00 17.98           C  
ANISOU 4430  CG  LEU B 224     2767   3104    959   -216   -201     34       C  
ATOM   4431  CD1 LEU B 224     -29.489 -20.001  38.234  1.00 19.31           C  
ANISOU 4431  CD1 LEU B 224     2818   3251   1268    -54     61     35       C  
ATOM   4432  CD2 LEU B 224     -31.622 -21.354  38.152  1.00 17.09           C  
ANISOU 4432  CD2 LEU B 224     2993   3058    441     13   -257   -163       C  
ATOM   4433  N   ILE B 225     -32.570 -19.140  42.436  1.00 16.14           N  
ANISOU 4433  N   ILE B 225     2960   2644    526    199    -45    -88       N  
ATOM   4434  CA  ILE B 225     -33.717 -18.386  42.929  1.00 16.15           C  
ANISOU 4434  CA  ILE B 225     2946   2513    675    205   -132   -140       C  
ATOM   4435  C   ILE B 225     -33.538 -18.175  44.434  1.00 16.20           C  
ANISOU 4435  C   ILE B 225     2919   2549    685    231   -135   -179       C  
ATOM   4436  O   ILE B 225     -33.662 -19.119  45.223  1.00 16.18           O  
ANISOU 4436  O   ILE B 225     2996   2572    577    317   -220   -158       O  
ATOM   4437  CB  ILE B 225     -35.038 -19.123  42.625  1.00 16.67           C  
ANISOU 4437  CB  ILE B 225     2891   2663    779    246   -240   -177       C  
ATOM   4438  CG1 ILE B 225     -35.150 -19.399  41.120  1.00 18.26           C  
ANISOU 4438  CG1 ILE B 225     3444   2596    896     74   -472   -371       C  
ATOM   4439  CG2 ILE B 225     -36.251 -18.345  43.137  1.00 15.24           C  
ANISOU 4439  CG2 ILE B 225     2926   2411    453    219   -291   -291       C  
ATOM   4440  CD1 ILE B 225     -36.209 -20.415  40.782  1.00 20.03           C  
ANISOU 4440  CD1 ILE B 225     3361   2882   1365    -58   -244   -261       C  
ATOM   4441  N   HIS B 226     -33.227 -16.940  44.813  1.00 15.45           N  
ANISOU 4441  N   HIS B 226     2723   2526    620    250   -214    -84       N  
ATOM   4442  CA  HIS B 226     -33.192 -16.565  46.228  1.00 15.91           C  
ANISOU 4442  CA  HIS B 226     2713   2599    732    213     11   -314       C  
ATOM   4443  C   HIS B 226     -34.597 -16.406  46.697  1.00 16.21           C  
ANISOU 4443  C   HIS B 226     2753   2736    670    279     57    -88       C  
ATOM   4444  O   HIS B 226     -35.429 -15.814  46.020  1.00 16.54           O  
ANISOU 4444  O   HIS B 226     3019   2628    636    268   -103   -146       O  
ATOM   4445  CB  HIS B 226     -32.404 -15.278  46.454  1.00 14.44           C  
ANISOU 4445  CB  HIS B 226     2420   2514    552    294    -58   -149       C  
ATOM   4446  CG  HIS B 226     -30.908 -15.453  46.339  1.00 15.06           C  
ANISOU 4446  CG  HIS B 226     2410   2460    853    223   -164   -194       C  
ATOM   4447  ND1 HIS B 226     -30.110 -15.641  47.414  1.00 17.43           N  
ANISOU 4447  ND1 HIS B 226     2554   2806   1259    284   -440    -80       N  
ATOM   4448  CD2 HIS B 226     -30.082 -15.484  45.226  1.00 14.87           C  
ANISOU 4448  CD2 HIS B 226     2589   2370    691    285   -176    100       C  
ATOM   4449  CE1 HIS B 226     -28.839 -15.778  47.002  1.00 15.54           C  
ANISOU 4449  CE1 HIS B 226     2524   2429    949    100   -345   -162       C  
ATOM   4450  NE2 HIS B 226     -28.824 -15.678  45.663  1.00 17.81           N  
ANISOU 4450  NE2 HIS B 226     2715   3056    994     69   -376    -80       N  
ATOM   4451  N   GLY B 227     -34.895 -16.936  47.869  1.00 16.21           N  
ANISOU 4451  N   GLY B 227     2794   2902    462    440     51   -216       N  
ATOM   4452  CA  GLY B 227     -36.273 -16.918  48.336  1.00 17.38           C  
ANISOU 4452  CA  GLY B 227     2871   3039    690    346    232    -92       C  
ATOM   4453  C   GLY B 227     -36.401 -16.864  49.842  1.00 16.71           C  
ANISOU 4453  C   GLY B 227     2819   2847    680    527    161   -180       C  
ATOM   4454  O   GLY B 227     -35.546 -16.319  50.524  1.00 18.52           O  
ANISOU 4454  O   GLY B 227     3156   2990    889    324    -90    -35       O  
ATOM   4455  N   GLY B 228     -37.468 -17.468  50.351  1.00 17.16           N  
ANISOU 4455  N   GLY B 228     3024   2768    728    446    176    -14       N  
ATOM   4456  CA  GLY B 228     -37.828 -17.350  51.752  1.00 17.62           C  
ANISOU 4456  CA  GLY B 228     3113   2749    829    530    363    -71       C  
ATOM   4457  C   GLY B 228     -37.172 -18.364  52.661  1.00 17.43           C  
ANISOU 4457  C   GLY B 228     2993   2728    898    494    337    -92       C  
ATOM   4458  O   GLY B 228     -37.393 -18.338  53.875  1.00 19.21           O  
ANISOU 4458  O   GLY B 228     3172   3248    879    388    295   -106       O  
ATOM   4459  N   GLY B 229     -36.376 -19.259  52.077  1.00 16.73           N  
ANISOU 4459  N   GLY B 229     2967   2275   1113    521    218     99       N  
ATOM   4460  CA  GLY B 229     -35.694 -20.302  52.831  1.00 16.35           C  
ANISOU 4460  CA  GLY B 229     2943   2387    883    480     78     52       C  
ATOM   4461  C   GLY B 229     -36.006 -21.721  52.413  1.00 16.30           C  
ANISOU 4461  C   GLY B 229     2959   2529    705    341     28    -55       C  
ATOM   4462  O   GLY B 229     -35.437 -22.649  52.973  1.00 16.71           O  
ANISOU 4462  O   GLY B 229     3388   2440    520    446     45   -188       O  
ATOM   4463  N   GLN B 230     -36.898 -21.888  51.435  1.00 16.43           N  
ANISOU 4463  N   GLN B 230     2899   2496    847    258     63   -162       N  
ATOM   4464  CA  GLN B 230     -37.241 -23.200  50.909  1.00 15.82           C  
ANISOU 4464  CA  GLN B 230     2754   2565    692    345   -201   -187       C  
ATOM   4465  C   GLN B 230     -35.998 -23.918  50.410  1.00 15.51           C  
ANISOU 4465  C   GLN B 230     2793   2551    546    337    -85    -74       C  
ATOM   4466  O   GLN B 230     -35.023 -23.281  49.966  1.00 15.73           O  
ANISOU 4466  O   GLN B 230     2906   2583    485    331    -39    -56       O  
ATOM   4467  CB  GLN B 230     -38.247 -23.085  49.761  1.00 16.26           C  
ANISOU 4467  CB  GLN B 230     2578   2691    907    341   -238     53       C  
ATOM   4468  CG  GLN B 230     -39.634 -22.632  50.189  1.00 16.71           C  
ANISOU 4468  CG  GLN B 230     2712   2660    974    285     -1    -53       C  
ATOM   4469  CD  GLN B 230     -39.830 -21.126  50.128  1.00 17.62           C  
ANISOU 4469  CD  GLN B 230     2789   2676   1228    244   -417   -312       C  
ATOM   4470  OE1 GLN B 230     -38.871 -20.348  50.012  1.00 19.14           O  
ANISOU 4470  OE1 GLN B 230     3007   2759   1504    226   -131    -26       O  
ATOM   4471  NE2 GLN B 230     -41.086 -20.703  50.208  1.00 17.47           N  
ANISOU 4471  NE2 GLN B 230     2973   2650   1014    453   -199   -314       N  
ATOM   4472  N   GLU B 231     -36.056 -25.249  50.480  1.00 14.92           N  
ANISOU 4472  N   GLU B 231     2733   2511    425    268    -64   -216       N  
ATOM   4473  CA  GLU B 231     -35.015 -26.140  49.946  1.00 15.75           C  
ANISOU 4473  CA  GLU B 231     2739   2570    675    376   -102   -213       C  
ATOM   4474  C   GLU B 231     -33.645 -25.823  50.539  1.00 15.81           C  
ANISOU 4474  C   GLU B 231     2775   2489    741    283    -26   -175       C  
ATOM   4475  O   GLU B 231     -32.661 -25.683  49.826  1.00 16.20           O  
ANISOU 4475  O   GLU B 231     2858   2618    677    378     13   -105       O  
ATOM   4476  CB  GLU B 231     -34.989 -26.099  48.400  1.00 15.46           C  
ANISOU 4476  CB  GLU B 231     2704   2485    683    210    -59    -65       C  
ATOM   4477  CG  GLU B 231     -36.336 -26.403  47.755  1.00 15.50           C  
ANISOU 4477  CG  GLU B 231     2597   2555    736    241      2     26       C  
ATOM   4478  CD  GLU B 231     -36.858 -27.777  48.117  1.00 15.70           C  
ANISOU 4478  CD  GLU B 231     2740   2494    729    305     70    -82       C  
ATOM   4479  OE1 GLU B 231     -37.952 -27.871  48.698  1.00 17.55           O  
ANISOU 4479  OE1 GLU B 231     2981   2790    896    171    334   -138       O  
ATOM   4480  OE2 GLU B 231     -36.163 -28.774  47.840  1.00 16.45           O  
ANISOU 4480  OE2 GLU B 231     2980   2531    739    302    161   -265       O  
ATOM   4481  N   LEU B 232     -33.612 -25.678  51.858  1.00 16.84           N  
ANISOU 4481  N   LEU B 232     2967   2683    747    277   -187   -178       N  
ATOM   4482  CA  LEU B 232     -32.359 -25.429  52.588  1.00 16.40           C  
ANISOU 4482  CA  LEU B 232     2877   2535    817    347   -124   -218       C  
ATOM   4483  C   LEU B 232     -31.731 -24.106  52.183  1.00 16.40           C  
ANISOU 4483  C   LEU B 232     2864   2644    722    390    -53   -113       C  
ATOM   4484  O   LEU B 232     -30.519 -23.905  52.338  1.00 17.05           O  
ANISOU 4484  O   LEU B 232     3014   2552    910    133   -333    -33       O  
ATOM   4485  CB  LEU B 232     -31.353 -26.583  52.408  1.00 17.47           C  
ANISOU 4485  CB  LEU B 232     2966   2499   1169    295    -21   -154       C  
ATOM   4486  CG  LEU B 232     -31.826 -28.021  52.683  1.00 18.13           C  
ANISOU 4486  CG  LEU B 232     3290   2577   1021    260    311     57       C  
ATOM   4487  CD1 LEU B 232     -30.743 -29.033  52.322  1.00 19.93           C  
ANISOU 4487  CD1 LEU B 232     3522   2810   1238    425    105   -160       C  
ATOM   4488  CD2 LEU B 232     -32.267 -28.247  54.128  1.00 18.84           C  
ANISOU 4488  CD2 LEU B 232     3522   2887    748    465    -40     69       C  
ATOM   4489  N   GLY B 233     -32.569 -23.207  51.670  1.00 15.30           N  
ANISOU 4489  N   GLY B 233     2922   2588    302    350   -101   -185       N  
ATOM   4490  CA  GLY B 233     -32.116 -21.890  51.230  1.00 16.62           C  
ANISOU 4490  CA  GLY B 233     3105   2506    702    389     99   -291       C  
ATOM   4491  C   GLY B 233     -31.490 -21.919  49.849  1.00 16.19           C  
ANISOU 4491  C   GLY B 233     2798   2560    791    277    117   -100       C  
ATOM   4492  O   GLY B 233     -31.009 -20.893  49.346  1.00 16.15           O  
ANISOU 4492  O   GLY B 233     2882   2667    585    290     29     45       O  
ATOM   4493  N   LEU B 234     -31.480 -23.103  49.239  1.00 16.04           N  
ANISOU 4493  N   LEU B 234     2686   2602    805    383     27   -214       N  
ATOM   4494  CA  LEU B 234     -30.857 -23.262  47.905  1.00 15.41           C  
ANISOU 4494  CA  LEU B 234     2570   2563    721    445    -50     38       C  
ATOM   4495  C   LEU B 234     -31.775 -22.923  46.720  1.00 14.74           C  
ANISOU 4495  C   LEU B 234     2425   2506    667    246    -43   -101       C  
ATOM   4496  O   LEU B 234     -31.291 -22.630  45.624  1.00 15.58           O  
ANISOU 4496  O   LEU B 234     2666   2420    833    208     77     66       O  
ATOM   4497  CB  LEU B 234     -30.268 -24.672  47.719  1.00 16.29           C  
ANISOU 4497  CB  LEU B 234     2688   2622    880    437    -70   -252       C  
ATOM   4498  CG  LEU B 234     -29.148 -25.068  48.684  1.00 17.24           C  
ANISOU 4498  CG  LEU B 234     2592   2618   1339    393   -167    -49       C  
ATOM   4499  CD1 LEU B 234     -28.925 -26.570  48.608  1.00 18.92           C  
ANISOU 4499  CD1 LEU B 234     3021   2624   1542    394   -250   -237       C  
ATOM   4500  CD2 LEU B 234     -27.878 -24.286  48.365  1.00 21.14           C  
ANISOU 4500  CD2 LEU B 234     2830   3273   1926     63   -132    128       C  
ATOM   4501  N   ARG B 235     -33.089 -22.995  46.942  1.00 14.29           N  
ANISOU 4501  N   ARG B 235     2290   2343    793    308   -259    -97       N  
ATOM   4502  CA  ARG B 235     -34.067 -22.835  45.866  1.00 14.61           C  
ANISOU 4502  CA  ARG B 235     2430   2399    720    266   -272    -56       C  
ATOM   4503  C   ARG B 235     -35.374 -22.242  46.399  1.00 14.63           C  
ANISOU 4503  C   ARG B 235     2582   2345    629    276   -163   -206       C  
ATOM   4504  O   ARG B 235     -36.165 -22.936  47.047  1.00 15.46           O  
ANISOU 4504  O   ARG B 235     2718   2411    742    330   -102     -4       O  
ATOM   4505  CB  ARG B 235     -34.307 -24.178  45.146  1.00 14.15           C  
ANISOU 4505  CB  ARG B 235     2329   2303    744    303   -219    -42       C  
ATOM   4506  CG  ARG B 235     -34.969 -24.054  43.774  1.00 14.80           C  
ANISOU 4506  CG  ARG B 235     2453   2481    687    228   -196    -88       C  
ATOM   4507  CD  ARG B 235     -36.468 -23.833  43.896  1.00 14.92           C  
ANISOU 4507  CD  ARG B 235     2445   2429    794    267   -233    -82       C  
ATOM   4508  NE  ARG B 235     -37.098 -23.820  42.581  1.00 14.20           N  
ANISOU 4508  NE  ARG B 235     2533   2251    609    183    -53   -190       N  
ATOM   4509  CZ  ARG B 235     -38.406 -23.877  42.382  1.00 15.39           C  
ANISOU 4509  CZ  ARG B 235     2554   2553    739    125    -49    -98       C  
ATOM   4510  NH1 ARG B 235     -39.242 -23.929  43.415  1.00 16.06           N  
ANISOU 4510  NH1 ARG B 235     2513   2786    802    205     27   -131       N  
ATOM   4511  NH2 ARG B 235     -38.885 -23.855  41.147  1.00 16.54           N  
ANISOU 4511  NH2 ARG B 235     2971   2551    763    192   -134     27       N  
ATOM   4512  N   GLY B 236     -35.584 -20.960  46.101  1.00 15.06           N  
ANISOU 4512  N   GLY B 236     2705   2356    661    274   -220   -160       N  
ATOM   4513  CA  GLY B 236     -36.745 -20.221  46.588  1.00 16.06           C  
ANISOU 4513  CA  GLY B 236     2747   2524    828    318   -151   -173       C  
ATOM   4514  C   GLY B 236     -38.013 -20.418  45.782  1.00 16.37           C  
ANISOU 4514  C   GLY B 236     2751   2474    994    276   -126   -283       C  
ATOM   4515  O   GLY B 236     -37.983 -20.994  44.701  1.00 16.93           O  
ANISOU 4515  O   GLY B 236     2975   2614    840    151    -62   -195       O  
ATOM   4516  N   GLY B 237     -39.123 -19.903  46.311  1.00 16.56           N  
ANISOU 4516  N   GLY B 237     2855   2457    979    258     -2   -293       N  
ATOM   4517  CA  GLY B 237     -40.445 -20.056  45.709  1.00 17.35           C  
ANISOU 4517  CA  GLY B 237     2666   2560   1363    106     87     19       C  
ATOM   4518  C   GLY B 237     -41.304 -21.020  46.505  1.00 16.35           C  
ANISOU 4518  C   GLY B 237     2874   2508    827    287    131     15       C  
ATOM   4519  O   GLY B 237     -40.792 -22.017  47.032  1.00 16.25           O  
ANISOU 4519  O   GLY B 237     3060   2498    613    336     83     -8       O  
ATOM   4520  N   THR B 238     -42.606 -20.759  46.601  1.00 14.70           N  
ANISOU 4520  N   THR B 238     2893   2213    478    329     50   -282       N  
ATOM   4521  CA  THR B 238     -43.398 -21.695  47.409  1.00 16.55           C  
ANISOU 4521  CA  THR B 238     3111   2503    673     80    176   -262       C  
ATOM   4522  C   THR B 238     -43.476 -23.085  46.806  1.00 15.87           C  
ANISOU 4522  C   THR B 238     2971   2280    778    172    -48     16       C  
ATOM   4523  O   THR B 238     -43.650 -23.265  45.598  1.00 16.19           O  
ANISOU 4523  O   THR B 238     2938   2475    737    241    247   -170       O  
ATOM   4524  CB  THR B 238     -44.722 -21.146  48.024  1.00 19.42           C  
ANISOU 4524  CB  THR B 238     3018   2578   1783    170     90   -144       C  
ATOM   4525  OG1 THR B 238     -45.887 -21.916  47.686  1.00 20.02           O  
ANISOU 4525  OG1 THR B 238     3114   3103   1389    286   -693   -449       O  
ATOM   4526  CG2 THR B 238     -44.948 -19.681  47.821  1.00 14.32           C  
ANISOU 4526  CG2 THR B 238     2457   2601    383    306    230    451       C  
ATOM   4527  N   SER B 239     -43.252 -24.062  47.677  1.00 15.38           N  
ANISOU 4527  N   SER B 239     3060   2102    680    109    137    -36       N  
ATOM   4528  CA  SER B 239     -43.234 -25.471  47.296  1.00 15.14           C  
ANISOU 4528  CA  SER B 239     2879   2028    844    133    -94    167       C  
ATOM   4529  C   SER B 239     -44.566 -25.829  46.667  1.00 15.31           C  
ANISOU 4529  C   SER B 239     2735   2333    749     48    106    -99       C  
ATOM   4530  O   SER B 239     -45.609 -25.668  47.304  1.00 17.08           O  
ANISOU 4530  O   SER B 239     2924   2596    968    100    307    -93       O  
ATOM   4531  CB  SER B 239     -42.980 -26.345  48.535  1.00 16.07           C  
ANISOU 4531  CB  SER B 239     3045   2297    762     71    128    310       C  
ATOM   4532  OG  SER B 239     -41.769 -25.954  49.153  1.00 15.92           O  
ANISOU 4532  OG  SER B 239     3021   2408    618    292    160    123       O  
ATOM   4533  N   PRO B 240     -44.551 -26.296  45.406  1.00 14.52           N  
ANISOU 4533  N   PRO B 240     2463   2350    704    -29    212    -46       N  
ATOM   4534  CA  PRO B 240     -45.824 -26.613  44.755  1.00 15.03           C  
ANISOU 4534  CA  PRO B 240     2515   2524    669    -98    239   -161       C  
ATOM   4535  C   PRO B 240     -46.286 -28.030  45.101  1.00 15.29           C  
ANISOU 4535  C   PRO B 240     2646   2534    625      2    327    -96       C  
ATOM   4536  O   PRO B 240     -46.028 -28.980  44.343  1.00 15.14           O  
ANISOU 4536  O   PRO B 240     2699   2388    662    -64     95   -114       O  
ATOM   4537  CB  PRO B 240     -45.489 -26.476  43.265  1.00 15.49           C  
ANISOU 4537  CB  PRO B 240     2504   2676    703     31    277    -73       C  
ATOM   4538  CG  PRO B 240     -44.051 -26.845  43.181  1.00 15.18           C  
ANISOU 4538  CG  PRO B 240     2554   2706    506     32      5   -191       C  
ATOM   4539  CD  PRO B 240     -43.417 -26.340  44.460  1.00 14.26           C  
ANISOU 4539  CD  PRO B 240     2541   2374    501     31    136   -283       C  
ATOM   4540  N   THR B 241     -46.972 -28.164  46.245  1.00 15.47           N  
ANISOU 4540  N   THR B 241     2726   2454    698    -40    400    -92       N  
ATOM   4541  CA  THR B 241     -47.239 -29.508  46.817  1.00 15.93           C  
ANISOU 4541  CA  THR B 241     2858   2292    901   -161    247   -231       C  
ATOM   4542  C   THR B 241     -47.859 -30.522  45.835  1.00 15.58           C  
ANISOU 4542  C   THR B 241     2700   2382    835    -72    221   -241       C  
ATOM   4543  O   THR B 241     -47.381 -31.657  45.768  1.00 15.31           O  
ANISOU 4543  O   THR B 241     2854   2410    551    -21    222   -273       O  
ATOM   4544  CB  THR B 241     -47.777 -29.490  48.295  1.00 18.25           C  
ANISOU 4544  CB  THR B 241     2989   2645   1300    -21    766   -217       C  
ATOM   4545  OG1 THR B 241     -48.751 -30.527  48.589  1.00 21.71           O  
ANISOU 4545  OG1 THR B 241     3125   3201   1921   -470    492   -437       O  
ATOM   4546  CG2 THR B 241     -48.178 -28.089  48.751  1.00 13.79           C  
ANISOU 4546  CG2 THR B 241     2475   2413    352      3    465     56       C  
ATOM   4547  N   PRO B 242     -48.851 -30.100  45.020  1.00 15.16           N  
ANISOU 4547  N   PRO B 242     2862   2401    496   -132    231   -245       N  
ATOM   4548  CA  PRO B 242     -49.424 -31.083  44.091  1.00 15.85           C  
ANISOU 4548  CA  PRO B 242     2882   2533    606     26    103   -348       C  
ATOM   4549  C   PRO B 242     -48.384 -31.630  43.105  1.00 15.84           C  
ANISOU 4549  C   PRO B 242     2799   2449    769     83    195   -120       C  
ATOM   4550  O   PRO B 242     -48.334 -32.833  42.891  1.00 16.04           O  
ANISOU 4550  O   PRO B 242     2917   2515    659    -26    284   -266       O  
ATOM   4551  CB  PRO B 242     -50.498 -30.291  43.343  1.00 16.79           C  
ANISOU 4551  CB  PRO B 242     2865   2781    732    -20    -21   -306       C  
ATOM   4552  CG  PRO B 242     -50.726 -29.060  44.131  1.00 17.23           C  
ANISOU 4552  CG  PRO B 242     2754   2681   1108      2    132   -306       C  
ATOM   4553  CD  PRO B 242     -49.450 -28.764  44.845  1.00 15.95           C  
ANISOU 4553  CD  PRO B 242     2725   2635    700    -20    126    -88       C  
ATOM   4554  N   LEU B 243     -47.540 -30.760  42.546  1.00 15.05           N  
ANISOU 4554  N   LEU B 243     2652   2421    644     71     87   -213       N  
ATOM   4555  CA  LEU B 243     -46.476 -31.177  41.607  1.00 14.77           C  
ANISOU 4555  CA  LEU B 243     2699   2282    629    171     74   -119       C  
ATOM   4556  C   LEU B 243     -45.432 -32.101  42.260  1.00 15.23           C  
ANISOU 4556  C   LEU B 243     2792   2263    730    163    -12   -187       C  
ATOM   4557  O   LEU B 243     -44.990 -33.107  41.669  1.00 15.27           O  
ANISOU 4557  O   LEU B 243     2959   2124    716    301    -72    -25       O  
ATOM   4558  CB  LEU B 243     -45.791 -29.958  41.006  1.00 15.16           C  
ANISOU 4558  CB  LEU B 243     2681   2413    665    106     63    -54       C  
ATOM   4559  CG  LEU B 243     -46.701 -29.018  40.205  1.00 14.84           C  
ANISOU 4559  CG  LEU B 243     2525   2199    913    157    106   -129       C  
ATOM   4560  CD1 LEU B 243     -45.931 -27.783  39.786  1.00 14.56           C  
ANISOU 4560  CD1 LEU B 243     2436   2342    751     48    -12    -94       C  
ATOM   4561  CD2 LEU B 243     -47.321 -29.671  38.976  1.00 16.23           C  
ANISOU 4561  CD2 LEU B 243     2718   2458    990    -39    -27   -109       C  
ATOM   4562  N   ILE B 244     -45.065 -31.776  43.494  1.00 14.26           N  
ANISOU 4562  N   ILE B 244     2763   2108    547    -48    120     66       N  
ATOM   4563  CA  ILE B 244     -44.109 -32.587  44.236  1.00 15.45           C  
ANISOU 4563  CA  ILE B 244     2831   2238    801    111     -7   -156       C  
ATOM   4564  C   ILE B 244     -44.698 -33.975  44.538  1.00 15.64           C  
ANISOU 4564  C   ILE B 244     3026   2279    636    127    202    -96       C  
ATOM   4565  O   ILE B 244     -44.063 -34.999  44.281  1.00 15.81           O  
ANISOU 4565  O   ILE B 244     3146   2314    547     84    381   -143       O  
ATOM   4566  CB  ILE B 244     -43.671 -31.859  45.528  1.00 15.47           C  
ANISOU 4566  CB  ILE B 244     2839   2331    705     87    -50    -90       C  
ATOM   4567  CG1 ILE B 244     -42.739 -30.672  45.228  1.00 14.93           C  
ANISOU 4567  CG1 ILE B 244     2878   2066    728    235    143   -139       C  
ATOM   4568  CG2 ILE B 244     -42.940 -32.796  46.476  1.00 15.95           C  
ANISOU 4568  CG2 ILE B 244     3035   2106    919    203     59    -35       C  
ATOM   4569  CD1 ILE B 244     -42.694 -29.642  46.352  1.00 15.84           C  
ANISOU 4569  CD1 ILE B 244     2961   2307    747     14    161   -256       C  
ATOM   4570  N   VAL B 245     -45.921 -34.002  45.068  1.00 16.14           N  
ANISOU 4570  N   VAL B 245     3019   2408    703     36    163   -136       N  
ATOM   4571  CA  VAL B 245     -46.635 -35.257  45.349  1.00 16.18           C  
ANISOU 4571  CA  VAL B 245     3142   2435    571    -57    108   -220       C  
ATOM   4572  C   VAL B 245     -46.749 -36.117  44.072  1.00 16.92           C  
ANISOU 4572  C   VAL B 245     3338   2399    689     88    144   -291       C  
ATOM   4573  O   VAL B 245     -46.455 -37.313  44.084  1.00 17.56           O  
ANISOU 4573  O   VAL B 245     3388   2440    844      8    261   -156       O  
ATOM   4574  CB  VAL B 245     -48.010 -34.995  46.032  1.00 16.97           C  
ANISOU 4574  CB  VAL B 245     3094   2470    881    -40     84   -391       C  
ATOM   4575  CG1 VAL B 245     -48.834 -36.275  46.136  1.00 18.46           C  
ANISOU 4575  CG1 VAL B 245     3186   2760   1069   -189    198   -158       C  
ATOM   4576  CG2 VAL B 245     -47.810 -34.397  47.431  1.00 17.77           C  
ANISOU 4576  CG2 VAL B 245     3156   2767    828    164    121   -453       C  
ATOM   4577  N   GLY B 246     -47.135 -35.494  42.966  1.00 16.47           N  
ANISOU 4577  N   GLY B 246     3210   2411    637    -87    219   -179       N  
ATOM   4578  CA  GLY B 246     -47.292 -36.217  41.716  1.00 18.24           C  
ANISOU 4578  CA  GLY B 246     3430   2741    758     36    234   -392       C  
ATOM   4579  C   GLY B 246     -45.991 -36.809  41.237  1.00 17.57           C  
ANISOU 4579  C   GLY B 246     3357   2531    784     12    154   -249       C  
ATOM   4580  O   GLY B 246     -45.980 -37.926  40.711  1.00 17.91           O  
ANISOU 4580  O   GLY B 246     3602   2409    795     -8    227   -135       O  
ATOM   4581  N   LEU B 247     -44.900 -36.069  41.418  1.00 16.76           N  
ANISOU 4581  N   LEU B 247     3171   2306    891     86    211   -211       N  
ATOM   4582  CA  LEU B 247     -43.594 -36.568  41.013  1.00 16.23           C  
ANISOU 4582  CA  LEU B 247     3243   2335    585    114    266   -168       C  
ATOM   4583  C   LEU B 247     -43.214 -37.810  41.824  1.00 17.34           C  
ANISOU 4583  C   LEU B 247     3502   2295    789     53    424    -53       C  
ATOM   4584  O   LEU B 247     -42.703 -38.772  41.275  1.00 17.24           O  
ANISOU 4584  O   LEU B 247     3607   2357    583    -30    285   -184       O  
ATOM   4585  CB  LEU B 247     -42.525 -35.486  41.138  1.00 16.23           C  
ANISOU 4585  CB  LEU B 247     3173   2346    646     45    520     14       C  
ATOM   4586  CG  LEU B 247     -41.088 -35.908  40.808  1.00 16.42           C  
ANISOU 4586  CG  LEU B 247     3281   2136    820    156    406      0       C  
ATOM   4587  CD1 LEU B 247     -40.961 -36.501  39.409  1.00 17.99           C  
ANISOU 4587  CD1 LEU B 247     3447   2429    960    292    332   -227       C  
ATOM   4588  CD2 LEU B 247     -40.177 -34.703  40.958  1.00 17.43           C  
ANISOU 4588  CD2 LEU B 247     3311   2256   1055     77    287      7       C  
ATOM   4589  N   GLY B 248     -43.475 -37.796  43.127  1.00 17.21           N  
ANISOU 4589  N   GLY B 248     3525   2278    734     55    302     58       N  
ATOM   4590  CA  GLY B 248     -43.206 -38.983  43.941  1.00 16.61           C  
ANISOU 4590  CA  GLY B 248     3649   2243    417    -28    378      2       C  
ATOM   4591  C   GLY B 248     -43.977 -40.205  43.462  1.00 17.70           C  
ANISOU 4591  C   GLY B 248     3721   2482    522    -73    352   -219       C  
ATOM   4592  O   GLY B 248     -43.427 -41.304  43.420  1.00 18.12           O  
ANISOU 4592  O   GLY B 248     3817   2516    548    -25    472   -108       O  
ATOM   4593  N   VAL B 249     -45.240 -40.011  43.096  1.00 17.57           N  
ANISOU 4593  N   VAL B 249     3583   2593    497    -81    438   -192       N  
ATOM   4594  CA  VAL B 249     -46.105 -41.114  42.665  1.00 19.02           C  
ANISOU 4594  CA  VAL B 249     3739   2628    857   -255    493    -19       C  
ATOM   4595  C   VAL B 249     -45.620 -41.661  41.336  1.00 19.34           C  
ANISOU 4595  C   VAL B 249     3895   2634    817   -268    482    -15       C  
ATOM   4596  O   VAL B 249     -45.631 -42.869  41.113  1.00 18.23           O  
ANISOU 4596  O   VAL B 249     3920   2644    361   -270    575    100       O  
ATOM   4597  CB  VAL B 249     -47.580 -40.656  42.587  1.00 20.45           C  
ANISOU 4597  CB  VAL B 249     3705   3040   1024   -259    547   -232       C  
ATOM   4598  CG1 VAL B 249     -48.519 -41.711  41.938  1.00 23.59           C  
ANISOU 4598  CG1 VAL B 249     4347   3444   1172   -438    229   -419       C  
ATOM   4599  CG2 VAL B 249     -48.042 -40.297  43.991  1.00 20.93           C  
ANISOU 4599  CG2 VAL B 249     4042   2903   1006   -233    581   -193       C  
ATOM   4600  N   ALA B 250     -45.176 -40.757  40.462  1.00 18.92           N  
ANISOU 4600  N   ALA B 250     3721   2652    815   -210    541    -32       N  
ATOM   4601  CA  ALA B 250     -44.641 -41.139  39.157  1.00 18.46           C  
ANISOU 4601  CA  ALA B 250     3832   2433    747   -221    553     75       C  
ATOM   4602  C   ALA B 250     -43.416 -42.026  39.310  1.00 17.90           C  
ANISOU 4602  C   ALA B 250     3815   2288    699   -258    503     42       C  
ATOM   4603  O   ALA B 250     -43.300 -43.044  38.635  1.00 19.05           O  
ANISOU 4603  O   ALA B 250     4025   2381    831   -151    349    -69       O  
ATOM   4604  CB  ALA B 250     -44.297 -39.900  38.336  1.00 17.81           C  
ANISOU 4604  CB  ALA B 250     3780   2390    597   -185    490    -13       C  
ATOM   4605  N   VAL B 251     -42.505 -41.634  40.203  1.00 17.54           N  
ANISOU 4605  N   VAL B 251     3650   2452    563   -176    604      2       N  
ATOM   4606  CA  VAL B 251     -41.265 -42.382  40.450  1.00 18.34           C  
ANISOU 4606  CA  VAL B 251     3765   2401    800    -58    440   -137       C  
ATOM   4607  C   VAL B 251     -41.602 -43.761  41.016  1.00 19.50           C  
ANISOU 4607  C   VAL B 251     3883   2572    954    -45    670     13       C  
ATOM   4608  O   VAL B 251     -41.084 -44.789  40.564  1.00 20.64           O  
ANISOU 4608  O   VAL B 251     4061   2620   1162    120    500    -67       O  
ATOM   4609  CB  VAL B 251     -40.316 -41.590  41.393  1.00 18.49           C  
ANISOU 4609  CB  VAL B 251     3556   2459   1008    -13    286     -4       C  
ATOM   4610  CG1 VAL B 251     -39.134 -42.436  41.843  1.00 19.65           C  
ANISOU 4610  CG1 VAL B 251     3925   2484   1054    168     75    -36       C  
ATOM   4611  CG2 VAL B 251     -39.820 -40.316  40.708  1.00 17.75           C  
ANISOU 4611  CG2 VAL B 251     3649   2284    811    -36    434   -278       C  
ATOM   4612  N   GLU B 252     -42.482 -43.775  42.006  1.00 19.18           N  
ANISOU 4612  N   GLU B 252     3885   2742    657   -135    531   -131       N  
ATOM   4613  CA  GLU B 252     -42.794 -45.014  42.664  1.00 19.89           C  
ANISOU 4613  CA  GLU B 252     4090   2567    897     -2    656   -225       C  
ATOM   4614  C   GLU B 252     -43.444 -46.043  41.751  1.00 21.65           C  
ANISOU 4614  C   GLU B 252     4166   3019   1037   -284    468   -234       C  
ATOM   4615  O   GLU B 252     -43.177 -47.228  41.902  1.00 23.64           O  
ANISOU 4615  O   GLU B 252     4469   3094   1417   -283    419   -276       O  
ATOM   4616  CB  GLU B 252     -43.668 -44.783  43.898  1.00 22.97           C  
ANISOU 4616  CB  GLU B 252     4335   3216   1175    -46   1000    -73       C  
ATOM   4617  CG  GLU B 252     -43.855 -46.040  44.731  1.00 26.06           C  
ANISOU 4617  CG  GLU B 252     4705   3721   1473     86    884    321       C  
ATOM   4618  CD  GLU B 252     -44.224 -45.702  46.187  1.00 32.92           C  
ANISOU 4618  CD  GLU B 252     5346   5029   2133   1017   1388   -510       C  
ATOM   4619  OE1 GLU B 252     -45.029 -44.766  46.359  1.00 31.56           O  
ANISOU 4619  OE1 GLU B 252     5028   4218   2745    336   1364   -810       O  
ATOM   4620  OE2 GLU B 252     -43.688 -46.288  47.172  1.00 41.74           O  
ANISOU 4620  OE2 GLU B 252     6403   6512   2941   1025   1597    606       O  
ATOM   4621  N   HIS B 253     -44.306 -45.600  40.837  1.00 21.11           N  
ANISOU 4621  N   HIS B 253     4178   2772   1069   -244    442   -137       N  
ATOM   4622  CA  HIS B 253     -45.044 -46.510  39.946  1.00 21.58           C  
ANISOU 4622  CA  HIS B 253     4058   3102   1038   -362    574   -280       C  
ATOM   4623  C   HIS B 253     -44.551 -46.506  38.511  1.00 20.00           C  
ANISOU 4623  C   HIS B 253     3839   2765    994   -281    486    -31       C  
ATOM   4624  O   HIS B 253     -45.308 -46.768  37.574  1.00 21.24           O  
ANISOU 4624  O   HIS B 253     3828   2815   1428   -290    206    -63       O  
ATOM   4625  CB  HIS B 253     -46.543 -46.199  39.994  1.00 25.03           C  
ANISOU 4625  CB  HIS B 253     3970   3502   2038   -470    556   -417       C  
ATOM   4626  CG  HIS B 253     -47.142 -46.298  41.374  1.00 27.94           C  
ANISOU 4626  CG  HIS B 253     4480   3911   2225   -473    869   -487       C  
ATOM   4627  ND1 HIS B 253     -47.413 -47.484  41.964  1.00 31.57           N  
ANISOU 4627  ND1 HIS B 253     4909   4320   2763   -504    946   -129       N  
ATOM   4628  CD2 HIS B 253     -47.507 -45.307  42.290  1.00 29.14           C  
ANISOU 4628  CD2 HIS B 253     4764   4112   2197   -497   1016   -627       C  
ATOM   4629  CE1 HIS B 253     -47.930 -47.266  43.190  1.00 32.07           C  
ANISOU 4629  CE1 HIS B 253     4979   4584   2620   -786   1211    377       C  
ATOM   4630  NE2 HIS B 253     -47.989 -45.936  43.387  1.00 36.37           N  
ANISOU 4630  NE2 HIS B 253     6067   4826   2926   -852   1443   -184       N  
ATOM   4631  N   PHE B 254     -43.278 -46.207  38.325  1.00 19.08           N  
ANISOU 4631  N   PHE B 254     3746   2699    805   -237    364   -102       N  
ATOM   4632  CA  PHE B 254     -42.722 -46.085  36.989  1.00 18.85           C  
ANISOU 4632  CA  PHE B 254     3598   2674    888   -205    396     51       C  
ATOM   4633  C   PHE B 254     -42.840 -47.417  36.241  1.00 19.02           C  
ANISOU 4633  C   PHE B 254     3680   2567    979   -195     23    111       C  
ATOM   4634  O   PHE B 254     -42.616 -48.459  36.815  1.00 19.24           O  
ANISOU 4634  O   PHE B 254     3776   2571    961   -278    188    207       O  
ATOM   4635  CB  PHE B 254     -41.269 -45.684  37.113  1.00 18.08           C  
ANISOU 4635  CB  PHE B 254     3557   2584    726   -209    270     28       C  
ATOM   4636  CG  PHE B 254     -40.635 -45.314  35.829  1.00 17.58           C  
ANISOU 4636  CG  PHE B 254     3389   2517    770   -172    271     23       C  
ATOM   4637  CD1 PHE B 254     -39.741 -46.168  35.222  1.00 17.78           C  
ANISOU 4637  CD1 PHE B 254     3485   2542    729   -212    222   -126       C  
ATOM   4638  CD2 PHE B 254     -40.928 -44.102  35.235  1.00 17.15           C  
ANISOU 4638  CD2 PHE B 254     3286   2539    691   -136     79    -35       C  
ATOM   4639  CE1 PHE B 254     -39.141 -45.812  34.039  1.00 17.39           C  
ANISOU 4639  CE1 PHE B 254     3473   2469    666    -72    183    -99       C  
ATOM   4640  CE2 PHE B 254     -40.333 -43.749  34.045  1.00 16.88           C  
ANISOU 4640  CE2 PHE B 254     3114   2465    831   -111    243   -192       C  
ATOM   4641  CZ  PHE B 254     -39.430 -44.600  33.442  1.00 16.79           C  
ANISOU 4641  CZ  PHE B 254     3342   2366    669     17     35   -292       C  
ATOM   4642  N   PRO B 255     -43.186 -47.364  34.957  1.00 19.40           N  
ANISOU 4642  N   PRO B 255     3874   2619    876   -144    176    110       N  
ATOM   4643  CA  PRO B 255     -43.522 -48.586  34.301  1.00 19.19           C  
ANISOU 4643  CA  PRO B 255     3996   2473    821   -174    253    247       C  
ATOM   4644  C   PRO B 255     -42.400 -49.512  34.348  1.00 21.44           C  
ANISOU 4644  C   PRO B 255     4042   2935   1170    -66    244    433       C  
ATOM   4645  O   PRO B 255     -41.214 -49.188  34.265  1.00 19.98           O  
ANISOU 4645  O   PRO B 255     3998   2660    931   -160    154    122       O  
ATOM   4646  CB  PRO B 255     -43.778 -48.158  32.871  1.00 18.32           C  
ANISOU 4646  CB  PRO B 255     3634   2402    922   -128   -106    179       C  
ATOM   4647  CG  PRO B 255     -44.390 -46.823  33.050  1.00 18.99           C  
ANISOU 4647  CG  PRO B 255     3744   2489    980    -74     78     -8       C  
ATOM   4648  CD  PRO B 255     -43.598 -46.204  34.164  1.00 18.50           C  
ANISOU 4648  CD  PRO B 255     3691   2533    803   -114    163     59       C  
ATOM   4649  N   SER B 256     -42.772 -50.719  34.580  1.00 23.80           N  
ANISOU 4649  N   SER B 256     4313   3024   1703   -178    120    390       N  
ATOM   4650  CA  SER B 256     -41.751 -51.651  34.514  1.00 25.64           C  
ANISOU 4650  CA  SER B 256     4768   2921   2052   -177    310   -622       C  
ATOM   4651  C   SER B 256     -42.135 -53.001  34.907  1.00 30.51           C  
ANISOU 4651  C   SER B 256     5079   3658   2855   -403    845    123       C  
ATOM   4652  O   SER B 256     -43.054 -53.280  35.549  1.00 25.65           O  
ANISOU 4652  O   SER B 256     5995   3121    630   -263    803    831       O  
ATOM   4653  CB  SER B 256     -40.528 -51.222  35.303  1.00 29.29           C  
ANISOU 4653  CB  SER B 256     4787   3946   2392    -57    -71     -1       C  
ATOM   4654  N   GLU B 257     -41.407 -53.832  34.243  1.00 34.57           N  
ANISOU 4654  N   GLU B 257     5190   4538   3407   -216   1096    -75       N  
ATOM   4655  CA  GLU B 257     -40.670 -53.178  33.249  1.00 26.65           C  
ANISOU 4655  CA  GLU B 257     5670   3642    811   -296     90   -437       C  
ATOM   4656  C   GLU B 257     -41.776 -52.850  32.295  1.00 27.09           C  
ANISOU 4656  C   GLU B 257     4775   3174   2343   -145    400   -246       C  
ATOM   4657  O   GLU B 257     -42.571 -51.930  32.386  1.00 30.00           O  
ANISOU 4657  O   GLU B 257     5006   3659   2733     64    621    -34       O  
ATOM   4658  CB  GLU B 257     -39.765 -54.178  32.620  1.00 31.64           C  
ANISOU 4658  CB  GLU B 257     5367   3684   2971    144    -31    -44       C  
ATOM   4659  N   ALA B 258     -41.800 -53.772  31.354  1.00 31.79           N  
ANISOU 4659  N   ALA B 258     5798   4587   1691    -80     82   -585       N  
ATOM   4660  CA  ALA B 258     -42.779 -53.918  30.378  1.00 29.01           C  
ANISOU 4660  CA  ALA B 258     4936   4140   1946     83    399    -48       C  
ATOM   4661  C   ALA B 258     -42.705 -52.698  29.526  1.00 25.84           C  
ANISOU 4661  C   ALA B 258     4626   3773   1418    129    626   -297       C  
ATOM   4662  O   ALA B 258     -43.126 -51.607  29.859  1.00 22.48           O  
ANISOU 4662  O   ALA B 258     4413   3389    740   -216    365   -108       O  
ATOM   4663  CB  ALA B 258     -44.173 -54.167  30.960  1.00 28.39           C  
ANISOU 4663  CB  ALA B 258     5141   3839   1804   -181    719   -609       C  
ATOM   4664  N   SER B 259     -42.131 -52.918  28.374  1.00 22.50           N  
ANISOU 4664  N   SER B 259     4382   2886   1281     82    455   -321       N  
ATOM   4665  CA  SER B 259     -42.293 -51.950  27.353  1.00 24.28           C  
ANISOU 4665  CA  SER B 259     4472   3380   1371     94    243    -37       C  
ATOM   4666  C   SER B 259     -43.752 -51.924  27.028  1.00 23.98           C  
ANISOU 4666  C   SER B 259     4389   3245   1476     92    313   -158       C  
ATOM   4667  O   SER B 259     -44.460 -52.836  27.263  1.00 23.60           O  
ANISOU 4667  O   SER B 259     4250   3417   1300    169    202   -257       O  
ATOM   4668  CB  SER B 259     -41.553 -52.317  26.114  1.00 26.52           C  
ANISOU 4668  CB  SER B 259     4550   3745   1780    309    274   -571       C  
ATOM   4669  OG  SER B 259     -40.832 -53.395  26.230  1.00 32.12           O  
ANISOU 4669  OG  SER B 259     5677   3817   2709    497    221   -140       O  
ATOM   4670  N   ALA B 260     -44.183 -50.839  26.444  1.00 22.60           N  
ANISOU 4670  N   ALA B 260     4306   3189   1089     -6     58    -88       N  
ATOM   4671  CA  ALA B 260     -45.556 -50.623  26.025  1.00 22.09           C  
ANISOU 4671  CA  ALA B 260     4165   2784   1441   -109    203     25       C  
ATOM   4672  C   ALA B 260     -45.973 -51.538  24.891  1.00 24.06           C  
ANISOU 4672  C   ALA B 260     4277   2759   2103     73   -334   -213       C  
ATOM   4673  O   ALA B 260     -45.142 -52.132  24.217  1.00 24.71           O  
ANISOU 4673  O   ALA B 260     4538   3034   1814    -23   -253   -436       O  
ATOM   4674  CB  ALA B 260     -45.689 -49.211  25.545  1.00 22.29           C  
ANISOU 4674  CB  ALA B 260     3928   2247   2293     22   -620   -529       C  
ATOM   4675  N   GLN B 261     -47.261 -51.594  24.608  1.00 24.75           N  
ANISOU 4675  N   GLN B 261     4263   3384   1755   -233    -29    -60       N  
ATOM   4676  CA  GLN B 261     -47.675 -52.287  23.406  1.00 26.77           C  
ANISOU 4676  CA  GLN B 261     4311   3633   2225   -348   -323   -351       C  
ATOM   4677  C   GLN B 261     -47.132 -51.577  22.157  1.00 26.84           C  
ANISOU 4677  C   GLN B 261     4506   3442   2248   -318   -367   -177       C  
ATOM   4678  O   GLN B 261     -47.065 -52.178  21.115  1.00 27.94           O  
ANISOU 4678  O   GLN B 261     4699   3648   2266   -406   -517   -293       O  
ATOM   4679  CB  GLN B 261     -49.190 -52.356  23.346  1.00 27.28           C  
ANISOU 4679  CB  GLN B 261     4322   3881   2162   -204    -33   -456       C  
ATOM   4680  N   GLN B 262     -47.044 -50.261  22.301  1.00 25.91           N  
ANISOU 4680  N   GLN B 262     4415   3360   2070      6   -357     -8       N  
ATOM   4681  CA  GLN B 262     -46.827 -49.337  21.248  1.00 25.55           C  
ANISOU 4681  CA  GLN B 262     4521   3068   2116    -42   -409    -27       C  
ATOM   4682  C   GLN B 262     -45.450 -49.613  20.762  1.00 25.18           C  
ANISOU 4682  C   GLN B 262     4591   3662   1313     44   -390      7       C  
ATOM   4683  O   GLN B 262     -45.208 -49.586  19.599  1.00 25.60           O  
ANISOU 4683  O   GLN B 262     4703   3795   1225      4   -478    -35       O  
ATOM   4684  CB  GLN B 262     -46.940 -47.911  21.767  1.00 23.90           C  
ANISOU 4684  CB  GLN B 262     4437   3270   1373   -237   -103   -226       C  
ATOM   4685  CG  GLN B 262     -46.497 -46.902  20.748  1.00 24.95           C  
ANISOU 4685  CG  GLN B 262     4652   2994   1832   -125   -341     18       C  
ATOM   4686  CD  GLN B 262     -46.816 -45.499  21.152  1.00 22.96           C  
ANISOU 4686  CD  GLN B 262     4129   3251   1343   -161    185   -156       C  
ATOM   4687  OE1 GLN B 262     -47.155 -45.233  22.298  1.00 21.69           O  
ANISOU 4687  OE1 GLN B 262     3786   3227   1225   -297     36   -115       O  
ATOM   4688  NE2 GLN B 262     -46.710 -44.584  20.206  1.00 23.17           N  
ANISOU 4688  NE2 GLN B 262     4112   3240   1451   -257   -238    -26       N  
ATOM   4689  N   THR B 263     -44.530 -49.900  21.671  1.00 24.28           N  
ANISOU 4689  N   THR B 263     4222   3306   1696   -261   -476   -206       N  
ATOM   4690  CA  THR B 263     -43.163 -50.251  21.293  1.00 25.75           C  
ANISOU 4690  CA  THR B 263     4289   3647   1847     32   -488   -234       C  
ATOM   4691  C   THR B 263     -43.400 -51.552  20.569  1.00 28.50           C  
ANISOU 4691  C   THR B 263     4898   3560   2370    -33   -514   -236       C  
ATOM   4692  O   THR B 263     -44.123 -52.343  21.076  1.00 31.55           O  
ANISOU 4692  O   THR B 263     4892   4241   2853   -209   -609    -23       O  
ATOM   4693  CB  THR B 263     -42.310 -50.440  22.533  1.00 27.01           C  
ANISOU 4693  CB  THR B 263     4621   3967   1674    -63   -386    -57       C  
ATOM   4694  OG1 THR B 263     -41.013 -50.991  22.213  1.00 31.81           O  
ANISOU 4694  OG1 THR B 263     5171   4573   2340    483   -127   -109       O  
ATOM   4695  CG2 THR B 263     -43.032 -51.289  23.419  1.00 27.54           C  
ANISOU 4695  CG2 THR B 263     4511   3797   2155    -55   -319    -88       C  
ATOM   4696  N   GLU B 264     -42.760 -51.774  19.418  1.00 27.59           N  
ANISOU 4696  N   GLU B 264     4782   3295   2404     -6   -376   -258       N  
ATOM   4697  CA  GLU B 264     -43.361 -52.498  18.233  1.00 32.64           C  
ANISOU 4697  CA  GLU B 264     5533   4018   2850    -76   -874   -322       C  
ATOM   4698  C   GLU B 264     -44.598 -51.858  17.521  1.00 32.19           C  
ANISOU 4698  C   GLU B 264     5111   4001   3118   -278   -623   -188       C  
ATOM   4699  O   GLU B 264     -45.660 -52.492  17.454  1.00 37.36           O  
ANISOU 4699  O   GLU B 264     5144   4407   4643   -397   -763   -906       O  
ATOM   4700  CB  GLU B 264     -43.709 -53.944  18.612  1.00 33.78           C  
ANISOU 4700  CB  GLU B 264     5527   3900   3407   -297   -331   -385       C  
ATOM   4701  CG  GLU B 264     -44.874 -54.036  19.570  1.00 36.13           C  
ANISOU 4701  CG  GLU B 264     5634   4363   3731   -172   -118   -400       C  
ATOM   4702  CD  GLU B 264     -44.591 -54.809  20.876  1.00 37.39           C  
ANISOU 4702  CD  GLU B 264     5846   4876   3482    448    126   -491       C  
ATOM   4703  OE1 GLU B 264     -43.588 -55.537  21.063  1.00 41.40           O  
ANISOU 4703  OE1 GLU B 264     6249   5431   4050    501   -321    166       O  
ATOM   4704  OE2 GLU B 264     -45.421 -54.718  21.778  1.00 35.49           O  
ANISOU 4704  OE2 GLU B 264     5718   4217   3547     74    167   -287       O  
ATOM   4705  N   PHE B 265     -44.496 -50.650  16.979  1.00 26.42           N  
ANISOU 4705  N   PHE B 265     4349   3982   1706    276   -354   -221       N  
ATOM   4706  CA  PHE B 265     -43.268 -50.033  16.504  1.00 24.77           C  
ANISOU 4706  CA  PHE B 265     4407   3178   1825   -103   -763   -538       C  
ATOM   4707  C   PHE B 265     -42.135 -50.947  16.040  1.00 25.67           C  
ANISOU 4707  C   PHE B 265     4580   3521   1652    -33   -391   -598       C  
ATOM   4708  O   PHE B 265     -41.688 -50.796  14.923  1.00 25.23           O  
ANISOU 4708  O   PHE B 265     4492   3551   1539      4   -367   -825       O  
ATOM   4709  CB  PHE B 265     -42.730 -48.964  17.459  1.00 24.14           C  
ANISOU 4709  CB  PHE B 265     4509   3056   1607   -127   -361   -584       C  
ATOM   4710  CG  PHE B 265     -41.403 -48.450  17.056  1.00 23.62           C  
ANISOU 4710  CG  PHE B 265     4491   2941   1540     76   -258   -385       C  
ATOM   4711  CD1 PHE B 265     -41.294 -47.529  16.048  1.00 22.77           C  
ANISOU 4711  CD1 PHE B 265     4376   2960   1313    229    -11   -492       C  
ATOM   4712  CD2 PHE B 265     -40.254 -48.928  17.638  1.00 22.70           C  
ANISOU 4712  CD2 PHE B 265     4426   2863   1337     41   -307   -400       C  
ATOM   4713  CE1 PHE B 265     -40.070 -47.058  15.657  1.00 21.41           C  
ANISOU 4713  CE1 PHE B 265     4151   2861   1122    213   -127   -643       C  
ATOM   4714  CE2 PHE B 265     -39.021 -48.480  17.238  1.00 22.59           C  
ANISOU 4714  CE2 PHE B 265     4352   3047   1184    255   -164   -195       C  
ATOM   4715  CZ  PHE B 265     -38.924 -47.538  16.241  1.00 21.63           C  
ANISOU 4715  CZ  PHE B 265     4262   2740   1216     81   -206   -327       C  
ATOM   4716  N   GLU B 266     -41.652 -51.863  16.874  1.00 27.21           N  
ANISOU 4716  N   GLU B 266     4725   3590   2024   -170   -497   -177       N  
ATOM   4717  CA  GLU B 266     -40.461 -52.667  16.538  1.00 28.57           C  
ANISOU 4717  CA  GLU B 266     5020   3852   1981     62   -421   -329       C  
ATOM   4718  C   GLU B 266     -40.673 -53.491  15.274  1.00 28.19           C  
ANISOU 4718  C   GLU B 266     4469   3936   2302   -622   -447   -435       C  
ATOM   4719  O   GLU B 266     -39.747 -53.631  14.476  1.00 32.28           O  
ANISOU 4719  O   GLU B 266     5489   4269   2507    -47     96   -728       O  
ATOM   4720  CB  GLU B 266     -40.034 -53.534  17.725  1.00 29.74           C  
ANISOU 4720  CB  GLU B 266     5221   3938   2141     87   -614   -246       C  
ATOM   4721  CG  GLU B 266     -39.192 -52.779  18.747  1.00 31.24           C  
ANISOU 4721  CG  GLU B 266     5580   4139   2147    -63   -634   -400       C  
ATOM   4722  CD  GLU B 266     -39.111 -53.455  20.102  1.00 33.30           C  
ANISOU 4722  CD  GLU B 266     5809   4530   2312    100   -988   -217       C  
ATOM   4723  OE1 GLU B 266     -39.779 -54.478  20.321  1.00 34.53           O  
ANISOU 4723  OE1 GLU B 266     6207   4656   2255    111   -782    227       O  
ATOM   4724  OE2 GLU B 266     -38.350 -52.975  20.968  1.00 31.85           O  
ANISOU 4724  OE2 GLU B 266     6162   4356   1583    230   -487   -684       O  
ATOM   4725  N   LYS B 267     -41.952 -53.866  15.091  1.00 24.07           N  
ANISOU 4725  N   LYS B 267     5064   2656   1424  -1088  -1091   -998       N  
ATOM   4726  CA ALYS B 267     -42.494 -54.598  13.970  0.50 23.49           C  
ANISOU 4726  CA ALYS B 267     4524   2915   1486  -1089   -973  -1304       C  
ATOM   4727  CA BLYS B 267     -42.506 -54.592  13.956  0.50 23.72           C  
ANISOU 4727  CA BLYS B 267     4568   2976   1467  -1071  -1008  -1300       C  
ATOM   4728  C   LYS B 267     -43.144 -53.775  12.868  1.00 30.45           C  
ANISOU 4728  C   LYS B 267     5157   4310   2102    -89   -685   -661       C  
ATOM   4729  O   LYS B 267     -43.837 -54.375  12.110  1.00 35.14           O  
ANISOU 4729  O   LYS B 267     5263   4975   3112   -327   -708  -1075       O  
ATOM   4730  CB ALYS B 267     -43.605 -55.525  14.456  0.50 29.71           C  
ANISOU 4730  CB ALYS B 267     4803   4024   2459   -833   -309   -649       C  
ATOM   4731  CB BLYS B 267     -43.632 -55.494  14.422  0.50 29.21           C  
ANISOU 4731  CB BLYS B 267     4776   3972   2350   -653   -385   -514       C  
ATOM   4732  CG ALYS B 267     -43.176 -56.729  15.300  0.50 31.61           C  
ANISOU 4732  CG ALYS B 267     5381   4462   2168   -506   -305   -501       C  
ATOM   4733  CG BLYS B 267     -43.161 -56.720  15.166  0.50 31.89           C  
ANISOU 4733  CG BLYS B 267     5627   4591   1897   -126   -562   -353       C  
ATOM   4734  CD ALYS B 267     -43.344 -56.557  16.823  0.50 30.68           C  
ANISOU 4734  CD ALYS B 267     5754   3712   2189   -397   -410   -737       C  
ATOM   4735  CD BLYS B 267     -44.109 -57.115  16.293  0.50 31.03           C  
ANISOU 4735  CD BLYS B 267     5798   4017   1972    408   -357   -323       C  
ATOM   4736  CE ALYS B 267     -42.012 -56.517  17.582  0.50 31.36           C  
ANISOU 4736  CE ALYS B 267     5697   3839   2377   -336   -408   -377       C  
ATOM   4737  CE BLYS B 267     -45.055 -58.182  15.808  0.20 27.45           C  
ANISOU 4737  CE BLYS B 267     5686   3480   1263    824   -465   -204       C  
ATOM   4738  NZ ALYS B 267     -42.094 -56.533  19.083  0.50 31.21           N  
ANISOU 4738  NZ ALYS B 267     5885   3600   2370     96   -347    -62       N  
ATOM   4739  NZ BLYS B 267     -45.077 -58.137  14.325  0.20 27.07           N  
ANISOU 4739  NZ BLYS B 267     5889   3178   1218    997   -311   -588       N  
ATOM   4740  N   ILE B 268     -43.007 -52.456  12.857  1.00 27.82           N  
ANISOU 4740  N   ILE B 268     4423   4220   1926   -122   -311   -755       N  
ATOM   4741  CA  ILE B 268     -43.388 -51.622  11.747  1.00 26.59           C  
ANISOU 4741  CA  ILE B 268     3984   4170   1946    141    -57   -836       C  
ATOM   4742  C   ILE B 268     -42.166 -50.935  11.153  1.00 24.17           C  
ANISOU 4742  C   ILE B 268     3866   4091   1226    123   -279   -751       C  
ATOM   4743  O   ILE B 268     -42.099 -50.844   9.938  1.00 23.82           O  
ANISOU 4743  O   ILE B 268     3635   4218   1195    348   -233   -956       O  
ATOM   4744  CB  ILE B 268     -44.431 -50.602  12.176  1.00 26.97           C  
ANISOU 4744  CB  ILE B 268     4004   4112   2131    183   -341   -884       C  
ATOM   4745  CG1 ILE B 268     -45.788 -51.297  12.287  1.00 28.64           C  
ANISOU 4745  CG1 ILE B 268     3705   4928   2247    288   -181  -1011       C  
ATOM   4746  CG2 ILE B 268     -44.474 -49.398  11.209  1.00 24.66           C  
ANISOU 4746  CG2 ILE B 268     3580   3991   1796    435   -425  -1113       C  
ATOM   4747  CD1 ILE B 268     -46.831 -50.427  12.960  1.00 29.98           C  
ANISOU 4747  CD1 ILE B 268     3925   4876   2587    443   -506  -1274       C  
ATOM   4748  N   ILE B 269     -41.205 -50.498  11.977  1.00 21.95           N  
ANISOU 4748  N   ILE B 269     3422   3705   1212    286    -12  -1016       N  
ATOM   4749  CA AILE B 269     -40.055 -49.763  11.426  0.50 21.96           C  
ANISOU 4749  CA AILE B 269     3552   3609   1181    171   -256   -771       C  
ATOM   4750  CA BILE B 269     -40.071 -49.763  11.464  0.50 22.18           C  
ANISOU 4750  CA BILE B 269     3501   3635   1291    160   -225   -827       C  
ATOM   4751  C   ILE B 269     -39.334 -50.523  10.356  1.00 22.55           C  
ANISOU 4751  C   ILE B 269     3634   3671   1261    151   -110   -811       C  
ATOM   4752  O   ILE B 269     -38.807 -49.894   9.509  1.00 23.79           O  
ANISOU 4752  O   ILE B 269     3728   3489   1820    184   -112   -416       O  
ATOM   4753  CB AILE B 269     -38.995 -49.200  12.436  0.50 22.45           C  
ANISOU 4753  CB AILE B 269     4035   3595    898    203   -282   -990       C  
ATOM   4754  CB BILE B 269     -39.056 -49.406  12.573  0.50 22.74           C  
ANISOU 4754  CB BILE B 269     3845   3600   1194     67   -183  -1178       C  
ATOM   4755  CG1AILE B 269     -38.853 -50.072  13.700  0.50 23.40           C  
ANISOU 4755  CG1AILE B 269     4098   3581   1210     39    -96   -641       C  
ATOM   4756  CG1BILE B 269     -38.955 -47.885  12.784  0.50 23.41           C  
ANISOU 4756  CG1BILE B 269     4067   3459   1365    110    -51   -698       C  
ATOM   4757  CG2AILE B 269     -39.247 -47.719  12.688  0.50 24.97           C  
ANISOU 4757  CG2AILE B 269     4336   3579   1571    203   -322   -874       C  
ATOM   4758  CG2BILE B 269     -37.686 -49.984  12.250  0.50 24.50           C  
ANISOU 4758  CG2BILE B 269     3738   3736   1833    117   -272   -745       C  
ATOM   4759  CD1AILE B 269     -37.698 -51.053  13.640  0.50 24.65           C  
ANISOU 4759  CD1AILE B 269     4332   3674   1359    114    145   -586       C  
ATOM   4760  CD1BILE B 269     -38.750 -46.998  11.575  0.50 20.18           C  
ANISOU 4760  CD1BILE B 269     3438   3558    671   -191    205  -1167       C  
ATOM   4761  N   ASN B 270     -39.218 -51.846  10.471  1.00 22.42           N  
ANISOU 4761  N   ASN B 270     3611   3626   1279     66   -140   -274       N  
ATOM   4762  CA  ASN B 270     -38.327 -52.581   9.584  1.00 23.39           C  
ANISOU 4762  CA  ASN B 270     3691   3576   1618    191   -209   -601       C  
ATOM   4763  C   ASN B 270     -38.921 -52.706   8.202  1.00 22.84           C  
ANISOU 4763  C   ASN B 270     3411   3764   1501    154     35   -460       C  
ATOM   4764  O   ASN B 270     -38.308 -53.224   7.283  1.00 21.99           O  
ANISOU 4764  O   ASN B 270     3804   3431   1117     15   -270   -694       O  
ATOM   4765  CB  ASN B 270     -37.999 -53.922  10.181  1.00 25.17           C  
ANISOU 4765  CB  ASN B 270     4120   3581   1861    182   -212   -538       C  
ATOM   4766  CG  ASN B 270     -36.975 -53.812  11.288  1.00 25.29           C  
ANISOU 4766  CG  ASN B 270     4231   3591   1784     58   -223   -577       C  
ATOM   4767  OD1 ASN B 270     -36.072 -52.990  11.235  1.00 25.83           O  
ANISOU 4767  OD1 ASN B 270     4030   3774   2009     53   -352   -911       O  
ATOM   4768  ND2 ASN B 270     -37.106 -54.642  12.285  1.00 31.06           N  
ANISOU 4768  ND2 ASN B 270     4880   4617   2301     -9   -233    146       N  
ATOM   4769  N   GLU B 271     -40.155 -52.240   8.087  1.00 20.98           N  
ANISOU 4769  N   GLU B 271     3424   3504   1042     39    -91   -455       N  
ATOM   4770  CA  GLU B 271     -40.820 -52.093   6.787  1.00 21.86           C  
ANISOU 4770  CA  GLU B 271     3407   3653   1245    189   -198   -493       C  
ATOM   4771  C   GLU B 271     -40.101 -51.031   6.038  1.00 22.76           C  
ANISOU 4771  C   GLU B 271     3832   3716   1100    200   -141   -548       C  
ATOM   4772  O   GLU B 271     -40.389 -50.732   4.870  1.00 21.26           O  
ANISOU 4772  O   GLU B 271     3817   3120   1139    158   -181   -685       O  
ATOM   4773  CB  GLU B 271     -42.280 -51.648   6.928  1.00 23.38           C  
ANISOU 4773  CB  GLU B 271     3519   3665   1698    263   -183   -823       C  
ATOM   4774  CG  GLU B 271     -43.198 -52.815   7.277  1.00 24.32           C  
ANISOU 4774  CG  GLU B 271     3436   3957   1847    -35   -120  -1110       C  
ATOM   4775  CD  GLU B 271     -44.655 -52.456   7.384  1.00 24.62           C  
ANISOU 4775  CD  GLU B 271     3721   3815   1817    289    142  -1273       C  
ATOM   4776  OE1 GLU B 271     -45.317 -53.090   8.238  1.00 26.41           O  
ANISOU 4776  OE1 GLU B 271     3902   4279   1852   -172    271  -1465       O  
ATOM   4777  OE2 GLU B 271     -45.085 -51.545   6.650  1.00 24.53           O  
ANISOU 4777  OE2 GLU B 271     3733   3853   1732    323     68  -1346       O  
ATOM   4778  N   TYR B 272     -39.171 -50.421   6.739  1.00 23.56           N  
ANISOU 4778  N   TYR B 272     3821   3585   1545   -118     70   -699       N  
ATOM   4779  CA  TYR B 272     -38.508 -49.273   6.165  1.00 21.91           C  
ANISOU 4779  CA  TYR B 272     3851   3366   1105    177     -2   -774       C  
ATOM   4780  C   TYR B 272     -37.004 -49.426   6.175  1.00 22.47           C  
ANISOU 4780  C   TYR B 272     3818   3160   1559    -67    261   -589       C  
ATOM   4781  O   TYR B 272     -36.440 -50.174   6.968  1.00 23.98           O  
ANISOU 4781  O   TYR B 272     3924   3827   1361    -32   -212   -561       O  
ATOM   4782  CB  TYR B 272     -38.928 -47.977   6.871  1.00 23.25           C  
ANISOU 4782  CB  TYR B 272     3658   3278   1896    155    189   -789       C  
ATOM   4783  CG  TYR B 272     -40.420 -47.770   6.833  1.00 23.20           C  
ANISOU 4783  CG  TYR B 272     3694   3451   1669    179   -376   -594       C  
ATOM   4784  CD1 TYR B 272     -41.026 -47.198   5.713  1.00 22.61           C  
ANISOU 4784  CD1 TYR B 272     4016   3203   1370    432    106   -598       C  
ATOM   4785  CD2 TYR B 272     -41.237 -48.210   7.891  1.00 23.81           C  
ANISOU 4785  CD2 TYR B 272     3811   3735   1499    284    -46   -892       C  
ATOM   4786  CE1 TYR B 272     -42.400 -47.038   5.657  1.00 22.92           C  
ANISOU 4786  CE1 TYR B 272     4112   3213   1384    596   -547   -691       C  
ATOM   4787  CE2 TYR B 272     -42.617 -48.072   7.846  1.00 25.68           C  
ANISOU 4787  CE2 TYR B 272     4005   3673   2077    835   -277   -933       C  
ATOM   4788  CZ  TYR B 272     -43.186 -47.487   6.734  1.00 24.01           C  
ANISOU 4788  CZ  TYR B 272     4016   3348   1756    977    117  -1051       C  
ATOM   4789  OH  TYR B 272     -44.555 -47.416   6.708  1.00 27.26           O  
ANISOU 4789  OH  TYR B 272     4020   3970   2367    823    -17  -1357       O  
ATOM   4790  N   SER B 273     -36.361 -48.704   5.267  1.00 22.45           N  
ANISOU 4790  N   SER B 273     4018   2944   1564   -154    270   -780       N  
ATOM   4791  CA  SER B 273     -34.926 -48.816   5.072  1.00 22.57           C  
ANISOU 4791  CA  SER B 273     4056   3221   1299   -399    607   -543       C  
ATOM   4792  C   SER B 273     -34.189 -47.687   5.778  1.00 22.66           C  
ANISOU 4792  C   SER B 273     3938   3255   1415   -181    212   -393       C  
ATOM   4793  O   SER B 273     -34.313 -46.532   5.387  1.00 21.48           O  
ANISOU 4793  O   SER B 273     4061   3216    883   -282    467   -573       O  
ATOM   4794  CB  SER B 273     -34.656 -48.828   3.586  1.00 25.24           C  
ANISOU 4794  CB  SER B 273     4313   3981   1294   -278    546   -305       C  
ATOM   4795  OG  SER B 273     -33.293 -48.634   3.335  1.00 23.57           O  
ANISOU 4795  OG  SER B 273     4784   3510    659   -502   1290   -436       O  
ATOM   4796  N   PHE B 274     -33.431 -48.025   6.817  1.00 22.13           N  
ANISOU 4796  N   PHE B 274     3921   3297   1187   -132    185   -696       N  
ATOM   4797  CA  PHE B 274     -32.813 -47.021   7.659  1.00 20.41           C  
ANISOU 4797  CA  PHE B 274     3615   3139   1000    -26    269   -576       C  
ATOM   4798  C   PHE B 274     -31.534 -47.505   8.338  1.00 20.61           C  
ANISOU 4798  C   PHE B 274     3780   3215    834     81    157   -457       C  
ATOM   4799  O   PHE B 274     -31.258 -48.697   8.378  1.00 23.32           O  
ANISOU 4799  O   PHE B 274     4146   3306   1405    177     63   -498       O  
ATOM   4800  CB  PHE B 274     -33.822 -46.560   8.722  1.00 19.88           C  
ANISOU 4800  CB  PHE B 274     3499   2974   1078    220    199   -460       C  
ATOM   4801  CG  PHE B 274     -34.191 -47.626   9.713  1.00 20.59           C  
ANISOU 4801  CG  PHE B 274     3627   3079   1114    -22    257   -499       C  
ATOM   4802  CD1 PHE B 274     -33.477 -47.768  10.908  1.00 20.64           C  
ANISOU 4802  CD1 PHE B 274     3931   2881   1029     90    202   -475       C  
ATOM   4803  CD2 PHE B 274     -35.250 -48.485   9.464  1.00 23.13           C  
ANISOU 4803  CD2 PHE B 274     3848   3365   1574   -174    151   -806       C  
ATOM   4804  CE1 PHE B 274     -33.804 -48.748  11.821  1.00 21.85           C  
ANISOU 4804  CE1 PHE B 274     3901   3187   1212    -95    247   -330       C  
ATOM   4805  CE2 PHE B 274     -35.572 -49.468  10.380  1.00 23.52           C  
ANISOU 4805  CE2 PHE B 274     4140   3483   1312    -93     75   -706       C  
ATOM   4806  CZ  PHE B 274     -34.853 -49.602  11.551  1.00 24.89           C  
ANISOU 4806  CZ  PHE B 274     4314   3439   1703   -237   -269   -772       C  
ATOM   4807  N   SER B 275     -30.789 -46.563   8.904  1.00 20.27           N  
ANISOU 4807  N   SER B 275     3638   3161    901    113    194   -517       N  
ATOM   4808  CA  SER B 275     -29.672 -46.872   9.754  1.00 20.84           C  
ANISOU 4808  CA  SER B 275     3660   3285    972    136    125   -551       C  
ATOM   4809  C   SER B 275     -29.902 -46.218  11.111  1.00 20.25           C  
ANISOU 4809  C   SER B 275     3865   2886    942    326    115   -394       C  
ATOM   4810  O   SER B 275     -30.296 -45.057  11.183  1.00 18.89           O  
ANISOU 4810  O   SER B 275     3787   2800    589    322   -108   -199       O  
ATOM   4811  CB  SER B 275     -28.417 -46.298   9.126  1.00 22.15           C  
ANISOU 4811  CB  SER B 275     3777   3565   1074    195    395   -581       C  
ATOM   4812  OG  SER B 275     -27.298 -46.591   9.926  1.00 31.65           O  
ANISOU 4812  OG  SER B 275     4002   4946   3077    257   -218   -344       O  
ATOM   4813  N   ARG B 276     -29.647 -46.950  12.184  1.00 19.45           N  
ANISOU 4813  N   ARG B 276     3713   2841    836    213    331   -361       N  
ATOM   4814  CA  ARG B 276     -29.903 -46.398  13.506  1.00 19.01           C  
ANISOU 4814  CA  ARG B 276     3917   2490    815    194    225   -324       C  
ATOM   4815  C   ARG B 276     -28.649 -45.777  14.095  1.00 19.98           C  
ANISOU 4815  C   ARG B 276     3887   2475   1226    311    -54    -85       C  
ATOM   4816  O   ARG B 276     -27.622 -46.443  14.272  1.00 23.56           O  
ANISOU 4816  O   ARG B 276     3873   2953   2125    506     79   -217       O  
ATOM   4817  CB  ARG B 276     -30.478 -47.446  14.460  1.00 19.93           C  
ANISOU 4817  CB  ARG B 276     3853   2949    767    266    425   -174       C  
ATOM   4818  CG  ARG B 276     -30.780 -46.876  15.840  1.00 20.72           C  
ANISOU 4818  CG  ARG B 276     4284   2819    769    327    111   -324       C  
ATOM   4819  CD  ARG B 276     -31.250 -47.944  16.803  1.00 21.51           C  
ANISOU 4819  CD  ARG B 276     4257   2710   1204    438    313   -245       C  
ATOM   4820  NE  ARG B 276     -31.715 -47.387  18.077  1.00 20.81           N  
ANISOU 4820  NE  ARG B 276     4267   2812    826    526    191     82       N  
ATOM   4821  CZ  ARG B 276     -32.120 -48.139  19.091  1.00 22.57           C  
ANISOU 4821  CZ  ARG B 276     4455   2561   1558    348    439    248       C  
ATOM   4822  NH1 ARG B 276     -32.107 -49.460  18.948  1.00 27.75           N  
ANISOU 4822  NH1 ARG B 276     5004   2624   2913    461    596     40       N  
ATOM   4823  NH2 ARG B 276     -32.543 -47.597  20.229  1.00 22.68           N  
ANISOU 4823  NH2 ARG B 276     4180   3038   1398    256    341    193       N  
ATOM   4824  N   ASN B 277     -28.751 -44.492  14.396  1.00 18.69           N  
ANISOU 4824  N   ASN B 277     3859   2464    779    322    139   -169       N  
ATOM   4825  CA  ASN B 277     -27.661 -43.774  15.046  1.00 18.10           C  
ANISOU 4825  CA  ASN B 277     3700   2436    742    424     -9     46       C  
ATOM   4826  C   ASN B 277     -27.515 -44.145  16.531  1.00 18.99           C  
ANISOU 4826  C   ASN B 277     3760   2761    692    412    -54    -33       C  
ATOM   4827  O   ASN B 277     -28.514 -44.306  17.244  1.00 18.63           O  
ANISOU 4827  O   ASN B 277     3809   2735    533    220    -84     54       O  
ATOM   4828  CB  ASN B 277     -27.847 -42.267  14.831  1.00 18.17           C  
ANISOU 4828  CB  ASN B 277     3750   2399    754    369    -77    101       C  
ATOM   4829  CG  ASN B 277     -27.936 -41.918  13.357  1.00 17.59           C  
ANISOU 4829  CG  ASN B 277     3613   2353    718    359    105     78       C  
ATOM   4830  OD1 ASN B 277     -27.056 -42.279  12.587  1.00 19.11           O  
ANISOU 4830  OD1 ASN B 277     3650   2920    689    512     81   -119       O  
ATOM   4831  ND2 ASN B 277     -29.006 -41.251  12.956  1.00 18.21           N  
ANISOU 4831  ND2 ASN B 277     3435   2341   1142    301    174     36       N  
ATOM   4832  N   SER B 278     -26.265 -44.296  16.972  1.00 19.12           N  
ANISOU 4832  N   SER B 278     3798   2772    694    479    -78   -122       N  
ATOM   4833  CA  SER B 278     -25.954 -44.832  18.303  1.00 20.28           C  
ANISOU 4833  CA  SER B 278     4100   2825    779    630     18     20       C  
ATOM   4834  C   SER B 278     -26.623 -46.196  18.511  1.00 21.37           C  
ANISOU 4834  C   SER B 278     4086   2939   1093    594    -74    -43       C  
ATOM   4835  O   SER B 278     -27.003 -46.533  19.634  1.00 22.14           O  
ANISOU 4835  O   SER B 278     4140   3015   1256    466     50    -17       O  
ATOM   4836  CB  SER B 278     -26.393 -43.862  19.411  1.00 20.53           C  
ANISOU 4836  CB  SER B 278     3784   3029    988    703     58   -126       C  
ATOM   4837  OG  SER B 278     -25.655 -44.096  20.606  1.00 20.99           O  
ANISOU 4837  OG  SER B 278     3828   3060   1085    530    -50   -127       O  
ATOM   4838  N   GLY B 279     -26.743 -46.983  17.437  1.00 21.38           N  
ANISOU 4838  N   GLY B 279     4243   2649   1229    454   -109     13       N  
ATOM   4839  CA  GLY B 279     -27.463 -48.258  17.463  1.00 23.40           C  
ANISOU 4839  CA  GLY B 279     4243   2920   1727    281    -82    -25       C  
ATOM   4840  C   GLY B 279     -26.969 -49.325  18.437  1.00 24.13           C  
ANISOU 4840  C   GLY B 279     4420   3276   1471    539     -1    -55       C  
ATOM   4841  O   GLY B 279     -27.727 -50.218  18.805  1.00 29.32           O  
ANISOU 4841  O   GLY B 279     5097   3475   2567    316    277    143       O  
ATOM   4842  N   ASP B 280     -25.697 -49.265  18.827  1.00 23.68           N  
ANISOU 4842  N   ASP B 280     4480   3516   1001    715   -203   -320       N  
ATOM   4843  CA  ASP B 280     -25.141 -50.201  19.793  1.00 24.94           C  
ANISOU 4843  CA  ASP B 280     4869   3703    902    766      5   -106       C  
ATOM   4844  C   ASP B 280     -25.077 -49.638  21.200  1.00 23.39           C  
ANISOU 4844  C   ASP B 280     4464   3419   1002    874   -108   -176       C  
ATOM   4845  O   ASP B 280     -24.684 -50.344  22.115  1.00 25.57           O  
ANISOU 4845  O   ASP B 280     4753   3553   1409    977   -164    138       O  
ATOM   4846  CB  ASP B 280     -23.732 -50.615  19.367  1.00 27.11           C  
ANISOU 4846  CB  ASP B 280     4818   3737   1743    978   -133    -68       C  
ATOM   4847  CG  ASP B 280     -23.689 -51.177  17.957  1.00 30.44           C  
ANISOU 4847  CG  ASP B 280     4801   4650   2112    603   -210   -675       C  
ATOM   4848  OD1 ASP B 280     -24.552 -52.012  17.606  1.00 32.76           O  
ANISOU 4848  OD1 ASP B 280     5760   3552   3135    633   -126  -1147       O  
ATOM   4849  OD2 ASP B 280     -22.794 -50.771  17.188  1.00 38.11           O  
ANISOU 4849  OD2 ASP B 280     5457   5772   3251    503    725   -879       O  
ATOM   4850  N   ASN B 281     -25.456 -48.381  21.363  1.00 22.80           N  
ANISOU 4850  N   ASN B 281     4257   3298   1108    706    -74   -242       N  
ATOM   4851  CA  ASN B 281     -25.236 -47.673  22.613  1.00 21.45           C  
ANISOU 4851  CA  ASN B 281     3918   3337    894    830   -105   -103       C  
ATOM   4852  C   ASN B 281     -26.490 -46.961  23.124  1.00 21.13           C  
ANISOU 4852  C   ASN B 281     3983   3131    915    666    -70   -260       C  
ATOM   4853  O   ASN B 281     -26.473 -46.313  24.192  1.00 22.27           O  
ANISOU 4853  O   ASN B 281     3959   3436   1063    746    150   -479       O  
ATOM   4854  CB  ASN B 281     -24.102 -46.661  22.443  1.00 23.93           C  
ANISOU 4854  CB  ASN B 281     3918   3580   1593    707   -157   -275       C  
ATOM   4855  CG  ASN B 281     -22.737 -47.318  22.337  1.00 23.81           C  
ANISOU 4855  CG  ASN B 281     4009   3825   1210    833   -176   -188       C  
ATOM   4856  OD1 ASN B 281     -22.158 -47.402  21.251  1.00 25.77           O  
ANISOU 4856  OD1 ASN B 281     4249   4255   1287    900     35   -125       O  
ATOM   4857  ND2 ASN B 281     -22.217 -47.793  23.467  1.00 26.12           N  
ANISOU 4857  ND2 ASN B 281     4772   3906   1245    486   -343     49       N  
ATOM   4858  N   ALA B 282     -27.578 -47.097  22.371  1.00 21.97           N  
ANISOU 4858  N   ALA B 282     3674   3231   1441    680    -55    -23       N  
ATOM   4859  CA  ALA B 282     -28.826 -46.416  22.701  1.00 20.69           C  
ANISOU 4859  CA  ALA B 282     3922   3042    894    559    322   -194       C  
ATOM   4860  C   ALA B 282     -29.817 -47.291  23.475  1.00 22.04           C  
ANISOU 4860  C   ALA B 282     3937   2948   1486    516    230    -30       C  
ATOM   4861  O   ALA B 282     -29.891 -48.499  23.260  1.00 23.44           O  
ANISOU 4861  O   ALA B 282     4348   2800   1758    270    314    384       O  
ATOM   4862  CB  ALA B 282     -29.481 -45.868  21.440  1.00 22.02           C  
ANISOU 4862  CB  ALA B 282     4071   2877   1417    571     15     19       C  
ATOM   4863  N   LEU B 283     -30.579 -46.655  24.371  1.00 21.47           N  
ANISOU 4863  N   LEU B 283     4124   3181    850    324    275    184       N  
ATOM   4864  CA  LEU B 283     -31.758 -47.261  25.009  1.00 22.95           C  
ANISOU 4864  CA  LEU B 283     4108   3267   1341    266    285     88       C  
ATOM   4865  C   LEU B 283     -32.790 -47.712  23.990  1.00 23.27           C  
ANISOU 4865  C   LEU B 283     4241   3126   1475    133    119    327       C  
ATOM   4866  O   LEU B 283     -32.951 -47.107  22.926  1.00 23.21           O  
ANISOU 4866  O   LEU B 283     4350   2839   1626    406    359    449       O  
ATOM   4867  CB  LEU B 283     -32.412 -46.276  25.979  1.00 23.74           C  
ANISOU 4867  CB  LEU B 283     3985   3589   1443    142    212   -160       C  
ATOM   4868  CG  LEU B 283     -31.541 -45.876  27.167  1.00 24.69           C  
ANISOU 4868  CG  LEU B 283     3967   3732   1680    297     36   -307       C  
ATOM   4869  CD1 LEU B 283     -32.383 -45.187  28.230  1.00 25.97           C  
ANISOU 4869  CD1 LEU B 283     3975   4147   1743     31     94   -618       C  
ATOM   4870  CD2 LEU B 283     -30.835 -47.102  27.733  1.00 25.77           C  
ANISOU 4870  CD2 LEU B 283     4262   3481   2046    102     65   -142       C  
ATOM   4871  N   SER B 284     -33.499 -48.783  24.332  1.00 23.36           N  
ANISOU 4871  N   SER B 284     4274   3243   1356    174    271    613       N  
ATOM   4872  CA  SER B 284     -34.473 -49.390  23.418  1.00 24.39           C  
ANISOU 4872  CA  SER B 284     4342   3029   1893    214    299    210       C  
ATOM   4873  C   SER B 284     -35.660 -48.483  23.121  1.00 21.27           C  
ANISOU 4873  C   SER B 284     4092   2831   1159     78    231     54       C  
ATOM   4874  O   SER B 284     -36.437 -48.731  22.196  1.00 21.60           O  
ANISOU 4874  O   SER B 284     4400   2922    884    174    237     60       O  
ATOM   4875  CB  SER B 284     -34.967 -50.721  23.978  1.00 26.14           C  
ANISOU 4875  CB  SER B 284     4574   3362   1994     30    764    332       C  
ATOM   4876  OG  SER B 284     -35.881 -50.496  25.027  1.00 26.41           O  
ANISOU 4876  OG  SER B 284     4408   3489   2135    129    702    212       O  
ATOM   4877  N   THR B 285     -35.809 -47.440  23.925  1.00 19.91           N  
ANISOU 4877  N   THR B 285     3791   2906    867    209    293     95       N  
ATOM   4878  CA  THR B 285     -36.958 -46.563  23.784  1.00 18.46           C  
ANISOU 4878  CA  THR B 285     3476   2768    768    -11    370    -15       C  
ATOM   4879  C   THR B 285     -36.694 -45.283  22.984  1.00 18.21           C  
ANISOU 4879  C   THR B 285     3481   2802    634     33    177      2       C  
ATOM   4880  O   THR B 285     -37.631 -44.533  22.710  1.00 17.15           O  
ANISOU 4880  O   THR B 285     3546   2552    416    -19    110      9       O  
ATOM   4881  CB  THR B 285     -37.598 -46.224  25.149  1.00 18.77           C  
ANISOU 4881  CB  THR B 285     3704   2748    677    -52    214   -262       C  
ATOM   4882  OG1 THR B 285     -36.579 -45.793  26.072  1.00 19.54           O  
ANISOU 4882  OG1 THR B 285     3575   2977    871    -22    169   -137       O  
ATOM   4883  CG2 THR B 285     -38.297 -47.437  25.712  1.00 17.99           C  
ANISOU 4883  CG2 THR B 285     3498   2828    510    -98    323   -399       C  
ATOM   4884  N   THR B 286     -35.442 -45.003  22.627  1.00 18.17           N  
ANISOU 4884  N   THR B 286     3564   2752    586    -31    297    165       N  
ATOM   4885  CA  THR B 286     -35.230 -43.983  21.590  1.00 19.13           C  
ANISOU 4885  CA  THR B 286     3709   2643    915    188    441    288       C  
ATOM   4886  C   THR B 286     -34.466 -44.487  20.374  1.00 18.59           C  
ANISOU 4886  C   THR B 286     3521   2680    859    115    278    136       C  
ATOM   4887  O   THR B 286     -33.330 -44.963  20.459  1.00 18.91           O  
ANISOU 4887  O   THR B 286     3699   2686    800    300    250     92       O  
ATOM   4888  CB  THR B 286     -34.880 -42.537  22.076  1.00 22.12           C  
ANISOU 4888  CB  THR B 286     3856   3109   1440   -319    397     -6       C  
ATOM   4889  OG1 THR B 286     -33.798 -41.958  21.319  1.00 22.28           O  
ANISOU 4889  OG1 THR B 286     3341   3532   1592    110    605   -249       O  
ATOM   4890  CG2 THR B 286     -34.582 -42.476  23.539  1.00 18.52           C  
ANISOU 4890  CG2 THR B 286     3295   2309   1430    -36    223    387       C  
ATOM   4891  N   TRP B 287     -35.139 -44.356  19.236  1.00 17.71           N  
ANISOU 4891  N   TRP B 287     3483   2522    724    170    365     67       N  
ATOM   4892  CA  TRP B 287     -34.629 -44.808  17.960  1.00 17.56           C  
ANISOU 4892  CA  TRP B 287     3588   2357    726    251    266    -27       C  
ATOM   4893  C   TRP B 287     -34.391 -43.590  17.126  1.00 17.43           C  
ANISOU 4893  C   TRP B 287     3468   2395    757    124    206    -41       C  
ATOM   4894  O   TRP B 287     -35.334 -43.010  16.571  1.00 18.95           O  
ANISOU 4894  O   TRP B 287     3545   2423   1232    149    149     49       O  
ATOM   4895  CB  TRP B 287     -35.656 -45.704  17.281  1.00 18.69           C  
ANISOU 4895  CB  TRP B 287     3644   2532    923    199    188    -15       C  
ATOM   4896  CG  TRP B 287     -35.703 -47.113  17.808  1.00 20.21           C  
ANISOU 4896  CG  TRP B 287     4086   2635    954    241    179     91       C  
ATOM   4897  CD1 TRP B 287     -36.029 -47.526  19.095  1.00 21.13           C  
ANISOU 4897  CD1 TRP B 287     4122   2696   1209    244    367    309       C  
ATOM   4898  CD2 TRP B 287     -35.429 -48.328  17.069  1.00 21.93           C  
ANISOU 4898  CD2 TRP B 287     4246   2571   1514    271    281     25       C  
ATOM   4899  NE1 TRP B 287     -35.969 -48.887  19.202  1.00 22.22           N  
ANISOU 4899  NE1 TRP B 287     4377   2652   1413    347    322     93       N  
ATOM   4900  CE2 TRP B 287     -35.610 -49.430  18.014  1.00 22.94           C  
ANISOU 4900  CE2 TRP B 287     4616   2653   1444    384    292     53       C  
ATOM   4901  CE3 TRP B 287     -35.071 -48.611  15.754  1.00 23.99           C  
ANISOU 4901  CE3 TRP B 287     4631   2785   1699    211    334   -425       C  
ATOM   4902  CZ2 TRP B 287     -35.440 -50.746  17.637  1.00 25.71           C  
ANISOU 4902  CZ2 TRP B 287     4825   2713   2229    430    500    -75       C  
ATOM   4903  CZ3 TRP B 287     -34.893 -49.945  15.389  1.00 25.57           C  
ANISOU 4903  CZ3 TRP B 287     4910   2685   2118    217    310   -241       C  
ATOM   4904  CH2 TRP B 287     -35.076 -50.984  16.310  1.00 26.42           C  
ANISOU 4904  CH2 TRP B 287     5116   3023   1899    208    -69    -64       C  
ATOM   4905  N   ASN B 288     -33.134 -43.165  17.072  1.00 17.58           N  
ANISOU 4905  N   ASN B 288     3483   2363    834     51    229    -30       N  
ATOM   4906  CA  ASN B 288     -32.731 -42.084  16.192  1.00 17.27           C  
ANISOU 4906  CA  ASN B 288     3439   2444    679     93    130     19       C  
ATOM   4907  C   ASN B 288     -32.272 -42.736  14.897  1.00 17.63           C  
ANISOU 4907  C   ASN B 288     3417   2354    924    205    129   -136       C  
ATOM   4908  O   ASN B 288     -31.248 -43.427  14.870  1.00 17.78           O  
ANISOU 4908  O   ASN B 288     3620   2300    834    233    112   -165       O  
ATOM   4909  CB  ASN B 288     -31.632 -41.221  16.833  1.00 17.41           C  
ANISOU 4909  CB  ASN B 288     3424   2314    875     74    322    -53       C  
ATOM   4910  CG  ASN B 288     -31.360 -39.955  16.046  1.00 17.32           C  
ANISOU 4910  CG  ASN B 288     3312   2352    914    282    315     64       C  
ATOM   4911  OD1 ASN B 288     -30.721 -39.998  14.996  1.00 16.31           O  
ANISOU 4911  OD1 ASN B 288     3258   2252    687    349    124   -133       O  
ATOM   4912  ND2 ASN B 288     -31.834 -38.817  16.554  1.00 16.59           N  
ANISOU 4912  ND2 ASN B 288     3165   2415    723    267    275    -36       N  
ATOM   4913  N   VAL B 289     -33.075 -42.541  13.850  1.00 17.65           N  
ANISOU 4913  N   VAL B 289     3639   2463    601    178    271   -155       N  
ATOM   4914  CA  VAL B 289     -32.915 -43.271  12.595  1.00 17.39           C  
ANISOU 4914  CA  VAL B 289     3730   2174    703    203    167   -172       C  
ATOM   4915  C   VAL B 289     -32.738 -42.366  11.402  1.00 17.36           C  
ANISOU 4915  C   VAL B 289     3396   2497    699    170    120    -74       C  
ATOM   4916  O   VAL B 289     -33.437 -41.388  11.241  1.00 16.67           O  
ANISOU 4916  O   VAL B 289     3470   2455    407     97    192    163       O  
ATOM   4917  CB  VAL B 289     -34.087 -44.234  12.311  1.00 17.20           C  
ANISOU 4917  CB  VAL B 289     3604   2325    604    226    121    106       C  
ATOM   4918  CG1 VAL B 289     -34.167 -45.325  13.387  1.00 17.57           C  
ANISOU 4918  CG1 VAL B 289     3762   2225    687    100      2     89       C  
ATOM   4919  CG2 VAL B 289     -35.413 -43.491  12.182  1.00 19.32           C  
ANISOU 4919  CG2 VAL B 289     3685   2600   1056    301     23   -103       C  
ATOM   4920  N   THR B 290     -31.772 -42.734  10.569  1.00 17.29           N  
ANISOU 4920  N   THR B 290     3420   2482    664     86    172    -29       N  
ATOM   4921  CA  THR B 290     -31.503 -42.061   9.297  1.00 17.65           C  
ANISOU 4921  CA  THR B 290     3395   2518    790     12    287     23       C  
ATOM   4922  C   THR B 290     -32.009 -42.942   8.172  1.00 18.44           C  
ANISOU 4922  C   THR B 290     3457   2969    578    104    305   -111       C  
ATOM   4923  O   THR B 290     -31.444 -44.012   7.930  1.00 20.24           O  
ANISOU 4923  O   THR B 290     3871   2899    920     99    293   -216       O  
ATOM   4924  CB  THR B 290     -29.986 -41.809   9.077  1.00 17.84           C  
ANISOU 4924  CB  THR B 290     3382   2674    721     38    164     95       C  
ATOM   4925  OG1 THR B 290     -29.453 -41.033  10.156  1.00 17.89           O  
ANISOU 4925  OG1 THR B 290     3343   2730    725    165    192    -40       O  
ATOM   4926  CG2 THR B 290     -29.724 -41.053   7.757  1.00 17.91           C  
ANISOU 4926  CG2 THR B 290     3582   2652    570    108    244    -42       C  
ATOM   4927  N   PHE B 291     -33.049 -42.466   7.488  1.00 17.97           N  
ANISOU 4927  N   PHE B 291     3360   2837    629    -91    231   -298       N  
ATOM   4928  CA  PHE B 291     -33.630 -43.164   6.348  1.00 19.27           C  
ANISOU 4928  CA  PHE B 291     3346   3273    700    -78    190   -482       C  
ATOM   4929  C   PHE B 291     -32.695 -43.073   5.152  1.00 20.08           C  
ANISOU 4929  C   PHE B 291     3810   3230    588   -170    285   -342       C  
ATOM   4930  O   PHE B 291     -31.943 -42.122   5.025  1.00 21.10           O  
ANISOU 4930  O   PHE B 291     4040   3339    635   -308    307   -405       O  
ATOM   4931  CB  PHE B 291     -35.014 -42.614   5.999  1.00 19.07           C  
ANISOU 4931  CB  PHE B 291     3351   3159    733     31    329   -567       C  
ATOM   4932  CG  PHE B 291     -36.045 -42.897   7.031  1.00 19.37           C  
ANISOU 4932  CG  PHE B 291     3585   3105    668      8    292   -214       C  
ATOM   4933  CD1 PHE B 291     -36.407 -41.927   7.931  1.00 20.14           C  
ANISOU 4933  CD1 PHE B 291     3435   3071   1146    196    331   -319       C  
ATOM   4934  CD2 PHE B 291     -36.626 -44.142   7.117  1.00 20.64           C  
ANISOU 4934  CD2 PHE B 291     3382   3275   1185   -142    366   -458       C  
ATOM   4935  CE1 PHE B 291     -37.340 -42.193   8.906  1.00 20.11           C  
ANISOU 4935  CE1 PHE B 291     3593   3011   1033     76    299   -355       C  
ATOM   4936  CE2 PHE B 291     -37.555 -44.414   8.087  1.00 21.12           C  
ANISOU 4936  CE2 PHE B 291     3608   3322   1092    151    576   -701       C  
ATOM   4937  CZ  PHE B 291     -37.917 -43.441   8.985  1.00 21.15           C  
ANISOU 4937  CZ  PHE B 291     3952   2714   1371    348    357   -527       C  
ATOM   4938  N   GLU B 292     -32.751 -44.067   4.278  1.00 20.47           N  
ANISOU 4938  N   GLU B 292     3939   3123    716   -219    498   -334       N  
ATOM   4939  CA  GLU B 292     -31.771 -44.224   3.191  1.00 22.73           C  
ANISOU 4939  CA  GLU B 292     4330   3648    657   -154    647   -474       C  
ATOM   4940  C   GLU B 292     -31.742 -43.110   2.146  1.00 23.65           C  
ANISOU 4940  C   GLU B 292     4514   3521    948   -353    497   -411       C  
ATOM   4941  O   GLU B 292     -30.674 -42.700   1.757  1.00 24.63           O  
ANISOU 4941  O   GLU B 292     4605   3592   1161   -575    370   -152       O  
ATOM   4942  CB  GLU B 292     -31.980 -45.595   2.501  1.00 22.96           C  
ANISOU 4942  CB  GLU B 292     4150   3723    849   -165    586   -515       C  
ATOM   4943  CG  GLU B 292     -30.906 -45.992   1.502  1.00 28.39           C  
ANISOU 4943  CG  GLU B 292     4574   4771   1442    151    929   -675       C  
ATOM   4944  CD  GLU B 292     -31.168 -47.295   0.754  1.00 21.61           C  
ANISOU 4944  CD  GLU B 292     2376   4719   1115   1978    472   -969       C  
ATOM   4945  OE1 GLU B 292     -32.218 -47.912   0.911  1.00 34.17           O  
ANISOU 4945  OE1 GLU B 292     4735   5668   2578   -250    263   -885       O  
ATOM   4946  OE2 GLU B 292     -30.333 -47.684  -0.078  1.00 31.13           O  
ANISOU 4946  OE2 GLU B 292     3085   7258   1482   3071    621   -895       O  
ATOM   4947  N   ASN B 293     -32.914 -42.679   1.698  1.00 25.07           N  
ANISOU 4947  N   ASN B 293     4608   3994    922   -333    273   -749       N  
ATOM   4948  CA  ASN B 293     -33.093 -41.988   0.396  1.00 27.74           C  
ANISOU 4948  CA  ASN B 293     4763   3692   2083   -421   -199     77       C  
ATOM   4949  C   ASN B 293     -34.053 -40.890   0.804  1.00 26.24           C  
ANISOU 4949  C   ASN B 293     5453   3655    859   -427     68   -490       C  
ATOM   4950  O   ASN B 293     -34.784 -41.080   1.758  1.00 25.16           O  
ANISOU 4950  O   ASN B 293     5250   3533    775   -344    -70   -362       O  
ATOM   4951  CB  ASN B 293     -33.940 -42.814  -0.594  1.00 27.68           C  
ANISOU 4951  CB  ASN B 293     5427   4252    838   -316     97   -317       C  
ATOM   4952  CG  ASN B 293     -33.244 -43.962  -1.319  1.00 25.16           C  
ANISOU 4952  CG  ASN B 293     3432   4871   1254   -467   1271    575       C  
ATOM   4953  OD1 ASN B 293     -32.364 -43.801  -2.118  1.00 38.44           O  
ANISOU 4953  OD1 ASN B 293     5111   7169   2325  -1885   2597   -566       O  
ATOM   4954  ND2 ASN B 293     -33.770 -45.140  -1.112  1.00 33.93           N  
ANISOU 4954  ND2 ASN B 293     5368   4346   3177   -438    229   -287       N  
ATOM   4955  N   ASP B 294     -34.162 -39.785   0.080  1.00 28.76           N  
ANISOU 4955  N   ASP B 294     5447   3750   1731   -303    400   -173       N  
ATOM   4956  CA  ASP B 294     -35.313 -38.941   0.334  1.00 27.81           C  
ANISOU 4956  CA  ASP B 294     5747   3090   1726   -272     90   -310       C  
ATOM   4957  C   ASP B 294     -36.640 -39.611  -0.022  1.00 27.31           C  
ANISOU 4957  C   ASP B 294     5534   3421   1420      8   -181    -90       C  
ATOM   4958  O   ASP B 294     -37.699 -39.229   0.508  1.00 27.26           O  
ANISOU 4958  O   ASP B 294     5382   3713   1262     34   -216    222       O  
ATOM   4959  CB  ASP B 294     -35.161 -37.594  -0.368  1.00 30.49           C  
ANISOU 4959  CB  ASP B 294     5763   3538   2281   -398    -22    121       C  
ATOM   4960  CG  ASP B 294     -34.064 -36.737   0.259  1.00 31.28           C  
ANISOU 4960  CG  ASP B 294     6143   3262   2481   -393      2    -13       C  
ATOM   4961  OD1 ASP B 294     -33.695 -36.996   1.424  1.00 34.68           O  
ANISOU 4961  OD1 ASP B 294     6134   4520   2521   -294   -175   -280       O  
ATOM   4962  OD2 ASP B 294     -33.574 -35.805  -0.402  1.00 32.62           O  
ANISOU 4962  OD2 ASP B 294     5610   3133   3652   -699    129   -121       O  
ATOM   4963  N   ASP B 295     -36.575 -40.616  -0.899  1.00 29.07           N  
ANISOU 4963  N   ASP B 295     5856   3934   1253   -295    -98   -314       N  
ATOM   4964  CA  ASP B 295     -37.790 -41.318  -1.329  1.00 28.32           C  
ANISOU 4964  CA  ASP B 295     5568   4114   1078   -215    -76    -95       C  
ATOM   4965  C   ASP B 295     -38.344 -42.183  -0.192  1.00 27.57           C  
ANISOU 4965  C   ASP B 295     5312   3983   1179   -197    -65    -81       C  
ATOM   4966  O   ASP B 295     -39.559 -42.303  -0.040  1.00 28.08           O  
ANISOU 4966  O   ASP B 295     5166   4070   1433    158   -190   -203       O  
ATOM   4967  CB  ASP B 295     -37.539 -42.194  -2.569  1.00 31.63           C  
ANISOU 4967  CB  ASP B 295     6007   4903   1106   -341      0   -403       C  
ATOM   4968  CG  ASP B 295     -37.498 -41.408  -3.860  1.00 35.24           C  
ANISOU 4968  CG  ASP B 295     6227   5470   1692    -78     -1    229       C  
ATOM   4969  OD1 ASP B 295     -38.137 -40.340  -3.959  1.00 34.89           O  
ANISOU 4969  OD1 ASP B 295     6730   5305   1218   -116   -444    182       O  
ATOM   4970  OD2 ASP B 295     -36.837 -41.898  -4.798  1.00 40.19           O  
ANISOU 4970  OD2 ASP B 295     7036   6811   1423   -226    332    117       O  
ATOM   4971  N   GLU B 296     -37.445 -42.775   0.596  1.00 26.04           N  
ANISOU 4971  N   GLU B 296     5427   3800    664   -175    -86   -350       N  
ATOM   4972  CA  GLU B 296     -37.812 -43.609   1.733  1.00 26.44           C  
ANISOU 4972  CA  GLU B 296     5286   3829    931   -157      1   -149       C  
ATOM   4973  C   GLU B 296     -38.426 -42.758   2.830  1.00 26.16           C  
ANISOU 4973  C   GLU B 296     5069   3479   1389    -17   -172   -273       C  
ATOM   4974  O   GLU B 296     -39.380 -43.182   3.473  1.00 26.54           O  
ANISOU 4974  O   GLU B 296     4830   3948   1306    108   -118   -471       O  
ATOM   4975  CB  GLU B 296     -36.593 -44.373   2.260  1.00 27.30           C  
ANISOU 4975  CB  GLU B 296     5040   3852   1481   -156     28   -165       C  
ATOM   4976  CG  GLU B 296     -36.918 -45.525   3.192  1.00 27.12           C  
ANISOU 4976  CG  GLU B 296     4726   3723   1854   -346    156   -220       C  
ATOM   4977  CD  GLU B 296     -37.749 -46.608   2.517  1.00 26.60           C  
ANISOU 4977  CD  GLU B 296     5259   3717   1129   -160    298   -699       C  
ATOM   4978  OE1 GLU B 296     -38.149 -47.576   3.197  1.00 27.12           O  
ANISOU 4978  OE1 GLU B 296     4940   3514   1848    -15   -115   -406       O  
ATOM   4979  OE2 GLU B 296     -38.015 -46.499   1.309  1.00 30.05           O  
ANISOU 4979  OE2 GLU B 296     6220   3943   1253   -235    163   -427       O  
ATOM   4980  N   VAL B 297     -37.900 -41.550   3.030  1.00 24.62           N  
ANISOU 4980  N   VAL B 297     4990   3196   1165    206   -181   -111       N  
ATOM   4981  CA  VAL B 297     -38.482 -40.615   4.000  1.00 23.54           C  
ANISOU 4981  CA  VAL B 297     4815   3203    925     83   -164      1       C  
ATOM   4982  C   VAL B 297     -39.940 -40.293   3.639  1.00 25.26           C  
ANISOU 4982  C   VAL B 297     4914   3450   1231    327   -171   -193       C  
ATOM   4983  O   VAL B 297     -40.832 -40.291   4.502  1.00 26.68           O  
ANISOU 4983  O   VAL B 297     5113   3533   1489    369     -5   -212       O  
ATOM   4984  CB  VAL B 297     -37.665 -39.307   4.095  1.00 23.57           C  
ANISOU 4984  CB  VAL B 297     4700   3223   1032    199   -243   -299       C  
ATOM   4985  CG1 VAL B 297     -38.383 -38.292   4.975  1.00 24.53           C  
ANISOU 4985  CG1 VAL B 297     4649   3350   1318    262   -169   -297       C  
ATOM   4986  CG2 VAL B 297     -36.273 -39.570   4.652  1.00 22.55           C  
ANISOU 4986  CG2 VAL B 297     4299   3000   1267     75     76   -334       C  
ATOM   4987  N   LYS B 298     -40.166 -40.036   2.352  1.00 26.06           N  
ANISOU 4987  N   LYS B 298     4912   3727   1260    137   -179    -74       N  
ATOM   4988  CA  LYS B 298     -41.488 -39.670   1.840  1.00 27.24           C  
ANISOU 4988  CA  LYS B 298     5025   4005   1318    414   -230    234       C  
ATOM   4989  C   LYS B 298     -42.498 -40.805   2.034  1.00 26.69           C  
ANISOU 4989  C   LYS B 298     4906   3807   1426    461   -403    -74       C  
ATOM   4990  O   LYS B 298     -43.643 -40.582   2.419  1.00 27.73           O  
ANISOU 4990  O   LYS B 298     4953   3969   1612    692   -295     49       O  
ATOM   4991  CB  LYS B 298     -41.413 -39.236   0.370  1.00 30.05           C  
ANISOU 4991  CB  LYS B 298     5683   4046   1687   -167     21    743       C  
ATOM   4992  CG  LYS B 298     -40.822 -37.839   0.191  1.00 37.38           C  
ANISOU 4992  CG  LYS B 298     5987   4390   3824   -588     21    975       C  
ATOM   4993  CD  LYS B 298     -40.992 -37.285  -1.217  1.00 39.90           C  
ANISOU 4993  CD  LYS B 298     6617   3828   4714  -1944    263   2091       C  
ATOM   4994  CE  LYS B 298     -40.349 -35.907  -1.331  1.00 47.45           C  
ANISOU 4994  CE  LYS B 298     7293   4590   6146  -2758    617   3036       C  
ATOM   4995  NZ  LYS B 298     -40.583 -35.224  -2.638  1.00 52.44           N  
ANISOU 4995  NZ  LYS B 298     9785   5122   5017  -1746   1603   2378       N  
ATOM   4996  N   ARG B 299     -42.043 -42.018   1.771  1.00 27.27           N  
ANISOU 4996  N   ARG B 299     4994   3858   1508    434   -259   -258       N  
ATOM   4997  CA  ARG B 299     -42.855 -43.191   1.966  1.00 26.03           C  
ANISOU 4997  CA  ARG B 299     4894   3709   1284    591   -188   -318       C  
ATOM   4998  C   ARG B 299     -43.181 -43.384   3.444  1.00 25.46           C  
ANISOU 4998  C   ARG B 299     4877   3639   1156    496   -452   -296       C  
ATOM   4999  O   ARG B 299     -44.331 -43.570   3.767  1.00 26.62           O  
ANISOU 4999  O   ARG B 299     4776   3745   1591    766   -350   -541       O  
ATOM   5000  CB  ARG B 299     -42.181 -44.416   1.381  1.00 25.76           C  
ANISOU 5000  CB  ARG B 299     4804   3720   1263    494   -468   -619       C  
ATOM   5001  CG  ARG B 299     -43.122 -45.586   1.218  1.00 25.32           C  
ANISOU 5001  CG  ARG B 299     4683   3856   1080    567   -993   -720       C  
ATOM   5002  CD  ARG B 299     -42.434 -46.662   0.415  1.00 26.17           C  
ANISOU 5002  CD  ARG B 299     5004   4030    908    472   -400   -557       C  
ATOM   5003  NE  ARG B 299     -41.352 -47.265   1.171  1.00 25.53           N  
ANISOU 5003  NE  ARG B 299     5185   3498   1017    357   -549   -671       N  
ATOM   5004  CZ  ARG B 299     -41.543 -48.224   2.064  1.00 25.61           C  
ANISOU 5004  CZ  ARG B 299     4837   3555   1338    282   -373   -581       C  
ATOM   5005  NH1 ARG B 299     -40.518 -48.731   2.724  1.00 22.42           N  
ANISOU 5005  NH1 ARG B 299     4732   2935    852    219   -304  -1010       N  
ATOM   5006  NH2 ARG B 299     -42.767 -48.669   2.288  1.00 24.82           N  
ANISOU 5006  NH2 ARG B 299     4669   3609   1152    452   -161   -885       N  
ATOM   5007  N   PHE B 300     -42.190 -43.303   4.334  1.00 24.58           N  
ANISOU 5007  N   PHE B 300     4853   3439   1046    591   -428   -383       N  
ATOM   5008  CA  PHE B 300     -42.410 -43.417   5.776  1.00 23.97           C  
ANISOU 5008  CA  PHE B 300     4446   3547   1115    625   -102   -456       C  
ATOM   5009  C   PHE B 300     -43.406 -42.401   6.316  1.00 25.44           C  
ANISOU 5009  C   PHE B 300     4697   3496   1469    724   -154   -381       C  
ATOM   5010  O   PHE B 300     -44.303 -42.768   7.073  1.00 27.30           O  
ANISOU 5010  O   PHE B 300     4567   3890   1913    637     56   -600       O  
ATOM   5011  CB  PHE B 300     -41.071 -43.345   6.523  1.00 22.88           C  
ANISOU 5011  CB  PHE B 300     4328   3465    901    440     -4   -560       C  
ATOM   5012  CG  PHE B 300     -41.203 -43.192   8.007  1.00 22.71           C  
ANISOU 5012  CG  PHE B 300     4270   3396    962    597    264   -605       C  
ATOM   5013  CD1 PHE B 300     -41.590 -44.271   8.799  1.00 24.49           C  
ANISOU 5013  CD1 PHE B 300     4351   3515   1438    399    213   -442       C  
ATOM   5014  CD2 PHE B 300     -40.939 -41.970   8.616  1.00 23.36           C  
ANISOU 5014  CD2 PHE B 300     4452   3171   1251    629    187   -414       C  
ATOM   5015  CE1 PHE B 300     -41.711 -44.124  10.171  1.00 22.96           C  
ANISOU 5015  CE1 PHE B 300     4171   3150   1401    556    142   -358       C  
ATOM   5016  CE2 PHE B 300     -41.059 -41.823   9.995  1.00 22.16           C  
ANISOU 5016  CE2 PHE B 300     4224   2956   1238    646    203   -315       C  
ATOM   5017  CZ  PHE B 300     -41.443 -42.902  10.772  1.00 22.64           C  
ANISOU 5017  CZ  PHE B 300     4148   3058   1395    526    352   -279       C  
ATOM   5018  N   THR B 301     -43.259 -41.138   5.927  1.00 26.59           N  
ANISOU 5018  N   THR B 301     4832   3500   1770    670    -81   -520       N  
ATOM   5019  CA  THR B 301     -44.117 -40.093   6.495  1.00 28.41           C  
ANISOU 5019  CA  THR B 301     4834   3438   2522    894   -198   -314       C  
ATOM   5020  C   THR B 301     -45.545 -40.133   5.946  1.00 29.96           C  
ANISOU 5020  C   THR B 301     5019   3998   2364    612   -367   -235       C  
ATOM   5021  O   THR B 301     -46.489 -39.815   6.667  1.00 33.37           O  
ANISOU 5021  O   THR B 301     5025   4502   3149    737   -304   -476       O  
ATOM   5022  CB  THR B 301     -43.536 -38.672   6.341  1.00 27.82           C  
ANISOU 5022  CB  THR B 301     4993   3585   1991    713   -355   -435       C  
ATOM   5023  OG1 THR B 301     -43.368 -38.371   4.959  1.00 29.40           O  
ANISOU 5023  OG1 THR B 301     5329   3647   2192    750     -5   -136       O  
ATOM   5024  CG2 THR B 301     -42.198 -38.535   7.056  1.00 27.10           C  
ANISOU 5024  CG2 THR B 301     4816   3409   2072    523   -144   -500       C  
ATOM   5025  N   SER B 302     -45.702 -40.523   4.684  1.00 29.81           N  
ANISOU 5025  N   SER B 302     5039   3943   2343    725   -369   -135       N  
ATOM   5026  CA  SER B 302     -47.036 -40.669   4.102  1.00 32.37           C  
ANISOU 5026  CA  SER B 302     5330   4594   2376    576   -675     31       C  
ATOM   5027  C   SER B 302     -47.799 -41.880   4.650  1.00 30.72           C  
ANISOU 5027  C   SER B 302     4770   4340   2560    683   -589   -341       C  
ATOM   5028  O   SER B 302     -49.015 -41.830   4.800  1.00 32.90           O  
ANISOU 5028  O   SER B 302     4623   5088   2788    802   -756   -465       O  
ATOM   5029  CB  SER B 302     -46.972 -40.736   2.576  1.00 34.69           C  
ANISOU 5029  CB  SER B 302     5863   4817   2501    817   -120   -296       C  
ATOM   5030  OG  SER B 302     -46.517 -42.003   2.151  1.00 37.60           O  
ANISOU 5030  OG  SER B 302     6111   5127   3048    759   -170   -702       O  
ATOM   5031  N   GLU B 303     -47.088 -42.968   4.928  1.00 28.23           N  
ANISOU 5031  N   GLU B 303     4710   3992   2023    759   -354   -729       N  
ATOM   5032  CA  GLU B 303     -47.729 -44.176   5.443  1.00 28.41           C  
ANISOU 5032  CA  GLU B 303     4781   4041   1970    600   -268  -1018       C  
ATOM   5033  C   GLU B 303     -48.019 -44.079   6.932  1.00 27.81           C  
ANISOU 5033  C   GLU B 303     4346   4279   1939    550   -314   -839       C  
ATOM   5034  O   GLU B 303     -49.001 -44.641   7.399  1.00 28.48           O  
ANISOU 5034  O   GLU B 303     4783   4433   1603     55   -359  -1108       O  
ATOM   5035  CB  GLU B 303     -46.896 -45.431   5.149  1.00 26.11           C  
ANISOU 5035  CB  GLU B 303     4486   4256   1176    677   -352  -1030       C  
ATOM   5036  CG  GLU B 303     -46.854 -45.790   3.663  1.00 27.06           C  
ANISOU 5036  CG  GLU B 303     4969   4242   1068    848   -166   -789       C  
ATOM   5037  CD  GLU B 303     -46.087 -47.064   3.360  1.00 27.87           C  
ANISOU 5037  CD  GLU B 303     4661   4384   1545    781   -877  -1375       C  
ATOM   5038  OE1 GLU B 303     -45.389 -47.590   4.246  1.00 27.03           O  
ANISOU 5038  OE1 GLU B 303     4361   4099   1808    939   -417   -842       O  
ATOM   5039  OE2 GLU B 303     -46.194 -47.556   2.229  1.00 32.15           O  
ANISOU 5039  OE2 GLU B 303     6053   4758   1404    887   -764  -1354       O  
ATOM   5040  N   ARG B 304     -47.162 -43.367   7.658  1.00 27.10           N  
ANISOU 5040  N   ARG B 304     4537   4114   1645    707   -452   -769       N  
ATOM   5041  CA  ARG B 304     -47.248 -43.303   9.114  1.00 25.68           C  
ANISOU 5041  CA  ARG B 304     4365   3732   1658    608   -401   -868       C  
ATOM   5042  C   ARG B 304     -47.444 -41.868   9.583  1.00 25.65           C  
ANISOU 5042  C   ARG B 304     4019   3738   1988    641   -350   -772       C  
ATOM   5043  O   ARG B 304     -46.583 -41.018   9.400  1.00 28.33           O  
ANISOU 5043  O   ARG B 304     4581   3871   2308    509     18   -526       O  
ATOM   5044  CB  ARG B 304     -45.977 -43.882   9.749  1.00 24.70           C  
ANISOU 5044  CB  ARG B 304     4272   3566   1544    606   -240   -658       C  
ATOM   5045  CG  ARG B 304     -45.519 -45.217   9.177  1.00 26.13           C  
ANISOU 5045  CG  ARG B 304     4533   3509   1885    361   -172   -950       C  
ATOM   5046  CD  ARG B 304     -46.392 -46.366   9.674  1.00 25.63           C  
ANISOU 5046  CD  ARG B 304     4195   3517   2023    530   -183   -775       C  
ATOM   5047  NE  ARG B 304     -46.070 -47.609   9.000  1.00 27.67           N  
ANISOU 5047  NE  ARG B 304     4252   3781   2479    266   -407  -1423       N  
ATOM   5048  CZ  ARG B 304     -46.812 -48.708   9.050  1.00 27.14           C  
ANISOU 5048  CZ  ARG B 304     3254   4317   2738    278   -407  -1290       C  
ATOM   5049  NH1 ARG B 304     -47.941 -48.732   9.756  1.00 26.06           N  
ANISOU 5049  NH1 ARG B 304     3114   4614   2172    547   -658  -1205       N  
ATOM   5050  NH2 ARG B 304     -46.396 -49.800   8.411  1.00 29.29           N  
ANISOU 5050  NH2 ARG B 304     4346   4121   2661    105   -141  -1303       N  
ATOM   5051  N   ASN B 305     -48.571 -41.585  10.200  1.00 23.62           N  
ANISOU 5051  N   ASN B 305     3546   3883   1544    626   -821   -867       N  
ATOM   5052  CA  ASN B 305     -48.795 -40.240  10.653  1.00 24.30           C  
ANISOU 5052  CA  ASN B 305     3581   3812   1839    578   -807   -812       C  
ATOM   5053  C   ASN B 305     -48.285 -40.093  12.083  1.00 22.68           C  
ANISOU 5053  C   ASN B 305     3483   3524   1611    451   -514   -641       C  
ATOM   5054  O   ASN B 305     -49.068 -39.890  12.991  1.00 24.76           O  
ANISOU 5054  O   ASN B 305     3625   4087   1693    517   -389   -455       O  
ATOM   5055  CB  ASN B 305     -50.285 -39.930  10.558  1.00 28.22           C  
ANISOU 5055  CB  ASN B 305     3646   4549   2524    781   -775   -731       C  
ATOM   5056  CG  ASN B 305     -50.601 -38.478  10.838  1.00 30.70           C  
ANISOU 5056  CG  ASN B 305     3534   4647   3481    857   -758   -310       C  
ATOM   5057  OD1 ASN B 305     -49.703 -37.661  10.998  1.00 35.01           O  
ANISOU 5057  OD1 ASN B 305     4481   5109   3712    244   -483   -292       O  
ATOM   5058  ND2 ASN B 305     -51.886 -38.150  10.909  1.00 33.89           N  
ANISOU 5058  ND2 ASN B 305     3600   5499   3774   1045   -373   -329       N  
ATOM   5059  N   TRP B 306     -46.973 -40.209  12.280  1.00 19.47           N  
ANISOU 5059  N   TRP B 306     3423   2970   1004    550   -482   -670       N  
ATOM   5060  CA  TRP B 306     -46.407 -40.257  13.631  1.00 18.96           C  
ANISOU 5060  CA  TRP B 306     3491   2886    827    300   -276   -436       C  
ATOM   5061  C   TRP B 306     -45.922 -38.911  14.092  1.00 19.60           C  
ANISOU 5061  C   TRP B 306     3523   3010    912     95    -38   -369       C  
ATOM   5062  O   TRP B 306     -45.294 -38.192  13.324  1.00 19.67           O  
ANISOU 5062  O   TRP B 306     3704   2694   1076    160    -55   -300       O  
ATOM   5063  CB  TRP B 306     -45.242 -41.236  13.671  1.00 19.18           C  
ANISOU 5063  CB  TRP B 306     3520   2875    892    291   -271   -381       C  
ATOM   5064  CG  TRP B 306     -45.621 -42.686  13.503  1.00 19.27           C  
ANISOU 5064  CG  TRP B 306     3702   2807    813    298   -136   -323       C  
ATOM   5065  CD1 TRP B 306     -46.884 -43.211  13.310  1.00 19.91           C  
ANISOU 5065  CD1 TRP B 306     3855   2655   1055    303   -167   -577       C  
ATOM   5066  CD2 TRP B 306     -44.731 -43.836  13.499  1.00 20.00           C  
ANISOU 5066  CD2 TRP B 306     3856   2878    865    335     48   -464       C  
ATOM   5067  NE1 TRP B 306     -46.831 -44.567  13.195  1.00 21.49           N  
ANISOU 5067  NE1 TRP B 306     4112   2684   1370    518    -33   -700       N  
ATOM   5068  CE2 TRP B 306     -45.579 -45.002  13.292  1.00 21.34           C  
ANISOU 5068  CE2 TRP B 306     3959   2950   1198    301    -26   -563       C  
ATOM   5069  CE3 TRP B 306     -43.377 -44.010  13.636  1.00 20.66           C  
ANISOU 5069  CE3 TRP B 306     3854   2968   1024    301     96   -253       C  
ATOM   5070  CZ2 TRP B 306     -45.073 -46.270  13.230  1.00 22.19           C  
ANISOU 5070  CZ2 TRP B 306     3974   3073   1382    426    -83   -190       C  
ATOM   5071  CZ3 TRP B 306     -42.868 -45.296  13.558  1.00 21.53           C  
ANISOU 5071  CZ3 TRP B 306     4167   2923   1088    306    -49   -478       C  
ATOM   5072  CH2 TRP B 306     -43.703 -46.402  13.358  1.00 22.72           C  
ANISOU 5072  CH2 TRP B 306     3922   3061   1650    354      2   -277       C  
ATOM   5073  N   LEU B 307     -46.210 -38.538  15.336  1.00 19.83           N  
ANISOU 5073  N   LEU B 307     3467   3064   1002    237    -49   -514       N  
ATOM   5074  CA  LEU B 307     -45.640 -37.316  15.877  1.00 18.45           C  
ANISOU 5074  CA  LEU B 307     3094   2899   1014    188     50   -222       C  
ATOM   5075  C   LEU B 307     -44.303 -37.646  16.473  1.00 17.79           C  
ANISOU 5075  C   LEU B 307     3223   2761    773    160     76   -165       C  
ATOM   5076  O   LEU B 307     -44.197 -38.404  17.460  1.00 17.15           O  
ANISOU 5076  O   LEU B 307     3184   2941    391     65     -2   -327       O  
ATOM   5077  CB  LEU B 307     -46.557 -36.704  16.918  1.00 18.28           C  
ANISOU 5077  CB  LEU B 307     3177   2993    774     43    -17   -356       C  
ATOM   5078  CG  LEU B 307     -48.006 -36.709  16.432  1.00 18.21           C  
ANISOU 5078  CG  LEU B 307     3008   3173    738     68    260   -108       C  
ATOM   5079  CD1 LEU B 307     -48.910 -36.300  17.576  1.00 19.20           C  
ANISOU 5079  CD1 LEU B 307     3134   3127   1034    -18    290   -647       C  
ATOM   5080  CD2 LEU B 307     -48.222 -35.787  15.232  1.00 18.98           C  
ANISOU 5080  CD2 LEU B 307     3027   3337    847    -49   -179    -43       C  
ATOM   5081  N   ILE B 308     -43.281 -37.107  15.820  1.00 17.40           N  
ANISOU 5081  N   ILE B 308     3231   2537    841    140     16   -267       N  
ATOM   5082  CA  ILE B 308     -41.883 -37.411  16.115  1.00 16.98           C  
ANISOU 5082  CA  ILE B 308     3231   2512    705    129     21   -314       C  
ATOM   5083  C   ILE B 308     -41.054 -36.142  16.141  1.00 18.34           C  
ANISOU 5083  C   ILE B 308     3336   2536   1094    197    -49   -232       C  
ATOM   5084  O   ILE B 308     -41.583 -35.042  16.209  1.00 19.14           O  
ANISOU 5084  O   ILE B 308     3368   2605   1297    308    -15   -321       O  
ATOM   5085  CB  ILE B 308     -41.257 -38.450  15.138  1.00 16.58           C  
ANISOU 5085  CB  ILE B 308     3304   2333    661    138    137   -143       C  
ATOM   5086  CG1 ILE B 308     -41.425 -38.022  13.666  1.00 16.79           C  
ANISOU 5086  CG1 ILE B 308     3404   2346    627    258    119   -233       C  
ATOM   5087  CG2 ILE B 308     -41.870 -39.825  15.373  1.00 16.43           C  
ANISOU 5087  CG2 ILE B 308     3486   2302    453    100    273   -257       C  
ATOM   5088  CD1 ILE B 308     -41.026 -39.093  12.668  1.00 15.75           C  
ANISOU 5088  CD1 ILE B 308     3222   2212    551    313    201    -89       C  
ATOM   5089  N   SER B 309     -39.741 -36.280  16.094  1.00 17.70           N  
ANISOU 5089  N   SER B 309     3284   2685    753    166      1   -290       N  
ATOM   5090  CA  SER B 309     -38.914 -35.104  16.303  1.00 18.22           C  
ANISOU 5090  CA  SER B 309     3481   2645    793    143    -81    -32       C  
ATOM   5091  C   SER B 309     -37.703 -35.087  15.384  1.00 19.40           C  
ANISOU 5091  C   SER B 309     3357   2716   1296    298    -70    -79       C  
ATOM   5092  O   SER B 309     -37.195 -36.121  15.013  1.00 17.96           O  
ANISOU 5092  O   SER B 309     3337   2724    762    115    158    -36       O  
ATOM   5093  CB  SER B 309     -38.461 -35.054  17.762  1.00 18.80           C  
ANISOU 5093  CB  SER B 309     3392   2883    866    210   -172   -238       C  
ATOM   5094  OG  SER B 309     -37.427 -34.114  17.887  1.00 20.91           O  
ANISOU 5094  OG  SER B 309     3486   3051   1407    169   -157   -124       O  
ATOM   5095  N   GLN B 310     -37.180 -33.925  15.007  1.00 18.66           N  
ANISOU 5095  N   GLN B 310     3382   2847    858    196   -206    -66       N  
ATOM   5096  CA  GLN B 310     -35.977 -33.951  14.158  1.00 19.32           C  
ANISOU 5096  CA  GLN B 310     3467   2992    880    214   -293    218       C  
ATOM   5097  C   GLN B 310     -34.754 -33.327  14.777  1.00 21.72           C  
ANISOU 5097  C   GLN B 310     3443   3211   1595    195   -142   -199       C  
ATOM   5098  O   GLN B 310     -33.636 -33.609  14.367  1.00 26.08           O  
ANISOU 5098  O   GLN B 310     3708   4201   1997    394     92     22       O  
ATOM   5099  CB  GLN B 310     -36.197 -33.328  12.771  1.00 20.78           C  
ANISOU 5099  CB  GLN B 310     3873   3248    775    130   -153    245       C  
ATOM   5100  CG  GLN B 310     -36.631 -34.321  11.708  1.00 20.02           C  
ANISOU 5100  CG  GLN B 310     3669   2940    997    335    188     61       C  
ATOM   5101  CD  GLN B 310     -36.286 -33.893  10.289  1.00 21.49           C  
ANISOU 5101  CD  GLN B 310     4004   3234    925    596    -68    294       C  
ATOM   5102  OE1 GLN B 310     -36.855 -32.939   9.758  1.00 24.93           O  
ANISOU 5102  OE1 GLN B 310     4552   3292   1626    900    -93    351       O  
ATOM   5103  NE2 GLN B 310     -35.380 -34.636   9.652  1.00 19.51           N  
ANISOU 5103  NE2 GLN B 310     3736   2922    751    272    -51    211       N  
ATOM   5104  N   GLY B 311     -34.936 -32.469  15.744  1.00 21.25           N  
ANISOU 5104  N   GLY B 311     3309   3129   1636    113    -95   -221       N  
ATOM   5105  CA  GLY B 311     -33.783 -31.953  16.402  1.00 18.28           C  
ANISOU 5105  CA  GLY B 311     3311   3057    575    315     67   -129       C  
ATOM   5106  C   GLY B 311     -34.334 -30.862  17.257  1.00 18.35           C  
ANISOU 5106  C   GLY B 311     3278   2751    942    336   -156   -103       C  
ATOM   5107  O   GLY B 311     -35.549 -30.733  17.353  1.00 19.38           O  
ANISOU 5107  O   GLY B 311     3254   2775   1335    242    138      1       O  
ATOM   5108  N   SER B 312     -33.440 -30.066  17.839  1.00 16.84           N  
ANISOU 5108  N   SER B 312     3276   2573    548    323     68   -133       N  
ATOM   5109  CA  SER B 312     -33.801 -29.006  18.793  1.00 18.80           C  
ANISOU 5109  CA  SER B 312     3681   2395   1067    200     40   -280       C  
ATOM   5110  C   SER B 312     -34.564 -27.894  18.116  1.00 17.65           C  
ANISOU 5110  C   SER B 312     3221   2550    933    312    166   -379       C  
ATOM   5111  O   SER B 312     -34.427 -27.666  16.894  1.00 18.37           O  
ANISOU 5111  O   SER B 312     3206   2797    975    244     53   -102       O  
ATOM   5112  CB  SER B 312     -32.562 -28.404  19.454  1.00 19.32           C  
ANISOU 5112  CB  SER B 312     3609   2735    994     98      3     92       C  
ATOM   5113  OG  SER B 312     -31.924 -27.484  18.573  1.00 18.43           O  
ANISOU 5113  OG  SER B 312     3466   2521   1012    234    122    -61       O  
ATOM   5114  N   ALA B 313     -35.309 -27.148  18.946  1.00 17.18           N  
ANISOU 5114  N   ALA B 313     3236   2624    667    316    181   -242       N  
ATOM   5115  CA  ALA B 313     -36.046 -25.934  18.520  1.00 17.41           C  
ANISOU 5115  CA  ALA B 313     2961   2641   1011    515    364   -452       C  
ATOM   5116  C   ALA B 313     -35.154 -24.824  17.955  1.00 18.60           C  
ANISOU 5116  C   ALA B 313     3276   2566   1223    474     18   -146       C  
ATOM   5117  O   ALA B 313     -35.554 -24.102  17.033  1.00 18.38           O  
ANISOU 5117  O   ALA B 313     3507   2719    755    325     61   -197       O  
ATOM   5118  CB  ALA B 313     -36.877 -25.370  19.666  1.00 17.96           C  
ANISOU 5118  CB  ALA B 313     3258   2810    753    426    309   -535       C  
ATOM   5119  N   SER B 314     -33.982 -24.645  18.561  1.00 17.75           N  
ANISOU 5119  N   SER B 314     3230   2742    770    347    215   -347       N  
ATOM   5120  CA  SER B 314     -33.082 -23.633  18.052  1.00 18.66           C  
ANISOU 5120  CA  SER B 314     3414   2715    960    220    116   -341       C  
ATOM   5121  C   SER B 314     -32.515 -24.022  16.713  1.00 18.03           C  
ANISOU 5121  C   SER B 314     3319   2604    925    358    123   -172       C  
ATOM   5122  O   SER B 314     -32.314 -23.153  15.914  1.00 18.56           O  
ANISOU 5122  O   SER B 314     3507   2718    826    417    213    -96       O  
ATOM   5123  CB  SER B 314     -31.975 -23.257  19.020  1.00 22.78           C  
ANISOU 5123  CB  SER B 314     4059   3109   1485    459   -528   -420       C  
ATOM   5124  OG  SER B 314     -31.363 -24.411  19.502  1.00 25.55           O  
ANISOU 5124  OG  SER B 314     4048   3328   2331    556   -502   -302       O  
ATOM   5125  N   ASN B 315     -32.248 -25.301  16.485  1.00 17.13           N  
ANISOU 5125  N   ASN B 315     3282   2519    705    260     20   -144       N  
ATOM   5126  CA  ASN B 315     -31.877 -25.702  15.142  1.00 18.11           C  
ANISOU 5126  CA  ASN B 315     3469   2637    774    404     85   -178       C  
ATOM   5127  C   ASN B 315     -33.000 -25.532  14.142  1.00 18.55           C  
ANISOU 5127  C   ASN B 315     3510   2677    860    405    -29     87       C  
ATOM   5128  O   ASN B 315     -32.759 -25.148  12.992  1.00 18.33           O  
ANISOU 5128  O   ASN B 315     3486   2588    890    382    113     -2       O  
ATOM   5129  CB  ASN B 315     -31.249 -27.093  15.118  1.00 18.29           C  
ANISOU 5129  CB  ASN B 315     3331   2679    939    455     72    103       C  
ATOM   5130  CG  ASN B 315     -29.866 -27.086  15.723  1.00 18.22           C  
ANISOU 5130  CG  ASN B 315     3497   2529    896    362     86    376       C  
ATOM   5131  OD1 ASN B 315     -28.935 -26.442  15.212  1.00 21.10           O  
ANISOU 5131  OD1 ASN B 315     3963   2739   1313     94    315    399       O  
ATOM   5132  ND2 ASN B 315     -29.736 -27.752  16.846  1.00 15.50           N  
ANISOU 5132  ND2 ASN B 315     2971   2303    614    525     91     82       N  
ATOM   5133  N   ALA B 316     -34.229 -25.764  14.569  1.00 18.66           N  
ANISOU 5133  N   ALA B 316     3436   2791    860    388    -41    -59       N  
ATOM   5134  CA  ALA B 316     -35.306 -25.533  13.621  1.00 18.40           C  
ANISOU 5134  CA  ALA B 316     3543   2849    598    234    -49    111       C  
ATOM   5135  C   ALA B 316     -35.360 -24.060  13.244  1.00 19.22           C  
ANISOU 5135  C   ALA B 316     3755   2840    708    359    -41     22       C  
ATOM   5136  O   ALA B 316     -35.565 -23.717  12.084  1.00 19.89           O  
ANISOU 5136  O   ALA B 316     3862   2990    705    224    -71     77       O  
ATOM   5137  CB  ALA B 316     -36.636 -26.008  14.167  1.00 20.06           C  
ANISOU 5137  CB  ALA B 316     3523   3158    939    223     36    284       C  
ATOM   5138  N   MET B 317     -35.107 -23.201  14.221  1.00 18.82           N  
ANISOU 5138  N   MET B 317     3570   2803    777    329    -86     27       N  
ATOM   5139  CA  MET B 317     -35.230 -21.793  14.054  1.00 19.52           C  
ANISOU 5139  CA  MET B 317     3761   2805    849    301     61   -110       C  
ATOM   5140  C   MET B 317     -34.108 -21.243  13.183  1.00 19.21           C  
ANISOU 5140  C   MET B 317     3701   2814    782    349     36   -200       C  
ATOM   5141  O   MET B 317     -34.311 -20.305  12.446  1.00 21.27           O  
ANISOU 5141  O   MET B 317     4047   2900   1132    289     53    -15       O  
ATOM   5142  CB  MET B 317     -35.247 -21.146  15.443  1.00 21.02           C  
ANISOU 5142  CB  MET B 317     3939   3156    891    404   -143   -246       C  
ATOM   5143  CG  MET B 317     -35.688 -19.708  15.484  1.00 25.28           C  
ANISOU 5143  CG  MET B 317     4550   3224   1828    375    156    107       C  
ATOM   5144  SD  MET B 317     -37.356 -19.565  14.826  1.00 32.49           S  
ANISOU 5144  SD  MET B 317     4543   4342   3460    689    266   -194       S  
ATOM   5145  CE  MET B 317     -38.087 -21.023  15.550  1.00 30.14           C  
ANISOU 5145  CE  MET B 317     5007   4229   2213    478    113     -3       C  
ATOM   5146  N   SER B 318     -32.926 -21.819  13.280  1.00 18.59           N  
ANISOU 5146  N   SER B 318     3672   2750    641    283    117    -45       N  
ATOM   5147  CA  SER B 318     -31.817 -21.398  12.453  1.00 19.74           C  
ANISOU 5147  CA  SER B 318     3624   3070    805    236    105   -123       C  
ATOM   5148  C   SER B 318     -31.775 -22.150  11.126  1.00 19.78           C  
ANISOU 5148  C   SER B 318     3671   2930    913    281    128   -179       C  
ATOM   5149  O   SER B 318     -30.850 -21.934  10.328  1.00 19.50           O  
ANISOU 5149  O   SER B 318     3794   2801    812    323    149   -171       O  
ATOM   5150  CB  SER B 318     -30.498 -21.612  13.204  1.00 19.47           C  
ANISOU 5150  CB  SER B 318     3648   2703   1046    252    118    -24       C  
ATOM   5151  OG  SER B 318     -30.276 -22.990  13.499  1.00 20.45           O  
ANISOU 5151  OG  SER B 318     3609   2801   1356    539     58    -43       O  
ATOM   5152  N   ASN B 319     -32.749 -23.031  10.878  1.00 19.83           N  
ANISOU 5152  N   ASN B 319     3806   2918    810    257    -37   -145       N  
ATOM   5153  CA  ASN B 319     -32.763 -23.836   9.653  1.00 19.02           C  
ANISOU 5153  CA  ASN B 319     3745   2599    883    308    160   -123       C  
ATOM   5154  C   ASN B 319     -31.442 -24.591   9.470  1.00 19.07           C  
ANISOU 5154  C   ASN B 319     3773   2748    722    309    102    -39       C  
ATOM   5155  O   ASN B 319     -30.829 -24.554   8.399  1.00 19.89           O  
ANISOU 5155  O   ASN B 319     3903   2893    760    277    184      0       O  
ATOM   5156  CB  ASN B 319     -33.012 -22.929   8.450  1.00 20.62           C  
ANISOU 5156  CB  ASN B 319     3849   2955   1030    261    -59     53       C  
ATOM   5157  CG  ASN B 319     -33.652 -23.653   7.283  1.00 20.17           C  
ANISOU 5157  CG  ASN B 319     3994   2453   1215    282     74    -83       C  
ATOM   5158  OD1 ASN B 319     -33.915 -23.047   6.239  1.00 23.62           O  
ANISOU 5158  OD1 ASN B 319     4280   3220   1474    323    -17    285       O  
ATOM   5159  ND2 ASN B 319     -33.919 -24.939   7.446  1.00 17.33           N  
ANISOU 5159  ND2 ASN B 319     3882   2377    323    251    260   -312       N  
ATOM   5160  N   THR B 320     -30.998 -25.257  10.536  1.00 18.46           N  
ANISOU 5160  N   THR B 320     3672   2636    704    390    190    -62       N  
ATOM   5161  CA  THR B 320     -29.769 -26.062  10.528  1.00 18.40           C  
ANISOU 5161  CA  THR B 320     3655   2680    654    310     -3    180       C  
ATOM   5162  C   THR B 320     -30.027 -27.445  11.135  1.00 18.23           C  
ANISOU 5162  C   THR B 320     3511   2526    887    361    146     64       C  
ATOM   5163  O   THR B 320     -31.016 -27.639  11.838  1.00 18.06           O  
ANISOU 5163  O   THR B 320     3542   2819    500    367     93    182       O  
ATOM   5164  CB  THR B 320     -28.629 -25.338  11.271  1.00 18.18           C  
ANISOU 5164  CB  THR B 320     3404   2588    913    311    240    -41       C  
ATOM   5165  OG1 THR B 320     -29.018 -25.115  12.625  1.00 18.11           O  
ANISOU 5165  OG1 THR B 320     3432   2686    762    453      6     43       O  
ATOM   5166  CG2 THR B 320     -28.389 -23.975  10.643  1.00 20.26           C  
ANISOU 5166  CG2 THR B 320     3798   2901   1000    216    208    285       C  
ATOM   5167  N   PRO B 321     -29.167 -28.409  10.800  1.00 17.73           N  
ANISOU 5167  N   PRO B 321     3394   2507    835    345    105    255       N  
ATOM   5168  CA  PRO B 321     -29.370 -29.759  11.301  1.00 18.02           C  
ANISOU 5168  CA  PRO B 321     3621   2452    773    599    120    249       C  
ATOM   5169  C   PRO B 321     -29.220 -29.759  12.804  1.00 17.43           C  
ANISOU 5169  C   PRO B 321     3497   2369    753    490    227    118       C  
ATOM   5170  O   PRO B 321     -28.678 -28.812  13.356  1.00 18.81           O  
ANISOU 5170  O   PRO B 321     3435   2742    967    169     76    241       O  
ATOM   5171  CB  PRO B 321     -28.224 -30.550  10.691  1.00 19.03           C  
ANISOU 5171  CB  PRO B 321     3611   2614   1003    505    444    403       C  
ATOM   5172  CG  PRO B 321     -27.677 -29.723   9.583  1.00 18.96           C  
ANISOU 5172  CG  PRO B 321     3730   2476    995    416    419    359       C  
ATOM   5173  CD  PRO B 321     -28.044 -28.294   9.850  1.00 17.93           C  
ANISOU 5173  CD  PRO B 321     3484   2513    814    526    166    204       C  
ATOM   5174  N   SER B 322     -29.695 -30.819  13.444  1.00 17.76           N  
ANISOU 5174  N   SER B 322     3517   2321    907    542   -206    371       N  
ATOM   5175  CA  SER B 322     -29.495 -31.054  14.872  1.00 17.07           C  
ANISOU 5175  CA  SER B 322     3164   2503    816    358   -120    179       C  
ATOM   5176  C   SER B 322     -28.043 -30.870  15.248  1.00 16.42           C  
ANISOU 5176  C   SER B 322     3111   2498    628    250      2    116       C  
ATOM   5177  O   SER B 322     -27.171 -31.356  14.542  1.00 17.42           O  
ANISOU 5177  O   SER B 322     3238   2591    788    443    -91   -139       O  
ATOM   5178  CB  SER B 322     -29.841 -32.505  15.166  1.00 17.21           C  
ANISOU 5178  CB  SER B 322     3279   2550    709    310   -172    294       C  
ATOM   5179  OG  SER B 322     -29.252 -32.953  16.371  1.00 15.99           O  
ANISOU 5179  OG  SER B 322     3105   2398    573    409   -148     31       O  
ATOM   5180  N   HIS B 323     -27.775 -30.184  16.354  1.00 15.60           N  
ANISOU 5180  N   HIS B 323     3026   2355    543    326     -4    186       N  
ATOM   5181  CA  HIS B 323     -26.408 -30.030  16.798  1.00 16.24           C  
ANISOU 5181  CA  HIS B 323     2963   2411    795    244     60    -41       C  
ATOM   5182  C   HIS B 323     -25.859 -31.364  17.161  1.00 16.33           C  
ANISOU 5182  C   HIS B 323     3021   2453    729    289     36    -15       C  
ATOM   5183  O   HIS B 323     -24.670 -31.566  17.063  1.00 17.93           O  
ANISOU 5183  O   HIS B 323     3128   2570   1113    412    -46     45       O  
ATOM   5184  CB  HIS B 323     -26.285 -29.038  17.963  1.00 15.61           C  
ANISOU 5184  CB  HIS B 323     2836   2432    662    321     52     -1       C  
ATOM   5185  CG  HIS B 323     -26.901 -29.512  19.260  1.00 15.99           C  
ANISOU 5185  CG  HIS B 323     2949   2385    738    316    112     63       C  
ATOM   5186  ND1 HIS B 323     -28.235 -29.653  19.429  1.00 16.19           N  
ANISOU 5186  ND1 HIS B 323     2990   2498    661    234      6     16       N  
ATOM   5187  CD2 HIS B 323     -26.314 -29.817  20.482  1.00 16.46           C  
ANISOU 5187  CD2 HIS B 323     2917   2600    736    250     90     13       C  
ATOM   5188  CE1 HIS B 323     -28.486 -30.067  20.684  1.00 16.36           C  
ANISOU 5188  CE1 HIS B 323     2978   2560    677    240     22     45       C  
ATOM   5189  NE2 HIS B 323     -27.306 -30.157  21.334  1.00 16.15           N  
ANISOU 5189  NE2 HIS B 323     2930   2690    514    330    101     18       N  
ATOM   5190  N   VAL B 324     -26.723 -32.274  17.594  1.00 15.57           N  
ANISOU 5190  N   VAL B 324     3097   2331    486    271   -120    -87       N  
ATOM   5191  CA  VAL B 324     -26.281 -33.596  18.026  1.00 16.12           C  
ANISOU 5191  CA  VAL B 324     3171   2255    696    270    -67   -183       C  
ATOM   5192  C   VAL B 324     -25.841 -34.402  16.806  1.00 17.01           C  
ANISOU 5192  C   VAL B 324     2988   2582    890    335     50   -295       C  
ATOM   5193  O   VAL B 324     -24.744 -34.973  16.771  1.00 16.68           O  
ANISOU 5193  O   VAL B 324     2995   2677    665    316     75   -191       O  
ATOM   5194  CB  VAL B 324     -27.388 -34.327  18.812  1.00 16.84           C  
ANISOU 5194  CB  VAL B 324     3391   2217    788    247    138   -296       C  
ATOM   5195  CG1 VAL B 324     -26.981 -35.771  19.079  1.00 16.35           C  
ANISOU 5195  CG1 VAL B 324     3043   2329    839    403    223   -256       C  
ATOM   5196  CG2 VAL B 324     -27.643 -33.612  20.140  1.00 16.14           C  
ANISOU 5196  CG2 VAL B 324     3042   2400    689    225    -30   -315       C  
ATOM   5197  N   LEU B 325     -26.686 -34.409  15.786  1.00 16.52           N  
ANISOU 5197  N   LEU B 325     3266   2430    579    206     58    -63       N  
ATOM   5198  CA  LEU B 325     -26.377 -35.133  14.546  1.00 17.76           C  
ANISOU 5198  CA  LEU B 325     3177   2720    848    297    102   -310       C  
ATOM   5199  C   LEU B 325     -25.104 -34.646  13.865  1.00 18.65           C  
ANISOU 5199  C   LEU B 325     3313   2892    879    267     57    -62       C  
ATOM   5200  O   LEU B 325     -24.318 -35.457  13.376  1.00 18.96           O  
ANISOU 5200  O   LEU B 325     3235   2938   1030    334     13     10       O  
ATOM   5201  CB  LEU B 325     -27.567 -35.095  13.583  1.00 18.23           C  
ANISOU 5201  CB  LEU B 325     3220   2826    879    262     38      0       C  
ATOM   5202  CG  LEU B 325     -28.891 -35.696  14.081  1.00 18.71           C  
ANISOU 5202  CG  LEU B 325     3335   2615   1158    209     62     94       C  
ATOM   5203  CD1 LEU B 325     -29.920 -35.632  12.964  1.00 19.93           C  
ANISOU 5203  CD1 LEU B 325     3470   2842   1260    183    -82   -126       C  
ATOM   5204  CD2 LEU B 325     -28.737 -37.117  14.614  1.00 17.45           C  
ANISOU 5204  CD2 LEU B 325     3208   2648    774    168    124     46       C  
ATOM   5205  N   THR B 326     -24.886 -33.336  13.856  1.00 17.99           N  
ANISOU 5205  N   THR B 326     3285   2900    649    255    -44   -109       N  
ATOM   5206  CA  THR B 326     -23.658 -32.831  13.245  1.00 19.48           C  
ANISOU 5206  CA  THR B 326     3216   3182   1001    260   -105    263       C  
ATOM   5207  C   THR B 326     -22.407 -33.130  14.064  1.00 18.77           C  
ANISOU 5207  C   THR B 326     3091   3272    770    336     52      4       C  
ATOM   5208  O   THR B 326     -21.363 -33.429  13.542  1.00 18.84           O  
ANISOU 5208  O   THR B 326     2857   3433    868    324    -18    387       O  
ATOM   5209  CB  THR B 326     -23.730 -31.391  12.645  1.00 20.91           C  
ANISOU 5209  CB  THR B 326     3468   2996   1479    426   -145    -14       C  
ATOM   5210  OG1 THR B 326     -22.965 -30.439  13.395  1.00 26.67           O  
ANISOU 5210  OG1 THR B 326     4300   3846   1987    243   -752   -290       O  
ATOM   5211  CG2 THR B 326     -25.110 -30.915  12.444  1.00 16.12           C  
ANISOU 5211  CG2 THR B 326     3223   2385    516    369    135   -116       C  
ATOM   5212  N   ALA B 327     -22.549 -33.143  15.371  1.00 18.08           N  
ANISOU 5212  N   ALA B 327     3073   3003    792    339    123    232       N  
ATOM   5213  CA  ALA B 327     -21.437 -33.457  16.215  1.00 17.68           C  
ANISOU 5213  CA  ALA B 327     2954   3079    681    382    179     13       C  
ATOM   5214  C   ALA B 327     -20.974 -34.901  16.034  1.00 18.82           C  
ANISOU 5214  C   ALA B 327     3008   3124   1019    392    217    -12       C  
ATOM   5215  O   ALA B 327     -19.775 -35.190  16.133  1.00 19.50           O  
ANISOU 5215  O   ALA B 327     3078   3299   1029    540    283    166       O  
ATOM   5216  CB  ALA B 327     -21.837 -33.222  17.648  1.00 16.75           C  
ANISOU 5216  CB  ALA B 327     2742   2845    774    399    362    101       C  
ATOM   5217  N   ILE B 328     -21.919 -35.804  15.774  1.00 18.88           N  
ANISOU 5217  N   ILE B 328     3149   2967   1055    328    245    190       N  
ATOM   5218  CA  ILE B 328     -21.591 -37.223  15.585  1.00 19.29           C  
ANISOU 5218  CA  ILE B 328     3318   3059    950    365    249    -54       C  
ATOM   5219  C   ILE B 328     -21.096 -37.490  14.173  1.00 19.68           C  
ANISOU 5219  C   ILE B 328     3324   3174    979    468    398    196       C  
ATOM   5220  O   ILE B 328     -20.665 -38.599  13.850  1.00 20.75           O  
ANISOU 5220  O   ILE B 328     3757   3249    876    525    512    -24       O  
ATOM   5221  CB  ILE B 328     -22.719 -38.219  15.985  1.00 18.28           C  
ANISOU 5221  CB  ILE B 328     3197   2911    837    533    312     77       C  
ATOM   5222  CG1 ILE B 328     -23.996 -38.060  15.164  1.00 19.38           C  
ANISOU 5222  CG1 ILE B 328     3288   3100    973    398    146     88       C  
ATOM   5223  CG2 ILE B 328     -22.994 -38.180  17.485  1.00 17.48           C  
ANISOU 5223  CG2 ILE B 328     2949   2902    791    625    142    -31       C  
ATOM   5224  CD1 ILE B 328     -24.950 -39.220  15.325  1.00 19.84           C  
ANISOU 5224  CD1 ILE B 328     3461   3006   1069    466    417    388       C  
ATOM   5225  N   GLY B 329     -21.161 -36.468  13.327  1.00 19.05           N  
ANISOU 5225  N   GLY B 329     3150   3270    817    326    143    212       N  
ATOM   5226  CA  GLY B 329     -20.524 -36.564  12.024  1.00 19.46           C  
ANISOU 5226  CA  GLY B 329     3319   3100    974    373    320    -92       C  
ATOM   5227  C   GLY B 329     -21.431 -36.834  10.839  1.00 19.28           C  
ANISOU 5227  C   GLY B 329     3078   3308    938    374    488   -207       C  
ATOM   5228  O   GLY B 329     -20.945 -37.176   9.758  1.00 20.53           O  
ANISOU 5228  O   GLY B 329     3363   3512    925    583    500   -240       O  
ATOM   5229  N   LEU B 330     -22.743 -36.687  11.022  1.00 18.06           N  
ANISOU 5229  N   LEU B 330     3080   2974    806    453    346    -36       N  
ATOM   5230  CA  LEU B 330     -23.682 -36.837   9.905  1.00 18.66           C  
ANISOU 5230  CA  LEU B 330     3380   2844    866    227    148     90       C  
ATOM   5231  C   LEU B 330     -23.619 -35.606   9.017  1.00 18.80           C  
ANISOU 5231  C   LEU B 330     3596   2738    807     97     29     29       C  
ATOM   5232  O   LEU B 330     -23.421 -34.490   9.511  1.00 18.11           O  
ANISOU 5232  O   LEU B 330     3522   2671    686    127    156     14       O  
ATOM   5233  CB  LEU B 330     -25.117 -37.054  10.395  1.00 19.23           C  
ANISOU 5233  CB  LEU B 330     3480   2861    965     56    295     -8       C  
ATOM   5234  CG  LEU B 330     -25.457 -38.324  11.186  1.00 20.40           C  
ANISOU 5234  CG  LEU B 330     3324   2790   1635   -115    270     26       C  
ATOM   5235  CD1 LEU B 330     -26.962 -38.561  11.138  1.00 19.61           C  
ANISOU 5235  CD1 LEU B 330     3271   2869   1310      8    301     65       C  
ATOM   5236  CD2 LEU B 330     -24.728 -39.526  10.601  1.00 22.76           C  
ANISOU 5236  CD2 LEU B 330     3551   3143   1952    406    168    180       C  
ATOM   5237  N   SER B 331     -23.788 -35.810   7.713  1.00 18.80           N  
ANISOU 5237  N   SER B 331     3577   2850    714    308    400    -56       N  
ATOM   5238  CA  SER B 331     -23.807 -34.690   6.789  1.00 19.31           C  
ANISOU 5238  CA  SER B 331     3706   2734    897    383    202    -52       C  
ATOM   5239  C   SER B 331     -25.172 -34.041   6.926  1.00 19.72           C  
ANISOU 5239  C   SER B 331     3554   2618   1320    262    213     62       C  
ATOM   5240  O   SER B 331     -26.090 -34.639   7.505  1.00 18.84           O  
ANISOU 5240  O   SER B 331     3513   2878    766    337    116    173       O  
ATOM   5241  CB  SER B 331     -23.595 -35.181   5.360  1.00 18.98           C  
ANISOU 5241  CB  SER B 331     3704   2608    898    385    183    -48       C  
ATOM   5242  OG  SER B 331     -24.662 -36.023   4.953  1.00 18.79           O  
ANISOU 5242  OG  SER B 331     3556   3047    536    352    303   -182       O  
ATOM   5243  N   GLU B 332     -25.312 -32.842   6.369  1.00 18.54           N  
ANISOU 5243  N   GLU B 332     3643   2678    721    401    335     20       N  
ATOM   5244  CA  GLU B 332     -26.567 -32.110   6.414  1.00 19.34           C  
ANISOU 5244  CA  GLU B 332     3623   2575   1148    388    148    117       C  
ATOM   5245  C   GLU B 332     -27.648 -32.890   5.703  1.00 19.13           C  
ANISOU 5245  C   GLU B 332     3697   2748    822    275    222     80       C  
ATOM   5246  O   GLU B 332     -28.786 -32.920   6.154  1.00 18.70           O  
ANISOU 5246  O   GLU B 332     3717   2688    698     87    249    344       O  
ATOM   5247  CB  GLU B 332     -26.396 -30.740   5.751  1.00 19.38           C  
ANISOU 5247  CB  GLU B 332     3674   2774    912    370    220    244       C  
ATOM   5248  CG  GLU B 332     -25.416 -29.791   6.439  1.00 21.72           C  
ANISOU 5248  CG  GLU B 332     3987   2809   1455     76    237    309       C  
ATOM   5249  CD  GLU B 332     -23.973 -29.965   5.985  1.00 23.69           C  
ANISOU 5249  CD  GLU B 332     4091   2932   1975    326    157     97       C  
ATOM   5250  OE1 GLU B 332     -23.678 -30.910   5.218  1.00 22.22           O  
ANISOU 5250  OE1 GLU B 332     3991   2934   1516    481    400    433       O  
ATOM   5251  OE2 GLU B 332     -23.138 -29.142   6.398  1.00 27.26           O  
ANISOU 5251  OE2 GLU B 332     4311   3744   2302     81   -549    425       O  
ATOM   5252  N   ALA B 333     -27.292 -33.501   4.571  1.00 19.31           N  
ANISOU 5252  N   ALA B 333     3814   2600    920    233    210     25       N  
ATOM   5253  CA  ALA B 333     -28.239 -34.330   3.833  1.00 19.47           C  
ANISOU 5253  CA  ALA B 333     3844   2791    762     66    206    101       C  
ATOM   5254  C   ALA B 333     -28.703 -35.528   4.660  1.00 19.78           C  
ANISOU 5254  C   ALA B 333     3750   2757   1005     58     91    143       C  
ATOM   5255  O   ALA B 333     -29.887 -35.861   4.678  1.00 22.09           O  
ANISOU 5255  O   ALA B 333     3806   3157   1430      1    135     32       O  
ATOM   5256  CB  ALA B 333     -27.640 -34.795   2.510  1.00 19.37           C  
ANISOU 5256  CB  ALA B 333     3696   2723    938    134    150   -104       C  
ATOM   5257  N   GLU B 334     -27.770 -36.178   5.341  1.00 18.07           N  
ANISOU 5257  N   GLU B 334     3498   2693    674    153    378     50       N  
ATOM   5258  CA  GLU B 334     -28.142 -37.277   6.208  1.00 17.99           C  
ANISOU 5258  CA  GLU B 334     3518   2627    690    244    321     45       C  
ATOM   5259  C   GLU B 334     -29.030 -36.742   7.329  1.00 18.01           C  
ANISOU 5259  C   GLU B 334     3462   2591    788    379    292     32       C  
ATOM   5260  O   GLU B 334     -30.060 -37.324   7.629  1.00 17.75           O  
ANISOU 5260  O   GLU B 334     3538   2481    723    286    217    -46       O  
ATOM   5261  CB  GLU B 334     -26.900 -37.943   6.784  1.00 18.71           C  
ANISOU 5261  CB  GLU B 334     3508   2601    999    370    401   -164       C  
ATOM   5262  CG  GLU B 334     -26.175 -38.854   5.809  1.00 20.67           C  
ANISOU 5262  CG  GLU B 334     3765   3436    651    623    449   -216       C  
ATOM   5263  CD  GLU B 334     -24.847 -39.359   6.333  1.00 22.12           C  
ANISOU 5263  CD  GLU B 334     3824   3442   1139    723    342   -525       C  
ATOM   5264  OE1 GLU B 334     -24.141 -38.638   7.072  1.00 22.55           O  
ANISOU 5264  OE1 GLU B 334     3891   3536   1139    553    222   -266       O  
ATOM   5265  OE2 GLU B 334     -24.497 -40.487   5.970  1.00 30.93           O  
ANISOU 5265  OE2 GLU B 334     4988   3585   3177   1137   -281   -955       O  
ATOM   5266  N   ALA B 335     -28.658 -35.614   7.915  1.00 18.35           N  
ANISOU 5266  N   ALA B 335     3411   2621    939    257    230     35       N  
ATOM   5267  CA  ALA B 335     -29.465 -35.042   8.997  1.00 18.99           C  
ANISOU 5267  CA  ALA B 335     3591   2544   1078    247    288    -53       C  
ATOM   5268  C   ALA B 335     -30.910 -34.779   8.556  1.00 20.22           C  
ANISOU 5268  C   ALA B 335     3513   2837   1330    156    347     89       C  
ATOM   5269  O   ALA B 335     -31.866 -34.974   9.322  1.00 20.48           O  
ANISOU 5269  O   ALA B 335     3843   2851   1084    247    451    280       O  
ATOM   5270  CB  ALA B 335     -28.813 -33.764   9.497  1.00 19.89           C  
ANISOU 5270  CB  ALA B 335     3766   2641   1149    214    269   -204       C  
ATOM   5271  N   ARG B 336     -31.077 -34.368   7.312  1.00 20.61           N  
ANISOU 5271  N   ARG B 336     3741   2731   1357    185    363    218       N  
ATOM   5272  CA  ARG B 336     -32.408 -34.108   6.811  1.00 22.46           C  
ANISOU 5272  CA  ARG B 336     3949   2999   1583    185    113    441       C  
ATOM   5273  C   ARG B 336     -33.293 -35.343   6.875  1.00 20.75           C  
ANISOU 5273  C   ARG B 336     3956   2948    979    151    428    324       C  
ATOM   5274  O   ARG B 336     -34.488 -35.191   7.023  1.00 22.21           O  
ANISOU 5274  O   ARG B 336     3945   3262   1229    387    205    421       O  
ATOM   5275  CB  ARG B 336     -32.380 -33.598   5.342  1.00 24.62           C  
ANISOU 5275  CB  ARG B 336     4208   3471   1672     73    343    641       C  
ATOM   5276  CG  ARG B 336     -31.730 -32.231   5.086  1.00 25.91           C  
ANISOU 5276  CG  ARG B 336     4506   3255   2081    144    205    375       C  
ATOM   5277  CD  ARG B 336     -31.785 -31.857   3.596  1.00 29.46           C  
ANISOU 5277  CD  ARG B 336     4814   3762   2614    231  -1033   1279       C  
ATOM   5278  NE  ARG B 336     -32.815 -32.701   3.045  1.00 34.77           N  
ANISOU 5278  NE  ARG B 336     5865   4115   3230    232  -1009    165       N  
ATOM   5279  CZ  ARG B 336     -32.670 -33.634   2.118  1.00 29.61           C  
ANISOU 5279  CZ  ARG B 336     5095   4174   1981    306   -392    659       C  
ATOM   5280  NH1 ARG B 336     -33.736 -34.328   1.835  1.00 33.52           N  
ANISOU 5280  NH1 ARG B 336     5589   3837   3310   -169   -171    397       N  
ATOM   5281  NH2 ARG B 336     -31.530 -33.862   1.456  1.00 29.52           N  
ANISOU 5281  NH2 ARG B 336     4748   3768   2700     47   -344    979       N  
ATOM   5282  N   ARG B 337     -32.724 -36.537   6.684  1.00 19.95           N  
ANISOU 5282  N   ARG B 337     4020   2791    769    193    200    407       N  
ATOM   5283  CA  ARG B 337     -33.484 -37.782   6.637  1.00 20.86           C  
ANISOU 5283  CA  ARG B 337     4203   2649   1072    190    224    290       C  
ATOM   5284  C   ARG B 337     -33.499 -38.449   7.992  1.00 18.96           C  
ANISOU 5284  C   ARG B 337     3666   2730    807    241    213     87       C  
ATOM   5285  O   ARG B 337     -33.811 -39.624   8.074  1.00 18.50           O  
ANISOU 5285  O   ARG B 337     3592   2764    671    123     48   -205       O  
ATOM   5286  CB  ARG B 337     -32.856 -38.775   5.656  1.00 22.67           C  
ANISOU 5286  CB  ARG B 337     4349   3256   1008    102    254   -120       C  
ATOM   5287  CG  ARG B 337     -32.333 -38.177   4.383  1.00 23.76           C  
ANISOU 5287  CG  ARG B 337     4245   3388   1394   -223    516   -174       C  
ATOM   5288  CD  ARG B 337     -32.148 -39.281   3.325  1.00 25.51           C  
ANISOU 5288  CD  ARG B 337     4732   3738   1222   -307    259   -404       C  
ATOM   5289  NE  ARG B 337     -30.995 -40.138   3.595  1.00 26.23           N  
ANISOU 5289  NE  ARG B 337     4490   3894   1581   -460    513   -434       N  
ATOM   5290  CZ  ARG B 337     -29.734 -39.852   3.267  1.00 26.03           C  
ANISOU 5290  CZ  ARG B 337     4499   3095   2295   -474    349   -282       C  
ATOM   5291  NH1 ARG B 337     -29.416 -38.700   2.667  1.00 22.26           N  
ANISOU 5291  NH1 ARG B 337     4118   3223   1117   -279    460   -245       N  
ATOM   5292  NH2 ARG B 337     -28.773 -40.719   3.569  1.00 28.17           N  
ANISOU 5292  NH2 ARG B 337     4508   3848   2347    -43    319   -578       N  
ATOM   5293  N   THR B 338     -33.161 -37.722   9.051  1.00 18.15           N  
ANISOU 5293  N   THR B 338     3525   2578    789    211    113    206       N  
ATOM   5294  CA  THR B 338     -33.004 -38.350  10.350  1.00 17.79           C  
ANISOU 5294  CA  THR B 338     3325   2623    808    159    268    281       C  
ATOM   5295  C   THR B 338     -34.085 -37.915  11.328  1.00 17.15           C  
ANISOU 5295  C   THR B 338     3381   2536    600    204    137    114       C  
ATOM   5296  O   THR B 338     -34.364 -36.723  11.444  1.00 18.60           O  
ANISOU 5296  O   THR B 338     3519   2644    902    250    152    228       O  
ATOM   5297  CB  THR B 338     -31.626 -38.008  10.910  1.00 17.72           C  
ANISOU 5297  CB  THR B 338     3441   2546    743    208    129    190       C  
ATOM   5298  OG1 THR B 338     -30.630 -38.516  10.019  1.00 18.07           O  
ANISOU 5298  OG1 THR B 338     3364   2659    839    218    103    202       O  
ATOM   5299  CG2 THR B 338     -31.434 -38.651  12.248  1.00 17.14           C  
ANISOU 5299  CG2 THR B 338     3388   2415    709    181    -60     45       C  
ATOM   5300  N   TYR B 339     -34.677 -38.891  12.019  1.00 16.12           N  
ANISOU 5300  N   TYR B 339     3151   2378    595    227    191    -40       N  
ATOM   5301  CA  TYR B 339     -35.798 -38.677  12.930  1.00 16.01           C  
ANISOU 5301  CA  TYR B 339     3044   2446    592    126    151     14       C  
ATOM   5302  C   TYR B 339     -35.575 -39.405  14.243  1.00 16.48           C  
ANISOU 5302  C   TYR B 339     3278   2240    741    150     97     58       C  
ATOM   5303  O   TYR B 339     -35.065 -40.522  14.266  1.00 15.67           O  
ANISOU 5303  O   TYR B 339     3483   2140    329    194    178    -73       O  
ATOM   5304  CB  TYR B 339     -37.091 -39.181  12.282  1.00 16.80           C  
ANISOU 5304  CB  TYR B 339     3168   2561    654    120     45     34       C  
ATOM   5305  CG  TYR B 339     -37.477 -38.366  11.076  1.00 17.83           C  
ANISOU 5305  CG  TYR B 339     3249   2717    807    256     76    181       C  
ATOM   5306  CD1 TYR B 339     -38.400 -37.336  11.182  1.00 18.83           C  
ANISOU 5306  CD1 TYR B 339     3388   2697   1067    273     94    265       C  
ATOM   5307  CD2 TYR B 339     -36.905 -38.613   9.830  1.00 17.77           C  
ANISOU 5307  CD2 TYR B 339     3372   2559    820    297     39     12       C  
ATOM   5308  CE1 TYR B 339     -38.765 -36.587  10.076  1.00 20.63           C  
ANISOU 5308  CE1 TYR B 339     3710   3042   1085    401     87    374       C  
ATOM   5309  CE2 TYR B 339     -37.242 -37.858   8.722  1.00 19.28           C  
ANISOU 5309  CE2 TYR B 339     3658   2907    758    333   -112     26       C  
ATOM   5310  CZ  TYR B 339     -38.173 -36.846   8.849  1.00 19.79           C  
ANISOU 5310  CZ  TYR B 339     3910   2858    749    470   -357    111       C  
ATOM   5311  OH  TYR B 339     -38.518 -36.105   7.747  1.00 20.90           O  
ANISOU 5311  OH  TYR B 339     4209   2799    932    473   -360    255       O  
ATOM   5312  N   ARG B 340     -35.945 -38.749  15.338  1.00 16.15           N  
ANISOU 5312  N   ARG B 340     3237   2189    710    167     76     65       N  
ATOM   5313  CA  ARG B 340     -36.000 -39.399  16.637  1.00 16.78           C  
ANISOU 5313  CA  ARG B 340     3401   2258    714     35     45     73       C  
ATOM   5314  C   ARG B 340     -37.414 -39.908  16.866  1.00 16.37           C  
ANISOU 5314  C   ARG B 340     3470   2161    585     99    185     -3       C  
ATOM   5315  O   ARG B 340     -38.366 -39.125  16.961  1.00 17.21           O  
ANISOU 5315  O   ARG B 340     3345   2464    728    148     14     98       O  
ATOM   5316  CB  ARG B 340     -35.588 -38.449  17.772  1.00 16.34           C  
ANISOU 5316  CB  ARG B 340     3305   2246    657    152     45     67       C  
ATOM   5317  CG  ARG B 340     -35.569 -39.149  19.134  1.00 17.16           C  
ANISOU 5317  CG  ARG B 340     3519   2375    627    141     51     62       C  
ATOM   5318  CD  ARG B 340     -35.467 -38.179  20.295  1.00 17.09           C  
ANISOU 5318  CD  ARG B 340     3237   2596    661    316    100    -62       C  
ATOM   5319  NE  ARG B 340     -36.628 -37.283  20.366  1.00 16.26           N  
ANISOU 5319  NE  ARG B 340     3194   2564    417    345    153    -69       N  
ATOM   5320  CZ  ARG B 340     -36.635 -36.131  21.025  1.00 16.27           C  
ANISOU 5320  CZ  ARG B 340     3067   2493    621    229     50     12       C  
ATOM   5321  NH1 ARG B 340     -35.546 -35.745  21.703  1.00 15.26           N  
ANISOU 5321  NH1 ARG B 340     3013   2509    274    138    220    -85       N  
ATOM   5322  NH2 ARG B 340     -37.729 -35.374  21.020  1.00 15.72           N  
ANISOU 5322  NH2 ARG B 340     3195   2306    469    291    297   -307       N  
ATOM   5323  N   ILE B 341     -37.536 -41.231  16.923  1.00 16.44           N  
ANISOU 5323  N   ILE B 341     3542   2157    546    -16     14   -172       N  
ATOM   5324  CA  ILE B 341     -38.785 -41.899  17.213  1.00 16.61           C  
ANISOU 5324  CA  ILE B 341     3542   2148    620     57    186    -11       C  
ATOM   5325  C   ILE B 341     -38.609 -42.457  18.620  1.00 17.25           C  
ANISOU 5325  C   ILE B 341     3579   2293    681    185     85     12       C  
ATOM   5326  O   ILE B 341     -37.746 -43.303  18.844  1.00 17.10           O  
ANISOU 5326  O   ILE B 341     3556   2557    382    250     76     95       O  
ATOM   5327  CB  ILE B 341     -39.061 -43.049  16.214  1.00 16.98           C  
ANISOU 5327  CB  ILE B 341     3622   2075    752    -32    186    -13       C  
ATOM   5328  CG1 ILE B 341     -38.949 -42.552  14.762  1.00 17.54           C  
ANISOU 5328  CG1 ILE B 341     3736   2127    798    145    284     58       C  
ATOM   5329  CG2 ILE B 341     -40.425 -43.662  16.486  1.00 18.79           C  
ANISOU 5329  CG2 ILE B 341     3617   2655    865    -73    132    -56       C  
ATOM   5330  CD1 ILE B 341     -38.797 -43.622  13.693  1.00 19.48           C  
ANISOU 5330  CD1 ILE B 341     4072   2773    556    -26     63   -233       C  
ATOM   5331  N   SER B 342     -39.411 -41.977  19.569  1.00 16.27           N  
ANISOU 5331  N   SER B 342     3459   1996    724      8    155    151       N  
ATOM   5332  CA  SER B 342     -39.243 -42.387  20.967  1.00 16.34           C  
ANISOU 5332  CA  SER B 342     3409   2190    610     21     59    -81       C  
ATOM   5333  C   SER B 342     -40.514 -43.003  21.554  1.00 17.58           C  
ANISOU 5333  C   SER B 342     3524   2512    643    -75     74      7       C  
ATOM   5334  O   SER B 342     -41.625 -42.704  21.120  1.00 18.26           O  
ANISOU 5334  O   SER B 342     3446   2529    962    -55    168    -82       O  
ATOM   5335  CB  SER B 342     -38.699 -41.240  21.823  1.00 17.05           C  
ANISOU 5335  CB  SER B 342     3402   2204    870    146    -88   -157       C  
ATOM   5336  OG  SER B 342     -39.503 -40.075  21.721  1.00 16.28           O  
ANISOU 5336  OG  SER B 342     3392   2178    614    177    -51   -202       O  
ATOM   5337  N   LEU B 343     -40.320 -43.906  22.505  1.00 17.14           N  
ANISOU 5337  N   LEU B 343     3534   2258    719    -87     41    -89       N  
ATOM   5338  CA  LEU B 343     -41.356 -44.808  22.949  1.00 17.28           C  
ANISOU 5338  CA  LEU B 343     3460   2324    780    -93    148   -174       C  
ATOM   5339  C   LEU B 343     -41.615 -44.632  24.443  1.00 17.39           C  
ANISOU 5339  C   LEU B 343     3369   2495    744   -214    129    -70       C  
ATOM   5340  O   LEU B 343     -40.805 -44.043  25.134  1.00 17.04           O  
ANISOU 5340  O   LEU B 343     3588   2354    532   -171     -2     29       O  
ATOM   5341  CB  LEU B 343     -40.899 -46.230  22.674  1.00 18.32           C  
ANISOU 5341  CB  LEU B 343     3713   2440    806    -19    323   -305       C  
ATOM   5342  CG  LEU B 343     -41.031 -46.715  21.218  1.00 20.36           C  
ANISOU 5342  CG  LEU B 343     3949   2860    926   -313    -55   -407       C  
ATOM   5343  CD1 LEU B 343     -42.478 -46.854  20.730  1.00 23.92           C  
ANISOU 5343  CD1 LEU B 343     4210   3278   1597     59   -549   -214       C  
ATOM   5344  CD2 LEU B 343     -40.223 -45.915  20.228  1.00 20.50           C  
ANISOU 5344  CD2 LEU B 343     3985   2647   1154     91     97   -119       C  
ATOM   5345  N   PRO B 344     -42.757 -45.122  24.941  1.00 17.55           N  
ANISOU 5345  N   PRO B 344     3353   2523    792   -189    152   -163       N  
ATOM   5346  CA  PRO B 344     -43.100 -44.952  26.353  1.00 17.54           C  
ANISOU 5346  CA  PRO B 344     3469   2459    735   -228     13   -290       C  
ATOM   5347  C   PRO B 344     -41.986 -45.495  27.233  1.00 17.44           C  
ANISOU 5347  C   PRO B 344     3475   2411    739   -124     80   -300       C  
ATOM   5348  O   PRO B 344     -41.623 -46.633  27.095  1.00 17.41           O  
ANISOU 5348  O   PRO B 344     3415   2449    749    -71    209   -158       O  
ATOM   5349  CB  PRO B 344     -44.377 -45.791  26.492  1.00 18.50           C  
ANISOU 5349  CB  PRO B 344     3298   2830    899   -162    -39    -91       C  
ATOM   5350  CG  PRO B 344     -45.006 -45.686  25.142  1.00 17.67           C  
ANISOU 5350  CG  PRO B 344     3155   2731    825   -203     28   -311       C  
ATOM   5351  CD  PRO B 344     -43.835 -45.793  24.200  1.00 17.55           C  
ANISOU 5351  CD  PRO B 344     3277   2610    779   -153    100   -105       C  
ATOM   5352  N   PRO B 345     -41.428 -44.675  28.122  1.00 17.52           N  
ANISOU 5352  N   PRO B 345     3507   2349    802   -154    -59   -192       N  
ATOM   5353  CA  PRO B 345     -40.324 -45.131  28.954  1.00 17.00           C  
ANISOU 5353  CA  PRO B 345     3435   2290    734   -118     80    -80       C  
ATOM   5354  C   PRO B 345     -40.731 -46.176  29.958  1.00 17.16           C  
ANISOU 5354  C   PRO B 345     3497   2336    687    -50     71    -82       C  
ATOM   5355  O   PRO B 345     -41.878 -46.255  30.367  1.00 16.53           O  
ANISOU 5355  O   PRO B 345     3469   2353    455   -260    111     15       O  
ATOM   5356  CB  PRO B 345     -39.905 -43.874  29.715  1.00 17.57           C  
ANISOU 5356  CB  PRO B 345     3697   2166    813   -100     14      8       C  
ATOM   5357  CG  PRO B 345     -40.335 -42.762  28.836  1.00 18.38           C  
ANISOU 5357  CG  PRO B 345     3412   2477   1091    -39   -214    205       C  
ATOM   5358  CD  PRO B 345     -41.621 -43.229  28.209  1.00 17.00           C  
ANISOU 5358  CD  PRO B 345     3465   2285    709   -164     33   -171       C  
ATOM   5359  N   TYR B 346     -39.768 -47.006  30.311  1.00 17.33           N  
ANISOU 5359  N   TYR B 346     3669   2215    698    -50     73     32       N  
ATOM   5360  CA  TYR B 346     -39.944 -47.999  31.364  1.00 18.06           C  
ANISOU 5360  CA  TYR B 346     3570   2338    952   -154     84    199       C  
ATOM   5361  C   TYR B 346     -38.598 -48.377  31.902  1.00 18.93           C  
ANISOU 5361  C   TYR B 346     3739   2546    907   -116     39     60       C  
ATOM   5362  O   TYR B 346     -37.616 -47.920  31.415  1.00 19.80           O  
ANISOU 5362  O   TYR B 346     3628   2689   1203    -40    247   -142       O  
ATOM   5363  CB  TYR B 346     -40.656 -49.220  30.824  1.00 18.73           C  
ANISOU 5363  CB  TYR B 346     3867   2418    831   -107    104    -19       C  
ATOM   5364  CG  TYR B 346     -39.882 -50.003  29.801  1.00 19.86           C  
ANISOU 5364  CG  TYR B 346     3811   2791    944    -30    283     24       C  
ATOM   5365  CD1 TYR B 346     -39.766 -49.567  28.506  1.00 19.14           C  
ANISOU 5365  CD1 TYR B 346     3682   2794    795   -221    121   -136       C  
ATOM   5366  CD2 TYR B 346     -39.272 -51.165  30.120  1.00 21.62           C  
ANISOU 5366  CD2 TYR B 346     4009   2842   1361     20    257    -44       C  
ATOM   5367  CE1 TYR B 346     -39.087 -50.277  27.559  1.00 21.98           C  
ANISOU 5367  CE1 TYR B 346     3819   2947   1584     18    147   -471       C  
ATOM   5368  CE2 TYR B 346     -38.580 -51.907  29.192  1.00 23.81           C  
ANISOU 5368  CE2 TYR B 346     4310   3235   1501    172    226   -299       C  
ATOM   5369  CZ  TYR B 346     -38.484 -51.461  27.925  1.00 22.77           C  
ANISOU 5369  CZ  TYR B 346     4196   3031   1422    149    412   -456       C  
ATOM   5370  OH  TYR B 346     -37.767 -52.252  27.068  1.00 24.48           O  
ANISOU 5370  OH  TYR B 346     4344   3628   1330    191    521   -642       O  
ATOM   5371  N   LYS B 347     -38.553 -49.183  32.939  1.00 19.27           N  
ANISOU 5371  N   LYS B 347     3641   2548   1129    134    192    179       N  
ATOM   5372  CA  LYS B 347     -37.267 -49.543  33.502  1.00 20.38           C  
ANISOU 5372  CA  LYS B 347     3743   2940   1059     91      7     50       C  
ATOM   5373  C   LYS B 347     -36.645 -50.643  32.647  1.00 23.47           C  
ANISOU 5373  C   LYS B 347     4065   3006   1846    253    116   -154       C  
ATOM   5374  O   LYS B 347     -37.081 -51.772  32.710  1.00 24.73           O  
ANISOU 5374  O   LYS B 347     4188   3329   1879    -17    -36    -28       O  
ATOM   5375  CB  LYS B 347     -37.423 -50.001  34.933  1.00 20.44           C  
ANISOU 5375  CB  LYS B 347     3787   2904   1076     71    -29     14       C  
ATOM   5376  CG  LYS B 347     -36.065 -50.164  35.625  1.00 22.29           C  
ANISOU 5376  CG  LYS B 347     3806   3220   1443    303   -130   -140       C  
ATOM   5377  CD  LYS B 347     -36.175 -50.412  37.113  1.00 26.63           C  
ANISOU 5377  CD  LYS B 347     4383   4210   1524    143      2    -71       C  
ATOM   5378  CE  LYS B 347     -34.848 -50.113  37.810  1.00 31.31           C  
ANISOU 5378  CE  LYS B 347     3993   4491   3410    240    -92   -380       C  
ATOM   5379  NZ  LYS B 347     -33.684 -50.814  37.204  1.00 32.21           N  
ANISOU 5379  NZ  LYS B 347     4056   4233   3946    370   -386   -754       N  
ATOM   5380  N   VAL B 348     -35.639 -50.290  31.869  1.00 23.34           N  
ANISOU 5380  N   VAL B 348     4278   3165   1425     99    129    -27       N  
ATOM   5381  CA  VAL B 348     -35.198 -51.114  30.753  1.00 25.81           C  
ANISOU 5381  CA  VAL B 348     4560   3454   1793    149    120   -348       C  
ATOM   5382  C   VAL B 348     -34.391 -52.286  31.121  1.00 28.99           C  
ANISOU 5382  C   VAL B 348     4870   4153   1990    498      8   -480       C  
ATOM   5383  O   VAL B 348     -34.064 -53.102  30.340  1.00 33.53           O  
ANISOU 5383  O   VAL B 348     5513   4126   3101    442   -264  -1158       O  
ATOM   5384  CB  VAL B 348     -34.435 -50.277  29.706  1.00 26.53           C  
ANISOU 5384  CB  VAL B 348     4394   3905   1780     60    218   -262       C  
ATOM   5385  CG1 VAL B 348     -35.372 -49.350  29.006  1.00 27.69           C  
ANISOU 5385  CG1 VAL B 348     4456   3726   2338    187    220   -150       C  
ATOM   5386  CG2 VAL B 348     -33.303 -49.549  30.382  1.00 27.58           C  
ANISOU 5386  CG2 VAL B 348     4623   3912   1943    -36     35   -456       C  
ATOM   5387  OXT VAL B 348     -33.952 -52.409  32.171  1.00 29.68           O  
ANISOU 5387  OXT VAL B 348     4821   4104   2350    343    -75    276       O  
TER    5388      VAL B 348                                                      
HETATM 5389  N1  PLP A 401     -43.335 -12.028  -8.527  1.00 14.45           N  
ANISOU 5389  N1  PLP A 401     2820   2166    502    -89    114    -10       N  
HETATM 5390  C2  PLP A 401     -44.256 -12.813  -9.140  1.00 14.70           C  
ANISOU 5390  C2  PLP A 401     2732   1995    858    -43     81     80       C  
HETATM 5391  C2A PLP A 401     -43.889 -14.233  -9.480  1.00 16.39           C  
ANISOU 5391  C2A PLP A 401     2964   2049   1212     31   -514   -249       C  
HETATM 5392  C3  PLP A 401     -45.595 -12.264  -9.464  1.00 16.32           C  
ANISOU 5392  C3  PLP A 401     2772   2348   1080    -14    -21     45       C  
HETATM 5393  O3  PLP A 401     -46.575 -12.992 -10.077  1.00 20.32           O  
ANISOU 5393  O3  PLP A 401     3164   2544   2011   -202   -243   -177       O  
HETATM 5394  C4  PLP A 401     -45.827 -10.854  -9.074  1.00 16.59           C  
ANISOU 5394  C4  PLP A 401     2993   2317    992    128    -55    195       C  
HETATM 5395  C4A PLP A 401     -47.112 -10.204  -9.332  1.00 18.40           C  
ANISOU 5395  C4A PLP A 401     2892   2978   1118    173   -143    101       C  
HETATM 5396  C5  PLP A 401     -44.745 -10.089  -8.413  1.00 16.18           C  
ANISOU 5396  C5  PLP A 401     2885   2484    779    127    194   -147       C  
HETATM 5397  C6  PLP A 401     -43.542 -10.740  -8.174  1.00 15.36           C  
ANISOU 5397  C6  PLP A 401     2848   2250    737     78    213    -19       C  
HETATM 5398  C5A PLP A 401     -44.946  -8.640  -8.018  1.00 17.83           C  
ANISOU 5398  C5A PLP A 401     3048   2437   1288     -7    267   -104       C  
HETATM 5399  O4P PLP A 401     -45.918  -8.528  -6.977  1.00 17.65           O  
ANISOU 5399  O4P PLP A 401     2937   2712   1057    -67    134   -154       O  
HETATM 5400  P   PLP A 401     -46.711  -7.154  -6.665  1.00 18.80           P  
ANISOU 5400  P   PLP A 401     3295   2726   1119    -11     71    -33       P  
HETATM 5401  O1P PLP A 401     -47.607  -6.996  -7.865  1.00 22.41           O  
ANISOU 5401  O1P PLP A 401     3710   3390   1413    473   -147     99       O  
HETATM 5402  O2P PLP A 401     -45.635  -6.115  -6.493  1.00 20.31           O  
ANISOU 5402  O2P PLP A 401     3417   2497   1802    -82    559   -100       O  
HETATM 5403  O3P PLP A 401     -47.465  -7.445  -5.388  1.00 19.12           O  
ANISOU 5403  O3P PLP A 401     3147   2823   1294     54    337   -362       O  
HETATM 5404  N   CYS A 402     -46.478 -10.155 -13.042  1.00 33.36           N  
ANISOU 5404  N   CYS A 402     5459   4787   2428    543  -1455    838       N  
HETATM 5405  CA  CYS A 402     -47.118  -9.356 -14.054  1.00 23.12           C  
ANISOU 5405  CA  CYS A 402     4268   3376   1138   -192   -749    273       C  
HETATM 5406  C   CYS A 402     -47.637 -10.317 -15.073  1.00 22.49           C  
ANISOU 5406  C   CYS A 402     3856   3058   1630   -115   -554     40       C  
HETATM 5407  O   CYS A 402     -48.686 -10.079 -15.644  1.00 19.16           O  
ANISOU 5407  O   CYS A 402     3468   2871    938    -82   -129   -241       O  
HETATM 5408  CB  CYS A 402     -46.093  -8.485 -14.725  1.00 26.73           C  
ANISOU 5408  CB  CYS A 402     5011   3136   2006   -727   -359   -244       C  
HETATM 5409  SG  CYS A 402     -47.011  -7.630 -15.977  1.00 34.57           S  
ANISOU 5409  SG  CYS A 402     5405   4569   3159     98   -560   -102       S  
HETATM 5410  OXT CYS A 402     -46.982 -11.322 -15.333  1.00 22.63           O  
ANISOU 5410  OXT CYS A 402     4119   3036   1443     30   -223    294       O  
HETATM 5411  N1  PLP B 401     -31.874 -32.178  29.608  1.00 14.67           N  
ANISOU 5411  N1  PLP B 401     2948   2180    446    337      1    136       N  
HETATM 5412  C2  PLP B 401     -32.282 -33.314  28.984  1.00 15.63           C  
ANISOU 5412  C2  PLP B 401     2793   2190    954    310   -126     98       C  
HETATM 5413  C2A PLP B 401     -31.261 -34.366  28.641  1.00 15.86           C  
ANISOU 5413  C2A PLP B 401     2818   2113   1094    320   -301    -87       C  
HETATM 5414  C3  PLP B 401     -33.717 -33.500  28.662  1.00 17.08           C  
ANISOU 5414  C3  PLP B 401     2850   2411   1226    313   -182    112       C  
HETATM 5415  O3  PLP B 401     -34.204 -34.612  28.036  1.00 19.49           O  
ANISOU 5415  O3  PLP B 401     3007   2462   1936    243   -175     19       O  
HETATM 5416  C4  PLP B 401     -34.620 -32.396  29.062  1.00 16.79           C  
ANISOU 5416  C4  PLP B 401     2869   2578    929    432   -226    136       C  
HETATM 5417  C4A PLP B 401     -36.057 -32.452  28.785  1.00 20.36           C  
ANISOU 5417  C4A PLP B 401     2908   3262   1566     60   -144    -95       C  
HETATM 5418  C5  PLP B 401     -34.058 -31.199  29.726  1.00 16.29           C  
ANISOU 5418  C5  PLP B 401     2879   2710    600    291    -52     80       C  
HETATM 5419  C6  PLP B 401     -32.690 -31.168  29.962  1.00 15.41           C  
ANISOU 5419  C6  PLP B 401     2815   2432    606    459    -75    147       C  
HETATM 5420  C5A PLP B 401     -34.951 -30.040  30.126  1.00 18.03           C  
ANISOU 5420  C5A PLP B 401     3158   2912    779    431    177    107       C  
HETATM 5421  O4P PLP B 401     -35.865 -30.424  31.159  1.00 18.77           O  
ANISOU 5421  O4P PLP B 401     3237   3024    871    207    199    125       O  
HETATM 5422  P   PLP B 401     -37.222 -29.607  31.492  1.00 19.81           P  
ANISOU 5422  P   PLP B 401     3396   3263    867    429     20    225       P  
HETATM 5423  O1P PLP B 401     -38.047 -29.865  30.262  1.00 23.45           O  
ANISOU 5423  O1P PLP B 401     3507   4388   1013    492   -370    819       O  
HETATM 5424  O2P PLP B 401     -36.782 -28.180  31.717  1.00 20.50           O  
ANISOU 5424  O2P PLP B 401     3523   3088   1174    432    298     14       O  
HETATM 5425  O3P PLP B 401     -37.770 -30.264  32.733  1.00 19.03           O  
ANISOU 5425  O3P PLP B 401     3174   2917   1138    193    307     19       O  
HETATM 5426  N   CYS B 402     -37.459 -29.966  22.479  1.00 25.31           N  
ANISOU 5426  N   CYS B 402     4936   2204   2474    157    584    157       N  
HETATM 5427  CA  CYS B 402     -36.111 -30.559  22.306  1.00 30.29           C  
ANISOU 5427  CA  CYS B 402     4653   3705   3150    -39     18    242       C  
HETATM 5428  C   CYS B 402     -36.220 -32.062  22.704  1.00 32.49           C  
ANISOU 5428  C   CYS B 402     4900   4046   3397   -457  -1238    868       C  
HETATM 5429  O   CYS B 402     -37.199 -32.804  22.457  1.00 25.23           O  
ANISOU 5429  O   CYS B 402     5558   2135   1892   -399    260   -197       O  
HETATM 5430  CB  CYS B 402     -35.011 -29.758  23.086  1.00 26.26           C  
ANISOU 5430  CB  CYS B 402     5146   3321   1507    315    -11     54       C  
HETATM 5431  SG  CYS B 402     -34.380 -28.169  22.407  1.00 33.77           S  
ANISOU 5431  SG  CYS B 402     7201   3583   2045    361   2111   -238       S  
HETATM 5432  OXT CYS B 402     -35.319 -32.625  23.283  1.00 34.26           O  
ANISOU 5432  OXT CYS B 402     5606   4511   2900    110  -1011   1177       O  
HETATM 5433  O   HOH A 501     -53.824  -7.114  19.718  1.00 32.55           O  
ANISOU 5433  O   HOH A 501     4801   5496   2067    710    290    424       O  
HETATM 5434  O   HOH A 502     -55.411 -22.285   7.939  1.00 41.61           O  
ANISOU 5434  O   HOH A 502     6709   5018   4080   -180   -138   -144       O  
HETATM 5435  O   HOH A 503     -58.987 -24.033 -13.730  1.00 32.56           O  
ANISOU 5435  O   HOH A 503     3589   5845   2936   -821    -48   1389       O  
HETATM 5436  O   HOH A 504     -37.687 -16.375  16.662  1.00 35.13           O  
ANISOU 5436  O   HOH A 504     6420   5696   1231   -126    840    -79       O  
HETATM 5437  O   HOH A 505     -47.767 -11.907 -12.275  1.00 32.26           O  
ANISOU 5437  O   HOH A 505     5460   4236   2559   -187   -790    -41       O  
HETATM 5438  O   HOH A 506     -63.307  -8.000 -18.847  1.00 37.63           O  
ANISOU 5438  O   HOH A 506     4506   6392   3399     76   -970    411       O  
HETATM 5439  O   HOH A 507     -61.309 -14.027   7.454  1.00 34.90           O  
ANISOU 5439  O   HOH A 507     5374   4751   3135     -2   1476    -12       O  
HETATM 5440  O   HOH A 508     -21.054 -15.371   4.778  1.00 46.18           O  
ANISOU 5440  O   HOH A 508     6940   6929   3674    637   -217    303       O  
HETATM 5441  O   HOH A 509     -24.613 -26.650 -14.015  1.00 35.08           O  
ANISOU 5441  O   HOH A 509     7400   4350   1576   1147   1325   -284       O  
HETATM 5442  O   HOH A 510     -28.749 -12.599   8.223  1.00 39.99           O  
ANISOU 5442  O   HOH A 510     5997   6098   3099    230   -281    297       O  
HETATM 5443  O   HOH A 511     -43.300 -15.984  17.413  1.00 34.98           O  
ANISOU 5443  O   HOH A 511     6110   4635   2544   -204   -289    836       O  
HETATM 5444  O   HOH A 512     -55.702 -18.653  11.665  1.00 43.10           O  
ANISOU 5444  O   HOH A 512     5891   5706   4778   -234   -165   1750       O  
HETATM 5445  O   HOH A 513     -27.186 -31.634  -4.188  1.00 36.11           O  
ANISOU 5445  O   HOH A 513     6352   3837   3532   1302    475   -321       O  
HETATM 5446  O   HOH A 514     -48.307 -26.223   7.681  1.00 33.17           O  
ANISOU 5446  O   HOH A 514     5434   3446   3723   -270    795    325       O  
HETATM 5447  O   HOH A 515     -39.933 -13.946  14.905  1.00 24.59           O  
ANISOU 5447  O   HOH A 515     4315   3649   1379    401    796    839       O  
HETATM 5448  O   HOH A 516     -57.218 -29.278  -9.785  1.00 37.18           O  
ANISOU 5448  O   HOH A 516     6946   3980   3197   -431   1162    171       O  
HETATM 5449  O   HOH A 517     -39.714 -20.140 -35.460  1.00 38.45           O  
ANISOU 5449  O   HOH A 517     5911   4839   3856    103   -532  -1546       O  
HETATM 5450  O   HOH A 518     -36.428 -28.179   1.176  1.00 23.09           O  
ANISOU 5450  O   HOH A 518     3820   3125   1826     40     52    -92       O  
HETATM 5451  O   HOH A 519     -37.577 -30.588 -18.147  1.00 33.69           O  
ANISOU 5451  O   HOH A 519     5720   3806   3272    763    521   -140       O  
HETATM 5452  O   HOH A 520     -21.272 -20.213  -9.824  1.00 29.61           O  
ANISOU 5452  O   HOH A 520     5222   4595   1433    200    330   -682       O  
HETATM 5453  O   HOH A 521     -50.340 -13.730  17.550  1.00 34.48           O  
ANISOU 5453  O   HOH A 521     5403   5931   1765    488    935   -309       O  
HETATM 5454  O   HOH A 522     -47.450 -14.091 -40.873  1.00 42.12           O  
ANISOU 5454  O   HOH A 522     5683   5534   4784  -2479   -742    462       O  
HETATM 5455  O   HOH A 523     -64.768 -16.557 -13.587  1.00 33.06           O  
ANISOU 5455  O   HOH A 523     4150   4351   4059   -748    349    510       O  
HETATM 5456  O   HOH A 524     -56.116 -20.366   2.328  1.00 29.03           O  
ANISOU 5456  O   HOH A 524     5023   2859   3146     27     86   -428       O  
HETATM 5457  O   HOH A 525     -38.028   0.515 -27.242  1.00 28.04           O  
ANISOU 5457  O   HOH A 525     5629   3491   1533   -184   -265    853       O  
HETATM 5458  O   HOH A 526     -45.038 -25.877  10.003  1.00 33.35           O  
ANISOU 5458  O   HOH A 526     5330   4132   3209    668     43    612       O  
HETATM 5459  O   HOH A 527     -38.284  -2.934   5.060  1.00 16.14           O  
ANISOU 5459  O   HOH A 527     2912   2500    720    350    209   -260       O  
HETATM 5460  O   HOH A 528     -35.179 -28.941   8.189  1.00 35.92           O  
ANISOU 5460  O   HOH A 528     5575   5582   2488    536    122   -180       O  
HETATM 5461  O   HOH A 529     -59.358 -15.369  -1.701  1.00 16.01           O  
ANISOU 5461  O   HOH A 529     2764   2522    797   -161    452   -166       O  
HETATM 5462  O   HOH A 530     -47.278  -2.813   9.341  1.00 20.19           O  
ANISOU 5462  O   HOH A 530     3423   3155   1090    416    -46   -382       O  
HETATM 5463  O   HOH A 531     -48.860  -8.559 -22.757  1.00 31.69           O  
ANISOU 5463  O   HOH A 531     4785   4046   3209   -418    492    709       O  
HETATM 5464  O   HOH A 532     -24.836 -10.640 -15.456  1.00 37.59           O  
ANISOU 5464  O   HOH A 532     5926   5749   2606    363    847   -547       O  
HETATM 5465  O   HOH A 533     -31.967 -16.518  16.964  1.00 35.98           O  
ANISOU 5465  O   HOH A 533     5687   4928   3054    461   -753   -560       O  
HETATM 5466  O   HOH A 534     -35.002 -18.205 -27.616  1.00 26.41           O  
ANISOU 5466  O   HOH A 534     4530   3731   1772   -278   1155   -262       O  
HETATM 5467  O   HOH A 535     -43.325  -8.504 -25.893  1.00 30.49           O  
ANISOU 5467  O   HOH A 535     4718   4988   1878      1  -1586   -758       O  
HETATM 5468  O   HOH A 536     -46.663   5.823  13.857  1.00 21.51           O  
ANISOU 5468  O   HOH A 536     3051   4078   1042    483    305   -315       O  
HETATM 5469  O   HOH A 537     -51.174  -6.345  15.895  1.00 21.90           O  
ANISOU 5469  O   HOH A 537     3867   3558    893     63    242   -181       O  
HETATM 5470  O   HOH A 538     -58.999 -27.743  -2.750  1.00 36.25           O  
ANISOU 5470  O   HOH A 538     5032   4976   3766   -859   -612    920       O  
HETATM 5471  O   HOH A 539     -52.502 -19.610 -12.363  1.00 19.60           O  
ANISOU 5471  O   HOH A 539     3541   3149    754   -257   -182    382       O  
HETATM 5472  O   HOH A 540     -55.190 -22.178   0.282  1.00 25.52           O  
ANISOU 5472  O   HOH A 540     4624   3069   2001   -329    987    244       O  
HETATM 5473  O   HOH A 541     -48.761 -19.676  13.615  1.00 32.50           O  
ANISOU 5473  O   HOH A 541     5091   3781   3478    -39    921    319       O  
HETATM 5474  O   HOH A 542     -48.562 -23.361 -19.493  1.00 18.48           O  
ANISOU 5474  O   HOH A 542     4035   2217    767   -291   -519    112       O  
HETATM 5475  O   HOH A 543     -32.657  -6.205  11.451  1.00 28.12           O  
ANISOU 5475  O   HOH A 543     4608   4989   1086   -440    -72   -694       O  
HETATM 5476  O   HOH A 544     -32.887 -24.318   2.878  1.00 16.77           O  
ANISOU 5476  O   HOH A 544     2916   2788    665    472   -107    281       O  
HETATM 5477  O   HOH A 545     -63.061  -5.659   9.476  1.00 21.41           O  
ANISOU 5477  O   HOH A 545     2975   3842   1316   -371     91    347       O  
HETATM 5478  O   HOH A 546     -21.688 -19.606   1.357  1.00 29.91           O  
ANISOU 5478  O   HOH A 546     3362   4729   3272   -213   -453   -429       O  
HETATM 5479  O   HOH A 547     -58.604  -9.298  10.954  1.00 22.06           O  
ANISOU 5479  O   HOH A 547     3565   3469   1346     90     21    648       O  
HETATM 5480  O   HOH A 548     -56.883   1.781  11.967  1.00 16.22           O  
ANISOU 5480  O   HOH A 548     2896   2979    286   -112   -177    214       O  
HETATM 5481  O   HOH A 549     -38.016  -0.417   9.874  1.00 25.41           O  
ANISOU 5481  O   HOH A 549     4543   3031   2078    -21    306    673       O  
HETATM 5482  O   HOH A 550     -62.047 -28.138  -8.775  1.00 34.09           O  
ANISOU 5482  O   HOH A 550     5656   3493   3803  -1162   -450    124       O  
HETATM 5483  O   HOH A 551     -27.571  -8.309 -15.207  1.00 34.07           O  
ANISOU 5483  O   HOH A 551     5038   5708   2198    -11    210     81       O  
HETATM 5484  O   HOH A 552     -51.401 -13.557 -36.389  1.00 34.25           O  
ANISOU 5484  O   HOH A 552     6082   4281   2650   -331     -3   1095       O  
HETATM 5485  O   HOH A 553     -48.521  -2.459  13.456  1.00 24.21           O  
ANISOU 5485  O   HOH A 553     3866   4052   1279    264    356     29       O  
HETATM 5486  O   HOH A 554     -66.730 -12.004  -4.322  1.00 26.80           O  
ANISOU 5486  O   HOH A 554     3364   4887   1930   -688    126   -498       O  
HETATM 5487  O   HOH A 555     -15.937 -11.893  -7.429  1.00 41.00           O  
ANISOU 5487  O   HOH A 555     4417   6501   4660   -301   1069   -180       O  
HETATM 5488  O   HOH A 556     -42.518 -28.083  -6.184  1.00 24.01           O  
ANISOU 5488  O   HOH A 556     3801   3648   1673   -295   -424    598       O  
HETATM 5489  O   HOH A 557     -44.534  -8.025 -23.536  1.00 24.33           O  
ANISOU 5489  O   HOH A 557     4042   3582   1620   -258     39   -639       O  
HETATM 5490  O   HOH A 558     -45.869 -22.145 -37.952  1.00 42.96           O  
ANISOU 5490  O   HOH A 558     6150   7839   2332    220   -111   -701       O  
HETATM 5491  O   HOH A 559     -22.440 -11.041 -11.900  1.00 25.03           O  
ANISOU 5491  O   HOH A 559     4510   3704   1295     92    788    241       O  
HETATM 5492  O   HOH A 560     -47.443   1.712   5.311  1.00 24.13           O  
ANISOU 5492  O   HOH A 560     3531   4406   1228   -307     23  -1067       O  
HETATM 5493  O   HOH A 561     -47.040 -18.338 -38.901  1.00 36.40           O  
ANISOU 5493  O   HOH A 561     5743   5441   2646   -284    198  -1252       O  
HETATM 5494  O   HOH A 562     -52.845 -14.013 -18.556  1.00 17.43           O  
ANISOU 5494  O   HOH A 562     3055   2618    946   -278    157    401       O  
HETATM 5495  O   HOH A 563     -45.746 -23.534 -33.090  1.00 35.05           O  
ANISOU 5495  O   HOH A 563     5775   4532   3008   -553    223    288       O  
HETATM 5496  O   HOH A 564     -66.457 -13.097  -0.588  1.00 28.93           O  
ANISOU 5496  O   HOH A 564     5199   3752   2042   -564    973     57       O  
HETATM 5497  O   HOH A 565     -44.369 -24.165 -27.933  1.00 35.96           O  
ANISOU 5497  O   HOH A 565     5625   5477   2561   1665    446  -1228       O  
HETATM 5498  O   HOH A 566     -65.700   3.247   7.494  1.00 20.06           O  
ANISOU 5498  O   HOH A 566     2632   3167   1820    326    354   -223       O  
HETATM 5499  O   HOH A 567     -39.762 -14.173  -9.485  1.00 17.52           O  
ANISOU 5499  O   HOH A 567     3368   2566    720     88     99    461       O  
HETATM 5500  O   HOH A 568     -52.876 -10.275 -30.333  1.00 36.49           O  
ANISOU 5500  O   HOH A 568     5770   5081   3013    118     85    603       O  
HETATM 5501  O   HOH A 569     -41.271 -14.393 -14.889  1.00 22.69           O  
ANISOU 5501  O   HOH A 569     4592   3323    706    -23   -257    102       O  
HETATM 5502  O   HOH A 570     -20.854 -24.592   0.841  1.00 35.74           O  
ANISOU 5502  O   HOH A 570     5642   4634   3301     61    754    -18       O  
HETATM 5503  O   HOH A 571     -42.259 -22.605  11.280  1.00 28.02           O  
ANISOU 5503  O   HOH A 571     4247   4353   2045    322   -234     33       O  
HETATM 5504  O   HOH A 572     -49.978   0.849  19.355  1.00 26.01           O  
ANISOU 5504  O   HOH A 572     4577   3482   1822    -15    218      9       O  
HETATM 5505  O   HOH A 573     -39.661  -4.018   2.953  1.00 19.30           O  
ANISOU 5505  O   HOH A 573     3001   3849    481    451   -535   -562       O  
HETATM 5506  O   HOH A 574     -53.593 -28.058 -16.825  1.00 32.05           O  
ANISOU 5506  O   HOH A 574     5643   3547   2987   -529    875  -1116       O  
HETATM 5507  O   HOH A 575     -33.723 -13.076 -18.449  1.00 26.48           O  
ANISOU 5507  O   HOH A 575     3887   3659   2514   -478    537   1257       O  
HETATM 5508  O   HOH A 576     -63.780 -12.863 -12.298  1.00 37.41           O  
ANISOU 5508  O   HOH A 576     5300   6289   2625   -292     -1    -25       O  
HETATM 5509  O   HOH A 577     -30.379 -12.572  10.202  1.00 31.84           O  
ANISOU 5509  O   HOH A 577     4878   4733   2485    951   -128      6       O  
HETATM 5510  O   HOH A 578     -51.731  -6.557  -3.261  1.00 17.43           O  
ANISOU 5510  O   HOH A 578     2699   2759   1165   -187   -276    124       O  
HETATM 5511  O   HOH A 579     -34.857  -1.617  12.609  1.00 32.49           O  
ANISOU 5511  O   HOH A 579     4947   5388   2007  -1035     80   -839       O  
HETATM 5512  O   HOH A 580     -40.612 -20.597  10.824  1.00 20.33           O  
ANISOU 5512  O   HOH A 580     4195   2820    709    299   -138     -8       O  
HETATM 5513  O   HOH A 581     -28.190 -25.791   7.407  1.00 19.32           O  
ANISOU 5513  O   HOH A 581     3644   3092    604    126   -278    347       O  
HETATM 5514  O   HOH A 582     -34.406 -14.110 -21.562  1.00 28.91           O  
ANISOU 5514  O   HOH A 582     4132   3001   3848   -502    314     33       O  
HETATM 5515  O   HOH A 583     -41.465 -11.111 -20.205  1.00 20.08           O  
ANISOU 5515  O   HOH A 583     3839   2596   1192    253    247   -103       O  
HETATM 5516  O   HOH A 584     -22.831  -3.483   4.721  1.00 27.70           O  
ANISOU 5516  O   HOH A 584     3757   4646   2119   -516    510   -476       O  
HETATM 5517  O   HOH A 585     -53.115 -27.165  -3.318  1.00 35.02           O  
ANISOU 5517  O   HOH A 585     5313   2980   5009   -700   -253    471       O  
HETATM 5518  O   HOH A 586     -25.266 -30.560  -0.961  1.00 37.26           O  
ANISOU 5518  O   HOH A 586     5321   4682   4154    601   1536  -1009       O  
HETATM 5519  O   HOH A 587     -27.830 -24.183 -18.198  1.00 39.37           O  
ANISOU 5519  O   HOH A 587     6118   5566   3272   1119   -506   -516       O  
HETATM 5520  O   HOH A 588     -50.952  -8.778 -18.446  1.00 18.63           O  
ANISOU 5520  O   HOH A 588     3164   2729   1183   -103   -149     23       O  
HETATM 5521  O   HOH A 589     -20.382  -0.924  -1.114  1.00 41.39           O  
ANISOU 5521  O   HOH A 589     5212   5307   5207    178    461    258       O  
HETATM 5522  O   HOH A 590     -45.148  -1.739 -21.521  1.00 25.26           O  
ANISOU 5522  O   HOH A 590     4478   3233   1887    148   -138     57       O  
HETATM 5523  O   HOH A 591     -20.117  -9.749 -11.486  1.00 32.30           O  
ANISOU 5523  O   HOH A 591     4538   5093   2640   -175    794    223       O  
HETATM 5524  O   HOH A 592     -42.220 -25.922 -22.658  1.00 24.82           O  
ANISOU 5524  O   HOH A 592     4793   3451   1185    506    718   -497       O  
HETATM 5525  O   HOH A 593     -32.269  -6.821 -15.152  1.00 36.90           O  
ANISOU 5525  O   HOH A 593     5980   5750   2289    434    787    735       O  
HETATM 5526  O   HOH A 594     -47.702 -24.593 -31.719  1.00 30.40           O  
ANISOU 5526  O   HOH A 594     6534   3770   1247     53    398    163       O  
HETATM 5527  O   HOH A 595     -72.291  -2.600   0.290  1.00 42.07           O  
ANISOU 5527  O   HOH A 595     5049   6287   4647   -250    -33    292       O  
HETATM 5528  O   HOH A 596     -37.265 -30.864   2.691  1.00 27.10           O  
ANISOU 5528  O   HOH A 596     4683   3847   1765    222    177   -201       O  
HETATM 5529  O   HOH A 597     -45.161 -16.508 -35.964  1.00 29.19           O  
ANISOU 5529  O   HOH A 597     5582   4163   1343   -193   -267   -128       O  
HETATM 5530  O   HOH A 598     -43.836   1.868   4.092  1.00 28.81           O  
ANISOU 5530  O   HOH A 598     4977   3852   2115   -302   -481   -146       O  
HETATM 5531  O   HOH A 599     -42.508 -12.045 -16.013  1.00 20.99           O  
ANISOU 5531  O   HOH A 599     4285   2563   1128   -175    253    110       O  
HETATM 5532  O   HOH A 600     -24.255 -13.162 -14.546  1.00 35.23           O  
ANISOU 5532  O   HOH A 600     4767   5975   2640    275    152    295       O  
HETATM 5533  O   HOH A 601     -48.802  -5.188  -4.586  1.00 19.67           O  
ANISOU 5533  O   HOH A 601     3259   3264    950    216   -285   -333       O  
HETATM 5534  O   HOH A 602     -33.728 -14.204  10.959  1.00 30.91           O  
ANISOU 5534  O   HOH A 602     4915   4166   2662    -78    520     -4       O  
HETATM 5535  O   HOH A 603     -29.390 -32.237  -2.196  1.00 31.46           O  
ANISOU 5535  O   HOH A 603     5627   3804   2521   1223   -352   -533       O  
HETATM 5536  O   HOH A 604     -31.715 -17.619 -19.943  1.00 24.51           O  
ANISOU 5536  O   HOH A 604     3830   4378   1106    142    859   -801       O  
HETATM 5537  O   HOH A 605     -67.764   6.692   9.100  1.00 35.11           O  
ANISOU 5537  O   HOH A 605     4339   4806   4193     80    124    840       O  
HETATM 5538  O   HOH A 606     -50.865 -17.117  -5.536  1.00 18.23           O  
ANISOU 5538  O   HOH A 606     3439   2708    778    128   -101    150       O  
HETATM 5539  O   HOH A 607     -43.567  -9.419  12.112  1.00 20.54           O  
ANISOU 5539  O   HOH A 607     3038   3471   1292    223   -230   -386       O  
HETATM 5540  O   HOH A 608     -48.998 -25.363   5.280  1.00 26.80           O  
ANISOU 5540  O   HOH A 608     4930   2787   2465    -84    712     55       O  
HETATM 5541  O   HOH A 609     -50.101 -23.218   2.297  1.00 18.79           O  
ANISOU 5541  O   HOH A 609     3599   2267   1272   -100    -22     -2       O  
HETATM 5542  O   HOH A 610     -52.396 -16.677 -10.637  1.00 22.06           O  
ANISOU 5542  O   HOH A 610     4255   3317    809   -690     -9    299       O  
HETATM 5543  O   HOH A 611     -42.172 -25.120 -25.255  1.00 26.93           O  
ANISOU 5543  O   HOH A 611     4682   3969   1579    191    181   -681       O  
HETATM 5544  O   HOH A 612     -56.672 -10.779  17.262  1.00 36.40           O  
ANISOU 5544  O   HOH A 612     6756   4129   2946    -30    912     94       O  
HETATM 5545  O   HOH A 613     -54.771  -7.597 -15.746  1.00 15.24           O  
ANISOU 5545  O   HOH A 613     2885   2331    575     -8   -410   -511       O  
HETATM 5546  O   HOH A 614     -31.076 -22.501   4.190  1.00 18.67           O  
ANISOU 5546  O   HOH A 614     2800   2981   1310    243   -103    343       O  
HETATM 5547  O   HOH A 615     -18.923  -6.856   3.986  1.00 36.47           O  
ANISOU 5547  O   HOH A 615     4108   5967   3782     72    249    151       O  
HETATM 5548  O   HOH A 616     -58.573   2.079  14.289  1.00 16.35           O  
ANISOU 5548  O   HOH A 616     2952   2886    373    163      8    312       O  
HETATM 5549  O   HOH A 617     -44.047 -15.890  19.804  1.00 38.14           O  
ANISOU 5549  O   HOH A 617     6181   5397   2913    422   -185    635       O  
HETATM 5550  O   HOH A 618     -45.184  -1.123   8.230  1.00 15.25           O  
ANISOU 5550  O   HOH A 618     2873   2373    547    -80    359    117       O  
HETATM 5551  O   HOH A 619     -47.801 -11.012 -34.370  1.00 30.13           O  
ANISOU 5551  O   HOH A 619     4587   3650   3210   -596     22    967       O  
HETATM 5552  O   HOH A 620     -22.332  -8.104 -14.250  1.00 37.96           O  
ANISOU 5552  O   HOH A 620     5481   5347   3593      5    772   -354       O  
HETATM 5553  O   HOH A 621     -53.427 -17.225  -6.657  1.00 21.97           O  
ANISOU 5553  O   HOH A 621     3890   3182   1274   -309   -184    158       O  
HETATM 5554  O   HOH A 622     -32.715  -3.528   2.618  1.00 27.37           O  
ANISOU 5554  O   HOH A 622     4802   4131   1467    950    504    573       O  
HETATM 5555  O   HOH A 623     -57.064  -6.897  -6.490  1.00 16.35           O  
ANISOU 5555  O   HOH A 623     2401   2932    879   -507     -2    170       O  
HETATM 5556  O   HOH A 624     -25.394 -24.387 -12.598  1.00 27.02           O  
ANISOU 5556  O   HOH A 624     4869   3540   1857    587   1732    210       O  
HETATM 5557  O   HOH A 625     -29.659 -22.625   6.691  1.00 22.89           O  
ANISOU 5557  O   HOH A 625     3886   3528   1281    354    306    654       O  
HETATM 5558  O   HOH A 626     -44.650 -17.704  -7.478  1.00 16.26           O  
ANISOU 5558  O   HOH A 626     3238   2306    635     -1     32     91       O  
HETATM 5559  O   HOH A 627     -32.909 -12.900   8.912  1.00 28.94           O  
ANISOU 5559  O   HOH A 627     4832   4488   1675    308   -347   -314       O  
HETATM 5560  O   HOH A 628     -65.087 -13.657 -26.777  1.00 44.69           O  
ANISOU 5560  O   HOH A 628     5189   7065   4724    437   -522   -613       O  
HETATM 5561  O   HOH A 629     -46.291  -3.868  13.075  1.00 18.99           O  
ANISOU 5561  O   HOH A 629     3253   3201    759    215    255   -356       O  
HETATM 5562  O   HOH A 630     -41.688  -9.760 -14.948  1.00 20.04           O  
ANISOU 5562  O   HOH A 630     3536   2819   1259    -64     29      5       O  
HETATM 5563  O   HOH A 631     -18.185 -14.675  -6.408  1.00 34.34           O  
ANISOU 5563  O   HOH A 631     3551   5585   3910   -221    567    -91       O  
HETATM 5564  O   HOH A 632     -57.663   3.322   4.390  1.00 19.28           O  
ANISOU 5564  O   HOH A 632     3092   2270   1962   -164    283    532       O  
HETATM 5565  O   HOH A 633     -37.529 -22.778 -31.212  1.00 38.37           O  
ANISOU 5565  O   HOH A 633     6436   3412   4729    484  -1488  -2003       O  
HETATM 5566  O   HOH A 634     -17.911 -11.979  -0.629  1.00 35.53           O  
ANISOU 5566  O   HOH A 634     3933   5311   4256    354   -315   -867       O  
HETATM 5567  O   HOH A 635     -26.522 -14.617   3.881  1.00 29.49           O  
ANISOU 5567  O   HOH A 635     4174   5539   1488    260    117   -817       O  
HETATM 5568  O   HOH A 636     -41.666   5.457  16.837  1.00 16.23           O  
ANISOU 5568  O   HOH A 636     3307   2482    377    -15    187   -105       O  
HETATM 5569  O   HOH A 637     -34.232  -7.656 -16.837  1.00 36.25           O  
ANISOU 5569  O   HOH A 637     5565   5105   3102    213    -57   1126       O  
HETATM 5570  O   HOH A 638     -34.589 -15.776   8.049  1.00 25.77           O  
ANISOU 5570  O   HOH A 638     4268   3397   2125    129    578    -54       O  
HETATM 5571  O   HOH A 639     -43.670 -12.021 -25.724  1.00 24.74           O  
ANISOU 5571  O   HOH A 639     4594   3569   1235    177    204    933       O  
HETATM 5572  O   HOH A 640     -22.844 -21.034   3.772  1.00 29.92           O  
ANISOU 5572  O   HOH A 640     4014   4941   2412    162   -219     -8       O  
HETATM 5573  O   HOH A 641     -31.245  -3.063 -12.430  1.00 24.28           O  
ANISOU 5573  O   HOH A 641     4166   3714   1343   -310    134    694       O  
HETATM 5574  O   HOH A 642     -65.248   6.307   4.400  1.00 36.70           O  
ANISOU 5574  O   HOH A 642     3909   5729   4306    193   -113    703       O  
HETATM 5575  O   HOH A 643     -37.021  -5.489 -22.158  1.00 30.60           O  
ANISOU 5575  O   HOH A 643     5280   4662   1683   -234     51    332       O  
HETATM 5576  O   HOH A 644     -56.252  -1.312  -2.876  1.00 17.50           O  
ANISOU 5576  O   HOH A 644     2995   2119   1534   -111   -110   -163       O  
HETATM 5577  O   HOH A 645     -57.472  -2.397  -9.280  1.00 15.75           O  
ANISOU 5577  O   HOH A 645     2850   2851    283    146   -244   -153       O  
HETATM 5578  O   HOH A 646     -59.424 -28.453  -5.825  1.00 35.92           O  
ANISOU 5578  O   HOH A 646     6444   4077   3126  -1510    128    106       O  
HETATM 5579  O   HOH A 647     -60.533  -5.457  16.343  1.00 26.44           O  
ANISOU 5579  O   HOH A 647     4217   3511   2317   -226    918    172       O  
HETATM 5580  O   HOH A 648     -36.563 -11.447 -25.315  1.00 25.37           O  
ANISOU 5580  O   HOH A 648     4257   3078   2303    426   -157    198       O  
HETATM 5581  O   HOH A 649     -68.174  -0.323  11.829  1.00 34.91           O  
ANISOU 5581  O   HOH A 649     4904   4894   3465   -611     73     22       O  
HETATM 5582  O   HOH A 650     -18.760 -10.057  -5.348  1.00 28.98           O  
ANISOU 5582  O   HOH A 650     3773   5202   2036    181    502   -587       O  
HETATM 5583  O   HOH A 651     -29.032  -5.202  10.372  1.00 36.23           O  
ANISOU 5583  O   HOH A 651     5683   6035   2044   -362  -1782    673       O  
HETATM 5584  O   HOH A 652     -26.476 -18.855   6.690  1.00 32.15           O  
ANISOU 5584  O   HOH A 652     6258   4374   1581   1075    165    492       O  
HETATM 5585  O   HOH A 653     -26.346   1.609  -9.380  1.00 40.35           O  
ANISOU 5585  O   HOH A 653     6252   6651   2426  -2031    384    459       O  
HETATM 5586  O   HOH A 654     -44.632 -27.305  -4.975  1.00 21.72           O  
ANISOU 5586  O   HOH A 654     4414   2964    871   -417   -361    127       O  
HETATM 5587  O   HOH A 655     -60.573   5.851  14.862  1.00 17.46           O  
ANISOU 5587  O   HOH A 655     3009   2683    941    265    101   -191       O  
HETATM 5588  O   HOH A 656     -43.464 -29.193 -12.025  1.00 26.18           O  
ANISOU 5588  O   HOH A 656     5471   2676   1800   -619   -330   -287       O  
HETATM 5589  O   HOH A 657     -18.974 -13.849 -11.301  1.00 41.66           O  
ANISOU 5589  O   HOH A 657     8577   4180   3073   1064   1871    408       O  
HETATM 5590  O   HOH A 658     -53.030 -14.424  -9.439  1.00 19.06           O  
ANISOU 5590  O   HOH A 658     3188   3141    910     72    206    408       O  
HETATM 5591  O   HOH A 659     -36.450  -7.956  14.232  1.00 28.01           O  
ANISOU 5591  O   HOH A 659     4626   3503   2513   -352   -159    172       O  
HETATM 5592  O   HOH A 660     -58.284 -14.057 -27.741  1.00 32.57           O  
ANISOU 5592  O   HOH A 660     5294   4698   2381   -158   -678     68       O  
HETATM 5593  O   HOH A 661     -63.291 -12.240  -6.039  1.00 25.93           O  
ANISOU 5593  O   HOH A 661     3829   3958   2064   -454   -302     75       O  
HETATM 5594  O   HOH A 662     -47.753   3.076  21.204  1.00 31.47           O  
ANISOU 5594  O   HOH A 662     4135   6215   1605    182   -662   -231       O  
HETATM 5595  O   HOH A 663     -49.687 -12.226 -32.558  1.00 32.68           O  
ANISOU 5595  O   HOH A 663     4627   4727   3061  -1225     28    758       O  
HETATM 5596  O   HOH A 664     -31.869 -31.623  -3.508  1.00 24.91           O  
ANISOU 5596  O   HOH A 664     5157   2918   1387    673   -375   -284       O  
HETATM 5597  O   HOH A 665     -58.229 -10.673   8.393  1.00 19.89           O  
ANISOU 5597  O   HOH A 665     3470   3073   1012    -88    439    -27       O  
HETATM 5598  O   HOH A 666     -47.379 -13.153 -19.866  1.00 16.93           O  
ANISOU 5598  O   HOH A 666     3100   2780    550    233    245    454       O  
HETATM 5599  O   HOH A 667     -44.486 -11.945 -28.265  1.00 28.40           O  
ANISOU 5599  O   HOH A 667     5619   3277   1892   -157   -393   -393       O  
HETATM 5600  O   HOH A 668     -66.491 -18.635 -13.301  1.00 30.47           O  
ANISOU 5600  O   HOH A 668     4321   4578   2676   -552   -659   -159       O  
HETATM 5601  O   HOH A 669     -40.061  -2.805  16.857  1.00 29.36           O  
ANISOU 5601  O   HOH A 669     5270   4474   1408   -495     13     -1       O  
HETATM 5602  O   HOH A 670     -40.848 -29.159  -9.878  1.00 24.78           O  
ANISOU 5602  O   HOH A 670     5040   2710   1664    122   -261   -391       O  
HETATM 5603  O   HOH A 671     -53.166   1.153  21.644  1.00 31.32           O  
ANISOU 5603  O   HOH A 671     5154   3961   2785    123     93   -130       O  
HETATM 5604  O   HOH A 672     -36.611   1.562  11.518  1.00 35.95           O  
ANISOU 5604  O   HOH A 672     5556   5539   2561   1105   1449    414       O  
HETATM 5605  O   HOH A 673     -45.884 -14.933 -21.605  1.00 22.69           O  
ANISOU 5605  O   HOH A 673     4193   3494    932   -989   -979    792       O  
HETATM 5606  O   HOH A 674     -40.043 -17.138  19.730  1.00 41.31           O  
ANISOU 5606  O   HOH A 674     7785   5825   2083   1338    651   -528       O  
HETATM 5607  O   HOH A 675     -33.643 -33.185  -2.522  1.00 29.70           O  
ANISOU 5607  O   HOH A 675     5593   2723   2968     78    163     37       O  
HETATM 5608  O   HOH A 676     -25.900 -11.107   4.568  1.00 32.06           O  
ANISOU 5608  O   HOH A 676     3247   6068   2866   -610   -666   1259       O  
HETATM 5609  O   HOH A 677     -64.502   3.815  16.138  1.00 36.34           O  
ANISOU 5609  O   HOH A 677     4970   6811   2024    361    958  -1137       O  
HETATM 5610  O   HOH A 678     -58.881 -23.019  -0.184  1.00 28.10           O  
ANISOU 5610  O   HOH A 678     5597   3385   1692    -92   -293     21       O  
HETATM 5611  O   HOH A 679     -49.631 -21.403   0.198  1.00 18.68           O  
ANISOU 5611  O   HOH A 679     3475   2443   1180     76    -14    159       O  
HETATM 5612  O   HOH A 680     -49.492 -14.174  -3.511  1.00 16.79           O  
ANISOU 5612  O   HOH A 680     3084   2526    767    242   -159    -58       O  
HETATM 5613  O   HOH A 681     -65.088   9.391  10.914  1.00 33.65           O  
ANISOU 5613  O   HOH A 681     4794   5053   2938    877    432    173       O  
HETATM 5614  O   HOH A 682     -20.367  -6.993 -10.468  1.00 32.45           O  
ANISOU 5614  O   HOH A 682     5278   4790   2258    448    910    296       O  
HETATM 5615  O   HOH A 683     -33.872 -10.951 -32.057  1.00 39.03           O  
ANISOU 5615  O   HOH A 683     6283   3168   5376   -141   -447    633       O  
HETATM 5616  O   HOH A 684     -31.979 -18.692  14.471  1.00 27.68           O  
ANISOU 5616  O   HOH A 684     4782   3648   2085    380    210   -908       O  
HETATM 5617  O   HOH A 685     -31.846  -0.034   3.391  1.00 25.89           O  
ANISOU 5617  O   HOH A 685     4171   3369   2294    204   1024   -179       O  
HETATM 5618  O   HOH A 686     -54.979 -22.053  -9.112  1.00 22.07           O  
ANISOU 5618  O   HOH A 686     3881   3496   1005   -319   -116     43       O  
HETATM 5619  O   HOH A 687     -40.228 -30.203   8.662  1.00 35.75           O  
ANISOU 5619  O   HOH A 687     6704   4478   2399     -8    477   1282       O  
HETATM 5620  O   HOH A 688     -38.021  -1.700 -21.707  1.00 22.93           O  
ANISOU 5620  O   HOH A 688     4401   3274   1036   -473   -156   -263       O  
HETATM 5621  O   HOH A 689     -32.073 -15.618  12.607  1.00 35.25           O  
ANISOU 5621  O   HOH A 689     4462   4948   3982   -515    275    587       O  
HETATM 5622  O   HOH A 690     -28.250 -20.637   9.685  1.00 25.57           O  
ANISOU 5622  O   HOH A 690     4464   3299   1950    278    330   -338       O  
HETATM 5623  O   HOH A 691     -30.457 -25.417 -18.211  1.00 34.83           O  
ANISOU 5623  O   HOH A 691     5788   4799   2646   1396   -304  -1615       O  
HETATM 5624  O   HOH A 692     -49.797  -8.622  15.214  1.00 23.66           O  
ANISOU 5624  O   HOH A 692     3645   4066   1277    118    666   -327       O  
HETATM 5625  O   HOH A 693     -50.574 -28.324  -2.865  1.00 28.17           O  
ANISOU 5625  O   HOH A 693     5485   2419   2797   -350  -1664   -544       O  
HETATM 5626  O   HOH A 694     -25.387 -15.741 -15.040  1.00 26.87           O  
ANISOU 5626  O   HOH A 694     4553   4717    937    846    198    186       O  
HETATM 5627  O   HOH A 695     -21.090   1.247  -8.146  1.00 36.18           O  
ANISOU 5627  O   HOH A 695     5332   5147   3267     55    653  -1119       O  
HETATM 5628  O   HOH A 696     -52.698 -27.691 -11.306  1.00 30.25           O  
ANISOU 5628  O   HOH A 696     5391   3826   2274  -1034   -243    836       O  
HETATM 5629  O   HOH A 697     -66.012  -9.802  -5.989  1.00 32.26           O  
ANISOU 5629  O   HOH A 697     3907   5185   3163   -643   -674     47       O  
HETATM 5630  O   HOH A 698     -54.230 -17.396 -12.658  1.00 20.53           O  
ANISOU 5630  O   HOH A 698     3158   3103   1539   -719   -415    677       O  
HETATM 5631  O   HOH A 699     -36.888 -33.809   0.726  1.00 32.23           O  
ANISOU 5631  O   HOH A 699     4934   3914   3396   -286    532    777       O  
HETATM 5632  O   HOH A 700     -36.734 -25.994   7.779  1.00 27.85           O  
ANISOU 5632  O   HOH A 700     4601   3938   2040    371    295   -182       O  
HETATM 5633  O   HOH A 701     -45.168 -27.728   1.721  1.00 37.79           O  
ANISOU 5633  O   HOH A 701     6445   5081   2831   1018    -73  -1430       O  
HETATM 5634  O   HOH A 702     -30.378  -8.557 -14.222  1.00 24.54           O  
ANISOU 5634  O   HOH A 702     4460   3833   1030   -567    842    281       O  
HETATM 5635  O   HOH A 703     -20.850 -21.754   0.149  1.00 31.32           O  
ANISOU 5635  O   HOH A 703     4566   4863   2471    -38   -126   -677       O  
HETATM 5636  O   HOH A 704     -25.664  -4.009 -13.635  1.00 35.96           O  
ANISOU 5636  O   HOH A 704     6126   5844   1690   -152    326   -297       O  
HETATM 5637  O   HOH A 705     -48.829 -29.057 -25.870  1.00 41.85           O  
ANISOU 5637  O   HOH A 705    10038   2853   3011  -1920  -2867    705       O  
HETATM 5638  O   HOH A 706     -58.248   4.818  24.864  1.00 22.19           O  
ANISOU 5638  O   HOH A 706     4103   3629    699    602    789    786       O  
HETATM 5639  O   HOH A 707     -18.804 -20.846   2.503  1.00 39.94           O  
ANISOU 5639  O   HOH A 707     5769   6247   3156   -430   -645   -777       O  
HETATM 5640  O   HOH A 708     -34.400 -30.587  -8.968  1.00 26.43           O  
ANISOU 5640  O   HOH A 708     4049   2843   3148    123   -857   -573       O  
HETATM 5641  O   HOH A 709     -33.195 -18.123   8.394  1.00 23.40           O  
ANISOU 5641  O   HOH A 709     4365   3544    981    325    340    -19       O  
HETATM 5642  O   HOH A 710     -58.407   0.336   1.533  1.00 21.99           O  
ANISOU 5642  O   HOH A 710     3803   3702    848    237    432   -226       O  
HETATM 5643  O   HOH A 711     -62.814 -18.060  -8.398  1.00 33.83           O  
ANISOU 5643  O   HOH A 711     4149   6016   2688    125   -148     43       O  
HETATM 5644  O   HOH A 712     -24.367 -13.063   4.285  1.00 33.73           O  
ANISOU 5644  O   HOH A 712     4982   4941   2892    515   -999   -240       O  
HETATM 5645  O   HOH A 713     -34.092 -10.206 -18.776  1.00 37.12           O  
ANISOU 5645  O   HOH A 713     6283   5105   2713   -313    988   1250       O  
HETATM 5646  O   HOH A 714     -71.341  -2.546   3.733  1.00 31.16           O  
ANISOU 5646  O   HOH A 714     3265   5006   3569   -238     25    875       O  
HETATM 5647  O   HOH A 715     -26.980 -24.114 -14.901  1.00 28.44           O  
ANISOU 5647  O   HOH A 715     5056   4307   1441    329    455   -307       O  
HETATM 5648  O   HOH A 716     -37.146 -15.287 -28.621  1.00 27.75           O  
ANISOU 5648  O   HOH A 716     4646   3763   2135    515    317     47       O  
HETATM 5649  O   HOH A 717     -50.204 -18.640 -40.825  1.00 33.74           O  
ANISOU 5649  O   HOH A 717     6310   5031   1476    343   -477   -529       O  
HETATM 5650  O   HOH A 718     -48.752 -18.537 -13.212  1.00 25.49           O  
ANISOU 5650  O   HOH A 718     3766   3856   2060   -321   -117   -562       O  
HETATM 5651  O   HOH A 719     -48.545   1.977  12.347  1.00 18.92           O  
ANISOU 5651  O   HOH A 719     3167   3401    620    -13    162    220       O  
HETATM 5652  O   HOH A 720     -42.264 -20.211 -36.557  1.00 39.51           O  
ANISOU 5652  O   HOH A 720     5968   5526   3516   -883     76   -785       O  
HETATM 5653  O   HOH A 721     -43.632  -4.544  15.666  1.00 24.42           O  
ANISOU 5653  O   HOH A 721     4188   4328    761    254    395    388       O  
HETATM 5654  O   HOH A 722     -41.642 -15.893 -11.689  1.00 32.25           O  
ANISOU 5654  O   HOH A 722     4882   4263   3110    -56    398    697       O  
HETATM 5655  O   HOH A 723     -20.651 -25.776  -6.366  1.00 31.74           O  
ANISOU 5655  O   HOH A 723     5254   4113   2690    847     15   -290       O  
HETATM 5656  O   HOH A 724     -44.714  -4.666  -3.917  1.00 18.59           O  
ANISOU 5656  O   HOH A 724     3266   2635   1162    229    297    293       O  
HETATM 5657  O   HOH A 725     -47.837   8.244  11.000  1.00 28.97           O  
ANISOU 5657  O   HOH A 725     4053   4753   2201    348    185   -353       O  
HETATM 5658  O   HOH A 726     -58.112   4.281   6.808  1.00 17.60           O  
ANISOU 5658  O   HOH A 726     2697   2469   1520    179    -50    760       O  
HETATM 5659  O   HOH A 727     -35.630  -8.618 -21.488  1.00 36.61           O  
ANISOU 5659  O   HOH A 727     5307   6184   2415   -892    570    755       O  
HETATM 5660  O   HOH A 728     -60.743 -21.484   1.975  1.00 33.54           O  
ANISOU 5660  O   HOH A 728     6380   3238   3122     55   1033    -98       O  
HETATM 5661  O   HOH A 729     -44.707  -6.609 -16.438  1.00 19.86           O  
ANISOU 5661  O   HOH A 729     3082   2924   1539   -249    456   -295       O  
HETATM 5662  O   HOH A 730     -58.665 -10.280 -29.236  1.00 36.48           O  
ANISOU 5662  O   HOH A 730     5953   5696   2210   1171  -1008    155       O  
HETATM 5663  O   HOH A 731     -26.491 -34.025  -0.862  1.00 38.64           O  
ANISOU 5663  O   HOH A 731     5954   4879   3847    714   1240   -545       O  
HETATM 5664  O   HOH A 732     -47.798 -22.625  11.957  1.00 28.10           O  
ANISOU 5664  O   HOH A 732     4592   3864   2221    263    385    233       O  
HETATM 5665  O   HOH A 733     -55.272   1.560  24.786  1.00 46.08           O  
ANISOU 5665  O   HOH A 733     6705   6205   4597    380     53   2503       O  
HETATM 5666  O   HOH A 734     -54.259 -28.004 -30.185  1.00 42.34           O  
ANISOU 5666  O   HOH A 734     6268   5332   4487   -701   -912    -55       O  
HETATM 5667  O   HOH A 735     -34.187 -28.401 -22.294  1.00 39.08           O  
ANISOU 5667  O   HOH A 735     5994   6046   2808    621   1131  -2010       O  
HETATM 5668  O   HOH A 736     -43.519 -29.125 -19.297  1.00 26.25           O  
ANISOU 5668  O   HOH A 736     5313   3041   1617   -374    166    410       O  
HETATM 5669  O   HOH A 737     -37.656 -30.378   5.699  1.00 33.05           O  
ANISOU 5669  O   HOH A 737     5456   3772   3326     49    156    774       O  
HETATM 5670  O   HOH A 738     -52.820 -29.047 -28.036  1.00 40.59           O  
ANISOU 5670  O   HOH A 738     7864   4233   3323  -1304   -729    615       O  
HETATM 5671  O   HOH A 739     -64.434 -22.135  -2.076  1.00 40.76           O  
ANISOU 5671  O   HOH A 739     4796   4914   5776  -1558    168    543       O  
HETATM 5672  O   HOH A 740     -49.358 -14.031 -34.701  1.00 34.34           O  
ANISOU 5672  O   HOH A 740     6222   4414   2410   -735    585   -327       O  
HETATM 5673  O   HOH A 741     -25.520  -3.124   7.142  1.00 34.26           O  
ANISOU 5673  O   HOH A 741     5589   4852   2575   -369    -33     18       O  
HETATM 5674  O   HOH A 742     -19.469 -26.665  -9.154  1.00 45.17           O  
ANISOU 5674  O   HOH A 742     5629   6293   5240    687    278   -206       O  
HETATM 5675  O   HOH A 743     -37.951 -15.959 -35.258  1.00 24.39           O  
ANISOU 5675  O   HOH A 743     3913   3804   1551    235    800    696       O  
HETATM 5676  O   HOH A 744     -47.930  -9.213 -18.436  1.00 22.94           O  
ANISOU 5676  O   HOH A 744     3698   3586   1429   -158    182     64       O  
HETATM 5677  O   HOH A 745     -40.115   0.010  11.561  1.00 18.65           O  
ANISOU 5677  O   HOH A 745     3224   2769   1090    393     95   -150       O  
HETATM 5678  O   HOH A 746     -40.943 -29.069  -4.252  1.00 30.23           O  
ANISOU 5678  O   HOH A 746     4688   3277   3521   -811  -1178    327       O  
HETATM 5679  O   HOH A 747     -50.650  -3.651  -5.784  1.00 17.20           O  
ANISOU 5679  O   HOH A 747     3186   2743    603     22    100   -261       O  
HETATM 5680  O   HOH A 748     -30.061 -30.790 -13.983  1.00 39.06           O  
ANISOU 5680  O   HOH A 748     6960   4352   3528   1336     44   -677       O  
HETATM 5681  O   HOH A 749     -55.131 -19.914   8.110  1.00 29.07           O  
ANISOU 5681  O   HOH A 749     4575   3516   2952   -113   -230    521       O  
HETATM 5682  O   HOH A 750     -45.868 -11.237 -18.085  1.00 20.84           O  
ANISOU 5682  O   HOH A 750     3787   3212    919    403    758    274       O  
HETATM 5683  O   HOH A 751     -65.669 -17.028 -25.688  1.00 45.23           O  
ANISOU 5683  O   HOH A 751     3960   8445   4778    -25   1100   -985       O  
HETATM 5684  O   HOH A 752     -31.818 -31.636  -9.568  1.00 30.76           O  
ANISOU 5684  O   HOH A 752     5444   3512   2729    604   -854    -82       O  
HETATM 5685  O   HOH A 753     -55.441  -9.127 -24.473  1.00 21.96           O  
ANISOU 5685  O   HOH A 753     4414   2903   1026   -419   -152    853       O  
HETATM 5686  O   HOH A 754     -64.069 -23.027   0.002  1.00 40.82           O  
ANISOU 5686  O   HOH A 754     6554   4451   4503   -364   1469    486       O  
HETATM 5687  O   HOH A 755     -42.514 -30.590  -2.648  1.00 38.22           O  
ANISOU 5687  O   HOH A 755     4517   4814   5190   -686     73   1089       O  
HETATM 5688  O   HOH A 756     -55.603 -28.775 -11.239  1.00 39.65           O  
ANISOU 5688  O   HOH A 756     6760   5729   2574   -787    661   -148       O  
HETATM 5689  O   HOH A 757     -33.988 -23.491 -22.355  1.00 29.19           O  
ANISOU 5689  O   HOH A 757     6208   3748   1134   1116    -72   -137       O  
HETATM 5690  O   HOH A 758     -37.585 -16.008  -6.100  1.00 15.15           O  
ANISOU 5690  O   HOH A 758     2500   2427    830     86    164    -62       O  
HETATM 5691  O   HOH A 759     -27.537 -21.984 -16.216  1.00 26.65           O  
ANISOU 5691  O   HOH A 759     3948   4096   2079    617    602   -429       O  
HETATM 5692  O   HOH A 760     -22.715 -16.448 -13.317  1.00 36.46           O  
ANISOU 5692  O   HOH A 760     4018   6659   3176    521    970   -151       O  
HETATM 5693  O   HOH A 761     -38.444 -21.177  12.599  1.00 32.91           O  
ANISOU 5693  O   HOH A 761     5415   4437   2652     36      3    507       O  
HETATM 5694  O   HOH A 762     -28.551 -31.491  -6.474  1.00 39.81           O  
ANISOU 5694  O   HOH A 762     6874   4324   3925    502   -647   -241       O  
HETATM 5695  O   HOH A 763     -52.712 -24.162   2.397  1.00 30.58           O  
ANISOU 5695  O   HOH A 763     4928   4287   2403   -415    473    358       O  
HETATM 5696  O   HOH A 764     -42.781   4.736   9.935  1.00 19.75           O  
ANISOU 5696  O   HOH A 764     3503   3114    887     21    257   -260       O  
HETATM 5697  O   HOH A 765     -45.305   5.470  10.719  1.00 21.59           O  
ANISOU 5697  O   HOH A 765     3281   3172   1749    440   -653    173       O  
HETATM 5698  O   HOH A 766     -36.997  -3.873 -16.771  1.00 28.48           O  
ANISOU 5698  O   HOH A 766     5420   4039   1362    173   -181     -2       O  
HETATM 5699  O   HOH A 767     -65.164 -19.455   2.050  1.00 42.94           O  
ANISOU 5699  O   HOH A 767     6017   4790   5506  -2581    156      5       O  
HETATM 5700  O   HOH A 768     -62.478 -10.230 -30.440  1.00 43.38           O  
ANISOU 5700  O   HOH A 768     6582   5470   4430    681  -1390    502       O  
HETATM 5701  O   HOH A 769     -57.108 -11.601 -27.351  1.00 29.51           O  
ANISOU 5701  O   HOH A 769     5160   4090   1960   -383   -534      2       O  
HETATM 5702  O   HOH A 770     -61.469 -20.646  -8.538  1.00 38.45           O  
ANISOU 5702  O   HOH A 770     5979   5149   3481   -415   -342    795       O  
HETATM 5703  O   HOH A 771     -47.961   0.073   3.592  1.00 27.32           O  
ANISOU 5703  O   HOH A 771     3615   4732   2032    -22    698    889       O  
HETATM 5704  O   HOH A 772     -45.665  -7.233 -12.683  1.00 20.41           O  
ANISOU 5704  O   HOH A 772     3211   2423   2121     99    425   -756       O  
HETATM 5705  O   HOH A 773     -22.556 -30.309 -15.136  1.00 42.38           O  
ANISOU 5705  O   HOH A 773     7985   4723   3394    -25    819   -772       O  
HETATM 5706  O   HOH A 774     -67.891   4.183   5.653  1.00 33.87           O  
ANISOU 5706  O   HOH A 774     5375   4488   3003    888    165    551       O  
HETATM 5707  O   HOH A 775     -51.598 -24.639   6.418  1.00 33.23           O  
ANISOU 5707  O   HOH A 775     5007   3548   4070   -828   1042    748       O  
HETATM 5708  O   HOH A 776     -37.246 -29.698 -21.046  1.00 30.99           O  
ANISOU 5708  O   HOH A 776     6245   2350   3177    164    140   -588       O  
HETATM 5709  O   HOH A 777     -38.828 -30.386  -5.181  1.00 21.70           O  
ANISOU 5709  O   HOH A 777     4157   2755   1331   -627   -568     75       O  
HETATM 5710  O   HOH A 778     -20.174  -0.671  -3.654  1.00 40.22           O  
ANISOU 5710  O   HOH A 778     5455   6417   3409   -811   1850   -387       O  
HETATM 5711  O   HOH A 779     -49.886  -7.282 -16.309  1.00 19.35           O  
ANISOU 5711  O   HOH A 779     3615   2738   1000   -434    -34    -17       O  
HETATM 5712  O   HOH A 780     -49.159  -5.124  14.352  1.00 20.93           O  
ANISOU 5712  O   HOH A 780     3659   3656    637    377    108   -622       O  
HETATM 5713  O   HOH A 781     -52.367 -24.991 -40.625  1.00 44.18           O  
ANISOU 5713  O   HOH A 781     6188   5698   4899  -1182     16  -1208       O  
HETATM 5714  O   HOH A 782     -21.674 -24.661   5.082  1.00 37.73           O  
ANISOU 5714  O   HOH A 782     4433   6282   3619    636    120   1230       O  
HETATM 5715  O   HOH A 783     -19.046 -15.477   2.562  1.00 44.23           O  
ANISOU 5715  O   HOH A 783     6679   6764   3362    361   -896  -2212       O  
HETATM 5716  O   HOH A 784     -45.131 -15.214  17.105  1.00 25.52           O  
ANISOU 5716  O   HOH A 784     5419   3842    435   -611   -290    135       O  
HETATM 5717  O   HOH A 785     -35.319 -31.286   5.513  1.00 34.74           O  
ANISOU 5717  O   HOH A 785     5288   4663   3247    145    508   1212       O  
HETATM 5718  O   HOH A 786     -55.988  -6.815  23.106  1.00 48.14           O  
ANISOU 5718  O   HOH A 786     6625   9928   1738    519     21   -213       O  
HETATM 5719  O   HOH A 787     -56.083 -28.279 -16.720  1.00 40.60           O  
ANISOU 5719  O   HOH A 787     6438   5702   3285    -86   1642   -300       O  
HETATM 5720  O   HOH A 788     -49.464   0.275  -1.282  1.00 28.62           O  
ANISOU 5720  O   HOH A 788     4630   3160   3083   -283    160   -821       O  
HETATM 5721  O   HOH A 789     -46.816   4.006   5.229  1.00 33.04           O  
ANISOU 5721  O   HOH A 789     5158   5000   2394    542    630   -323       O  
HETATM 5722  O   HOH A 790     -45.402  -4.188 -27.505  1.00 38.51           O  
ANISOU 5722  O   HOH A 790     9864   3532   1235   -667    339    281       O  
HETATM 5723  O   HOH A 791     -16.392 -13.170   1.596  1.00 45.47           O  
ANISOU 5723  O   HOH A 791     7290   7130   2855    754    -43   -856       O  
HETATM 5724  O   HOH A 792     -51.080  -7.887 -20.954  1.00 22.39           O  
ANISOU 5724  O   HOH A 792     4664   3123    717    231    168    213       O  
HETATM 5725  O   HOH A 793     -41.494  -1.595 -18.080  1.00 25.43           O  
ANISOU 5725  O   HOH A 793     4706   3749   1205    149   -751      0       O  
HETATM 5726  O   HOH A 794     -60.146 -12.524   8.821  1.00 28.83           O  
ANISOU 5726  O   HOH A 794     4382   4655   1915   -452    -38    898       O  
HETATM 5727  O   HOH A 795     -62.127 -15.336  -2.324  1.00 27.53           O  
ANISOU 5727  O   HOH A 795     3588   3782   3090   -325   -290    754       O  
HETATM 5728  O   HOH A 796     -38.204 -32.694  -8.845  1.00 42.85           O  
ANISOU 5728  O   HOH A 796     7490   3509   5280   -234     38      3       O  
HETATM 5729  O   HOH A 797     -51.868 -29.292 -21.310  1.00 41.44           O  
ANISOU 5729  O   HOH A 797     6336   3982   5425   -235    429  -1349       O  
HETATM 5730  O   HOH A 798     -48.011   0.114  14.701  1.00 24.78           O  
ANISOU 5730  O   HOH A 798     4043   3655   1715    150    678    317       O  
HETATM 5731  O   HOH A 799     -39.582 -16.541  15.290  1.00 33.16           O  
ANISOU 5731  O   HOH A 799     5558   5239   1800    442    832   -299       O  
HETATM 5732  O   HOH A 800     -64.954 -19.078 -20.308  1.00 39.07           O  
ANISOU 5732  O   HOH A 800     5295   6593   2954  -2469    473     40       O  
HETATM 5733  O   HOH A 801     -46.238 -29.657 -11.814  1.00 36.17           O  
ANISOU 5733  O   HOH A 801     7049   4010   2684  -1786    260   -298       O  
HETATM 5734  O   HOH A 802     -19.512  -5.339   4.981  1.00 33.59           O  
ANISOU 5734  O   HOH A 802     3947   5314   3501  -1132   -407   -526       O  
HETATM 5735  O   HOH A 803     -36.283 -29.752 -12.094  1.00 34.34           O  
ANISOU 5735  O   HOH A 803     6347   4631   2066    148   -519  -2160       O  
HETATM 5736  O   HOH A 804     -40.031 -32.225   6.591  1.00 42.51           O  
ANISOU 5736  O   HOH A 804     7083   4210   4857    486     54   1110       O  
HETATM 5737  O   HOH A 805     -44.498   4.220  14.928  1.00 23.97           O  
ANISOU 5737  O   HOH A 805     3915   3872   1318    493    450   -441       O  
HETATM 5738  O   HOH A 806     -18.689  -1.827  -7.931  1.00 43.59           O  
ANISOU 5738  O   HOH A 806     4769   4557   7232    -15   1288   -255       O  
HETATM 5739  O   HOH A 807     -34.621 -11.775 -23.174  1.00 27.24           O  
ANISOU 5739  O   HOH A 807     4422   2895   3030   -189   1095   -273       O  
HETATM 5740  O   HOH A 808     -21.493  -6.084 -13.207  1.00 41.96           O  
ANISOU 5740  O   HOH A 808     5837   6182   3922    266   1507   -444       O  
HETATM 5741  O   HOH A 809     -46.239  -9.572 -32.682  1.00 30.54           O  
ANISOU 5741  O   HOH A 809     5428   3105   3071   -716   1690   1175       O  
HETATM 5742  O   HOH A 810     -22.890  -4.262 -13.414  1.00 41.35           O  
ANISOU 5742  O   HOH A 810     5532   7039   3139    -65    785   -698       O  
HETATM 5743  O   HOH A 811     -47.515  -6.514 -18.761  1.00 27.15           O  
ANISOU 5743  O   HOH A 811     3707   4416   2193    134    384    113       O  
HETATM 5744  O   HOH A 812     -45.265  -8.713  14.261  1.00 26.37           O  
ANISOU 5744  O   HOH A 812     3228   4992   1796    959   -993  -1010       O  
HETATM 5745  O   HOH A 813     -46.645 -13.011  17.862  1.00 37.12           O  
ANISOU 5745  O   HOH A 813     6233   6228   1640    353   -268   -726       O  
HETATM 5746  O   HOH A 814     -63.604  -0.901   1.504  1.00 48.94           O  
ANISOU 5746  O   HOH A 814     7119   6808   4665   2773   -421   2204       O  
HETATM 5747  O   HOH A 815     -29.678 -19.964   6.233  1.00 30.29           O  
ANISOU 5747  O   HOH A 815     6075   3695   1735    577   -265    372       O  
HETATM 5748  O   HOH A 816     -44.578   1.438  15.552  1.00 26.52           O  
ANISOU 5748  O   HOH A 816     5141   3255   1678     71    971   -502       O  
HETATM 5749  O   HOH A 817     -47.256  -5.754 -21.355  1.00 36.19           O  
ANISOU 5749  O   HOH A 817     5291   5900   2558   -340    128    513       O  
HETATM 5750  O   HOH A 818     -45.072  -2.111  16.094  1.00 31.12           O  
ANISOU 5750  O   HOH A 818     5080   4761   1981    477    590   -574       O  
HETATM 5751  O   HOH A 819     -47.726  -0.326  17.952  1.00 33.88           O  
ANISOU 5751  O   HOH A 819     5210   4118   3544    934    -33    336       O  
HETATM 5752  O   HOH A 820     -44.196 -15.173 -40.485  1.00 40.74           O  
ANISOU 5752  O   HOH A 820     7848   4221   3410   -169  -1054   -535       O  
HETATM 5753  O   HOH A 821     -66.052   1.694  14.918  1.00 44.37           O  
ANISOU 5753  O   HOH A 821     6141   8122   2594  -1650    715   -429       O  
HETATM 5754  O   HOH A 822     -48.386 -30.139 -28.186  1.00 59.96           O  
ANISOU 5754  O   HOH A 822    11915   2841   8024   -387  -1524   -585       O  
HETATM 5755  O   HOH A 823     -66.483 -13.357   3.999  1.00 32.94           O  
ANISOU 5755  O   HOH A 823     6395   3409   2709    675    313   -946       O  
HETATM 5756  O   HOH A 824     -44.381 -17.112 -38.558  1.00 39.51           O  
ANISOU 5756  O   HOH A 824     7830   5034   2149  -1125   -935    381       O  
HETATM 5757  O   HOH A 825     -28.090 -14.542   6.495  1.00 33.40           O  
ANISOU 5757  O   HOH A 825     5342   4861   2487    447   -660    182       O  
HETATM 5758  O   HOH A 826     -63.023 -29.454  -4.328  1.00 49.41           O  
ANISOU 5758  O   HOH A 826     6270   6754   5747  -1790    758   -119       O  
HETATM 5759  O   HOH A 827     -66.401 -19.156   6.428  1.00 37.82           O  
ANISOU 5759  O   HOH A 827     5514   4591   4262    634   1472    601       O  
HETATM 5760  O   HOH A 828     -37.214  -2.558  16.543  1.00 38.32           O  
ANISOU 5760  O   HOH A 828     5516   7061   1981  -1084    239  -1787       O  
HETATM 5761  O   HOH A 829     -29.343  -1.059 -11.589  1.00 25.30           O  
ANISOU 5761  O   HOH A 829     4477   3992   1141   -172   -442    233       O  
HETATM 5762  O   HOH A 830     -39.792 -29.875 -22.629  1.00 45.60           O  
ANISOU 5762  O   HOH A 830     7453   5653   4220  -1288   -685  -1900       O  
HETATM 5763  O   HOH A 831     -49.184 -26.615 -32.514  1.00 43.23           O  
ANISOU 5763  O   HOH A 831     8463   5362   2600    168   1392   -583       O  
HETATM 5764  O   HOH A 832     -26.663 -20.162 -17.407  1.00 40.17           O  
ANISOU 5764  O   HOH A 832     5714   6198   3348    -69    228    -54       O  
HETATM 5765  O   HOH A 833     -39.117 -27.869  12.431  1.00 38.12           O  
ANISOU 5765  O   HOH A 833     7793   4234   2457   -215  -1452    812       O  
HETATM 5766  O   HOH A 834     -40.090 -32.625 -12.874  1.00 45.19           O  
ANISOU 5766  O   HOH A 834     9289   3480   4400  -1715    418    774       O  
HETATM 5767  O   HOH A 835     -35.434 -30.255 -22.662  1.00 47.97           O  
ANISOU 5767  O   HOH A 835     7349   5839   5037    772   -402   -300       O  
HETATM 5768  O   HOH A 836     -61.504 -23.143 -39.081  1.00 52.83           O  
ANISOU 5768  O   HOH A 836     8829   6438   4803   -419     80   -753       O  
HETATM 5769  O   HOH A 837     -21.064  -1.451   5.243  1.00 34.30           O  
ANISOU 5769  O   HOH A 837     4735   4003   4293     75    521  -1543       O  
HETATM 5770  O   HOH A 838     -45.308  -6.038  14.768  1.00 33.55           O  
ANISOU 5770  O   HOH A 838     5290   4503   2952    446    101   -463       O  
HETATM 5771  O   HOH A 839     -31.447 -13.171 -16.681  1.00 31.28           O  
ANISOU 5771  O   HOH A 839     5057   4410   2414    -98    649    343       O  
HETATM 5772  O   HOH A 840     -43.517  -0.038  17.739  1.00 41.84           O  
ANISOU 5772  O   HOH A 840     6316   5345   4237    334    701  -1147       O  
HETATM 5773  O   HOH A 841     -34.760  -1.745 -16.107  1.00 45.43           O  
ANISOU 5773  O   HOH A 841     7730   6379   3150  -1651  -1438    197       O  
HETATM 5774  O   HOH A 842     -65.083 -14.124   1.727  1.00 36.13           O  
ANISOU 5774  O   HOH A 842     4945   5717   3065    396   -498     30       O  
HETATM 5775  O   HOH A 843     -47.185  -7.135 -24.033  1.00 37.36           O  
ANISOU 5775  O   HOH A 843     5629   5061   3504   -303    527    304       O  
HETATM 5776  O   HOH A 844     -39.411 -35.160   3.760  1.00 40.51           O  
ANISOU 5776  O   HOH A 844     7186   3621   4583    490    462   1081       O  
HETATM 5777  O   HOH A 845     -55.266 -21.088   4.729  1.00 27.77           O  
ANISOU 5777  O   HOH A 845     4680   3575   2295    143     99    330       O  
HETATM 5778  O   HOH A 846     -43.261  -7.389 -15.595  1.00 18.77           O  
ANISOU 5778  O   HOH A 846     4302   2121    706    303    358     -3       O  
HETATM 5779  O   HOH A 847     -32.267 -15.824 -21.913  1.00 36.26           O  
ANISOU 5779  O   HOH A 847     4223   4652   4902    279    151   -477       O  
HETATM 5780  O   HOH A 848     -41.131 -29.392  11.100  1.00 45.02           O  
ANISOU 5780  O   HOH A 848     8597   6448   2059  -1041    246   1366       O  
HETATM 5781  O   HOH A 849     -49.222 -10.621  16.437  1.00 36.41           O  
ANISOU 5781  O   HOH A 849     4730   6386   2718    966    388   -900       O  
HETATM 5782  O   HOH A 850     -45.755  -0.750 -24.006  1.00 33.86           O  
ANISOU 5782  O   HOH A 850     5782   3207   3875    853    -90   -246       O  
HETATM 5783  O   HOH A 851     -50.737  -8.292 -25.758  1.00 42.08           O  
ANISOU 5783  O   HOH A 851     5155   5651   5180   -441   -812   -214       O  
HETATM 5784  O   HOH A 852     -32.632  -8.957 -16.899  1.00 40.31           O  
ANISOU 5784  O   HOH A 852     5784   6334   3199   -358   1371    148       O  
HETATM 5785  O   HOH A 853     -52.425  -1.775  22.130  1.00 39.80           O  
ANISOU 5785  O   HOH A 853     7163   6480   1478    319    834    331       O  
HETATM 5786  O   HOH A 854     -38.216 -17.981 -37.108  1.00 45.56           O  
ANISOU 5786  O   HOH A 854     5627   6673   5008   -563     51   -784       O  
HETATM 5787  O   HOH A 855     -23.157 -22.495 -12.722  1.00 41.20           O  
ANISOU 5787  O   HOH A 855     6121   6505   3027   -674    937   -564       O  
HETATM 5788  O   HOH A 856     -27.630  -0.472 -13.250  1.00 39.26           O  
ANISOU 5788  O   HOH A 856     5747   5853   3315   -149   -376    810       O  
HETATM 5789  O   HOH A 857     -57.070  -7.160 -25.742  1.00 29.83           O  
ANISOU 5789  O   HOH A 857     5771   3907   1653    790   -409  -1158       O  
HETATM 5790  O   HOH A 858     -24.023 -17.036   4.786  1.00 45.81           O  
ANISOU 5790  O   HOH A 858     7268   6018   4117    107   -580  -1418       O  
HETATM 5791  O   HOH A 859     -63.057 -14.469 -10.034  1.00 35.28           O  
ANISOU 5791  O   HOH A 859     4292   5435   3675   -557   -167    417       O  
HETATM 5792  O   HOH A 860     -29.779  -4.253 -14.430  1.00 35.29           O  
ANISOU 5792  O   HOH A 860     6936   4589   1881   1256    497    721       O  
HETATM 5793  O   HOH A 861     -18.916 -21.697  -9.942  1.00 44.67           O  
ANISOU 5793  O   HOH A 861     5314   6132   5525    857   -427  -2522       O  
HETATM 5794  O   HOH A 862     -45.138 -17.167  18.694  1.00 45.18           O  
ANISOU 5794  O   HOH A 862     7412   6778   2976   -686    680   1088       O  
HETATM 5795  O   HOH A 863     -25.691 -26.112   8.447  1.00 23.32           O  
ANISOU 5795  O   HOH A 863     4188   2889   1780    525   -665   1000       O  
HETATM 5796  O   HOH A 864     -37.360   0.233  15.953  1.00 44.16           O  
ANISOU 5796  O   HOH A 864     6037   7835   2907   -457  -1086    319       O  
HETATM 5797  O   HOH A 865     -39.535 -23.486  14.261  1.00 31.52           O  
ANISOU 5797  O   HOH A 865     4839   4088   3047    435   -159    206       O  
HETATM 5798  O   HOH A 866     -15.204 -14.655  -6.629  1.00 43.73           O  
ANISOU 5798  O   HOH A 866     4579   6944   5091   1524   -147   -722       O  
HETATM 5799  O   HOH A 867     -62.879   7.255  16.294  1.00 26.64           O  
ANISOU 5799  O   HOH A 867     3102   4105   2913    128    104   -175       O  
HETATM 5800  O   HOH A 868     -51.996 -11.211 -34.329  1.00 41.12           O  
ANISOU 5800  O   HOH A 868     5322   5490   4809   -181    531   1115       O  
HETATM 5801  O   HOH A 869     -61.854  -6.461  13.415  1.00 37.02           O  
ANISOU 5801  O   HOH A 869     5681   4642   3741   -298    804   -526       O  
HETATM 5802  O   HOH A 870     -55.897 -30.260 -13.653  1.00 46.47           O  
ANISOU 5802  O   HOH A 870     7178   4765   5710   -893   1975   -748       O  
HETATM 5803  O   HOH A 871     -48.675 -29.160  -3.779  1.00 43.14           O  
ANISOU 5803  O   HOH A 871     6699   4515   5177    914  -2685   -159       O  
HETATM 5804  O   HOH A 872     -26.586 -20.399  12.024  1.00 40.09           O  
ANISOU 5804  O   HOH A 872     5887   4902   4441   -104   -563   -262       O  
HETATM 5805  O   HOH A 873     -50.243  -6.006  18.465  1.00 40.42           O  
ANISOU 5805  O   HOH A 873     5990   6664   2704    838    351    125       O  
HETATM 5806  O   HOH A 874     -25.184 -20.341 -15.556  1.00 42.92           O  
ANISOU 5806  O   HOH A 874     6271   6194   3839  -1072   -704    -59       O  
HETATM 5807  O   HOH A 875     -21.102 -17.843   4.169  1.00 41.42           O  
ANISOU 5807  O   HOH A 875     5504   6690   3543   -756   -720   -849       O  
HETATM 5808  O   HOH A 876     -39.141  -0.787 -19.349  1.00 33.93           O  
ANISOU 5808  O   HOH A 876     5431   3838   3623   -617    103    173       O  
HETATM 5809  O   HOH A 877     -42.813 -30.216  -8.004  1.00 35.06           O  
ANISOU 5809  O   HOH A 877     6357   3661   3304    -15    305    272       O  
HETATM 5810  O   HOH A 878     -35.139 -30.119 -14.300  1.00 38.94           O  
ANISOU 5810  O   HOH A 878     5930   4479   4384   1088  -1059   -916       O  
HETATM 5811  O   HOH A 879     -29.378 -14.481 -18.170  1.00 39.81           O  
ANISOU 5811  O   HOH A 879     7045   5398   2682    692    491    152       O  
HETATM 5812  O   HOH A 880     -62.710  -3.507  16.386  1.00 39.63           O  
ANISOU 5812  O   HOH A 880     5326   5301   4430   -253   1256   -383       O  
HETATM 5813  O   HOH A 881     -53.995 -23.796   4.770  1.00 36.11           O  
ANISOU 5813  O   HOH A 881     5589   4503   3627  -1373   -209   -758       O  
HETATM 5814  O   HOH A 882     -54.535 -10.371 -26.937  1.00 30.22           O  
ANISOU 5814  O   HOH A 882     5040   3988   2454   -633   1076     46       O  
HETATM 5815  O   HOH A 883     -46.490  -0.031  15.587  1.00 38.60           O  
ANISOU 5815  O   HOH A 883     5777   4973   3915   -195    192   -325       O  
HETATM 5816  O   HOH A 884     -30.565 -10.768 -16.279  1.00 37.59           O  
ANISOU 5816  O   HOH A 884     6160   5524   2599   -470   1410    500       O  
HETATM 5817  O   HOH A 885     -64.209 -16.541 -10.687  1.00 30.98           O  
ANISOU 5817  O   HOH A 885     3422   4986   3360   -863    242   -296       O  
HETATM 5818  O   HOH A 886     -35.434  -1.573  15.334  1.00 37.08           O  
ANISOU 5818  O   HOH A 886     4774   6739   2576   -972   -967    506       O  
HETATM 5819  O   HOH A 887     -20.625 -17.103   6.021  1.00 47.92           O  
ANISOU 5819  O   HOH A 887     6574   8017   3615   -391   -853    384       O  
HETATM 5820  O   HOH A 888     -45.527   0.263 -19.746  1.00 38.06           O  
ANISOU 5820  O   HOH A 888     7584   3609   3268    627  -1806   -626       O  
HETATM 5821  O   HOH A 889     -64.455 -13.150  -8.063  1.00 37.52           O  
ANISOU 5821  O   HOH A 889     4751   5784   3719   -626    352    696       O  
HETATM 5822  O   HOH A 890     -49.774 -10.935  19.824  1.00 37.95           O  
ANISOU 5822  O   HOH A 890     5569   8576    272    663      9    399       O  
HETATM 5823  O   HOH A 891     -64.168 -16.955  -6.176  1.00 35.23           O  
ANISOU 5823  O   HOH A 891     4325   5842   3219     42    248   -480       O  
HETATM 5824  O   HOH A 892     -38.684 -30.728 -11.026  1.00 31.25           O  
ANISOU 5824  O   HOH A 892     7002   3234   1636   -444   -103     80       O  
HETATM 5825  O   HOH A 893     -34.852 -10.576 -27.285  1.00 34.38           O  
ANISOU 5825  O   HOH A 893     5968   4221   2872   -213     28    740       O  
HETATM 5826  O   HOH A 894     -26.394 -14.114 -17.235  1.00 37.90           O  
ANISOU 5826  O   HOH A 894     6277   5866   2256    427    501    550       O  
HETATM 5827  O   HOH A 895     -32.413  -1.936  12.252  1.00 34.00           O  
ANISOU 5827  O   HOH A 895     3966   6812   2139   -523   -346    959       O  
HETATM 5828  O   HOH A 896     -65.465 -21.284   0.082  1.00 49.06           O  
ANISOU 5828  O   HOH A 896     6868   4482   7288   -382    538    130       O  
HETATM 5829  O   HOH A 897     -36.297 -31.959 -16.166  1.00 42.75           O  
ANISOU 5829  O   HOH A 897     7282   5293   3668    749    -29    607       O  
HETATM 5830  O   HOH A 898     -48.009  -8.080 -35.428  1.00 29.75           O  
ANISOU 5830  O   HOH A 898     4991   4043   2266   -566    -34    571       O  
HETATM 5831  O   HOH A 899     -23.756 -19.014 -15.394  1.00 46.23           O  
ANISOU 5831  O   HOH A 899     5549   7971   4045   -252    762    141       O  
HETATM 5832  O   HOH A 900     -69.472 -11.901  -5.250  1.00 46.08           O  
ANISOU 5832  O   HOH A 900     5481   7646   4381  -1293   -204   -351       O  
HETATM 5833  O   HOH A 901     -63.027 -14.815  -4.737  1.00 30.86           O  
ANISOU 5833  O   HOH A 901     4007   5118   2599   -905    513    726       O  
HETATM 5834  O   HOH A 902     -33.410 -14.001   6.459  1.00 24.25           O  
ANISOU 5834  O   HOH A 902     3515   3954   1743     44    -64    166       O  
HETATM 5835  O   HOH A 903     -52.364 -29.137 -24.198  1.00 44.63           O  
ANISOU 5835  O   HOH A 903     6997   4520   5437  -1181   -818    426       O  
HETATM 5836  O   HOH A 904     -39.869 -29.340 -25.085  1.00 55.10           O  
ANISOU 5836  O   HOH A 904     9065   5871   5996    338   -288  -2976       O  
HETATM 5837  O   HOH A 905     -65.797 -10.767  -8.689  1.00 37.35           O  
ANISOU 5837  O   HOH A 905     5105   6758   2329   -779     28   -687       O  
HETATM 5838  O   HOH A 906     -64.669  10.498  13.574  1.00 46.40           O  
ANISOU 5838  O   HOH A 906     3682   7111   6836   1316    335   -959       O  
HETATM 5839  O   HOH A 907     -43.193  -5.044  18.390  1.00 38.08           O  
ANISOU 5839  O   HOH A 907     6314   5306   2849    430     24   -374       O  
HETATM 5840  O   HOH A 908     -49.697  -1.347  21.306  1.00 33.19           O  
ANISOU 5840  O   HOH A 908     5493   4083   3032    136   -467    168       O  
HETATM 5841  O   HOH A 909     -29.013   2.611  -9.528  1.00 34.34           O  
ANISOU 5841  O   HOH A 909     6629   5143   1272   -380    379  -1020       O  
HETATM 5842  O   HOH A 910     -63.788  -5.832  14.264  1.00 36.78           O  
ANISOU 5842  O   HOH A 910     5651   4362   3962    -41    914    -30       O  
HETATM 5843  O   HOH A 911     -67.706  -4.203 -28.703  1.00 50.82           O  
ANISOU 5843  O   HOH A 911     7081   6634   5595    723   -456   -618       O  
HETATM 5844  O   HOH A 912     -31.327 -15.369   6.069  1.00 31.25           O  
ANISOU 5844  O   HOH A 912     5543   4313   2015    842    489   -457       O  
HETATM 5845  O   HOH A 913     -48.129  -3.000  19.305  1.00 41.16           O  
ANISOU 5845  O   HOH A 913     5590   4808   5238    401   -674    832       O  
HETATM 5846  O   HOH A 914     -70.843 -19.678 -29.293  1.00 53.18           O  
ANISOU 5846  O   HOH A 914     6464   7583   6156    -36    427   -978       O  
HETATM 5847  O   HOH A 915     -47.871  -4.691 -25.977  1.00 33.91           O  
ANISOU 5847  O   HOH A 915     5333   5326   2225   -923   -262    445       O  
HETATM 5848  O   HOH A 916     -30.857   0.759 -10.455  1.00 19.63           O  
ANISOU 5848  O   HOH A 916     3337   3425    695    -89    624   -182       O  
HETATM 5849  O   HOH A 917     -37.294 -29.072 -26.236  1.00 45.56           O  
ANISOU 5849  O   HOH A 917     6709   5563   5037   1541    125  -1087       O  
HETATM 5850  O   HOH A 918     -50.484  -5.281 -26.929  1.00 40.29           O  
ANISOU 5850  O   HOH A 918     6338   7343   1624  -1307  -1289    882       O  
HETATM 5851  O   HOH A 919     -34.738  -0.779 -18.408  1.00 42.56           O  
ANISOU 5851  O   HOH A 919     6967   5237   3963    446  -2122   -407       O  
HETATM 5852  O   HOH A 920     -48.150 -28.933  -8.535  1.00 49.88           O  
ANISOU 5852  O   HOH A 920     8021   5475   5453  -2640   1016   -505       O  
HETATM 5853  O   HOH A 921     -27.305   0.027  -0.112  0.50 44.86           O  
ANISOU 5853  O   HOH A 921     5476   5747   5819     33   -359   -272       O  
HETATM 5854  O   HOH A 922     -46.260  -6.242 -36.943  1.00 37.38           O  
ANISOU 5854  O   HOH A 922     7263   4401   2537    771   -859   -219       O  
HETATM 5855  O   HOH A 923     -45.007 -31.447  -5.153  1.00 40.90           O  
ANISOU 5855  O   HOH A 923     6316   4861   4360   -550   -515    -67       O  
HETATM 5856  O   HOH A 924     -62.795   3.070  25.828  1.00 49.07           O  
ANISOU 5856  O   HOH A 924     7577   6890   4177   -243    612  -1725       O  
HETATM 5857  O   HOH A 925     -45.808   2.851 -20.858  1.00 41.63           O  
ANISOU 5857  O   HOH A 925     6634   4531   4650   -651   -529   1008       O  
HETATM 5858  O   HOH A 926     -70.403  -4.976 -23.524  1.00 52.85           O  
ANISOU 5858  O   HOH A 926     5786   7570   6724    798    384    425       O  
HETATM 5859  O   HOH A 927     -47.958   1.690 -23.326  1.00 43.63           O  
ANISOU 5859  O   HOH A 927     7272   5177   4126    -91   2081   1230       O  
HETATM 5860  O   HOH A 928     -64.486 -35.033 -17.923  1.00 55.05           O  
ANISOU 5860  O   HOH A 928     6528   6928   7459    166    719    716       O  
HETATM 5861  O   HOH B 501     -32.909 -35.369  13.480  1.00 30.13           O  
ANISOU 5861  O   HOH B 501     4059   4607   2782    355    151   -336       O  
HETATM 5862  O   HOH B 502     -36.630 -47.302  46.097  1.00 37.37           O  
ANISOU 5862  O   HOH B 502     5693   4714   3792    -24     80   -510       O  
HETATM 5863  O   HOH B 503     -35.572 -43.271  -0.575  1.00 34.95           O  
ANISOU 5863  O   HOH B 503     6275   4671   2331   -425    -39   -361       O  
HETATM 5864  O   HOH B 504     -39.147 -51.271  23.534  1.00 32.25           O  
ANISOU 5864  O   HOH B 504     6003   4638   1611    696    794   -671       O  
HETATM 5865  O   HOH B 505      -8.526 -35.978  24.151  1.00 37.57           O  
ANISOU 5865  O   HOH B 505     5543   6399   2330   1415    191    -43       O  
HETATM 5866  O   HOH B 506     -35.159 -41.540  51.431  1.00 34.04           O  
ANISOU 5866  O   HOH B 506     5079   4780   3073    943    402    657       O  
HETATM 5867  O   HOH B 507     -46.640 -43.419  45.263  1.00 34.11           O  
ANISOU 5867  O   HOH B 507     6141   4132   2687    456   1863    135       O  
HETATM 5868  O   HOH B 508     -37.727 -28.317  24.248  1.00 21.49           O  
ANISOU 5868  O   HOH B 508     4307   3511    344   -687    -73   -388       O  
HETATM 5869  O   HOH B 509      -8.139 -41.324  34.106  1.00 40.95           O  
ANISOU 5869  O   HOH B 509     5796   6034   3729    577     -3   -184       O  
HETATM 5870  O   HOH B 510     -36.724 -51.118  20.815  1.00 32.22           O  
ANISOU 5870  O   HOH B 510     6478   3665   2098    458    867   -275       O  
HETATM 5871  O   HOH B 511     -56.975 -28.654  59.224  1.00 38.97           O  
ANISOU 5871  O   HOH B 511     5848   5157   3802   -699    120   -137       O  
HETATM 5872  O   HOH B 512     -25.489 -43.832  46.950  1.00 31.86           O  
ANISOU 5872  O   HOH B 512     5046   4671   2388    362     44   -100       O  
HETATM 5873  O   HOH B 513     -40.048 -49.921  24.268  1.00 26.36           O  
ANISOU 5873  O   HOH B 513     3934   3524   2557    -90   -283   -179       O  
HETATM 5874  O   HOH B 514     -38.358 -56.819  11.929  1.00 30.79           O  
ANISOU 5874  O   HOH B 514     5093   5341   1264   -392    232   -697       O  
HETATM 5875  O   HOH B 515     -41.433 -31.700  53.984  1.00 21.44           O  
ANISOU 5875  O   HOH B 515     3735   2821   1589    132    454   -281       O  
HETATM 5876  O   HOH B 516     -34.738 -47.094   0.200  1.00 35.61           O  
ANISOU 5876  O   HOH B 516     6031   4674   2822   -367     27     23       O  
HETATM 5877  O   HOH B 517     -29.191 -47.254  45.615  1.00 28.77           O  
ANISOU 5877  O   HOH B 517     4705   3278   2946   -284    535    575       O  
HETATM 5878  O   HOH B 518      -7.020 -39.369  36.813  1.00 43.31           O  
ANISOU 5878  O   HOH B 518     5696   6203   4556   1030    821   -356       O  
HETATM 5879  O   HOH B 519     -27.828 -32.563  52.980  1.00 25.61           O  
ANISOU 5879  O   HOH B 519     4335   4206   1188    110   -151    253       O  
HETATM 5880  O   HOH B 520     -36.224 -43.297  25.627  1.00 20.73           O  
ANISOU 5880  O   HOH B 520     3770   3104   1002    108    129   -239       O  
HETATM 5881  O   HOH B 521     -44.227 -55.136   9.342  1.00 30.20           O  
ANISOU 5881  O   HOH B 521     4132   5033   2307   -749   -643   -322       O  
HETATM 5882  O   HOH B 522     -25.336 -21.958  49.555  1.00 27.84           O  
ANISOU 5882  O   HOH B 522     4346   5025   1207   -421    326   -545       O  
HETATM 5883  O   HOH B 523     -38.834 -45.180  48.924  1.00 37.33           O  
ANISOU 5883  O   HOH B 523     5404   4925   3853    485    875    613       O  
HETATM 5884  O   HOH B 524     -32.716 -23.655  41.099  1.00 17.21           O  
ANISOU 5884  O   HOH B 524     2776   3065    698    -15    370   -560       O  
HETATM 5885  O   HOH B 525     -30.896 -36.645   2.087  1.00 34.90           O  
ANISOU 5885  O   HOH B 525     4987   5232   3042   -489    323    -92       O  
HETATM 5886  O   HOH B 526     -29.950 -35.811  55.452  1.00 30.25           O  
ANISOU 5886  O   HOH B 526     6542   3685   1265   1636    -95    121       O  
HETATM 5887  O   HOH B 527     -37.377 -47.184  38.009  1.00 27.37           O  
ANISOU 5887  O   HOH B 527     4992   3405   2003    335    608     78       O  
HETATM 5888  O   HOH B 528     -30.593 -30.488  17.921  1.00 17.24           O  
ANISOU 5888  O   HOH B 528     3116   2682    752    314    592     38       O  
HETATM 5889  O   HOH B 529     -25.277 -33.375  54.654  1.00 36.40           O  
ANISOU 5889  O   HOH B 529     5875   5270   2685    114    388   -138       O  
HETATM 5890  O   HOH B 530     -52.152 -37.314  16.071  1.00 41.72           O  
ANISOU 5890  O   HOH B 530     5797   5362   4689   -677   -327    726       O  
HETATM 5891  O   HOH B 531     -58.806 -30.563  45.889  1.00 28.09           O  
ANISOU 5891  O   HOH B 531     3668   3901   3101    -59   -343   -589       O  
HETATM 5892  O   HOH B 532     -47.238 -36.797  11.249  1.00 38.11           O  
ANISOU 5892  O   HOH B 532     6175   5338   2964    193     60   -540       O  
HETATM 5893  O   HOH B 533     -41.038 -26.750  51.551  1.00 23.95           O  
ANISOU 5893  O   HOH B 533     3378   4143   1578    411    297    -29       O  
HETATM 5894  O   HOH B 534      -8.721 -28.296  28.296  1.00 29.51           O  
ANISOU 5894  O   HOH B 534     4562   4239   2409    946    803   -248       O  
HETATM 5895  O   HOH B 535     -11.753 -36.614  45.347  1.00 21.77           O  
ANISOU 5895  O   HOH B 535     3760   3707    802    507    317    352       O  
HETATM 5896  O   HOH B 536     -38.145 -23.989  16.503  1.00 28.69           O  
ANISOU 5896  O   HOH B 536     4606   4279   2013    627    109    151       O  
HETATM 5897  O   HOH B 537     -28.916 -33.097  23.228  1.00 23.66           O  
ANISOU 5897  O   HOH B 537     3890   3790   1307    179   -340   -502       O  
HETATM 5898  O   HOH B 538     -33.375 -28.773  12.245  1.00 27.07           O  
ANISOU 5898  O   HOH B 538     4618   4037   1631   -601   -262   -983       O  
HETATM 5899  O   HOH B 539     -23.773 -26.577   6.614  1.00 32.78           O  
ANISOU 5899  O   HOH B 539     4796   3910   3749     39    459    385       O  
HETATM 5900  O   HOH B 540     -39.856 -26.432  47.380  1.00 23.19           O  
ANISOU 5900  O   HOH B 540     3458   3890   1461    782    509   -522       O  
HETATM 5901  O   HOH B 541     -44.364 -43.010  36.206  1.00 17.96           O  
ANISOU 5901  O   HOH B 541     3293   2716    814     75    405   -301       O  
HETATM 5902  O   HOH B 542     -48.139 -26.948  62.602  1.00 39.93           O  
ANISOU 5902  O   HOH B 542     7024   6450   1697    207   -823   -252       O  
HETATM 5903  O   HOH B 543     -14.164 -21.131  26.218  1.00 23.82           O  
ANISOU 5903  O   HOH B 543     4063   3799   1188   -282    812   -243       O  
HETATM 5904  O   HOH B 544     -36.302 -45.605  -1.779  1.00 44.42           O  
ANISOU 5904  O   HOH B 544     6671   5945   4260   -993   -643   -641       O  
HETATM 5905  O   HOH B 545     -22.813 -28.371  19.781  1.00 22.55           O  
ANISOU 5905  O   HOH B 545     3424   3393   1747    277    -97    799       O  
HETATM 5906  O   HOH B 546     -33.777 -47.538  40.278  1.00 28.74           O  
ANISOU 5906  O   HOH B 546     5057   3259   2603   -759    343    -92       O  
HETATM 5907  O   HOH B 547     -35.702 -33.934  25.576  1.00 35.95           O  
ANISOU 5907  O   HOH B 547     5984   5019   2655    687  -1109     33       O  
HETATM 5908  O   HOH B 548     -40.008 -28.943  33.544  1.00 21.55           O  
ANISOU 5908  O   HOH B 548     3500   4241    447    227   -234   -405       O  
HETATM 5909  O   HOH B 549     -50.234 -43.611  10.714  1.00 33.64           O  
ANISOU 5909  O   HOH B 549     4132   4752   3897    489   -453   -165       O  
HETATM 5910  O   HOH B 550     -22.960 -29.520  16.888  1.00 23.95           O  
ANISOU 5910  O   HOH B 550     4142   3311   1645    272     70    -58       O  
HETATM 5911  O   HOH B 551      -9.264 -22.870  40.151  1.00 35.18           O  
ANISOU 5911  O   HOH B 551     4714   5137   3514    355   -533   -234       O  
HETATM 5912  O   HOH B 552     -50.298 -27.250  50.074  1.00 16.12           O  
ANISOU 5912  O   HOH B 552     2857   2692    575     29    342    302       O  
HETATM 5913  O   HOH B 553     -25.099 -38.523  48.821  1.00 24.65           O  
ANISOU 5913  O   HOH B 553     4595   3558   1211    883    144    175       O  
HETATM 5914  O   HOH B 554     -20.400 -26.355  48.038  1.00 33.84           O  
ANISOU 5914  O   HOH B 554     5056   5341   2458   -447   -251   -349       O  
HETATM 5915  O   HOH B 555     -28.348 -49.864  21.553  1.00 37.49           O  
ANISOU 5915  O   HOH B 555     6268   4145   3831   -525    362   -478       O  
HETATM 5916  O   HOH B 556     -46.564 -41.318  47.216  1.00 24.33           O  
ANISOU 5916  O   HOH B 556     4925   2362   1955   -282    288   -201       O  
HETATM 5917  O   HOH B 557     -34.547 -29.140  14.659  1.00 20.62           O  
ANISOU 5917  O   HOH B 557     4032   3473    328     64   -207   -419       O  
HETATM 5918  O   HOH B 558     -32.978 -41.931  51.501  1.00 33.46           O  
ANISOU 5918  O   HOH B 558     5567   4281   2864    474    339    947       O  
HETATM 5919  O   HOH B 559      -9.455 -42.941  35.823  1.00 33.38           O  
ANISOU 5919  O   HOH B 559     4679   4960   3043    124   -321    172       O  
HETATM 5920  O   HOH B 560     -29.827 -18.982  50.821  1.00 34.02           O  
ANISOU 5920  O   HOH B 560     6285   4833   1808  -1719    301   -806       O  
HETATM 5921  O   HOH B 561     -31.996 -21.830  43.155  1.00 15.20           O  
ANISOU 5921  O   HOH B 561     2688   2500    587    372    325     71       O  
HETATM 5922  O   HOH B 562     -29.561 -44.802   6.178  1.00 30.46           O  
ANISOU 5922  O   HOH B 562     5318   4759   1494    845    844   -237       O  
HETATM 5923  O   HOH B 563     -35.956 -40.426  32.491  1.00 17.84           O  
ANISOU 5923  O   HOH B 563     3483   2581    714    408    -19   -177       O  
HETATM 5924  O   HOH B 564     -16.627 -37.768  40.998  1.00 20.03           O  
ANISOU 5924  O   HOH B 564     3180   3691    737   1032     80    202       O  
HETATM 5925  O   HOH B 565     -41.813 -31.725  34.932  1.00 16.08           O  
ANISOU 5925  O   HOH B 565     3120   2689    299    318    101   -309       O  
HETATM 5926  O   HOH B 566     -38.438 -31.616  15.620  1.00 30.71           O  
ANISOU 5926  O   HOH B 566     5180   3509   2980    423    351    170       O  
HETATM 5927  O   HOH B 567     -43.986 -24.785  57.555  1.00 30.14           O  
ANISOU 5927  O   HOH B 567     5157   4519   1775   1105    151    -43       O  
HETATM 5928  O   HOH B 568     -39.124 -38.377  19.509  1.00 17.33           O  
ANISOU 5928  O   HOH B 568     2957   2886    742   -141    226    387       O  
HETATM 5929  O   HOH B 569     -31.084 -31.824  22.091  1.00 24.03           O  
ANISOU 5929  O   HOH B 569     3830   2851   2449    484    992    -97       O  
HETATM 5930  O   HOH B 570     -24.444 -42.937  12.800  1.00 24.78           O  
ANISOU 5930  O   HOH B 570     3244   4543   1628    931    512   -141       O  
HETATM 5931  O   HOH B 571     -38.704 -46.001  40.127  1.00 26.42           O  
ANISOU 5931  O   HOH B 571     4407   3065   2566    863    705    241       O  
HETATM 5932  O   HOH B 572     -29.864 -44.797  -1.829  1.00 55.90           O  
ANISOU 5932  O   HOH B 572     7923   7937   5377  -2041   4071  -1833       O  
HETATM 5933  O   HOH B 573     -27.673 -32.419  28.667  1.00 17.92           O  
ANISOU 5933  O   HOH B 573     3296   2724    785    218    623    541       O  
HETATM 5934  O   HOH B 574     -25.736 -18.519  25.786  1.00 24.19           O  
ANISOU 5934  O   HOH B 574     4015   3216   1959    234   -277    255       O  
HETATM 5935  O   HOH B 575     -23.964 -43.706  15.500  1.00 25.20           O  
ANISOU 5935  O   HOH B 575     4362   4024   1188    565    731    -17       O  
HETATM 5936  O   HOH B 576      -9.213 -41.917  31.785  1.00 36.13           O  
ANISOU 5936  O   HOH B 576     5822   5181   2724    944    -95   -261       O  
HETATM 5937  O   HOH B 577     -38.154 -41.633  31.392  1.00 22.49           O  
ANISOU 5937  O   HOH B 577     4125   3285   1136    132    208    -60       O  
HETATM 5938  O   HOH B 578     -40.189 -49.363  37.635  1.00 26.72           O  
ANISOU 5938  O   HOH B 578     4783   3920   1450    304    386    302       O  
HETATM 5939  O   HOH B 579     -36.943 -37.261  55.473  1.00 31.97           O  
ANISOU 5939  O   HOH B 579     4967   4565   2615    -90   1037    500       O  
HETATM 5940  O   HOH B 580     -12.247 -43.596  34.633  1.00 24.50           O  
ANISOU 5940  O   HOH B 580     3795   3549   1965    860    -10    186       O  
HETATM 5941  O   HOH B 581     -35.764 -52.756   6.438  1.00 21.92           O  
ANISOU 5941  O   HOH B 581     3601   3166   1562   -742   -144    -66       O  
HETATM 5942  O   HOH B 582     -48.216 -29.354  35.098  1.00 18.93           O  
ANISOU 5942  O   HOH B 582     2895   3165   1132    450   -257     11       O  
HETATM 5943  O   HOH B 583     -24.339 -36.880   2.389  1.00 34.91           O  
ANISOU 5943  O   HOH B 583     4704   6194   2365   1079    -78  -1075       O  
HETATM 5944  O   HOH B 584     -51.950 -27.915  52.572  1.00 17.31           O  
ANISOU 5944  O   HOH B 584     3386   2626    565    -71     -9    107       O  
HETATM 5945  O   HOH B 585     -24.825 -22.220  23.095  1.00 36.00           O  
ANISOU 5945  O   HOH B 585     5000   6114   2562    137    701   1128       O  
HETATM 5946  O   HOH B 586     -52.876 -41.405  13.113  1.00 39.15           O  
ANISOU 5946  O   HOH B 586     4785   6147   3944   -244  -1078    793       O  
HETATM 5947  O   HOH B 587     -32.500 -32.384   9.906  1.00 30.55           O  
ANISOU 5947  O   HOH B 587     4964   4379   2263    351    384     79       O  
HETATM 5948  O   HOH B 588     -15.489 -44.217  23.979  1.00 41.01           O  
ANISOU 5948  O   HOH B 588     4591   6017   4972    929   1057   -620       O  
HETATM 5949  O   HOH B 589     -11.185 -41.690  24.111  1.00 35.91           O  
ANISOU 5949  O   HOH B 589     5032   6162   2448   1946    919   -716       O  
HETATM 5950  O   HOH B 590     -17.323 -22.473  42.904  1.00 33.15           O  
ANISOU 5950  O   HOH B 590     4691   4836   3068   -365   -701   1469       O  
HETATM 5951  O   HOH B 591     -13.109 -45.855  35.447  1.00 28.50           O  
ANISOU 5951  O   HOH B 591     4577   3894   2357    970   -270    119       O  
HETATM 5952  O   HOH B 592     -15.982 -35.312  42.315  1.00 21.97           O  
ANISOU 5952  O   HOH B 592     3517   3339   1491    388   -290    118       O  
HETATM 5953  O   HOH B 593     -33.279 -30.323  50.228  1.00 20.34           O  
ANISOU 5953  O   HOH B 593     2956   3793    976    593   -141   -663       O  
HETATM 5954  O   HOH B 594     -20.021 -20.887  22.906  1.00 38.92           O  
ANISOU 5954  O   HOH B 594     6471   5816   2499   -155     -8    213       O  
HETATM 5955  O   HOH B 595     -38.823 -23.810  46.393  1.00 16.68           O  
ANISOU 5955  O   HOH B 595     3068   2707    559    403    321    153       O  
HETATM 5956  O   HOH B 596     -14.667 -34.794  44.813  1.00 24.34           O  
ANISOU 5956  O   HOH B 596     3628   4514   1104    -91   -598    393       O  
HETATM 5957  O   HOH B 597     -32.769 -51.018  21.104  1.00 40.97           O  
ANISOU 5957  O   HOH B 597     7200   4530   3838    940   1278    259       O  
HETATM 5958  O   HOH B 598     -26.877 -42.998   9.947  1.00 30.38           O  
ANISOU 5958  O   HOH B 598     3968   5500   2074   1381   -111   -599       O  
HETATM 5959  O   HOH B 599     -11.194 -23.897  42.982  1.00 38.54           O  
ANISOU 5959  O   HOH B 599     6305   5248   3088    172   -403   -416       O  
HETATM 5960  O   HOH B 600     -42.345 -48.835  25.622  1.00 19.67           O  
ANISOU 5960  O   HOH B 600     3728   2452   1293    -28   -490   -346       O  
HETATM 5961  O   HOH B 601     -40.045 -32.879  19.644  1.00 19.43           O  
ANISOU 5961  O   HOH B 601     3661   2791    928    872    225   -457       O  
HETATM 5962  O   HOH B 602     -17.994 -46.091  19.992  1.00 32.35           O  
ANISOU 5962  O   HOH B 602     4988   4856   2446   1485    993   -511       O  
HETATM 5963  O   HOH B 603     -26.853 -47.696  35.447  1.00 31.25           O  
ANISOU 5963  O   HOH B 603     4562   5243   2068   1020   -197  -1350       O  
HETATM 5964  O   HOH B 604     -43.979 -40.596  10.170  1.00 29.72           O  
ANISOU 5964  O   HOH B 604     5656   4124   1511    395   -285   -199       O  
HETATM 5965  O   HOH B 605     -59.607 -34.017  46.001  1.00 38.26           O  
ANISOU 5965  O   HOH B 605     5391   5283   3863   -841   -234   -625       O  
HETATM 5966  O   HOH B 606     -46.572 -37.700  48.822  1.00 22.69           O  
ANISOU 5966  O   HOH B 606     4254   3236   1130    182    -28   -271       O  
HETATM 5967  O   HOH B 607     -48.958 -50.881  26.658  1.00 34.51           O  
ANISOU 5967  O   HOH B 607     3013   5768   4329   -469   1038  -1669       O  
HETATM 5968  O   HOH B 608     -11.386 -26.156  25.031  1.00 40.07           O  
ANISOU 5968  O   HOH B 608     5607   7417   2197  -1854   1605   -444       O  
HETATM 5969  O   HOH B 609     -29.165 -49.656  11.986  1.00 30.52           O  
ANISOU 5969  O   HOH B 609     5703   3929   1964    661    209   -266       O  
HETATM 5970  O   HOH B 610      -6.152 -32.017  38.827  1.00 35.12           O  
ANISOU 5970  O   HOH B 610     5003   5911   2428   -277   -140    524       O  
HETATM 5971  O   HOH B 611     -42.372 -22.159  43.420  1.00 25.75           O  
ANISOU 5971  O   HOH B 611     4441   4572    769  -1283    530   -510       O  
HETATM 5972  O   HOH B 612     -30.158 -37.794  30.565  1.00 15.99           O  
ANISOU 5972  O   HOH B 612     3024   2389    662    542    288    340       O  
HETATM 5973  O   HOH B 613     -46.221 -34.550  31.635  1.00 17.16           O  
ANISOU 5973  O   HOH B 613     2771   2790    956   -166    212    196       O  
HETATM 5974  O   HOH B 614     -18.649 -31.346  18.376  1.00 27.06           O  
ANISOU 5974  O   HOH B 614     4749   3722   1809    383   1480   -343       O  
HETATM 5975  O   HOH B 615     -19.088 -41.255  45.846  1.00 28.64           O  
ANISOU 5975  O   HOH B 615     3774   5110   1998    797   -923   -505       O  
HETATM 5976  O   HOH B 616     -25.194 -24.122  53.062  1.00 36.90           O  
ANISOU 5976  O   HOH B 616     6314   4855   2851   -239   1143     18       O  
HETATM 5977  O   HOH B 617     -44.027 -38.163  55.258  1.00 34.45           O  
ANISOU 5977  O   HOH B 617     5179   4587   3321   -309    675    214       O  
HETATM 5978  O   HOH B 618     -33.528 -22.572  54.974  1.00 30.67           O  
ANISOU 5978  O   HOH B 618     6129   4717    805    229   -196   -314       O  
HETATM 5979  O   HOH B 619     -37.509 -40.524  27.328  1.00 22.41           O  
ANISOU 5979  O   HOH B 619     4494   3010   1007     63   -467     18       O  
HETATM 5980  O   HOH B 620     -35.526 -26.015  53.828  1.00 24.16           O  
ANISOU 5980  O   HOH B 620     3623   4378   1178    347    269    335       O  
HETATM 5981  O   HOH B 621     -42.939 -25.016  39.368  1.00 27.59           O  
ANISOU 5981  O   HOH B 621     4480   3676   2325    521   -591   -570       O  
HETATM 5982  O   HOH B 622     -50.071 -35.296  54.625  1.00 25.26           O  
ANISOU 5982  O   HOH B 622     3875   3436   2285   -561     -1    255       O  
HETATM 5983  O   HOH B 623     -16.143 -42.921  46.313  1.00 34.20           O  
ANISOU 5983  O   HOH B 623     5265   5614   2114   1096      5   -406       O  
HETATM 5984  O   HOH B 624     -43.935 -33.789  22.343  1.00 15.99           O  
ANISOU 5984  O   HOH B 624     2773   2820    481     39   -175   -458       O  
HETATM 5985  O   HOH B 625     -36.462 -19.455  56.236  1.00 27.94           O  
ANISOU 5985  O   HOH B 625     4363   4596   1654   1283    276     39       O  
HETATM 5986  O   HOH B 626      -9.625 -21.692  26.963  1.00 39.51           O  
ANISOU 5986  O   HOH B 626     6638   5916   2457    909   2033    514       O  
HETATM 5987  O   HOH B 627     -28.337 -43.062   4.987  1.00 36.62           O  
ANISOU 5987  O   HOH B 627     5418   5478   3017    373    515   -978       O  
HETATM 5988  O   HOH B 628     -41.116 -53.708  11.261  1.00 30.59           O  
ANISOU 5988  O   HOH B 628     5373   4026   2222   -743    -72   -717       O  
HETATM 5989  O   HOH B 629     -23.389 -45.855  32.040  1.00 27.30           O  
ANISOU 5989  O   HOH B 629     4869   2995   2507    815   -391    222       O  
HETATM 5990  O   HOH B 630     -43.844 -49.674  38.987  1.00 23.49           O  
ANISOU 5990  O   HOH B 630     4581   2730   1614   -143   -173    798       O  
HETATM 5991  O   HOH B 631     -32.950 -19.414  48.020  1.00 20.43           O  
ANISOU 5991  O   HOH B 631     3671   3009   1080    156    161    441       O  
HETATM 5992  O   HOH B 632     -36.986 -35.075   5.672  1.00 35.11           O  
ANISOU 5992  O   HOH B 632     5236   4926   3177   -132     60   1248       O  
HETATM 5993  O   HOH B 633     -32.821 -43.718  38.154  1.00 20.51           O  
ANISOU 5993  O   HOH B 633     3707   3087    999    609   -287   -145       O  
HETATM 5994  O   HOH B 634     -21.103 -33.457  10.640  1.00 24.07           O  
ANISOU 5994  O   HOH B 634     4085   3639   1420    361    808    661       O  
HETATM 5995  O   HOH B 635     -38.971 -32.973  53.187  1.00 21.21           O  
ANISOU 5995  O   HOH B 635     3956   3427    673      7    607    154       O  
HETATM 5996  O   HOH B 636     -10.093 -34.123  25.455  1.00 27.30           O  
ANISOU 5996  O   HOH B 636     3492   4791   2088   1085    153    366       O  
HETATM 5997  O   HOH B 637     -16.634 -21.691  22.484  1.00 37.38           O  
ANISOU 5997  O   HOH B 637     5365   6037   2798   -369    696   -389       O  
HETATM 5998  O   HOH B 638     -39.189 -39.067  28.574  1.00 21.85           O  
ANISOU 5998  O   HOH B 638     3940   3600    759    355   -448    860       O  
HETATM 5999  O   HOH B 639      -9.159 -28.434  39.395  1.00 31.98           O  
ANISOU 5999  O   HOH B 639     3980   4543   3626    243   -687    475       O  
HETATM 6000  O   HOH B 640     -16.518 -29.677  19.956  1.00 33.59           O  
ANISOU 6000  O   HOH B 640     4921   5688   2153    314    869    874       O  
HETATM 6001  O   HOH B 641     -14.477 -16.623  27.602  1.00 33.17           O  
ANISOU 6001  O   HOH B 641     4362   5320   2920   -685    649   1085       O  
HETATM 6002  O   HOH B 642     -22.420 -22.782  23.964  1.00 24.89           O  
ANISOU 6002  O   HOH B 642     3472   3918   2066    553    605    249       O  
HETATM 6003  O   HOH B 643     -52.538 -42.386  43.294  1.00 37.48           O  
ANISOU 6003  O   HOH B 643     7199   4688   2352  -1147   1367   -467       O  
HETATM 6004  O   HOH B 644      -9.787 -11.938  43.455  1.00 53.34           O  
ANISOU 6004  O   HOH B 644     5345   8941   5980  -1247    199    860       O  
HETATM 6005  O   HOH B 645     -48.747 -46.057  24.439  1.00 30.73           O  
ANISOU 6005  O   HOH B 645     4200   5243   2231   -907    243   -649       O  
HETATM 6006  O   HOH B 646     -35.588 -33.440   3.728  1.00 35.15           O  
ANISOU 6006  O   HOH B 646     5181   5012   3159   -534   -198    502       O  
HETATM 6007  O   HOH B 647     -39.809 -25.986  45.220  1.00 33.70           O  
ANISOU 6007  O   HOH B 647     4500   4976   3328    296    344    129       O  
HETATM 6008  O   HOH B 648     -23.602 -45.844  49.558  1.00 39.71           O  
ANISOU 6008  O   HOH B 648     6587   5648   2851   -543    288    144       O  
HETATM 6009  O   HOH B 649     -23.730 -47.138  25.902  1.00 27.19           O  
ANISOU 6009  O   HOH B 649     5356   3753   1222    623    792    235       O  
HETATM 6010  O   HOH B 650      -8.661 -22.155  31.666  1.00 34.86           O  
ANISOU 6010  O   HOH B 650     4282   6456   2507  -1023    912      0       O  
HETATM 6011  O   HOH B 651     -11.835 -34.577  23.177  1.00 30.02           O  
ANISOU 6011  O   HOH B 651     3920   5504   1979   1149   1175     38       O  
HETATM 6012  O   HOH B 652     -32.178 -45.373  40.225  1.00 20.53           O  
ANISOU 6012  O   HOH B 652     3833   2849   1119    598    182    321       O  
HETATM 6013  O   HOH B 653     -28.576 -34.945  26.218  1.00 32.18           O  
ANISOU 6013  O   HOH B 653     4257   4487   3482    955      0   -183       O  
HETATM 6014  O   HOH B 654     -31.030 -44.504  18.468  1.00 17.54           O  
ANISOU 6014  O   HOH B 654     3322   2500    843    286    345    597       O  
HETATM 6015  O   HOH B 655     -19.900 -32.731  46.344  1.00 29.00           O  
ANISOU 6015  O   HOH B 655     4311   4963   1742    388    378   -659       O  
HETATM 6016  O   HOH B 656     -38.606 -42.303  25.233  1.00 20.61           O  
ANISOU 6016  O   HOH B 656     4123   2404   1304   -117   -813    499       O  
HETATM 6017  O   HOH B 657     -46.395 -25.812  59.783  1.00 34.85           O  
ANISOU 6017  O   HOH B 657     5151   5435   2654    698    113   -249       O  
HETATM 6018  O   HOH B 658     -41.671 -41.840  -1.831  1.00 36.36           O  
ANISOU 6018  O   HOH B 658     6709   5389   1714   -650  -1272    563       O  
HETATM 6019  O   HOH B 659     -22.315 -27.895  46.936  1.00 31.98           O  
ANISOU 6019  O   HOH B 659     5349   4870   1929     84   -602    -12       O  
HETATM 6020  O   HOH B 660      -5.383 -33.074  31.668  1.00 31.92           O  
ANISOU 6020  O   HOH B 660     4151   5391   2583    859      1   -398       O  
HETATM 6021  O   HOH B 661     -21.373 -46.080  28.154  1.00 28.72           O  
ANISOU 6021  O   HOH B 661     4801   3823   2285   1420    113   -560       O  
HETATM 6022  O   HOH B 662     -12.439 -19.013  26.476  1.00 36.66           O  
ANISOU 6022  O   HOH B 662     5181   5754   2993  -1138    699    160       O  
HETATM 6023  O   HOH B 663     -32.970 -50.472  34.246  1.00 25.42           O  
ANISOU 6023  O   HOH B 663     4846   2342   2469    409    195   -433       O  
HETATM 6024  O   HOH B 664     -41.638 -24.338  41.506  1.00 23.62           O  
ANISOU 6024  O   HOH B 664     3495   3119   2359    120   -631     72       O  
HETATM 6025  O   HOH B 665     -34.753 -34.912  18.308  1.00 16.51           O  
ANISOU 6025  O   HOH B 665     2973   2934    365   -395   -339    478       O  
HETATM 6026  O   HOH B 666     -38.375 -26.803  51.276  1.00 20.27           O  
ANISOU 6026  O   HOH B 666     3103   3442   1155    233   -310   -555       O  
HETATM 6027  O   HOH B 667     -39.154 -20.433  42.192  1.00 31.53           O  
ANISOU 6027  O   HOH B 667     5420   3809   2750    634   -963   -134       O  
HETATM 6028  O   HOH B 668     -35.721 -53.897  28.190  1.00 41.54           O  
ANISOU 6028  O   HOH B 668     6591   4512   4679   1159    657   -540       O  
HETATM 6029  O   HOH B 669     -18.629 -32.489  52.499  1.00 29.72           O  
ANISOU 6029  O   HOH B 669     4882   4062   2348    194   -195   -323       O  
HETATM 6030  O   HOH B 670     -55.405 -25.625  53.203  1.00 20.33           O  
ANISOU 6030  O   HOH B 670     3769   3469    486   -141   -242     54       O  
HETATM 6031  O   HOH B 671     -22.256 -31.580  46.077  1.00 28.17           O  
ANISOU 6031  O   HOH B 671     4424   4532   1747    305    269    -12       O  
HETATM 6032  O   HOH B 672     -15.512 -47.843  39.183  1.00 34.25           O  
ANISOU 6032  O   HOH B 672     6533   4218   2263    266  -1076    868       O  
HETATM 6033  O   HOH B 673     -26.227 -45.246  48.114  1.00 38.76           O  
ANISOU 6033  O   HOH B 673     6005   6386   2334    -20     45    920       O  
HETATM 6034  O   HOH B 674     -13.929 -29.927  44.706  1.00 31.25           O  
ANISOU 6034  O   HOH B 674     5083   4605   2184    936   -685    469       O  
HETATM 6035  O   HOH B 675     -15.093 -23.657  42.601  1.00 32.37           O  
ANISOU 6035  O   HOH B 675     6247   4152   1898    -15    541     15       O  
HETATM 6036  O   HOH B 676     -29.165 -22.897  16.112  1.00 26.76           O  
ANISOU 6036  O   HOH B 676     4698   4775    692    428   -995    166       O  
HETATM 6037  O   HOH B 677      -5.029 -37.788  22.989  1.00 45.60           O  
ANISOU 6037  O   HOH B 677     7865   6245   3216   1644   2974   -199       O  
HETATM 6038  O   HOH B 678     -18.285 -38.136   9.475  1.00 35.25           O  
ANISOU 6038  O   HOH B 678     5134   5861   2398    157    688   -474       O  
HETATM 6039  O   HOH B 679     -15.797 -26.288  42.065  1.00 26.00           O  
ANISOU 6039  O   HOH B 679     4583   4348    946    -91    680   -292       O  
HETATM 6040  O   HOH B 680     -45.311 -51.315  33.448  1.00 24.92           O  
ANISOU 6040  O   HOH B 680     3434   3343   2691   -897   -731    424       O  
HETATM 6041  O   HOH B 681     -36.183 -37.149  34.526  1.00 15.22           O  
ANISOU 6041  O   HOH B 681     3000   2501    280    554     72   -218       O  
HETATM 6042  O   HOH B 682     -26.634 -19.489  40.754  1.00 27.28           O  
ANISOU 6042  O   HOH B 682     4493   4915    957    926   -618    591       O  
HETATM 6043  O   HOH B 683     -37.429 -54.483  31.914  1.00 36.42           O  
ANISOU 6043  O   HOH B 683     5913   4674   3251    235    485     94       O  
HETATM 6044  O   HOH B 684     -31.494 -29.469  23.124  1.00 19.44           O  
ANISOU 6044  O   HOH B 684     3487   2846   1053    272   -346   -452       O  
HETATM 6045  O   HOH B 685     -14.603 -23.993  23.447  1.00 34.22           O  
ANISOU 6045  O   HOH B 685     5111   5555   2333   -274    374   -216       O  
HETATM 6046  O   HOH B 686     -21.911 -49.158  39.968  1.00 51.55           O  
ANISOU 6046  O   HOH B 686     6475   6311   6799   1553  -1462   3022       O  
HETATM 6047  O   HOH B 687     -49.026 -30.838  28.867  1.00 16.97           O  
ANISOU 6047  O   HOH B 687     2798   2883    766    366      0   -102       O  
HETATM 6048  O   HOH B 688     -22.205 -29.524  49.075  1.00 32.18           O  
ANISOU 6048  O   HOH B 688     4857   4771   2597    133   -146     10       O  
HETATM 6049  O   HOH B 689     -25.725 -46.349  33.106  1.00 25.74           O  
ANISOU 6049  O   HOH B 689     5118   3656   1004   1035    309   -105       O  
HETATM 6050  O   HOH B 690      -7.279 -29.705  38.156  1.00 35.27           O  
ANISOU 6050  O   HOH B 690     5450   6464   1486   -631   -368    -98       O  
HETATM 6051  O   HOH B 691     -56.174 -31.250  55.256  1.00 35.92           O  
ANISOU 6051  O   HOH B 691     5207   4915   3524   -334   1354     60       O  
HETATM 6052  O   HOH B 692     -31.791 -20.408  16.545  1.00 24.35           O  
ANISOU 6052  O   HOH B 692     4818   3372   1060    406    178   -510       O  
HETATM 6053  O   HOH B 693     -53.871 -32.199  39.270  1.00 33.51           O  
ANISOU 6053  O   HOH B 693     5033   4723   2974   -883     52   -676       O  
HETATM 6054  O   HOH B 694     -29.995 -46.746  43.397  1.00 27.98           O  
ANISOU 6054  O   HOH B 694     5083   3004   2541   1178   1297    715       O  
HETATM 6055  O   HOH B 695     -39.580 -43.725  50.365  1.00 40.67           O  
ANISOU 6055  O   HOH B 695     7058   4678   3715    719    549    197       O  
HETATM 6056  O   HOH B 696     -27.818 -16.167  41.502  1.00 26.67           O  
ANISOU 6056  O   HOH B 696     3963   3932   2235    772   1004    164       O  
HETATM 6057  O   HOH B 697     -44.001 -38.157  10.753  1.00 27.99           O  
ANISOU 6057  O   HOH B 697     4829   4264   1541    591   -172   -140       O  
HETATM 6058  O   HOH B 698     -44.352 -55.777  34.940  1.00 38.56           O  
ANISOU 6058  O   HOH B 698     6622   5566   2461   -998    295   -197       O  
HETATM 6059  O   HOH B 699     -25.541 -41.074  49.541  1.00 29.74           O  
ANISOU 6059  O   HOH B 699     4465   4125   2710    840    -58   -260       O  
HETATM 6060  O   HOH B 700     -45.804 -50.993  30.722  1.00 26.86           O  
ANISOU 6060  O   HOH B 700     4849   3123   2234     51    804    627       O  
HETATM 6061  O   HOH B 701     -14.093 -37.416  19.568  1.00 34.60           O  
ANISOU 6061  O   HOH B 701     5028   5596   2522   1425    361  -1224       O  
HETATM 6062  O   HOH B 702      -9.762 -19.693  37.454  1.00 34.24           O  
ANISOU 6062  O   HOH B 702     4801   4436   3771    418   -122  -1071       O  
HETATM 6063  O   HOH B 703     -34.673 -53.523  37.286  1.00 42.41           O  
ANISOU 6063  O   HOH B 703     5834   5775   4504   -301    126   -359       O  
HETATM 6064  O   HOH B 704     -30.323 -50.200  35.145  1.00 32.27           O  
ANISOU 6064  O   HOH B 704     6917   2585   2758    988  -1645  -1213       O  
HETATM 6065  O   HOH B 705     -52.663 -25.195  63.186  1.00 24.37           O  
ANISOU 6065  O   HOH B 705     4695   3536   1029    125   1090    -29       O  
HETATM 6066  O   HOH B 706     -29.321 -40.990  -0.140  1.00 41.35           O  
ANISOU 6066  O   HOH B 706     6433   5678   3597   -427    476  -1310       O  
HETATM 6067  O   HOH B 707     -51.781 -41.623  31.305  1.00 34.56           O  
ANISOU 6067  O   HOH B 707     6264   4065   2801     88  -1554    813       O  
HETATM 6068  O   HOH B 708     -48.528 -54.587  20.465  1.00 40.76           O  
ANISOU 6068  O   HOH B 708     5888   4760   4839  -1264   -746    316       O  
HETATM 6069  O   HOH B 709     -36.703 -26.360  34.318  1.00 20.03           O  
ANISOU 6069  O   HOH B 709     3232   3242   1135    -26    -38    671       O  
HETATM 6070  O   HOH B 710     -55.801 -33.583  39.873  1.00 42.14           O  
ANISOU 6070  O   HOH B 710     5849   6499   3663   -457  -1003    -57       O  
HETATM 6071  O   HOH B 711     -46.784 -44.442  36.688  1.00 31.96           O  
ANISOU 6071  O   HOH B 711     4520   4387   3236    171   -241    342       O  
HETATM 6072  O   HOH B 712     -14.436 -32.030  47.689  1.00 27.27           O  
ANISOU 6072  O   HOH B 712     4488   4097   1775    310   -451    246       O  
HETATM 6073  O   HOH B 713     -23.011 -19.388  48.512  1.00 38.30           O  
ANISOU 6073  O   HOH B 713     6567   5029   2956   -222   -550    848       O  
HETATM 6074  O   HOH B 714     -11.569 -18.270  32.890  1.00 26.15           O  
ANISOU 6074  O   HOH B 714     3449   4298   2189   -687    563   -678       O  
HETATM 6075  O   HOH B 715     -46.042 -37.879   8.784  1.00 36.96           O  
ANISOU 6075  O   HOH B 715     6711   4275   3055   1085   -443   -523       O  
HETATM 6076  O   HOH B 716     -20.611 -16.662  24.417  1.00 34.27           O  
ANISOU 6076  O   HOH B 716     6370   5292   1356    553   1085   -128       O  
HETATM 6077  O   HOH B 717     -41.865 -42.083  51.028  1.00 38.66           O  
ANISOU 6077  O   HOH B 717     6843   3989   3857    590    687    708       O  
HETATM 6078  O   HOH B 718     -23.628 -47.238  18.607  1.00 22.99           O  
ANISOU 6078  O   HOH B 718     3817   3502   1413    808    310     59       O  
HETATM 6079  O   HOH B 719     -23.950 -47.348  47.242  1.00 34.48           O  
ANISOU 6079  O   HOH B 719     5383   5773   1944    299   -998    546       O  
HETATM 6080  O   HOH B 720     -32.574 -35.823  16.396  1.00 24.56           O  
ANISOU 6080  O   HOH B 720     4057   3175   2098   -192   -701    115       O  
HETATM 6081  O   HOH B 721     -37.306 -46.667  28.799  1.00 19.45           O  
ANISOU 6081  O   HOH B 721     3331   3304    753    353    433    -76       O  
HETATM 6082  O   HOH B 722     -31.037 -46.682  47.641  1.00 34.59           O  
ANISOU 6082  O   HOH B 722     5004   4384   3754   -159   -372   1130       O  
HETATM 6083  O   HOH B 723     -14.376 -26.765  23.019  1.00 28.58           O  
ANISOU 6083  O   HOH B 723     4701   5424    733     15    603    315       O  
HETATM 6084  O   HOH B 724     -44.341 -18.561  56.952  1.00 27.19           O  
ANISOU 6084  O   HOH B 724     3781   4482   2065    614   -822   -826       O  
HETATM 6085  O   HOH B 725     -20.038 -46.436  46.422  1.00 31.17           O  
ANISOU 6085  O   HOH B 725     5379   4740   1723    290    653      1       O  
HETATM 6086  O   HOH B 726     -33.321 -40.516  24.849  1.00 25.07           O  
ANISOU 6086  O   HOH B 726     4182   2888   2455     77    268    163       O  
HETATM 6087  O   HOH B 727     -31.599 -38.848  -0.963  1.00 35.03           O  
ANISOU 6087  O   HOH B 727     6129   4771   2410   -680    675   -457       O  
HETATM 6088  O   HOH B 728     -28.001 -25.390  52.421  1.00 28.06           O  
ANISOU 6088  O   HOH B 728     4921   3770   1968    375   -379   -452       O  
HETATM 6089  O   HOH B 729     -32.922 -50.905   6.848  1.00 31.94           O  
ANISOU 6089  O   HOH B 729     4544   3795   3795  -1342  -1094    378       O  
HETATM 6090  O   HOH B 730     -18.910 -45.918  33.194  1.00 23.68           O  
ANISOU 6090  O   HOH B 730     3873   3822   1301   1368   -675    247       O  
HETATM 6091  O   HOH B 731     -25.631 -47.071  39.833  1.00 31.74           O  
ANISOU 6091  O   HOH B 731     5307   4906   1847    589   1171   -866       O  
HETATM 6092  O   HOH B 732     -45.516 -38.731  46.466  1.00 19.01           O  
ANISOU 6092  O   HOH B 732     3909   2651    662   -199    510     48       O  
HETATM 6093  O   HOH B 733     -38.800 -45.276  -1.233  1.00 36.97           O  
ANISOU 6093  O   HOH B 733     7459   5353   1233  -1699  -1742    411       O  
HETATM 6094  O   HOH B 734     -30.326 -43.797  49.935  1.00 31.79           O  
ANISOU 6094  O   HOH B 734     5201   4181   2695    -56    383    420       O  
HETATM 6095  O   HOH B 735     -15.773 -41.862  15.773  1.00 35.11           O  
ANISOU 6095  O   HOH B 735     6001   5664   1674    -98   1780    -27       O  
HETATM 6096  O   HOH B 736     -31.841 -51.094   9.966  1.00 33.73           O  
ANISOU 6096  O   HOH B 736     4885   5028   2901     77   -162    692       O  
HETATM 6097  O   HOH B 737     -21.691 -45.792  34.170  1.00 27.04           O  
ANISOU 6097  O   HOH B 737     4345   3725   2203    684  -1494    689       O  
HETATM 6098  O   HOH B 738     -32.841 -18.279  10.912  1.00 23.61           O  
ANISOU 6098  O   HOH B 738     3932   3060   1978    439    456   -111       O  
HETATM 6099  O   HOH B 739      -9.763 -29.732  42.062  1.00 31.63           O  
ANISOU 6099  O   HOH B 739     4858   4290   2867    500  -1179   -379       O  
HETATM 6100  O   HOH B 740     -43.804 -35.223  13.627  1.00 23.33           O  
ANISOU 6100  O   HOH B 740     4148   3410   1304    783    749    182       O  
HETATM 6101  O   HOH B 741     -24.837 -32.894  31.982  1.00 14.74           O  
ANISOU 6101  O   HOH B 741     2469   2638    490   -250    146     -5       O  
HETATM 6102  O   HOH B 742     -25.823 -28.196  13.030  1.00 23.58           O  
ANISOU 6102  O   HOH B 742     3466   3846   1645    153     15   -179       O  
HETATM 6103  O   HOH B 743     -35.026 -20.306  49.680  1.00 14.28           O  
ANISOU 6103  O   HOH B 743     2617   2501    305    295     20     84       O  
HETATM 6104  O   HOH B 744     -43.183 -22.916  50.540  1.00 16.66           O  
ANISOU 6104  O   HOH B 744     2788   3149    392     52   -227    218       O  
HETATM 6105  O   HOH B 745     -24.891 -32.771   3.029  1.00 22.50           O  
ANISOU 6105