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***  VIRAL PROTEIN/RNA BINDING PROTEIN 31-JUL-12 4B4N  ***

elNémo ID: 22101122370966482

Job options:

ID        	=	 22101122370966482
JOBID     	=	 VIRAL PROTEIN/RNA BINDING PROTEIN 31-JUL-12 4B4N
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    VIRAL PROTEIN/RNA BINDING PROTEIN       31-JUL-12   4B4N              
TITLE     CPSF6 DEFINES A CONSERVED CAPSID INTERFACE THAT MODULATES HIV-1       
TITLE    2 REPLICATION                                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GAG PROTEIN;                                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: N-TERMINAL DOMAIN, RESIDUES 33-178;                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR SUBUNIT 6; 
COMPND   8 CHAIN: B;                                                            
COMPND   9 FRAGMENT: RESIDUES 313-327;                                          
COMPND  10 SYNONYM: CPSF6, CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR 68   
COMPND  11 KDA SUBUNIT, CFIM68, CPSF 68 KDA SUBUNIT, PRE-MRNA CLEAVAGE FACTOR IM
COMPND  12 68 KDA SUBUNIT, PROTEIN HPBRII-4/7;                                  
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;                 
SOURCE   3 ORGANISM_TAXID: 11676;                                               
SOURCE   4 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE   5 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   9 ORGANISM_COMMON: HUMAN;                                              
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE  12 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 4932                                        
KEYWDS    VIRAL PROTEIN-RNA BINDING PROTEIN COMPLEX, HIV-1, CYCLOPHILIN         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.J.PRICE,L.C.JAMES                                                   
REVDAT   2   08-MAY-19 4B4N    1       REMARK                                   
REVDAT   1   19-SEP-12 4B4N    0                                                
JRNL        AUTH   A.J.PRICE,A.J.FLETCHER,T.SCHALLER,T.ELLIOTT,K.LEE,           
JRNL        AUTH 2 V.N.KEWALRAMANI,J.W.CHIN,G.J.TOWERS,L.C.JAMES                
JRNL        TITL   CPSF6 DEFINES A CONSERVED CAPSID INTERFACE THAT MODULATES    
JRNL        TITL 2 HIV-1 REPLICATION.                                           
JRNL        REF    PLOS PATHOG.                  V.   8  2896 2012              
JRNL        REFN                   ISSN 1553-7366                               
JRNL        PMID   22956906                                                     
JRNL        DOI    10.1371/JOURNAL.PPAT.1002896                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.81 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.81                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.25                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 13664                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.191                           
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.273                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 682                             
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) : 1.81                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.86                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 861                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 88.22                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3140                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 53                           
REMARK   3   BIN FREE R VALUE                    : 0.4940                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1178                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 99                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.19600                                             
REMARK   3    B22 (A**2) : 0.08000                                              
REMARK   3    B33 (A**2) : 0.11600                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.334         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.161         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.118         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.731         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.918                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1217 ; 0.015 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  1179 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1656 ; 1.656 ; 1.955       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2717 ; 0.847 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   150 ; 6.196 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    53 ;36.554 ;24.717       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   203 ;15.147 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     7 ;17.165 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   183 ; 0.092 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1363 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   268 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   369 ; 0.258 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    45 ; 0.262 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):   603 ; 0.173 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    22 ; 0.240 ; 0.200       
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):  1217 ;17.136 ; 2.914       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1179 ; 8.093 ; 2.958       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1655 ;19.950 ; 4.309       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   147 ;26.865 ; 9.152       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   959 ;22.965 ;28.520       
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):  2396 ; 4.468 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):    30 ;29.738 ; 5.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2434 ;13.930 ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL PLUS MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 4B4N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-JUL-12.                  
REMARK 100 THE DEPOSITION ID IS D_1290053583.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13664                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.8                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.04400                            
REMARK 200   FOR THE DATA SET  : 14.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
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: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2GON                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.52                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 17 DEGREES (SITTING DROPS).PROTEIN/      
REMARK 280  PEPTIDE SOLUTION (0.37 MM HIV-1 CAN AND 4 MM CPSF6313-327 IN 20     
REMARK 280  MM HEPES PH 7, 50 MM NACL, 1 MM DTT) WAS MIXED WITH RESERVOIR       
REMARK 280  SOLUTION (20% W/V PEG 3350, 0.2 M POTASSIUM PHOSPHATE DIBASIC)      
REMARK 280  IN A 1:1 MIX., VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       20.28000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       40.41000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       23.18000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       40.41000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       20.28000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       23.18000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1080 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8400 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.6 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     HIS A    87                                                      
REMARK 465     ALA A    88                                                      
REMARK 465     GLY A    89                                                      
REMARK 465     PRO A    90                                                      
REMARK 465     ILE A    91                                                      
REMARK 465     ALA A    92                                                      
REMARK 465     PRO A    93                                                      
REMARK 465     GLY A    94                                                      
REMARK 465     GLN A    95                                                      
REMARK 465     MET A    96                                                      
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   NE2  GLN A   112     O    HOH A  2074              2.02            
REMARK 500   NZ   LYS A    70     O    GLN B   328              2.18            
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    ALA A  31     -106.22     53.22                                   
REMARK 500    HIS A  62       44.67   -143.96                                   
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 A2009        DISTANCE =  6.02 ANGSTROMS                       
REMARK 525    HOH B2001        DISTANCE =  5.98 ANGSTROMS                       
DBREF  4B4N A    1   146  UNP    A9PKC6   A9PKC6_9HIV1    33    178             
DBREF  4B4N B  322   336  UNP    Q16630   CPSF6_HUMAN    313    327             
SEQRES   1 A  146  PRO ILE VAL GLN ASN LEU GLN GLY GLN MET VAL HIS GLN          
SEQRES   2 A  146  ALA ILE SER PRO ARG THR LEU ASN ALA TRP VAL LYS VAL          
SEQRES   3 A  146  VAL GLU GLU LYS ALA PHE SER PRO GLU VAL ILE PRO MET          
SEQRES   4 A  146  PHE SER ALA LEU SER GLU GLY ALA THR PRO GLN ASP LEU          
SEQRES   5 A  146  ASN THR MET LEU ASN THR VAL GLY GLY HIS GLN ALA ALA          
SEQRES   6 A  146  MET GLN MET LEU LYS GLU THR ILE ASN GLU GLU ALA ALA          
SEQRES   7 A  146  GLU TRP ASP ARG LEU HIS PRO VAL HIS ALA GLY PRO ILE          
SEQRES   8 A  146  ALA PRO GLY GLN MET ARG GLU PRO ARG GLY SER ASP ILE          
SEQRES   9 A  146  ALA GLY THR THR SER THR LEU GLN GLU GLN ILE GLY TRP          
SEQRES  10 A  146  MET THR HIS ASN PRO PRO ILE PRO VAL GLY GLU ILE TYR          
SEQRES  11 A  146  LYS ARG TRP ILE ILE LEU GLY LEU ASN LYS ILE VAL ARG          
SEQRES  12 A  146  MET TYR SER                                                  
SEQRES   1 B   15  PRO VAL LEU PHE PRO GLY GLN PRO PHE GLY GLN PRO PRO          
SEQRES   2 B   15  LEU GLY                                                      
FORMUL   3  HOH   *99(H2 O)                                                     
HELIX    1   1 SER A   16  ALA A   31  1                                  16    
HELIX    2   2 GLU A   35  SER A   44  1                                  10    
HELIX    3   3 THR A   48  ASN A   57  1                                  10    
HELIX    4   4 HIS A   62  LEU A   83  1                                  22    
HELIX    5   5 ARG A  100  ALA A  105  1                                   6    
HELIX    6   6 THR A  110  THR A  119  1                                  10    
HELIX    7   7 PRO A  125  TYR A  145  1                                  21    
SHEET    1  AA 2 ILE A   2  GLN A   4  0                                        
SHEET    2  AA 2 MET A  10  HIS A  12 -1  O  VAL A  11   N  VAL A   3           
CISPEP   1 ASN A  121    PRO A  122          0        -4.52                     
CRYST1   40.560   46.360   80.820  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.024655  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.021570  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012373        0.00000                         
ATOM      1  N   PRO A   1      18.331  -0.363  -0.126  1.00 23.60           N  
ANISOU    1  N   PRO A   1     3173   3618   2173    126    -64   -876       N  
ATOM      2  CA  PRO A   1      19.496  -0.532  -0.970  1.00 21.89           C  
ANISOU    2  CA  PRO A   1     2541   3065   2708    108    -11   -491       C  
ATOM      3  C   PRO A   1      20.646  -1.177  -0.222  1.00 22.60           C  
ANISOU    3  C   PRO A   1     3009   3248   2330    528     11   -576       C  
ATOM      4  O   PRO A   1      20.584  -1.310   0.990  1.00 24.52           O  
ANISOU    4  O   PRO A   1     3157   4019   2137    359    -18   -463       O  
ATOM      5  CB  PRO A   1      19.843   0.922  -1.389  1.00 23.28           C  
ANISOU    5  CB  PRO A   1     3180   3054   2611    640   -165   -602       C  
ATOM      6  CG  PRO A   1      19.086   1.789  -0.451  1.00 26.63           C  
ANISOU    6  CG  PRO A   1     3949   2545   3623    573    307   -757       C  
ATOM      7  CD  PRO A   1      17.840   1.028  -0.180  1.00 23.28           C  
ANISOU    7  CD  PRO A   1     3028   3505   2311    495    123   -789       C  
ATOM      8  N   ILE A   2      21.655  -1.623  -0.976  1.00 21.46           N  
ANISOU    8  N   ILE A   2     3201   3102   1847    115     69  -1038       N  
ATOM      9  CA  ILE A   2      22.949  -2.054  -0.455  1.00 19.76           C  
ANISOU    9  CA  ILE A   2     2874   2965   1668   -261   -348   -182       C  
ATOM     10  C   ILE A   2      23.887  -0.876  -0.615  1.00 23.71           C  
ANISOU   10  C   ILE A   2     2614   3539   2855   -180   -528    689       C  
ATOM     11  O   ILE A   2      24.143  -0.399  -1.731  1.00 28.07           O  
ANISOU   11  O   ILE A   2     3159   4463   3042    157    -16   1078       O  
ATOM     12  CB  ILE A   2      23.513  -3.308  -1.115  1.00 22.05           C  
ANISOU   12  CB  ILE A   2     2232   3489   2657     86   -547   -549       C  
ATOM     13  CG1 ILE A   2      22.567  -4.493  -0.948  1.00 23.78           C  
ANISOU   13  CG1 ILE A   2     2478   3574   2982    130   -446   -402       C  
ATOM     14  CG2 ILE A   2      24.885  -3.680  -0.526  1.00 26.55           C  
ANISOU   14  CG2 ILE A   2     3332   3140   3613    519  -1285   -817       C  
ATOM     15  CD1 ILE A   2      22.322  -4.883   0.454  1.00 33.44           C  
ANISOU   15  CD1 ILE A   2     3985   4082   4636   -353    100    235       C  
ATOM     16  N   VAL A   3      24.372  -0.395   0.516  1.00 22.70           N  
ANISOU   16  N   VAL A   3     3741   2160   2725   -247   -439    641       N  
ATOM     17  CA  VAL A   3      25.292   0.746   0.584  1.00 22.54           C  
ANISOU   17  CA  VAL A   3     3443   2352   2769   -219   -567   -225       C  
ATOM     18  C   VAL A   3      26.600   0.353   1.280  1.00 23.22           C  
ANISOU   18  C   VAL A   3     3370   2613   2838     56   -416   -503       C  
ATOM     19  O   VAL A   3      26.636  -0.581   2.090  1.00 26.95           O  
ANISOU   19  O   VAL A   3     4027   3232   2978   -545   -749   -500       O  
ATOM     20  CB  VAL A   3      24.641   1.896   1.391  1.00 25.45           C  
ANISOU   20  CB  VAL A   3     3415   3192   3060    533    140    123       C  
ATOM     21  CG1 VAL A   3      23.323   2.294   0.740  1.00 29.09           C  
ANISOU   21  CG1 VAL A   3     3807   2710   4534    -38   -256   -255       C  
ATOM     22  CG2 VAL A   3      24.394   1.462   2.872  1.00 31.58           C  
ANISOU   22  CG2 VAL A   3     4609   3464   3923    117    394    163       C  
ATOM     23  N   GLN A   4      27.666   1.069   0.962  1.00 25.27           N  
ANISOU   23  N   GLN A   4     3156   3524   2922    565   -164    667       N  
ATOM     24  CA  GLN A   4      28.905   1.013   1.719  1.00 26.44           C  
ANISOU   24  CA  GLN A   4     3745   3261   3037    451   -194    -96       C  
ATOM     25  C   GLN A   4      28.728   1.871   2.968  1.00 27.87           C  
ANISOU   25  C   GLN A   4     4931   2147   3510     58    -60     73       C  
ATOM     26  O   GLN A   4      28.325   3.018   2.868  1.00 31.87           O  
ANISOU   26  O   GLN A   4     4251   2693   5164    853    200   1064       O  
ATOM     27  CB  GLN A   4      30.059   1.548   0.881  1.00 29.23           C  
ANISOU   27  CB  GLN A   4     3909   3604   3593   -273   -293     62       C  
ATOM     28  CG  GLN A   4      31.402   1.266   1.498  1.00 37.18           C  
ANISOU   28  CG  GLN A   4     4591   4837   4696    -68   -312    592       C  
ATOM     29  CD  GLN A   4      32.553   1.611   0.583  1.00 44.14           C  
ANISOU   29  CD  GLN A   4     4731   6858   5178   -893     -9      7       C  
ATOM     30  OE1 GLN A   4      32.630   1.124  -0.542  1.00 47.03           O  
ANISOU   30  OE1 GLN A   4     5401   7777   4690   -964   -631    622       O  
ATOM     31  NE2 GLN A   4      33.469   2.437   1.072  1.00 47.71           N  
ANISOU   31  NE2 GLN A   4     5313   6242   6573  -1940    277   1543       N  
ATOM     32  N   ASN A   5      28.959   1.298   4.138  1.00 25.18           N  
ANISOU   32  N   ASN A   5     3680   2286   3600    154   -558   -353       N  
ATOM     33  CA  ASN A   5      28.872   2.037   5.359  1.00 23.18           C  
ANISOU   33  CA  ASN A   5     3092   2149   3565    460    -67   -382       C  
ATOM     34  C   ASN A   5      30.222   2.696   5.651  1.00 28.32           C  
ANISOU   34  C   ASN A   5     3127   3581   4052    471   -130   -398       C  
ATOM     35  O   ASN A   5      31.119   2.684   4.813  1.00 28.71           O  
ANISOU   35  O   ASN A   5     3602   3273   4030   -869   -438   -504       O  
ATOM     36  CB  ASN A   5      28.312   1.183   6.513  1.00 26.63           C  
ANISOU   36  CB  ASN A   5     3997   3134   2984    489   -504   -258       C  
ATOM     37  CG  ASN A   5      29.289   0.119   7.041  1.00 25.08           C  
ANISOU   37  CG  ASN A   5     3149   3174   3206    337     74     56       C  
ATOM     38  OD1 ASN A   5      30.475   0.089   6.694  1.00 26.04           O  
ANISOU   38  OD1 ASN A   5     3395   2551   3947    746   -207   -356       O  
ATOM     39  ND2 ASN A   5      28.773  -0.766   7.902  1.00 26.34           N  
ANISOU   39  ND2 ASN A   5     3408   3209   3387    616   -552    535       N  
ATOM     40  N   LEU A   6      30.352   3.284   6.830  1.00 34.62           N  
ANISOU   40  N   LEU A   6     4195   4630   4327   -262   -549   -548       N  
ATOM     41  CA  LEU A   6      31.577   3.964   7.216  1.00 40.51           C  
ANISOU   41  CA  LEU A   6     4425   5095   5872   -463   -563   -456       C  
ATOM     42  C   LEU A   6      32.794   3.014   7.365  1.00 38.67           C  
ANISOU   42  C   LEU A   6     4607   4403   5682   -465   -240    142       C  
ATOM     43  O   LEU A   6      33.895   3.334   6.899  1.00 43.10           O  
ANISOU   43  O   LEU A   6     5070   4846   6458  -1271    100  -1904       O  
ATOM     44  CB  LEU A   6      31.353   4.755   8.507  1.00 41.99           C  
ANISOU   44  CB  LEU A   6     4906   5091   5954    223   -503    165       C  
ATOM     45  CG  LEU A   6      31.896   6.185   8.478  1.00 48.53           C  
ANISOU   45  CG  LEU A   6     6205   5123   7109    -37    496   -495       C  
ATOM     46  CD1 LEU A   6      31.766   6.793   9.865  1.00 48.53           C  
ANISOU   46  CD1 LEU A   6     6217   5613   6607   -292    566   -323       C  
ATOM     47  CD2 LEU A   6      33.341   6.254   7.993  1.00 50.40           C  
ANISOU   47  CD2 LEU A   6     6761   6372   6014   -343    946    263       C  
ATOM     48  N   GLN A   7      32.598   1.846   7.981  1.00 43.57           N  
ANISOU   48  N   GLN A   7     5500   4560   6495    162   -971    182       N  
ATOM     49  CA  GLN A   7      33.673   0.840   8.064  1.00 36.75           C  
ANISOU   49  CA  GLN A   7     5016   3589   5359   -104   -710   -553       C  
ATOM     50  C   GLN A   7      34.107   0.335   6.665  1.00 40.23           C  
ANISOU   50  C   GLN A   7     4044   6340   4901    355  -1079   -209       C  
ATOM     51  O   GLN A   7      35.141  -0.322   6.546  1.00 47.16           O  
ANISOU   51  O   GLN A   7     4056   4760   9099    142  -2593  -1622       O  
ATOM     52  CB  GLN A   7      33.233  -0.374   8.895  1.00 38.85           C  
ANISOU   52  CB  GLN A   7     5007   5407   4346   -778  -1289   -400       C  
ATOM     53  CG  GLN A   7      33.072  -0.183  10.398  1.00 44.31           C  
ANISOU   53  CG  GLN A   7     6077   5864   4895   -236    193  -1368       C  
ATOM     54  CD  GLN A   7      34.386  -0.083  11.173  1.00 47.47           C  
ANISOU   54  CD  GLN A   7     6193   6577   5265    660   -442   -670       C  
ATOM     55  OE1 GLN A   7      34.388   0.387  12.309  1.00 63.96           O  
ANISOU   55  OE1 GLN A   7     9289   8444   6568   1726   -295  -2164       O  
ATOM     56  NE2 GLN A   7      35.494  -0.526  10.579  1.00 43.47           N  
ANISOU   56  NE2 GLN A   7     5256   5190   6067     -3   -693     13       N  
ATOM     57  N   GLY A   8      33.336   0.620   5.611  1.00 29.01           N  
ANISOU   57  N   GLY A   8     4090   2855   4077    -32   -917    -39       N  
ATOM     58  CA  GLY A   8      33.610   0.067   4.265  1.00 29.37           C  
ANISOU   58  CA  GLY A   8     3744   2808   4604   -286    608    123       C  
ATOM     59  C   GLY A   8      32.882  -1.266   3.965  1.00 27.58           C  
ANISOU   59  C   GLY A   8     3815   3343   3318   -537    301   -335       C  
ATOM     60  O   GLY A   8      33.152  -1.927   2.942  1.00 25.83           O  
ANISOU   60  O   GLY A   8     3442   3077   3295   -376     94   -292       O  
ATOM     61  N   GLN A   9      31.943  -1.665   4.832  1.00 22.48           N  
ANISOU   61  N   GLN A   9     2836   2280   3425      5   -285    222       N  
ATOM     62  CA  GLN A   9      31.161  -2.899   4.593  1.00 22.57           C  
ANISOU   62  CA  GLN A   9     2843   2718   3015   -370    184     82       C  
ATOM     63  C   GLN A   9      29.934  -2.598   3.726  1.00 22.28           C  
ATOM     64  O   GLN A   9      29.354  -1.517   3.839  1.00 22.26           O  
ANISOU   64  O   GLN A   9     2863   2434   3158    393   -777    119       O  
ATOM     65  CB  GLN A   9      30.699  -3.514   5.919  1.00 23.34           C  
ANISOU   65  CB  GLN A   9     3275   3324   2270    156   -451    125       C  
ATOM     66  CG  GLN A   9      31.821  -3.795   6.920  1.00 23.40           C  
ANISOU   66  CG  GLN A   9     2755   2791   3344    675   -299    314       C  
ATOM     67  CD  GLN A   9      31.336  -3.741   8.351  1.00 24.95           C  
ANISOU   67  CD  GLN A   9     3072   3853   2555    716   -820   -232       C  
ATOM     68  OE1 GLN A   9      30.351  -3.080   8.654  1.00 30.03           O  
ANISOU   68  OE1 GLN A   9     3710   4399   3300    608    -11    -38       O  
ATOM     69  NE2 GLN A   9      32.040  -4.409   9.249  1.00 26.30           N  
ANISOU   69  NE2 GLN A   9     3859   2726   3408    585   -379    415       N  
ATOM     70  N   MET A  10      29.562  -3.533   2.844  1.00 26.36           N  
ANISOU   70  N   MET A  10     3310   2778   3926     39   -130   -370       N  
ATOM     71  CA  MET A  10      28.339  -3.423   2.038  1.00 25.63           C  
ANISOU   71  CA  MET A  10     3588   2932   3218    -63   -148   -297       C  
ATOM     72  C   MET A  10      27.219  -3.938   2.924  1.00 24.55           C  
ANISOU   72  C   MET A  10     3552   2942   2833    411   -206   -117       C  
ATOM     73  O   MET A  10      27.202  -5.121   3.273  1.00 32.34           O  
ANISOU   73  O   MET A  10     4166   2969   5153   -741    808    314       O  
ATOM     74  CB  MET A  10      28.418  -4.262   0.712  1.00 26.06           C  
ANISOU   74  CB  MET A  10     3690   2841   3368    333     78     -5       C  
ATOM     75  CG  MET A  10      29.506  -3.814  -0.242  1.00 31.86           C  
ANISOU   75  CG  MET A  10     4424   4115   3563   -199    134   -707       C  
ATOM     76  SD  MET A  10      29.641  -2.011  -0.428  1.00 42.77           S  
ANISOU   76  SD  MET A  10     5626   4890   5734   1304    558    912       S  
ATOM     77  CE  MET A  10      28.215  -1.716  -1.510  1.00 35.09           C  
ANISOU   77  CE  MET A  10     4283   4425   4624    380    -31   -592       C  
ATOM     78  N   VAL A  11      26.299  -3.053   3.293  1.00 21.72           N  
ANISOU   78  N   VAL A  11     3166   2739   2346    186    -60   -299       N  
ATOM     79  CA  VAL A  11      25.210  -3.387   4.208  1.00 23.43           C  
ANISOU   79  CA  VAL A  11     2956   2690   3255     55   -254    499       C  
ATOM     80  C   VAL A  11      23.862  -2.997   3.610  1.00 18.61           C  
ANISOU   80  C   VAL A  11     2611   1729   2729     76    -46   -166       C  
ATOM     81  O   VAL A  11      23.752  -2.099   2.797  1.00 22.58           O  
ANISOU   81  O   VAL A  11     3729   2938   1912   -429    242    257       O  
ATOM     82  CB  VAL A  11      25.369  -2.731   5.598  1.00 26.67           C  
ANISOU   82  CB  VAL A  11     3471   2965   3694    342    -93    433       C  
ATOM     83  CG1 VAL A  11      26.581  -3.320   6.340  1.00 33.48           C  
ANISOU   83  CG1 VAL A  11     3512   5567   3641   -168   -805    464       C  
ATOM     84  CG2 VAL A  11      25.451  -1.212   5.505  1.00 23.56           C  
ANISOU   84  CG2 VAL A  11     3846   2946   2158   -573    105   -409       C  
ATOM     85  N   HIS A  12      22.823  -3.670   4.039  1.00 22.87           N  
ANISOU   85  N   HIS A  12     2708   2761   3219    129    726   -118       N  
ATOM     86  CA  HIS A  12      21.446  -3.369   3.571  1.00 21.81           C  
ANISOU   86  CA  HIS A  12     3476   2184   2625    308   -257    242       C  
ATOM     87  C   HIS A  12      20.806  -2.334   4.496  1.00 24.22           C  
ANISOU   87  C   HIS A  12     3806   3234   2161    498    -72    -29       C  
ATOM     88  O   HIS A  12      20.960  -2.411   5.711  1.00 22.05           O  
ANISOU   88  O   HIS A  12     3525   2898   1954    470  -1205   -642       O  
ATOM     89  CB  HIS A  12      20.605  -4.645   3.568  1.00 21.84           C  
ANISOU   89  CB  HIS A  12     2758   2790   2748    371    472   -158       C  
ATOM     90  CG  HIS A  12      19.166  -4.414   3.321  1.00 17.45           C  
ANISOU   90  CG  HIS A  12     2510   1742   2377    -81     12    -52       C  
ATOM     91  ND1 HIS A  12      18.640  -4.219   2.058  1.00 21.70           N  
ANISOU   91  ND1 HIS A  12     2852   2782   2609    -11   -345   -461       N  
ATOM     92  CD2 HIS A  12      18.129  -4.337   4.185  1.00 18.62           C  
ANISOU   92  CD2 HIS A  12     2442   2727   1906    165    193    491       C  
ATOM     93  CE1 HIS A  12      17.341  -4.022   2.164  1.00 21.25           C  
ANISOU   93  CE1 HIS A  12     2787   3041   2243    279   -716    135       C  
ATOM     94  NE2 HIS A  12      17.007  -4.087   3.440  1.00 25.42           N  
ANISOU   94  NE2 HIS A  12     3120   3429   3108    588   -161    145       N  
ATOM     95  N   GLN A  13      20.131  -1.355   3.895  1.00 25.73           N  
ANISOU   95  N   GLN A  13     3673   3618   2483    636   -437   -135       N  
ATOM     96  CA  GLN A  13      19.257  -0.395   4.598  1.00 28.10           C  
ANISOU   96  CA  GLN A  13     4416   3261   2997    947   -487   -305       C  
ATOM     97  C   GLN A  13      17.913  -0.364   3.899  1.00 28.55           C  
ANISOU   97  C   GLN A  13     3623   3889   3336   1450    560   -410       C  
ATOM     98  O   GLN A  13      17.861  -0.388   2.686  1.00 30.11           O  
ANISOU   98  O   GLN A  13     4611   3356   3472   1106   -224  -1293       O  
ATOM     99  CB  GLN A  13      19.892   1.011   4.627  1.00 35.26           C  
ANISOU   99  CB  GLN A  13     5191   4336   3867    239   -134   -529       C  
ATOM    100  CG  GLN A  13      20.455   1.529   3.310  1.00 44.94           C  
ANISOU  100  CG  GLN A  13     6274   5133   5668   -932   -158    249       C  
ATOM    101  CD  GLN A  13      20.679   3.051   3.286  1.00 54.90           C  
ANISOU  101  CD  GLN A  13     8850   5180   6828   -751  -1466   -457       C  
ATOM    102  OE1 GLN A  13      20.268   3.739   2.336  1.00 62.42           O  
ANISOU  102  OE1 GLN A  13    10417   3073  10226   1497  -1111   1654       O  
ATOM    103  NE2 GLN A  13      21.340   3.579   4.324  1.00 46.00           N  
ANISOU  103  NE2 GLN A  13     5977   5904   5597   1271   -740  -1527       N  
ATOM    104  N   ALA A  14      16.813  -0.247   4.631  1.00 37.85           N  
ANISOU  104  N   ALA A  14     3808   6487   4083   1590    790   -612       N  
ATOM    105  CA  ALA A  14      15.492  -0.056   3.987  1.00 32.64           C  
ANISOU  105  CA  ALA A  14     4249   5024   3127    810    202     -5       C  
ATOM    106  C   ALA A  14      15.486   1.174   3.113  1.00 32.05           C  
ANISOU  106  C   ALA A  14     4020   4557   3598    431      4   -583       C  
ATOM    107  O   ALA A  14      16.181   2.175   3.405  1.00 29.23           O  
ANISOU  107  O   ALA A  14     3796   4278   3032   1178   -449   -718       O  
ATOM    108  CB  ALA A  14      14.394   0.084   5.046  1.00 36.21           C  
ANISOU  108  CB  ALA A  14     4251   5121   4382    653    596    176       C  
ATOM    109  N   ILE A  15      14.718   1.118   2.026  1.00 30.13           N  
ANISOU  109  N   ILE A  15     3441   4088   3919    557    -40   -407       N  
ATOM    110  CA  ILE A  15      14.526   2.315   1.228  1.00 30.27           C  
ANISOU  110  CA  ILE A  15     3462   4220   3818    334    152   -229       C  
ATOM    111  C   ILE A  15      13.866   3.323   2.178  1.00 29.78           C  
ANISOU  111  C   ILE A  15     4105   3791   3418    841   -139    274       C  
ATOM    112  O   ILE A  15      12.984   2.982   2.981  1.00 39.56           O  
ANISOU  112  O   ILE A  15     3979   5904   5146   1489   1134     -5       O  
ATOM    113  CB  ILE A  15      13.753   2.088  -0.108  1.00 31.28           C  
ANISOU  113  CB  ILE A  15     4029   4400   3453    370    192   -397       C  
ATOM    114  CG1 ILE A  15      13.745   3.388  -0.924  1.00 29.70           C  
ANISOU  114  CG1 ILE A  15     3891   4462   2930    657    -39   -827       C  
ATOM    115  CG2 ILE A  15      12.335   1.556   0.129  1.00 38.04           C  
ANISOU  115  CG2 ILE A  15     4200   5647   4606    473   -421    752       C  
ATOM    116  CD1 ILE A  15      13.149   3.244  -2.314  1.00 32.95           C  
ANISOU  116  CD1 ILE A  15     4401   4660   3459    937   -269  -1041       C  
ATOM    117  N   SER A  16      14.349   4.545   2.140  1.00 31.02           N  
ANISOU  117  N   SER A  16     4993   3654   3139    943  -1107  -1704       N  
ATOM    118  CA  SER A  16      13.930   5.546   3.142  1.00 33.97           C  
ANISOU  118  CA  SER A  16     5305   4091   3509    791    436  -1503       C  
ATOM    119  C   SER A  16      12.637   6.269   2.728  1.00 39.41           C  
ANISOU  119  C   SER A  16     5615   5248   4107   1284    503   -828       C  
ATOM    120  O   SER A  16      12.410   6.510   1.529  1.00 35.02           O  
ANISOU  120  O   SER A  16     4890   4932   3482   2169    449  -1660       O  
ATOM    121  CB  SER A  16      15.042   6.547   3.308  1.00 29.53           C  
ANISOU  121  CB  SER A  16     4445   4045   2727    323   -213  -1217       C  
ATOM    122  OG  SER A  16      15.031   7.418   2.203  1.00 41.70           O  
ANISOU  122  OG  SER A  16     6128   5327   4388    511    267    942       O  
ATOM    123  N   PRO A  17      11.797   6.648   3.725  1.00 44.93           N  
ANISOU  123  N   PRO A  17     5581   7353   4135   1120    454  -1143       N  
ATOM    124  CA  PRO A  17      10.584   7.402   3.411  1.00 39.04           C  
ANISOU  124  CA  PRO A  17     6222   5209   3400   1117    520   -938       C  
ATOM    125  C   PRO A  17      10.888   8.693   2.636  1.00 35.33           C  
ANISOU  125  C   PRO A  17     4538   4693   4191    915    310  -1342       C  
ATOM    126  O   PRO A  17      10.077   9.090   1.796  1.00 45.16           O  
ANISOU  126  O   PRO A  17     6899   5144   5114   2015  -1531  -2865       O  
ATOM    127  CB  PRO A  17       9.976   7.710   4.799  1.00 39.42           C  
ANISOU  127  CB  PRO A  17     5286   6165   3525    730    453   -870       C  
ATOM    128  CG  PRO A  17      11.095   7.564   5.761  1.00 35.68           C  
ANISOU  128  CG  PRO A  17     4924   4736   3895   1029    735     59       C  
ATOM    129  CD  PRO A  17      11.976   6.491   5.187  1.00 44.28           C  
ANISOU  129  CD  PRO A  17     6747   5574   4502   1658   1008   -626       C  
ATOM    130  N   ARG A  18      12.044   9.315   2.888  1.00 29.17           N  
ANISOU  130  N   ARG A  18     4602   3748   2732    784   -267  -1627       N  
ATOM    131  CA  ARG A  18      12.488  10.480   2.125  1.00 33.42           C  
ANISOU  131  CA  ARG A  18     4768   4059   3869    743     39   -817       C  
ATOM    132  C   ARG A  18      12.557  10.224   0.595  1.00 39.67           C  
ANISOU  132  C   ARG A  18     6303   4486   4283   1793   -605  -1373       C  
ATOM    133  O   ARG A  18      11.863  10.893  -0.232  1.00 41.93           O  
ANISOU  133  O   ARG A  18     7288   2758   5883   1759  -2084  -1930       O  
ATOM    134  CB  ARG A  18      13.854  10.916   2.660  1.00 38.80           C  
ANISOU  134  CB  ARG A  18     5067   5260   4414    443     44   -722       C  
ATOM    135  CG  ARG A  18      14.501  12.080   1.917  1.00 45.92           C  
ANISOU  135  CG  ARG A  18     5938   5654   5853   -192   -688    -87       C  
ATOM    136  CD  ARG A  18      15.674  12.647   2.707  1.00 53.84           C  
ANISOU  136  CD  ARG A  18     5407   6943   8104   -164   -882   -233       C  
ATOM    137  NE  ARG A  18      16.189  13.922   2.175  1.00 69.73           N  
ANISOU  137  NE  ARG A  18     7630   7767  11095  -1225   -693    772       N  
ATOM    138  CZ  ARG A  18      17.348  14.494   2.538  1.00 65.04           C  
ANISOU  138  CZ  ARG A  18     7109   8294   9309   -991   -444   1508       C  
ATOM    139  NH1 ARG A  18      18.149  13.902   3.424  1.00 61.68           N  
ANISOU  139  NH1 ARG A  18     6438   8776   8221  -1636  -1062    676       N  
ATOM    140  NH2 ARG A  18      17.719  15.665   2.006  1.00 62.50           N  
ANISOU  140  NH2 ARG A  18     8600   6251   8896  -1250   -355   -558       N  
ATOM    141  N   THR A  19      13.423   9.285   0.233  1.00 34.60           N  
ANISOU  141  N   THR A  19     6233   2860   4053   1060   -824  -1239       N  
ATOM    142  CA  THR A  19      13.563   8.752  -1.141  1.00 29.70           C  
ANISOU  142  CA  THR A  19     4081   4230   2973    476   1257   -220       C  
ATOM    143  C   THR A  19      12.207   8.504  -1.802  1.00 32.64           C  
ANISOU  143  C   THR A  19     5184   3789   3428    788     56  -1162       C  
ATOM    144  O   THR A  19      11.976   8.950  -2.942  1.00 36.01           O  
ANISOU  144  O   THR A  19     6714   3305   3662   1279    979  -1772       O  
ATOM    145  CB  THR A  19      14.375   7.417  -1.096  1.00 32.41           C  
ANISOU  145  CB  THR A  19     4874   4401   3038    457     41   -486       C  
ATOM    146  OG1 THR A  19      15.716   7.688  -0.688  1.00 37.12           O  
ANISOU  146  OG1 THR A  19     5432   5337   3332    364   -942  -1287       O  
ATOM    147  CG2 THR A  19      14.450   6.713  -2.459  1.00 38.72           C  
ANISOU  147  CG2 THR A  19     5262   5193   4255   1364    542  -1537       C  
ATOM    148  N   LEU A  20      11.315   7.809  -1.092  1.00 32.00           N  
ANISOU  148  N   LEU A  20     4437   3684   4037    826   -557   -829       N  
ATOM    149  CA  LEU A  20      10.031   7.402  -1.656  1.00 34.16           C  
ANISOU  149  CA  LEU A  20     4479   4710   3791   1160    -31   -758       C  
ATOM    150  C   LEU A  20       9.169   8.638  -1.906  1.00 32.32           C  
ANISOU  150  C   LEU A  20     4575   4074   3631   1059   -408  -1312       C  
ATOM    151  O   LEU A  20       8.427   8.666  -2.864  1.00 33.93           O  
ANISOU  151  O   LEU A  20     5144   3974   3771   1311   -626  -1151       O  
ATOM    152  CB  LEU A  20       9.280   6.395  -0.769  1.00 34.38           C  
ANISOU  152  CB  LEU A  20     4132   4412   4516   1375   1165  -1232       C  
ATOM    153  CG  LEU A  20       9.649   4.924  -0.724  1.00 37.71           C  
ANISOU  153  CG  LEU A  20     5221   4523   4582      6    742   -717       C  
ATOM    154  CD1 LEU A  20       8.842   4.223   0.367  1.00 37.47           C  
ANISOU  154  CD1 LEU A  20     4407   4947   4883   -637    848  -2149       C  
ATOM    155  CD2 LEU A  20       9.454   4.248  -2.101  1.00 42.50           C  
ANISOU  155  CD2 LEU A  20     5292   5443   5410   -392   -539  -1174       C  
ATOM    156  N   ASN A  21       9.296   9.662  -1.050  1.00 34.10           N  
ANISOU  156  N   ASN A  21     4871   4342   3742   1507    301  -1701       N  
ATOM    157  CA  ASN A  21       8.527  10.890  -1.184  1.00 32.50           C  
ANISOU  157  CA  ASN A  21     5003   4106   3237   1043   -834   -336       C  
ATOM    158  C   ASN A  21       8.983  11.718  -2.356  1.00 31.53           C  
ANISOU  158  C   ASN A  21     4242   4673   3064    627   -370   -731       C  
ATOM    159  O   ASN A  21       8.149  12.341  -3.029  1.00 37.16           O  
ANISOU  159  O   ASN A  21     5393   4056   4668   1903    -23   -830       O  
ATOM    160  CB  ASN A  21       8.643  11.783   0.079  1.00 37.22           C  
ANISOU  160  CB  ASN A  21     5353   4500   4287    976   -341  -1109       C  
ATOM    161  CG  ASN A  21       8.061  11.140   1.309  1.00 40.02           C  
ANISOU  161  CG  ASN A  21     5565   4864   4774    621    358  -1107       C  
ATOM    162  OD1 ASN A  21       7.397  10.094   1.242  1.00 61.70           O  
ANISOU  162  OD1 ASN A  21     8371   5769   9303  -1075   2704  -1937       O  
ATOM    163  ND2 ASN A  21       8.301  11.764   2.452  1.00 47.56           N  
ANISOU  163  ND2 ASN A  21     8101   5264   4704   1001    765  -1171       N  
ATOM    164  N   ALA A  22      10.304  11.743  -2.564  1.00 31.40           N  
ANISOU  164  N   ALA A  22     4315   3851   3765    128   -542   -385       N  
ATOM    165  CA  ALA A  22      10.930  12.374  -3.713  1.00 30.87           C  
ANISOU  165  CA  ALA A  22     3783   3798   4148     17     80  -1261       C  
ATOM    166  C   ALA A  22      10.467  11.685  -4.979  1.00 28.69           C  
ANISOU  166  C   ALA A  22     3867   3386   3645   -496   -808    -87       C  
ATOM    167  O   ALA A  22      10.158  12.355  -5.948  1.00 32.14           O  
ANISOU  167  O   ALA A  22     4744   3036   4429    963   -715   -707       O  
ATOM    168  CB  ALA A  22      12.471  12.314  -3.623  1.00 29.77           C  
ANISOU  168  CB  ALA A  22     3836   2843   4630     30      5  -1803       C  
ATOM    169  N   TRP A  23      10.440  10.355  -4.975  1.00 31.52           N  
ANISOU  169  N   TRP A  23     5096   3261   3617    627   -630  -1150       N  
ATOM    170  CA  TRP A  23       9.999   9.614  -6.154  1.00 26.74           C  
ANISOU  170  CA  TRP A  23     3543   2921   3693    111   -373   -770       C  
ATOM    171  C   TRP A  23       8.520   9.914  -6.460  1.00 24.90           C  
ANISOU  171  C   TRP A  23     3450   2875   3137    515   -124   -866       C  
ATOM    172  O   TRP A  23       8.136  10.055  -7.612  1.00 26.50           O  
ANISOU  172  O   TRP A  23     3163   2719   4184   1072   -783   -378       O  
ATOM    173  CB  TRP A  23      10.296   8.114  -5.992  1.00 25.99           C  
ANISOU  173  CB  TRP A  23     3711   2945   3219    164   -451   -856       C  
ATOM    174  CG  TRP A  23       9.730   7.252  -7.141  1.00 25.34           C  
ANISOU  174  CG  TRP A  23     3218   2916   3492    550   -998   -836       C  
ATOM    175  CD1 TRP A  23       8.836   6.236  -7.022  1.00 25.59           C  
ANISOU  175  CD1 TRP A  23     2572   3235   3915    542   -119   -288       C  
ATOM    176  CD2 TRP A  23      10.020   7.375  -8.531  1.00 26.13           C  
ANISOU  176  CD2 TRP A  23     3520   2197   4210    637      2    443       C  
ATOM    177  NE1 TRP A  23       8.540   5.706  -8.273  1.00 28.94           N  
ANISOU  177  NE1 TRP A  23     3194   3469   4331    917   -362    -65       N  
ATOM    178  CE2 TRP A  23       9.261   6.388  -9.211  1.00 30.81           C  
ANISOU  178  CE2 TRP A  23     4025   4324   3357    642   -455   -153       C  
ATOM    179  CE3 TRP A  23      10.856   8.206  -9.275  1.00 27.14           C  
ANISOU  179  CE3 TRP A  23     4242   2337   3730    529    486     96       C  
ATOM    180  CZ2 TRP A  23       9.304   6.234 -10.596  1.00 29.59           C  
ANISOU  180  CZ2 TRP A  23     3392   4145   3705    231    192   -695       C  
ATOM    181  CZ3 TRP A  23      10.896   8.053 -10.643  1.00 27.00           C  
ANISOU  181  CZ3 TRP A  23     3140   3189   3927    -65   -186   -464       C  
ATOM    182  CH2 TRP A  23      10.119   7.073 -11.296  1.00 25.24           C  
ANISOU  182  CH2 TRP A  23     3985   1923   3680    586    -48   -606       C  
ATOM    183  N   VAL A  24       7.710  10.072  -5.412  1.00 26.78           N  
ANISOU  183  N   VAL A  24     3392   3143   3638   -154   -391   -291       N  
ATOM    184  CA  VAL A  24       6.298  10.442  -5.576  1.00 28.13           C  
ANISOU  184  CA  VAL A  24     3487   3501   3700   -183   -283   -891       C  
ATOM    185  C   VAL A  24       6.158  11.795  -6.262  1.00 32.21           C  
ANISOU  185  C   VAL A  24     3372   3556   5307    692   -892  -1108       C  
ATOM    186  O   VAL A  24       5.339  11.950  -7.168  1.00 36.40           O  
ANISOU  186  O   VAL A  24     3989   4879   4960   1118   -770  -1383       O  
ATOM    187  CB  VAL A  24       5.549  10.307  -4.248  1.00 30.51           C  
ANISOU  187  CB  VAL A  24     3644   3749   4199     62    188   -904       C  
ATOM    188  CG1 VAL A  24       4.148  10.916  -4.297  1.00 39.63           C  
ANISOU  188  CG1 VAL A  24     4894   5038   5126   1204   -511   -917       C  
ATOM    189  CG2 VAL A  24       5.473   8.831  -3.864  1.00 34.95           C  
ANISOU  189  CG2 VAL A  24     5038   3742   4499    384    723  -1225       C  
ATOM    190  N   LYS A  25       7.006  12.753  -5.902  1.00 32.96           N  
ANISOU  190  N   LYS A  25     3967   3178   5378    718   -723  -1127       N  
ATOM    191  CA  LYS A  25       6.935  14.067  -6.504  1.00 31.70           C  
ANISOU  191  CA  LYS A  25     3805   3814   4423     -2   -275   -306       C  
ATOM    192  C   LYS A  25       7.398  14.073  -7.923  1.00 28.64           C  
ANISOU  192  C   LYS A  25     3423   3697   3759    743  -1779  -1108       C  
ATOM    193  O   LYS A  25       6.814  14.776  -8.750  1.00 31.21           O  
ANISOU  193  O   LYS A  25     5192   2436   4228    855  -1674   -815       O  
ATOM    194  CB  LYS A  25       7.828  15.059  -5.788  1.00 35.13           C  
ANISOU  194  CB  LYS A  25     3653   5041   4652   -323   -673   -300       C  
ATOM    195  CG  LYS A  25       7.393  15.447  -4.392  1.00 37.02           C  
ANISOU  195  CG  LYS A  25     3866   4821   5379    -61   -196   -608       C  
ATOM    196  CD  LYS A  25       8.279  16.593  -3.947  1.00 31.74           C  
ANISOU  196  CD  LYS A  25     4265   4033   3759   1013  -1605   -820       C  
ATOM    197  CE  LYS A  25       8.287  16.681  -2.460  1.00 35.82           C  
ANISOU  197  CE  LYS A  25     5118   4533   3959   -263     95   -514       C  
ATOM    198  NZ  LYS A  25       9.468  17.438  -2.049  1.00 35.96           N  
ANISOU  198  NZ  LYS A  25     3913   4528   5219     26   -305    610       N  
ATOM    199  N   VAL A  26       8.482  13.331  -8.193  1.00 29.36           N  
ANISOU  199  N   VAL A  26     4129   2582   4443    785    -33    120       N  
ATOM    200  CA  VAL A  26       8.996  13.225  -9.526  1.00 32.59           C  
ANISOU  200  CA  VAL A  26     3984   4057   4341    499   -392   -908       C  
ATOM    201  C   VAL A  26       7.848  12.868 -10.488  1.00 31.78           C  
ANISOU  201  C   VAL A  26     3955   3682   4436    523   -921    295       C  
ATOM    202  O   VAL A  26       7.664  13.506 -11.517  1.00 37.22           O  
ANISOU  202  O   VAL A  26     5002   4747   4391   1958  -1282    -36       O  
ATOM    203  CB  VAL A  26      10.087  12.112  -9.642  1.00 30.88           C  
ANISOU  203  CB  VAL A  26     3749   4192   3791    799   -807   -153       C  
ATOM    204  CG1 VAL A  26      10.458  11.870 -11.095  1.00 31.31           C  
ANISOU  204  CG1 VAL A  26     4298   3755   3842    654    160     95       C  
ATOM    205  CG2 VAL A  26      11.326  12.497  -8.892  1.00 34.00           C  
ANISOU  205  CG2 VAL A  26     3468   4396   5054    730   -475   -949       C  
ATOM    206  N   VAL A  27       7.094  11.841 -10.128  1.00 26.75           N  
ANISOU  206  N   VAL A  27     2957   3068   4138    924   -341   -802       N  
ATOM    207  CA  VAL A  27       6.122  11.284 -11.040  1.00 31.25           C  
ANISOU  207  CA  VAL A  27     2808   3593   5472    606   -510   -770       C  
ATOM    208  C   VAL A  27       4.979  12.270 -11.185  1.00 32.30           C  
ANISOU  208  C   VAL A  27     4393   3026   4853   1299   -999   -417       C  
ATOM    209  O   VAL A  27       4.566  12.603 -12.303  1.00 37.98           O  
ANISOU  209  O   VAL A  27     4909   4325   5194   1358   -812   -385       O  
ATOM    210  CB  VAL A  27       5.582   9.929 -10.546  1.00 33.24           C  
ANISOU  210  CB  VAL A  27     3698   3976   4955     35   -520   -133       C  
ATOM    211  CG1 VAL A  27       4.417   9.499 -11.446  1.00 37.47           C  
ANISOU  211  CG1 VAL A  27     4489   4612   5133   -385   -740   -605       C  
ATOM    212  CG2 VAL A  27       6.696   8.884 -10.552  1.00 35.14           C  
ANISOU  212  CG2 VAL A  27     4609   3742   4997    305   -669  -1513       C  
ATOM    213  N   GLU A  28       4.491  12.708 -10.036  1.00 34.46           N  
ANISOU  213  N   GLU A  28     4021   4340   4732   1163    186    263       N  
ATOM    214  CA  GLU A  28       3.454  13.733  -9.964  1.00 38.80           C  
ANISOU  214  CA  GLU A  28     4502   4996   5243   1382   -537   -432       C  
ATOM    215  C   GLU A  28       3.739  14.981 -10.832  1.00 37.54           C  
ANISOU  215  C   GLU A  28     4063   3817   6384    843  -1052   -967       C  
ATOM    216  O   GLU A  28       2.920  15.367 -11.674  1.00 42.71           O  
ANISOU  216  O   GLU A  28     5288   5043   5895   2752   -872  -1401       O  
ATOM    217  CB  GLU A  28       3.203  14.108  -8.504  1.00 43.95           C  
ANISOU  217  CB  GLU A  28     5842   4908   5946   1685    184   -341       C  
ATOM    218  CG  GLU A  28       2.297  13.144  -7.748  1.00 42.81           C  
ANISOU  218  CG  GLU A  28     4476   5375   6414   1479    497   -391       C  
ATOM    219  CD  GLU A  28       2.010  13.616  -6.329  1.00 54.29           C  
ANISOU  219  CD  GLU A  28     8370   6293   5963    577    398    615       C  
ATOM    220  OE1 GLU A  28       2.250  14.810  -6.013  1.00 71.88           O  
ANISOU  220  OE1 GLU A  28    10524   7323   9465   2028   -264  -1909       O  
ATOM    221  OE2 GLU A  28       1.545  12.797  -5.519  1.00 54.95           O  
ANISOU  221  OE2 GLU A  28     6648   5332   8895    487    -12   2272       O  
ATOM    222  N   GLU A  29       4.904  15.585 -10.680  1.00 35.53           N  
ANISOU  222  N   GLU A  29     4499   2504   6495    578  -1664  -1077       N  
ATOM    223  CA  GLU A  29       5.204  16.814 -11.402  1.00 43.98           C  
ANISOU  223  CA  GLU A  29     5726   5119   5864    123   -619     72       C  
ATOM    224  C   GLU A  29       5.550  16.602 -12.853  1.00 50.37           C  
ANISOU  224  C   GLU A  29     6722   6063   6352   1765  -1869  -1428       C  
ATOM    225  O   GLU A  29       5.071  17.328 -13.734  1.00 62.55           O  
ANISOU  225  O   GLU A  29     8660   7428   7676   1543  -2254    303       O  
ATOM    226  CB  GLU A  29       6.422  17.510 -10.791  1.00 50.90           C  
ANISOU  226  CB  GLU A  29     6012   6837   6491     89  -1269  -1110       C  
ATOM    227  CG  GLU A  29       6.211  18.205  -9.465  1.00 45.29           C  
ANISOU  227  CG  GLU A  29     5219   5758   6230    300   -237   -963       C  
ATOM    228  CD  GLU A  29       7.448  19.021  -9.080  1.00 50.00           C  
ANISOU  228  CD  GLU A  29     6088   6176   6732   -454   -748   -256       C  
ATOM    229  OE1 GLU A  29       7.945  19.803  -9.954  1.00 52.27           O  
ANISOU  229  OE1 GLU A  29     7748   6288   5824    410    -89   -259       O  
ATOM    230  OE2 GLU A  29       7.930  18.860  -7.919  1.00 43.68           O  
ANISOU  230  OE2 GLU A  29     6388   6227   3979   1221   1990  -1004       O  
ATOM    231  N   LYS A  30       6.440  15.637 -13.089  1.00 44.17           N  
ANISOU  231  N   LYS A  30     6056   4170   6554   1185  -1084   -158       N  
ATOM    232  CA  LYS A  30       7.130  15.521 -14.364  1.00 47.98           C  
ANISOU  232  CA  LYS A  30     6655   5317   6258    370   -718   -685       C  
ATOM    233  C   LYS A  30       6.423  14.517 -15.303  1.00 48.45           C  
ANISOU  233  C   LYS A  30     6357   7194   4854   -651   -915   -215       C  
ATOM    234  O   LYS A  30       6.665  14.543 -16.505  1.00 50.33           O  
ANISOU  234  O   LYS A  30     6515   7724   4883  -1039  -1392     72       O  
ATOM    235  CB  LYS A  30       8.618  15.123 -14.127  1.00 51.13           C  
ANISOU  235  CB  LYS A  30     6010   6681   6737  -1056    735    -73       C  
ATOM    236  CG  LYS A  30       9.642  16.237 -13.819  1.00 51.26           C  
ANISOU  236  CG  LYS A  30     7749   6265   5462   -390    -85  -2146       C  
ATOM    237  CD  LYS A  30       9.089  17.542 -13.235  1.00 61.93           C  
ANISOU  237  CD  LYS A  30     9434   6067   8029   1188    636   -263       C  
ATOM    238  CE  LYS A  30       8.659  18.539 -14.323  1.00 60.19           C  
ANISOU  238  CE  LYS A  30     9109   6564   7196   1429    241   -159       C  
ATOM    239  NZ  LYS A  30       8.332  19.897 -13.808  1.00 52.87           N  
ANISOU  239  NZ  LYS A  30     8405   4377   7303  -1220   -372    622       N  
ATOM    240  N   ALA A  31       5.544  13.672 -14.743  1.00 44.09           N  
ANISOU  240  N   ALA A  31     4510   6450   5791    -67   -927  -1437       N  
ATOM    241  CA  ALA A  31       4.882  12.570 -15.464  1.00 48.17           C  
ANISOU  241  CA  ALA A  31     5581   5717   7002   1132   -388  -1969       C  
ATOM    242  C   ALA A  31       5.970  11.723 -16.132  1.00 45.14           C  
ANISOU  242  C   ALA A  31     7447   3746   5958   2317   -137   -903       C  
ATOM    243  O   ALA A  31       6.694  11.028 -15.404  1.00 56.51           O  
ANISOU  243  O   ALA A  31     6688   9161   5619   1764  -2001   -188       O  
ATOM    244  CB  ALA A  31       3.838  13.091 -16.462  1.00 55.39           C  
ANISOU  244  CB  ALA A  31     5699   7885   7460   -137   -649   -700       C  
ATOM    245  N   PHE A  32       6.127  11.817 -17.467  1.00 40.82           N  
ANISOU  245  N   PHE A  32     6138   3828   5542   1575   -737   -536       N  
ATOM    246  CA  PHE A  32       7.182  11.057 -18.203  1.00 41.63           C  
ANISOU  246  CA  PHE A  32     5284   6255   4276     83    344   -589       C  
ATOM    247  C   PHE A  32       7.977  11.908 -19.210  1.00 39.53           C  
ANISOU  247  C   PHE A  32     5949   4103   4965    704   -833    385       C  
ATOM    248  O   PHE A  32       8.139  11.553 -20.382  1.00 49.13           O  
ANISOU  248  O   PHE A  32     7335   6183   5149    827  -2013    532       O  
ATOM    249  CB  PHE A  32       6.608   9.785 -18.850  1.00 39.31           C  
ANISOU  249  CB  PHE A  32     5482   4208   5244   1296   -354    393       C  
ATOM    250  CG  PHE A  32       6.049   8.808 -17.854  1.00 36.43           C  
ANISOU  250  CG  PHE A  32     4242   4541   5056    387   -246   -260       C  
ATOM    251  CD1 PHE A  32       6.890   8.082 -17.031  1.00 42.09           C  
ANISOU  251  CD1 PHE A  32     5474   4482   6035    354     31    844       C  
ATOM    252  CD2 PHE A  32       4.700   8.621 -17.733  1.00 37.12           C  
ANISOU  252  CD2 PHE A  32     4391   4544   5168   1094    672   -654       C  
ATOM    253  CE1 PHE A  32       6.376   7.193 -16.106  1.00 47.65           C  
ANISOU  253  CE1 PHE A  32     4817   5868   7418    -54   1050   1076       C  
ATOM    254  CE2 PHE A  32       4.173   7.735 -16.816  1.00 41.26           C  
ANISOU  254  CE2 PHE A  32     5216   5778   4682   1409    707    486       C  
ATOM    255  CZ  PHE A  32       5.009   7.017 -15.998  1.00 41.68           C  
ANISOU  255  CZ  PHE A  32     3941   6445   5448   1770   1036    301       C  
ATOM    256  N   SER A  33       8.513  13.012 -18.710  1.00 42.39           N  
ANISOU  256  N   SER A  33     5737   4793   5575   -406    206   -340       N  
ATOM    257  CA  SER A  33       9.446  13.843 -19.454  1.00 42.01           C  
ANISOU  257  CA  SER A  33     5540   4767   5654    317    204      0       C  
ATOM    258  C   SER A  33      10.828  13.168 -19.397  1.00 37.11           C  
ANISOU  258  C   SER A  33     4767   4579   4751   -474  -1368   1428       C  
ATOM    259  O   SER A  33      11.016  12.252 -18.595  1.00 38.06           O  
ANISOU  259  O   SER A  33     5130   4610   4720    718  -1492   1203       O  
ATOM    260  CB  SER A  33       9.464  15.265 -18.844  1.00 48.17           C  
ANISOU  260  CB  SER A  33     6385   5200   6717    585   -319   -667       C  
ATOM    261  OG  SER A  33      10.331  15.353 -17.728  1.00 57.47           O  
ANISOU  261  OG  SER A  33     8760   6379   6696  -1036   -688   -775       O  
ATOM    262  N   PRO A  34      11.785  13.589 -20.262  1.00 51.60           N  
ANISOU  262  N   PRO A  34     5782   6573   7250    406    317   1625       N  
ATOM    263  CA  PRO A  34      13.097  12.897 -20.303  1.00 44.67           C  
ANISOU  263  CA  PRO A  34     5969   5629   5374    146     46    689       C  
ATOM    264  C   PRO A  34      13.788  12.736 -18.935  1.00 48.40           C  
ANISOU  264  C   PRO A  34     6830   5423   6134   1075   -801    449       C  
ATOM    265  O   PRO A  34      14.362  11.683 -18.682  1.00 58.78           O  
ANISOU  265  O   PRO A  34     8087   6879   7366   2057  -1346   1109       O  
ATOM    266  CB  PRO A  34      13.938  13.776 -21.255  1.00 45.96           C  
ANISOU  266  CB  PRO A  34     5637   6309   5514   -139    311    361       C  
ATOM    267  CG  PRO A  34      13.191  15.091 -21.348  1.00 51.64           C  
ANISOU  267  CG  PRO A  34     6277   6908   6436    -97   -536   1320       C  
ATOM    268  CD  PRO A  34      11.741  14.717 -21.221  1.00 48.44           C  
ANISOU  268  CD  PRO A  34     5377   7831   5193    625     34   1969       C  
ATOM    269  N   GLU A  35      13.679  13.765 -18.080  1.00 43.77           N  
ANISOU  269  N   GLU A  35     7127   5254   4249   -475   -264    778       N  
ATOM    270  CA  GLU A  35      14.316  13.854 -16.754  1.00 38.69           C  
ANISOU  270  CA  GLU A  35     5404   4218   5075   -882   -567   -177       C  
ATOM    271  C   GLU A  35      13.762  12.948 -15.617  1.00 36.12           C  
ANISOU  271  C   GLU A  35     5129   3964   4629   -536  -1556    500       C  
ATOM    272  O   GLU A  35      14.302  12.945 -14.485  1.00 35.44           O  
ANISOU  272  O   GLU A  35     5612   3560   4293    928  -1286   -327       O  
ATOM    273  CB  GLU A  35      14.193  15.297 -16.255  1.00 41.49           C  
ANISOU  273  CB  GLU A  35     5542   4152   6069    699   -358   -852       C  
ATOM    274  CG  GLU A  35      12.868  15.620 -15.558  1.00 40.09           C  
ANISOU  274  CG  GLU A  35     5267   4523   5441   -121   -608  -1382       C  
ATOM    275  CD  GLU A  35      12.564  17.140 -15.522  1.00 57.19           C  
ANISOU  275  CD  GLU A  35     9609   5068   7053   1538  -2086    -38       C  
ATOM    276  OE1 GLU A  35      13.022  17.843 -14.569  1.00 58.97           O  
ANISOU  276  OE1 GLU A  35    10023   4635   7745   -137   1246  -1598       O  
ATOM    277  OE2 GLU A  35      11.851  17.641 -16.439  1.00 55.55           O  
ANISOU  277  OE2 GLU A  35     7665   7452   5990   2226   -703    573       O  
ATOM    278  N   VAL A  36      12.663  12.255 -15.879  1.00 31.88           N  
ANISOU  278  N   VAL A  36     3512   4332   4266     27   -349    643       N  
ATOM    279  CA  VAL A  36      12.121  11.290 -14.933  1.00 28.62           C  
ANISOU  279  CA  VAL A  36     3757   3632   3483    389   -629    246       C  
ATOM    280  C   VAL A  36      13.119  10.119 -14.758  1.00 27.04           C  
ANISOU  280  C   VAL A  36     3152   3667   3453    246   -478    263       C  
ATOM    281  O   VAL A  36      13.309   9.575 -13.632  1.00 26.10           O  
ANISOU  281  O   VAL A  36     3515   2409   3991    561   -932    152       O  
ATOM    282  CB  VAL A  36      10.760  10.758 -15.435  1.00 33.94           C  
ANISOU  282  CB  VAL A  36     2584   5664   4645    875   -299    636       C  
ATOM    283  CG1 VAL A  36      10.189   9.702 -14.511  1.00 41.51           C  
ANISOU  283  CG1 VAL A  36     4081   6317   5371    630   -992   1024       C  
ATOM    284  CG2 VAL A  36       9.777  11.904 -15.556  1.00 40.91           C  
ANISOU  284  CG2 VAL A  36     4840   4487   6215    631   -534   -566       C  
ATOM    285  N   ILE A  37      13.780   9.757 -15.848  1.00 23.71           N  
ANISOU  285  N   ILE A  37     3117   2828   3062    543  -1161    699       N  
ATOM    286  CA  ILE A  37      14.725   8.647 -15.815  1.00 26.25           C  
ANISOU  286  CA  ILE A  37     3054   3395   3524    780     25     29       C  
ATOM    287  C   ILE A  37      15.982   8.979 -15.003  1.00 22.06           C  
ANISOU  287  C   ILE A  37     2789   2946   2644    347    346    547       C  
ATOM    288  O   ILE A  37      16.415   8.147 -14.196  1.00 25.92           O  
ANISOU  288  O   ILE A  37     4040   1980   3828    977    -78    464       O  
ATOM    289  CB  ILE A  37      15.046   8.131 -17.222  1.00 28.84           C  
ANISOU  289  CB  ILE A  37     3638   3467   3851     58   -267   -333       C  
ATOM    290  CG1 ILE A  37      13.774   7.504 -17.826  1.00 30.55           C  
ANISOU  290  CG1 ILE A  37     3557   3855   4192    168   -241   -582       C  
ATOM    291  CG2 ILE A  37      16.241   7.181 -17.180  1.00 25.58           C  
ANISOU  291  CG2 ILE A  37     3729   2611   3378    -42   -338   -148       C  
ATOM    292  CD1 ILE A  37      13.873   7.260 -19.304  1.00 32.92           C  
ANISOU  292  CD1 ILE A  37     3817   4930   3760     -1   -668     37       C  
ATOM    293  N   PRO A  38      16.560  10.167 -15.199  1.00 25.17           N  
ANISOU  293  N   PRO A  38     3413   2583   3566    267   -549    505       N  
ATOM    294  CA  PRO A  38      17.682  10.513 -14.346  1.00 25.76           C  
ANISOU  294  CA  PRO A  38     3832   2798   3158    -54   -428    248       C  
ATOM    295  C   PRO A  38      17.337  10.562 -12.847  1.00 23.10           C  
ANISOU  295  C   PRO A  38     3051   2376   3349   -364    -88    495       C  
ATOM    296  O   PRO A  38      18.135  10.115 -12.011  1.00 23.91           O  
ANISOU  296  O   PRO A  38     2921   2797   3364   -441  -1104   -313       O  
ATOM    297  CB  PRO A  38      18.076  11.919 -14.848  1.00 27.38           C  
ANISOU  297  CB  PRO A  38     3462   3223   3716   -321   -236    703       C  
ATOM    298  CG  PRO A  38      17.743  11.876 -16.293  1.00 33.32           C  
ANISOU  298  CG  PRO A  38     4496   4088   4076   -475    -93   1206       C  
ATOM    299  CD  PRO A  38      16.498  11.041 -16.402  1.00 28.11           C  
ANISOU  299  CD  PRO A  38     4338   2691   3648   -314   -694    258       C  
ATOM    300  N   MET A  39      16.166  11.104 -12.525  1.00 25.43           N  
ANISOU  300  N   MET A  39     3732   2307   3621    178   -504   -267       N  
ATOM    301  CA  MET A  39      15.665  11.127 -11.148  1.00 26.10           C  
ANISOU  301  CA  MET A  39     3006   2795   4115   -382    406    298       C  
ATOM    302  C   MET A  39      15.516   9.692 -10.617  1.00 25.47           C  
ANISOU  302  C   MET A  39     3921   2494   3260    133   -770    -18       C  
ATOM    303  O   MET A  39      16.000   9.364  -9.511  1.00 22.23           O  
ANISOU  303  O   MET A  39     3332   1906   3206    271  -1131   -933       O  
ATOM    304  CB  MET A  39      14.318  11.898 -11.076  1.00 31.81           C  
ANISOU  304  CB  MET A  39     3942   3537   4608    194   -416   -596       C  
ATOM    305  CG  MET A  39      14.465  13.423 -11.031  1.00 36.32           C  
ANISOU  305  CG  MET A  39     4561   3926   5311   -865   -716   -634       C  
ATOM    306  SD  MET A  39      15.368  13.999  -9.551  1.00 47.51           S  
ANISOU  306  SD  MET A  39     7075   5647   5329  -1903     38   -980       S  
ATOM    307  CE  MET A  39      14.796  12.966  -8.184  1.00 51.03           C  
ANISOU  307  CE  MET A  39     6749   6367   6273   -728    647    505       C  
ATOM    308  N   PHE A  40      14.831   8.840 -11.383  1.00 23.04           N  
ANISOU  308  N   PHE A  40     2805   2443   3505     60   -367   -170       N  
ATOM    309  CA  PHE A  40      14.642   7.415 -10.972  1.00 21.56           C  
ANISOU  309  CA  PHE A  40     3031   2591   2569   -219   -349   -485       C  
ATOM    310  C   PHE A  40      15.967   6.713 -10.630  1.00 19.09           C  
ANISOU  310  C   PHE A  40     3382   1679   2190     -4   -167   -337       C  
ATOM    311  O   PHE A  40      16.114   6.014  -9.585  1.00 18.91           O  
ANISOU  311  O   PHE A  40     3079   1946   2158    -26    134   -158       O  
ATOM    312  CB  PHE A  40      13.929   6.619 -12.095  1.00 19.95           C  
ANISOU  312  CB  PHE A  40     2545   2410   2622   -139      1   -686       C  
ATOM    313  CG  PHE A  40      13.760   5.186 -11.757  1.00 21.94           C  
ANISOU  313  CG  PHE A  40     2624   3063   2648   -815    366     79       C  
ATOM    314  CD1 PHE A  40      12.871   4.815 -10.768  1.00 22.68           C  
ANISOU  314  CD1 PHE A  40     3004   4093   1518   -190    258    216       C  
ATOM    315  CD2 PHE A  40      14.510   4.206 -12.388  1.00 25.62           C  
ANISOU  315  CD2 PHE A  40     3158   2984   3591    261   -411    381       C  
ATOM    316  CE1 PHE A  40      12.726   3.475 -10.428  1.00 27.21           C  
ANISOU  316  CE1 PHE A  40     3348   3324   3666     97    252   -663       C  
ATOM    317  CE2 PHE A  40      14.366   2.864 -12.045  1.00 24.42           C  
ANISOU  317  CE2 PHE A  40     3012   3095   3169   -682  -1040    -47       C  
ATOM    318  CZ  PHE A  40      13.482   2.508 -11.071  1.00 22.48           C  
ANISOU  318  CZ  PHE A  40     3569   2758   2214   -242   -674   -908       C  
ATOM    319  N   SER A  41      16.935   6.882 -11.530  1.00 20.86           N  
ANISOU  319  N   SER A  41     3219   2355   2352    291   -307    165       N  
ATOM    320  CA  SER A  41      18.250   6.248 -11.403  1.00 21.68           C  
ANISOU  320  CA  SER A  41     2991   2644   2600    -22   -342   -474       C  
ATOM    321  C   SER A  41      18.968   6.795 -10.158  1.00 24.55           C  
ANISOU  321  C   SER A  41     3064   3019   3243   -251   -815   -386       C  
ATOM    322  O   SER A  41      19.501   6.033  -9.352  1.00 24.68           O  
ANISOU  322  O   SER A  41     3738   1836   3802   -330    154     18       O  
ATOM    323  CB  SER A  41      19.068   6.492 -12.659  1.00 23.81           C  
ANISOU  323  CB  SER A  41     3080   2667   3298     41    149     81       C  
ATOM    324  OG  SER A  41      20.370   5.923 -12.558  1.00 30.64           O  
ANISOU  324  OG  SER A  41     3886   3836   3917   1145      8    193       O  
ATOM    325  N   ALA A  42      18.985   8.115 -10.013  1.00 24.92           N  
ANISOU  325  N   ALA A  42     3369   2575   3524    -75   -845    -77       N  
ATOM    326  CA  ALA A  42      19.612   8.731  -8.835  1.00 28.41           C  
ANISOU  326  CA  ALA A  42     4568   2409   3817    156   -609   -553       C  
ATOM    327  C   ALA A  42      18.948   8.234  -7.513  1.00 27.92           C  
ANISOU  327  C   ALA A  42     3269   3678   3661     25   -927   -601       C  
ATOM    328  O   ALA A  42      19.626   7.910  -6.552  1.00 34.38           O  
ANISOU  328  O   ALA A  42     4435   4415   4212    285  -1651   -701       O  
ATOM    329  CB  ALA A  42      19.580  10.277  -8.960  1.00 26.47           C  
ANISOU  329  CB  ALA A  42     4014   2697   3343    293  -1240    770       C  
ATOM    330  N   LEU A  43      17.623   8.116  -7.487  1.00 25.71           N  
ANISOU  330  N   LEU A  43     3516   2800   3450   -406   -471   -668       N  
ATOM    331  CA  LEU A  43      16.908   7.724  -6.274  1.00 25.90           C  
ANISOU  331  CA  LEU A  43     3669   3028   3143   -491   -633   -633       C  
ATOM    332  C   LEU A  43      17.014   6.238  -5.964  1.00 27.29           C  
ANISOU  332  C   LEU A  43     4408   3105   2856    437   -316   -304       C  
ATOM    333  O   LEU A  43      16.635   5.798  -4.887  1.00 25.86           O  
ANISOU  333  O   LEU A  43     3895   2898   3032    -13   -367   -387       O  
ATOM    334  CB  LEU A  43      15.429   8.105  -6.358  1.00 24.51           C  
ANISOU  334  CB  LEU A  43     3798   2666   2849    319   -837   -490       C  
ATOM    335  CG  LEU A  43      15.163   9.585  -6.254  1.00 28.40           C  
ANISOU  335  CG  LEU A  43     3499   2960   4332    598   -920   -293       C  
ATOM    336  CD1 LEU A  43      13.711   9.888  -6.634  1.00 23.52           C  
ANISOU  336  CD1 LEU A  43     3165   2299   3471    504   -266    276       C  
ATOM    337  CD2 LEU A  43      15.527  10.058  -4.842  1.00 35.08           C  
ANISOU  337  CD2 LEU A  43     4860   4049   4419    749    -47   -362       C  
ATOM    338  N   SER A  44      17.485   5.460  -6.916  1.00 24.01           N  
ANISOU  338  N   SER A  44     3099   2986   3036    589    329     41       N  
ATOM    339  CA  SER A  44      17.491   4.007  -6.755  1.00 29.30           C  
ANISOU  339  CA  SER A  44     3914   3124   4094     21   -449     35       C  
ATOM    340  C   SER A  44      18.928   3.426  -6.742  1.00 26.91           C  
ANISOU  340  C   SER A  44     3675   3301   3247   -377   -622   -782       C  
ATOM    341  O   SER A  44      19.141   2.238  -7.020  1.00 25.33           O  
ANISOU  341  O   SER A  44     2799   3350   3472    700   -641    157       O  
ATOM    342  CB  SER A  44      16.642   3.386  -7.863  1.00 27.11           C  
ANISOU  342  CB  SER A  44     3449   3419   3430    -42   -285    624       C  
ATOM    343  OG  SER A  44      17.251   3.617  -9.095  1.00 27.11           O  
ANISOU  343  OG  SER A  44     4532   3550   2217    490    -38  -1485       O  
ATOM    344  N   GLU A  45      19.902   4.259  -6.368  1.00 26.04           N  
ANISOU  344  N   GLU A  45     3300   2670   3923  -1025    137    327       N  
ATOM    345  CA  GLU A  45      21.287   3.833  -6.213  1.00 24.65           C  
ANISOU  345  CA  GLU A  45     3562   2476   3326   -789    166    180       C  
ATOM    346  C   GLU A  45      21.362   2.639  -5.274  1.00 23.12           C  
ANISOU  346  C   GLU A  45     3561   2840   2380    175   -370   -242       C  
ATOM    347  O   GLU A  45      20.824   2.694  -4.178  1.00 22.93           O  
ANISOU  347  O   GLU A  45     3029   2966   2717   -506    -28  -1569       O  
ATOM    348  CB  GLU A  45      22.147   4.984  -5.656  1.00 32.11           C  
ANISOU  348  CB  GLU A  45     4127   3556   4514  -1559   -319    240       C  
ATOM    349  CG  GLU A  45      23.501   5.084  -6.326  1.00 42.71           C  
ANISOU  349  CG  GLU A  45     5061   5216   5949   -660    864    315       C  
ATOM    350  CD  GLU A  45      23.401   5.755  -7.693  1.00 54.21           C  
ANISOU  350  CD  GLU A  45     8488   5513   6595    171    213    767       C  
ATOM    351  OE1 GLU A  45      23.069   6.981  -7.753  1.00 79.13           O  
ANISOU  351  OE1 GLU A  45     8702   6619  14745   3240   3319  -1119       O  
ATOM    352  OE2 GLU A  45      23.632   5.057  -8.709  1.00 69.31           O  
ANISOU  352  OE2 GLU A  45    10758   6991   8586  -1565   2075   -509       O  
ATOM    353  N   GLY A  46      21.990   1.552  -5.712  1.00 23.36           N  
ANISOU  353  N   GLY A  46     3245   3275   2353    297    754   -318       N  
ATOM    354  CA  GLY A  46      22.128   0.347  -4.847  1.00 23.77           C  
ANISOU  354  CA  GLY A  46     3199   3465   2365     30   -182   -277       C  
ATOM    355  C   GLY A  46      20.833  -0.422  -4.532  1.00 23.28           C  
ANISOU  355  C   GLY A  46     3248   2912   2683    427    -16     31       C  
ATOM    356  O   GLY A  46      20.858  -1.325  -3.700  1.00 20.51           O  
ANISOU  356  O   GLY A  46     3019   2543   2228    497   -371   -464       O  
ATOM    357  N   ALA A  47      19.720  -0.119  -5.231  1.00 18.58           N  
ANISOU  357  N   ALA A  47     3001   2300   1759   -106    -29   -415       N  
ATOM    358  CA  ALA A  47      18.406  -0.649  -4.888  1.00 20.10           C  
ANISOU  358  CA  ALA A  47     2655   2671   2310    242    -49   -185       C  
ATOM    359  C   ALA A  47      18.380  -2.150  -5.053  1.00 19.43           C  
ANISOU  359  C   ALA A  47     2174   2794   2414   -119    381   -468       C  
ATOM    360  O   ALA A  47      19.020  -2.698  -5.991  1.00 17.88           O  
ANISOU  360  O   ALA A  47     3425   1795   1570     22    581     28       O  
ATOM    361  CB  ALA A  47      17.323  -0.020  -5.764  1.00 23.31           C  
ANISOU  361  CB  ALA A  47     2630   3265   2960    -33    -69     59       C  
ATOM    362  N   THR A  48      17.647  -2.815  -4.159  1.00 17.39           N  
ANISOU  362  N   THR A  48     2553   2661   1392     41    -82   -456       N  
ATOM    363  CA  THR A  48      17.334  -4.244  -4.319  1.00 20.15           C  
ANISOU  363  CA  THR A  48     2405   3016   2234   -211    262   -743       C  
ATOM    364  C   THR A  48      16.093  -4.300  -5.220  1.00 19.35           C  
ANISOU  364  C   THR A  48     2727   2665   1958     -9     64   -209       C  
ATOM    365  O   THR A  48      15.419  -3.280  -5.392  1.00 17.11           O  
ANISOU  365  O   THR A  48     2452   2465   1583   -115    -23   -194       O  
ATOM    366  CB  THR A  48      16.985  -4.885  -2.975  1.00 21.28           C  
ANISOU  366  CB  THR A  48     2508   2579   2998   -404   -190     81       C  
ATOM    367  OG1 THR A  48      15.829  -4.220  -2.453  1.00 22.72           O  
ANISOU  367  OG1 THR A  48     2576   3624   2429   -297   -163   -470       O  
ATOM    368  CG2 THR A  48      18.113  -4.740  -1.945  1.00 20.48           C  
ANISOU  368  CG2 THR A  48     2421   2681   2677    505     63   -388       C  
ATOM    369  N   PRO A  49      15.767  -5.485  -5.783  1.00 18.65           N  
ANISOU  369  N   PRO A  49     2578   2581   1927    194     59   -255       N  
ATOM    370  CA  PRO A  49      14.448  -5.596  -6.442  1.00 18.46           C  
ANISOU  370  CA  PRO A  49     2417   2448   2147    139     47    -14       C  
ATOM    371  C   PRO A  49      13.268  -5.225  -5.531  1.00 18.83           C  
ANISOU  371  C   PRO A  49     2083   2731   2338    173     18   -193       C  
ATOM    372  O   PRO A  49      12.337  -4.588  -5.976  1.00 17.21           O  
ANISOU  372  O   PRO A  49     2631   1607   2301    140    223    -92       O  
ATOM    373  CB  PRO A  49      14.398  -7.075  -6.885  1.00 18.51           C  
ANISOU  373  CB  PRO A  49     2461   2393   2177    225   -421    127       C  
ATOM    374  CG  PRO A  49      15.837  -7.388  -7.165  1.00 17.80           C  
ANISOU  374  CG  PRO A  49     2363   1901   2499   -161   -151    -93       C  
ATOM    375  CD  PRO A  49      16.625  -6.663  -6.079  1.00 18.37           C  
ANISOU  375  CD  PRO A  49     2495   2475   2008    251   -131   -367       C  
ATOM    376  N   GLN A  50      13.334  -5.565  -4.254  1.00 18.92           N  
ANISOU  376  N   GLN A  50     2467   2298   2423    -26    482    -67       N  
ATOM    377  CA  GLN A  50      12.285  -5.128  -3.292  1.00 23.16           C  
ANISOU  377  CA  GLN A  50     3062   3005   2732    466    655      7       C  
ATOM    378  C   GLN A  50      12.079  -3.586  -3.288  1.00 23.04           C  
ANISOU  378  C   GLN A  50     2882   3094   2775    545    302   -154       C  
ATOM    379  O   GLN A  50      10.936  -3.088  -3.352  1.00 20.88           O  
ANISOU  379  O   GLN A  50     2795   2453   2686    288    434   -375       O  
ATOM    380  CB  GLN A  50      12.643  -5.562  -1.869  1.00 22.63           C  
ANISOU  380  CB  GLN A  50     2907   3259   2430     62    621    274       C  
ATOM    381  CG  GLN A  50      11.518  -5.240  -0.905  1.00 27.87           C  
ANISOU  381  CG  GLN A  50     3011   4081   3496    927    518     68       C  
ATOM    382  CD  GLN A  50      11.925  -5.014   0.556  1.00 40.53           C  
ANISOU  382  CD  GLN A  50     4133   7929   3335   -964    916   -562       C  
ATOM    383  OE1 GLN A  50      13.023  -4.521   0.906  1.00 37.18           O  
ANISOU  383  OE1 GLN A  50     4813   5611   3701   -816    883   -631       O  
ATOM    384  NE2 GLN A  50      11.013  -5.338   1.415  1.00 41.49           N  
ANISOU  384  NE2 GLN A  50     4612   7734   3418  -2087    464    823       N  
ATOM    385  N   ASP A  51      13.194  -2.862  -3.212  1.00 20.29           N  
ANISOU  385  N   ASP A  51     2735   2831   2140    567     63   -528       N  
ATOM    386  CA  ASP A  51      13.215  -1.429  -3.261  1.00 20.16           C  
ANISOU  386  CA  ASP A  51     2788   2678   2192   -122    121   -277       C  
ATOM    387  C   ASP A  51      12.564  -0.889  -4.499  1.00 19.27           C  
ANISOU  387  C   ASP A  51     2386   2577   2356    405    140   -463       C  
ATOM    388  O   ASP A  51      11.757   0.041  -4.437  1.00 18.54           O  
ANISOU  388  O   ASP A  51     2571   2386   2088    473    304  -1001       O  
ATOM    389  CB  ASP A  51      14.653  -0.902  -3.223  1.00 22.83           C  
ANISOU  389  CB  ASP A  51     2656   3008   3008    700   -226   -414       C  
ATOM    390  CG  ASP A  51      15.342  -1.153  -1.905  1.00 24.02           C  
ANISOU  390  CG  ASP A  51     3053   3186   2887    269   -150   -227       C  
ATOM    391  OD1 ASP A  51      14.670  -1.283  -0.858  1.00 25.92           O  
ANISOU  391  OD1 ASP A  51     2599   3838   3411   -181    255   -887       O  
ATOM    392  OD2 ASP A  51      16.581  -1.236  -1.932  1.00 21.98           O  
ANISOU  392  OD2 ASP A  51     2790   2810   2752   -446    -47   -329       O  
ATOM    393  N   LEU A  52      12.976  -1.424  -5.641  1.00 19.06           N  
ANISOU  393  N   LEU A  52     2940   1616   2683    767     17   -540       N  
ATOM    394  CA  LEU A  52      12.456  -0.987  -6.921  1.00 18.35           C  
ANISOU  394  CA  LEU A  52     2436   2392   2141    113    -66   -466       C  
ATOM    395  C   LEU A  52      10.953  -1.181  -7.036  1.00 19.37           C  
ANISOU  395  C   LEU A  52     2693   2844   1822    174    534   -549       C  
ATOM    396  O   LEU A  52      10.260  -0.315  -7.559  1.00 20.77           O  
ANISOU  396  O   LEU A  52     2658   2763   2470    -45    508   -486       O  
ATOM    397  CB  LEU A  52      13.194  -1.725  -8.059  1.00 16.82           C  
ANISOU  397  CB  LEU A  52     2325   2069   1993   -377   -259   -529       C  
ATOM    398  CG  LEU A  52      14.681  -1.375  -8.198  1.00 18.52           C  
ANISOU  398  CG  LEU A  52     2392   2643   1999     88    167   -296       C  
ATOM    399  CD1 LEU A  52      15.430  -2.377  -9.062  1.00 17.09           C  
ANISOU  399  CD1 LEU A  52     2013   2244   2236    -29   -188   -397       C  
ATOM    400  CD2 LEU A  52      14.839   0.051  -8.724  1.00 21.14           C  
ANISOU  400  CD2 LEU A  52     2730   2558   2741    -58     11   -385       C  
ATOM    401  N   ASN A  53      10.434  -2.311  -6.560  1.00 18.15           N  
ANISOU  401  N   ASN A  53     2958   2506   1431    503    -80   -759       N  
ATOM    402  CA  ASN A  53       8.995  -2.548  -6.631  1.00 21.51           C  
ANISOU  402  CA  ASN A  53     3011   2538   2623    256    410   -601       C  
ATOM    403  C   ASN A  53       8.181  -1.632  -5.702  1.00 22.90           C  
ANISOU  403  C   ASN A  53     2524   3333   2841    362    628   -705       C  
ATOM    404  O   ASN A  53       7.087  -1.198  -6.060  1.00 21.89           O  
ANISOU  404  O   ASN A  53     2512   3115   2689    261    310   -539       O  
ATOM    405  CB  ASN A  53       8.692  -3.973  -6.332  1.00 20.55           C  
ANISOU  405  CB  ASN A  53     2695   2329   2781    133    608   -656       C  
ATOM    406  CG  ASN A  53       9.121  -4.888  -7.440  1.00 18.24           C  
ANISOU  406  CG  ASN A  53     2380   2405   2144   -165   -262   -806       C  
ATOM    407  OD1 ASN A  53       9.023  -4.551  -8.606  1.00 19.25           O  
ANISOU  407  OD1 ASN A  53     2849   2001   2463      4    732   -874       O  
ATOM    408  ND2 ASN A  53       9.661  -6.044  -7.060  1.00 20.97           N  
ANISOU  408  ND2 ASN A  53     3323   2411   2235   -112    486   -371       N  
ATOM    409  N   THR A  54       8.777  -1.270  -4.571  1.00 22.29           N  
ANISOU  409  N   THR A  54     2909   2951   2609    564    492   -385       N  
ATOM    410  CA  THR A  54       8.191  -0.255  -3.674  1.00 23.92           C  
ANISOU  410  CA  THR A  54     2946   2785   3357    659    521   -485       C  
ATOM    411  C   THR A  54       8.048   1.093  -4.395  1.00 25.37           C  
ANISOU  411  C   THR A  54     3065   3218   3354    448    670   -431       C  
ATOM    412  O   THR A  54       6.981   1.757  -4.293  1.00 24.27           O  
ANISOU  412  O   THR A  54     2817   3187   3217    148    634   -361       O  
ATOM    413  CB  THR A  54       9.060  -0.156  -2.410  1.00 28.15           C  
ANISOU  413  CB  THR A  54     4028   3659   3006    576    181   -531       C  
ATOM    414  OG1 THR A  54       8.988  -1.397  -1.676  1.00 27.43           O  
ANISOU  414  OG1 THR A  54     3654   3540   3229     16    872   -743       O  
ATOM    415  CG2 THR A  54       8.619   0.941  -1.510  1.00 33.52           C  
ANISOU  415  CG2 THR A  54     4604   3848   4282   1779    373   -246       C  
ATOM    416  N   MET A  55       9.091   1.492  -5.149  1.00 19.27           N  
ANISOU  416  N   MET A  55     2498   1955   2866    313   -189   -623       N  
ATOM    417  CA  MET A  55       9.041   2.703  -5.944  1.00 21.06           C  
ANISOU  417  CA  MET A  55     2833   2897   2270    -89    -69    -60       C  
ATOM    418  C   MET A  55       7.988   2.627  -7.051  1.00 24.00           C  
ANISOU  418  C   MET A  55     2731   2974   3412   -358   -549   -603       C  
ATOM    419  O   MET A  55       7.228   3.603  -7.320  1.00 25.28           O  
ANISOU  419  O   MET A  55     2573   4095   2938    593   -334   -938       O  
ATOM    420  CB  MET A  55      10.402   2.976  -6.584  1.00 20.02           C  
ANISOU  420  CB  MET A  55     2189   2610   2808    -70   -277   -570       C  
ATOM    421  CG  MET A  55      11.520   3.304  -5.555  1.00 25.84           C  
ANISOU  421  CG  MET A  55     2571   3967   3279   -688   -347   -502       C  
ATOM    422  SD  MET A  55      13.127   3.511  -6.377  1.00 23.12           S  
ANISOU  422  SD  MET A  55     2769   2876   3139    121    204    -82       S  
ATOM    423  CE  MET A  55      12.981   5.205  -6.896  1.00 26.62           C  
ANISOU  423  CE  MET A  55     3830   3312   2970   -110     92    730       C  
ATOM    424  N   LEU A  56       7.966   1.492  -7.727  1.00 22.50           N  
ANISOU  424  N   LEU A  56     2987   2956   2605   -127   -204   -523       N  
ATOM    425  CA  LEU A  56       7.037   1.330  -8.885  1.00 22.63           C  
ANISOU  425  CA  LEU A  56     2552   3095   2948     82   -399    -77       C  
ATOM    426  C   LEU A  56       5.566   1.364  -8.503  1.00 26.86           C  
ANISOU  426  C   LEU A  56     2867   3912   3425    158     13   -447       C  
ATOM    427  O   LEU A  56       4.723   1.989  -9.202  1.00 28.85           O  
ANISOU  427  O   LEU A  56     2551   5099   3308    471    146  -1050       O  
ATOM    428  CB  LEU A  56       7.391   0.085  -9.678  1.00 21.40           C  
ANISOU  428  CB  LEU A  56     1853   3683   2594   -108   -418   -478       C  
ATOM    429  CG  LEU A  56       8.679   0.351 -10.486  1.00 19.53           C  
ANISOU  429  CG  LEU A  56     2109   3175   2135   -120   -300   -255       C  
ATOM    430  CD1 LEU A  56       9.067  -0.938 -11.174  1.00 25.86           C  
ANISOU  430  CD1 LEU A  56     3078   4193   2553    199   -443   -705       C  
ATOM    431  CD2 LEU A  56       8.571   1.513 -11.448  1.00 20.91           C  
ANISOU  431  CD2 LEU A  56     2343   2646   2953    152    290   -596       C  
ATOM    432  N   ASN A  57       5.273   0.756  -7.369  1.00 22.58           N  
ANISOU  432  N   ASN A  57     2459   2938   3182   -413   -249   -508       N  
ATOM    433  CA  ASN A  57       3.922   0.675  -6.890  1.00 26.53           C  
ANISOU  433  CA  ASN A  57     2832   3395   3852    -99   -212   -970       C  
ATOM    434  C   ASN A  57       3.350   1.972  -6.346  1.00 31.56           C  
ANISOU  434  C   ASN A  57     2605   4513   4871    248    825  -1690       C  
ATOM    435  O   ASN A  57       2.173   2.030  -6.100  1.00 34.93           O  
ANISOU  435  O   ASN A  57     2936   5178   5156   1085   1780   -843       O  
ATOM    436  CB  ASN A  57       3.758  -0.498  -5.901  1.00 28.27           C  
ANISOU  436  CB  ASN A  57     2636   4262   3843    325    473   -606       C  
ATOM    437  CG  ASN A  57       3.682  -1.858  -6.617  1.00 28.63           C  
ANISOU  437  CG  ASN A  57     3378   3509   3988   -479    294   -208       C  
ATOM    438  OD1 ASN A  57       3.185  -1.972  -7.763  1.00 31.03           O  
ANISOU  438  OD1 ASN A  57     2889   4540   4359    -85    687  -1151       O  
ATOM    439  ND2 ASN A  57       4.181  -2.877  -5.965  1.00 26.94           N  
ANISOU  439  ND2 ASN A  57     4087   2926   3222    490    741   -538       N  
ATOM    440  N   THR A  58       4.178   3.002  -6.210  1.00 31.04           N  
ANISOU  440  N   THR A  58     4381   3805   3607   -196    944  -1245       N  
ATOM    441  CA  THR A  58       3.714   4.314  -5.792  1.00 31.63           C  
ANISOU  441  CA  THR A  58     3507   4107   4404    862    773    140       C  
ATOM    442  C   THR A  58       3.114   5.061  -6.989  1.00 33.17           C  
ANISOU  442  C   THR A  58     4134   3680   4788   1317    -62   -475       C  
ATOM    443  O   THR A  58       2.414   6.054  -6.816  1.00 41.67           O  
ANISOU  443  O   THR A  58     4405   4346   7081   1891   1121  -2218       O  
ATOM    444  CB  THR A  58       4.823   5.179  -5.137  1.00 30.89           C  
ANISOU  444  CB  THR A  58     4380   4134   3222   1040    522   -463       C  
ATOM    445  OG1 THR A  58       5.813   5.542  -6.094  1.00 30.83           O  
ANISOU  445  OG1 THR A  58     3777   4848   3086    705    230   -357       O  
ATOM    446  CG2 THR A  58       5.509   4.448  -3.946  1.00 28.75           C  
ANISOU  446  CG2 THR A  58     4104   4118   2698    699    433   -801       C  
ATOM    447  N   VAL A  59       3.402   4.585  -8.190  1.00 33.68           N  
ANISOU  447  N   VAL A  59     3338   5221   4236    288    358     86       N  
ATOM    448  CA  VAL A  59       2.908   5.235  -9.375  1.00 32.32           C  
ANISOU  448  CA  VAL A  59     3815   4052   4413    258     51   -367       C  
ATOM    449  C   VAL A  59       1.396   4.987  -9.434  1.00 39.47           C  
ANISOU  449  C   VAL A  59     3696   4890   6408    235  -1116  -1637       C  
ATOM    450  O   VAL A  59       0.923   3.837  -9.522  1.00 39.90           O  
ANISOU  450  O   VAL A  59     2970   5093   7096    -25   -351  -1357       O  
ATOM    451  CB  VAL A  59       3.607   4.780 -10.666  1.00 30.88           C  
ANISOU  451  CB  VAL A  59     3682   3962   4089   -185    417    323       C  
ATOM    452  CG1 VAL A  59       3.030   5.579 -11.868  1.00 36.38           C  
ANISOU  452  CG1 VAL A  59     4967   3792   5062    313   -457   -171       C  
ATOM    453  CG2 VAL A  59       5.124   4.963 -10.549  1.00 31.15           C  
ANISOU  453  CG2 VAL A  59     4280   3558   3996    443  -1234    173       C  
ATOM    454  N   GLY A  60       0.641   6.068  -9.277  1.00 45.15           N  
ANISOU  454  N   GLY A  60     4467   5227   7459    687  -1509  -1261       N  
ATOM    455  CA  GLY A  60      -0.808   6.011  -9.486  1.00 42.16           C  
ANISOU  455  CA  GLY A  60     4513   6263   5239    808     31   -465       C  
ATOM    456  C   GLY A  60      -1.153   6.754 -10.753  1.00 51.67           C  
ANISOU  456  C   GLY A  60     5374   7413   6846    760  -1614    656       C  
ATOM    457  O   GLY A  60      -0.392   7.649 -11.186  1.00 51.98           O  
ANISOU  457  O   GLY A  60     4677   5843   9227   1924     98    122       O  
ATOM    458  N   GLY A  61      -2.262   6.349 -11.369  1.00 48.09           N  
ANISOU  458  N   GLY A  61     4588   5838   7844   -400   -581   1061       N  
ATOM    459  CA  GLY A  61      -2.899   7.140 -12.433  1.00 49.38           C  
ANISOU  459  CA  GLY A  61     5714   6998   6047    -61  -1189   -421       C  
ATOM    460  C   GLY A  61      -2.189   7.255 -13.774  1.00 55.95           C  
ANISOU  460  C   GLY A  61     7036   7518   6703    317   -737   -671       C  
ATOM    461  O   GLY A  61      -2.283   8.307 -14.452  1.00 64.36           O  
ANISOU  461  O   GLY A  61    10251   7671   6530   -436  -3037   -270       O  
ATOM    462  N   HIS A  62      -1.487   6.194 -14.172  1.00 47.73           N  
ANISOU  462  N   HIS A  62     5356   6498   6278   -261   -169   -897       N  
ATOM    463  CA  HIS A  62      -0.756   6.218 -15.429  1.00 46.20           C  
ANISOU  463  CA  HIS A  62     4929   5498   7123    175   -184  -1470       C  
ATOM    464  C   HIS A  62      -0.837   4.839 -16.043  1.00 46.78           C  
ANISOU  464  C   HIS A  62     3451   4770   9553   -198   -796  -1482       C  
ATOM    465  O   HIS A  62       0.147   4.312 -16.574  1.00 43.86           O  
ANISOU  465  O   HIS A  62     3681   6532   6450    228  -1280  -2122       O  
ATOM    466  CB  HIS A  62       0.712   6.640 -15.186  1.00 46.14           C  
ANISOU  466  CB  HIS A  62     5184   5187   7158      4  -1223  -1289       C  
ATOM    467  CG  HIS A  62       0.961   8.114 -15.313  1.00 39.95           C  
ANISOU  467  CG  HIS A  62     3981   5355   5843   -825    375   -269       C  
ATOM    468  ND1 HIS A  62       1.247   8.918 -14.223  1.00 48.71           N  
ANISOU  468  ND1 HIS A  62     6986   5480   6040    949    339   -792       N  
ATOM    469  CD2 HIS A  62       1.004   8.924 -16.401  1.00 44.96           C  
ANISOU  469  CD2 HIS A  62     7470   4108   5504   2100    153   -828       C  
ATOM    470  CE1 HIS A  62       1.439  10.160 -14.634  1.00 49.16           C  
ANISOU  470  CE1 HIS A  62     6765   5399   6515   -236   -767   -391       C  
ATOM    471  NE2 HIS A  62       1.307  10.190 -15.952  1.00 51.50           N  
ANISOU  471  NE2 HIS A  62     7953   4947   6668   2197  -2418  -1104       N  
ATOM    472  N   GLN A  63      -2.041   4.295 -16.007  1.00 44.01           N  
ANISOU  472  N   GLN A  63     2583   4589   9548    592    555   -693       N  
ATOM    473  CA  GLN A  63      -2.289   2.852 -16.104  1.00 42.01           C  
ANISOU  473  CA  GLN A  63     3871   4829   7261    184    197   -483       C  
ATOM    474  C   GLN A  63      -1.752   2.193 -17.369  1.00 33.93           C  
ANISOU  474  C   GLN A  63     3403   4560   4928   -259   -406    195       C  
ATOM    475  O   GLN A  63      -1.247   1.051 -17.308  1.00 43.12           O  
ANISOU  475  O   GLN A  63     3542   4786   8054    669  -1844  -2366       O  
ATOM    476  CB  GLN A  63      -3.810   2.550 -15.988  1.00 44.17           C  
ANISOU  476  CB  GLN A  63     3842   6617   6320   -250    -55  -1426       C  
ATOM    477  CG  GLN A  63      -4.449   2.899 -14.644  1.00 51.10           C  
ANISOU  477  CG  GLN A  63     4989   7466   6959    186   -175   -906       C  
ATOM    478  CD  GLN A  63      -4.802   4.386 -14.481  1.00 55.71           C  
ANISOU  478  CD  GLN A  63     7312   7148   6705    886     23   -951       C  
ATOM    479  OE1 GLN A  63      -4.937   5.136 -15.466  1.00 63.53           O  
ANISOU  479  OE1 GLN A  63     5836   8569   9732   2430    186   1006       O  
ATOM    480  NE2 GLN A  63      -4.956   4.813 -13.229  1.00 56.88           N  
ANISOU  480  NE2 GLN A  63     8118   6204   7289   1519    229  -1763       N  
ATOM    481  N   ALA A  64      -1.862   2.888 -18.507  1.00 43.35           N  
ANISOU  481  N   ALA A  64     5369   5281   5821    634   -579   -289       N  
ATOM    482  CA  ALA A  64      -1.349   2.349 -19.775  1.00 40.52           C  
ANISOU  482  CA  ALA A  64     4398   5884   5112   -430   -865    -70       C  
ATOM    483  C   ALA A  64       0.181   2.218 -19.734  1.00 44.64           C  
ANISOU  483  C   ALA A  64     4394   4475   8089    480  -1406  -1242       C  
ATOM    484  O   ALA A  64       0.729   1.142 -19.991  1.00 41.00           O  
ANISOU  484  O   ALA A  64     4374   5284   5920    874  -3393  -2357       O  
ATOM    485  CB  ALA A  64      -1.772   3.227 -20.939  1.00 49.51           C  
ANISOU  485  CB  ALA A  64     5801   6044   6967    610  -1730    -47       C  
ATOM    486  N   ALA A  65       0.853   3.324 -19.407  1.00 40.50           N  
ANISOU  486  N   ALA A  65     3618   5158   6612    384  -2517   -832       N  
ATOM    487  CA  ALA A  65       2.312   3.329 -19.163  1.00 32.71           C  
ANISOU  487  CA  ALA A  65     3270   3781   5374     21   -469   -502       C  
ATOM    488  C   ALA A  65       2.789   2.190 -18.298  1.00 29.40           C  
ANISOU  488  C   ALA A  65     3384   3982   3802   -298   -411   -495       C  
ATOM    489  O   ALA A  65       3.748   1.496 -18.651  1.00 29.56           O  
ANISOU  489  O   ALA A  65     3152   3156   4921   -496   -771   -623       O  
ATOM    490  CB  ALA A  65       2.745   4.639 -18.525  1.00 32.76           C  
ANISOU  490  CB  ALA A  65     4225   4276   3946   -177   -622   -643       C  
ATOM    491  N   MET A  66       2.167   2.020 -17.142  1.00 27.75           N  
ANISOU  491  N   MET A  66     1761   4224   4556    113   -150   -374       N  
ATOM    492  CA  MET A  66       2.618   0.992 -16.205  1.00 30.54           C  
ANISOU  492  CA  MET A  66     3403   3613   4587   -951   -114    494       C  
ATOM    493  C   MET A  66       2.398  -0.419 -16.766  1.00 37.09           C  
ANISOU  493  C   MET A  66     4205   4323   5564    367  -1446   -756       C  
ATOM    494  O   MET A  66       3.064  -1.384 -16.353  1.00 39.10           O  
ANISOU  494  O   MET A  66     2994   4192   7668    466  -1204  -1350       O  
ATOM    495  CB  MET A  66       1.916   1.140 -14.845  1.00 34.34           C  
ANISOU  495  CB  MET A  66     3118   4632   5294      7    -14   -408       C  
ATOM    496  CG  MET A  66       2.316   2.353 -14.005  1.00 31.98           C  
ANISOU  496  CG  MET A  66     3524   3990   4635   -456    234    551       C  
ATOM    497  SD  MET A  66       4.097   2.460 -13.660  1.00 34.19           S  
ANISOU  497  SD  MET A  66     3693   4112   5184     80    302   -516       S  
ATOM    498  CE  MET A  66       4.704   3.425 -15.062  1.00 35.68           C  
ANISOU  498  CE  MET A  66     3814   5626   4114    223   -988   -320       C  
ATOM    499  N   GLN A  67       1.462  -0.542 -17.703  1.00 37.22           N  
ANISOU  499  N   GLN A  67     2862   4817   6460    763  -1258   -623       N  
ATOM    500  CA  GLN A  67       1.233  -1.799 -18.409  1.00 36.75           C  
ANISOU  500  CA  GLN A  67     3180   4784   5997    315   -659   -757       C  
ATOM    501  C   GLN A  67       2.342  -2.057 -19.425  1.00 30.33           C  
ANISOU  501  C   GLN A  67     3648   3640   4235     88  -1202   -321       C  
ATOM    502  O   GLN A  67       2.793  -3.174 -19.574  1.00 32.41           O  
ANISOU  502  O   GLN A  67     2779   4155   5379     18  -1759  -1371       O  
ATOM    503  CB  GLN A  67      -0.184  -1.817 -19.042  1.00 37.81           C  
ANISOU  503  CB  GLN A  67     4204   5116   5045  -1341  -1067    365       C  
ATOM    504  CG  GLN A  67      -1.229  -2.265 -18.021  1.00 42.29           C  
ANISOU  504  CG  GLN A  67     3528   6133   6406   -442   -496    -72       C  
ATOM    505  CD  GLN A  67      -0.936  -3.673 -17.481  1.00 57.21           C  
ANISOU  505  CD  GLN A  67     8101   6969   6668    544   -852    791       C  
ATOM    506  OE1 GLN A  67      -0.407  -4.557 -18.207  1.00 50.26           O  
ANISOU  506  OE1 GLN A  67     4334   6472   8290  -1502  -1135   -966       O  
ATOM    507  NE2 GLN A  67      -1.265  -3.889 -16.187  1.00 53.13           N  
ANISOU  507  NE2 GLN A  67     4193   9016   6979    869   -628  -1144       N  
ATOM    508  N   MET A  68       2.825  -0.990 -20.050  1.00 30.77           N  
ANISOU  508  N   MET A  68     3251   4635   3803    431  -1184   -167       N  
ATOM    509  CA  MET A  68       3.934  -1.054 -20.961  1.00 28.78           C  
ANISOU  509  CA  MET A  68     3833   3984   3118     16   -585    106       C  
ATOM    510  C   MET A  68       5.185  -1.457 -20.223  1.00 29.80           C  
ANISOU  510  C   MET A  68     3386   4285   3650    208   -537   -433       C  
ATOM    511  O   MET A  68       5.984  -2.240 -20.723  1.00 32.02           O  
ANISOU  511  O   MET A  68     3216   4670   4279    -12   -780  -1072       O  
ATOM    512  CB  MET A  68       4.195   0.301 -21.569  1.00 35.51           C  
ANISOU  512  CB  MET A  68     5001   2891   5599   1596   -659    185       C  
ATOM    513  CG  MET A  68       3.119   0.773 -22.506  1.00 41.69           C  
ANISOU  513  CG  MET A  68     5005   4846   5989    483  -1611   -452       C  
ATOM    514  SD  MET A  68       3.617   2.383 -23.129  1.00 60.15           S  
ANISOU  514  SD  MET A  68     6769   6238   9845    567    131   1637       S  
ATOM    515  CE  MET A  68       5.205   2.058 -23.932  1.00 43.52           C  
ANISOU  515  CE  MET A  68     5668   4699   6166   1036   -188   1322       C  
ATOM    516  N   LEU A  69       5.337  -0.918 -19.017  1.00 25.72           N  
ANISOU  516  N   LEU A  69     2619   3321   3830    704   -837   -254       N  
ATOM    517  CA  LEU A  69       6.444  -1.286 -18.166  1.00 25.01           C  
ANISOU  517  CA  LEU A  69     2878   3518   3104    351   -542    104       C  
ATOM    518  C   LEU A  69       6.424  -2.769 -17.793  1.00 22.32           C  
ANISOU  518  C   LEU A  69     2498   3330   2651    274   -367   -119       C  
ATOM    519  O   LEU A  69       7.447  -3.459 -17.911  1.00 20.73           O  
ANISOU  519  O   LEU A  69     2157   2691   3027    -69   -701  -1092       O  
ATOM    520  CB  LEU A  69       6.438  -0.395 -16.948  1.00 29.00           C  
ANISOU  520  CB  LEU A  69     3832   4340   2843    272   -394   -167       C  
ATOM    521  CG  LEU A  69       7.615  -0.589 -16.033  1.00 28.42           C  
ANISOU  521  CG  LEU A  69     2900   4074   3821    -85   -208   -615       C  
ATOM    522  CD1 LEU A  69       8.921  -0.465 -16.799  1.00 23.82           C  
ANISOU  522  CD1 LEU A  69     3283   3566   2199   -616     26   -602       C  
ATOM    523  CD2 LEU A  69       7.503   0.435 -14.934  1.00 30.49           C  
ANISOU  523  CD2 LEU A  69     2805   4311   4467   -289     51  -1350       C  
ATOM    524  N   LYS A  70       5.271  -3.273 -17.394  1.00 22.43           N  
ANISOU  524  N   LYS A  70     2478   2992   3052     18   -382   -698       N  
ATOM    525  CA  LYS A  70       5.121  -4.727 -17.141  1.00 22.87           C  
ANISOU  525  CA  LYS A  70     2223   3108   3358    514   -816    200       C  
ATOM    526  C   LYS A  70       5.470  -5.598 -18.361  1.00 22.55           C  
ANISOU  526  C   LYS A  70     2165   3221   3180    137   -818    140       C  
ATOM    527  O   LYS A  70       6.146  -6.640 -18.239  1.00 22.01           O  
ANISOU  527  O   LYS A  70     2378   2220   3764   -482   -756   -163       O  
ATOM    528  CB  LYS A  70       3.694  -5.034 -16.672  1.00 30.11           C  
ANISOU  528  CB  LYS A  70     3072   4782   3582   -591   -600  -1152       C  
ATOM    529  CG  LYS A  70       3.380  -4.551 -15.272  1.00 33.90           C  
ANISOU  529  CG  LYS A  70     3596   5425   3859   -288    768   -864       C  
ATOM    530  CD  LYS A  70       1.915  -4.762 -14.903  1.00 38.25           C  
ANISOU  530  CD  LYS A  70     3063   5512   5955    156    358   -532       C  
ATOM    531  CE  LYS A  70       1.531  -3.838 -13.758  1.00 43.69           C  
ANISOU  531  CE  LYS A  70     4869   7262   4466   -111    443   -367       C  
ATOM    532  NZ  LYS A  70       0.924  -4.597 -12.637  1.00 53.63           N  
ANISOU  532  NZ  LYS A  70     7335   5788   7253  -1409    568    404       N  
ATOM    533  N   GLU A  71       4.974  -5.212 -19.528  1.00 24.34           N  
ANISOU  533  N   GLU A  71     2875   3390   2982     60  -1188   -608       N  
ATOM    534  CA  GLU A  71       5.313  -5.879 -20.809  1.00 23.44           C  
ANISOU  534  CA  GLU A  71     2761   2879   3265   -222    246      8       C  
ATOM    535  C   GLU A  71       6.824  -6.003 -20.989  1.00 27.09           C  
ANISOU  535  C   GLU A  71     2753   3217   4322   -242    -55   -311       C  
ATOM    536  O   GLU A  71       7.334  -7.080 -21.347  1.00 24.76           O  
ANISOU  536  O   GLU A  71     3491   3143   2774   -631   -785  -1025       O  
ATOM    537  CB  GLU A  71       4.720  -5.070 -21.956  1.00 29.57           C  
ANISOU  537  CB  GLU A  71     3871   3517   3845    714   -486    -47       C  
ATOM    538  CG  GLU A  71       4.114  -5.796 -23.135  1.00 42.79           C  
ANISOU  538  CG  GLU A  71     6728   4663   4867    164  -1335   -284       C  
ATOM    539  CD  GLU A  71       3.412  -4.807 -24.108  1.00 53.97           C  
ANISOU  539  CD  GLU A  71     7463   8348   4692   2629  -1540   -660       C  
ATOM    540  OE1 GLU A  71       2.673  -3.875 -23.641  1.00 45.41           O  
ANISOU  540  OE1 GLU A  71     6725   6791   3738   1391  -1202  -1045       O  
ATOM    541  OE2 GLU A  71       3.605  -4.959 -25.351  1.00 63.19           O  
ANISOU  541  OE2 GLU A  71    10724   7881   5403    947   1231  -2681       O  
ATOM    542  N   THR A  72       7.542  -4.912 -20.724  1.00 26.41           N  
ANISOU  542  N   THR A  72     2868   3313   3852   -317    -21   -373       N  
ATOM    543  CA  THR A  72       9.014  -4.914 -20.892  1.00 24.99           C  
ANISOU  543  CA  THR A  72     2752   3166   3577    -99   -253   -466       C  
ATOM    544  C   THR A  72       9.633  -5.860 -19.881  1.00 23.65           C  
ANISOU  544  C   THR A  72     2571   3405   3008   -251    130   -383       C  
ATOM    545  O   THR A  72      10.512  -6.671 -20.206  1.00 21.35           O  
ANISOU  545  O   THR A  72     2069   3284   2756   -474   -190   -479       O  
ATOM    546  CB  THR A  72       9.582  -3.482 -20.737  1.00 30.01           C  
ANISOU  546  CB  THR A  72     2994   3591   4816   -640   -362    408       C  
ATOM    547  OG1 THR A  72       9.045  -2.640 -21.791  1.00 29.78           O  
ANISOU  547  OG1 THR A  72     4039   4065   3208    165   -633   -133       O  
ATOM    548  CG2 THR A  72      11.150  -3.470 -20.758  1.00 25.08           C  
ANISOU  548  CG2 THR A  72     3045   2523   3961   -876  -1090   -867       C  
ATOM    549  N   ILE A  73       9.174  -5.786 -18.632  1.00 20.41           N  
ANISOU  549  N   ILE A  73     2021   2768   2963   -319    -15    -93       N  
ATOM    550  CA  ILE A  73       9.712  -6.697 -17.610  1.00 20.94           C  
ANISOU  550  CA  ILE A  73     2184   2585   3184   -484   -366   -114       C  
ATOM    551  C   ILE A  73       9.503  -8.191 -17.978  1.00 23.28           C  
ANISOU  551  C   ILE A  73     2551   2809   3483    -68   -490   -849       C  
ATOM    552  O   ILE A  73      10.417  -9.058 -17.827  1.00 18.74           O  
ANISOU  552  O   ILE A  73     1787   2642   2689   -527   -238   -914       O  
ATOM    553  CB  ILE A  73       9.125  -6.355 -16.231  1.00 19.89           C  
ANISOU  553  CB  ILE A  73     2249   2501   2805   -167   -412   -407       C  
ATOM    554  CG1 ILE A  73       9.671  -4.996 -15.773  1.00 18.76           C  
ANISOU  554  CG1 ILE A  73     2089   2550   2486   -163    -88   -469       C  
ATOM    555  CG2 ILE A  73       9.432  -7.425 -15.173  1.00 21.80           C  
ANISOU  555  CG2 ILE A  73     3027   2094   3162   -279    352    -28       C  
ATOM    556  CD1 ILE A  73       8.834  -4.347 -14.725  1.00 19.34           C  
ANISOU  556  CD1 ILE A  73     2356   2647   2345   -247    107   -381       C  
ATOM    557  N   ASN A  74       8.302  -8.492 -18.465  1.00 21.09           N  
ANISOU  557  N   ASN A  74     2466   2721   2824     35   -172  -1045       N  
ATOM    558  CA  ASN A  74       7.992  -9.843 -18.851  1.00 21.87           C  
ANISOU  558  CA  ASN A  74     2810   2515   2982   -147   -284   -495       C  
ATOM    559  C   ASN A  74       8.905 -10.282 -19.999  1.00 19.81           C  
ANISOU  559  C   ASN A  74     1931   2520   3075   -266   -213   -356       C  
ATOM    560  O   ASN A  74       9.393 -11.416 -19.992  1.00 22.22           O  
ANISOU  560  O   ASN A  74     2949   2849   2643    242   -587  -1123       O  
ATOM    561  CB  ASN A  74       6.526  -9.961 -19.278  1.00 24.59           C  
ANISOU  561  CB  ASN A  74     2530   3292   3521   -257    -50   -541       C  
ATOM    562  CG  ASN A  74       5.570  -9.787 -18.135  1.00 26.26           C  
ANISOU  562  CG  ASN A  74     2919   3890   3165   -285    -77   -224       C  
ATOM    563  OD1 ASN A  74       5.900 -10.126 -17.002  1.00 26.93           O  
ANISOU  563  OD1 ASN A  74     2843   3817   3570   -898   -296    -29       O  
ATOM    564  ND2 ASN A  74       4.366  -9.266 -18.418  1.00 26.49           N  
ANISOU  564  ND2 ASN A  74     3083   4075   2907   -154   -495  -1013       N  
ATOM    565  N   GLU A  75       9.144  -9.391 -20.971  1.00 20.34           N  
ANISOU  565  N   GLU A  75     2362   2622   2743   -102   -343   -451       N  
ATOM    566  CA  GLU A  75       9.989  -9.726 -22.125  1.00 21.87           C  
ANISOU  566  CA  GLU A  75     2667   2829   2811   -618   -393   -768       C  
ATOM    567  C   GLU A  75      11.413  -9.977 -21.699  1.00 20.76           C  
ANISOU  567  C   GLU A  75     3015   2518   2354    361   -372   -716       C  
ATOM    568  O   GLU A  75      12.015 -10.975 -22.050  1.00 20.47           O  
ANISOU  568  O   GLU A  75     3302   2329   2146    427   -494   -632       O  
ATOM    569  CB  GLU A  75       9.971  -8.628 -23.203  1.00 26.62           C  
ANISOU  569  CB  GLU A  75     2979   3429   3705     67   -675   -103       C  
ATOM    570  CG  GLU A  75       8.641  -8.560 -23.925  1.00 33.89           C  
ANISOU  570  CG  GLU A  75     3914   4683   4278   -128  -1281   -573       C  
ATOM    571  CD  GLU A  75       8.585  -7.488 -24.983  1.00 43.23           C  
ANISOU  571  CD  GLU A  75     7176   4687   4562  -1015  -1161    -37       C  
ATOM    572  OE1 GLU A  75       9.057  -6.363 -24.753  1.00 44.00           O  
ANISOU  572  OE1 GLU A  75     6405   4439   5871  -1158  -1934   1401       O  
ATOM    573  OE2 GLU A  75       8.047  -7.788 -26.056  1.00 54.89           O  
ANISOU  573  OE2 GLU A  75     7125   8195   5536  -1204  -2870   1577       O  
ATOM    574  N   GLU A  76      11.945  -9.067 -20.906  1.00 21.56           N  
ANISOU  574  N   GLU A  76     2801   2666   2721   -301   -656   -415       N  
ATOM    575  CA  GLU A  76      13.299  -9.218 -20.398  1.00 21.08           C  
ANISOU  575  CA  GLU A  76     2849   2704   2453     96   -465   -508       C  
ATOM    576  C   GLU A  76      13.456 -10.457 -19.500  1.00 18.22           C  
ANISOU  576  C   GLU A  76     2221   2537   2162   -168   -741   -580       C  
ATOM    577  O   GLU A  76      14.450 -11.171 -19.609  1.00 22.62           O  
ANISOU  577  O   GLU A  76     3367   2393   2833    352   -639   -134       O  
ATOM    578  CB  GLU A  76      13.683  -7.931 -19.659  1.00 21.81           C  
ANISOU  578  CB  GLU A  76     2809   2487   2988   -244   -294   -480       C  
ATOM    579  CG  GLU A  76      13.819  -6.740 -20.596  1.00 21.61           C  
ANISOU  579  CG  GLU A  76     2367   3001   2843   -168   -706   -328       C  
ATOM    580  CD  GLU A  76      14.935  -6.888 -21.628  1.00 29.87           C  
ANISOU  580  CD  GLU A  76     4189   4074   3086    559    140   -181       C  
ATOM    581  OE1 GLU A  76      15.982  -7.552 -21.384  1.00 28.70           O  
ANISOU  581  OE1 GLU A  76     3287   3934   3680   -167   -279   -568       O  
ATOM    582  OE2 GLU A  76      14.784  -6.294 -22.706  1.00 39.60           O  
ANISOU  582  OE2 GLU A  76     5865   5748   3433    948    122    322       O  
ATOM    583  N   ALA A  77      12.479 -10.720 -18.637  1.00 18.43           N  
ANISOU  583  N   ALA A  77     2721   2004   2276   -246   -705   -511       N  
ATOM    584  CA  ALA A  77      12.516 -11.870 -17.765  1.00 19.16           C  
ANISOU  584  CA  ALA A  77     2225   2349   2705    -45   -620   -204       C  
ATOM    585  C   ALA A  77      12.488 -13.202 -18.569  1.00 20.52           C  
ANISOU  585  C   ALA A  77     3033   2733   2030    446   -648   -372       C  
ATOM    586  O   ALA A  77      13.224 -14.112 -18.264  1.00 20.93           O  
ANISOU  586  O   ALA A  77     2510   1988   3455     96   -195  -1136       O  
ATOM    587  CB  ALA A  77      11.364 -11.824 -16.758  1.00 21.11           C  
ANISOU  587  CB  ALA A  77     2485   2603   2933    -34   -376   -194       C  
ATOM    588  N   ALA A  78      11.614 -13.292 -19.563  1.00 22.22           N  
ANISOU  588  N   ALA A  78     2979   2710   2754   -411   -830   -922       N  
ATOM    589  CA  ALA A  78      11.551 -14.444 -20.445  1.00 22.84           C  
ANISOU  589  CA  ALA A  78     3403   2247   3027    534   -566   -627       C  
ATOM    590  C   ALA A  78      12.902 -14.717 -21.194  1.00 22.67           C  
ANISOU  590  C   ALA A  78     3080   2915   2617   -261   -551    -52       C  
ATOM    591  O   ALA A  78      13.398 -15.857 -21.214  1.00 26.42           O  
ANISOU  591  O   ALA A  78     2868   3212   3955   -159  -1086   -670       O  
ATOM    592  CB  ALA A  78      10.377 -14.299 -21.422  1.00 23.07           C  
ANISOU  592  CB  ALA A  78     2867   2399   3498   -271   -646   -981       C  
ATOM    593  N   GLU A  79      13.528 -13.678 -21.738  1.00 20.50           N  
ANISOU  593  N   GLU A  79     2778   2756   2254     44   -248   -145       N  
ATOM    594  CA  GLU A  79      14.841 -13.804 -22.368  1.00 23.13           C  
ANISOU  594  CA  GLU A  79     3160   2509   3117    644   -293   -607       C  
ATOM    595  C   GLU A  79      15.932 -14.191 -21.364  1.00 23.35           C  
ANISOU  595  C   GLU A  79     3176   2970   2726    302   -488  -1025       C  
ATOM    596  O   GLU A  79      16.825 -14.956 -21.677  1.00 21.69           O  
ANISOU  596  O   GLU A  79     3567   2469   2205     71   -423  -1049       O  
ATOM    597  CB  GLU A  79      15.197 -12.491 -23.082  1.00 25.38           C  
ANISOU  597  CB  GLU A  79     3655   3244   2744   -145     61   -483       C  
ATOM    598  CG  GLU A  79      16.445 -12.538 -23.910  1.00 32.48           C  
ANISOU  598  CG  GLU A  79     4521   4723   3094   -143    268   -908       C  
ATOM    599  CD  GLU A  79      16.281 -13.377 -25.178  1.00 32.16           C  
ANISOU  599  CD  GLU A  79     4609   3523   4086   -760    924  -1557       C  
ATOM    600  OE1 GLU A  79      15.230 -13.995 -25.426  1.00 35.97           O  
ANISOU  600  OE1 GLU A  79     4207   5783   3675   -279   -684  -1154       O  
ATOM    601  OE2 GLU A  79      17.221 -13.407 -25.933  1.00 40.48           O  
ANISOU  601  OE2 GLU A  79     5525   4591   5264    264   1876   -751       O  
ATOM    602  N   TRP A  80      15.874 -13.635 -20.163  1.00 22.97           N  
ANISOU  602  N   TRP A  80     3235   3567   1925    460   -592   -380       N  
ATOM    603  CA  TRP A  80      16.802 -14.052 -19.094  1.00 19.07           C  
ANISOU  603  CA  TRP A  80     2264   2745   2236    739    124     67       C  
ATOM    604  C   TRP A  80      16.722 -15.556 -18.893  1.00 17.87           C  
ANISOU  604  C   TRP A  80     2709   2652   1429    140    227   -948       C  
ATOM    605  O   TRP A  80      17.750 -16.241 -18.900  1.00 22.37           O  
ANISOU  605  O   TRP A  80     2897   2382   3219    -99   -364   -886       O  
ATOM    606  CB  TRP A  80      16.482 -13.341 -17.770  1.00 21.43           C  
ANISOU  606  CB  TRP A  80     3011   2567   2564    -35   -528   -556       C  
ATOM    607  CG  TRP A  80      17.390 -13.812 -16.631  1.00 22.78           C  
ANISOU  607  CG  TRP A  80     3046   3445   2164   -171     -7   -328       C  
ATOM    608  CD1 TRP A  80      17.196 -14.896 -15.824  1.00 20.41           C  
ANISOU  608  CD1 TRP A  80     3085   2498   2169    603    159   -878       C  
ATOM    609  CD2 TRP A  80      18.672 -13.258 -16.255  1.00 23.24           C  
ANISOU  609  CD2 TRP A  80     3147   2863   2816    278   -385   -953       C  
ATOM    610  NE1 TRP A  80      18.233 -15.013 -14.939  1.00 20.68           N  
ANISOU  610  NE1 TRP A  80     3238   2549   2067    621    129   -148       N  
ATOM    611  CE2 TRP A  80      19.163 -14.043 -15.189  1.00 22.06           C  
ANISOU  611  CE2 TRP A  80     2948   2529   2905    223   -243   -513       C  
ATOM    612  CE3 TRP A  80      19.446 -12.179 -16.725  1.00 19.38           C  
ANISOU  612  CE3 TRP A  80     2582   2597   2182    574   -111   -802       C  
ATOM    613  CZ2 TRP A  80      20.384 -13.772 -14.549  1.00 20.70           C  
ANISOU  613  CZ2 TRP A  80     2959   2517   2389    490   -206   -757       C  
ATOM    614  CZ3 TRP A  80      20.662 -11.910 -16.117  1.00 21.95           C  
ANISOU  614  CZ3 TRP A  80     2507   2139   3691    407   -304   -403       C  
ATOM    615  CH2 TRP A  80      21.123 -12.696 -15.028  1.00 21.30           C  
ANISOU  615  CH2 TRP A  80     3064   2691   2335    779    476   -895       C  
ATOM    616  N   ASP A  81      15.516 -16.076 -18.695  1.00 21.54           N  
ANISOU  616  N   ASP A  81     2739   2777   2668     -8   -201   -684       N  
ATOM    617  CA  ASP A  81      15.342 -17.525 -18.430  1.00 25.84           C  
ANISOU  617  CA  ASP A  81     3363   3044   3411   -552     24   -860       C  
ATOM    618  C   ASP A  81      15.867 -18.366 -19.567  1.00 26.39           C  
ANISOU  618  C   ASP A  81     3698   3153   3174   -126   -611  -1091       C  
ATOM    619  O   ASP A  81      16.544 -19.369 -19.346  1.00 30.20           O  
ANISOU  619  O   ASP A  81     4427   3107   3940    158   -416  -1950       O  
ATOM    620  CB  ASP A  81      13.872 -17.857 -18.130  1.00 26.94           C  
ANISOU  620  CB  ASP A  81     3124   3125   3986   -342   -578   -949       C  
ATOM    621  CG  ASP A  81      13.450 -17.384 -16.734  1.00 31.32           C  
ANISOU  621  CG  ASP A  81     3567   4671   3659    242     71   -309       C  
ATOM    622  OD1 ASP A  81      14.335 -17.052 -15.924  1.00 31.65           O  
ANISOU  622  OD1 ASP A  81     5397   3216   3410     -5    153   -787       O  
ATOM    623  OD2 ASP A  81      12.251 -17.301 -16.450  1.00 31.76           O  
ANISOU  623  OD2 ASP A  81     3247   4746   4074  -1192   -150  -2017       O  
ATOM    624  N   ARG A  82      15.586 -17.935 -20.780  1.00 29.45           N  
ANISOU  624  N   ARG A  82     4563   3055   3569    372    -51   -451       N  
ATOM    625  CA  ARG A  82      15.994 -18.668 -21.995  1.00 30.98           C  
ANISOU  625  CA  ARG A  82     4173   4055   3539    531   -358   -726       C  
ATOM    626  C   ARG A  82      17.539 -18.708 -22.105  1.00 32.44           C  
ANISOU  626  C   ARG A  82     4437   3047   4839    665    326  -1091       C  
ATOM    627  O   ARG A  82      18.096 -19.672 -22.571  1.00 33.04           O  
ANISOU  627  O   ARG A  82     4786   3455   4311   1321   -902  -1402       O  
ATOM    628  CB  ARG A  82      15.335 -17.958 -23.197  1.00 32.23           C  
ANISOU  628  CB  ARG A  82     4756   4456   3030   -309     58   -183       C  
ATOM    629  CG  ARG A  82      15.147 -18.752 -24.462  1.00 36.69           C  
ANISOU  629  CG  ARG A  82     6193   4480   3266    696   -251   -210       C  
ATOM    630  CD  ARG A  82      14.589 -17.844 -25.559  1.00 33.77           C  
ANISOU  630  CD  ARG A  82     3679   5091   4059    519  -1640   -322       C  
ATOM    631  NE  ARG A  82      15.522 -16.768 -25.934  1.00 41.25           N  
ANISOU  631  NE  ARG A  82     6006   4417   5247   -253   -305  -1500       N  
ATOM    632  CZ  ARG A  82      16.628 -16.912 -26.682  1.00 47.71           C  
ANISOU  632  CZ  ARG A  82     6513   5006   6608   -795    230  -1431       C  
ATOM    633  NH1 ARG A  82      17.007 -18.091 -27.153  1.00 50.82           N  
ANISOU  633  NH1 ARG A  82     6887   6809   5612   1334   1784   -526       N  
ATOM    634  NH2 ARG A  82      17.391 -15.869 -26.962  1.00 43.77           N  
ANISOU  634  NH2 ARG A  82     7080   5044   4506     59   1000    262       N  
ATOM    635  N   LEU A  83      18.221 -17.674 -21.606  1.00 28.37           N  
ANISOU  635  N   LEU A  83     3698   4240   2839    283     80   -936       N  
ATOM    636  CA  LEU A  83      19.667 -17.549 -21.686  1.00 24.74           C  
ANISOU  636  CA  LEU A  83     3682   3258   2459   1606    -52   -589       C  
ATOM    637  C   LEU A  83      20.420 -18.036 -20.421  1.00 29.57           C  
ANISOU  637  C   LEU A  83     4237   4091   2907    665   -415    152       C  
ATOM    638  O   LEU A  83      21.654 -17.924 -20.335  1.00 29.11           O  
ANISOU  638  O   LEU A  83     4954   3498   2606   1507   -405   -469       O  
ATOM    639  CB  LEU A  83      20.062 -16.106 -22.008  1.00 27.96           C  
ANISOU  639  CB  LEU A  83     4144   3910   2568    511    -85   -668       C  
ATOM    640  CG  LEU A  83      19.629 -15.524 -23.356  1.00 27.62           C  
ANISOU  640  CG  LEU A  83     3408   3755   3330    900   -229   -182       C  
ATOM    641  CD1 LEU A  83      20.035 -14.068 -23.447  1.00 31.82           C  
ANISOU  641  CD1 LEU A  83     3956   4566   3565   -101    301   -340       C  
ATOM    642  CD2 LEU A  83      20.200 -16.343 -24.515  1.00 31.01           C  
ANISOU  642  CD2 LEU A  83     4098   4810   2872    908    381    351       C  
ATOM    643  N   HIS A  84      19.657 -18.567 -19.467  1.00 24.92           N  
ANISOU  643  N   HIS A  84     3614   3386   2466   1549    273  -1026       N  
ATOM    644  CA  HIS A  84      20.174 -19.133 -18.213  1.00 28.17           C  
ANISOU  644  CA  HIS A  84     3955   3495   3253    525   -198   -764       C  
ATOM    645  C   HIS A  84      19.459 -20.444 -18.049  1.00 32.89           C  
ANISOU  645  C   HIS A  84     4659   3428   4408    684    903    -27       C  
ATOM    646  O   HIS A  84      18.405 -20.531 -17.383  1.00 31.07           O  
ANISOU  646  O   HIS A  84     4398   3400   4006    511    717  -1063       O  
ATOM    647  CB  HIS A  84      19.908 -18.173 -17.053  1.00 29.87           C  
ANISOU  647  CB  HIS A  84     3792   4598   2956    448   -941  -1394       C  
ATOM    648  CG  HIS A  84      20.704 -16.914 -17.172  1.00 29.51           C  
ANISOU  648  CG  HIS A  84     3997   4773   2441    346    129   -680       C  
ATOM    649  ND1 HIS A  84      20.278 -15.825 -17.905  1.00 30.60           N  
ANISOU  649  ND1 HIS A  84     4416   3980   3227   -183   -572  -1431       N  
ATOM    650  CD2 HIS A  84      21.953 -16.615 -16.746  1.00 30.40           C  
ANISOU  650  CD2 HIS A  84     3882   4002   3665    300    251  -1139       C  
ATOM    651  CE1 HIS A  84      21.212 -14.896 -17.886  1.00 27.13           C  
ANISOU  651  CE1 HIS A  84     4169   3502   2635   -311    717   -835       C  
ATOM    652  NE2 HIS A  84      22.241 -15.355 -17.195  1.00 33.48           N  
ANISOU  652  NE2 HIS A  84     4451   3785   4483     84    210   -733       N  
ATOM    653  N   PRO A  85      19.991 -21.471 -18.725  1.00 29.83           N  
ANISOU  653  N   PRO A  85     3465   3842   4026    197    691   -458       N  
ATOM    654  CA  PRO A  85      19.355 -22.772 -18.674  1.00 31.55           C  
ANISOU  654  CA  PRO A  85     4403   3574   4008     20   1043    397       C  
ATOM    655  C   PRO A  85      19.205 -23.263 -17.193  1.00 31.90           C  
ANISOU  655  C   PRO A  85     3871   4778   3470   -498   -335     55       C  
ATOM    656  O   PRO A  85      20.138 -23.164 -16.409  1.00 31.02           O  
ANISOU  656  O   PRO A  85     4587   3839   3357   1019  -1082   -829       O  
ATOM    657  CB  PRO A  85      20.287 -23.661 -19.504  1.00 29.22           C  
ANISOU  657  CB  PRO A  85     4197   3204   3697   -339    459   -318       C  
ATOM    658  CG  PRO A  85      21.190 -22.773 -20.277  1.00 31.47           C  
ANISOU  658  CG  PRO A  85     5387   3234   3336   -193    667   -275       C  
ATOM    659  CD  PRO A  85      21.149 -21.413 -19.647  1.00 27.00           C  
ANISOU  659  CD  PRO A  85     3936   3782   2539    637    239   -697       C  
ATOM    660  N   VAL A  86      18.038 -23.788 -16.838  1.00 32.88           N  
ANISOU  660  N   VAL A  86     3877   3975   4641   -111    260    348       N  
ATOM    661  CA  VAL A  86      17.753 -24.213 -15.439  1.00 38.41           C  
ANISOU  661  CA  VAL A  86     4776   4575   5243    187    454     -6       C  
ATOM    662  C   VAL A  86      18.593 -25.430 -14.958  1.00 41.11           C  
ANISOU  662  C   VAL A  86     5577   4119   5923    888   -391   -729       C  
ATOM    663  O   VAL A  86      19.088 -26.225 -15.779  1.00 34.16           O  
ANISOU  663  O   VAL A  86     4897   3022   5061   1171    684    522       O  
ATOM    664  CB  VAL A  86      16.240 -24.534 -15.255  1.00 42.20           C  
ANISOU  664  CB  VAL A  86     4337   5298   6399    750   1294  -1109       C  
ATOM    665  CG1 VAL A  86      15.403 -23.274 -15.437  1.00 40.99           C  
ANISOU  665  CG1 VAL A  86     6165   3950   5459   -180   1305     33       C  
ATOM    666  CG2 VAL A  86      15.760 -25.632 -16.241  1.00 43.81           C  
ANISOU  666  CG2 VAL A  86     4662   6132   5850   -924   1612   -468       C  
ATOM    667  N   ARG A  97      21.116 -21.244  -4.923  1.00 29.83           N  
ANISOU  667  N   ARG A  97     6568   2099   2668    762  -1231   -155       N  
ATOM    668  CA  ARG A  97      20.202 -21.270  -6.120  1.00 26.61           C  
ANISOU  668  CA  ARG A  97     3248   2841   4021   -461   -627   -144       C  
ATOM    669  C   ARG A  97      20.409 -19.993  -6.960  1.00 26.76           C  
ANISOU  669  C   ARG A  97     4103   2790   3272    627   -444     22       C  
ATOM    670  O   ARG A  97      20.539 -18.913  -6.395  1.00 29.98           O  
ANISOU  670  O   ARG A  97     5226   2652   3511     60    191    396       O  
ATOM    671  CB  ARG A  97      18.710 -21.474  -5.783  1.00 28.28           C  
ANISOU  671  CB  ARG A  97     4232   3270   3243   -166    917     23       C  
ATOM    672  CG  ARG A  97      17.846 -20.244  -5.438  1.00 29.39           C  
ANISOU  672  CG  ARG A  97     3328   3356   4481     95    451    397       C  
ATOM    673  CD  ARG A  97      16.428 -20.644  -5.016  1.00 35.48           C  
ANISOU  673  CD  ARG A  97     3991   4156   5331   -318   1015    122       C  
ATOM    674  NE  ARG A  97      15.572 -19.474  -4.727  1.00 32.97           N  
ANISOU  674  NE  ARG A  97     4207   4287   4033    251   -430    306       N  
ATOM    675  CZ  ARG A  97      14.915 -18.739  -5.642  1.00 24.74           C  
ANISOU  675  CZ  ARG A  97     2902   3152   3343    218     89    -79       C  
ATOM    676  NH1 ARG A  97      14.960 -19.041  -6.945  1.00 26.22           N  
ANISOU  676  NH1 ARG A  97     4268   2765   2927   -262    922    524       N  
ATOM    677  NH2 ARG A  97      14.209 -17.679  -5.246  1.00 23.29           N  
ANISOU  677  NH2 ARG A  97     2923   2998   2925     45    318   -144       N  
ATOM    678  N   GLU A  98      20.470 -20.136  -8.284  1.00 27.11           N  
ANISOU  678  N   GLU A  98     4157   2840   3304    499    256    761       N  
ATOM    679  CA  GLU A  98      20.675 -19.014  -9.197  1.00 25.95           C  
ANISOU  679  CA  GLU A  98     3991   3485   2381     91   -312    843       C  
ATOM    680  C   GLU A  98      19.310 -18.397  -9.545  1.00 23.18           C  
ANISOU  680  C   GLU A  98     3353   2878   2575    -21    934    254       C  
ATOM    681  O   GLU A  98      18.313 -19.115  -9.718  1.00 24.84           O  
ANISOU  681  O   GLU A  98     3991   2333   3114    -59    441   1377       O  
ATOM    682  CB  GLU A  98      21.379 -19.501 -10.487  1.00 32.60           C  
ANISOU  682  CB  GLU A  98     4207   3949   4229    665    533    809       C  
ATOM    683  CG  GLU A  98      22.786 -20.087 -10.295  1.00 39.23           C  
ANISOU  683  CG  GLU A  98     4450   4351   6104    439    278    459       C  
ATOM    684  CD  GLU A  98      23.930 -19.094 -10.432  1.00 39.28           C  
ANISOU  684  CD  GLU A  98     4748   5175   4999   -255    753   1060       C  
ATOM    685  OE1 GLU A  98      23.731 -17.983 -10.954  1.00 45.64           O  
ANISOU  685  OE1 GLU A  98     5840   6246   5255    -32  -1440   1023       O  
ATOM    686  OE2 GLU A  98      25.060 -19.419 -10.016  1.00 48.14           O  
ANISOU  686  OE2 GLU A  98     6177   6734   5379    537    544   1658       O  
ATOM    687  N   PRO A  99      19.252 -17.062  -9.698  1.00 20.33           N  
ANISOU  687  N   PRO A  99     2799   2944   1979    164    828   -467       N  
ATOM    688  CA  PRO A  99      17.958 -16.422  -9.919  1.00 23.09           C  
ANISOU  688  CA  PRO A  99     2694   3117   2958     33    392   -224       C  
ATOM    689  C   PRO A  99      17.346 -16.650 -11.285  1.00 20.65           C  
ANISOU  689  C   PRO A  99     2602   2619   2626    308    157    195       C  
ATOM    690  O   PRO A  99      18.046 -16.675 -12.288  1.00 24.58           O  
ANISOU  690  O   PRO A  99     2988   3758   2590    255    267    113       O  
ATOM    691  CB  PRO A  99      18.271 -14.919  -9.734  1.00 23.71           C  
ANISOU  691  CB  PRO A  99     2675   3068   3265    318    -13   -356       C  
ATOM    692  CG  PRO A  99      19.686 -14.789 -10.096  1.00 20.65           C  
ANISOU  692  CG  PRO A  99     2967   2786   2091   -142    181    -28       C  
ATOM    693  CD  PRO A  99      20.357 -16.079  -9.702  1.00 20.91           C  
ANISOU  693  CD  PRO A  99     3131   2562   2251    -97    366     -1       C  
ATOM    694  N   ARG A 100      16.034 -16.806 -11.302  1.00 20.16           N  
ANISOU  694  N   ARG A 100     2789   2579   2292     12    503   -365       N  
ATOM    695  CA  ARG A 100      15.252 -16.757 -12.512  1.00 19.76           C  
ANISOU  695  CA  ARG A 100     2831   2029   2645   -143    -86   -637       C  
ATOM    696  C   ARG A 100      14.758 -15.353 -12.803  1.00 18.33           C  
ANISOU  696  C   ARG A 100     2114   2366   2484   -118     74   -136       C  
ATOM    697  O   ARG A 100      14.926 -14.463 -11.978  1.00 19.82           O  
ANISOU  697  O   ARG A 100     3005   2528   1996    240   -153   -105       O  
ATOM    698  CB  ARG A 100      14.050 -17.682 -12.392  1.00 22.05           C  
ANISOU  698  CB  ARG A 100     2387   3500   2489   -354    577    588       C  
ATOM    699  CG  ARG A 100      14.348 -19.064 -11.863  1.00 28.61           C  
ANISOU  699  CG  ARG A 100     3727   3357   3785     -8    571    -45       C  
ATOM    700  CD  ARG A 100      15.429 -19.785 -12.639  1.00 28.51           C  
ANISOU  700  CD  ARG A 100     4371   2999   3462   -351    737   -391       C  
ATOM    701  NE  ARG A 100      15.011 -19.912 -14.018  1.00 30.64           N  
ANISOU  701  NE  ARG A 100     4221   3918   3501   -957     30   -995       N  
ATOM    702  CZ  ARG A 100      15.853 -20.031 -15.050  1.00 33.20           C  
ANISOU  702  CZ  ARG A 100     3835   4573   4204   -246   -208   -866       C  
ATOM    703  NH1 ARG A 100      17.163 -20.028 -14.876  1.00 28.45           N  
ANISOU  703  NH1 ARG A 100     3450   3336   4022    517   -190   -733       N  
ATOM    704  NH2 ARG A 100      15.379 -20.150 -16.281  1.00 33.43           N  
ANISOU  704  NH2 ARG A 100     5628   3286   3788    165   -452   -758       N  
ATOM    705  N   GLY A 101      14.160 -15.146 -13.976  1.00 20.55           N  
ANISOU  705  N   GLY A 101     2573   2523   2710    -97   -663   -613       N  
ATOM    706  CA  GLY A 101      13.583 -13.830 -14.316  1.00 19.88           C  
ANISOU  706  CA  GLY A 101     3202   2245   2106     -4   -450   -575       C  
ATOM    707  C   GLY A 101      12.641 -13.297 -13.216  1.00 21.26           C  
ANISOU  707  C   GLY A 101     2312   2540   3224    -11      6   -120       C  
ATOM    708  O   GLY A 101      12.700 -12.106 -12.856  1.00 19.39           O  
ANISOU  708  O   GLY A 101     2360   2208   2797     46    -37     71       O  
ATOM    709  N   SER A 102      11.780 -14.169 -12.666  1.00 22.05           N  
ANISOU  709  N   SER A 102     2989   2571   2817   -102     75     -2       N  
ATOM    710  CA  SER A 102      10.856 -13.775 -11.593  1.00 22.34           C  
ANISOU  710  CA  SER A 102     2650   2447   3390     51    210     95       C  
ATOM    711  C   SER A 102      11.556 -13.420 -10.279  1.00 20.86           C  
ANISOU  711  C   SER A 102     2415   2693   2815    -20    523     39       C  
ATOM    712  O   SER A 102      11.079 -12.561  -9.511  1.00 22.90           O  
ANISOU  712  O   SER A 102     2714   2951   3033   -419    119   -798       O  
ATOM    713  CB  SER A 102       9.817 -14.869 -11.339  1.00 24.02           C  
ANISOU  713  CB  SER A 102     2702   2795   3629   -283    305     93       C  
ATOM    714  OG  SER A 102      10.488 -16.067 -11.092  1.00 24.86           O  
ANISOU  714  OG  SER A 102     3326   2833   3283   -378    228    210       O  
ATOM    715  N   ASP A 103      12.672 -14.088 -10.022  1.00 18.19           N  
ANISOU  715  N   ASP A 103     2855   1902   2151   -116    423    220       N  
ATOM    716  CA  ASP A 103      13.538 -13.755  -8.911  1.00 20.77           C  
ANISOU  716  CA  ASP A 103     2824   2846   2220   -195    410    -45       C  
ATOM    717  C   ASP A 103      14.189 -12.377  -9.075  1.00 19.54           C  
ANISOU  717  C   ASP A 103     2899   2502   2021    -11     23   -116       C  
ATOM    718  O   ASP A 103      14.199 -11.599  -8.125  1.00 17.13           O  
ANISOU  718  O   ASP A 103     2935   1982   1591   -241   -152     76       O  
ATOM    719  CB  ASP A 103      14.614 -14.814  -8.744  1.00 21.83           C  
ANISOU  719  CB  ASP A 103     2356   3026   2912   -289    110    272       C  
ATOM    720  CG  ASP A 103      14.064 -16.155  -8.366  1.00 22.44           C  
ANISOU  720  CG  ASP A 103     2817   2572   3135    199    523    -27       C  
ATOM    721  OD1 ASP A 103      13.138 -16.203  -7.532  1.00 21.06           O  
ANISOU  721  OD1 ASP A 103     3064   2417   2521   -233    531    473       O  
ATOM    722  OD2 ASP A 103      14.582 -17.171  -8.889  1.00 20.76           O  
ANISOU  722  OD2 ASP A 103     3271   1876   2739   -277    396   -235       O  
ATOM    723  N   ILE A 104      14.702 -12.065 -10.270  1.00 19.24           N  
ANISOU  723  N   ILE A 104     2920   2230   2158   -499    407   -549       N  
ATOM    724  CA  ILE A 104      15.216 -10.705 -10.561  1.00 18.15           C  
ANISOU  724  CA  ILE A 104     2433   2505   1957   -264    208   -137       C  
ATOM    725  C   ILE A 104      14.148  -9.597 -10.389  1.00 16.57           C  
ANISOU  725  C   ILE A 104     2833   2197   1263   -114   -111    423       C  
ATOM    726  O   ILE A 104      14.420  -8.541  -9.812  1.00 17.73           O  
ANISOU  726  O   ILE A 104     2575   2416   1743    -68    499     41       O  
ATOM    727  CB  ILE A 104      15.855 -10.638 -11.943  1.00 16.07           C  
ANISOU  727  CB  ILE A 104     2535   1908   1662   -458     23    250       C  
ATOM    728  CG1 ILE A 104      17.119 -11.510 -11.959  1.00 19.09           C  
ANISOU  728  CG1 ILE A 104     2890   2534   1829   -345     72    304       C  
ATOM    729  CG2 ILE A 104      16.157  -9.175 -12.349  1.00 14.12           C  
ANISOU  729  CG2 ILE A 104     1914   1674   1777   -128     50    126       C  
ATOM    730  CD1 ILE A 104      17.585 -11.960 -13.315  1.00 21.10           C  
ANISOU  730  CD1 ILE A 104     3111   2212   2691   -545    783   -295       C  
ATOM    731  N   ALA A 105      12.934  -9.878 -10.814  1.00 16.00           N  
ANISOU  731  N   ALA A 105     2374   2017   1686   -196    420    176       N  
ATOM    732  CA  ALA A 105      11.837  -8.945 -10.682  1.00 20.75           C  
ANISOU  732  CA  ALA A 105     2754   2402   2725   -104    568   -173       C  
ATOM    733  C   ALA A 105      11.218  -8.915  -9.281  1.00 20.10           C  
ANISOU  733  C   ALA A 105     2699   2704   2233   -380    170    123       C  
ATOM    734  O   ALA A 105      10.266  -8.155  -9.034  1.00 17.87           O  
ANISOU  734  O   ALA A 105     2400   2139   2251   -685      0   -146       O  
ATOM    735  CB  ALA A 105      10.774  -9.226 -11.729  1.00 20.47           C  
ANISOU  735  CB  ALA A 105     2555   2575   2646    111    331     23       C  
ATOM    736  N   GLY A 106      11.751  -9.744  -8.384  1.00 21.18           N  
ANISOU  736  N   GLY A 106     2998   2517   2530   -605    202     51       N  
ATOM    737  CA  GLY A 106      11.280  -9.815  -6.986  1.00 21.19           C  
ANISOU  737  CA  GLY A 106     2939   2635   2476    426    200     67       C  
ATOM    738  C   GLY A 106       9.951 -10.470  -6.668  1.00 24.09           C  
ANISOU  738  C   GLY A 106     2954   3601   2596    251    226     83       C  
ATOM    739  O   GLY A 106       9.511 -10.429  -5.504  1.00 25.02           O  
ANISOU  739  O   GLY A 106     3283   3975   2245     63     94    589       O  
ATOM    740  N   THR A 107       9.268 -11.053  -7.646  1.00 20.07           N  
ANISOU  740  N   THR A 107     3001   2604   2020    -99    668    204       N  
ATOM    741  CA  THR A 107       7.977 -11.674  -7.341  1.00 24.88           C  
ANISOU  741  CA  THR A 107     2825   2790   3836    -83    183    145       C  
ATOM    742  C   THR A 107       8.116 -13.022  -6.606  1.00 22.07           C  
ANISOU  742  C   THR A 107     2610   3241   2531     34    336    442       C  
ATOM    743  O   THR A 107       7.222 -13.442  -5.897  1.00 25.68           O  
ANISOU  743  O   THR A 107     3315   3354   3087    210   1542   -511       O  
ATOM    744  CB  THR A 107       7.094 -11.931  -8.604  1.00 22.58           C  
ANISOU  744  CB  THR A 107     2397   2718   3463   -516    243    812       C  
ATOM    745  OG1 THR A 107       7.807 -12.743  -9.532  1.00 27.24           O  
ANISOU  745  OG1 THR A 107     4111   2956   3282   -735    438    460       O  
ATOM    746  CG2 THR A 107       6.709 -10.688  -9.274  1.00 21.50           C  
ANISOU  746  CG2 THR A 107     2466   3124   2578   -175    264    755       C  
ATOM    747  N   THR A 108       9.217 -13.713  -6.854  1.00 21.61           N  
ANISOU  747  N   THR A 108     2545   2634   3031   -149    312     -7       N  
ATOM    748  CA  THR A 108       9.452 -15.040  -6.321  1.00 20.61           C  
ANISOU  748  CA  THR A 108     2805   2395   2630   -699    810     63       C  
ATOM    749  C   THR A 108      10.684 -15.205  -5.466  1.00 20.41           C  
ANISOU  749  C   THR A 108     3317   2115   2321   -148    577   -798       C  
ATOM    750  O   THR A 108      11.002 -16.313  -5.039  1.00 24.86           O  
ANISOU  750  O   THR A 108     3772   2480   3194     15     85     82       O  
ATOM    751  CB  THR A 108       9.577 -16.078  -7.453  1.00 21.18           C  
ANISOU  751  CB  THR A 108     3303   2007   2735   -516    375    114       C  
ATOM    752  OG1 THR A 108      10.596 -15.682  -8.378  1.00 26.32           O  
ANISOU  752  OG1 THR A 108     4316   2534   3148  -1024    563    226       O  
ATOM    753  CG2 THR A 108       8.238 -16.303  -8.170  1.00 24.04           C  
ANISOU  753  CG2 THR A 108     3087   2646   3400   -256    111   1103       C  
ATOM    754  N   SER A 109      11.383 -14.112  -5.184  1.00 21.85           N  
ANISOU  754  N   SER A 109     2590   2430   3282   -422    885      0       N  
ATOM    755  CA  SER A 109      12.550 -14.183  -4.344  1.00 22.59           C  
ANISOU  755  CA  SER A 109     3385   2536   2660   -281    202    451       C  
ATOM    756  C   SER A 109      12.341 -13.397  -3.034  1.00 23.00           C  
ANISOU  756  C   SER A 109     3181   2928   2629    220    810    573       C  
ATOM    757  O   SER A 109      11.529 -12.466  -2.949  1.00 20.21           O  
ANISOU  757  O   SER A 109     3024   2190   2464   -264    339   -262       O  
ATOM    758  CB  SER A 109      13.746 -13.609  -5.086  1.00 25.75           C  
ANISOU  758  CB  SER A 109     3569   3253   2959    -89    906     90       C  
ATOM    759  OG  SER A 109      13.443 -12.292  -5.562  1.00 22.63           O  
ANISOU  759  OG  SER A 109     3012   2908   2675     -6    597   -484       O  
ATOM    760  N   THR A 110      13.102 -13.769  -2.021  1.00 22.41           N  
ANISOU  760  N   THR A 110     3218   2698   2597     57    292   -205       N  
ATOM    761  CA  THR A 110      13.038 -13.103  -0.729  1.00 22.55           C  
ANISOU  761  CA  THR A 110     3056   2992   2518     42    585   -127       C  
ATOM    762  C   THR A 110      14.069 -11.965  -0.733  1.00 21.70           C  
ANISOU  762  C   THR A 110     3015   2598   2630    130    518    -73       C  
ATOM    763  O   THR A 110      14.994 -11.980  -1.511  1.00 18.77           O  
ANISOU  763  O   THR A 110     3007   2338   1784   -339    241     19       O  
ATOM    764  CB  THR A 110      13.361 -14.068   0.437  1.00 19.42           C  
ANISOU  764  CB  THR A 110     2451   2649   2278    142    311   -193       C  
ATOM    765  OG1 THR A 110      14.685 -14.572   0.320  1.00 22.66           O  
ANISOU  765  OG1 THR A 110     2874   2926   2809    764    338    544       O  
ATOM    766  CG2 THR A 110      12.448 -15.230   0.437  1.00 24.52           C  
ANISOU  766  CG2 THR A 110     3189   3107   3017   -203    386    480       C  
ATOM    767  N   LEU A 111      13.935 -11.017   0.173  1.00 22.13           N  
ANISOU  767  N   LEU A 111     3590   2852   1964   -184   1196      3       N  
ATOM    768  CA  LEU A 111      14.935 -10.018   0.358  1.00 19.91           C  
ANISOU  768  CA  LEU A 111     3239   2614   1710    127    -67    -54       C  
ATOM    769  C   LEU A 111      16.251 -10.615   0.713  1.00 20.40           C  
ANISOU  769  C   LEU A 111     3154   2173   2424    169    670   -166       C  
ATOM    770  O   LEU A 111      17.271 -10.165   0.210  1.00 18.94           O  
ANISOU  770  O   LEU A 111     2979   2431   1785   -122    546   -241       O  
ATOM    771  CB  LEU A 111      14.529  -8.990   1.433  1.00 22.38           C  
ANISOU  771  CB  LEU A 111     3584   3218   1699    322    553    151       C  
ATOM    772  CG  LEU A 111      15.517  -7.851   1.722  1.00 24.75           C  
ANISOU  772  CG  LEU A 111     3583   3066   2753    479    152     78       C  
ATOM    773  CD1 LEU A 111      15.867  -6.998   0.497  1.00 26.14           C  
ANISOU  773  CD1 LEU A 111     4242   2985   2706     -8    319   -357       C  
ATOM    774  CD2 LEU A 111      14.877  -6.985   2.798  1.00 25.60           C  
ANISOU  774  CD2 LEU A 111     4519   3217   1988    303     44     65       C  
ATOM    775  N   GLN A 112      16.262 -11.646   1.566  1.00 22.08           N  
ANISOU  775  N   GLN A 112     3304   3063   2022    338    122    172       N  
ATOM    776  CA  GLN A 112      17.557 -12.237   1.883  1.00 26.49           C  
ANISOU  776  CA  GLN A 112     3458   3921   2687    462    129   -276       C  
ATOM    777  C   GLN A 112      18.189 -12.903   0.684  1.00 21.91           C  
ANISOU  777  C   GLN A 112     2916   2915   2493    609     96    208       C  
ATOM    778  O   GLN A 112      19.380 -12.778   0.538  1.00 22.66           O  
ANISOU  778  O   GLN A 112     3095   3209   2303    600    163    261       O  
ATOM    779  CB  GLN A 112      17.532 -13.137   3.116  1.00 31.63           C  
ANISOU  779  CB  GLN A 112     4572   3733   3710    745    248    323       C  
ATOM    780  CG  GLN A 112      17.620 -12.306   4.425  1.00 33.33           C  
ANISOU  780  CG  GLN A 112     4791   4399   3474    174   -356    180       C  
ATOM    781  CD  GLN A 112      18.936 -11.473   4.644  1.00 44.25           C  
ANISOU  781  CD  GLN A 112     6728   5349   4734   -647    111   -101       C  
ATOM    782  OE1 GLN A 112      19.004 -10.671   5.585  1.00 56.69           O  
ANISOU  782  OE1 GLN A 112    10746   6706   4088   1087  -2330   -378       O  
ATOM    783  NE2 GLN A 112      19.975 -11.672   3.797  1.00 55.60           N  
ANISOU  783  NE2 GLN A 112     5529   7913   7684   -252    574    -59       N  
ATOM    784  N   GLU A 113      17.402 -13.557  -0.181  1.00 24.03           N  
ANISOU  784  N   GLU A 113     4010   2941   2178    270     96    653       N  
ATOM    785  CA  GLU A 113      17.950 -14.083  -1.465  1.00 24.41           C  
ANISOU  785  CA  GLU A 113     3467   2750   3055    320    343    -78       C  
ATOM    786  C   GLU A 113      18.563 -12.986  -2.329  1.00 21.39           C  
ANISOU  786  C   GLU A 113     3101   2759   2265    360   -168    -48       C  
ATOM    787  O   GLU A 113      19.686 -13.134  -2.899  1.00 19.29           O  
ANISOU  787  O   GLU A 113     2974   2288   2067   -463   -304    278       O  
ATOM    788  CB  GLU A 113      16.886 -14.861  -2.261  1.00 24.97           C  
ANISOU  788  CB  GLU A 113     3690   3265   2532    -94    670    336       C  
ATOM    789  CG  GLU A 113      16.655 -16.262  -1.681  1.00 26.70           C  
ANISOU  789  CG  GLU A 113     3799   2845   3500    223    766   -146       C  
ATOM    790  CD  GLU A 113      15.420 -16.962  -2.222  1.00 27.40           C  
ANISOU  790  CD  GLU A 113     3448   2763   4198    502    203    393       C  
ATOM    791  OE1 GLU A 113      14.456 -16.299  -2.667  1.00 26.23           O  
ANISOU  791  OE1 GLU A 113     4047   3067   2850    244    -94   1275       O  
ATOM    792  OE2 GLU A 113      15.415 -18.197  -2.212  1.00 28.58           O  
ANISOU  792  OE2 GLU A 113     4357   2538   3964   -637    224   1795       O  
ATOM    793  N   GLN A 114      17.832 -11.888  -2.438  1.00 17.62           N  
ANISOU  793  N   GLN A 114     3143   2192   1359    302    457   -141       N  
ATOM    794  CA  GLN A 114      18.292 -10.750  -3.227  1.00 18.08           C  
ANISOU  794  CA  GLN A 114     2826   2267   1775   -136    397   -149       C  
ATOM    795  C   GLN A 114      19.603 -10.196  -2.696  1.00 20.94           C  
ANISOU  795  C   GLN A 114     2749   3096   2111    239     20     25       C  
ATOM    796  O   GLN A 114      20.541  -9.948  -3.463  1.00 18.95           O  
ANISOU  796  O   GLN A 114     3265   2557   1377     73    -89    -28       O  
ATOM    797  CB  GLN A 114      17.212  -9.663  -3.266  1.00 19.14           C  
ANISOU  797  CB  GLN A 114     3040   1960   2271   -260    672    134       C  
ATOM    798  CG  GLN A 114      15.936 -10.005  -4.020  1.00 20.05           C  
ANISOU  798  CG  GLN A 114     2884   2689   2045    429    432    770       C  
ATOM    799  CD  GLN A 114      14.816  -9.018  -3.752  1.00 22.50           C  
ANISOU  799  CD  GLN A 114     2995   2803   2748    359    568     55       C  
ATOM    800  OE1 GLN A 114      15.075  -7.885  -3.431  1.00 22.07           O  
ANISOU  800  OE1 GLN A 114     3175   2965   2245    218    425    142       O  
ATOM    801  NE2 GLN A 114      13.577  -9.453  -3.883  1.00 21.68           N  
ANISOU  801  NE2 GLN A 114     3134   3170   1933    -42    444     68       N  
ATOM    802  N   ILE A 115      19.678  -9.997  -1.384  1.00 23.07           N  
ANISOU  802  N   ILE A 115     3026   3796   1941    246   -105   -158       N  
ATOM    803  CA  ILE A 115      20.934  -9.554  -0.752  1.00 23.06           C  
ANISOU  803  CA  ILE A 115     3460   3023   2277    163   -115   -117       C  
ATOM    804  C   ILE A 115      22.047 -10.579  -0.982  1.00 21.97           C  
ANISOU  804  C   ILE A 115     3134   3414   1797   -183    -24   -385       C  
ATOM    805  O   ILE A 115      23.200 -10.190  -1.245  1.00 21.59           O  
ANISOU  805  O   ILE A 115     3077   3218   1906     65   -407   -952       O  
ATOM    806  CB  ILE A 115      20.739  -9.310   0.786  1.00 25.48           C  
ANISOU  806  CB  ILE A 115     3420   3737   2522    348   -424   -961       C  
ATOM    807  CG1 ILE A 115      19.767  -8.151   1.055  1.00 24.75           C  
ANISOU  807  CG1 ILE A 115     3723   3068   2613      4   -311  -1187       C  
ATOM    808  CG2 ILE A 115      22.038  -8.906   1.423  1.00 28.26           C  
ANISOU  808  CG2 ILE A 115     3316   3418   4003    829   -727  -1332       C  
ATOM    809  CD1 ILE A 115      19.267  -8.057   2.488  1.00 25.88           C  
ANISOU  809  CD1 ILE A 115     3683   3207   2943     45    536   -311       C  
ATOM    810  N   GLY A 116      21.692 -11.876  -0.899  1.00 21.09           N  
ANISOU  810  N   GLY A 116     3301   3355   1354     40   -259   -828       N  
ATOM    811  CA  GLY A 116      22.618 -12.987  -1.092  1.00 22.02           C  
ANISOU  811  CA  GLY A 116     3045   3212   2108    359     43     52       C  
ATOM    812  C   GLY A 116      23.247 -12.952  -2.510  1.00 24.41           C  
ANISOU  812  C   GLY A 116     3034   4256   1982    814   -100   -215       C  
ATOM    813  O   GLY A 116      24.463 -13.063  -2.678  1.00 20.79           O  
ANISOU  813  O   GLY A 116     3122   3111   1663    707   -224    -35       O  
ATOM    814  N   TRP A 117      22.426 -12.717  -3.516  1.00 21.60           N  
ANISOU  814  N   TRP A 117     3408   2990   1808    674   -332   -316       N  
ATOM    815  CA  TRP A 117      22.938 -12.569  -4.911  1.00 20.10           C  
ANISOU  815  CA  TRP A 117     2086   3178   2373    366     57     24       C  
ATOM    816  C   TRP A 117      23.770 -11.304  -5.084  1.00 16.51           C  
ANISOU  816  C   TRP A 117     2088   2803   1380    354   -668    211       C  
ATOM    817  O   TRP A 117      24.873 -11.326  -5.664  1.00 18.43           O  
ANISOU  817  O   TRP A 117     2654   2483   1862    612    232   -594       O  
ATOM    818  CB  TRP A 117      21.798 -12.570  -5.938  1.00 17.16           C  
ANISOU  818  CB  TRP A 117     2198   2644   1677    203     84   -449       C  
ATOM    819  CG  TRP A 117      21.121 -13.895  -6.044  1.00 18.60           C  
ANISOU  819  CG  TRP A 117     2807   2499   1761    226   -210    254       C  
ATOM    820  CD1 TRP A 117      21.733 -15.128  -6.126  1.00 19.48           C  
ANISOU  820  CD1 TRP A 117     3280   2256   1863    -36   -265   -586       C  
ATOM    821  CD2 TRP A 117      19.707 -14.148  -6.044  1.00 22.20           C  
ANISOU  821  CD2 TRP A 117     3268   2742   2424    113    722   -165       C  
ATOM    822  NE1 TRP A 117      20.794 -16.110  -6.142  1.00 22.87           N  
ANISOU  822  NE1 TRP A 117     3201   2467   3020     92   -369    -97       N  
ATOM    823  CE2 TRP A 117      19.538 -15.553  -6.131  1.00 23.71           C  
ANISOU  823  CE2 TRP A 117     3464   2602   2942    227    784   -247       C  
ATOM    824  CE3 TRP A 117      18.563 -13.329  -6.009  1.00 21.11           C  
ANISOU  824  CE3 TRP A 117     2943   2521   2556    180    527    220       C  
ATOM    825  CZ2 TRP A 117      18.258 -16.158  -6.150  1.00 23.73           C  
ANISOU  825  CZ2 TRP A 117     3446   2927   2643    273   -111    237       C  
ATOM    826  CZ3 TRP A 117      17.314 -13.919  -5.994  1.00 21.02           C  
ANISOU  826  CZ3 TRP A 117     3402   2918   1667   -198  -1147   -272       C  
ATOM    827  CH2 TRP A 117      17.163 -15.329  -6.087  1.00 19.27           C  
ANISOU  827  CH2 TRP A 117     2816   2864   1641    -87     31    174       C  
ATOM    828  N   MET A 118      23.240 -10.203  -4.548  1.00 22.16           N  
ANISOU  828  N   MET A 118     3057   2933   2428    250     -2    182       N  
ATOM    829  CA  MET A 118      23.863  -8.907  -4.715  1.00 18.81           C  
ANISOU  829  CA  MET A 118     2629   2569   1948    165    224   -810       C  
ATOM    830  C   MET A 118      25.240  -8.858  -4.088  1.00 23.69           C  
ANISOU  830  C   MET A 118     2890   3845   2263   -138     61   -389       C  
ATOM    831  O   MET A 118      26.130  -8.177  -4.617  1.00 22.77           O  
ANISOU  831  O   MET A 118     2860   2733   3057   -350   -162   -865       O  
ATOM    832  CB  MET A 118      22.957  -7.820  -4.163  1.00 17.45           C  
ANISOU  832  CB  MET A 118     2425   2144   2062    293    227     -9       C  
ATOM    833  CG  MET A 118      21.818  -7.506  -5.125  1.00 18.06           C  
ANISOU  833  CG  MET A 118     2316   2302   2243     88    147    101       C  
ATOM    834  SD  MET A 118      20.538  -6.441  -4.467  1.00 22.76           S  
ANISOU  834  SD  MET A 118     2785   3144   2719    430     82   -424       S  
ATOM    835  CE  MET A 118      21.397  -4.861  -4.530  1.00 23.89           C  
ANISOU  835  CE  MET A 118     3206   2720   3150    340   -208    -60       C  
ATOM    836  N   THR A 119      25.434  -9.599  -2.992  1.00 23.76           N  
ANISOU  836  N   THR A 119     3206   2946   2874    786   -134  -1077       N  
ATOM    837  CA  THR A 119      26.722  -9.615  -2.260  1.00 25.44           C  
ANISOU  837  CA  THR A 119     3802   3617   2247    956   -591   -472       C  
ATOM    838  C   THR A 119      27.452 -10.940  -2.537  1.00 28.33           C  
ANISOU  838  C   THR A 119     3369   4035   3357   1117   -380  -1024       C  
ATOM    839  O   THR A 119      28.399 -11.308  -1.823  1.00 33.86           O  
ANISOU  839  O   THR A 119     4226   5081   3557   2340   -265  -1141       O  
ATOM    840  CB  THR A 119      26.489  -9.399  -0.733  1.00 22.06           C  
ANISOU  840  CB  THR A 119     2956   3146   2277    457   -201   -175       C  
ATOM    841  OG1 THR A 119      25.644 -10.454  -0.217  1.00 23.51           O  
ANISOU  841  OG1 THR A 119     3723   3134   2075    734   -256   -131       O  
ATOM    842  CG2 THR A 119      25.875  -8.033  -0.471  1.00 23.66           C  
ANISOU  842  CG2 THR A 119     2597   3544   2847    271   -114   -949       C  
ATOM    843  N   HIS A 120      27.023 -11.665  -3.576  1.00 24.94           N  
ANISOU  843  N   HIS A 120     3549   3873   2053   1787   -892   -202       N  
ATOM    844  CA  HIS A 120      27.719 -12.905  -3.955  1.00 27.78           C  
ANISOU  844  CA  HIS A 120     3875   3492   3187   1104   -202   -351       C  
ATOM    845  C   HIS A 120      29.120 -12.553  -4.496  1.00 28.57           C  
ANISOU  845  C   HIS A 120     4870   3919   2065    518    429   -593       C  
ATOM    846  O   HIS A 120      29.405 -11.380  -4.847  1.00 26.80           O  
ANISOU  846  O   HIS A 120     4153   3354   2674    417  -1248   -836       O  
ATOM    847  CB  HIS A 120      26.865 -13.704  -4.920  1.00 27.26           C  
ANISOU  847  CB  HIS A 120     4100   3063   3194    495    272    217       C  
ATOM    848  CG  HIS A 120      27.464 -14.998  -5.364  1.00 32.76           C  
ANISOU  848  CG  HIS A 120     4835   2840   4769    408    -10   -311       C  
ATOM    849  ND1 HIS A 120      28.309 -15.093  -6.457  1.00 34.64           N  
ANISOU  849  ND1 HIS A 120     4035   3799   5326    877   -526     65       N  
ATOM    850  CD2 HIS A 120      27.295 -16.260  -4.903  1.00 35.70           C  
ANISOU  850  CD2 HIS A 120     4410   3813   5339    660   1291    929       C  
ATOM    851  CE1 HIS A 120      28.644 -16.358  -6.639  1.00 38.98           C  
ANISOU  851  CE1 HIS A 120     5908   3664   5237    632    136   -905       C  
ATOM    852  NE2 HIS A 120      28.035 -17.087  -5.715  1.00 41.83           N  
ANISOU  852  NE2 HIS A 120     6742   3159   5991   2007    834    400       N  
ATOM    853  N   ASN A 121      30.014 -13.541  -4.463  1.00 29.26           N  
ANISOU  853  N   ASN A 121     3990   4254   2873    299   -975   -577       N  
ATOM    854  CA  ASN A 121      31.396 -13.367  -4.893  1.00 30.71           C  
ANISOU  854  CA  ASN A 121     4011   4671   2986    303   -937  -1289       C  
ATOM    855  C   ASN A 121      31.715 -14.209  -6.155  1.00 34.42           C  
ANISOU  855  C   ASN A 121     5954   4000   3123   1242    421   -544       C  
ATOM    856  O   ASN A 121      31.880 -15.428  -6.049  1.00 33.51           O  
ANISOU  856  O   ASN A 121     4257   4718   3757   1186   -296     26       O  
ATOM    857  CB  ASN A 121      32.323 -13.755  -3.723  1.00 36.62           C  
ANISOU  857  CB  ASN A 121     4936   5883   3094    134  -1198  -1141       C  
ATOM    858  CG  ASN A 121      31.867 -13.147  -2.372  1.00 34.36           C  
ANISOU  858  CG  ASN A 121     5254   3985   3816     38    573   -220       C  
ATOM    859  OD1 ASN A 121      32.140 -11.968  -2.056  1.00 37.58           O  
ANISOU  859  OD1 ASN A 121     5826   4143   4309    808  -3075   -693       O  
ATOM    860  ND2 ASN A 121      31.176 -13.963  -1.564  1.00 35.89           N  
ANISOU  860  ND2 ASN A 121     3451   5432   4752   -471   1090    164       N  
ATOM    861  N   PRO A 122      31.708 -13.582  -7.362  1.00 25.69           N  
ANISOU  861  N   PRO A 122     3357   3109   3292     31    291   -595       N  
ATOM    862  CA  PRO A 122      31.351 -12.194  -7.707  1.00 29.80           C  
ANISOU  862  CA  PRO A 122     3231   3994   4097    313    166   -291       C  
ATOM    863  C   PRO A 122      29.838 -11.951  -7.723  1.00 24.91           C  
ANISOU  863  C   PRO A 122     2707   3558   3199   -234  -1271  -1328       C  
ATOM    864  O   PRO A 122      29.074 -12.931  -7.757  1.00 22.42           O  
ANISOU  864  O   PRO A 122     2893   3120   2504    293   -349   -765       O  
ATOM    865  CB  PRO A 122      31.927 -12.028  -9.105  1.00 32.44           C  
ANISOU  865  CB  PRO A 122     4421   4212   3694    768    162    546       C  
ATOM    866  CG  PRO A 122      31.705 -13.364  -9.710  1.00 31.80           C  
ANISOU  866  CG  PRO A 122     4620   4410   3053    376     79    444       C  
ATOM    867  CD  PRO A 122      31.989 -14.360  -8.583  1.00 32.95           C  
ANISOU  867  CD  PRO A 122     5226   4577   2715   1048     22      0       C  
ATOM    868  N   PRO A 123      29.420 -10.665  -7.593  1.00 35.12           N  
ANISOU  868  N   PRO A 123     3266   3599   6477   -248   -301   -885       N  
ATOM    869  CA  PRO A 123      27.982 -10.412  -7.511  1.00 30.39           C  
ANISOU  869  CA  PRO A 123     3187   3615   4742   -371  -1041   -226       C  
ATOM    870  C   PRO A 123      27.147 -10.959  -8.650  1.00 28.81           C  
ANISOU  870  C   PRO A 123     3126   4655   3163   -238   -340    158       C  
ATOM    871  O   PRO A 123      27.596 -11.076  -9.796  1.00 24.34           O  
ANISOU  871  O   PRO A 123     1895   4395   2957    418   -272    618       O  
ATOM    872  CB  PRO A 123      27.885  -8.879  -7.484  1.00 31.00           C  
ANISOU  872  CB  PRO A 123     3292   3371   5115   -669    -69  -1216       C  
ATOM    873  CG  PRO A 123      29.116  -8.476  -6.660  1.00 33.18           C  
ANISOU  873  CG  PRO A 123     3686   3726   5192    -66   -718   -238       C  
ATOM    874  CD  PRO A 123      30.196  -9.477  -7.114  1.00 34.80           C  
ANISOU  874  CD  PRO A 123     3374   3970   5877   -149   -306  -1048       C  
ATOM    875  N   ILE A 124      25.914 -11.258  -8.299  1.00 23.45           N  
ANISOU  875  N   ILE A 124     2403   3244   3261    688   -467    654       N  
ATOM    876  CA  ILE A 124      24.897 -11.564  -9.270  1.00 21.96           C  
ANISOU  876  CA  ILE A 124     2119   2948   3276    483   -132    240       C  
ATOM    877  C   ILE A 124      23.962 -10.389  -9.039  1.00 21.30           C  
ANISOU  877  C   ILE A 124     2526   2634   2933    319    197     50       C  
ATOM    878  O   ILE A 124      23.096 -10.436  -8.151  1.00 18.39           O  
ANISOU  878  O   ILE A 124     2459   2257   2268     43   -178   -144       O  
ATOM    879  CB  ILE A 124      24.267 -12.915  -8.944  1.00 26.01           C  
ANISOU  879  CB  ILE A 124     3579   2858   3444    235    322     20       C  
ATOM    880  CG1 ILE A 124      25.336 -14.017  -8.998  1.00 26.65           C  
ANISOU  880  CG1 ILE A 124     3131   3193   3801    302    786    296       C  
ATOM    881  CG2 ILE A 124      23.120 -13.207  -9.879  1.00 28.29           C  
ANISOU  881  CG2 ILE A 124     2858   3787   4103     99    413   -261       C  
ATOM    882  CD1 ILE A 124      24.880 -15.320  -8.370  1.00 30.53           C  
ANISOU  882  CD1 ILE A 124     4424   3106   4068   -129   1200   -282       C  
ATOM    883  N   PRO A 125      24.202  -9.294  -9.769  1.00 19.51           N  
ANISOU  883  N   PRO A 125     1954   2869   2588    439      5     31       N  
ATOM    884  CA  PRO A 125      23.658  -8.014  -9.393  1.00 19.71           C  
ANISOU  884  CA  PRO A 125     2611   2608   2269    224    -57   -186       C  
ATOM    885  C   PRO A 125      22.153  -7.828  -9.774  1.00 15.69           C  
ANISOU  885  C   PRO A 125     2513   1454   1994   -135   -299   -494       C  
ATOM    886  O   PRO A 125      21.811  -7.009 -10.652  1.00 15.93           O  
ANISOU  886  O   PRO A 125     2185   1867   2000   -263    147     36       O  
ATOM    887  CB  PRO A 125      24.580  -7.037 -10.120  1.00 22.12           C  
ANISOU  887  CB  PRO A 125     2349   3165   2889    268    -25    108       C  
ATOM    888  CG  PRO A 125      24.910  -7.773 -11.378  1.00 21.97           C  
ANISOU  888  CG  PRO A 125     3068   3132   2147     94    278    615       C  
ATOM    889  CD  PRO A 125      25.100  -9.181 -10.940  1.00 20.94           C  
ANISOU  889  CD  PRO A 125     2668   2820   2465   -292    -47     -5       C  
ATOM    890  N   VAL A 126      21.272  -8.513  -9.066  1.00 15.29           N  
ANISOU  890  N   VAL A 126     2362   1880   1566    349    279   -382       N  
ATOM    891  CA  VAL A 126      19.849  -8.560  -9.449  1.00 16.35           C  
ANISOU  891  CA  VAL A 126     2570   1853   1788   -345    -57   -206       C  
ATOM    892  C   VAL A 126      19.146  -7.216  -9.397  1.00 15.94           C  
ANISOU  892  C   VAL A 126     2234   2365   1459   -183    154   -103       C  
ATOM    893  O   VAL A 126      18.248  -6.978 -10.187  1.00 15.55           O  
ANISOU  893  O   VAL A 126     2296   1834   1775    -83    -54   -124       O  
ATOM    894  CB  VAL A 126      19.028  -9.602  -8.643  1.00 19.29           C  
ANISOU  894  CB  VAL A 126     3083   2152   2091   -144    436    -63       C  
ATOM    895  CG1 VAL A 126      19.483 -11.009  -8.992  1.00 16.44           C  
ANISOU  895  CG1 VAL A 126     2393   2009   1844   -492   -186   -331       C  
ATOM    896  CG2 VAL A 126      19.133  -9.374  -7.135  1.00 19.92           C  
ANISOU  896  CG2 VAL A 126     3382   2133   2051   -380    438   -420       C  
ATOM    897  N   GLY A 127      19.540  -6.348  -8.457  1.00 16.65           N  
ANISOU  897  N   GLY A 127     2637   2233   1455   -264   -442     36       N  
ATOM    898  CA  GLY A 127      19.053  -4.974  -8.421  1.00 12.93           C  
ANISOU  898  CA  GLY A 127     1754   2186    972    -86    165   -303       C  
ATOM    899  C   GLY A 127      19.423  -4.216  -9.721  1.00 15.74           C  
ANISOU  899  C   GLY A 127     2529   1788   1662     40   -193    222       C  
ATOM    900  O   GLY A 127      18.546  -3.583 -10.343  1.00 15.29           O  
ANISOU  900  O   GLY A 127     2353   2001   1454    708   -231   -545       O  
ATOM    901  N   GLU A 128      20.679  -4.344 -10.161  1.00 15.87           N  
ANISOU  901  N   GLU A 128     2531   2204   1294   -304   -169   -343       N  
ATOM    902  CA  GLU A 128      21.113  -3.647 -11.380  1.00 16.05           C  
ANISOU  902  CA  GLU A 128     2633   1652   1812   -147    407   -494       C  
ATOM    903  C   GLU A 128      20.470  -4.229 -12.621  1.00 15.65           C  
ANISOU  903  C   GLU A 128     1586   2431   1929   -194    219    -65       C  
ATOM    904  O   GLU A 128      20.106  -3.478 -13.539  1.00 15.13           O  
ANISOU  904  O   GLU A 128     2035   1976   1737   -518   -389   -226       O  
ATOM    905  CB  GLU A 128      22.612  -3.572 -11.478  1.00 19.86           C  
ANISOU  905  CB  GLU A 128     2660   2549   2337    146     89    -55       C  
ATOM    906  CG  GLU A 128      23.278  -2.797 -10.347  1.00 25.23           C  
ANISOU  906  CG  GLU A 128     2955   3428   3200     15   -328   -579       C  
ATOM    907  CD  GLU A 128      22.767  -1.334 -10.186  1.00 32.66           C  
ANISOU  907  CD  GLU A 128     4551   3199   4659   -515    -62    151       C  
ATOM    908  OE1 GLU A 128      22.922  -0.532 -11.146  1.00 33.90           O  
ANISOU  908  OE1 GLU A 128     4406   4109   4364    668    903    571       O  
ATOM    909  OE2 GLU A 128      22.207  -0.972  -9.106  1.00 35.07           O  
ANISOU  909  OE2 GLU A 128     4902   3936   4485  -1282    286    626       O  
ATOM    910  N   ILE A 129      20.266  -5.546 -12.639  1.00 15.98           N  
ANISOU  910  N   ILE A 129     2070   2284   1714   -387   -207    -50       N  
ATOM    911  CA  ILE A 129      19.630  -6.185 -13.780  1.00 15.01           C  
ANISOU  911  CA  ILE A 129     1837   2308   1558   -269     24   -229       C  
ATOM    912  C   ILE A 129      18.169  -5.728 -13.917  1.00 15.78           C  
ANISOU  912  C   ILE A 129     2340   1658   1996    253    175     59       C  
ATOM    913  O   ILE A 129      17.702  -5.368 -15.008  1.00 13.94           O  
ANISOU  913  O   ILE A 129     1821   1975   1498    -22    259   -127       O  
ATOM    914  CB  ILE A 129      19.716  -7.722 -13.663  1.00 15.11           C  
ANISOU  914  CB  ILE A 129     1972   2204   1564     99    154   -267       C  
ATOM    915  CG1 ILE A 129      21.202  -8.187 -13.709  1.00 18.01           C  
ANISOU  915  CG1 ILE A 129     2266   2487   2087    214    117   -428       C  
ATOM    916  CG2 ILE A 129      18.922  -8.432 -14.791  1.00 16.16           C  
ANISOU  916  CG2 ILE A 129     2157   2201   1779    396    332   -683       C  
ATOM    917  CD1 ILE A 129      21.452  -9.582 -13.188  1.00 17.24           C  
ANISOU  917  CD1 ILE A 129     2417   2684   1448     30   -525   -409       C  
ATOM    918  N   TYR A 130      17.428  -5.785 -12.818  1.00 15.01           N  
ANISOU  918  N   TYR A 130     2436   1949   1317     48   -245    -98       N  
ATOM    919  CA  TYR A 130      16.037  -5.404 -12.808  1.00 15.31           C  
ANISOU  919  CA  TYR A 130     2197   2127   1493   -300   -142   -154       C  
ATOM    920  C   TYR A 130      15.939  -3.940 -13.162  1.00 14.37           C  
ANISOU  920  C   TYR A 130     1646   2329   1483     58   -197   -273       C  
ATOM    921  O   TYR A 130      15.090  -3.562 -13.908  1.00 11.56           O  
ANISOU  921  O   TYR A 130     1643   1685   1064      7     56   -172       O  
ATOM    922  CB  TYR A 130      15.416  -5.654 -11.433  1.00 15.59           C  
ANISOU  922  CB  TYR A 130     2141   1930   1851   -488    160    -60       C  
ATOM    923  CG  TYR A 130      13.894  -5.506 -11.353  1.00 15.22           C  
ANISOU  923  CG  TYR A 130     2439   1308   2035    -42    221      4       C  
ATOM    924  CD1 TYR A 130      13.051  -5.683 -12.463  1.00 16.32           C  
ANISOU  924  CD1 TYR A 130     1946   2398   1854   -708    467   -135       C  
ATOM    925  CD2 TYR A 130      13.308  -5.187 -10.153  1.00 16.34           C  
ANISOU  925  CD2 TYR A 130     2271   2264   1672   -357    -26   -304       C  
ATOM    926  CE1 TYR A 130      11.667  -5.530 -12.372  1.00 15.88           C  
ANISOU  926  CE1 TYR A 130     2053   2219   1760   -393    -76   -332       C  
ATOM    927  CE2 TYR A 130      11.964  -5.048 -10.039  1.00 14.19           C  
ANISOU  927  CE2 TYR A 130     2112   1609   1668   -175    189   -101       C  
ATOM    928  CZ  TYR A 130      11.131  -5.264 -11.128  1.00 17.39           C  
ANISOU  928  CZ  TYR A 130     2007   2506   2092   -291    199   -351       C  
ATOM    929  OH  TYR A 130       9.788  -5.121 -10.964  1.00 15.81           O  
ANISOU  929  OH  TYR A 130     2009   2175   1820    280    387   -425       O  
ATOM    930  N   LYS A 131      16.846  -3.136 -12.622  1.00 14.50           N  
ANISOU  930  N   LYS A 131     1575   2303   1628    -51   -139   -353       N  
ATOM    931  CA  LYS A 131      16.900  -1.735 -12.914  1.00 17.44           C  
ANISOU  931  CA  LYS A 131     1720   2423   2482    276   -801   -269       C  
ATOM    932  C   LYS A 131      17.091  -1.483 -14.380  1.00 15.20           C  
ANISOU  932  C   LYS A 131     1516   1895   2365   -296   -340   -597       C  
ATOM    933  O   LYS A 131      16.421  -0.613 -14.918  1.00 16.49           O  
ANISOU  933  O   LYS A 131     2287   2192   1784   -328   -325   -305       O  
ATOM    934  CB  LYS A 131      17.960  -0.980 -12.068  1.00 21.18           C  
ANISOU  934  CB  LYS A 131     2295   3207   2544     65  -1667    -35       C  
ATOM    935  CG  LYS A 131      17.752   0.527 -12.147  1.00 28.50           C  
ANISOU  935  CG  LYS A 131     3383   3553   3889   -147   -956   -623       C  
ATOM    936  CD  LYS A 131      18.852   1.430 -11.578  1.00 30.43           C  
ANISOU  936  CD  LYS A 131     3587   4654   3321    -89   -681  -1325       C  
ATOM    937  CE  LYS A 131      19.213   1.089 -10.177  1.00 35.07           C  
ANISOU  937  CE  LYS A 131     3882   5452   3990    789  -1661  -1477       C  
ATOM    938  NZ  LYS A 131      20.169   2.170  -9.706  1.00 43.98           N  
ANISOU  938  NZ  LYS A 131     5370   7169   4168  -1235    123  -2176       N  
ATOM    939  N   ARG A 132      17.950  -2.261 -15.042  1.00 15.59           N  
ANISOU  939  N   ARG A 132     1705   1990   2227   -408     39   -335       N  
ATOM    940  CA AARG A 132      18.118  -2.168 -16.510  0.50 19.04           C  
ANISOU  940  CA AARG A 132     2350   2574   2308    164   -229    242       C  
ATOM    941  CA BARG A 132      18.121  -2.164 -16.506  0.50 19.17           C  
ANISOU  941  CA BARG A 132     2366   2603   2311    153   -247    266       C  
ATOM    942  C   ARG A 132      16.783  -2.402 -17.219  1.00 17.65           C  
ANISOU  942  C   ARG A 132     2204   2177   2324   -233    -10    -95       C  
ATOM    943  O   ARG A 132      16.410  -1.633 -18.132  1.00 17.29           O  
ANISOU  943  O   ARG A 132     1628   2037   2904   -728    171    130       O  
ATOM    944  CB AARG A 132      19.164  -3.193 -17.018  0.50 17.44           C  
ANISOU  944  CB AARG A 132     2342   2014   2268   -369    415   -180       C  
ATOM    945  CB BARG A 132      19.183  -3.181 -17.000  0.50 17.82           C  
ANISOU  945  CB BARG A 132     2362   2084   2322   -340    385   -157       C  
ATOM    946  CG AARG A 132      19.153  -3.426 -18.511  0.50 20.64           C  
ANISOU  946  CG AARG A 132     2943   2597   2300    -51    180    350       C  
ATOM    947  CG BARG A 132      19.290  -3.307 -18.498  0.50 21.70           C  
ANISOU  947  CG BARG A 132     3194   2682   2369     44     66    473       C  
ATOM    948  CD AARG A 132      20.154  -4.500 -18.938  0.50 27.85           C  
ANISOU  948  CD AARG A 132     4105   3099   3375    186    221  -1066       C  
ATOM    949  CD BARG A 132      20.390  -4.274 -18.944  0.50 29.48           C  
ANISOU  949  CD BARG A 132     4215   3269   3714    314    559   -333       C  
ATOM    950  NE AARG A 132      20.215  -4.603 -20.403  0.50 32.04           N  
ANISOU  950  NE AARG A 132     3423   5254   3497    224    885   -340       N  
ATOM    951  NE BARG A 132      20.113  -4.698 -20.320  0.50 33.81           N  
ANISOU  951  NE BARG A 132     4078   4969   3797    262    494    -89       N  
ATOM    952  CZ AARG A 132      19.455  -5.407 -21.152  0.50 29.76           C  
ANISOU  952  CZ AARG A 132     3544   4425   3338    583    765   -633       C  
ATOM    953  CZ BARG A 132      20.612  -4.117 -21.405  0.50 28.74           C  
ANISOU  953  CZ BARG A 132     3674   3559   3684    106    102   -167       C  
ATOM    954  NH1AARG A 132      18.551  -6.246 -20.618  0.50 27.09           N  
ANISOU  954  NH1AARG A 132     1762   5386   3142    490   -556    -69       N  
ATOM    955  NH1BARG A 132      21.459  -3.115 -21.302  0.50 25.50           N  
ANISOU  955  NH1BARG A 132     1607   4675   3404     59    407     53       N  
ATOM    956  NH2AARG A 132      19.607  -5.374 -22.456  0.50 35.58           N  
ANISOU  956  NH2AARG A 132     3597   6601   3320    153   1047   -301       N  
ATOM    957  NH2BARG A 132      20.263  -4.549 -22.586  0.50 30.94           N  
ANISOU  957  NH2BARG A 132     4852   3731   3171    202    596   -647       N  
ATOM    958  N   TRP A 133      16.073  -3.475 -16.843  1.00 15.56           N  
ANISOU  958  N   TRP A 133     2139   2280   1493     23   -302    359       N  
ATOM    959  CA  TRP A 133      14.750  -3.756 -17.443  1.00 17.05           C  
ANISOU  959  CA  TRP A 133     2198   2194   2085   -313   -186    163       C  
ATOM    960  C   TRP A 133      13.768  -2.575 -17.296  1.00 17.07           C  
ANISOU  960  C   TRP A 133     2173   2176   2135   -325   -268    -34       C  
ATOM    961  O   TRP A 133      13.045  -2.184 -18.233  1.00 15.00           O  
ANISOU  961  O   TRP A 133     1933   2009   1757   -174     -3    -11       O  
ATOM    962  CB  TRP A 133      14.118  -5.023 -16.864  1.00 13.90           C  
ANISOU  962  CB  TRP A 133     1680   2131   1467   -255   -642    348       C  
ATOM    963  CG  TRP A 133      14.966  -6.225 -16.995  1.00 17.10           C  
ANISOU  963  CG  TRP A 133     2826   1906   1763   -134    -89   -230       C  
ATOM    964  CD1 TRP A 133      16.147  -6.365 -17.690  1.00 18.41           C  
ANISOU  964  CD1 TRP A 133     2657   2014   2321   -104   -243   -159       C  
ATOM    965  CD2 TRP A 133      14.717  -7.487 -16.383  1.00 14.82           C  
ANISOU  965  CD2 TRP A 133     2230   1614   1785     67   -306   -560       C  
ATOM    966  NE1 TRP A 133      16.652  -7.652 -17.514  1.00 16.52           N  
ANISOU  966  NE1 TRP A 133     2482   2143   1652   -250   -294   -839       N  
ATOM    967  CE2 TRP A 133      15.767  -8.360 -16.754  1.00 14.70           C  
ANISOU  967  CE2 TRP A 133     2419   1913   1251    204      8   -601       C  
ATOM    968  CE3 TRP A 133      13.708  -7.971 -15.549  1.00 15.99           C  
ANISOU  968  CE3 TRP A 133     1897   1749   2428    572     32   -687       C  
ATOM    969  CZ2 TRP A 133      15.822  -9.665 -16.309  1.00 16.04           C  
ANISOU  969  CZ2 TRP A 133     2134   2176   1783    293   -230   -123       C  
ATOM    970  CZ3 TRP A 133      13.767  -9.276 -15.134  1.00 19.14           C  
ANISOU  970  CZ3 TRP A 133     2464   2270   2537     30   -102   -198       C  
ATOM    971  CH2 TRP A 133      14.810 -10.096 -15.514  1.00 13.83           C  
ANISOU  971  CH2 TRP A 133     2085   1667   1502    -29   -762     61       C  
ATOM    972  N   ILE A 134      13.734  -2.028 -16.103  1.00 13.82           N  
ANISOU  972  N   ILE A 134     1485   2037   1729   -252   -195     53       N  
ATOM    973  CA  ILE A 134      12.836  -0.916 -15.801  1.00 15.22           C  
ANISOU  973  CA  ILE A 134     1633   1903   2247   -648   -191   -303       C  
ATOM    974  C   ILE A 134      13.184   0.326 -16.628  1.00 15.00           C  
ANISOU  974  C   ILE A 134     2072   2118   1510     42     70   -162       C  
ATOM    975  O   ILE A 134      12.299   0.986 -17.256  1.00 17.55           O  
ANISOU  975  O   ILE A 134     2388   2259   2019     87    -63   -179       O  
ATOM    976  CB  ILE A 134      12.853  -0.626 -14.289  1.00 13.99           C  
ANISOU  976  CB  ILE A 134     1605   1844   1866     33   -212   -149       C  
ATOM    977  CG1 ILE A 134      12.247  -1.798 -13.480  1.00 16.52           C  
ANISOU  977  CG1 ILE A 134     2066   2018   2191    105     82   -176       C  
ATOM    978  CG2 ILE A 134      12.102   0.671 -13.972  1.00 13.09           C  
ANISOU  978  CG2 ILE A 134     1345   1764   1863   -151    -64    -11       C  
ATOM    979  CD1 ILE A 134      12.610  -1.725 -12.001  1.00 17.89           C  
ANISOU  979  CD1 ILE A 134     2200   2266   2330   -442    441    -73       C  
ATOM    980  N   ILE A 135      14.469   0.633 -16.689  1.00 13.27           N  
ANISOU  980  N   ILE A 135     1965   1684   1391     63   -190    202       N  
ATOM    981  CA  ILE A 135      14.895   1.783 -17.475  1.00 16.77           C  
ANISOU  981  CA  ILE A 135     2468   1825   2077     97     25    443       C  
ATOM    982  C   ILE A 135      14.617   1.583 -18.971  1.00 18.22           C  
ANISOU  982  C   ILE A 135     2583   2097   2242   -147   -177    -69       C  
ATOM    983  O   ILE A 135      14.190   2.522 -19.685  1.00 17.20           O  
ANISOU  983  O   ILE A 135     1902   2232   2399    150   -232   -380       O  
ATOM    984  CB  ILE A 135      16.362   2.129 -17.201  1.00 15.92           C  
ANISOU  984  CB  ILE A 135     2256   1681   2110   -153   -121    409       C  
ATOM    985  CG1 ILE A 135      16.453   2.659 -15.768  1.00 19.41           C  
ANISOU  985  CG1 ILE A 135     2889   1956   2527   -361   -215    278       C  
ATOM    986  CG2 ILE A 135      16.887   3.195 -18.192  1.00 21.61           C  
ANISOU  986  CG2 ILE A 135     3174   2910   2125   -450   -154    839       C  
ATOM    987  CD1 ILE A 135      17.883   2.883 -15.324  1.00 25.99           C  
ANISOU  987  CD1 ILE A 135     2802   3710   3363   -161   -702    315       C  
ATOM    988  N   LEU A 136      14.824   0.370 -19.463  1.00 17.92           N  
ANISOU  988  N   LEU A 136     2756   2084   1966    327    167    337       N  
ATOM    989  CA  LEU A 136      14.382   0.087 -20.827  1.00 18.82           C  
ANISOU  989  CA  LEU A 136     2296   2449   2403   -330   -170   -115       C  
ATOM    990  C   LEU A 136      12.882   0.394 -21.003  1.00 21.04           C  
ANISOU  990  C   LEU A 136     2657   2876   2462    180    -21   -146       C  
ATOM    991  O   LEU A 136      12.480   1.035 -21.971  1.00 22.56           O  
ANISOU  991  O   LEU A 136     3142   2719   2710    425    391    264       O  
ATOM    992  CB  LEU A 136      14.701  -1.317 -21.196  1.00 18.04           C  
ANISOU  992  CB  LEU A 136     2672   2240   1941   -338   -568    275       C  
ATOM    993  CG  LEU A 136      16.176  -1.698 -21.475  1.00 22.47           C  
ANISOU  993  CG  LEU A 136     3081   2786   2670   -440    102    -45       C  
ATOM    994  CD1 LEU A 136      16.269  -3.219 -21.568  1.00 21.65           C  
ANISOU  994  CD1 LEU A 136     3627   3094   1505    997   -161    169       C  
ATOM    995  CD2 LEU A 136      16.733  -1.034 -22.744  1.00 27.09           C  
ANISOU  995  CD2 LEU A 136     4451   3470   2370    679    600   -286       C  
ATOM    996  N   GLY A 137      12.059  -0.078 -20.072  1.00 21.25           N  
ANISOU  996  N   GLY A 137     2970   2674   2429    317    -56     97       N  
ATOM    997  CA  GLY A 137      10.618   0.212 -20.063  1.00 22.87           C  
ANISOU  997  CA  GLY A 137     2951   2830   2906    395   -735    125       C  
ATOM    998  C   GLY A 137      10.272   1.708 -20.036  1.00 19.93           C  
ANISOU  998  C   GLY A 137     2547   2896   2129    587   -523   -558       C  
ATOM    999  O   GLY A 137       9.390   2.193 -20.772  1.00 20.19           O  
ANISOU  999  O   GLY A 137     2711   3326   1631    320   -491   -301       O  
ATOM   1000  N   LEU A 138      10.989   2.454 -19.212  1.00 16.27           N  
ANISOU 1000  N   LEU A 138     1914   2366   1899    335   -730    244       N  
ATOM   1001  CA  LEU A 138      10.708   3.856 -19.024  1.00 19.67           C  
ANISOU 1001  CA  LEU A 138     2175   2467   2829    188   -513    -18       C  
ATOM   1002  C   LEU A 138      11.121   4.650 -20.267  1.00 18.94           C  
ANISOU 1002  C   LEU A 138     2202   2527   2465    311  -1014    -39       C  
ATOM   1003  O   LEU A 138      10.492   5.677 -20.617  1.00 22.66           O  
ANISOU 1003  O   LEU A 138     3196   2729   2682    886  -1041    222       O  
ATOM   1004  CB  LEU A 138      11.456   4.366 -17.790  1.00 19.79           C  
ANISOU 1004  CB  LEU A 138     2798   1926   2793    548   -516   -200       C  
ATOM   1005  CG  LEU A 138      10.908   3.876 -16.455  1.00 23.06           C  
ANISOU 1005  CG  LEU A 138     3458   2545   2756    859    234   -805       C  
ATOM   1006  CD1 LEU A 138      11.835   4.384 -15.338  1.00 28.00           C  
ANISOU 1006  CD1 LEU A 138     3969   3331   3335    390    353   -573       C  
ATOM   1007  CD2 LEU A 138       9.472   4.282 -16.219  1.00 25.98           C  
ANISOU 1007  CD2 LEU A 138     2926   3748   3195    247   -366   -890       C  
ATOM   1008  N   ASN A 139      12.181   4.190 -20.933  1.00 18.55           N  
ANISOU 1008  N   ASN A 139     2607   2364   2076    305   -504    155       N  
ATOM   1009  CA  ASN A 139      12.636   4.875 -22.145  1.00 22.66           C  
ANISOU 1009  CA  ASN A 139     3195   3067   2346    592   -293    332       C  
ATOM   1010  C   ASN A 139      11.551   4.745 -23.198  1.00 22.57           C  
ANISOU 1010  C   ASN A 139     3384   2844   2347    176   -483    137       C  
ATOM   1011  O   ASN A 139      11.315   5.716 -23.923  1.00 23.70           O  
ANISOU 1011  O   ASN A 139     2962   3190   2851    520   -368    491       O  
ATOM   1012  CB  ASN A 139      13.968   4.345 -22.671  1.00 25.24           C  
ANISOU 1012  CB  ASN A 139     2624   3476   3489    311   -267    692       C  
ATOM   1013  CG  ASN A 139      15.193   4.893 -21.912  1.00 27.26           C  
ANISOU 1013  CG  ASN A 139     3318   3122   3914    -69   -335    218       C  
ATOM   1014  OD1 ASN A 139      16.125   4.165 -21.627  1.00 41.25           O  
ANISOU 1014  OD1 ASN A 139     4399   5008   6264    590  -2180   1241       O  
ATOM   1015  ND2 ASN A 139      15.201   6.146 -21.627  1.00 33.91           N  
ANISOU 1015  ND2 ASN A 139     4490   3337   5055    188  -1038    361       N  
ATOM   1016  N   LYS A 140      10.865   3.588 -23.246  1.00 22.81           N  
ANISOU 1016  N   LYS A 140     2651   3035   2980    657   -651    534       N  
ATOM   1017  CA  LYS A 140       9.809   3.358 -24.242  1.00 22.12           C  
ANISOU 1017  CA  LYS A 140     2760   2994   2650    637   -796    650       C  
ATOM   1018  C   LYS A 140       8.620   4.231 -23.876  1.00 25.50           C  
ANISOU 1018  C   LYS A 140     2712   4280   2696    508   -416      8       C  
ATOM   1019  O   LYS A 140       7.961   4.770 -24.769  1.00 26.00           O  
ANISOU 1019  O   LYS A 140     3287   3993   2596    474   -845    -42       O  
ATOM   1020  CB  LYS A 140       9.313   1.937 -24.325  1.00 27.45           C  
ANISOU 1020  CB  LYS A 140     4031   3331   3066    819   -483    479       C  
ATOM   1021  CG  LYS A 140      10.333   0.856 -24.730  1.00 33.96           C  
ANISOU 1021  CG  LYS A 140     4130   4697   4076    726   -400   -681       C  
ATOM   1022  CD  LYS A 140       9.584  -0.433 -25.080  1.00 38.72           C  
ANISOU 1022  CD  LYS A 140     5945   4082   4683   -507    841    692       C  
ATOM   1023  CE  LYS A 140      10.266  -1.710 -24.608  1.00 46.05           C  
ANISOU 1023  CE  LYS A 140     6604   5225   5665   -181   -674    379       C  
ATOM   1024  NZ  LYS A 140       9.312  -2.879 -24.706  1.00 43.17           N  
ANISOU 1024  NZ  LYS A 140     5452   5885   5066    154    632   -184       N  
ATOM   1025  N   ILE A 141       8.326   4.370 -22.580  1.00 23.34           N  
ANISOU 1025  N   ILE A 141     2867   3449   2550    667   -562     66       N  
ATOM   1026  CA  ILE A 141       7.222   5.239 -22.156  1.00 25.18           C  
ANISOU 1026  CA  ILE A 141     3058   3746   2761    241      6   -748       C  
ATOM   1027  C   ILE A 141       7.508   6.721 -22.471  1.00 23.74           C  
ANISOU 1027  C   ILE A 141     2801   3411   2807    797   -292   -256       C  
ATOM   1028  O   ILE A 141       6.665   7.426 -23.016  1.00 27.64           O  
ANISOU 1028  O   ILE A 141     3542   3535   3423   1106   -835    -53       O  
ATOM   1029  CB  ILE A 141       6.889   5.063 -20.645  1.00 25.33           C  
ANISOU 1029  CB  ILE A 141     2596   4153   2872    813   -270    449       C  
ATOM   1030  CG1 ILE A 141       6.365   3.635 -20.357  1.00 27.90           C  
ANISOU 1030  CG1 ILE A 141     2864   4118   3617    739    347   -382       C  
ATOM   1031  CG2 ILE A 141       5.824   6.066 -20.201  1.00 28.90           C  
ANISOU 1031  CG2 ILE A 141     4285   3519   3176   1297   -405    149       C  
ATOM   1032  CD1 ILE A 141       6.702   3.089 -18.973  1.00 30.53           C  
ANISOU 1032  CD1 ILE A 141     3198   3755   4646    506    201    880       C  
ATOM   1033  N   VAL A 142       8.692   7.186 -22.086  1.00 24.77           N  
ANISOU 1033  N   VAL A 142     2817   3349   3245    689    -67   -542       N  
ATOM   1034  CA  VAL A 142       9.129   8.559 -22.339  1.00 26.56           C  
ANISOU 1034  CA  VAL A 142     2981   3493   3617    774   -263    217       C  
ATOM   1035  C   VAL A 142       9.016   8.883 -23.847  1.00 30.27           C  
ANISOU 1035  C   VAL A 142     4332   3462   3705   1171    -40    410       C  
ATOM   1036  O   VAL A 142       8.454   9.942 -24.248  1.00 31.51           O  
ANISOU 1036  O   VAL A 142     2939   3854   5179   1030   -256   1102       O  
ATOM   1037  CB  VAL A 142      10.555   8.792 -21.748  1.00 25.66           C  
ANISOU 1037  CB  VAL A 142     3461   3167   3122    697   -503    574       C  
ATOM   1038  CG1 VAL A 142      11.262   9.993 -22.376  1.00 35.21           C  
ANISOU 1038  CG1 VAL A 142     3533   4181   5663   -250    -42    159       C  
ATOM   1039  CG2 VAL A 142      10.458   8.962 -20.238  1.00 31.63           C  
ANISOU 1039  CG2 VAL A 142     4331   3742   3945    476  -1135   -634       C  
ATOM   1040  N   ARG A 143       9.501   7.956 -24.673  1.00 26.78           N  
ANISOU 1040  N   ARG A 143     2807   3980   3385    837   -404    174       N  
ATOM   1041  CA  ARG A 143       9.435   8.082 -26.147  1.00 34.25           C  
ANISOU 1041  CA  ARG A 143     4637   4793   3581   1218   -256    553       C  
ATOM   1042  C   ARG A 143       7.997   8.336 -26.604  1.00 30.90           C  
ANISOU 1042  C   ARG A 143     4350   4201   3188    282   -335   1029       C  
ATOM   1043  O   ARG A 143       7.728   9.310 -27.348  1.00 36.00           O  
ANISOU 1043  O   ARG A 143     5416   5023   3237   2627   -153   1004       O  
ATOM   1044  CB  ARG A 143      10.042   6.825 -26.786  1.00 35.17           C  
ANISOU 1044  CB  ARG A 143     4814   4567   3981    792    -42   -220       C  
ATOM   1045  CG  ARG A 143       9.887   6.647 -28.286  1.00 38.09           C  
ANISOU 1045  CG  ARG A 143     4518   5497   4456    -91   -379    611       C  
ATOM   1046  CD  ARG A 143      11.054   7.122 -29.170  1.00 40.02           C  
ANISOU 1046  CD  ARG A 143     4310   5335   5560   -400   -238    615       C  
ATOM   1047  NE  ARG A 143      12.446   7.108 -28.657  1.00 39.79           N  
ANISOU 1047  NE  ARG A 143     4086   5931   5099   1302     48   -416       N  
ATOM   1048  CZ  ARG A 143      13.468   6.433 -29.203  1.00 34.06           C  
ANISOU 1048  CZ  ARG A 143     4040   4807   4092    327   -228    200       C  
ATOM   1049  NH1 ARG A 143      13.289   5.617 -30.253  1.00 40.63           N  
ANISOU 1049  NH1 ARG A 143     4986   5354   5096    528   -526   -742       N  
ATOM   1050  NH2 ARG A 143      14.693   6.555 -28.688  1.00 35.80           N  
ANISOU 1050  NH2 ARG A 143     4340   5173   4089   1105   -587   1721       N  
ATOM   1051  N   MET A 144       7.089   7.480 -26.142  1.00 27.39           N  
ANISOU 1051  N   MET A 144     3820   3845   2741    593   -630   1377       N  
ATOM   1052  CA  MET A 144       5.657   7.606 -26.363  1.00 30.21           C  
ANISOU 1052  CA  MET A 144     4189   4363   2924    472  -1206    332       C  
ATOM   1053  C   MET A 144       5.046   8.978 -25.982  1.00 32.67           C  
ANISOU 1053  C   MET A 144     4122   5164   3127    795  -1216   -202       C  
ATOM   1054  O   MET A 144       4.144   9.456 -26.654  1.00 39.95           O  
ANISOU 1054  O   MET A 144     4609   7282   3286   1429  -1851    660       O  
ATOM   1055  CB  MET A 144       4.957   6.490 -25.603  1.00 33.06           C  
ANISOU 1055  CB  MET A 144     4413   3952   4196   -290  -1109   -478       C  
ATOM   1056  CG  MET A 144       3.451   6.430 -25.744  1.00 46.05           C  
ANISOU 1056  CG  MET A 144     4976   6881   5639    350   -146  -1003       C  
ATOM   1057  SD  MET A 144       2.813   4.865 -25.089  1.00 53.38           S  
ANISOU 1057  SD  MET A 144     6959   6662   6658    361    810   -128       S  
ATOM   1058  CE  MET A 144       2.539   5.259 -23.351  1.00 42.60           C  
ANISOU 1058  CE  MET A 144     5407   5128   5650   -522   -623    -25       C  
ATOM   1059  N   TYR A 145       5.533   9.594 -24.908  1.00 23.88           N  
ANISOU 1059  N   TYR A 145     2393   4141   2539   1026  -1805    745       N  
ATOM   1060  CA  TYR A 145       5.080  10.923 -24.457  1.00 27.96           C  
ANISOU 1060  CA  TYR A 145     3369   3926   3327    267   -177    566       C  
ATOM   1061  C   TYR A 145       5.838  12.064 -25.085  1.00 32.34           C  
ANISOU 1061  C   TYR A 145     4780   3821   3686    211   -106    639       C  
ATOM   1062  O   TYR A 145       5.600  13.220 -24.731  1.00 42.84           O  
ANISOU 1062  O   TYR A 145     5937   4740   5597   1698   -929    -22       O  
ATOM   1063  CB  TYR A 145       5.254  11.065 -22.944  1.00 25.75           C  
ANISOU 1063  CB  TYR A 145     2507   3752   3521   -339  -1094   -134       C  
ATOM   1064  CG  TYR A 145       4.185  10.354 -22.110  1.00 33.73           C  
ANISOU 1064  CG  TYR A 145     3388   3938   5489   -318    617    189       C  
ATOM   1065  CD1 TYR A 145       4.053   8.952 -22.139  1.00 35.91           C  
ANISOU 1065  CD1 TYR A 145     4264   3859   5520    853    223    403       C  
ATOM   1066  CD2 TYR A 145       3.287  11.088 -21.315  1.00 34.82           C  
ANISOU 1066  CD2 TYR A 145     4708   4572   3947   -546   1019   -262       C  
ATOM   1067  CE1 TYR A 145       3.074   8.300 -21.389  1.00 36.79           C  
ANISOU 1067  CE1 TYR A 145     4098   3984   5896   1332    -55    962       C  
ATOM   1068  CE2 TYR A 145       2.308  10.446 -20.549  1.00 34.81           C  
ANISOU 1068  CE2 TYR A 145     3378   3790   6055   1114   1716   -498       C  
ATOM   1069  CZ  TYR A 145       2.207   9.048 -20.587  1.00 40.35           C  
ANISOU 1069  CZ  TYR A 145     5078   4725   5529    109    172   -259       C  
ATOM   1070  OH  TYR A 145       1.232   8.402 -19.840  1.00 42.73           O  
ANISOU 1070  OH  TYR A 145     3727   5929   6578   1878    881    272       O  
ATOM   1071  N   SER A 146       6.737  11.774 -26.017  1.00 31.10           N  
ANISOU 1071  N   SER A 146     2760   4044   5011    724    -67    913       N  
ATOM   1072  CA  SER A 146       7.564  12.828 -26.642  1.00 37.57           C  
ANISOU 1072  CA  SER A 146     4542   4688   5042   -467   -415    976       C  
ATOM   1073  C   SER A 146       6.895  13.681 -27.730  1.00 48.36           C  
ANISOU 1073  C   SER A 146     5672   7954   4748   1668  -1200    571       C  
ATOM   1074  O   SER A 146       6.305  13.149 -28.674  1.00 57.11           O  
ANISOU 1074  O   SER A 146     6930   9680   5087    955  -1953    403       O  
ATOM   1075  CB  SER A 146       8.859  12.219 -27.186  1.00 38.90           C  
ANISOU 1075  CB  SER A 146     4603   4418   5757    318   -610   1262       C  
ATOM   1076  OG  SER A 146       9.705  11.965 -26.091  1.00 54.90           O  
ANISOU 1076  OG  SER A 146     4736   7576   8548   -829  -1866   1354       O  
TER    1077      SER A 146                                                      
ATOM   1078  N   PRO B 322       3.480 -15.194 -17.898  1.00 27.85           N  
ANISOU 1078  N   PRO B 322     3417   3470   3695   -592   -796    251       N  
ATOM   1079  CA  PRO B 322       4.419 -14.085 -17.640  1.00 30.91           C  
ANISOU 1079  CA  PRO B 322     3396   4082   4264   -722  -1012    159       C  
ATOM   1080  C   PRO B 322       4.806 -13.907 -16.173  1.00 32.50           C  
ANISOU 1080  C   PRO B 322     4292   4629   3428  -1534   -532    672       C  
ATOM   1081  O   PRO B 322       4.240 -14.541 -15.293  1.00 36.18           O  
ANISOU 1081  O   PRO B 322     4507   4343   4894  -2391   -513    459       O  
ATOM   1082  CB  PRO B 322       3.638 -12.841 -18.094  1.00 29.54           C  
ANISOU 1082  CB  PRO B 322     3556   3436   4231   -482   -329    149       C  
ATOM   1083  CG  PRO B 322       2.209 -13.236 -17.947  1.00 31.76           C  
ANISOU 1083  CG  PRO B 322     3334   3866   4866      0   -163     16       C  
ATOM   1084  CD  PRO B 322       2.164 -14.694 -18.354  1.00 27.38           C  
ANISOU 1084  CD  PRO B 322     3137   3633   3633    226     91   -153       C  
ATOM   1085  N   VAL B 323       5.748 -13.004 -15.910  1.00 30.43           N  
ANISOU 1085  N   VAL B 323     3171   4687   3701   -664   -798    504       N  
ATOM   1086  CA  VAL B 323       6.148 -12.684 -14.532  1.00 28.51           C  
ANISOU 1086  CA  VAL B 323     3170   3991   3671   -328     19   -659       C  
ATOM   1087  C   VAL B 323       5.053 -11.809 -13.894  1.00 23.46           C  
ANISOU 1087  C   VAL B 323     3087   2627   3198   -589     41    -49       C  
ATOM   1088  O   VAL B 323       4.668 -12.020 -12.738  1.00 29.92           O  
ANISOU 1088  O   VAL B 323     4350   3698   3319  -1065    222   -686       O  
ATOM   1089  CB  VAL B 323       7.538 -11.936 -14.455  1.00 23.76           C  
ANISOU 1089  CB  VAL B 323     2780   2912   3333     49   -155   -361       C  
ATOM   1090  CG1 VAL B 323       7.802 -11.492 -13.040  1.00 27.86           C  
ANISOU 1090  CG1 VAL B 323     3381   3763   3441   -128   -303      4       C  
ATOM   1091  CG2 VAL B 323       8.682 -12.827 -14.849  1.00 24.27           C  
ANISOU 1091  CG2 VAL B 323     3108   2808   3303     66    339    258       C  
ATOM   1092  N   LEU B 324       4.575 -10.830 -14.664  1.00 24.87           N  
ANISOU 1092  N   LEU B 324     2756   3565   3127    298    -95   -146       N  
ATOM   1093  CA  LEU B 324       3.582  -9.856 -14.213  1.00 25.53           C  
ANISOU 1093  CA  LEU B 324     2770   2714   4213   -150   -146   -713       C  
ATOM   1094  C   LEU B 324       2.303  -9.829 -15.080  1.00 26.57           C  
ANISOU 1094  C   LEU B 324     2839   4547   2708    152     50    -84       C  
ATOM   1095  O   LEU B 324       2.317  -9.480 -16.266  1.00 24.82           O  
ANISOU 1095  O   LEU B 324     2656   3620   3153   -617   -251   -220       O  
ATOM   1096  CB  LEU B 324       4.181  -8.443 -14.158  1.00 25.04           C  
ANISOU 1096  CB  LEU B 324     2264   3188   4060   -613   -213    208       C  
ATOM   1097  CG  LEU B 324       5.242  -8.257 -13.061  1.00 21.64           C  
ANISOU 1097  CG  LEU B 324     3436   2490   2292   -402     -8    278       C  
ATOM   1098  CD1 LEU B 324       5.840  -6.868 -13.227  1.00 24.77           C  
ANISOU 1098  CD1 LEU B 324     2985   2636   3788   -396    447    137       C  
ATOM   1099  CD2 LEU B 324       4.691  -8.424 -11.632  1.00 27.99           C  
ANISOU 1099  CD2 LEU B 324     3270   4073   3292    488    655    357       C  
ATOM   1100  N   PHE B 325       1.195 -10.197 -14.445  1.00 33.73           N  
ANISOU 1100  N   PHE B 325     3026   5556   4232  -1139    -15   -762       N  
ATOM   1101  CA  PHE B 325      -0.114 -10.130 -15.076  1.00 35.16           C  
ANISOU 1101  CA  PHE B 325     3594   4788   4975   -913   -781    103       C  
ATOM   1102  C   PHE B 325      -0.675  -8.705 -15.051  1.00 40.18           C  
ANISOU 1102  C   PHE B 325     5561   4837   4866   -370  -1001   -846       C  
ATOM   1103  O   PHE B 325      -0.314  -7.896 -14.184  1.00 45.25           O  
ANISOU 1103  O   PHE B 325     4548   5627   7015  -1086   -470  -2429       O  
ATOM   1104  CB  PHE B 325      -1.089 -11.117 -14.398  1.00 38.93           C  
ANISOU 1104  CB  PHE B 325     5047   4986   4758  -1179    348     -5       C  
ATOM   1105  CG  PHE B 325      -0.757 -12.569 -14.669  1.00 34.16           C  
ANISOU 1105  CG  PHE B 325     4171   4747   4059   -980   -736    262       C  
ATOM   1106  CD1 PHE B 325      -0.967 -13.116 -15.938  1.00 35.39           C  
ANISOU 1106  CD1 PHE B 325     4541   4708   4197     43     12   -678       C  
ATOM   1107  CD2 PHE B 325      -0.224 -13.381 -13.677  1.00 32.09           C  
ANISOU 1107  CD2 PHE B 325     3993   3646   4553  -1093   -164    806       C  
ATOM   1108  CE1 PHE B 325      -0.652 -14.441 -16.203  1.00 36.48           C  
ANISOU 1108  CE1 PHE B 325     4355   4011   5492   -746   -739    558       C  
ATOM   1109  CE2 PHE B 325       0.103 -14.713 -13.934  1.00 42.58           C  
ANISOU 1109  CE2 PHE B 325     6575   5024   4577    -40     12   -214       C  
ATOM   1110  CZ  PHE B 325      -0.112 -15.245 -15.195  1.00 37.00           C  
ANISOU 1110  CZ  PHE B 325     4487   4967   4602  -1118    185    810       C  
ATOM   1111  N   PRO B 326      -1.544  -8.377 -16.020  1.00 42.47           N  
ANISOU 1111  N   PRO B 326     5618   5399   5119    283   -973   -848       N  
ATOM   1112  CA  PRO B 326      -2.135  -7.031 -15.978  1.00 42.61           C  
ANISOU 1112  CA  PRO B 326     5619   5634   4938    398   -580   -157       C  
ATOM   1113  C   PRO B 326      -2.988  -6.867 -14.730  1.00 45.53           C  
ANISOU 1113  C   PRO B 326     5189   6716   5395   -170   -255   -885       C  
ATOM   1114  O   PRO B 326      -3.890  -7.684 -14.489  1.00 69.87           O  
ANISOU 1114  O   PRO B 326     7097   9533   9918  -1763    296   1012       O  
ATOM   1115  CB  PRO B 326      -2.989  -6.980 -17.258  1.00 41.46           C  
ANISOU 1115  CB  PRO B 326     4210   5974   5566   -189   -816   -596       C  
ATOM   1116  CG  PRO B 326      -2.369  -7.989 -18.153  1.00 37.32           C  
ANISOU 1116  CG  PRO B 326     4290   4962   4927   -631   -650    -92       C  
ATOM   1117  CD  PRO B 326      -1.896  -9.090 -17.266  1.00 33.00           C  
ANISOU 1117  CD  PRO B 326     3129   4857   4552   -801   -774   -139       C  
ATOM   1118  N   GLY B 327      -2.698  -5.843 -13.928  1.00 46.65           N  
ANISOU 1118  N   GLY B 327     4539   7267   5918   -599    465  -1025       N  
ATOM   1119  CA  GLY B 327      -3.294  -5.754 -12.597  1.00 42.74           C  
ANISOU 1119  CA  GLY B 327     5273   5608   5358   -412    527   -165       C  
ATOM   1120  C   GLY B 327      -2.803  -6.916 -11.735  1.00 48.57           C  
ANISOU 1120  C   GLY B 327     3525   7421   7508     61   -198   1444       C  
ATOM   1121  O   GLY B 327      -3.582  -7.739 -11.222  1.00 52.61           O  
ANISOU 1121  O   GLY B 327     5578   5747   8663  -1863   -619    827       O  
ATOM   1122  N   GLN B 328      -1.481  -7.034 -11.689  1.00 50.08           N  
ANISOU 1122  N   GLN B 328     3560   8562   6905  -1775  -2207   -302       N  
ATOM   1123  CA  GLN B 328      -0.760  -7.715 -10.619  1.00 43.53           C  
ANISOU 1123  CA  GLN B 328     5707   5370   5460    -79   -697   -877       C  
ATOM   1124  C   GLN B 328       0.281  -6.642 -10.266  1.00 40.04           C  
ANISOU 1124  C   GLN B 328     4668   7105   3440   -713    443   -766       C  
ATOM   1125  O   GLN B 328       0.983  -6.180 -11.142  1.00 50.30           O  
ANISOU 1125  O   GLN B 328     4035   9467   5610  -2030    129    119       O  
ATOM   1126  CB  GLN B 328      -0.103  -8.991 -11.145  1.00 42.53           C  
ANISOU 1126  CB  GLN B 328     5219   4407   6531   -555   -664    163       C  
ATOM   1127  CG  GLN B 328       1.028  -9.569 -10.296  1.00 42.46           C  
ANISOU 1127  CG  GLN B 328     5264   5055   5813   -336   -578   -184       C  
ATOM   1128  CD  GLN B 328       1.666 -10.807 -10.930  1.00 37.85           C  
ANISOU 1128  CD  GLN B 328     4996   5699   3683   -394    558    548       C  
ATOM   1129  OE1 GLN B 328       1.310 -11.205 -12.056  1.00 46.79           O  
ANISOU 1129  OE1 GLN B 328     4653   7578   5545  -1497    620   -769       O  
ATOM   1130  NE2 GLN B 328       2.609 -11.423 -10.219  1.00 35.14           N  
ANISOU 1130  NE2 GLN B 328     3696   4207   5446   -453    728    370       N  
ATOM   1131  N   PRO B 329       0.307  -6.165  -9.012  1.00 39.32           N  
ANISOU 1131  N   PRO B 329     4273   5961   4705  -1880    -59  -1706       N  
ATOM   1132  CA  PRO B 329       1.320  -5.183  -8.685  1.00 30.59           C  
ANISOU 1132  CA  PRO B 329     2990   4865   3765   -801    403   -277       C  
ATOM   1133  C   PRO B 329       2.727  -5.692  -8.961  1.00 30.26           C  
ANISOU 1133  C   PRO B 329     3389   3433   4674   -301   1331  -1235       C  
ATOM   1134  O   PRO B 329       3.011  -6.906  -8.871  1.00 29.06           O  
ANISOU 1134  O   PRO B 329     2840   4011   4191   -394   1288   -370       O  
ATOM   1135  CB  PRO B 329       1.129  -4.970  -7.183  1.00 27.06           C  
ANISOU 1135  CB  PRO B 329     2779   4095   3406    347    -21   -515       C  
ATOM   1136  CG  PRO B 329      -0.368  -5.172  -6.987  1.00 36.19           C  
ANISOU 1136  CG  PRO B 329     3567   5369   4812  -1235    167    -89       C  
ATOM   1137  CD  PRO B 329      -0.825  -6.122  -8.066  1.00 38.74           C  
ANISOU 1137  CD  PRO B 329     4427   5342   4948  -1391    375   -526       C  
ATOM   1138  N   PHE B 330       3.595  -4.742  -9.263  1.00 30.97           N  
ANISOU 1138  N   PHE B 330     2723   4099   4944     12   1017   -436       N  
ATOM   1139  CA  PHE B 330       5.031  -5.029  -9.342  1.00 24.56           C  
ANISOU 1139  CA  PHE B 330     2630   3274   3426   -107    666   -225       C  
ATOM   1140  C   PHE B 330       5.459  -5.722  -8.029  1.00 25.34           C  
ANISOU 1140  C   PHE B 330     3478   3301   2846    205    371   -816       C  
ATOM   1141  O   PHE B 330       5.051  -5.332  -6.941  1.00 20.66           O  
ANISOU 1141  O   PHE B 330     2889   2502   2459    -48    951    132       O  
ATOM   1142  CB  PHE B 330       5.812  -3.728  -9.617  1.00 23.29           C  
ANISOU 1142  CB  PHE B 330     2736   2984   3129    107    116    507       C  
ATOM   1143  CG  PHE B 330       5.425  -3.021 -10.901  1.00 20.60           C  
ANISOU 1143  CG  PHE B 330     2818   2437   2570     60     73   -374       C  
ATOM   1144  CD1 PHE B 330       5.982  -3.398 -12.099  1.00 16.79           C  
ANISOU 1144  CD1 PHE B 330     2108   2302   1967   -266    113    526       C  
ATOM   1145  CD2 PHE B 330       4.524  -1.975 -10.886  1.00 18.50           C  
ANISOU 1145  CD2 PHE B 330     2138   2813   2075    187     28    541       C  
ATOM   1146  CE1 PHE B 330       5.690  -2.714 -13.257  1.00 20.71           C  
ANISOU 1146  CE1 PHE B 330     3150   2744   1972    391   -355    174       C  
ATOM   1147  CE2 PHE B 330       4.181  -1.287 -12.054  1.00 21.81           C  
ANISOU 1147  CE2 PHE B 330     3216   3608   1463   -104   -241     49       C  
ATOM   1148  CZ  PHE B 330       4.781  -1.644 -13.240  1.00 19.68           C  
ANISOU 1148  CZ  PHE B 330     2862   2700   1915    363    -35    116       C  
ATOM   1149  N   GLY B 331       6.190  -6.839  -8.127  1.00 28.19           N  
ANISOU 1149  N   GLY B 331     3719   3146   3845   -227    -66   -495       N  
ATOM   1150  CA  GLY B 331       6.669  -7.533  -6.943  1.00 26.96           C  
ANISOU 1150  CA  GLY B 331     3341   3352   3551   -181    759     -4       C  
ATOM   1151  C   GLY B 331       5.688  -8.522  -6.342  1.00 27.62           C  
ANISOU 1151  C   GLY B 331     3225   3833   3435   -777     80    131       C  
ATOM   1152  O   GLY B 331       6.068  -9.339  -5.532  1.00 33.16           O  
ANISOU 1152  O   GLY B 331     3787   3777   5035    245    392    643       O  
ATOM   1153  N   GLN B 332       4.430  -8.442  -6.734  1.00 35.00           N  
ANISOU 1153  N   GLN B 332     2900   4086   6312  -1248    885    124       N  
ATOM   1154  CA  GLN B 332       3.410  -9.359  -6.180  1.00 30.34           C  
ANISOU 1154  CA  GLN B 332     3401   3526   4601   -508    937    638       C  
ATOM   1155  C   GLN B 332       3.662 -10.801  -6.608  1.00 29.58           C  
ANISOU 1155  C   GLN B 332     3767   3392   4077   -453    140    424       C  
ATOM   1156  O   GLN B 332       3.709 -11.082  -7.800  1.00 34.71           O  
ANISOU 1156  O   GLN B 332     4454   3826   4906   -855    109   -353       O  
ATOM   1157  CB  GLN B 332       2.020  -8.932  -6.657  1.00 34.74           C  
ANISOU 1157  CB  GLN B 332     4055   4515   4627   -473    234    385       C  
ATOM   1158  CG  GLN B 332       0.878  -9.601  -5.903  1.00 33.95           C  
ANISOU 1158  CG  GLN B 332     3928   3785   5187   -209     91    789       C  
ATOM   1159  CD  GLN B 332      -0.477  -9.036  -6.266  1.00 37.76           C  
ANISOU 1159  CD  GLN B 332     4367   4446   5531    576    294   -405       C  
ATOM   1160  OE1 GLN B 332      -0.876  -8.008  -5.733  1.00 41.25           O  
ANISOU 1160  OE1 GLN B 332     5955   4155   5561   1434   1839    336       O  
ATOM   1161  NE2 GLN B 332      -1.204  -9.720  -7.162  1.00 45.67           N  
ANISOU 1161  NE2 GLN B 332     6016   6125   5212    -37   -708    119       N  
ATOM   1162  N   PRO B 333       3.846 -11.716  -5.634  1.00 34.84           N  
ANISOU 1162  N   PRO B 333     4897   4240   4100   -863   -253    517       N  
ATOM   1163  CA  PRO B 333       3.957 -13.120  -6.044  1.00 30.90           C  
ANISOU 1163  CA  PRO B 333     3804   4046   3888   -244    132    256       C  
ATOM   1164  C   PRO B 333       2.652 -13.582  -6.708  1.00 27.74           C  
ANISOU 1164  C   PRO B 333     3564   3882   3093   -274    482    593       C  
ATOM   1165  O   PRO B 333       1.563 -13.148  -6.300  1.00 35.20           O  
ANISOU 1165  O   PRO B 333     3969   4442   4961    796    407    825       O  
ATOM   1166  CB  PRO B 333       4.213 -13.880  -4.740  1.00 31.95           C  
ANISOU 1166  CB  PRO B 333     3226   4662   4249     39    -30     80       C  
ATOM   1167  CG  PRO B 333       4.013 -12.908  -3.635  1.00 39.03           C  
ANISOU 1167  CG  PRO B 333     5680   4809   4339     17    930    631       C  
ATOM   1168  CD  PRO B 333       4.127 -11.520  -4.197  1.00 38.84           C  
ANISOU 1168  CD  PRO B 333     4931   5190   4636   -451    476    739       C  
ATOM   1169  N   PRO B 334       2.755 -14.447  -7.736  1.00 24.33           N  
ANISOU 1169  N   PRO B 334     3235   2699   3308   -311    149    915       N  
ATOM   1170  CA  PRO B 334       1.566 -14.827  -8.446  1.00 25.50           C  
ANISOU 1170  CA  PRO B 334     3550   3569   2567    -77   -220    961       C  
ATOM   1171  C   PRO B 334       0.637 -15.701  -7.630  1.00 27.57           C  
ANISOU 1171  C   PRO B 334     3217   2605   4650   -384   -120    920       C  
ATOM   1172  O   PRO B 334       1.115 -16.453  -6.780  1.00 34.55           O  
ANISOU 1172  O   PRO B 334     3744   5099   4284   -604   -750   1149       O  
ATOM   1173  CB  PRO B 334       2.104 -15.591  -9.650  1.00 33.29           C  
ANISOU 1173  CB  PRO B 334     4454   3653   4541    174   -399   -407       C  
ATOM   1174  CG  PRO B 334       3.540 -15.807  -9.433  1.00 30.54           C  
ANISOU 1174  CG  PRO B 334     4063   3683   3857   -879   -841    -68       C  
ATOM   1175  CD  PRO B 334       3.852 -15.368  -8.031  1.00 26.50           C  
ANISOU 1175  CD  PRO B 334     3893   3450   2726   -142    778    265       C  
ATOM   1176  N   LEU B 335      -0.678 -15.563  -7.852  1.00 28.61           N  
ANISOU 1176  N   LEU B 335     3669   3858   3341   -113   -328    835       N  
ATOM   1177  CA  LEU B 335      -1.669 -16.361  -7.145  1.00 28.17           C  
ANISOU 1177  CA  LEU B 335     3287   3541   3875   -181   -390    520       C  
ATOM   1178  C   LEU B 335      -1.661 -17.825  -7.531  1.00 31.02           C  
ANISOU 1178  C   LEU B 335     4218   3971   3596    340    953   -691       C  
ATOM   1179  O   LEU B 335      -2.083 -18.679  -6.745  1.00 41.54           O  
ANISOU 1179  O   LEU B 335     6150   5610   4022  -1092   -859    884       O  
ATOM   1180  CB  LEU B 335      -3.093 -15.853  -7.324  1.00 29.37           C  
ANISOU 1180  CB  LEU B 335     3394   4261   3502    208  -1251   -406       C  
ATOM   1181  CG  LEU B 335      -3.790 -14.824  -6.455  1.00 32.98           C  
ANISOU 1181  CG  LEU B 335     5000   4185   3343    -56  -1367   -769       C  
ATOM   1182  CD1 LEU B 335      -3.174 -14.700  -5.050  1.00 35.92           C  
ANISOU 1182  CD1 LEU B 335     5204   5204   3239    348  -1096    163       C  
ATOM   1183  CD2 LEU B 335      -3.829 -13.494  -7.209  1.00 37.20           C  
ANISOU 1183  CD2 LEU B 335     5769   4893   3470   -634   1193   -103       C  
ATOM   1184  N   GLY B 336      -1.279 -18.141  -8.754  1.00 29.92           N  
ANISOU 1184  N   GLY B 336     4379   4148   2838   -428    183    -17       N  
ATOM   1185  CA  GLY B 336      -0.860 -19.508  -9.052  1.00 37.84           C  
ANISOU 1185  CA  GLY B 336     4586   4321   5470     28   -538   -682       C  
ATOM   1186  C   GLY B 336       0.658 -19.678  -8.917  1.00 46.84           C  
ANISOU 1186  C   GLY B 336     3801   7827   6166  -1742   1595   -434       C  
ATOM   1187  O   GLY B 336       1.434 -19.478  -9.880  1.00 45.62           O  
ANISOU 1187  O   GLY B 336     7444   6103   3786  -1691   2296   -938       O  
TER    1188      GLY B 336                                                      
HETATM 1189  O   HOH A2001      24.550   2.397  -2.787  1.00 46.95           O  
ANISOU 1189  O   HOH A2001     7703   7141   2995    -63  -1910   -110       O  
HETATM 1190  O   HOH A2002      25.782   4.535   3.932  1.00 40.75           O  
ANISOU 1190  O   HOH A2002     4883   4055   6543    581    180     64       O  
HETATM 1191  O   HOH A2003      29.433  -7.611   1.031  1.00 36.11           O  
ANISOU 1191  O   HOH A2003     4622   6354   2740   -554  -1064    117       O  
HETATM 1192  O   HOH A2004      30.234   1.570  10.000  1.00 44.24           O  
ANISOU 1192  O   HOH A2004     6433   5420   4954   -208  -2830  -2392       O  
HETATM 1193  O   HOH A2005      26.177  -0.169   9.188  1.00 28.38           O  
ANISOU 1193  O   HOH A2005     3825   3856   3100    586    628   -558       O  
HETATM 1194  O   HOH A2006      32.063   2.837  12.049  1.00 49.52           O  
ANISOU 1194  O   HOH A2006     6523   4154   8135    858  -2141   -500       O  
HETATM 1195  O   HOH A2007      37.520   0.484   3.207  1.00 43.40           O  
ANISOU 1195  O   HOH A2007     5998   5051   5440   1451   -192    486       O  
HETATM 1196  O   HOH A2008      28.126  -7.918   2.860  1.00 46.60           O  
ANISOU 1196  O   HOH A2008     5592   5502   6610   1916  -1267   -148       O  
HETATM 1197  O   HOH A2009      31.152  -5.423  -2.759  1.00 50.25           O  
ANISOU 1197  O   HOH A2009     7132   7851   4109    205    552   3109       O  
HETATM 1198  O   HOH A2010      15.407  -3.592   0.191  1.00 18.91           O  
ANISOU 1198  O   HOH A2010     2821   2933   1428    164   -162   -346       O  
HETATM 1199  O   HOH A2011      14.468  -4.514   5.862  1.00 47.29           O  
ANISOU 1199  O   HOH A2011     5576   6336   6053   1652  -2405  -1923       O  
HETATM 1200  O   HOH A2012      17.750   3.964   2.772  1.00 45.49           O  
ANISOU 1200  O   HOH A2012     5711   5197   6377    843    635  -2055       O  
HETATM 1201  O   HOH A2013      16.495   5.173   0.202  1.00 30.95           O  
ANISOU 1201  O   HOH A2013     3501   4655   3600    613   -422  -1296       O  
HETATM 1202  O   HOH A2014       6.227  13.423  -1.838  1.00 48.12           O  
ANISOU 1202  O   HOH A2014     5238   4294   8748     53   1784  -1006       O  
HETATM 1203  O   HOH A2015      -2.798   8.698 -18.566  1.00 44.64           O  
ANISOU 1203  O   HOH A2015     5345   5620   5994   2210    893   2316       O  
HETATM 1204  O   HOH A2016       5.737   7.764  -8.040  1.00 33.05           O  
ANISOU 1204  O   HOH A2016     5003   3479   4074   1778    423  -1200       O  
HETATM 1205  O   HOH A2017      12.007  19.135  -2.839  1.00 59.21           O  
ANISOU 1205  O   HOH A2017     7625   5001   9872   3339  -2313  -2223       O  
HETATM 1206  O   HOH A2018       8.644 -12.419 -24.756  1.00 34.37           O  
ANISOU 1206  O   HOH A2018     4535   5418   3105   -161  -1686    -17       O  
HETATM 1207  O   HOH A2019      18.943 -11.693 -21.321  1.00 36.34           O  
ANISOU 1207  O   HOH A2019     4994   3743   5068   1056   -950  -1670       O  
HETATM 1208  O   HOH A2020      17.489  -4.500 -25.599  1.00 40.14           O  
ANISOU 1208  O   HOH A2020     6219   4751   4281  -1207    -81   -107       O  
HETATM 1209  O   HOH A2021      16.230  -2.587 -26.347  1.00 48.30           O  
ANISOU 1209  O   HOH A2021     6848   6653   4850  -1574   1012   -231       O  
HETATM 1210  O   HOH A2022       3.895  14.734  -3.846  1.00 43.55           O  
ANISOU 1210  O   HOH A2022     4542   3303   8700    172   1092  -1172       O  
HETATM 1211  O   HOH A2023      24.836 -11.989 -13.120  1.00 44.49           O  
ANISOU 1211  O   HOH A2023     5855   6664   4383   -289   -654  -1934       O  
HETATM 1212  O   HOH A2024      24.765  -9.041 -14.838  1.00 59.16           O  
ANISOU 1212  O   HOH A2024     3662  12327   6486    943  -1116  -1901       O  
HETATM 1213  O   HOH A2025      13.053 -18.802   1.428  1.00 29.88           O  
ANISOU 1213  O   HOH A2025     4082   4312   2960    390     81    858       O  
HETATM 1214  O   HOH A2026      22.350   7.371  -3.045  1.00 45.27           O  
ANISOU 1214  O   HOH A2026     7714   5968   3516    253  -1964   -150       O  
HETATM 1215  O   HOH A2027      29.357  -7.209  -1.779  1.00 29.90           O  
ANISOU 1215  O   HOH A2027     3381   3402   4576   -696  -1844    478       O  
HETATM 1216  O   HOH A2028      21.514  -2.414  -7.204  1.00 31.75           O  
ANISOU 1216  O   HOH A2028     6147   2299   3617  -1292    218   -901       O  
HETATM 1217  O   HOH A2029      21.629  -7.057 -17.579  1.00 46.48           O  
ANISOU 1217  O   HOH A2029     4817   8839   4002    290   1279   1023       O  
HETATM 1218  O   HOH A2030       8.526  -4.537  -2.641  1.00 31.44           O  
ANISOU 1218  O   HOH A2030     3978   5265   2702    484   1718    785       O  
HETATM 1219  O   HOH A2031      11.019   3.711 -27.859  1.00 43.11           O  
ANISOU 1219  O   HOH A2031     6275   5853   4251    -89   1654  -1698       O  
HETATM 1220  O   HOH A2032       8.065  -7.253 -10.354  1.00 25.78           O  
ANISOU 1220  O   HOH A2032     2736   3256   3803     75   1337   -125       O  
HETATM 1221  O   HOH A2033       9.124  -6.565  -4.145  1.00 28.02           O  
ANISOU 1221  O   HOH A2033     3332   3592   3720    -44    354    886       O  
HETATM 1222  O   HOH A2034       4.825   1.339  -2.925  1.00 38.56           O  
ANISOU 1222  O   HOH A2034     4853   5025   4770   1385     55    562       O  
HETATM 1223  O   HOH A2035      10.945  -1.327   0.210  1.00 54.66           O  
ANISOU 1223  O   HOH A2035     6609   6505   7655  -1447  -2041   -814       O  
HETATM 1224  O   HOH A2036       2.005   1.465 -10.110  1.00 37.31           O  
ANISOU 1224  O   HOH A2036     2506   6282   5386   -232   -681   -347       O  
HETATM 1225  O   HOH A2037      -0.036   1.501  -7.993  1.00 50.49           O  
ANISOU 1225  O   HOH A2037     3527   7271   8385   1720   -881     62       O  
HETATM 1226  O   HOH A2038       1.203  -0.796  -8.992  1.00 47.44           O  
ANISOU 1226  O   HOH A2038     3128   5912   8983    660   -592   -226       O  
HETATM 1227  O   HOH A2039      -0.873   3.314 -12.278  1.00 55.85           O  
ANISOU 1227  O   HOH A2039     4284   9314   7622    435  -2325    984       O  
HETATM 1228  O   HOH A2040      -0.340   6.169 -19.080  1.00 55.00           O  
ANISOU 1228  O   HOH A2040     6287   5483   9125   1117   -997    355       O  
HETATM 1229  O   HOH A2041      -3.413   6.021 -18.802  1.00 49.86           O  
ANISOU 1229  O   HOH A2041     4589   5758   8594    803  -2655    967       O  
HETATM 1230  O   HOH A2042       7.518   0.033 -21.380  1.00 51.67           O  
ANISOU 1230  O   HOH A2042     4133   8567   6932  -1068   1102    925       O  
HETATM 1231  O   HOH A2043       7.649 -13.129 -18.582  1.00 26.68           O  
ANISOU 1231  O   HOH A2043     4192   2661   3282  -1136   -652   -900       O  
HETATM 1232  O   HOH A2044       3.634  -9.394 -21.210  1.00 31.22           O  
ANISOU 1232  O   HOH A2044     2699   3864   5297  -1303   -603  -1087       O  
HETATM 1233  O   HOH A2045       7.003 -10.954 -22.926  1.00 47.84           O  
ANISOU 1233  O   HOH A2045     5719   6374   6083    275  -1264   -306       O  
HETATM 1234  O   HOH A2046      11.218 -12.230 -24.353  1.00 27.78           O  
ANISOU 1234  O   HOH A2046     4040   3458   3056     97   -374  -1813       O  
HETATM 1235  O   HOH A2047       9.195  -9.328 -27.546  1.00 60.82           O  
ANISOU 1235  O   HOH A2047     6419   9538   7149   3649   -549   1606       O  
HETATM 1236  O   HOH A2048      16.969 -10.112 -20.287  1.00 25.94           O  
ANISOU 1236  O   HOH A2048     3343   3372   3142   -581    142   -979       O  
HETATM 1237  O   HOH A2049      17.407  -6.038 -23.763  1.00 43.37           O  
ANISOU 1237  O   HOH A2049     5223   5534   5719    719   1373  -1073       O  
HETATM 1238  O   HOH A2050      16.853  -8.685 -23.479  1.00 37.09           O  
ANISOU 1238  O   HOH A2050     5807   4406   3878   2040   -562   -411       O  
HETATM 1239  O   HOH A2051      11.716 -17.951 -21.105  1.00 36.72           O  
ANISOU 1239  O   HOH A2051     4884   3334   5733   -377   -569  -1657       O  
HETATM 1240  O   HOH A2052      18.734 -11.631 -26.099  1.00 34.60           O  
ANISOU 1240  O   HOH A2052     6017   3316   3811   -313   1078   -877       O  
HETATM 1241  O   HOH A2053      20.412 -17.323 -13.305  1.00 30.78           O  
ANISOU 1241  O   HOH A2053     3967   4173   3552    535     14  -1115       O  
HETATM 1242  O   HOH A2054      11.124 -16.549 -14.192  1.00 25.55           O  
ANISOU 1242  O   HOH A2054     3111   2846   3749  -1319    110  -1004       O  
HETATM 1243  O   HOH A2055      19.641 -19.500 -27.066  1.00 50.28           O  
ANISOU 1243  O   HOH A2055     7207   5556   6339  -1333  -1755    871       O  
HETATM 1244  O   HOH A2056      15.927 -21.390 -25.905  1.00 53.93           O  
ANISOU 1244  O   HOH A2056     6629   5831   8028   -759   -876   2520       O  
HETATM 1245  O   HOH A2057      21.740 -21.391 -16.284  1.00 31.23           O  
ANISOU 1245  O   HOH A2057     3404   4807   3654   -139    224  -1214       O  
HETATM 1246  O   HOH A2058      24.036 -13.781 -16.377  1.00 35.66           O  
ANISOU 1246  O   HOH A2058     4758   4269   4521   -338  -1026   -954       O  
HETATM 1247  O   HOH A2059      19.693 -18.115  -3.305  1.00 46.76           O  
ANISOU 1247  O   HOH A2059     6598   5113   6053    554    172  -2244       O  
HETATM 1248  O   HOH A2060      17.644 -19.466  -1.817  1.00 47.87           O  
ANISOU 1248  O   HOH A2060     4896   7024   6269     11   -788   2172       O  
HETATM 1249  O   HOH A2061      16.393 -20.891  -8.760  1.00 31.99           O  
ANISOU 1249  O   HOH A2061     4252   3249   4652    283    309    842       O  
HETATM 1250  O   HOH A2062      20.162 -22.696  -9.488  1.00 39.69           O  
ANISOU 1250  O   HOH A2062     7604   1887   5588    104  -1383    425       O  
HETATM 1251  O   HOH A2063      22.828 -16.310 -12.732  1.00 34.63           O  
ANISOU 1251  O   HOH A2063     4915   4476   3766    930    577   -203       O  
HETATM 1252  O   HOH A2064      25.866 -21.767 -11.478  1.00 52.07           O  
ANISOU 1252  O   HOH A2064     6925   5901   6959  -1431   2809  -1028       O  
HETATM 1253  O   HOH A2065      10.889 -18.792 -12.064  1.00 29.36           O  
ANISOU 1253  O   HOH A2065     5151   2347   3656   -790  -1030   -293       O  
HETATM 1254  O   HOH A2066       9.185 -11.064  -2.987  1.00 28.22           O  
ANISOU 1254  O   HOH A2066     4496   5044   1181   1155   1178     52       O  
HETATM 1255  O   HOH A2067      10.911  -8.432  -3.514  1.00 30.77           O  
ANISOU 1255  O   HOH A2067     3261   3879   4549  -1126    917   -336       O  
HETATM 1256  O   HOH A2068       7.412  -9.433  -3.565  1.00 34.10           O  
ANISOU 1256  O   HOH A2068     4129   5033   3792    233  -1704    694       O  
HETATM 1257  O   HOH A2069       5.891 -13.944 -10.980  1.00 29.36           O  
ANISOU 1257  O   HOH A2069     3608   4685   2860   -502    289   -752       O  
HETATM 1258  O   HOH A2070      10.841 -17.251  -2.477  1.00 23.39           O  
ANISOU 1258  O   HOH A2070     3441   1551   3892    262    602    229       O  
HETATM 1259  O   HOH A2071      11.004  -9.855  -1.158  1.00 40.39           O  
ANISOU 1259  O   HOH A2071     6552   4647   4145  -1519   -708    906       O  
HETATM 1260  O   HOH A2072      15.143 -16.464   1.702  1.00 37.07           O  
ANISOU 1260  O   HOH A2072     7448   3406   3231    651   1963   1503       O  
HETATM 1261  O   HOH A2073      14.092 -12.187   3.608  1.00 29.35           O  
ANISOU 1261  O   HOH A2073     5453   3717   1980   -193   -121   1704       O  
HETATM 1262  O   HOH A2074      21.189 -12.967   2.837  1.00 34.85           O  
ANISOU 1262  O   HOH A2074     2826   5263   5151   -241    279   -626       O  
HETATM 1263  O   HOH A2075      21.036 -15.688  -2.538  1.00 27.04           O  
ANISOU 1263  O   HOH A2075     5095   3230   1947    856    228    495       O  
HETATM 1264  O   HOH A2076      12.770 -18.873  -1.545  1.00 26.01           O  
ANISOU 1264  O   HOH A2076     3772   2420   3691   -513   -150    314       O  
HETATM 1265  O   HOH A2077      26.389 -13.688  -0.912  1.00 41.53           O  
ANISOU 1265  O   HOH A2077     6229   7500   2049    546   -434   1565       O  
HETATM 1266  O   HOH A2078      24.870  -6.119  -6.703  1.00 27.35           O  
ANISOU 1266  O   HOH A2078     3436   3796   3157   -519   -529   -119       O  
HETATM 1267  O   HOH A2079      25.017  -4.841  -4.079  1.00 23.89           O  
ANISOU 1267  O   HOH A2079     2763   3423   2890    -95    547   -281       O  
HETATM 1268  O   HOH A2080      28.563 -13.111   0.698  1.00 48.42           O  
ANISOU 1268  O   HOH A2080     6089   8854   3451    586   -402   1819       O  
HETATM 1269  O   HOH A2081      30.623  -9.699  -3.080  1.00 33.80           O  
ANISOU 1269  O   HOH A2081     4766   5527   2547   -815   -258   -825       O  
HETATM 1270  O   HOH A2082      30.041 -10.484  -0.166  1.00 40.97           O  
ANISOU 1270  O   HOH A2082     4658   6397   4510    700  -2406   -983       O  
HETATM 1271  O   HOH A2083      22.340  -5.324  -7.842  1.00 14.82           O  
ANISOU 1271  O   HOH A2083     2138   1966   1525   -383    313    142       O  
HETATM 1272  O   HOH A2084      21.156  -1.135 -13.926  1.00 23.81           O  
ANISOU 1272  O   HOH A2084     2717   2580   3748   -132   -165    677       O  
HETATM 1273  O   HOH A2085      24.171  -5.967 -14.045  1.00 35.55           O  
ANISOU 1273  O   HOH A2085     5023   4098   4384   -216    342   1634       O  
HETATM 1274  O   HOH A2086      18.975  -8.675 -18.606  1.00 28.72           O  
ANISOU 1274  O   HOH A2086     4077   4037   2795   2463    691   -961       O  
HETATM 1275  O   HOH A2087      13.784   1.001 -24.367  1.00 31.74           O  
ANISOU 1275  O   HOH A2087     4135   5878   2044    857    759   1405       O  
HETATM 1276  O   HOH A2088      12.889   3.595 -26.148  1.00 38.13           O  
ANISOU 1276  O   HOH A2088     6186   5566   2732    646  -1398    -63       O  
HETATM 1277  O   HOH A2089      13.114   7.713 -24.643  1.00 35.15           O  
ANISOU 1277  O   HOH A2089     5310   4790   3254   -630  -1136   1529       O  
HETATM 1278  O   HOH A2090      16.040   2.136 -23.837  1.00 41.84           O  
ANISOU 1278  O   HOH A2090     5644   3685   6567    -45    174   -266       O  
HETATM 1279  O   HOH A2091       7.917   3.947 -27.236  1.00 30.66           O  
ANISOU 1279  O   HOH A2091     5210   4074   2363   1473   -756    294       O  
HETATM 1280  O   HOH A2092      16.234   8.862 -26.694  1.00 37.90           O  
ANISOU 1280  O   HOH A2092     4516   5476   4406   1542   1250    626       O  
HETATM 1281  O   HOH B2001      -3.193 -23.213 -11.287  1.00 54.23           O  
ANISOU 1281  O   HOH B2001     4583   9302   6719   -603  -1570   1209       O  
HETATM 1282  O   HOH B2002       8.352 -14.915 -17.409  1.00 58.12           O  
ANISOU 1282  O   HOH B2002     9451   7064   5567  -1871  -1462   -428       O  
HETATM 1283  O   HOH B2003      -3.904 -10.379 -13.100  1.00 47.05           O  
ANISOU 1283  O   HOH B2003     4805   5793   7276   -727    981  -1900       O  
HETATM 1284  O   HOH B2004       3.076 -17.322  -5.400  1.00 59.96           O  
ANISOU 1284  O   HOH B2004     3597   8606  10579   1420   2043   3990       O  
HETATM 1285  O   HOH B2005      -1.306 -13.696  -9.894  1.00 37.72           O  
ANISOU 1285  O   HOH B2005     5151   5697   3482   -450  -2057  -1174       O  
HETATM 1286  O   HOH B2006      -4.082 -19.973  -7.477  1.00 43.41           O  
ANISOU 1286  O   HOH B2006     5407   4641   6444   -879   -424    779       O  
HETATM 1287  O   HOH B2007      26.072  -4.581 -12.497  1.00 43.65           O  
ANISOU 1287  O   HOH B2007     5916   4233   6436  -1528   -322   1685       O  
MASTER      303    0    0    7    2    0    0    6 1277    2    0   14          
END                                                                             



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