HEADER    MEMBRANE PROTEIN                        03-JAN-17   5UEN              
TITLE     CRYSTAL STRUCTURE OF THE HUMAN ADENOSINE A1 RECEPTOR A1AR-BRIL IN     
TITLE    2 COMPLEX WITH THE COVALENT ANTAGONIST DU172 AT 3.2A RESOLUTION        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ADENOSINE RECEPTOR A1,SOLUBLE CYTOCHROME B562,ADENOSINE    
COMPND   3 RECEPTOR A1;                                                         
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 FRAGMENT: UNP P30542 REISUES 2-210, UNP P0ABE7 RESIDUES 23-127, UNP  
COMPND   6 P30542 RESIDUES 228-31,UNP P30542 REISUES 2-210, UNP P0ABE7 RESIDUES 
COMPND   7 23-127, UNP P30542 RESIDUES 228-31,UNP P30542 REISUES 2-210, UNP     
COMPND   8 P0ABE7 RESIDUES 23-127, UNP P30542 RESIDUES 228-31;                  
COMPND   9 SYNONYM: CYTOCHROME B-562;                                           
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ESCHERICHIA COLI;                 
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606, 562;                                           
SOURCE   5 GENE: ADORA1, CYBC;                                                  
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    GPCR, TRANSMEMBRANE, RECEPTOR, ADENOSINE, MEMBRANE PROTEIN            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.GLUKHOVA,D.M.THAL,A.T.NGUYEN,E.A.VECCHIO,M.JORG,P.J.SCAMMELLS,      
AUTHOR   2 L.T.MAY,P.M.SEXTON,A.CHRISTOPOULOS                                   
REVDAT   4   08-JAN-20 5UEN    1       REMARK                                   
REVDAT   3   27-SEP-17 5UEN    1       REMARK                                   
REVDAT   2   15-MAR-17 5UEN    1       JRNL                                     
REVDAT   1   01-MAR-17 5UEN    0                                                
JRNL        AUTH   A.GLUKHOVA,D.M.THAL,A.T.NGUYEN,E.A.VECCHIO,M.JORG,           
JRNL        AUTH 2 P.J.SCAMMELLS,L.T.MAY,P.M.SEXTON,A.CHRISTOPOULOS             
JRNL        TITL   STRUCTURE OF THE ADENOSINE A1 RECEPTOR REVEALS THE BASIS FOR 
JRNL        TITL 2 SUBTYPE SELECTIVITY.                                         
JRNL        REF    CELL                          V. 168   867 2017              
JRNL        REFN                   ISSN 1097-4172                               
JRNL        PMID   28235198                                                     
JRNL        DOI    10.1016/J.CELL.2017.01.042                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0155                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 21759                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.288                           
REMARK   3   R VALUE            (WORKING SET) : 0.286                           
REMARK   3   FREE R VALUE                     : 0.316                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1105                            
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) : 3.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.28                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1598                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.17                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3660                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 69                           
REMARK   3   BIN FREE R VALUE                    : 0.4240                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6061                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 189                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 92.83                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -6.32000                                             
REMARK   3    B22 (A**2) : 6.09000                                              
REMARK   3    B33 (A**2) : 0.23000                                              
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.553         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.482         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 59.391        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : NULL                          
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : NULL                          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  NULL ;  NULL ;  NULL       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  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 : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : NULL                                          
REMARK   3   ION PROBE RADIUS   : NULL                                          
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : WITH TLS ADDED                                 
REMARK   4                                                                      
REMARK   4 5UEN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JAN-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000224321.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-MAR-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0-8.0                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX2                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9537                             
REMARK 200  MONOCHROMATOR                  : SILICON DOUBLE CRYSTAL             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.5.15                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23000                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 14.10                              
REMARK 200  R MERGE                    (I) : 0.32800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 14.40                              
REMARK 200  R MERGE FOR SHELL          (I) : 2.76700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> 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 2.5.6                                          
REMARK 200 STARTING MODEL: 4EIY                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.15                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.63                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES PH 7.0-8.0, 28-38% PEG      
REMARK 280  300 AND 500-700 MM NH4F, LIPIDIC CUBIC PHASE, TEMPERATURE 293K      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   X,-Y,-Z                                                 
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   -X,-Y+1/2,Z+1/2                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       56.48000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       62.08550            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       56.48000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       62.08550            
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 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     GLY A     0                                                      
REMARK 465     PRO A     1                                                      
REMARK 465     PRO A     2                                                      
REMARK 465     PRO A     3                                                      
REMARK 465     LEU A  1014                                                      
REMARK 465     LYS A  1015                                                      
REMARK 465     VAL A  1016                                                      
REMARK 465     ILE A  1017                                                      
REMARK 465     GLU A  1018                                                      
REMARK 465     LYS A  1019                                                      
REMARK 465     ALA A  1020                                                      
REMARK 465     ASP A  1021                                                      
REMARK 465     ASN A  1022                                                      
REMARK 465     ALA A  1023                                                      
REMARK 465     ALA A  1024                                                      
REMARK 465     GLN A  1025                                                      
REMARK 465     GLN A  1041                                                      
REMARK 465     LYS A  1042                                                      
REMARK 465     ALA A  1043                                                      
REMARK 465     THR A  1044                                                      
REMARK 465     PRO A  1045                                                      
REMARK 465     PRO A  1046                                                      
REMARK 465     LYS A  1047                                                      
REMARK 465     LEU A  1048                                                      
REMARK 465     GLU A  1049                                                      
REMARK 465     ASP A  1050                                                      
REMARK 465     LYS A  1051                                                      
REMARK 465     SER A  1052                                                      
REMARK 465     PRO A  1053                                                      
REMARK 465     ASP A  1054                                                      
REMARK 465     SER A  1055                                                      
REMARK 465     GLN A   317                                                      
REMARK 465     GLY B     0                                                      
REMARK 465     PRO B     1                                                      
REMARK 465     PRO B     2                                                      
REMARK 465     PRO B     3                                                      
REMARK 465     SER B     4                                                      
REMARK 465     ILE B     5                                                      
REMARK 465     ALA B  1043                                                      
REMARK 465     THR B  1044                                                      
REMARK 465     PRO B  1045                                                      
REMARK 465     PRO B  1046                                                      
REMARK 465     LYS B  1047                                                      
REMARK 465     LEU B  1048                                                      
REMARK 465     GLU B  1049                                                      
REMARK 465     ASP B  1050                                                      
REMARK 465     LYS B  1051                                                      
REMARK 465     SER B  1052                                                      
REMARK 465     PRO B  1053                                                      
REMARK 465     ASP B  1054                                                      
REMARK 465     SER B  1055                                                      
REMARK 465     PRO B  1056                                                      
REMARK 465     GLU B  1057                                                      
REMARK 465     MET B  1058                                                      
REMARK 465     LYS B  1059                                                      
REMARK 465     ASP B  1060                                                      
REMARK 465     PHE B  1061                                                      
REMARK 465     GLN B   310                                                      
REMARK 465     PRO B   311                                                      
REMARK 465     LEU B   312                                                      
REMARK 465     GLU B   313                                                      
REMARK 465     VAL B   314                                                      
REMARK 465     LEU B   315                                                      
REMARK 465     PHE B   316                                                      
REMARK 465     GLN B   317                                                      
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    ARG A  41       56.18    -99.57                                   
REMARK 500    VAL A 189      -61.70   -108.85                                   
REMARK 500    ARG B  41       56.07    -99.62                                   
REMARK 500    VAL B 189      -62.29   -109.33                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     OLA A 1204                                                       
REMARK 610     OLA A 1205                                                       
REMARK 610     OLA B 1204                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DU1 A 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1202                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1203                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1204                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1205                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DU1 B 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA B 1202                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA B 1203                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA B 1204                
DBREF  5UEN A    2   211  UNP    P30542   AA1R_HUMAN       2    211             
DBREF  5UEN A 1001  1105  UNP    P0ABE7   C562_ECOLX      23    127             
DBREF  5UEN A  228   311  UNP    P30542   AA1R_HUMAN     228    311             
DBREF  5UEN B    2   211  UNP    P30542   AA1R_HUMAN       2    211             
DBREF  5UEN B 1001  1105  UNP    P0ABE7   C562_ECOLX      23    127             
DBREF  5UEN B  228   311  UNP    P30542   AA1R_HUMAN     228    311             
SEQADV 5UEN GLY A    0  UNP  P30542              EXPRESSION TAG                 
SEQADV 5UEN PRO A    1  UNP  P30542              EXPRESSION TAG                 
SEQADV 5UEN ALA A  159  UNP  P30542    ASN   159 ENGINEERED MUTATION            
SEQADV 5UEN TRP A 1007  UNP  P0ABE7    MET    29 CONFLICT                       
SEQADV 5UEN ILE A 1102  UNP  P0ABE7    HIS   124 CONFLICT                       
SEQADV 5UEN LEU A 1106  UNP  P0ABE7              LINKER                         
SEQADV 5UEN GLU A  220  UNP  P0ABE7              LINKER                         
SEQADV 5UEN ARG A  221  UNP  P0ABE7              LINKER                         
SEQADV 5UEN ALA A  222  UNP  P0ABE7              LINKER                         
SEQADV 5UEN ARG A  223  UNP  P0ABE7              LINKER                         
SEQADV 5UEN SER A  224  UNP  P0ABE7              LINKER                         
SEQADV 5UEN THR A  225  UNP  P0ABE7              LINKER                         
SEQADV 5UEN LEU A  226  UNP  P0ABE7              LINKER                         
SEQADV 5UEN GLN A  227  UNP  P0ABE7              LINKER                         
SEQADV 5UEN LEU A  312  UNP  P30542              EXPRESSION TAG                 
SEQADV 5UEN GLU A  313  UNP  P30542              EXPRESSION TAG                 
SEQADV 5UEN VAL A  314  UNP  P30542              EXPRESSION TAG                 
SEQADV 5UEN LEU A  315  UNP  P30542              EXPRESSION TAG                 
SEQADV 5UEN PHE A  316  UNP  P30542              EXPRESSION TAG                 
SEQADV 5UEN GLN A  317  UNP  P30542              EXPRESSION TAG                 
SEQADV 5UEN GLY B    0  UNP  P30542              EXPRESSION TAG                 
SEQADV 5UEN PRO B    1  UNP  P30542              EXPRESSION TAG                 
SEQADV 5UEN ALA B  159  UNP  P30542    ASN   159 ENGINEERED MUTATION            
SEQADV 5UEN TRP B 1007  UNP  P0ABE7    MET    29 CONFLICT                       
SEQADV 5UEN ILE B 1102  UNP  P0ABE7    HIS   124 CONFLICT                       
SEQADV 5UEN LEU B 1106  UNP  P0ABE7              LINKER                         
SEQADV 5UEN GLU B  220  UNP  P0ABE7              LINKER                         
SEQADV 5UEN ARG B  221  UNP  P0ABE7              LINKER                         
SEQADV 5UEN ALA B  222  UNP  P0ABE7              LINKER                         
SEQADV 5UEN ARG B  223  UNP  P0ABE7              LINKER                         
SEQADV 5UEN SER B  224  UNP  P0ABE7              LINKER                         
SEQADV 5UEN THR B  225  UNP  P0ABE7              LINKER                         
SEQADV 5UEN LEU B  226  UNP  P0ABE7              LINKER                         
SEQADV 5UEN GLN B  227  UNP  P0ABE7              LINKER                         
SEQADV 5UEN LEU B  312  UNP  P30542              EXPRESSION TAG                 
SEQADV 5UEN GLU B  313  UNP  P30542              EXPRESSION TAG                 
SEQADV 5UEN VAL B  314  UNP  P30542              EXPRESSION TAG                 
SEQADV 5UEN LEU B  315  UNP  P30542              EXPRESSION TAG                 
SEQADV 5UEN PHE B  316  UNP  P30542              EXPRESSION TAG                 
SEQADV 5UEN GLN B  317  UNP  P30542              EXPRESSION TAG                 
SEQRES   1 A  416  GLY PRO PRO PRO SER ILE SER ALA PHE GLN ALA ALA TYR          
SEQRES   2 A  416  ILE GLY ILE GLU VAL LEU ILE ALA LEU VAL SER VAL PRO          
SEQRES   3 A  416  GLY ASN VAL LEU VAL ILE TRP ALA VAL LYS VAL ASN GLN          
SEQRES   4 A  416  ALA LEU ARG ASP ALA THR PHE CYS PHE ILE VAL SER LEU          
SEQRES   5 A  416  ALA VAL ALA ASP VAL ALA VAL GLY ALA LEU VAL ILE PRO          
SEQRES   6 A  416  LEU ALA ILE LEU ILE ASN ILE GLY PRO GLN THR TYR PHE          
SEQRES   7 A  416  HIS THR CYS LEU MET VAL ALA CYS PRO VAL LEU ILE LEU          
SEQRES   8 A  416  THR GLN SER SER ILE LEU ALA LEU LEU ALA ILE ALA VAL          
SEQRES   9 A  416  ASP ARG TYR LEU ARG VAL LYS ILE PRO LEU ARG TYR LYS          
SEQRES  10 A  416  MET VAL VAL THR PRO ARG ARG ALA ALA VAL ALA ILE ALA          
SEQRES  11 A  416  GLY CYS TRP ILE LEU SER PHE VAL VAL GLY LEU THR PRO          
SEQRES  12 A  416  MET PHE GLY TRP ASN ASN LEU SER ALA VAL GLU ARG ALA          
SEQRES  13 A  416  TRP ALA ALA ALA GLY SER MET GLY GLU PRO VAL ILE LYS          
SEQRES  14 A  416  CYS GLU PHE GLU LYS VAL ILE SER MET GLU TYR MET VAL          
SEQRES  15 A  416  TYR PHE ASN PHE PHE VAL TRP VAL LEU PRO PRO LEU LEU          
SEQRES  16 A  416  LEU MET VAL LEU ILE TYR LEU GLU VAL PHE TYR LEU ILE          
SEQRES  17 A  416  ARG LYS GLN LEU ALA ASP LEU GLU ASP ASN TRP GLU THR          
SEQRES  18 A  416  LEU ASN ASP ASN LEU LYS VAL ILE GLU LYS ALA ASP ASN          
SEQRES  19 A  416  ALA ALA GLN VAL LYS ASP ALA LEU THR LYS MET ARG ALA          
SEQRES  20 A  416  ALA ALA LEU ASP ALA GLN LYS ALA THR PRO PRO LYS LEU          
SEQRES  21 A  416  GLU ASP LYS SER PRO ASP SER PRO GLU MET LYS ASP PHE          
SEQRES  22 A  416  ARG HIS GLY PHE ASP ILE LEU VAL GLY GLN ILE ASP ASP          
SEQRES  23 A  416  ALA LEU LYS LEU ALA ASN GLU GLY LYS VAL LYS GLU ALA          
SEQRES  24 A  416  GLN ALA ALA ALA GLU GLN LEU LYS THR THR ARG ASN ALA          
SEQRES  25 A  416  TYR ILE GLN LYS TYR LEU GLU ARG ALA ARG SER THR LEU          
SEQRES  26 A  416  GLN LYS GLU LEU LYS ILE ALA LYS SER LEU ALA LEU ILE          
SEQRES  27 A  416  LEU PHE LEU PHE ALA LEU SER TRP LEU PRO LEU HIS ILE          
SEQRES  28 A  416  LEU ASN CYS ILE THR LEU PHE CYS PRO SER CYS HIS LYS          
SEQRES  29 A  416  PRO SER ILE LEU THR TYR ILE ALA ILE PHE LEU THR HIS          
SEQRES  30 A  416  GLY ASN SER ALA MET ASN PRO ILE VAL TYR ALA PHE ARG          
SEQRES  31 A  416  ILE GLN LYS PHE ARG VAL THR PHE LEU LYS ILE TRP ASN          
SEQRES  32 A  416  ASP HIS PHE ARG CYS GLN PRO LEU GLU VAL LEU PHE GLN          
SEQRES   1 B  416  GLY PRO PRO PRO SER ILE SER ALA PHE GLN ALA ALA TYR          
SEQRES   2 B  416  ILE GLY ILE GLU VAL LEU ILE ALA LEU VAL SER VAL PRO          
SEQRES   3 B  416  GLY ASN VAL LEU VAL ILE TRP ALA VAL LYS VAL ASN GLN          
SEQRES   4 B  416  ALA LEU ARG ASP ALA THR PHE CYS PHE ILE VAL SER LEU          
SEQRES   5 B  416  ALA VAL ALA ASP VAL ALA VAL GLY ALA LEU VAL ILE PRO          
SEQRES   6 B  416  LEU ALA ILE LEU ILE ASN ILE GLY PRO GLN THR TYR PHE          
SEQRES   7 B  416  HIS THR CYS LEU MET VAL ALA CYS PRO VAL LEU ILE LEU          
SEQRES   8 B  416  THR GLN SER SER ILE LEU ALA LEU LEU ALA ILE ALA VAL          
SEQRES   9 B  416  ASP ARG TYR LEU ARG VAL LYS ILE PRO LEU ARG TYR LYS          
SEQRES  10 B  416  MET VAL VAL THR PRO ARG ARG ALA ALA VAL ALA ILE ALA          
SEQRES  11 B  416  GLY CYS TRP ILE LEU SER PHE VAL VAL GLY LEU THR PRO          
SEQRES  12 B  416  MET PHE GLY TRP ASN ASN LEU SER ALA VAL GLU ARG ALA          
SEQRES  13 B  416  TRP ALA ALA ALA GLY SER MET GLY GLU PRO VAL ILE LYS          
SEQRES  14 B  416  CYS GLU PHE GLU LYS VAL ILE SER MET GLU TYR MET VAL          
SEQRES  15 B  416  TYR PHE ASN PHE PHE VAL TRP VAL LEU PRO PRO LEU LEU          
SEQRES  16 B  416  LEU MET VAL LEU ILE TYR LEU GLU VAL PHE TYR LEU ILE          
SEQRES  17 B  416  ARG LYS GLN LEU ALA ASP LEU GLU ASP ASN TRP GLU THR          
SEQRES  18 B  416  LEU ASN ASP ASN LEU LYS VAL ILE GLU LYS ALA ASP ASN          
SEQRES  19 B  416  ALA ALA GLN VAL LYS ASP ALA LEU THR LYS MET ARG ALA          
SEQRES  20 B  416  ALA ALA LEU ASP ALA GLN LYS ALA THR PRO PRO LYS LEU          
SEQRES  21 B  416  GLU ASP LYS SER PRO ASP SER PRO GLU MET LYS ASP PHE          
SEQRES  22 B  416  ARG HIS GLY PHE ASP ILE LEU VAL GLY GLN ILE ASP ASP          
SEQRES  23 B  416  ALA LEU LYS LEU ALA ASN GLU GLY LYS VAL LYS GLU ALA          
SEQRES  24 B  416  GLN ALA ALA ALA GLU GLN LEU LYS THR THR ARG ASN ALA          
SEQRES  25 B  416  TYR ILE GLN LYS TYR LEU GLU ARG ALA ARG SER THR LEU          
SEQRES  26 B  416  GLN LYS GLU LEU LYS ILE ALA LYS SER LEU ALA LEU ILE          
SEQRES  27 B  416  LEU PHE LEU PHE ALA LEU SER TRP LEU PRO LEU HIS ILE          
SEQRES  28 B  416  LEU ASN CYS ILE THR LEU PHE CYS PRO SER CYS HIS LYS          
SEQRES  29 B  416  PRO SER ILE LEU THR TYR ILE ALA ILE PHE LEU THR HIS          
SEQRES  30 B  416  GLY ASN SER ALA MET ASN PRO ILE VAL TYR ALA PHE ARG          
SEQRES  31 B  416  ILE GLN LYS PHE ARG VAL THR PHE LEU LYS ILE TRP ASN          
SEQRES  32 B  416  ASP HIS PHE ARG CYS GLN PRO LEU GLU VAL LEU PHE GLN          
HET    DU1  A1201      35                                                       
HET    OLA  A1202      20                                                       
HET    OLA  A1203      20                                                       
HET    OLA  A1204      14                                                       
HET    OLA  A1205      12                                                       
HET    DU1  B1201      35                                                       
HET    OLA  B1202      20                                                       
HET    OLA  B1203      20                                                       
HET    OLA  B1204      13                                                       
HETNAM     DU1 4-{[3-(8-CYCLOHEXYL-2,6-DIOXO-1-PROPYL-1,2,6,7-                  
HETNAM   2 DU1  TETRAHYDRO-3H-PURIN-3-YL)PROPYL]CARBAMOYL}BENZENE-1-            
HETNAM   3 DU1  SULFONYL FLUORIDE                                               
HETNAM     OLA OLEIC ACID                                                       
FORMUL   3  DU1    2(C24 H30 F N5 O5 S)                                         
FORMUL   4  OLA    7(C18 H34 O2)                                                
HELIX    1 AA1 SER A    6  ASN A   37  1                                  32    
HELIX    2 AA2 GLN A   38  ARG A   41  5                                   4    
HELIX    3 AA3 ASP A   42  LEU A   61  1                                  20    
HELIX    4 AA4 LEU A   61  GLY A   72  1                                  12    
HELIX    5 AA5 PHE A   77  ILE A  111  1                                  35    
HELIX    6 AA6 ARG A  114  VAL A  119  1                                   6    
HELIX    7 AA7 THR A  120  THR A  141  1                                  22    
HELIX    8 AA8 PRO A  142  GLY A  145  5                                   4    
HELIX    9 AA9 ASN A  148  GLY A  160  1                                  13    
HELIX   10 AB1 GLU A  170  ILE A  175  1                                   6    
HELIX   11 AB2 SER A  176  PHE A  183  1                                   8    
HELIX   12 AB3 PHE A  183  VAL A  189  1                                   7    
HELIX   13 AB4 VAL A  189  ASN A 1013  1                                  36    
HELIX   14 AB5 LYS A 1027  ALA A 1040  1                                  14    
HELIX   15 AB6 GLU A 1057  GLY A 1082  1                                  26    
HELIX   16 AB7 LYS A 1083  TYR A 1101  1                                  19    
HELIX   17 AB8 TYR A 1101  CYS A  260  1                                  47    
HELIX   18 AB9 PRO A  266  ILE A  292  1                                  27    
HELIX   19 AC1 ILE A  292  PHE A  307  1                                  16    
HELIX   20 AC2 CYS A  309  PHE A  316  1                                   8    
HELIX   21 AC3 ALA B    7  ASN B   37  1                                  31    
HELIX   22 AC4 GLN B   38  ARG B   41  5                                   4    
HELIX   23 AC5 ASP B   42  LEU B   61  1                                  20    
HELIX   24 AC6 LEU B   61  GLY B   72  1                                  12    
HELIX   25 AC7 PHE B   77  ILE B  111  1                                  35    
HELIX   26 AC8 ARG B  114  VAL B  119  1                                   6    
HELIX   27 AC9 THR B  120  THR B  141  1                                  22    
HELIX   28 AD1 PRO B  142  GLY B  145  5                                   4    
HELIX   29 AD2 ASN B  148  GLY B  160  1                                  13    
HELIX   30 AD3 GLU B  170  ILE B  175  1                                   6    
HELIX   31 AD4 SER B  176  PHE B  183  1                                   8    
HELIX   32 AD5 PHE B  183  VAL B  189  1                                   7    
HELIX   33 AD6 VAL B  189  LYS B 1019  1                                  42    
HELIX   34 AD7 ASN B 1022  LYS B 1042  1                                  21    
HELIX   35 AD8 HIS B 1063  GLY B 1082  1                                  20    
HELIX   36 AD9 LYS B 1083  TYR B 1101  1                                  19    
HELIX   37 AE1 TYR B 1101  CYS B  260  1                                  47    
HELIX   38 AE2 PRO B  266  ILE B  292  1                                  27    
HELIX   39 AE3 ILE B  292  PHE B  307  1                                  16    
SHEET    1 AA1 2 THR A  75  TYR A  76  0                                        
SHEET    2 AA1 2 VAL A 166  ILE A 167 -1  O  ILE A 167   N  THR A  75           
SHEET    1 AA2 2 THR B  75  TYR B  76  0                                        
SHEET    2 AA2 2 VAL B 166  ILE B 167 -1  O  ILE B 167   N  THR B  75           
SSBOND   1 CYS A   80    CYS A  169                          1555   1555  2.02  
SSBOND   2 CYS A  260    CYS A  263                          1555   1555  2.04  
SSBOND   3 CYS B   80    CYS B  169                          1555   1555  2.04  
SSBOND   4 CYS B  260    CYS B  263                          1555   1555  2.04  
LINK         OH  TYR A 271                 S   DU1 A1201     1555   1555  1.61  
LINK         OH  TYR B 271                 S   DU1 B1201     1555   1555  1.61  
SITE     1 AC1 13 TYR A  12  ASN A  70  VAL A  87  LEU A  88                    
SITE     2 AC1 13 THR A  91  PHE A 171  GLU A 172  MET A 180                    
SITE     3 AC1 13 TRP A 247  LEU A 250  ASN A 254  TYR A 271                    
SITE     4 AC1 13 ILE A 274                                                     
SITE     1 AC2  4 ALA A 125  VAL A 137  PHE A 144  OLA A1203                    
SITE     1 AC3  4 CYS A  46  VAL A  49  ILE A  89  OLA A1202                    
SITE     1 AC4  3 ILE A   5  ALA A   7  LEU A  18                               
SITE     1 AC5  4 PHE A   8  ASN A  70  ILE A 268  TYR A 271                    
SITE     1 AC6 11 TYR B  12  VAL B  87  LEU B  88  THR B  91                    
SITE     2 AC6 11 PHE B 171  MET B 180  TRP B 247  LEU B 250                    
SITE     3 AC6 11 ASN B 254  TYR B 271  ILE B 274                               
SITE     1 AC7  4 ALA B 125  PHE B 136  VAL B 137  OLA B1203                    
SITE     1 AC8  4 VAL B  49  ILE B  89  TRP B 132  OLA B1202                    
SITE     1 AC9  2 ALA B  10  VAL B  17                                          
CRYST1   96.492  112.960  124.171  90.00  90.00  90.00 P 2 21 21     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010364  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008853  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008053        0.00000                         
ATOM      1  N   SER A   4      68.894  48.668 161.549  1.00 96.89           N  
ANISOU    1  N   SER A   4    14529  11500  10785    577   -992     87       N  
ATOM      2  CA  SER A   4      69.423  49.799 160.724  1.00 96.11           C  
ANISOU    2  CA  SER A   4    14372  11400  10743    541   -948     35       C  
ATOM      3  C   SER A   4      68.352  50.375 159.779  1.00 94.30           C  
ANISOU    3  C   SER A   4    14159  11154  10516    511   -857     59       C  
ATOM      4  O   SER A   4      68.614  50.614 158.596  1.00 94.66           O  
ANISOU    4  O   SER A   4    14157  11191  10618    492   -812     45       O  
ATOM      5  CB  SER A   4      70.675  49.345 159.947  1.00 96.80           C  
ANISOU    5  CB  SER A   4    14380  11490  10909    553   -972      1       C  
ATOM      6  OG  SER A   4      70.420  48.175 159.183  1.00 96.12           O  
ANISOU    6  OG  SER A   4    14293  11387  10841    578   -960     36       O  
ATOM      7  N   ILE A   5      67.147  50.593 160.316  1.00 92.50           N  
ANISOU    7  N   ILE A   5    13997  10926  10222    508   -829     98       N  
ATOM      8  CA  ILE A   5      66.043  51.231 159.579  1.00 90.40           C  
ANISOU    8  CA  ILE A   5    13749  10647   9950    482   -746    124       C  
ATOM      9  C   ILE A   5      65.687  52.561 160.264  1.00 89.01           C  
ANISOU    9  C   ILE A   5    13602  10475   9740    465   -725    100       C  
ATOM     10  O   ILE A   5      65.637  52.661 161.495  1.00 88.13           O  
ANISOU   10  O   ILE A   5    13530  10379   9573    479   -764     92       O  
ATOM     11  CB  ILE A   5      64.816  50.292 159.437  1.00 89.90           C  
ANISOU   11  CB  ILE A   5    13731  10580   9845    495   -722    197       C  
ATOM     12  CG1 ILE A   5      65.165  49.130 158.494  1.00 90.31           C  
ANISOU   12  CG1 ILE A   5    13752  10618   9941    506   -732    212       C  
ATOM     13  CG2 ILE A   5      63.592  51.043 158.908  1.00 88.74           C  
ANISOU   13  CG2 ILE A   5    13606  10430   9681    471   -642    227       C  
ATOM     14  CD1 ILE A   5      64.157  47.996 158.469  1.00 90.30           C  
ANISOU   14  CD1 ILE A   5    13797  10609   9903    517   -729    280       C  
ATOM     15  N   SER A   6      65.448  53.572 159.434  1.00 87.07           N  
ANISOU   15  N   SER A   6    13338  10214   9528    435   -662     87       N  
ATOM     16  CA  SER A   6      65.250  54.952 159.877  1.00 85.42           C  
ANISOU   16  CA  SER A   6    13151   9997   9306    416   -638     55       C  
ATOM     17  C   SER A   6      63.825  55.184 160.390  1.00 83.35           C  
ANISOU   17  C   SER A   6    12954   9738   8975    430   -597     97       C  
ATOM     18  O   SER A   6      62.853  54.666 159.823  1.00 83.25           O  
ANISOU   18  O   SER A   6    12953   9728   8950    435   -554    154       O  
ATOM     19  CB  SER A   6      65.553  55.908 158.714  1.00 85.60           C  
ANISOU   19  CB  SER A   6    13129   9997   9396    379   -586     32       C  
ATOM     20  OG  SER A   6      65.316  57.258 159.059  1.00 86.72           O  
ANISOU   20  OG  SER A   6    13296  10121   9531    361   -561      2       O  
ATOM     21  N   ALA A   7      63.705  55.981 161.454  1.00 81.22           N  
ANISOU   21  N   ALA A   7    12725   9474   8661    435   -608     66       N  
ATOM     22  CA  ALA A   7      62.403  56.336 162.051  1.00 79.61           C  
ANISOU   22  CA  ALA A   7    12580   9278   8388    452   -567     96       C  
ATOM     23  C   ALA A   7      61.428  56.948 161.035  1.00 77.12           C  
ANISOU   23  C   ALA A   7    12261   8943   8096    440   -483    129       C  
ATOM     24  O   ALA A   7      60.212  56.716 161.109  1.00 76.31           O  
ANISOU   24  O   ALA A   7    12190   8856   7947    456   -443    183       O  
ATOM     25  CB  ALA A   7      62.607  57.294 163.219  1.00 80.71           C  
ANISOU   25  CB  ALA A   7    12758   9419   8487    456   -590     41       C  
ATOM     26  N   PHE A   8      61.975  57.727 160.101  1.00 74.92           N  
ANISOU   26  N   PHE A   8    11942   8635   7887    410   -459     99       N  
ATOM     27  CA  PHE A   8      61.215  58.259 158.973  1.00 73.17           C  
ANISOU   27  CA  PHE A   8    11709   8394   7697    395   -386    132       C  
ATOM     28  C   PHE A   8      60.685  57.142 158.071  1.00 71.17           C  
ANISOU   28  C   PHE A   8    11435   8156   7449    397   -366    197       C  
ATOM     29  O   PHE A   8      59.519  57.160 157.675  1.00 69.73           O  
ANISOU   29  O   PHE A   8    11268   7978   7246    402   -314    249       O  
ATOM     30  CB  PHE A   8      62.078  59.229 158.136  1.00 73.47           C  
ANISOU   30  CB  PHE A   8    11705   8399   7811    358   -373     89       C  
ATOM     31  CG  PHE A   8      62.277  60.617 158.720  1.00 74.07           C  
ANISOU   31  CG  PHE A   8    11806   8445   7890    348   -370     35       C  
ATOM     32  CD1 PHE A   8      61.668  61.063 159.903  1.00 74.58           C  
ANISOU   32  CD1 PHE A   8    11931   8513   7892    376   -373     20       C  
ATOM     33  CD2 PHE A   8      63.074  61.518 158.017  1.00 74.05           C  
ANISOU   33  CD2 PHE A   8    11767   8410   7957    308   -361      0       C  
ATOM     34  CE1 PHE A   8      61.885  62.347 160.366  1.00 75.25           C  
ANISOU   34  CE1 PHE A   8    12042   8564   7984    366   -370    -34       C  
ATOM     35  CE2 PHE A   8      63.290  62.808 158.480  1.00 74.41           C  
ANISOU   35  CE2 PHE A   8    11837   8419   8013    293   -360    -51       C  
ATOM     36  CZ  PHE A   8      62.695  63.223 159.656  1.00 75.09           C  
ANISOU   36  CZ  PHE A   8    11987   8503   8037    323   -366    -70       C  
ATOM     37  N   GLN A   9      61.540  56.178 157.752  1.00 70.48           N  
ANISOU   37  N   GLN A   9    11313   8075   7390    393   -409    191       N  
ATOM     38  CA  GLN A   9      61.151  55.009 156.953  1.00 69.72           C  
ANISOU   38  CA  GLN A   9    11202   7988   7298    395   -399    243       C  
ATOM     39  C   GLN A   9      60.074  54.186 157.663  1.00 68.54           C  
ANISOU   39  C   GLN A   9    11100   7861   7079    419   -404    300       C  
ATOM     40  O   GLN A   9      59.071  53.776 157.047  1.00 68.68           O  
ANISOU   40  O   GLN A   9    11125   7886   7085    415   -364    357       O  
ATOM     41  CB  GLN A   9      62.368  54.131 156.632  1.00 70.40           C  
ANISOU   41  CB  GLN A   9    11246   8076   7426    394   -450    217       C  
ATOM     42  CG  GLN A   9      62.156  53.221 155.432  1.00 70.50           C  
ANISOU   42  CG  GLN A   9    11233   8086   7464    388   -429    254       C  
ATOM     43  CD  GLN A   9      63.340  52.314 155.146  1.00 71.34           C  
ANISOU   43  CD  GLN A   9    11299   8194   7612    396   -477    225       C  
ATOM     44  OE1 GLN A   9      64.425  52.474 155.712  1.00 72.41           O  
ANISOU   44  OE1 GLN A   9    11412   8331   7766    403   -525    175       O  
ATOM     45  NE2 GLN A   9      63.133  51.350 154.251  1.00 71.41           N  
ANISOU   45  NE2 GLN A   9    11297   8200   7634    398   -467    254       N  
ATOM     46  N   ALA A  10      60.285  53.960 158.958  1.00 67.10           N  
ANISOU   46  N   ALA A  10    10950   7694   6849    441   -453    285       N  
ATOM     47  CA  ALA A  10      59.281  53.332 159.814  1.00 66.08           C  
ANISOU   47  CA  ALA A  10    10870   7591   6646    462   -457    337       C  
ATOM     48  C   ALA A  10      57.961  54.107 159.825  1.00 65.01           C  
ANISOU   48  C   ALA A  10    10760   7465   6475    464   -389    370       C  
ATOM     49  O   ALA A  10      56.892  53.501 159.787  1.00 64.12           O  
ANISOU   49  O   ALA A  10    10665   7372   6324    468   -365    434       O  
ATOM     50  CB  ALA A  10      59.812  53.181 161.232  1.00 66.85           C  
ANISOU   50  CB  ALA A  10    10998   7705   6695    483   -519    308       C  
ATOM     51  N   ALA A  11      58.045  55.438 159.875  1.00 64.86           N  
ANISOU   51  N   ALA A  11    10742   7431   6470    461   -359    327       N  
ATOM     52  CA  ALA A  11      56.852  56.296 159.802  1.00 64.26           C  
ANISOU   52  CA  ALA A  11    10686   7358   6370    469   -291    353       C  
ATOM     53  C   ALA A  11      56.128  56.185 158.452  1.00 62.67           C  
ANISOU   53  C   ALA A  11    10455   7151   6203    451   -238    406       C  
ATOM     54  O   ALA A  11      54.900  56.055 158.411  1.00 62.12           O  
ANISOU   54  O   ALA A  11    10399   7104   6098    460   -197    464       O  
ATOM     55  CB  ALA A  11      57.217  57.744 160.089  1.00 64.86           C  
ANISOU   55  CB  ALA A  11    10771   7407   6463    469   -277    290       C  
ATOM     56  N   TYR A  12      56.893  56.241 157.362  1.00 61.49           N  
ANISOU   56  N   TYR A  12    10264   6977   6123    424   -238    386       N  
ATOM     57  CA  TYR A  12      56.355  56.009 156.016  1.00 60.86           C  
ANISOU   57  CA  TYR A  12    10154   6894   6075    403   -196    433       C  
ATOM     58  C   TYR A  12      55.641  54.657 155.939  1.00 60.47           C  
ANISOU   58  C   TYR A  12    10112   6871   5990    405   -205    497       C  
ATOM     59  O   TYR A  12      54.446  54.589 155.582  1.00 60.50           O  
ANISOU   59  O   TYR A  12    10122   6892   5971    404   -163    556       O  
ATOM     60  CB  TYR A  12      57.468  56.093 154.954  1.00 60.65           C  
ANISOU   60  CB  TYR A  12    10080   6844   6120    375   -204    398       C  
ATOM     61  CG  TYR A  12      57.074  55.529 153.605  1.00 60.24           C  
ANISOU   61  CG  TYR A  12    10000   6796   6092    353   -174    443       C  
ATOM     62  CD1 TYR A  12      56.199  56.220 152.768  1.00 59.92           C  
ANISOU   62  CD1 TYR A  12     9951   6753   6060    341   -114    480       C  
ATOM     63  CD2 TYR A  12      57.565  54.292 153.170  1.00 60.17           C  
ANISOU   63  CD2 TYR A  12     9973   6791   6096    347   -208    448       C  
ATOM     64  CE1 TYR A  12      55.826  55.700 151.535  1.00 59.55           C  
ANISOU   64  CE1 TYR A  12     9879   6714   6030    319    -89    521       C  
ATOM     65  CE2 TYR A  12      57.195  53.766 151.939  1.00 59.52           C  
ANISOU   65  CE2 TYR A  12     9869   6713   6031    327   -182    484       C  
ATOM     66  CZ  TYR A  12      56.332  54.471 151.127  1.00 59.23           C  
ANISOU   66  CZ  TYR A  12     9825   6680   5999    311   -123    520       C  
ATOM     67  OH  TYR A  12      55.965  53.946 149.915  1.00 58.85           O  
ANISOU   67  OH  TYR A  12     9757   6639   5963    288   -101    556       O  
ATOM     68  N   ILE A  13      56.374  53.600 156.305  1.00 60.14           N  
ANISOU   68  N   ILE A  13    10073   6832   5946    409   -264    485       N  
ATOM     69  CA  ILE A  13      55.836  52.228 156.303  1.00 59.76           C  
ANISOU   69  CA  ILE A  13    10038   6798   5867    409   -285    541       C  
ATOM     70  C   ILE A  13      54.570  52.120 157.168  1.00 60.04           C  
ANISOU   70  C   ILE A  13    10112   6866   5831    423   -266    596       C  
ATOM     71  O   ILE A  13      53.575  51.521 156.743  1.00 59.72           O  
ANISOU   71  O   ILE A  13    10075   6843   5773    411   -243    660       O  
ATOM     72  CB  ILE A  13      56.902  51.197 156.757  1.00 59.79           C  
ANISOU   72  CB  ILE A  13    10043   6793   5879    419   -357    515       C  
ATOM     73  CG1 ILE A  13      58.015  51.083 155.703  1.00 59.60           C  
ANISOU   73  CG1 ILE A  13     9973   6745   5927    405   -368    472       C  
ATOM     74  CG2 ILE A  13      56.284  49.816 157.001  1.00 59.50           C  
ANISOU   74  CG2 ILE A  13    10034   6768   5806    421   -383    576       C  
ATOM     75  CD1 ILE A  13      59.325  50.560 156.254  1.00 59.91           C  
ANISOU   75  CD1 ILE A  13    10002   6775   5984    422   -437    424       C  
ATOM     76  N   GLY A  14      54.613  52.720 158.361  1.00 60.53           N  
ANISOU   76  N   GLY A  14    10203   6942   5854    446   -275    570       N  
ATOM     77  CA  GLY A  14      53.479  52.734 159.286  1.00 60.77           C  
ANISOU   77  CA  GLY A  14    10268   7010   5810    464   -253    615       C  
ATOM     78  C   GLY A  14      52.258  53.465 158.755  1.00 60.67           C  
ANISOU   78  C   GLY A  14    10246   7012   5791    463   -180    654       C  
ATOM     79  O   GLY A  14      51.134  52.959 158.844  1.00 60.53           O  
ANISOU   79  O   GLY A  14    10237   7028   5732    462   -157    722       O  
ATOM     80  N   ILE A  15      52.482  54.656 158.201  1.00 60.80           N  
ANISOU   80  N   ILE A  15    10246   7004   5852    463   -145    615       N  
ATOM     81  CA  ILE A  15      51.402  55.450 157.600  1.00 60.76           C  
ANISOU   81  CA  ILE A  15    10229   7007   5851    466    -77    651       C  
ATOM     82  C   ILE A  15      50.805  54.716 156.394  1.00 60.27           C  
ANISOU   82  C   ILE A  15    10137   6952   5810    436    -59    713       C  
ATOM     83  O   ILE A  15      49.571  54.631 156.264  1.00 60.26           O  
ANISOU   83  O   ILE A  15    10132   6983   5779    438    -20    777       O  
ATOM     84  CB  ILE A  15      51.885  56.877 157.236  1.00 61.01           C  
ANISOU   84  CB  ILE A  15    10250   6999   5930    470    -50    594       C  
ATOM     85  CG1 ILE A  15      52.157  57.673 158.524  1.00 61.54           C  
ANISOU   85  CG1 ILE A  15    10355   7064   5962    501    -60    539       C  
ATOM     86  CG2 ILE A  15      50.864  57.620 156.374  1.00 60.95           C  
ANISOU   86  CG2 ILE A  15    10225   6994   5940    470     15    637       C  
ATOM     87  CD1 ILE A  15      53.092  58.850 158.346  1.00 61.90           C  
ANISOU   87  CD1 ILE A  15    10397   7061   6061    495    -62    466       C  
ATOM     88  N   GLU A  16      51.673  54.177 155.535  1.00 60.02           N  
ANISOU   88  N   GLU A  16    10081   6894   5828    410    -88    695       N  
ATOM     89  CA  GLU A  16      51.222  53.354 154.394  1.00 59.55           C  
ANISOU   89  CA  GLU A  16     9999   6840   5786    380    -79    746       C  
ATOM     90  C   GLU A  16      50.386  52.155 154.846  1.00 58.91           C  
ANISOU   90  C   GLU A  16     9938   6791   5654    375    -96    810       C  
ATOM     91  O   GLU A  16      49.259  51.941 154.355  1.00 58.47           O  
ANISOU   91  O   GLU A  16     9873   6762   5582    360    -64    874       O  
ATOM     92  CB  GLU A  16      52.417  52.868 153.569  1.00 59.87           C  
ANISOU   92  CB  GLU A  16    10016   6848   5881    358   -113    706       C  
ATOM     93  CG  GLU A  16      53.062  53.941 152.699  1.00 60.13           C  
ANISOU   93  CG  GLU A  16    10019   6856   5971    348    -85    663       C  
ATOM     94  CD  GLU A  16      52.379  54.121 151.352  1.00 60.27           C  
ANISOU   94  CD  GLU A  16    10009   6879   6010    322    -40    706       C  
ATOM     95  OE1 GLU A  16      51.134  54.092 151.288  1.00 60.35           O  
ANISOU   95  OE1 GLU A  16    10025   6916   5988    322     -9    767       O  
ATOM     96  OE2 GLU A  16      53.097  54.296 150.344  1.00 60.85           O  
ANISOU   96  OE2 GLU A  16    10054   6934   6131    301    -34    680       O  
ATOM     97  N   VAL A  17      50.942  51.400 155.797  1.00 58.77           N  
ANISOU   97  N   VAL A  17     9947   6772   5611    385   -149    795       N  
ATOM     98  CA  VAL A  17      50.252  50.257 156.408  1.00 58.94           C  
ANISOU   98  CA  VAL A  17     9992   6820   5580    380   -173    855       C  
ATOM     99  C   VAL A  17      48.903  50.663 157.012  1.00 59.35           C  
ANISOU   99  C   VAL A  17    10055   6920   5574    391   -126    910       C  
ATOM    100  O   VAL A  17      47.924  49.938 156.855  1.00 59.09           O  
ANISOU  100  O   VAL A  17    10020   6915   5514    371   -117    980       O  
ATOM    101  CB  VAL A  17      51.144  49.550 157.466  1.00 59.00           C  
ANISOU  101  CB  VAL A  17    10030   6818   5567    396   -239    827       C  
ATOM    102  CG1 VAL A  17      50.342  48.600 158.352  1.00 59.31           C  
ANISOU  102  CG1 VAL A  17    10103   6890   5542    393   -257    893       C  
ATOM    103  CG2 VAL A  17      52.270  48.785 156.785  1.00 58.91           C  
ANISOU  103  CG2 VAL A  17    10006   6765   5611    384   -287    792       C  
ATOM    104  N   LEU A  18      48.855  51.815 157.685  1.00 60.04           N  
ANISOU  104  N   LEU A  18    10149   7017   5643    423    -98    876       N  
ATOM    105  CA  LEU A  18      47.611  52.314 158.293  1.00 60.66           C  
ANISOU  105  CA  LEU A  18    10235   7145   5668    444    -48    920       C  
ATOM    106  C   LEU A  18      46.582  52.686 157.223  1.00 60.48           C  
ANISOU  106  C   LEU A  18    10176   7136   5665    430      7    970       C  
ATOM    107  O   LEU A  18      45.412  52.268 157.298  1.00 60.35           O  
ANISOU  107  O   LEU A  18    10152   7166   5610    422     32   1042       O  
ATOM    108  CB  LEU A  18      47.904  53.510 159.209  1.00 61.32           C  
ANISOU  108  CB  LEU A  18    10338   7227   5731    485    -32    859       C  
ATOM    109  CG  LEU A  18      46.843  53.939 160.234  1.00 61.98           C  
ANISOU  109  CG  LEU A  18    10441   7365   5743    518      8    888       C  
ATOM    110  CD1 LEU A  18      47.529  54.646 161.398  1.00 62.48           C  
ANISOU  110  CD1 LEU A  18    10540   7420   5776    553     -7    815       C  
ATOM    111  CD2 LEU A  18      45.751  54.822 159.636  1.00 62.01           C  
ANISOU  111  CD2 LEU A  18    10417   7386   5757    532     80    920       C  
ATOM    112  N   ILE A  19      47.029  53.451 156.223  1.00 60.92           N  
ANISOU  112  N   ILE A  19    10208   7156   5782    425     26    935       N  
ATOM    113  CA  ILE A  19      46.170  53.816 155.080  1.00 61.11           C  
ANISOU  113  CA  ILE A  19    10196   7190   5830    409     73    981       C  
ATOM    114  C   ILE A  19      45.611  52.564 154.396  1.00 60.92           C  
ANISOU  114  C   ILE A  19    10159   7186   5801    367     57   1047       C  
ATOM    115  O   ILE A  19      44.410  52.491 154.121  1.00 60.70           O  
ANISOU  115  O   ILE A  19    10111   7199   5751    358     91   1115       O  
ATOM    116  CB  ILE A  19      46.913  54.694 154.041  1.00 60.76           C  
ANISOU  116  CB  ILE A  19    10131   7101   5854    402     86    934       C  
ATOM    117  CG1 ILE A  19      47.222  56.076 154.627  1.00 61.37           C  
ANISOU  117  CG1 ILE A  19    10221   7156   5938    441    110    879       C  
ATOM    118  CG2 ILE A  19      46.081  54.867 152.772  1.00 60.23           C  
ANISOU  118  CG2 ILE A  19    10028   7046   5810    380    125    989       C  
ATOM    119  CD1 ILE A  19      48.404  56.768 153.973  1.00 61.45           C  
ANISOU  119  CD1 ILE A  19    10222   7113   6012    429    100    815       C  
ATOM    120  N   ALA A  20      46.485  51.592 154.130  1.00 61.10           N  
ANISOU  120  N   ALA A  20    10190   7178   5845    342      5   1026       N  
ATOM    121  CA  ALA A  20      46.046  50.305 153.576  1.00 61.01           C  
ANISOU  121  CA  ALA A  20    10176   7176   5827    301    -18   1081       C  
ATOM    122  C   ALA A  20      45.065  49.567 154.505  1.00 61.38           C  
ANISOU  122  C   ALA A  20    10241   7269   5811    297    -23   1147       C  
ATOM    123  O   ALA A  20      44.063  49.018 154.037  1.00 60.89           O  
ANISOU  123  O   ALA A  20    10163   7235   5734    265    -11   1216       O  
ATOM    124  CB  ALA A  20      47.242  49.426 153.267  1.00 60.90           C  
ANISOU  124  CB  ALA A  20    10175   7117   5847    285    -75   1037       C  
ATOM    125  N   LEU A  21      45.355  49.571 155.808  1.00 62.10           N  
ANISOU  125  N   LEU A  21    10363   7368   5863    326    -41   1128       N  
ATOM    126  CA  LEU A  21      44.482  48.947 156.819  1.00 62.98           C  
ANISOU  126  CA  LEU A  21    10492   7528   5908    324    -44   1190       C  
ATOM    127  C   LEU A  21      43.113  49.619 156.959  1.00 63.64           C  
ANISOU  127  C   LEU A  21    10552   7672   5955    336     20   1245       C  
ATOM    128  O   LEU A  21      42.149  48.956 157.345  1.00 63.90           O  
ANISOU  128  O   LEU A  21    10584   7752   5943    317     25   1317       O  
ATOM    129  CB  LEU A  21      45.156  48.892 158.203  1.00 63.28           C  
ANISOU  129  CB  LEU A  21    10570   7565   5906    355    -77   1153       C  
ATOM    130  CG  LEU A  21      46.158  47.763 158.464  1.00 63.40           C  
ANISOU  130  CG  LEU A  21    10615   7542   5931    342   -150   1135       C  
ATOM    131  CD1 LEU A  21      46.900  48.016 159.772  1.00 63.56           C  
ANISOU  131  CD1 LEU A  21    10669   7564   5917    379   -179   1088       C  
ATOM    132  CD2 LEU A  21      45.482  46.397 158.472  1.00 63.44           C  
ANISOU  132  CD2 LEU A  21    10632   7560   5910    302   -177   1214       C  
ATOM    133  N   VAL A  22      43.028  50.924 156.684  1.00 63.99           N  
ANISOU  133  N   VAL A  22    10575   7715   6020    368     68   1213       N  
ATOM    134  CA  VAL A  22      41.716  51.598 156.615  1.00 64.19           C  
ANISOU  134  CA  VAL A  22    10570   7794   6022    383    131   1265       C  
ATOM    135  C   VAL A  22      41.044  51.389 155.244  1.00 63.87           C  
ANISOU  135  C   VAL A  22    10488   7760   6017    344    147   1318       C  
ATOM    136  O   VAL A  22      39.824  51.226 155.170  1.00 63.89           O  
ANISOU  136  O   VAL A  22    10464   7819   5992    333    177   1392       O  
ATOM    137  CB  VAL A  22      41.821  53.105 156.955  1.00 64.55           C  
ANISOU  137  CB  VAL A  22    10617   7834   6075    439    176   1212       C  
ATOM    138  CG1 VAL A  22      40.460  53.789 156.863  1.00 64.80           C  
ANISOU  138  CG1 VAL A  22    10614   7920   6086    463    242   1267       C  
ATOM    139  CG2 VAL A  22      42.391  53.296 158.359  1.00 64.95           C  
ANISOU  139  CG2 VAL A  22    10710   7885   6082    476    159   1161       C  
ATOM    140  N   SER A  23      41.839  51.383 154.174  1.00 63.45           N  
ANISOU  140  N   SER A  23    10430   7656   6022    322    127   1281       N  
ATOM    141  CA  SER A  23      41.321  51.272 152.799  1.00 63.10           C  
ANISOU  141  CA  SER A  23    10348   7615   6009    285    140   1322       C  
ATOM    142  C   SER A  23      40.633  49.937 152.469  1.00 63.04           C  
ANISOU  142  C   SER A  23    10335   7633   5982    231    113   1392       C  
ATOM    143  O   SER A  23      39.483  49.929 152.026  1.00 63.36           O  
ANISOU  143  O   SER A  23    10342   7721   6009    212    141   1460       O  
ATOM    144  CB  SER A  23      42.452  51.522 151.791  1.00 62.88           C  
ANISOU  144  CB  SER A  23    10319   7528   6043    274    122   1260       C  
ATOM    145  OG  SER A  23      41.991  51.443 150.457  1.00 62.70           O  
ANISOU  145  OG  SER A  23    10264   7512   6046    238    135   1296       O  
ATOM    146  N   VAL A  24      41.336  48.825 152.686  1.00 62.62           N  
ANISOU  146  N   VAL A  24    10315   7548   5928    206     57   1376       N  
ATOM    147  CA  VAL A  24      40.875  47.498 152.231  1.00 62.13           C  
ANISOU  147  CA  VAL A  24    10256   7492   5858    148     22   1431       C  
ATOM    148  C   VAL A  24      39.537  47.070 152.865  1.00 62.86           C  
ANISOU  148  C   VAL A  24    10338   7650   5896    130     38   1520       C  
ATOM    149  O   VAL A  24      38.611  46.698 152.133  1.00 62.98           O  
ANISOU  149  O   VAL A  24    10324   7695   5909     87     46   1582       O  
ATOM    150  CB  VAL A  24      41.963  46.403 152.416  1.00 61.60           C  
ANISOU  150  CB  VAL A  24    10232   7368   5805    133    -42   1392       C  
ATOM    151  CG1 VAL A  24      41.411  45.006 152.140  1.00 61.54           C  
ANISOU  151  CG1 VAL A  24    10236   7361   5783     75    -80   1453       C  
ATOM    152  CG2 VAL A  24      43.146  46.682 151.505  1.00 61.31           C  
ANISOU  152  CG2 VAL A  24    10193   7275   5825    139    -56   1316       C  
ATOM    153  N   PRO A  25      39.424  47.130 154.213  1.00 63.61           N  
ANISOU  153  N   PRO A  25    10453   7772   5944    160     43   1527       N  
ATOM    154  CA  PRO A  25      38.156  46.718 154.830  1.00 63.98           C  
ANISOU  154  CA  PRO A  25    10483   7888   5935    142     63   1614       C  
ATOM    155  C   PRO A  25      36.957  47.587 154.431  1.00 64.15           C  
ANISOU  155  C   PRO A  25    10450   7974   5950    153    126   1662       C  
ATOM    156  O   PRO A  25      35.881  47.047 154.180  1.00 64.02           O  
ANISOU  156  O   PRO A  25    10403   8006   5913    111    133   1742       O  
ATOM    157  CB  PRO A  25      38.434  46.839 156.336  1.00 64.23           C  
ANISOU  157  CB  PRO A  25    10549   7937   5917    183     62   1596       C  
ATOM    158  CG  PRO A  25      39.916  46.834 156.461  1.00 64.01           C  
ANISOU  158  CG  PRO A  25    10561   7837   5921    204     18   1509       C  
ATOM    159  CD  PRO A  25      40.398  47.551 155.240  1.00 63.64           C  
ANISOU  159  CD  PRO A  25    10491   7751   5938    209     32   1459       C  
ATOM    160  N   GLY A  26      37.153  48.906 154.366  1.00 64.13           N  
ANISOU  160  N   GLY A  26    10433   7967   5965    208    170   1614       N  
ATOM    161  CA  GLY A  26      36.091  49.842 153.994  1.00 64.26           C  
ANISOU  161  CA  GLY A  26    10397   8037   5981    231    231   1654       C  
ATOM    162  C   GLY A  26      35.469  49.555 152.644  1.00 63.93           C  
ANISOU  162  C   GLY A  26    10315   8006   5969    181    229   1705       C  
ATOM    163  O   GLY A  26      34.246  49.471 152.521  1.00 63.37           O  
ANISOU  163  O   GLY A  26    10199   8002   5874    164    255   1783       O  
ATOM    164  N   ASN A  27      36.321  49.379 151.637  1.00 64.35           N  
ANISOU  164  N   ASN A  27    10380   7998   6070    155    196   1661       N  
ATOM    165  CA  ASN A  27      35.863  49.111 150.271  1.00 65.12           C  
ANISOU  165  CA  ASN A  27    10445   8101   6194    106    190   1699       C  
ATOM    166  C   ASN A  27      35.308  47.696 150.100  1.00 65.97           C  
ANISOU  166  C   ASN A  27    10555   8227   6280     34    149   1762       C  
ATOM    167  O   ASN A  27      34.322  47.501 149.373  1.00 66.49           O  
ANISOU  167  O   ASN A  27    10581   8338   6342     -5    157   1827       O  
ATOM    168  CB  ASN A  27      36.977  49.399 149.265  1.00 64.72           C  
ANISOU  168  CB  ASN A  27    10409   7983   6196    103    173   1630       C  
ATOM    169  CG  ASN A  27      37.277  50.884 149.144  1.00 64.70           C  
ANISOU  169  CG  ASN A  27    10392   7967   6221    161    217   1587       C  
ATOM    170  OD1 ASN A  27      36.448  51.657 148.659  1.00 64.59           O  
ANISOU  170  OD1 ASN A  27    10337   7990   6212    175    258   1627       O  
ATOM    171  ND2 ASN A  27      38.462  51.291 149.586  1.00 64.65           N  
ANISOU  171  ND2 ASN A  27    10421   7908   6235    195    208   1507       N  
ATOM    172  N   VAL A  28      35.913  46.717 150.779  1.00 67.11           N  
ANISOU  172  N   VAL A  28    10748   8339   6411     17    103   1744       N  
ATOM    173  CA  VAL A  28      35.320  45.370 150.866  1.00 67.96           C  
ANISOU  173  CA  VAL A  28    10864   8462   6492    -48     64   1809       C  
ATOM    174  C   VAL A  28      33.909  45.466 151.470  1.00 69.40           C  
ANISOU  174  C   VAL A  28    11004   8735   6628    -54    102   1898       C  
ATOM    175  O   VAL A  28      32.978  44.830 150.976  1.00 69.77           O  
ANISOU  175  O   VAL A  28    11023   8820   6665   -114     93   1970       O  
ATOM    176  CB  VAL A  28      36.202  44.383 151.677  1.00 67.72           C  
ANISOU  176  CB  VAL A  28    10896   8381   6453    -56     10   1779       C  
ATOM    177  CG1 VAL A  28      35.453  43.085 151.984  1.00 68.21           C  
ANISOU  177  CG1 VAL A  28    10968   8464   6483   -121    -23   1857       C  
ATOM    178  CG2 VAL A  28      37.488  44.064 150.926  1.00 67.13           C  
ANISOU  178  CG2 VAL A  28    10855   8222   6427    -60    -31   1701       C  
ATOM    179  N   LEU A  29      33.765  46.277 152.518  1.00 70.47           N  
ANISOU  179  N   LEU A  29    11133   8906   6734      6    146   1891       N  
ATOM    180  CA  LEU A  29      32.468  46.522 153.154  1.00 71.61           C  
ANISOU  180  CA  LEU A  29    11233   9144   6832     14    192   1968       C  
ATOM    181  C   LEU A  29      31.493  47.254 152.216  1.00 72.14           C  
ANISOU  181  C   LEU A  29    11231   9261   6916     16    235   2012       C  
ATOM    182  O   LEU A  29      30.294  46.956 152.220  1.00 73.56           O  
ANISOU  182  O   LEU A  29    11363   9515   7068    -16    251   2097       O  
ATOM    183  CB  LEU A  29      32.647  47.309 154.461  1.00 71.86           C  
ANISOU  183  CB  LEU A  29    11279   9197   6828     89    231   1936       C  
ATOM    184  CG  LEU A  29      31.521  47.217 155.486  1.00 72.74           C  
ANISOU  184  CG  LEU A  29    11360   9401   6874     95    269   2010       C  
ATOM    185  CD1 LEU A  29      31.535  45.868 156.196  1.00 73.39           C  
ANISOU  185  CD1 LEU A  29    11479   9486   6918     39    222   2053       C  
ATOM    186  CD2 LEU A  29      31.632  48.353 156.496  1.00 72.88           C  
ANISOU  186  CD2 LEU A  29    11383   9442   6863    182    322   1965       C  
ATOM    187  N   VAL A  30      32.003  48.201 151.422  1.00 71.55           N  
ANISOU  187  N   VAL A  30    11150   9148   6885     51    251   1957       N  
ATOM    188  CA  VAL A  30      31.197  48.853 150.373  1.00 71.74           C  
ANISOU  188  CA  VAL A  30    11113   9210   6932     49    282   1997       C  
ATOM    189  C   VAL A  30      30.710  47.840 149.334  1.00 72.04           C  
ANISOU  189  C   VAL A  30    11133   9258   6977    -37    240   2052       C  
ATOM    190  O   VAL A  30      29.525  47.844 148.978  1.00 71.91           O  
ANISOU  190  O   VAL A  30    11059   9314   6949    -62    259   2131       O  
ATOM    191  CB  VAL A  30      31.965  50.007 149.671  1.00 71.44           C  
ANISOU  191  CB  VAL A  30    11081   9119   6942     97    300   1927       C  
ATOM    192  CG1 VAL A  30      31.260  50.472 148.401  1.00 71.39           C  
ANISOU  192  CG1 VAL A  30    11020   9141   6962     81    317   1971       C  
ATOM    193  CG2 VAL A  30      32.131  51.188 150.616  1.00 71.85           C  
ANISOU  193  CG2 VAL A  30    11139   9174   6987    184    350   1886       C  
ATOM    194  N   ILE A  31      31.617  46.986 148.853  1.00 72.68           N  
ANISOU  194  N   ILE A  31    11264   9270   7081    -82    184   2010       N  
ATOM    195  CA  ILE A  31      31.261  45.957 147.855  1.00 73.04           C  
ANISOU  195  CA  ILE A  31    11304   9314   7133   -167    139   2050       C  
ATOM    196  C   ILE A  31      30.265  44.948 148.446  1.00 74.30           C  
ANISOU  196  C   ILE A  31    11450   9528   7251   -224    123   2135       C  
ATOM    197  O   ILE A  31      29.315  44.541 147.770  1.00 75.19           O  
ANISOU  197  O   ILE A  31    11522   9687   7358   -283    113   2204       O  
ATOM    198  CB  ILE A  31      32.506  45.217 147.300  1.00 72.30           C  
ANISOU  198  CB  ILE A  31    11271   9129   7069   -196     83   1979       C  
ATOM    199  CG1 ILE A  31      33.408  46.183 146.528  1.00 71.69           C  
ANISOU  199  CG1 ILE A  31    11197   9006   7034   -153    100   1904       C  
ATOM    200  CG2 ILE A  31      32.100  44.073 146.371  1.00 72.55           C  
ANISOU  200  CG2 ILE A  31    11305   9156   7102   -284     34   2017       C  
ATOM    201  CD1 ILE A  31      34.843  45.722 146.408  1.00 71.32           C  
ANISOU  201  CD1 ILE A  31    11210   8874   7015   -151     60   1818       C  
ATOM    202  N   TRP A  32      30.500  44.559 149.701  1.00 74.87           N  
ANISOU  202  N   TRP A  32    11556   9596   7293   -208    118   2133       N  
ATOM    203  CA  TRP A  32      29.569  43.725 150.484  1.00 75.64           C  
ANISOU  203  CA  TRP A  32    11641   9753   7346   -254    111   2217       C  
ATOM    204  C   TRP A  32      28.184  44.375 150.543  1.00 75.64           C  
ANISOU  204  C   TRP A  32    11559   9859   7322   -243    168   2297       C  
ATOM    205  O   TRP A  32      27.183  43.757 150.168  1.00 75.79           O  
ANISOU  205  O   TRP A  32    11537   9931   7328   -311    155   2378       O  
ATOM    206  CB  TRP A  32      30.115  43.540 151.909  1.00 76.34           C  
ANISOU  206  CB  TRP A  32    11776   9826   7402   -217    111   2194       C  
ATOM    207  CG  TRP A  32      29.596  42.375 152.691  1.00 77.67           C  
ANISOU  207  CG  TRP A  32    11959  10021   7529   -276     82   2265       C  
ATOM    208  CD1 TRP A  32      28.319  41.885 152.724  1.00 78.75           C  
ANISOU  208  CD1 TRP A  32    12048  10236   7637   -335     90   2365       C  
ATOM    209  CD2 TRP A  32      30.355  41.577 153.605  1.00 78.23           C  
ANISOU  209  CD2 TRP A  32    12098  10042   7582   -281     41   2244       C  
ATOM    210  NE1 TRP A  32      28.246  40.813 153.587  1.00 79.50           N  
ANISOU  210  NE1 TRP A  32    12179  10329   7698   -381     56   2409       N  
ATOM    211  CE2 TRP A  32      29.482  40.604 154.139  1.00 79.00           C  
ANISOU  211  CE2 TRP A  32    12189  10186   7640   -347     25   2337       C  
ATOM    212  CE3 TRP A  32      31.696  41.583 154.015  1.00 77.86           C  
ANISOU  212  CE3 TRP A  32    12115   9916   7550   -238     14   2159       C  
ATOM    213  CZ2 TRP A  32      29.909  39.644 155.059  1.00 79.34           C  
ANISOU  213  CZ2 TRP A  32    12291  10196   7658   -370    -17   2349       C  
ATOM    214  CZ3 TRP A  32      32.120  40.627 154.929  1.00 77.95           C  
ANISOU  214  CZ3 TRP A  32    12183   9897   7537   -257    -29   2169       C  
ATOM    215  CH2 TRP A  32      31.227  39.673 155.444  1.00 78.93           C  
ANISOU  215  CH2 TRP A  32    12302  10065   7620   -322    -44   2265       C  
ATOM    216  N   ALA A  33      28.153  45.632 150.989  1.00 75.72           N  
ANISOU  216  N   ALA A  33    11544   9897   7328   -157    228   2271       N  
ATOM    217  CA  ALA A  33      26.906  46.382 151.191  1.00 76.48           C  
ANISOU  217  CA  ALA A  33    11563  10094   7401   -126    289   2338       C  
ATOM    218  C   ALA A  33      25.990  46.426 149.970  1.00 76.80           C  
ANISOU  218  C   ALA A  33    11537  10179   7461   -171    288   2399       C  
ATOM    219  O   ALA A  33      24.773  46.334 150.110  1.00 77.53           O  
ANISOU  219  O   ALA A  33    11565  10365   7529   -192    311   2485       O  
ATOM    220  CB  ALA A  33      27.214  47.801 151.657  1.00 76.45           C  
ANISOU  220  CB  ALA A  33    11554  10089   7402    -21    348   2281       C  
ATOM    221  N   VAL A  34      26.574  46.567 148.782  1.00 76.66           N  
ANISOU  221  N   VAL A  34    11535  10103   7489   -186    261   2355       N  
ATOM    222  CA  VAL A  34      25.793  46.600 147.540  1.00 76.84           C  
ANISOU  222  CA  VAL A  34    11501  10164   7528   -231    253   2408       C  
ATOM    223  C   VAL A  34      25.261  45.209 147.186  1.00 77.44           C  
ANISOU  223  C   VAL A  34    11576  10258   7590   -340    196   2470       C  
ATOM    224  O   VAL A  34      24.127  45.090 146.722  1.00 77.23           O  
ANISOU  224  O   VAL A  34    11483  10307   7553   -383    199   2551       O  
ATOM    225  CB  VAL A  34      26.608  47.188 146.363  1.00 76.12           C  
ANISOU  225  CB  VAL A  34    11430  10008   7484   -215    241   2342       C  
ATOM    226  CG1 VAL A  34      25.835  47.106 145.047  1.00 76.23           C  
ANISOU  226  CG1 VAL A  34    11392  10063   7509   -270    225   2398       C  
ATOM    227  CG2 VAL A  34      26.987  48.635 146.654  1.00 75.96           C  
ANISOU  227  CG2 VAL A  34    11404   9975   7481   -113    298   2293       C  
ATOM    228  N   LYS A  35      26.067  44.169 147.406  1.00 78.68           N  
ANISOU  228  N   LYS A  35    11805  10341   7746   -384    144   2432       N  
ATOM    229  CA  LYS A  35      25.675  42.803 147.045  1.00 80.41           C  
ANISOU  229  CA  LYS A  35    12037  10558   7957   -489     84   2482       C  
ATOM    230  C   LYS A  35      24.480  42.307 147.863  1.00 81.95           C  
ANISOU  230  C   LYS A  35    12186  10842   8110   -530     96   2583       C  
ATOM    231  O   LYS A  35      23.544  41.727 147.306  1.00 82.50           O  
ANISOU  231  O   LYS A  35    12212  10961   8172   -609     73   2656       O  
ATOM    232  CB  LYS A  35      26.851  41.831 147.194  1.00 80.73           C  
ANISOU  232  CB  LYS A  35    12169  10494   8009   -516     26   2417       C  
ATOM    233  CG  LYS A  35      26.510  40.407 146.774  1.00 82.24           C  
ANISOU  233  CG  LYS A  35    12384  10667   8196   -624    -39   2460       C  
ATOM    234  CD  LYS A  35      27.729  39.512 146.674  1.00 82.96           C  
ANISOU  234  CD  LYS A  35    12566  10645   8309   -643    -97   2387       C  
ATOM    235  CE  LYS A  35      27.305  38.055 146.527  1.00 84.19           C  
ANISOU  235  CE  LYS A  35    12751  10781   8456   -748   -162   2437       C  
ATOM    236  NZ  LYS A  35      28.431  37.163 146.131  1.00 84.54           N  
ANISOU  236  NZ  LYS A  35    12880  10711   8528   -769   -223   2363       N  
ATOM    237  N   VAL A  36      24.528  42.525 149.177  1.00 82.95           N  
ANISOU  237  N   VAL A  36    12320  10991   8205   -478    132   2585       N  
ATOM    238  CA  VAL A  36      23.451  42.095 150.081  1.00 83.74           C  
ANISOU  238  CA  VAL A  36    12376  11182   8259   -511    151   2680       C  
ATOM    239  C   VAL A  36      22.163  42.923 149.938  1.00 84.50           C  
ANISOU  239  C   VAL A  36    12367  11395   8342   -487    210   2752       C  
ATOM    240  O   VAL A  36      21.071  42.361 149.935  1.00 85.61           O  
ANISOU  240  O   VAL A  36    12451  11614   8461   -555    204   2846       O  
ATOM    241  CB  VAL A  36      23.923  42.047 151.563  1.00 84.11           C  
ANISOU  241  CB  VAL A  36    12467  11221   8270   -463    171   2659       C  
ATOM    242  CG1 VAL A  36      24.163  43.441 152.141  1.00 83.87           C  
ANISOU  242  CG1 VAL A  36    12420  11211   8232   -346    241   2609       C  
ATOM    243  CG2 VAL A  36      22.927  41.273 152.423  1.00 85.56           C  
ANISOU  243  CG2 VAL A  36    12619  11484   8403   -521    175   2761       C  
ATOM    244  N   ASN A  37      22.296  44.241 149.797  1.00 85.18           N  
ANISOU  244  N   ASN A  37    12426  11492   8444   -392    263   2710       N  
ATOM    245  CA  ASN A  37      21.151  45.161 149.793  1.00 86.56           C  
ANISOU  245  CA  ASN A  37    12504  11774   8609   -347    326   2771       C  
ATOM    246  C   ASN A  37      20.574  45.339 148.382  1.00 88.30           C  
ANISOU  246  C   ASN A  37    12668  12020   8862   -386    308   2806       C  
ATOM    247  O   ASN A  37      21.261  45.828 147.485  1.00 88.09           O  
ANISOU  247  O   ASN A  37    12668  11928   8873   -363    294   2745       O  
ATOM    248  CB  ASN A  37      21.583  46.521 150.363  1.00 85.71           C  
ANISOU  248  CB  ASN A  37    12401  11659   8506   -222    391   2707       C  
ATOM    249  CG  ASN A  37      20.411  47.397 150.784  1.00 85.81           C  
ANISOU  249  CG  ASN A  37    12322  11786   8497   -161    464   2768       C  
ATOM    250  OD1 ASN A  37      19.251  47.105 150.490  1.00 86.10           O  
ANISOU  250  OD1 ASN A  37    12279  11913   8522   -208    468   2861       O  
ATOM    251  ND2 ASN A  37      20.715  48.488 151.479  1.00 85.41           N  
ANISOU  251  ND2 ASN A  37    12279  11729   8441    -53    522   2715       N  
ATOM    252  N   GLN A  38      19.314  44.948 148.199  1.00 91.23           N  
ANISOU  252  N   GLN A  38    12959  12488   9214   -445    307   2908       N  
ATOM    253  CA  GLN A  38      18.617  45.123 146.913  1.00 93.11           C  
ANISOU  253  CA  GLN A  38    13134  12767   9476   -484    290   2953       C  
ATOM    254  C   GLN A  38      18.214  46.579 146.632  1.00 94.17           C  
ANISOU  254  C   GLN A  38    13202  12950   9628   -384    352   2955       C  
ATOM    255  O   GLN A  38      18.030  46.950 145.470  1.00 95.25           O  
ANISOU  255  O   GLN A  38    13307  13089   9792   -394    336   2964       O  
ATOM    256  CB  GLN A  38      17.387  44.214 146.819  1.00 94.96           C  
ANISOU  256  CB  GLN A  38    13300  13094   9686   -586    265   3064       C  
ATOM    257  CG  GLN A  38      17.732  42.745 146.603  1.00 95.88           C  
ANISOU  257  CG  GLN A  38    13482  13148   9798   -704    185   3066       C  
ATOM    258  CD  GLN A  38      16.508  41.853 146.470  1.00 97.54           C  
ANISOU  258  CD  GLN A  38    13625  13445   9987   -813    156   3177       C  
ATOM    259  OE1 GLN A  38      15.466  42.274 145.964  1.00 98.44           O  
ANISOU  259  OE1 GLN A  38    13643  13657  10102   -821    174   3246       O  
ATOM    260  NE2 GLN A  38      16.634  40.602 146.917  1.00 98.12           N  
ANISOU  260  NE2 GLN A  38    13751  13485  10044   -901    108   3196       N  
ATOM    261  N   ALA A  39      18.082  47.397 147.678  1.00 95.65           N  
ANISOU  261  N   ALA A  39    13370  13174   9799   -288    421   2946       N  
ATOM    262  CA  ALA A  39      17.823  48.842 147.530  1.00 96.75           C  
ANISOU  262  CA  ALA A  39    13460  13341   9958   -178    482   2935       C  
ATOM    263  C   ALA A  39      18.978  49.606 146.867  1.00 97.53           C  
ANISOU  263  C   ALA A  39    13623  13332  10100   -126    474   2839       C  
ATOM    264  O   ALA A  39      18.773  50.708 146.353  1.00 98.32           O  
ANISOU  264  O   ALA A  39    13684  13442  10227    -58    507   2837       O  
ATOM    265  CB  ALA A  39      17.499  49.467 148.879  1.00 97.14           C  
ANISOU  265  CB  ALA A  39    13487  13446   9976    -88    556   2937       C  
ATOM    266  N   LEU A  40      20.179  49.024 146.894  1.00 98.16           N  
ANISOU  266  N   LEU A  40    13798  13310  10188   -158    431   2763       N  
ATOM    267  CA  LEU A  40      21.348  49.552 146.184  1.00 97.57           C  
ANISOU  267  CA  LEU A  40    13786  13132  10154   -128    415   2673       C  
ATOM    268  C   LEU A  40      21.625  48.811 144.860  1.00 97.63           C  
ANISOU  268  C   LEU A  40    13813  13099  10181   -220    347   2672       C  
ATOM    269  O   LEU A  40      22.785  48.688 144.456  1.00 96.77           O  
ANISOU  269  O   LEU A  40    13776  12895  10094   -227    316   2593       O  
ATOM    270  CB  LEU A  40      22.584  49.450 147.092  1.00 97.03           C  
ANISOU  270  CB  LEU A  40    13808  12977  10081    -95    413   2582       C  
ATOM    271  CG  LEU A  40      22.461  50.002 148.513  1.00 97.17           C  
ANISOU  271  CG  LEU A  40    13824  13025  10068    -13    471   2570       C  
ATOM    272  CD1 LEU A  40      23.701  49.672 149.327  1.00 96.46           C  
ANISOU  272  CD1 LEU A  40    13826  12851   9970     -1    453   2486       C  
ATOM    273  CD2 LEU A  40      22.229  51.500 148.475  1.00 97.37           C  
ANISOU  273  CD2 LEU A  40    13812  13067  10115     90    534   2555       C  
ATOM    274  N   ARG A  41      20.579  48.332 144.179  1.00 98.51           N  
ANISOU  274  N   ARG A  41    13860  13285  10284   -290    323   2758       N  
ATOM    275  CA  ARG A  41      20.739  47.597 142.918  1.00 98.96           C  
ANISOU  275  CA  ARG A  41    13935  13313  10353   -382    258   2759       C  
ATOM    276  C   ARG A  41      20.470  48.529 141.734  1.00 98.26           C  
ANISOU  276  C   ARG A  41    13799  13244  10290   -356    267   2774       C  
ATOM    277  O   ARG A  41      19.635  48.256 140.868  1.00 99.58           O  
ANISOU  277  O   ARG A  41    13911  13471  10452   -417    239   2841       O  
ATOM    278  CB  ARG A  41      19.825  46.360 142.903  1.00100.87           C  
ANISOU  278  CB  ARG A  41    14144  13615  10566   -490    215   2841       C  
ATOM    279  CG  ARG A  41      20.201  45.300 141.869  1.00102.18           C  
ANISOU  279  CG  ARG A  41    14357  13728  10738   -594    138   2823       C  
ATOM    280  CD  ARG A  41      19.915  43.873 142.346  1.00103.33           C  
ANISOU  280  CD  ARG A  41    14525  13876  10858   -692     91   2860       C  
ATOM    281  NE  ARG A  41      20.785  43.485 143.461  1.00103.85           N  
ANISOU  281  NE  ARG A  41    14666  13873  10917   -665     95   2805       N  
ATOM    282  CZ  ARG A  41      20.681  42.353 144.161  1.00106.17           C  
ANISOU  282  CZ  ARG A  41    14990  14159  11189   -731     63   2832       C  
ATOM    283  NH1 ARG A  41      19.739  41.450 143.879  1.00107.42           N  
ANISOU  283  NH1 ARG A  41    15112  14369  11330   -833     24   2913       N  
ATOM    284  NH2 ARG A  41      21.530  42.117 145.160  1.00106.56           N  
ANISOU  284  NH2 ARG A  41    15108  14146  11232   -696     68   2780       N  
ATOM    285  N   ASP A  42      21.225  49.626 141.708  1.00 96.24           N  
ANISOU  285  N   ASP A  42    13570  12933  10061   -268    303   2709       N  
ATOM    286  CA  ASP A  42      21.027  50.729 140.774  1.00 94.34           C  
ANISOU  286  CA  ASP A  42    13289  12706   9847   -222    323   2722       C  
ATOM    287  C   ASP A  42      22.348  51.032 140.068  1.00 91.65           C  
ANISOU  287  C   ASP A  42    13022  12263   9536   -212    306   2631       C  
ATOM    288  O   ASP A  42      23.430  50.691 140.569  1.00 92.32           O  
ANISOU  288  O   ASP A  42    13183  12269   9625   -208    296   2552       O  
ATOM    289  CB  ASP A  42      20.533  51.962 141.544  1.00 95.34           C  
ANISOU  289  CB  ASP A  42    13368  12874   9982   -111    396   2740       C  
ATOM    290  CG  ASP A  42      19.619  52.850 140.726  1.00 96.91           C  
ANISOU  290  CG  ASP A  42    13484  13138  10196    -78    415   2808       C  
ATOM    291  OD1 ASP A  42      19.897  53.071 139.529  1.00 97.72           O  
ANISOU  291  OD1 ASP A  42    13594  13215  10319   -103    387   2802       O  
ATOM    292  OD2 ASP A  42      18.620  53.337 141.295  1.00 98.14           O  
ANISOU  292  OD2 ASP A  42    13567  13376  10345    -26    460   2869       O  
ATOM    293  N   ALA A  43      22.247  51.677 138.906  1.00 88.80           N  
ANISOU  293  N   ALA A  43    12636  11908   9194   -208    302   2647       N  
ATOM    294  CA  ALA A  43      23.407  51.967 138.054  1.00 85.77           C  
ANISOU  294  CA  ALA A  43    12312  11441   8835   -209    285   2573       C  
ATOM    295  C   ALA A  43      24.520  52.683 138.814  1.00 82.88           C  
ANISOU  295  C   ALA A  43    12004  10992   8493   -129    322   2486       C  
ATOM    296  O   ALA A  43      25.678  52.273 138.735  1.00 82.01           O  
ANISOU  296  O   ALA A  43    11964  10804   8391   -150    298   2408       O  
ATOM    297  CB  ALA A  43      22.984  52.785 136.843  1.00 86.24           C  
ANISOU  297  CB  ALA A  43    12324  11532   8908   -199    288   2617       C  
ATOM    298  N   THR A  44      24.157  53.728 139.560  1.00 80.59           N  
ANISOU  298  N   THR A  44    11684  10721   8214    -39    378   2499       N  
ATOM    299  CA  THR A  44      25.108  54.504 140.369  1.00 78.68           C  
ANISOU  299  CA  THR A  44    11493  10406   7994     39    414   2419       C  
ATOM    300  C   THR A  44      25.954  53.607 141.272  1.00 77.75           C  
ANISOU  300  C   THR A  44    11442  10238   7861     15    393   2353       C  
ATOM    301  O   THR A  44      27.178  53.744 141.320  1.00 76.58           O  
ANISOU  301  O   THR A  44    11357  10007   7732     28    386   2270       O  
ATOM    302  CB  THR A  44      24.383  55.558 141.242  1.00 78.54           C  
ANISOU  302  CB  THR A  44    11432  10429   7981    135    476   2448       C  
ATOM    303  OG1 THR A  44      23.664  56.471 140.404  1.00 78.57           O  
ANISOU  303  OG1 THR A  44    11376  10471   8005    167    495   2506       O  
ATOM    304  CG2 THR A  44      25.373  56.347 142.103  1.00 78.14           C  
ANISOU  304  CG2 THR A  44    11439  10299   7949    212    510   2360       C  
ATOM    305  N   PHE A  45      25.295  52.681 141.964  1.00 78.14           N  
ANISOU  305  N   PHE A  45    11475  10340   7875    -21    382   2396       N  
ATOM    306  CA  PHE A  45      25.967  51.807 142.924  1.00 77.72           C  
ANISOU  306  CA  PHE A  45    11480  10247   7803    -41    362   2347       C  
ATOM    307  C   PHE A  45      26.855  50.781 142.226  1.00 76.58           C  
ANISOU  307  C   PHE A  45    11393  10040   7664   -118    301   2302       C  
ATOM    308  O   PHE A  45      27.981  50.538 142.674  1.00 76.71           O  
ANISOU  308  O   PHE A  45    11474   9983   7688   -108    287   2224       O  
ATOM    309  CB  PHE A  45      24.954  51.141 143.855  1.00 79.00           C  
ANISOU  309  CB  PHE A  45    11605  10485   7923    -60    369   2415       C  
ATOM    310  CG  PHE A  45      24.108  52.125 144.611  1.00 80.35           C  
ANISOU  310  CG  PHE A  45    11720  10721   8086     21    434   2453       C  
ATOM    311  CD1 PHE A  45      24.684  52.976 145.547  1.00 80.65           C  
ANISOU  311  CD1 PHE A  45    11792  10721   8130    110    477   2391       C  
ATOM    312  CD2 PHE A  45      22.745  52.232 144.362  1.00 81.89           C  
ANISOU  312  CD2 PHE A  45    11829  11016   8269     14    452   2549       C  
ATOM    313  CE1 PHE A  45      23.914  53.901 146.237  1.00 81.73           C  
ANISOU  313  CE1 PHE A  45    11880  10913   8257    192    538   2420       C  
ATOM    314  CE2 PHE A  45      21.966  53.153 145.052  1.00 82.88           C  
ANISOU  314  CE2 PHE A  45    11900  11203   8388     98    515   2582       C  
ATOM    315  CZ  PHE A  45      22.552  53.990 145.991  1.00 82.69           C  
ANISOU  315  CZ  PHE A  45    11914  11136   8367    189    559   2516       C  
ATOM    316  N   CYS A  46      26.380  50.232 141.106  1.00 75.54           N  
ANISOU  316  N   CYS A  46    11235   9936   7528   -190    265   2346       N  
ATOM    317  CA  CYS A  46      27.199  49.341 140.265  1.00 74.32           C  
ANISOU  317  CA  CYS A  46    11134   9724   7379   -260    209   2299       C  
ATOM    318  C   CYS A  46      28.541  49.958 139.829  1.00 72.24           C  
ANISOU  318  C   CYS A  46    10920   9377   7149   -222    215   2208       C  
ATOM    319  O   CYS A  46      29.532  49.241 139.676  1.00 70.44           O  
ANISOU  319  O   CYS A  46    10751   9085   6926   -253    180   2144       O  
ATOM    320  CB  CYS A  46      26.406  48.886 139.038  1.00 75.28           C  
ANISOU  320  CB  CYS A  46    11216   9895   7489   -335    175   2360       C  
ATOM    321  SG  CYS A  46      24.877  48.015 139.456  1.00 77.55           S  
ANISOU  321  SG  CYS A  46    11443  10280   7740   -398    159   2468       S  
ATOM    322  N   PHE A  47      28.568  51.279 139.642  1.00 71.38           N  
ANISOU  322  N   PHE A  47    10787   9270   7063   -156    259   2205       N  
ATOM    323  CA  PHE A  47      29.821  52.006 139.406  1.00 70.63           C  
ANISOU  323  CA  PHE A  47    10734   9098   7001   -114    272   2123       C  
ATOM    324  C   PHE A  47      30.604  52.220 140.707  1.00 70.14           C  
ANISOU  324  C   PHE A  47    10716   8986   6946    -58    291   2058       C  
ATOM    325  O   PHE A  47      31.840  52.240 140.686  1.00 70.44           O  
ANISOU  325  O   PHE A  47    10804   8953   7005    -50    280   1979       O  
ATOM    326  CB  PHE A  47      29.568  53.359 138.730  1.00 70.42           C  
ANISOU  326  CB  PHE A  47    10671   9085   6999    -67    309   2146       C  
ATOM    327  CG  PHE A  47      28.804  53.271 137.432  1.00 70.63           C  
ANISOU  327  CG  PHE A  47    10653   9165   7017   -118    291   2212       C  
ATOM    328  CD1 PHE A  47      29.217  52.421 136.411  1.00 70.57           C  
ANISOU  328  CD1 PHE A  47    10670   9143   6999   -193    245   2194       C  
ATOM    329  CD2 PHE A  47      27.676  54.061 137.220  1.00 71.12           C  
ANISOU  329  CD2 PHE A  47    10648   9293   7080    -86    319   2292       C  
ATOM    330  CE1 PHE A  47      28.506  52.346 135.218  1.00 70.94           C  
ANISOU  330  CE1 PHE A  47    10677   9242   7032   -242    225   2253       C  
ATOM    331  CE2 PHE A  47      26.965  53.987 136.031  1.00 71.31           C  
ANISOU  331  CE2 PHE A  47    10630   9371   7094   -133    298   2356       C  
ATOM    332  CZ  PHE A  47      27.381  53.132 135.028  1.00 71.23           C  
ANISOU  332  CZ  PHE A  47    10646   9348   7069   -213    250   2336       C  
ATOM    333  N   ILE A  48      29.895  52.401 141.824  1.00 69.91           N  
ANISOU  333  N   ILE A  48    10665   8999   6899    -18    319   2092       N  
ATOM    334  CA  ILE A  48      30.538  52.514 143.147  1.00 69.86           C  
ANISOU  334  CA  ILE A  48    10700   8955   6888     31    334   2036       C  
ATOM    335  C   ILE A  48      31.246  51.209 143.556  1.00 68.84           C  
ANISOU  335  C   ILE A  48    10624   8787   6744    -18    285   1997       C  
ATOM    336  O   ILE A  48      32.276  51.248 144.237  1.00 68.02           O  
ANISOU  336  O   ILE A  48    10569   8625   6648     10    280   1926       O  
ATOM    337  CB  ILE A  48      29.530  52.999 144.228  1.00 71.08           C  
ANISOU  337  CB  ILE A  48    10816   9172   7019     85    379   2085       C  
ATOM    338  CG1 ILE A  48      29.167  54.471 143.969  1.00 71.31           C  
ANISOU  338  CG1 ILE A  48    10809   9212   7073    157    430   2097       C  
ATOM    339  CG2 ILE A  48      30.080  52.837 145.647  1.00 71.20           C  
ANISOU  339  CG2 ILE A  48    10876   9161   7014    121    386   2035       C  
ATOM    340  CD1 ILE A  48      27.929  54.949 144.699  1.00 71.84           C  
ANISOU  340  CD1 ILE A  48    10821   9357   7118    207    477   2161       C  
ATOM    341  N   VAL A  49      30.704  50.071 143.126  1.00 68.75           N  
ANISOU  341  N   VAL A  49    10604   8805   6712    -94    246   2045       N  
ATOM    342  CA  VAL A  49      31.359  48.771 143.314  1.00 68.26           C  
ANISOU  342  CA  VAL A  49    10595   8699   6641   -146    193   2011       C  
ATOM    343  C   VAL A  49      32.669  48.736 142.512  1.00 67.71           C  
ANISOU  343  C   VAL A  49    10569   8552   6603   -154    169   1929       C  
ATOM    344  O   VAL A  49      33.719  48.374 143.051  1.00 67.68           O  
ANISOU  344  O   VAL A  49    10617   8489   6609   -141    149   1862       O  
ATOM    345  CB  VAL A  49      30.439  47.590 142.898  1.00 68.17           C  
ANISOU  345  CB  VAL A  49    10566   8732   6604   -231    154   2082       C  
ATOM    346  CG1 VAL A  49      31.187  46.258 142.934  1.00 67.91           C  
ANISOU  346  CG1 VAL A  49    10594   8638   6569   -285     95   2042       C  
ATOM    347  CG2 VAL A  49      29.207  47.521 143.789  1.00 68.62           C  
ANISOU  347  CG2 VAL A  49    10576   8867   6626   -229    177   2164       C  
ATOM    348  N   SER A  50      32.600  49.122 141.235  1.00 67.01           N  
ANISOU  348  N   SER A  50    10458   8470   6531   -173    171   1936       N  
ATOM    349  CA  SER A  50      33.787  49.189 140.370  1.00 65.95           C  
ANISOU  349  CA  SER A  50    10357   8274   6425   -180    155   1863       C  
ATOM    350  C   SER A  50      34.837  50.142 140.942  1.00 65.00           C  
ANISOU  350  C   SER A  50    10260   8103   6333   -110    184   1792       C  
ATOM    351  O   SER A  50      36.031  49.822 140.964  1.00 64.54           O  
ANISOU  351  O   SER A  50    10244   7984   6292   -109    163   1718       O  
ATOM    352  CB  SER A  50      33.398  49.620 138.954  1.00 66.16           C  
ANISOU  352  CB  SER A  50    10349   8329   6457   -207    161   1893       C  
ATOM    353  OG  SER A  50      34.542  49.789 138.132  1.00 66.00           O  
ANISOU  353  OG  SER A  50    10357   8257   6460   -210    154   1824       O  
ATOM    354  N   LEU A  51      34.378  51.302 141.412  1.00 64.50           N  
ANISOU  354  N   LEU A  51    10166   8063   6275    -52    231   1815       N  
ATOM    355  CA  LEU A  51      35.250  52.280 142.066  1.00 63.86           C  
ANISOU  355  CA  LEU A  51    10108   7936   6220     12    259   1751       C  
ATOM    356  C   LEU A  51      35.855  51.744 143.374  1.00 63.66           C  
ANISOU  356  C   LEU A  51    10124   7880   6182     31    243   1705       C  
ATOM    357  O   LEU A  51      37.024  52.005 143.668  1.00 63.03           O  
ANISOU  357  O   LEU A  51    10079   7744   6125     57    238   1630       O  
ATOM    358  CB  LEU A  51      34.485  53.587 142.312  1.00 63.94           C  
ANISOU  358  CB  LEU A  51    10079   7979   6236     71    312   1790       C  
ATOM    359  CG  LEU A  51      35.214  54.768 142.959  1.00 63.91           C  
ANISOU  359  CG  LEU A  51    10095   7928   6258    140    345   1731       C  
ATOM    360  CD1 LEU A  51      36.511  55.095 142.246  1.00 63.54           C  
ANISOU  360  CD1 LEU A  51    10075   7815   6249    132    334   1661       C  
ATOM    361  CD2 LEU A  51      34.304  55.984 142.977  1.00 64.27           C  
ANISOU  361  CD2 LEU A  51    10100   8006   6311    194    394   1778       C  
ATOM    362  N   ALA A  52      35.062  50.995 144.144  1.00 63.94           N  
ANISOU  362  N   ALA A  52    10156   7957   6181     17    233   1754       N  
ATOM    363  CA  ALA A  52      35.544  50.343 145.374  1.00 63.94           C  
ANISOU  363  CA  ALA A  52    10196   7934   6161     27    211   1722       C  
ATOM    364  C   ALA A  52      36.597  49.277 145.079  1.00 63.43           C  
ANISOU  364  C   ALA A  52    10177   7812   6109    -12    157   1669       C  
ATOM    365  O   ALA A  52      37.640  49.248 145.731  1.00 63.12           O  
ANISOU  365  O   ALA A  52    10176   7724   6080     14    143   1604       O  
ATOM    366  CB  ALA A  52      34.385  49.733 146.151  1.00 64.44           C  
ANISOU  366  CB  ALA A  52    10242   8061   6181     11    213   1797       C  
ATOM    367  N   VAL A  53      36.321  48.428 144.085  1.00 63.37           N  
ANISOU  367  N   VAL A  53    10166   7811   6101    -75    127   1696       N  
ATOM    368  CA  VAL A  53      37.264  47.387 143.618  1.00 63.14           C  
ANISOU  368  CA  VAL A  53    10178   7725   6085   -113     76   1645       C  
ATOM    369  C   VAL A  53      38.650  47.973 143.311  1.00 63.09           C  
ANISOU  369  C   VAL A  53    10191   7662   6117    -79     81   1557       C  
ATOM    370  O   VAL A  53      39.679  47.424 143.736  1.00 62.57           O  
ANISOU  370  O   VAL A  53    10164   7545   6062    -71     50   1498       O  
ATOM    371  CB  VAL A  53      36.709  46.646 142.368  1.00 62.80           C  
ANISOU  371  CB  VAL A  53    10123   7700   6037   -183     51   1683       C  
ATOM    372  CG1 VAL A  53      37.779  45.786 141.689  1.00 62.40           C  
ANISOU  372  CG1 VAL A  53    10114   7588   6005   -211      8   1617       C  
ATOM    373  CG2 VAL A  53      35.495  45.797 142.738  1.00 63.23           C  
ANISOU  373  CG2 VAL A  53    10166   7803   6056   -229     33   1764       C  
ATOM    374  N   ALA A  54      38.660  49.089 142.580  1.00 63.60           N  
ANISOU  374  N   ALA A  54    10226   7736   6203    -60    118   1553       N  
ATOM    375  CA  ALA A  54      39.894  49.826 142.290  1.00 63.50           C  
ANISOU  375  CA  ALA A  54    10224   7676   6227    -30    129   1478       C  
ATOM    376  C   ALA A  54      40.628  50.270 143.565  1.00 63.44           C  
ANISOU  376  C   ALA A  54    10239   7636   6227     23    135   1427       C  
ATOM    377  O   ALA A  54      41.853  50.153 143.653  1.00 63.36           O  
ANISOU  377  O   ALA A  54    10254   7579   6241     34    115   1356       O  
ATOM    378  CB  ALA A  54      39.601  51.030 141.400  1.00 63.54           C  
ANISOU  378  CB  ALA A  54    10192   7701   6250    -19    171   1497       C  
ATOM    379  N   ASP A  55      39.875  50.766 144.546  1.00 63.47           N  
ANISOU  379  N   ASP A  55    10234   7672   6208     57    160   1463       N  
ATOM    380  CA  ASP A  55      40.459  51.200 145.822  1.00 63.59           C  
ANISOU  380  CA  ASP A  55    10274   7665   6223    108    165   1418       C  
ATOM    381  C   ASP A  55      40.972  50.022 146.669  1.00 62.53           C  
ANISOU  381  C   ASP A  55    10179   7509   6070     98    117   1395       C  
ATOM    382  O   ASP A  55      42.023  50.143 147.311  1.00 63.05           O  
ANISOU  382  O   ASP A  55    10271   7535   6148    126    102   1331       O  
ATOM    383  CB  ASP A  55      39.466  52.065 146.621  1.00 64.82           C  
ANISOU  383  CB  ASP A  55    10410   7864   6355    151    209   1460       C  
ATOM    384  CG  ASP A  55      39.157  53.416 145.944  1.00 65.53           C  
ANISOU  384  CG  ASP A  55    10468   7960   6471    177    257   1471       C  
ATOM    385  OD1 ASP A  55      39.997  53.937 145.166  1.00 65.34           O  
ANISOU  385  OD1 ASP A  55    10444   7894   6485    174    258   1426       O  
ATOM    386  OD2 ASP A  55      38.061  53.963 146.213  1.00 66.34           O  
ANISOU  386  OD2 ASP A  55    10542   8108   6555    202    293   1525       O  
ATOM    387  N   VAL A  56      40.261  48.890 146.648  1.00 61.28           N  
ANISOU  387  N   VAL A  56    10023   7374   5883     55     91   1449       N  
ATOM    388  CA  VAL A  56      40.740  47.653 147.305  1.00 60.20           C  
ANISOU  388  CA  VAL A  56     9928   7211   5733     38     39   1435       C  
ATOM    389  C   VAL A  56      42.091  47.251 146.711  1.00 58.81           C  
ANISOU  389  C   VAL A  56     9775   6973   5595     32      5   1360       C  
ATOM    390  O   VAL A  56      43.013  46.882 147.447  1.00 58.20           O  
ANISOU  390  O   VAL A  56     9729   6859   5523     53    -25   1312       O  
ATOM    391  CB  VAL A  56      39.762  46.452 147.161  1.00 60.18           C  
ANISOU  391  CB  VAL A  56     9926   7236   5700    -18     13   1507       C  
ATOM    392  CG1 VAL A  56      40.371  45.177 147.748  1.00 60.08           C  
ANISOU  392  CG1 VAL A  56     9963   7182   5682    -34    -44   1489       C  
ATOM    393  CG2 VAL A  56      38.434  46.728 147.841  1.00 60.52           C  
ANISOU  393  CG2 VAL A  56     9942   7347   5703    -13     45   1585       C  
ATOM    394  N   ALA A  57      42.191  47.330 145.383  1.00 57.53           N  
ANISOU  394  N   ALA A  57     9595   6806   5458      5     11   1352       N  
ATOM    395  CA  ALA A  57      43.433  47.011 144.680  1.00 56.62           C  
ANISOU  395  CA  ALA A  57     9493   6640   5377      0    -13   1281       C  
ATOM    396  C   ALA A  57      44.607  47.918 145.063  1.00 55.76           C  
ANISOU  396  C   ALA A  57     9385   6501   5299     47      0   1209       C  
ATOM    397  O   ALA A  57      45.742  47.452 145.096  1.00 55.55           O  
ANISOU  397  O   ALA A  57     9377   6433   5296     55    -31   1148       O  
ATOM    398  CB  ALA A  57      43.215  47.037 143.175  1.00 56.52           C  
ANISOU  398  CB  ALA A  57     9458   6639   5377    -38     -1   1291       C  
ATOM    399  N   VAL A  58      44.340  49.194 145.358  1.00 54.89           N  
ANISOU  399  N   VAL A  58     9254   6410   5192     78     43   1215       N  
ATOM    400  CA  VAL A  58      45.397  50.126 145.791  1.00 54.15           C  
ANISOU  400  CA  VAL A  58     9162   6286   5126    119     53   1149       C  
ATOM    401  C   VAL A  58      45.980  49.669 147.138  1.00 53.83           C  
ANISOU  401  C   VAL A  58     9155   6225   5073    147     18   1116       C  
ATOM    402  O   VAL A  58      47.204  49.444 147.269  1.00 53.62           O  
ANISOU  402  O   VAL A  58     9140   6161   5072    158    -10   1052       O  
ATOM    403  CB  VAL A  58      44.876  51.585 145.882  1.00 54.23           C  
ANISOU  403  CB  VAL A  58     9149   6314   5140    147    106   1166       C  
ATOM    404  CG1 VAL A  58      45.912  52.525 146.500  1.00 54.20           C  
ANISOU  404  CG1 VAL A  58     9154   6276   5163    186    112   1097       C  
ATOM    405  CG2 VAL A  58      44.463  52.096 144.507  1.00 54.36           C  
ANISOU  405  CG2 VAL A  58     9134   6347   5174    122    137   1195       C  
ATOM    406  N   GLY A  59      45.083  49.509 148.114  1.00 53.61           N  
ANISOU  406  N   GLY A  59     9138   6228   5003    157     21   1164       N  
ATOM    407  CA  GLY A  59      45.436  49.066 149.467  1.00 53.54           C  
ANISOU  407  CA  GLY A  59     9161   6211   4968    181    -10   1148       C  
ATOM    408  C   GLY A  59      46.007  47.660 149.558  1.00 53.25           C  
ANISOU  408  C   GLY A  59     9154   6146   4933    161    -69   1137       C  
ATOM    409  O   GLY A  59      46.897  47.411 150.367  1.00 53.20           O  
ANISOU  409  O   GLY A  59     9171   6113   4928    185   -103   1093       O  
ATOM    410  N   ALA A  60      45.499  46.746 148.730  1.00 52.95           N  
ANISOU  410  N   ALA A  60     9114   6109   4893    117    -82   1176       N  
ATOM    411  CA  ALA A  60      45.956  45.348 148.719  1.00 52.76           C  
ANISOU  411  CA  ALA A  60     9122   6051   4873     96   -139   1168       C  
ATOM    412  C   ALA A  60      47.169  45.072 147.818  1.00 52.31           C  
ANISOU  412  C   ALA A  60     9064   5948   4863     96   -161   1099       C  
ATOM    413  O   ALA A  60      47.919  44.138 148.098  1.00 52.57           O  
ANISOU  413  O   ALA A  60     9124   5942   4907    102   -210   1070       O  
ATOM    414  CB  ALA A  60      44.809  44.427 148.331  1.00 53.02           C  
ANISOU  414  CB  ALA A  60     9159   6105   4880     46   -149   1242       C  
ATOM    415  N   LEU A  61      47.343  45.848 146.739  1.00 51.54           N  
ANISOU  415  N   LEU A  61     8933   5855   4792     90   -125   1076       N  
ATOM    416  CA  LEU A  61      48.463  45.661 145.793  1.00 51.15           C  
ANISOU  416  CA  LEU A  61     8876   5772   4785     88   -136   1011       C  
ATOM    417  C   LEU A  61      49.434  46.844 145.722  1.00 50.74           C  
ANISOU  417  C   LEU A  61     8798   5714   4767    118   -110    952       C  
ATOM    418  O   LEU A  61      50.651  46.643 145.839  1.00 50.53           O  
ANISOU  418  O   LEU A  61     8773   5657   4769    139   -136    889       O  
ATOM    419  CB  LEU A  61      47.942  45.333 144.384  1.00 51.08           C  
ANISOU  419  CB  LEU A  61     8854   5774   4777     44   -123   1034       C  
ATOM    420  CG  LEU A  61      48.953  45.089 143.249  1.00 50.86           C  
ANISOU  420  CG  LEU A  61     8817   5721   4784     38   -128    972       C  
ATOM    421  CD1 LEU A  61      49.924  43.970 143.580  1.00 50.92           C  
ANISOU  421  CD1 LEU A  61     8854   5684   4810     55   -181    923       C  
ATOM    422  CD2 LEU A  61      48.220  44.793 141.954  1.00 50.74           C  
ANISOU  422  CD2 LEU A  61     8793   5726   4757     -8   -114   1004       C  
ATOM    423  N   VAL A  62      48.914  48.060 145.530  1.00 50.59           N  
ANISOU  423  N   VAL A  62     8754   5722   4746    120    -61    972       N  
ATOM    424  CA  VAL A  62      49.775  49.226 145.267  1.00 50.51           C  
ANISOU  424  CA  VAL A  62     8718   5701   4771    138    -34    921       C  
ATOM    425  C   VAL A  62      50.607  49.601 146.494  1.00 50.54           C  
ANISOU  425  C   VAL A  62     8734   5686   4783    177    -53    874       C  
ATOM    426  O   VAL A  62      51.812  49.826 146.371  1.00 50.21           O  
ANISOU  426  O   VAL A  62     8679   5620   4776    188    -64    811       O  
ATOM    427  CB  VAL A  62      48.970  50.454 144.760  1.00 50.55           C  
ANISOU  427  CB  VAL A  62     8697   5732   4774    132     21    959       C  
ATOM    428  CG1 VAL A  62      49.843  51.708 144.660  1.00 50.64           C  
ANISOU  428  CG1 VAL A  62     8689   5726   4823    150     46    910       C  
ATOM    429  CG2 VAL A  62      48.325  50.141 143.414  1.00 50.51           C  
ANISOU  429  CG2 VAL A  62     8676   5749   4765     92     37    999       C  
ATOM    430  N   ILE A  63      49.970  49.658 147.665  1.00 50.68           N  
ANISOU  430  N   ILE A  63     8773   5716   4764    196    -58    904       N  
ATOM    431  CA  ILE A  63      50.667  50.066 148.893  1.00 50.89           C  
ANISOU  431  CA  ILE A  63     8814   5729   4789    232    -77    861       C  
ATOM    432  C   ILE A  63      51.737  49.057 149.365  1.00 50.76           C  
ANISOU  432  C   ILE A  63     8816   5686   4783    243   -136    817       C  
ATOM    433  O   ILE A  63      52.838  49.475 149.748  1.00 50.84           O  
ANISOU  433  O   ILE A  63     8819   5677   4819    264   -153    757       O  
ATOM    434  CB  ILE A  63      49.671  50.469 150.011  1.00 51.32           C  
ANISOU  434  CB  ILE A  63     8889   5813   4797    252    -60    903       C  
ATOM    435  CG1 ILE A  63      48.978  51.785 149.620  1.00 51.45           C  
ANISOU  435  CG1 ILE A  63     8883   5846   4817    257     -1    922       C  
ATOM    436  CG2 ILE A  63      50.386  50.646 151.349  1.00 51.69           C  
ANISOU  436  CG2 ILE A  63     8959   5849   4831    287    -90    859       C  
ATOM    437  CD1 ILE A  63      47.804  52.176 150.496  1.00 51.79           C  
ANISOU  437  CD1 ILE A  63     8937   5924   4813    278     25    971       C  
ATOM    438  N   PRO A  64      51.427  47.743 149.345  1.00 50.61           N  
ANISOU  438  N   PRO A  64     8818   5663   4747    229   -171    849       N  
ATOM    439  CA  PRO A  64      52.450  46.714 149.586  1.00 50.66           C  
ANISOU  439  CA  PRO A  64     8840   5637   4771    241   -228    809       C  
ATOM    440  C   PRO A  64      53.657  46.766 148.644  1.00 50.71           C  
ANISOU  440  C   PRO A  64     8816   5620   4831    242   -231    744       C  
ATOM    441  O   PRO A  64      54.796  46.674 149.112  1.00 50.54           O  
ANISOU  441  O   PRO A  64     8790   5578   4832    268   -265    691       O  
ATOM    442  CB  PRO A  64      51.679  45.417 149.382  1.00 50.71           C  
ANISOU  442  CB  PRO A  64     8872   5639   4753    216   -252    863       C  
ATOM    443  CG  PRO A  64      50.318  45.748 149.860  1.00 50.73           C  
ANISOU  443  CG  PRO A  64     8883   5680   4709    203   -222    933       C  
ATOM    444  CD  PRO A  64      50.071  47.167 149.428  1.00 50.57           C  
ANISOU  444  CD  PRO A  64     8830   5683   4699    206   -164    926       C  
ATOM    445  N   LEU A  65      53.407  46.910 147.341  1.00 50.80           N  
ANISOU  445  N   LEU A  65     8805   5638   4858    214   -197    751       N  
ATOM    446  CA  LEU A  65      54.485  47.057 146.353  1.00 51.13           C  
ANISOU  446  CA  LEU A  65     8813   5667   4945    213   -189    693       C  
ATOM    447  C   LEU A  65      55.407  48.239 146.667  1.00 51.45           C  
ANISOU  447  C   LEU A  65     8824   5707   5015    231   -175    642       C  
ATOM    448  O   LEU A  65      56.630  48.123 146.552  1.00 51.79           O  
ANISOU  448  O   LEU A  65     8847   5736   5095    245   -195    584       O  
ATOM    449  CB  LEU A  65      53.912  47.219 144.943  1.00 51.09           C  
ANISOU  449  CB  LEU A  65     8790   5679   4943    176   -147    716       C  
ATOM    450  CG  LEU A  65      53.412  45.952 144.241  1.00 51.19           C  
ANISOU  450  CG  LEU A  65     8823   5685   4941    152   -166    741       C  
ATOM    451  CD1 LEU A  65      52.551  46.298 143.034  1.00 50.98           C  
ANISOU  451  CD1 LEU A  65     8781   5686   4902    113   -122    779       C  
ATOM    452  CD2 LEU A  65      54.572  45.061 143.831  1.00 51.44           C  
ANISOU  452  CD2 LEU A  65     8852   5687   5003    167   -199    680       C  
ATOM    453  N   ALA A  66      54.812  49.362 147.068  1.00 51.52           N  
ANISOU  453  N   ALA A  66     8833   5731   5010    231   -141    665       N  
ATOM    454  CA  ALA A  66      55.561  50.563 147.450  1.00 51.76           C  
ANISOU  454  CA  ALA A  66     8844   5757   5066    243   -128    620       C  
ATOM    455  C   ALA A  66      56.453  50.302 148.655  1.00 52.13           C  
ANISOU  455  C   ALA A  66     8903   5790   5115    274   -180    577       C  
ATOM    456  O   ALA A  66      57.625  50.686 148.657  1.00 52.31           O  
ANISOU  456  O   ALA A  66     8898   5801   5174    281   -192    519       O  
ATOM    457  CB  ALA A  66      54.613  51.720 147.740  1.00 51.75           C  
ANISOU  457  CB  ALA A  66     8848   5768   5044    243    -85    656       C  
ATOM    458  N   ILE A  67      55.896  49.634 149.664  1.00 52.52           N  
ANISOU  458  N   ILE A  67     8990   5842   5122    290   -210    608       N  
ATOM    459  CA  ILE A  67      56.655  49.252 150.864  1.00 53.21           C  
ANISOU  459  CA  ILE A  67     9094   5919   5202    320   -266    575       C  
ATOM    460  C   ILE A  67      57.796  48.288 150.496  1.00 53.74           C  
ANISOU  460  C   ILE A  67     9145   5967   5306    329   -310    534       C  
ATOM    461  O   ILE A  67      58.954  48.515 150.883  1.00 54.17           O  
ANISOU  461  O   ILE A  67     9179   6014   5389    347   -339    479       O  
ATOM    462  CB  ILE A  67      55.732  48.632 151.951  1.00 53.14           C  
ANISOU  462  CB  ILE A  67     9133   5923   5136    331   -288    628       C  
ATOM    463  CG1 ILE A  67      54.755  49.687 152.481  1.00 53.06           C  
ANISOU  463  CG1 ILE A  67     9134   5936   5089    332   -244    657       C  
ATOM    464  CG2 ILE A  67      56.544  48.067 153.113  1.00 53.43           C  
ANISOU  464  CG2 ILE A  67     9189   5950   5162    360   -352    600       C  
ATOM    465  CD1 ILE A  67      53.510  49.115 153.121  1.00 53.12           C  
ANISOU  465  CD1 ILE A  67     9176   5967   5038    332   -243    726       C  
ATOM    466  N   LEU A  68      57.466  47.238 149.739  1.00 53.84           N  
ANISOU  466  N   LEU A  68     9165   5971   5320    318   -315    559       N  
ATOM    467  CA  LEU A  68      58.465  46.266 149.280  1.00 54.37           C  
ANISOU  467  CA  LEU A  68     9219   6017   5422    331   -352    519       C  
ATOM    468  C   LEU A  68      59.584  46.911 148.465  1.00 54.70           C  
ANISOU  468  C   LEU A  68     9205   6061   5515    330   -331    458       C  
ATOM    469  O   LEU A  68      60.751  46.587 148.668  1.00 54.93           O  
ANISOU  469  O   LEU A  68     9213   6081   5576    355   -368    408       O  
ATOM    470  CB  LEU A  68      57.811  45.133 148.473  1.00 54.42           C  
ANISOU  470  CB  LEU A  68     9245   6010   5419    314   -353    555       C  
ATOM    471  CG  LEU A  68      57.008  44.077 149.252  1.00 54.60           C  
ANISOU  471  CG  LEU A  68     9322   6021   5402    316   -392    609       C  
ATOM    472  CD1 LEU A  68      56.382  43.094 148.270  1.00 54.61           C  
ANISOU  472  CD1 LEU A  68     9340   6008   5400    290   -390    638       C  
ATOM    473  CD2 LEU A  68      57.858  43.345 150.288  1.00 54.84           C  
ANISOU  473  CD2 LEU A  68     9369   6027   5437    355   -459    586       C  
ATOM    474  N   ILE A  69      59.228  47.819 147.557  1.00 55.27           N  
ANISOU  474  N   ILE A  69     9254   6150   5596    300   -273    466       N  
ATOM    475  CA  ILE A  69      60.228  48.594 146.801  1.00 56.04           C  
ANISOU  475  CA  ILE A  69     9298   6254   5738    291   -247    415       C  
ATOM    476  C   ILE A  69      61.037  49.521 147.725  1.00 57.02           C  
ANISOU  476  C   ILE A  69     9405   6379   5880    304   -263    375       C  
ATOM    477  O   ILE A  69      62.252  49.663 147.546  1.00 57.13           O  
ANISOU  477  O   ILE A  69     9376   6394   5935    311   -275    322       O  
ATOM    478  CB  ILE A  69      59.575  49.390 145.634  1.00 55.51           C  
ANISOU  478  CB  ILE A  69     9214   6203   5671    253   -182    442       C  
ATOM    479  CG1 ILE A  69      59.045  48.425 144.552  1.00 55.57           C  
ANISOU  479  CG1 ILE A  69     9231   6214   5667    238   -171    466       C  
ATOM    480  CG2 ILE A  69      60.542  50.394 145.011  1.00 55.42           C  
ANISOU  480  CG2 ILE A  69     9151   6201   5703    239   -152    398       C  
ATOM    481  CD1 ILE A  69      60.094  47.773 143.668  1.00 55.73           C  
ANISOU  481  CD1 ILE A  69     9219   6234   5721    244   -177    415       C  
ATOM    482  N   ASN A  70      60.371  50.134 148.705  1.00 58.07           N  
ANISOU  482  N   ASN A  70     9569   6512   5980    307   -262    400       N  
ATOM    483  CA  ASN A  70      61.037  51.022 149.665  1.00 59.43           C  
ANISOU  483  CA  ASN A  70     9734   6682   6162    318   -281    361       C  
ATOM    484  C   ASN A  70      62.079  50.285 150.508  1.00 60.41           C  
ANISOU  484  C   ASN A  70     9855   6801   6296    349   -348    322       C  
ATOM    485  O   ASN A  70      63.234  50.716 150.588  1.00 60.79           O  
ANISOU  485  O   ASN A  70     9863   6851   6382    351   -366    269       O  
ATOM    486  CB  ASN A  70      60.010  51.696 150.583  1.00 59.95           C  
ANISOU  486  CB  ASN A  70     9844   6752   6183    321   -267    396       C  
ATOM    487  CG  ASN A  70      60.640  52.713 151.523  1.00 60.57           C  
ANISOU  487  CG  ASN A  70     9920   6825   6268    328   -283    352       C  
ATOM    488  OD1 ASN A  70      60.802  52.455 152.716  1.00 60.95           O  
ANISOU  488  OD1 ASN A  70     9995   6875   6288    352   -328    341       O  
ATOM    489  ND2 ASN A  70      61.006  53.868 150.986  1.00 60.77           N  
ANISOU  489  ND2 ASN A  70     9916   6844   6329    305   -248    326       N  
ATOM    490  N   ILE A  71      61.665  49.179 151.126  1.00 61.28           N  
ANISOU  490  N   ILE A  71    10004   6906   6372    371   -388    351       N  
ATOM    491  CA  ILE A  71      62.580  48.371 151.957  1.00 62.16           C  
ANISOU  491  CA  ILE A  71    10117   7011   6490    405   -457    322       C  
ATOM    492  C   ILE A  71      63.549  47.497 151.140  1.00 63.24           C  
ANISOU  492  C   ILE A  71    10214   7138   6673    419   -477    289       C  
ATOM    493  O   ILE A  71      64.603  47.112 151.646  1.00 63.83           O  
ANISOU  493  O   ILE A  71    10269   7211   6770    448   -529    251       O  
ATOM    494  CB  ILE A  71      61.818  47.505 152.998  1.00 61.94           C  
ANISOU  494  CB  ILE A  71    10148   6978   6407    425   -496    370       C  
ATOM    495  CG1 ILE A  71      61.094  46.315 152.333  1.00 61.90           C  
ANISOU  495  CG1 ILE A  71    10167   6958   6392    420   -493    416       C  
ATOM    496  CG2 ILE A  71      60.873  48.381 153.813  1.00 61.69           C  
ANISOU  496  CG2 ILE A  71    10151   6961   6326    415   -472    400       C  
ATOM    497  CD1 ILE A  71      60.096  45.604 153.227  1.00 61.97           C  
ANISOU  497  CD1 ILE A  71    10234   6965   6344    425   -518    477       C  
ATOM    498  N   GLY A  72      63.195  47.194 149.890  1.00 64.21           N  
ANISOU  498  N   GLY A  72    10327   7259   6809    401   -436    302       N  
ATOM    499  CA  GLY A  72      63.969  46.278 149.049  1.00 65.55           C  
ANISOU  499  CA  GLY A  72    10467   7420   7017    418   -449    270       C  
ATOM    500  C   GLY A  72      65.242  46.853 148.445  1.00 67.00           C  
ANISOU  500  C   GLY A  72    10580   7621   7254    417   -435    209       C  
ATOM    501  O   GLY A  72      65.605  47.996 148.735  1.00 67.25           O  
ANISOU  501  O   GLY A  72    10586   7667   7297    400   -421    190       O  
ATOM    502  N   PRO A  73      65.928  46.062 147.592  1.00 68.98           N  
ANISOU  502  N   PRO A  73    10800   7870   7537    435   -437    178       N  
ATOM    503  CA  PRO A  73      67.174  46.465 146.944  1.00 70.20           C  
ANISOU  503  CA  PRO A  73    10881   8048   7743    436   -422    121       C  
ATOM    504  C   PRO A  73      66.939  47.208 145.625  1.00 70.78           C  
ANISOU  504  C   PRO A  73    10925   8143   7824    393   -348    123       C  
ATOM    505  O   PRO A  73      65.793  47.530 145.285  1.00 70.91           O  
ANISOU  505  O   PRO A  73    10979   8156   7808    361   -310    170       O  
ATOM    506  CB  PRO A  73      67.846  45.118 146.668  1.00 70.56           C  
ANISOU  506  CB  PRO A  73    10916   8080   7811    483   -458     93       C  
ATOM    507  CG  PRO A  73      66.700  44.222 146.336  1.00 70.05           C  
ANISOU  507  CG  PRO A  73    10915   7987   7710    479   -453    138       C  
ATOM    508  CD  PRO A  73      65.538  44.697 147.180  1.00 69.52           C  
ANISOU  508  CD  PRO A  73    10904   7914   7596    454   -454    195       C  
ATOM    509  N   GLN A  74      68.026  47.476 144.898  1.00 71.45           N  
ANISOU  509  N   GLN A  74    10941   8253   7951    391   -327     76       N  
ATOM    510  CA  GLN A  74      67.938  47.941 143.512  1.00 71.69           C  
ANISOU  510  CA  GLN A  74    10941   8308   7989    354   -259     76       C  
ATOM    511  C   GLN A  74      67.322  46.845 142.651  1.00 71.08           C  
ANISOU  511  C   GLN A  74    10896   8221   7889    364   -246     90       C  
ATOM    512  O   GLN A  74      67.448  45.659 142.967  1.00 72.42           O  
ANISOU  512  O   GLN A  74    11090   8366   8058    406   -291     79       O  
ATOM    513  CB  GLN A  74      69.316  48.303 142.957  1.00 73.00           C  
ANISOU  513  CB  GLN A  74    11023   8508   8203    354   -243     21       C  
ATOM    514  CG  GLN A  74      69.911  49.577 143.536  1.00 73.86           C  
ANISOU  514  CG  GLN A  74    11094   8631   8337    327   -244      8       C  
ATOM    515  CD  GLN A  74      71.247  49.941 142.906  1.00 75.26           C  
ANISOU  515  CD  GLN A  74    11182   8849   8564    318   -225    -40       C  
ATOM    516  OE1 GLN A  74      71.458  49.760 141.702  1.00 75.76           O  
ANISOU  516  OE1 GLN A  74    11212   8939   8634    309   -178    -50       O  
ATOM    517  NE2 GLN A  74      72.157  50.465 143.720  1.00 76.21           N  
ANISOU  517  NE2 GLN A  74    11262   8978   8715    319   -261    -70       N  
ATOM    518  N   THR A  75      66.665  47.249 141.566  1.00 69.71           N  
ANISOU  518  N   THR A  75    10725   8062   7697    323   -188    115       N  
ATOM    519  CA  THR A  75      65.960  46.315 140.687  1.00 68.88           C  
ANISOU  519  CA  THR A  75    10656   7951   7565    322   -174    131       C  
ATOM    520  C   THR A  75      66.345  46.530 139.234  1.00 68.35           C  
ANISOU  520  C   THR A  75    10543   7920   7505    299   -116    108       C  
ATOM    521  O   THR A  75      66.887  47.575 138.878  1.00 68.17           O  
ANISOU  521  O   THR A  75    10469   7928   7502    273    -78     97       O  
ATOM    522  CB  THR A  75      64.435  46.493 140.800  1.00 68.37           C  
ANISOU  522  CB  THR A  75    10651   7871   7453    291   -162    200       C  
ATOM    523  OG1 THR A  75      64.070  47.822 140.410  1.00 67.86           O  
ANISOU  523  OG1 THR A  75    10568   7831   7385    246   -111    227       O  
ATOM    524  CG2 THR A  75      63.966  46.239 142.221  1.00 68.47           C  
ANISOU  524  CG2 THR A  75    10710   7853   7450    312   -214    227       C  
ATOM    525  N   TYR A  76      66.044  45.538 138.399  1.00 67.47           N  
ANISOU  525  N   TYR A  76    10455   7804   7375    307   -109    101       N  
ATOM    526  CA  TYR A  76      66.114  45.705 136.949  1.00 67.24           C  
ANISOU  526  CA  TYR A  76    10398   7813   7336    279    -50     89       C  
ATOM    527  C   TYR A  76      65.182  46.838 136.517  1.00 66.61           C  
ANISOU  527  C   TYR A  76    10326   7752   7228    221     -4    147       C  
ATOM    528  O   TYR A  76      64.233  47.169 137.235  1.00 66.48           O  
ANISOU  528  O   TYR A  76    10352   7714   7193    207    -19    198       O  
ATOM    529  CB  TYR A  76      65.678  44.426 136.227  1.00 67.30           C  
ANISOU  529  CB  TYR A  76    10447   7804   7316    293    -57     79       C  
ATOM    530  CG  TYR A  76      66.625  43.254 136.344  1.00 67.42           C  
ANISOU  530  CG  TYR A  76    10454   7800   7360    355    -94     16       C  
ATOM    531  CD1 TYR A  76      67.914  43.312 135.811  1.00 67.62           C  
ANISOU  531  CD1 TYR A  76    10409   7862   7418    380    -71    -45       C  
ATOM    532  CD2 TYR A  76      66.220  42.070 136.955  1.00 67.51           C  
ANISOU  532  CD2 TYR A  76    10525   7758   7364    388   -151     21       C  
ATOM    533  CE1 TYR A  76      68.779  42.232 135.905  1.00 68.34           C  
ANISOU  533  CE1 TYR A  76    10490   7936   7538    443   -104   -103       C  
ATOM    534  CE2 TYR A  76      67.074  40.981 137.052  1.00 68.16           C  
ANISOU  534  CE2 TYR A  76    10603   7816   7475    449   -187    -34       C  
ATOM    535  CZ  TYR A  76      68.352  41.063 136.527  1.00 68.57           C  
ANISOU  535  CZ  TYR A  76    10585   7905   7563    480   -163    -98       C  
ATOM    536  OH  TYR A  76      69.193  39.979 136.630  1.00 68.62           O  
ANISOU  536  OH  TYR A  76    10584   7887   7600    547   -199   -153       O  
ATOM    537  N   PHE A  77      65.440  47.431 135.352  1.00 66.19           N  
ANISOU  537  N   PHE A  77    10233   7741   7172    188     52    141       N  
ATOM    538  CA  PHE A  77      64.505  48.423 134.797  1.00 65.52           C  
ANISOU  538  CA  PHE A  77    10159   7674   7060    134     96    201       C  
ATOM    539  C   PHE A  77      63.070  47.868 134.633  1.00 65.16           C  
ANISOU  539  C   PHE A  77    10179   7610   6966    120     87    253       C  
ATOM    540  O   PHE A  77      62.091  48.530 135.021  1.00 64.64           O  
ANISOU  540  O   PHE A  77    10140   7536   6884     96     91    312       O  
ATOM    541  CB  PHE A  77      65.014  48.968 133.460  1.00 65.67           C  
ANISOU  541  CB  PHE A  77    10129   7745   7077    101    157    188       C  
ATOM    542  CG  PHE A  77      64.213  50.129 132.939  1.00 65.09           C  
ANISOU  542  CG  PHE A  77    10058   7688   6982     47    201    251       C  
ATOM    543  CD1 PHE A  77      64.499  51.424 133.352  1.00 64.92           C  
ANISOU  543  CD1 PHE A  77    10008   7666   6990     25    216    269       C  
ATOM    544  CD2 PHE A  77      63.160  49.928 132.048  1.00 64.61           C  
ANISOU  544  CD2 PHE A  77    10032   7642   6874     19    223    294       C  
ATOM    545  CE1 PHE A  77      63.760  52.498 132.882  1.00 64.66           C  
ANISOU  545  CE1 PHE A  77     9982   7642   6942    -19    254    329       C  
ATOM    546  CE2 PHE A  77      62.415  50.997 131.574  1.00 64.36           C  
ANISOU  546  CE2 PHE A  77    10002   7626   6824    -26    260    356       C  
ATOM    547  CZ  PHE A  77      62.716  52.286 131.992  1.00 64.55           C  
ANISOU  547  CZ  PHE A  77     9999   7645   6881    -43    276    374       C  
ATOM    548  N   HIS A  78      62.960  46.656 134.084  1.00 65.59           N  
ANISOU  548  N   HIS A  78    10259   7660   7000    135     74    230       N  
ATOM    549  CA  HIS A  78      61.652  46.030 133.804  1.00 65.38           C  
ANISOU  549  CA  HIS A  78    10291   7620   6928    115     63    275       C  
ATOM    550  C   HIS A  78      60.825  45.799 135.074  1.00 64.57           C  
ANISOU  550  C   HIS A  78    10237   7476   6820    126     16    318       C  
ATOM    551  O   HIS A  78      59.606  46.000 135.064  1.00 64.25           O  
ANISOU  551  O   HIS A  78    10228   7436   6746     95     21    380       O  
ATOM    552  CB  HIS A  78      61.808  44.714 132.997  1.00 66.22           C  
ANISOU  552  CB  HIS A  78    10419   7722   7017    130     53    232       C  
ATOM    553  CG  HIS A  78      62.051  43.495 133.837  1.00 66.87           C  
ANISOU  553  CG  HIS A  78    10536   7753   7116    178     -7    201       C  
ATOM    554  ND1 HIS A  78      63.311  42.990 134.080  1.00 67.44           N  
ANISOU  554  ND1 HIS A  78    10579   7815   7228    230    -25    134       N  
ATOM    555  CD2 HIS A  78      61.188  42.678 134.490  1.00 67.43           C  
ANISOU  555  CD2 HIS A  78    10667   7779   7171    182    -54    234       C  
ATOM    556  CE1 HIS A  78      63.212  41.920 134.851  1.00 68.01           C  
ANISOU  556  CE1 HIS A  78    10696   7836   7308    266    -83    126       C  
ATOM    557  NE2 HIS A  78      61.934  41.710 135.115  1.00 67.63           N  
ANISOU  557  NE2 HIS A  78    10704   7765   7225    235   -101    187       N  
ATOM    558  N   THR A  79      61.499  45.381 136.150  1.00 64.18           N  
ANISOU  558  N   THR A  79    10188   7395   6800    170    -27    286       N  
ATOM    559  CA  THR A  79      60.863  45.120 137.444  1.00 63.78           C  
ANISOU  559  CA  THR A  79    10181   7309   6743    184    -73    323       C  
ATOM    560  C   THR A  79      60.212  46.386 137.986  1.00 63.21           C  
ANISOU  560  C   THR A  79    10105   7248   6662    160    -52    375       C  
ATOM    561  O   THR A  79      59.051  46.375 138.390  1.00 62.31           O  
ANISOU  561  O   THR A  79    10029   7125   6518    145    -60    432       O  
ATOM    562  CB  THR A  79      61.892  44.626 138.485  1.00 64.02           C  
ANISOU  562  CB  THR A  79    10203   7311   6809    236   -123    276       C  
ATOM    563  OG1 THR A  79      62.610  43.500 137.966  1.00 64.55           O  
ANISOU  563  OG1 THR A  79    10268   7365   6890    268   -141    222       O  
ATOM    564  CG2 THR A  79      61.210  44.239 139.805  1.00 63.73           C  
ANISOU  564  CG2 THR A  79    10216   7239   6757    250   -173    317       C  
ATOM    565  N   CYS A  80      60.981  47.471 137.983  1.00 63.30           N  
ANISOU  565  N   CYS A  80    10069   7278   6703    156    -25    353       N  
ATOM    566  CA  CYS A  80      60.500  48.766 138.437  1.00 63.04           C  
ANISOU  566  CA  CYS A  80    10031   7250   6668    136     -2    393       C  
ATOM    567  C   CYS A  80      59.426  49.312 137.501  1.00 62.51           C  
ANISOU  567  C   CYS A  80     9972   7207   6571     93     42    450       C  
ATOM    568  O   CYS A  80      58.428  49.871 137.966  1.00 62.57           O  
ANISOU  568  O   CYS A  80    10002   7210   6559     83     48    504       O  
ATOM    569  CB  CYS A  80      61.660  49.755 138.551  1.00 63.56           C  
ANISOU  569  CB  CYS A  80    10044   7326   6776    137     13    353       C  
ATOM    570  SG  CYS A  80      61.237  51.298 139.389  1.00 63.93           S  
ANISOU  570  SG  CYS A  80    10095   7364   6830    121     28    388       S  
ATOM    571  N   LEU A  81      59.620  49.140 136.193  1.00 62.10           N  
ANISOU  571  N   LEU A  81     9899   7181   6511     71     74    438       N  
ATOM    572  CA  LEU A  81      58.600  49.537 135.218  1.00 61.80           C  
ANISOU  572  CA  LEU A  81     9869   7170   6440     30    112    493       C  
ATOM    573  C   LEU A  81      57.265  48.810 135.438  1.00 61.15           C  
ANISOU  573  C   LEU A  81     9837   7077   6317     24     88    545       C  
ATOM    574  O   LEU A  81      56.208  49.442 135.395  1.00 60.64           O  
ANISOU  574  O   LEU A  81     9783   7025   6232      1    106    607       O  
ATOM    575  CB  LEU A  81      59.095  49.312 133.784  1.00 62.53           C  
ANISOU  575  CB  LEU A  81     9936   7297   6524      9    145    466       C  
ATOM    576  CG  LEU A  81      58.175  49.765 132.634  1.00 62.49           C  
ANISOU  576  CG  LEU A  81     9934   7327   6482    -36    184    521       C  
ATOM    577  CD1 LEU A  81      57.787  51.235 132.763  1.00 62.45           C  
ANISOU  577  CD1 LEU A  81     9911   7328   6486    -56    217    572       C  
ATOM    578  CD2 LEU A  81      58.823  49.489 131.283  1.00 62.85           C  
ANISOU  578  CD2 LEU A  81     9952   7410   6515    -53    216    484       C  
ATOM    579  N   MET A  82      57.317  47.496 135.671  1.00 60.98           N  
ANISOU  579  N   MET A  82     9845   7034   6288     43     46    521       N  
ATOM    580  CA  MET A  82      56.102  46.698 135.932  1.00 60.60           C  
ANISOU  580  CA  MET A  82     9845   6973   6204     32     18    569       C  
ATOM    581  C   MET A  82      55.356  47.114 137.191  1.00 58.82           C  
ANISOU  581  C   MET A  82     9640   6735   5974     42      2    618       C  
ATOM    582  O   MET A  82      54.129  47.206 137.184  1.00 58.09           O  
ANISOU  582  O   MET A  82     9566   6655   5850     19      8    681       O  
ATOM    583  CB  MET A  82      56.433  45.206 136.034  1.00 62.19           C  
ANISOU  583  CB  MET A  82    10078   7143   6406     53    -28    530       C  
ATOM    584  CG  MET A  82      56.610  44.518 134.692  1.00 63.64           C  
ANISOU  584  CG  MET A  82    10264   7341   6575     35    -16    499       C  
ATOM    585  SD  MET A  82      57.267  42.847 134.908  1.00 65.67           S  
ANISOU  585  SD  MET A  82    10557   7549   6845     73    -71    437       S  
ATOM    586  CE  MET A  82      55.876  42.041 135.708  1.00 65.52           C  
ANISOU  586  CE  MET A  82    10601   7498   6796     55   -119    506       C  
ATOM    587  N   VAL A  83      56.108  47.356 138.261  1.00 57.80           N  
ANISOU  587  N   VAL A  83     9503   6583   5872     77    -17    586       N  
ATOM    588  CA  VAL A  83      55.547  47.745 139.564  1.00 56.85           C  
ANISOU  588  CA  VAL A  83     9404   6452   5745     92    -32    622       C  
ATOM    589  C   VAL A  83      54.911  49.146 139.527  1.00 55.65           C  
ANISOU  589  C   VAL A  83     9234   6321   5588     76     11    665       C  
ATOM    590  O   VAL A  83      53.974  49.417 140.276  1.00 55.45           O  
ANISOU  590  O   VAL A  83     9229   6297   5540     80     10    713       O  
ATOM    591  CB  VAL A  83      56.627  47.647 140.680  1.00 57.15           C  
ANISOU  591  CB  VAL A  83     9438   6464   5812    134    -68    570       C  
ATOM    592  CG1 VAL A  83      56.139  48.216 142.004  1.00 57.22           C  
ANISOU  592  CG1 VAL A  83     9466   6467   5809    149    -79    600       C  
ATOM    593  CG2 VAL A  83      57.071  46.202 140.869  1.00 57.34           C  
ANISOU  593  CG2 VAL A  83     9485   6461   5838    156   -118    540       C  
ATOM    594  N   ALA A  84      55.406  50.019 138.649  1.00 54.72           N  
ANISOU  594  N   ALA A  84     9081   6220   5490     60     51    649       N  
ATOM    595  CA  ALA A  84      54.861  51.370 138.513  1.00 54.06           C  
ANISOU  595  CA  ALA A  84     8983   6149   5407     46     93    690       C  
ATOM    596  C   ALA A  84      53.457  51.454 137.888  1.00 53.53           C  
ANISOU  596  C   ALA A  84     8926   6108   5303     18    115    764       C  
ATOM    597  O   ALA A  84      52.764  52.440 138.098  1.00 53.69           O  
ANISOU  597  O   ALA A  84     8944   6135   5321     18    140    807       O  
ATOM    598  CB  ALA A  84      55.828  52.238 137.724  1.00 54.18           C  
ANISOU  598  CB  ALA A  84     8957   6173   5455     31    127    657       C  
ATOM    599  N   CYS A  85      53.040  50.440 137.126  1.00 53.08           N  
ANISOU  599  N   CYS A  85     8881   6066   5220     -2    104    776       N  
ATOM    600  CA  CYS A  85      51.812  50.517 136.303  1.00 52.83           C  
ANISOU  600  CA  CYS A  85     8851   6066   5154    -36    124    843       C  
ATOM    601  C   CYS A  85      50.434  50.290 136.978  1.00 52.45           C  
ANISOU  601  C   CYS A  85     8827   6026   5075    -36    111    910       C  
ATOM    602  O   CYS A  85      49.461  50.981 136.622  1.00 52.26           O  
ANISOU  602  O   CYS A  85     8791   6029   5035    -51    138    971       O  
ATOM    603  CB  CYS A  85      51.947  49.599 135.084  1.00 53.20           C  
ANISOU  603  CB  CYS A  85     8900   6129   5182    -65    119    826       C  
ATOM    604  SG  CYS A  85      53.317  50.060 133.981  1.00 53.67           S  
ANISOU  604  SG  CYS A  85     8922   6200   5267    -74    152    765       S  
ATOM    605  N   PRO A  86      50.321  49.317 137.916  1.00 52.23           N  
ANISOU  605  N   PRO A  86     8828   5977   5037    -21     69    903       N  
ATOM    606  CA  PRO A  86      49.025  49.056 138.573  1.00 51.86           C  
ANISOU  606  CA  PRO A  86     8800   5945   4959    -25     59    969       C  
ATOM    607  C   PRO A  86      48.290  50.298 139.084  1.00 51.37           C  
ANISOU  607  C   PRO A  86     8722   5900   4894     -9     93   1016       C  
ATOM    608  O   PRO A  86      47.078  50.443 138.856  1.00 51.23           O  
ANISOU  608  O   PRO A  86     8698   5914   4850    -26    107   1084       O  
ATOM    609  CB  PRO A  86      49.413  48.147 139.741  1.00 52.10           C  
ANISOU  609  CB  PRO A  86     8861   5943   4990      0     13    942       C  
ATOM    610  CG  PRO A  86      50.584  47.382 139.238  1.00 52.25           C  
ANISOU  610  CG  PRO A  86     8884   5936   5030      1     -9    874       C  
ATOM    611  CD  PRO A  86      51.309  48.273 138.261  1.00 52.35           C  
ANISOU  611  CD  PRO A  86     8861   5961   5067     -4     29    841       C  
ATOM    612  N   VAL A  87      49.024  51.185 139.753  1.00 51.16           N  
ANISOU  612  N   VAL A  87     8689   5852   4896     23    105    980       N  
ATOM    613  CA  VAL A  87      48.474  52.458 140.225  1.00 51.07           C  
ANISOU  613  CA  VAL A  87     8667   5848   4887     43    140   1012       C  
ATOM    614  C   VAL A  87      47.940  53.325 139.071  1.00 50.79           C  
ANISOU  614  C   VAL A  87     8604   5837   4855     21    181   1055       C  
ATOM    615  O   VAL A  87      46.886  53.949 139.214  1.00 50.70           O  
ANISOU  615  O   VAL A  87     8586   5847   4830     29    204   1113       O  
ATOM    616  CB  VAL A  87      49.497  53.240 141.092  1.00 51.40           C  
ANISOU  616  CB  VAL A  87     8711   5856   4962     78    141    954       C  
ATOM    617  CG1 VAL A  87      50.647  53.794 140.260  1.00 51.50           C  
ANISOU  617  CG1 VAL A  87     8700   5854   5013     65    156    906       C  
ATOM    618  CG2 VAL A  87      48.810  54.353 141.869  1.00 51.64           C  
ANISOU  618  CG2 VAL A  87     8743   5887   4988    107    168    984       C  
ATOM    619  N   LEU A  88      48.642  53.319 137.930  1.00 50.58           N  
ANISOU  619  N   LEU A  88     8562   5812   4843     -4    189   1029       N  
ATOM    620  CA  LEU A  88      48.211  54.060 136.730  1.00 50.35           C  
ANISOU  620  CA  LEU A  88     8509   5809   4813    -30    225   1071       C  
ATOM    621  C   LEU A  88      46.893  53.520 136.193  1.00 50.32           C  
ANISOU  621  C   LEU A  88     8504   5846   4769    -56    221   1141       C  
ATOM    622  O   LEU A  88      45.993  54.299 135.848  1.00 50.42           O  
ANISOU  622  O   LEU A  88     8499   5883   4774    -59    247   1202       O  
ATOM    623  CB  LEU A  88      49.266  54.009 135.619  1.00 50.16           C  
ANISOU  623  CB  LEU A  88     8469   5785   4804    -56    233   1027       C  
ATOM    624  CG  LEU A  88      50.682  54.468 135.968  1.00 50.20           C  
ANISOU  624  CG  LEU A  88     8466   5756   4851    -39    236    956       C  
ATOM    625  CD1 LEU A  88      51.589  54.342 134.758  1.00 50.33           C  
ANISOU  625  CD1 LEU A  88     8460   5785   4875    -68    249    922       C  
ATOM    626  CD2 LEU A  88      50.666  55.891 136.499  1.00 50.27           C  
ANISOU  626  CD2 LEU A  88     8468   5744   4888    -18    263    969       C  
ATOM    627  N   ILE A  89      46.780  52.192 136.148  1.00 50.29           N  
ANISOU  627  N   ILE A  89     8518   5848   4741    -76    185   1132       N  
ATOM    628  CA  ILE A  89      45.531  51.533 135.737  1.00 50.57           C  
ANISOU  628  CA  ILE A  89     8555   5921   4737   -107    173   1196       C  
ATOM    629  C   ILE A  89      44.414  51.897 136.717  1.00 51.03           C  
ANISOU  629  C   ILE A  89     8610   5994   4783    -84    180   1255       C  
ATOM    630  O   ILE A  89      43.345  52.426 136.325  1.00 51.60           O  
ANISOU  630  O   ILE A  89     8659   6105   4840    -93    201   1324       O  
ATOM    631  CB  ILE A  89      45.673  49.988 135.689  1.00 50.59           C  
ANISOU  631  CB  ILE A  89     8586   5914   4721   -131    128   1170       C  
ATOM    632  CG1 ILE A  89      46.720  49.562 134.650  1.00 50.79           C  
ANISOU  632  CG1 ILE A  89     8613   5929   4754   -150    124   1108       C  
ATOM    633  CG2 ILE A  89      44.328  49.319 135.381  1.00 50.63           C  
ANISOU  633  CG2 ILE A  89     8593   5957   4687   -169    111   1239       C  
ATOM    634  CD1 ILE A  89      47.311  48.189 134.893  1.00 50.89           C  
ANISOU  634  CD1 ILE A  89     8659   5911   4766   -151     80   1055       C  
ATOM    635  N   LEU A  90      44.683  51.631 137.995  1.00 51.30           N  
ANISOU  635  N   LEU A  90     8665   6003   4822    -52    163   1229       N  
ATOM    636  CA  LEU A  90      43.657  51.752 139.025  1.00 51.49           C  
ANISOU  636  CA  LEU A  90     8690   6046   4826    -31    166   1280       C  
ATOM    637  C   LEU A  90      43.161  53.187 139.177  1.00 51.89           C  
ANISOU  637  C   LEU A  90     8717   6109   4889      0    211   1314       C  
ATOM    638  O   LEU A  90      41.947  53.417 139.270  1.00 52.00           O  
ANISOU  638  O   LEU A  90     8712   6161   4881      3    226   1382       O  
ATOM    639  CB  LEU A  90      44.163  51.201 140.356  1.00 51.37           C  
ANISOU  639  CB  LEU A  90     8705   6000   4811     -3    138   1241       C  
ATOM    640  CG  LEU A  90      44.437  49.695 140.367  1.00 51.19           C  
ANISOU  640  CG  LEU A  90     8709   5963   4774    -31     90   1222       C  
ATOM    641  CD1 LEU A  90      45.176  49.317 141.648  1.00 51.35           C  
ANISOU  641  CD1 LEU A  90     8759   5949   4801      2     63   1176       C  
ATOM    642  CD2 LEU A  90      43.164  48.886 140.187  1.00 51.27           C  
ANISOU  642  CD2 LEU A  90     8719   6010   4748    -69     75   1293       C  
ATOM    643  N   THR A  91      44.093  54.142 139.175  1.00 52.42           N  
ANISOU  643  N   THR A  91     8783   6142   4992     24    231   1266       N  
ATOM    644  CA  THR A  91      43.739  55.569 139.220  1.00 53.08           C  
ANISOU  644  CA  THR A  91     8848   6224   5093     54    272   1292       C  
ATOM    645  C   THR A  91      42.899  55.973 138.007  1.00 53.59           C  
ANISOU  645  C   THR A  91     8884   6327   5151     29    294   1358       C  
ATOM    646  O   THR A  91      41.925  56.718 138.157  1.00 54.02           O  
ANISOU  646  O   THR A  91     8921   6403   5201     53    320   1415       O  
ATOM    647  CB  THR A  91      44.978  56.486 139.316  1.00 52.98           C  
ANISOU  647  CB  THR A  91     8842   6163   5123     73    286   1227       C  
ATOM    648  OG1 THR A  91      45.787  56.087 140.428  1.00 53.05           O  
ANISOU  648  OG1 THR A  91     8877   6141   5138     95    260   1165       O  
ATOM    649  CG2 THR A  91      44.573  57.940 139.508  1.00 53.15           C  
ANISOU  649  CG2 THR A  91     8855   6173   5166    108    325   1252       C  
ATOM    650  N   GLN A  92      43.262  55.477 136.821  1.00 53.94           N  
ANISOU  650  N   GLN A  92     8922   6381   5190    -15    284   1352       N  
ATOM    651  CA  GLN A  92      42.474  55.758 135.616  1.00 54.40           C  
ANISOU  651  CA  GLN A  92     8953   6481   5235    -44    298   1416       C  
ATOM    652  C   GLN A  92      41.070  55.157 135.700  1.00 55.07           C  
ANISOU  652  C   GLN A  92     9025   6617   5282    -57    286   1489       C  
ATOM    653  O   GLN A  92      40.084  55.819 135.323  1.00 55.57           O  
ANISOU  653  O   GLN A  92     9059   6715   5338    -52    308   1558       O  
ATOM    654  CB  GLN A  92      43.185  55.282 134.347  1.00 54.16           C  
ANISOU  654  CB  GLN A  92     8923   6456   5200    -91    289   1389       C  
ATOM    655  CG  GLN A  92      42.585  55.832 133.055  1.00 54.31           C  
ANISOU  655  CG  GLN A  92     8915   6514   5207   -119    308   1450       C  
ATOM    656  CD  GLN A  92      42.534  57.354 133.017  1.00 54.35           C  
ANISOU  656  CD  GLN A  92     8903   6503   5242    -88    347   1477       C  
ATOM    657  OE1 GLN A  92      43.546  58.022 133.198  1.00 53.91           O  
ANISOU  657  OE1 GLN A  92     8855   6404   5222    -72    362   1429       O  
ATOM    658  NE2 GLN A  92      41.348  57.903 132.793  1.00 54.71           N  
ANISOU  658  NE2 GLN A  92     8926   6583   5278    -79    361   1557       N  
ATOM    659  N   SER A  93      40.974  53.923 136.206  1.00 55.71           N  
ANISOU  659  N   SER A  93     9124   6701   5339    -74    252   1476       N  
ATOM    660  CA  SER A  93      39.653  53.303 136.434  1.00 56.47           C  
ANISOU  660  CA  SER A  93     9208   6846   5401    -91    238   1545       C  
ATOM    661  C   SER A  93      38.728  54.176 137.292  1.00 57.35           C  
ANISOU  661  C   SER A  93     9297   6978   5513    -43    269   1596       C  
ATOM    662  O   SER A  93      37.543  54.356 136.964  1.00 57.66           O  
ANISOU  662  O   SER A  93     9303   7070   5535    -51    279   1672       O  
ATOM    663  CB  SER A  93      39.795  51.913 137.062  1.00 56.32           C  
ANISOU  663  CB  SER A  93     9219   6816   5363   -112    196   1520       C  
ATOM    664  OG  SER A  93      38.544  51.247 137.108  1.00 56.59           O  
ANISOU  664  OG  SER A  93     9239   6898   5363   -142    180   1590       O  
ATOM    665  N   SER A  94      39.284  54.728 138.372  1.00 58.10           N  
ANISOU  665  N   SER A  94     9411   7036   5629      6    284   1552       N  
ATOM    666  CA  SER A  94      38.522  55.591 139.282  1.00 58.85           C  
ANISOU  666  CA  SER A  94     9491   7145   5724     60    316   1587       C  
ATOM    667  C   SER A  94      37.855  56.773 138.573  1.00 59.42           C  
ANISOU  667  C   SER A  94     9527   7237   5811     79    352   1641       C  
ATOM    668  O   SER A  94      36.661  57.047 138.786  1.00 59.58           O  
ANISOU  668  O   SER A  94     9517   7304   5816    100    370   1708       O  
ATOM    669  CB  SER A  94      39.420  56.112 140.406  1.00 58.92           C  
ANISOU  669  CB  SER A  94     9530   7101   5754    109    325   1518       C  
ATOM    670  OG  SER A  94      40.054  55.047 141.093  1.00 59.21           O  
ANISOU  670  OG  SER A  94     9599   7120   5778     96    289   1471       O  
ATOM    671  N   ILE A  95      38.627  57.437 137.711  1.00 59.81           N  
ANISOU  671  N   ILE A  95     9580   7254   5890     72    362   1614       N  
ATOM    672  CA  ILE A  95      38.181  58.652 137.018  1.00 60.18           C  
ANISOU  672  CA  ILE A  95     9601   7308   5957     91    395   1661       C  
ATOM    673  C   ILE A  95      36.995  58.314 136.113  1.00 60.47           C  
ANISOU  673  C   ILE A  95     9598   7412   5965     58    389   1747       C  
ATOM    674  O   ILE A  95      35.939  58.978 136.171  1.00 60.61           O  
ANISOU  674  O   ILE A  95     9582   7462   5981     91    412   1813       O  
ATOM    675  CB  ILE A  95      39.330  59.288 136.190  1.00 60.35           C  
ANISOU  675  CB  ILE A  95     9634   7282   6012     77    402   1618       C  
ATOM    676  CG1 ILE A  95      40.485  59.719 137.107  1.00 60.36           C  
ANISOU  676  CG1 ILE A  95     9668   7218   6045    108    407   1536       C  
ATOM    677  CG2 ILE A  95      38.830  60.497 135.390  1.00 60.94           C  
ANISOU  677  CG2 ILE A  95     9684   7364   6107     91    433   1677       C  
ATOM    678  CD1 ILE A  95      41.817  59.845 136.399  1.00 60.39           C  
ANISOU  678  CD1 ILE A  95     9685   7185   6075     77    403   1479       C  
ATOM    679  N   LEU A  96      37.171  57.262 135.310  1.00 60.52           N  
ANISOU  679  N   LEU A  96     9608   7439   5947     -4    356   1743       N  
ATOM    680  CA  LEU A  96      36.130  56.801 134.381  1.00 61.07           C  
ANISOU  680  CA  LEU A  96     9643   7574   5984    -47    341   1818       C  
ATOM    681  C   LEU A  96      34.882  56.284 135.120  1.00 61.63           C  
ANISOU  681  C   LEU A  96     9689   7697   6028    -41    334   1876       C  
ATOM    682  O   LEU A  96      33.730  56.573 134.718  1.00 61.85           O  
ANISOU  682  O   LEU A  96     9673   7782   6043    -42    342   1956       O  
ATOM    683  CB  LEU A  96      36.695  55.731 133.442  1.00 60.81           C  
ANISOU  683  CB  LEU A  96     9628   7544   5929   -116    305   1787       C  
ATOM    684  CG  LEU A  96      37.845  56.183 132.530  1.00 60.71           C  
ANISOU  684  CG  LEU A  96     9632   7497   5938   -129    314   1739       C  
ATOM    685  CD1 LEU A  96      38.516  54.995 131.858  1.00 60.61           C  
ANISOU  685  CD1 LEU A  96     9643   7482   5902   -186    280   1690       C  
ATOM    686  CD2 LEU A  96      37.363  57.190 131.491  1.00 61.00           C  
ANISOU  686  CD2 LEU A  96     9637   7562   5977   -131    336   1802       C  
ATOM    687  N   ALA A  97      35.120  55.548 136.211  1.00 61.94           N  
ANISOU  687  N   ALA A  97     9756   7720   6059    -35    320   1837       N  
ATOM    688  CA  ALA A  97      34.039  55.131 137.115  1.00 62.25           C  
ANISOU  688  CA  ALA A  97     9773   7805   6073    -24    320   1888       C  
ATOM    689  C   ALA A  97      33.254  56.329 137.668  1.00 62.55           C  
ANISOU  689  C   ALA A  97     9777   7864   6123     45    366   1932       C  
ATOM    690  O   ALA A  97      32.023  56.303 137.690  1.00 62.89           O  
ANISOU  690  O   ALA A  97     9775   7972   6147     46    373   2009       O  
ATOM    691  CB  ALA A  97      34.588  54.281 138.254  1.00 62.14           C  
ANISOU  691  CB  ALA A  97     9799   7760   6049    -22    301   1834       C  
ATOM    692  N   LEU A  98      33.964  57.372 138.098  1.00 62.63           N  
ANISOU  692  N   LEU A  98     9809   7820   6167    101    395   1884       N  
ATOM    693  CA  LEU A  98      33.307  58.611 138.558  1.00 63.15           C  
ANISOU  693  CA  LEU A  98     9849   7893   6250    173    440   1918       C  
ATOM    694  C   LEU A  98      32.541  59.326 137.433  1.00 63.22           C  
ANISOU  694  C   LEU A  98     9813   7938   6270    173    453   1992       C  
ATOM    695  O   LEU A  98      31.395  59.785 137.634  1.00 63.66           O  
ANISOU  695  O   LEU A  98     9824   8043   6320    212    477   2059       O  
ATOM    696  CB  LEU A  98      34.321  59.566 139.204  1.00 63.12           C  
ANISOU  696  CB  LEU A  98     9886   7814   6283    227    463   1843       C  
ATOM    697  CG  LEU A  98      34.826  59.116 140.588  1.00 63.01           C  
ANISOU  697  CG  LEU A  98     9909   7775   6256    249    458   1781       C  
ATOM    698  CD1 LEU A  98      36.159  59.770 140.925  1.00 62.88           C  
ANISOU  698  CD1 LEU A  98     9938   7678   6275    273    463   1694       C  
ATOM    699  CD2 LEU A  98      33.804  59.402 141.680  1.00 63.29           C  
ANISOU  699  CD2 LEU A  98     9924   7851   6270    305    488   1817       C  
ATOM    700  N   LEU A  99      33.171  59.411 136.259  1.00 62.93           N  
ANISOU  700  N   LEU A  99     9786   7880   6245    132    439   1981       N  
ATOM    701  CA  LEU A  99      32.510  59.987 135.077  1.00 63.38           C  
ANISOU  701  CA  LEU A  99     9803   7973   6306    122    444   2054       C  
ATOM    702  C   LEU A  99      31.218  59.239 134.713  1.00 63.76           C  
ANISOU  702  C   LEU A  99     9800   8109   6314     86    424   2137       C  
ATOM    703  O   LEU A  99      30.198  59.875 134.390  1.00 63.87           O  
ANISOU  703  O   LEU A  99     9766   8170   6332    113    440   2214       O  
ATOM    704  CB  LEU A  99      33.462  60.032 133.877  1.00 63.19           C  
ANISOU  704  CB  LEU A  99     9799   7917   6290     74    429   2026       C  
ATOM    705  CG  LEU A  99      32.942  60.678 132.584  1.00 63.64           C  
ANISOU  705  CG  LEU A  99     9822   8007   6349     60    433   2098       C  
ATOM    706  CD1 LEU A  99      32.567  62.145 132.743  1.00 64.04           C  
ANISOU  706  CD1 LEU A  99     9857   8036   6438    133    472   2135       C  
ATOM    707  CD2 LEU A  99      33.991  60.550 131.491  1.00 63.49           C  
ANISOU  707  CD2 LEU A  99     9831   7962   6331      6    418   2060       C  
ATOM    708  N   ALA A 100      31.260  57.903 134.778  1.00 63.93           N  
ANISOU  708  N   ALA A 100     9834   8152   6303     25    387   2122       N  
ATOM    709  CA  ALA A 100      30.036  57.092 134.610  1.00 64.40           C  
ANISOU  709  CA  ALA A 100     9849   8294   6326    -15    364   2196       C  
ATOM    710  C   ALA A 100      28.933  57.488 135.614  1.00 65.29           C  
ANISOU  710  C   ALA A 100     9917   8452   6435     43    395   2251       C  
ATOM    711  O   ALA A 100      27.761  57.688 135.233  1.00 65.87           O  
ANISOU  711  O   ALA A 100     9931   8597   6499     44    398   2336       O  
ATOM    712  CB  ALA A 100      30.353  55.607 134.727  1.00 63.97           C  
ANISOU  712  CB  ALA A 100     9824   8238   6241    -84    320   2162       C  
ATOM    713  N   ILE A 101      29.326  57.620 136.885  1.00 65.71           N  
ANISOU  713  N   ILE A 101     9999   8468   6498     92    417   2200       N  
ATOM    714  CA  ILE A 101      28.414  58.055 137.954  1.00 66.78           C  
ANISOU  714  CA  ILE A 101    10100   8643   6628    157    454   2237       C  
ATOM    715  C   ILE A 101      27.828  59.433 137.649  1.00 67.73           C  
ANISOU  715  C   ILE A 101    10181   8774   6778    226    493   2284       C  
ATOM    716  O   ILE A 101      26.614  59.631 137.795  1.00 69.01           O  
ANISOU  716  O   ILE A 101    10282   9007   6929    253    511   2359       O  
ATOM    717  CB  ILE A 101      29.101  58.080 139.344  1.00 66.94           C  
ANISOU  717  CB  ILE A 101    10167   8613   6651    202    472   2163       C  
ATOM    718  CG1 ILE A 101      29.408  56.654 139.815  1.00 66.75           C  
ANISOU  718  CG1 ILE A 101    10173   8593   6595    140    433   2137       C  
ATOM    719  CG2 ILE A 101      28.225  58.774 140.383  1.00 67.55           C  
ANISOU  719  CG2 ILE A 101    10212   8727   6725    281    519   2195       C  
ATOM    720  CD1 ILE A 101      30.346  56.568 141.006  1.00 66.64           C  
ANISOU  720  CD1 ILE A 101    10215   8520   6582    172    439   2055       C  
ATOM    721  N   ALA A 102      28.682  60.374 137.236  1.00 67.85           N  
ANISOU  721  N   ALA A 102    10229   8719   6831    254    507   2242       N  
ATOM    722  CA  ALA A 102      28.213  61.727 136.865  1.00 68.48           C  
ANISOU  722  CA  ALA A 102    10279   8794   6944    320    541   2285       C  
ATOM    723  C   ALA A 102      27.164  61.716 135.742  1.00 68.64           C  
ANISOU  723  C   ALA A 102    10236   8890   6953    291    526   2384       C  
ATOM    724  O   ALA A 102      26.089  62.328 135.883  1.00 68.63           O  
ANISOU  724  O   ALA A 102    10179   8938   6958    347    552   2453       O  
ATOM    725  CB  ALA A 102      29.384  62.615 136.473  1.00 68.60           C  
ANISOU  725  CB  ALA A 102    10345   8719   7001    336    550   2226       C  
ATOM    726  N   VAL A 103      27.465  61.012 134.647  1.00 68.79           N  
ANISOU  726  N   VAL A 103    10260   8921   6954    208    484   2391       N  
ATOM    727  CA  VAL A 103      26.501  60.909 133.535  1.00 69.87           C  
ANISOU  727  CA  VAL A 103    10339   9134   7073    171    462   2484       C  
ATOM    728  C   VAL A 103      25.238  60.126 133.924  1.00 70.65           C  
ANISOU  728  C   VAL A 103    10378   9328   7137    152    451   2550       C  
ATOM    729  O   VAL A 103      24.137  60.458 133.455  1.00 71.16           O  
ANISOU  729  O   VAL A 103    10375   9462   7198    165    452   2639       O  
ATOM    730  CB  VAL A 103      27.117  60.366 132.211  1.00 69.48           C  
ANISOU  730  CB  VAL A 103    10312   9079   7006     85    420   2473       C  
ATOM    731  CG1 VAL A 103      28.282  61.237 131.769  1.00 69.21           C  
ANISOU  731  CG1 VAL A 103    10326   8962   7007    104    436   2420       C  
ATOM    732  CG2 VAL A 103      27.555  58.914 132.315  1.00 69.12           C  
ANISOU  732  CG2 VAL A 103    10298   9036   6925      6    381   2425       C  
ATOM    733  N   ASP A 104      25.384  59.109 134.783  1.00 71.51           N  
ANISOU  733  N   ASP A 104    10508   9440   7222    122    440   2512       N  
ATOM    734  CA  ASP A 104      24.201  58.420 135.330  1.00 73.04           C  
ANISOU  734  CA  ASP A 104    10646   9721   7385    108    435   2575       C  
ATOM    735  C   ASP A 104      23.328  59.371 136.163  1.00 74.62           C  
ANISOU  735  C   ASP A 104    10794   9955   7600    205    488   2618       C  
ATOM    736  O   ASP A 104      22.101  59.390 136.003  1.00 75.38           O  
ANISOU  736  O   ASP A 104    10815  10140   7685    210    491   2706       O  
ATOM    737  CB  ASP A 104      24.582  57.201 136.174  1.00 72.53           C  
ANISOU  737  CB  ASP A 104    10619   9644   7292     61    415   2527       C  
ATOM    738  CG  ASP A 104      23.365  56.394 136.607  1.00 72.72           C  
ANISOU  738  CG  ASP A 104    10585   9763   7283     28    404   2599       C  
ATOM    739  OD1 ASP A 104      22.669  55.845 135.727  1.00 72.72           O  
ANISOU  739  OD1 ASP A 104    10543   9824   7263    -38    368   2663       O  
ATOM    740  OD2 ASP A 104      23.095  56.316 137.824  1.00 73.01           O  
ANISOU  740  OD2 ASP A 104    10615   9813   7310     67    433   2595       O  
ATOM    741  N   ARG A 105      23.965  60.147 137.043  1.00 75.52           N  
ANISOU  741  N   ARG A 105    10951  10001   7741    282    529   2554       N  
ATOM    742  CA  ARG A 105      23.266  61.203 137.793  1.00 76.99           C  
ANISOU  742  CA  ARG A 105    11100  10206   7946    387    583   2581       C  
ATOM    743  C   ARG A 105      22.609  62.239 136.872  1.00 78.49           C  
ANISOU  743  C   ARG A 105    11238  10417   8164    429    595   2653       C  
ATOM    744  O   ARG A 105      21.492  62.687 137.147  1.00 79.60           O  
ANISOU  744  O   ARG A 105    11311  10625   8308    487    624   2720       O  
ATOM    745  CB  ARG A 105      24.213  61.921 138.766  1.00 77.05           C  
ANISOU  745  CB  ARG A 105    11173  10122   7978    457    619   2489       C  
ATOM    746  CG  ARG A 105      24.514  61.172 140.056  1.00 76.91           C  
ANISOU  746  CG  ARG A 105    11189  10102   7931    452    625   2435       C  
ATOM    747  CD  ARG A 105      23.267  60.960 140.910  1.00 77.59           C  
ANISOU  747  CD  ARG A 105    11212  10282   7987    486    654   2495       C  
ATOM    748  NE  ARG A 105      22.785  59.581 140.877  1.00 77.55           N  
ANISOU  748  NE  ARG A 105    11180  10347   7939    398    616   2537       N  
ATOM    749  CZ  ARG A 105      21.724  59.134 141.548  1.00 78.24           C  
ANISOU  749  CZ  ARG A 105    11209  10524   7992    401    633   2596       C  
ATOM    750  NH1 ARG A 105      20.995  59.948 142.313  1.00 79.27           N  
ANISOU  750  NH1 ARG A 105    11298  10695   8126    495    689   2619       N  
ATOM    751  NH2 ARG A 105      21.386  57.850 141.451  1.00 78.30           N  
ANISOU  751  NH2 ARG A 105    11200  10584   7965    310    593   2632       N  
ATOM    752  N   TYR A 106      23.303  62.622 135.797  1.00 79.13           N  
ANISOU  752  N   TYR A 106    11350  10446   8267    402    574   2640       N  
ATOM    753  CA  TYR A 106      22.718  63.513 134.784  1.00 80.49           C  
ANISOU  753  CA  TYR A 106    11478  10641   8464    430    576   2715       C  
ATOM    754  C   TYR A 106      21.476  62.912 134.124  1.00 81.72           C  
ANISOU  754  C   TYR A 106    11550  10911   8589    383    547   2817       C  
ATOM    755  O   TYR A 106      20.402  63.525 134.143  1.00 82.26           O  
ANISOU  755  O   TYR A 106    11548  11038   8668    443    568   2893       O  
ATOM    756  CB  TYR A 106      23.753  63.864 133.713  1.00 80.51           C  
ANISOU  756  CB  TYR A 106    11532  10572   8486    393    554   2683       C  
ATOM    757  CG  TYR A 106      23.224  64.744 132.600  1.00 81.37           C  
ANISOU  757  CG  TYR A 106    11600  10700   8615    413    551   2764       C  
ATOM    758  CD1 TYR A 106      22.955  66.097 132.823  1.00 82.06           C  
ANISOU  758  CD1 TYR A 106    11677  10753   8749    514    592   2786       C  
ATOM    759  CD2 TYR A 106      22.993  64.227 131.322  1.00 81.45           C  
ANISOU  759  CD2 TYR A 106    11586  10764   8598    332    505   2818       C  
ATOM    760  CE1 TYR A 106      22.470  66.909 131.808  1.00 82.64           C  
ANISOU  760  CE1 TYR A 106    11715  10841   8843    536    586   2865       C  
ATOM    761  CE2 TYR A 106      22.512  65.033 130.299  1.00 82.13           C  
ANISOU  761  CE2 TYR A 106    11634  10870   8698    350    499   2896       C  
ATOM    762  CZ  TYR A 106      22.252  66.372 130.547  1.00 82.78           C  
ANISOU  762  CZ  TYR A 106    11706  10916   8830    453    539   2922       C  
ATOM    763  OH  TYR A 106      21.773  67.176 129.542  1.00 83.71           O  
ANISOU  763  OH  TYR A 106    11788  11052   8964    473    531   3004       O  
ATOM    764  N   LEU A 107      21.632  61.712 133.556  1.00 82.78           N  
ANISOU  764  N   LEU A 107    11692  11075   8685    277    496   2816       N  
ATOM    765  CA  LEU A 107      20.543  61.055 132.806  1.00 84.08           C  
ANISOU  765  CA  LEU A 107    11784  11345   8817    214    458   2908       C  
ATOM    766  C   LEU A 107      19.231  60.887 133.588  1.00 86.20           C  
ANISOU  766  C   LEU A 107    11970  11709   9073    247    478   2976       C  
ATOM    767  O   LEU A 107      18.150  61.053 133.017  1.00 86.95           O  
ANISOU  767  O   LEU A 107    11985  11889   9163    248    467   3070       O  
ATOM    768  CB  LEU A 107      20.997  59.694 132.269  1.00 83.19           C  
ANISOU  768  CB  LEU A 107    11705  11237   8663     95    402   2879       C  
ATOM    769  CG  LEU A 107      21.990  59.729 131.104  1.00 82.57           C  
ANISOU  769  CG  LEU A 107    11683  11103   8587     44    372   2840       C  
ATOM    770  CD1 LEU A 107      22.652  58.370 130.930  1.00 82.21           C  
ANISOU  770  CD1 LEU A 107    11688  11041   8506    -54    328   2782       C  
ATOM    771  CD2 LEU A 107      21.309  60.164 129.814  1.00 83.03           C  
ANISOU  771  CD2 LEU A 107    11688  11219   8638     26    349   2926       C  
ATOM    772  N   ARG A 108      19.329  60.566 134.881  1.00 87.85           N  
ANISOU  772  N   ARG A 108    12197  11907   9274    274    507   2932       N  
ATOM    773  CA  ARG A 108      18.141  60.381 135.735  1.00 89.80           C  
ANISOU  773  CA  ARG A 108    12367  12247   9504    306    533   2992       C  
ATOM    774  C   ARG A 108      17.262  61.625 135.765  1.00 91.58           C  
ANISOU  774  C   ARG A 108    12524  12510   9761    414    578   3055       C  
ATOM    775  O   ARG A 108      16.067  61.563 135.461  1.00 92.77           O  
ANISOU  775  O   ARG A 108    12582  12764   9902    411    572   3150       O  
ATOM    776  CB  ARG A 108      18.548  60.021 137.169  1.00 89.93           C  
ANISOU  776  CB  ARG A 108    12426  12233   9508    332    565   2924       C  
ATOM    777  CG  ARG A 108      19.109  58.623 137.320  1.00 89.63           C  
ANISOU  777  CG  ARG A 108    12437  12182   9435    228    521   2882       C  
ATOM    778  CD  ARG A 108      19.816  58.455 138.649  1.00 89.60           C  
ANISOU  778  CD  ARG A 108    12494  12122   9424    261    550   2801       C  
ATOM    779  NE  ARG A 108      18.889  58.505 139.781  1.00 90.36           N  
ANISOU  779  NE  ARG A 108    12536  12292   9503    314    594   2840       N  
ATOM    780  CZ  ARG A 108      18.112  57.493 140.183  1.00 91.35           C  
ANISOU  780  CZ  ARG A 108    12616  12501   9589    256    580   2892       C  
ATOM    781  NH1 ARG A 108      18.110  56.315 139.557  1.00 91.61           N  
ANISOU  781  NH1 ARG A 108    12655  12553   9600    141    519   2913       N  
ATOM    782  NH2 ARG A 108      17.315  57.659 141.234  1.00 91.96           N  
ANISOU  782  NH2 ARG A 108    12643  12646   9650    312    628   2925       N  
ATOM    783  N   VAL A 109      17.873  62.748 136.133  1.00 92.48           N  
ANISOU  783  N   VAL A 109    12684  12539   9914    507    620   3002       N  
ATOM    784  CA  VAL A 109      17.181  64.037 136.178  1.00 94.10           C  
ANISOU  784  CA  VAL A 109    12839  12758  10157    620    664   3049       C  
ATOM    785  C   VAL A 109      16.881  64.609 134.777  1.00 94.74           C  
ANISOU  785  C   VAL A 109    12885  12851  10260    613    635   3121       C  
ATOM    786  O   VAL A 109      15.874  65.301 134.599  1.00 95.69           O  
ANISOU  786  O   VAL A 109    12928  13029  10398    680    653   3200       O  
ATOM    787  CB  VAL A 109      17.935  65.065 137.069  1.00 94.49           C  
ANISOU  787  CB  VAL A 109    12954  12703  10242    722    718   2965       C  
ATOM    788  CG1 VAL A 109      19.272  65.504 136.463  1.00 93.84           C  
ANISOU  788  CG1 VAL A 109    12964  12502  10189    702    700   2895       C  
ATOM    789  CG2 VAL A 109      17.049  66.267 137.360  1.00 95.71           C  
ANISOU  789  CG2 VAL A 109    13052  12882  10431    848    769   3013       C  
ATOM    790  N   LYS A 110      17.738  64.320 133.794  1.00 94.63           N  
ANISOU  790  N   LYS A 110    12926  12786  10241    533    590   3094       N  
ATOM    791  CA  LYS A 110      17.555  64.851 132.435  1.00 95.30           C  
ANISOU  791  CA  LYS A 110    12987  12880  10340    519    560   3158       C  
ATOM    792  C   LYS A 110      16.438  64.144 131.658  1.00 96.02           C  
ANISOU  792  C   LYS A 110    12990  13095  10397    452    515   3259       C  
ATOM    793  O   LYS A 110      15.623  64.811 131.023  1.00 96.78           O  
ANISOU  793  O   LYS A 110    13020  13242  10508    491    511   3346       O  
ATOM    794  CB  LYS A 110      18.873  64.794 131.646  1.00 94.75           C  
ANISOU  794  CB  LYS A 110    13005  12720  10273    457    531   3094       C  
ATOM    795  CG  LYS A 110      18.834  65.406 130.248  1.00 94.88           C  
ANISOU  795  CG  LYS A 110    13011  12738  10302    443    503   3154       C  
ATOM    796  CD  LYS A 110      18.600  66.907 130.264  1.00 95.52           C  
ANISOU  796  CD  LYS A 110    13078  12777  10437    558    543   3188       C  
ATOM    797  CE  LYS A 110      18.512  67.450 128.846  1.00 96.20           C  
ANISOU  797  CE  LYS A 110    13150  12871  10530    537    510   3259       C  
ATOM    798  NZ  LYS A 110      18.288  68.921 128.817  1.00 97.05           N  
ANISOU  798  NZ  LYS A 110    13249  12930  10694    648    545   3297       N  
ATOM    799  N   ILE A 111      16.413  62.810 131.698  1.00 96.37           N  
ANISOU  799  N   ILE A 111    13035  13184  10394    349    477   3248       N  
ATOM    800  CA  ILE A 111      15.418  62.014 130.954  1.00 97.37           C  
ANISOU  800  CA  ILE A 111    13085  13426  10484    267    427   3337       C  
ATOM    801  C   ILE A 111      14.740  60.967 131.859  1.00 98.04           C  
ANISOU  801  C   ILE A 111    13127  13586  10537    228    427   3350       C  
ATOM    802  O   ILE A 111      14.882  59.755 131.644  1.00 98.22           O  
ANISOU  802  O   ILE A 111    13168  13629  10522    118    380   3336       O  
ATOM    803  CB  ILE A 111      16.028  61.369 129.677  1.00 96.99           C  
ANISOU  803  CB  ILE A 111    13081  13362  10407    155    363   3324       C  
ATOM    804  CG1 ILE A 111      17.314  60.583 129.982  1.00 96.35           C  
ANISOU  804  CG1 ILE A 111    13102  13193  10311     95    353   3212       C  
ATOM    805  CG2 ILE A 111      16.325  62.447 128.641  1.00 96.99           C  
ANISOU  805  CG2 ILE A 111    13093  13323  10433    191    360   3348       C  
ATOM    806  CD1 ILE A 111      17.716  59.616 128.882  1.00 96.25           C  
ANISOU  806  CD1 ILE A 111    13123  13188  10259    -25    289   3199       C  
ATOM    807  N   PRO A 112      13.982  61.437 132.873  1.00 99.23           N  
ANISOU  807  N   PRO A 112    13219  13780  10702    318    480   3380       N  
ATOM    808  CA  PRO A 112      13.370  60.522 133.850  1.00100.41           C  
ANISOU  808  CA  PRO A 112    13327  14000  10820    288    489   3393       C  
ATOM    809  C   PRO A 112      12.339  59.541 133.272  1.00102.04           C  
ANISOU  809  C   PRO A 112    13452  14327  10991    187    436   3483       C  
ATOM    810  O   PRO A 112      12.228  58.418 133.771  1.00102.16           O  
ANISOU  810  O   PRO A 112    13469  14373  10971    110    417   3474       O  
ATOM    811  CB  PRO A 112      12.716  61.471 134.866  1.00100.58           C  
ANISOU  811  CB  PRO A 112    13296  14050  10868    420    562   3414       C  
ATOM    812  CG  PRO A 112      12.485  62.732 134.119  1.00101.14           C  
ANISOU  812  CG  PRO A 112    13338  14108  10980    502    573   3457       C  
ATOM    813  CD  PRO A 112      13.604  62.840 133.128  1.00100.08           C  
ANISOU  813  CD  PRO A 112    13292  13877  10855    453    534   3407       C  
ATOM    814  N   LEU A 113      11.608  59.951 132.235  1.00103.88           N  
ANISOU  814  N   LEU A 113    13614  14624  11229    185    408   3568       N  
ATOM    815  CA  LEU A 113      10.600  59.084 131.606  1.00105.42           C  
ANISOU  815  CA  LEU A 113    13727  14936  11390     87    351   3657       C  
ATOM    816  C   LEU A 113      11.230  57.910 130.849  1.00105.72           C  
ANISOU  816  C   LEU A 113    13831  14945  11391    -53    280   3619       C  
ATOM    817  O   LEU A 113      10.757  56.777 130.964  1.00106.77           O  
ANISOU  817  O   LEU A 113    13938  15140  11490   -150    244   3644       O  
ATOM    818  CB  LEU A 113       9.699  59.892 130.668  1.00106.56           C  
ANISOU  818  CB  LEU A 113    13780  15156  11551    126    337   3758       C  
ATOM    819  CG  LEU A 113       8.838  60.971 131.341  1.00107.55           C  
ANISOU  819  CG  LEU A 113    13819  15330  11712    264    402   3814       C  
ATOM    820  CD1 LEU A 113       8.265  61.932 130.306  1.00108.43           C  
ANISOU  820  CD1 LEU A 113    13869  15480  11850    316    386   3897       C  
ATOM    821  CD2 LEU A 113       7.725  60.353 132.177  1.00108.05           C  
ANISOU  821  CD2 LEU A 113    13784  15513  11755    252    419   3873       C  
ATOM    822  N   ARG A 114      12.295  58.188 130.096  1.00105.17           N  
ANISOU  822  N   ARG A 114    13848  14781  11328    -64    263   3557       N  
ATOM    823  CA  ARG A 114      13.012  57.166 129.313  1.00104.67           C  
ANISOU  823  CA  ARG A 114    13856  14681  11230   -187    200   3509       C  
ATOM    824  C   ARG A 114      14.245  56.553 130.023  1.00103.32           C  
ANISOU  824  C   ARG A 114    13795  14404  11056   -209    211   3392       C  
ATOM    825  O   ARG A 114      14.904  55.661 129.460  1.00102.23           O  
ANISOU  825  O   ARG A 114    13721  14228  10892   -304    163   3343       O  
ATOM    826  CB  ARG A 114      13.422  57.752 127.952  1.00104.97           C  
ANISOU  826  CB  ARG A 114    13919  14693  11270   -196    170   3516       C  
ATOM    827  CG  ARG A 114      12.251  58.070 127.034  1.00105.70           C  
ANISOU  827  CG  ARG A 114    13911  14896  11353   -206    137   3632       C  
ATOM    828  CD  ARG A 114      12.649  58.980 125.880  1.00106.09           C  
ANISOU  828  CD  ARG A 114    13981  14913  11412   -180    125   3645       C  
ATOM    829  NE  ARG A 114      13.631  58.373 124.973  1.00105.59           N  
ANISOU  829  NE  ARG A 114    14006  14794  11316   -273     80   3581       N  
ATOM    830  CZ  ARG A 114      14.942  58.648 124.917  1.00105.28           C  
ANISOU  830  CZ  ARG A 114    14067  14644  11290   -256    101   3488       C  
ATOM    831  NH1 ARG A 114      15.522  59.544 125.723  1.00105.25           N  
ANISOU  831  NH1 ARG A 114    14096  14560  11333   -153    164   3442       N  
ATOM    832  NH2 ARG A 114      15.698  58.013 124.023  1.00104.92           N  
ANISOU  832  NH2 ARG A 114    14087  14567  11208   -346     57   3439       N  
ATOM    833  N   TYR A 115      14.545  57.003 131.249  1.00102.76           N  
ANISOU  833  N   TYR A 115    13744  14288  11011   -121    273   3348       N  
ATOM    834  CA  TYR A 115      15.735  56.536 131.980  1.00101.98           C  
ANISOU  834  CA  TYR A 115    13746  14088  10912   -130    285   3240       C  
ATOM    835  C   TYR A 115      15.844  55.013 132.064  1.00102.78           C  
ANISOU  835  C   TYR A 115    13878  14197  10975   -248    235   3218       C  
ATOM    836  O   TYR A 115      16.879  54.453 131.707  1.00102.24           O  
ANISOU  836  O   TYR A 115    13895  14052  10897   -303    205   3142       O  
ATOM    837  CB  TYR A 115      15.791  57.117 133.401  1.00101.35           C  
ANISOU  837  CB  TYR A 115    13669  13984  10855    -27    355   3209       C  
ATOM    838  CG  TYR A 115      16.950  56.584 134.228  1.00 99.95           C  
ANISOU  838  CG  TYR A 115    13589  13713  10674    -38    363   3104       C  
ATOM    839  CD1 TYR A 115      18.268  56.919 133.911  1.00 98.92           C  
ANISOU  839  CD1 TYR A 115    13549  13473  10563    -27    363   3016       C  
ATOM    840  CD2 TYR A 115      16.734  55.732 135.314  1.00 99.03           C  
ANISOU  840  CD2 TYR A 115    13471  13619  10534    -63    370   3096       C  
ATOM    841  CE1 TYR A 115      19.335  56.430 134.655  1.00 97.60           C  
ANISOU  841  CE1 TYR A 115    13465  13224  10394    -36    367   2921       C  
ATOM    842  CE2 TYR A 115      17.796  55.238 136.061  1.00 98.15           C  
ANISOU  842  CE2 TYR A 115    13449  13423  10419    -72    373   3004       C  
ATOM    843  CZ  TYR A 115      19.094  55.592 135.729  1.00 97.25           C  
ANISOU  843  CZ  TYR A 115    13421  13203  10326    -57    371   2916       C  
ATOM    844  OH  TYR A 115      20.153  55.111 136.464  1.00 96.12           O  
ANISOU  844  OH  TYR A 115    13360  12980  10181    -64    372   2826       O  
ATOM    845  N   LYS A 116      14.783  54.357 132.534  1.00104.98           N  
ANISOU  845  N   LYS A 116    14087  14568  11232   -287    226   3286       N  
ATOM    846  CA  LYS A 116      14.806  52.903 132.744  1.00105.75           C  
ANISOU  846  CA  LYS A 116    14212  14671  11297   -398    179   3272       C  
ATOM    847  C   LYS A 116      14.982  52.101 131.453  1.00105.58           C  
ANISOU  847  C   LYS A 116    14219  14646  11249   -513    103   3269       C  
ATOM    848  O   LYS A 116      15.668  51.078 131.456  1.00105.32           O  
ANISOU  848  O   LYS A 116    14261  14556  11199   -588     67   3208       O  
ATOM    849  CB  LYS A 116      13.558  52.423 133.502  1.00107.38           C  
ANISOU  849  CB  LYS A 116    14329  14984  11486   -419    186   3356       C  
ATOM    850  CG  LYS A 116      13.587  52.727 134.994  1.00108.52           C  
ANISOU  850  CG  LYS A 116    14473  15120  11640   -335    254   3335       C  
ATOM    851  CD  LYS A 116      12.695  51.777 135.791  1.00110.19           C  
ANISOU  851  CD  LYS A 116    14630  15413  11822   -394    248   3394       C  
ATOM    852  CE  LYS A 116      12.936  51.899 137.288  1.00110.78           C  
ANISOU  852  CE  LYS A 116    14726  15466  11896   -324    309   3357       C  
ATOM    853  NZ  LYS A 116      12.498  53.220 137.822  1.00111.75           N  
ANISOU  853  NZ  LYS A 116    14792  15626  12042   -189    384   3379       N  
ATOM    854  N   MET A 117      14.376  52.561 130.359  1.00105.93           N  
ANISOU  854  N   MET A 117    14206  14752  11290   -524     79   3334       N  
ATOM    855  CA  MET A 117      14.598  51.935 129.049  1.00105.68           C  
ANISOU  855  CA  MET A 117    14206  14717  11229   -625     10   3326       C  
ATOM    856  C   MET A 117      15.973  52.280 128.453  1.00101.96           C  
ANISOU  856  C   MET A 117    13833  14139  10766   -606     13   3232       C  
ATOM    857  O   MET A 117      16.542  51.460 127.728  1.00101.83           O  
ANISOU  857  O   MET A 117    13878  14087  10724   -692    -36   3183       O  
ATOM    858  CB  MET A 117      13.455  52.237 128.059  1.00109.05           C  
ANISOU  858  CB  MET A 117    14537  15254  11641   -652    -23   3431       C  
ATOM    859  CG  MET A 117      13.306  53.680 127.592  1.00111.63           C  
ANISOU  859  CG  MET A 117    14822  15596  11996   -551     12   3471       C  
ATOM    860  SD  MET A 117      12.115  53.863 126.238  1.00116.10           S  
ANISOU  860  SD  MET A 117    15289  16286  12537   -601    -44   3589       S  
ATOM    861  CE  MET A 117      10.563  53.561 127.088  1.00116.79           C  
ANISOU  861  CE  MET A 117    15248  16501  12624   -604    -37   3694       C  
ATOM    862  N   VAL A 118      16.505  53.470 128.754  1.00 98.33           N  
ANISOU  862  N   VAL A 118    13387  13628  10343   -497     71   3204       N  
ATOM    863  CA  VAL A 118      17.853  53.855 128.274  1.00 94.91           C  
ANISOU  863  CA  VAL A 118    13043  13094   9922   -477     79   3115       C  
ATOM    864  C   VAL A 118      18.974  53.138 129.045  1.00 91.09           C  
ANISOU  864  C   VAL A 118    12652  12516   9442   -491     85   3010       C  
ATOM    865  O   VAL A 118      19.718  52.353 128.461  1.00 89.50           O  
ANISOU  865  O   VAL A 118    12516  12270   9220   -562     46   2950       O  
ATOM    866  CB  VAL A 118      18.066  55.398 128.311  1.00 94.75           C  
ANISOU  866  CB  VAL A 118    13011  13046   9944   -361    135   3123       C  
ATOM    867  CG1 VAL A 118      19.520  55.777 128.031  1.00 93.40           C  
ANISOU  867  CG1 VAL A 118    12933  12766   9789   -340    150   3027       C  
ATOM    868  CG2 VAL A 118      17.146  56.095 127.311  1.00 95.41           C  
ANISOU  868  CG2 VAL A 118    13017  13209  10023   -352    120   3221       C  
ATOM    869  N   VAL A 119      19.095  53.425 130.341  1.00 88.47           N  
ANISOU  869  N   VAL A 119    12324  12156   9135   -419    135   2987       N  
ATOM    870  CA  VAL A 119      20.189  52.904 131.180  1.00 86.22           C  
ANISOU  870  CA  VAL A 119    12123  11780   8857   -416    145   2889       C  
ATOM    871  C   VAL A 119      19.834  51.528 131.759  1.00 85.55           C  
ANISOU  871  C   VAL A 119    12044  11717   8744   -495    110   2894       C  
ATOM    872  O   VAL A 119      19.203  51.434 132.814  1.00 84.78           O  
ANISOU  872  O   VAL A 119    11908  11658   8646   -470    135   2930       O  
ATOM    873  CB  VAL A 119      20.540  53.889 132.323  1.00 85.55           C  
ANISOU  873  CB  VAL A 119    12046  11651   8807   -302    213   2858       C  
ATOM    874  CG1 VAL A 119      21.683  53.347 133.180  1.00 84.90           C  
ANISOU  874  CG1 VAL A 119    12049  11480   8730   -301    218   2759       C  
ATOM    875  CG2 VAL A 119      20.889  55.262 131.758  1.00 85.32           C  
ANISOU  875  CG2 VAL A 119    12015  11591   8809   -228    245   2855       C  
ATOM    876  N   THR A 120      20.251  50.471 131.061  1.00 85.16           N  
ANISOU  876  N   THR A 120    12044  11642   8670   -590     53   2859       N  
ATOM    877  CA  THR A 120      19.956  49.090 131.456  1.00 84.40           C  
ANISOU  877  CA  THR A 120    11962  11556   8549   -677     10   2863       C  
ATOM    878  C   THR A 120      21.185  48.410 132.071  1.00 83.39           C  
ANISOU  878  C   THR A 120    11931  11325   8427   -681      5   2762       C  
ATOM    879  O   THR A 120      22.326  48.799 131.769  1.00 82.59           O  
ANISOU  879  O   THR A 120    11889  11147   8342   -646     18   2683       O  
ATOM    880  CB  THR A 120      19.480  48.254 130.251  1.00 84.68           C  
ANISOU  880  CB  THR A 120    11988  11634   8550   -788    -59   2895       C  
ATOM    881  OG1 THR A 120      20.486  48.248 129.230  1.00 84.31           O  
ANISOU  881  OG1 THR A 120    12009  11526   8499   -806    -79   2823       O  
ATOM    882  CG2 THR A 120      18.190  48.824 129.683  1.00 85.29           C  
ANISOU  882  CG2 THR A 120    11964  11823   8618   -790    -62   3003       C  
ATOM    883  N   PRO A 121      20.959  47.382 132.923  1.00 83.43           N  
ANISOU  883  N   PRO A 121    11949  11327   8420   -726    -13   2767       N  
ATOM    884  CA  PRO A 121      22.047  46.631 133.562  1.00 83.17           C  
ANISOU  884  CA  PRO A 121    12006  11201   8393   -733    -24   2680       C  
ATOM    885  C   PRO A 121      23.167  46.197 132.613  1.00 83.28           C  
ANISOU  885  C   PRO A 121    12098  11137   8407   -769    -59   2593       C  
ATOM    886  O   PRO A 121      24.345  46.388 132.931  1.00 83.20           O  
ANISOU  886  O   PRO A 121    12150  11045   8417   -720    -40   2509       O  
ATOM    887  CB  PRO A 121      21.329  45.407 134.135  1.00 83.34           C  
ANISOU  887  CB  PRO A 121    12019  11252   8392   -812    -61   2726       C  
ATOM    888  CG  PRO A 121      19.967  45.900 134.451  1.00 83.75           C  
ANISOU  888  CG  PRO A 121    11969  11413   8436   -798    -35   2831       C  
ATOM    889  CD  PRO A 121      19.639  46.928 133.408  1.00 84.04           C  
ANISOU  889  CD  PRO A 121    11954  11496   8479   -767    -22   2862       C  
ATOM    890  N   ARG A 122      22.794  45.627 131.466  1.00 84.05           N  
ANISOU  890  N   ARG A 122    12191  11263   8480   -852   -111   2614       N  
ATOM    891  CA  ARG A 122      23.772  45.187 130.458  1.00 84.10           C  
ANISOU  891  CA  ARG A 122    12268  11206   8478   -890   -144   2534       C  
ATOM    892  C   ARG A 122      24.607  46.350 129.909  1.00 82.50           C  
ANISOU  892  C   ARG A 122    12075  10975   8294   -818   -103   2489       C  
ATOM    893  O   ARG A 122      25.836  46.231 129.767  1.00 82.22           O  
ANISOU  893  O   ARG A 122    12107  10861   8270   -801   -101   2398       O  
ATOM    894  CB  ARG A 122      23.097  44.403 129.320  1.00 85.84           C  
ANISOU  894  CB  ARG A 122    12478  11473   8663   -995   -207   2569       C  
ATOM    895  CG  ARG A 122      22.059  45.149 128.488  1.00 87.58           C  
ANISOU  895  CG  ARG A 122    12615  11793   8867  -1004   -207   2656       C  
ATOM    896  CD  ARG A 122      21.443  44.232 127.445  1.00 89.28           C  
ANISOU  896  CD  ARG A 122    12829  12050   9043  -1116   -277   2684       C  
ATOM    897  NE  ARG A 122      20.272  44.834 126.803  1.00 90.66           N  
ANISOU  897  NE  ARG A 122    12912  12332   9201  -1131   -283   2783       N  
ATOM    898  CZ  ARG A 122      20.301  45.780 125.858  1.00 91.47           C  
ANISOU  898  CZ  ARG A 122    12988  12467   9297  -1101   -269   2798       C  
ATOM    899  NH1 ARG A 122      21.452  46.282 125.402  1.00 91.02           N  
ANISOU  899  NH1 ARG A 122    12988  12347   9248  -1055   -245   2721       N  
ATOM    900  NH2 ARG A 122      19.153  46.237 125.358  1.00 92.53           N  
ANISOU  900  NH2 ARG A 122    13036  12703   9416  -1116   -281   2896       N  
ATOM    901  N   ARG A 123      23.942  47.472 129.631  1.00 81.31           N  
ANISOU  901  N   ARG A 123    11856  10889   8149   -774    -71   2555       N  
ATOM    902  CA  ARG A 123      24.627  48.682 129.156  1.00 79.77           C  
ANISOU  902  CA  ARG A 123    11664  10669   7974   -705    -30   2526       C  
ATOM    903  C   ARG A 123      25.554  49.253 130.230  1.00 77.71           C  
ANISOU  903  C   ARG A 123    11438  10336   7751   -618     19   2463       C  
ATOM    904  O   ARG A 123      26.685  49.661 129.924  1.00 77.19           O  
ANISOU  904  O   ARG A 123    11419  10207   7702   -587     35   2391       O  
ATOM    905  CB  ARG A 123      23.622  49.739 128.684  1.00 80.70           C  
ANISOU  905  CB  ARG A 123    11700  10869   8092   -675    -10   2618       C  
ATOM    906  CG  ARG A 123      23.058  49.449 127.308  1.00 82.07           C  
ANISOU  906  CG  ARG A 123    11849  11103   8228   -751    -58   2662       C  
ATOM    907  CD  ARG A 123      21.846  50.314 126.986  1.00 83.23           C  
ANISOU  907  CD  ARG A 123    11904  11344   8374   -728    -47   2770       C  
ATOM    908  NE  ARG A 123      21.108  49.777 125.845  1.00 84.08           N  
ANISOU  908  NE  ARG A 123    11982  11522   8439   -817   -105   2822       N  
ATOM    909  CZ  ARG A 123      19.904  50.191 125.438  1.00 84.90           C  
ANISOU  909  CZ  ARG A 123    12000  11723   8532   -825   -116   2924       C  
ATOM    910  NH1 ARG A 123      19.260  51.172 126.071  1.00 85.05           N  
ANISOU  910  NH1 ARG A 123    11951  11780   8581   -742    -69   2988       N  
ATOM    911  NH2 ARG A 123      19.338  49.611 124.383  1.00 85.91           N  
ANISOU  911  NH2 ARG A 123    12111  11911   8618   -915   -175   2962       N  
ATOM    912  N   ALA A 124      25.074  49.263 131.477  1.00 75.94           N  
ANISOU  912  N   ALA A 124    11190  10125   7537   -582     42   2491       N  
ATOM    913  CA  ALA A 124      25.906  49.646 132.621  1.00 74.23           C  
ANISOU  913  CA  ALA A 124    11010   9842   7348   -508     82   2430       C  
ATOM    914  C   ALA A 124      27.132  48.734 132.756  1.00 72.82           C  
ANISOU  914  C   ALA A 124    10916   9579   7172   -536     55   2334       C  
ATOM    915  O   ALA A 124      28.246  49.212 133.001  1.00 72.25           O  
ANISOU  915  O   ALA A 124    10885   9439   7125   -484     80   2261       O  
ATOM    916  CB  ALA A 124      25.088  49.627 133.901  1.00 74.55           C  
ANISOU  916  CB  ALA A 124    11012   9923   7389   -478    105   2481       C  
ATOM    917  N   ALA A 125      26.921  47.430 132.579  1.00 71.75           N  
ANISOU  917  N   ALA A 125    10804   9446   7013   -618      2   2336       N  
ATOM    918  CA  ALA A 125      28.015  46.450 132.600  1.00 70.47           C  
ANISOU  918  CA  ALA A 125    10720   9202   6851   -648    -29   2248       C  
ATOM    919  C   ALA A 125      29.024  46.685 131.469  1.00 68.98           C  
ANISOU  919  C   ALA A 125    10568   8973   6667   -650    -33   2180       C  
ATOM    920  O   ALA A 125      30.246  46.674 131.703  1.00 68.36           O  
ANISOU  920  O   ALA A 125    10541   8821   6608   -617    -23   2095       O  
ATOM    921  CB  ALA A 125      27.462  45.033 132.536  1.00 71.08           C  
ANISOU  921  CB  ALA A 125    10813   9290   6902   -739    -88   2271       C  
ATOM    922  N   VAL A 126      28.511  46.908 130.255  1.00 68.21           N  
ANISOU  922  N   VAL A 126    10440   8926   6548   -689    -46   2219       N  
ATOM    923  CA  VAL A 126      29.369  47.244 129.102  1.00 67.44           C  
ANISOU  923  CA  VAL A 126    10369   8805   6448   -692    -43   2165       C  
ATOM    924  C   VAL A 126      30.182  48.510 129.408  1.00 66.47           C  
ANISOU  924  C   VAL A 126    10246   8647   6361   -605     12   2132       C  
ATOM    925  O   VAL A 126      31.416  48.529 129.236  1.00 65.72           O  
ANISOU  925  O   VAL A 126    10197   8491   6281   -587     21   2049       O  
ATOM    926  CB  VAL A 126      28.549  47.415 127.795  1.00 67.70           C  
ANISOU  926  CB  VAL A 126    10362   8913   6447   -744    -65   2227       C  
ATOM    927  CG1 VAL A 126      29.398  48.005 126.668  1.00 67.58           C  
ANISOU  927  CG1 VAL A 126    10367   8882   6427   -735    -50   2182       C  
ATOM    928  CG2 VAL A 126      27.952  46.079 127.353  1.00 68.03           C  
ANISOU  928  CG2 VAL A 126    10418   8977   6452   -840   -128   2241       C  
ATOM    929  N   ALA A 127      29.484  49.545 129.882  1.00 66.14           N  
ANISOU  929  N   ALA A 127    10150   8644   6335   -551     50   2196       N  
ATOM    930  CA  ALA A 127      30.128  50.792 130.307  1.00 65.59           C  
ANISOU  930  CA  ALA A 127    10079   8538   6303   -467    103   2170       C  
ATOM    931  C   ALA A 127      31.228  50.543 131.343  1.00 65.11           C  
ANISOU  931  C   ALA A 127    10071   8400   6268   -430    114   2085       C  
ATOM    932  O   ALA A 127      32.341  51.057 131.190  1.00 65.16           O  
ANISOU  932  O   ALA A 127    10107   8353   6297   -398    134   2021       O  
ATOM    933  CB  ALA A 127      29.102  51.776 130.851  1.00 65.71           C  
ANISOU  933  CB  ALA A 127    10031   8603   6331   -413    138   2250       C  
ATOM    934  N   ILE A 128      30.923  49.742 132.370  1.00 64.53           N  
ANISOU  934  N   ILE A 128    10007   8322   6188   -438     98   2089       N  
ATOM    935  CA  ILE A 128      31.927  49.372 133.378  1.00 63.76           C  
ANISOU  935  CA  ILE A 128     9961   8154   6109   -408     99   2013       C  
ATOM    936  C   ILE A 128      33.123  48.718 132.685  1.00 62.65           C  
ANISOU  936  C   ILE A 128     9876   7957   5971   -439     73   1928       C  
ATOM    937  O   ILE A 128      34.240  49.235 132.765  1.00 61.51           O  
ANISOU  937  O   ILE A 128     9756   7761   5852   -398     95   1862       O  
ATOM    938  CB  ILE A 128      31.347  48.443 134.483  1.00 64.68           C  
ANISOU  938  CB  ILE A 128    10083   8281   6212   -425     78   2038       C  
ATOM    939  CG1 ILE A 128      30.393  49.228 135.392  1.00 65.22           C  
ANISOU  939  CG1 ILE A 128    10099   8398   6282   -374    117   2105       C  
ATOM    940  CG2 ILE A 128      32.453  47.820 135.342  1.00 64.39           C  
ANISOU  940  CG2 ILE A 128    10106   8169   6188   -408     66   1958       C  
ATOM    941  CD1 ILE A 128      29.396  48.367 136.144  1.00 65.72           C  
ANISOU  941  CD1 ILE A 128    10143   8506   6319   -409     98   2164       C  
ATOM    942  N   ALA A 129      32.873  47.614 131.978  1.00 62.62           N  
ANISOU  942  N   ALA A 129     9888   7965   5939   -512     27   1931       N  
ATOM    943  CA  ALA A 129      33.942  46.887 131.268  1.00 62.31           C  
ANISOU  943  CA  ALA A 129     9902   7876   5897   -542      0   1849       C  
ATOM    944  C   ALA A 129      34.826  47.817 130.421  1.00 62.03           C  
ANISOU  944  C   ALA A 129     9866   7827   5875   -514     32   1807       C  
ATOM    945  O   ALA A 129      36.068  47.716 130.453  1.00 62.05           O  
ANISOU  945  O   ALA A 129     9906   7773   5897   -492     38   1725       O  
ATOM    946  CB  ALA A 129      33.348  45.790 130.400  1.00 62.67           C  
ANISOU  946  CB  ALA A 129     9958   7947   5905   -626    -49   1869       C  
ATOM    947  N   GLY A 130      34.175  48.730 129.691  1.00 61.55           N  
ANISOU  947  N   GLY A 130     9759   7820   5804   -514     54   1868       N  
ATOM    948  CA  GLY A 130      34.873  49.769 128.930  1.00 60.81           C  
ANISOU  948  CA  GLY A 130     9658   7720   5724   -488     88   1846       C  
ATOM    949  C   GLY A 130      35.857  50.579 129.759  1.00 60.12           C  
ANISOU  949  C   GLY A 130     9583   7577   5681   -418    127   1795       C  
ATOM    950  O   GLY A 130      37.013  50.791 129.338  1.00 59.94           O  
ANISOU  950  O   GLY A 130     9583   7517   5673   -409    140   1729       O  
ATOM    951  N   CYS A 131      35.409  51.013 130.941  1.00 59.76           N  
ANISOU  951  N   CYS A 131     9521   7528   5655   -371    145   1824       N  
ATOM    952  CA  CYS A 131      36.266  51.777 131.858  1.00 59.07           C  
ANISOU  952  CA  CYS A 131     9447   7389   5608   -305    178   1775       C  
ATOM    953  C   CYS A 131      37.537  51.011 132.168  1.00 57.51           C  
ANISOU  953  C   CYS A 131     9298   7129   5421   -307    160   1682       C  
ATOM    954  O   CYS A 131      38.628  51.546 132.026  1.00 56.95           O  
ANISOU  954  O   CYS A 131     9240   7020   5376   -283    180   1624       O  
ATOM    955  CB  CYS A 131      35.555  52.117 133.168  1.00 59.82           C  
ANISOU  955  CB  CYS A 131     9525   7492   5713   -259    195   1813       C  
ATOM    956  SG  CYS A 131      34.054  53.097 132.953  1.00 61.60           S  
ANISOU  956  SG  CYS A 131     9685   7788   5930   -240    222   1923       S  
ATOM    957  N   TRP A 132      37.382  49.751 132.561  1.00 56.32           N  
ANISOU  957  N   TRP A 132     9173   6972   5253   -338    121   1670       N  
ATOM    958  CA  TRP A 132      38.530  48.897 132.858  1.00 55.45           C  
ANISOU  958  CA  TRP A 132     9110   6803   5154   -338     97   1585       C  
ATOM    959  C   TRP A 132      39.407  48.640 131.633  1.00 55.12           C  
ANISOU  959  C   TRP A 132     9085   6749   5109   -367     91   1529       C  
ATOM    960  O   TRP A 132      40.631  48.717 131.733  1.00 54.90           O  
ANISOU  960  O   TRP A 132     9077   6676   5106   -341     99   1456       O  
ATOM    961  CB  TRP A 132      38.088  47.579 133.500  1.00 55.09           C  
ANISOU  961  CB  TRP A 132     9090   6750   5090   -368     53   1593       C  
ATOM    962  CG  TRP A 132      37.705  47.740 134.938  1.00 54.52           C  
ANISOU  962  CG  TRP A 132     9013   6674   5026   -329     61   1619       C  
ATOM    963  CD1 TRP A 132      36.442  47.805 135.445  1.00 54.63           C  
ANISOU  963  CD1 TRP A 132     8997   6737   5021   -335     65   1699       C  
ATOM    964  CD2 TRP A 132      38.594  47.873 136.049  1.00 53.93           C  
ANISOU  964  CD2 TRP A 132     8963   6550   4976   -278     68   1565       C  
ATOM    965  NE1 TRP A 132      36.489  47.963 136.810  1.00 54.44           N  
ANISOU  965  NE1 TRP A 132     8980   6697   5006   -289     76   1696       N  
ATOM    966  CE2 TRP A 132      37.799  48.007 137.206  1.00 54.00           C  
ANISOU  966  CE2 TRP A 132     8960   6581   4976   -255     76   1614       C  
ATOM    967  CE3 TRP A 132      39.987  47.886 136.181  1.00 53.67           C  
ANISOU  967  CE3 TRP A 132     8959   6461   4972   -250     67   1479       C  
ATOM    968  CZ2 TRP A 132      38.349  48.151 138.483  1.00 53.76           C  
ANISOU  968  CZ2 TRP A 132     8949   6517   4959   -206     82   1580       C  
ATOM    969  CZ3 TRP A 132      40.536  48.032 137.459  1.00 53.54           C  
ANISOU  969  CZ3 TRP A 132     8959   6410   4972   -202     69   1447       C  
ATOM    970  CH2 TRP A 132      39.714  48.164 138.589  1.00 53.45           C  
ANISOU  970  CH2 TRP A 132     8940   6420   4947   -181     76   1496       C  
ATOM    971  N   ILE A 133      38.795  48.363 130.483  1.00 55.10           N  
ANISOU  971  N   ILE A 133     9071   6789   5072   -419     78   1564       N  
ATOM    972  CA  ILE A 133      39.575  48.152 129.248  1.00 54.91           C  
ANISOU  972  CA  ILE A 133     9063   6763   5036   -447     76   1513       C  
ATOM    973  C   ILE A 133      40.431  49.391 128.953  1.00 54.28           C  
ANISOU  973  C   ILE A 133     8965   6674   4983   -409    122   1488       C  
ATOM    974  O   ILE A 133      41.668  49.294 128.826  1.00 53.86           O  
ANISOU  974  O   ILE A 133     8932   6584   4948   -395    130   1411       O  
ATOM    975  CB  ILE A 133      38.670  47.805 128.040  1.00 55.30           C  
ANISOU  975  CB  ILE A 133     9100   6870   5038   -511     55   1562       C  
ATOM    976  CG1 ILE A 133      38.001  46.437 128.245  1.00 55.65           C  
ANISOU  976  CG1 ILE A 133     9171   6914   5058   -558      3   1572       C  
ATOM    977  CG2 ILE A 133      39.464  47.786 126.733  1.00 55.31           C  
ANISOU  977  CG2 ILE A 133     9114   6877   5021   -534     62   1512       C  
ATOM    978  CD1 ILE A 133      36.680  46.297 127.521  1.00 56.18           C  
ANISOU  978  CD1 ILE A 133     9211   7048   5085   -616    -17   1652       C  
ATOM    979  N   LEU A 134      39.770  50.549 128.891  1.00 53.99           N  
ANISOU  979  N   LEU A 134     8891   6670   4952   -392    153   1555       N  
ATOM    980  CA  LEU A 134      40.462  51.819 128.628  1.00 53.74           C  
ANISOU  980  CA  LEU A 134     8841   6626   4948   -359    196   1545       C  
ATOM    981  C   LEU A 134      41.516  52.132 129.705  1.00 53.45           C  
ANISOU  981  C   LEU A 134     8821   6530   4958   -308    211   1480       C  
ATOM    982  O   LEU A 134      42.591  52.656 129.393  1.00 52.98           O  
ANISOU  982  O   LEU A 134     8763   6446   4920   -296    234   1432       O  
ATOM    983  CB  LEU A 134      39.450  52.965 128.500  1.00 53.88           C  
ANISOU  983  CB  LEU A 134     8819   6682   4968   -344    221   1634       C  
ATOM    984  CG  LEU A 134      39.937  54.335 127.978  1.00 53.93           C  
ANISOU  984  CG  LEU A 134     8809   6684   4999   -322    263   1643       C  
ATOM    985  CD1 LEU A 134      40.525  54.238 126.571  1.00 54.06           C  
ANISOU  985  CD1 LEU A 134     8828   6721   4989   -366    266   1623       C  
ATOM    986  CD2 LEU A 134      38.798  55.344 128.016  1.00 54.00           C  
ANISOU  986  CD2 LEU A 134     8781   6724   5012   -300    282   1736       C  
ATOM    987  N   SER A 135      41.206  51.785 130.960  1.00 53.55           N  
ANISOU  987  N   SER A 135     8843   6521   4980   -281    197   1482       N  
ATOM    988  CA  SER A 135      42.141  51.928 132.090  1.00 53.21           C  
ANISOU  988  CA  SER A 135     8819   6424   4974   -235    202   1421       C  
ATOM    989  C   SER A 135      43.389  51.081 131.926  1.00 53.16           C  
ANISOU  989  C   SER A 135     8841   6382   4975   -243    182   1334       C  
ATOM    990  O   SER A 135      44.500  51.563 132.158  1.00 53.00           O  
ANISOU  990  O   SER A 135     8823   6327   4988   -216    199   1278       O  
ATOM    991  CB  SER A 135      41.478  51.541 133.404  1.00 53.16           C  
ANISOU  991  CB  SER A 135     8821   6412   4965   -212    186   1444       C  
ATOM    992  OG  SER A 135      40.287  52.267 133.590  1.00 53.60           O  
ANISOU  992  OG  SER A 135     8846   6505   5012   -199    206   1523       O  
ATOM    993  N   PHE A 136      43.200  49.816 131.553  1.00 53.34           N  
ANISOU  993  N   PHE A 136     8886   6411   4969   -281    146   1323       N  
ATOM    994  CA  PHE A 136      44.324  48.945 131.201  1.00 53.36           C  
ANISOU  994  CA  PHE A 136     8915   6383   4976   -289    127   1241       C  
ATOM    995  C   PHE A 136      45.092  49.500 129.995  1.00 53.47           C  
ANISOU  995  C   PHE A 136     8913   6411   4990   -301    157   1211       C  
ATOM    996  O   PHE A 136      46.327  49.500 130.006  1.00 53.19           O  
ANISOU  996  O   PHE A 136     8881   6347   4980   -281    165   1141       O  
ATOM    997  CB  PHE A 136      43.873  47.494 130.953  1.00 53.45           C  
ANISOU  997  CB  PHE A 136     8957   6394   4955   -329     81   1239       C  
ATOM    998  CG  PHE A 136      43.840  46.648 132.200  1.00 53.27           C  
ANISOU  998  CG  PHE A 136     8963   6332   4943   -311     46   1226       C  
ATOM    999  CD1 PHE A 136      45.019  46.178 132.766  1.00 53.17           C  
ANISOU  999  CD1 PHE A 136     8974   6267   4958   -278     32   1151       C  
ATOM   1000  CD2 PHE A 136      42.633  46.310 132.807  1.00 53.38           C  
ANISOU 1000  CD2 PHE A 136     8978   6364   4937   -328     26   1294       C  
ATOM   1001  CE1 PHE A 136      44.994  45.395 133.912  1.00 53.15           C  
ANISOU 1001  CE1 PHE A 136     9000   6229   4963   -262     -2   1144       C  
ATOM   1002  CE2 PHE A 136      42.603  45.523 133.953  1.00 53.20           C  
ANISOU 1002  CE2 PHE A 136     8983   6308   4921   -315     -5   1289       C  
ATOM   1003  CZ  PHE A 136      43.785  45.066 134.506  1.00 53.09           C  
ANISOU 1003  CZ  PHE A 136     8998   6239   4934   -282    -21   1214       C  
ATOM   1004  N   VAL A 137      44.376  50.000 128.981  1.00 53.59           N  
ANISOU 1004  N   VAL A 137     8907   6475   4978   -334    173   1268       N  
ATOM   1005  CA  VAL A 137      45.043  50.625 127.824  1.00 53.94           C  
ANISOU 1005  CA  VAL A 137     8935   6541   5018   -348    205   1250       C  
ATOM   1006  C   VAL A 137      45.934  51.797 128.256  1.00 53.65           C  
ANISOU 1006  C   VAL A 137     8878   6476   5027   -309    242   1228       C  
ATOM   1007  O   VAL A 137      47.123  51.835 127.909  1.00 54.05           O  
ANISOU 1007  O   VAL A 137     8928   6513   5094   -305    257   1165       O  
ATOM   1008  CB  VAL A 137      44.037  51.071 126.724  1.00 54.53           C  
ANISOU 1008  CB  VAL A 137     8988   6675   5053   -388    214   1326       C  
ATOM   1009  CG1 VAL A 137      44.689  51.993 125.692  1.00 54.56           C  
ANISOU 1009  CG1 VAL A 137     8971   6700   5057   -397    254   1323       C  
ATOM   1010  CG2 VAL A 137      43.440  49.856 126.025  1.00 55.00           C  
ANISOU 1010  CG2 VAL A 137     9069   6763   5063   -437    176   1329       C  
ATOM   1011  N   VAL A 138      45.366  52.732 129.019  1.00 53.12           N  
ANISOU 1011  N   VAL A 138     8797   6401   4983   -280    257   1278       N  
ATOM   1012  CA  VAL A 138      46.108  53.925 129.452  1.00 52.83           C  
ANISOU 1012  CA  VAL A 138     8746   6334   4991   -246    290   1261       C  
ATOM   1013  C   VAL A 138      47.243  53.554 130.416  1.00 52.76           C  
ANISOU 1013  C   VAL A 138     8753   6276   5016   -215    278   1180       C  
ATOM   1014  O   VAL A 138      48.368  54.020 130.269  1.00 52.48           O  
ANISOU 1014  O   VAL A 138     8707   6222   5009   -208    297   1132       O  
ATOM   1015  CB  VAL A 138      45.168  54.969 130.103  1.00 52.59           C  
ANISOU 1015  CB  VAL A 138     8702   6302   4975   -218    307   1330       C  
ATOM   1016  CG1 VAL A 138      45.956  56.119 130.723  1.00 52.55           C  
ANISOU 1016  CG1 VAL A 138     8691   6253   5019   -181    334   1303       C  
ATOM   1017  CG2 VAL A 138      44.170  55.512 129.078  1.00 52.72           C  
ANISOU 1017  CG2 VAL A 138     8697   6368   4965   -244    321   1412       C  
ATOM   1018  N   GLY A 139      46.936  52.709 131.390  1.00 52.99           N  
ANISOU 1018  N   GLY A 139     8803   6286   5041   -198    245   1170       N  
ATOM   1019  CA  GLY A 139      47.904  52.290 132.396  1.00 53.18           C  
ANISOU 1019  CA  GLY A 139     8844   6266   5094   -166    226   1100       C  
ATOM   1020  C   GLY A 139      49.038  51.400 131.917  1.00 53.68           C  
ANISOU 1020  C   GLY A 139     8916   6318   5160   -175    211   1025       C  
ATOM   1021  O   GLY A 139      50.159  51.513 132.435  1.00 53.67           O  
ANISOU 1021  O   GLY A 139     8911   6286   5193   -149    211    964       O  
ATOM   1022  N   LEU A 140      48.761  50.510 130.956  1.00 54.27           N  
ANISOU 1022  N   LEU A 140     9000   6418   5199   -210    198   1025       N  
ATOM   1023  CA  LEU A 140      49.806  49.632 130.391  1.00 54.46           C  
ANISOU 1023  CA  LEU A 140     9034   6434   5223   -215    187    950       C  
ATOM   1024  C   LEU A 140      50.628  50.266 129.265  1.00 54.96           C  
ANISOU 1024  C   LEU A 140     9069   6523   5289   -231    226    924       C  
ATOM   1025  O   LEU A 140      51.626  49.676 128.857  1.00 54.85           O  
ANISOU 1025  O   LEU A 140     9055   6505   5280   -227    225    856       O  
ATOM   1026  CB  LEU A 140      49.218  48.303 129.899  1.00 54.49           C  
ANISOU 1026  CB  LEU A 140     9069   6446   5188   -245    152    950       C  
ATOM   1027  CG  LEU A 140      48.610  47.371 130.943  1.00 54.37           C  
ANISOU 1027  CG  LEU A 140     9087   6401   5170   -235    106    964       C  
ATOM   1028  CD1 LEU A 140      47.958  46.180 130.258  1.00 54.45           C  
ANISOU 1028  CD1 LEU A 140     9127   6421   5139   -277     74    971       C  
ATOM   1029  CD2 LEU A 140      49.665  46.907 131.934  1.00 54.40           C  
ANISOU 1029  CD2 LEU A 140     9104   6354   5210   -192     85    897       C  
ATOM   1030  N   THR A 141      50.241  51.449 128.775  1.00 55.60           N  
ANISOU 1030  N   THR A 141     9125   6631   5368   -246    262    979       N  
ATOM   1031  CA  THR A 141      51.016  52.137 127.723  1.00 56.21           C  
ANISOU 1031  CA  THR A 141     9174   6734   5447   -265    302    963       C  
ATOM   1032  C   THR A 141      52.544  52.153 128.004  1.00 56.62           C  
ANISOU 1032  C   THR A 141     9210   6762   5539   -241    312    882       C  
ATOM   1033  O   THR A 141      53.322  51.728 127.136  1.00 56.79           O  
ANISOU 1033  O   THR A 141     9222   6806   5547   -254    324    834       O  
ATOM   1034  CB  THR A 141      50.448  53.551 127.422  1.00 56.14           C  
ANISOU 1034  CB  THR A 141     9143   6743   5443   -277    337   1038       C  
ATOM   1035  OG1 THR A 141      49.140  53.428 126.850  1.00 55.88           O  
ANISOU 1035  OG1 THR A 141     9117   6747   5366   -304    329   1109       O  
ATOM   1036  CG2 THR A 141      51.342  54.323 126.453  1.00 56.26           C  
ANISOU 1036  CG2 THR A 141     9129   6780   5464   -298    378   1024       C  
ATOM   1037  N   PRO A 142      52.969  52.582 129.217  1.00 56.81           N  
ANISOU 1037  N   PRO A 142     9231   6744   5608   -205    304    864       N  
ATOM   1038  CA  PRO A 142      54.388  52.482 129.594  1.00 57.54           C  
ANISOU 1038  CA  PRO A 142     9307   6816   5740   -181    304    787       C  
ATOM   1039  C   PRO A 142      55.032  51.102 129.375  1.00 58.73           C  
ANISOU 1039  C   PRO A 142     9468   6964   5879   -171    279    718       C  
ATOM   1040  O   PRO A 142      56.193  51.037 128.953  1.00 58.73           O  
ANISOU 1040  O   PRO A 142     9443   6975   5897   -166    295    660       O  
ATOM   1041  CB  PRO A 142      54.379  52.829 131.086  1.00 57.07           C  
ANISOU 1041  CB  PRO A 142     9256   6710   5716   -145    282    785       C  
ATOM   1042  CG  PRO A 142      53.225  53.741 131.241  1.00 56.66           C  
ANISOU 1042  CG  PRO A 142     9210   6661   5655   -153    296    863       C  
ATOM   1043  CD  PRO A 142      52.193  53.306 130.240  1.00 56.44           C  
ANISOU 1043  CD  PRO A 142     9192   6673   5578   -186    299    914       C  
ATOM   1044  N   MET A 143      54.288  50.026 129.652  1.00 60.04           N  
ANISOU 1044  N   MET A 143     9673   7118   6020   -167    240    725       N  
ATOM   1045  CA  MET A 143      54.756  48.660 129.371  1.00 61.26           C  
ANISOU 1045  CA  MET A 143     9847   7264   6162   -157    213    664       C  
ATOM   1046  C   MET A 143      54.966  48.402 127.873  1.00 61.85           C  
ANISOU 1046  C   MET A 143     9913   7384   6201   -189    240    645       C  
ATOM   1047  O   MET A 143      55.827  47.595 127.517  1.00 62.80           O  
ANISOU 1047  O   MET A 143    10034   7502   6323   -173    236    575       O  
ATOM   1048  CB  MET A 143      53.791  47.605 129.924  1.00 62.24           C  
ANISOU 1048  CB  MET A 143    10018   7363   6265   -156    166    687       C  
ATOM   1049  CG  MET A 143      53.730  47.528 131.440  1.00 62.86           C  
ANISOU 1049  CG  MET A 143    10111   7398   6373   -120    133    692       C  
ATOM   1050  SD  MET A 143      54.977  46.443 132.160  1.00 64.56           S  
ANISOU 1050  SD  MET A 143    10338   7567   6622    -72     93    605       S  
ATOM   1051  CE  MET A 143      54.417  44.842 131.591  1.00 64.92           C  
ANISOU 1051  CE  MET A 143    10434   7600   6631    -89     55    594       C  
ATOM   1052  N   PHE A 144      54.192  49.065 127.004  1.00 61.74           N  
ANISOU 1052  N   PHE A 144     9891   7411   6152   -229    268    705       N  
ATOM   1053  CA  PHE A 144      54.355  48.879 125.553  1.00 61.88           C  
ANISOU 1053  CA  PHE A 144     9903   7480   6128   -263    295    691       C  
ATOM   1054  C   PHE A 144      55.629  49.528 124.994  1.00 61.15           C  
ANISOU 1054  C   PHE A 144     9765   7412   6054   -260    341    649       C  
ATOM   1055  O   PHE A 144      56.091  49.120 123.927  1.00 61.58           O  
ANISOU 1055  O   PHE A 144     9814   7505   6077   -274    361    611       O  
ATOM   1056  CB  PHE A 144      53.140  49.394 124.756  1.00 62.72           C  
ANISOU 1056  CB  PHE A 144    10013   7627   6188   -309    307    774       C  
ATOM   1057  CG  PHE A 144      51.809  48.793 125.163  1.00 63.28           C  
ANISOU 1057  CG  PHE A 144    10121   7686   6236   -321    265    823       C  
ATOM   1058  CD1 PHE A 144      51.700  47.469 125.623  1.00 63.37           C  
ANISOU 1058  CD1 PHE A 144    10171   7663   6244   -308    219    785       C  
ATOM   1059  CD2 PHE A 144      50.638  49.560 125.048  1.00 63.16           C  
ANISOU 1059  CD2 PHE A 144    10098   7695   6203   -346    272    913       C  
ATOM   1060  CE1 PHE A 144      50.460  46.946 125.977  1.00 63.41           C  
ANISOU 1060  CE1 PHE A 144    10205   7660   6227   -327    182    836       C  
ATOM   1061  CE2 PHE A 144      49.400  49.034 125.398  1.00 62.94           C  
ANISOU 1061  CE2 PHE A 144    10095   7664   6153   -359    235    963       C  
ATOM   1062  CZ  PHE A 144      49.310  47.725 125.853  1.00 63.20           C  
ANISOU 1062  CZ  PHE A 144    10165   7664   6181   -353    191    925       C  
ATOM   1063  N   GLY A 145      56.191  50.518 125.694  1.00 59.75           N  
ANISOU 1063  N   GLY A 145     9557   7217   5926   -243    357    654       N  
ATOM   1064  CA  GLY A 145      57.399  51.206 125.217  1.00 59.22           C  
ANISOU 1064  CA  GLY A 145     9442   7176   5882   -247    400    620       C  
ATOM   1065  C   GLY A 145      57.650  52.627 125.696  1.00 58.15           C  
ANISOU 1065  C   GLY A 145     9275   7028   5788   -252    424    657       C  
ATOM   1066  O   GLY A 145      58.809  53.040 125.785  1.00 57.86           O  
ANISOU 1066  O   GLY A 145     9200   6994   5789   -245    444    616       O  
ATOM   1067  N   TRP A 146      56.588  53.379 125.987  1.00 57.09           N  
ANISOU 1067  N   TRP A 146     9157   6881   5652   -265    421    733       N  
ATOM   1068  CA  TRP A 146      56.718  54.794 126.369  1.00 56.86           C  
ANISOU 1068  CA  TRP A 146     9106   6836   5663   -271    444    772       C  
ATOM   1069  C   TRP A 146      57.316  54.947 127.783  1.00 57.28           C  
ANISOU 1069  C   TRP A 146     9156   6835   5771   -232    420    732       C  
ATOM   1070  O   TRP A 146      56.595  55.087 128.778  1.00 56.88           O  
ANISOU 1070  O   TRP A 146     9131   6748   5731   -210    394    760       O  
ATOM   1071  CB  TRP A 146      55.363  55.519 126.248  1.00 55.96           C  
ANISOU 1071  CB  TRP A 146     9010   6723   5528   -288    449    863       C  
ATOM   1072  CG  TRP A 146      55.450  57.021 126.086  1.00 55.45           C  
ANISOU 1072  CG  TRP A 146     8923   6652   5491   -307    484    912       C  
ATOM   1073  CD1 TRP A 146      56.564  57.807 126.210  1.00 55.47           C  
ANISOU 1073  CD1 TRP A 146     8894   6641   5538   -312    507    884       C  
ATOM   1074  CD2 TRP A 146      54.368  57.912 125.791  1.00 54.95           C  
ANISOU 1074  CD2 TRP A 146     8869   6593   5416   -323    496   1000       C  
ATOM   1075  NE1 TRP A 146      56.239  59.124 126.002  1.00 55.42           N  
ANISOU 1075  NE1 TRP A 146     8882   6625   5548   -333    532    949       N  
ATOM   1076  CE2 TRP A 146      54.899  59.218 125.746  1.00 55.08           C  
ANISOU 1076  CE2 TRP A 146     8862   6591   5471   -336    527   1020       C  
ATOM   1077  CE3 TRP A 146      53.000  57.734 125.559  1.00 54.73           C  
ANISOU 1077  CE3 TRP A 146     8862   6583   5349   -327    483   1065       C  
ATOM   1078  CZ2 TRP A 146      54.110  60.341 125.470  1.00 55.05           C  
ANISOU 1078  CZ2 TRP A 146     8863   6581   5471   -349    545   1103       C  
ATOM   1079  CZ3 TRP A 146      52.211  58.857 125.295  1.00 54.69           C  
ANISOU 1079  CZ3 TRP A 146     8855   6578   5347   -338    502   1148       C  
ATOM   1080  CH2 TRP A 146      52.773  60.138 125.249  1.00 54.86           C  
ANISOU 1080  CH2 TRP A 146     8858   6575   5409   -346    532   1165       C  
ATOM   1081  N   ASN A 147      58.646  54.926 127.845  1.00 58.24           N  
ANISOU 1081  N   ASN A 147     9243   6958   5925   -224    429    668       N  
ATOM   1082  CA  ASN A 147      59.387  54.980 129.113  1.00 58.78           C  
ANISOU 1082  CA  ASN A 147     9305   6984   6045   -189    402    622       C  
ATOM   1083  C   ASN A 147      60.820  55.505 128.896  1.00 60.30           C  
ANISOU 1083  C   ASN A 147     9443   7191   6276   -199    427    575       C  
ATOM   1084  O   ASN A 147      61.165  55.906 127.783  1.00 61.17           O  
ANISOU 1084  O   ASN A 147     9523   7343   6372   -235    469    586       O  
ATOM   1085  CB  ASN A 147      59.369  53.592 129.780  1.00 58.24           C  
ANISOU 1085  CB  ASN A 147     9264   6896   5969   -148    355    576       C  
ATOM   1086  CG  ASN A 147      59.790  52.475 128.841  1.00 58.09           C  
ANISOU 1086  CG  ASN A 147     9239   6911   5920   -148    359    530       C  
ATOM   1087  OD1 ASN A 147      60.934  52.424 128.387  1.00 58.34           O  
ANISOU 1087  OD1 ASN A 147     9230   6967   5967   -147    379    478       O  
ATOM   1088  ND2 ASN A 147      58.870  51.559 128.566  1.00 57.71           N  
ANISOU 1088  ND2 ASN A 147     9232   6865   5828   -149    338    547       N  
ATOM   1089  N   ASN A 148      61.639  55.516 129.952  1.00 61.61           N  
ANISOU 1089  N   ASN A 148     9595   7326   6487   -170    401    527       N  
ATOM   1090  CA  ASN A 148      63.029  55.998 129.883  1.00 63.19           C  
ANISOU 1090  CA  ASN A 148     9738   7540   6729   -180    419    482       C  
ATOM   1091  C   ASN A 148      64.083  54.899 129.652  1.00 64.17           C  
ANISOU 1091  C   ASN A 148     9830   7692   6856   -154    411    406       C  
ATOM   1092  O   ASN A 148      65.273  55.124 129.922  1.00 65.23           O  
ANISOU 1092  O   ASN A 148     9916   7834   7033   -150    413    360       O  
ATOM   1093  CB  ASN A 148      63.385  56.744 131.178  1.00 63.56           C  
ANISOU 1093  CB  ASN A 148     9783   7539   6827   -167    393    471       C  
ATOM   1094  CG  ASN A 148      62.424  57.869 131.499  1.00 64.02           C  
ANISOU 1094  CG  ASN A 148     9873   7563   6888   -185    400    537       C  
ATOM   1095  OD1 ASN A 148      61.955  58.581 130.608  1.00 65.07           O  
ANISOU 1095  OD1 ASN A 148    10005   7713   7006   -222    438    591       O  
ATOM   1096  ND2 ASN A 148      62.137  58.045 132.782  1.00 63.91           N  
ANISOU 1096  ND2 ASN A 148     9888   7502   6893   -156    364    533       N  
ATOM   1097  N   LEU A 149      63.681  53.727 129.154  1.00 64.67           N  
ANISOU 1097  N   LEU A 149     9920   7772   6879   -136    403    392       N  
ATOM   1098  CA  LEU A 149      64.622  52.616 128.975  1.00 66.27           C  
ANISOU 1098  CA  LEU A 149    10099   7993   7086   -102    393    317       C  
ATOM   1099  C   LEU A 149      65.872  53.054 128.198  1.00 68.22           C  
ANISOU 1099  C   LEU A 149    10275   8293   7352   -122    439    283       C  
ATOM   1100  O   LEU A 149      66.999  52.878 128.668  1.00 68.45           O  
ANISOU 1100  O   LEU A 149    10260   8325   7422    -96    427    227       O  
ATOM   1101  CB  LEU A 149      63.943  51.432 128.276  1.00 66.15           C  
ANISOU 1101  CB  LEU A 149    10124   7990   7018    -92    387    311       C  
ATOM   1102  CG  LEU A 149      64.795  50.199 127.936  1.00 66.61           C  
ANISOU 1102  CG  LEU A 149    10168   8065   7074    -53    379    233       C  
ATOM   1103  CD1 LEU A 149      65.525  49.668 129.161  1.00 66.77           C  
ANISOU 1103  CD1 LEU A 149    10181   8046   7144      0    330    182       C  
ATOM   1104  CD2 LEU A 149      63.926  49.116 127.319  1.00 66.84           C  
ANISOU 1104  CD2 LEU A 149    10251   8093   7050    -50    367    234       C  
ATOM   1105  N   SER A 150      65.652  53.647 127.028  1.00 70.31           N  
ANISOU 1105  N   SER A 150    10526   8601   7584   -170    490    321       N  
ATOM   1106  CA  SER A 150      66.738  54.155 126.176  1.00 72.34           C  
ANISOU 1106  CA  SER A 150    10716   8917   7852   -198    541    301       C  
ATOM   1107  C   SER A 150      67.595  55.215 126.879  1.00 73.10           C  
ANISOU 1107  C   SER A 150    10765   8999   8011   -214    542    299       C  
ATOM   1108  O   SER A 150      68.818  55.235 126.716  1.00 74.52           O  
ANISOU 1108  O   SER A 150    10879   9214   8218   -214    560    253       O  
ATOM   1109  CB  SER A 150      66.168  54.737 124.880  1.00 72.86           C  
ANISOU 1109  CB  SER A 150    10786   9029   7869   -253    593    359       C  
ATOM   1110  OG  SER A 150      65.187  55.724 125.167  1.00 73.96           O  
ANISOU 1110  OG  SER A 150    10960   9132   8010   -283    588    437       O  
ATOM   1111  N   ALA A 151      66.945  56.088 127.650  1.00 72.52           N  
ANISOU 1111  N   ALA A 151    10722   8874   7957   -229    522    349       N  
ATOM   1112  CA  ALA A 151      67.642  57.100 128.448  1.00 72.36           C  
ANISOU 1112  CA  ALA A 151    10669   8827   7996   -245    514    346       C  
ATOM   1113  C   ALA A 151      68.528  56.479 129.531  1.00 72.30           C  
ANISOU 1113  C   ALA A 151    10638   8800   8030   -197    467    276       C  
ATOM   1114  O   ALA A 151      69.628  56.964 129.778  1.00 72.69           O  
ANISOU 1114  O   ALA A 151    10630   8862   8124   -210    470    247       O  
ATOM   1115  CB  ALA A 151      66.646  58.071 129.069  1.00 71.97           C  
ANISOU 1115  CB  ALA A 151    10669   8721   7955   -262    500    409       C  
ATOM   1116  N   VAL A 152      68.050  55.407 130.166  1.00 72.26           N  
ANISOU 1116  N   VAL A 152    10678   8767   8010   -145    422    254       N  
ATOM   1117  CA  VAL A 152      68.828  54.715 131.210  1.00 72.51           C  
ANISOU 1117  CA  VAL A 152    10693   8780   8077    -94    372    192       C  
ATOM   1118  C   VAL A 152      69.948  53.851 130.607  1.00 73.32           C  
ANISOU 1118  C   VAL A 152    10739   8934   8186    -68    385    127       C  
ATOM   1119  O   VAL A 152      71.050  53.774 131.171  1.00 73.79           O  
ANISOU 1119  O   VAL A 152    10746   9001   8290    -46    364     78       O  
ATOM   1120  CB  VAL A 152      67.921  53.875 132.141  1.00 71.98           C  
ANISOU 1120  CB  VAL A 152    10696   8662   7991    -48    317    196       C  
ATOM   1121  CG1 VAL A 152      68.743  53.152 133.195  1.00 72.36           C  
ANISOU 1121  CG1 VAL A 152    10729   8691   8073      4    263    137       C  
ATOM   1122  CG2 VAL A 152      66.901  54.766 132.838  1.00 71.53           C  
ANISOU 1122  CG2 VAL A 152    10688   8559   7931    -67    305    255       C  
ATOM   1123  N   GLU A 153      69.661  53.200 129.478  1.00 74.23           N  
ANISOU 1123  N   GLU A 153    10862   9085   8255    -67    419    125       N  
ATOM   1124  CA  GLU A 153      70.668  52.407 128.746  1.00 75.48           C  
ANISOU 1124  CA  GLU A 153    10966   9298   8412    -41    442     62       C  
ATOM   1125  C   GLU A 153      71.895  53.228 128.327  1.00 76.41           C  
ANISOU 1125  C   GLU A 153    10994   9471   8564    -75    485     46       C  
ATOM   1126  O   GLU A 153      73.023  52.725 128.371  1.00 76.52           O  
ANISOU 1126  O   GLU A 153    10948   9517   8607    -41    483    -14       O  
ATOM   1127  CB  GLU A 153      70.046  51.745 127.510  1.00 76.06           C  
ANISOU 1127  CB  GLU A 153    11071   9403   8423    -46    477     68       C  
ATOM   1128  CG  GLU A 153      69.179  50.535 127.832  1.00 76.16           C  
ANISOU 1128  CG  GLU A 153    11158   9372   8407     -2    432     58       C  
ATOM   1129  CD  GLU A 153      68.405  49.995 126.641  1.00 76.90           C  
ANISOU 1129  CD  GLU A 153    11290   9491   8435    -18    461     71       C  
ATOM   1130  OE1 GLU A 153      68.368  50.644 125.572  1.00 77.82           O  
ANISOU 1130  OE1 GLU A 153    11384   9660   8521    -66    517     98       O  
ATOM   1131  OE2 GLU A 153      67.820  48.902 126.784  1.00 77.74           O  
ANISOU 1131  OE2 GLU A 153    11453   9565   8518     15    425     54       O  
ATOM   1132  N   ARG A 154      71.663  54.478 127.915  1.00 76.91           N  
ANISOU 1132  N   ARG A 154    11049   9545   8627   -141    522    103       N  
ATOM   1133  CA  ARG A 154      72.744  55.423 127.614  1.00 77.83           C  
ANISOU 1133  CA  ARG A 154    11085   9707   8780   -186    559    101       C  
ATOM   1134  C   ARG A 154      73.650  55.641 128.820  1.00 77.56           C  
ANISOU 1134  C   ARG A 154    11009   9648   8811   -168    514     64       C  
ATOM   1135  O   ARG A 154      74.866  55.547 128.700  1.00 78.55           O  
ANISOU 1135  O   ARG A 154    11054   9821   8968   -162    526     19       O  
ATOM   1136  CB  ARG A 154      72.193  56.780 127.152  1.00 78.51           C  
ANISOU 1136  CB  ARG A 154    11184   9788   8858   -260    596    178       C  
ATOM   1137  CG  ARG A 154      71.762  56.825 125.706  1.00 79.43           C  
ANISOU 1137  CG  ARG A 154    11305   9958   8916   -296    656    214       C  
ATOM   1138  CD  ARG A 154      71.199  58.188 125.319  1.00 79.92           C  
ANISOU 1138  CD  ARG A 154    11382  10008   8974   -366    686    297       C  
ATOM   1139  NE  ARG A 154      72.231  59.113 124.841  1.00 80.84           N  
ANISOU 1139  NE  ARG A 154    11424  10169   9120   -423    729    306       N  
ATOM   1140  CZ  ARG A 154      71.996  60.310 124.299  1.00 81.01           C  
ANISOU 1140  CZ  ARG A 154    11444  10192   9141   -491    765    376       C  
ATOM   1141  NH1 ARG A 154      70.751  60.771 124.154  1.00 80.45           N  
ANISOU 1141  NH1 ARG A 154    11442  10081   9042   -507    762    444       N  
ATOM   1142  NH2 ARG A 154      73.020  61.061 123.896  1.00 81.63           N  
ANISOU 1142  NH2 ARG A 154    11452  10314   9250   -544    802    381       N  
ATOM   1143  N   ALA A 155      73.048  55.934 129.971  1.00 76.47           N  
ANISOU 1143  N   ALA A 155    10923   9439   8690   -159    462     84       N  
ATOM   1144  CA  ALA A 155      73.792  56.139 131.215  1.00 76.86           C  
ANISOU 1144  CA  ALA A 155    10945   9461   8795   -142    410     50       C  
ATOM   1145  C   ALA A 155      74.469  54.860 131.726  1.00 77.27           C  
ANISOU 1145  C   ALA A 155    10974   9521   8860    -68    368    -17       C  
ATOM   1146  O   ALA A 155      75.553  54.929 132.312  1.00 77.98           O  
ANISOU 1146  O   ALA A 155    11002   9627   8998    -57    343    -58       O  
ATOM   1147  CB  ALA A 155      72.878  56.715 132.286  1.00 76.60           C  
ANISOU 1147  CB  ALA A 155    10983   9353   8766   -147    367     88       C  
ATOM   1148  N   TRP A 156      73.832  53.707 131.504  1.00 77.30           N  
ANISOU 1148  N   TRP A 156    11029   9515   8824    -19    358    -28       N  
ATOM   1149  CA  TRP A 156      74.403  52.402 131.892  1.00 77.37           C  
ANISOU 1149  CA  TRP A 156    11025   9526   8845     55    319    -90       C  
ATOM   1150  C   TRP A 156      75.675  52.073 131.079  1.00 78.51           C  
ANISOU 1150  C   TRP A 156    11077   9746   9007     68    358   -144       C  
ATOM   1151  O   TRP A 156      76.702  51.633 131.635  1.00 79.07           O  
ANISOU 1151  O   TRP A 156    11091   9830   9119    112    326   -195       O  
ATOM   1152  CB  TRP A 156      73.338  51.307 131.725  1.00 76.77           C  
ANISOU 1152  CB  TRP A 156    11031   9417   8720     93    303    -84       C  
ATOM   1153  CG  TRP A 156      73.570  50.048 132.511  1.00 76.80           C  
ANISOU 1153  CG  TRP A 156    11054   9389   8737    170    243   -130       C  
ATOM   1154  CD1 TRP A 156      73.675  48.782 132.011  1.00 76.93           C  
ANISOU 1154  CD1 TRP A 156    11080   9412   8735    222    241   -172       C  
ATOM   1155  CD2 TRP A 156      73.697  49.927 133.936  1.00 76.77           C  
ANISOU 1155  CD2 TRP A 156    11066   9338   8764    202    173   -137       C  
ATOM   1156  NE1 TRP A 156      73.870  47.882 133.030  1.00 77.00           N  
ANISOU 1156  NE1 TRP A 156    11110   9378   8767    286    174   -202       N  
ATOM   1157  CE2 TRP A 156      73.887  48.555 134.223  1.00 76.80           C  
ANISOU 1157  CE2 TRP A 156    11088   9322   8770    274    131   -179       C  
ATOM   1158  CE3 TRP A 156      73.682  50.846 134.997  1.00 76.60           C  
ANISOU 1158  CE3 TRP A 156    11047   9288   8768    177    141   -114       C  
ATOM   1159  CZ2 TRP A 156      74.064  48.076 135.530  1.00 76.44           C  
ANISOU 1159  CZ2 TRP A 156    11061   9233   8748    321     58   -192       C  
ATOM   1160  CZ3 TRP A 156      73.861  50.369 136.299  1.00 76.49           C  
ANISOU 1160  CZ3 TRP A 156    11052   9235   8774    223     69   -132       C  
ATOM   1161  CH2 TRP A 156      74.041  48.993 136.551  1.00 76.37           C  
ANISOU 1161  CH2 TRP A 156    11053   9204   8758    294     28   -168       C  
ATOM   1162  N   ALA A 157      75.597  52.303 129.767  1.00 79.43           N  
ANISOU 1162  N   ALA A 157    11174   9913   9089     31    427   -129       N  
ATOM   1163  CA  ALA A 157      76.746  52.160 128.863  1.00 80.79           C  
ANISOU 1163  CA  ALA A 157    11255  10168   9270     34    478   -172       C  
ATOM   1164  C   ALA A 157      77.814  53.232 129.113  1.00 81.93           C  
ANISOU 1164  C   ALA A 157    11310  10349   9468    -11    490   -170       C  
ATOM   1165  O   ALA A 157      79.005  52.923 129.148  1.00 82.46           O  
ANISOU 1165  O   ALA A 157    11293  10465   9572     16    492   -221       O  
ATOM   1166  CB  ALA A 157      76.287  52.205 127.413  1.00 80.93           C  
ANISOU 1166  CB  ALA A 157    11285  10234   9230      0    549   -149       C  
ATOM   1167  N   ALA A 158      77.381  54.478 129.304  1.00 82.42           N  
ANISOU 1167  N   ALA A 158    11391  10385   9538    -82    496   -111       N  
ATOM   1168  CA  ALA A 158      78.274  55.597 129.649  1.00 83.43           C  
ANISOU 1168  CA  ALA A 158    11447  10531   9719   -136    499   -103       C  
ATOM   1169  C   ALA A 158      79.026  55.346 130.955  1.00 84.04           C  
ANISOU 1169  C   ALA A 158    11492  10585   9851    -95    428   -148       C  
ATOM   1170  O   ALA A 158      80.214  55.651 131.057  1.00 85.60           O  
ANISOU 1170  O   ALA A 158    11598  10830  10095   -109    431   -176       O  
ATOM   1171  CB  ALA A 158      77.492  56.901 129.741  1.00 83.07           C  
ANISOU 1171  CB  ALA A 158    11449  10441   9671   -211    507    -32       C  
ATOM   1172  N   ALA A 159      78.327  54.800 131.948  1.00 83.77           N  
ANISOU 1172  N   ALA A 159    11534  10482   9811    -47    365   -151       N  
ATOM   1173  CA  ALA A 159      78.970  54.280 133.159  1.00 84.30           C  
ANISOU 1173  CA  ALA A 159    11581  10529   9919      6    293   -197       C  
ATOM   1174  C   ALA A 159      79.855  53.073 132.830  1.00 84.99           C  
ANISOU 1174  C   ALA A 159    11608  10667  10016     78    294   -259       C  
ATOM   1175  O   ALA A 159      80.883  52.869 133.473  1.00 85.71           O  
ANISOU 1175  O   ALA A 159    11632  10778  10153    108    256   -301       O  
ATOM   1176  CB  ALA A 159      77.930  53.904 134.204  1.00 83.73           C  
ANISOU 1176  CB  ALA A 159    11610  10376   9828     41    231   -180       C  
ATOM   1177  N   GLY A 160      79.439  52.276 131.842  1.00 84.91           N  
ANISOU 1177  N   GLY A 160    11623  10676   9961    106    336   -267       N  
ATOM   1178  CA  GLY A 160      80.244  51.165 131.330  1.00 85.06           C  
ANISOU 1178  CA  GLY A 160    11587  10745   9984    174    349   -329       C  
ATOM   1179  C   GLY A 160      79.875  49.865 132.000  1.00 84.65           C  
ANISOU 1179  C   GLY A 160    11597  10638   9926    260    288   -360       C  
ATOM   1180  O   GLY A 160      80.754  49.129 132.450  1.00 85.04           O  
ANISOU 1180  O   GLY A 160    11598  10700  10012    326    252   -411       O  
ATOM   1181  N   SER A 161      78.572  49.587 132.055  1.00 83.90           N  
ANISOU 1181  N   SER A 161    11609  10482   9786    258    275   -324       N  
ATOM   1182  CA  SER A 161      78.045  48.388 132.709  1.00 83.01           C  
ANISOU 1182  CA  SER A 161    11568  10306   9662    329    215   -341       C  
ATOM   1183  C   SER A 161      77.270  47.539 131.705  1.00 82.49           C  
ANISOU 1183  C   SER A 161    11562  10235   9542    347    248   -345       C  
ATOM   1184  O   SER A 161      76.572  48.070 130.841  1.00 81.55           O  
ANISOU 1184  O   SER A 161    11470  10133   9382    290    300   -307       O  
ATOM   1185  CB  SER A 161      77.144  48.789 133.868  1.00 82.19           C  
ANISOU 1185  CB  SER A 161    11541  10131   9555    310    158   -293       C  
ATOM   1186  OG  SER A 161      77.875  49.470 134.871  1.00 82.57           O  
ANISOU 1186  OG  SER A 161    11540  10180   9650    299    119   -297       O  
ATOM   1187  N   MET A 162      77.402  46.220 131.830  1.00 82.96           N  
ANISOU 1187  N   MET A 162    11646  10271   9604    425    215   -390       N  
ATOM   1188  CA  MET A 162      76.818  45.271 130.876  1.00 83.05           C  
ANISOU 1188  CA  MET A 162    11711  10276   9568    449    241   -408       C  
ATOM   1189  C   MET A 162      75.392  44.886 131.272  1.00 80.86           C  
ANISOU 1189  C   MET A 162    11547   9922   9251    440    202   -363       C  
ATOM   1190  O   MET A 162      74.984  45.060 132.423  1.00 80.48           O  
ANISOU 1190  O   MET A 162    11537   9821   9219    438    146   -330       O  
ATOM   1191  CB  MET A 162      77.674  44.000 130.794  1.00 84.98           C  
ANISOU 1191  CB  MET A 162    11926  10525   9836    541    223   -483       C  
ATOM   1192  CG  MET A 162      79.154  44.219 130.498  1.00 86.67           C  
ANISOU 1192  CG  MET A 162    12018  10817  10093    565    256   -534       C  
ATOM   1193  SD  MET A 162      79.482  44.986 128.895  1.00 88.80           S  
ANISOU 1193  SD  MET A 162    12222  11190  10328    504    365   -537       S  
ATOM   1194  CE  MET A 162      79.432  46.739 129.276  1.00 87.89           C  
ANISOU 1194  CE  MET A 162    12069  11095  10228    401    379   -466       C  
ATOM   1195  N   GLY A 163      74.643  44.359 130.305  1.00 78.86           N  
ANISOU 1195  N   GLY A 163    11348   9667   8946    432    233   -362       N  
ATOM   1196  CA  GLY A 163      73.304  43.823 130.552  1.00 76.95           C  
ANISOU 1196  CA  GLY A 163    11212   9358   8667    425    197   -323       C  
ATOM   1197  C   GLY A 163      72.251  44.883 130.800  1.00 74.83           C  
ANISOU 1197  C   GLY A 163    10981   9075   8373    352    203   -244       C  
ATOM   1198  O   GLY A 163      72.475  46.064 130.524  1.00 75.06           O  
ANISOU 1198  O   GLY A 163    10962   9148   8408    299    245   -218       O  
ATOM   1199  N   GLU A 164      71.103  44.454 131.325  1.00 72.71           N  
ANISOU 1199  N   GLU A 164    10798   8746   8081    349    161   -204       N  
ATOM   1200  CA  GLU A 164      69.983  45.357 131.601  1.00 70.95           C  
ANISOU 1200  CA  GLU A 164    10618   8507   7833    288    164   -128       C  
ATOM   1201  C   GLU A 164      70.335  46.302 132.754  1.00 70.08           C  
ANISOU 1201  C   GLU A 164    10477   8385   7763    279    138   -107       C  
ATOM   1202  O   GLU A 164      71.016  45.890 133.696  1.00 70.66           O  
ANISOU 1202  O   GLU A 164    10535   8436   7875    327     90   -138       O  
ATOM   1203  CB  GLU A 164      68.717  44.574 131.962  1.00 70.34           C  
ANISOU 1203  CB  GLU A 164    10633   8370   7722    292    121    -93       C  
ATOM   1204  CG  GLU A 164      67.440  45.411 131.956  1.00 69.73           C  
ANISOU 1204  CG  GLU A 164    10598   8287   7609    231    136    -15       C  
ATOM   1205  CD  GLU A 164      66.239  44.702 132.559  1.00 69.06           C  
ANISOU 1205  CD  GLU A 164    10595   8145   7498    235     88     24       C  
ATOM   1206  OE1 GLU A 164      66.346  43.506 132.906  1.00 69.52           O  
ANISOU 1206  OE1 GLU A 164    10686   8164   7562    281     43     -7       O  
ATOM   1207  OE2 GLU A 164      65.178  45.349 132.696  1.00 67.90           O  
ANISOU 1207  OE2 GLU A 164    10480   7993   7325    192     95     89       O  
ATOM   1208  N   PRO A 165      69.885  47.570 132.677  1.00 68.88           N  
ANISOU 1208  N   PRO A 165    10319   8247   7603    218    170    -54       N  
ATOM   1209  CA  PRO A 165      70.067  48.485 133.802  1.00 68.04           C  
ANISOU 1209  CA  PRO A 165    10198   8121   7530    206    143    -34       C  
ATOM   1210  C   PRO A 165      69.438  48.037 135.125  1.00 66.85           C  
ANISOU 1210  C   PRO A 165    10110   7910   7378    236     76    -14       C  
ATOM   1211  O   PRO A 165      68.210  47.845 135.215  1.00 66.12           O  
ANISOU 1211  O   PRO A 165    10085   7787   7248    223     68     31       O  
ATOM   1212  CB  PRO A 165      69.409  49.776 133.313  1.00 67.93           C  
ANISOU 1212  CB  PRO A 165    10188   8124   7498    138    191     24       C  
ATOM   1213  CG  PRO A 165      69.551  49.732 131.837  1.00 68.34           C  
ANISOU 1213  CG  PRO A 165    10212   8228   7523    113    252     16       C  
ATOM   1214  CD  PRO A 165      69.443  48.285 131.461  1.00 68.64           C  
ANISOU 1214  CD  PRO A 165    10281   8260   7538    160    235    -21       C  
ATOM   1215  N   VAL A 166      70.307  47.846 136.117  1.00 66.85           N  
ANISOU 1215  N   VAL A 166    10082   7898   7418    275     29    -49       N  
ATOM   1216  CA  VAL A 166      69.923  47.713 137.517  1.00 66.75           C  
ANISOU 1216  CA  VAL A 166    10115   7837   7409    297    -32    -30       C  
ATOM   1217  C   VAL A 166      69.991  49.106 138.150  1.00 66.78           C  
ANISOU 1217  C   VAL A 166    10099   7844   7429    257    -27     -7       C  
ATOM   1218  O   VAL A 166      71.010  49.792 138.033  1.00 67.12           O  
ANISOU 1218  O   VAL A 166    10073   7919   7509    242    -12    -36       O  
ATOM   1219  CB  VAL A 166      70.869  46.768 138.284  1.00 67.26           C  
ANISOU 1219  CB  VAL A 166    10160   7888   7506    363    -91    -80       C  
ATOM   1220  CG1 VAL A 166      70.450  46.653 139.751  1.00 67.04           C  
ANISOU 1220  CG1 VAL A 166    10182   7815   7474    382   -156    -56       C  
ATOM   1221  CG2 VAL A 166      70.918  45.403 137.607  1.00 67.69           C  
ANISOU 1221  CG2 VAL A 166    10231   7934   7551    407    -95   -111       C  
ATOM   1222  N   ILE A 167      68.913  49.507 138.823  1.00 66.18           N  
ANISOU 1222  N   ILE A 167    10083   7733   7326    240    -41     42       N  
ATOM   1223  CA  ILE A 167      68.776  50.861 139.376  1.00 65.96           C  
ANISOU 1223  CA  ILE A 167    10051   7700   7308    202    -32     66       C  
ATOM   1224  C   ILE A 167      67.957  50.880 140.663  1.00 65.65           C  
ANISOU 1224  C   ILE A 167    10076   7619   7247    216    -77     97       C  
ATOM   1225  O   ILE A 167      67.225  49.927 140.963  1.00 65.84           O  
ANISOU 1225  O   ILE A 167    10153   7620   7241    243   -104    116       O  
ATOM   1226  CB  ILE A 167      68.141  51.851 138.354  1.00 65.66           C  
ANISOU 1226  CB  ILE A 167    10013   7679   7254    144     33    109       C  
ATOM   1227  CG1 ILE A 167      66.827  51.311 137.753  1.00 65.02           C  
ANISOU 1227  CG1 ILE A 167     9991   7590   7124    139     51    155       C  
ATOM   1228  CG2 ILE A 167      69.129  52.192 137.246  1.00 66.18           C  
ANISOU 1228  CG2 ILE A 167    10006   7793   7346    120     79     80       C  
ATOM   1229  CD1 ILE A 167      65.568  51.757 138.465  1.00 64.54           C  
ANISOU 1229  CD1 ILE A 167     9990   7496   7034    129     41    211       C  
ATOM   1230  N   LYS A 168      68.104  51.970 141.421  1.00 65.52           N  
ANISOU 1230  N   LYS A 168    10054   7594   7247    196    -84    100       N  
ATOM   1231  CA  LYS A 168      67.194  52.278 142.522  1.00 65.05           C  
ANISOU 1231  CA  LYS A 168    10054   7500   7158    201   -111    134       C  
ATOM   1232  C   LYS A 168      65.842  52.611 141.907  1.00 64.32           C  
ANISOU 1232  C   LYS A 168    10005   7402   7030    173    -65    193       C  
ATOM   1233  O   LYS A 168      65.726  53.571 141.141  1.00 63.81           O  
ANISOU 1233  O   LYS A 168     9921   7349   6974    133    -16    211       O  
ATOM   1234  CB  LYS A 168      67.695  53.457 143.372  1.00 65.45           C  
ANISOU 1234  CB  LYS A 168    10090   7543   7235    183   -124    117       C  
ATOM   1235  CG  LYS A 168      66.659  53.976 144.366  1.00 65.33           C  
ANISOU 1235  CG  LYS A 168    10138   7496   7186    184   -137    152       C  
ATOM   1236  CD  LYS A 168      67.278  54.650 145.574  1.00 65.81           C  
ANISOU 1236  CD  LYS A 168    10196   7545   7264    187   -178    120       C  
ATOM   1237  CE  LYS A 168      66.188  55.177 146.499  1.00 65.84           C  
ANISOU 1237  CE  LYS A 168    10266   7521   7229    191   -182    152       C  
ATOM   1238  NZ  LYS A 168      66.718  55.605 147.824  1.00 66.48           N  
ANISOU 1238  NZ  LYS A 168    10355   7590   7313    202   -232    117       N  
ATOM   1239  N   CYS A 169      64.833  51.813 142.249  1.00 64.12           N  
ANISOU 1239  N   CYS A 169    10036   7360   6965    194    -84    227       N  
ATOM   1240  CA  CYS A 169      63.513  51.925 141.639  1.00 63.85           C  
ANISOU 1240  CA  CYS A 169    10038   7326   6893    171    -47    286       C  
ATOM   1241  C   CYS A 169      62.811  53.221 142.045  1.00 64.13           C  
ANISOU 1241  C   CYS A 169    10094   7351   6922    149    -23    322       C  
ATOM   1242  O   CYS A 169      62.340  53.360 143.175  1.00 64.07           O  
ANISOU 1242  O   CYS A 169    10122   7323   6896    167    -49    335       O  
ATOM   1243  CB  CYS A 169      62.650  50.719 142.009  1.00 63.58           C  
ANISOU 1243  CB  CYS A 169    10057   7277   6820    196    -78    313       C  
ATOM   1244  SG  CYS A 169      60.982  50.739 141.317  1.00 63.42           S  
ANISOU 1244  SG  CYS A 169    10079   7263   6754    167    -40    388       S  
ATOM   1245  N   GLU A 170      62.767  54.163 141.106  1.00 64.71           N  
ANISOU 1245  N   GLU A 170    10142   7436   7008    111     28    339       N  
ATOM   1246  CA  GLU A 170      62.105  55.448 141.286  1.00 65.15           C  
ANISOU 1246  CA  GLU A 170    10214   7477   7063     90     56    375       C  
ATOM   1247  C   GLU A 170      61.128  55.656 140.144  1.00 64.03           C  
ANISOU 1247  C   GLU A 170    10080   7351   6898     62    105    431       C  
ATOM   1248  O   GLU A 170      61.405  55.264 139.016  1.00 64.05           O  
ANISOU 1248  O   GLU A 170    10055   7379   6900     44    127    428       O  
ATOM   1249  CB  GLU A 170      63.140  56.569 141.295  1.00 66.84           C  
ANISOU 1249  CB  GLU A 170    10386   7685   7322     65     67    340       C  
ATOM   1250  CG  GLU A 170      64.070  56.539 142.502  1.00 68.48           C  
ANISOU 1250  CG  GLU A 170    10587   7879   7552     88     16    286       C  
ATOM   1251  CD  GLU A 170      65.331  57.364 142.303  1.00 70.25           C  
ANISOU 1251  CD  GLU A 170    10755   8107   7827     58     22    245       C  
ATOM   1252  OE1 GLU A 170      66.034  57.142 141.286  1.00 71.76           O  
ANISOU 1252  OE1 GLU A 170    10896   8328   8038     39     45    230       O  
ATOM   1253  OE2 GLU A 170      65.629  58.222 143.172  1.00 70.80           O  
ANISOU 1253  OE2 GLU A 170    10831   8152   7914     52      3    225       O  
ATOM   1254  N   PHE A 171      59.995  56.287 140.437  1.00 63.37           N  
ANISOU 1254  N   PHE A 171    10030   7253   6792     61    121    482       N  
ATOM   1255  CA  PHE A 171      58.936  56.506 139.446  1.00 62.75           C  
ANISOU 1255  CA  PHE A 171     9960   7190   6689     39    162    544       C  
ATOM   1256  C   PHE A 171      59.434  57.342 138.269  1.00 63.45           C  
ANISOU 1256  C   PHE A 171    10011   7294   6804      0    206    548       C  
ATOM   1257  O   PHE A 171      59.295  56.943 137.110  1.00 63.68           O  
ANISOU 1257  O   PHE A 171    10025   7353   6817    -22    229    567       O  
ATOM   1258  CB  PHE A 171      57.737  57.190 140.102  1.00 61.98           C  
ANISOU 1258  CB  PHE A 171     9900   7076   6572     51    171    593       C  
ATOM   1259  CG  PHE A 171      56.538  57.308 139.210  1.00 61.08           C  
ANISOU 1259  CG  PHE A 171     9794   6981   6430     34    206    662       C  
ATOM   1260  CD1 PHE A 171      55.611  56.280 139.135  1.00 60.50           C  
ANISOU 1260  CD1 PHE A 171     9743   6928   6315     41    193    696       C  
ATOM   1261  CD2 PHE A 171      56.325  58.457 138.458  1.00 60.93           C  
ANISOU 1261  CD2 PHE A 171     9761   6960   6426      9    248    696       C  
ATOM   1262  CE1 PHE A 171      54.496  56.391 138.320  1.00 60.33           C  
ANISOU 1262  CE1 PHE A 171     9725   6929   6267     23    221    761       C  
ATOM   1263  CE2 PHE A 171      55.215  58.573 137.638  1.00 60.79           C  
ANISOU 1263  CE2 PHE A 171     9750   6965   6383     -5    276    763       C  
ATOM   1264  CZ  PHE A 171      54.300  57.539 137.568  1.00 60.55           C  
ANISOU 1264  CZ  PHE A 171     9736   6959   6309      2    262    795       C  
ATOM   1265  N   GLU A 172      60.029  58.490 138.581  1.00 64.33           N  
ANISOU 1265  N   GLU A 172    10107   7382   6952    -13    215    532       N  
ATOM   1266  CA  GLU A 172      60.584  59.387 137.558  1.00 64.81           C  
ANISOU 1266  CA  GLU A 172    10130   7452   7041    -56    255    539       C  
ATOM   1267  C   GLU A 172      61.760  58.807 136.762  1.00 64.87           C  
ANISOU 1267  C   GLU A 172    10088   7495   7064    -74    260    495       C  
ATOM   1268  O   GLU A 172      62.080  59.323 135.689  1.00 65.95           O  
ANISOU 1268  O   GLU A 172    10193   7653   7211   -112    299    511       O  
ATOM   1269  CB  GLU A 172      60.966  60.757 138.148  1.00 65.72           C  
ANISOU 1269  CB  GLU A 172    10246   7527   7197    -69    259    529       C  
ATOM   1270  CG  GLU A 172      62.103  60.774 139.166  1.00 66.68           C  
ANISOU 1270  CG  GLU A 172    10353   7631   7352    -58    220    461       C  
ATOM   1271  CD  GLU A 172      61.610  60.849 140.602  1.00 67.23           C  
ANISOU 1271  CD  GLU A 172    10468   7666   7409    -19    184    451       C  
ATOM   1272  OE1 GLU A 172      60.862  59.928 141.011  1.00 67.43           O  
ANISOU 1272  OE1 GLU A 172    10523   7701   7394     14    166    465       O  
ATOM   1273  OE2 GLU A 172      61.972  61.819 141.318  1.00 67.95           O  
ANISOU 1273  OE2 GLU A 172    10567   7721   7527    -25    175    428       O  
ATOM   1274  N   LYS A 173      62.403  57.759 137.282  1.00 64.40           N  
ANISOU 1274  N   LYS A 173    10020   7443   7006    -44    222    443       N  
ATOM   1275  CA  LYS A 173      63.488  57.069 136.567  1.00 64.46           C  
ANISOU 1275  CA  LYS A 173     9979   7486   7025    -49    225    398       C  
ATOM   1276  C   LYS A 173      62.977  56.128 135.470  1.00 63.30           C  
ANISOU 1276  C   LYS A 173     9838   7373   6838    -52    244    417       C  
ATOM   1277  O   LYS A 173      63.653  55.966 134.456  1.00 63.41           O  
ANISOU 1277  O   LYS A 173     9811   7425   6856    -71    272    398       O  
ATOM   1278  CB  LYS A 173      64.364  56.296 137.559  1.00 65.37           C  
ANISOU 1278  CB  LYS A 173    10084   7594   7160    -11    173    336       C  
ATOM   1279  CG  LYS A 173      65.656  55.712 136.998  1.00 66.33           C  
ANISOU 1279  CG  LYS A 173    10147   7750   7305     -9    174    281       C  
ATOM   1280  CD  LYS A 173      66.636  56.779 136.547  1.00 67.26           C  
ANISOU 1280  CD  LYS A 173    10206   7885   7463    -51    205    267       C  
ATOM   1281  CE  LYS A 173      68.023  56.176 136.333  1.00 68.29           C  
ANISOU 1281  CE  LYS A 173    10273   8051   7622    -38    196    205       C  
ATOM   1282  NZ  LYS A 173      69.018  57.161 135.828  1.00 69.31           N  
ANISOU 1282  NZ  LYS A 173    10337   8205   7791    -85    229    193       N  
ATOM   1283  N   VAL A 174      61.809  55.511 135.676  1.00 62.09           N  
ANISOU 1283  N   VAL A 174     9733   7210   6645    -34    230    453       N  
ATOM   1284  CA  VAL A 174      61.246  54.548 134.705  1.00 61.78           C  
ANISOU 1284  CA  VAL A 174     9708   7200   6566    -39    240    469       C  
ATOM   1285  C   VAL A 174      60.050  55.081 133.902  1.00 61.38           C  
ANISOU 1285  C   VAL A 174     9676   7163   6482    -70    275    542       C  
ATOM   1286  O   VAL A 174      59.951  54.804 132.707  1.00 61.28           O  
ANISOU 1286  O   VAL A 174     9652   7186   6444    -94    303    553       O  
ATOM   1287  CB  VAL A 174      60.892  53.177 135.352  1.00 61.39           C  
ANISOU 1287  CB  VAL A 174     9695   7134   6494      0    192    453       C  
ATOM   1288  CG1 VAL A 174      62.100  52.608 136.085  1.00 61.57           C  
ANISOU 1288  CG1 VAL A 174     9697   7145   6550     34    155    385       C  
ATOM   1289  CG2 VAL A 174      59.681  53.260 136.277  1.00 60.83           C  
ANISOU 1289  CG2 VAL A 174     9673   7036   6401     12    171    502       C  
ATOM   1290  N   ILE A 175      59.152  55.830 134.545  1.00 60.80           N  
ANISOU 1290  N   ILE A 175     9630   7063   6406    -68    275    589       N  
ATOM   1291  CA  ILE A 175      57.979  56.390 133.862  1.00 60.32           C  
ANISOU 1291  CA  ILE A 175     9585   7015   6318    -92    305    663       C  
ATOM   1292  C   ILE A 175      58.344  57.747 133.256  1.00 60.51           C  
ANISOU 1292  C   ILE A 175     9580   7041   6368   -125    347    684       C  
ATOM   1293  O   ILE A 175      58.953  58.588 133.927  1.00 61.02           O  
ANISOU 1293  O   ILE A 175     9635   7075   6473   -122    345    663       O  
ATOM   1294  CB  ILE A 175      56.768  56.543 134.815  1.00 59.85           C  
ANISOU 1294  CB  ILE A 175     9566   6930   6242    -68    288    708       C  
ATOM   1295  CG1 ILE A 175      56.385  55.191 135.449  1.00 59.62           C  
ANISOU 1295  CG1 ILE A 175     9567   6899   6186    -41    245    694       C  
ATOM   1296  CG2 ILE A 175      55.569  57.146 134.083  1.00 59.88           C  
ANISOU 1296  CG2 ILE A 175     9578   6951   6221    -90    319    786       C  
ATOM   1297  CD1 ILE A 175      55.782  54.164 134.499  1.00 59.65           C  
ANISOU 1297  CD1 ILE A 175     9580   6934   6149    -58    244    715       C  
ATOM   1298  N   SER A 176      57.970  57.947 131.991  1.00 60.19           N  
ANISOU 1298  N   SER A 176     9530   7036   6304   -160    382    726       N  
ATOM   1299  CA  SER A 176      58.232  59.200 131.277  1.00 59.77           C  
ANISOU 1299  CA  SER A 176     9452   6986   6270   -196    423    758       C  
ATOM   1300  C   SER A 176      57.311  60.306 131.790  1.00 58.92           C  
ANISOU 1300  C   SER A 176     9370   6841   6174   -190    429    816       C  
ATOM   1301  O   SER A 176      56.096  60.120 131.855  1.00 58.27           O  
ANISOU 1301  O   SER A 176     9316   6762   6062   -176    423    865       O  
ATOM   1302  CB  SER A 176      58.024  59.008 129.769  1.00 59.96           C  
ANISOU 1302  CB  SER A 176     9462   7064   6256   -233    455    791       C  
ATOM   1303  OG  SER A 176      58.217  60.214 129.046  1.00 60.49           O  
ANISOU 1303  OG  SER A 176     9507   7136   6338   -272    495    831       O  
ATOM   1304  N   MET A 177      57.889  61.450 132.157  1.00 58.62           N  
ANISOU 1304  N   MET A 177     9322   6767   6183   -199    440    809       N  
ATOM   1305  CA  MET A 177      57.095  62.604 132.597  1.00 58.42           C  
ANISOU 1305  CA  MET A 177     9322   6699   6173   -191    449    859       C  
ATOM   1306  C   MET A 177      56.230  63.176 131.479  1.00 58.09           C  
ANISOU 1306  C   MET A 177     9281   6678   6110   -216    483    941       C  
ATOM   1307  O   MET A 177      55.103  63.608 131.731  1.00 57.46           O  
ANISOU 1307  O   MET A 177     9228   6581   6022   -195    485    994       O  
ATOM   1308  CB  MET A 177      57.983  63.692 133.204  1.00 58.93           C  
ANISOU 1308  CB  MET A 177     9379   6715   6294   -200    450    828       C  
ATOM   1309  CG  MET A 177      58.488  63.340 134.595  1.00 59.16           C  
ANISOU 1309  CG  MET A 177     9421   6715   6343   -165    410    762       C  
ATOM   1310  SD  MET A 177      57.165  63.194 135.821  1.00 58.94           S  
ANISOU 1310  SD  MET A 177     9445   6658   6289   -109    386    782       S  
ATOM   1311  CE  MET A 177      57.715  61.756 136.707  1.00 59.01           C  
ANISOU 1311  CE  MET A 177     9454   6682   6281    -78    338    714       C  
ATOM   1312  N   GLU A 178      56.751  63.142 130.252  1.00 58.24           N  
ANISOU 1312  N   GLU A 178     9270   6738   6118   -259    509    950       N  
ATOM   1313  CA  GLU A 178      55.985  63.513 129.055  1.00 58.24           C  
ANISOU 1313  CA  GLU A 178     9268   6770   6088   -287    538   1027       C  
ATOM   1314  C   GLU A 178      54.677  62.719 128.955  1.00 57.46           C  
ANISOU 1314  C   GLU A 178     9192   6699   5938   -266    523   1067       C  
ATOM   1315  O   GLU A 178      53.598  63.300 128.741  1.00 57.15           O  
ANISOU 1315  O   GLU A 178     9168   6658   5889   -261    532   1139       O  
ATOM   1316  CB  GLU A 178      56.830  63.308 127.799  1.00 58.77           C  
ANISOU 1316  CB  GLU A 178     9299   6890   6138   -334    566   1018       C  
ATOM   1317  CG  GLU A 178      57.972  64.306 127.673  1.00 59.77           C  
ANISOU 1317  CG  GLU A 178     9398   6996   6314   -368    588   1003       C  
ATOM   1318  CD  GLU A 178      58.981  63.918 126.610  1.00 60.66           C  
ANISOU 1318  CD  GLU A 178     9468   7169   6411   -409    615    976       C  
ATOM   1319  OE1 GLU A 178      59.512  62.787 126.692  1.00 60.98           O  
ANISOU 1319  OE1 GLU A 178     9494   7240   6434   -394    601    912       O  
ATOM   1320  OE2 GLU A 178      59.255  64.745 125.704  1.00 61.51           O  
ANISOU 1320  OE2 GLU A 178     9556   7292   6522   -455    650   1020       O  
ATOM   1321  N   TYR A 179      54.789  61.399 129.137  1.00 56.90           N  
ANISOU 1321  N   TYR A 179     9125   6654   5839   -252    498   1020       N  
ATOM   1322  CA  TYR A 179      53.622  60.517 129.233  1.00 56.33           C  
ANISOU 1322  CA  TYR A 179     9076   6603   5723   -234    476   1048       C  
ATOM   1323  C   TYR A 179      52.651  60.964 130.342  1.00 55.85           C  
ANISOU 1323  C   TYR A 179     9041   6504   5675   -194    462   1081       C  
ATOM   1324  O   TYR A 179      51.446  61.102 130.104  1.00 55.72           O  
ANISOU 1324  O   TYR A 179     9034   6504   5633   -190    465   1148       O  
ATOM   1325  CB  TYR A 179      54.057  59.050 129.441  1.00 56.15           C  
ANISOU 1325  CB  TYR A 179     9056   6597   5679   -223    447    983       C  
ATOM   1326  CG  TYR A 179      52.972  58.157 130.003  1.00 55.90           C  
ANISOU 1326  CG  TYR A 179     9054   6569   5616   -199    415   1001       C  
ATOM   1327  CD1 TYR A 179      51.968  57.646 129.184  1.00 55.96           C  
ANISOU 1327  CD1 TYR A 179     9068   6618   5574   -220    413   1052       C  
ATOM   1328  CD2 TYR A 179      52.942  57.835 131.363  1.00 55.81           C  
ANISOU 1328  CD2 TYR A 179     9062   6520   5621   -160    384    971       C  
ATOM   1329  CE1 TYR A 179      50.971  56.834 129.693  1.00 55.91           C  
ANISOU 1329  CE1 TYR A 179     9085   6615   5540   -204    383   1072       C  
ATOM   1330  CE2 TYR A 179      51.944  57.030 131.887  1.00 55.64           C  
ANISOU 1330  CE2 TYR A 179     9065   6504   5570   -142    357    993       C  
ATOM   1331  CZ  TYR A 179      50.960  56.535 131.055  1.00 55.83           C  
ANISOU 1331  CZ  TYR A 179     9093   6568   5549   -166    356   1045       C  
ATOM   1332  OH  TYR A 179      49.970  55.736 131.581  1.00 56.12           O  
ANISOU 1332  OH  TYR A 179     9152   6611   5558   -154    328   1070       O  
ATOM   1333  N   MET A 180      53.185  61.201 131.537  1.00 55.31           N  
ANISOU 1333  N   MET A 180     8982   6389   5644   -165    447   1033       N  
ATOM   1334  CA  MET A 180      52.351  61.567 132.687  1.00 54.91           C  
ANISOU 1334  CA  MET A 180     8957   6304   5601   -122    435   1052       C  
ATOM   1335  C   MET A 180      51.627  62.906 132.512  1.00 54.83           C  
ANISOU 1335  C   MET A 180     8951   6271   5608   -117    463   1119       C  
ATOM   1336  O   MET A 180      50.450  63.030 132.864  1.00 54.66           O  
ANISOU 1336  O   MET A 180     8945   6252   5570    -89    462   1168       O  
ATOM   1337  CB  MET A 180      53.179  61.578 133.980  1.00 54.98           C  
ANISOU 1337  CB  MET A 180     8977   6270   5643    -95    412    982       C  
ATOM   1338  CG  MET A 180      53.291  60.220 134.662  1.00 54.46           C  
ANISOU 1338  CG  MET A 180     8921   6215   5553    -74    375    937       C  
ATOM   1339  SD  MET A 180      51.852  59.852 135.689  1.00 54.09           S  
ANISOU 1339  SD  MET A 180     8908   6168   5474    -33    356    978       S  
ATOM   1340  CE  MET A 180      50.933  58.722 134.656  1.00 54.11           C  
ANISOU 1340  CE  MET A 180     8906   6228   5424    -58    352   1026       C  
ATOM   1341  N   VAL A 181      52.328  63.892 131.958  1.00 54.90           N  
ANISOU 1341  N   VAL A 181     8947   6261   5651   -145    487   1122       N  
ATOM   1342  CA  VAL A 181      51.773  65.233 131.763  1.00 55.38           C  
ANISOU 1342  CA  VAL A 181     9015   6289   5736   -141    512   1183       C  
ATOM   1343  C   VAL A 181      50.869  65.294 130.528  1.00 55.29           C  
ANISOU 1343  C   VAL A 181     8992   6323   5690   -162    530   1267       C  
ATOM   1344  O   VAL A 181      49.674  65.621 130.643  1.00 55.30           O  
ANISOU 1344  O   VAL A 181     9004   6326   5681   -134    533   1328       O  
ATOM   1345  CB  VAL A 181      52.898  66.292 131.675  1.00 56.00           C  
ANISOU 1345  CB  VAL A 181     9086   6322   5867   -167    528   1158       C  
ATOM   1346  CG1 VAL A 181      52.357  67.667 131.289  1.00 56.52           C  
ANISOU 1346  CG1 VAL A 181     9162   6352   5960   -169    554   1227       C  
ATOM   1347  CG2 VAL A 181      53.629  66.368 133.006  1.00 56.05           C  
ANISOU 1347  CG2 VAL A 181     9107   6281   5908   -142    505   1081       C  
ATOM   1348  N   TYR A 182      51.434  64.971 129.360  1.00 55.05           N  
ANISOU 1348  N   TYR A 182     8940   6336   5641   -210    542   1268       N  
ATOM   1349  CA  TYR A 182      50.706  65.141 128.097  1.00 55.05           C  
ANISOU 1349  CA  TYR A 182     8928   6381   5606   -238    560   1348       C  
ATOM   1350  C   TYR A 182      49.628  64.073 127.919  1.00 54.71           C  
ANISOU 1350  C   TYR A 182     8887   6390   5507   -229    540   1375       C  
ATOM   1351  O   TYR A 182      48.463  64.398 127.656  1.00 54.76           O  
ANISOU 1351  O   TYR A 182     8896   6413   5497   -217    542   1450       O  
ATOM   1352  CB  TYR A 182      51.652  65.135 126.888  1.00 55.27           C  
ANISOU 1352  CB  TYR A 182     8932   6445   5623   -294    581   1340       C  
ATOM   1353  CG  TYR A 182      52.785  66.154 126.940  1.00 55.51           C  
ANISOU 1353  CG  TYR A 182     8952   6430   5707   -316    601   1317       C  
ATOM   1354  CD1 TYR A 182      52.546  67.487 127.294  1.00 55.76           C  
ANISOU 1354  CD1 TYR A 182     8999   6400   5785   -303    612   1358       C  
ATOM   1355  CD2 TYR A 182      54.095  65.789 126.605  1.00 55.41           C  
ANISOU 1355  CD2 TYR A 182     8915   6437   5700   -350    609   1256       C  
ATOM   1356  CE1 TYR A 182      53.578  68.420 127.322  1.00 55.99           C  
ANISOU 1356  CE1 TYR A 182     9022   6385   5865   -330    628   1338       C  
ATOM   1357  CE2 TYR A 182      55.132  66.710 126.643  1.00 55.69           C  
ANISOU 1357  CE2 TYR A 182     8936   6436   5785   -376    626   1238       C  
ATOM   1358  CZ  TYR A 182      54.869  68.025 126.995  1.00 55.99           C  
ANISOU 1358  CZ  TYR A 182     8993   6410   5869   -370    634   1280       C  
ATOM   1359  OH  TYR A 182      55.896  68.940 127.028  1.00 56.12           O  
ANISOU 1359  OH  TYR A 182     8998   6387   5937   -403    649   1264       O  
ATOM   1360  N   PHE A 183      50.006  62.806 128.086  1.00 54.53           N  
ANISOU 1360  N   PHE A 183     8865   6393   5459   -233    518   1316       N  
ATOM   1361  CA  PHE A 183      49.081  61.704 127.836  1.00 54.58           C  
ANISOU 1361  CA  PHE A 183     8876   6449   5413   -235    496   1338       C  
ATOM   1362  C   PHE A 183      48.123  61.512 129.014  1.00 54.56           C  
ANISOU 1362  C   PHE A 183     8890   6427   5412   -189    475   1351       C  
ATOM   1363  O   PHE A 183      46.920  61.739 128.875  1.00 54.90           O  
ANISOU 1363  O   PHE A 183     8931   6490   5437   -179    476   1423       O  
ATOM   1364  CB  PHE A 183      49.843  60.411 127.503  1.00 54.29           C  
ANISOU 1364  CB  PHE A 183     8838   6442   5348   -257    480   1270       C  
ATOM   1365  CG  PHE A 183      48.997  59.354 126.866  1.00 54.01           C  
ANISOU 1365  CG  PHE A 183     8807   6459   5255   -276    461   1295       C  
ATOM   1366  CD1 PHE A 183      48.640  59.453 125.531  1.00 54.31           C  
ANISOU 1366  CD1 PHE A 183     8834   6549   5253   -317    475   1345       C  
ATOM   1367  CD2 PHE A 183      48.557  58.254 127.597  1.00 53.57           C  
ANISOU 1367  CD2 PHE A 183     8769   6402   5182   -258    426   1271       C  
ATOM   1368  CE1 PHE A 183      47.863  58.472 124.930  1.00 54.38           C  
ANISOU 1368  CE1 PHE A 183     8848   6606   5205   -339    453   1366       C  
ATOM   1369  CE2 PHE A 183      47.773  57.278 127.008  1.00 53.68           C  
ANISOU 1369  CE2 PHE A 183     8789   6461   5144   -282    405   1295       C  
ATOM   1370  CZ  PHE A 183      47.427  57.385 125.669  1.00 53.97           C  
ANISOU 1370  CZ  PHE A 183     8814   6548   5141   -323    418   1340       C  
ATOM   1371  N   ASN A 184      48.646  61.129 130.174  1.00 54.55           N  
ANISOU 1371  N   ASN A 184     8904   6391   5432   -160    458   1287       N  
ATOM   1372  CA  ASN A 184      47.790  60.794 131.313  1.00 54.87           C  
ANISOU 1372  CA  ASN A 184     8961   6421   5467   -119    438   1295       C  
ATOM   1373  C   ASN A 184      47.003  62.013 131.845  1.00 55.40           C  
ANISOU 1373  C   ASN A 184     9031   6459   5557    -82    457   1347       C  
ATOM   1374  O   ASN A 184      45.757  61.993 131.892  1.00 55.68           O  
ANISOU 1374  O   ASN A 184     9063   6521   5571    -65    456   1410       O  
ATOM   1375  CB  ASN A 184      48.630  60.147 132.422  1.00 54.89           C  
ANISOU 1375  CB  ASN A 184     8978   6391   5484    -98    413   1214       C  
ATOM   1376  CG  ASN A 184      47.812  59.776 133.641  1.00 55.03           C  
ANISOU 1376  CG  ASN A 184     9015   6402   5491    -58    394   1222       C  
ATOM   1377  OD1 ASN A 184      48.074  60.245 134.746  1.00 55.14           O  
ANISOU 1377  OD1 ASN A 184     9042   6375   5530    -23    392   1191       O  
ATOM   1378  ND2 ASN A 184      46.815  58.935 133.444  1.00 55.25           N  
ANISOU 1378  ND2 ASN A 184     9043   6471   5477    -67    379   1263       N  
ATOM   1379  N   PHE A 185      47.725  63.074 132.213  1.00 55.59           N  
ANISOU 1379  N   PHE A 185     9061   6431   5629    -69    474   1322       N  
ATOM   1380  CA  PHE A 185      47.105  64.214 132.898  1.00 55.66           C  
ANISOU 1380  CA  PHE A 185     9082   6400   5667    -25    490   1354       C  
ATOM   1381  C   PHE A 185      46.262  65.102 131.967  1.00 55.61           C  
ANISOU 1381  C   PHE A 185     9062   6406   5661    -29    514   1442       C  
ATOM   1382  O   PHE A 185      45.057  65.321 132.228  1.00 55.43           O  
ANISOU 1382  O   PHE A 185     9036   6396   5626      5    518   1499       O  
ATOM   1383  CB  PHE A 185      48.175  65.022 133.648  1.00 56.02           C  
ANISOU 1383  CB  PHE A 185     9143   6378   5763    -13    494   1292       C  
ATOM   1384  CG  PHE A 185      47.638  66.206 134.412  1.00 56.50           C  
ANISOU 1384  CG  PHE A 185     9223   6388   5855     34    510   1312       C  
ATOM   1385  CD1 PHE A 185      46.540  66.079 135.257  1.00 56.56           C  
ANISOU 1385  CD1 PHE A 185     9241   6405   5844     84    507   1335       C  
ATOM   1386  CD2 PHE A 185      48.256  67.449 134.306  1.00 57.08           C  
ANISOU 1386  CD2 PHE A 185     9304   6403   5978     28    527   1305       C  
ATOM   1387  CE1 PHE A 185      46.054  67.171 135.961  1.00 57.08           C  
ANISOU 1387  CE1 PHE A 185     9325   6424   5936    134    524   1348       C  
ATOM   1388  CE2 PHE A 185      47.776  68.543 135.010  1.00 57.44           C  
ANISOU 1388  CE2 PHE A 185     9374   6394   6054     75    541   1318       C  
ATOM   1389  CZ  PHE A 185      46.672  68.404 135.838  1.00 57.44           C  
ANISOU 1389  CZ  PHE A 185     9384   6405   6033    131    540   1337       C  
ATOM   1390  N   PHE A 186      46.881  65.598 130.891  1.00 55.65           N  
ANISOU 1390  N   PHE A 186     9055   6411   5678    -71    530   1456       N  
ATOM   1391  CA  PHE A 186      46.184  66.512 129.959  1.00 55.86           C  
ANISOU 1391  CA  PHE A 186     9070   6445   5706    -77    551   1544       C  
ATOM   1392  C   PHE A 186      45.080  65.858 129.117  1.00 55.83           C  
ANISOU 1392  C   PHE A 186     9047   6515   5649    -92    543   1613       C  
ATOM   1393  O   PHE A 186      44.070  66.510 128.835  1.00 55.65           O  
ANISOU 1393  O   PHE A 186     9016   6501   5627    -71    553   1691       O  
ATOM   1394  CB  PHE A 186      47.161  67.249 129.023  1.00 55.91           C  
ANISOU 1394  CB  PHE A 186     9071   6434   5738   -123    571   1546       C  
ATOM   1395  CG  PHE A 186      48.087  68.234 129.707  1.00 56.05           C  
ANISOU 1395  CG  PHE A 186     9106   6373   5816   -113    581   1500       C  
ATOM   1396  CD1 PHE A 186      47.789  68.819 130.949  1.00 56.06           C  
ANISOU 1396  CD1 PHE A 186     9132   6316   5851    -58    579   1480       C  
ATOM   1397  CD2 PHE A 186      49.262  68.617 129.066  1.00 56.28           C  
ANISOU 1397  CD2 PHE A 186     9125   6389   5867   -163    594   1478       C  
ATOM   1398  CE1 PHE A 186      48.660  69.726 131.534  1.00 56.26           C  
ANISOU 1398  CE1 PHE A 186     9176   6268   5931    -55    585   1434       C  
ATOM   1399  CE2 PHE A 186      50.131  69.529 129.646  1.00 56.54           C  
ANISOU 1399  CE2 PHE A 186     9172   6351   5957   -162    601   1437       C  
ATOM   1400  CZ  PHE A 186      49.831  70.082 130.884  1.00 56.56           C  
ANISOU 1400  CZ  PHE A 186     9203   6291   5993   -109    594   1414       C  
ATOM   1401  N   VAL A 187      45.264  64.598 128.709  1.00 55.84           N  
ANISOU 1401  N   VAL A 187     9040   6567   5606   -127    524   1586       N  
ATOM   1402  CA  VAL A 187      44.234  63.897 127.916  1.00 55.97           C  
ANISOU 1402  CA  VAL A 187     9040   6655   5569   -148    511   1646       C  
ATOM   1403  C   VAL A 187      43.275  63.058 128.772  1.00 55.85           C  
ANISOU 1403  C   VAL A 187     9027   6662   5531   -119    488   1651       C  
ATOM   1404  O   VAL A 187      42.061  63.102 128.560  1.00 55.91           O  
ANISOU 1404  O   VAL A 187     9018   6707   5516   -109    484   1724       O  
ATOM   1405  CB  VAL A 187      44.848  63.021 126.800  1.00 55.78           C  
ANISOU 1405  CB  VAL A 187     9010   6679   5504   -208    503   1623       C  
ATOM   1406  CG1 VAL A 187      43.768  62.265 126.035  1.00 55.82           C  
ANISOU 1406  CG1 VAL A 187     9002   6755   5451   -233    484   1680       C  
ATOM   1407  CG2 VAL A 187      45.662  63.877 125.838  1.00 56.13           C  
ANISOU 1407  CG2 VAL A 187     9047   6715   5563   -241    530   1633       C  
ATOM   1408  N   TRP A 188      43.810  62.295 129.723  1.00 55.88           N  
ANISOU 1408  N   TRP A 188     9048   6645   5539   -108    471   1578       N  
ATOM   1409  CA  TRP A 188      43.005  61.293 130.439  1.00 56.06           C  
ANISOU 1409  CA  TRP A 188     9073   6694   5531    -93    446   1580       C  
ATOM   1410  C   TRP A 188      42.598  61.652 131.880  1.00 56.32           C  
ANISOU 1410  C   TRP A 188     9117   6694   5587    -34    449   1572       C  
ATOM   1411  O   TRP A 188      41.820  60.913 132.494  1.00 55.87           O  
ANISOU 1411  O   TRP A 188     9060   6664   5505    -22    432   1586       O  
ATOM   1412  CB  TRP A 188      43.707  59.931 130.382  1.00 55.72           C  
ANISOU 1412  CB  TRP A 188     9042   6663   5463   -126    418   1515       C  
ATOM   1413  CG  TRP A 188      43.780  59.399 128.990  1.00 55.67           C  
ANISOU 1413  CG  TRP A 188     9026   6704   5420   -181    412   1529       C  
ATOM   1414  CD1 TRP A 188      44.896  59.268 128.212  1.00 55.55           C  
ANISOU 1414  CD1 TRP A 188     9012   6687   5405   -215    419   1482       C  
ATOM   1415  CD2 TRP A 188      42.684  58.956 128.195  1.00 55.88           C  
ANISOU 1415  CD2 TRP A 188     9038   6791   5401   -210    399   1596       C  
ATOM   1416  NE1 TRP A 188      44.561  58.758 126.983  1.00 55.56           N  
ANISOU 1416  NE1 TRP A 188     9005   6743   5359   -260    412   1512       N  
ATOM   1417  CE2 TRP A 188      43.208  58.557 126.945  1.00 55.78           C  
ANISOU 1417  CE2 TRP A 188     9024   6810   5360   -261    397   1582       C  
ATOM   1418  CE3 TRP A 188      41.303  58.872 128.410  1.00 56.19           C  
ANISOU 1418  CE3 TRP A 188     9062   6865   5420   -199    388   1668       C  
ATOM   1419  CZ2 TRP A 188      42.399  58.075 125.912  1.00 56.08           C  
ANISOU 1419  CZ2 TRP A 188     9051   6908   5346   -302    382   1634       C  
ATOM   1420  CZ3 TRP A 188      40.496  58.385 127.383  1.00 56.46           C  
ANISOU 1420  CZ3 TRP A 188     9081   6962   5408   -242    372   1723       C  
ATOM   1421  CH2 TRP A 188      41.049  57.988 126.152  1.00 56.37           C  
ANISOU 1421  CH2 TRP A 188     9073   6978   5366   -293    367   1704       C  
ATOM   1422  N   VAL A 189      43.111  62.762 132.420  1.00 56.97           N  
ANISOU 1422  N   VAL A 189     9211   6718   5715      0    471   1550       N  
ATOM   1423  CA  VAL A 189      42.605  63.280 133.707  1.00 57.69           C  
ANISOU 1423  CA  VAL A 189     9313   6779   5824     60    480   1548       C  
ATOM   1424  C   VAL A 189      41.787  64.578 133.555  1.00 58.67           C  
ANISOU 1424  C   VAL A 189     9427   6891   5972     98    509   1616       C  
ATOM   1425  O   VAL A 189      40.599  64.588 133.894  1.00 59.21           O  
ANISOU 1425  O   VAL A 189     9480   6990   6023    131    513   1669       O  
ATOM   1426  CB  VAL A 189      43.733  63.464 134.754  1.00 57.65           C  
ANISOU 1426  CB  VAL A 189     9337   6714   5851     79    476   1460       C  
ATOM   1427  CG1 VAL A 189      43.183  64.014 136.071  1.00 57.61           C  
ANISOU 1427  CG1 VAL A 189     9348   6682   5857    143    486   1456       C  
ATOM   1428  CG2 VAL A 189      44.467  62.145 134.996  1.00 57.34           C  
ANISOU 1428  CG2 VAL A 189     9307   6688   5790     52    445   1397       C  
ATOM   1429  N   LEU A 190      42.397  65.658 133.056  1.00 59.31           N  
ANISOU 1429  N   LEU A 190     9514   6926   6092     93    528   1616       N  
ATOM   1430  CA  LEU A 190      41.717  66.982 133.093  1.00 59.99           C  
ANISOU 1430  CA  LEU A 190     9599   6982   6210    139    554   1671       C  
ATOM   1431  C   LEU A 190      40.335  67.071 132.393  1.00 60.75           C  
ANISOU 1431  C   LEU A 190     9662   7135   6282    149    560   1772       C  
ATOM   1432  O   LEU A 190      39.373  67.619 132.976  1.00 61.14           O  
ANISOU 1432  O   LEU A 190     9705   7182   6340    208    574   1811       O  
ATOM   1433  CB  LEU A 190      42.634  68.101 132.584  1.00 60.09           C  
ANISOU 1433  CB  LEU A 190     9626   6933   6270    123    571   1661       C  
ATOM   1434  CG  LEU A 190      43.741  68.581 133.531  1.00 60.00           C  
ANISOU 1434  CG  LEU A 190     9648   6847   6301    136    573   1575       C  
ATOM   1435  CD1 LEU A 190      44.619  69.609 132.823  1.00 60.22           C  
ANISOU 1435  CD1 LEU A 190     9683   6822   6373    105    587   1576       C  
ATOM   1436  CD2 LEU A 190      43.173  69.154 134.824  1.00 60.14           C  
ANISOU 1436  CD2 LEU A 190     9688   6826   6337    209    582   1560       C  
ATOM   1437  N   PRO A 191      40.224  66.541 131.155  1.00 61.37           N  
ANISOU 1437  N   PRO A 191     9719   7269   6329     94    548   1814       N  
ATOM   1438  CA  PRO A 191      38.921  66.624 130.477  1.00 62.30           C  
ANISOU 1438  CA  PRO A 191     9802   7445   6421    100    548   1911       C  
ATOM   1439  C   PRO A 191      37.783  65.856 131.173  1.00 63.36           C  
ANISOU 1439  C   PRO A 191     9916   7634   6523    127    536   1936       C  
ATOM   1440  O   PRO A 191      36.677  66.424 131.312  1.00 64.27           O  
ANISOU 1440  O   PRO A 191    10007   7767   6644    174    549   2003       O  
ATOM   1441  CB  PRO A 191      39.207  66.106 129.057  1.00 61.97           C  
ANISOU 1441  CB  PRO A 191     9747   7452   6346     28    534   1936       C  
ATOM   1442  CG  PRO A 191      40.690  66.171 128.900  1.00 61.60           C  
ANISOU 1442  CG  PRO A 191     9726   7359   6320     -5    538   1861       C  
ATOM   1443  CD  PRO A 191      41.273  66.005 130.265  1.00 61.25           C  
ANISOU 1443  CD  PRO A 191     9707   7264   6299     27    537   1778       C  
ATOM   1444  N   PRO A 192      38.035  64.601 131.626  1.00 64.02           N  
ANISOU 1444  N   PRO A 192    10007   7741   6575     99    513   1885       N  
ATOM   1445  CA  PRO A 192      37.029  63.972 132.488  1.00 64.64           C  
ANISOU 1445  CA  PRO A 192    10070   7861   6628    127    505   1904       C  
ATOM   1446  C   PRO A 192      36.637  64.817 133.699  1.00 66.07           C  
ANISOU 1446  C   PRO A 192    10258   8006   6839    206    532   1899       C  
ATOM   1447  O   PRO A 192      35.440  64.973 133.964  1.00 66.70           O  
ANISOU 1447  O   PRO A 192    10307   8127   6908    245    542   1961       O  
ATOM   1448  CB  PRO A 192      37.710  62.677 132.937  1.00 63.90           C  
ANISOU 1448  CB  PRO A 192     9999   7771   6510     90    478   1833       C  
ATOM   1449  CG  PRO A 192      38.574  62.318 131.788  1.00 63.74           C  
ANISOU 1449  CG  PRO A 192     9985   7752   6481     28    464   1811       C  
ATOM   1450  CD  PRO A 192      39.053  63.618 131.195  1.00 63.73           C  
ANISOU 1450  CD  PRO A 192     9986   7708   6517     38    490   1824       C  
ATOM   1451  N   LEU A 193      37.631  65.366 134.404  1.00 67.33           N  
ANISOU 1451  N   LEU A 193    10456   8092   7034    230    544   1826       N  
ATOM   1452  CA  LEU A 193      37.378  66.193 135.593  1.00 68.70           C  
ANISOU 1452  CA  LEU A 193    10644   8223   7233    305    569   1807       C  
ATOM   1453  C   LEU A 193      36.517  67.405 135.263  1.00 69.91           C  
ANISOU 1453  C   LEU A 193    10778   8370   7414    356    597   1878       C  
ATOM   1454  O   LEU A 193      35.489  67.637 135.920  1.00 70.48           O  
ANISOU 1454  O   LEU A 193    10832   8466   7481    415    614   1913       O  
ATOM   1455  CB  LEU A 193      38.684  66.656 136.246  1.00 68.91           C  
ANISOU 1455  CB  LEU A 193    10717   8169   7296    312    572   1715       C  
ATOM   1456  CG  LEU A 193      39.550  65.592 136.923  1.00 69.14           C  
ANISOU 1456  CG  LEU A 193    10769   8196   7304    284    546   1636       C  
ATOM   1457  CD1 LEU A 193      40.881  66.204 137.335  1.00 69.43           C  
ANISOU 1457  CD1 LEU A 193    10843   8154   7381    285    547   1555       C  
ATOM   1458  CD2 LEU A 193      38.847  64.972 138.124  1.00 69.40           C  
ANISOU 1458  CD2 LEU A 193    10802   8262   7305    321    543   1630       C  
ATOM   1459  N   LEU A 194      36.926  68.157 134.240  1.00 70.85           N  
ANISOU 1459  N   LEU A 194    10899   8457   7561    334    601   1903       N  
ATOM   1460  CA  LEU A 194      36.163  69.345 133.835  1.00 72.33           C  
ANISOU 1460  CA  LEU A 194    11071   8630   7779    382    625   1976       C  
ATOM   1461  C   LEU A 194      34.739  68.983 133.357  1.00 72.92           C  
ANISOU 1461  C   LEU A 194    11091   8792   7820    391    621   2071       C  
ATOM   1462  O   LEU A 194      33.740  69.639 133.754  1.00 73.58           O  
ANISOU 1462  O   LEU A 194    11154   8884   7918    461    642   2119       O  
ATOM   1463  CB  LEU A 194      36.921  70.137 132.768  1.00 72.94           C  
ANISOU 1463  CB  LEU A 194    11163   8660   7891    347    627   1990       C  
ATOM   1464  CG  LEU A 194      38.263  70.744 133.215  1.00 73.30           C  
ANISOU 1464  CG  LEU A 194    11257   8613   7979    341    634   1906       C  
ATOM   1465  CD1 LEU A 194      38.965  71.408 132.037  1.00 73.84           C  
ANISOU 1465  CD1 LEU A 194    11332   8649   8074    294    636   1931       C  
ATOM   1466  CD2 LEU A 194      38.097  71.727 134.368  1.00 73.66           C  
ANISOU 1466  CD2 LEU A 194    11332   8589   8065    421    657   1875       C  
ATOM   1467  N   LEU A 195      34.651  67.922 132.545  1.00 72.63           N  
ANISOU 1467  N   LEU A 195    11031   8824   7739    322    593   2095       N  
ATOM   1468  CA  LEU A 195      33.350  67.418 132.082  1.00 72.65           C  
ANISOU 1468  CA  LEU A 195    10980   8917   7705    317    581   2182       C  
ATOM   1469  C   LEU A 195      32.423  67.027 133.254  1.00 73.07           C  
ANISOU 1469  C   LEU A 195    11012   9010   7741    367    590   2186       C  
ATOM   1470  O   LEU A 195      31.236  67.399 133.274  1.00 73.93           O  
ANISOU 1470  O   LEU A 195    11076   9162   7848    413    603   2260       O  
ATOM   1471  CB  LEU A 195      33.546  66.230 131.134  1.00 72.07           C  
ANISOU 1471  CB  LEU A 195    10896   8903   7584    227    546   2188       C  
ATOM   1472  CG  LEU A 195      32.305  65.617 130.465  1.00 72.14           C  
ANISOU 1472  CG  LEU A 195    10851   9008   7549    202    524   2275       C  
ATOM   1473  CD1 LEU A 195      31.462  66.662 129.753  1.00 72.88           C  
ANISOU 1473  CD1 LEU A 195    10908   9120   7661    237    536   2371       C  
ATOM   1474  CD2 LEU A 195      32.722  64.526 129.492  1.00 71.74           C  
ANISOU 1474  CD2 LEU A 195    10803   8998   7454    111    489   2264       C  
ATOM   1475  N   MET A 196      32.983  66.293 134.220  1.00 72.56           N  
ANISOU 1475  N   MET A 196    10976   8930   7662    359    584   2109       N  
ATOM   1476  CA  MET A 196      32.263  65.922 135.447  1.00 72.61           C  
ANISOU 1476  CA  MET A 196    10970   8968   7650    404    595   2104       C  
ATOM   1477  C   MET A 196      31.833  67.143 136.261  1.00 73.54           C  
ANISOU 1477  C   MET A 196    11090   9047   7802    500    636   2108       C  
ATOM   1478  O   MET A 196      30.672  67.230 136.691  1.00 74.18           O  
ANISOU 1478  O   MET A 196    11130   9182   7871    550    654   2160       O  
ATOM   1479  CB  MET A 196      33.119  65.017 136.336  1.00 71.85           C  
ANISOU 1479  CB  MET A 196    10913   8850   7534    378    580   2016       C  
ATOM   1480  CG  MET A 196      33.135  63.563 135.928  1.00 71.13           C  
ANISOU 1480  CG  MET A 196    10813   8814   7399    300    541   2019       C  
ATOM   1481  SD  MET A 196      34.015  62.566 137.139  1.00 70.81           S  
ANISOU 1481  SD  MET A 196    10817   8745   7340    286    524   1925       S  
ATOM   1482  CE  MET A 196      35.716  62.867 136.673  1.00 70.03           C  
ANISOU 1482  CE  MET A 196    10768   8562   7276    256    514   1840       C  
ATOM   1483  N   VAL A 197      32.775  68.069 136.468  1.00 74.00           N  
ANISOU 1483  N   VAL A 197    11196   9014   7904    525    651   2050       N  
ATOM   1484  CA  VAL A 197      32.480  69.355 137.127  1.00 75.08           C  
ANISOU 1484  CA  VAL A 197    11346   9097   8081    616    688   2046       C  
ATOM   1485  C   VAL A 197      31.327  70.091 136.429  1.00 76.35           C  
ANISOU 1485  C   VAL A 197    11458   9291   8258    659    704   2146       C  
ATOM   1486  O   VAL A 197      30.459  70.649 137.103  1.00 77.08           O  
ANISOU 1486  O   VAL A 197    11533   9394   8360    740    734   2169       O  
ATOM   1487  CB  VAL A 197      33.735  70.266 137.215  1.00 74.62           C  
ANISOU 1487  CB  VAL A 197    11347   8930   8072    620    694   1974       C  
ATOM   1488  CG1 VAL A 197      33.375  71.702 137.598  1.00 75.09           C  
ANISOU 1488  CG1 VAL A 197    11422   8927   8180    708    728   1983       C  
ATOM   1489  CG2 VAL A 197      34.735  69.699 138.214  1.00 74.00           C  
ANISOU 1489  CG2 VAL A 197    11314   8820   7982    601    683   1873       C  
ATOM   1490  N   LEU A 198      31.315  70.080 135.095  1.00 77.31           N  
ANISOU 1490  N   LEU A 198    11559   9433   8380    607    684   2206       N  
ATOM   1491  CA  LEU A 198      30.195  70.686 134.358  1.00 79.21           C  
ANISOU 1491  CA  LEU A 198    11748   9714   8631    642    692   2309       C  
ATOM   1492  C   LEU A 198      28.863  69.913 134.551  1.00 79.85           C  
ANISOU 1492  C   LEU A 198    11763   9906   8669    653    689   2374       C  
ATOM   1493  O   LEU A 198      27.795  70.510 134.864  1.00 81.00           O  
ANISOU 1493  O   LEU A 198    11869  10080   8828    730    714   2429       O  
ATOM   1494  CB  LEU A 198      30.537  70.795 132.871  1.00 79.97           C  
ANISOU 1494  CB  LEU A 198    11840   9812   8731    577    668   2358       C  
ATOM   1495  CG  LEU A 198      29.763  71.861 132.087  1.00 81.46           C  
ANISOU 1495  CG  LEU A 198    11998  10000   8950    622    677   2453       C  
ATOM   1496  CD1 LEU A 198      30.220  73.269 132.461  1.00 81.83           C  
ANISOU 1496  CD1 LEU A 198    12091   9936   9062    690    707   2426       C  
ATOM   1497  CD2 LEU A 198      29.909  71.627 130.588  1.00 81.51           C  
ANISOU 1497  CD2 LEU A 198    11988  10043   8937    544    647   2512       C  
ATOM   1498  N   ILE A 199      28.946  68.589 134.371  1.00 80.06           N  
ANISOU 1498  N   ILE A 199    11777   9993   8646    574    657   2366       N  
ATOM   1499  CA  ILE A 199      27.776  67.707 134.518  1.00 80.31           C  
ANISOU 1499  CA  ILE A 199    11747  10131   8634    564    648   2425       C  
ATOM   1500  C   ILE A 199      27.055  67.927 135.857  1.00 81.28           C  
ANISOU 1500  C   ILE A 199    11853  10272   8757    648    684   2417       C  
ATOM   1501  O   ILE A 199      25.819  68.027 135.889  1.00 81.64           O  
ANISOU 1501  O   ILE A 199    11835  10390   8794    689    697   2494       O  
ATOM   1502  CB  ILE A 199      28.160  66.213 134.353  1.00 79.34           C  
ANISOU 1502  CB  ILE A 199    11632  10050   8462    468    608   2396       C  
ATOM   1503  CG1 ILE A 199      28.456  65.895 132.884  1.00 78.84           C  
ANISOU 1503  CG1 ILE A 199    11564  10004   8385    387    572   2428       C  
ATOM   1504  CG2 ILE A 199      27.059  65.283 134.857  1.00 79.69           C  
ANISOU 1504  CG2 ILE A 199    11623  10189   8463    460    601   2440       C  
ATOM   1505  CD1 ILE A 199      29.372  64.704 132.686  1.00 78.13           C  
ANISOU 1505  CD1 ILE A 199    11511   9910   8265    300    539   2365       C  
ATOM   1506  N   TYR A 200      27.825  67.998 136.951  1.00 82.01           N  
ANISOU 1506  N   TYR A 200    12000  10302   8856    674    701   2325       N  
ATOM   1507  CA  TYR A 200      27.222  68.178 138.276  1.00 83.60           C  
ANISOU 1507  CA  TYR A 200    12193  10521   9051    753    738   2309       C  
ATOM   1508  C   TYR A 200      26.530  69.535 138.413  1.00 85.19           C  
ANISOU 1508  C   TYR A 200    12375  10700   9293    857    779   2345       C  
ATOM   1509  O   TYR A 200      25.367  69.577 138.811  1.00 86.71           O  
ANISOU 1509  O   TYR A 200    12510  10963   9471    912    803   2400       O  
ATOM   1510  CB  TYR A 200      28.231  67.926 139.412  1.00 83.12           C  
ANISOU 1510  CB  TYR A 200    12198  10401   8982    754    742   2201       C  
ATOM   1511  CG  TYR A 200      28.429  66.451 139.699  1.00 82.39           C  
ANISOU 1511  CG  TYR A 200    12105  10359   8838    678    711   2181       C  
ATOM   1512  CD1 TYR A 200      27.385  65.675 140.202  1.00 82.68           C  
ANISOU 1512  CD1 TYR A 200    12091  10489   8831    678    715   2229       C  
ATOM   1513  CD2 TYR A 200      29.649  65.828 139.459  1.00 81.78           C  
ANISOU 1513  CD2 TYR A 200    12077  10235   8758    607    677   2116       C  
ATOM   1514  CE1 TYR A 200      27.551  64.321 140.463  1.00 82.21           C  
ANISOU 1514  CE1 TYR A 200    12036  10469   8727    607    683   2214       C  
ATOM   1515  CE2 TYR A 200      29.829  64.476 139.718  1.00 81.46           C  
ANISOU 1515  CE2 TYR A 200    12041  10233   8674    542    646   2098       C  
ATOM   1516  CZ  TYR A 200      28.777  63.722 140.221  1.00 81.71           C  
ANISOU 1516  CZ  TYR A 200    12028  10351   8664    541    648   2148       C  
ATOM   1517  OH  TYR A 200      28.953  62.379 140.467  1.00 81.63           O  
ANISOU 1517  OH  TYR A 200    12026  10373   8614    473    614   2134       O  
ATOM   1518  N   LEU A 201      27.208  70.622 138.031  1.00 85.57           N  
ANISOU 1518  N   LEU A 201    12467  10652   9393    883    786   2321       N  
ATOM   1519  CA  LEU A 201      26.573  71.948 137.968  1.00 87.11           C  
ANISOU 1519  CA  LEU A 201    12648  10816   9634    979    819   2363       C  
ATOM   1520  C   LEU A 201      25.212  71.876 137.261  1.00 88.59           C  
ANISOU 1520  C   LEU A 201    12747  11101   9810    995    818   2480       C  
ATOM   1521  O   LEU A 201      24.186  72.366 137.794  1.00 90.00           O  
ANISOU 1521  O   LEU A 201    12883  11316   9996   1085    853   2518       O  
ATOM   1522  CB  LEU A 201      27.476  72.971 137.260  1.00 86.80           C  
ANISOU 1522  CB  LEU A 201    12660  10667   9649    975    814   2345       C  
ATOM   1523  CG  LEU A 201      28.698  73.481 138.024  1.00 86.64           C  
ANISOU 1523  CG  LEU A 201    12724  10536   9658    987    824   2235       C  
ATOM   1524  CD1 LEU A 201      29.730  74.073 137.071  1.00 86.09           C  
ANISOU 1524  CD1 LEU A 201    12697  10381   9630    938    804   2225       C  
ATOM   1525  CD2 LEU A 201      28.288  74.497 139.080  1.00 87.51           C  
ANISOU 1525  CD2 LEU A 201    12854  10598   9797   1102    868   2204       C  
ATOM   1526  N   GLU A 202      25.201  71.227 136.092  1.00 89.14           N  
ANISOU 1526  N   GLU A 202    12790  11219   9860    908    777   2535       N  
ATOM   1527  CA  GLU A 202      23.938  71.000 135.379  1.00 90.69           C  
ANISOU 1527  CA  GLU A 202    12900  11519  10038    906    765   2647       C  
ATOM   1528  C   GLU A 202      22.919  70.174 136.208  1.00 91.19           C  
ANISOU 1528  C   GLU A 202    12902  11686  10057    921    778   2671       C  
ATOM   1529  O   GLU A 202      21.709  70.529 136.279  1.00 92.17           O  
ANISOU 1529  O   GLU A 202    12955  11878  10185    986    799   2746       O  
ATOM   1530  CB  GLU A 202      24.197  70.328 134.025  1.00 91.29           C  
ANISOU 1530  CB  GLU A 202    12965  11629  10090    799    715   2689       C  
ATOM   1531  CG  GLU A 202      23.015  70.377 133.045  1.00 92.63           C  
ANISOU 1531  CG  GLU A 202    13053  11890  10252    798    697   2810       C  
ATOM   1532  CD  GLU A 202      22.620  71.789 132.616  1.00 93.90           C  
ANISOU 1532  CD  GLU A 202    13201  12008  10466    883    717   2868       C  
ATOM   1533  OE1 GLU A 202      23.506  72.661 132.508  1.00 94.71           O  
ANISOU 1533  OE1 GLU A 202    13368  12004  10612    904    728   2825       O  
ATOM   1534  OE2 GLU A 202      21.421  72.018 132.373  1.00 94.50           O  
ANISOU 1534  OE2 GLU A 202    13202  12159  10543    929    721   2960       O  
ATOM   1535  N   VAL A 203      23.410  69.099 136.840  1.00 90.81           N  
ANISOU 1535  N   VAL A 203    12881  11653   9969    862    765   2609       N  
ATOM   1536  CA  VAL A 203      22.549  68.238 137.667  1.00 90.93           C  
ANISOU 1536  CA  VAL A 203    12846  11764   9939    863    775   2629       C  
ATOM   1537  C   VAL A 203      21.884  69.035 138.794  1.00 91.72           C  
ANISOU 1537  C   VAL A 203    12927  11868  10053    983    833   2623       C  
ATOM   1538  O   VAL A 203      20.679  68.887 139.034  1.00 92.71           O  
ANISOU 1538  O   VAL A 203    12974  12090  10160   1018    851   2692       O  
ATOM   1539  CB  VAL A 203      23.313  67.013 138.243  1.00 90.24           C  
ANISOU 1539  CB  VAL A 203    12802  11674   9809    785    752   2558       C  
ATOM   1540  CG1 VAL A 203      22.481  66.270 139.299  1.00 90.56           C  
ANISOU 1540  CG1 VAL A 203    12800  11800   9806    797    770   2573       C  
ATOM   1541  CG2 VAL A 203      23.730  66.060 137.122  1.00 89.53           C  
ANISOU 1541  CG2 VAL A 203    12717  11602   9698    668    696   2574       C  
ATOM   1542  N   PHE A 204      22.664  69.880 139.468  1.00 92.08           N  
ANISOU 1542  N   PHE A 204    13042  11811  10130   1044    861   2540       N  
ATOM   1543  CA  PHE A 204      22.137  70.765 140.508  1.00 93.22           C  
ANISOU 1543  CA  PHE A 204    13182  11945  10291   1164    918   2522       C  
ATOM   1544  C   PHE A 204      21.155  71.763 139.915  1.00 94.72           C  
ANISOU 1544  C   PHE A 204    13314  12154  10521   1244    938   2607       C  
ATOM   1545  O   PHE A 204      20.021  71.890 140.419  1.00 96.44           O  
ANISOU 1545  O   PHE A 204    13464  12450  10727   1316    973   2655       O  
ATOM   1546  CB  PHE A 204      23.270  71.512 141.234  1.00 92.80           C  
ANISOU 1546  CB  PHE A 204    13224  11766  10266   1204    936   2411       C  
ATOM   1547  CG  PHE A 204      24.150  70.616 142.069  1.00 91.77           C  
ANISOU 1547  CG  PHE A 204    13149  11623  10097   1147    923   2324       C  
ATOM   1548  CD1 PHE A 204      23.615  69.914 143.153  1.00 91.71           C  
ANISOU 1548  CD1 PHE A 204    13116  11691  10036   1162    944   2315       C  
ATOM   1549  CD2 PHE A 204      25.509  70.481 141.785  1.00 90.84           C  
ANISOU 1549  CD2 PHE A 204    13103  11418   9992   1080    890   2254       C  
ATOM   1550  CE1 PHE A 204      24.415  69.087 143.922  1.00 91.02           C  
ANISOU 1550  CE1 PHE A 204    13080  11591   9913   1111    928   2240       C  
ATOM   1551  CE2 PHE A 204      26.309  69.654 142.555  1.00 90.24           C  
ANISOU 1551  CE2 PHE A 204    13073  11331   9881   1033    875   2177       C  
ATOM   1552  CZ  PHE A 204      25.764  68.965 143.633  1.00 90.30           C  
ANISOU 1552  CZ  PHE A 204    13060  11411   9837   1049    893   2170       C  
ATOM   1553  N   TYR A 205      21.585  72.442 138.841  1.00103.60           N  
ANISOU 1553  N   TYR A 205    11362  11058  16940   2457     88    153       N  
ATOM   1554  CA  TYR A 205      20.720  73.410 138.146  1.00103.64           C  
ANISOU 1554  CA  TYR A 205    11412  11060  16906   2497     82    147       C  
ATOM   1555  C   TYR A 205      19.332  72.830 137.838  1.00103.93           C  
ANISOU 1555  C   TYR A 205    11428  11105  16954   2530     38    123       C  
ATOM   1556  O   TYR A 205      18.310  73.470 138.155  1.00104.05           O  
ANISOU 1556  O   TYR A 205    11449  11121  16961   2545     27    122       O  
ATOM   1557  CB  TYR A 205      21.369  73.928 136.851  1.00103.94           C  
ANISOU 1557  CB  TYR A 205    11502  11089  16900   2523    101    146       C  
ATOM   1558  CG  TYR A 205      20.382  74.645 135.941  1.00104.28           C  
ANISOU 1558  CG  TYR A 205    11585  11129  16905   2572     87    135       C  
ATOM   1559  CD1 TYR A 205      19.845  75.884 136.298  1.00104.49           C  
ANISOU 1559  CD1 TYR A 205    11641  11151  16908   2579     97    145       C  
ATOM   1560  CD2 TYR A 205      19.966  74.069 134.738  1.00104.53           C  
ANISOU 1560  CD2 TYR A 205    11625  11165  16926   2611     62    112       C  
ATOM   1561  CE1 TYR A 205      18.929  76.531 135.478  1.00104.83           C  
ANISOU 1561  CE1 TYR A 205    11721  11193  16917   2624     84    134       C  
ATOM   1562  CE2 TYR A 205      19.050  74.707 133.912  1.00104.79           C  
ANISOU 1562  CE2 TYR A 205    11694  11196  16924   2656     48    101       C  
ATOM   1563  CZ  TYR A 205      18.529  75.936 134.288  1.00105.04           C  
ANISOU 1563  CZ  TYR A 205    11754  11222  16932   2663     59    112       C  
ATOM   1564  OH  TYR A 205      17.626  76.585 133.477  1.00105.83           O  
ANISOU 1564  OH  TYR A 205    11891  11320  16997   2708     45    101       O  
ATOM   1565  N   LEU A 206      19.307  71.632 137.233  1.00104.62           N  
ANISOU 1565  N   LEU A 206    11491  11200  17060   2541     15    105       N  
ATOM   1566  CA  LEU A 206      18.022  70.983 136.917  1.00105.37           C  
ANISOU 1566  CA  LEU A 206    11563  11303  17168   2571    -27     80       C  
ATOM   1567  C   LEU A 206      17.127  70.766 138.167  1.00105.88           C  
ANISOU 1567  C   LEU A 206    11586  11375  17269   2553    -45     81       C  
ATOM   1568  O   LEU A 206      15.928  71.141 138.187  1.00106.11           O  
ANISOU 1568  O   LEU A 206    11617  11406  17290   2577    -67     72       O  
ATOM   1569  CB  LEU A 206      18.246  69.653 136.191  1.00105.25           C  
ANISOU 1569  CB  LEU A 206    11524  11294  17172   2580    -47     61       C  
ATOM   1570  CG  LEU A 206      18.184  69.631 134.655  1.00105.51           C  
ANISOU 1570  CG  LEU A 206    11592  11325  17170   2624    -56     44       C  
ATOM   1571  CD1 LEU A 206      19.063  70.686 134.003  1.00105.67           C  
ANISOU 1571  CD1 LEU A 206    11669  11334  17146   2631    -20     59       C  
ATOM   1572  CD2 LEU A 206      18.543  68.244 134.140  1.00105.72           C  
ANISOU 1572  CD2 LEU A 206    11588  11358  17222   2624    -73     28       C  
ATOM   1573  N   ILE A 207      17.737  70.181 139.200  1.00106.32           N  
ANISOU 1573  N   ILE A 207    11602  11433  17362   2509    -36     93       N  
ATOM   1574  CA  ILE A 207      17.016  69.821 140.423  1.00106.87           C  
ANISOU 1574  CA  ILE A 207    11626  11508  17469   2488    -53     94       C  
ATOM   1575  C   ILE A 207      16.504  71.069 141.145  1.00107.34           C  
ANISOU 1575  C   ILE A 207    11706  11564  17513   2484    -41    108       C  
ATOM   1576  O   ILE A 207      15.336  71.112 141.560  1.00108.10           O  
ANISOU 1576  O   ILE A 207    11786  11665  17620   2495    -64    100       O  
ATOM   1577  CB  ILE A 207      17.868  68.949 141.383  1.00106.70           C  
ANISOU 1577  CB  ILE A 207    11560  11490  17490   2441    -43    104       C  
ATOM   1578  CG1 ILE A 207      18.180  67.586 140.741  1.00106.62           C  
ANISOU 1578  CG1 ILE A 207    11524  11486  17501   2445    -61     87       C  
ATOM   1579  CG2 ILE A 207      17.120  68.705 142.698  1.00106.58           C  
ANISOU 1579  CG2 ILE A 207    11502  11480  17511   2418    -57    107       C  
ATOM   1580  CD1 ILE A 207      19.261  66.803 141.469  1.00106.47           C  
ANISOU 1580  CD1 ILE A 207    11470  11467  17514   2402    -46     98       C  
ATOM   1581  N   ARG A 208      17.358  72.083 141.271  1.00108.02           N  
ANISOU 1581  N   ARG A 208    11828  11642  17573   2470     -4    130       N  
ATOM   1582  CA  ARG A 208      16.950  73.337 141.934  1.00108.94           C  
ANISOU 1582  CA  ARG A 208    11966  11753  17671   2466      9    145       C  
ATOM   1583  C   ARG A 208      15.796  74.022 141.177  1.00110.00           C  
ANISOU 1583  C   ARG A 208    12133  11886  17773   2513     -8    132       C  
ATOM   1584  O   ARG A 208      14.840  74.515 141.807  1.00109.50           O  
ANISOU 1584  O   ARG A 208    12064  11825  17713   2517    -19    133       O  
ATOM   1585  CB  ARG A 208      18.132  74.312 142.110  1.00108.83           C  
ANISOU 1585  CB  ARG A 208    11987  11729  17633   2444     53    169       C  
ATOM   1586  CG  ARG A 208      19.333  73.787 142.883  1.00108.64           C  
ANISOU 1586  CG  ARG A 208    11935  11704  17637   2397     75    184       C  
ATOM   1587  CD  ARG A 208      19.318  74.057 144.384  1.00108.30           C  
ANISOU 1587  CD  ARG A 208    11865  11663  17620   2359     85    202       C  
ATOM   1588  NE  ARG A 208      20.568  73.598 145.004  1.00107.90           N  
ANISOU 1588  NE  ARG A 208    11793  11612  17592   2317    108    216       N  
ATOM   1589  CZ  ARG A 208      20.778  73.439 146.314  1.00107.70           C  
ANISOU 1589  CZ  ARG A 208    11734  11589  17598   2278    115    229       C  
ATOM   1590  NH1 ARG A 208      19.821  73.695 147.208  1.00107.82           N  
ANISOU 1590  NH1 ARG A 208    11730  11606  17627   2273    102    231       N  
ATOM   1591  NH2 ARG A 208      21.966  73.012 146.740  1.00107.25           N  
ANISOU 1591  NH2 ARG A 208    11660  11531  17559   2242    136    240       N  
ATOM   1592  N   LYS A 209      15.858  74.010 139.839  1.00111.44           N  
ANISOU 1592  N   LYS A 209    12347  12067  17926   2549    -13    118       N  
ATOM   1593  CA  LYS A 209      14.769  74.551 139.018  1.00112.79           C  
ANISOU 1593  CA  LYS A 209    12548  12238  18067   2596    -33    103       C  
ATOM   1594  C   LYS A 209      13.474  73.736 139.161  1.00112.86           C  
ANISOU 1594  C   LYS A 209    12518  12258  18104   2613    -76     81       C  
ATOM   1595  O   LYS A 209      12.384  74.318 139.327  1.00112.93           O  
ANISOU 1595  O   LYS A 209    12534  12269  18104   2633    -91     76       O  
ATOM   1596  CB  LYS A 209      15.174  74.639 137.543  1.00114.18           C  
ANISOU 1596  CB  LYS A 209    12765  12409  18206   2630    -29     94       C  
ATOM   1597  CG  LYS A 209      14.264  75.542 136.715  1.00115.32           C  
ANISOU 1597  CG  LYS A 209    12954  12551  18309   2677    -39     84       C  
ATOM   1598  CD  LYS A 209      14.853  75.825 135.330  1.00116.53           C  
ANISOU 1598  CD  LYS A 209    13156  12698  18421   2707    -26     80       C  
ATOM   1599  CE  LYS A 209      14.614  74.670 134.364  1.00117.59           C  
ANISOU 1599  CE  LYS A 209    13273  12840  18565   2733    -56     54       C  
ATOM   1600  NZ  LYS A 209      13.175  74.487 134.009  1.00118.22           N  
ANISOU 1600  NZ  LYS A 209    13344  12927  18644   2771    -96     31       N  
ATOM   1601  N   GLN A 210      13.595  72.404 139.107  1.00113.18           N  
ANISOU 1601  N   GLN A 210    12516  12306  18179   2604    -95     68       N  
ATOM   1602  CA  GLN A 210      12.416  71.537 139.304  1.00113.76           C  
ANISOU 1602  CA  GLN A 210    12548  12390  18284   2616   -135     46       C  
ATOM   1603  C   GLN A 210      11.779  71.693 140.701  1.00115.02           C  
ANISOU 1603  C   GLN A 210    12675  12552  18472   2590   -140     55       C  
ATOM   1604  O   GLN A 210      10.535  71.722 140.833  1.00115.17           O  
ANISOU 1604  O   GLN A 210    12683  12578  18498   2610   -167     41       O  
ATOM   1605  CB  GLN A 210      12.747  70.071 139.019  1.00112.93           C  
ANISOU 1605  CB  GLN A 210    12404  12291  18211   2609   -153     31       C  
ATOM   1606  CG  GLN A 210      12.889  69.780 137.530  1.00112.82           C  
ANISOU 1606  CG  GLN A 210    12417  12277  18172   2647   -162     14       C  
ATOM   1607  CD  GLN A 210      13.338  68.362 137.238  1.00112.38           C  
ANISOU 1607  CD  GLN A 210    12324  12226  18146   2638   -176      1       C  
ATOM   1608  OE1 GLN A 210      12.799  67.416 137.800  1.00112.35           O  
ANISOU 1608  OE1 GLN A 210    12273  12231  18184   2626   -200     -9       O  
ATOM   1609  NE2 GLN A 210      14.316  68.205 136.344  1.00112.26           N  
ANISOU 1609  NE2 GLN A 210    12332  12207  18112   2643   -161      1       N  
ATOM   1610  N   LEU A 211      12.627  71.809 141.728  1.00116.31           N  
ANISOU 1610  N   LEU A 211    12826  12713  18654   2546   -114     78       N  
ATOM   1611  CA  LEU A 211      12.153  72.157 143.076  1.00116.98           C  
ANISOU 1611  CA  LEU A 211    12887  12799  18760   2520   -112     90       C  
ATOM   1612  C   LEU A 211      11.473  73.526 143.091  1.00118.56           C  
ANISOU 1612  C   LEU A 211    13126  12995  18925   2540   -106     97       C  
ATOM   1613  O   LEU A 211      10.382  73.672 143.658  1.00118.89           O  
ANISOU 1613  O   LEU A 211    13151  13041  18979   2546   -125     91       O  
ATOM   1614  CB  LEU A 211      13.302  72.140 144.099  1.00116.82           C  
ANISOU 1614  CB  LEU A 211    12850  12775  18759   2470    -81    115       C  
ATOM   1615  CG  LEU A 211      13.837  70.772 144.536  1.00116.97           C  
ANISOU 1615  CG  LEU A 211    12820  12800  18823   2440    -88    111       C  
ATOM   1616  CD1 LEU A 211      15.155  70.932 145.279  1.00116.87           C  
ANISOU 1616  CD1 LEU A 211    12804  12782  18817   2397    -53    136       C  
ATOM   1617  CD2 LEU A 211      12.820  70.044 145.406  1.00116.56           C  
ANISOU 1617  CD2 LEU A 211    12718  12756  18812   2432   -118    101       C  
ATOM   1618  N   ALA A1001      12.114  74.513 142.458  1.00120.62           N  
ANISOU 1618  N   ALA A1001    13439  13247  19144   2551    -79    108       N  
ATOM   1619  CA  ALA A1001      11.543  75.866 142.350  1.00121.71           C  
ANISOU 1619  CA  ALA A1001    13619  13379  19244   2573    -70    114       C  
ATOM   1620  C   ALA A1001      10.165  75.881 141.674  1.00123.49           C  
ANISOU 1620  C   ALA A1001    13852  13611  19458   2619   -105     91       C  
ATOM   1621  O   ALA A1001       9.257  76.588 142.141  1.00124.42           O  
ANISOU 1621  O   ALA A1001    13974  13729  19569   2628   -113     92       O  
ATOM   1622  CB  ALA A1001      12.499  76.797 141.614  1.00121.79           C  
ANISOU 1622  CB  ALA A1001    13684  13378  19210   2580    -37    128       C  
ATOM   1623  N   ASP A1002      10.010  75.096 140.602  1.00125.48           N  
ANISOU 1623  N   ASP A1002    14101  13866  19707   2648   -127     69       N  
ATOM   1624  CA  ASP A1002       8.726  75.022 139.875  1.00126.92           C  
ANISOU 1624  CA  ASP A1002    14288  14054  19879   2693   -162     44       C  
ATOM   1625  C   ASP A1002       7.558  74.479 140.725  1.00127.15           C  
ANISOU 1625  C   ASP A1002    14270  14093  19946   2688   -193     32       C  
ATOM   1626  O   ASP A1002       6.431  74.998 140.654  1.00127.23           O  
ANISOU 1626  O   ASP A1002    14290  14106  19944   2715   -211     22       O  
ATOM   1627  CB  ASP A1002       8.869  74.177 138.599  1.00127.85           C  
ANISOU 1627  CB  ASP A1002    14409  14175  19990   2722   -179     23       C  
ATOM   1628  CG  ASP A1002       9.729  74.845 137.531  1.00128.75           C  
ANISOU 1628  CG  ASP A1002    14578  14280  20059   2740   -154     29       C  
ATOM   1629  OD1 ASP A1002      10.369  75.885 137.807  1.00129.73           O  
ANISOU 1629  OD1 ASP A1002    14736  14395  20159   2726   -120     52       O  
ATOM   1630  OD2 ASP A1002       9.767  74.317 136.399  1.00129.35           O  
ANISOU 1630  OD2 ASP A1002    14664  14358  20124   2769   -168     12       O  
ATOM   1631  N   LEU A1003       7.828  73.447 141.522  1.00127.51           N  
ANISOU 1631  N   LEU A1003    14266  14144  20038   2653   -198     33       N  
ATOM   1632  CA  LEU A1003       6.807  72.897 142.427  1.00127.92           C  
ANISOU 1632  CA  LEU A1003    14269  14203  20128   2644   -225     24       C  
ATOM   1633  C   LEU A1003       6.362  73.899 143.494  1.00128.66           C  
ANISOU 1633  C   LEU A1003    14368  14295  20220   2628   -213     41       C  
ATOM   1634  O   LEU A1003       5.159  74.024 143.769  1.00128.84           O  
ANISOU 1634  O   LEU A1003    14379  14323  20250   2644   -237     30       O  
ATOM   1635  CB  LEU A1003       7.306  71.615 143.095  1.00127.77           C  
ANISOU 1635  CB  LEU A1003    14197  14189  20157   2607   -229     24       C  
ATOM   1636  CG  LEU A1003       7.478  70.405 142.167  1.00128.19           C  
ANISOU 1636  CG  LEU A1003    14234  14248  20223   2622   -249      3       C  
ATOM   1637  CD1 LEU A1003       8.114  69.274 142.943  1.00128.42           C  
ANISOU 1637  CD1 LEU A1003    14214  14280  20298   2582   -247      8       C  
ATOM   1638  CD2 LEU A1003       6.153  69.934 141.574  1.00128.19           C  
ANISOU 1638  CD2 LEU A1003    14220  14256  20228   2661   -289    -26       C  
ATOM   1639  N   GLU A1004       7.323  74.610 144.088  1.00130.23           N  
ANISOU 1639  N   GLU A1004    14584  14486  20409   2598   -177     68       N  
ATOM   1640  CA  GLU A1004       7.001  75.684 145.048  1.00132.04           C  
ANISOU 1640  CA  GLU A1004    14824  14712  20631   2584   -163     86       C  
ATOM   1641  C   GLU A1004       6.302  76.866 144.357  1.00134.01           C  
ANISOU 1641  C   GLU A1004    15123  14957  20835   2624   -164     82       C  
ATOM   1642  O   GLU A1004       5.428  77.507 144.957  1.00133.35           O  
ANISOU 1642  O   GLU A1004    15040  14875  20750   2628   -171     84       O  
ATOM   1643  CB  GLU A1004       8.252  76.178 145.792  1.00131.88           C  
ANISOU 1643  CB  GLU A1004    14813  14684  20610   2542   -123    115       C  
ATOM   1644  CG  GLU A1004       7.935  76.957 147.069  1.00131.75           C  
ANISOU 1644  CG  GLU A1004    14789  14666  20601   2517   -111    133       C  
ATOM   1645  CD  GLU A1004       9.125  77.715 147.636  1.00131.59           C  
ANISOU 1645  CD  GLU A1004    14789  14636  20569   2483    -69    162       C  
ATOM   1646  OE1 GLU A1004      10.265  77.213 147.545  1.00132.34           O  
ANISOU 1646  OE1 GLU A1004    14879  14729  20673   2461    -52    169       O  
ATOM   1647  OE2 GLU A1004       8.917  78.817 148.189  1.00131.36           O  
ANISOU 1647  OE2 GLU A1004    14782  14603  20523   2479    -54    176       O  
ATOM   1648  N   ASP A1005       6.687  77.145 143.107  1.00136.05           N  
ANISOU 1648  N   ASP A1005    15423  15211  21056   2654   -158     76       N  
ATOM   1649  CA  ASP A1005       5.998  78.147 142.282  1.00137.73           C  
ANISOU 1649  CA  ASP A1005    15683  15421  21225   2697   -163     69       C  
ATOM   1650  C   ASP A1005       4.527  77.760 142.066  1.00139.78           C  
ANISOU 1650  C   ASP A1005    15923  15691  21495   2730   -204     43       C  
ATOM   1651  O   ASP A1005       3.629  78.576 142.317  1.00141.22           O  
ANISOU 1651  O   ASP A1005    16120  15873  21663   2746   -211     43       O  
ATOM   1652  CB  ASP A1005       6.714  78.332 140.933  1.00137.94           C  
ANISOU 1652  CB  ASP A1005    15754  15442  21213   2724   -151     66       C  
ATOM   1653  CG  ASP A1005       6.177  79.511 140.132  1.00138.45           C  
ANISOU 1653  CG  ASP A1005    15874  15501  21228   2765   -149     63       C  
ATOM   1654  OD1 ASP A1005       6.111  80.633 140.678  1.00139.01           O  
ANISOU 1654  OD1 ASP A1005    15969  15566  21280   2758   -129     81       O  
ATOM   1655  OD2 ASP A1005       5.833  79.317 138.946  1.00138.43           O  
ANISOU 1655  OD2 ASP A1005    15891  15501  21204   2806   -166     44       O  
ATOM   1656  N   ASN A1006       4.287  76.521 141.626  1.00140.84           N  
ANISOU 1656  N   ASN A1006    16024  15832  21654   2739   -232     21       N  
ATOM   1657  CA  ASN A1006       2.910  76.010 141.467  1.00141.91           C  
ANISOU 1657  CA  ASN A1006    16135  15978  21806   2767   -273     -4       C  
ATOM   1658  C   ASN A1006       2.129  75.968 142.788  1.00142.88           C  
ANISOU 1658  C   ASN A1006    16218  16105  21962   2744   -283     -1       C  
ATOM   1659  O   ASN A1006       0.943  76.318 142.818  1.00142.78           O  
ANISOU 1659  O   ASN A1006    16206  16098  21946   2768   -305    -13       O  
ATOM   1660  CB  ASN A1006       2.903  74.607 140.843  1.00142.86           C  
ANISOU 1660  CB  ASN A1006    16222  16106  21951   2776   -298    -27       C  
ATOM   1661  CG  ASN A1006       3.273  74.607 139.376  1.00144.30           C  
ANISOU 1661  CG  ASN A1006    16442  16285  22098   2812   -299    -39       C  
ATOM   1662  OD1 ASN A1006       2.862  75.482 138.614  1.00145.24           O  
ANISOU 1662  OD1 ASN A1006    16605  16401  22176   2849   -299    -43       O  
ATOM   1663  ND2 ASN A1006       4.035  73.598 138.964  1.00144.87           N  
ANISOU 1663  ND2 ASN A1006    16497  16359  22187   2802   -299    -44       N  
ATOM   1664  N   TRP A1007       2.795  75.528 143.860  1.00145.28           N  
ANISOU 1664  N   TRP A1007    16488  16409  22301   2697   -268     15       N  
ATOM   1665  CA  TRP A1007       2.185  75.480 145.196  1.00146.87           C  
ANISOU 1665  CA  TRP A1007    16653  16615  22536   2670   -274     21       C  
ATOM   1666  C   TRP A1007       1.807  76.871 145.710  1.00148.60           C  
ANISOU 1666  C   TRP A1007    16902  16828  22728   2672   -259     37       C  
ATOM   1667  O   TRP A1007       0.715  77.057 146.254  1.00149.54           O  
ANISOU 1667  O   TRP A1007    17006  16952  22859   2678   -277     30       O  
ATOM   1668  CB  TRP A1007       3.122  74.797 146.196  1.00147.35           C  
ANISOU 1668  CB  TRP A1007    16676  16674  22634   2619   -257     38       C  
ATOM   1669  CG  TRP A1007       2.562  74.668 147.604  1.00147.61           C  
ANISOU 1669  CG  TRP A1007    16669  16711  22705   2589   -262     45       C  
ATOM   1670  CD1 TRP A1007       3.066  75.246 148.733  1.00147.63           C  
ANISOU 1670  CD1 TRP A1007    16669  16709  22714   2552   -236     71       C  
ATOM   1671  CD2 TRP A1007       1.411  73.915 148.019  1.00147.86           C  
ANISOU 1671  CD2 TRP A1007    16656  16751  22770   2594   -296     26       C  
ATOM   1672  NE1 TRP A1007       2.308  74.900 149.824  1.00147.08           N  
ANISOU 1672  NE1 TRP A1007    16558  16645  22681   2533   -251     70       N  
ATOM   1673  CE2 TRP A1007       1.284  74.087 149.416  1.00147.53           C  
ANISOU 1673  CE2 TRP A1007    16588  16709  22755   2558   -287     42       C  
ATOM   1674  CE3 TRP A1007       0.476  73.112 147.347  1.00148.23           C  
ANISOU 1674  CE3 TRP A1007    16684  16807  22830   2624   -332     -3       C  
ATOM   1675  CZ2 TRP A1007       0.262  73.485 150.161  1.00147.65           C  
ANISOU 1675  CZ2 TRP A1007    16559  16732  22808   2552   -313     30       C  
ATOM   1676  CZ3 TRP A1007      -0.555  72.514 148.091  1.00148.25           C  
ANISOU 1676  CZ3 TRP A1007    16641  16816  22869   2618   -358    -15       C  
ATOM   1677  CH2 TRP A1007      -0.638  72.695 149.488  1.00147.96           C  
ANISOU 1677  CH2 TRP A1007    16579  16778  22858   2582   -348      1       C  
ATOM   1678  N   GLU A1008       2.708  77.837 145.537  1.00150.21           N  
ANISOU 1678  N   GLU A1008    17151  17023  22899   2666   -225     58       N  
ATOM   1679  CA  GLU A1008       2.429  79.226 145.929  1.00150.78           C  
ANISOU 1679  CA  GLU A1008    17257  17089  22942   2669   -208     74       C  
ATOM   1680  C   GLU A1008       1.387  79.893 145.017  1.00151.63           C  
ANISOU 1680  C   GLU A1008    17399  17197  23014   2721   -227     57       C  
ATOM   1681  O   GLU A1008       0.564  80.672 145.500  1.00152.43           O  
ANISOU 1681  O   GLU A1008    17509  17299  23108   2728   -232     60       O  
ATOM   1682  CB  GLU A1008       3.713  80.061 145.982  1.00150.64           C  
ANISOU 1682  CB  GLU A1008    17276  17060  22898   2649   -165    101       C  
ATOM   1683  CG  GLU A1008       3.542  81.383 146.728  1.00150.50           C  
ANISOU 1683  CG  GLU A1008    17284  17036  22861   2639   -145    121       C  
ATOM   1684  CD  GLU A1008       4.855  82.057 147.096  1.00150.56           C  
ANISOU 1684  CD  GLU A1008    17316  17034  22855   2607   -102    149       C  
ATOM   1685  OE1 GLU A1008       5.899  81.713 146.503  1.00151.47           O  
ANISOU 1685  OE1 GLU A1008    17442  17145  22963   2602    -86    152       O  
ATOM   1686  OE2 GLU A1008       4.839  82.941 147.983  1.00149.91           O  
ANISOU 1686  OE2 GLU A1008    17242  16947  22768   2588    -83    168       O  
ATOM   1687  N   THR A1009       1.423  79.586 143.716  1.00151.65           N  
ANISOU 1687  N   THR A1009    17423  17201  22995   2756   -239     40       N  
ATOM   1688  CA  THR A1009       0.390  80.056 142.775  1.00151.96           C  
ANISOU 1688  CA  THR A1009    17491  17242  23003   2807   -262     20       C  
ATOM   1689  C   THR A1009      -1.016  79.608 143.197  1.00152.18           C  
ANISOU 1689  C   THR A1009    17481  17281  23059   2819   -299      0       C  
ATOM   1690  O   THR A1009      -1.957  80.413 143.217  1.00152.62           O  
ANISOU 1690  O   THR A1009    17555  17338  23095   2843   -308     -4       O  
ATOM   1691  CB  THR A1009       0.663  79.559 141.336  1.00151.98           C  
ANISOU 1691  CB  THR A1009    17513  17245  22985   2841   -272      2       C  
ATOM   1692  OG1 THR A1009       1.955  80.005 140.911  1.00152.29           O  
ANISOU 1692  OG1 THR A1009    17590  17275  22998   2831   -237     20       O  
ATOM   1693  CG2 THR A1009      -0.394  80.078 140.354  1.00152.21           C  
ANISOU 1693  CG2 THR A1009    17575  17278  22981   2895   -295    -18       C  
ATOM   1694  N   LEU A1010      -1.141  78.329 143.543  1.00151.46           N  
ANISOU 1694  N   LEU A1010    17337  17197  23011   2802   -319    -12       N  
ATOM   1695  CA  LEU A1010      -2.428  77.746 143.946  1.00150.77           C  
ANISOU 1695  CA  LEU A1010    17209  17120  22956   2811   -354    -33       C  
ATOM   1696  C   LEU A1010      -2.975  78.353 145.252  1.00151.03           C  
ANISOU 1696  C   LEU A1010    17226  17153  23003   2788   -349    -19       C  
ATOM   1697  O   LEU A1010      -4.182  78.553 145.376  1.00150.44           O  
ANISOU 1697  O   LEU A1010    17145  17084  22931   2809   -373    -33       O  
ATOM   1698  CB  LEU A1010      -2.298  76.224 144.090  1.00149.48           C  
ANISOU 1698  CB  LEU A1010    16992  16964  22838   2793   -372    -47       C  
ATOM   1699  CG  LEU A1010      -3.580  75.398 144.112  1.00148.76           C  
ANISOU 1699  CG  LEU A1010    16860  16883  22777   2811   -413    -75       C  
ATOM   1700  CD1 LEU A1010      -4.211  75.348 142.733  1.00148.71           C  
ANISOU 1700  CD1 LEU A1010    16877  16881  22743   2863   -438   -102       C  
ATOM   1701  CD2 LEU A1010      -3.283  73.985 144.588  1.00148.44           C  
ANISOU 1701  CD2 LEU A1010    16765  16848  22786   2780   -423    -81       C  
ATOM   1702  N   ASN A1011      -2.081  78.634 146.207  1.00151.91           N  
ANISOU 1702  N   ASN A1011    17334  17258  23125   2744   -318      8       N  
ATOM   1703  CA  ASN A1011      -2.458  79.169 147.538  1.00152.56           C  
ANISOU 1703  CA  ASN A1011    17400  17340  23223   2717   -310     24       C  
ATOM   1704  C   ASN A1011      -2.749  80.677 147.564  1.00153.90           C  
ANISOU 1704  C   ASN A1011    17618  17504  23353   2733   -295     37       C  
ATOM   1705  O   ASN A1011      -3.555  81.132 148.384  1.00154.38           O  
ANISOU 1705  O   ASN A1011    17667  17567  23422   2728   -301     39       O  
ATOM   1706  CB  ASN A1011      -1.374  78.862 148.586  1.00152.33           C  
ANISOU 1706  CB  ASN A1011    17347  17307  23222   2664   -283     48       C  
ATOM   1707  CG  ASN A1011      -1.293  77.386 148.946  1.00152.74           C  
ANISOU 1707  CG  ASN A1011    17342  17366  23323   2642   -300     37       C  
ATOM   1708  OD1 ASN A1011      -1.971  76.546 148.356  1.00153.56           O  
ANISOU 1708  OD1 ASN A1011    17427  17478  23441   2665   -331     11       O  
ATOM   1709  ND2 ASN A1011      -0.459  77.069 149.928  1.00152.61           N  
ANISOU 1709  ND2 ASN A1011    17302  17348  23335   2596   -280     57       N  
ATOM   1710  N   ASP A1012      -2.063  81.446 146.717  1.00155.04           N  
ANISOU 1710  N   ASP A1012    17814  17641  23454   2750   -273     45       N  
ATOM   1711  CA  ASP A1012      -2.375  82.868 146.546  1.00155.64           C  
ANISOU 1711  CA  ASP A1012    17939  17710  23486   2771   -260     55       C  
ATOM   1712  C   ASP A1012      -3.780  83.050 145.969  1.00157.17           C  
ANISOU 1712  C   ASP A1012    18139  17910  23666   2817   -294     30       C  
ATOM   1713  O   ASP A1012      -4.601  83.762 146.555  1.00157.32           O  
ANISOU 1713  O   ASP A1012    18161  17930  23681   2821   -299     33       O  
ATOM   1714  CB  ASP A1012      -1.346  83.545 145.635  1.00155.54           C  
ANISOU 1714  CB  ASP A1012    17979  17687  23429   2782   -231     67       C  
ATOM   1715  CG  ASP A1012       0.025  83.684 146.289  1.00155.35           C  
ANISOU 1715  CG  ASP A1012    17957  17655  23412   2737   -193     95       C  
ATOM   1716  OD1 ASP A1012       0.255  83.106 147.374  1.00155.14           O  
ANISOU 1716  OD1 ASP A1012    17887  17632  23426   2697   -190    104       O  
ATOM   1717  OD2 ASP A1012       0.886  84.383 145.711  1.00155.63           O  
ANISOU 1717  OD2 ASP A1012    18037  17682  23412   2741   -165    108       O  
ATOM   1718  N   ASN A1013      -4.038  82.387 144.846  1.00159.07           N  
ANISOU 1718  N   ASN A1013    18381  18155  23900   2851   -317      6       N  
ATOM   1719  CA  ASN A1013      -5.339  82.459 144.174  1.00160.19           C  
ANISOU 1719  CA  ASN A1013    18530  18305  24030   2897   -351    -20       C  
ATOM   1720  C   ASN A1013      -6.464  81.900 145.033  1.00159.98           C  
ANISOU 1720  C   ASN A1013    18452  18288  24044   2890   -380    -34       C  
ATOM   1721  O   ASN A1013      -7.531  82.493 145.104  1.00159.13           O  
ANISOU 1721  O   ASN A1013    18352  18183  23924   2913   -396    -43       O  
ATOM   1722  CB  ASN A1013      -5.294  81.690 142.865  1.00161.03           C  
ANISOU 1722  CB  ASN A1013    18641  18415  24127   2930   -370    -44       C  
ATOM   1723  CG  ASN A1013      -4.338  82.296 141.841  1.00161.41           C  
ANISOU 1723  CG  ASN A1013    18743  18453  24130   2947   -345    -34       C  
ATOM   1724  OD1 ASN A1013      -3.624  83.267 142.112  1.00161.34           O  
ANISOU 1724  OD1 ASN A1013    18769  18435  24098   2931   -312     -9       O  
ATOM   1725  ND2 ASN A1013      -4.314  81.706 140.654  1.00161.81           N  
ANISOU 1725  ND2 ASN A1013    18802  18507  24170   2978   -362    -54       N  
ATOM   1726  N   VAL A1026     -11.875  86.581 139.498  1.00187.28           N  
ANISOU 1726  N   VAL A1026    22152  21754  27251   3211   -480   -131       N  
ATOM   1727  CA  VAL A1026     -12.111  85.141 139.595  1.00187.33           C  
ANISOU 1727  CA  VAL A1026    22101  21770  27304   3200   -507   -152       C  
ATOM   1728  C   VAL A1026     -11.541  84.411 138.371  1.00188.99           C  
ANISOU 1728  C   VAL A1026    22321  21980  27503   3221   -512   -166       C  
ATOM   1729  O   VAL A1026     -10.884  83.378 138.519  1.00189.57           O  
ANISOU 1729  O   VAL A1026    22362  22055  27609   3193   -511   -166       O  
ATOM   1730  CB  VAL A1026     -13.618  84.817 139.773  1.00186.58           C  
ANISOU 1730  CB  VAL A1026    21974  21687  27229   3223   -547   -180       C  
ATOM   1731  CG1 VAL A1026     -13.856  83.308 139.812  1.00185.91           C  
ANISOU 1731  CG1 VAL A1026    21831  21612  27192   3213   -574   -202       C  
ATOM   1732  CG2 VAL A1026     -14.167  85.482 141.032  1.00186.26           C  
ANISOU 1732  CG2 VAL A1026    21921  21646  27201   3200   -541   -166       C  
ATOM   1733  N   LYS A1027     -11.789  84.952 137.175  1.00190.17           N  
ANISOU 1733  N   LYS A1027    22518  22129  27608   3270   -519   -178       N  
ATOM   1734  CA  LYS A1027     -11.298  84.363 135.913  1.00190.06           C  
ANISOU 1734  CA  LYS A1027    22519  22115  27579   3295   -525   -192       C  
ATOM   1735  C   LYS A1027      -9.765  84.323 135.847  1.00189.99           C  
ANISOU 1735  C   LYS A1027    22526  22095  27563   3264   -488   -167       C  
ATOM   1736  O   LYS A1027      -9.173  83.293 135.479  1.00190.12           O  
ANISOU 1736  O   LYS A1027    22522  22115  27600   3254   -492   -174       O  
ATOM   1737  CB  LYS A1027     -11.853  85.139 134.712  1.00189.51           C  
ANISOU 1737  CB  LYS A1027    22502  22045  27457   3353   -536   -207       C  
ATOM   1738  CG  LYS A1027     -11.615  84.472 133.365  1.00189.06           C  
ANISOU 1738  CG  LYS A1027    22457  21990  27386   3386   -550   -227       C  
ATOM   1739  CD  LYS A1027     -12.393  85.160 132.260  1.00188.91           C  
ANISOU 1739  CD  LYS A1027    22483  21973  27320   3446   -568   -246       C  
ATOM   1740  CE  LYS A1027     -12.195  84.461 130.926  1.00188.69           C  
ANISOU 1740  CE  LYS A1027    22465  21948  27279   3479   -583   -267       C  
ATOM   1741  NZ  LYS A1027     -13.031  85.069 129.857  1.00189.23           N  
ANISOU 1741  NZ  LYS A1027    22574  22019  27304   3539   -604   -288       N  
ATOM   1742  N   ASP A1028      -9.142  85.447 136.211  1.00189.24           N  
ANISOU 1742  N   ASP A1028    22471  21990  27442   3249   -453   -139       N  
ATOM   1743  CA  ASP A1028      -7.679  85.568 136.300  1.00188.76           C  
ANISOU 1743  CA  ASP A1028    22427  21917  27375   3216   -413   -112       C  
ATOM   1744  C   ASP A1028      -7.056  84.581 137.300  1.00189.70           C  
ANISOU 1744  C   ASP A1028    22491  22038  27546   3162   -407   -102       C  
ATOM   1745  O   ASP A1028      -5.931  84.124 137.093  1.00189.89           O  
ANISOU 1745  O   ASP A1028    22516  22058  27575   3142   -387    -92       O  
ATOM   1746  CB  ASP A1028      -7.281  87.007 136.675  1.00187.39           C  
ANISOU 1746  CB  ASP A1028    22300  21732  27167   3208   -378    -83       C  
ATOM   1747  CG  ASP A1028      -5.797  87.283 136.481  1.00186.64           C  
ANISOU 1747  CG  ASP A1028    22235  21625  27054   3184   -338    -59       C  
ATOM   1748  OD1 ASP A1028      -5.240  86.854 135.451  1.00186.22           O  
ANISOU 1748  OD1 ASP A1028    22197  21569  26986   3202   -337    -67       O  
ATOM   1749  OD2 ASP A1028      -5.190  87.943 137.353  1.00186.07           O  
ANISOU 1749  OD2 ASP A1028    22170  21545  26983   3149   -306    -31       O  
ATOM   1750  N   ALA A1029      -7.779  84.271 138.378  1.00190.33           N  
ANISOU 1750  N   ALA A1029    22527  22126  27664   3141   -422   -105       N  
ATOM   1751  CA  ALA A1029      -7.363  83.226 139.322  1.00190.73           C  
ANISOU 1751  CA  ALA A1029    22521  22180  27767   3094   -421   -100       C  
ATOM   1752  C   ALA A1029      -7.558  81.828 138.723  1.00192.13           C  
ANISOU 1752  C   ALA A1029    22661  22367  27972   3105   -451   -127       C  
ATOM   1753  O   ALA A1029      -6.625  81.013 138.714  1.00191.96           O  
ANISOU 1753  O   ALA A1029    22620  22343  27970   3079   -441   -122       O  
ATOM   1754  CB  ALA A1029      -8.130  83.353 140.632  1.00190.05           C  
ANISOU 1754  CB  ALA A1029    22399  22098  27711   3070   -429    -95       C  
ATOM   1755  N   LEU A1030      -8.767  81.570 138.218  1.00193.24           N  
ANISOU 1755  N   LEU A1030    22792  22517  28112   3143   -488   -156       N  
ATOM   1756  CA  LEU A1030      -9.133  80.266 137.637  1.00193.22           C  
ANISOU 1756  CA  LEU A1030    22754  22524  28137   3158   -520   -185       C  
ATOM   1757  C   LEU A1030      -8.244  79.840 136.464  1.00192.64           C  
ANISOU 1757  C   LEU A1030    22703  22447  28043   3173   -514   -190       C  
ATOM   1758  O   LEU A1030      -7.839  78.675 136.393  1.00192.43           O  
ANISOU 1758  O   LEU A1030    22641  22424  28048   3157   -522   -198       O  
ATOM   1759  CB  LEU A1030     -10.603  80.258 137.186  1.00193.75           C  
ANISOU 1759  CB  LEU A1030    22815  22601  28198   3202   -560   -216       C  
ATOM   1760  CG  LEU A1030     -11.672  80.214 138.284  1.00193.91           C  
ANISOU 1760  CG  LEU A1030    22796  22628  28251   3189   -578   -222       C  
ATOM   1761  CD1 LEU A1030     -13.036  80.570 137.712  1.00193.99           C  
ANISOU 1761  CD1 LEU A1030    22817  22646  28243   3238   -610   -248       C  
ATOM   1762  CD2 LEU A1030     -11.721  78.852 138.957  1.00194.05           C  
ANISOU 1762  CD2 LEU A1030    22749  22653  28327   3157   -593   -231       C  
ATOM   1763  N   THR A1031      -7.949  80.774 135.556  1.00191.11           N  
ANISOU 1763  N   THR A1031    22567  22246  27798   3204   -499   -184       N  
ATOM   1764  CA  THR A1031      -7.071  80.483 134.408  1.00189.48           C  
ANISOU 1764  CA  THR A1031    22389  22036  27569   3220   -490   -187       C  
ATOM   1765  C   THR A1031      -5.639  80.113 134.840  1.00187.47           C  
ANISOU 1765  C   THR A1031    22125  21774  27330   3173   -458   -163       C  
ATOM   1766  O   THR A1031      -5.041  79.176 134.293  1.00187.66           O  
ANISOU 1766  O   THR A1031    22135  21799  27367   3170   -461   -171       O  
ATOM   1767  CB  THR A1031      -7.026  81.658 133.405  1.00189.45           C  
ANISOU 1767  CB  THR A1031    22452  22024  27505   3261   -478   -184       C  
ATOM   1768  OG1 THR A1031      -6.740  82.878 134.098  1.00189.79           O  
ANISOU 1768  OG1 THR A1031    22525  22058  27527   3244   -447   -155       O  
ATOM   1769  CG2 THR A1031      -8.357  81.794 132.673  1.00189.34           C  
ANISOU 1769  CG2 THR A1031    22447  22019  27473   3315   -515   -213       C  
ATOM   1770  N   LYS A1032      -5.111  80.842 135.827  1.00184.82           N  
ANISOU 1770  N   LYS A1032    21796  21430  26995   3137   -427   -134       N  
ATOM   1771  CA  LYS A1032      -3.798  80.538 136.418  1.00182.50           C  
ANISOU 1771  CA  LYS A1032    21489  21129  26720   3089   -395   -109       C  
ATOM   1772  C   LYS A1032      -3.801  79.220 137.202  1.00183.19           C  
ANISOU 1772  C   LYS A1032    21512  21225  26865   3054   -410   -116       C  
ATOM   1773  O   LYS A1032      -2.826  78.460 137.139  1.00183.05           O  
ANISOU 1773  O   LYS A1032    21479  21206  26865   3030   -399   -111       O  
ATOM   1774  CB  LYS A1032      -3.325  81.686 137.319  1.00180.13           C  
ANISOU 1774  CB  LYS A1032    21212  20819  26406   3060   -360    -78       C  
ATOM   1775  CG  LYS A1032      -2.952  82.950 136.564  1.00178.75           C  
ANISOU 1775  CG  LYS A1032    21105  20634  26175   3086   -336    -66       C  
ATOM   1776  CD  LYS A1032      -2.690  84.106 137.517  1.00177.01           C  
ANISOU 1776  CD  LYS A1032    20905  20406  25944   3060   -305    -37       C  
ATOM   1777  CE  LYS A1032      -2.422  85.398 136.764  1.00176.14           C  
ANISOU 1777  CE  LYS A1032    20862  20285  25777   3088   -282    -26       C  
ATOM   1778  NZ  LYS A1032      -2.482  86.580 137.664  1.00175.66           N  
ANISOU 1778  NZ  LYS A1032    20820  20218  25705   3071   -259     -3       N  
ATOM   1779  N   MET A1033      -4.886  78.958 137.939  1.00183.97           N  
ANISOU 1779  N   MET A1033    21573  21332  26993   3051   -435   -128       N  
ATOM   1780  CA  MET A1033      -5.092  77.648 138.589  1.00183.92           C  
ANISOU 1780  CA  MET A1033    21503  21334  27042   3024   -455   -139       C  
ATOM   1781  C   MET A1033      -5.120  76.505 137.569  1.00184.61           C  
ANISOU 1781  C   MET A1033    21574  21428  27138   3047   -480   -165       C  
ATOM   1782  O   MET A1033      -4.516  75.448 137.792  1.00184.84           O  
ANISOU 1782  O   MET A1033    21569  21460  27202   3020   -480   -166       O  
ATOM   1783  CB  MET A1033      -6.387  77.630 139.413  1.00183.12           C  
ANISOU 1783  CB  MET A1033    21369  21241  26966   3025   -480   -150       C  
ATOM   1784  CG  MET A1033      -6.279  78.335 140.755  1.00182.23           C  
ANISOU 1784  CG  MET A1033    21249  21123  26864   2987   -458   -124       C  
ATOM   1785  SD  MET A1033      -7.738  78.110 141.791  1.00180.95           S  
ANISOU 1785  SD  MET A1033    21041  20972  26740   2983   -488   -138       S  
ATOM   1786  CE  MET A1033      -7.190  78.865 143.321  1.00179.59           C  
ANISOU 1786  CE  MET A1033    20864  20791  26578   2931   -453   -101       C  
ATOM   1787  N   ARG A1034      -5.822  76.732 136.456  1.00185.63           N  
ANISOU 1787  N   ARG A1034    21731  21560  27237   3098   -501   -188       N  
ATOM   1788  CA  ARG A1034      -5.888  75.763 135.357  1.00186.39           C  
ANISOU 1788  CA  ARG A1034    21820  21664  27337   3125   -525   -214       C  
ATOM   1789  C   ARG A1034      -4.499  75.543 134.755  1.00187.65           C  
ANISOU 1789  C   ARG A1034    22000  21815  27482   3114   -500   -201       C  
ATOM   1790  O   ARG A1034      -4.008  74.407 134.712  1.00187.80           O  
ANISOU 1790  O   ARG A1034    21984  21837  27531   3096   -505   -207       O  
ATOM   1791  CB  ARG A1034      -6.872  76.224 134.280  1.00186.00           C  
ANISOU 1791  CB  ARG A1034    21801  21617  27251   3183   -550   -238       C  
ATOM   1792  CG  ARG A1034      -7.374  75.096 133.391  1.00185.39           C  
ANISOU 1792  CG  ARG A1034    21700  21551  27189   3212   -586   -271       C  
ATOM   1793  CD  ARG A1034      -8.416  75.579 132.394  1.00185.49           C  
ANISOU 1793  CD  ARG A1034    21742  21568  27166   3269   -612   -296       C  
ATOM   1794  NE  ARG A1034      -9.413  74.549 132.081  1.00185.91           N  
ANISOU 1794  NE  ARG A1034    21754  21633  27247   3291   -653   -330       N  
ATOM   1795  CZ  ARG A1034     -10.416  74.183 132.882  1.00185.71           C  
ANISOU 1795  CZ  ARG A1034    21686  21616  27258   3282   -677   -343       C  
ATOM   1796  NH1 ARG A1034     -10.595  74.745 134.080  1.00185.41           N  
ANISOU 1796  NH1 ARG A1034    21637  21575  27232   3252   -663   -324       N  
ATOM   1797  NH2 ARG A1034     -11.259  73.233 132.486  1.00185.71           N  
ANISOU 1797  NH2 ARG A1034    21652  21627  27282   3303   -714   -375       N  
ATOM   1798  N   ALA A1035      -3.856  76.638 134.344  1.00189.00           N  
ANISOU 1798  N   ALA A1035    22225  21976  27608   3123   -471   -182       N  
ATOM   1799  CA  ALA A1035      -2.478  76.600 133.817  1.00189.48           C  
ANISOU 1799  CA  ALA A1035    22311  22028  27652   3111   -441   -167       C  
ATOM   1800  C   ALA A1035      -1.504  75.892 134.767  1.00190.09           C  
ANISOU 1800  C   ALA A1035    22351  22104  27770   3056   -422   -149       C  
ATOM   1801  O   ALA A1035      -0.651  75.117 134.323  1.00189.30           O  
ANISOU 1801  O   ALA A1035    22242  22002  27678   3046   -416   -150       O  
ATOM   1802  CB  ALA A1035      -1.985  78.009 133.515  1.00189.33           C  
ANISOU 1802  CB  ALA A1035    22355  21998  27582   3122   -409   -145       C  
ATOM   1803  N   ALA A1036      -1.648  76.157 136.067  1.00190.95           N  
ANISOU 1803  N   ALA A1036    22436  22212  27902   3021   -413   -132       N  
ATOM   1804  CA  ALA A1036      -0.892  75.445 137.104  1.00190.89           C  
ANISOU 1804  CA  ALA A1036    22386  22204  27937   2968   -399   -117       C  
ATOM   1805  C   ALA A1036      -1.253  73.956 137.165  1.00191.28           C  
ANISOU 1805  C   ALA A1036    22380  22264  28033   2962   -429   -139       C  
ATOM   1806  O   ALA A1036      -0.371  73.118 137.389  1.00190.75           O  
ANISOU 1806  O   ALA A1036    22288  22197  27992   2932   -419   -133       O  
ATOM   1807  CB  ALA A1036      -1.109  76.094 138.463  1.00190.30           C  
ANISOU 1807  CB  ALA A1036    22300  22127  27876   2936   -385    -97       C  
ATOM   1808  N   ALA A1037      -2.536  73.630 136.971  1.00192.14           N  
ANISOU 1808  N   ALA A1037    22469  22382  28152   2991   -465   -166       N  
ATOM   1809  CA  ALA A1037      -2.982  72.226 136.946  1.00192.67           C  
ANISOU 1809  CA  ALA A1037    22484  22458  28261   2989   -496   -190       C  
ATOM   1810  C   ALA A1037      -2.424  71.456 135.740  1.00193.55           C  
ANISOU 1810  C   ALA A1037    22603  22571  28365   3009   -503   -205       C  
ATOM   1811  O   ALA A1037      -2.003  70.303 135.876  1.00193.19           O  
ANISOU 1811  O   ALA A1037    22520  22529  28354   2987   -509   -210       O  
ATOM   1812  CB  ALA A1037      -4.504  72.140 136.977  1.00192.67           C  
ANISOU 1812  CB  ALA A1037    22465  22468  28271   3017   -533   -215       C  
ATOM   1813  N   LEU A1038      -2.428  72.099 134.570  1.00194.63           N  
ANISOU 1813  N   LEU A1038    22789  22705  28454   3050   -502   -211       N  
ATOM   1814  CA  LEU A1038      -1.846  71.519 133.349  1.00194.55           C  
ANISOU 1814  CA  LEU A1038    22794  22695  28430   3072   -506   -224       C  
ATOM   1815  C   LEU A1038      -0.327  71.328 133.458  1.00193.65           C  
ANISOU 1815  C   LEU A1038    22686  22572  28317   3036   -472   -200       C  
ATOM   1816  O   LEU A1038       0.210  70.348 132.936  1.00193.22           O  
ANISOU 1816  O   LEU A1038    22616  22521  28278   3034   -478   -210       O  
ATOM   1817  CB  LEU A1038      -2.169  72.383 132.122  1.00194.92           C  
ANISOU 1817  CB  LEU A1038    22897  22740  28424   3123   -510   -233       C  
ATOM   1818  CG  LEU A1038      -3.642  72.492 131.716  1.00194.75           C  
ANISOU 1818  CG  LEU A1038    22874  22727  28395   3167   -547   -261       C  
ATOM   1819  CD1 LEU A1038      -3.822  73.571 130.658  1.00194.71           C  
ANISOU 1819  CD1 LEU A1038    22931  22717  28333   3213   -542   -263       C  
ATOM   1820  CD2 LEU A1038      -4.175  71.157 131.217  1.00194.36           C  
ANISOU 1820  CD2 LEU A1038    22784  22688  28376   3182   -583   -293       C  
ATOM   1821  N   ASP A1039       0.351  72.267 134.122  1.00192.21           N  
ANISOU 1821  N   ASP A1039    22527  22381  28121   3010   -437   -171       N  
ATOM   1822  CA  ASP A1039       1.781  72.127 134.437  1.00190.69           C  
ANISOU 1822  CA  ASP A1039    22336  22181  27935   2971   -403   -147       C  
ATOM   1823  C   ASP A1039       2.015  71.004 135.451  1.00190.99           C  
ANISOU 1823  C   ASP A1039    22313  22224  28027   2927   -408   -144       C  
ATOM   1824  O   ASP A1039       2.934  70.195 135.285  1.00191.23           O  
ANISOU 1824  O   ASP A1039    22330  22254  28074   2908   -400   -142       O  
ATOM   1825  CB  ASP A1039       2.350  73.444 134.986  1.00188.79           C  
ANISOU 1825  CB  ASP A1039    22133  21931  27667   2953   -366   -116       C  
ATOM   1826  CG  ASP A1039       3.863  73.416 135.133  1.00187.28           C  
ANISOU 1826  CG  ASP A1039    21951  21730  27474   2918   -329    -93       C  
ATOM   1827  OD1 ASP A1039       4.563  73.223 134.117  1.00186.41           O  
ANISOU 1827  OD1 ASP A1039    21865  21617  27343   2933   -322    -96       O  
ATOM   1828  OD2 ASP A1039       4.353  73.599 136.257  1.00185.61           O  
ANISOU 1828  OD2 ASP A1039    21723  21516  27283   2876   -308    -71       O  
ATOM   1829  N   ALA A1040       1.183  70.968 136.492  1.00191.04           N  
ANISOU 1829  N   ALA A1040    22286  22235  28062   2912   -421   -145       N  
ATOM   1830  CA  ALA A1040       1.266  69.931 137.527  1.00190.44           C  
ANISOU 1830  CA  ALA A1040    22152  22163  28040   2872   -427   -144       C  
ATOM   1831  C   ALA A1040       0.978  68.518 136.987  1.00190.59           C  
ANISOU 1831  C   ALA A1040    22134  22191  28089   2883   -458   -171       C  
ATOM   1832  O   ALA A1040       0.032  68.274 136.224  1.00190.99           O  
ANISOU 1832  O   ALA A1040    22185  22249  28134   2922   -489   -198       O  
ATOM   1833  CB  ALA A1040       0.334  70.262 138.690  1.00189.50           C  
ANISOU 1833  CB  ALA A1040    22009  22047  27942   2857   -436   -140       C  
ATOM   1834  N   PRO A1056      -1.293  52.525 142.038  1.00155.38           N  
ANISOU 1834  N   PRO A1056    17028  17793  24216   2658   -675   -328       N  
ATOM   1835  CA  PRO A1056      -1.744  52.640 143.425  1.00155.93           C  
ANISOU 1835  CA  PRO A1056    17069  17862  24314   2627   -670   -316       C  
ATOM   1836  C   PRO A1056      -1.830  54.090 143.901  1.00157.26           C  
ANISOU 1836  C   PRO A1056    17272  18026  24451   2626   -651   -294       C  
ATOM   1837  O   PRO A1056      -2.886  54.515 144.374  1.00156.13           O  
ANISOU 1837  O   PRO A1056    17121  17886  24313   2634   -663   -301       O  
ATOM   1838  CB  PRO A1056      -0.694  51.847 144.217  1.00154.85           C  
ANISOU 1838  CB  PRO A1056    16904  17721  24210   2582   -651   -297       C  
ATOM   1839  CG  PRO A1056       0.501  51.737 143.331  1.00154.66           C  
ANISOU 1839  CG  PRO A1056    16906  17694  24161   2586   -636   -291       C  
ATOM   1840  CD  PRO A1056       0.109  52.090 141.925  1.00154.73           C  
ANISOU 1840  CD  PRO A1056    16949  17706  24134   2634   -652   -312       C  
ATOM   1841  N   GLU A1057      -0.730  54.830 143.772  1.00159.87           N  
ANISOU 1841  N   GLU A1057    17639  18351  24750   2617   -621   -270       N  
ATOM   1842  CA  GLU A1057      -0.687  56.256 144.111  1.00162.37           C  
ANISOU 1842  CA  GLU A1057    17994  18663  25033   2617   -600   -249       C  
ATOM   1843  C   GLU A1057      -1.149  57.115 142.933  1.00166.04           C  
ANISOU 1843  C   GLU A1057    18505  19130  25452   2664   -610   -262       C  
ATOM   1844  O   GLU A1057      -1.938  58.062 143.110  1.00167.41           O  
ANISOU 1844  O   GLU A1057    18696  19304  25607   2680   -613   -261       O  
ATOM   1845  CB  GLU A1057       0.728  56.672 144.516  1.00162.09           C  
ANISOU 1845  CB  GLU A1057    17978  18620  24986   2585   -563   -216       C  
ATOM   1846  CG  GLU A1057       1.266  55.944 145.738  1.00162.04           C  
ANISOU 1846  CG  GLU A1057    17931  18613  25023   2537   -551   -201       C  
ATOM   1847  CD  GLU A1057       2.572  56.533 146.245  1.00162.09           C  
ANISOU 1847  CD  GLU A1057    17958  18612  25014   2506   -513   -168       C  
ATOM   1848  OE1 GLU A1057       2.626  57.755 146.499  1.00160.98           O  
ANISOU 1848  OE1 GLU A1057    17850  18467  24844   2506   -495   -150       O  
ATOM   1849  OE2 GLU A1057       3.548  55.770 146.402  1.00162.95           O  
ANISOU 1849  OE2 GLU A1057    18051  18720  25143   2480   -502   -160       O  
ATOM   1850  N   MET A1058      -0.654  56.776 141.737  1.00168.61           N  
ANISOU 1850  N   MET A1058    18848  19455  25758   2687   -613   -273       N  
ATOM   1851  CA  MET A1058      -1.029  57.470 140.489  1.00169.59           C  
ANISOU 1851  CA  MET A1058    19016  19581  25837   2734   -623   -287       C  
ATOM   1852  C   MET A1058      -2.545  57.609 140.302  1.00170.37           C  
ANISOU 1852  C   MET A1058    19107  19686  25937   2767   -655   -313       C  
ATOM   1853  O   MET A1058      -3.006  58.621 139.783  1.00170.78           O  
ANISOU 1853  O   MET A1058    19197  19738  25951   2798   -657   -316       O  
ATOM   1854  CB  MET A1058      -0.407  56.787 139.256  1.00169.60           C  
ANISOU 1854  CB  MET A1058    19028  19583  25828   2754   -629   -301       C  
ATOM   1855  CG  MET A1058      -0.904  55.371 138.971  1.00169.70           C  
ANISOU 1855  CG  MET A1058    18996  19603  25878   2760   -659   -329       C  
ATOM   1856  SD  MET A1058      -0.022  54.556 137.626  1.00170.22           S  
ANISOU 1856  SD  MET A1058    19072  19669  25932   2777   -662   -342       S  
ATOM   1857  CE  MET A1058      -0.643  55.442 136.198  1.00169.78           C  
ANISOU 1857  CE  MET A1058    19068  19615  25823   2836   -676   -360       C  
ATOM   1858  N   LYS A1059      -3.307  56.602 140.740  1.00170.09           N  
ANISOU 1858  N   LYS A1059    19022  19656  25945   2760   -680   -332       N  
ATOM   1859  CA  LYS A1059      -4.777  56.659 140.725  1.00169.26           C  
ANISOU 1859  CA  LYS A1059    18903  19558  25849   2786   -710   -356       C  
ATOM   1860  C   LYS A1059      -5.318  57.695 141.709  1.00169.12           C  
ANISOU 1860  C   LYS A1059    18892  19538  25825   2775   -700   -340       C  
ATOM   1861  O   LYS A1059      -6.259  58.408 141.385  1.00168.32           O  
ANISOU 1861  O   LYS A1059    18810  19441  25703   2807   -715   -352       O  
ATOM   1862  CB  LYS A1059      -5.383  55.292 141.058  1.00168.04           C  
ANISOU 1862  CB  LYS A1059    18692  19410  25746   2776   -735   -378       C  
ATOM   1863  CG  LYS A1059      -5.091  54.201 140.035  1.00167.15           C  
ANISOU 1863  CG  LYS A1059    18568  19300  25640   2792   -751   -400       C  
ATOM   1864  CD  LYS A1059      -5.409  52.821 140.584  1.00166.09           C  
ANISOU 1864  CD  LYS A1059    18375  19169  25561   2770   -769   -415       C  
ATOM   1865  CE  LYS A1059      -5.044  51.740 139.582  1.00165.88           C  
ANISOU 1865  CE  LYS A1059    18339  19146  25543   2784   -783   -435       C  
ATOM   1866  NZ  LYS A1059      -5.326  50.375 140.105  1.00166.10           N  
ANISOU 1866  NZ  LYS A1059    18309  19175  25623   2763   -799   -449       N  
ATOM   1867  N   ASP A1060      -4.715  57.763 142.898  1.00168.79           N  
ANISOU 1867  N   ASP A1060    18836  19492  25804   2731   -676   -313       N  
ATOM   1868  CA  ASP A1060      -5.094  58.751 143.914  1.00168.11           C  
ANISOU 1868  CA  ASP A1060    18756  19403  25713   2716   -664   -295       C  
ATOM   1869  C   ASP A1060      -4.704  60.176 143.517  1.00169.25           C  
ANISOU 1869  C   ASP A1060    18958  19542  25804   2732   -642   -277       C  
ATOM   1870  O   ASP A1060      -5.449  61.117 143.811  1.00169.57           O  
ANISOU 1870  O   ASP A1060    19014  19583  25829   2744   -644   -275       O  
ATOM   1871  CB  ASP A1060      -4.496  58.396 145.282  1.00166.50           C  
ANISOU 1871  CB  ASP A1060    18520  19195  25544   2664   -643   -271       C  
ATOM   1872  CG  ASP A1060      -5.073  57.113 145.861  1.00164.87           C  
ANISOU 1872  CG  ASP A1060    18256  18993  25391   2648   -665   -287       C  
ATOM   1873  OD1 ASP A1060      -5.618  56.290 145.094  1.00164.07           O  
ANISOU 1873  OD1 ASP A1060    18138  18897  25301   2673   -692   -316       O  
ATOM   1874  OD2 ASP A1060      -4.973  56.924 147.091  1.00163.23           O  
ANISOU 1874  OD2 ASP A1060    18020  18784  25215   2611   -654   -271       O  
ATOM   1875  N   PHE A1061      -3.554  60.338 142.855  1.00170.41           N  
ANISOU 1875  N   PHE A1061    19136  19684  25925   2732   -621   -265       N  
ATOM   1876  CA  PHE A1061      -3.172  61.648 142.296  1.00171.64           C  
ANISOU 1876  CA  PHE A1061    19350  19836  26029   2752   -602   -250       C  
ATOM   1877  C   PHE A1061      -4.101  62.026 141.145  1.00171.84           C  
ANISOU 1877  C   PHE A1061    19402  19865  26023   2804   -626   -276       C  
ATOM   1878  O   PHE A1061      -4.701  63.112 141.147  1.00171.25           O  
ANISOU 1878  O   PHE A1061    19356  19790  25921   2824   -626   -273       O  
ATOM   1879  CB  PHE A1061      -1.718  61.661 141.807  1.00172.13           C  
ANISOU 1879  CB  PHE A1061    19438  19891  26071   2740   -574   -233       C  
ATOM   1880  CG  PHE A1061      -0.701  61.437 142.895  1.00172.67           C  
ANISOU 1880  CG  PHE A1061    19486  19954  26163   2689   -547   -206       C  
ATOM   1881  CD1 PHE A1061      -0.718  62.204 144.061  1.00172.33           C  
ANISOU 1881  CD1 PHE A1061    19443  19907  26124   2662   -528   -182       C  
ATOM   1882  CD2 PHE A1061       0.293  60.471 142.749  1.00173.36           C  
ANISOU 1882  CD2 PHE A1061    19556  20040  26270   2669   -539   -203       C  
ATOM   1883  CE1 PHE A1061       0.222  62.000 145.060  1.00172.44           C  
ANISOU 1883  CE1 PHE A1061    19440  19917  26160   2616   -503   -158       C  
ATOM   1884  CE2 PHE A1061       1.237  60.265 143.745  1.00173.39           C  
ANISOU 1884  CE2 PHE A1061    19543  20041  26296   2623   -514   -178       C  
ATOM   1885  CZ  PHE A1061       1.202  61.031 144.902  1.00173.16           C  
ANISOU 1885  CZ  PHE A1061    19513  20008  26270   2597   -496   -156       C  
ATOM   1886  N   ARG A1062      -4.218  61.114 140.177  1.00172.45           N  
ANISOU 1886  N   ARG A1062    19468  19947  26106   2828   -649   -301       N  
ATOM   1887  CA  ARG A1062      -5.161  61.248 139.060  1.00173.17           C  
ANISOU 1887  CA  ARG A1062    19577  20045  26175   2879   -677   -330       C  
ATOM   1888  C   ARG A1062      -6.532  61.678 139.559  1.00175.88           C  
ANISOU 1888  C   ARG A1062    19909  20393  26525   2892   -697   -342       C  
ATOM   1889  O   ARG A1062      -7.101  62.644 139.047  1.00176.85           O  
ANISOU 1889  O   ARG A1062    20067  20515  26610   2926   -702   -347       O  
ATOM   1890  CB  ARG A1062      -5.288  59.925 138.290  1.00171.55           C  
ANISOU 1890  CB  ARG A1062    19343  19845  25991   2893   -703   -358       C  
ATOM   1891  CG  ARG A1062      -6.140  59.980 137.027  1.00170.15           C  
ANISOU 1891  CG  ARG A1062    19184  19674  25789   2946   -732   -389       C  
ATOM   1892  CD  ARG A1062      -6.531  58.586 136.559  1.00168.89           C  
ANISOU 1892  CD  ARG A1062    18984  19521  25663   2956   -762   -419       C  
ATOM   1893  NE  ARG A1062      -5.383  57.683 136.441  1.00167.62           N  
ANISOU 1893  NE  ARG A1062    18810  19358  25520   2931   -749   -412       N  
ATOM   1894  CZ  ARG A1062      -4.497  57.676 135.441  1.00167.39           C  
ANISOU 1894  CZ  ARG A1062    18812  19326  25463   2945   -739   -410       C  
ATOM   1895  NH1 ARG A1062      -4.587  58.535 134.424  1.00167.60           N  
ANISOU 1895  NH1 ARG A1062    18886  19352  25440   2985   -739   -414       N  
ATOM   1896  NH2 ARG A1062      -3.497  56.798 135.459  1.00167.13           N  
ANISOU 1896  NH2 ARG A1062    18761  19291  25450   2919   -727   -402       N  
ATOM   1897  N   HIS A1063      -7.054  60.962 140.555  1.00178.84           N  
ANISOU 1897  N   HIS A1063    20232  20770  26945   2866   -708   -347       N  
ATOM   1898  CA  HIS A1063      -8.413  61.204 141.047  1.00181.61           C  
ANISOU 1898  CA  HIS A1063    20566  21127  27309   2878   -730   -361       C  
ATOM   1899  C   HIS A1063      -8.533  62.415 141.985  1.00182.88           C  
ANISOU 1899  C   HIS A1063    20746  21284  27456   2862   -710   -336       C  
ATOM   1900  O   HIS A1063      -9.589  63.056 142.033  1.00184.51           O  
ANISOU 1900  O   HIS A1063    20959  21492  27651   2885   -724   -347       O  
ATOM   1901  CB  HIS A1063      -8.992  59.956 141.707  1.00182.03           C  
ANISOU 1901  CB  HIS A1063    20559  21186  27419   2858   -751   -378       C  
ATOM   1902  CG  HIS A1063     -10.478  59.997 141.833  1.00182.60           C  
ANISOU 1902  CG  HIS A1063    20611  21264  27502   2881   -781   -402       C  
ATOM   1903  ND1 HIS A1063     -11.322  59.763 140.768  1.00182.83           N  
ANISOU 1903  ND1 HIS A1063    20645  21301  27521   2925   -812   -435       N  
ATOM   1904  CD2 HIS A1063     -11.271  60.291 142.888  1.00182.41           C  
ANISOU 1904  CD2 HIS A1063    20566  21241  27498   2866   -785   -399       C  
ATOM   1905  CE1 HIS A1063     -12.574  59.886 141.171  1.00182.49           C  
ANISOU 1905  CE1 HIS A1063    20582  21264  27492   2936   -833   -451       C  
ATOM   1906  NE2 HIS A1063     -12.570  60.208 142.452  1.00182.43           N  
ANISOU 1906  NE2 HIS A1063    20559  21252  27503   2901   -817   -430       N  
ATOM   1907  N   GLY A1064      -7.470  62.724 142.727  1.00183.26           N  
ANISOU 1907  N   GLY A1064    20801  21324  27505   2824   -677   -304       N  
ATOM   1908  CA  GLY A1064      -7.372  64.004 143.434  1.00184.25           C  
ANISOU 1908  CA  GLY A1064    20954  21444  27608   2812   -653   -278       C  
ATOM   1909  C   GLY A1064      -7.460  65.171 142.467  1.00185.93           C  
ANISOU 1909  C   GLY A1064    21224  21654  27764   2851   -649   -278       C  
ATOM   1910  O   GLY A1064      -8.187  66.153 142.711  1.00185.77           O  
ANISOU 1910  O   GLY A1064    21223  21634  27725   2865   -650   -276       O  
ATOM   1911  N   PHE A1065      -6.722  65.043 141.358  1.00188.24           N  
ANISOU 1911  N   PHE A1065    21544  21945  28032   2870   -644   -282       N  
ATOM   1912  CA  PHE A1065      -6.794  66.004 140.252  1.00190.05           C  
ANISOU 1912  CA  PHE A1065    21828  22172  28208   2912   -642   -286       C  
ATOM   1913  C   PHE A1065      -8.160  66.004 139.539  1.00190.86           C  
ANISOU 1913  C   PHE A1065    21931  22283  28303   2958   -679   -319       C  
ATOM   1914  O   PHE A1065      -8.608  67.064 139.106  1.00191.04           O  
ANISOU 1914  O   PHE A1065    21994  22305  28287   2989   -679   -319       O  
ATOM   1915  CB  PHE A1065      -5.654  65.763 139.253  1.00190.64           C  
ANISOU 1915  CB  PHE A1065    21929  22243  28261   2918   -628   -282       C  
ATOM   1916  CG  PHE A1065      -4.348  66.413 139.644  1.00191.37           C  
ANISOU 1916  CG  PHE A1065    22048  22325  28336   2888   -587   -248       C  
ATOM   1917  CD1 PHE A1065      -3.722  66.139 140.864  1.00191.60           C  
ANISOU 1917  CD1 PHE A1065    22048  22351  28397   2838   -567   -225       C  
ATOM   1918  CD2 PHE A1065      -3.735  67.311 138.772  1.00191.98           C  
ANISOU 1918  CD2 PHE A1065    22182  22397  28364   2909   -569   -238       C  
ATOM   1919  CE1 PHE A1065      -2.514  66.738 141.188  1.00191.85           C  
ANISOU 1919  CE1 PHE A1065    22106  22375  28413   2811   -530   -195       C  
ATOM   1920  CE2 PHE A1065      -2.531  67.919 139.102  1.00192.12           C  
ANISOU 1920  CE2 PHE A1065    22225  22406  28366   2882   -531   -207       C  
ATOM   1921  CZ  PHE A1065      -1.921  67.635 140.311  1.00192.16           C  
ANISOU 1921  CZ  PHE A1065    22200  22408  28403   2832   -512   -186       C  
ATOM   1922  N   ASP A1066      -8.802  64.837 139.410  1.00190.84           N  
ANISOU 1922  N   ASP A1066    21885  22289  28336   2964   -709   -346       N  
ATOM   1923  CA  ASP A1066     -10.195  64.765 138.922  1.00190.39           C  
ANISOU 1923  CA  ASP A1066    21820  22241  28278   3004   -745   -378       C  
ATOM   1924  C   ASP A1066     -11.122  65.564 139.835  1.00190.94           C  
ANISOU 1924  C   ASP A1066    21886  22312  28351   3000   -747   -373       C  
ATOM   1925  O   ASP A1066     -11.846  66.450 139.364  1.00190.24           O  
ANISOU 1925  O   ASP A1066    21828  22224  28228   3036   -757   -381       O  
ATOM   1926  CB  ASP A1066     -10.725  63.315 138.844  1.00189.27           C  
ANISOU 1926  CB  ASP A1066    21625  22107  28182   3004   -775   -407       C  
ATOM   1927  CG  ASP A1066     -10.036  62.467 137.778  1.00188.45           C  
ANISOU 1927  CG  ASP A1066    21523  22003  28074   3016   -780   -419       C  
ATOM   1928  OD1 ASP A1066      -9.385  63.023 136.866  1.00188.04           O  
ANISOU 1928  OD1 ASP A1066    21517  21948  27981   3037   -767   -412       O  
ATOM   1929  OD2 ASP A1066     -10.167  61.225 137.861  1.00187.72           O  
ANISOU 1929  OD2 ASP A1066    21386  21915  28022   3005   -797   -435       O  
ATOM   1930  N   ILE A1067     -11.083  65.249 141.135  1.00192.27           N  
ANISOU 1930  N   ILE A1067    22016  22478  28557   2957   -739   -359       N  
ATOM   1931  CA  ILE A1067     -11.912  65.934 142.145  1.00193.23           C  
ANISOU 1931  CA  ILE A1067    22130  22601  28688   2948   -739   -352       C  
ATOM   1932  C   ILE A1067     -11.625  67.442 142.174  1.00195.44           C  
ANISOU 1932  C   ILE A1067    22462  22874  28921   2955   -714   -328       C  
ATOM   1933  O   ILE A1067     -12.563  68.239 142.282  1.00196.16           O  
ANISOU 1933  O   ILE A1067    22567  22967  28996   2976   -724   -334       O  
ATOM   1934  CB  ILE A1067     -11.742  65.319 143.566  1.00191.88           C  
ANISOU 1934  CB  ILE A1067    21911  22429  28566   2897   -730   -337       C  
ATOM   1935  CG1 ILE A1067     -12.345  63.910 143.620  1.00191.18           C  
ANISOU 1935  CG1 ILE A1067    21768  22347  28525   2894   -759   -364       C  
ATOM   1936  CG2 ILE A1067     -12.407  66.186 144.635  1.00190.85           C  
ANISOU 1936  CG2 ILE A1067    21778  22296  28437   2885   -724   -324       C  
ATOM   1937  CD1 ILE A1067     -11.837  63.053 144.767  1.00190.47           C  
ANISOU 1937  CD1 ILE A1067    21632  22255  28482   2844   -747   -350       C  
ATOM   1938  N   LEU A1068     -10.347  67.819 142.071  1.00198.03           N  
ANISOU 1938  N   LEU A1068    22821  23194  29228   2938   -682   -302       N  
ATOM   1939  CA  LEU A1068      -9.960  69.235 142.045  1.00200.47           C  
ANISOU 1939  CA  LEU A1068    23181  23495  29491   2943   -656   -278       C  
ATOM   1940  C   LEU A1068     -10.441  69.940 140.767  1.00203.97           C  
ANISOU 1940  C   LEU A1068    23670  23940  29886   2997   -669   -295       C  
ATOM   1941  O   LEU A1068     -11.253  70.881 140.837  1.00204.46           O  
ANISOU 1941  O   LEU A1068    23754  24003  29927   3019   -674   -297       O  
ATOM   1942  CB  LEU A1068      -8.441  69.376 142.213  1.00199.86           C  
ANISOU 1942  CB  LEU A1068    23122  23408  29405   2911   -619   -248       C  
ATOM   1943  CG  LEU A1068      -7.858  70.802 142.219  1.00199.52           C  
ANISOU 1943  CG  LEU A1068    23134  23357  29318   2912   -587   -221       C  
ATOM   1944  CD1 LEU A1068      -6.877  71.018 143.362  1.00198.83           C  
ANISOU 1944  CD1 LEU A1068    23038  23262  29244   2861   -553   -188       C  
ATOM   1945  CD2 LEU A1068      -7.209  71.137 140.882  1.00199.91           C  
ANISOU 1945  CD2 LEU A1068    23231  23403  29323   2943   -579   -223       C  
ATOM   1946  N   VAL A1069      -9.976  69.454 139.614  1.00207.41           N  
ANISOU 1946  N   VAL A1069    24121  24376  30308   3020   -674   -308       N  
ATOM   1947  CA  VAL A1069     -10.321  70.049 138.307  1.00209.24           C  
ANISOU 1947  CA  VAL A1069    24397  24609  30493   3072   -686   -323       C  
ATOM   1948  C   VAL A1069     -11.841  70.076 138.091  1.00211.33           C  
ANISOU 1948  C   VAL A1069    24650  24883  30760   3108   -722   -353       C  
ATOM   1949  O   VAL A1069     -12.363  71.028 137.507  1.00212.17           O  
ANISOU 1949  O   VAL A1069    24796  24990  30827   3145   -727   -358       O  
ATOM   1950  CB  VAL A1069      -9.599  69.334 137.125  1.00208.89           C  
ANISOU 1950  CB  VAL A1069    24363  24564  30438   3088   -688   -335       C  
ATOM   1951  CG1 VAL A1069     -10.108  69.817 135.770  1.00208.71           C  
ANISOU 1951  CG1 VAL A1069    24382  24544  30371   3145   -705   -355       C  
ATOM   1952  CG2 VAL A1069      -8.089  69.543 137.206  1.00208.23           C  
ANISOU 1952  CG2 VAL A1069    24303  24472  30343   3058   -650   -304       C  
ATOM   1953  N   GLY A1070     -12.538  69.044 138.569  1.00213.30           N  
ANISOU 1953  N   GLY A1070    24846  25141  31057   3097   -747   -373       N  
ATOM   1954  CA  GLY A1070     -14.006  69.036 138.603  1.00215.18           C  
ANISOU 1954  CA  GLY A1070    25065  25387  31304   3124   -780   -399       C  
ATOM   1955  C   GLY A1070     -14.597  70.192 139.392  1.00217.54           C  
ANISOU 1955  C   GLY A1070    25379  25685  31590   3121   -772   -385       C  
ATOM   1956  O   GLY A1070     -15.565  70.821 138.944  1.00218.42           O  
ANISOU 1956  O   GLY A1070    25511  25801  31678   3159   -790   -402       O  
ATOM   1957  N   GLN A1071     -14.013  70.480 140.558  1.00220.23           N  
ANISOU 1957  N   GLN A1071    25711  26019  31946   3076   -744   -355       N  
ATOM   1958  CA  GLN A1071     -14.449  71.617 141.386  1.00222.80           C  
ANISOU 1958  CA  GLN A1071    26052  26341  32259   3069   -733   -338       C  
ATOM   1959  C   GLN A1071     -14.061  72.969 140.775  1.00226.62           C  
ANISOU 1959  C   GLN A1071    26601  26818  32685   3093   -712   -323       C  
ATOM   1960  O   GLN A1071     -14.797  73.956 140.931  1.00227.63           O  
ANISOU 1960  O   GLN A1071    26751  26947  32791   3111   -715   -322       O  
ATOM   1961  CB  GLN A1071     -13.905  71.495 142.811  1.00221.22           C  
ANISOU 1961  CB  GLN A1071    25823  26137  32092   3014   -709   -311       C  
ATOM   1962  CG  GLN A1071     -14.575  70.393 143.620  1.00220.28           C  
ANISOU 1962  CG  GLN A1071    25642  26025  32030   2992   -731   -326       C  
ATOM   1963  CD  GLN A1071     -13.792  69.995 144.860  1.00219.59           C  
ANISOU 1963  CD  GLN A1071    25524  25932  31977   2936   -707   -300       C  
ATOM   1964  OE1 GLN A1071     -12.812  70.640 145.225  1.00219.49           O  
ANISOU 1964  OE1 GLN A1071    25536  25910  31947   2913   -674   -270       O  
ATOM   1965  NE2 GLN A1071     -14.216  68.917 145.509  1.00219.31           N  
ANISOU 1965  NE2 GLN A1071    25433  25901  31991   2915   -723   -312       N  
ATOM   1966  N   ILE A1072     -12.911  73.011 140.092  1.00229.82           N  
ANISOU 1966  N   ILE A1072    27036  27218  33067   3092   -691   -310       N  
ATOM   1967  CA  ILE A1072     -12.512  74.185 139.298  1.00231.29           C  
ANISOU 1967  CA  ILE A1072    27285  27396  33196   3120   -673   -299       C  
ATOM   1968  C   ILE A1072     -13.490  74.415 138.137  1.00233.35           C  
ANISOU 1968  C   ILE A1072    27569  27663  33427   3178   -703   -328       C  
ATOM   1969  O   ILE A1072     -13.818  75.562 137.837  1.00235.06           O  
ANISOU 1969  O   ILE A1072    27829  27877  33604   3204   -697   -324       O  
ATOM   1970  CB  ILE A1072     -11.046  74.081 138.792  1.00230.73           C  
ANISOU 1970  CB  ILE A1072    27240  27318  33109   3106   -644   -280       C  
ATOM   1971  CG1 ILE A1072     -10.085  74.208 139.983  1.00229.87           C  
ANISOU 1971  CG1 ILE A1072    27119  27201  33020   3051   -611   -247       C  
ATOM   1972  CG2 ILE A1072     -10.735  75.158 137.749  1.00230.59           C  
ANISOU 1972  CG2 ILE A1072    27286  27293  33032   3142   -631   -275       C  
ATOM   1973  CD1 ILE A1072      -8.629  73.947 139.664  1.00229.23           C  
ANISOU 1973  CD1 ILE A1072    27051  27112  32931   3031   -583   -229       C  
ATOM   1974  N   ASP A1073     -13.948  73.336 137.497  1.00233.32           N  
ANISOU 1974  N   ASP A1073    27538  27669  33444   3197   -733   -359       N  
ATOM   1975  CA  ASP A1073     -15.001  73.426 136.472  1.00231.81           C  
ANISOU 1975  CA  ASP A1073    27359  27485  33230   3251   -766   -391       C  
ATOM   1976  C   ASP A1073     -16.353  73.843 137.068  1.00229.80           C  
ANISOU 1976  C   ASP A1073    27090  27238  32986   3263   -787   -403       C  
ATOM   1977  O   ASP A1073     -17.061  74.665 136.473  1.00229.74           O  
ANISOU 1977  O   ASP A1073    27115  27231  32941   3304   -798   -414       O  
ATOM   1978  CB  ASP A1073     -15.150  72.100 135.703  1.00231.75           C  
ANISOU 1978  CB  ASP A1073    27321  27485  33246   3267   -794   -421       C  
ATOM   1979  CG  ASP A1073     -13.957  71.795 134.806  1.00231.59           C  
ANISOU 1979  CG  ASP A1073    27325  27459  33207   3269   -778   -414       C  
ATOM   1980  OD1 ASP A1073     -13.464  72.711 134.119  1.00231.31           O  
ANISOU 1980  OD1 ASP A1073    27344  27418  33124   3290   -760   -402       O  
ATOM   1981  OD2 ASP A1073     -13.524  70.626 134.771  1.00230.68           O  
ANISOU 1981  OD2 ASP A1073    27175  27347  33124   3250   -783   -421       O  
ATOM   1982  N   ASP A1074     -16.705  73.278 138.229  1.00226.45           N  
ANISOU 1982  N   ASP A1074    26615  26816  32609   3227   -792   -402       N  
ATOM   1983  CA  ASP A1074     -17.918  73.690 138.966  1.00223.46           C  
ANISOU 1983  CA  ASP A1074    26219  26443  32242   3231   -808   -410       C  
ATOM   1984  C   ASP A1074     -17.879  75.155 139.413  1.00222.62           C  
ANISOU 1984  C   ASP A1074    26154  26329  32101   3230   -784   -385       C  
ATOM   1985  O   ASP A1074     -18.925  75.808 139.464  1.00223.49           O  
ANISOU 1985  O   ASP A1074    26272  26443  32198   3256   -800   -396       O  
ATOM   1986  CB  ASP A1074     -18.168  72.791 140.189  1.00221.56           C  
ANISOU 1986  CB  ASP A1074    25916  26205  32060   3189   -814   -410       C  
ATOM   1987  CG  ASP A1074     -18.792  71.452 139.820  1.00220.32           C  
ANISOU 1987  CG  ASP A1074    25712  26057  31939   3200   -848   -444       C  
ATOM   1988  OD1 ASP A1074     -18.584  70.972 138.686  1.00220.02           O  
ANISOU 1988  OD1 ASP A1074    25685  26022  31887   3227   -860   -462       O  
ATOM   1989  OD2 ASP A1074     -19.496  70.875 140.676  1.00218.58           O  
ANISOU 1989  OD2 ASP A1074    25444  25842  31761   3180   -863   -454       O  
ATOM   1990  N   ALA A1075     -16.686  75.654 139.751  1.00220.92           N  
ANISOU 1990  N   ALA A1075    25963  26103  31872   3201   -747   -351       N  
ATOM   1991  CA  ALA A1075     -16.494  77.082 140.029  1.00219.79           C  
ANISOU 1991  CA  ALA A1075    25866  25952  31690   3202   -721   -326       C  
ATOM   1992  C   ALA A1075     -16.616  77.897 138.739  1.00220.00           C  
ANISOU 1992  C   ALA A1075    25950  25978  31662   3253   -725   -334       C  
ATOM   1993  O   ALA A1075     -17.454  78.805 138.648  1.00220.78           O  
ANISOU 1993  O   ALA A1075    26073  26078  31734   3282   -733   -340       O  
ATOM   1994  CB  ALA A1075     -15.143  77.325 140.686  1.00218.51           C  
ANISOU 1994  CB  ALA A1075    25714  25779  31530   3156   -681   -289       C  
ATOM   1995  N   LEU A1076     -15.798  77.539 137.745  1.00218.26           N  
ANISOU 1995  N   LEU A1076    25749  25754  31423   3265   -719   -337       N  
ATOM   1996  CA  LEU A1076     -15.783  78.186 136.418  1.00216.41           C  
ANISOU 1996  CA  LEU A1076    25570  25518  31137   3314   -721   -345       C  
ATOM   1997  C   LEU A1076     -17.186  78.325 135.825  1.00214.11           C  
ANISOU 1997  C   LEU A1076    25281  25237  30834   3364   -758   -378       C  
ATOM   1998  O   LEU A1076     -17.542  79.394 135.318  1.00214.38           O  
ANISOU 1998  O   LEU A1076    25361  25268  30824   3398   -756   -377       O  
ATOM   1999  CB  LEU A1076     -14.881  77.401 135.448  1.00216.35           C  
ANISOU 1999  CB  LEU A1076    25568  25509  31125   3320   -718   -351       C  
ATOM   2000  CG  LEU A1076     -14.546  78.017 134.085  1.00216.61           C  
ANISOU 2000  CG  LEU A1076    25660  25538  31103   3363   -713   -354       C  
ATOM   2001  CD1 LEU A1076     -13.656  79.243 134.242  1.00216.59           C  
ANISOU 2001  CD1 LEU A1076    25708  25522  31063   3351   -672   -320       C  
ATOM   2002  CD2 LEU A1076     -13.871  76.986 133.193  1.00215.75           C  
ANISOU 2002  CD2 LEU A1076    25543  25430  31000   3369   -718   -366       C  
ATOM   2003  N   LYS A1077     -17.979  77.254 135.928  1.00209.91           N  
ANISOU 2003  N   LYS A1077    24697  24715  30341   3366   -791   -405       N  
ATOM   2004  CA  LYS A1077     -19.405  77.250 135.542  1.00206.59           C  
ANISOU 2004  CA  LYS A1077    24269  24306  29920   3408   -829   -439       C  
ATOM   2005  C   LYS A1077     -20.182  78.488 136.022  1.00206.01           C  
ANISOU 2005  C   LYS A1077    24218  24231  29823   3420   -827   -431       C  
ATOM   2006  O   LYS A1077     -21.060  78.980 135.309  1.00206.25           O  
ANISOU 2006  O   LYS A1077    24272  24267  29825   3467   -848   -452       O  
ATOM   2007  CB  LYS A1077     -20.088  75.972 136.061  1.00204.37           C  
ANISOU 2007  CB  LYS A1077    23920  24035  29695   3391   -857   -462       C  
ATOM   2008  CG  LYS A1077     -21.540  75.792 135.636  1.00202.82           C  
ANISOU 2008  CG  LYS A1077    23708  23850  29502   3433   -898   -499       C  
ATOM   2009  CD  LYS A1077     -22.052  74.409 136.006  1.00200.76           C  
ANISOU 2009  CD  LYS A1077    23382  23598  29297   3417   -924   -523       C  
ATOM   2010  CE  LYS A1077     -23.550  74.288 135.778  1.00199.53           C  
ANISOU 2010  CE  LYS A1077    23207  23454  29149   3453   -964   -559       C  
ATOM   2011  NZ  LYS A1077     -23.929  74.465 134.348  1.00199.05           N  
ANISOU 2011  NZ  LYS A1077    23181  23399  29050   3510   -985   -584       N  
ATOM   2012  N   LEU A1078     -19.859  78.979 137.220  1.00205.21           N  
ANISOU 2012  N   LEU A1078    24110  24123  29734   3379   -801   -403       N  
ATOM   2013  CA  LEU A1078     -20.461  80.216 137.741  1.00204.95           C  
ANISOU 2013  CA  LEU A1078    24103  24089  29680   3386   -795   -391       C  
ATOM   2014  C   LEU A1078     -19.923  81.454 137.020  1.00205.38           C  
ANISOU 2014  C   LEU A1078    24225  24133  29674   3411   -771   -374       C  
ATOM   2015  O   LEU A1078     -20.699  82.332 136.634  1.00207.43           O  
ANISOU 2015  O   LEU A1078    24516  24395  29900   3449   -782   -383       O  
ATOM   2016  CB  LEU A1078     -20.218  80.354 139.248  1.00204.06           C  
ANISOU 2016  CB  LEU A1078    23962  23971  29598   3333   -773   -365       C  
ATOM   2017  CG  LEU A1078     -20.732  79.214 140.138  1.00203.49           C  
ANISOU 2017  CG  LEU A1078    23823  23908  29587   3303   -793   -378       C  
ATOM   2018  CD1 LEU A1078     -20.056  79.251 141.497  1.00203.16           C  
ANISOU 2018  CD1 LEU A1078    23759  23859  29573   3246   -764   -346       C  
ATOM   2019  CD2 LEU A1078     -22.249  79.268 140.280  1.00203.04           C  
ANISOU 2019  CD2 LEU A1078    23744  23861  29540   3330   -827   -405       C  
ATOM   2020  N   ALA A1079     -18.601  81.506 136.825  1.00204.14           N  
ANISOU 2020  N   ALA A1079    24092  23967  29505   3391   -740   -350       N  
ATOM   2021  CA  ALA A1079     -17.919  82.679 136.237  1.00202.44           C  
ANISOU 2021  CA  ALA A1079    23941  23740  29234   3408   -712   -330       C  
ATOM   2022  C   ALA A1079     -18.435  83.098 134.852  1.00201.22           C  
ANISOU 2022  C   ALA A1079    23829  23589  29034   3469   -730   -352       C  
ATOM   2023  O   ALA A1079     -18.338  84.273 134.488  1.00201.23           O  
ANISOU 2023  O   ALA A1079    23884  23583  28989   3491   -714   -339       O  
ATOM   2024  CB  ALA A1079     -16.414  82.447 136.184  1.00202.05           C  
ANISOU 2024  CB  ALA A1079    23903  23681  29183   3376   -678   -305       C  
ATOM   2025  N   ASN A1080     -18.966  82.139 134.092  1.00198.84           N  
ANISOU 2025  N   ASN A1080    23506  23298  28747   3496   -764   -385       N  
ATOM   2026  CA  ASN A1080     -19.636  82.426 132.818  1.00196.27           C  
ANISOU 2026  CA  ASN A1080    23213  22977  28382   3556   -787   -410       C  
ATOM   2027  C   ASN A1080     -20.925  83.229 133.023  1.00194.00           C  
ANISOU 2027  C   ASN A1080    22934  22695  28080   3585   -807   -423       C  
ATOM   2028  O   ASN A1080     -21.222  84.129 132.234  1.00194.03           O  
ANISOU 2028  O   ASN A1080    22986  22696  28036   3628   -808   -427       O  
ATOM   2029  CB  ASN A1080     -19.944  81.129 132.056  1.00195.91           C  
ANISOU 2029  CB  ASN A1080    23134  22942  28360   3575   -820   -444       C  
ATOM   2030  CG  ASN A1080     -18.690  80.403 131.601  1.00195.04           C  
ANISOU 2030  CG  ASN A1080    23024  22826  28254   3556   -803   -435       C  
ATOM   2031  OD1 ASN A1080     -17.618  80.552 132.188  1.00194.02           O  
ANISOU 2031  OD1 ASN A1080    22900  22687  28130   3515   -769   -404       O  
ATOM   2032  ND2 ASN A1080     -18.824  79.602 130.551  1.00194.93           N  
ANISOU 2032  ND2 ASN A1080    23004  22819  28239   3587   -827   -462       N  
ATOM   2033  N   GLU A1081     -21.682  82.901 134.073  1.00190.87           N  
ANISOU 2033  N   GLU A1081    22490  22305  27725   3562   -821   -428       N  
ATOM   2034  CA  GLU A1081     -22.883  83.667 134.437  1.00188.58           C  
ANISOU 2034  CA  GLU A1081    22203  22020  27426   3583   -837   -437       C  
ATOM   2035  C   GLU A1081     -22.503  84.993 135.099  1.00188.64           C  
ANISOU 2035  C   GLU A1081    22249  22017  27407   3566   -803   -403       C  
ATOM   2036  O   GLU A1081     -23.005  86.051 134.710  1.00190.10           O  
ANISOU 2036  O   GLU A1081    22477  22201  27551   3601   -805   -404       O  
ATOM   2037  CB  GLU A1081     -23.794  82.865 135.370  1.00185.28           C  
ANISOU 2037  CB  GLU A1081    21722  21613  27063   3562   -863   -454       C  
ATOM   2038  CG  GLU A1081     -24.370  81.599 134.750  1.00182.69           C  
ANISOU 2038  CG  GLU A1081    21354  21297  26762   3582   -900   -492       C  
ATOM   2039  CD  GLU A1081     -24.904  80.624 135.780  1.00180.23           C  
ANISOU 2039  CD  GLU A1081    20975  20993  26511   3548   -916   -502       C  
ATOM   2040  OE1 GLU A1081     -25.416  81.071 136.829  1.00178.39           O  
ANISOU 2040  OE1 GLU A1081    20727  20760  26294   3527   -913   -492       O  
ATOM   2041  OE2 GLU A1081     -24.822  79.400 135.539  1.00178.60           O  
ANISOU 2041  OE2 GLU A1081    20729  20791  26336   3541   -932   -520       O  
ATOM   2042  N   GLY A1082     -21.621  84.921 136.098  1.00186.87           N  
ANISOU 2042  N   GLY A1082    22009  21785  27207   3513   -773   -374       N  
ATOM   2043  CA  GLY A1082     -21.125  86.094 136.821  1.00184.96           C  
ANISOU 2043  CA  GLY A1082    21799  21532  26944   3490   -738   -339       C  
ATOM   2044  C   GLY A1082     -21.743  86.215 138.200  1.00183.79           C  
ANISOU 2044  C   GLY A1082    21614  21387  26830   3458   -740   -332       C  
ATOM   2045  O   GLY A1082     -22.500  87.153 138.465  1.00183.45           O  
ANISOU 2045  O   GLY A1082    21589  21344  26768   3475   -744   -331       O  
ATOM   2046  N   LYS A1083     -21.428  85.252 139.067  1.00182.24           N  
ANISOU 2046  N   LYS A1083    21365  21193  26684   3413   -738   -327       N  
ATOM   2047  CA  LYS A1083     -21.914  85.230 140.449  1.00180.74           C  
ANISOU 2047  CA  LYS A1083    21135  21005  26532   3377   -738   -319       C  
ATOM   2048  C   LYS A1083     -20.776  84.853 141.399  1.00179.30           C  
ANISOU 2048  C   LYS A1083    20930  20815  26378   3319   -708   -290       C  
ATOM   2049  O   LYS A1083     -20.330  83.703 141.418  1.00178.34           O  
ANISOU 2049  O   LYS A1083    20772  20696  26291   3298   -712   -296       O  
ATOM   2050  CB  LYS A1083     -23.087  84.256 140.592  1.00180.65           C  
ANISOU 2050  CB  LYS A1083    21070  21007  26560   3387   -779   -353       C  
ATOM   2051  CG  LYS A1083     -24.329  84.703 139.836  1.00180.56           C  
ANISOU 2051  CG  LYS A1083    21076  21003  26522   3442   -810   -381       C  
ATOM   2052  CD  LYS A1083     -25.496  83.751 140.026  1.00180.36           C  
ANISOU 2052  CD  LYS A1083    20997  20992  26538   3450   -849   -415       C  
ATOM   2053  CE  LYS A1083     -26.738  84.271 139.322  1.00180.40           C  
ANISOU 2053  CE  LYS A1083    21021  21005  26516   3505   -879   -443       C  
ATOM   2054  NZ  LYS A1083     -27.888  83.332 139.436  1.00180.63           N  
ANISOU 2054  NZ  LYS A1083    20998  21048  26585   3515   -918   -478       N  
ATOM   2055  N   VAL A1084     -20.314  85.835 142.174  1.00178.47           N  
ANISOU 2055  N   VAL A1084    20847  20700  26260   3294   -676   -258       N  
ATOM   2056  CA  VAL A1084     -19.162  85.672 143.067  1.00178.04           C  
ANISOU 2056  CA  VAL A1084    20780  20638  26227   3239   -643   -228       C  
ATOM   2057  C   VAL A1084     -19.550  84.890 144.324  1.00177.09           C  
ANISOU 2057  C   VAL A1084    20597  20523  26163   3200   -653   -229       C  
ATOM   2058  O   VAL A1084     -18.853  83.944 144.700  1.00178.17           O  
ANISOU 2058  O   VAL A1084    20701  20660  26335   3165   -646   -223       O  
ATOM   2059  CB  VAL A1084     -18.546  87.043 143.463  1.00178.16           C  
ANISOU 2059  CB  VAL A1084    20842  20641  26207   3227   -606   -194       C  
ATOM   2060  CG1 VAL A1084     -17.382  86.868 144.440  1.00177.75           C  
ANISOU 2060  CG1 VAL A1084    20774  20581  26179   3170   -572   -163       C  
ATOM   2061  CG2 VAL A1084     -18.089  87.804 142.222  1.00178.10           C  
ANISOU 2061  CG2 VAL A1084    20898  20628  26144   3265   -594   -192       C  
ATOM   2062  N   LYS A1085     -20.663  85.279 144.946  1.00175.28           N  
ANISOU 2062  N   LYS A1085    20354  20300  25943   3206   -669   -236       N  
ATOM   2063  CA  LYS A1085     -21.116  84.708 146.234  1.00173.62           C  
ANISOU 2063  CA  LYS A1085    20089  20094  25784   3168   -676   -235       C  
ATOM   2064  C   LYS A1085     -20.975  83.181 146.251  1.00173.34           C  
ANISOU 2064  C   LYS A1085    20000  20065  25794   3151   -692   -252       C  
ATOM   2065  O   LYS A1085     -20.277  82.617 147.101  1.00172.77           O  
ANISOU 2065  O   LYS A1085    19898  19989  25756   3105   -676   -235       O  
ATOM   2066  CB  LYS A1085     -22.583  85.068 146.535  1.00172.44           C  
ANISOU 2066  CB  LYS A1085    19927  19953  25639   3192   -703   -255       C  
ATOM   2067  CG  LYS A1085     -22.925  86.545 146.674  1.00171.33           C  
ANISOU 2067  CG  LYS A1085    19831  19807  25457   3208   -691   -241       C  
ATOM   2068  CD  LYS A1085     -22.154  87.245 147.782  1.00170.22           C  
ANISOU 2068  CD  LYS A1085    19700  19658  25319   3164   -653   -203       C  
ATOM   2069  CE  LYS A1085     -22.490  88.728 147.801  1.00169.91           C  
ANISOU 2069  CE  LYS A1085    19708  19613  25235   3185   -642   -190       C  
ATOM   2070  NZ  LYS A1085     -21.571  89.519 148.666  1.00169.59           N  
ANISOU 2070  NZ  LYS A1085    19687  19562  25188   3146   -602   -153       N  
ATOM   2071  N   GLU A1086     -21.609  82.532 145.276  1.00173.02           N  
ANISOU 2071  N   GLU A1086    19952  20033  25755   3188   -724   -285       N  
ATOM   2072  CA  GLU A1086     -21.591  81.071 145.153  1.00172.87           C  
ANISOU 2072  CA  GLU A1086    19885  20020  25777   3177   -743   -304       C  
ATOM   2073  C   GLU A1086     -20.172  80.516 144.946  1.00174.06           C  
ANISOU 2073  C   GLU A1086    20038  20164  25932   3151   -719   -287       C  
ATOM   2074  O   GLU A1086     -19.832  79.466 145.508  1.00174.57           O  
ANISOU 2074  O   GLU A1086    20057  20230  26040   3116   -720   -286       O  
ATOM   2075  CB  GLU A1086     -22.514  80.614 144.013  1.00171.71           C  
ANISOU 2075  CB  GLU A1086    19736  19883  25622   3228   -781   -343       C  
ATOM   2076  CG  GLU A1086     -23.998  80.897 144.239  1.00169.89           C  
ANISOU 2076  CG  GLU A1086    19491  19661  25397   3252   -810   -366       C  
ATOM   2077  CD  GLU A1086     -24.829  80.814 142.965  1.00168.10           C  
ANISOU 2077  CD  GLU A1086    19279  19443  25146   3309   -843   -400       C  
ATOM   2078  OE1 GLU A1086     -24.433  81.415 141.944  1.00166.24           O  
ANISOU 2078  OE1 GLU A1086    19094  19204  24865   3341   -836   -398       O  
ATOM   2079  OE2 GLU A1086     -25.895  80.162 142.988  1.00166.59           O  
ANISOU 2079  OE2 GLU A1086    19050  19262  24983   3323   -876   -430       O  
ATOM   2080  N   ALA A1087     -19.341  81.235 144.182  1.00175.21           N  
ANISOU 2080  N   ALA A1087    20237  20302  26033   3165   -697   -272       N  
ATOM   2081  CA  ALA A1087     -17.948  80.816 143.930  1.00175.47           C  
ANISOU 2081  CA  ALA A1087    20277  20328  26065   3142   -672   -255       C  
ATOM   2082  C   ALA A1087     -17.117  80.625 145.209  1.00176.07           C  
ANISOU 2082  C   ALA A1087    20328  20398  26173   3083   -645   -226       C  
ATOM   2083  O   ALA A1087     -16.156  79.845 145.206  1.00177.83           O  
ANISOU 2083  O   ALA A1087    20534  20618  26414   3058   -633   -218       O  
ATOM   2084  CB  ALA A1087     -17.245  81.784 142.982  1.00175.08           C  
ANISOU 2084  CB  ALA A1087    20291  20269  25959   3167   -651   -242       C  
ATOM   2085  N   GLN A1088     -17.486  81.324 146.288  1.00174.80           N  
ANISOU 2085  N   GLN A1088    20162  20235  26018   3063   -635   -210       N  
ATOM   2086  CA  GLN A1088     -16.859  81.111 147.602  1.00173.11           C  
ANISOU 2086  CA  GLN A1088    19918  20017  25838   3009   -612   -185       C  
ATOM   2087  C   GLN A1088     -17.160  79.721 148.190  1.00172.64           C  
ANISOU 2087  C   GLN A1088    19794  19964  25835   2984   -632   -199       C  
ATOM   2088  O   GLN A1088     -16.343  79.188 148.951  1.00172.46           O  
ANISOU 2088  O   GLN A1088    19746  19938  25842   2940   -614   -181       O  
ATOM   2089  CB  GLN A1088     -17.272  82.209 148.590  1.00171.65           C  
ANISOU 2089  CB  GLN A1088    19744  19829  25646   2996   -599   -166       C  
ATOM   2090  CG  GLN A1088     -16.767  83.600 148.218  1.00170.90           C  
ANISOU 2090  CG  GLN A1088    19711  19725  25498   3010   -572   -145       C  
ATOM   2091  CD  GLN A1088     -17.504  84.719 148.934  1.00170.78           C  
ANISOU 2091  CD  GLN A1088    19709  19708  25469   3012   -568   -135       C  
ATOM   2092  OE1 GLN A1088     -18.072  84.525 150.009  1.00170.54           O  
ANISOU 2092  OE1 GLN A1088    19641  19681  25472   2988   -575   -134       O  
ATOM   2093  NE2 GLN A1088     -17.496  85.905 148.334  1.00171.00           N  
ANISOU 2093  NE2 GLN A1088    19793  19731  25448   3041   -557   -128       N  
ATOM   2094  N   ALA A1089     -18.316  79.143 147.843  1.00171.99           N  
ANISOU 2094  N   ALA A1089    19686  19892  25769   3011   -668   -232       N  
ATOM   2095  CA  ALA A1089     -18.649  77.764 148.245  1.00170.59           C  
ANISOU 2095  CA  ALA A1089    19448  19721  25644   2993   -689   -249       C  
ATOM   2096  C   ALA A1089     -17.712  76.730 147.611  1.00169.69           C  
ANISOU 2096  C   ALA A1089    19325  19607  25542   2985   -687   -253       C  
ATOM   2097  O   ALA A1089     -17.349  75.742 148.260  1.00169.17           O  
ANISOU 2097  O   ALA A1089    19215  19541  25518   2950   -685   -250       O  
ATOM   2098  CB  ALA A1089     -20.099  77.433 147.913  1.00170.33           C  
ANISOU 2098  CB  ALA A1089    19394  19700  25623   3028   -729   -285       C  
ATOM   2099  N   ALA A1090     -17.330  76.960 146.353  1.00168.75           N  
ANISOU 2099  N   ALA A1090    19245  19486  25384   3019   -687   -260       N  
ATOM   2100  CA  ALA A1090     -16.346  76.114 145.663  1.00167.72           C  
ANISOU 2100  CA  ALA A1090    19113  19353  25257   3014   -681   -261       C  
ATOM   2101  C   ALA A1090     -14.937  76.279 146.246  1.00166.59           C  
ANISOU 2101  C   ALA A1090    18980  19201  25115   2970   -642   -226       C  
ATOM   2102  O   ALA A1090     -14.209  75.291 146.407  1.00166.71           O  
ANISOU 2102  O   ALA A1090    18966  19216  25160   2943   -637   -223       O  
ATOM   2103  CB  ALA A1090     -16.338  76.418 144.170  1.00167.61           C  
ANISOU 2103  CB  ALA A1090    19142  19340  25199   3062   -690   -277       C  
ATOM   2104  N   ALA A1091     -14.570  77.525 146.563  1.00165.15           N  
ANISOU 2104  N   ALA A1091    18837  19011  24901   2965   -615   -201       N  
ATOM   2105  CA  ALA A1091     -13.265  77.847 147.165  1.00163.87           C  
ANISOU 2105  CA  ALA A1091    18687  18839  24736   2924   -576   -167       C  
ATOM   2106  C   ALA A1091     -12.994  77.088 148.469  1.00163.37           C  
ANISOU 2106  C   ALA A1091    18572  18776  24723   2873   -569   -154       C  
ATOM   2107  O   ALA A1091     -11.881  76.597 148.679  1.00163.17           O  
ANISOU 2107  O   ALA A1091    18538  18746  24712   2842   -549   -139       O  
ATOM   2108  CB  ALA A1091     -13.145  79.348 147.398  1.00162.82           C  
ANISOU 2108  CB  ALA A1091    18601  18699  24563   2928   -552   -144       C  
ATOM   2109  N   GLU A1092     -14.010  76.996 149.331  1.00162.66           N  
ANISOU 2109  N   GLU A1092    18449  18691  24661   2866   -586   -162       N  
ATOM   2110  CA  GLU A1092     -13.916  76.210 150.573  1.00161.64           C  
ANISOU 2110  CA  GLU A1092    18267  18563  24583   2821   -583   -154       C  
ATOM   2111  C   GLU A1092     -13.699  74.713 150.317  1.00161.04           C  
ANISOU 2111  C   GLU A1092    18150  18492  24544   2812   -599   -171       C  
ATOM   2112  O   GLU A1092     -12.963  74.056 151.057  1.00159.77           O  
ANISOU 2112  O   GLU A1092    17960  18329  24415   2771   -585   -156       O  
ATOM   2113  CB  GLU A1092     -15.169  76.393 151.436  1.00161.54           C  
ANISOU 2113  CB  GLU A1092    18228  18556  24591   2820   -601   -162       C  
ATOM   2114  CG  GLU A1092     -15.315  77.779 152.042  1.00161.86           C  
ANISOU 2114  CG  GLU A1092    18301  18592  24606   2816   -582   -140       C  
ATOM   2115  CD  GLU A1092     -16.590  77.933 152.853  1.00162.53           C  
ANISOU 2115  CD  GLU A1092    18359  18682  24712   2817   -601   -150       C  
ATOM   2116  OE1 GLU A1092     -16.906  77.027 153.655  1.00162.24           O  
ANISOU 2116  OE1 GLU A1092    18272  18650  24722   2791   -612   -156       O  
ATOM   2117  OE2 GLU A1092     -17.275  78.966 152.693  1.00163.38           O  
ANISOU 2117  OE2 GLU A1092    18496  18790  24789   2843   -605   -152       O  
ATOM   2118  N   GLN A1093     -14.350  74.187 149.276  1.00161.09           N  
ANISOU 2118  N   GLN A1093    18154  18505  24547   2850   -629   -202       N  
ATOM   2119  CA  GLN A1093     -14.206  72.778 148.886  1.00160.79           C  
ANISOU 2119  CA  GLN A1093    18079  18472  24541   2847   -646   -221       C  
ATOM   2120  C   GLN A1093     -12.833  72.505 148.251  1.00160.80           C  
ANISOU 2120  C   GLN A1093    18101  18468  24528   2838   -625   -209       C  
ATOM   2121  O   GLN A1093     -12.214  71.459 148.516  1.00161.06           O  
ANISOU 2121  O   GLN A1093    18100  18500  24594   2811   -622   -207       O  
ATOM   2122  CB  GLN A1093     -15.328  72.365 147.921  1.00160.69           C  
ANISOU 2122  CB  GLN A1093    18060  18468  24526   2893   -684   -259       C  
ATOM   2123  CG  GLN A1093     -16.747  72.482 148.479  1.00160.01           C  
ANISOU 2123  CG  GLN A1093    17949  18389  24458   2903   -709   -276       C  
ATOM   2124  CD  GLN A1093     -17.175  71.292 149.324  1.00159.03           C  
ANISOU 2124  CD  GLN A1093    17762  18269  24391   2875   -724   -286       C  
ATOM   2125  OE1 GLN A1093     -16.355  70.635 149.965  1.00158.14           O  
ANISOU 2125  OE1 GLN A1093    17625  18153  24307   2835   -708   -271       O  
ATOM   2126  NE2 GLN A1093     -18.474  71.014 149.333  1.00158.44           N  
ANISOU 2126  NE2 GLN A1093    17663  18203  24333   2896   -755   -314       N  
ATOM   2127  N   LEU A1094     -12.365  73.440 147.417  1.00160.32           N  
ANISOU 2127  N   LEU A1094    18094  18402  24418   2862   -611   -200       N  
ATOM   2128  CA  LEU A1094     -11.023  73.353 146.812  1.00158.96           C  
ANISOU 2128  CA  LEU A1094    17946  18223  24227   2855   -587   -186       C  
ATOM   2129  C   LEU A1094      -9.899  73.286 147.859  1.00157.32           C  
ANISOU 2129  C   LEU A1094    17726  18008  24038   2803   -554   -155       C  
ATOM   2130  O   LEU A1094      -8.922  72.551 147.669  1.00157.60           O  
ANISOU 2130  O   LEU A1094    17752  18041  24085   2784   -544   -149       O  
ATOM   2131  CB  LEU A1094     -10.775  74.523 145.848  1.00159.25           C  
ANISOU 2131  CB  LEU A1094    18046  18254  24206   2889   -574   -180       C  
ATOM   2132  CG  LEU A1094     -11.561  74.492 144.527  1.00159.72           C  
ANISOU 2132  CG  LEU A1094    18126  18320  24241   2943   -603   -211       C  
ATOM   2133  CD1 LEU A1094     -11.505  75.847 143.836  1.00159.77           C  
ANISOU 2133  CD1 LEU A1094    18194  18321  24190   2975   -590   -203       C  
ATOM   2134  CD2 LEU A1094     -11.059  73.393 143.587  1.00159.73           C  
ANISOU 2134  CD2 LEU A1094    18116  18324  24250   2953   -614   -228       C  
ATOM   2135  N   LYS A1095     -10.041  74.047 148.948  1.00155.35           N  
ANISOU 2135  N   LYS A1095    17477  17755  23792   2779   -539   -134       N  
ATOM   2136  CA  LYS A1095      -9.108  73.964 150.086  1.00153.95           C  
ANISOU 2136  CA  LYS A1095    17283  17573  23637   2728   -511   -106       C  
ATOM   2137  C   LYS A1095      -9.149  72.599 150.790  1.00153.57           C  
ANISOU 2137  C   LYS A1095    17175  17530  23644   2698   -523   -113       C  
ATOM   2138  O   LYS A1095      -8.111  72.098 151.233  1.00152.84           O  
ANISOU 2138  O   LYS A1095    17068  17433  23570   2663   -503    -96       O  
ATOM   2139  CB  LYS A1095      -9.377  75.083 151.100  1.00152.99           C  
ANISOU 2139  CB  LYS A1095    17173  17448  23507   2713   -494    -84       C  
ATOM   2140  CG  LYS A1095      -9.025  76.473 150.601  1.00152.35           C  
ANISOU 2140  CG  LYS A1095    17152  17360  23373   2732   -472    -69       C  
ATOM   2141  CD  LYS A1095      -9.429  77.537 151.607  1.00151.61           C  
ANISOU 2141  CD  LYS A1095    17068  17263  23273   2718   -459    -51       C  
ATOM   2142  CE  LYS A1095      -8.923  78.912 151.204  1.00151.04           C  
ANISOU 2142  CE  LYS A1095    17054  17182  23149   2731   -433    -32       C  
ATOM   2143  NZ  LYS A1095      -9.180  79.919 152.269  1.00150.61           N  
ANISOU 2143  NZ  LYS A1095    17007  17124  23091   2713   -417    -12       N  
ATOM   2144  N   THR A1096     -10.343  72.012 150.895  1.00154.10           N  
ANISOU 2144  N   THR A1096    17208  17605  23738   2712   -555   -138       N  
ATOM   2145  CA  THR A1096     -10.509  70.649 151.423  1.00154.62           C  
ANISOU 2145  CA  THR A1096    17216  17675  23855   2689   -571   -150       C  
ATOM   2146  C   THR A1096      -9.849  69.622 150.498  1.00155.44           C  
ANISOU 2146  C   THR A1096    17313  17780  23965   2696   -577   -162       C  
ATOM   2147  O   THR A1096      -9.133  68.736 150.969  1.00155.30           O  
ANISOU 2147  O   THR A1096    17266  17761  23979   2663   -568   -155       O  
ATOM   2148  CB  THR A1096     -11.998  70.270 151.611  1.00154.83           C  
ANISOU 2148  CB  THR A1096    17210  17709  23906   2707   -605   -177       C  
ATOM   2149  OG1 THR A1096     -12.706  71.355 152.226  1.00155.73           O  
ANISOU 2149  OG1 THR A1096    17339  17823  24006   2710   -602   -168       O  
ATOM   2150  CG2 THR A1096     -12.141  69.015 152.475  1.00154.48           C  
ANISOU 2150  CG2 THR A1096    17107  17669  23919   2674   -615   -182       C  
ATOM   2151  N   THR A1097     -10.095  69.752 149.191  1.00157.30           N  
ANISOU 2151  N   THR A1097    17578  18018  24170   2739   -592   -182       N  
ATOM   2152  CA  THR A1097      -9.451  68.894 148.179  1.00158.58           C  
ANISOU 2152  CA  THR A1097    17740  18181  24331   2750   -597   -194       C  
ATOM   2153  C   THR A1097      -7.919  69.016 148.205  1.00159.40           C  
ANISOU 2153  C   THR A1097    17864  18277  24423   2723   -562   -167       C  
ATOM   2154  O   THR A1097      -7.207  68.002 148.161  1.00160.02           O  
ANISOU 2154  O   THR A1097    17918  18355  24525   2703   -560   -168       O  
ATOM   2155  CB  THR A1097      -9.971  69.211 146.759  1.00158.98           C  
ANISOU 2155  CB  THR A1097    17825  18234  24343   2803   -616   -218       C  
ATOM   2156  OG1 THR A1097     -11.380  68.971 146.704  1.00159.94           O  
ANISOU 2156  OG1 THR A1097    17924  18364  24480   2828   -650   -246       O  
ATOM   2157  CG2 THR A1097      -9.287  68.322 145.705  1.00158.91           C  
ANISOU 2157  CG2 THR A1097    17816  18226  24333   2814   -622   -230       C  
ATOM   2158  N   ARG A1098      -7.435  70.257 148.277  1.00160.33           N  
ANISOU 2158  N   ARG A1098    18026  18388  24504   2721   -536   -144       N  
ATOM   2159  CA  ARG A1098      -5.998  70.559 148.373  1.00160.62           C  
ANISOU 2159  CA  ARG A1098    18085  18416  24525   2695   -500   -116       C  
ATOM   2160  C   ARG A1098      -5.336  69.814 149.534  1.00160.80           C  
ANISOU 2160  C   ARG A1098    18066  18438  24592   2645   -486   -100       C  
ATOM   2161  O   ARG A1098      -4.377  69.050 149.331  1.00161.07           O  
ANISOU 2161  O   ARG A1098    18090  18470  24638   2628   -477    -96       O  
ATOM   2162  CB  ARG A1098      -5.782  72.073 148.528  1.00160.49           C  
ANISOU 2162  CB  ARG A1098    18117  18393  24468   2698   -475    -94       C  
ATOM   2163  CG  ARG A1098      -4.326  72.519 148.618  1.00160.75           C  
ANISOU 2163  CG  ARG A1098    18177  18417  24483   2672   -437    -65       C  
ATOM   2164  CD  ARG A1098      -4.207  74.031 148.509  1.00160.97           C  
ANISOU 2164  CD  ARG A1098    18257  18438  24464   2684   -415    -48       C  
ATOM   2165  NE  ARG A1098      -4.930  74.737 149.571  1.00160.77           N  
ANISOU 2165  NE  ARG A1098    18225  18413  24446   2673   -413    -38       N  
ATOM   2166  CZ  ARG A1098      -4.514  74.884 150.832  1.00160.43           C  
ANISOU 2166  CZ  ARG A1098    18164  18367  24425   2630   -393    -14       C  
ATOM   2167  NH1 ARG A1098      -3.361  74.373 151.252  1.00160.20           N  
ANISOU 2167  NH1 ARG A1098    18120  18334  24413   2594   -372      1       N  
ATOM   2168  NH2 ARG A1098      -5.267  75.551 151.700  1.00160.65           N  
ANISOU 2168  NH2 ARG A1098    18188  18396  24457   2624   -394     -8       N  
ATOM   2169  N   ASN A1099      -5.876  70.029 150.733  1.00161.28           N  
ANISOU 2169  N   ASN A1099    18104  18499  24675   2622   -486    -91       N  
ATOM   2170  CA  ASN A1099      -5.363  69.399 151.957  1.00161.30           C  
ANISOU 2170  CA  ASN A1099    18066  18501  24719   2574   -473    -74       C  
ATOM   2171  C   ASN A1099      -5.607  67.890 151.994  1.00160.98           C  
ANISOU 2171  C   ASN A1099    17975  18466  24724   2566   -497    -94       C  
ATOM   2172  O   ASN A1099      -4.830  67.159 152.612  1.00161.18           O  
ANISOU 2172  O   ASN A1099    17972  18489  24778   2530   -484    -83       O  
ATOM   2173  CB  ASN A1099      -5.982  70.043 153.206  1.00162.36           C  
ANISOU 2173  CB  ASN A1099    18188  18634  24865   2555   -468    -61       C  
ATOM   2174  CG  ASN A1099      -5.608  71.504 153.361  1.00164.22           C  
ANISOU 2174  CG  ASN A1099    18471  18863  25060   2554   -441    -37       C  
ATOM   2175  OD1 ASN A1099      -5.318  72.192 152.381  1.00166.28           O  
ANISOU 2175  OD1 ASN A1099    18777  19121  25279   2581   -434    -37       O  
ATOM   2176  ND2 ASN A1099      -5.612  71.986 154.600  1.00164.61           N  
ANISOU 2176  ND2 ASN A1099    18509  18910  25122   2523   -426    -17       N  
ATOM   2177  N   ALA A1100      -6.684  67.431 151.348  1.00160.63           N  
ANISOU 2177  N   ALA A1100    17918  18428  24685   2599   -530   -125       N  
ATOM   2178  CA  ALA A1100      -6.975  65.998 151.247  1.00159.53           C  
ANISOU 2178  CA  ALA A1100    17731  18294  24586   2597   -554   -147       C  
ATOM   2179  C   ALA A1100      -5.980  65.270 150.341  1.00158.60           C  
ANISOU 2179  C   ALA A1100    17620  18176  24464   2599   -549   -151       C  
ATOM   2180  O   ALA A1100      -5.364  64.291 150.764  1.00159.30           O  
ANISOU 2180  O   ALA A1100    17676  18264  24586   2570   -545   -146       O  
ATOM   2181  CB  ALA A1100      -8.398  65.772 150.758  1.00159.68           C  
ANISOU 2181  CB  ALA A1100    17739  18322  24611   2633   -590   -179       C  
ATOM   2182  N   TYR A1101      -5.829  65.754 149.107  1.00157.33           N  
ANISOU 2182  N   TYR A1101    17500  18014  24261   2635   -551   -159       N  
ATOM   2183  CA  TYR A1101      -5.032  65.058 148.080  1.00156.49           C  
ANISOU 2183  CA  TYR A1101    17401  17907  24148   2645   -551   -167       C  
ATOM   2184  C   TYR A1101      -3.691  65.715 147.725  1.00154.55           C  
ANISOU 2184  C   TYR A1101    17198  17654  23868   2636   -518   -143       C  
ATOM   2185  O   TYR A1101      -2.661  65.031 147.663  1.00153.28           O  
ANISOU 2185  O   TYR A1101    17027  17491  23720   2615   -505   -135       O  
ATOM   2186  CB  TYR A1101      -5.864  64.881 146.803  1.00157.73           C  
ANISOU 2186  CB  TYR A1101    17570  18070  24288   2694   -581   -199       C  
ATOM   2187  CG  TYR A1101      -7.084  64.000 146.985  1.00159.51           C  
ANISOU 2187  CG  TYR A1101    17750  18304  24550   2704   -616   -227       C  
ATOM   2188  CD1 TYR A1101      -8.304  64.541 147.406  1.00160.63           C  
ANISOU 2188  CD1 TYR A1101    17888  18449  24693   2717   -632   -236       C  
ATOM   2189  CD2 TYR A1101      -7.021  62.616 146.759  1.00159.76           C  
ANISOU 2189  CD2 TYR A1101    17743  18339  24617   2698   -633   -245       C  
ATOM   2190  CE1 TYR A1101      -9.425  63.739 147.573  1.00160.96           C  
ANISOU 2190  CE1 TYR A1101    17888  18499  24770   2725   -663   -262       C  
ATOM   2191  CE2 TYR A1101      -8.139  61.812 146.927  1.00160.33           C  
ANISOU 2191  CE2 TYR A1101    17774  18418  24723   2706   -664   -271       C  
ATOM   2192  CZ  TYR A1101      -9.342  62.378 147.327  1.00160.90           C  
ANISOU 2192  CZ  TYR A1101    17843  18494  24796   2720   -679   -279       C  
ATOM   2193  OH  TYR A1101     -10.447  61.579 147.514  1.00160.99           O  
ANISOU 2193  OH  TYR A1101    17813  18513  24843   2727   -709   -306       O  
ATOM   2194  N   ILE A1102      -3.694  67.031 147.509  1.00153.41           N  
ANISOU 2194  N   ILE A1102    17100  17506  23682   2652   -503   -131       N  
ATOM   2195  CA  ILE A1102      -2.581  67.692 146.798  1.00152.52           C  
ANISOU 2195  CA  ILE A1102    17034  17386  23528   2657   -476   -115       C  
ATOM   2196  C   ILE A1102      -1.281  67.769 147.619  1.00151.56           C  
ANISOU 2196  C   ILE A1102    16911  17258  23416   2611   -441    -84       C  
ATOM   2197  O   ILE A1102      -0.182  67.696 147.046  1.00153.13           O  
ANISOU 2197  O   ILE A1102    17130  17452  23599   2607   -423    -76       O  
ATOM   2198  CB  ILE A1102      -2.995  69.090 146.257  1.00152.48           C  
ANISOU 2198  CB  ILE A1102    17082  17377  23474   2690   -471   -112       C  
ATOM   2199  CG1 ILE A1102      -4.251  68.984 145.366  1.00152.36           C  
ANISOU 2199  CG1 ILE A1102    17070  17370  23449   2738   -506   -144       C  
ATOM   2200  CG2 ILE A1102      -1.852  69.760 145.498  1.00152.71           C  
ANISOU 2200  CG2 ILE A1102    17160  17399  23461   2696   -443    -97       C  
ATOM   2201  CD1 ILE A1102      -4.147  68.003 144.213  1.00152.35           C  
ANISOU 2201  CD1 ILE A1102    17063  17373  23450   2762   -526   -168       C  
ATOM   2202  N   GLN A1103      -1.398  67.901 148.944  1.00149.17           N  
ANISOU 2202  N   GLN A1103    16584  16954  23139   2577   -432    -68       N  
ATOM   2203  CA  GLN A1103      -0.223  67.865 149.837  1.00147.37           C  
ANISOU 2203  CA  GLN A1103    16347  16721  22925   2532   -401    -40       C  
ATOM   2204  C   GLN A1103       0.670  66.633 149.633  1.00147.31           C  
ANISOU 2204  C   GLN A1103    16313  16714  22942   2513   -400    -43       C  
ATOM   2205  O   GLN A1103       1.895  66.744 149.694  1.00147.35           O  
ANISOU 2205  O   GLN A1103    16332  16714  22939   2491   -372    -24       O  
ATOM   2206  CB  GLN A1103      -0.637  67.958 151.313  1.00145.54           C  
ANISOU 2206  CB  GLN A1103    16084  16490  22724   2499   -397    -27       C  
ATOM   2207  CG  GLN A1103      -0.916  69.381 151.797  1.00144.14           C  
ANISOU 2207  CG  GLN A1103    15939  16309  22519   2500   -381    -10       C  
ATOM   2208  CD  GLN A1103      -0.957  69.483 153.317  1.00142.96           C  
ANISOU 2208  CD  GLN A1103    15760  16158  22398   2460   -370      8       C  
ATOM   2209  OE1 GLN A1103      -0.057  69.009 154.010  1.00141.63           O  
ANISOU 2209  OE1 GLN A1103    15571  15988  22253   2423   -352     24       O  
ATOM   2210  NE2 GLN A1103      -1.998  70.109 153.839  1.00142.68           N  
ANISOU 2210  NE2 GLN A1103    15724  16125  22362   2468   -380      6       N  
ATOM   2211  N   LYS A1104       0.053  65.478 149.389  1.00153.13           N  
ANISOU 2211  N   LYS A1104    19948  21713  16522   3176   2441   1464       N  
ATOM   2212  CA  LYS A1104       0.782  64.223 149.155  1.00151.08           C  
ANISOU 2212  CA  LYS A1104    19714  21394  16294   2970   2401   1569       C  
ATOM   2213  C   LYS A1104       1.740  64.333 147.960  1.00147.39           C  
ANISOU 2213  C   LYS A1104    19374  20642  15984   2896   2351   1567       C  
ATOM   2214  O   LYS A1104       2.939  64.051 148.094  1.00146.32           O  
ANISOU 2214  O   LYS A1104    19335  20361  15896   2804   2315   1535       O  
ATOM   2215  CB  LYS A1104      -0.207  63.075 148.940  1.00152.16           C  
ANISOU 2215  CB  LYS A1104    19714  21731  16366   2867   2410   1738       C  
ATOM   2216  CG  LYS A1104       0.409  61.692 148.794  1.00151.87           C  
ANISOU 2216  CG  LYS A1104    19692  21661  16350   2658   2364   1854       C  
ATOM   2217  CD  LYS A1104      -0.661  60.691 148.359  1.00152.26           C  
ANISOU 2217  CD  LYS A1104    19613  21881  16357   2565   2365   2022       C  
ATOM   2218  CE  LYS A1104      -0.089  59.409 147.769  1.00151.17           C  
ANISOU 2218  CE  LYS A1104    19505  21650  16281   2363   2304   2139       C  
ATOM   2219  NZ  LYS A1104      -1.017  58.824 146.759  1.00151.17           N  
ANISOU 2219  NZ  LYS A1104    19423  21709  16305   2300   2294   2275       N  
ATOM   2220  N   TYR A1105       1.205  64.758 146.813  1.00144.17           N  
ANISOU 2220  N   TYR A1105    18961  20164  15652   2938   2349   1601       N  
ATOM   2221  CA  TYR A1105       2.005  64.925 145.588  1.00141.56           C  
ANISOU 2221  CA  TYR A1105    18740  19579  15467   2876   2304   1606       C  
ATOM   2222  C   TYR A1105       3.166  65.893 145.829  1.00139.97           C  
ANISOU 2222  C   TYR A1105    18678  19171  15331   2933   2284   1459       C  
ATOM   2223  O   TYR A1105       4.331  65.572 145.524  1.00139.67           O  
ANISOU 2223  O   TYR A1105    18736  18964  15367   2822   2243   1452       O  
ATOM   2224  CB  TYR A1105       1.131  65.425 144.428  1.00141.77           C  
ANISOU 2224  CB  TYR A1105    18732  19583  15550   2944   2310   1652       C  
ATOM   2225  CG  TYR A1105       1.804  65.412 143.064  1.00139.93           C  
ANISOU 2225  CG  TYR A1105    18588  19124  15455   2861   2265   1687       C  
ATOM   2226  CD1 TYR A1105       1.831  64.252 142.284  1.00138.65           C  
ANISOU 2226  CD1 TYR A1105    18396  18962  15323   2702   2236   1817       C  
ATOM   2227  CD2 TYR A1105       2.399  66.565 142.542  1.00139.19           C  
ANISOU 2227  CD2 TYR A1105    18606  18820  15458   2940   2248   1592       C  
ATOM   2228  CE1 TYR A1105       2.440  64.238 141.033  1.00137.32           C  
ANISOU 2228  CE1 TYR A1105    18302  18601  15272   2630   2195   1846       C  
ATOM   2229  CE2 TYR A1105       3.009  66.562 141.292  1.00137.72           C  
ANISOU 2229  CE2 TYR A1105    18494  18441  15390   2862   2208   1629       C  
ATOM   2230  CZ  TYR A1105       3.028  65.398 140.541  1.00136.99           C  
ANISOU 2230  CZ  TYR A1105    18365  18364  15320   2710   2184   1753       C  
ATOM   2231  OH  TYR A1105       3.631  65.390 139.302  1.00135.18           O  
ANISOU 2231  OH  TYR A1105    18204  17956  15200   2636   2144   1786       O  
ATOM   2232  N   LEU A1106       2.841  67.056 146.402  1.00139.12           N  
ANISOU 2232  N   LEU A1106    18581  19085  15193   3107   2312   1340       N  
ATOM   2233  CA  LEU A1106       3.841  68.065 146.749  1.00138.83           C  
ANISOU 2233  CA  LEU A1106    18673  18867  15210   3176   2293   1192       C  
ATOM   2234  C   LEU A1106       4.938  67.497 147.652  1.00137.73           C  
ANISOU 2234  C   LEU A1106    18584  18708  15039   3078   2276   1153       C  
ATOM   2235  O   LEU A1106       6.120  67.594 147.322  1.00136.79           O  
ANISOU 2235  O   LEU A1106    18578  18387  15009   3006   2236   1114       O  
ATOM   2236  CB  LEU A1106       3.182  69.263 147.445  1.00140.76           C  
ANISOU 2236  CB  LEU A1106    18899  19181  15400   3383   2324   1070       C  
ATOM   2237  CG  LEU A1106       4.100  70.446 147.828  1.00141.29           C  
ANISOU 2237  CG  LEU A1106    19099  19060  15523   3475   2300    906       C  
ATOM   2238  CD1 LEU A1106       4.548  71.221 146.583  1.00140.70           C  
ANISOU 2238  CD1 LEU A1106    19131  18731  15597   3481   2260    895       C  
ATOM   2239  CD2 LEU A1106       3.396  71.335 148.838  1.00143.01           C  
ANISOU 2239  CD2 LEU A1106    19275  19409  15650   3670   2333    787       C  
ATOM   2240  N   GLU A 220       4.536  66.912 148.780  1.00137.85           N  
ANISOU 2240  N   GLU A 220    18512  18939  14926   3076   2306   1166       N  
ATOM   2241  CA  GLU A 220       5.484  66.358 149.762  1.00137.14           C  
ANISOU 2241  CA  GLU A 220    18459  18857  14789   2992   2293   1130       C  
ATOM   2242  C   GLU A 220       6.340  65.215 149.193  1.00134.29           C  
ANISOU 2242  C   GLU A 220    18137  18396  14489   2795   2248   1227       C  
ATOM   2243  O   GLU A 220       7.560  65.184 149.417  1.00134.23           O  
ANISOU 2243  O   GLU A 220    18228  18248  14525   2734   2215   1167       O  
ATOM   2244  CB  GLU A 220       4.754  65.893 151.032  1.00138.60           C  
ANISOU 2244  CB  GLU A 220    18528  19318  14815   3024   2334   1145       C  
ATOM   2245  CG  GLU A 220       4.213  67.024 151.897  1.00141.00           C  
ANISOU 2245  CG  GLU A 220    18809  19719  15044   3222   2373   1011       C  
ATOM   2246  CD  GLU A 220       3.278  66.539 153.000  1.00143.25           C  
ANISOU 2246  CD  GLU A 220    18954  20311  15163   3256   2421   1046       C  
ATOM   2247  OE1 GLU A 220       3.377  65.365 153.412  1.00144.58           O  
ANISOU 2247  OE1 GLU A 220    19068  20594  15268   3118   2417   1146       O  
ATOM   2248  OE2 GLU A 220       2.442  67.335 153.472  1.00144.38           O  
ANISOU 2248  OE2 GLU A 220    19037  20585  15235   3423   2459    971       O  
ATOM   2249  N   ARG A 221       5.708  64.298 148.453  1.00131.38           N  
ANISOU 2249  N   ARG A 221    17692  18098  14125   2702   2243   1372       N  
ATOM   2250  CA  ARG A 221       6.435  63.178 147.836  1.00128.40           C  
ANISOU 2250  CA  ARG A 221    17347  17630  13808   2522   2195   1466       C  
ATOM   2251  C   ARG A 221       7.399  63.654 146.731  1.00125.65           C  
ANISOU 2251  C   ARG A 221    17118  17019  13602   2491   2155   1427       C  
ATOM   2252  O   ARG A 221       8.550  63.175 146.653  1.00124.59           O  
ANISOU 2252  O   ARG A 221    17061  16761  13517   2382   2113   1418       O  
ATOM   2253  CB  ARG A 221       5.462  62.118 147.291  1.00128.26           C  
ANISOU 2253  CB  ARG A 221    17218  17752  13763   2435   2195   1628       C  
ATOM   2254  CG  ARG A 221       5.959  60.687 147.384  1.00127.46           C  
ANISOU 2254  CG  ARG A 221    17108  17669  13650   2257   2153   1726       C  
ATOM   2255  CD  ARG A 221       5.996  60.212 148.832  1.00128.58           C  
ANISOU 2255  CD  ARG A 221    17207  17976  13670   2241   2167   1717       C  
ATOM   2256  NE  ARG A 221       5.924  58.758 148.952  1.00129.21           N  
ANISOU 2256  NE  ARG A 221    17232  18147  13712   2083   2133   1851       N  
ATOM   2257  CZ  ARG A 221       6.003  58.082 150.103  1.00131.19           C  
ANISOU 2257  CZ  ARG A 221    17446  18538  13863   2031   2131   1876       C  
ATOM   2258  NH1 ARG A 221       6.169  58.713 151.268  1.00132.34           N  
ANISOU 2258  NH1 ARG A 221    17596  18757  13928   2125   2166   1772       N  
ATOM   2259  NH2 ARG A 221       5.918  56.754 150.086  1.00131.23           N  
ANISOU 2259  NH2 ARG A 221    17407  18606  13848   1882   2091   2007       N  
ATOM   2260  N   ALA A 222       6.935  64.599 145.903  1.00123.40           N  
ANISOU 2260  N   ALA A 222    16847  16658  13379   2588   2166   1405       N  
ATOM   2261  CA  ALA A 222       7.804  65.227 144.901  1.00121.08           C  
ANISOU 2261  CA  ALA A 222    16666  16123  13215   2575   2131   1361       C  
ATOM   2262  C   ALA A 222       8.987  65.945 145.562  1.00120.14           C  
ANISOU 2262  C   ALA A 222    16660  15867  13121   2604   2115   1223       C  
ATOM   2263  O   ALA A 222      10.149  65.759 145.151  1.00119.27           O  
ANISOU 2263  O   ALA A 222    16635  15595  13084   2507   2074   1208       O  
ATOM   2264  CB  ALA A 222       7.015  66.200 144.039  1.00121.47           C  
ANISOU 2264  CB  ALA A 222    16707  16129  13315   2689   2147   1359       C  
ATOM   2265  N   ARG A 223       8.684  66.750 146.586  1.00120.42           N  
ANISOU 2265  N   ARG A 223    16690  15973  13089   2738   2146   1120       N  
ATOM   2266  CA  ARG A 223       9.710  67.386 147.423  1.00120.27           C  
ANISOU 2266  CA  ARG A 223    16766  15856  13073   2772   2133    984       C  
ATOM   2267  C   ARG A 223      10.719  66.365 147.915  1.00118.90           C  
ANISOU 2267  C   ARG A 223    16617  15679  12880   2629   2107   1002       C  
ATOM   2268  O   ARG A 223      11.914  66.519 147.671  1.00118.94           O  
ANISOU 2268  O   ARG A 223    16722  15509  12959   2567   2069    952       O  
ATOM   2269  CB  ARG A 223       9.098  68.089 148.647  1.00121.77           C  
ANISOU 2269  CB  ARG A 223    16919  16185  13163   2927   2173    884       C  
ATOM   2270  CG  ARG A 223       8.596  69.503 148.414  1.00123.26           C  
ANISOU 2270  CG  ARG A 223    17138  16304  13389   3097   2183    793       C  
ATOM   2271  CD  ARG A 223       8.005  70.047 149.707  1.00125.48           C  
ANISOU 2271  CD  ARG A 223    17372  16745  13557   3246   2220    693       C  
ATOM   2272  NE  ARG A 223       7.265  71.294 149.515  1.00127.62           N  
ANISOU 2272  NE  ARG A 223    17649  16990  13848   3424   2231    617       N  
ATOM   2273  CZ  ARG A 223       6.552  71.916 150.458  1.00129.34           C  
ANISOU 2273  CZ  ARG A 223    17818  17349  13974   3585   2262    525       C  
ATOM   2274  NH1 ARG A 223       6.463  71.428 151.696  1.00130.08           N  
ANISOU 2274  NH1 ARG A 223    17849  17632  13941   3589   2291    498       N  
ATOM   2275  NH2 ARG A 223       5.906  73.035 150.154  1.00130.40           N  
ANISOU 2275  NH2 ARG A 223    17965  17440  14141   3745   2263    459       N  
ATOM   2276  N   SER A 224      10.232  65.318 148.585  1.00118.08           N  
ANISOU 2276  N   SER A 224    16420  15768  12675   2575   2123   1078       N  
ATOM   2277  CA  SER A 224      11.120  64.304 149.173  1.00116.30           C  
ANISOU 2277  CA  SER A 224    16213  15555  12420   2445   2095   1098       C  
ATOM   2278  C   SER A 224      11.965  63.598 148.112  1.00113.17           C  
ANISOU 2278  C   SER A 224    15870  15006  12124   2300   2044   1165       C  
ATOM   2279  O   SER A 224      13.186  63.497 148.275  1.00112.70           O  
ANISOU 2279  O   SER A 224    15892  14825  12101   2234   2010   1110       O  
ATOM   2280  CB  SER A 224      10.339  63.280 150.014  1.00117.12           C  
ANISOU 2280  CB  SER A 224    16201  15901  12398   2408   2118   1186       C  
ATOM   2281  OG  SER A 224       9.594  62.385 149.204  1.00117.66           O  
ANISOU 2281  OG  SER A 224    16191  16037  12475   2327   2112   1333       O  
ATOM   2282  N   THR A 225      11.329  63.144 147.025  1.00110.82           N  
ANISOU 2282  N   THR A 225    15524  14715  11867   2254   2039   1276       N  
ATOM   2283  CA  THR A 225      12.058  62.431 145.959  1.00108.40           C  
ANISOU 2283  CA  THR A 225    15258  14276  11650   2121   1989   1341       C  
ATOM   2284  C   THR A 225      13.061  63.324 145.203  1.00106.38           C  
ANISOU 2284  C   THR A 225    15115  13796  11506   2131   1964   1259       C  
ATOM   2285  O   THR A 225      14.162  62.859 144.852  1.00105.66           O  
ANISOU 2285  O   THR A 225    15085  13589  11470   2026   1920   1256       O  
ATOM   2286  CB  THR A 225      11.107  61.745 144.959  1.00108.16           C  
ANISOU 2286  CB  THR A 225    15147  14311  11636   2072   1987   1477       C  
ATOM   2287  OG1 THR A 225      10.144  62.692 144.479  1.00110.54           O  
ANISOU 2287  OG1 THR A 225    15417  14630  11950   2193   2024   1470       O  
ATOM   2288  CG2 THR A 225      10.378  60.584 145.624  1.00108.40           C  
ANISOU 2288  CG2 THR A 225    15075  14543  11567   2012   1993   1577       C  
ATOM   2289  N   LEU A 226      12.693  64.592 144.967  1.00105.36           N  
ANISOU 2289  N   LEU A 226    15012  13609  11409   2255   1988   1194       N  
ATOM   2290  CA  LEU A 226      13.641  65.561 144.389  1.00103.60           C  
ANISOU 2290  CA  LEU A 226    14900  13176  11286   2270   1963   1111       C  
ATOM   2291  C   LEU A 226      14.800  65.885 145.337  1.00102.46           C  
ANISOU 2291  C   LEU A 226    14836  12959  11132   2265   1948    994       C  
ATOM   2292  O   LEU A 226      15.970  65.907 144.924  1.00102.21           O  
ANISOU 2292  O   LEU A 226    14885  12777  11171   2188   1909    963       O  
ATOM   2293  CB  LEU A 226      12.935  66.860 143.984  1.00104.56           C  
ANISOU 2293  CB  LEU A 226    15033  13250  11443   2409   1986   1070       C  
ATOM   2294  CG  LEU A 226      12.119  66.845 142.690  1.00104.26           C  
ANISOU 2294  CG  LEU A 226    14950  13205  11456   2410   1989   1169       C  
ATOM   2295  CD1 LEU A 226      11.235  68.071 142.655  1.00105.43           C  
ANISOU 2295  CD1 LEU A 226    15093  13355  11609   2570   2017   1122       C  
ATOM   2296  CD2 LEU A 226      13.015  66.812 141.462  1.00102.92           C  
ANISOU 2296  CD2 LEU A 226    14849  12859  11395   2312   1947   1197       C  
ATOM   2297  N   GLN A 227      14.473  66.140 146.604  1.00102.07           N  
ANISOU 2297  N   GLN A 227    14764  13024  10993   2349   1977    927       N  
ATOM   2298  CA  GLN A 227      15.493  66.404 147.627  1.00101.59           C  
ANISOU 2298  CA  GLN A 227    14772  12918  10909   2350   1964    815       C  
ATOM   2299  C   GLN A 227      16.398  65.202 147.887  1.00 99.77           C  
ANISOU 2299  C   GLN A 227    14548  12698  10662   2206   1931    853       C  
ATOM   2300  O   GLN A 227      17.556  65.388 148.248  1.00 99.52           O  
ANISOU 2300  O   GLN A 227    14594  12564  10654   2171   1904    772       O  
ATOM   2301  CB  GLN A 227      14.860  66.897 148.934  1.00103.23           C  
ANISOU 2301  CB  GLN A 227    14942  13267  11013   2476   2003    737       C  
ATOM   2302  CG  GLN A 227      14.354  68.330 148.845  1.00104.58           C  
ANISOU 2302  CG  GLN A 227    15144  13378  11212   2633   2021    648       C  
ATOM   2303  CD  GLN A 227      13.516  68.746 150.042  1.00106.07           C  
ANISOU 2303  CD  GLN A 227    15275  13736  11289   2770   2063    581       C  
ATOM   2304  OE1 GLN A 227      13.599  68.149 151.116  1.00106.27           O  
ANISOU 2304  OE1 GLN A 227    15261  13898  11217   2749   2076    570       O  
ATOM   2305  NE2 GLN A 227      12.701  69.781 149.861  1.00107.36           N  
ANISOU 2305  NE2 GLN A 227    15430  13895  11463   2914   2082    535       N  
ATOM   2306  N   LYS A 228      15.882  63.984 147.700  1.00 98.13           N  
ANISOU 2306  N   LYS A 228    14260  12608  10417   2124   1929    975       N  
ATOM   2307  CA  LYS A 228      16.718  62.774 147.732  1.00 96.08           C  
ANISOU 2307  CA  LYS A 228    14009  12339  10158   1982   1887   1024       C  
ATOM   2308  C   LYS A 228      17.699  62.727 146.557  1.00 93.32           C  
ANISOU 2308  C   LYS A 228    13730  11806   9921   1896   1842   1030       C  
ATOM   2309  O   LYS A 228      18.871  62.364 146.747  1.00 92.19           O  
ANISOU 2309  O   LYS A 228    13643  11587   9797   1818   1804    992       O  
ATOM   2310  CB  LYS A 228      15.859  61.503 147.783  1.00 96.72           C  
ANISOU 2310  CB  LYS A 228    13988  12585  10175   1916   1889   1158       C  
ATOM   2311  CG  LYS A 228      15.281  61.219 149.163  1.00 98.22           C  
ANISOU 2311  CG  LYS A 228    14113  12966  10239   1956   1919   1156       C  
ATOM   2312  CD  LYS A 228      14.107  60.251 149.097  1.00 98.69           C  
ANISOU 2312  CD  LYS A 228    14059  13200  10236   1916   1931   1294       C  
ATOM   2313  CE  LYS A 228      13.446  60.081 150.456  1.00100.51           C  
ANISOU 2313  CE  LYS A 228    14216  13638  10334   1964   1967   1295       C  
ATOM   2314  NZ  LYS A 228      12.159  59.337 150.355  1.00101.28           N  
ANISOU 2314  NZ  LYS A 228    14195  13915  10369   1940   1986   1428       N  
ATOM   2315  N   GLU A 229      17.227  63.098 145.360  1.00 91.93           N  
ANISOU 2315  N   GLU A 229    13547  11568   9814   1912   1846   1076       N  
ATOM   2316  CA  GLU A 229      18.122  63.286 144.198  1.00 89.49           C  
ANISOU 2316  CA  GLU A 229    13305  11085   9611   1848   1808   1072       C  
ATOM   2317  C   GLU A 229      19.197  64.348 144.470  1.00 88.26           C  
ANISOU 2317  C   GLU A 229    13250  10785   9499   1880   1797    946       C  
ATOM   2318  O   GLU A 229      20.380  64.149 144.133  1.00 87.57           O  
ANISOU 2318  O   GLU A 229    13221  10587   9461   1794   1757    920       O  
ATOM   2319  CB  GLU A 229      17.341  63.643 142.921  1.00 89.08           C  
ANISOU 2319  CB  GLU A 229    13227  11000   9618   1875   1818   1140       C  
ATOM   2320  CG  GLU A 229      16.820  62.436 142.151  1.00 88.87           C  
ANISOU 2320  CG  GLU A 229    13128  11045   9591   1788   1802   1269       C  
ATOM   2321  CD  GLU A 229      17.933  61.611 141.503  1.00 88.68           C  
ANISOU 2321  CD  GLU A 229    13141  10932   9621   1658   1747   1289       C  
ATOM   2322  OE1 GLU A 229      18.906  62.181 140.962  1.00 89.16           O  
ANISOU 2322  OE1 GLU A 229    13275  10848   9750   1638   1726   1233       O  
ATOM   2323  OE2 GLU A 229      17.838  60.371 141.524  1.00 88.55           O  
ANISOU 2323  OE2 GLU A 229    13077  10990   9574   1575   1722   1363       O  
ATOM   2324  N   LEU A 230      18.783  65.456 145.087  1.00 87.82           N  
ANISOU 2324  N   LEU A 230    13213  10732   9422   2003   1828    865       N  
ATOM   2325  CA  LEU A 230      19.724  66.502 145.506  1.00 87.48           C  
ANISOU 2325  CA  LEU A 230    13265  10559   9412   2041   1815    739       C  
ATOM   2326  C   LEU A 230      20.736  65.999 146.544  1.00 86.60           C  
ANISOU 2326  C   LEU A 230    13184  10465   9255   1983   1795    677       C  
ATOM   2327  O   LEU A 230      21.926  66.286 146.435  1.00 85.62           O  
ANISOU 2327  O   LEU A 230    13136  10211   9182   1932   1762    614       O  
ATOM   2328  CB  LEU A 230      18.981  67.716 146.084  1.00 88.81           C  
ANISOU 2328  CB  LEU A 230    13442  10744   9557   2194   1849    660       C  
ATOM   2329  CG  LEU A 230      19.818  68.989 146.297  1.00 89.37           C  
ANISOU 2329  CG  LEU A 230    13618  10654   9682   2244   1829    533       C  
ATOM   2330  CD1 LEU A 230      20.272  69.626 144.978  1.00 88.89           C  
ANISOU 2330  CD1 LEU A 230    13620  10416   9738   2209   1799    551       C  
ATOM   2331  CD2 LEU A 230      19.031  69.997 147.124  1.00 90.91           C  
ANISOU 2331  CD2 LEU A 230    13811  10896   9831   2404   1859    447       C  
ATOM   2332  N   LYS A 231      20.258  65.250 147.537  1.00 86.61           N  
ANISOU 2332  N   LYS A 231    13121  10628   9157   1989   1815    699       N  
ATOM   2333  CA  LYS A 231      21.101  64.758 148.645  1.00 86.14           C  
ANISOU 2333  CA  LYS A 231    13082  10604   9040   1945   1798    644       C  
ATOM   2334  C   LYS A 231      22.238  63.865 148.173  1.00 84.75           C  
ANISOU 2334  C   LYS A 231    12937  10353   8908   1807   1748    675       C  
ATOM   2335  O   LYS A 231      23.362  64.023 148.644  1.00 84.38           O  
ANISOU 2335  O   LYS A 231    12954  10235   8871   1775   1722    592       O  
ATOM   2336  CB  LYS A 231      20.267  64.004 149.694  1.00 86.26           C  
ANISOU 2336  CB  LYS A 231    13013  10825   8938   1966   1826    687       C  
ATOM   2337  CG  LYS A 231      20.988  63.759 151.010  1.00 86.17           C  
ANISOU 2337  CG  LYS A 231    13021  10863   8853   1952   1817    614       C  
ATOM   2338  CD  LYS A 231      20.172  62.846 151.911  1.00 86.61           C  
ANISOU 2338  CD  LYS A 231    12985  11127   8793   1949   1839    684       C  
ATOM   2339  CE  LYS A 231      20.904  62.500 153.199  1.00 86.77           C  
ANISOU 2339  CE  LYS A 231    13023  11206   8738   1926   1826    624       C  
ATOM   2340  NZ  LYS A 231      20.394  61.234 153.803  1.00 86.87           N  
ANISOU 2340  NZ  LYS A 231    12953  11394   8658   1864   1825    728       N  
ATOM   2341  N   ILE A 232      21.951  62.946 147.247  1.00 84.10           N  
ANISOU 2341  N   ILE A 232    12809  10289   8853   1729   1732    788       N  
ATOM   2342  CA  ILE A 232      22.980  62.025 146.732  1.00 83.09           C  
ANISOU 2342  CA  ILE A 232    12705  10098   8766   1603   1680    818       C  
ATOM   2343  C   ILE A 232      23.998  62.794 145.883  1.00 82.15           C  
ANISOU 2343  C   ILE A 232    12666   9804   8743   1580   1655    758       C  
ATOM   2344  O   ILE A 232      25.221  62.661 146.084  1.00 81.50           O  
ANISOU 2344  O   ILE A 232    12636   9651   8678   1519   1620    700       O  
ATOM   2345  CB  ILE A 232      22.366  60.857 145.921  1.00 83.01           C  
ANISOU 2345  CB  ILE A 232    12626  10150   8761   1531   1663    951       C  
ATOM   2346  CG1 ILE A 232      21.437  60.008 146.801  1.00 84.19           C  
ANISOU 2346  CG1 ILE A 232    12696  10477   8813   1536   1680   1019       C  
ATOM   2347  CG2 ILE A 232      23.457  59.966 145.337  1.00 82.19           C  
ANISOU 2347  CG2 ILE A 232    12550   9973   8705   1413   1604    970       C  
ATOM   2348  CD1 ILE A 232      20.566  59.033 146.023  1.00 84.18           C  
ANISOU 2348  CD1 ILE A 232    12620  10546   8816   1482   1669   1152       C  
ATOM   2349  N   ALA A 233      23.478  63.609 144.957  1.00 81.98           N  
ANISOU 2349  N   ALA A 233    12649   9717   8780   1627   1673    775       N  
ATOM   2350  CA  ALA A 233      24.302  64.447 144.072  1.00 81.08           C  
ANISOU 2350  CA  ALA A 233    12606   9442   8758   1608   1652    732       C  
ATOM   2351  C   ALA A 233      25.432  65.172 144.808  1.00 80.80           C  
ANISOU 2351  C   ALA A 233    12652   9319   8730   1613   1636    609       C  
ATOM   2352  O   ALA A 233      26.577  65.165 144.353  1.00 79.72           O  
ANISOU 2352  O   ALA A 233    12562   9082   8644   1536   1600    582       O  
ATOM   2353  CB  ALA A 233      23.430  65.455 143.333  1.00 81.60           C  
ANISOU 2353  CB  ALA A 233    12670   9463   8868   1690   1679    751       C  
ATOM   2354  N   LYS A 234      25.103  65.783 145.947  1.00 81.49           N  
ANISOU 2354  N   LYS A 234    12750   9449   8763   1705   1663    535       N  
ATOM   2355  CA  LYS A 234      26.101  66.452 146.787  1.00 81.55           C  
ANISOU 2355  CA  LYS A 234    12831   9386   8768   1716   1647    412       C  
ATOM   2356  C   LYS A 234      27.161  65.479 147.302  1.00 79.86           C  
ANISOU 2356  C   LYS A 234    12623   9196   8522   1620   1614    398       C  
ATOM   2357  O   LYS A 234      28.356  65.789 147.249  1.00 79.84           O  
ANISOU 2357  O   LYS A 234    12683   9090   8560   1569   1582    332       O  
ATOM   2358  CB  LYS A 234      25.436  67.171 147.966  1.00 83.38           C  
ANISOU 2358  CB  LYS A 234    13061   9683   8934   1840   1682    336       C  
ATOM   2359  CG  LYS A 234      24.606  68.385 147.574  1.00 84.78           C  
ANISOU 2359  CG  LYS A 234    13254   9806   9149   1951   1705    316       C  
ATOM   2360  CD  LYS A 234      24.164  69.160 148.812  1.00 86.43           C  
ANISOU 2360  CD  LYS A 234    13475  10069   9296   2076   1730    214       C  
ATOM   2361  CE  LYS A 234      23.167  70.261 148.484  1.00 87.58           C  
ANISOU 2361  CE  LYS A 234    13624  10183   9469   2202   1752    198       C  
ATOM   2362  NZ  LYS A 234      22.494  70.788 149.706  1.00 88.66           N  
ANISOU 2362  NZ  LYS A 234    13745  10419   9524   2335   1782    113       N  
ATOM   2363  N   SER A 235      26.725  64.310 147.778  1.00 78.29           N  
ANISOU 2363  N   SER A 235    12358   9133   8253   1593   1618    462       N  
ATOM   2364  CA  SER A 235      27.644  63.268 148.266  1.00 76.54           C  
ANISOU 2364  CA  SER A 235    12138   8943   8000   1502   1581    460       C  
ATOM   2365  C   SER A 235      28.592  62.822 147.153  1.00 74.15           C  
ANISOU 2365  C   SER A 235    11857   8542   7772   1399   1536    488       C  
ATOM   2366  O   SER A 235      29.811  62.766 147.346  1.00 73.19           O  
ANISOU 2366  O   SER A 235    11783   8360   7666   1343   1502    426       O  
ATOM   2367  CB  SER A 235      26.878  62.043 148.789  1.00 76.46           C  
ANISOU 2367  CB  SER A 235    12050   9090   7910   1485   1588    547       C  
ATOM   2368  OG  SER A 235      25.844  62.416 149.672  1.00 77.22           O  
ANISOU 2368  OG  SER A 235    12108   9298   7931   1581   1634    538       O  
ATOM   2369  N   LEU A 236      28.018  62.527 145.990  1.00 72.42           N  
ANISOU 2369  N   LEU A 236    11602   8316   7597   1376   1537    580       N  
ATOM   2370  CA  LEU A 236      28.807  62.108 144.831  1.00 71.04           C  
ANISOU 2370  CA  LEU A 236    11439   8062   7490   1285   1497    611       C  
ATOM   2371  C   LEU A 236      29.736  63.217 144.325  1.00 70.57           C  
ANISOU 2371  C   LEU A 236    11450   7862   7500   1277   1486    536       C  
ATOM   2372  O   LEU A 236      30.845  62.927 143.870  1.00 70.15           O  
ANISOU 2372  O   LEU A 236    11420   7750   7482   1197   1447    517       O  
ATOM   2373  CB  LEU A 236      27.899  61.617 143.698  1.00 70.66           C  
ANISOU 2373  CB  LEU A 236    11334   8044   7470   1271   1502    723       C  
ATOM   2374  CG  LEU A 236      27.089  60.355 144.016  1.00 70.49           C  
ANISOU 2374  CG  LEU A 236    11240   8152   7388   1252   1499    812       C  
ATOM   2375  CD1 LEU A 236      26.027  60.154 142.945  1.00 70.51           C  
ANISOU 2375  CD1 LEU A 236    11188   8181   7418   1258   1512    913       C  
ATOM   2376  CD2 LEU A 236      27.984  59.130 144.159  1.00 69.62           C  
ANISOU 2376  CD2 LEU A 236    11129   8057   7266   1158   1443    821       C  
ATOM   2377  N   ALA A 237      29.289  64.472 144.417  1.00 70.30           N  
ANISOU 2377  N   ALA A 237    11447   7776   7486   1360   1517    494       N  
ATOM   2378  CA  ALA A 237      30.133  65.625 144.090  1.00 69.70           C  
ANISOU 2378  CA  ALA A 237    11445   7563   7474   1355   1504    420       C  
ATOM   2379  C   ALA A 237      31.307  65.739 145.059  1.00 69.20           C  
ANISOU 2379  C   ALA A 237    11432   7471   7388   1328   1479    317       C  
ATOM   2380  O   ALA A 237      32.462  65.858 144.631  1.00 68.61           O  
ANISOU 2380  O   ALA A 237    11395   7315   7356   1253   1445    284       O  
ATOM   2381  CB  ALA A 237      29.315  66.905 144.101  1.00 70.87           C  
ANISOU 2381  CB  ALA A 237    11618   7663   7644   1459   1536    395       C  
ATOM   2382  N   LEU A 238      31.010  65.676 146.360  1.00 69.16           N  
ANISOU 2382  N   LEU A 238    11423   7544   7310   1385   1497    268       N  
ATOM   2383  CA  LEU A 238      32.046  65.685 147.413  1.00 68.99           C  
ANISOU 2383  CA  LEU A 238    11443   7516   7254   1364   1475    171       C  
ATOM   2384  C   LEU A 238      33.150  64.659 147.158  1.00 68.03           C  
ANISOU 2384  C   LEU A 238    11314   7396   7136   1254   1431    186       C  
ATOM   2385  O   LEU A 238      34.330  64.947 147.362  1.00 68.02           O  
ANISOU 2385  O   LEU A 238    11361   7328   7152   1209   1401    110       O  
ATOM   2386  CB  LEU A 238      31.425  65.430 148.794  1.00 69.35           C  
ANISOU 2386  CB  LEU A 238    11461   7682   7203   1434   1501    144       C  
ATOM   2387  CG  LEU A 238      32.372  65.324 149.989  1.00 69.30           C  
ANISOU 2387  CG  LEU A 238    11488   7693   7147   1419   1481     50       C  
ATOM   2388  CD1 LEU A 238      33.187  66.600 150.124  1.00 69.81           C  
ANISOU 2388  CD1 LEU A 238    11634   7629   7258   1435   1467    -61       C  
ATOM   2389  CD2 LEU A 238      31.587  65.032 151.256  1.00 69.90           C  
ANISOU 2389  CD2 LEU A 238    11526   7908   7122   1490   1511     40       C  
ATOM   2390  N   ILE A 239      32.756  63.466 146.720  1.00 67.22           N  
ANISOU 2390  N   ILE A 239    11152   7371   7018   1212   1423    280       N  
ATOM   2391  CA  ILE A 239      33.718  62.436 146.324  1.00 66.41           C  
ANISOU 2391  CA  ILE A 239    11038   7268   6925   1113   1376    300       C  
ATOM   2392  C   ILE A 239      34.615  62.927 145.179  1.00 66.08           C  
ANISOU 2392  C   ILE A 239    11028   7114   6963   1054   1351    285       C  
ATOM   2393  O   ILE A 239      35.833  62.731 145.227  1.00 66.34           O  
ANISOU 2393  O   ILE A 239    11086   7114   7005    991   1314    234       O  
ATOM   2394  CB  ILE A 239      32.997  61.108 145.988  1.00 66.05           C  
ANISOU 2394  CB  ILE A 239    10924   7318   6854   1086   1367    408       C  
ATOM   2395  CG1 ILE A 239      32.457  60.486 147.288  1.00 66.58           C  
ANISOU 2395  CG1 ILE A 239    10962   7501   6832   1119   1378    416       C  
ATOM   2396  CG2 ILE A 239      33.922  60.122 145.279  1.00 65.28           C  
ANISOU 2396  CG2 ILE A 239    10816   7203   6783    991   1313    432       C  
ATOM   2397  CD1 ILE A 239      31.298  59.539 147.082  1.00 66.51           C  
ANISOU 2397  CD1 ILE A 239    10884   7592   6793   1120   1386    530       C  
ATOM   2398  N   LEU A 240      34.024  63.577 144.175  1.00 65.68           N  
ANISOU 2398  N   LEU A 240    10975   7012   6966   1075   1372    330       N  
ATOM   2399  CA  LEU A 240      34.798  64.155 143.064  1.00 65.10           C  
ANISOU 2399  CA  LEU A 240    10931   6838   6966   1019   1352    324       C  
ATOM   2400  C   LEU A 240      35.758  65.236 143.563  1.00 65.02           C  
ANISOU 2400  C   LEU A 240    10991   6737   6976   1016   1341    220       C  
ATOM   2401  O   LEU A 240      36.947  65.237 143.206  1.00 64.84           O  
ANISOU 2401  O   LEU A 240    10989   6667   6980    940   1307    186       O  
ATOM   2402  CB  LEU A 240      33.872  64.721 141.981  1.00 65.54           C  
ANISOU 2402  CB  LEU A 240    10972   6859   7072   1050   1377    396       C  
ATOM   2403  CG  LEU A 240      34.522  65.321 140.728  1.00 65.48           C  
ANISOU 2403  CG  LEU A 240    10985   6756   7136    992   1358    408       C  
ATOM   2404  CD1 LEU A 240      35.369  64.285 140.001  1.00 64.63           C  
ANISOU 2404  CD1 LEU A 240    10843   6677   7034    898   1320    436       C  
ATOM   2405  CD2 LEU A 240      33.460  65.906 139.798  1.00 65.83           C  
ANISOU 2405  CD2 LEU A 240    11015   6773   7222   1037   1386    482       C  
ATOM   2406  N   PHE A 241      35.238  66.143 144.390  1.00 65.16           N  
ANISOU 2406  N   PHE A 241    11043   6734   6979   1099   1369    167       N  
ATOM   2407  CA  PHE A 241      36.058  67.189 145.004  1.00 65.45           C  
ANISOU 2407  CA  PHE A 241    11152   6685   7031   1105   1355     61       C  
ATOM   2408  C   PHE A 241      37.235  66.584 145.765  1.00 64.91           C  
ANISOU 2408  C   PHE A 241    11093   6645   6925   1046   1323     -3       C  
ATOM   2409  O   PHE A 241      38.379  67.009 145.583  1.00 65.18           O  
ANISOU 2409  O   PHE A 241    11165   6606   6992    984   1292    -56       O  
ATOM   2410  CB  PHE A 241      35.225  68.067 145.942  1.00 66.55           C  
ANISOU 2410  CB  PHE A 241    11319   6820   7145   1217   1387      8       C  
ATOM   2411  CG  PHE A 241      36.023  69.136 146.636  1.00 67.63           C  
ANISOU 2411  CG  PHE A 241    11531   6866   7296   1228   1368   -106       C  
ATOM   2412  CD1 PHE A 241      36.413  70.279 145.954  1.00 68.35           C  
ANISOU 2412  CD1 PHE A 241    11680   6822   7466   1210   1350   -127       C  
ATOM   2413  CD2 PHE A 241      36.395  68.997 147.967  1.00 68.28           C  
ANISOU 2413  CD2 PHE A 241    11630   6998   7316   1252   1365   -191       C  
ATOM   2414  CE1 PHE A 241      37.154  71.269 146.588  1.00 69.16           C  
ANISOU 2414  CE1 PHE A 241    11856   6835   7587   1215   1326   -233       C  
ATOM   2415  CE2 PHE A 241      37.139  69.980 148.605  1.00 69.08           C  
ANISOU 2415  CE2 PHE A 241    11801   7014   7431   1261   1343   -302       C  
ATOM   2416  CZ  PHE A 241      37.520  71.117 147.915  1.00 69.39           C  
ANISOU 2416  CZ  PHE A 241    11900   6913   7552   1241   1323   -323       C  
ATOM   2417  N   LEU A 242      36.948  65.585 146.601  1.00 64.07           N  
ANISOU 2417  N   LEU A 242    10947   6648   6745   1062   1328      6       N  
ATOM   2418  CA  LEU A 242      37.989  64.896 147.373  1.00 63.13           C  
ANISOU 2418  CA  LEU A 242    10833   6567   6583   1012   1295    -48       C  
ATOM   2419  C   LEU A 242      38.996  64.185 146.471  1.00 61.59           C  
ANISOU 2419  C   LEU A 242    10621   6358   6421    912   1253    -22       C  
ATOM   2420  O   LEU A 242      40.201  64.248 146.724  1.00 61.51           O  
ANISOU 2420  O   LEU A 242    10638   6318   6413    859   1220    -91       O  
ATOM   2421  CB  LEU A 242      37.370  63.918 148.378  1.00 63.07           C  
ANISOU 2421  CB  LEU A 242    10784   6685   6492   1048   1306    -25       C  
ATOM   2422  CG  LEU A 242      36.659  64.591 149.563  1.00 63.98           C  
ANISOU 2422  CG  LEU A 242    10917   6835   6555   1145   1342    -80       C  
ATOM   2423  CD1 LEU A 242      35.697  63.624 150.239  1.00 63.96           C  
ANISOU 2423  CD1 LEU A 242    10856   6971   6475   1182   1362    -18       C  
ATOM   2424  CD2 LEU A 242      37.654  65.149 150.572  1.00 64.41           C  
ANISOU 2424  CD2 LEU A 242    11027   6856   6588   1145   1323   -199       C  
ATOM   2425  N   PHE A 243      38.509  63.534 145.415  1.00 60.24           N  
ANISOU 2425  N   PHE A 243    10403   6211   6274    888   1253     71       N  
ATOM   2426  CA  PHE A 243      39.381  62.889 144.427  1.00 58.97           C  
ANISOU 2426  CA  PHE A 243    10219   6040   6144    801   1214     96       C  
ATOM   2427  C   PHE A 243      40.320  63.905 143.789  1.00 58.64           C  
ANISOU 2427  C   PHE A 243    10218   5901   6161    754   1201     50       C  
ATOM   2428  O   PHE A 243      41.545  63.718 143.796  1.00 58.10           O  
ANISOU 2428  O   PHE A 243    10158   5823   6093    689   1164      0       O  
ATOM   2429  CB  PHE A 243      38.552  62.194 143.342  1.00 58.51           C  
ANISOU 2429  CB  PHE A 243    10106   6019   6106    794   1219    203       C  
ATOM   2430  CG  PHE A 243      39.376  61.425 142.350  1.00 57.94           C  
ANISOU 2430  CG  PHE A 243    10004   5953   6057    715   1176    226       C  
ATOM   2431  CD1 PHE A 243      39.714  60.100 142.589  1.00 57.52           C  
ANISOU 2431  CD1 PHE A 243     9918   5968   5967    684   1137    236       C  
ATOM   2432  CD2 PHE A 243      39.820  62.026 141.175  1.00 57.93           C  
ANISOU 2432  CD2 PHE A 243    10007   5890   6113    672   1171    237       C  
ATOM   2433  CE1 PHE A 243      40.479  59.389 141.676  1.00 56.95           C  
ANISOU 2433  CE1 PHE A 243     9817   5904   5915    621   1093    248       C  
ATOM   2434  CE2 PHE A 243      40.589  61.321 140.261  1.00 57.27           C  
ANISOU 2434  CE2 PHE A 243     9890   5826   6044    603   1132    252       C  
ATOM   2435  CZ  PHE A 243      40.919  60.004 140.511  1.00 56.68           C  
ANISOU 2435  CZ  PHE A 243     9782   5820   5933    582   1093    253       C  
ATOM   2436  N   ALA A 244      39.736  64.979 143.253  1.00 58.77           N  
ANISOU 2436  N   ALA A 244    10258   5847   6224    785   1228     70       N  
ATOM   2437  CA  ALA A 244      40.507  66.052 142.600  1.00 58.65           C  
ANISOU 2437  CA  ALA A 244    10284   5730   6268    739   1215     40       C  
ATOM   2438  C   ALA A 244      41.517  66.692 143.549  1.00 58.83           C  
ANISOU 2438  C   ALA A 244    10363   5707   6282    722   1195    -67       C  
ATOM   2439  O   ALA A 244      42.687  66.894 143.188  1.00 58.24           O  
ANISOU 2439  O   ALA A 244    10301   5595   6230    644   1163   -101       O  
ATOM   2440  CB  ALA A 244      39.571  67.113 142.041  1.00 59.02           C  
ANISOU 2440  CB  ALA A 244    10353   5706   6363    789   1245     80       C  
ATOM   2441  N   LEU A 245      41.058  66.983 144.766  1.00 59.33           N  
ANISOU 2441  N   LEU A 245    10455   5781   6306    797   1214   -121       N  
ATOM   2442  CA  LEU A 245      41.897  67.606 145.788  1.00 60.09           C  
ANISOU 2442  CA  LEU A 245    10605   5837   6387    794   1196   -230       C  
ATOM   2443  C   LEU A 245      43.038  66.679 146.213  1.00 59.46           C  
ANISOU 2443  C   LEU A 245    10506   5817   6267    728   1160   -270       C  
ATOM   2444  O   LEU A 245      44.174  67.134 146.375  1.00 59.83           O  
ANISOU 2444  O   LEU A 245    10587   5817   6328    673   1131   -339       O  
ATOM   2445  CB  LEU A 245      41.058  68.018 147.005  1.00 61.13           C  
ANISOU 2445  CB  LEU A 245    10763   5986   6476    897   1225   -278       C  
ATOM   2446  CG  LEU A 245      41.671  69.037 147.972  1.00 62.33           C  
ANISOU 2446  CG  LEU A 245    10984   6071   6626    916   1211   -395       C  
ATOM   2447  CD1 LEU A 245      41.738  70.422 147.338  1.00 63.17           C  
ANISOU 2447  CD1 LEU A 245    11148   6041   6811    912   1202   -410       C  
ATOM   2448  CD2 LEU A 245      40.869  69.082 149.264  1.00 63.04           C  
ANISOU 2448  CD2 LEU A 245    11079   6221   6650   1019   1238   -441       C  
ATOM   2449  N   SER A 246      42.735  65.390 146.378  1.00 58.58           N  
ANISOU 2449  N   SER A 246    10342   5807   6108    733   1160   -225       N  
ATOM   2450  CA  SER A 246      43.756  64.379 146.678  1.00 57.68           C  
ANISOU 2450  CA  SER A 246    10204   5752   5957    675   1120   -253       C  
ATOM   2451  C   SER A 246      44.763  64.206 145.537  1.00 56.78           C  
ANISOU 2451  C   SER A 246    10072   5615   5886    585   1086   -239       C  
ATOM   2452  O   SER A 246      45.972  64.115 145.783  1.00 56.48           O  
ANISOU 2452  O   SER A 246    10042   5578   5839    530   1051   -303       O  
ATOM   2453  CB  SER A 246      43.100  63.025 146.986  1.00 57.29           C  
ANISOU 2453  CB  SER A 246    10104   5807   5855    700   1120   -193       C  
ATOM   2454  OG  SER A 246      42.249  63.101 148.125  1.00 57.89           O  
ANISOU 2454  OG  SER A 246    10189   5926   5879    777   1149   -206       O  
ATOM   2455  N   TRP A 247      44.264  64.176 144.296  1.00 56.17           N  
ANISOU 2455  N   TRP A 247     9964   5524   5851    571   1097   -158       N  
ATOM   2456  CA  TRP A 247      45.104  63.835 143.125  1.00 55.12           C  
ANISOU 2456  CA  TRP A 247     9799   5395   5749    490   1067   -133       C  
ATOM   2457  C   TRP A 247      45.856  64.980 142.441  1.00 55.16           C  
ANISOU 2457  C   TRP A 247     9832   5317   5807    431   1060   -156       C  
ATOM   2458  O   TRP A 247      46.951  64.747 141.925  1.00 54.67           O  
ANISOU 2458  O   TRP A 247     9748   5271   5749    357   1027   -175       O  
ATOM   2459  CB  TRP A 247      44.290  63.052 142.086  1.00 54.47           C  
ANISOU 2459  CB  TRP A 247     9660   5355   5678    496   1074    -33       C  
ATOM   2460  CG  TRP A 247      44.211  61.600 142.417  1.00 53.89           C  
ANISOU 2460  CG  TRP A 247     9545   5372   5558    503   1049    -15       C  
ATOM   2461  CD1 TRP A 247      43.140  60.920 142.918  1.00 53.73           C  
ANISOU 2461  CD1 TRP A 247     9507   5402   5505    559   1065     31       C  
ATOM   2462  CD2 TRP A 247      45.270  60.655 142.300  1.00 53.30           C  
ANISOU 2462  CD2 TRP A 247     9441   5345   5463    450    999    -44       C  
ATOM   2463  NE1 TRP A 247      43.464  59.598 143.105  1.00 53.10           N  
ANISOU 2463  NE1 TRP A 247     9393   5391   5390    540   1024     38       N  
ATOM   2464  CE2 TRP A 247      44.770  59.410 142.735  1.00 52.97           C  
ANISOU 2464  CE2 TRP A 247     9370   5372   5381    478    982    -11       C  
ATOM   2465  CE3 TRP A 247      46.595  60.737 141.858  1.00 53.27           C  
ANISOU 2465  CE3 TRP A 247     9431   5337   5471    382    965    -95       C  
ATOM   2466  CZ2 TRP A 247      45.552  58.250 142.737  1.00 52.78           C  
ANISOU 2466  CZ2 TRP A 247     9317   5402   5333    445    927    -29       C  
ATOM   2467  CZ3 TRP A 247      47.369  59.594 141.863  1.00 52.98           C  
ANISOU 2467  CZ3 TRP A 247     9360   5365   5406    354    915   -117       C  
ATOM   2468  CH2 TRP A 247      46.847  58.361 142.297  1.00 52.72           C  
ANISOU 2468  CH2 TRP A 247     9303   5389   5337    388    895    -86       C  
ATOM   2469  N   LEU A 248      45.292  66.192 142.430  1.00 55.64           N  
ANISOU 2469  N   LEU A 248     9940   5293   5905    463   1086   -154       N  
ATOM   2470  CA  LEU A 248      45.905  67.323 141.688  1.00 55.97           C  
ANISOU 2470  CA  LEU A 248    10013   5247   6005    403   1076   -159       C  
ATOM   2471  C   LEU A 248      47.349  67.707 142.076  1.00 55.90           C  
ANISOU 2471  C   LEU A 248    10029   5216   5994    329   1039   -244       C  
ATOM   2472  O   LEU A 248      48.156  68.026 141.187  1.00 55.99           O  
ANISOU 2472  O   LEU A 248    10028   5208   6035    246   1018   -230       O  
ATOM   2473  CB  LEU A 248      45.000  68.565 141.714  1.00 56.94           C  
ANISOU 2473  CB  LEU A 248    10190   5273   6171    460   1103   -146       C  
ATOM   2474  CG  LEU A 248      43.826  68.530 140.722  1.00 56.95           C  
ANISOU 2474  CG  LEU A 248    10162   5274   6200    496   1132    -43       C  
ATOM   2475  CD1 LEU A 248      42.801  69.610 141.054  1.00 57.80           C  
ANISOU 2475  CD1 LEU A 248    10323   5301   6337    580   1159    -43       C  
ATOM   2476  CD2 LEU A 248      44.303  68.656 139.276  1.00 56.74           C  
ANISOU 2476  CD2 LEU A 248    10106   5234   6217    412   1117     19       C  
ATOM   2477  N   PRO A 249      47.682  67.686 143.384  1.00 55.98           N  
ANISOU 2477  N   PRO A 249    10071   5233   5964    357   1031   -330       N  
ATOM   2478  CA  PRO A 249      49.062  67.972 143.810  1.00 56.37           C  
ANISOU 2478  CA  PRO A 249    10140   5271   6006    287    994   -413       C  
ATOM   2479  C   PRO A 249      50.150  67.132 143.111  1.00 55.74           C  
ANISOU 2479  C   PRO A 249    10000   5265   5913    203    961   -406       C  
ATOM   2480  O   PRO A 249      51.101  67.700 142.551  1.00 55.74           O  
ANISOU 2480  O   PRO A 249    10001   5237   5940    119    938   -420       O  
ATOM   2481  CB  PRO A 249      49.021  67.681 145.314  1.00 56.52           C  
ANISOU 2481  CB  PRO A 249    10184   5321   5969    347    994   -491       C  
ATOM   2482  CG  PRO A 249      47.629  68.018 145.706  1.00 56.72           C  
ANISOU 2482  CG  PRO A 249    10234   5321   5995    445   1035   -465       C  
ATOM   2483  CD  PRO A 249      46.769  67.606 144.544  1.00 56.16           C  
ANISOU 2483  CD  PRO A 249    10118   5270   5950    454   1057   -356       C  
ATOM   2484  N   LEU A 250      49.988  65.807 143.126  1.00 55.07           N  
ANISOU 2484  N   LEU A 250     9862   5276   5786    225    956   -382       N  
ATOM   2485  CA  LEU A 250      50.948  64.891 142.486  1.00 54.53           C  
ANISOU 2485  CA  LEU A 250     9733   5287   5699    161    921   -380       C  
ATOM   2486  C   LEU A 250      51.089  65.142 140.973  1.00 54.45           C  
ANISOU 2486  C   LEU A 250     9685   5271   5731    101    921   -314       C  
ATOM   2487  O   LEU A 250      52.171  64.943 140.410  1.00 54.04           O  
ANISOU 2487  O   LEU A 250     9596   5263   5674     28    891   -332       O  
ATOM   2488  CB  LEU A 250      50.562  63.428 142.746  1.00 53.77           C  
ANISOU 2488  CB  LEU A 250     9592   5279   5556    206    912   -359       C  
ATOM   2489  CG  LEU A 250      51.593  62.346 142.394  1.00 53.22           C  
ANISOU 2489  CG  LEU A 250     9466   5295   5458    160    865   -380       C  
ATOM   2490  CD1 LEU A 250      52.798  62.390 143.321  1.00 53.47           C  
ANISOU 2490  CD1 LEU A 250     9514   5343   5457    129    833   -478       C  
ATOM   2491  CD2 LEU A 250      50.947  60.974 142.446  1.00 52.68           C  
ANISOU 2491  CD2 LEU A 250     9361   5294   5360    209    854   -337       C  
ATOM   2492  N   HIS A 251      50.000  65.573 140.330  1.00 54.55           N  
ANISOU 2492  N   HIS A 251     9706   5239   5781    133    954   -237       N  
ATOM   2493  CA  HIS A 251      50.043  66.014 138.931  1.00 54.64           C  
ANISOU 2493  CA  HIS A 251     9691   5234   5834     78    957   -170       C  
ATOM   2494  C   HIS A 251      50.806  67.330 138.790  1.00 55.48           C  
ANISOU 2494  C   HIS A 251     9839   5261   5978      8    947   -197       C  
ATOM   2495  O   HIS A 251      51.737  67.425 137.980  1.00 55.46           O  
ANISOU 2495  O   HIS A 251     9801   5289   5982    -77    924   -189       O  
ATOM   2496  CB  HIS A 251      48.636  66.145 138.340  1.00 54.46           C  
ANISOU 2496  CB  HIS A 251     9667   5183   5840    136    994    -81       C  
ATOM   2497  CG  HIS A 251      47.957  64.831 138.121  1.00 53.53           C  
ANISOU 2497  CG  HIS A 251     9496   5149   5692    182    998    -35       C  
ATOM   2498  ND1 HIS A 251      48.475  63.859 137.293  1.00 52.88           N  
ANISOU 2498  ND1 HIS A 251     9348   5151   5593    141    971    -16       N  
ATOM   2499  CD2 HIS A 251      46.803  64.329 138.618  1.00 53.16           C  
ANISOU 2499  CD2 HIS A 251     9452   5117   5630    263   1021     -6       C  
ATOM   2500  CE1 HIS A 251      47.670  62.812 137.295  1.00 52.28           C  
ANISOU 2500  CE1 HIS A 251     9240   5126   5496    195    974     22       C  
ATOM   2501  NE2 HIS A 251      46.646  63.072 138.087  1.00 52.42           N  
ANISOU 2501  NE2 HIS A 251     9297   5105   5513    264   1005     33       N  
ATOM   2502  N   ILE A 252      50.448  68.325 139.600  1.00 56.35           N  
ANISOU 2502  N   ILE A 252    10023   5275   6111     42    958   -231       N  
ATOM   2503  CA  ILE A 252      51.182  69.603 139.587  1.00 57.57           C  
ANISOU 2503  CA  ILE A 252    10227   5341   6305    -25    939   -263       C  
ATOM   2504  C   ILE A 252      52.693  69.346 139.743  1.00 58.05           C  
ANISOU 2504  C   ILE A 252    10260   5458   6336   -112    901   -327       C  
ATOM   2505  O   ILE A 252      53.510  69.921 139.003  1.00 58.19           O  
ANISOU 2505  O   ILE A 252    10267   5464   6378   -208    880   -312       O  
ATOM   2506  CB  ILE A 252      50.662  70.591 140.662  1.00 58.15           C  
ANISOU 2506  CB  ILE A 252    10387   5307   6398     36    949   -315       C  
ATOM   2507  CG1 ILE A 252      49.249  71.076 140.297  1.00 58.20           C  
ANISOU 2507  CG1 ILE A 252    10419   5250   6443    112    983   -246       C  
ATOM   2508  CG2 ILE A 252      51.593  71.798 140.807  1.00 59.00           C  
ANISOU 2508  CG2 ILE A 252    10549   5324   6542    -41    916   -364       C  
ATOM   2509  CD1 ILE A 252      48.471  71.645 141.467  1.00 58.89           C  
ANISOU 2509  CD1 ILE A 252    10573   5272   6530    209    999   -301       C  
ATOM   2510  N   LEU A 253      53.044  68.463 140.683  1.00 58.26           N  
ANISOU 2510  N   LEU A 253    10273   5553   6309    -81    890   -394       N  
ATOM   2511  CA  LEU A 253      54.433  68.021 140.864  1.00 58.69           C  
ANISOU 2511  CA  LEU A 253    10292   5680   6327   -151    852   -458       C  
ATOM   2512  C   LEU A 253      55.046  67.396 139.593  1.00 58.89           C  
ANISOU 2512  C   LEU A 253    10235   5797   6344   -218    837   -411       C  
ATOM   2513  O   LEU A 253      56.217  67.639 139.294  1.00 59.18           O  
ANISOU 2513  O   LEU A 253    10245   5863   6374   -306    809   -440       O  
ATOM   2514  CB  LEU A 253      54.552  67.045 142.041  1.00 58.29           C  
ANISOU 2514  CB  LEU A 253    10236   5691   6218    -93    843   -525       C  
ATOM   2515  CG  LEU A 253      54.436  67.645 143.450  1.00 58.86           C  
ANISOU 2515  CG  LEU A 253    10381   5700   6281    -48    846   -602       C  
ATOM   2516  CD1 LEU A 253      54.266  66.568 144.513  1.00 58.34           C  
ANISOU 2516  CD1 LEU A 253    10305   5706   6154     20    843   -644       C  
ATOM   2517  CD2 LEU A 253      55.648  68.500 143.785  1.00 59.70           C  
ANISOU 2517  CD2 LEU A 253    10517   5769   6397   -128    814   -676       C  
ATOM   2518  N   ASN A 254      54.266  66.597 138.860  1.00 58.85           N  
ANISOU 2518  N   ASN A 254    10185   5841   6335   -176    854   -341       N  
ATOM   2519  CA  ASN A 254      54.738  66.004 137.595  1.00 58.95           C  
ANISOU 2519  CA  ASN A 254    10117   5943   6338   -229    840   -297       C  
ATOM   2520  C   ASN A 254      54.917  67.039 136.495  1.00 59.72           C  
ANISOU 2520  C   ASN A 254    10210   6001   6478   -308    845   -237       C  
ATOM   2521  O   ASN A 254      55.858  66.945 135.700  1.00 59.17           O  
ANISOU 2521  O   ASN A 254    10082   6004   6394   -387    824   -232       O  
ATOM   2522  CB  ASN A 254      53.796  64.896 137.103  1.00 58.54           C  
ANISOU 2522  CB  ASN A 254    10022   5947   6272   -162    853   -239       C  
ATOM   2523  CG  ASN A 254      53.863  63.647 137.958  1.00 57.97           C  
ANISOU 2523  CG  ASN A 254     9933   5939   6151   -105    833   -290       C  
ATOM   2524  OD1 ASN A 254      54.649  63.563 138.901  1.00 57.99           O  
ANISOU 2524  OD1 ASN A 254     9952   5953   6126   -114    810   -370       O  
ATOM   2525  ND2 ASN A 254      53.032  62.667 137.627  1.00 57.48           N  
ANISOU 2525  ND2 ASN A 254     9840   5919   6080    -49    837   -241       N  
ATOM   2526  N   CYS A 255      54.007  68.011 136.448  1.00 61.25           N  
ANISOU 2526  N   CYS A 255    10464   6086   6722   -284    872   -189       N  
ATOM   2527  CA  CYS A 255      54.106  69.130 135.503  1.00 62.65           C  
ANISOU 2527  CA  CYS A 255    10652   6204   6947   -359    873   -127       C  
ATOM   2528  C   CYS A 255      55.316  70.011 135.800  1.00 64.03           C  
ANISOU 2528  C   CYS A 255    10852   6345   7130   -455    842   -179       C  
ATOM   2529  O   CYS A 255      56.117  70.288 134.894  1.00 64.04           O  
ANISOU 2529  O   CYS A 255    10808   6389   7132   -553    824   -147       O  
ATOM   2530  CB  CYS A 255      52.825  69.966 135.505  1.00 62.95           C  
ANISOU 2530  CB  CYS A 255    10755   6124   7038   -299    903    -72       C  
ATOM   2531  SG  CYS A 255      51.391  69.091 134.842  1.00 62.50           S  
ANISOU 2531  SG  CYS A 255    10658   6109   6977   -208    939     12       S  
ATOM   2532  N   ILE A 256      55.464  70.432 137.059  1.00 65.62           N  
ANISOU 2532  N   ILE A 256    11120   6478   7334   -429    833   -258       N  
ATOM   2533  CA  ILE A 256      56.606  71.292 137.416  1.00 67.75           C  
ANISOU 2533  CA  ILE A 256    11418   6709   7613   -522    799   -313       C  
ATOM   2534  C   ILE A 256      57.963  70.588 137.269  1.00 67.90           C  
ANISOU 2534  C   ILE A 256    11361   6858   7579   -596    770   -358       C  
ATOM   2535  O   ILE A 256      58.931  71.238 136.903  1.00 69.10           O  
ANISOU 2535  O   ILE A 256    11501   7013   7739   -703    744   -359       O  
ATOM   2536  CB  ILE A 256      56.472  71.996 138.802  1.00 68.89           C  
ANISOU 2536  CB  ILE A 256    11656   6745   7773   -478    792   -394       C  
ATOM   2537  CG1 ILE A 256      56.556  71.001 139.962  1.00 68.46           C  
ANISOU 2537  CG1 ILE A 256    11594   6757   7661   -405    794   -478       C  
ATOM   2538  CG2 ILE A 256      55.203  72.855 138.847  1.00 69.52           C  
ANISOU 2538  CG2 ILE A 256    11809   6694   7909   -410    816   -351       C  
ATOM   2539  CD1 ILE A 256      56.101  71.571 141.292  1.00 69.12           C  
ANISOU 2539  CD1 ILE A 256    11762   6746   7752   -334    798   -548       C  
ATOM   2540  N   THR A 257      58.035  69.279 137.511  1.00 67.46           N  
ANISOU 2540  N   THR A 257    11252   6910   7470   -541    771   -391       N  
ATOM   2541  CA  THR A 257      59.273  68.518 137.245  1.00 67.62           C  
ANISOU 2541  CA  THR A 257    11190   7063   7436   -600    741   -432       C  
ATOM   2542  C   THR A 257      59.588  68.425 135.745  1.00 67.70           C  
ANISOU 2542  C   THR A 257    11121   7155   7444   -671    739   -358       C  
ATOM   2543  O   THR A 257      60.752  68.561 135.348  1.00 68.08           O  
ANISOU 2543  O   THR A 257    11118   7278   7470   -764    713   -376       O  
ATOM   2544  CB  THR A 257      59.239  67.092 137.840  1.00 66.80           C  
ANISOU 2544  CB  THR A 257    11051   7049   7278   -518    734   -484       C  
ATOM   2545  OG1 THR A 257      58.033  66.435 137.450  1.00 66.23           O  
ANISOU 2545  OG1 THR A 257    10970   6979   7213   -436    761   -422       O  
ATOM   2546  CG2 THR A 257      59.328  67.135 139.362  1.00 67.10           C  
ANISOU 2546  CG2 THR A 257    11151   7040   7302   -472    726   -571       C  
ATOM   2547  N   LEU A 258      58.555  68.197 134.927  1.00 67.38           N  
ANISOU 2547  N   LEU A 258    11067   7109   7423   -626    767   -275       N  
ATOM   2548  CA  LEU A 258      58.703  68.170 133.464  1.00 67.07           C  
ANISOU 2548  CA  LEU A 258    10955   7144   7382   -686    769   -196       C  
ATOM   2549  C   LEU A 258      59.130  69.525 132.921  1.00 68.38           C  
ANISOU 2549  C   LEU A 258    11143   7250   7587   -796    762   -148       C  
ATOM   2550  O   LEU A 258      60.167  69.626 132.266  1.00 68.66           O  
ANISOU 2550  O   LEU A 258    11115   7376   7597   -894    741   -143       O  
ATOM   2551  CB  LEU A 258      57.396  67.754 132.774  1.00 65.85           C  
ANISOU 2551  CB  LEU A 258    10792   6980   7245   -612    800   -116       C  
ATOM   2552  CG  LEU A 258      57.372  67.771 131.236  1.00 65.12           C  
ANISOU 2552  CG  LEU A 258    10630   6958   7153   -665    806    -27       C  
ATOM   2553  CD1 LEU A 258      58.456  66.880 130.655  1.00 64.74           C  
ANISOU 2553  CD1 LEU A 258    10480   7075   7043   -707    779    -62       C  
ATOM   2554  CD2 LEU A 258      56.009  67.365 130.712  1.00 64.18           C  
ANISOU 2554  CD2 LEU A 258    10511   6819   7052   -583    836     44       C  
ATOM   2555  N   PHE A 259      58.328  70.555 133.193  1.00 69.71           N  
ANISOU 2555  N   PHE A 259    11400   7271   7816   -780    777   -112       N  
ATOM   2556  CA  PHE A 259      58.565  71.886 132.618  1.00 71.75           C  
ANISOU 2556  CA  PHE A 259    11688   7449   8122   -880    766    -51       C  
ATOM   2557  C   PHE A 259      59.759  72.598 133.256  1.00 74.63           C  
ANISOU 2557  C   PHE A 259    12079   7789   8487   -974    729   -115       C  
ATOM   2558  O   PHE A 259      60.532  73.254 132.554  1.00 75.06           O  
ANISOU 2558  O   PHE A 259    12105   7864   8547  -1094    707    -74       O  
ATOM   2559  CB  PHE A 259      57.311  72.763 132.714  1.00 71.32           C  
ANISOU 2559  CB  PHE A 259    11725   7237   8136   -824    786      3       C  
ATOM   2560  CG  PHE A 259      56.104  72.184 132.024  1.00 70.19           C  
ANISOU 2560  CG  PHE A 259    11557   7115   7997   -741    821     75       C  
ATOM   2561  CD1 PHE A 259      56.172  71.761 130.699  1.00 69.88           C  
ANISOU 2561  CD1 PHE A 259    11433   7181   7937   -782    827    151       C  
ATOM   2562  CD2 PHE A 259      54.888  72.073 132.693  1.00 69.87           C  
ANISOU 2562  CD2 PHE A 259    11574   6995   7977   -622    848     68       C  
ATOM   2563  CE1 PHE A 259      55.060  71.226 130.062  1.00 69.18           C  
ANISOU 2563  CE1 PHE A 259    11321   7112   7852   -707    857    216       C  
ATOM   2564  CE2 PHE A 259      53.772  71.541 132.059  1.00 69.27           C  
ANISOU 2564  CE2 PHE A 259    11473   6942   7905   -549    879    136       C  
ATOM   2565  CZ  PHE A 259      53.859  71.117 130.742  1.00 68.91           C  
ANISOU 2565  CZ  PHE A 259    11345   6994   7841   -592    883    210       C  
ATOM   2566  N   CYS A 260      59.898  72.463 134.577  1.00 77.85           N  
ANISOU 2566  N   CYS A 260    12537   8157   8886   -922    721   -214       N  
ATOM   2567  CA  CYS A 260      61.021  73.032 135.329  1.00 80.91           C  
ANISOU 2567  CA  CYS A 260    12949   8524   9268  -1000    684   -289       C  
ATOM   2568  C   CYS A 260      61.848  71.934 136.035  1.00 81.62           C  
ANISOU 2568  C   CYS A 260    12985   8738   9288   -976    671   -387       C  
ATOM   2569  O   CYS A 260      61.660  71.681 137.228  1.00 81.36           O  
ANISOU 2569  O   CYS A 260    13001   8666   9245   -901    671   -466       O  
ATOM   2570  CB  CYS A 260      60.501  74.064 136.337  1.00 82.55           C  
ANISOU 2570  CB  CYS A 260    13276   8557   9531   -965    678   -324       C  
ATOM   2571  SG  CYS A 260      61.816  74.981 137.159  1.00 86.15           S  
ANISOU 2571  SG  CYS A 260    13773   8963   9993  -1073    626   -406       S  
ATOM   2572  N   PRO A 261      62.764  71.265 135.297  1.00 83.05           N  
ANISOU 2572  N   PRO A 261    13063   9074   9417  -1036    658   -384       N  
ATOM   2573  CA  PRO A 261      63.687  70.322 135.957  1.00 83.58           C  
ANISOU 2573  CA  PRO A 261    13079   9255   9420  -1022    637   -482       C  
ATOM   2574  C   PRO A 261      64.709  71.011 136.880  1.00 85.59           C  
ANISOU 2574  C   PRO A 261    13370   9476   9673  -1094    603   -561       C  
ATOM   2575  O   PRO A 261      65.251  70.369 137.787  1.00 85.64           O  
ANISOU 2575  O   PRO A 261    13367   9535   9636  -1058    586   -653       O  
ATOM   2576  CB  PRO A 261      64.385  69.629 134.782  1.00 82.99           C  
ANISOU 2576  CB  PRO A 261    12886   9350   9297  -1075    629   -451       C  
ATOM   2577  CG  PRO A 261      64.314  70.614 133.668  1.00 83.48           C  
ANISOU 2577  CG  PRO A 261    12940   9381   9395  -1171    635   -350       C  
ATOM   2578  CD  PRO A 261      63.022  71.360 133.846  1.00 83.31           C  
ANISOU 2578  CD  PRO A 261    13020   9190   9445  -1118    660   -295       C  
ATOM   2579  N   SER A 262      64.961  72.299 136.640  1.00 87.95           N  
ANISOU 2579  N   SER A 262    13711   9686  10019  -1194    588   -523       N  
ATOM   2580  CA  SER A 262      65.818  73.122 137.499  1.00 89.61           C  
ANISOU 2580  CA  SER A 262    13968   9838  10239  -1267    552   -591       C  
ATOM   2581  C   SER A 262      65.212  73.401 138.889  1.00 89.90           C  
ANISOU 2581  C   SER A 262    14112   9742  10302  -1177    554   -664       C  
ATOM   2582  O   SER A 262      65.954  73.557 139.862  1.00 90.60           O  
ANISOU 2582  O   SER A 262    14224   9827  10373  -1198    526   -754       O  
ATOM   2583  CB  SER A 262      66.134  74.447 136.791  1.00 90.97           C  
ANISOU 2583  CB  SER A 262    14163   9937  10463  -1401    531   -517       C  
ATOM   2584  OG  SER A 262      67.138  75.173 137.474  1.00 92.83           O  
ANISOU 2584  OG  SER A 262    14427  10140  10702  -1492    489   -579       O  
ATOM   2585  N   CYS A 263      63.881  73.472 138.971  1.00 89.61           N  
ANISOU 2585  N   CYS A 263    14135   9608  10303  -1076    587   -627       N  
ATOM   2586  CA  CYS A 263      63.166  73.748 140.229  1.00 90.07           C  
ANISOU 2586  CA  CYS A 263    14290   9550  10382   -980    593   -691       C  
ATOM   2587  C   CYS A 263      63.400  72.684 141.308  1.00 90.67           C  
ANISOU 2587  C   CYS A 263    14348   9707  10395   -900    594   -787       C  
ATOM   2588  O   CYS A 263      63.323  71.486 141.029  1.00 89.73           O  
ANISOU 2588  O   CYS A 263    14160   9704  10230   -851    609   -778       O  
ATOM   2589  CB  CYS A 263      61.653  73.853 139.983  1.00 88.97           C  
ANISOU 2589  CB  CYS A 263    14197   9322  10282   -880    633   -625       C  
ATOM   2590  SG  CYS A 263      61.108  75.300 139.042  1.00 89.73           S  
ANISOU 2590  SG  CYS A 263    14351   9273  10466   -944    628   -523       S  
ATOM   2591  N   HIS A 264      63.681  73.144 142.530  1.00 92.70           N  
ANISOU 2591  N   HIS A 264    14671   9899  10652   -888    573   -877       N  
ATOM   2592  CA  HIS A 264      63.743  72.289 143.715  1.00 92.87           C  
ANISOU 2592  CA  HIS A 264    14693   9973  10618   -802    574   -966       C  
ATOM   2593  C   HIS A 264      62.361  72.259 144.367  1.00 92.00           C  
ANISOU 2593  C   HIS A 264    14651   9781  10523   -673    608   -965       C  
ATOM   2594  O   HIS A 264      61.685  73.291 144.446  1.00 91.42           O  
ANISOU 2594  O   HIS A 264    14654   9576  10505   -659    615   -947       O  
ATOM   2595  CB  HIS A 264      64.770  72.826 144.721  1.00 94.86           C  
ANISOU 2595  CB  HIS A 264    14979  10206  10857   -857    533  -1067       C  
ATOM   2596  CG  HIS A 264      66.164  72.931 144.180  1.00 96.86           C  
ANISOU 2596  CG  HIS A 264    15165  10544  11092   -989    497  -1074       C  
ATOM   2597  ND1 HIS A 264      66.970  71.831 143.977  1.00 97.16           N  
ANISOU 2597  ND1 HIS A 264    15108  10742  11066  -1001    488  -1096       N  
ATOM   2598  CD2 HIS A 264      66.901  74.009 143.816  1.00 98.44           C  
ANISOU 2598  CD2 HIS A 264    15379  10695  11328  -1115    465  -1063       C  
ATOM   2599  CE1 HIS A 264      68.140  72.225 143.503  1.00 97.84           C  
ANISOU 2599  CE1 HIS A 264    15145  10882  11144  -1126    456  -1099       C  
ATOM   2600  NE2 HIS A 264      68.124  73.542 143.396  1.00 98.67           N  
ANISOU 2600  NE2 HIS A 264    15315  10865  11310  -1202    441  -1075       N  
ATOM   2601  N   LYS A 265      61.945  71.075 144.821  1.00 91.61           N  
ANISOU 2601  N   LYS A 265    14571   9811  10423   -579    627   -982       N  
ATOM   2602  CA  LYS A 265      60.679  70.903 145.541  1.00 91.18           C  
ANISOU 2602  CA  LYS A 265    14569   9706  10369   -455    660   -983       C  
ATOM   2603  C   LYS A 265      60.875  70.035 146.784  1.00 89.46           C  
ANISOU 2603  C   LYS A 265    14347   9556  10085   -389    653  -1065       C  
ATOM   2604  O   LYS A 265      61.209  68.859 146.648  1.00 88.10           O  
ANISOU 2604  O   LYS A 265    14108   9498   9866   -379    647  -1062       O  
ATOM   2605  CB  LYS A 265      59.619  70.294 144.620  1.00 91.26           C  
ANISOU 2605  CB  LYS A 265    14543   9740  10390   -402    698   -884       C  
ATOM   2606  CG  LYS A 265      58.912  71.337 143.763  1.00 92.49           C  
ANISOU 2606  CG  LYS A 265    14737   9789  10616   -421    715   -807       C  
ATOM   2607  CD  LYS A 265      57.830  72.076 144.547  1.00 92.52           C  
ANISOU 2607  CD  LYS A 265    14828   9676  10649   -333    735   -825       C  
ATOM   2608  CE  LYS A 265      57.655  73.519 144.101  1.00 93.16           C  
ANISOU 2608  CE  LYS A 265    14973   9618  10803   -379    725   -796       C  
ATOM   2609  NZ  LYS A 265      56.424  74.108 144.701  1.00 93.51           N  
ANISOU 2609  NZ  LYS A 265    15092   9560  10875   -272    748   -804       N  
ATOM   2610  N   PRO A 266      60.672  70.612 147.994  1.00 88.91           N  
ANISOU 2610  N   PRO A 266    14350   9419  10012   -343    650  -1139       N  
ATOM   2611  CA  PRO A 266      60.860  69.890 149.263  1.00 87.76           C  
ANISOU 2611  CA  PRO A 266    14207   9337   9801   -283    642  -1218       C  
ATOM   2612  C   PRO A 266      60.204  68.510 149.335  1.00 85.12           C  
ANISOU 2612  C   PRO A 266    13826   9096   9420   -200    663  -1179       C  
ATOM   2613  O   PRO A 266      59.117  68.304 148.785  1.00 83.87           O  
ANISOU 2613  O   PRO A 266    13663   8921   9282   -149    698  -1101       O  
ATOM   2614  CB  PRO A 266      60.219  70.826 150.291  1.00 88.82           C  
ANISOU 2614  CB  PRO A 266    14430   9368   9949   -222    652  -1273       C  
ATOM   2615  CG  PRO A 266      60.441  72.182 149.734  1.00 89.96           C  
ANISOU 2615  CG  PRO A 266    14620   9396  10163   -296    636  -1264       C  
ATOM   2616  CD  PRO A 266      60.361  72.037 148.238  1.00 89.74           C  
ANISOU 2616  CD  PRO A 266    14541   9384  10173   -352    647  -1159       C  
ATOM   2617  N   SER A 267      60.878  67.591 150.022  1.00 83.39           N  
ANISOU 2617  N   SER A 267    13573   8970   9139   -191    638  -1232       N  
ATOM   2618  CA  SER A 267      60.446  66.199 150.103  1.00 81.55           C  
ANISOU 2618  CA  SER A 267    13294   8829   8862   -126    644  -1198       C  
ATOM   2619  C   SER A 267      59.107  66.023 150.824  1.00 80.99           C  
ANISOU 2619  C   SER A 267    13262   8734   8775    -21    680  -1176       C  
ATOM   2620  O   SER A 267      58.331  65.153 150.454  1.00 80.29           O  
ANISOU 2620  O   SER A 267    13141   8686   8678     26    697  -1106       O  
ATOM   2621  CB  SER A 267      61.514  65.337 150.786  1.00 80.89           C  
ANISOU 2621  CB  SER A 267    13175   8841   8716   -139    601  -1267       C  
ATOM   2622  OG  SER A 267      62.773  65.470 150.155  1.00 80.76           O  
ANISOU 2622  OG  SER A 267    13115   8862   8706   -233    568  -1292       O  
ATOM   2623  N   ILE A 268      58.829  66.851 151.838  1.00 81.57           N  
ANISOU 2623  N   ILE A 268    13401   8747   8845     14    690  -1235       N  
ATOM   2624  CA  ILE A 268      57.570  66.745 152.593  1.00 81.57           C  
ANISOU 2624  CA  ILE A 268    13433   8737   8822    117    726  -1221       C  
ATOM   2625  C   ILE A 268      56.363  66.982 151.680  1.00 80.92           C  
ANISOU 2625  C   ILE A 268    13351   8605   8787    150    767  -1127       C  
ATOM   2626  O   ILE A 268      55.365  66.255 151.765  1.00 80.31           O  
ANISOU 2626  O   ILE A 268    13256   8570   8688    219    793  -1070       O  
ATOM   2627  CB  ILE A 268      57.546  67.686 153.836  1.00 83.09           C  
ANISOU 2627  CB  ILE A 268    13695   8877   8998    152    726  -1314       C  
ATOM   2628  CG1 ILE A 268      56.431  67.299 154.825  1.00 83.58           C  
ANISOU 2628  CG1 ILE A 268    13772   8975   9009    261    757  -1312       C  
ATOM   2629  CG2 ILE A 268      57.422  69.152 153.441  1.00 83.87           C  
ANISOU 2629  CG2 ILE A 268    13850   8849   9166    125    732  -1328       C  
ATOM   2630  CD1 ILE A 268      56.695  66.026 155.606  1.00 83.24           C  
ANISOU 2630  CD1 ILE A 268    13690   9046   8888    285    740  -1323       C  
ATOM   2631  N   LEU A 269      56.479  67.961 150.783  1.00 80.94           N  
ANISOU 2631  N   LEU A 269    13372   8524   8856     96    769  -1105       N  
ATOM   2632  CA  LEU A 269      55.418  68.267 149.820  1.00 80.78           C  
ANISOU 2632  CA  LEU A 269    13353   8453   8886    120    804  -1014       C  
ATOM   2633  C   LEU A 269      55.212  67.107 148.842  1.00 79.90           C  
ANISOU 2633  C   LEU A 269    13169   8420   8769    112    810   -926       C  
ATOM   2634  O   LEU A 269      54.073  66.799 148.480  1.00 79.48           O  
ANISOU 2634  O   LEU A 269    13105   8370   8724    169    842   -853       O  
ATOM   2635  CB  LEU A 269      55.707  69.573 149.062  1.00 81.84           C  
ANISOU 2635  CB  LEU A 269    13523   8479   9092     53    797  -1007       C  
ATOM   2636  CG  LEU A 269      55.571  70.894 149.844  1.00 82.91           C  
ANISOU 2636  CG  LEU A 269    13743   8504   9254     76    792  -1078       C  
ATOM   2637  CD1 LEU A 269      56.028  72.083 149.008  1.00 83.55           C  
ANISOU 2637  CD1 LEU A 269    13857   8479   9409     -9    771  -1064       C  
ATOM   2638  CD2 LEU A 269      54.148  71.106 150.340  1.00 83.04           C  
ANISOU 2638  CD2 LEU A 269    13795   8488   9267    193    832  -1065       C  
ATOM   2639  N   THR A 270      56.307  66.460 148.431  1.00 79.79           N  
ANISOU 2639  N   THR A 270    13102   8473   8738     43    775   -937       N  
ATOM   2640  CA  THR A 270      56.239  65.238 147.616  1.00 78.68           C  
ANISOU 2640  CA  THR A 270    12892   8417   8584     41    769   -872       C  
ATOM   2641  C   THR A 270      55.567  64.095 148.381  1.00 78.98           C  
ANISOU 2641  C   THR A 270    12917   8521   8569    121    773   -861       C  
ATOM   2642  O   THR A 270      54.724  63.390 147.827  1.00 78.60           O  
ANISOU 2642  O   THR A 270    12838   8501   8525    157    789   -783       O  
ATOM   2643  CB  THR A 270      57.645  64.777 147.165  1.00 77.68           C  
ANISOU 2643  CB  THR A 270    12712   8359   8442    -39    724   -905       C  
ATOM   2644  OG1 THR A 270      58.269  65.817 146.401  1.00 77.42           O  
ANISOU 2644  OG1 THR A 270    12684   8276   8454   -124    719   -905       O  
ATOM   2645  CG2 THR A 270      57.572  63.501 146.323  1.00 76.68           C  
ANISOU 2645  CG2 THR A 270    12515   8319   8301    -33    712   -848       C  
ATOM   2646  N   TYR A 271      55.946  63.930 149.649  1.00 80.41           N  
ANISOU 2646  N   TYR A 271    13121   8728   8701    145    757   -935       N  
ATOM   2647  CA  TYR A 271      55.456  62.835 150.489  1.00 80.99           C  
ANISOU 2647  CA  TYR A 271    13183   8871   8718    211    753   -926       C  
ATOM   2648  C   TYR A 271      53.974  62.982 150.866  1.00 79.45           C  
ANISOU 2648  C   TYR A 271    13014   8654   8520    292    800   -876       C  
ATOM   2649  O   TYR A 271      53.230  62.002 150.781  1.00 78.64           O  
ANISOU 2649  O   TYR A 271    12880   8603   8396    332    805   -810       O  
ATOM   2650  CB  TYR A 271      56.335  62.651 151.744  1.00 83.87           C  
ANISOU 2650  CB  TYR A 271    13562   9275   9026    209    720  -1019       C  
ATOM   2651  CG  TYR A 271      57.495  61.680 151.567  1.00 86.69           C  
ANISOU 2651  CG  TYR A 271    13871   9709   9358    164    667  -1045       C  
ATOM   2652  CD1 TYR A 271      57.268  60.308 151.524  1.00 88.77           C  
ANISOU 2652  CD1 TYR A 271    14094  10044   9590    195    644  -1000       C  
ATOM   2653  CD2 TYR A 271      58.817  62.127 151.460  1.00 88.94           C  
ANISOU 2653  CD2 TYR A 271    14149   9995   9648     93    635  -1115       C  
ATOM   2654  CE1 TYR A 271      58.315  59.405 151.376  1.00 91.11           C  
ANISOU 2654  CE1 TYR A 271    14347  10408   9863    164    589  -1028       C  
ATOM   2655  CE2 TYR A 271      59.874  61.234 151.305  1.00 90.90           C  
ANISOU 2655  CE2 TYR A 271    14347  10321   9868     60    586  -1143       C  
ATOM   2656  CZ  TYR A 271      59.619  59.871 151.251  1.00 93.44           C  
ANISOU 2656  CZ  TYR A 271    14631  10710  10161     99    562  -1102       C  
ATOM   2657  OH  TYR A 271      60.654  58.956 151.126  1.00100.76           O  
ANISOU 2657  OH  TYR A 271    15510  11712  11060     77    506  -1135       O  
ATOM   2658  N   ILE A 272      53.544  64.183 151.268  1.00 78.96           N  
ANISOU 2658  N   ILE A 272    13005   8517   8477    318    830   -908       N  
ATOM   2659  CA  ILE A 272      52.110  64.406 151.579  1.00 78.26           C  
ANISOU 2659  CA  ILE A 272    12937   8413   8384    401    876   -864       C  
ATOM   2660  C   ILE A 272      51.204  64.246 150.349  1.00 76.43           C  
ANISOU 2660  C   ILE A 272    12676   8165   8198    408    903   -759       C  
ATOM   2661  O   ILE A 272      50.075  63.751 150.462  1.00 75.54           O  
ANISOU 2661  O   ILE A 272    12547   8087   8066    469    930   -698       O  
ATOM   2662  CB  ILE A 272      51.821  65.767 152.280  1.00 79.46           C  
ANISOU 2662  CB  ILE A 272    13156   8486   8549    439    898   -930       C  
ATOM   2663  CG1 ILE A 272      52.075  66.960 151.347  1.00 80.26           C  
ANISOU 2663  CG1 ILE A 272    13287   8480   8728    389    899   -929       C  
ATOM   2664  CG2 ILE A 272      52.597  65.877 153.594  1.00 80.04           C  
ANISOU 2664  CG2 ILE A 272    13258   8584   8569    443    874  -1035       C  
ATOM   2665  CD1 ILE A 272      52.000  68.308 152.036  1.00 81.93           C  
ANISOU 2665  CD1 ILE A 272    13571   8601   8957    418    904  -1007       C  
ATOM   2666  N   ALA A 273      51.706  64.663 149.187  1.00 75.38           N  
ANISOU 2666  N   ALA A 273    12532   7987   8121    342    893   -737       N  
ATOM   2667  CA  ALA A 273      51.019  64.442 147.910  1.00 73.99           C  
ANISOU 2667  CA  ALA A 273    12321   7804   7986    337    912   -639       C  
ATOM   2668  C   ALA A 273      50.798  62.954 147.655  1.00 72.29           C  
ANISOU 2668  C   ALA A 273    12046   7680   7738    347    897   -582       C  
ATOM   2669  O   ALA A 273      49.702  62.546 147.275  1.00 72.63           O  
ANISOU 2669  O   ALA A 273    12069   7739   7787    390    921   -504       O  
ATOM   2670  CB  ALA A 273      51.802  65.062 146.758  1.00 73.84           C  
ANISOU 2670  CB  ALA A 273    12294   7739   8022    254    897   -631       C  
ATOM   2671  N   ILE A 274      51.840  62.156 147.884  1.00 70.74           N  
ANISOU 2671  N   ILE A 274    11824   7542   7509    309    852   -624       N  
ATOM   2672  CA  ILE A 274      51.772  60.700 147.711  1.00 68.96           C  
ANISOU 2672  CA  ILE A 274    11549   7398   7255    318    823   -581       C  
ATOM   2673  C   ILE A 274      50.892  60.040 148.780  1.00 67.66           C  
ANISOU 2673  C   ILE A 274    11392   7276   7039    386    833   -561       C  
ATOM   2674  O   ILE A 274      50.133  59.115 148.468  1.00 66.76           O  
ANISOU 2674  O   ILE A 274    11245   7201   6917    410    831   -486       O  
ATOM   2675  CB  ILE A 274      53.191  60.082 147.662  1.00 69.00           C  
ANISOU 2675  CB  ILE A 274    11525   7452   7240    262    767   -638       C  
ATOM   2676  CG1 ILE A 274      53.886  60.526 146.364  1.00 69.17           C  
ANISOU 2676  CG1 ILE A 274    11518   7454   7306    194    759   -632       C  
ATOM   2677  CG2 ILE A 274      53.148  58.554 147.729  1.00 68.64           C  
ANISOU 2677  CG2 ILE A 274    11438   7482   7159    282    726   -608       C  
ATOM   2678  CD1 ILE A 274      55.389  60.390 146.383  1.00 69.40           C  
ANISOU 2678  CD1 ILE A 274    11527   7522   7320    133    713   -707       C  
ATOM   2679  N   PHE A 275      50.984  60.510 150.025  1.00 67.25           N  
ANISOU 2679  N   PHE A 275    11381   7220   6951    415    842   -626       N  
ATOM   2680  CA  PHE A 275      50.082  60.043 151.082  1.00 66.76           C  
ANISOU 2680  CA  PHE A 275    11325   7205   6835    480    858   -605       C  
ATOM   2681  C   PHE A 275      48.618  60.374 150.788  1.00 65.58           C  
ANISOU 2681  C   PHE A 275    11176   7038   6703    534    910   -530       C  
ATOM   2682  O   PHE A 275      47.737  59.567 151.096  1.00 64.96           O  
ANISOU 2682  O   PHE A 275    11074   7017   6590    573    917   -467       O  
ATOM   2683  CB  PHE A 275      50.470  60.609 152.462  1.00 68.08           C  
ANISOU 2683  CB  PHE A 275    11536   7376   6956    504    860   -697       C  
ATOM   2684  CG  PHE A 275      51.736  60.022 153.046  1.00 68.78           C  
ANISOU 2684  CG  PHE A 275    11618   7506   7006    466    806   -763       C  
ATOM   2685  CD1 PHE A 275      51.957  58.639 153.065  1.00 68.75           C  
ANISOU 2685  CD1 PHE A 275    11577   7573   6973    457    762   -727       C  
ATOM   2686  CD2 PHE A 275      52.696  60.855 153.620  1.00 69.61           C  
ANISOU 2686  CD2 PHE A 275    11759   7581   7106    442    795   -864       C  
ATOM   2687  CE1 PHE A 275      53.119  58.113 153.610  1.00 68.89           C  
ANISOU 2687  CE1 PHE A 275    11590   7629   6956    428    710   -791       C  
ATOM   2688  CE2 PHE A 275      53.856  60.331 154.170  1.00 69.76           C  
ANISOU 2688  CE2 PHE A 275    11770   7644   7088    409    746   -926       C  
ATOM   2689  CZ  PHE A 275      54.066  58.960 154.168  1.00 69.36           C  
ANISOU 2689  CZ  PHE A 275    11680   7665   7008    405    704   -890       C  
ATOM   2690  N   LEU A 276      48.363  61.549 150.203  1.00 64.80           N  
ANISOU 2690  N   LEU A 276    11102   6862   6656    535    944   -534       N  
ATOM   2691  CA  LEU A 276      46.998  61.936 149.804  1.00 64.27           C  
ANISOU 2691  CA  LEU A 276    11034   6774   6612    588    992   -463       C  
ATOM   2692  C   LEU A 276      46.371  60.986 148.773  1.00 63.13           C  
ANISOU 2692  C   LEU A 276    10836   6664   6485    579    989   -359       C  
ATOM   2693  O   LEU A 276      45.191  60.633 148.893  1.00 63.24           O  
ANISOU 2693  O   LEU A 276    10831   6715   6481    629   1016   -292       O  
ATOM   2694  CB  LEU A 276      46.970  63.370 149.258  1.00 64.72           C  
ANISOU 2694  CB  LEU A 276    11130   6731   6729    584   1017   -486       C  
ATOM   2695  CG  LEU A 276      46.792  64.493 150.276  1.00 65.53           C  
ANISOU 2695  CG  LEU A 276    11290   6789   6819    636   1039   -564       C  
ATOM   2696  CD1 LEU A 276      47.241  65.830 149.707  1.00 65.80           C  
ANISOU 2696  CD1 LEU A 276    11369   6710   6919    604   1038   -602       C  
ATOM   2697  CD2 LEU A 276      45.337  64.565 150.716  1.00 65.84           C  
ANISOU 2697  CD2 LEU A 276    11325   6857   6831    728   1084   -522       C  
ATOM   2698  N   THR A 277      47.165  60.575 147.782  1.00 61.96           N  
ANISOU 2698  N   THR A 277    10661   6512   6369    515    955   -348       N  
ATOM   2699  CA  THR A 277      46.687  59.712 146.698  1.00 60.99           C  
ANISOU 2699  CA  THR A 277    10488   6416   6267    502    945   -259       C  
ATOM   2700  C   THR A 277      46.342  58.312 147.184  1.00 60.38           C  
ANISOU 2700  C   THR A 277    10381   6418   6143    519    917   -218       C  
ATOM   2701  O   THR A 277      45.292  57.776 146.829  1.00 60.40           O  
ANISOU 2701  O   THR A 277    10355   6446   6146    545    929   -134       O  
ATOM   2702  CB  THR A 277      47.717  59.570 145.559  1.00 60.74           C  
ANISOU 2702  CB  THR A 277    10431   6374   6273    432    910   -268       C  
ATOM   2703  OG1 THR A 277      48.953  59.067 146.074  1.00 60.61           O  
ANISOU 2703  OG1 THR A 277    10413   6390   6226    397    862   -339       O  
ATOM   2704  CG2 THR A 277      47.953  60.897 144.880  1.00 61.33           C  
ANISOU 2704  CG2 THR A 277    10530   6372   6400    404    936   -283       C  
ATOM   2705  N   HIS A 278      47.233  57.724 147.983  1.00 60.10           N  
ANISOU 2705  N   HIS A 278    10349   6418   6066    503    874   -275       N  
ATOM   2706  CA  HIS A 278      46.961  56.426 148.613  1.00 59.62           C  
ANISOU 2706  CA  HIS A 278    10267   6427   5957    518    839   -239       C  
ATOM   2707  C   HIS A 278      45.826  56.546 149.630  1.00 59.70           C  
ANISOU 2707  C   HIS A 278    10290   6470   5923    577    879   -208       C  
ATOM   2708  O   HIS A 278      44.971  55.659 149.719  1.00 59.41           O  
ANISOU 2708  O   HIS A 278    10225   6482   5864    594    873   -129       O  
ATOM   2709  CB  HIS A 278      48.213  55.854 149.281  1.00 59.69           C  
ANISOU 2709  CB  HIS A 278    10282   6465   5931    490    782   -311       C  
ATOM   2710  CG  HIS A 278      49.347  55.609 148.333  1.00 59.53           C  
ANISOU 2710  CG  HIS A 278    10240   6433   5944    437    738   -345       C  
ATOM   2711  ND1 HIS A 278      50.663  55.827 148.679  1.00 59.94           N  
ANISOU 2711  ND1 HIS A 278    10303   6485   5984    404    708   -436       N  
ATOM   2712  CD2 HIS A 278      49.360  55.192 147.045  1.00 59.22           C  
ANISOU 2712  CD2 HIS A 278    10163   6390   5945    412    720   -301       C  
ATOM   2713  CE1 HIS A 278      51.440  55.537 147.651  1.00 59.72           C  
ANISOU 2713  CE1 HIS A 278    10244   6460   5986    362    674   -446       C  
ATOM   2714  NE2 HIS A 278      50.674  55.151 146.645  1.00 59.32           N  
ANISOU 2714  NE2 HIS A 278    10163   6408   5967    367    680   -367       N  
ATOM   2715  N   GLY A 279      45.827  57.653 150.377  1.00 60.17           N  
ANISOU 2715  N   GLY A 279    10388   6504   5969    606    918   -270       N  
ATOM   2716  CA  GLY A 279      44.759  57.985 151.320  1.00 60.80           C  
ANISOU 2716  CA  GLY A 279    10478   6617   6004    671    963   -255       C  
ATOM   2717  C   GLY A 279      43.379  58.113 150.698  1.00 61.07           C  
ANISOU 2717  C   GLY A 279    10488   6653   6059    707   1008   -165       C  
ATOM   2718  O   GLY A 279      42.382  57.724 151.319  1.00 61.57           O  
ANISOU 2718  O   GLY A 279    10534   6783   6077    749   1028   -113       O  
ATOM   2719  N   ASN A 280      43.315  58.634 149.470  1.00 60.93           N  
ANISOU 2719  N   ASN A 280    10468   6573   6109    689   1021   -142       N  
ATOM   2720  CA  ASN A 280      42.046  58.746 148.727  1.00 60.76           C  
ANISOU 2720  CA  ASN A 280    10420   6550   6114    721   1060    -54       C  
ATOM   2721  C   ASN A 280      41.260  57.422 148.637  1.00 60.86           C  
ANISOU 2721  C   ASN A 280    10384   6639   6100    720   1042     42       C  
ATOM   2722  O   ASN A 280      40.026  57.437 148.616  1.00 60.81           O  
ANISOU 2722  O   ASN A 280    10355   6666   6084    762   1079    110       O  
ATOM   2723  CB  ASN A 280      42.293  59.304 147.321  1.00 60.01           C  
ANISOU 2723  CB  ASN A 280    10324   6381   6094    687   1063    -40       C  
ATOM   2724  CG  ASN A 280      41.013  59.696 146.612  1.00 59.79           C  
ANISOU 2724  CG  ASN A 280    10278   6342   6096    727   1108     37       C  
ATOM   2725  OD1 ASN A 280      40.641  59.095 145.602  1.00 59.17           O  
ANISOU 2725  OD1 ASN A 280    10161   6274   6044    705   1098    112       O  
ATOM   2726  ND2 ASN A 280      40.329  60.702 147.139  1.00 60.31           N  
ANISOU 2726  ND2 ASN A 280    10371   6387   6155    789   1154     16       N  
ATOM   2727  N   SER A 281      41.973  56.293 148.603  1.00 60.96           N  
ANISOU 2727  N   SER A 281    10380   6679   6101    673    982     48       N  
ATOM   2728  CA  SER A 281      41.335  54.967 148.637  1.00 61.36           C  
ANISOU 2728  CA  SER A 281    10391   6795   6125    665    950    135       C  
ATOM   2729  C   SER A 281      40.580  54.657 149.940  1.00 62.41           C  
ANISOU 2729  C   SER A 281    10520   7007   6186    703    966    162       C  
ATOM   2730  O   SER A 281      39.700  53.790 149.942  1.00 62.68           O  
ANISOU 2730  O   SER A 281    10518   7096   6199    703    957    253       O  
ATOM   2731  CB  SER A 281      42.360  53.859 148.369  1.00 61.23           C  
ANISOU 2731  CB  SER A 281    10365   6783   6115    612    873    123       C  
ATOM   2732  OG  SER A 281      42.944  53.999 147.083  1.00 61.49           O  
ANISOU 2732  OG  SER A 281    10389   6764   6208    577    857    111       O  
ATOM   2733  N   ALA A 282      40.923  55.348 151.033  1.00 63.44           N  
ANISOU 2733  N   ALA A 282    10682   7145   6273    732    988     84       N  
ATOM   2734  CA  ALA A 282      40.230  55.180 152.321  1.00 64.14           C  
ANISOU 2734  CA  ALA A 282    10764   7319   6284    773   1009    101       C  
ATOM   2735  C   ALA A 282      38.962  56.036 152.494  1.00 65.17           C  
ANISOU 2735  C   ALA A 282    10884   7475   6399    840   1082    126       C  
ATOM   2736  O   ALA A 282      38.101  55.693 153.308  1.00 65.35           O  
ANISOU 2736  O   ALA A 282    10882   7590   6358    872   1100    173       O  
ATOM   2737  CB  ALA A 282      41.195  55.457 153.462  1.00 64.38           C  
ANISOU 2737  CB  ALA A 282    10832   7360   6269    776    995      2       C  
ATOM   2738  N   MET A 283      38.836  57.118 151.724  1.00 66.30           N  
ANISOU 2738  N   MET A 283    11046   7544   6601    863   1119     99       N  
ATOM   2739  CA  MET A 283      37.823  58.152 151.991  1.00 67.98           C  
ANISOU 2739  CA  MET A 283    11261   7767   6801    939   1185     93       C  
ATOM   2740  C   MET A 283      36.399  57.710 151.629  1.00 68.77           C  
ANISOU 2740  C   MET A 283    11306   7931   6889    965   1213    206       C  
ATOM   2741  O   MET A 283      35.468  57.840 152.451  1.00 69.43           O  
ANISOU 2741  O   MET A 283    11368   8100   6911   1022   1251    224       O  
ATOM   2742  CB  MET A 283      38.170  59.453 151.244  1.00 68.13           C  
ANISOU 2742  CB  MET A 283    11321   7674   6892    952   1207     32       C  
ATOM   2743  CG  MET A 283      39.550  60.022 151.560  1.00 68.40           C  
ANISOU 2743  CG  MET A 283    11407   7639   6940    923   1181    -78       C  
ATOM   2744  SD  MET A 283      39.895  61.625 150.783  1.00 69.02           S  
ANISOU 2744  SD  MET A 283    11538   7585   7100    933   1203   -143       S  
ATOM   2745  CE  MET A 283      41.642  61.832 151.136  1.00 68.50           C  
ANISOU 2745  CE  MET A 283    11517   7466   7043    870   1155   -253       C  
ATOM   2746  N   ASN A 284      36.243  57.176 150.412  1.00 69.12           N  
ANISOU 2746  N   ASN A 284    11326   7945   6990    922   1193    279       N  
ATOM   2747  CA  ASN A 284      34.925  56.824 149.852  1.00 69.74           C  
ANISOU 2747  CA  ASN A 284    11353   8072   7071    940   1217    386       C  
ATOM   2748  C   ASN A 284      34.020  56.027 150.824  1.00 70.47           C  
ANISOU 2748  C   ASN A 284    11402   8292   7081    956   1223    454       C  
ATOM   2749  O   ASN A 284      32.905  56.489 151.140  1.00 71.41           O  
ANISOU 2749  O   ASN A 284    11493   8471   7165   1018   1276    483       O  
ATOM   2750  CB  ASN A 284      35.068  56.127 148.480  1.00 69.18           C  
ANISOU 2750  CB  ASN A 284    11261   7957   7065    880   1179    451       C  
ATOM   2751  CG  ASN A 284      35.420  57.089 147.353  1.00 69.32           C  
ANISOU 2751  CG  ASN A 284    11303   7874   7160    879   1195    417       C  
ATOM   2752  OD1 ASN A 284      35.303  58.308 147.480  1.00 69.93           O  
ANISOU 2752  OD1 ASN A 284    11410   7908   7250    928   1238    364       O  
ATOM   2753  ND2 ASN A 284      35.851  56.531 146.228  1.00 68.96           N  
ANISOU 2753  ND2 ASN A 284    11244   7790   7165    823   1156    449       N  
ATOM   2754  N   PRO A 285      34.501  54.868 151.337  1.00 70.38           N  
ANISOU 2754  N   PRO A 285    11382   8324   7033    903   1168    478       N  
ATOM   2755  CA  PRO A 285      33.736  54.143 152.364  1.00 70.63           C  
ANISOU 2755  CA  PRO A 285    11375   8479   6980    910   1169    543       C  
ATOM   2756  C   PRO A 285      33.323  55.001 153.557  1.00 70.92           C  
ANISOU 2756  C   PRO A 285    11416   8585   6945    985   1226    488       C  
ATOM   2757  O   PRO A 285      32.196  54.867 154.030  1.00 70.57           O  
ANISOU 2757  O   PRO A 285    11323   8646   6841   1018   1260    552       O  
ATOM   2758  CB  PRO A 285      34.705  53.052 152.825  1.00 70.66           C  
ANISOU 2758  CB  PRO A 285    11393   8489   6964    845   1095    540       C  
ATOM   2759  CG  PRO A 285      35.585  52.821 151.659  1.00 70.02           C  
ANISOU 2759  CG  PRO A 285    11334   8304   6966    796   1049    520       C  
ATOM   2760  CD  PRO A 285      35.753  54.160 151.006  1.00 70.01           C  
ANISOU 2760  CD  PRO A 285    11359   8221   7019    834   1098    450       C  
ATOM   2761  N   ILE A 286      34.224  55.877 154.017  1.00 71.32           N  
ANISOU 2761  N   ILE A 286    11519   8580   6998   1010   1234    369       N  
ATOM   2762  CA  ILE A 286      33.944  56.731 155.177  1.00 72.53           C  
ANISOU 2762  CA  ILE A 286    11682   8793   7083   1085   1282    298       C  
ATOM   2763  C   ILE A 286      32.882  57.774 154.834  1.00 73.31           C  
ANISOU 2763  C   ILE A 286    11767   8891   7196   1166   1347    298       C  
ATOM   2764  O   ILE A 286      31.940  57.960 155.613  1.00 74.20           O  
ANISOU 2764  O   ILE A 286    11844   9113   7235   1228   1389    313       O  
ATOM   2765  CB  ILE A 286      35.219  57.405 155.748  1.00 72.41           C  
ANISOU 2765  CB  ILE A 286    11730   8711   7071   1089   1267    166       C  
ATOM   2766  CG1 ILE A 286      36.169  56.335 156.309  1.00 72.14           C  
ANISOU 2766  CG1 ILE A 286    11703   8703   7004   1021   1204    167       C  
ATOM   2767  CG2 ILE A 286      34.864  58.404 156.848  1.00 73.19           C  
ANISOU 2767  CG2 ILE A 286    11841   8862   7105   1177   1316     84       C  
ATOM   2768  CD1 ILE A 286      37.566  56.829 156.614  1.00 72.14           C  
ANISOU 2768  CD1 ILE A 286    11761   8626   7021   1005   1177     46       C  
ATOM   2769  N   VAL A 287      33.025  58.441 153.685  1.00 73.19           N  
ANISOU 2769  N   VAL A 287    11777   8761   7270   1167   1354    282       N  
ATOM   2770  CA  VAL A 287      32.019  59.437 153.258  1.00 73.82           C  
ANISOU 2770  CA  VAL A 287    11846   8829   7372   1245   1410    286       C  
ATOM   2771  C   VAL A 287      30.647  58.803 152.950  1.00 73.70           C  
ANISOU 2771  C   VAL A 287    11757   8915   7331   1256   1434    410       C  
ATOM   2772  O   VAL A 287      29.608  59.398 153.288  1.00 74.56           O  
ANISOU 2772  O   VAL A 287    11836   9090   7401   1338   1485    414       O  
ATOM   2773  CB  VAL A 287      32.520  60.366 152.107  1.00 73.65           C  
ANISOU 2773  CB  VAL A 287    11872   8658   7453   1241   1409    242       C  
ATOM   2774  CG1 VAL A 287      32.818  59.608 150.825  1.00 72.62           C  
ANISOU 2774  CG1 VAL A 287    11728   8474   7391   1159   1372    318       C  
ATOM   2775  CG2 VAL A 287      31.522  61.481 151.830  1.00 74.53           C  
ANISOU 2775  CG2 VAL A 287    11981   8753   7583   1332   1463    235       C  
ATOM   2776  N   TYR A 288      30.637  57.602 152.356  1.00 72.96           N  
ANISOU 2776  N   TYR A 288    11630   8836   7254   1177   1393    507       N  
ATOM   2777  CA  TYR A 288      29.371  56.867 152.166  1.00 73.41           C  
ANISOU 2777  CA  TYR A 288    11615   8998   7280   1174   1406    631       C  
ATOM   2778  C   TYR A 288      28.656  56.630 153.501  1.00 74.90           C  
ANISOU 2778  C   TYR A 288    11760   9340   7356   1213   1433    650       C  
ATOM   2779  O   TYR A 288      27.447  56.847 153.607  1.00 75.45           O  
ANISOU 2779  O   TYR A 288    11776   9502   7387   1268   1480    700       O  
ATOM   2780  CB  TYR A 288      29.573  55.506 151.477  1.00 72.42           C  
ANISOU 2780  CB  TYR A 288    11466   8864   7183   1077   1345    725       C  
ATOM   2781  CG  TYR A 288      30.137  55.532 150.068  1.00 71.34           C  
ANISOU 2781  CG  TYR A 288    11355   8603   7147   1033   1316    725       C  
ATOM   2782  CD1 TYR A 288      29.722  56.476 149.129  1.00 71.48           C  
ANISOU 2782  CD1 TYR A 288    11377   8556   7223   1076   1355    718       C  
ATOM   2783  CD2 TYR A 288      31.072  54.580 149.664  1.00 70.68           C  
ANISOU 2783  CD2 TYR A 288    11287   8472   7096    951   1247    736       C  
ATOM   2784  CE1 TYR A 288      30.240  56.483 147.842  1.00 70.69           C  
ANISOU 2784  CE1 TYR A 288    11294   8354   7208   1033   1329    723       C  
ATOM   2785  CE2 TYR A 288      31.596  54.583 148.381  1.00 70.18           C  
ANISOU 2785  CE2 TYR A 288    11239   8308   7115    914   1221    733       C  
ATOM   2786  CZ  TYR A 288      31.177  55.532 147.475  1.00 70.09           C  
ANISOU 2786  CZ  TYR A 288    11230   8242   7158    952   1263    729       C  
ATOM   2787  OH  TYR A 288      31.699  55.528 146.204  1.00 69.84           O  
ANISOU 2787  OH  TYR A 288    11210   8124   7202    912   1237    731       O  
ATOM   2788  N   ALA A 289      29.409  56.190 154.508  1.00 75.80           N  
ANISOU 2788  N   ALA A 289    11893   9488   7416   1184   1403    612       N  
ATOM   2789  CA  ALA A 289      28.859  55.906 155.838  1.00 77.14           C  
ANISOU 2789  CA  ALA A 289    12023   9813   7473   1212   1423    630       C  
ATOM   2790  C   ALA A 289      28.268  57.146 156.494  1.00 79.04           C  
ANISOU 2790  C   ALA A 289    12259  10104   7665   1326   1491    551       C  
ATOM   2791  O   ALA A 289      27.173  57.091 157.051  1.00 79.94           O  
ANISOU 2791  O   ALA A 289    12311  10360   7702   1372   1531    601       O  
ATOM   2792  CB  ALA A 289      29.929  55.303 156.735  1.00 77.02           C  
ANISOU 2792  CB  ALA A 289    12039   9806   7416   1162   1373    591       C  
ATOM   2793  N   PHE A 290      28.994  58.259 156.418  1.00 80.60           N  
ANISOU 2793  N   PHE A 290    12523  10189   7909   1372   1501    427       N  
ATOM   2794  CA  PHE A 290      28.522  59.531 156.976  1.00 82.80           C  
ANISOU 2794  CA  PHE A 290    12810  10492   8155   1487   1557    336       C  
ATOM   2795  C   PHE A 290      27.334  60.111 156.203  1.00 84.27           C  
ANISOU 2795  C   PHE A 290    12960  10684   8372   1553   1603    379       C  
ATOM   2796  O   PHE A 290      26.344  60.504 156.823  1.00 85.60           O  
ANISOU 2796  O   PHE A 290    13083  10971   8469   1638   1651    376       O  
ATOM   2797  CB  PHE A 290      29.660  60.562 157.039  1.00 83.21           C  
ANISOU 2797  CB  PHE A 290    12949  10405   8259   1509   1545    194       C  
ATOM   2798  CG  PHE A 290      30.486  60.476 158.293  1.00 84.09           C  
ANISOU 2798  CG  PHE A 290    13088  10559   8302   1505   1526    113       C  
ATOM   2799  CD1 PHE A 290      31.266  59.356 158.563  1.00 83.83           C  
ANISOU 2799  CD1 PHE A 290    13056  10545   8250   1411   1475    150       C  
ATOM   2800  CD2 PHE A 290      30.481  61.523 159.215  1.00 85.65           C  
ANISOU 2800  CD2 PHE A 290    13312  10778   8452   1599   1556     -5       C  
ATOM   2801  CE1 PHE A 290      32.020  59.279 159.724  1.00 84.58           C  
ANISOU 2801  CE1 PHE A 290    13175  10682   8279   1408   1456     77       C  
ATOM   2802  CE2 PHE A 290      31.239  61.454 160.376  1.00 86.02           C  
ANISOU 2802  CE2 PHE A 290    13382  10869   8432   1596   1538    -83       C  
ATOM   2803  CZ  PHE A 290      32.009  60.330 160.631  1.00 85.60           C  
ANISOU 2803  CZ  PHE A 290    13327  10837   8359   1499   1490    -39       C  
ATOM   2804  N   ARG A 291      27.419  60.152 154.870  1.00 85.06           N  
ANISOU 2804  N   ARG A 291    13077  10668   8573   1515   1588    419       N  
ATOM   2805  CA  ARG A 291      26.397  60.848 154.062  1.00 86.41           C  
ANISOU 2805  CA  ARG A 291    13223  10822   8783   1582   1629    448       C  
ATOM   2806  C   ARG A 291      25.246  59.972 153.549  1.00 86.46           C  
ANISOU 2806  C   ARG A 291    13146  10932   8772   1556   1640    591       C  
ATOM   2807  O   ARG A 291      24.080  60.354 153.681  1.00 87.35           O  
ANISOU 2807  O   ARG A 291    13205  11138   8843   1635   1687    617       O  
ATOM   2808  CB  ARG A 291      27.056  61.578 152.894  1.00 86.91           C  
ANISOU 2808  CB  ARG A 291    13352  10704   8964   1568   1613    407       C  
ATOM   2809  CG  ARG A 291      27.947  62.727 153.336  1.00 88.06           C  
ANISOU 2809  CG  ARG A 291    13578  10746   9132   1612   1610    265       C  
ATOM   2810  CD  ARG A 291      28.386  63.579 152.153  1.00 88.49           C  
ANISOU 2810  CD  ARG A 291    13689  10631   9299   1606   1599    236       C  
ATOM   2811  NE  ARG A 291      27.268  64.314 151.555  1.00 89.38           N  
ANISOU 2811  NE  ARG A 291    13780  10740   9439   1688   1638    265       N  
ATOM   2812  CZ  ARG A 291      26.720  65.426 152.055  1.00 90.62           C  
ANISOU 2812  CZ  ARG A 291    13953  10900   9577   1803   1671    190       C  
ATOM   2813  NH1 ARG A 291      27.159  65.974 153.192  1.00 91.13           N  
ANISOU 2813  NH1 ARG A 291    14055  10974   9593   1854   1672     76       N  
ATOM   2814  NH2 ARG A 291      25.703  65.989 151.410  1.00 91.27           N  
ANISOU 2814  NH2 ARG A 291    14012  10978   9688   1873   1701    226       N  
ATOM   2815  N   ILE A 292      25.566  58.818 152.962  1.00 86.13           N  
ANISOU 2815  N   ILE A 292    13092  10874   8760   1449   1593    680       N  
ATOM   2816  CA  ILE A 292      24.552  57.955 152.335  1.00 86.56           C  
ANISOU 2816  CA  ILE A 292    13072  11005   8811   1411   1593    817       C  
ATOM   2817  C   ILE A 292      23.882  57.044 153.375  1.00 88.62           C  
ANISOU 2817  C   ILE A 292    13263  11444   8961   1393   1596    892       C  
ATOM   2818  O   ILE A 292      24.515  56.142 153.935  1.00 88.03           O  
ANISOU 2818  O   ILE A 292    13197  11394   8856   1320   1551    910       O  
ATOM   2819  CB  ILE A 292      25.122  57.113 151.170  1.00 84.90           C  
ANISOU 2819  CB  ILE A 292    12877  10696   8685   1307   1536    879       C  
ATOM   2820  CG1 ILE A 292      25.823  58.026 150.151  1.00 84.10           C  
ANISOU 2820  CG1 ILE A 292    12840  10428   8684   1319   1533    808       C  
ATOM   2821  CG2 ILE A 292      24.004  56.316 150.495  1.00 84.79           C  
ANISOU 2821  CG2 ILE A 292    12788  10756   8670   1275   1535   1015       C  
ATOM   2822  CD1 ILE A 292      26.324  57.331 148.901  1.00 82.95           C  
ANISOU 2822  CD1 ILE A 292    12703  10193   8620   1230   1483    862       C  
ATOM   2823  N   GLN A 293      22.594  57.304 153.603  1.00 91.38           N  
ANISOU 2823  N   GLN A 293    13543  11920   9254   1461   1648    937       N  
ATOM   2824  CA  GLN A 293      21.742  56.576 154.565  1.00 93.67           C  
ANISOU 2824  CA  GLN A 293    13752  12405   9430   1454   1662   1017       C  
ATOM   2825  C   GLN A 293      21.688  55.044 154.413  1.00 93.13           C  
ANISOU 2825  C   GLN A 293    13647  12385   9353   1329   1606   1150       C  
ATOM   2826  O   GLN A 293      21.715  54.319 155.412  1.00 93.53           O  
ANISOU 2826  O   GLN A 293    13670  12546   9319   1290   1588   1188       O  
ATOM   2827  CB  GLN A 293      20.308  57.142 154.509  1.00 95.95           C  
ANISOU 2827  CB  GLN A 293    13966  12811   9677   1546   1726   1052       C  
ATOM   2828  CG  GLN A 293      19.606  56.977 153.159  1.00 96.41           C  
ANISOU 2828  CG  GLN A 293    13993  12827   9810   1524   1726   1142       C  
ATOM   2829  CD  GLN A 293      18.578  58.052 152.837  1.00 98.11           C  
ANISOU 2829  CD  GLN A 293    14175  13076  10026   1643   1788   1119       C  
ATOM   2830  OE1 GLN A 293      18.527  59.121 153.456  1.00 99.73           O  
ANISOU 2830  OE1 GLN A 293    14399  13294  10199   1753   1828   1013       O  
ATOM   2831  NE2 GLN A 293      17.753  57.768 151.843  1.00 98.01           N  
ANISOU 2831  NE2 GLN A 293    14113  13074  10052   1624   1791   1216       N  
ATOM   2832  N   LYS A 294      21.605  54.565 153.173  1.00 91.76           N  
ANISOU 2832  N   LYS A 294    13472  12128   9264   1270   1574   1221       N  
ATOM   2833  CA  LYS A 294      21.418  53.135 152.893  1.00 90.51           C  
ANISOU 2833  CA  LYS A 294    13277  12006   9106   1157   1515   1352       C  
ATOM   2834  C   LYS A 294      22.680  52.307 153.150  1.00 88.64           C  
ANISOU 2834  C   LYS A 294    13098  11693   8888   1070   1441   1334       C  
ATOM   2835  O   LYS A 294      22.583  51.126 153.482  1.00 88.10           O  
ANISOU 2835  O   LYS A 294    13001  11688   8784    987   1390   1428       O  
ATOM   2836  CB  LYS A 294      20.941  52.934 151.452  1.00 90.72           C  
ANISOU 2836  CB  LYS A 294    13285  11964   9218   1128   1503   1422       C  
ATOM   2837  CG  LYS A 294      19.539  53.464 151.178  1.00 92.25           C  
ANISOU 2837  CG  LYS A 294    13407  12257   9387   1199   1566   1472       C  
ATOM   2838  CD  LYS A 294      19.358  53.903 149.730  1.00 92.23           C  
ANISOU 2838  CD  LYS A 294    13416  12142   9484   1213   1571   1477       C  
ATOM   2839  CE  LYS A 294      18.003  54.561 149.503  1.00 93.17           C  
ANISOU 2839  CE  LYS A 294    13466  12356   9577   1298   1636   1513       C  
ATOM   2840  NZ  LYS A 294      17.711  54.768 148.055  1.00 92.62           N  
ANISOU 2840  NZ  LYS A 294    13396  12194   9599   1296   1633   1546       N  
ATOM   2841  N   PHE A 295      23.853  52.916 152.979  1.00 87.39           N  
ANISOU 2841  N   PHE A 295    13019  11398   8785   1086   1430   1217       N  
ATOM   2842  CA  PHE A 295      25.129  52.273 153.329  1.00 86.61           C  
ANISOU 2842  CA  PHE A 295    12976  11233   8698   1019   1364   1180       C  
ATOM   2843  C   PHE A 295      25.327  52.196 154.850  1.00 87.21           C  
ANISOU 2843  C   PHE A 295    13049  11417   8670   1033   1371   1149       C  
ATOM   2844  O   PHE A 295      25.818  51.182 155.365  1.00 88.07           O  
ANISOU 2844  O   PHE A 295    13163  11547   8749    959   1312   1189       O  
ATOM   2845  CB  PHE A 295      26.319  53.006 152.682  1.00 85.89           C  
ANISOU 2845  CB  PHE A 295    12965  10975   8695   1032   1354   1063       C  
ATOM   2846  CG  PHE A 295      26.545  52.658 151.230  1.00 84.95           C  
ANISOU 2846  CG  PHE A 295    12857  10742   8675    981   1316   1099       C  
ATOM   2847  CD1 PHE A 295      26.915  51.365 150.860  1.00 84.66           C  
ANISOU 2847  CD1 PHE A 295    12819  10683   8664    887   1238   1168       C  
ATOM   2848  CD2 PHE A 295      26.421  53.622 150.233  1.00 84.25           C  
ANISOU 2848  CD2 PHE A 295    12785  10569   8657   1027   1352   1061       C  
ATOM   2849  CE1 PHE A 295      27.134  51.039 149.527  1.00 83.49           C  
ANISOU 2849  CE1 PHE A 295    12679  10438   8602    846   1201   1193       C  
ATOM   2850  CE2 PHE A 295      26.644  53.302 148.901  1.00 83.49           C  
ANISOU 2850  CE2 PHE A 295    12696  10379   8647    980   1317   1093       C  
ATOM   2851  CZ  PHE A 295      26.998  52.007 148.547  1.00 82.95           C  
ANISOU 2851  CZ  PHE A 295    12622  10298   8598    891   1243   1156       C  
ATOM   2852  N   ARG A 296      24.956  53.271 155.551  1.00 87.19           N  
ANISOU 2852  N   ARG A 296    13038  11478   8612   1131   1440   1074       N  
ATOM   2853  CA  ARG A 296      25.028  53.338 157.018  1.00 87.03           C  
ANISOU 2853  CA  ARG A 296    13007  11578   8483   1160   1457   1037       C  
ATOM   2854  C   ARG A 296      24.250  52.204 157.695  1.00 86.29           C  
ANISOU 2854  C   ARG A 296    12838  11649   8298   1102   1439   1170       C  
ATOM   2855  O   ARG A 296      24.776  51.534 158.587  1.00 85.52           O  
ANISOU 2855  O   ARG A 296    12749  11601   8144   1053   1400   1182       O  
ATOM   2856  CB  ARG A 296      24.524  54.705 157.513  1.00 88.75           C  
ANISOU 2856  CB  ARG A 296    13216  11845   8657   1286   1536    942       C  
ATOM   2857  CG  ARG A 296      24.358  54.821 159.023  1.00 90.88           C  
ANISOU 2857  CG  ARG A 296    13458  12271   8801   1330   1564    908       C  
ATOM   2858  CD  ARG A 296      24.372  56.258 159.522  1.00 92.33           C  
ANISOU 2858  CD  ARG A 296    13667  12450   8961   1456   1622    765       C  
ATOM   2859  NE  ARG A 296      25.733  56.745 159.754  1.00 92.87           N  
ANISOU 2859  NE  ARG A 296    13827  12390   9070   1456   1595    637       N  
ATOM   2860  CZ  ARG A 296      26.052  57.894 160.355  1.00 94.27           C  
ANISOU 2860  CZ  ARG A 296    14043  12546   9227   1549   1627    499       C  
ATOM   2861  NH1 ARG A 296      25.109  58.716 160.816  1.00 95.53           N  
ANISOU 2861  NH1 ARG A 296    14163  12808   9325   1660   1688    461       N  
ATOM   2862  NH2 ARG A 296      27.336  58.226 160.504  1.00 94.15           N  
ANISOU 2862  NH2 ARG A 296    14108  12409   9252   1532   1594    394       N  
ATOM   2863  N   VAL A 297      23.008  52.000 157.263  1.00 85.52           N  
ANISOU 2863  N   VAL A 297    12667  11637   8186   1104   1466   1274       N  
ATOM   2864  CA  VAL A 297      22.145  50.936 157.803  1.00 85.46           C  
ANISOU 2864  CA  VAL A 297    12581  11793   8096   1041   1449   1416       C  
ATOM   2865  C   VAL A 297      22.712  49.535 157.494  1.00 84.24           C  
ANISOU 2865  C   VAL A 297    12449  11576   7983    911   1352   1507       C  
ATOM   2866  O   VAL A 297      22.605  48.624 158.315  1.00 85.37           O  
ANISOU 2866  O   VAL A 297    12562  11822   8052    847   1315   1589       O  
ATOM   2867  CB  VAL A 297      20.676  51.071 157.289  1.00 85.79           C  
ANISOU 2867  CB  VAL A 297    12536  11936   8122   1070   1498   1506       C  
ATOM   2868  CG1 VAL A 297      19.801  49.885 157.702  1.00 86.23           C  
ANISOU 2868  CG1 VAL A 297    12509  12150   8102    986   1470   1668       C  
ATOM   2869  CG2 VAL A 297      20.051  52.373 157.781  1.00 86.90           C  
ANISOU 2869  CG2 VAL A 297    12649  12165   8205   1205   1588   1419       C  
ATOM   2870  N   THR A 298      23.315  49.377 156.319  1.00 82.44           N  
ANISOU 2870  N   THR A 298    12272  11181   7870    876   1309   1491       N  
ATOM   2871  CA  THR A 298      23.916  48.108 155.910  1.00 81.36           C  
ANISOU 2871  CA  THR A 298    12162  10966   7784    766   1212   1559       C  
ATOM   2872  C   THR A 298      25.207  47.796 156.680  1.00 81.39           C  
ANISOU 2872  C   THR A 298    12229  10922   7773    738   1160   1491       C  
ATOM   2873  O   THR A 298      25.331  46.697 157.246  1.00 82.34           O  
ANISOU 2873  O   THR A 298    12341  11089   7853    660   1095   1571       O  
ATOM   2874  CB  THR A 298      24.196  48.085 154.397  1.00 79.78           C  
ANISOU 2874  CB  THR A 298    11994  10610   7707    747   1183   1550       C  
ATOM   2875  OG1 THR A 298      23.012  48.461 153.687  1.00 79.37           O  
ANISOU 2875  OG1 THR A 298    11884  10603   7668    780   1234   1607       O  
ATOM   2876  CG2 THR A 298      24.634  46.694 153.949  1.00 79.09           C  
ANISOU 2876  CG2 THR A 298    11924  10459   7667    638   1079   1630       C  
ATOM   2877  N   PHE A 299      26.144  48.753 156.724  1.00 80.88           N  
ANISOU 2877  N   PHE A 299    12226  10766   7738    798   1186   1347       N  
ATOM   2878  CA  PHE A 299      27.432  48.550 157.433  1.00 80.54           C  
ANISOU 2878  CA  PHE A 299    12244  10674   7683    777   1139   1270       C  
ATOM   2879  C   PHE A 299      27.229  48.101 158.891  1.00 82.05           C  
ANISOU 2879  C   PHE A 299    12403  11017   7752    763   1135   1312       C  
ATOM   2880  O   PHE A 299      27.930  47.201 159.378  1.00 82.01           O  
ANISOU 2880  O   PHE A 299    12423  11003   7731    697   1062   1337       O  
ATOM   2881  CB  PHE A 299      28.320  49.811 157.420  1.00 79.67           C  
ANISOU 2881  CB  PHE A 299    12194  10469   7605    852   1180   1109       C  
ATOM   2882  CG  PHE A 299      28.734  50.297 156.043  1.00 78.38           C  
ANISOU 2882  CG  PHE A 299    12070  10151   7559    859   1179   1058       C  
ATOM   2883  CD1 PHE A 299      28.852  49.435 154.943  1.00 77.43           C  
ANISOU 2883  CD1 PHE A 299    11951   9950   7516    789   1117   1127       C  
ATOM   2884  CD2 PHE A 299      29.042  51.644 155.857  1.00 78.08           C  
ANISOU 2884  CD2 PHE A 299    12067  10046   7551    937   1235    939       C  
ATOM   2885  CE1 PHE A 299      29.244  49.919 153.698  1.00 76.13           C  
ANISOU 2885  CE1 PHE A 299    11817   9656   7450    798   1119   1079       C  
ATOM   2886  CE2 PHE A 299      29.437  52.125 154.613  1.00 76.94           C  
ANISOU 2886  CE2 PHE A 299    11957   9766   7510    940   1234    898       C  
ATOM   2887  CZ  PHE A 299      29.537  51.262 153.535  1.00 75.86           C  
ANISOU 2887  CZ  PHE A 299    11815   9563   7442    871   1178    969       C  
ATOM   2888  N   LEU A 300      26.271  48.731 159.571  1.00 83.26           N  
ANISOU 2888  N   LEU A 300    12500  11314   7819    827   1212   1319       N  
ATOM   2889  CA  LEU A 300      25.839  48.301 160.905  1.00 84.68           C  
ANISOU 2889  CA  LEU A 300    12632  11671   7872    814   1217   1378       C  
ATOM   2890  C   LEU A 300      25.372  46.846 160.915  1.00 84.66           C  
ANISOU 2890  C   LEU A 300    12588  11728   7849    703   1145   1545       C  
ATOM   2891  O   LEU A 300      25.754  46.083 161.802  1.00 85.20           O  
ANISOU 2891  O   LEU A 300    12660  11852   7857    647   1094   1587       O  
ATOM   2892  CB  LEU A 300      24.709  49.197 161.428  1.00 86.17           C  
ANISOU 2892  CB  LEU A 300    12751  12013   7973    906   1313   1367       C  
ATOM   2893  CG  LEU A 300      25.091  50.628 161.814  1.00 86.87           C  
ANISOU 2893  CG  LEU A 300    12875  12079   8049   1023   1380   1202       C  
ATOM   2894  CD1 LEU A 300      23.847  51.496 161.948  1.00 87.91           C  
ANISOU 2894  CD1 LEU A 300    12939  12336   8124   1120   1468   1197       C  
ATOM   2895  CD2 LEU A 300      25.899  50.643 163.105  1.00 87.33           C  
ANISOU 2895  CD2 LEU A 300    12963  12191   8028   1030   1367   1131       C  
ATOM   2896  N   LYS A 301      24.556  46.470 159.929  1.00 84.23           N  
ANISOU 2896  N   LYS A 301    12497  11659   7848    669   1138   1641       N  
ATOM   2897  CA  LYS A 301      24.033  45.097 159.838  1.00 84.25           C  
ANISOU 2897  CA  LYS A 301    12460  11708   7841    559   1065   1805       C  
ATOM   2898  C   LYS A 301      25.154  44.084 159.598  1.00 83.75           C  
ANISOU 2898  C   LYS A 301    12466  11509   7844    475    954   1813       C  
ATOM   2899  O   LYS A 301      25.191  43.039 160.248  1.00 84.18           O  
ANISOU 2899  O   LYS A 301    12511  11619   7851    395    885   1908       O  
ATOM   2900  CB  LYS A 301      22.958  44.973 158.753  1.00 83.54           C  
ANISOU 2900  CB  LYS A 301    12318  11619   7801    545   1079   1894       C  
ATOM   2901  CG  LYS A 301      22.174  43.666 158.821  1.00 83.40           C  
ANISOU 2901  CG  LYS A 301    12245  11688   7753    435   1015   2073       C  
ATOM   2902  CD  LYS A 301      20.964  43.678 157.914  1.00 83.00           C  
ANISOU 2902  CD  LYS A 301    12130  11674   7731    431   1045   2159       C  
ATOM   2903  CE  LYS A 301      19.796  44.440 158.519  1.00 83.81           C  
ANISOU 2903  CE  LYS A 301    12143  11968   7730    501   1146   2178       C  
ATOM   2904  NZ  LYS A 301      18.557  44.258 157.719  1.00 83.84           N  
ANISOU 2904  NZ  LYS A 301    12074  12028   7751    481   1163   2285       N  
ATOM   2905  N   ILE A 302      26.067  44.407 158.683  1.00 83.39           N  
ANISOU 2905  N   ILE A 302    12487  11291   7904    495    935   1713       N  
ATOM   2906  CA  ILE A 302      27.226  43.546 158.411  1.00 83.15           C  
ANISOU 2906  CA  ILE A 302    12525  11129   7939    431    831   1698       C  
ATOM   2907  C   ILE A 302      28.117  43.449 159.658  1.00 83.92           C  
ANISOU 2907  C   ILE A 302    12656  11260   7967    431    808   1644       C  
ATOM   2908  O   ILE A 302      28.545  42.346 160.029  1.00 84.10           O  
ANISOU 2908  O   ILE A 302    12698  11273   7981    355    715   1708       O  
ATOM   2909  CB  ILE A 302      28.036  44.032 157.180  1.00 82.09           C  
ANISOU 2909  CB  ILE A 302    12446  10819   7922    461    826   1591       C  
ATOM   2910  CG1 ILE A 302      27.190  43.904 155.906  1.00 81.90           C  
ANISOU 2910  CG1 ILE A 302    12389  10760   7968    447    831   1660       C  
ATOM   2911  CG2 ILE A 302      29.329  43.232 157.018  1.00 81.65           C  
ANISOU 2911  CG2 ILE A 302    12458  10643   7922    409    724   1555       C  
ATOM   2912  CD1 ILE A 302      27.663  44.766 154.758  1.00 81.41           C  
ANISOU 2912  CD1 ILE A 302    12363  10569   8000    499    863   1556       C  
ATOM   2913  N   TRP A 303      28.372  44.593 160.301  1.00 84.77           N  
ANISOU 2913  N   TRP A 303    12773  11408   8027    515    887   1528       N  
ATOM   2914  CA  TRP A 303      29.149  44.638 161.552  1.00 85.75           C  
ANISOU 2914  CA  TRP A 303    12924  11581   8075    525    876   1469       C  
ATOM   2915  C   TRP A 303      28.526  43.749 162.627  1.00 87.55           C  
ANISOU 2915  C   TRP A 303    13100  11968   8194    466    847   1600       C  
ATOM   2916  O   TRP A 303      29.189  42.844 163.145  1.00 87.70           O  
ANISOU 2916  O   TRP A 303    13149  11974   8199    403    763   1636       O  
ATOM   2917  CB  TRP A 303      29.268  46.081 162.064  1.00 85.95           C  
ANISOU 2917  CB  TRP A 303    12956  11643   8059    631    973   1332       C  
ATOM   2918  CG  TRP A 303      29.999  46.229 163.379  1.00 86.34           C  
ANISOU 2918  CG  TRP A 303    13027  11754   8022    649    970   1263       C  
ATOM   2919  CD1 TRP A 303      31.256  45.784 163.676  1.00 85.88           C  
ANISOU 2919  CD1 TRP A 303    13030  11617   7983    614    899   1211       C  
ATOM   2920  CD2 TRP A 303      29.518  46.887 164.560  1.00 87.20           C  
ANISOU 2920  CD2 TRP A 303    13096  12023   8011    711   1040   1233       C  
ATOM   2921  NE1 TRP A 303      31.584  46.112 164.974  1.00 86.28           N  
ANISOU 2921  NE1 TRP A 303    13082  11767   7933    647    920   1155       N  
ATOM   2922  CE2 TRP A 303      30.536  46.793 165.537  1.00 87.31           C  
ANISOU 2922  CE2 TRP A 303    13151  12045   7976    707   1007   1165       C  
ATOM   2923  CE3 TRP A 303      28.321  47.543 164.890  1.00 87.86           C  
ANISOU 2923  CE3 TRP A 303    13110  12250   8021    774   1127   1253       C  
ATOM   2924  CZ2 TRP A 303      30.393  47.328 166.826  1.00 88.37           C  
ANISOU 2924  CZ2 TRP A 303    13261  12326   7990    761   1057   1118       C  
ATOM   2925  CZ3 TRP A 303      28.179  48.078 166.173  1.00 88.81           C  
ANISOU 2925  CZ3 TRP A 303    13204  12519   8020    832   1177   1202       C  
ATOM   2926  CH2 TRP A 303      29.212  47.965 167.123  1.00 89.13           C  
ANISOU 2926  CH2 TRP A 303    13288  12563   8013    824   1142   1135       C  
ATOM   2927  N   ASN A 304      27.251  44.000 162.923  1.00 89.37           N  
ANISOU 2927  N   ASN A 304    13252  12350   8351    486    913   1675       N  
ATOM   2928  CA  ASN A 304      26.497  43.233 163.926  1.00 91.32           C  
ANISOU 2928  CA  ASN A 304    13436  12775   8486    428    896   1811       C  
ATOM   2929  C   ASN A 304      26.435  41.740 163.598  1.00 91.45           C  
ANISOU 2929  C   ASN A 304    13456  12750   8540    305    783   1960       C  
ATOM   2930  O   ASN A 304      26.736  40.902 164.452  1.00 92.42           O  
ANISOU 2930  O   ASN A 304    13584  12924   8605    240    716   2027       O  
ATOM   2931  CB  ASN A 304      25.070  43.781 164.078  1.00 92.64           C  
ANISOU 2931  CB  ASN A 304    13510  13108   8578    472    988   1867       C  
ATOM   2932  CG  ASN A 304      25.025  45.128 164.772  1.00 93.98           C  
ANISOU 2932  CG  ASN A 304    13667  13362   8677    592   1091   1735       C  
ATOM   2933  OD1 ASN A 304      25.609  45.312 165.843  1.00 95.29           O  
ANISOU 2933  OD1 ASN A 304    13850  13587   8767    615   1095   1673       O  
ATOM   2934  ND2 ASN A 304      24.313  46.077 164.170  1.00 94.32           N  
ANISOU 2934  ND2 ASN A 304    13681  13413   8744    673   1172   1690       N  
ATOM   2935  N   ASP A 305      26.057  41.416 162.361  1.00 90.87           N  
ANISOU 2935  N   ASP A 305    13380  12581   8563    274    757   2009       N  
ATOM   2936  CA  ASP A 305      25.872  40.017 161.955  1.00 90.92           C  
ANISOU 2936  CA  ASP A 305    13388  12545   8612    160    646   2152       C  
ATOM   2937  C   ASP A 305      27.174  39.235 161.742  1.00 90.60           C  
ANISOU 2937  C   ASP A 305    13433  12343   8647    114    533   2115       C  
ATOM   2938  O   ASP A 305      27.167  38.012 161.893  1.00 91.66           O  
ANISOU 2938  O   ASP A 305    13575  12468   8784     20    429   2231       O  
ATOM   2939  CB  ASP A 305      25.000  39.922 160.695  1.00 90.59           C  
ANISOU 2939  CB  ASP A 305    13312  12459   8646    144    653   2215       C  
ATOM   2940  CG  ASP A 305      23.583  40.434 160.919  1.00 91.70           C  
ANISOU 2940  CG  ASP A 305    13357  12775   8707    172    747   2285       C  
ATOM   2941  OD1 ASP A 305      23.325  41.087 161.952  1.00 92.51           O  
ANISOU 2941  OD1 ASP A 305    13422  13024   8703    226    822   2254       O  
ATOM   2942  OD2 ASP A 305      22.721  40.186 160.052  1.00 92.43           O  
ANISOU 2942  OD2 ASP A 305    13410  12865   8844    143    745   2366       O  
ATOM   2943  N   HIS A 306      28.273  39.912 161.392  1.00 90.12           N  
ANISOU 2943  N   HIS A 306    13437  12158   8646    179    547   1958       N  
ATOM   2944  CA  HIS A 306      29.536  39.207 161.096  1.00 89.69           C  
ANISOU 2944  CA  HIS A 306    13459  11951   8665    143    441   1913       C  
ATOM   2945  C   HIS A 306      30.768  39.643 161.912  1.00 89.63           C  
ANISOU 2945  C   HIS A 306    13505  11924   8627    187    443   1785       C  
ATOM   2946  O   HIS A 306      31.525  38.782 162.358  1.00 89.48           O  
ANISOU 2946  O   HIS A 306    13524  11867   8604    138    348   1804       O  
ATOM   2947  CB  HIS A 306      29.829  39.265 159.590  1.00 89.08           C  
ANISOU 2947  CB  HIS A 306    13414  11715   8718    154    420   1861       C  
ATOM   2948  CG  HIS A 306      28.795  38.579 158.749  1.00 89.42           C  
ANISOU 2948  CG  HIS A 306    13416  11756   8802     97    387   1990       C  
ATOM   2949  ND1 HIS A 306      28.966  37.307 158.247  1.00 89.51           N  
ANISOU 2949  ND1 HIS A 306    13453  11681   8876     16    263   2070       N  
ATOM   2950  CD2 HIS A 306      27.572  38.986 158.329  1.00 89.97           C  
ANISOU 2950  CD2 HIS A 306    13421  11901   8861    109    459   2051       C  
ATOM   2951  CE1 HIS A 306      27.897  36.961 157.551  1.00 89.79           C  
ANISOU 2951  CE1 HIS A 306    13442  11736   8937    -22    260   2175       C  
ATOM   2952  NE2 HIS A 306      27.035  37.961 157.587  1.00 90.08           N  
ANISOU 2952  NE2 HIS A 306    13422  11875   8929     32    379   2167       N  
ATOM   2953  N   PHE A 307      30.973  40.949 162.109  1.00 90.27           N  
ANISOU 2953  N   PHE A 307    13587  12025   8685    277    544   1657       N  
ATOM   2954  CA  PHE A 307      32.204  41.467 162.749  1.00 90.76           C  
ANISOU 2954  CA  PHE A 307    13702  12052   8729    322    547   1520       C  
ATOM   2955  C   PHE A 307      32.011  41.995 164.178  1.00 93.39           C  
ANISOU 2955  C   PHE A 307    14008  12543   8933    358    608   1501       C  
ATOM   2956  O   PHE A 307      32.813  42.799 164.664  1.00 93.55           O  
ANISOU 2956  O   PHE A 307    14062  12549   8933    418    644   1368       O  
ATOM   2957  CB  PHE A 307      32.837  42.542 161.847  1.00 89.22           C  
ANISOU 2957  CB  PHE A 307    13545  11735   8618    392    599   1370       C  
ATOM   2958  CG  PHE A 307      33.469  41.980 160.606  1.00 87.43           C  
ANISOU 2958  CG  PHE A 307    13359  11349   8510    358    524   1358       C  
ATOM   2959  CD1 PHE A 307      32.723  41.803 159.446  1.00 86.40           C  
ANISOU 2959  CD1 PHE A 307    13204  11175   8448    341    525   1421       C  
ATOM   2960  CD2 PHE A 307      34.807  41.595 160.607  1.00 86.56           C  
ANISOU 2960  CD2 PHE A 307    13309  11141   8439    344    448   1283       C  
ATOM   2961  CE1 PHE A 307      33.302  41.265 158.310  1.00 85.56           C  
ANISOU 2961  CE1 PHE A 307    13131  10931   8445    313    454   1406       C  
ATOM   2962  CE2 PHE A 307      35.392  41.059 159.471  1.00 85.52           C  
ANISOU 2962  CE2 PHE A 307    13209  10875   8410    318    376   1266       C  
ATOM   2963  CZ  PHE A 307      34.638  40.891 158.320  1.00 85.09           C  
ANISOU 2963  CZ  PHE A 307    13129  10779   8421    303    379   1327       C  
ATOM   2964  N   ARG A 308      30.968  41.522 164.857  1.00 96.67           N  
ANISOU 2964  N   ARG A 308    14360  13110   9258    321    616   1633       N  
ATOM   2965  CA  ARG A 308      30.667  41.957 166.221  1.00 99.14           C  
ANISOU 2965  CA  ARG A 308    14634  13596   9436    354    674   1627       C  
ATOM   2966  C   ARG A 308      31.453  41.119 167.233  1.00101.03           C  
ANISOU 2966  C   ARG A 308    14903  13862   9619    299    590   1657       C  
ATOM   2967  O   ARG A 308      31.652  39.917 167.041  1.00100.85           O  
ANISOU 2967  O   ARG A 308    14900  13784   9633    213    484   1757       O  
ATOM   2968  CB  ARG A 308      29.163  41.838 166.492  1.00100.17           C  
ANISOU 2968  CB  ARG A 308    14673  13898   9487    337    723   1761       C  
ATOM   2969  CG  ARG A 308      28.640  42.708 167.627  1.00100.98           C  
ANISOU 2969  CG  ARG A 308    14723  14188   9458    408    820   1721       C  
ATOM   2970  CD  ARG A 308      28.689  44.193 167.286  1.00100.46           C  
ANISOU 2970  CD  ARG A 308    14667  14085   9417    526    921   1562       C  
ATOM   2971  NE  ARG A 308      27.764  44.983 168.097  1.00101.37           N  
ANISOU 2971  NE  ARG A 308    14711  14389   9415    598   1018   1550       N  
ATOM   2972  CZ  ARG A 308      27.940  45.310 169.377  1.00102.63           C  
ANISOU 2972  CZ  ARG A 308    14855  14682   9456    636   1047   1503       C  
ATOM   2973  NH1 ARG A 308      29.015  44.909 170.060  1.00102.82           N  
ANISOU 2973  NH1 ARG A 308    14931  14675   9460    605    986   1467       N  
ATOM   2974  NH2 ARG A 308      27.013  46.042 169.995  1.00103.70           N  
ANISOU 2974  NH2 ARG A 308    14919  14993   9488    709   1136   1490       N  
ATOM   2975  N   CYS A 309      31.897  41.777 168.301  1.00128.03           N  
ANISOU 2975  N   CYS A 309    14505  21972  12167  -4848   1539  -3139       N  
ATOM   2976  CA  CYS A 309      32.625  41.147 169.401  1.00126.19           C  
ANISOU 2976  CA  CYS A 309    13883  21636  12425  -4390   1852  -3271       C  
ATOM   2977  C   CYS A 309      32.046  41.709 170.701  1.00122.11           C  
ANISOU 2977  C   CYS A 309    12950  21287  12158  -4036   1460  -3055       C  
ATOM   2978  O   CYS A 309      32.749  42.316 171.513  1.00119.34           O  
ANISOU 2978  O   CYS A 309    12397  20906  12038  -3796   1447  -3001       O  
ATOM   2979  CB  CYS A 309      34.123  41.440 169.271  1.00127.99           C  
ANISOU 2979  CB  CYS A 309    14003  21635  12991  -4256   2320  -3372       C  
ATOM   2980  SG  CYS A 309      34.476  43.171 168.885  1.00128.59           S  
ANISOU 2980  SG  CYS A 309    14068  21870  12919  -4267   2103  -3238       S  
ATOM   2981  N   GLN A 310      30.743  41.484 170.880  1.00122.49           N  
ANISOU 2981  N   GLN A 310    12954  21411  12173  -4090   1188  -2900       N  
ATOM   2982  CA  GLN A 310      29.971  42.061 171.995  1.00121.52           C  
ANISOU 2982  CA  GLN A 310    12563  21272  12337  -3827   1073  -2704       C  
ATOM   2983  C   GLN A 310      30.474  41.677 173.396  1.00120.17           C  
ANISOU 2983  C   GLN A 310    12389  20977  12290  -3586   1233  -2825       C  
ATOM   2984  O   GLN A 310      30.412  42.509 174.310  1.00119.55           O  
ANISOU 2984  O   GLN A 310    12378  20778  12266  -3485   1292  -2750       O  
ATOM   2985  CB  GLN A 310      28.475  41.723 171.863  1.00122.89           C  
ANISOU 2985  CB  GLN A 310    12578  21404  12707  -3937    861  -2430       C  
ATOM   2986  CG  GLN A 310      27.568  42.502 172.813  1.00123.00           C  
ANISOU 2986  CG  GLN A 310    12295  21203  13234  -3688   1008  -2172       C  
ATOM   2987  CD  GLN A 310      26.102  42.138 172.679  1.00125.80           C  
ANISOU 2987  CD  GLN A 310    12297  21388  14111  -3769    846  -1764       C  
ATOM   2988  OE1 GLN A 310      25.662  41.629 171.647  1.00128.27           O  
ANISOU 2988  OE1 GLN A 310    12603  21801  14333  -4143    359  -1535       O  
ATOM   2989  NE2 GLN A 310      25.333  42.405 173.730  1.00126.77           N  
ANISOU 2989  NE2 GLN A 310    12196  21153  14815  -3499   1286  -1628       N  
ATOM   2990  N   PRO A 311      30.963  40.427 173.575  1.00120.18           N  
ANISOU 2990  N   PRO A 311    12403  20929  12329  -3586   1309  -2971       N  
ATOM   2991  CA  PRO A 311      31.541  40.076 174.877  1.00119.91           C  
ANISOU 2991  CA  PRO A 311    12392  20734  12431  -3501   1262  -2949       C  
ATOM   2992  C   PRO A 311      32.727  40.939 175.341  1.00120.29           C  
ANISOU 2992  C   PRO A 311    12475  20682  12548  -3542   1103  -2814       C  
ATOM   2993  O   PRO A 311      32.954  41.020 176.544  1.00120.90           O  
ANISOU 2993  O   PRO A 311    12784  20581  12572  -3659    894  -2684       O  
ATOM   2994  CB  PRO A 311      31.967  38.619 174.686  1.00120.57           C  
ANISOU 2994  CB  PRO A 311    12344  20737  12728  -3509   1369  -3039       C  
ATOM   2995  CG  PRO A 311      31.016  38.094 173.673  1.00120.84           C  
ANISOU 2995  CG  PRO A 311    12465  20890  12556  -3613   1496  -3168       C  
ATOM   2996  CD  PRO A 311      30.820  39.234 172.718  1.00121.35           C  
ANISOU 2996  CD  PRO A 311    12623  21082  12401  -3746   1427  -3108       C  
ATOM   2997  N   LEU A 312      33.457  41.575 174.419  1.00120.74           N  
ANISOU 2997  N   LEU A 312    12400  20798  12675  -3543   1167  -2810       N  
ATOM   2998  CA  LEU A 312      34.450  42.605 174.784  1.00121.27           C  
ANISOU 2998  CA  LEU A 312    12477  20778  12819  -3599    966  -2626       C  
ATOM   2999  C   LEU A 312      33.785  43.874 175.330  1.00120.41           C  
ANISOU 2999  C   LEU A 312    12715  20697  12337  -3643    920  -2608       C  
ATOM   3000  O   LEU A 312      34.282  44.470 176.286  1.00122.08           O  
ANISOU 3000  O   LEU A 312    13236  20727  12420  -3829    700  -2456       O  
ATOM   3001  CB  LEU A 312      35.348  42.982 173.597  1.00122.21           C  
ANISOU 3001  CB  LEU A 312    12371  20902  13159  -3573   1174  -2645       C  
ATOM   3002  CG  LEU A 312      36.364  41.944 173.117  1.00125.16           C  
ANISOU 3002  CG  LEU A 312    12404  20989  14160  -3546   1494  -2608       C  
ATOM   3003  CD1 LEU A 312      37.034  42.418 171.833  1.00127.05           C  
ANISOU 3003  CD1 LEU A 312    12622  21131  14518  -3571   1967  -2720       C  
ATOM   3004  CD2 LEU A 312      37.401  41.650 174.195  1.00127.72           C  
ANISOU 3004  CD2 LEU A 312    12379  20999  15149  -3589   1105  -2169       C  
ATOM   3005  N   GLU A 313      32.683  44.294 174.706  1.00119.16           N  
ANISOU 3005  N   GLU A 313    12532  20671  12072  -3550   1131  -2692       N  
ATOM   3006  CA  GLU A 313      31.904  45.446 175.188  1.00119.42           C  
ANISOU 3006  CA  GLU A 313    12774  20572  12026  -3538   1313  -2628       C  
ATOM   3007  C   GLU A 313      31.226  45.157 176.534  1.00120.02           C  
ANISOU 3007  C   GLU A 313    13256  20321  12025  -3608   1557  -2657       C  
ATOM   3008  O   GLU A 313      31.163  46.036 177.399  1.00121.99           O  
ANISOU 3008  O   GLU A 313    14008  20253  12090  -3754   1814  -2652       O  
ATOM   3009  CB  GLU A 313      30.873  45.900 174.140  1.00120.07           C  
ANISOU 3009  CB  GLU A 313    12541  20763  12317  -3460   1394  -2514       C  
ATOM   3010  CG  GLU A 313      31.501  46.565 172.918  1.00120.21           C  
ANISOU 3010  CG  GLU A 313    12426  21001  12244  -3532   1204  -2478       C  
ATOM   3011  CD  GLU A 313      30.487  47.153 171.947  1.00122.01           C  
ANISOU 3011  CD  GLU A 313    12411  21271  12675  -3620   1076  -2206       C  
ATOM   3012  OE1 GLU A 313      29.287  46.817 172.049  1.00123.55           O  
ANISOU 3012  OE1 GLU A 313    12389  21331  13222  -3616   1074  -1984       O  
ATOM   3013  OE2 GLU A 313      30.892  47.941 171.062  1.00122.33           O  
ANISOU 3013  OE2 GLU A 313    12444  21433  12600  -3743    918  -2133       O  
ATOM   3014  N   VAL A 314      30.735  43.926 176.704  1.00118.44           N  
ANISOU 3014  N   VAL A 314    12956  20132  11911  -3566   1558  -2714       N  
ATOM   3015  CA  VAL A 314      30.191  43.460 177.993  1.00118.93           C  
ANISOU 3015  CA  VAL A 314    13487  19852  11849  -3688   1807  -2769       C  
ATOM   3016  C   VAL A 314      31.311  43.349 179.042  1.00119.11           C  
ANISOU 3016  C   VAL A 314    14085  19697  11474  -4065   1445  -2719       C  
ATOM   3017  O   VAL A 314      31.117  43.699 180.209  1.00121.96           O  
ANISOU 3017  O   VAL A 314    15251  19636  11451  -4408   1666  -2742       O  
ATOM   3018  CB  VAL A 314      29.450  42.103 177.844  1.00118.11           C  
ANISOU 3018  CB  VAL A 314    13087  19835  11952  -3559   1819  -2816       C  
ATOM   3019  CG1 VAL A 314      29.021  41.549 179.200  1.00120.39           C  
ANISOU 3019  CG1 VAL A 314    13929  19751  12062  -3729   2073  -2889       C  
ATOM   3020  CG2 VAL A 314      28.231  42.249 176.938  1.00118.40           C  
ANISOU 3020  CG2 VAL A 314    12626  19930  12429  -3361   2004  -2687       C  
ATOM   3021  N   LEU A 315      32.470  42.854 178.604  1.00116.71           N  
ANISOU 3021  N   LEU A 315    13407  19608  11330  -4084    915  -2586       N  
ATOM   3022  CA  LEU A 315      33.686  42.747 179.431  1.00118.24           C  
ANISOU 3022  CA  LEU A 315    13889  19596  11440  -4498    318  -2293       C  
ATOM   3023  C   LEU A 315      34.131  44.081 180.054  1.00119.81           C  
ANISOU 3023  C   LEU A 315    14767  19552  11200  -4896    183  -2168       C  
ATOM   3024  O   LEU A 315      34.658  44.092 181.163  1.00123.41           O  
ANISOU 3024  O   LEU A 315    15930  19665  11292  -5495   -289  -1911       O  
ATOM   3025  CB  LEU A 315      34.815  42.105 178.600  1.00117.76           C  
ANISOU 3025  CB  LEU A 315    13033  19682  12026  -4335     -9  -2083       C  
ATOM   3026  CG  LEU A 315      36.292  42.130 178.977  1.00121.52           C  
ANISOU 3026  CG  LEU A 315    13320  19919  12934  -4654   -679  -1562       C  
ATOM   3027  CD1 LEU A 315      36.543  41.509 180.344  1.00126.21           C  
ANISOU 3027  CD1 LEU A 315    14373  20166  13413  -5205  -1332  -1175       C  
ATOM   3028  CD2 LEU A 315      37.107  41.422 177.901  1.00121.51           C  
ANISOU 3028  CD2 LEU A 315    12393  19928  13846  -4321   -509  -1451       C  
ATOM   3029  N   PHE A 316      33.912  45.192 179.348  1.00117.55           N  
ANISOU 3029  N   PHE A 316    14354  19401  10908  -4661    541  -2306       N  
ATOM   3030  CA  PHE A 316      34.119  46.533 179.924  1.00119.52           C  
ANISOU 3030  CA  PHE A 316    15343  19368  10698  -5019    616  -2267       C  
ATOM   3031  C   PHE A 316      32.986  46.888 180.889  1.00122.01           C  
ANISOU 3031  C   PHE A 316    16587  19204  10568  -5244   1364  -2501       C  
ATOM   3032  O   PHE A 316      31.893  47.271 180.472  1.00120.40           O  
ANISOU 3032  O   PHE A 316    16137  18950  10658  -4856   2129  -2694       O  
ATOM   3033  CB  PHE A 316      34.247  47.609 178.831  1.00116.66           C  
ANISOU 3033  CB  PHE A 316    14498  19268  10560  -4679    804  -2318       C  
ATOM   3034  CG  PHE A 316      35.651  47.801 178.330  1.00116.18           C  
ANISOU 3034  CG  PHE A 316    14020  19380  10743  -4738    184  -2044       C  
ATOM   3035  CD1 PHE A 316      36.543  48.614 179.025  1.00119.64           C  
ANISOU 3035  CD1 PHE A 316    15013  19564  10880  -5240   -271  -1769       C  
ATOM   3036  CD2 PHE A 316      36.084  47.178 177.163  1.00113.53           C  
ANISOU 3036  CD2 PHE A 316    12812  19354  10970  -4363    128  -2032       C  
ATOM   3037  CE1 PHE A 316      37.841  48.799 178.568  1.00120.39           C  
ANISOU 3037  CE1 PHE A 316    14588  19737  11416  -5282   -840  -1410       C  
ATOM   3038  CE2 PHE A 316      37.380  47.358 176.699  1.00114.76           C  
ANISOU 3038  CE2 PHE A 316    12537  19513  11553  -4391   -223  -1757       C  
ATOM   3039  CZ  PHE A 316      38.261  48.170 177.403  1.00118.00           C  
ANISOU 3039  CZ  PHE A 316    13293  19693  11846  -4808   -742  -1406       C  
TER    3040      PHE A 316                                                      
ATOM   3041  N   SER B   6      61.723  24.440 111.833  1.00122.86           N  
ANISOU 3041  N   SER B   6    17156  15588  13936   -884   2062   -463       N  
ATOM   3042  CA  SER B   6      60.785  25.485 111.340  1.00122.70           C  
ANISOU 3042  CA  SER B   6    17179  15750  13691   -989   1923   -243       C  
ATOM   3043  C   SER B   6      59.357  24.929 111.271  1.00122.22           C  
ANISOU 3043  C   SER B   6    17150  15712  13574  -1031   1866   -243       C  
ATOM   3044  O   SER B   6      58.535  25.245 112.139  1.00122.40           O  
ANISOU 3044  O   SER B   6    17219  15604  13681   -908   1742    -70       O  
ATOM   3045  CB  SER B   6      61.270  26.032 109.990  1.00124.64           C  
ANISOU 3045  CB  SER B   6    17384  16287  13684  -1205   1971   -261       C  
ATOM   3046  OG  SER B   6      60.303  26.865 109.382  1.00125.56           O  
ANISOU 3046  OG  SER B   6    17518  16602  13585  -1327   1845    -45       O  
ATOM   3047  N   ALA B   7      59.085  24.082 110.274  1.00122.73           N  
ANISOU 3047  N   ALA B   7    17187  15942  13502  -1211   1967   -452       N  
ATOM   3048  CA  ALA B   7      57.756  23.481 110.070  1.00122.21           C  
ANISOU 3048  CA  ALA B   7    17143  15937  13353  -1290   1928   -480       C  
ATOM   3049  C   ALA B   7      57.234  22.735 111.302  1.00119.96           C  
ANISOU 3049  C   ALA B   7    16898  15362  13318  -1096   1903   -500       C  
ATOM   3050  O   ALA B   7      56.031  22.743 111.584  1.00119.35           O  
ANISOU 3050  O   ALA B   7    16854  15283  13210  -1084   1796   -386       O  
ATOM   3051  CB  ALA B   7      57.778  22.548 108.866  1.00124.63           C  
ANISOU 3051  CB  ALA B   7    17408  16448  13496  -1529   2085   -768       C  
ATOM   3052  N   PHE B   8      58.151  22.102 112.028  1.00118.32           N  
ANISOU 3052  N   PHE B   8    16674  14921  13359   -948   2001   -630       N  
ATOM   3053  CA  PHE B   8      57.850  21.467 113.322  1.00115.70           C  
ANISOU 3053  CA  PHE B   8    16367  14307  13285   -751   1970   -613       C  
ATOM   3054  C   PHE B   8      57.419  22.509 114.359  1.00111.31           C  
ANISOU 3054  C   PHE B   8    15858  13661  12773   -605   1792   -324       C  
ATOM   3055  O   PHE B   8      56.432  22.299 115.075  1.00109.60           O  
ANISOU 3055  O   PHE B   8    15680  13341  12621   -530   1707   -245       O  
ATOM   3056  CB  PHE B   8      59.064  20.683 113.822  1.00116.32           C  
ANISOU 3056  CB  PHE B   8    16391  14182  13620   -631   2108   -769       C  
ATOM   3057  CG  PHE B   8      59.630  19.757 112.775  1.00118.64           C  
ANISOU 3057  CG  PHE B   8    16628  14550  13899   -773   2316  -1070       C  
ATOM   3058  CD1 PHE B   8      58.810  18.812 112.170  1.00119.61           C  
ANISOU 3058  CD1 PHE B   8    16763  14721  13962   -910   2399  -1262       C  
ATOM   3059  CD2 PHE B   8      60.947  19.883 112.330  1.00119.82           C  
ANISOU 3059  CD2 PHE B   8    16710  14740  14074   -794   2436  -1171       C  
ATOM   3060  CE1 PHE B   8      59.306  17.969 111.176  1.00122.07           C  
ANISOU 3060  CE1 PHE B   8    17021  15103  14255  -1066   2614  -1571       C  
ATOM   3061  CE2 PHE B   8      61.443  19.051 111.340  1.00122.03           C  
ANISOU 3061  CE2 PHE B   8    16932  15090  14341   -937   2647  -1469       C  
ATOM   3062  CZ  PHE B   8      60.625  18.090 110.763  1.00123.44           C  
ANISOU 3062  CZ  PHE B   8    17125  15304  14471  -1078   2743  -1678       C  
ATOM   3063  N   GLN B   9      58.144  23.634 114.415  1.00108.63           N  
ANISOU 3063  N   GLN B   9    15512  13363  12396   -578   1747   -179       N  
ATOM   3064  CA  GLN B   9      57.794  24.723 115.343  1.00105.66           C  
ANISOU 3064  CA  GLN B   9    15178  12901  12063   -463   1605     73       C  
ATOM   3065  C   GLN B   9      56.428  25.324 114.987  1.00104.75           C  
ANISOU 3065  C   GLN B   9    15096  12907  11795   -533   1489    239       C  
ATOM   3066  O   GLN B   9      55.584  25.570 115.865  1.00103.81           O  
ANISOU 3066  O   GLN B   9    15013  12670  11758   -431   1393    372       O  
ATOM   3067  CB  GLN B   9      58.873  25.809 115.326  1.00105.20           C  
ANISOU 3067  CB  GLN B   9    15105  12877  11987   -453   1603    173       C  
ATOM   3068  CG  GLN B   9      58.854  26.710 116.547  1.00103.75           C  
ANISOU 3068  CG  GLN B   9    14957  12541  11921   -316   1506    364       C  
ATOM   3069  CD  GLN B   9      59.862  27.846 116.478  1.00103.62           C  
ANISOU 3069  CD  GLN B   9    14931  12565  11874   -331   1509    460       C  
ATOM   3070  OE1 GLN B   9      60.726  27.883 115.601  1.00105.00           O  
ANISOU 3070  OE1 GLN B   9    15065  12870  11959   -425   1586    379       O  
ATOM   3071  NE2 GLN B   9      59.753  28.781 117.410  1.00102.31           N  
ANISOU 3071  NE2 GLN B   9    14799  12288  11783   -250   1436    622       N  
ATOM   3072  N   ALA B  10      56.222  25.539 113.688  1.00105.52           N  
ANISOU 3072  N   ALA B  10    15169  13254  11669   -715   1502    233       N  
ATOM   3073  CA  ALA B  10      54.925  25.955 113.158  1.00105.87           C  
ANISOU 3073  CA  ALA B  10    15215  13459  11551   -810   1399    390       C  
ATOM   3074  C   ALA B  10      53.819  24.956 113.500  1.00105.11           C  
ANISOU 3074  C   ALA B  10    15136  13302  11496   -794   1382    308       C  
ATOM   3075  O   ALA B  10      52.715  25.364 113.838  1.00104.00           O  
ANISOU 3075  O   ALA B  10    15008  13155  11349   -756   1270    484       O  
ATOM   3076  CB  ALA B  10      55.007  26.156 111.651  1.00107.94           C  
ANISOU 3076  CB  ALA B  10    15428  14036  11547  -1042   1429    373       C  
ATOM   3077  N   ALA B  11      54.118  23.660 113.412  1.00105.16           N  
ANISOU 3077  N   ALA B  11    15138  13257  11560   -823   1503     43       N  
ATOM   3078  CA  ALA B  11      53.166  22.607 113.800  1.00104.20           C  
ANISOU 3078  CA  ALA B  11    15036  13047  11505   -807   1505    -56       C  
ATOM   3079  C   ALA B  11      52.843  22.637 115.297  1.00101.99           C  
ANISOU 3079  C   ALA B  11    14797  12504  11450   -593   1427     54       C  
ATOM   3080  O   ALA B  11      51.671  22.552 115.681  1.00101.73           O  
ANISOU 3080  O   ALA B  11    14785  12452  11415   -570   1342    140       O  
ATOM   3081  CB  ALA B  11      53.686  21.236 113.398  1.00105.06           C  
ANISOU 3081  CB  ALA B  11    15127  13122  11668   -881   1677   -372       C  
ATOM   3082  N   TYR B  12      53.878  22.754 116.131  1.00100.40           N  
ANISOU 3082  N   TYR B  12    14598  12121  11429   -450   1457     53       N  
ATOM   3083  CA  TYR B  12      53.697  22.935 117.581  1.00 97.74           C  
ANISOU 3083  CA  TYR B  12    14290  11566  11278   -270   1381    173       C  
ATOM   3084  C   TYR B  12      52.801  24.150 117.868  1.00 96.12           C  
ANISOU 3084  C   TYR B  12    14111  11400  11007   -244   1247    416       C  
ATOM   3085  O   TYR B  12      51.756  24.026 118.541  1.00 94.65           O  
ANISOU 3085  O   TYR B  12    13948  11140  10871   -188   1176    487       O  
ATOM   3086  CB  TYR B  12      55.054  23.091 118.290  1.00 97.13           C  
ANISOU 3086  CB  TYR B  12    14194  11354  11356   -159   1425    164       C  
ATOM   3087  CG  TYR B  12      54.950  23.633 119.703  1.00 95.93           C  
ANISOU 3087  CG  TYR B  12    14066  11043  11337    -16   1336    320       C  
ATOM   3088  CD1 TYR B  12      54.467  22.839 120.746  1.00 95.39           C  
ANISOU 3088  CD1 TYR B  12    14008  10818  11416     75   1311    307       C  
ATOM   3089  CD2 TYR B  12      55.320  24.946 119.996  1.00 95.64           C  
ANISOU 3089  CD2 TYR B  12    14042  11020  11276      9   1284    474       C  
ATOM   3090  CE1 TYR B  12      54.364  23.337 122.037  1.00 94.06           C  
ANISOU 3090  CE1 TYR B  12    13857  10534  11344    177   1235    438       C  
ATOM   3091  CE2 TYR B  12      55.222  25.454 121.284  1.00 94.58           C  
ANISOU 3091  CE2 TYR B  12    13929  10754  11251    111   1221    588       C  
ATOM   3092  CZ  TYR B  12      54.742  24.645 122.299  1.00 93.92           C  
ANISOU 3092  CZ  TYR B  12    13852  10541  11291    188   1196    567       C  
ATOM   3093  OH  TYR B  12      54.637  25.145 123.571  1.00 93.55           O  
ANISOU 3093  OH  TYR B  12    13822  10393  11330    262   1139    669       O  
ATOM   3094  N   ILE B  13      53.206  25.302 117.326  1.00 95.73           N  
ANISOU 3094  N   ILE B  13    14051  11463  10858   -289   1225    540       N  
ATOM   3095  CA  ILE B  13      52.457  26.560 117.493  1.00 94.67           C  
ANISOU 3095  CA  ILE B  13    13927  11352  10692   -265   1121    782       C  
ATOM   3096  C   ILE B  13      51.003  26.417 117.011  1.00 95.04           C  
ANISOU 3096  C   ILE B  13    13960  11520  10630   -336   1051    860       C  
ATOM   3097  O   ILE B  13      50.075  26.853 117.692  1.00 95.15           O  
ANISOU 3097  O   ILE B  13    13984  11452  10715   -256    975   1002       O  
ATOM   3098  CB  ILE B  13      53.163  27.742 116.778  1.00 94.97           C  
ANISOU 3098  CB  ILE B  13    13944  11503  10636   -328   1124    902       C  
ATOM   3099  CG1 ILE B  13      54.475  28.087 117.499  1.00 94.24           C  
ANISOU 3099  CG1 ILE B  13    13865  11273  10669   -242   1174    866       C  
ATOM   3100  CG2 ILE B  13      52.275  28.984 116.734  1.00 95.17           C  
ANISOU 3100  CG2 ILE B  13    13961  11558  10640   -319   1031   1165       C  
ATOM   3101  CD1 ILE B  13      55.490  28.808 116.642  1.00 95.26           C  
ANISOU 3101  CD1 ILE B  13    13969  11528  10696   -330   1216    891       C  
ATOM   3102  N   GLY B  14      50.821  25.789 115.852  1.00 95.31           N  
ANISOU 3102  N   GLY B  14    13963  11758  10492   -495   1085    757       N  
ATOM   3103  CA  GLY B  14      49.498  25.545 115.272  1.00 95.10           C  
ANISOU 3103  CA  GLY B  14    13909  11894  10329   -598   1023    815       C  
ATOM   3104  C   GLY B  14      48.623  24.629 116.105  1.00 93.18           C  
ANISOU 3104  C   GLY B  14    13695  11515  10193   -526   1006    738       C  
ATOM   3105  O   GLY B  14      47.449  24.927 116.328  1.00 92.95           O  
ANISOU 3105  O   GLY B  14    13652  11509  10154   -506    915    889       O  
ATOM   3106  N   ILE B  15      49.195  23.517 116.565  1.00 91.80           N  
ANISOU 3106  N   ILE B  15    13550  11196  10134   -486   1096    515       N  
ATOM   3107  CA  ILE B  15      48.478  22.572 117.430  1.00 90.50           C  
ANISOU 3107  CA  ILE B  15    13413  10879  10092   -415   1088    439       C  
ATOM   3108  C   ILE B  15      48.110  23.243 118.763  1.00 88.23           C  
ANISOU 3108  C   ILE B  15    13152  10410   9960   -243   1003    610       C  
ATOM   3109  O   ILE B  15      46.961  23.123 119.226  1.00 86.76           O  
ANISOU 3109  O   ILE B  15    12971  10201   9793   -216    936    679       O  
ATOM   3110  CB  ILE B  15      49.289  21.268 117.647  1.00 90.51           C  
ANISOU 3110  CB  ILE B  15    13427  10741  10221   -399   1214    188       C  
ATOM   3111  CG1 ILE B  15      49.362  20.470 116.340  1.00 92.42           C  
ANISOU 3111  CG1 ILE B  15    13644  11161  10311   -595   1319    -18       C  
ATOM   3112  CG2 ILE B  15      48.671  20.397 118.740  1.00 89.52           C  
ANISOU 3112  CG2 ILE B  15    13330  10423  10260   -301   1198    151       C  
ATOM   3113  CD1 ILE B  15      50.515  19.487 116.275  1.00 93.16           C  
ANISOU 3113  CD1 ILE B  15    13727  11130  10536   -588   1479   -260       C  
ATOM   3114  N   GLU B  16      49.073  23.959 119.354  1.00 87.55           N  
ANISOU 3114  N   GLU B  16    13078  10212   9975   -145   1013    667       N  
ATOM   3115  CA  GLU B  16      48.813  24.739 120.577  1.00 86.82           C  
ANISOU 3115  CA  GLU B  16    13006   9967  10012    -12    950    813       C  
ATOM   3116  C   GLU B  16      47.683  25.756 120.379  1.00 86.01           C  
ANISOU 3116  C   GLU B  16    12885   9943   9851    -21    866   1018       C  
ATOM   3117  O   GLU B  16      46.715  25.797 121.160  1.00 85.94           O  
ANISOU 3117  O   GLU B  16    12882   9854   9916     42    815   1086       O  
ATOM   3118  CB  GLU B  16      50.086  25.462 121.043  1.00 87.69           C  
ANISOU 3118  CB  GLU B  16    13123   9990  10202     51    984    837       C  
ATOM   3119  CG  GLU B  16      51.124  24.558 121.695  1.00 88.55           C  
ANISOU 3119  CG  GLU B  16    13234   9975  10434    107   1048    691       C  
ATOM   3120  CD  GLU B  16      50.875  24.314 123.177  1.00 88.45           C  
ANISOU 3120  CD  GLU B  16    13240   9795  10571    213   1012    719       C  
ATOM   3121  OE1 GLU B  16      49.701  24.133 123.576  1.00 89.61           O  
ANISOU 3121  OE1 GLU B  16    13402   9918  10726    227    959    761       O  
ATOM   3122  OE2 GLU B  16      51.862  24.293 123.950  1.00 88.46           O  
ANISOU 3122  OE2 GLU B  16    13230   9705  10673    271   1036    703       O  
ATOM   3123  N   VAL B  17      47.816  26.557 119.322  1.00 85.58           N  
ANISOU 3123  N   VAL B  17    12795  10049   9672   -104    855   1123       N  
ATOM   3124  CA  VAL B  17      46.797  27.539 118.930  1.00 85.06           C  
ANISOU 3124  CA  VAL B  17    12684  10077   9556   -121    779   1352       C  
ATOM   3125  C   VAL B  17      45.428  26.882 118.710  1.00 85.34           C  
ANISOU 3125  C   VAL B  17    12689  10212   9522   -172    722   1367       C  
ATOM   3126  O   VAL B  17      44.417  27.435 119.127  1.00 84.88           O  
ANISOU 3126  O   VAL B  17    12602  10118   9528   -111    661   1528       O  
ATOM   3127  CB  VAL B  17      47.235  28.344 117.675  1.00 85.76           C  
ANISOU 3127  CB  VAL B  17    12726  10357   9502   -230    775   1470       C  
ATOM   3128  CG1 VAL B  17      46.071  29.099 117.037  1.00 86.69           C  
ANISOU 3128  CG1 VAL B  17    12767  10623   9547   -277    688   1723       C  
ATOM   3129  CG2 VAL B  17      48.350  29.321 118.039  1.00 85.26           C  
ANISOU 3129  CG2 VAL B  17    12686  10174   9534   -164    816   1519       C  
ATOM   3130  N   LEU B  18      45.404  25.712 118.072  1.00 86.15           N  
ANISOU 3130  N   LEU B  18    12792  10434   9504   -287    754   1191       N  
ATOM   3131  CA  LEU B  18      44.149  24.982 117.823  1.00 86.53           C  
ANISOU 3131  CA  LEU B  18    12814  10593   9468   -362    710   1177       C  
ATOM   3132  C   LEU B  18      43.531  24.484 119.133  1.00 84.36           C  
ANISOU 3132  C   LEU B  18    12579  10114   9359   -237    694   1137       C  
ATOM   3133  O   LEU B  18      42.330  24.689 119.386  1.00 84.01           O  
ANISOU 3133  O   LEU B  18    12500  10094   9323   -215    623   1264       O  
ATOM   3134  CB  LEU B  18      44.389  23.813 116.854  1.00 88.34           C  
ANISOU 3134  CB  LEU B  18    13042  10982   9539   -534    777    955       C  
ATOM   3135  CG  LEU B  18      43.167  23.194 116.151  1.00 89.90           C  
ANISOU 3135  CG  LEU B  18    13194  11394   9569   -689    736    946       C  
ATOM   3136  CD1 LEU B  18      43.567  22.611 114.801  1.00 91.82           C  
ANISOU 3136  CD1 LEU B  18    13411  11883   9593   -914    807    785       C  
ATOM   3137  CD2 LEU B  18      42.467  22.146 117.014  1.00 89.24           C  
ANISOU 3137  CD2 LEU B  18    13150  11162   9592   -637    744    821       C  
ATOM   3138  N   ILE B  19      44.358  23.851 119.967  1.00 82.84           N  
ANISOU 3138  N   ILE B  19    12445   9730   9298   -157    758    977       N  
ATOM   3139  CA  ILE B  19      43.918  23.395 121.300  1.00 81.44           C  
ANISOU 3139  CA  ILE B  19    12303   9361   9278    -45    743    949       C  
ATOM   3140  C   ILE B  19      43.363  24.559 122.121  1.00 80.60           C  
ANISOU 3140  C   ILE B  19    12185   9170   9267     61    685   1140       C  
ATOM   3141  O   ILE B  19      42.289  24.438 122.720  1.00 79.70           O  
ANISOU 3141  O   ILE B  19    12062   9020   9198     96    640   1190       O  
ATOM   3142  CB  ILE B  19      45.056  22.692 122.079  1.00 80.40           C  
ANISOU 3142  CB  ILE B  19    12215   9050   9281     23    813    796       C  
ATOM   3143  CG1 ILE B  19      45.399  21.350 121.414  1.00 81.32           C  
ANISOU 3143  CG1 ILE B  19    12335   9201   9359    -70    892    587       C  
ATOM   3144  CG2 ILE B  19      44.669  22.455 123.540  1.00 79.07           C  
ANISOU 3144  CG2 ILE B  19    12072   8704   9264    131    784    815       C  
ATOM   3145  CD1 ILE B  19      46.803  20.873 121.698  1.00 81.34           C  
ANISOU 3145  CD1 ILE B  19    12348   9076   9478    -20    979    463       C  
ATOM   3146  N   ALA B  20      44.091  25.677 122.139  1.00 81.00           N  
ANISOU 3146  N   ALA B  20    12234   9186   9356    105    698   1236       N  
ATOM   3147  CA  ALA B  20      43.602  26.896 122.796  1.00 81.00           C  
ANISOU 3147  CA  ALA B  20    12216   9097   9462    193    671   1409       C  
ATOM   3148  C   ALA B  20      42.293  27.410 122.178  1.00 82.61           C  
ANISOU 3148  C   ALA B  20    12347   9426   9613    165    607   1591       C  
ATOM   3149  O   ALA B  20      41.380  27.802 122.901  1.00 82.31           O  
ANISOU 3149  O   ALA B  20    12287   9306   9679    237    584   1680       O  
ATOM   3150  CB  ALA B  20      44.667  27.983 122.762  1.00 80.89           C  
ANISOU 3150  CB  ALA B  20    12210   9030   9491    221    712   1469       C  
ATOM   3151  N   LEU B  21      42.210  27.396 120.848  1.00 85.26           N  
ANISOU 3151  N   LEU B  21    12634   9974   9785     51    580   1648       N  
ATOM   3152  CA  LEU B  21      40.996  27.817 120.120  1.00 87.67           C  
ANISOU 3152  CA  LEU B  21    12846  10449  10015      1    506   1849       C  
ATOM   3153  C   LEU B  21      39.785  26.913 120.357  1.00 88.54           C  
ANISOU 3153  C   LEU B  21    12937  10609  10093    -23    462   1805       C  
ATOM   3154  O   LEU B  21      38.654  27.383 120.247  1.00 89.04           O  
ANISOU 3154  O   LEU B  21    12918  10743  10170    -11    401   1989       O  
ATOM   3155  CB  LEU B  21      41.252  27.937 118.605  1.00 89.50           C  
ANISOU 3155  CB  LEU B  21    13021  10943  10042   -151    483   1919       C  
ATOM   3156  CG  LEU B  21      41.922  29.230 118.111  1.00 90.42           C  
ANISOU 3156  CG  LEU B  21    13104  11073  10178   -140    489   2101       C  
ATOM   3157  CD1 LEU B  21      42.324  29.087 116.649  1.00 91.93           C  
ANISOU 3157  CD1 LEU B  21    13251  11546  10133   -321    475   2116       C  
ATOM   3158  CD2 LEU B  21      41.021  30.447 118.306  1.00 90.94           C  
ANISOU 3158  CD2 LEU B  21    13084  11086  10381    -50    442   2392       C  
ATOM   3159  N   VAL B  22      40.008  25.629 120.645  1.00 88.98           N  
ANISOU 3159  N   VAL B  22    13058  10631  10118    -60    495   1574       N  
ATOM   3160  CA  VAL B  22      38.904  24.746 121.072  1.00 89.16           C  
ANISOU 3160  CA  VAL B  22    13076  10660  10138    -74    463   1518       C  
ATOM   3161  C   VAL B  22      38.604  24.907 122.577  1.00 88.75           C  
ANISOU 3161  C   VAL B  22    13060  10378  10283     72    470   1518       C  
ATOM   3162  O   VAL B  22      37.438  24.871 122.986  1.00 88.50           O  
ANISOU 3162  O   VAL B  22    12988  10352  10285     95    427   1589       O  
ATOM   3163  CB  VAL B  22      39.174  23.262 120.721  1.00 88.90           C  
ANISOU 3163  CB  VAL B  22    13092  10679  10007   -188    507   1275       C  
ATOM   3164  CG1 VAL B  22      38.015  22.377 121.170  1.00 88.52           C  
ANISOU 3164  CG1 VAL B  22    13040  10631   9961   -211    477   1223       C  
ATOM   3165  CG2 VAL B  22      39.385  23.093 119.221  1.00 90.40           C  
ANISOU 3165  CG2 VAL B  22    13240  11123   9982   -365    515   1250       C  
ATOM   3166  N   SER B  23      39.648  25.094 123.386  1.00 89.00           N  
ANISOU 3166  N   SER B  23    13155  10227  10431    155    525   1441       N  
ATOM   3167  CA  SER B  23      39.512  25.186 124.848  1.00 88.50           C  
ANISOU 3167  CA  SER B  23    13126   9969  10527    261    541   1417       C  
ATOM   3168  C   SER B  23      38.719  26.407 125.353  1.00 89.00           C  
ANISOU 3168  C   SER B  23    13137   9973  10703    343    529   1589       C  
ATOM   3169  O   SER B  23      37.748  26.249 126.102  1.00 89.39           O  
ANISOU 3169  O   SER B  23    13170   9976  10816    378    513   1602       O  
ATOM   3170  CB  SER B  23      40.898  25.177 125.503  1.00 87.90           C  
ANISOU 3170  CB  SER B  23    13114   9754  10527    306    599   1312       C  
ATOM   3171  OG  SER B  23      40.809  25.260 126.917  1.00 87.36           O  
ANISOU 3171  OG  SER B  23    13073   9534  10586    379    613   1290       O  
ATOM   3172  N   VAL B  24      39.137  27.608 124.946  1.00 89.36           N  
ANISOU 3172  N   VAL B  24    13154  10011  10786    370    549   1718       N  
ATOM   3173  CA  VAL B  24      38.596  28.860 125.506  1.00 89.79           C  
ANISOU 3173  CA  VAL B  24    13161   9953  11000    458    575   1864       C  
ATOM   3174  C   VAL B  24      37.086  29.032 125.261  1.00 90.88           C  
ANISOU 3174  C   VAL B  24    13200  10171  11157    470    524   2019       C  
ATOM   3175  O   VAL B  24      36.346  29.289 126.217  1.00 91.35           O  
ANISOU 3175  O   VAL B  24    13241  10117  11351    539    549   2028       O  
ATOM   3176  CB  VAL B  24      39.395  30.109 125.027  1.00 90.27           C  
ANISOU 3176  CB  VAL B  24    13206   9977  11112    478    616   1980       C  
ATOM   3177  CG1 VAL B  24      38.706  31.412 125.430  1.00 90.54           C  
ANISOU 3177  CG1 VAL B  24    13173   9888  11338    564    658   2147       C  
ATOM   3178  CG2 VAL B  24      40.819  30.075 125.582  1.00 89.41           C  
ANISOU 3178  CG2 VAL B  24    13188   9762  11021    480    677   1828       C  
ATOM   3179  N   PRO B  25      36.619  28.882 124.002  1.00 91.58           N  
ANISOU 3179  N   PRO B  25    13217  10471  11107    393    455   2139       N  
ATOM   3180  CA  PRO B  25      35.178  29.041 123.758  1.00 91.90           C  
ANISOU 3180  CA  PRO B  25    13142  10611  11161    399    397   2308       C  
ATOM   3181  C   PRO B  25      34.302  28.014 124.482  1.00 90.31           C  
ANISOU 3181  C   PRO B  25    12959  10407  10947    391    375   2187       C  
ATOM   3182  O   PRO B  25      33.259  28.387 125.017  1.00 91.36           O  
ANISOU 3182  O   PRO B  25    13021  10492  11197    457    374   2282       O  
ATOM   3183  CB  PRO B  25      35.050  28.878 122.234  1.00 93.53           C  
ANISOU 3183  CB  PRO B  25    13278  11092  11168    274    321   2430       C  
ATOM   3184  CG  PRO B  25      36.412  29.136 121.704  1.00 93.60           C  
ANISOU 3184  CG  PRO B  25    13346  11100  11115    236    357   2380       C  
ATOM   3185  CD  PRO B  25      37.331  28.580 122.750  1.00 92.10           C  
ANISOU 3185  CD  PRO B  25    13287  10715  10989    282    428   2130       C  
ATOM   3186  N   GLY B  26      34.730  26.751 124.501  1.00 87.81           N  
ANISOU 3186  N   GLY B  26    12729  10130  10505    312    369   1981       N  
ATOM   3187  CA  GLY B  26      33.986  25.675 125.168  1.00 86.07           C  
ANISOU 3187  CA  GLY B  26    12533   9900  10268    290    351   1859       C  
ATOM   3188  C   GLY B  26      33.713  25.945 126.639  1.00 83.64           C  
ANISOU 3188  C   GLY B  26    12250   9393  10136    394    396   1819       C  
ATOM   3189  O   GLY B  26      32.572  25.845 127.102  1.00 83.29           O  
ANISOU 3189  O   GLY B  26    12153   9358  10136    413    375   1861       O  
ATOM   3190  N   ASN B  27      34.766  26.311 127.362  1.00 81.89           N  
ANISOU 3190  N   ASN B  27    12101   9008  10003    448    460   1738       N  
ATOM   3191  CA  ASN B  27      34.663  26.585 128.799  1.00 80.94           C  
ANISOU 3191  CA  ASN B  27    12008   8718  10026    515    515   1678       C  
ATOM   3192  C   ASN B  27      33.948  27.906 129.103  1.00 81.80           C  
ANISOU 3192  C   ASN B  27    12033   8752  10296    596    560   1822       C  
ATOM   3193  O   ASN B  27      33.187  27.988 130.075  1.00 81.76           O  
ANISOU 3193  O   ASN B  27    12006   8672  10387    630    592   1796       O  
ATOM   3194  CB  ASN B  27      36.042  26.536 129.457  1.00 79.51           C  
ANISOU 3194  CB  ASN B  27    11918   8420   9871    521    567   1550       C  
ATOM   3195  CG  ASN B  27      36.609  25.134 129.503  1.00 78.26           C  
ANISOU 3195  CG  ASN B  27    11828   8288   9618    462    539   1405       C  
ATOM   3196  OD1 ASN B  27      36.091  24.268 130.213  1.00 77.97           O  
ANISOU 3196  OD1 ASN B  27    11807   8235   9582    443    520   1335       O  
ATOM   3197  ND2 ASN B  27      37.679  24.902 128.751  1.00 77.70           N  
ANISOU 3197  ND2 ASN B  27    11790   8251   9479    431    545   1363       N  
ATOM   3198  N   VAL B  28      34.170  28.924 128.269  1.00 82.91           N  
ANISOU 3198  N   VAL B  28    12119   8907  10475    625    572   1974       N  
ATOM   3199  CA  VAL B  28      33.357  30.152 128.330  1.00 84.56           C  
ANISOU 3199  CA  VAL B  28    12220   9045  10862    707    616   2150       C  
ATOM   3200  C   VAL B  28      31.874  29.802 128.148  1.00 85.59           C  
ANISOU 3200  C   VAL B  28    12245   9288  10984    709    556   2253       C  
ATOM   3201  O   VAL B  28      31.023  30.316 128.874  1.00 86.71           O  
ANISOU 3201  O   VAL B  28    12321   9333  11291    777    610   2292       O  
ATOM   3202  CB  VAL B  28      33.807  31.216 127.288  1.00 85.21           C  
ANISOU 3202  CB  VAL B  28    12245   9146  10983    728    623   2339       C  
ATOM   3203  CG1 VAL B  28      32.793  32.353 127.162  1.00 86.35           C  
ANISOU 3203  CG1 VAL B  28    12246   9234  11329    816    656   2568       C  
ATOM   3204  CG2 VAL B  28      35.174  31.784 127.660  1.00 84.60           C  
ANISOU 3204  CG2 VAL B  28    12260   8925  10958    737    705   2242       C  
ATOM   3205  N   LEU B  29      31.584  28.914 127.197  1.00 85.76           N  
ANISOU 3205  N   LEU B  29    12248   9520  10813    622    454   2281       N  
ATOM   3206  CA  LEU B  29      30.220  28.434 126.956  1.00 86.80           C  
ANISOU 3206  CA  LEU B  29    12282   9798  10897    594    385   2366       C  
ATOM   3207  C   LEU B  29      29.679  27.620 128.143  1.00 85.87           C  
ANISOU 3207  C   LEU B  29    12214   9610  10800    593    403   2196       C  
ATOM   3208  O   LEU B  29      28.491  27.729 128.474  1.00 86.45           O  
ANISOU 3208  O   LEU B  29    12194   9703  10949    625    397   2272       O  
ATOM   3209  CB  LEU B  29      30.159  27.607 125.665  1.00 87.88           C  
ANISOU 3209  CB  LEU B  29    12401  10193  10794    464    284   2397       C  
ATOM   3210  CG  LEU B  29      28.788  27.462 125.001  1.00 89.80           C  
ANISOU 3210  CG  LEU B  29    12499  10651  10970    416    199   2573       C  
ATOM   3211  CD1 LEU B  29      28.381  28.753 124.298  1.00 91.57           C  
ANISOU 3211  CD1 LEU B  29    12565  10927  11300    478    182   2881       C  
ATOM   3212  CD2 LEU B  29      28.801  26.299 124.019  1.00 90.28           C  
ANISOU 3212  CD2 LEU B  29    12583  10957  10761    243    121   2494       C  
ATOM   3213  N   VAL B  30      30.540  26.813 128.772  1.00 84.54           N  
ANISOU 3213  N   VAL B  30    12180   9368  10571    554    423   1984       N  
ATOM   3214  CA  VAL B  30      30.177  26.110 130.017  1.00 83.50           C  
ANISOU 3214  CA  VAL B  30    12099   9156  10469    548    444   1835       C  
ATOM   3215  C   VAL B  30      29.834  27.098 131.137  1.00 83.68           C  
ANISOU 3215  C   VAL B  30    12086   9017  10689    635    538   1845       C  
ATOM   3216  O   VAL B  30      28.813  26.932 131.812  1.00 83.63           O  
ANISOU 3216  O   VAL B  30    12031   9007  10734    643    548   1834       O  
ATOM   3217  CB  VAL B  30      31.289  25.135 130.492  1.00 82.63           C  
ANISOU 3217  CB  VAL B  30    12123   8990  10281    496    449   1643       C  
ATOM   3218  CG1 VAL B  30      31.050  24.644 131.922  1.00 82.31           C  
ANISOU 3218  CG1 VAL B  30    12125   8853  10293    492    478   1523       C  
ATOM   3219  CG2 VAL B  30      31.378  23.939 129.557  1.00 83.16           C  
ANISOU 3219  CG2 VAL B  30    12220   9198  10178    398    381   1590       C  
ATOM   3220  N   ILE B  31      30.684  28.111 131.328  1.00 83.61           N  
ANISOU 3220  N   ILE B  31    12100   8878  10790    686    618   1852       N  
ATOM   3221  CA  ILE B  31      30.452  29.131 132.370  1.00 84.16           C  
ANISOU 3221  CA  ILE B  31    12137   8779  11058    750    738   1833       C  
ATOM   3222  C   ILE B  31      29.180  29.935 132.069  1.00 86.54           C  
ANISOU 3222  C   ILE B  31    12287   9081  11513    826    763   2012       C  
ATOM   3223  O   ILE B  31      28.404  30.233 132.981  1.00 87.26           O  
ANISOU 3223  O   ILE B  31    12327   9089  11737    858    841   1972       O  
ATOM   3224  CB  ILE B  31      31.664  30.080 132.540  1.00 83.73           C  
ANISOU 3224  CB  ILE B  31    12137   8587  11088    772    828   1800       C  
ATOM   3225  CG1 ILE B  31      32.887  29.306 133.054  1.00 82.45           C  
ANISOU 3225  CG1 ILE B  31    12105   8422  10798    700    812   1626       C  
ATOM   3226  CG2 ILE B  31      31.349  31.214 133.518  1.00 84.45           C  
ANISOU 3226  CG2 ILE B  31    12185   8502  11399    822    976   1770       C  
ATOM   3227  CD1 ILE B  31      34.209  29.987 132.760  1.00 82.49           C  
ANISOU 3227  CD1 ILE B  31    12162   8362  10817    703    856   1620       C  
ATOM   3228  N   TRP B  32      28.987  30.278 130.794  1.00 88.41           N  
ANISOU 3228  N   TRP B  32    12440   9420  11732    849    700   2214       N  
ATOM   3229  CA  TRP B  32      27.750  30.908 130.297  1.00 91.00           C  
ANISOU 3229  CA  TRP B  32    12594   9793  12187    917    692   2440       C  
ATOM   3230  C   TRP B  32      26.533  30.046 130.646  1.00 91.54           C  
ANISOU 3230  C   TRP B  32    12611   9973  12196    886    638   2412       C  
ATOM   3231  O   TRP B  32      25.588  30.524 131.283  1.00 93.10           O  
ANISOU 3231  O   TRP B  32    12710  10093  12570    952    710   2447       O  
ATOM   3232  CB  TRP B  32      27.837  31.091 128.770  1.00 92.56           C  
ANISOU 3232  CB  TRP B  32    12718  10159  12290    899    592   2665       C  
ATOM   3233  CG  TRP B  32      26.922  32.114 128.157  1.00 94.48           C  
ANISOU 3233  CG  TRP B  32    12766  10418  12711    986    596   2962       C  
ATOM   3234  CD1 TRP B  32      25.620  32.384 128.485  1.00 95.53           C  
ANISOU 3234  CD1 TRP B  32    12754  10542  13002   1054    620   3074       C  
ATOM   3235  CD2 TRP B  32      27.244  32.975 127.062  1.00 95.70           C  
ANISOU 3235  CD2 TRP B  32    12837  10614  12908   1011    571   3208       C  
ATOM   3236  NE1 TRP B  32      25.124  33.374 127.675  1.00 97.82           N  
ANISOU 3236  NE1 TRP B  32    12865  10852  13450   1130    613   3387       N  
ATOM   3237  CE2 TRP B  32      26.098  33.753 126.790  1.00 97.89           C  
ANISOU 3237  CE2 TRP B  32    12908  10895  13387   1102    579   3482       C  
ATOM   3238  CE3 TRP B  32      28.396  33.170 126.288  1.00 95.59           C  
ANISOU 3238  CE3 TRP B  32    12894  10638  12788    963    544   3233       C  
ATOM   3239  CZ2 TRP B  32      26.068  34.715 125.772  1.00 99.92           C  
ANISOU 3239  CZ2 TRP B  32    13025  11193  13746   1146    554   3801       C  
ATOM   3240  CZ3 TRP B  32      28.370  34.128 125.280  1.00 97.54           C  
ANISOU 3240  CZ3 TRP B  32    13011  10930  13116    996    521   3531       C  
ATOM   3241  CH2 TRP B  32      27.211  34.887 125.031  1.00 99.69           C  
ANISOU 3241  CH2 TRP B  32    13076  11207  13594   1087    522   3822       C  
ATOM   3242  N   ALA B  33      26.588  28.775 130.243  1.00 90.78           N  
ANISOU 3242  N   ALA B  33    12581  10049  11861    781    526   2336       N  
ATOM   3243  CA  ALA B  33      25.475  27.829 130.415  1.00 90.61           C  
ANISOU 3243  CA  ALA B  33    12517  10161  11750    726    461   2311       C  
ATOM   3244  C   ALA B  33      24.960  27.717 131.851  1.00 89.64           C  
ANISOU 3244  C   ALA B  33    12411   9913  11735    749    542   2167       C  
ATOM   3245  O   ALA B  33      23.754  27.610 132.061  1.00 89.26           O  
ANISOU 3245  O   ALA B  33    12258   9926  11731    759    533   2224       O  
ATOM   3246  CB  ALA B  33      25.869  26.452 129.898  1.00 90.00           C  
ANISOU 3246  CB  ALA B  33    12541  10235  11419    597    362   2196       C  
ATOM   3247  N   VAL B  34      25.869  27.743 132.824  1.00 89.40           N  
ANISOU 3247  N   VAL B  34    12502   9728  11735    742    620   1986       N  
ATOM   3248  CA  VAL B  34      25.486  27.666 134.237  1.00 90.33           C  
ANISOU 3248  CA  VAL B  34    12639   9748  11932    735    704   1838       C  
ATOM   3249  C   VAL B  34      24.849  28.975 134.710  1.00 92.99           C  
ANISOU 3249  C   VAL B  34    12857   9949  12525    834    839   1903       C  
ATOM   3250  O   VAL B  34      23.887  28.944 135.479  1.00 94.48           O  
ANISOU 3250  O   VAL B  34    12980  10126  12790    837    891   1860       O  
ATOM   3251  CB  VAL B  34      26.685  27.287 135.145  1.00 88.80           C  
ANISOU 3251  CB  VAL B  34    12598   9465  11676    675    741   1640       C  
ATOM   3252  CG1 VAL B  34      26.298  27.314 136.622  1.00 88.43           C  
ANISOU 3252  CG1 VAL B  34    12557   9343  11697    644    832   1498       C  
ATOM   3253  CG2 VAL B  34      27.209  25.907 134.779  1.00 88.20           C  
ANISOU 3253  CG2 VAL B  34    12622   9496  11392    588    625   1575       C  
ATOM   3254  N   LYS B  35      25.376  30.113 134.255  1.00 94.41           N  
ANISOU 3254  N   LYS B  35    13004  10019  12847    910    907   2002       N  
ATOM   3255  CA  LYS B  35      24.875  31.419 134.693  1.00 96.59           C  
ANISOU 3255  CA  LYS B  35    13166  10122  13409   1008   1064   2055       C  
ATOM   3256  C   LYS B  35      23.435  31.673 134.242  1.00 98.82           C  
ANISOU 3256  C   LYS B  35    13258  10471  13818   1084   1047   2256       C  
ATOM   3257  O   LYS B  35      22.610  32.132 135.036  1.00100.07           O  
ANISOU 3257  O   LYS B  35    13325  10530  14165   1129   1168   2217       O  
ATOM   3258  CB  LYS B  35      25.782  32.554 134.201  1.00 97.83           C  
ANISOU 3258  CB  LYS B  35    13328  10140  13702   1069   1137   2138       C  
ATOM   3259  CG  LYS B  35      25.341  33.933 134.676  1.00100.20           C  
ANISOU 3259  CG  LYS B  35    13515  10221  14336   1168   1329   2177       C  
ATOM   3260  CD  LYS B  35      26.435  34.978 134.539  1.00100.99           C  
ANISOU 3260  CD  LYS B  35    13662  10145  14561   1195   1433   2178       C  
ATOM   3261  CE  LYS B  35      25.980  36.302 135.128  1.00103.46           C  
ANISOU 3261  CE  LYS B  35    13868  10208  15232   1281   1655   2177       C  
ATOM   3262  NZ  LYS B  35      26.922  37.412 134.817  1.00104.76           N  
ANISOU 3262  NZ  LYS B  35    14056  10194  15554   1316   1759   2223       N  
ATOM   3263  N   VAL B  36      23.150  31.384 132.973  1.00100.20           N  
ANISOU 3263  N   VAL B  36    13362  10823  13885   1087    904   2468       N  
ATOM   3264  CA  VAL B  36      21.807  31.587 132.407  1.00102.28           C  
ANISOU 3264  CA  VAL B  36    13423  11196  14243   1147    861   2702       C  
ATOM   3265  C   VAL B  36      20.767  30.579 132.926  1.00101.53           C  
ANISOU 3265  C   VAL B  36    13302  11234  14037   1085    809   2615       C  
ATOM   3266  O   VAL B  36      19.639  30.964 133.231  1.00102.75           O  
ANISOU 3266  O   VAL B  36    13301  11372  14367   1151    867   2700       O  
ATOM   3267  CB  VAL B  36      21.829  31.613 130.850  1.00103.52           C  
ANISOU 3267  CB  VAL B  36    13497  11544  14290   1140    716   2972       C  
ATOM   3268  CG1 VAL B  36      22.126  30.240 130.248  1.00102.30           C  
ANISOU 3268  CG1 VAL B  36    13452  11628  13786    993    554   2893       C  
ATOM   3269  CG2 VAL B  36      20.519  32.170 130.300  1.00106.21           C  
ANISOU 3269  CG2 VAL B  36    13591  11970  14794   1223    695   3268       C  
ATOM   3270  N   ASN B  37      21.153  29.308 133.043  1.00 99.68           N  
ANISOU 3270  N   ASN B  37    13216  11121  13535    959    711   2449       N  
ATOM   3271  CA  ASN B  37      20.227  28.225 133.391  1.00 99.20           C  
ANISOU 3271  CA  ASN B  37    13143  11206  13340    879    642   2379       C  
ATOM   3272  C   ASN B  37      20.107  28.049 134.910  1.00 98.52           C  
ANISOU 3272  C   ASN B  37    13124  10992  13316    856    753   2149       C  
ATOM   3273  O   ASN B  37      21.088  27.729 135.581  1.00 97.06           O  
ANISOU 3273  O   ASN B  37    13098  10722  13057    799    783   1960       O  
ATOM   3274  CB  ASN B  37      20.701  26.917 132.739  1.00 97.83           C  
ANISOU 3274  CB  ASN B  37    13092  11210  12869    746    495   2315       C  
ATOM   3275  CG  ASN B  37      19.623  25.845 132.689  1.00 98.22           C  
ANISOU 3275  CG  ASN B  37    13095  11449  12774    654    404   2308       C  
ATOM   3276  OD1 ASN B  37      18.562  25.968 133.304  1.00 99.26           O  
ANISOU 3276  OD1 ASN B  37    13122  11582  13008    683    446   2324       O  
ATOM   3277  ND2 ASN B  37      19.898  24.779 131.944  1.00 97.97           N  
ANISOU 3277  ND2 ASN B  37    13140  11576  12505    534    290   2272       N  
ATOM   3278  N   GLN B  38      18.900  28.253 135.439  1.00100.23           N  
ANISOU 3278  N   GLN B  38    13206  11213  13662    892    812   2175       N  
ATOM   3279  CA  GLN B  38      18.629  28.061 136.873  1.00100.38           C  
ANISOU 3279  CA  GLN B  38    13267  11149  13723    848    918   1961       C  
ATOM   3280  C   GLN B  38      18.572  26.584 137.291  1.00 99.06           C  
ANISOU 3280  C   GLN B  38    13217  11118  13303    706    813   1819       C  
ATOM   3281  O   GLN B  38      18.782  26.270 138.463  1.00 98.74           O  
ANISOU 3281  O   GLN B  38    13261  11018  13234    636    876   1628       O  
ATOM   3282  CB  GLN B  38      17.330  28.777 137.277  1.00102.75           C  
ANISOU 3282  CB  GLN B  38    13371  11408  14259    932   1031   2031       C  
ATOM   3283  CG  GLN B  38      16.046  28.122 136.777  1.00103.93           C  
ANISOU 3283  CG  GLN B  38    13387  11768  14332    913    917   2170       C  
ATOM   3284  CD  GLN B  38      14.872  29.087 136.668  1.00106.44           C  
ANISOU 3284  CD  GLN B  38    13461  12051  14929   1043   1009   2350       C  
ATOM   3285  OE1 GLN B  38      14.799  30.097 137.374  1.00107.36           O  
ANISOU 3285  OE1 GLN B  38    13514  11963  15313   1129   1197   2293       O  
ATOM   3286  NE2 GLN B  38      13.944  28.774 135.777  1.00107.67           N  
ANISOU 3286  NE2 GLN B  38    13468  12410  15029   1049    883   2568       N  
ATOM   3287  N   ALA B  39      18.283  25.689 136.340  1.00 99.05           N  
ANISOU 3287  N   ALA B  39    13212  11301  13120    650    658   1915       N  
ATOM   3288  CA  ALA B  39      18.315  24.234 136.583  1.00 97.40           C  
ANISOU 3288  CA  ALA B  39    13119  11201  12684    512    560   1790       C  
ATOM   3289  C   ALA B  39      19.715  23.697 136.906  1.00 95.63           C  
ANISOU 3289  C   ALA B  39    13088  10894  12352    451    548   1640       C  
ATOM   3290  O   ALA B  39      19.842  22.612 137.474  1.00 94.65           O  
ANISOU 3290  O   ALA B  39    13062  10799  12099    348    506   1518       O  
ATOM   3291  CB  ALA B  39      17.737  23.483 135.391  1.00 97.73           C  
ANISOU 3291  CB  ALA B  39    13109  11454  12569    453    419   1915       C  
ATOM   3292  N   LEU B  40      20.751  24.452 136.527  1.00 95.93           N  
ANISOU 3292  N   LEU B  40    13168  10829  12449    515    585   1665       N  
ATOM   3293  CA  LEU B  40      22.139  24.154 136.881  1.00 95.30           C  
ANISOU 3293  CA  LEU B  40    13247  10659  12300    474    591   1538       C  
ATOM   3294  C   LEU B  40      22.650  25.007 138.062  1.00 95.73           C  
ANISOU 3294  C   LEU B  40    13329  10554  12487    497    729   1427       C  
ATOM   3295  O   LEU B  40      23.839  25.331 138.118  1.00 95.20           O  
ANISOU 3295  O   LEU B  40    13349  10400  12422    503    759   1379       O  
ATOM   3296  CB  LEU B  40      23.038  24.385 135.657  1.00 95.31           C  
ANISOU 3296  CB  LEU B  40    13282  10672  12260    507    540   1626       C  
ATOM   3297  CG  LEU B  40      22.612  23.736 134.337  1.00 95.98           C  
ANISOU 3297  CG  LEU B  40    13327  10935  12206    465    420   1737       C  
ATOM   3298  CD1 LEU B  40      23.507  24.205 133.198  1.00 96.25           C  
ANISOU 3298  CD1 LEU B  40    13376  10980  12212    494    395   1825       C  
ATOM   3299  CD2 LEU B  40      22.635  22.220 134.456  1.00 95.38           C  
ANISOU 3299  CD2 LEU B  40    13346  10934  11958    343    345   1617       C  
ATOM   3300  N   ARG B  41      21.773  25.351 139.011  1.00 97.52           N  
ANISOU 3300  N   ARG B  41    13481  10756  12815    495    821   1373       N  
ATOM   3301  CA  ARG B  41      22.155  26.178 140.168  1.00 98.78           C  
ANISOU 3301  CA  ARG B  41    13656  10783  13092    486    975   1241       C  
ATOM   3302  C   ARG B  41      22.393  25.278 141.389  1.00 97.58           C  
ANISOU 3302  C   ARG B  41    13596  10675  12803    348    965   1081       C  
ATOM   3303  O   ARG B  41      21.802  25.467 142.454  1.00 97.54           O  
ANISOU 3303  O   ARG B  41    13548  10667  12843    293   1060    979       O  
ATOM   3304  CB  ARG B  41      21.090  27.248 140.433  1.00101.78           C  
ANISOU 3304  CB  ARG B  41    13881  11095  13696    566   1114   1272       C  
ATOM   3305  CG  ARG B  41      21.577  28.408 141.292  1.00103.26           C  
ANISOU 3305  CG  ARG B  41    14068  11113  14051    574   1306   1145       C  
ATOM   3306  CD  ARG B  41      20.529  29.497 141.370  1.00105.91           C  
ANISOU 3306  CD  ARG B  41    14234  11349  14655    675   1459   1192       C  
ATOM   3307  NE  ARG B  41      20.386  30.237 140.114  1.00107.93           N  
ANISOU 3307  NE  ARG B  41    14389  11553  15063    822   1439   1417       N  
ATOM   3308  CZ  ARG B  41      19.532  31.246 139.908  1.00110.78           C  
ANISOU 3308  CZ  ARG B  41    14578  11813  15699    943   1558   1529       C  
ATOM   3309  NH1 ARG B  41      18.714  31.666 140.876  1.00112.04           N  
ANISOU 3309  NH1 ARG B  41    14645  11899  16025    940   1725   1411       N  
ATOM   3310  NH2 ARG B  41      19.495  31.847 138.719  1.00111.75           N  
ANISOU 3310  NH2 ARG B  41    14608  11910  15939   1066   1516   1770       N  
ATOM   3311  N   ASP B  42      23.296  24.316 141.212  1.00 96.58           N  
ANISOU 3311  N   ASP B  42    13587  10590  12517    287    854   1067       N  
ATOM   3312  CA  ASP B  42      23.553  23.252 142.181  1.00 95.19           C  
ANISOU 3312  CA  ASP B  42    13491  10471  12204    158    807    972       C  
ATOM   3313  C   ASP B  42      25.051  23.196 142.492  1.00 92.95           C  
ANISOU 3313  C   ASP B  42    13313  10137  11864    117    802    922       C  
ATOM   3314  O   ASP B  42      25.876  23.668 141.698  1.00 92.99           O  
ANISOU 3314  O   ASP B  42    13347  10081  11902    189    799    966       O  
ATOM   3315  CB  ASP B  42      23.068  21.909 141.616  1.00 95.56           C  
ANISOU 3315  CB  ASP B  42    13558  10620  12129    121    669   1031       C  
ATOM   3316  CG  ASP B  42      22.567  20.959 142.695  1.00 96.88           C  
ANISOU 3316  CG  ASP B  42    13741  10858  12210     -1    644    964       C  
ATOM   3317  OD1 ASP B  42      23.205  20.860 143.770  1.00 98.19           O  
ANISOU 3317  OD1 ASP B  42    13957  11012  12338    -86    675    887       O  
ATOM   3318  OD2 ASP B  42      21.533  20.298 142.465  1.00 97.70           O  
ANISOU 3318  OD2 ASP B  42    13802  11046  12274    -26    589    998       O  
ATOM   3319  N   ALA B  43      25.388  22.612 143.641  1.00 90.92           N  
ANISOU 3319  N   ALA B  43    13103   9922  11521     -4    797    842       N  
ATOM   3320  CA  ALA B  43      26.773  22.545 144.126  1.00 88.94           C  
ANISOU 3320  CA  ALA B  43    12929   9650  11212    -62    792    806       C  
ATOM   3321  C   ALA B  43      27.728  21.968 143.084  1.00 87.35           C  
ANISOU 3321  C   ALA B  43    12795   9418  10975     -2    692    884       C  
ATOM   3322  O   ALA B  43      28.778  22.553 142.823  1.00 87.32           O  
ANISOU 3322  O   ALA B  43    12824   9357  10996     31    720    881       O  
ATOM   3323  CB  ALA B  43      26.853  21.736 145.418  1.00 88.59           C  
ANISOU 3323  CB  ALA B  43    12905   9695  11058   -214    764    760       C  
ATOM   3324  N   THR B  44      27.344  20.837 142.486  1.00 85.73           N  
ANISOU 3324  N   THR B  44    12606   9251  10716      0    589    940       N  
ATOM   3325  CA  THR B  44      28.142  20.176 141.441  1.00 84.25           C  
ANISOU 3325  CA  THR B  44    12475   9036  10500     43    511    990       C  
ATOM   3326  C   THR B  44      28.535  21.140 140.322  1.00 82.89           C  
ANISOU 3326  C   THR B  44    12293   8817  10383    147    543   1025       C  
ATOM   3327  O   THR B  44      29.699  21.189 139.923  1.00 81.92           O  
ANISOU 3327  O   THR B  44    12220   8651  10254    170    534   1030       O  
ATOM   3328  CB  THR B  44      27.387  18.972 140.830  1.00 84.32           C  
ANISOU 3328  CB  THR B  44    12487   9092  10457     22    427   1021       C  
ATOM   3329  OG1 THR B  44      27.126  18.006 141.853  1.00 84.72           O  
ANISOU 3329  OG1 THR B  44    12550   9173  10463    -77    393   1004       O  
ATOM   3330  CG2 THR B  44      28.194  18.298 139.711  1.00 83.77           C  
ANISOU 3330  CG2 THR B  44    12472   8990  10366     51    374   1041       C  
ATOM   3331  N   PHE B  45      27.565  21.913 139.843  1.00 82.33           N  
ANISOU 3331  N   PHE B  45    12148   8760  10373    206    580   1063       N  
ATOM   3332  CA  PHE B  45      27.788  22.826 138.719  1.00 81.74           C  
ANISOU 3332  CA  PHE B  45    12044   8655  10357    301    601   1135       C  
ATOM   3333  C   PHE B  45      28.660  24.012 139.124  1.00 81.02           C  
ANISOU 3333  C   PHE B  45    11964   8467  10350    332    699   1102       C  
ATOM   3334  O   PHE B  45      29.557  24.400 138.369  1.00 81.48           O  
ANISOU 3334  O   PHE B  45    12052   8489  10415    377    696   1137       O  
ATOM   3335  CB  PHE B  45      26.460  23.278 138.112  1.00 82.58           C  
ANISOU 3335  CB  PHE B  45    12043   8812  10518    355    605   1222       C  
ATOM   3336  CG  PHE B  45      25.608  22.134 137.640  1.00 82.91           C  
ANISOU 3336  CG  PHE B  45    12071   8969  10461    306    510   1249       C  
ATOM   3337  CD1 PHE B  45      26.025  21.335 136.582  1.00 83.18           C  
ANISOU 3337  CD1 PHE B  45    12151   9058  10394    281    428   1271       C  
ATOM   3338  CD2 PHE B  45      24.405  21.833 138.271  1.00 83.64           C  
ANISOU 3338  CD2 PHE B  45    12104   9117  10557    268    512   1236       C  
ATOM   3339  CE1 PHE B  45      25.256  20.261 136.157  1.00 83.78           C  
ANISOU 3339  CE1 PHE B  45    12218   9237  10375    213    355   1273       C  
ATOM   3340  CE2 PHE B  45      23.625  20.768 137.844  1.00 84.01           C  
ANISOU 3340  CE2 PHE B  45    12139   9272  10507    208    428   1255       C  
ATOM   3341  CZ  PHE B  45      24.051  19.978 136.788  1.00 84.08           C  
ANISOU 3341  CZ  PHE B  45    12198   9330  10416    176    351   1269       C  
ATOM   3342  N   CYS B  46      28.438  24.543 140.328  1.00 79.84           N  
ANISOU 3342  N   CYS B  46    11793   8285  10254    289    792   1021       N  
ATOM   3343  CA  CYS B  46      29.305  25.592 140.890  1.00 79.04           C  
ANISOU 3343  CA  CYS B  46    11710   8099  10219    279    901    955       C  
ATOM   3344  C   CYS B  46      30.798  25.212 140.925  1.00 77.45           C  
ANISOU 3344  C   CYS B  46    11598   7897   9933    239    856    934       C  
ATOM   3345  O   CYS B  46      31.662  26.078 140.781  1.00 77.26           O  
ANISOU 3345  O   CYS B  46    11591   7808   9956    260    918    921       O  
ATOM   3346  CB  CYS B  46      28.828  25.986 142.289  1.00 79.63           C  
ANISOU 3346  CB  CYS B  46    11754   8172  10328    193   1010    838       C  
ATOM   3347  SG  CYS B  46      27.127  26.594 142.324  1.00 81.01           S  
ANISOU 3347  SG  CYS B  46    11805   8327  10646    250   1097    852       S  
ATOM   3348  N   PHE B  47      31.091  23.924 141.109  1.00 76.16           N  
ANISOU 3348  N   PHE B  47    11479   7799   9659    183    753    938       N  
ATOM   3349  CA  PHE B  47      32.461  23.411 140.978  1.00 74.87           C  
ANISOU 3349  CA  PHE B  47    11379   7632   9435    164    700    946       C  
ATOM   3350  C   PHE B  47      32.867  23.243 139.508  1.00 73.67           C  
ANISOU 3350  C   PHE B  47    11248   7460   9284    251    649   1012       C  
ATOM   3351  O   PHE B  47      34.043  23.410 139.170  1.00 73.10           O  
ANISOU 3351  O   PHE B  47    11211   7359   9205    266    650   1015       O  
ATOM   3352  CB  PHE B  47      32.630  22.076 141.710  1.00 74.68           C  
ANISOU 3352  CB  PHE B  47    11378   7665   9329     79    620    947       C  
ATOM   3353  CG  PHE B  47      32.265  22.121 143.173  1.00 75.28           C  
ANISOU 3353  CG  PHE B  47    11430   7800   9371    -35    657    893       C  
ATOM   3354  CD1 PHE B  47      32.810  23.083 144.024  1.00 75.59           C  
ANISOU 3354  CD1 PHE B  47    11461   7847   9412   -102    748    824       C  
ATOM   3355  CD2 PHE B  47      31.388  21.180 143.709  1.00 75.57           C  
ANISOU 3355  CD2 PHE B  47    11451   7898   9365    -96    606    903       C  
ATOM   3356  CE1 PHE B  47      32.470  23.112 145.372  1.00 75.92           C  
ANISOU 3356  CE1 PHE B  47    11475   7972   9400   -238    789    759       C  
ATOM   3357  CE2 PHE B  47      31.046  21.210 145.054  1.00 76.04           C  
ANISOU 3357  CE2 PHE B  47    11482   8034   9375   -221    639    855       C  
ATOM   3358  CZ  PHE B  47      31.588  22.177 145.886  1.00 76.03           C  
ANISOU 3358  CZ  PHE B  47    11469   8055   9362   -297    733    779       C  
ATOM   3359  N   ILE B  48      31.909  22.897 138.644  1.00 73.51           N  
ANISOU 3359  N   ILE B  48    11199   7472   9258    291    606   1061       N  
ATOM   3360  CA  ILE B  48      32.160  22.810 137.193  1.00 73.71           C  
ANISOU 3360  CA  ILE B  48    11231   7513   9262    346    565   1118       C  
ATOM   3361  C   ILE B  48      32.502  24.185 136.586  1.00 74.01           C  
ANISOU 3361  C   ILE B  48    11243   7508   9370    415    627   1168       C  
ATOM   3362  O   ILE B  48      33.292  24.268 135.634  1.00 74.22           O  
ANISOU 3362  O   ILE B  48    11292   7537   9369    440    609   1198       O  
ATOM   3363  CB  ILE B  48      30.980  22.120 136.451  1.00 74.26           C  
ANISOU 3363  CB  ILE B  48    11264   7665   9287    340    504   1159       C  
ATOM   3364  CG1 ILE B  48      30.944  20.631 136.817  1.00 73.94           C  
ANISOU 3364  CG1 ILE B  48    11267   7644   9183    268    444   1108       C  
ATOM   3365  CG2 ILE B  48      31.086  22.281 134.931  1.00 75.17           C  
ANISOU 3365  CG2 ILE B  48    11362   7832   9364    373    474   1225       C  
ATOM   3366  CD1 ILE B  48      29.647  19.928 136.478  1.00 74.63           C  
ANISOU 3366  CD1 ILE B  48    11318   7813   9225    232    398   1123       C  
ATOM   3367  N   VAL B  49      31.927  25.250 137.147  1.00 73.48           N  
ANISOU 3367  N   VAL B  49    11123   7392   9402    439    711   1172       N  
ATOM   3368  CA  VAL B  49      32.283  26.620 136.768  1.00 73.69           C  
ANISOU 3368  CA  VAL B  49    11123   7341   9532    500    793   1217       C  
ATOM   3369  C   VAL B  49      33.740  26.898 137.158  1.00 72.63           C  
ANISOU 3369  C   VAL B  49    11057   7155   9382    467    830   1149       C  
ATOM   3370  O   VAL B  49      34.520  27.388 136.334  1.00 73.41           O  
ANISOU 3370  O   VAL B  49    11171   7232   9488    504    834   1196       O  
ATOM   3371  CB  VAL B  49      31.338  27.668 137.417  1.00 74.90           C  
ANISOU 3371  CB  VAL B  49    11199   7424   9834    528    904   1214       C  
ATOM   3372  CG1 VAL B  49      31.823  29.097 137.159  1.00 75.29           C  
ANISOU 3372  CG1 VAL B  49    11226   7356  10024    584   1012   1249       C  
ATOM   3373  CG2 VAL B  49      29.909  27.499 136.905  1.00 75.87           C  
ANISOU 3373  CG2 VAL B  49    11231   7607   9987    573    865   1312       C  
ATOM   3374  N   SER B  50      34.098  26.576 138.404  1.00 71.14           N  
ANISOU 3374  N   SER B  50    10901   6968   9160    386    852   1048       N  
ATOM   3375  CA  SER B  50      35.474  26.735 138.892  1.00 70.32           C  
ANISOU 3375  CA  SER B  50    10847   6847   9021    334    876    991       C  
ATOM   3376  C   SER B  50      36.460  25.928 138.051  1.00 69.56           C  
ANISOU 3376  C   SER B  50    10795   6784   8849    353    787   1030       C  
ATOM   3377  O   SER B  50      37.531  26.427 137.689  1.00 69.39           O  
ANISOU 3377  O   SER B  50    10796   6736   8830    364    811   1033       O  
ATOM   3378  CB  SER B  50      35.580  26.327 140.366  1.00 69.99           C  
ANISOU 3378  CB  SER B  50    10814   6849   8927    221    890    904       C  
ATOM   3379  OG  SER B  50      36.922  26.384 140.823  1.00 70.06           O  
ANISOU 3379  OG  SER B  50    10857   6875   8886    158    896    872       O  
ATOM   3380  N   LEU B  51      36.083  24.689 137.739  1.00 69.49           N  
ANISOU 3380  N   LEU B  51    10794   6828   8780    352    698   1050       N  
ATOM   3381  CA  LEU B  51      36.883  23.822 136.869  1.00 68.95           C  
ANISOU 3381  CA  LEU B  51    10758   6780   8660    368    634   1066       C  
ATOM   3382  C   LEU B  51      37.002  24.378 135.440  1.00 69.12           C  
ANISOU 3382  C   LEU B  51    10772   6807   8682    427    639   1119       C  
ATOM   3383  O   LEU B  51      38.072  24.288 134.829  1.00 69.17           O  
ANISOU 3383  O   LEU B  51    10805   6812   8663    435    634   1115       O  
ATOM   3384  CB  LEU B  51      36.301  22.402 136.855  1.00 68.48           C  
ANISOU 3384  CB  LEU B  51    10704   6756   8558    342    562   1060       C  
ATOM   3385  CG  LEU B  51      37.010  21.318 136.038  1.00 68.34           C  
ANISOU 3385  CG  LEU B  51    10714   6739   8511    346    519   1050       C  
ATOM   3386  CD1 LEU B  51      38.498  21.238 136.340  1.00 67.91           C  
ANISOU 3386  CD1 LEU B  51    10677   6648   8474    344    531   1039       C  
ATOM   3387  CD2 LEU B  51      36.346  19.975 136.299  1.00 68.50           C  
ANISOU 3387  CD2 LEU B  51    10738   6768   8520    306    470   1034       C  
ATOM   3388  N   ALA B  52      35.913  24.953 134.923  1.00 69.43           N  
ANISOU 3388  N   ALA B  52    10764   6863   8750    462    647   1180       N  
ATOM   3389  CA  ALA B  52      35.920  25.603 133.603  1.00 69.73           C  
ANISOU 3389  CA  ALA B  52    10776   6932   8787    506    646   1267       C  
ATOM   3390  C   ALA B  52      36.828  26.835 133.579  1.00 69.88           C  
ANISOU 3390  C   ALA B  52    10801   6878   8870    533    718   1287       C  
ATOM   3391  O   ALA B  52      37.633  26.991 132.659  1.00 69.78           O  
ANISOU 3391  O   ALA B  52    10804   6890   8819    540    708   1317       O  
ATOM   3392  CB  ALA B  52      34.509  25.981 133.182  1.00 70.26           C  
ANISOU 3392  CB  ALA B  52    10766   7042   8887    536    635   1362       C  
ATOM   3393  N   VAL B  53      36.702  27.683 134.604  1.00 70.03           N  
ANISOU 3393  N   VAL B  53    10810   6813   8985    534    799   1256       N  
ATOM   3394  CA  VAL B  53      37.551  28.880 134.779  1.00 70.26           C  
ANISOU 3394  CA  VAL B  53    10850   6756   9089    539    890   1248       C  
ATOM   3395  C   VAL B  53      39.045  28.534 134.692  1.00 70.20           C  
ANISOU 3395  C   VAL B  53    10901   6769   9003    503    870   1197       C  
ATOM   3396  O   VAL B  53      39.811  29.214 133.996  1.00 69.89           O  
ANISOU 3396  O   VAL B  53    10869   6710   8975    521    896   1236       O  
ATOM   3397  CB  VAL B  53      37.246  29.594 136.127  1.00 70.22           C  
ANISOU 3397  CB  VAL B  53    10834   6667   9180    505    996   1165       C  
ATOM   3398  CG1 VAL B  53      38.301  30.646 136.473  1.00 70.44           C  
ANISOU 3398  CG1 VAL B  53    10886   6614   9261    473   1096   1115       C  
ATOM   3399  CG2 VAL B  53      35.856  30.226 136.097  1.00 71.21           C  
ANISOU 3399  CG2 VAL B  53    10882   6743   9431    559   1048   1225       C  
ATOM   3400  N   ALA B  54      39.442  27.475 135.398  1.00 70.29           N  
ANISOU 3400  N   ALA B  54    10942   6819   8944    454    824   1125       N  
ATOM   3401  CA  ALA B  54      40.816  26.958 135.333  1.00 70.32           C  
ANISOU 3401  CA  ALA B  54    10981   6848   8888    428    798   1093       C  
ATOM   3402  C   ALA B  54      41.231  26.564 133.908  1.00 70.53           C  
ANISOU 3402  C   ALA B  54    11014   6916   8867    465    755   1133       C  
ATOM   3403  O   ALA B  54      42.351  26.867 133.480  1.00 70.39           O  
ANISOU 3403  O   ALA B  54    11010   6898   8834    463    774   1130       O  
ATOM   3404  CB  ALA B  54      40.984  25.774 136.279  1.00 70.02           C  
ANISOU 3404  CB  ALA B  54    10950   6843   8809    379    748   1048       C  
ATOM   3405  N   ASP B  55      40.328  25.906 133.180  1.00 70.81           N  
ANISOU 3405  N   ASP B  55    11035   7000   8868    481    704   1162       N  
ATOM   3406  CA  ASP B  55      40.600  25.504 131.794  1.00 71.61           C  
ANISOU 3406  CA  ASP B  55    11137   7168   8901    485    673   1182       C  
ATOM   3407  C   ASP B  55      40.660  26.706 130.828  1.00 71.82           C  
ANISOU 3407  C   ASP B  55    11139   7214   8934    507    700   1274       C  
ATOM   3408  O   ASP B  55      41.500  26.725 129.917  1.00 71.35           O  
ANISOU 3408  O   ASP B  55    11089   7200   8820    494    701   1276       O  
ATOM   3409  CB  ASP B  55      39.581  24.455 131.312  1.00 72.15           C  
ANISOU 3409  CB  ASP B  55    11192   7303   8915    465    617   1175       C  
ATOM   3410  CG  ASP B  55      39.696  23.109 132.056  1.00 71.72           C  
ANISOU 3410  CG  ASP B  55    11163   7221   8864    438    592   1091       C  
ATOM   3411  OD1 ASP B  55      40.789  22.768 132.566  1.00 71.11           O  
ANISOU 3411  OD1 ASP B  55    11106   7098   8815    437    606   1049       O  
ATOM   3412  OD2 ASP B  55      38.679  22.376 132.116  1.00 71.68           O  
ANISOU 3412  OD2 ASP B  55    11149   7244   8842    417    556   1082       O  
ATOM   3413  N   VAL B  56      39.803  27.710 131.043  1.00 72.18           N  
ANISOU 3413  N   VAL B  56    11145   7220   9057    539    729   1354       N  
ATOM   3414  CA  VAL B  56      39.872  28.971 130.275  1.00 73.42           C  
ANISOU 3414  CA  VAL B  56    11268   7366   9262    568    765   1471       C  
ATOM   3415  C   VAL B  56      41.244  29.614 130.470  1.00 73.37           C  
ANISOU 3415  C   VAL B  56    11302   7297   9278    557    824   1431       C  
ATOM   3416  O   VAL B  56      41.852  30.092 129.511  1.00 73.78           O  
ANISOU 3416  O   VAL B  56    11349   7385   9300    553    828   1493       O  
ATOM   3417  CB  VAL B  56      38.776  30.002 130.678  1.00 74.26           C  
ANISOU 3417  CB  VAL B  56    11313   7392   9507    617    815   1562       C  
ATOM   3418  CG1 VAL B  56      38.984  31.343 129.969  1.00 74.95           C  
ANISOU 3418  CG1 VAL B  56    11360   7434   9683    652    865   1699       C  
ATOM   3419  CG2 VAL B  56      37.378  29.474 130.374  1.00 74.64           C  
ANISOU 3419  CG2 VAL B  56    11303   7522   9535    629    753   1630       C  
ATOM   3420  N   ALA B  57      41.717  29.620 131.716  1.00 73.22           N  
ANISOU 3420  N   ALA B  57    11316   7203   9299    537    868   1330       N  
ATOM   3421  CA  ALA B  57      43.034  30.170 132.048  1.00 73.03           C  
ANISOU 3421  CA  ALA B  57    11324   7138   9284    507    923   1281       C  
ATOM   3422  C   ALA B  57      44.190  29.443 131.357  1.00 72.85           C  
ANISOU 3422  C   ALA B  57    11325   7192   9163    488    881   1251       C  
ATOM   3423  O   ALA B  57      45.177  30.082 131.011  1.00 72.82           O  
ANISOU 3423  O   ALA B  57    11330   7181   9155    474    918   1259       O  
ATOM   3424  CB  ALA B  57      43.247  30.184 133.556  1.00 72.46           C  
ANISOU 3424  CB  ALA B  57    11270   7017   9244    460    967   1181       C  
ATOM   3425  N   VAL B  58      44.071  28.129 131.151  1.00 72.40           N  
ANISOU 3425  N   VAL B  58    11270   7197   9038    485    817   1209       N  
ATOM   3426  CA  VAL B  58      45.109  27.358 130.440  1.00 72.24           C  
ANISOU 3426  CA  VAL B  58    11261   7236   8950    470    798   1164       C  
ATOM   3427  C   VAL B  58      45.216  27.844 128.985  1.00 73.40           C  
ANISOU 3427  C   VAL B  58    11395   7454   9039    464    800   1227       C  
ATOM   3428  O   VAL B  58      46.303  28.260 128.523  1.00 73.57           O  
ANISOU 3428  O   VAL B  58    11422   7492   9038    448    831   1224       O  
ATOM   3429  CB  VAL B  58      44.833  25.831 130.497  1.00 71.54           C  
ANISOU 3429  CB  VAL B  58    11173   7173   8834    464    750   1100       C  
ATOM   3430  CG1 VAL B  58      45.797  25.043 129.612  1.00 71.57           C  
ANISOU 3430  CG1 VAL B  58    11177   7222   8794    450    757   1041       C  
ATOM   3431  CG2 VAL B  58      44.913  25.327 131.933  1.00 71.14           C  
ANISOU 3431  CG2 VAL B  58    11125   7069   8834    459    741   1064       C  
ATOM   3432  N   GLY B  59      44.075  27.812 128.294  1.00 74.05           N  
ANISOU 3432  N   GLY B  59    11450   7593   9089    465    765   1296       N  
ATOM   3433  CA  GLY B  59      43.970  28.246 126.900  1.00 74.53           C  
ANISOU 3433  CA  GLY B  59    11480   7760   9074    438    751   1386       C  
ATOM   3434  C   GLY B  59      44.243  29.720 126.652  1.00 74.72           C  
ANISOU 3434  C   GLY B  59    11487   7747   9155    455    791   1506       C  
ATOM   3435  O   GLY B  59      44.823  30.074 125.629  1.00 74.83           O  
ANISOU 3435  O   GLY B  59    11488   7841   9101    419    794   1558       O  
ATOM   3436  N   ALA B  60      43.831  30.574 127.588  1.00 74.90           N  
ANISOU 3436  N   ALA B  60    11505   7644   9307    500    833   1545       N  
ATOM   3437  CA  ALA B  60      44.031  32.029 127.480  1.00 75.40           C  
ANISOU 3437  CA  ALA B  60    11550   7627   9469    518    894   1654       C  
ATOM   3438  C   ALA B  60      45.379  32.540 128.011  1.00 74.52           C  
ANISOU 3438  C   ALA B  60    11484   7441   9386    495    963   1573       C  
ATOM   3439  O   ALA B  60      45.853  33.570 127.538  1.00 75.44           O  
ANISOU 3439  O   ALA B  60    11592   7526   9542    487   1008   1655       O  
ATOM   3440  CB  ALA B  60      42.895  32.766 128.174  1.00 76.07           C  
ANISOU 3440  CB  ALA B  60    11597   7597   9707    571    934   1723       C  
ATOM   3441  N   LEU B  61      45.971  31.853 128.995  1.00 72.80           N  
ANISOU 3441  N   LEU B  61    11307   7202   9151    476    969   1430       N  
ATOM   3442  CA  LEU B  61      47.259  32.265 129.597  1.00 71.96           C  
ANISOU 3442  CA  LEU B  61    11230   7053   9055    438   1026   1355       C  
ATOM   3443  C   LEU B  61      48.398  31.256 129.402  1.00 71.09           C  
ANISOU 3443  C   LEU B  61    11132   7030   8845    412    990   1271       C  
ATOM   3444  O   LEU B  61      49.487  31.642 128.970  1.00 70.65           O  
ANISOU 3444  O   LEU B  61    11081   7000   8759    384   1019   1268       O  
ATOM   3445  CB  LEU B  61      47.089  32.569 131.096  1.00 71.60           C  
ANISOU 3445  CB  LEU B  61    11200   6914   9091    418   1080   1278       C  
ATOM   3446  CG  LEU B  61      48.307  33.026 131.911  1.00 71.46           C  
ANISOU 3446  CG  LEU B  61    11203   6875   9074    349   1141   1195       C  
ATOM   3447  CD1 LEU B  61      48.961  34.269 131.321  1.00 72.17           C  
ANISOU 3447  CD1 LEU B  61    11299   6916   9206    329   1214   1246       C  
ATOM   3448  CD2 LEU B  61      47.892  33.270 133.354  1.00 71.40           C  
ANISOU 3448  CD2 LEU B  61    11200   6806   9122    303   1195   1115       C  
ATOM   3449  N   VAL B  62      48.160  29.981 129.726  1.00 70.60           N  
ANISOU 3449  N   VAL B  62    11069   7003   8750    422    938   1207       N  
ATOM   3450  CA  VAL B  62      49.243  28.978 129.740  1.00 69.95           C  
ANISOU 3450  CA  VAL B  62    10983   6970   8624    410    921   1129       C  
ATOM   3451  C   VAL B  62      49.764  28.690 128.333  1.00 70.07           C  
ANISOU 3451  C   VAL B  62    10987   7068   8565    401    920   1128       C  
ATOM   3452  O   VAL B  62      50.977  28.667 128.121  1.00 69.69           O  
ANISOU 3452  O   VAL B  62    10931   7049   8498    382    947   1091       O  
ATOM   3453  CB  VAL B  62      48.827  27.658 130.445  1.00 69.37           C  
ANISOU 3453  CB  VAL B  62    10902   6889   8564    425    875   1077       C  
ATOM   3454  CG1 VAL B  62      49.900  26.582 130.305  1.00 69.19           C  
ANISOU 3454  CG1 VAL B  62    10857   6896   8536    428    869   1018       C  
ATOM   3455  CG2 VAL B  62      48.541  27.920 131.914  1.00 69.11           C  
ANISOU 3455  CG2 VAL B  62    10872   6805   8580    407    880   1070       C  
ATOM   3456  N   ILE B  63      48.853  28.481 127.383  1.00 70.16           N  
ANISOU 3456  N   ILE B  63    10993   7137   8526    399    891   1165       N  
ATOM   3457  CA  ILE B  63      49.250  28.136 126.008  1.00 70.74           C  
ANISOU 3457  CA  ILE B  63    11052   7323   8503    359    894   1148       C  
ATOM   3458  C   ILE B  63      49.967  29.289 125.267  1.00 70.52           C  
ANISOU 3458  C   ILE B  63    11018   7337   8438    327    927   1220       C  
ATOM   3459  O   ILE B  63      50.976  29.044 124.597  1.00 71.24           O  
ANISOU 3459  O   ILE B  63    11100   7497   8470    290    956   1163       O  
ATOM   3460  CB  ILE B  63      48.067  27.532 125.208  1.00 71.94           C  
ANISOU 3460  CB  ILE B  63    11190   7561   8583    334    851   1163       C  
ATOM   3461  CG1 ILE B  63      47.734  26.139 125.772  1.00 72.07           C  
ANISOU 3461  CG1 ILE B  63    11214   7539   8629    349    836   1054       C  
ATOM   3462  CG2 ILE B  63      48.398  27.421 123.725  1.00 73.01           C  
ANISOU 3462  CG2 ILE B  63    11304   7846   8590    258    862   1155       C  
ATOM   3463  CD1 ILE B  63      46.447  25.519 125.260  1.00 72.63           C  
ANISOU 3463  CD1 ILE B  63    11275   7680   8641    318    795   1058       C  
ATOM   3464  N   PRO B  64      49.458  30.535 125.378  1.00 69.67           N  
ANISOU 3464  N   PRO B  64    10910   7182   8380    339    934   1345       N  
ATOM   3465  CA  PRO B  64      50.192  31.706 124.880  1.00 69.53           C  
ANISOU 3465  CA  PRO B  64    10889   7170   8360    310    975   1424       C  
ATOM   3466  C   PRO B  64      51.596  31.892 125.463  1.00 68.75           C  
ANISOU 3466  C   PRO B  64    10808   7029   8283    296   1026   1340       C  
ATOM   3467  O   PRO B  64      52.529  32.158 124.712  1.00 69.45           O  
ANISOU 3467  O   PRO B  64    10889   7188   8311    252   1050   1342       O  
ATOM   3468  CB  PRO B  64      49.293  32.866 125.289  1.00 69.85           C  
ANISOU 3468  CB  PRO B  64    10921   7103   8513    345    991   1553       C  
ATOM   3469  CG  PRO B  64      47.931  32.295 125.192  1.00 70.02           C  
ANISOU 3469  CG  PRO B  64    10919   7156   8529    373    933   1592       C  
ATOM   3470  CD  PRO B  64      48.051  30.877 125.667  1.00 69.50           C  
ANISOU 3470  CD  PRO B  64    10875   7115   8416    375    906   1438       C  
ATOM   3471  N   LEU B  65      51.736  31.763 126.779  1.00 67.78           N  
ANISOU 3471  N   LEU B  65    10702   6815   8237    318   1040   1274       N  
ATOM   3472  CA  LEU B  65      53.055  31.830 127.437  1.00 67.64           C  
ANISOU 3472  CA  LEU B  65    10685   6786   8228    291   1077   1202       C  
ATOM   3473  C   LEU B  65      54.041  30.807 126.872  1.00 67.91           C  
ANISOU 3473  C   LEU B  65    10692   6912   8198    284   1069   1124       C  
ATOM   3474  O   LEU B  65      55.213  31.125 126.653  1.00 68.14           O  
ANISOU 3474  O   LEU B  65    10706   6979   8203    250   1106   1105       O  
ATOM   3475  CB  LEU B  65      52.928  31.626 128.955  1.00 66.91           C  
ANISOU 3475  CB  LEU B  65    10599   6624   8200    295   1077   1149       C  
ATOM   3476  CG  LEU B  65      52.431  32.826 129.766  1.00 66.99           C  
ANISOU 3476  CG  LEU B  65    10631   6532   8288    272   1131   1177       C  
ATOM   3477  CD1 LEU B  65      51.981  32.402 131.157  1.00 66.51           C  
ANISOU 3477  CD1 LEU B  65    10571   6436   8262    262   1121   1118       C  
ATOM   3478  CD2 LEU B  65      53.508  33.900 129.856  1.00 67.48           C  
ANISOU 3478  CD2 LEU B  65    10702   6579   8359    208   1202   1172       C  
ATOM   3479  N   ALA B  66      53.556  29.589 126.638  1.00 68.27           N  
ANISOU 3479  N   ALA B  66    10726   6985   8229    312   1034   1074       N  
ATOM   3480  CA  ALA B  66      54.365  28.515 126.055  1.00 69.40           C  
ANISOU 3480  CA  ALA B  66    10835   7190   8343    309   1049    983       C  
ATOM   3481  C   ALA B  66      54.839  28.878 124.652  1.00 70.90           C  
ANISOU 3481  C   ALA B  66    11015   7485   8437    255   1082    985       C  
ATOM   3482  O   ALA B  66      56.012  28.694 124.324  1.00 71.49           O  
ANISOU 3482  O   ALA B  66    11059   7604   8498    235   1127    925       O  
ATOM   3483  CB  ALA B  66      53.583  27.208 126.030  1.00 69.25           C  
ANISOU 3483  CB  ALA B  66    10811   7160   8342    338   1022    923       C  
ATOM   3484  N   ILE B  67      53.925  29.408 123.843  1.00 72.34           N  
ANISOU 3484  N   ILE B  67    11214   7721   8552    224   1060   1065       N  
ATOM   3485  CA  ILE B  67      54.250  29.875 122.487  1.00 74.23           C  
ANISOU 3485  CA  ILE B  67    11437   8088   8677    150   1080   1100       C  
ATOM   3486  C   ILE B  67      55.265  31.031 122.539  1.00 74.89           C  
ANISOU 3486  C   ILE B  67    11522   8159   8770    127   1118   1157       C  
ATOM   3487  O   ILE B  67      56.291  30.991 121.850  1.00 75.18           O  
ANISOU 3487  O   ILE B  67    11536   8284   8742     76   1159   1107       O  
ATOM   3488  CB  ILE B  67      52.973  30.277 121.703  1.00 74.96           C  
ANISOU 3488  CB  ILE B  67    11526   8255   8699    117   1032   1223       C  
ATOM   3489  CG1 ILE B  67      52.099  29.033 121.446  1.00 75.40           C  
ANISOU 3489  CG1 ILE B  67    11574   8361   8711    107   1003   1141       C  
ATOM   3490  CG2 ILE B  67      53.318  30.950 120.376  1.00 75.96           C  
ANISOU 3490  CG2 ILE B  67    11627   8532   8701     23   1042   1304       C  
ATOM   3491  CD1 ILE B  67      50.645  29.350 121.169  1.00 75.92           C  
ANISOU 3491  CD1 ILE B  67    11630   8469   8747    100    940   1273       C  
ATOM   3492  N   LEU B  68      54.983  32.035 123.369  1.00 75.12           N  
ANISOU 3492  N   LEU B  68    11577   8078   8885    155   1116   1246       N  
ATOM   3493  CA  LEU B  68      55.889  33.177 123.560  1.00 75.95           C  
ANISOU 3493  CA  LEU B  68    11690   8149   9016    122   1163   1290       C  
ATOM   3494  C   LEU B  68      57.285  32.750 124.024  1.00 75.92           C  
ANISOU 3494  C   LEU B  68    11667   8163   9014    111   1199   1176       C  
ATOM   3495  O   LEU B  68      58.284  33.256 123.514  1.00 76.93           O  
ANISOU 3495  O   LEU B  68    11782   8351   9097     59   1238   1179       O  
ATOM   3496  CB  LEU B  68      55.303  34.204 124.543  1.00 76.03           C  
ANISOU 3496  CB  LEU B  68    11731   8013   9144    147   1179   1363       C  
ATOM   3497  CG  LEU B  68      54.145  35.084 124.052  1.00 77.06           C  
ANISOU 3497  CG  LEU B  68    11860   8101   9316    158   1169   1521       C  
ATOM   3498  CD1 LEU B  68      53.641  35.970 125.183  1.00 76.84           C  
ANISOU 3498  CD1 LEU B  68    11856   7900   9438    186   1215   1548       C  
ATOM   3499  CD2 LEU B  68      54.541  35.933 122.851  1.00 78.10           C  
ANISOU 3499  CD2 LEU B  68    11973   8308   9391     99   1184   1644       C  
ATOM   3500  N   ILE B  69      57.349  31.821 124.979  1.00 75.17           N  
ANISOU 3500  N   ILE B  69    11560   8025   8975    158   1182   1093       N  
ATOM   3501  CA  ILE B  69      58.635  31.250 125.418  1.00 74.75           C  
ANISOU 3501  CA  ILE B  69    11461   8001   8939    158   1206   1012       C  
ATOM   3502  C   ILE B  69      59.302  30.438 124.293  1.00 75.44           C  
ANISOU 3502  C   ILE B  69    11504   8189   8971    147   1236    935       C  
ATOM   3503  O   ILE B  69      60.522  30.497 124.128  1.00 75.53           O  
ANISOU 3503  O   ILE B  69    11472   8253   8971    121   1279    899       O  
ATOM   3504  CB  ILE B  69      58.472  30.399 126.708  1.00 74.05           C  
ANISOU 3504  CB  ILE B  69    11351   7850   8931    209   1173    976       C  
ATOM   3505  CG1 ILE B  69      58.105  31.301 127.902  1.00 73.99           C  
ANISOU 3505  CG1 ILE B  69    11377   7770   8963    184   1167   1022       C  
ATOM   3506  CG2 ILE B  69      59.727  29.585 127.026  1.00 73.88           C  
ANISOU 3506  CG2 ILE B  69    11254   7870   8947    222   1188    922       C  
ATOM   3507  CD1 ILE B  69      59.238  32.135 128.475  1.00 74.61           C  
ANISOU 3507  CD1 ILE B  69    11439   7872   9035    116   1208   1023       C  
ATOM   3508  N   ASN B  70      58.503  29.694 123.526  1.00 75.85           N  
ANISOU 3508  N   ASN B  70    11561   8272   8985    154   1224    901       N  
ATOM   3509  CA  ASN B  70      59.017  28.898 122.402  1.00 76.95           C  
ANISOU 3509  CA  ASN B  70    11660   8510   9065    120   1274    798       C  
ATOM   3510  C   ASN B  70      59.645  29.772 121.314  1.00 78.05           C  
ANISOU 3510  C   ASN B  70    11794   8770   9090     32   1311    828       C  
ATOM   3511  O   ASN B  70      60.781  29.533 120.905  1.00 78.02           O  
ANISOU 3511  O   ASN B  70    11742   8828   9071      4   1372    748       O  
ATOM   3512  CB  ASN B  70      57.903  28.032 121.799  1.00 77.15           C  
ANISOU 3512  CB  ASN B  70    11698   8561   9052    113   1258    750       C  
ATOM   3513  CG  ASN B  70      58.399  27.112 120.705  1.00 78.06           C  
ANISOU 3513  CG  ASN B  70    11771   8772   9115     58   1333    604       C  
ATOM   3514  OD1 ASN B  70      58.161  27.358 119.525  1.00 78.83           O  
ANISOU 3514  OD1 ASN B  70    11871   9007   9072    -38   1348    599       O  
ATOM   3515  ND2 ASN B  70      59.100  26.051 121.091  1.00 78.48           N  
ANISOU 3515  ND2 ASN B  70    11774   8757   9287    112   1389    488       N  
ATOM   3516  N   ILE B  71      58.902  30.777 120.857  1.00 78.98           N  
ANISOU 3516  N   ILE B  71    11951   8918   9137    -11   1275    954       N  
ATOM   3517  CA  ILE B  71      59.403  31.703 119.820  1.00 80.17           C  
ANISOU 3517  CA  ILE B  71    12095   9187   9179   -105   1300   1022       C  
ATOM   3518  C   ILE B  71      60.402  32.745 120.352  1.00 80.34           C  
ANISOU 3518  C   ILE B  71    12120   9159   9243   -114   1328   1073       C  
ATOM   3519  O   ILE B  71      61.195  33.289 119.579  1.00 81.48           O  
ANISOU 3519  O   ILE B  71    12246   9402   9308   -191   1366   1090       O  
ATOM   3520  CB  ILE B  71      58.250  32.403 119.048  1.00 80.78           C  
ANISOU 3520  CB  ILE B  71    12191   9326   9176   -154   1249   1176       C  
ATOM   3521  CG1 ILE B  71      57.554  33.476 119.907  1.00 80.35           C  
ANISOU 3521  CG1 ILE B  71    12174   9123   9232    -98   1214   1328       C  
ATOM   3522  CG2 ILE B  71      57.268  31.362 118.512  1.00 81.26           C  
ANISOU 3522  CG2 ILE B  71    12241   9463   9171   -169   1221   1119       C  
ATOM   3523  CD1 ILE B  71      56.244  33.991 119.343  1.00 80.90           C  
ANISOU 3523  CD1 ILE B  71    12241   9222   9275   -112   1158   1497       C  
ATOM   3524  N   GLY B  72      60.367  33.018 121.659  1.00 79.30           N  
ANISOU 3524  N   GLY B  72    12011   8891   9227    -53   1315   1090       N  
ATOM   3525  CA  GLY B  72      61.197  34.060 122.273  1.00 79.10           C  
ANISOU 3525  CA  GLY B  72    11995   8818   9241    -83   1347   1129       C  
ATOM   3526  C   GLY B  72      62.665  33.703 122.473  1.00 79.02           C  
ANISOU 3526  C   GLY B  72    11929   8867   9226   -101   1390   1035       C  
ATOM   3527  O   GLY B  72      63.103  32.625 122.074  1.00 79.28           O  
ANISOU 3527  O   GLY B  72    11910   8967   9244    -81   1407    936       O  
ATOM   3528  N   PRO B  73      63.439  34.617 123.097  1.00 79.08           N  
ANISOU 3528  N   PRO B  73    11941   8848   9258   -145   1419   1063       N  
ATOM   3529  CA  PRO B  73      64.865  34.425 123.358  1.00 79.24           C  
ANISOU 3529  CA  PRO B  73    11895   8938   9273   -173   1456    997       C  
ATOM   3530  C   PRO B  73      65.129  33.712 124.685  1.00 78.88           C  
ANISOU 3530  C   PRO B  73    11805   8854   9310   -121   1430    954       C  
ATOM   3531  O   PRO B  73      64.190  33.237 125.334  1.00 78.28           O  
ANISOU 3531  O   PRO B  73    11753   8700   9290    -63   1386    960       O  
ATOM   3532  CB  PRO B  73      65.378  35.865 123.431  1.00 79.88           C  
ANISOU 3532  CB  PRO B  73    12009   9009   9332   -265   1494   1062       C  
ATOM   3533  CG  PRO B  73      64.252  36.601 124.071  1.00 79.51           C  
ANISOU 3533  CG  PRO B  73    12035   8822   9352   -255   1479   1132       C  
ATOM   3534  CD  PRO B  73      62.983  35.929 123.604  1.00 79.28           C  
ANISOU 3534  CD  PRO B  73    12025   8768   9326   -180   1429   1156       C  
ATOM   3535  N   GLN B  74      66.402  33.640 125.074  1.00 79.40           N  
ANISOU 3535  N   GLN B  74    11796   8990   9380   -151   1455    926       N  
ATOM   3536  CA  GLN B  74      66.784  33.231 126.429  1.00 78.85           C  
ANISOU 3536  CA  GLN B  74    11668   8917   9373   -136   1424    928       C  
ATOM   3537  C   GLN B  74      66.264  34.251 127.434  1.00 77.50           C  
ANISOU 3537  C   GLN B  74    11566   8678   9200   -203   1415    967       C  
ATOM   3538  O   GLN B  74      66.100  35.426 127.103  1.00 77.58           O  
ANISOU 3538  O   GLN B  74    11646   8651   9177   -272   1455    990       O  
ATOM   3539  CB  GLN B  74      68.306  33.114 126.572  1.00 80.21           C  
ANISOU 3539  CB  GLN B  74    11731   9205   9540   -173   1452    915       C  
ATOM   3540  CG  GLN B  74      68.915  31.933 125.836  1.00 81.20           C  
ANISOU 3540  CG  GLN B  74    11757   9380   9712    -96   1478    861       C  
ATOM   3541  CD  GLN B  74      70.411  31.798 126.064  1.00 82.46           C  
ANISOU 3541  CD  GLN B  74    11787   9652   9891   -121   1507    864       C  
ATOM   3542  OE1 GLN B  74      70.917  32.042 127.164  1.00 82.48           O  
ANISOU 3542  OE1 GLN B  74    11736   9700   9900   -165   1473    922       O  
ATOM   3543  NE2 GLN B  74      71.129  31.397 125.018  1.00 83.64           N  
ANISOU 3543  NE2 GLN B  74    11872   9862  10043   -104   1573    801       N  
ATOM   3544  N   THR B  75      66.014  33.790 128.656  1.00 76.40           N  
ANISOU 3544  N   THR B  75    11400   8523   9103   -191   1372    973       N  
ATOM   3545  CA  THR B  75      65.441  34.629 129.710  1.00 75.22           C  
ANISOU 3545  CA  THR B  75    11311   8315   8954   -266   1377    980       C  
ATOM   3546  C   THR B  75      66.245  34.526 130.992  1.00 74.46           C  
ANISOU 3546  C   THR B  75    11134   8319   8837   -349   1358    982       C  
ATOM   3547  O   THR B  75      67.026  33.594 131.170  1.00 75.05           O  
ANISOU 3547  O   THR B  75    11098   8490   8927   -312   1319   1008       O  
ATOM   3548  CB  THR B  75      63.993  34.205 130.027  1.00 74.91           C  
ANISOU 3548  CB  THR B  75    11327   8170   8965   -194   1337    986       C  
ATOM   3549  OG1 THR B  75      63.971  32.846 130.487  1.00 73.93           O  
ANISOU 3549  OG1 THR B  75    11131   8079   8879   -119   1273    992       O  
ATOM   3550  CG2 THR B  75      63.110  34.338 128.796  1.00 75.34           C  
ANISOU 3550  CG2 THR B  75    11449   8149   9026   -129   1346   1003       C  
ATOM   3551  N   TYR B  76      66.026  35.482 131.892  1.00 73.57           N  
ANISOU 3551  N   TYR B  76    11068   8187   8698   -468   1392    959       N  
ATOM   3552  CA  TYR B  76      66.527  35.383 133.265  1.00 73.47           C  
ANISOU 3552  CA  TYR B  76    10983   8289   8642   -577   1368    960       C  
ATOM   3553  C   TYR B  76      65.946  34.131 133.925  1.00 73.27           C  
ANISOU 3553  C   TYR B  76    10905   8276   8655   -494   1281   1004       C  
ATOM   3554  O   TYR B  76      64.899  33.631 133.497  1.00 72.83           O  
ANISOU 3554  O   TYR B  76    10905   8107   8661   -378   1259   1004       O  
ATOM   3555  CB  TYR B  76      66.102  36.600 134.089  1.00 73.12           C  
ANISOU 3555  CB  TYR B  76    11016   8197   8568   -729   1442    893       C  
ATOM   3556  CG  TYR B  76      66.769  37.906 133.719  1.00 73.22           C  
ANISOU 3556  CG  TYR B  76    11070   8198   8550   -847   1540    849       C  
ATOM   3557  CD1 TYR B  76      68.144  38.081 133.870  1.00 73.75           C  
ANISOU 3557  CD1 TYR B  76    11055   8427   8539   -955   1547    853       C  
ATOM   3558  CD2 TYR B  76      66.018  38.985 133.248  1.00 72.86           C  
ANISOU 3558  CD2 TYR B  76    11138   7975   8568   -857   1631    816       C  
ATOM   3559  CE1 TYR B  76      68.753  39.286 133.541  1.00 74.21           C  
ANISOU 3559  CE1 TYR B  76    11155   8471   8569  -1076   1642    809       C  
ATOM   3560  CE2 TYR B  76      66.617  40.190 132.917  1.00 73.35           C  
ANISOU 3560  CE2 TYR B  76    11238   8006   8623   -968   1729    786       C  
ATOM   3561  CZ  TYR B  76      67.982  40.339 133.065  1.00 73.95           C  
ANISOU 3561  CZ  TYR B  76    11243   8244   8608  -1082   1736    774       C  
ATOM   3562  OH  TYR B  76      68.571  41.535 132.736  1.00 74.55           O  
ANISOU 3562  OH  TYR B  76    11360   8286   8678  -1203   1837    742       O  
ATOM   3563  N   PHE B  77      66.610  33.629 134.964  1.00 73.98           N  
ANISOU 3563  N   PHE B  77    10882   8515   8710   -562   1228   1054       N  
ATOM   3564  CA  PHE B  77      66.037  32.523 135.750  1.00 74.00           C  
ANISOU 3564  CA  PHE B  77    10830   8534   8751   -508   1144   1116       C  
ATOM   3565  C   PHE B  77      64.635  32.846 136.313  1.00 73.47           C  
ANISOU 3565  C   PHE B  77    10869   8363   8681   -534   1156   1062       C  
ATOM   3566  O   PHE B  77      63.707  32.022 136.205  1.00 73.06           O  
ANISOU 3566  O   PHE B  77    10838   8224   8696   -418   1110   1084       O  
ATOM   3567  CB  PHE B  77      66.979  32.116 136.887  1.00 75.15           C  
ANISOU 3567  CB  PHE B  77    10825   8885   8842   -613   1082   1206       C  
ATOM   3568  CG  PHE B  77      66.564  30.859 137.591  1.00 75.38           C  
ANISOU 3568  CG  PHE B  77    10772   8941   8929   -546    987   1311       C  
ATOM   3569  CD1 PHE B  77      66.944  29.616 137.098  1.00 75.59           C  
ANISOU 3569  CD1 PHE B  77    10696   8945   9080   -387    939   1404       C  
ATOM   3570  CD2 PHE B  77      65.779  30.913 138.741  1.00 75.65           C  
ANISOU 3570  CD2 PHE B  77    10826   9015   8902   -649    956   1312       C  
ATOM   3571  CE1 PHE B  77      66.554  28.449 137.743  1.00 76.11           C  
ANISOU 3571  CE1 PHE B  77    10682   9013   9222   -323    858   1515       C  
ATOM   3572  CE2 PHE B  77      65.385  29.752 139.389  1.00 75.77           C  
ANISOU 3572  CE2 PHE B  77    10762   9057   8968   -595    865   1425       C  
ATOM   3573  CZ  PHE B  77      65.775  28.519 138.892  1.00 76.05           C  
ANISOU 3573  CZ  PHE B  77    10696   9056   9140   -428    813   1535       C  
ATOM   3574  N   HIS B  78      64.486  34.044 136.885  1.00 73.76           N  
ANISOU 3574  N   HIS B  78    10969   8402   8652   -690   1229    982       N  
ATOM   3575  CA  HIS B  78      63.223  34.465 137.524  1.00 73.56           C  
ANISOU 3575  CA  HIS B  78    11030   8282   8635   -735   1266    914       C  
ATOM   3576  C   HIS B  78      62.049  34.517 136.537  1.00 72.65           C  
ANISOU 3576  C   HIS B  78    11019   7964   8619   -582   1289    896       C  
ATOM   3577  O   HIS B  78      60.929  34.127 136.882  1.00 72.32           O  
ANISOU 3577  O   HIS B  78    11009   7854   8613   -535   1265    891       O  
ATOM   3578  CB  HIS B  78      63.381  35.816 138.268  1.00 74.64           C  
ANISOU 3578  CB  HIS B  78    11209   8444   8704   -945   1375    805       C  
ATOM   3579  CG  HIS B  78      63.182  37.028 137.405  1.00 74.85           C  
ANISOU 3579  CG  HIS B  78    11341   8302   8794   -938   1492    735       C  
ATOM   3580  ND1 HIS B  78      64.225  37.717 136.824  1.00 75.21           N  
ANISOU 3580  ND1 HIS B  78    11383   8379   8815   -993   1542    728       N  
ATOM   3581  CD2 HIS B  78      62.052  37.675 137.028  1.00 74.93           C  
ANISOU 3581  CD2 HIS B  78    11452   8112   8903   -883   1567    689       C  
ATOM   3582  CE1 HIS B  78      63.745  38.731 136.124  1.00 75.30           C  
ANISOU 3582  CE1 HIS B  78    11491   8210   8908   -973   1642    687       C  
ATOM   3583  NE2 HIS B  78      62.429  38.726 136.230  1.00 74.67           N  
ANISOU 3583  NE2 HIS B  78    11471   7987   8912   -902   1658    670       N  
ATOM   3584  N   THR B  79      62.321  34.997 135.320  1.00 72.43           N  
ANISOU 3584  N   THR B  79    11033   7862   8624   -519   1331    897       N  
ATOM   3585  CA  THR B  79      61.317  35.109 134.258  1.00 71.81           C  
ANISOU 3585  CA  THR B  79    11034   7628   8621   -392   1346    906       C  
ATOM   3586  C   THR B  79      60.756  33.739 133.904  1.00 71.69           C  
ANISOU 3586  C   THR B  79    10993   7606   8639   -250   1255    954       C  
ATOM   3587  O   THR B  79      59.538  33.554 133.838  1.00 70.74           O  
ANISOU 3587  O   THR B  79    10922   7392   8564   -185   1243    954       O  
ATOM   3588  CB  THR B  79      61.920  35.725 132.977  1.00 71.63           C  
ANISOU 3588  CB  THR B  79    11034   7579   8599   -369   1390    924       C  
ATOM   3589  OG1 THR B  79      62.560  36.966 133.288  1.00 72.23           O  
ANISOU 3589  OG1 THR B  79    11132   7659   8653   -509   1480    880       O  
ATOM   3590  CG2 THR B  79      60.849  35.957 131.909  1.00 71.06           C  
ANISOU 3590  CG2 THR B  79    11033   7377   8590   -267   1402    958       C  
ATOM   3591  N   CYS B  80      61.662  32.791 133.681  1.00 73.01           N  
ANISOU 3591  N   CYS B  80    11075   7869   8796   -205   1202    992       N  
ATOM   3592  CA  CYS B  80      61.289  31.419 133.365  1.00 73.74           C  
ANISOU 3592  CA  CYS B  80    11130   7946   8940    -80   1135   1025       C  
ATOM   3593  C   CYS B  80      60.618  30.746 134.557  1.00 73.56           C  
ANISOU 3593  C   CYS B  80    11083   7932   8932    -91   1077   1049       C  
ATOM   3594  O   CYS B  80      59.633  30.023 134.382  1.00 72.76           O  
ANISOU 3594  O   CYS B  80    11009   7757   8879     -5   1042   1055       O  
ATOM   3595  CB  CYS B  80      62.516  30.619 132.924  1.00 75.54           C  
ANISOU 3595  CB  CYS B  80    11257   8258   9188    -36   1117   1054       C  
ATOM   3596  SG  CYS B  80      62.127  28.999 132.222  1.00 76.56           S  
ANISOU 3596  SG  CYS B  80    11346   8326   9415    117   1080   1062       S  
ATOM   3597  N   LEU B  81      61.138  30.993 135.761  1.00 74.59           N  
ANISOU 3597  N   LEU B  81    11160   8169   9010   -212   1066   1066       N  
ATOM   3598  CA  LEU B  81      60.505  30.476 136.978  1.00 75.08           C  
ANISOU 3598  CA  LEU B  81    11195   8268   9061   -257   1013   1094       C  
ATOM   3599  C   LEU B  81      59.060  30.974 137.148  1.00 74.69           C  
ANISOU 3599  C   LEU B  81    11251   8105   9023   -261   1048   1028       C  
ATOM   3600  O   LEU B  81      58.175  30.183 137.474  1.00 74.28           O  
ANISOU 3600  O   LEU B  81    11200   8020   9002   -208    997   1052       O  
ATOM   3601  CB  LEU B  81      61.335  30.827 138.220  1.00 76.40           C  
ANISOU 3601  CB  LEU B  81    11284   8608   9135   -430   1004   1117       C  
ATOM   3602  CG  LEU B  81      60.864  30.281 139.577  1.00 76.98           C  
ANISOU 3602  CG  LEU B  81    11305   8776   9165   -515    942   1165       C  
ATOM   3603  CD1 LEU B  81      60.720  28.767 139.537  1.00 77.10           C  
ANISOU 3603  CD1 LEU B  81    11244   8780   9269   -383    844   1284       C  
ATOM   3604  CD2 LEU B  81      61.822  30.689 140.688  1.00 78.03           C  
ANISOU 3604  CD2 LEU B  81    11346   9125   9177   -716    934   1193       C  
ATOM   3605  N   MET B  82      58.833  32.270 136.925  1.00 74.87           N  
ANISOU 3605  N   MET B  82    11351   8059   9034   -320   1140    953       N  
ATOM   3606  CA  MET B  82      57.481  32.860 137.029  1.00 74.67           C  
ANISOU 3606  CA  MET B  82    11411   7908   9052   -314   1193    898       C  
ATOM   3607  C   MET B  82      56.492  32.280 136.018  1.00 73.96           C  
ANISOU 3607  C   MET B  82    11361   7709   9032   -154   1156    932       C  
ATOM   3608  O   MET B  82      55.342  31.998 136.358  1.00 72.96           O  
ANISOU 3608  O   MET B  82    11258   7527   8935   -124   1141    925       O  
ATOM   3609  CB  MET B  82      57.525  34.378 136.841  1.00 75.78           C  
ANISOU 3609  CB  MET B  82    11614   7968   9212   -391   1315    828       C  
ATOM   3610  CG  MET B  82      57.955  35.133 138.078  1.00 77.45           C  
ANISOU 3610  CG  MET B  82    11810   8256   9360   -586   1386    745       C  
ATOM   3611  SD  MET B  82      58.270  36.876 137.787  1.00 79.15           S  
ANISOU 3611  SD  MET B  82    12090   8362   9620   -688   1549    657       S  
ATOM   3612  CE  MET B  82      58.732  37.405 139.439  1.00 80.10           C  
ANISOU 3612  CE  MET B  82    12177   8620   9634   -950   1623    532       C  
ATOM   3613  N   VAL B  83      56.948  32.128 134.775  1.00 73.91           N  
ANISOU 3613  N   VAL B  83    11355   7687   9038    -70   1148    964       N  
ATOM   3614  CA  VAL B  83      56.116  31.616 133.677  1.00 73.01           C  
ANISOU 3614  CA  VAL B  83    11273   7504   8964     51   1118    991       C  
ATOM   3615  C   VAL B  83      55.756  30.131 133.866  1.00 71.97           C  
ANISOU 3615  C   VAL B  83    11102   7393   8848    121   1037   1011       C  
ATOM   3616  O   VAL B  83      54.706  29.684 133.399  1.00 71.04           O  
ANISOU 3616  O   VAL B  83    11014   7219   8756    190   1013   1016       O  
ATOM   3617  CB  VAL B  83      56.799  31.861 132.305  1.00 73.49           C  
ANISOU 3617  CB  VAL B  83    11336   7575   9008     87   1140   1007       C  
ATOM   3618  CG1 VAL B  83      56.047  31.179 131.161  1.00 73.51           C  
ANISOU 3618  CG1 VAL B  83    11356   7554   9021    182   1106   1027       C  
ATOM   3619  CG2 VAL B  83      56.903  33.361 132.030  1.00 73.83           C  
ANISOU 3619  CG2 VAL B  83    11425   7567   9058     28   1222   1009       C  
ATOM   3620  N   ALA B  84      56.608  29.380 134.561  1.00 71.57           N  
ANISOU 3620  N   ALA B  84    10977   7423   8790     97    997   1034       N  
ATOM   3621  CA  ALA B  84      56.347  27.964 134.829  1.00 71.39           C  
ANISOU 3621  CA  ALA B  84    10906   7404   8814    160    928   1070       C  
ATOM   3622  C   ALA B  84      55.203  27.679 135.817  1.00 71.13           C  
ANISOU 3622  C   ALA B  84    10891   7350   8784    137    892   1077       C  
ATOM   3623  O   ALA B  84      54.648  26.585 135.785  1.00 72.02           O  
ANISOU 3623  O   ALA B  84    10989   7429   8944    201    844   1101       O  
ATOM   3624  CB  ALA B  84      57.619  27.285 135.308  1.00 72.14           C  
ANISOU 3624  CB  ALA B  84    10894   7588   8927    146    896   1127       C  
ATOM   3625  N   CYS B  85      54.845  28.640 136.668  1.00 70.96           N  
ANISOU 3625  N   CYS B  85    10899   7344   8718     38    927   1046       N  
ATOM   3626  CA  CYS B  85      53.904  28.399 137.787  1.00 70.56           C  
ANISOU 3626  CA  CYS B  85    10850   7304   8655    -14    901   1044       C  
ATOM   3627  C   CYS B  85      52.381  28.382 137.497  1.00 69.01           C  
ANISOU 3627  C   CYS B  85    10717   7006   8496     46    908   1015       C  
ATOM   3628  O   CYS B  85      51.674  27.561 138.087  1.00 69.43           O  
ANISOU 3628  O   CYS B  85    10755   7068   8557     51    856   1037       O  
ATOM   3629  CB  CYS B  85      54.192  29.390 138.927  1.00 71.88           C  
ANISOU 3629  CB  CYS B  85    11009   7548   8751   -174    953    999       C  
ATOM   3630  SG  CYS B  85      55.867  29.288 139.600  1.00 73.68           S  
ANISOU 3630  SG  CYS B  85    11136   7952   8907   -286    924   1054       S  
ATOM   3631  N   PRO B  86      51.864  29.287 136.632  1.00 68.06           N  
ANISOU 3631  N   PRO B  86    10655   6798   8403     87    969    983       N  
ATOM   3632  CA  PRO B  86      50.414  29.317 136.348  1.00 66.98           C  
ANISOU 3632  CA  PRO B  86    10559   6582   8308    143    972    977       C  
ATOM   3633  C   PRO B  86      49.774  27.957 136.050  1.00 65.78           C  
ANISOU 3633  C   PRO B  86    10395   6429   8167    219    891   1009       C  
ATOM   3634  O   PRO B  86      48.711  27.634 136.600  1.00 65.61           O  
ANISOU 3634  O   PRO B  86    10379   6391   8156    216    871   1004       O  
ATOM   3635  CB  PRO B  86      50.325  30.231 135.126  1.00 67.23           C  
ANISOU 3635  CB  PRO B  86    10625   6547   8370    194   1023    991       C  
ATOM   3636  CG  PRO B  86      51.438  31.199 135.326  1.00 67.93           C  
ANISOU 3636  CG  PRO B  86    10713   6652   8442    118   1089    966       C  
ATOM   3637  CD  PRO B  86      52.536  30.468 136.055  1.00 68.27           C  
ANISOU 3637  CD  PRO B  86    10707   6804   8429     62   1043    963       C  
ATOM   3638  N   VAL B  87      50.438  27.168 135.207  1.00 64.84           N  
ANISOU 3638  N   VAL B  87    10258   6326   8051    276    857   1030       N  
ATOM   3639  CA  VAL B  87      49.989  25.801 134.901  1.00 63.38           C  
ANISOU 3639  CA  VAL B  87    10059   6128   7893    335    800   1041       C  
ATOM   3640  C   VAL B  87      49.935  24.915 136.156  1.00 62.38           C  
ANISOU 3640  C   VAL B  87     9890   6028   7783    301    749   1073       C  
ATOM   3641  O   VAL B  87      48.995  24.129 136.309  1.00 62.35           O  
ANISOU 3641  O   VAL B  87     9893   5997   7801    322    712   1079       O  
ATOM   3642  CB  VAL B  87      50.847  25.150 133.786  1.00 63.44           C  
ANISOU 3642  CB  VAL B  87    10047   6140   7917    388    804   1031       C  
ATOM   3643  CG1 VAL B  87      52.259  24.829 134.268  1.00 63.74           C  
ANISOU 3643  CG1 VAL B  87    10019   6218   7979    371    802   1057       C  
ATOM   3644  CG2 VAL B  87      50.161  23.905 133.233  1.00 63.62           C  
ANISOU 3644  CG2 VAL B  87    10070   6127   7973    437    777   1011       C  
ATOM   3645  N   LEU B  88      50.912  25.073 137.056  1.00 61.31           N  
ANISOU 3645  N   LEU B  88     9705   5960   7629    234    743   1105       N  
ATOM   3646  CA  LEU B  88      50.953  24.327 138.327  1.00 60.57           C  
ANISOU 3646  CA  LEU B  88     9552   5926   7534    177    686   1168       C  
ATOM   3647  C   LEU B  88      49.765  24.685 139.209  1.00 59.96           C  
ANISOU 3647  C   LEU B  88     9507   5861   7414    108    688   1140       C  
ATOM   3648  O   LEU B  88      49.131  23.800 139.790  1.00 60.14           O  
ANISOU 3648  O   LEU B  88     9508   5889   7450    101    635   1180       O  
ATOM   3649  CB  LEU B  88      52.252  24.581 139.103  1.00 60.42           C  
ANISOU 3649  CB  LEU B  88     9460   6017   7478     93    678   1220       C  
ATOM   3650  CG  LEU B  88      53.572  24.332 138.379  1.00 60.67           C  
ANISOU 3650  CG  LEU B  88     9440   6055   7555    148    684   1252       C  
ATOM   3651  CD1 LEU B  88      54.748  24.634 139.293  1.00 61.46           C  
ANISOU 3651  CD1 LEU B  88     9454   6293   7604     45    667   1319       C  
ATOM   3652  CD2 LEU B  88      53.638  22.907 137.858  1.00 61.01           C  
ANISOU 3652  CD2 LEU B  88     9440   6026   7714    256    650   1300       C  
ATOM   3653  N   ILE B  89      49.460  25.979 139.283  1.00 59.75           N  
ANISOU 3653  N   ILE B  89     9525   5826   7351     58    760   1068       N  
ATOM   3654  CA  ILE B  89      48.284  26.462 140.024  1.00 59.86           C  
ANISOU 3654  CA  ILE B  89     9566   5832   7346     -1    793   1017       C  
ATOM   3655  C   ILE B  89      47.014  25.889 139.394  1.00 59.56           C  
ANISOU 3655  C   ILE B  89     9559   5714   7354     93    766   1020       C  
ATOM   3656  O   ILE B  89      46.196  25.228 140.064  1.00 59.70           O  
ANISOU 3656  O   ILE B  89     9566   5752   7366     69    727   1032       O  
ATOM   3657  CB  ILE B  89      48.194  28.016 140.029  1.00 59.77           C  
ANISOU 3657  CB  ILE B  89     9592   5782   7333    -52    904    932       C  
ATOM   3658  CG1 ILE B  89      49.412  28.630 140.742  1.00 60.45           C  
ANISOU 3658  CG1 ILE B  89     9648   5963   7355   -179    941    909       C  
ATOM   3659  CG2 ILE B  89      46.902  28.493 140.689  1.00 59.68           C  
ANISOU 3659  CG2 ILE B  89     9600   5738   7339    -97    960    867       C  
ATOM   3660  CD1 ILE B  89      49.705  30.060 140.360  1.00 61.01           C  
ANISOU 3660  CD1 ILE B  89     9759   5970   7452   -207   1055    836       C  
ATOM   3661  N   LEU B  90      46.872  26.133 138.094  1.00 59.78           N  
ANISOU 3661  N   LEU B  90     9621   5672   7419    188    785   1015       N  
ATOM   3662  CA  LEU B  90      45.633  25.805 137.391  1.00 59.91           C  
ANISOU 3662  CA  LEU B  90     9661   5636   7463    259    767   1017       C  
ATOM   3663  C   LEU B  90      45.351  24.308 137.382  1.00 60.27           C  
ANISOU 3663  C   LEU B  90     9691   5689   7517    287    691   1046       C  
ATOM   3664  O   LEU B  90      44.211  23.895 137.634  1.00 60.38           O  
ANISOU 3664  O   LEU B  90     9710   5695   7534    287    668   1044       O  
ATOM   3665  CB  LEU B  90      45.657  26.367 135.967  1.00 59.80           C  
ANISOU 3665  CB  LEU B  90     9672   5585   7464    329    795   1025       C  
ATOM   3666  CG  LEU B  90      45.663  27.898 135.891  1.00 60.03           C  
ANISOU 3666  CG  LEU B  90     9714   5573   7518    313    879   1016       C  
ATOM   3667  CD1 LEU B  90      45.927  28.335 134.468  1.00 60.25           C  
ANISOU 3667  CD1 LEU B  90     9753   5588   7549    370    890   1056       C  
ATOM   3668  CD2 LEU B  90      44.363  28.489 136.410  1.00 60.35           C  
ANISOU 3668  CD2 LEU B  90     9754   5568   7608    306    921   1003       C  
ATOM   3669  N   THR B  91      46.389  23.507 137.125  1.00 61.09           N  
ANISOU 3669  N   THR B  91     9769   5801   7639    308    663   1072       N  
ATOM   3670  CA  THR B  91      46.269  22.042 137.187  1.00 61.30           C  
ANISOU 3670  CA  THR B  91     9771   5807   7711    333    609   1101       C  
ATOM   3671  C   THR B  91      45.870  21.577 138.589  1.00 61.49           C  
ANISOU 3671  C   THR B  91     9763   5870   7728    264    564   1149       C  
ATOM   3672  O   THR B  91      45.028  20.688 138.721  1.00 61.31           O  
ANISOU 3672  O   THR B  91     9743   5821   7730    272    528   1162       O  
ATOM   3673  CB  THR B  91      47.572  21.324 136.766  1.00 61.71           C  
ANISOU 3673  CB  THR B  91     9781   5844   7822    371    607   1126       C  
ATOM   3674  OG1 THR B  91      47.979  21.783 135.474  1.00 62.23           O  
ANISOU 3674  OG1 THR B  91     9873   5894   7876    414    654   1073       O  
ATOM   3675  CG2 THR B  91      47.371  19.809 136.706  1.00 62.09           C  
ANISOU 3675  CG2 THR B  91     9802   5831   7958    405    577   1149       C  
ATOM   3676  N   GLN B  92      46.462  22.178 139.624  1.00 61.80           N  
ANISOU 3676  N   GLN B  92     9771   5987   7722    181    568   1174       N  
ATOM   3677  CA  GLN B  92      46.095  21.842 141.003  1.00 62.24           C  
ANISOU 3677  CA  GLN B  92     9789   6119   7740     83    528   1221       C  
ATOM   3678  C   GLN B  92      44.651  22.223 141.317  1.00 61.94           C  
ANISOU 3678  C   GLN B  92     9791   6073   7668     52    550   1159       C  
ATOM   3679  O   GLN B  92      43.934  21.447 141.960  1.00 62.33           O  
ANISOU 3679  O   GLN B  92     9824   6145   7714     17    503   1195       O  
ATOM   3680  CB  GLN B  92      47.050  22.485 142.021  1.00 62.78           C  
ANISOU 3680  CB  GLN B  92     9808   6307   7738    -32    535   1247       C  
ATOM   3681  CG  GLN B  92      46.928  21.910 143.429  1.00 63.41           C  
ANISOU 3681  CG  GLN B  92     9823   6505   7764   -154    475   1330       C  
ATOM   3682  CD  GLN B  92      47.146  20.401 143.473  1.00 63.74           C  
ANISOU 3682  CD  GLN B  92     9804   6519   7891   -100    389   1468       C  
ATOM   3683  OE1 GLN B  92      48.166  19.889 142.994  1.00 63.79           O  
ANISOU 3683  OE1 GLN B  92     9765   6492   7980    -30    371   1539       O  
ATOM   3684  NE2 GLN B  92      46.177  19.682 144.033  1.00 63.67           N  
ANISOU 3684  NE2 GLN B  92     9792   6515   7883   -132    346   1504       N  
ATOM   3685  N   SER B  93      44.222  23.399 140.854  1.00 61.97           N  
ANISOU 3685  N   SER B  93     9838   6042   7663     68    623   1078       N  
ATOM   3686  CA  SER B  93      42.809  23.804 141.003  1.00 62.03           C  
ANISOU 3686  CA  SER B  93     9869   6026   7671     62    657   1026       C  
ATOM   3687  C   SER B  93      41.837  22.761 140.443  1.00 61.64           C  
ANISOU 3687  C   SER B  93     9830   5936   7651    129    601   1051       C  
ATOM   3688  O   SER B  93      40.836  22.419 141.093  1.00 61.71           O  
ANISOU 3688  O   SER B  93     9830   5969   7646     87    585   1046       O  
ATOM   3689  CB  SER B  93      42.549  25.171 140.355  1.00 62.10           C  
ANISOU 3689  CB  SER B  93     9908   5974   7712    100    747    967       C  
ATOM   3690  OG  SER B  93      41.244  25.633 140.663  1.00 62.29           O  
ANISOU 3690  OG  SER B  93     9931   5974   7760     91    793    925       O  
ATOM   3691  N   SER B  94      42.148  22.247 139.255  1.00 61.73           N  
ANISOU 3691  N   SER B  94     9858   5898   7698    216    579   1067       N  
ATOM   3692  CA  SER B  94      41.313  21.230 138.603  1.00 62.03           C  
ANISOU 3692  CA  SER B  94     9907   5903   7757    260    538   1072       C  
ATOM   3693  C   SER B  94      41.073  19.998 139.481  1.00 62.31           C  
ANISOU 3693  C   SER B  94     9918   5949   7806    215    480   1116       C  
ATOM   3694  O   SER B  94      39.929  19.534 139.623  1.00 62.88           O  
ANISOU 3694  O   SER B  94     9996   6023   7872    200    458   1109       O  
ATOM   3695  CB  SER B  94      41.937  20.789 137.272  1.00 62.19           C  
ANISOU 3695  CB  SER B  94     9941   5883   7803    327    540   1062       C  
ATOM   3696  OG  SER B  94      42.169  21.905 136.429  1.00 62.42           O  
ANISOU 3696  OG  SER B  94     9987   5916   7812    359    585   1043       O  
ATOM   3697  N   ILE B  95      42.153  19.504 140.089  1.00 61.86           N  
ANISOU 3697  N   ILE B  95     9824   5907   7773    188    453   1177       N  
ATOM   3698  CA  ILE B  95      42.124  18.276 140.890  1.00 61.70           C  
ANISOU 3698  CA  ILE B  95     9763   5889   7790    150    393   1259       C  
ATOM   3699  C   ILE B  95      41.203  18.478 142.096  1.00 61.66           C  
ANISOU 3699  C   ILE B  95     9746   5967   7713     50    375   1268       C  
ATOM   3700  O   ILE B  95      40.297  17.664 142.345  1.00 62.48           O  
ANISOU 3700  O   ILE B  95     9851   6059   7829     30    340   1288       O  
ATOM   3701  CB  ILE B  95      43.545  17.867 141.356  1.00 62.14           C  
ANISOU 3701  CB  ILE B  95     9754   5962   7891    140    367   1357       C  
ATOM   3702  CG1 ILE B  95      44.447  17.560 140.152  1.00 62.14           C  
ANISOU 3702  CG1 ILE B  95     9757   5873   7979    239    398   1335       C  
ATOM   3703  CG2 ILE B  95      43.502  16.654 142.276  1.00 62.91           C  
ANISOU 3703  CG2 ILE B  95     9792   6067   8042     95    300   1482       C  
ATOM   3704  CD1 ILE B  95      45.933  17.664 140.432  1.00 62.64           C  
ANISOU 3704  CD1 ILE B  95     9754   5969   8074    240    395   1410       C  
ATOM   3705  N   LEU B  96      41.423  19.584 142.809  1.00 60.87           N  
ANISOU 3705  N   LEU B  96     9637   5951   7538    -23    411   1239       N  
ATOM   3706  CA  LEU B  96      40.623  19.930 143.995  1.00 60.65           C  
ANISOU 3706  CA  LEU B  96     9593   6018   7433   -141    420   1217       C  
ATOM   3707  C   LEU B  96      39.155  20.211 143.637  1.00 59.75           C  
ANISOU 3707  C   LEU B  96     9515   5864   7322   -110    455   1137       C  
ATOM   3708  O   LEU B  96      38.228  19.773 144.353  1.00 59.52           O  
ANISOU 3708  O   LEU B  96     9470   5881   7262   -176    433   1143       O  
ATOM   3709  CB  LEU B  96      41.244  21.125 144.729  1.00 61.14           C  
ANISOU 3709  CB  LEU B  96     9637   6170   7420   -240    479   1169       C  
ATOM   3710  CG  LEU B  96      42.665  20.888 145.280  1.00 61.98           C  
ANISOU 3710  CG  LEU B  96     9687   6364   7497   -304    436   1264       C  
ATOM   3711  CD1 LEU B  96      43.303  22.197 145.729  1.00 62.09           C  
ANISOU 3711  CD1 LEU B  96     9697   6457   7436   -400    513   1185       C  
ATOM   3712  CD2 LEU B  96      42.664  19.866 146.415  1.00 62.84           C  
ANISOU 3712  CD2 LEU B  96     9726   6584   7565   -411    349   1392       C  
ATOM   3713  N   ALA B  97      38.952  20.914 142.520  1.00 59.03           N  
ANISOU 3713  N   ALA B  97     9460   5698   7269    -14    505   1078       N  
ATOM   3714  CA  ALA B  97      37.609  21.115 141.963  1.00 58.91           C  
ANISOU 3714  CA  ALA B  97     9459   5649   7273     33    527   1036       C  
ATOM   3715  C   ALA B  97      36.903  19.785 141.666  1.00 58.97           C  
ANISOU 3715  C   ALA B  97     9471   5641   7292     50    457   1073       C  
ATOM   3716  O   ALA B  97      35.726  19.618 142.003  1.00 58.85           O  
ANISOU 3716  O   ALA B  97     9444   5652   7260     19    453   1058       O  
ATOM   3717  CB  ALA B  97      37.671  21.975 140.709  1.00 58.74           C  
ANISOU 3717  CB  ALA B  97     9460   5567   7290    130    573   1012       C  
ATOM   3718  N   LEU B  98      37.621  18.841 141.053  1.00 59.15           N  
ANISOU 3718  N   LEU B  98     9504   5615   7352     92    414   1113       N  
ATOM   3719  CA  LEU B  98      37.069  17.499 140.809  1.00 59.50           C  
ANISOU 3719  CA  LEU B  98     9554   5625   7428     94    364   1137       C  
ATOM   3720  C   LEU B  98      36.781  16.734 142.110  1.00 59.83           C  
ANISOU 3720  C   LEU B  98     9565   5709   7459      2    317   1200       C  
ATOM   3721  O   LEU B  98      35.715  16.093 142.252  1.00 59.49           O  
ANISOU 3721  O   LEU B  98     9523   5671   7409    -28    293   1199       O  
ATOM   3722  CB  LEU B  98      38.001  16.682 139.908  1.00 60.00           C  
ANISOU 3722  CB  LEU B  98     9628   5607   7562    152    358   1148       C  
ATOM   3723  CG  LEU B  98      38.048  17.102 138.440  1.00 59.98           C  
ANISOU 3723  CG  LEU B  98     9656   5579   7552    220    396   1082       C  
ATOM   3724  CD1 LEU B  98      39.333  16.615 137.778  1.00 60.41           C  
ANISOU 3724  CD1 LEU B  98     9711   5569   7673    264    414   1079       C  
ATOM   3725  CD2 LEU B  98      36.824  16.590 137.692  1.00 60.02           C  
ANISOU 3725  CD2 LEU B  98     9678   5592   7535    212    388   1038       C  
ATOM   3726  N   LEU B  99      37.724  16.807 143.055  1.00 60.19           N  
ANISOU 3726  N   LEU B  99     9574   5802   7493    -52    301   1266       N  
ATOM   3727  CA  LEU B  99      37.534  16.197 144.378  1.00 60.90           C  
ANISOU 3727  CA  LEU B  99     9619   5969   7550   -163    250   1351       C  
ATOM   3728  C   LEU B  99      36.299  16.754 145.096  1.00 61.18           C  
ANISOU 3728  C   LEU B  99     9652   6093   7497   -247    274   1287       C  
ATOM   3729  O   LEU B  99      35.535  15.983 145.702  1.00 61.74           O  
ANISOU 3729  O   LEU B  99     9707   6199   7552   -314    233   1329       O  
ATOM   3730  CB  LEU B  99      38.784  16.363 145.251  1.00 61.30           C  
ANISOU 3730  CB  LEU B  99     9615   6100   7576   -228    227   1440       C  
ATOM   3731  CG  LEU B  99      38.763  15.734 146.653  1.00 62.46           C  
ANISOU 3731  CG  LEU B  99     9695   6364   7672   -366    162   1565       C  
ATOM   3732  CD1 LEU B  99      38.640  14.214 146.600  1.00 62.89           C  
ANISOU 3732  CD1 LEU B  99     9726   6332   7836   -339     95   1691       C  
ATOM   3733  CD2 LEU B  99      40.005  16.151 147.423  1.00 63.26           C  
ANISOU 3733  CD2 LEU B  99     9732   6584   7718   -447    144   1646       C  
ATOM   3734  N   ALA B 100      36.097  18.075 145.017  1.00 60.98           N  
ANISOU 3734  N   ALA B 100     9641   6095   7433   -243    350   1187       N  
ATOM   3735  CA  ALA B 100      34.859  18.694 145.529  1.00 61.28           C  
ANISOU 3735  CA  ALA B 100     9669   6189   7424   -300    402   1106       C  
ATOM   3736  C   ALA B 100      33.596  18.080 144.892  1.00 61.36           C  
ANISOU 3736  C   ALA B 100     9692   6155   7464   -247    379   1096       C  
ATOM   3737  O   ALA B 100      32.635  17.719 145.602  1.00 61.55           O  
ANISOU 3737  O   ALA B 100     9694   6241   7450   -326    367   1093       O  
ATOM   3738  CB  ALA B 100      34.883  20.201 145.319  1.00 61.12           C  
ANISOU 3738  CB  ALA B 100     9655   6154   7411   -274    506   1005       C  
ATOM   3739  N   ILE B 101      33.622  17.942 143.562  1.00 61.19           N  
ANISOU 3739  N   ILE B 101     9703   6047   7500   -133    373   1091       N  
ATOM   3740  CA  ILE B 101      32.525  17.313 142.809  1.00 61.02           C  
ANISOU 3740  CA  ILE B 101     9690   6002   7493    -97    348   1082       C  
ATOM   3741  C   ILE B 101      32.286  15.881 143.279  1.00 60.98           C  
ANISOU 3741  C   ILE B 101     9684   5995   7489   -161    280   1139       C  
ATOM   3742  O   ILE B 101      31.133  15.491 143.498  1.00 60.64           O  
ANISOU 3742  O   ILE B 101     9629   5989   7421   -206    266   1128       O  
ATOM   3743  CB  ILE B 101      32.778  17.320 141.276  1.00 60.88           C  
ANISOU 3743  CB  ILE B 101     9701   5919   7511      3    350   1068       C  
ATOM   3744  CG1 ILE B 101      32.709  18.751 140.729  1.00 60.30           C  
ANISOU 3744  CG1 ILE B 101     9617   5850   7443     67    413   1036       C  
ATOM   3745  CG2 ILE B 101      31.765  16.433 140.537  1.00 61.14           C  
ANISOU 3745  CG2 ILE B 101     9741   5952   7538      2    317   1059       C  
ATOM   3746  CD1 ILE B 101      33.247  18.908 139.321  1.00 59.86           C  
ANISOU 3746  CD1 ILE B 101     9584   5756   7404    146    415   1038       C  
ATOM   3747  N   ALA B 102      33.366  15.109 143.428  1.00 61.57           N  
ANISOU 3747  N   ALA B 102     9763   6021   7608   -164    243   1209       N  
ATOM   3748  CA  ALA B 102      33.256  13.719 143.925  1.00 62.52           C  
ANISOU 3748  CA  ALA B 102     9872   6114   7767   -222    185   1291       C  
ATOM   3749  C   ALA B 102      32.590  13.624 145.305  1.00 63.17           C  
ANISOU 3749  C   ALA B 102     9916   6308   7778   -346    158   1335       C  
ATOM   3750  O   ALA B 102      31.639  12.845 145.491  1.00 63.09           O  
ANISOU 3750  O   ALA B 102     9904   6302   7763   -396    131   1349       O  
ATOM   3751  CB  ALA B 102      34.621  13.045 143.952  1.00 62.84           C  
ANISOU 3751  CB  ALA B 102     9898   6079   7898   -195    161   1384       C  
ATOM   3752  N   VAL B 103      33.076  14.422 146.261  1.00 63.67           N  
ANISOU 3752  N   VAL B 103     9946   6471   7771   -414    172   1348       N  
ATOM   3753  CA  VAL B 103      32.473  14.433 147.609  1.00 64.54           C  
ANISOU 3753  CA  VAL B 103    10014   6720   7787   -561    159   1371       C  
ATOM   3754  C   VAL B 103      31.041  14.992 147.606  1.00 64.82           C  
ANISOU 3754  C   VAL B 103    10052   6801   7774   -579    212   1256       C  
ATOM   3755  O   VAL B 103      30.197  14.522 148.377  1.00 64.59           O  
ANISOU 3755  O   VAL B 103     9996   6851   7692   -682    191   1274       O  
ATOM   3756  CB  VAL B 103      33.349  15.128 148.688  1.00 65.05           C  
ANISOU 3756  CB  VAL B 103    10035   6913   7768   -668    171   1398       C  
ATOM   3757  CG1 VAL B 103      34.718  14.463 148.769  1.00 65.48           C  
ANISOU 3757  CG1 VAL B 103    10062   6941   7876   -655    105   1548       C  
ATOM   3758  CG2 VAL B 103      33.494  16.625 148.457  1.00 65.08           C  
ANISOU 3758  CG2 VAL B 103    10054   6929   7742   -639    270   1259       C  
ATOM   3759  N   ASP B 104      30.761  15.970 146.738  1.00 65.49           N  
ANISOU 3759  N   ASP B 104    10157   6839   7886   -480    280   1153       N  
ATOM   3760  CA  ASP B 104      29.371  16.440 146.561  1.00 66.17           C  
ANISOU 3760  CA  ASP B 104    10227   6951   7962   -470    329   1070       C  
ATOM   3761  C   ASP B 104      28.466  15.323 146.024  1.00 66.80           C  
ANISOU 3761  C   ASP B 104    10318   7004   8059   -458    270   1102       C  
ATOM   3762  O   ASP B 104      27.363  15.123 146.533  1.00 66.52           O  
ANISOU 3762  O   ASP B 104    10251   7038   7983   -528    272   1083       O  
ATOM   3763  CB  ASP B 104      29.291  17.659 145.638  1.00 65.96           C  
ANISOU 3763  CB  ASP B 104    10203   6870   7988   -355    406    996       C  
ATOM   3764  CG  ASP B 104      27.888  18.247 145.572  1.00 66.30           C  
ANISOU 3764  CG  ASP B 104    10201   6945   8045   -342    464    934       C  
ATOM   3765  OD1 ASP B 104      27.391  18.726 146.614  1.00 67.15           O  
ANISOU 3765  OD1 ASP B 104    10267   7125   8122   -432    527    875       O  
ATOM   3766  OD2 ASP B 104      27.278  18.220 144.484  1.00 65.91           O  
ANISOU 3766  OD2 ASP B 104    10147   6860   8035   -251    451    946       O  
ATOM   3767  N   ARG B 105      28.940  14.608 145.001  1.00 67.75           N  
ANISOU 3767  N   ARG B 105    10478   7027   8237   -382    230   1136       N  
ATOM   3768  CA  ARG B 105      28.239  13.415 144.496  1.00 69.03           C  
ANISOU 3768  CA  ARG B 105    10656   7152   8418   -395    183   1155       C  
ATOM   3769  C   ARG B 105      28.058  12.339 145.576  1.00 70.39           C  
ANISOU 3769  C   ARG B 105    10814   7351   8577   -512    131   1234       C  
ATOM   3770  O   ARG B 105      27.000  11.705 145.648  1.00 70.65           O  
ANISOU 3770  O   ARG B 105    10840   7411   8590   -568    111   1229       O  
ATOM   3771  CB  ARG B 105      28.972  12.801 143.292  1.00 69.27           C  
ANISOU 3771  CB  ARG B 105    10731   7066   8519   -317    172   1157       C  
ATOM   3772  CG  ARG B 105      28.767  13.516 141.963  1.00 69.09           C  
ANISOU 3772  CG  ARG B 105    10719   7041   8491   -228    207   1090       C  
ATOM   3773  CD  ARG B 105      27.311  13.496 141.512  1.00 69.36           C  
ANISOU 3773  CD  ARG B 105    10728   7147   8478   -250    203   1054       C  
ATOM   3774  NE  ARG B 105      26.647  14.790 141.676  1.00 68.69           N  
ANISOU 3774  NE  ARG B 105    10590   7140   8366   -218    243   1037       N  
ATOM   3775  CZ  ARG B 105      25.383  15.038 141.339  1.00 68.95           C  
ANISOU 3775  CZ  ARG B 105    10574   7251   8372   -220    248   1026       C  
ATOM   3776  NH1 ARG B 105      24.604  14.084 140.832  1.00 69.53           N  
ANISOU 3776  NH1 ARG B 105    10648   7356   8411   -272    207   1021       N  
ATOM   3777  NH2 ARG B 105      24.883  16.250 141.527  1.00 69.36           N  
ANISOU 3777  NH2 ARG B 105    10565   7345   8442   -176    300   1021       N  
ATOM   3778  N   TYR B 106      29.086  12.130 146.402  1.00 71.17           N  
ANISOU 3778  N   TYR B 106    10901   7454   8686   -555    104   1322       N  
ATOM   3779  CA  TYR B 106      28.977  11.215 147.550  1.00 72.01           C  
ANISOU 3779  CA  TYR B 106    10975   7611   8773   -680     47   1434       C  
ATOM   3780  C   TYR B 106      27.900  11.659 148.544  1.00 72.96           C  
ANISOU 3780  C   TYR B 106    11056   7887   8777   -799     63   1393       C  
ATOM   3781  O   TYR B 106      26.988  10.889 148.853  1.00 73.22           O  
ANISOU 3781  O   TYR B 106    11079   7948   8791   -873     33   1419       O  
ATOM   3782  CB  TYR B 106      30.325  11.089 148.266  1.00 72.14           C  
ANISOU 3782  CB  TYR B 106    10961   7640   8809   -711     12   1559       C  
ATOM   3783  CG  TYR B 106      30.299  10.221 149.502  1.00 72.80           C  
ANISOU 3783  CG  TYR B 106    10992   7803   8866   -852    -56   1714       C  
ATOM   3784  CD1 TYR B 106      30.207   8.835 149.396  1.00 73.59           C  
ANISOU 3784  CD1 TYR B 106    11091   7792   9076   -857   -106   1829       C  
ATOM   3785  CD2 TYR B 106      30.372  10.782 150.781  1.00 73.03           C  
ANISOU 3785  CD2 TYR B 106    10964   8022   8759   -995    -65   1748       C  
ATOM   3786  CE1 TYR B 106      30.185   8.028 150.527  1.00 74.86           C  
ANISOU 3786  CE1 TYR B 106    11194   8026   9224   -988   -175   2002       C  
ATOM   3787  CE2 TYR B 106      30.351   9.984 151.916  1.00 74.48           C  
ANISOU 3787  CE2 TYR B 106    11089   8309   8900  -1143   -137   1912       C  
ATOM   3788  CZ  TYR B 106      30.258   8.607 151.783  1.00 75.24           C  
ANISOU 3788  CZ  TYR B 106    11182   8288   9118  -1133   -198   2054       C  
ATOM   3789  OH  TYR B 106      30.233   7.801 152.894  1.00 76.42           O  
ANISOU 3789  OH  TYR B 106    11263   8536   9237  -1280   -275   2247       O  
ATOM   3790  N   LEU B 107      28.010  12.897 149.029  1.00 73.76           N  
ANISOU 3790  N   LEU B 107    11133   8083   8807   -822    123   1318       N  
ATOM   3791  CA  LEU B 107      27.093  13.423 150.061  1.00 74.66           C  
ANISOU 3791  CA  LEU B 107    11200   8349   8816   -949    166   1254       C  
ATOM   3792  C   LEU B 107      25.603  13.344 149.696  1.00 74.97           C  
ANISOU 3792  C   LEU B 107    11230   8398   8854   -936    190   1179       C  
ATOM   3793  O   LEU B 107      24.778  13.051 150.563  1.00 75.50           O  
ANISOU 3793  O   LEU B 107    11260   8575   8849  -1062    187   1179       O  
ATOM   3794  CB  LEU B 107      27.451  14.870 150.427  1.00 74.66           C  
ANISOU 3794  CB  LEU B 107    11179   8412   8774   -961    262   1145       C  
ATOM   3795  CG  LEU B 107      28.734  15.060 151.240  1.00 75.05           C  
ANISOU 3795  CG  LEU B 107    11212   8536   8766  -1052    247   1207       C  
ATOM   3796  CD1 LEU B 107      29.180  16.514 151.199  1.00 74.78           C  
ANISOU 3796  CD1 LEU B 107    11177   8509   8726  -1028    356   1077       C  
ATOM   3797  CD2 LEU B 107      28.561  14.591 152.676  1.00 76.23           C  
ANISOU 3797  CD2 LEU B 107    11306   8869   8789  -1264    210   1274       C  
ATOM   3798  N   ARG B 108      25.268  13.598 148.430  1.00 75.08           N  
ANISOU 3798  N   ARG B 108    11269   8316   8939   -797    211   1125       N  
ATOM   3799  CA  ARG B 108      23.870  13.543 147.961  1.00 75.60           C  
ANISOU 3799  CA  ARG B 108    11310   8407   9004   -780    227   1072       C  
ATOM   3800  C   ARG B 108      23.239  12.174 148.211  1.00 76.18           C  
ANISOU 3800  C   ARG B 108    11391   8498   9054   -873    154   1137       C  
ATOM   3801  O   ARG B 108      22.191  12.068 148.858  1.00 76.28           O  
ANISOU 3801  O   ARG B 108    11360   8613   9008   -966    164   1114       O  
ATOM   3802  CB  ARG B 108      23.779  13.880 146.468  1.00 74.96           C  
ANISOU 3802  CB  ARG B 108    11249   8242   8990   -633    238   1042       C  
ATOM   3803  CG  ARG B 108      24.031  15.346 146.155  1.00 74.79           C  
ANISOU 3803  CG  ARG B 108    11203   8206   9006   -539    321    982       C  
ATOM   3804  CD  ARG B 108      24.306  15.563 144.677  1.00 74.54           C  
ANISOU 3804  CD  ARG B 108    11195   8095   9028   -408    312    992       C  
ATOM   3805  NE  ARG B 108      23.120  15.313 143.867  1.00 74.94           N  
ANISOU 3805  NE  ARG B 108    11210   8187   9075   -386    293    994       N  
ATOM   3806  CZ  ARG B 108      22.100  16.157 143.694  1.00 75.40           C  
ANISOU 3806  CZ  ARG B 108    11189   8303   9156   -347    343    976       C  
ATOM   3807  NH1 ARG B 108      22.080  17.362 144.274  1.00 75.56           N  
ANISOU 3807  NH1 ARG B 108    11160   8321   9226   -318    435    935       N  
ATOM   3808  NH2 ARG B 108      21.081  15.784 142.920  1.00 75.85           N  
ANISOU 3808  NH2 ARG B 108    11205   8419   9194   -341    307    999       N  
ATOM   3809  N   VAL B 109      23.893  11.138 147.695  1.00 76.65           N  
ANISOU 3809  N   VAL B 109    11501   8449   9172   -848     93   1212       N  
ATOM   3810  CA  VAL B 109      23.445   9.757 147.884  1.00 77.95           C  
ANISOU 3810  CA  VAL B 109    11679   8590   9348   -934     34   1282       C  
ATOM   3811  C   VAL B 109      23.670   9.239 149.322  1.00 79.23           C  
ANISOU 3811  C   VAL B 109    11810   8828   9463  -1077     -7   1391       C  
ATOM   3812  O   VAL B 109      22.891   8.410 149.804  1.00 80.56           O  
ANISOU 3812  O   VAL B 109    11965   9038   9605  -1183    -41   1436       O  
ATOM   3813  CB  VAL B 109      24.067   8.794 146.827  1.00 78.17           C  
ANISOU 3813  CB  VAL B 109    11765   8451   9485   -866      9   1311       C  
ATOM   3814  CG1 VAL B 109      25.574   8.625 147.002  1.00 78.27           C  
ANISOU 3814  CG1 VAL B 109    11793   8368   9575   -824     -6   1399       C  
ATOM   3815  CG2 VAL B 109      23.388   7.432 146.869  1.00 79.37           C  
ANISOU 3815  CG2 VAL B 109    11930   8559   9666   -956    -25   1353       C  
ATOM   3816  N   LYS B 110      24.715   9.721 150.000  1.00 78.84           N  
ANISOU 3816  N   LYS B 110    11744   8814   9395  -1095     -8   1443       N  
ATOM   3817  CA  LYS B 110      25.031   9.254 151.358  1.00 79.65           C  
ANISOU 3817  CA  LYS B 110    11803   9024   9435  -1249    -59   1573       C  
ATOM   3818  C   LYS B 110      24.086   9.825 152.422  1.00 80.55           C  
ANISOU 3818  C   LYS B 110    11862   9338   9403  -1395    -22   1506       C  
ATOM   3819  O   LYS B 110      23.617   9.082 153.284  1.00 82.19           O  
ANISOU 3819  O   LYS B 110    12038   9638   9551  -1540    -69   1594       O  
ATOM   3820  CB  LYS B 110      26.491   9.568 151.716  1.00 79.52           C  
ANISOU 3820  CB  LYS B 110    11772   9009   9430  -1239    -76   1659       C  
ATOM   3821  CG  LYS B 110      26.965   9.050 153.072  1.00 80.77           C  
ANISOU 3821  CG  LYS B 110    11866   9301   9518  -1408   -145   1835       C  
ATOM   3822  CD  LYS B 110      26.990   7.530 153.150  1.00 81.83           C  
ANISOU 3822  CD  LYS B 110    11994   9339   9758  -1436   -229   2023       C  
ATOM   3823  CE  LYS B 110      27.406   7.061 154.532  1.00 83.30           C  
ANISOU 3823  CE  LYS B 110    12098   9686   9867  -1615   -307   2233       C  
ATOM   3824  NZ  LYS B 110      27.441   5.577 154.619  1.00 84.51           N  
ANISOU 3824  NZ  LYS B 110    12233   9720  10157  -1636   -383   2443       N  
ATOM   3825  N   ILE B 111      23.825  11.134 152.370  1.00 80.58           N  
ANISOU 3825  N   ILE B 111    11852   9402   9363  -1361     69   1352       N  
ATOM   3826  CA  ILE B 111      22.972  11.810 153.364  1.00 81.75           C  
ANISOU 3826  CA  ILE B 111    11940   9727   9393  -1497    139   1252       C  
ATOM   3827  C   ILE B 111      21.894  12.672 152.682  1.00 82.78           C  
ANISOU 3827  C   ILE B 111    12055   9834   9563  -1398    234   1090       C  
ATOM   3828  O   ILE B 111      21.884  13.899 152.829  1.00 82.55           O  
ANISOU 3828  O   ILE B 111    11996   9835   9532  -1378    341    965       O  
ATOM   3829  CB  ILE B 111      23.811  12.626 154.389  1.00 81.60           C  
ANISOU 3829  CB  ILE B 111    11886   9841   9277  -1613    183   1230       C  
ATOM   3830  CG1 ILE B 111      24.802  13.578 153.699  1.00 80.67           C  
ANISOU 3830  CG1 ILE B 111    11800   9620   9231  -1475    234   1170       C  
ATOM   3831  CG2 ILE B 111      24.575  11.683 155.306  1.00 82.22           C  
ANISOU 3831  CG2 ILE B 111    11940  10011   9286  -1761     76   1425       C  
ATOM   3832  CD1 ILE B 111      25.349  14.666 154.594  1.00 81.25           C  
ANISOU 3832  CD1 ILE B 111    11836   9824   9209  -1591    322   1077       C  
ATOM   3833  N   PRO B 112      20.963  12.025 151.948  1.00 84.57           N  
ANISOU 3833  N   PRO B 112    12291  10007   9833  -1344    201   1098       N  
ATOM   3834  CA  PRO B 112      19.944  12.768 151.190  1.00 86.02           C  
ANISOU 3834  CA  PRO B 112    12441  10176  10064  -1240    274    986       C  
ATOM   3835  C   PRO B 112      18.974  13.603 152.043  1.00 88.93           C  
ANISOU 3835  C   PRO B 112    12725  10680  10384  -1325    381    868       C  
ATOM   3836  O   PRO B 112      18.532  14.664 151.592  1.00 89.73           O  
ANISOU 3836  O   PRO B 112    12781  10754  10558  -1223    477    772       O  
ATOM   3837  CB  PRO B 112      19.195  11.666 150.426  1.00 85.42           C  
ANISOU 3837  CB  PRO B 112    12385  10057  10010  -1222    199   1039       C  
ATOM   3838  CG  PRO B 112      19.412  10.431 151.221  1.00 85.59           C  
ANISOU 3838  CG  PRO B 112    12431  10107   9982  -1364    117   1151       C  
ATOM   3839  CD  PRO B 112      20.769  10.566 151.843  1.00 85.04           C  
ANISOU 3839  CD  PRO B 112    12380  10026   9902  -1393    100   1219       C  
ATOM   3840  N   LEU B 113      18.661  13.141 153.254  1.00 92.07           N  
ANISOU 3840  N   LEU B 113    13092  11218  10670  -1512    371    880       N  
ATOM   3841  CA  LEU B 113      17.754  13.864 154.154  1.00 94.73           C  
ANISOU 3841  CA  LEU B 113    13344  11696  10952  -1620    488    749       C  
ATOM   3842  C   LEU B 113      18.365  15.168 154.675  1.00 96.39           C  
ANISOU 3842  C   LEU B 113    13529  11926  11166  -1638    618    624       C  
ATOM   3843  O   LEU B 113      17.692  16.197 154.704  1.00 97.80           O  
ANISOU 3843  O   LEU B 113    13642  12108  11409  -1601    759    480       O  
ATOM   3844  CB  LEU B 113      17.340  12.974 155.332  1.00 96.31           C  
ANISOU 3844  CB  LEU B 113    13519  12062  11010  -1843    439    801       C  
ATOM   3845  CG  LEU B 113      16.521  11.729 154.973  1.00 96.80           C  
ANISOU 3845  CG  LEU B 113    13594  12116  11069  -1858    337    899       C  
ATOM   3846  CD1 LEU B 113      16.480  10.751 156.140  1.00 97.87           C  
ANISOU 3846  CD1 LEU B 113    13719  12394  11072  -2081    265   1002       C  
ATOM   3847  CD2 LEU B 113      15.113  12.113 154.537  1.00 96.98           C  
ANISOU 3847  CD2 LEU B 113    13547  12164  11134  -1801    408    795       C  
ATOM   3848  N   ARG B 114      19.635  15.113 155.075  1.00 97.75           N  
ANISOU 3848  N   ARG B 114    13747  12109  11284  -1696    577    681       N  
ATOM   3849  CA  ARG B 114      20.367  16.276 155.599  1.00 99.52           C  
ANISOU 3849  CA  ARG B 114    13957  12364  11492  -1742    695    563       C  
ATOM   3850  C   ARG B 114      21.212  17.036 154.550  1.00 99.01           C  
ANISOU 3850  C   ARG B 114    13939  12120  11560  -1544    721    552       C  
ATOM   3851  O   ARG B 114      21.845  18.049 154.887  1.00 99.29           O  
ANISOU 3851  O   ARG B 114    13967  12159  11599  -1574    828    448       O  
ATOM   3852  CB  ARG B 114      21.249  15.831 156.779  1.00101.52           C  
ANISOU 3852  CB  ARG B 114    14211  12783  11578  -1962    637    636       C  
ATOM   3853  CG  ARG B 114      20.450  15.416 158.015  1.00103.95           C  
ANISOU 3853  CG  ARG B 114    14455  13309  11730  -2202    651    612       C  
ATOM   3854  CD  ARG B 114      21.203  14.458 158.939  1.00105.24           C  
ANISOU 3854  CD  ARG B 114    14616  13633  11735  -2400    519    794       C  
ATOM   3855  NE  ARG B 114      22.466  15.016 159.443  1.00106.16           N  
ANISOU 3855  NE  ARG B 114    14732  13828  11776  -2490    536    795       N  
ATOM   3856  CZ  ARG B 114      23.697  14.708 159.015  1.00105.63           C  
ANISOU 3856  CZ  ARG B 114    14707  13676  11752  -2405    434    949       C  
ATOM   3857  NH1 ARG B 114      23.909  13.817 158.043  1.00104.50           N  
ANISOU 3857  NH1 ARG B 114    14618  13348  11739  -2222    312   1109       N  
ATOM   3858  NH2 ARG B 114      24.747  15.309 159.576  1.00106.20           N  
ANISOU 3858  NH2 ARG B 114    14762  13855  11734  -2516    463    932       N  
ATOM   3859  N   TYR B 115      21.208  16.577 153.293  1.00 98.77           N  
ANISOU 3859  N   TYR B 115    13953  11945  11630  -1361    635    647       N  
ATOM   3860  CA  TYR B 115      22.042  17.182 152.234  1.00 98.16           C  
ANISOU 3860  CA  TYR B 115    13920  11711  11662  -1183    643    658       C  
ATOM   3861  C   TYR B 115      21.871  18.694 152.114  1.00 98.87           C  
ANISOU 3861  C   TYR B 115    13966  11748  11851  -1113    809    511       C  
ATOM   3862  O   TYR B 115      22.856  19.426 152.148  1.00 98.76           O  
ANISOU 3862  O   TYR B 115    13977  11689  11856  -1100    861    473       O  
ATOM   3863  CB  TYR B 115      21.774  16.542 150.862  1.00 96.97           C  
ANISOU 3863  CB  TYR B 115    13805  11443  11593  -1020    550    751       C  
ATOM   3864  CG  TYR B 115      22.546  17.202 149.728  1.00 95.69           C  
ANISOU 3864  CG  TYR B 115    13681  11143  11534   -848    564    759       C  
ATOM   3865  CD1 TYR B 115      23.935  17.086 149.645  1.00 95.17           C  
ANISOU 3865  CD1 TYR B 115    13675  11027  11457   -836    519    813       C  
ATOM   3866  CD2 TYR B 115      21.892  17.953 148.749  1.00 95.19           C  
ANISOU 3866  CD2 TYR B 115    13580  11010  11577   -704    620    729       C  
ATOM   3867  CE1 TYR B 115      24.649  17.694 148.619  1.00 93.87           C  
ANISOU 3867  CE1 TYR B 115    13543  10746  11376   -691    534    818       C  
ATOM   3868  CE2 TYR B 115      22.598  18.558 147.715  1.00 94.27           C  
ANISOU 3868  CE2 TYR B 115    13492  10783  11543   -562    628    752       C  
ATOM   3869  CZ  TYR B 115      23.976  18.429 147.656  1.00 93.36           C  
ANISOU 3869  CZ  TYR B 115    13447  10618  11406   -558    588    786       C  
ATOM   3870  OH  TYR B 115      24.683  19.028 146.637  1.00 92.48           O  
ANISOU 3870  OH  TYR B 115    13362  10405  11368   -428    598    806       O  
ATOM   3871  N   LYS B 116      20.628  19.149 151.977  1.00100.16           N  
ANISOU 3871  N   LYS B 116    14056  11910  12090  -1070    896    437       N  
ATOM   3872  CA  LYS B 116      20.346  20.577 151.755  1.00101.39           C  
ANISOU 3872  CA  LYS B 116    14152  11978  12394   -976   1067    318       C  
ATOM   3873  C   LYS B 116      20.752  21.463 152.935  1.00102.52           C  
ANISOU 3873  C   LYS B 116    14272  12177  12503  -1129   1224    152       C  
ATOM   3874  O   LYS B 116      21.228  22.580 152.724  1.00102.51           O  
ANISOU 3874  O   LYS B 116    14265  12069  12613  -1063   1346     71       O  
ATOM   3875  CB  LYS B 116      18.877  20.811 151.383  1.00102.62           C  
ANISOU 3875  CB  LYS B 116    14209  12124  12656   -895   1126    298       C  
ATOM   3876  CG  LYS B 116      18.557  20.424 149.945  1.00102.36           C  
ANISOU 3876  CG  LYS B 116    14181  12015  12693   -717   1013    441       C  
ATOM   3877  CD  LYS B 116      17.148  20.822 149.554  1.00103.53           C  
ANISOU 3877  CD  LYS B 116    14207  12169  12960   -632   1078    440       C  
ATOM   3878  CE  LYS B 116      16.846  20.458 148.107  1.00102.89           C  
ANISOU 3878  CE  LYS B 116    14120  12052  12920   -485    960    590       C  
ATOM   3879  NZ  LYS B 116      16.816  18.986 147.878  1.00102.12           N  
ANISOU 3879  NZ  LYS B 116    14095  12033  12673   -557    792    671       N  
ATOM   3880  N   MET B 117      20.571  20.974 154.161  1.00103.91           N  
ANISOU 3880  N   MET B 117    14431  12527  12520  -1346   1227    100       N  
ATOM   3881  CA  MET B 117      21.056  21.699 155.343  1.00105.87           C  
ANISOU 3881  CA  MET B 117    14660  12874  12689  -1541   1368    -62       C  
ATOM   3882  C   MET B 117      22.583  21.606 155.511  1.00104.27           C  
ANISOU 3882  C   MET B 117    14531  12698  12385  -1606   1293      0       C  
ATOM   3883  O   MET B 117      23.194  22.540 156.033  1.00105.45           O  
ANISOU 3883  O   MET B 117    14675  12864  12525  -1700   1427   -138       O  
ATOM   3884  CB  MET B 117      20.317  21.277 156.629  1.00108.63           C  
ANISOU 3884  CB  MET B 117    14952  13437  12884  -1781   1406   -144       C  
ATOM   3885  CG  MET B 117      20.550  19.854 157.127  1.00109.50           C  
ANISOU 3885  CG  MET B 117    15098  13709  12798  -1921   1210     23       C  
ATOM   3886  SD  MET B 117      20.195  19.673 158.890  1.00113.02           S  
ANISOU 3886  SD  MET B 117    15477  14453  13012  -2276   1279    -88       S  
ATOM   3887  CE  MET B 117      21.594  20.532 159.612  1.00113.78           C  
ANISOU 3887  CE  MET B 117    15590  14633  13007  -2442   1368   -190       C  
ATOM   3888  N   VAL B 118      23.194  20.499 155.074  1.00101.55           N  
ANISOU 3888  N   VAL B 118    14249  12355  11978  -1561   1093    198       N  
ATOM   3889  CA  VAL B 118      24.665  20.351 155.139  1.00 99.62           C  
ANISOU 3889  CA  VAL B 118    14060  12127  11661  -1598   1012    284       C  
ATOM   3890  C   VAL B 118      25.385  21.193 154.071  1.00 97.59           C  
ANISOU 3890  C   VAL B 118    13845  11680  11552  -1404   1055    271       C  
ATOM   3891  O   VAL B 118      26.126  22.116 154.410  1.00 97.07           O  
ANISOU 3891  O   VAL B 118    13781  11618  11481  -1467   1160    167       O  
ATOM   3892  CB  VAL B 118      25.110  18.865 155.054  1.00 98.97           C  
ANISOU 3892  CB  VAL B 118    14016  12090  11497  -1610    801    508       C  
ATOM   3893  CG1 VAL B 118      26.626  18.732 154.893  1.00 98.40           C  
ANISOU 3893  CG1 VAL B 118    13986  11998  11401  -1596    720    618       C  
ATOM   3894  CG2 VAL B 118      24.651  18.099 156.293  1.00100.20           C  
ANISOU 3894  CG2 VAL B 118    14125  12460  11485  -1843    757    543       C  
ATOM   3895  N   VAL B 119      25.172  20.858 152.797  1.00 95.99           N  
ANISOU 3895  N   VAL B 119    13674  11328  11467  -1191    975    374       N  
ATOM   3896  CA  VAL B 119      25.872  21.497 151.671  1.00 94.63           C  
ANISOU 3896  CA  VAL B 119    13543  10991  11421  -1009    987    396       C  
ATOM   3897  C   VAL B 119      25.139  22.764 151.215  1.00 94.17           C  
ANISOU 3897  C   VAL B 119    13435  10813  11529   -897   1151    279       C  
ATOM   3898  O   VAL B 119      24.225  22.701 150.389  1.00 93.63           O  
ANISOU 3898  O   VAL B 119    13337  10673  11562   -758   1137    325       O  
ATOM   3899  CB  VAL B 119      26.034  20.518 150.478  1.00 93.93           C  
ANISOU 3899  CB  VAL B 119    13505  10816  11368   -854    828    560       C  
ATOM   3900  CG1 VAL B 119      26.773  21.187 149.315  1.00 93.53           C  
ANISOU 3900  CG1 VAL B 119    13491  10619  11427   -686    842    582       C  
ATOM   3901  CG2 VAL B 119      26.754  19.249 150.923  1.00 93.84           C  
ANISOU 3901  CG2 VAL B 119    13528  10886  11240   -950    683    687       C  
ATOM   3902  N   THR B 120      25.556  23.909 151.754  1.00 94.27           N  
ANISOU 3902  N   THR B 120    13431  10807  11577   -965   1312    134       N  
ATOM   3903  CA  THR B 120      24.937  25.203 151.458  1.00 94.50           C  
ANISOU 3903  CA  THR B 120    13402  10701  11801   -870   1499     17       C  
ATOM   3904  C   THR B 120      25.802  26.033 150.503  1.00 93.78           C  
ANISOU 3904  C   THR B 120    13348  10447  11837   -723   1529     51       C  
ATOM   3905  O   THR B 120      27.026  25.843 150.456  1.00 93.34           O  
ANISOU 3905  O   THR B 120    13360  10412  11690   -758   1455     95       O  
ATOM   3906  CB  THR B 120      24.703  26.017 152.747  1.00 96.14           C  
ANISOU 3906  CB  THR B 120    13558  10977  11994  -1062   1704   -204       C  
ATOM   3907  OG1 THR B 120      25.947  26.226 153.428  1.00 95.90           O  
ANISOU 3907  OG1 THR B 120    13576  11028  11833  -1225   1721   -266       O  
ATOM   3908  CG2 THR B 120      23.744  25.289 153.670  1.00 97.01           C  
ANISOU 3908  CG2 THR B 120    13620  11255  11984  -1213   1690   -245       C  
ATOM   3909  N   PRO B 121      25.173  26.965 149.751  1.00 93.74           N  
ANISOU 3909  N   PRO B 121    13286  10282  12046   -562   1639     44       N  
ATOM   3910  CA  PRO B 121      25.889  27.846 148.818  1.00 93.64           C  
ANISOU 3910  CA  PRO B 121    13296  10109  12173   -423   1680     88       C  
ATOM   3911  C   PRO B 121      27.149  28.499 149.394  1.00 94.37           C  
ANISOU 3911  C   PRO B 121    13442  10193  12220   -541   1768    -25       C  
ATOM   3912  O   PRO B 121      28.200  28.481 148.746  1.00 94.26           O  
ANISOU 3912  O   PRO B 121    13492  10141  12179   -483   1686     60       O  
ATOM   3913  CB  PRO B 121      24.845  28.910 148.481  1.00 94.73           C  
ANISOU 3913  CB  PRO B 121    13328  10099  12563   -301   1848     54       C  
ATOM   3914  CG  PRO B 121      23.549  28.195 148.584  1.00 94.60           C  
ANISOU 3914  CG  PRO B 121    13245  10171  12528   -291   1794     93       C  
ATOM   3915  CD  PRO B 121      23.713  27.180 149.676  1.00 94.15           C  
ANISOU 3915  CD  PRO B 121    13236  10302  12232   -494   1718     26       C  
ATOM   3916  N   ARG B 122      27.038  29.056 150.601  1.00 95.97           N  
ANISOU 3916  N   ARG B 122    13615  10446  12403   -720   1937   -223       N  
ATOM   3917  CA  ARG B 122      28.177  29.699 151.274  1.00 96.85           C  
ANISOU 3917  CA  ARG B 122    13767  10583  12448   -878   2037   -357       C  
ATOM   3918  C   ARG B 122      29.313  28.705 151.558  1.00 94.00           C  
ANISOU 3918  C   ARG B 122    13478  10396  11841   -989   1848   -262       C  
ATOM   3919  O   ARG B 122      30.492  29.017 151.336  1.00 93.47           O  
ANISOU 3919  O   ARG B 122    13459  10307  11745   -999   1832   -245       O  
ATOM   3920  CB  ARG B 122      27.725  30.390 152.575  1.00100.78           C  
ANISOU 3920  CB  ARG B 122    14209  11135  12947  -1087   2264   -610       C  
ATOM   3921  CG  ARG B 122      28.730  31.384 153.143  1.00103.48           C  
ANISOU 3921  CG  ARG B 122    14577  11462  13279  -1244   2431   -788       C  
ATOM   3922  CD  ARG B 122      28.221  32.030 154.426  1.00106.78           C  
ANISOU 3922  CD  ARG B 122    14935  11945  13689  -1477   2675  -1067       C  
ATOM   3923  NE  ARG B 122      28.125  31.063 155.524  1.00108.26           N  
ANISOU 3923  NE  ARG B 122    15115  12421  13594  -1711   2581  -1092       N  
ATOM   3924  CZ  ARG B 122      29.152  30.594 156.242  1.00109.12           C  
ANISOU 3924  CZ  ARG B 122    15263  12758  13437  -1929   2484  -1083       C  
ATOM   3925  NH1 ARG B 122      30.408  30.987 156.009  1.00109.41           N  
ANISOU 3925  NH1 ARG B 122    15352  12775  13440  -1950   2468  -1065       N  
ATOM   3926  NH2 ARG B 122      28.920  29.711 157.213  1.00109.48           N  
ANISOU 3926  NH2 ARG B 122    15283  13065  13246  -2135   2397  -1075       N  
ATOM   3927  N   ARG B 123      28.953  27.507 152.021  1.00 91.63           N  
ANISOU 3927  N   ARG B 123    13174  10259  11381  -1066   1705   -186       N  
ATOM   3928  CA  ARG B 123      29.935  26.447 152.273  1.00 89.42           C  
ANISOU 3928  CA  ARG B 123    12940  10131  10903  -1153   1518    -56       C  
ATOM   3929  C   ARG B 123      30.583  25.966 150.976  1.00 86.40           C  
ANISOU 3929  C   ARG B 123    12613   9640  10573   -951   1364    127       C  
ATOM   3930  O   ARG B 123      31.796  25.742 150.934  1.00 85.91           O  
ANISOU 3930  O   ARG B 123    12589   9620  10431   -982   1286    194       O  
ATOM   3931  CB  ARG B 123      29.299  25.278 153.028  1.00 89.45           C  
ANISOU 3931  CB  ARG B 123    12918  10310  10758  -1273   1410      0       C  
ATOM   3932  CG  ARG B 123      29.131  25.548 154.519  1.00 91.18           C  
ANISOU 3932  CG  ARG B 123    13089  10720  10835  -1550   1525   -162       C  
ATOM   3933  CD  ARG B 123      28.236  24.520 155.186  1.00 91.69           C  
ANISOU 3933  CD  ARG B 123    13116  10939  10782  -1654   1442   -112       C  
ATOM   3934  NE  ARG B 123      28.613  24.248 156.578  1.00 92.83           N  
ANISOU 3934  NE  ARG B 123    13228  11344  10698  -1952   1441   -156       N  
ATOM   3935  CZ  ARG B 123      28.014  23.358 157.367  1.00 93.06           C  
ANISOU 3935  CZ  ARG B 123    13218  11553  10585  -2099   1366   -104       C  
ATOM   3936  NH1 ARG B 123      26.981  22.637 156.935  1.00 92.25           N  
ANISOU 3936  NH1 ARG B 123    13110  11390  10548  -1978   1293    -23       N  
ATOM   3937  NH2 ARG B 123      28.447  23.188 158.614  1.00 94.55           N  
ANISOU 3937  NH2 ARG B 123    13368  12002  10553  -2387   1363   -128       N  
ATOM   3938  N   ALA B 124      29.775  25.825 149.924  1.00 83.83           N  
ANISOU 3938  N   ALA B 124    12282   9191  10376   -757   1328    204       N  
ATOM   3939  CA  ALA B 124      30.288  25.521 148.583  1.00 81.03           C  
ANISOU 3939  CA  ALA B 124    11973   8734  10081   -574   1213    349       C  
ATOM   3940  C   ALA B 124      31.259  26.603 148.098  1.00 80.00           C  
ANISOU 3940  C   ALA B 124    11868   8495  10031   -520   1297    315       C  
ATOM   3941  O   ALA B 124      32.318  26.289 147.540  1.00 79.17           O  
ANISOU 3941  O   ALA B 124    11812   8382   9887   -475   1203    404       O  
ATOM   3942  CB  ALA B 124      29.142  25.356 147.597  1.00 80.45           C  
ANISOU 3942  CB  ALA B 124    11870   8577  10118   -410   1183    421       C  
ATOM   3943  N   ALA B 125      30.901  27.867 148.330  1.00 87.49           N  
ANISOU 3943  N   ALA B 125    12548   9365  11329   -342   2322    368       N  
ATOM   3944  CA  ALA B 125      31.773  28.999 147.993  1.00 86.57           C  
ANISOU 3944  CA  ALA B 125    12396   9173  11323   -252   2342    433       C  
ATOM   3945  C   ALA B 125      33.088  28.973 148.786  1.00 85.12           C  
ANISOU 3945  C   ALA B 125    12449   9049  10843   -419   2326    378       C  
ATOM   3946  O   ALA B 125      34.173  29.160 148.207  1.00 84.09           O  
ANISOU 3946  O   ALA B 125    12360   8960  10628   -316   2171    516       O  
ATOM   3947  CB  ALA B 125      31.044  30.316 148.213  1.00 88.65           C  
ANISOU 3947  CB  ALA B 125    12464   9228  11989   -241   2623    316       C  
ATOM   3948  N   VAL B 126      32.988  28.728 150.096  1.00 84.70           N  
ANISOU 3948  N   VAL B 126    12548   9004  10628   -691   2480    182       N  
ATOM   3949  CA  VAL B 126      34.180  28.574 150.954  1.00 83.23           C  
ANISOU 3949  CA  VAL B 126    12598   8892  10131   -892   2436    142       C  
ATOM   3950  C   VAL B 126      35.060  27.438 150.423  1.00 80.23           C  
ANISOU 3950  C   VAL B 126    12332   8666   9486   -813   2104    337       C  
ATOM   3951  O   VAL B 126      36.274  27.616 150.233  1.00 78.73           O  
ANISOU 3951  O   VAL B 126    12213   8509   9190   -780   1974    430       O  
ATOM   3952  CB  VAL B 126      33.801  28.326 152.444  1.00 84.69           C  
ANISOU 3952  CB  VAL B 126    12945   9086  10146  -1237   2632    -85       C  
ATOM   3953  CG1 VAL B 126      35.013  27.910 153.278  1.00 84.20           C  
ANISOU 3953  CG1 VAL B 126    13138   9135   9717  -1460   2507    -74       C  
ATOM   3954  CG2 VAL B 126      33.149  29.565 153.051  1.00 87.13           C  
ANISOU 3954  CG2 VAL B 126    13154   9227  10723  -1350   3001   -315       C  
ATOM   3955  N   ALA B 127      34.434  26.289 150.165  1.00 79.11           N  
ANISOU 3955  N   ALA B 127    12189   8604   9263   -783   1980    389       N  
ATOM   3956  CA  ALA B 127      35.120  25.135 149.571  1.00 76.74           C  
ANISOU 3956  CA  ALA B 127    11964   8428   8764   -697   1686    562       C  
ATOM   3957  C   ALA B 127      35.821  25.506 148.265  1.00 74.93           C  
ANISOU 3957  C   ALA B 127    11630   8202   8637   -443   1539    735       C  
ATOM   3958  O   ALA B 127      36.995  25.176 148.086  1.00 73.03           O  
ANISOU 3958  O   ALA B 127    11481   8017   8250   -428   1370    830       O  
ATOM   3959  CB  ALA B 127      34.150  23.982 149.345  1.00 76.36           C  
ANISOU 3959  CB  ALA B 127    11889   8443   8680   -678   1615    578       C  
ATOM   3960  N   ILE B 128      35.113  26.204 147.372  1.00 75.05           N  
ANISOU 3960  N   ILE B 128    11450   8151   8913   -260   1603    777       N  
ATOM   3961  CA  ILE B 128      35.715  26.680 146.118  1.00 74.66           C  
ANISOU 3961  CA  ILE B 128    11305   8102   8959    -45   1481    942       C  
ATOM   3962  C   ILE B 128      36.938  27.540 146.437  1.00 74.89           C  
ANISOU 3962  C   ILE B 128    11410   8085   8959    -84   1519    931       C  
ATOM   3963  O   ILE B 128      38.058  27.196 146.041  1.00 74.06           O  
ANISOU 3963  O   ILE B 128    11381   8043   8714    -42   1353   1028       O  
ATOM   3964  CB  ILE B 128      34.705  27.450 145.226  1.00 75.58           C  
ANISOU 3964  CB  ILE B 128    11196   8139   9382    124   1548   1003       C  
ATOM   3965  CG1 ILE B 128      33.673  26.479 144.634  1.00 75.47           C  
ANISOU 3965  CG1 ILE B 128    11102   8201   9370    187   1444   1058       C  
ATOM   3966  CG2 ILE B 128      35.411  28.173 144.076  1.00 75.10           C  
ANISOU 3966  CG2 ILE B 128    11058   8064   9410    302   1451   1169       C  
ATOM   3967  CD1 ILE B 128      32.378  27.127 144.195  1.00 76.85           C  
ANISOU 3967  CD1 ILE B 128    11051   8282   9864    284   1542   1074       C  
ATOM   3968  N   ALA B 129      36.725  28.623 147.185  1.00 76.42           N  
ANISOU 3968  N   ALA B 129    11579   8162   9292   -177   1749    796       N  
ATOM   3969  CA  ALA B 129      37.822  29.536 147.564  1.00 76.61           C  
ANISOU 3969  CA  ALA B 129    11670   8135   9300   -233   1815    763       C  
ATOM   3970  C   ALA B 129      39.045  28.791 148.119  1.00 75.62           C  
ANISOU 3970  C   ALA B 129    11744   8113   8875   -366   1656    780       C  
ATOM   3971  O   ALA B 129      40.194  29.078 147.733  1.00 74.20           O  
ANISOU 3971  O   ALA B 129    11593   7942   8656   -304   1557    863       O  
ATOM   3972  CB  ALA B 129      37.331  30.567 148.570  1.00 78.55           C  
ANISOU 3972  CB  ALA B 129    11895   8252   9696   -388   2113    564       C  
ATOM   3973  N   GLY B 130      38.782  27.824 149.002  1.00 75.86           N  
ANISOU 3973  N   GLY B 130    11901   8212   8709   -551   1624    711       N  
ATOM   3974  CA  GLY B 130      39.819  26.937 149.537  1.00 74.97           C  
ANISOU 3974  CA  GLY B 130    11961   8193   8330   -684   1435    760       C  
ATOM   3975  C   GLY B 130      40.642  26.249 148.465  1.00 73.23           C  
ANISOU 3975  C   GLY B 130    11714   8031   8076   -499   1187    939       C  
ATOM   3976  O   GLY B 130      41.884  26.239 148.543  1.00 72.86           O  
ANISOU 3976  O   GLY B 130    11737   8000   7944   -523   1070    996       O  
ATOM   3977  N   CYS B 131      39.955  25.696 147.457  1.00 72.31           N  
ANISOU 3977  N   CYS B 131    11491   7945   8037   -327   1118   1017       N  
ATOM   3978  CA  CYS B 131      40.634  25.026 146.338  1.00 71.21           C  
ANISOU 3978  CA  CYS B 131    11319   7861   7875   -164    916   1162       C  
ATOM   3979  C   CYS B 131      41.629  25.962 145.684  1.00 70.21           C  
ANISOU 3979  C   CYS B 131    11149   7693   7835    -52    912   1222       C  
ATOM   3980  O   CYS B 131      42.787  25.606 145.515  1.00 69.78           O  
ANISOU 3980  O   CYS B 131    11145   7660   7706    -45    778   1282       O  
ATOM   3981  CB  CYS B 131      39.650  24.533 145.273  1.00 71.40           C  
ANISOU 3981  CB  CYS B 131    11224   7925   7980    -11    877   1223       C  
ATOM   3982  SG  CYS B 131      38.421  23.363 145.874  1.00 73.02           S  
ANISOU 3982  SG  CYS B 131    11461   8180   8100   -121    880   1157       S  
ATOM   3983  N   TRP B 132      41.175  27.164 145.346  1.00 69.86           N  
ANISOU 3983  N   TRP B 132    11001   7574   7968     29   1065   1203       N  
ATOM   3984  CA  TRP B 132      42.041  28.163 144.728  1.00 69.23           C  
ANISOU 3984  CA  TRP B 132    10877   7443   7983    131   1083   1259       C  
ATOM   3985  C   TRP B 132      43.174  28.612 145.654  1.00 69.32           C  
ANISOU 3985  C   TRP B 132    10999   7424   7913     -7   1111   1193       C  
ATOM   3986  O   TRP B 132      44.320  28.711 145.212  1.00 68.17           O  
ANISOU 3986  O   TRP B 132    10870   7284   7745     46   1018   1258       O  
ATOM   3987  CB  TRP B 132      41.228  29.361 144.233  1.00 69.88           C  
ANISOU 3987  CB  TRP B 132    10815   7433   8302    239   1239   1266       C  
ATOM   3988  CG  TRP B 132      40.481  29.067 142.969  1.00 69.44           C  
ANISOU 3988  CG  TRP B 132    10637   7416   8329    402   1152   1394       C  
ATOM   3989  CD1 TRP B 132      39.153  28.780 142.841  1.00 69.96           C  
ANISOU 3989  CD1 TRP B 132    10610   7487   8481    428   1180   1392       C  
ATOM   3990  CD2 TRP B 132      41.027  29.021 141.648  1.00 68.34           C  
ANISOU 3990  CD2 TRP B 132    10458   7325   8181    540   1020   1539       C  
ATOM   3991  NE1 TRP B 132      38.836  28.563 141.521  1.00 69.27           N  
ANISOU 3991  NE1 TRP B 132    10428   7456   8434    570   1056   1540       N  
ATOM   3992  CE2 TRP B 132      39.969  28.704 140.767  1.00 68.35           C  
ANISOU 3992  CE2 TRP B 132    10350   7370   8248    631    962   1629       C  
ATOM   3993  CE3 TRP B 132      42.309  29.220 141.122  1.00 67.70           C  
ANISOU 3993  CE3 TRP B 132    10423   7255   8043    579    951   1596       C  
ATOM   3994  CZ2 TRP B 132      40.152  28.583 139.390  1.00 68.28           C  
ANISOU 3994  CZ2 TRP B 132    10293   7428   8220    739    836   1776       C  
ATOM   3995  CZ3 TRP B 132      42.494  29.099 139.752  1.00 67.49           C  
ANISOU 3995  CZ3 TRP B 132    10346   7285   8011    692    845   1728       C  
ATOM   3996  CH2 TRP B 132      41.419  28.784 138.901  1.00 67.87           C  
ANISOU 3996  CH2 TRP B 132    10302   7388   8098    761    787   1818       C  
ATOM   3997  N   ILE B 133      42.869  28.855 146.930  1.00 70.58           N  
ANISOU 3997  N   ILE B 133    11236   7556   8022   -202   1239   1059       N  
ATOM   3998  CA  ILE B 133      43.916  29.245 147.893  1.00 71.33           C  
ANISOU 3998  CA  ILE B 133    11449   7640   8010   -375   1254    995       C  
ATOM   3999  C   ILE B 133      45.006  28.164 147.943  1.00 70.68           C  
ANISOU 3999  C   ILE B 133    11457   7636   7759   -413   1008   1089       C  
ATOM   4000  O   ILE B 133      46.199  28.449 147.718  1.00 70.85           O  
ANISOU 4000  O   ILE B 133    11488   7646   7783   -382    930   1139       O  
ATOM   4001  CB  ILE B 133      43.340  29.502 149.310  1.00 72.97           C  
ANISOU 4001  CB  ILE B 133    11750   7831   8143   -631   1426    826       C  
ATOM   4002  CG1 ILE B 133      42.433  30.739 149.305  1.00 74.30           C  
ANISOU 4002  CG1 ILE B 133    11806   7883   8540   -600   1704    710       C  
ATOM   4003  CG2 ILE B 133      44.453  29.704 150.341  1.00 73.58           C  
ANISOU 4003  CG2 ILE B 133    11972   7930   8055   -853   1397    776       C  
ATOM   4004  CD1 ILE B 133      41.365  30.706 150.377  1.00 75.77           C  
ANISOU 4004  CD1 ILE B 133    12035   8049   8704   -808   1896    536       C  
ATOM   4005  N   LEU B 134      44.580  26.926 148.197  1.00 70.11           N  
ANISOU 4005  N   LEU B 134    11436   7631   7571   -472    889   1116       N  
ATOM   4006  CA  LEU B 134      45.507  25.792 148.266  1.00 69.15           C  
ANISOU 4006  CA  LEU B 134    11379   7561   7334   -508    652   1215       C  
ATOM   4007  C   LEU B 134      46.253  25.576 146.941  1.00 67.59           C  
ANISOU 4007  C   LEU B 134    11085   7358   7238   -291    536   1323       C  
ATOM   4008  O   LEU B 134      47.440  25.231 146.945  1.00 66.94           O  
ANISOU 4008  O   LEU B 134    11025   7270   7138   -305    393   1384       O  
ATOM   4009  CB  LEU B 134      44.759  24.520 148.689  1.00 69.46           C  
ANISOU 4009  CB  LEU B 134    11473   7656   7261   -597    565   1226       C  
ATOM   4010  CG  LEU B 134      45.560  23.275 149.080  1.00 69.59           C  
ANISOU 4010  CG  LEU B 134    11566   7705   7167   -688    327   1325       C  
ATOM   4011  CD1 LEU B 134      46.486  23.535 150.262  1.00 70.49           C  
ANISOU 4011  CD1 LEU B 134    11800   7818   7162   -916    262   1325       C  
ATOM   4012  CD2 LEU B 134      44.603  22.119 149.374  1.00 69.67           C  
ANISOU 4012  CD2 LEU B 134    11617   7761   7094   -754    279   1330       C  
ATOM   4013  N   SER B 135      45.561  25.808 145.821  1.00 67.22           N  
ANISOU 4013  N   SER B 135    10929   7308   7302   -109    602   1346       N  
ATOM   4014  CA  SER B 135      46.158  25.744 144.475  1.00 66.68           C  
ANISOU 4014  CA  SER B 135    10776   7243   7315     72    531   1432       C  
ATOM   4015  C   SER B 135      47.254  26.775 144.276  1.00 67.02           C  
ANISOU 4015  C   SER B 135    10807   7230   7425    105    571   1437       C  
ATOM   4016  O   SER B 135      48.317  26.448 143.747  1.00 67.00           O  
ANISOU 4016  O   SER B 135    10792   7225   7440    155    466   1488       O  
ATOM   4017  CB  SER B 135      45.105  25.961 143.392  1.00 66.26           C  
ANISOU 4017  CB  SER B 135    10618   7207   7348    221    598   1464       C  
ATOM   4018  OG  SER B 135      44.037  25.063 143.549  1.00 66.21           O  
ANISOU 4018  OG  SER B 135    10612   7251   7291    192    573   1451       O  
ATOM   4019  N   PHE B 136      46.980  28.017 144.678  1.00 67.39           N  
ANISOU 4019  N   PHE B 136    10848   7224   7533     76    736   1375       N  
ATOM   4020  CA  PHE B 136      48.008  29.060 144.692  1.00 67.60           C  
ANISOU 4020  CA  PHE B 136    10875   7191   7616     77    792   1362       C  
ATOM   4021  C   PHE B 136      49.159  28.684 145.636  1.00 67.84           C  
ANISOU 4021  C   PHE B 136    11001   7230   7545    -77    679   1345       C  
ATOM   4022  O   PHE B 136      50.329  28.862 145.280  1.00 67.03           O  
ANISOU 4022  O   PHE B 136    10883   7103   7481    -38    615   1381       O  
ATOM   4023  CB  PHE B 136      47.421  30.438 145.048  1.00 68.85           C  
ANISOU 4023  CB  PHE B 136    11005   7274   7879     57   1011   1283       C  
ATOM   4024  CG  PHE B 136      46.911  31.209 143.856  1.00 69.05           C  
ANISOU 4024  CG  PHE B 136    10909   7255   8072    242   1094   1350       C  
ATOM   4025  CD1 PHE B 136      47.800  31.832 142.993  1.00 68.77           C  
ANISOU 4025  CD1 PHE B 136    10835   7187   8104    347   1084   1415       C  
ATOM   4026  CD2 PHE B 136      45.546  31.317 143.591  1.00 69.74           C  
ANISOU 4026  CD2 PHE B 136    10914   7328   8253    301   1172   1358       C  
ATOM   4027  CE1 PHE B 136      47.340  32.543 141.889  1.00 68.93           C  
ANISOU 4027  CE1 PHE B 136    10754   7170   8264    495   1141   1503       C  
ATOM   4028  CE2 PHE B 136      45.082  32.024 142.491  1.00 69.75           C  
ANISOU 4028  CE2 PHE B 136    10796   7287   8416    459   1216   1453       C  
ATOM   4029  CZ  PHE B 136      45.981  32.638 141.638  1.00 69.37           C  
ANISOU 4029  CZ  PHE B 136    10727   7215   8415    551   1194   1533       C  
ATOM   4030  N   VAL B 137      48.836  28.140 146.813  1.00 69.12           N  
ANISOU 4030  N   VAL B 137    11257   7425   7580   -263    644   1300       N  
ATOM   4031  CA  VAL B 137      49.886  27.678 147.744  1.00 70.14           C  
ANISOU 4031  CA  VAL B 137    11476   7570   7602   -435    493   1319       C  
ATOM   4032  C   VAL B 137      50.793  26.619 147.090  1.00 69.88           C  
ANISOU 4032  C   VAL B 137    11398   7542   7609   -342    280   1431       C  
ATOM   4033  O   VAL B 137      52.019  26.762 147.093  1.00 70.40           O  
ANISOU 4033  O   VAL B 137    11452   7576   7719   -353    193   1464       O  
ATOM   4034  CB  VAL B 137      49.303  27.154 149.085  1.00 70.80           C  
ANISOU 4034  CB  VAL B 137    11682   7701   7515   -676    472   1273       C  
ATOM   4035  CG1 VAL B 137      50.354  26.410 149.906  1.00 71.31           C  
ANISOU 4035  CG1 VAL B 137    11830   7792   7473   -848    248   1350       C  
ATOM   4036  CG2 VAL B 137      48.741  28.306 149.904  1.00 71.86           C  
ANISOU 4036  CG2 VAL B 137    11869   7815   7619   -823    702   1130       C  
ATOM   4037  N   VAL B 138      50.188  25.578 146.524  1.00 69.36           N  
ANISOU 4037  N   VAL B 138    11298   7507   7548   -256    210   1477       N  
ATOM   4038  CA  VAL B 138      50.952  24.485 145.903  1.00 69.26           C  
ANISOU 4038  CA  VAL B 138    11230   7483   7599   -179     35   1561       C  
ATOM   4039  C   VAL B 138      51.709  24.966 144.658  1.00 68.44           C  
ANISOU 4039  C   VAL B 138    11030   7340   7631     -8     76   1572       C  
ATOM   4040  O   VAL B 138      52.895  24.665 144.485  1.00 68.31           O  
ANISOU 4040  O   VAL B 138    10976   7278   7698      1    -28   1607       O  
ATOM   4041  CB  VAL B 138      50.045  23.287 145.537  1.00 69.30           C  
ANISOU 4041  CB  VAL B 138    11219   7528   7581   -134    -18   1588       C  
ATOM   4042  CG1 VAL B 138      50.804  22.238 144.719  1.00 69.08           C  
ANISOU 4042  CG1 VAL B 138    11114   7471   7661    -40   -151   1648       C  
ATOM   4043  CG2 VAL B 138      49.462  22.658 146.793  1.00 70.17           C  
ANISOU 4043  CG2 VAL B 138    11433   7672   7556   -322    -81   1588       C  
ATOM   4044  N   GLY B 139      51.018  25.715 143.806  1.00 68.09           N  
ANISOU 4044  N   GLY B 139    10943   7309   7619    112    226   1546       N  
ATOM   4045  CA  GLY B 139      51.597  26.219 142.566  1.00 68.07           C  
ANISOU 4045  CA  GLY B 139    10865   7281   7715    253    278   1562       C  
ATOM   4046  C   GLY B 139      52.677  27.282 142.717  1.00 68.69           C  
ANISOU 4046  C   GLY B 139    10944   7301   7854    238    327   1542       C  
ATOM   4047  O   GLY B 139      53.613  27.307 141.918  1.00 68.32           O  
ANISOU 4047  O   GLY B 139    10844   7221   7890    310    311   1555       O  
ATOM   4048  N   LEU B 140      52.548  28.163 143.718  1.00 69.50           N  
ANISOU 4048  N   LEU B 140    11103   7386   7917    134    406   1494       N  
ATOM   4049  CA  LEU B 140      53.565  29.202 143.976  1.00 69.91           C  
ANISOU 4049  CA  LEU B 140    11161   7383   8019     98    460   1462       C  
ATOM   4050  C   LEU B 140      54.749  28.740 144.835  1.00 70.79           C  
ANISOU 4050  C   LEU B 140    11305   7478   8114    -33    304   1473       C  
ATOM   4051  O   LEU B 140      55.715  29.487 144.981  1.00 71.61           O  
ANISOU 4051  O   LEU B 140    11402   7538   8268    -62    326   1451       O  
ATOM   4052  CB  LEU B 140      52.942  30.458 144.607  1.00 70.13           C  
ANISOU 4052  CB  LEU B 140    11224   7387   8033     35    642   1389       C  
ATOM   4053  CG  LEU B 140      51.948  31.241 143.740  1.00 69.65           C  
ANISOU 4053  CG  LEU B 140    11100   7305   8056    173    803   1396       C  
ATOM   4054  CD1 LEU B 140      51.310  32.360 144.548  1.00 70.52           C  
ANISOU 4054  CD1 LEU B 140    11231   7366   8195     89    990   1307       C  
ATOM   4055  CD2 LEU B 140      52.614  31.791 142.486  1.00 69.21           C  
ANISOU 4055  CD2 LEU B 140    10978   7215   8104    319    832   1449       C  
ATOM   4056  N   THR B 141      54.694  27.534 145.403  1.00 71.11           N  
ANISOU 4056  N   THR B 141    11373   7546   8096   -118    137   1518       N  
ATOM   4057  CA  THR B 141      55.819  27.004 146.206  1.00 71.96           C  
ANISOU 4057  CA  THR B 141    11495   7631   8214   -249    -52   1566       C  
ATOM   4058  C   THR B 141      57.199  27.199 145.528  1.00 72.38           C  
ANISOU 4058  C   THR B 141    11454   7612   8434   -164    -92   1581       C  
ATOM   4059  O   THR B 141      58.111  27.755 146.158  1.00 73.06           O  
ANISOU 4059  O   THR B 141    11552   7671   8535   -265   -132   1575       O  
ATOM   4060  CB  THR B 141      55.568  25.540 146.648  1.00 71.69           C  
ANISOU 4060  CB  THR B 141    11478   7618   8142   -317   -241   1644       C  
ATOM   4061  OG1 THR B 141      54.465  25.516 147.564  1.00 71.79           O  
ANISOU 4061  OG1 THR B 141    11600   7696   7981   -455   -202   1617       O  
ATOM   4062  CG2 THR B 141      56.799  24.930 147.329  1.00 72.66           C  
ANISOU 4062  CG2 THR B 141    11582   7695   8329   -434   -470   1731       C  
ATOM   4063  N   PRO B 142      57.343  26.804 144.242  1.00 72.35           N  
ANISOU 4063  N   PRO B 142    11358   7581   8550      5    -64   1587       N  
ATOM   4064  CA  PRO B 142      58.574  27.106 143.495  1.00 73.06           C  
ANISOU 4064  CA  PRO B 142    11359   7599   8802     82    -50   1572       C  
ATOM   4065  C   PRO B 142      59.035  28.575 143.553  1.00 73.89           C  
ANISOU 4065  C   PRO B 142    11483   7683   8908     73     86   1518       C  
ATOM   4066  O   PRO B 142      60.238  28.830 143.644  1.00 74.26           O  
ANISOU 4066  O   PRO B 142    11482   7669   9061     47     40   1512       O  
ATOM   4067  CB  PRO B 142      58.213  26.717 142.061  1.00 72.18           C  
ANISOU 4067  CB  PRO B 142    11186   7492   8745    238     35   1558       C  
ATOM   4068  CG  PRO B 142      57.202  25.642 142.208  1.00 71.66           C  
ANISOU 4068  CG  PRO B 142    11143   7478   8604    228    -35   1591       C  
ATOM   4069  CD  PRO B 142      56.434  25.946 143.458  1.00 71.72           C  
ANISOU 4069  CD  PRO B 142    11253   7536   8458    104    -51   1601       C  
ATOM   4070  N   MET B 143      58.092  29.518 143.502  1.00 74.61           N  
ANISOU 4070  N   MET B 143    11631   7811   8907     95    253   1480       N  
ATOM   4071  CA  MET B 143      58.405  30.946 143.682  1.00 75.84           C  
ANISOU 4071  CA  MET B 143    11807   7935   9071     72    398   1425       C  
ATOM   4072  C   MET B 143      58.966  31.273 145.068  1.00 76.91           C  
ANISOU 4072  C   MET B 143    12003   8070   9149   -120    334   1398       C  
ATOM   4073  O   MET B 143      59.756  32.211 145.192  1.00 77.61           O  
ANISOU 4073  O   MET B 143    12085   8117   9286   -151    400   1354       O  
ATOM   4074  CB  MET B 143      57.179  31.833 143.421  1.00 76.18           C  
ANISOU 4074  CB  MET B 143    11879   7995   9070    128    588   1398       C  
ATOM   4075  CG  MET B 143      56.724  31.876 141.973  1.00 75.99           C  
ANISOU 4075  CG  MET B 143    11798   7974   9101    301    664   1438       C  
ATOM   4076  SD  MET B 143      57.614  33.095 140.982  1.00 77.25           S  
ANISOU 4076  SD  MET B 143    11912   8064   9374    391    799   1429       S  
ATOM   4077  CE  MET B 143      57.069  34.633 141.735  1.00 78.42           C  
ANISOU 4077  CE  MET B 143    12097   8166   9532    339    982   1378       C  
ATOM   4078  N   PHE B 144      58.565  30.521 146.099  1.00 77.22           N  
ANISOU 4078  N   PHE B 144    12108   8159   9072   -265    205   1425       N  
ATOM   4079  CA  PHE B 144      59.079  30.761 147.459  1.00 78.03           C  
ANISOU 4079  CA  PHE B 144    12285   8280   9081   -493    122   1412       C  
ATOM   4080  C   PHE B 144      60.539  30.335 147.644  1.00 78.13           C  
ANISOU 4080  C   PHE B 144    12236   8251   9198   -543    -80   1477       C  
ATOM   4081  O   PHE B 144      61.199  30.834 148.558  1.00 79.25           O  
ANISOU 4081  O   PHE B 144    12420   8401   9288   -718   -131   1463       O  
ATOM   4082  CB  PHE B 144      58.213  30.085 148.540  1.00 78.89           C  
ANISOU 4082  CB  PHE B 144    12499   8462   9011   -669     40   1430       C  
ATOM   4083  CG  PHE B 144      56.745  30.468 148.511  1.00 78.77           C  
ANISOU 4083  CG  PHE B 144    12536   8480   8913   -646    240   1355       C  
ATOM   4084  CD1 PHE B 144      56.320  31.749 148.126  1.00 78.89           C  
ANISOU 4084  CD1 PHE B 144    12535   8458   8979   -571    488   1261       C  
ATOM   4085  CD2 PHE B 144      55.779  29.544 148.920  1.00 78.57           C  
ANISOU 4085  CD2 PHE B 144    12564   8509   8778   -707    178   1383       C  
ATOM   4086  CE1 PHE B 144      54.968  32.075 148.119  1.00 79.17           C  
ANISOU 4086  CE1 PHE B 144    12590   8502   8987   -549    662   1201       C  
ATOM   4087  CE2 PHE B 144      54.427  29.866 148.913  1.00 78.64           C  
ANISOU 4087  CE2 PHE B 144    12602   8537   8737   -689    360   1309       C  
ATOM   4088  CZ  PHE B 144      54.020  31.131 148.508  1.00 79.15           C  
ANISOU 4088  CZ  PHE B 144    12634   8557   8882   -607    600   1219       C  
ATOM   4089  N   GLY B 145      61.045  29.434 146.793  1.00 77.01           N  
ANISOU 4089  N   GLY B 145    11985   8059   9215   -404   -188   1540       N  
ATOM   4090  CA  GLY B 145      62.441  28.980 146.896  1.00 77.52           C  
ANISOU 4090  CA  GLY B 145    11954   8055   9444   -435   -376   1600       C  
ATOM   4091  C   GLY B 145      62.777  27.600 146.347  1.00 77.31           C  
ANISOU 4091  C   GLY B 145    11815   7969   9590   -343   -536   1680       C  
ATOM   4092  O   GLY B 145      63.917  27.369 145.934  1.00 77.76           O  
ANISOU 4092  O   GLY B 145    11746   7933   9865   -293   -609   1695       O  
ATOM   4093  N   TRP B 146      61.807  26.680 146.349  1.00 76.26           N  
ANISOU 4093  N   TRP B 146    11716   7875   9382   -328   -579   1721       N  
ATOM   4094  CA  TRP B 146      62.051  25.298 145.926  1.00 76.24           C  
ANISOU 4094  CA  TRP B 146    11608   7807   9551   -260   -726   1792       C  
ATOM   4095  C   TRP B 146      62.248  25.192 144.401  1.00 76.22           C  
ANISOU 4095  C   TRP B 146    11498   7747   9715    -59   -576   1717       C  
ATOM   4096  O   TRP B 146      61.310  24.909 143.643  1.00 75.46           O  
ANISOU 4096  O   TRP B 146    11421   7694   9555     38   -462   1682       O  
ATOM   4097  CB  TRP B 146      60.916  24.380 146.409  1.00 75.71           C  
ANISOU 4097  CB  TRP B 146    11620   7803   9341   -317   -803   1850       C  
ATOM   4098  CG  TRP B 146      61.285  22.918 146.529  1.00 75.83           C  
ANISOU 4098  CG  TRP B 146    11544   7742   9523   -329  -1023   1960       C  
ATOM   4099  CD1 TRP B 146      62.426  22.306 146.084  1.00 76.43           C  
ANISOU 4099  CD1 TRP B 146    11456   7688   9896   -266  -1129   1996       C  
ATOM   4100  CD2 TRP B 146      60.481  21.888 147.107  1.00 75.69           C  
ANISOU 4100  CD2 TRP B 146    11585   7759   9414   -407  -1148   2043       C  
ATOM   4101  NE1 TRP B 146      62.388  20.968 146.366  1.00 77.28           N  
ANISOU 4101  NE1 TRP B 146    11507   7736  10120   -296  -1318   2104       N  
ATOM   4102  CE2 TRP B 146      61.205  20.680 146.993  1.00 76.75           C  
ANISOU 4102  CE2 TRP B 146    11581   7772   9806   -384  -1338   2140       C  
ATOM   4103  CE3 TRP B 146      59.219  21.867 147.715  1.00 75.32           C  
ANISOU 4103  CE3 TRP B 146    11686   7822   9109   -498  -1109   2039       C  
ATOM   4104  CZ2 TRP B 146      60.709  19.458 147.465  1.00 76.96           C  
ANISOU 4104  CZ2 TRP B 146    11621   7786   9833   -447  -1499   2247       C  
ATOM   4105  CZ3 TRP B 146      58.729  20.655 148.190  1.00 75.84           C  
ANISOU 4105  CZ3 TRP B 146    11774   7886   9153   -569  -1265   2136       C  
ATOM   4106  CH2 TRP B 146      59.476  19.464 148.060  1.00 76.54           C  
ANISOU 4106  CH2 TRP B 146    11729   7854   9495   -542  -1463   2246       C  
ATOM   4107  N   ASN B 147      63.489  25.416 143.972  1.00 77.61           N  
ANISOU 4107  N   ASN B 147    11558   7827  10101    -19   -578   1691       N  
ATOM   4108  CA  ASN B 147      63.849  25.438 142.548  1.00 77.85           C  
ANISOU 4108  CA  ASN B 147    11495   7801  10284    131   -416   1601       C  
ATOM   4109  C   ASN B 147      65.350  25.150 142.352  1.00 79.97           C  
ANISOU 4109  C   ASN B 147    11599   7927  10858    137   -493   1593       C  
ATOM   4110  O   ASN B 147      66.049  24.845 143.321  1.00 81.47           O  
ANISOU 4110  O   ASN B 147    11739   8063  11152     35   -702   1681       O  
ATOM   4111  CB  ASN B 147      63.427  26.785 141.929  1.00 76.77           C  
ANISOU 4111  CB  ASN B 147    11439   7729  10002    192   -182   1519       C  
ATOM   4112  CG  ASN B 147      63.904  27.983 142.731  1.00 76.99           C  
ANISOU 4112  CG  ASN B 147    11518   7764   9969    103   -168   1510       C  
ATOM   4113  OD1 ASN B 147      65.102  28.226 142.849  1.00 77.29           O  
ANISOU 4113  OD1 ASN B 147    11477   7725  10164     74   -216   1499       O  
ATOM   4114  ND2 ASN B 147      62.963  28.754 143.264  1.00 76.78           N  
ANISOU 4114  ND2 ASN B 147    11616   7824   9729     54    -88   1504       N  
ATOM   4115  N   ASN B 148      65.835  25.233 141.111  1.00 81.13           N  
ANISOU 4115  N   ASN B 148    11660   8012  11153    242   -329   1490       N  
ATOM   4116  CA  ASN B 148      67.252  24.982 140.787  1.00 83.20           C  
ANISOU 4116  CA  ASN B 148    11748   8122  11740    255   -357   1450       C  
ATOM   4117  C   ASN B 148      68.136  26.243 140.737  1.00 83.90           C  
ANISOU 4117  C   ASN B 148    11830   8189  11859    242   -263   1391       C  
ATOM   4118  O   ASN B 148      69.229  26.196 140.169  1.00 85.25           O  
ANISOU 4118  O   ASN B 148    11862   8239  12290    271   -213   1319       O  
ATOM   4119  CB  ASN B 148      67.359  24.257 139.436  1.00 83.63           C  
ANISOU 4119  CB  ASN B 148    11705   8108  11962    347   -206   1343       C  
ATOM   4120  CG  ASN B 148      66.534  22.984 139.378  1.00 83.73           C  
ANISOU 4120  CG  ASN B 148    11712   8132  11969    360   -275   1381       C  
ATOM   4121  OD1 ASN B 148      66.452  22.236 140.354  1.00 85.07           O  
ANISOU 4121  OD1 ASN B 148    11859   8273  12191    303   -494   1499       O  
ATOM   4122  ND2 ASN B 148      65.929  22.723 138.222  1.00 82.89           N  
ANISOU 4122  ND2 ASN B 148    11629   8069  11795    420    -93   1287       N  
ATOM   4123  N   LEU B 149      67.698  27.354 141.333  1.00 83.50           N  
ANISOU 4123  N   LEU B 149    11918   8240  11567    192   -227   1408       N  
ATOM   4124  CA  LEU B 149      68.458  28.610 141.261  1.00 83.89           C  
ANISOU 4124  CA  LEU B 149    11970   8270  11633    179   -116   1344       C  
ATOM   4125  C   LEU B 149      69.918  28.408 141.674  1.00 85.72           C  
ANISOU 4125  C   LEU B 149    12044   8374  12149    124   -259   1355       C  
ATOM   4126  O   LEU B 149      70.831  28.743 140.915  1.00 85.70           O  
ANISOU 4126  O   LEU B 149    11943   8282  12335    173   -138   1262       O  
ATOM   4127  CB  LEU B 149      67.807  29.695 142.131  1.00 83.39           C  
ANISOU 4127  CB  LEU B 149    12063   8315  11304    100    -90   1368       C  
ATOM   4128  CG  LEU B 149      68.493  31.062 142.231  1.00 83.29           C  
ANISOU 4128  CG  LEU B 149    12069   8288  11288     67     24   1304       C  
ATOM   4129  CD1 LEU B 149      68.772  31.656 140.860  1.00 82.76           C  
ANISOU 4129  CD1 LEU B 149    11972   8179  11292    186    258   1207       C  
ATOM   4130  CD2 LEU B 149      67.640  32.015 143.055  1.00 82.91           C  
ANISOU 4130  CD2 LEU B 149    12175   8341  10985    -15     82   1311       C  
ATOM   4131  N   SER B 150      70.119  27.832 142.860  1.00 87.19           N  
ANISOU 4131  N   SER B 150    12204   8551  12372     13   -522   1477       N  
ATOM   4132  CA  SER B 150      71.464  27.541 143.379  1.00 89.42           C  
ANISOU 4132  CA  SER B 150    12320   8710  12945    -54   -716   1528       C  
ATOM   4133  C   SER B 150      72.264  26.605 142.467  1.00 90.16           C  
ANISOU 4133  C   SER B 150    12200   8633  13423     44   -699   1477       C  
ATOM   4134  O   SER B 150      73.472  26.791 142.290  1.00 90.87           O  
ANISOU 4134  O   SER B 150    12135   8600  13791     44   -704   1432       O  
ATOM   4135  CB  SER B 150      71.373  26.938 144.781  1.00 90.85           C  
ANISOU 4135  CB  SER B 150    12522   8921  13073   -209  -1030   1702       C  
ATOM   4136  OG  SER B 150      70.674  27.808 145.650  1.00 90.99           O  
ANISOU 4136  OG  SER B 150    12737   9091  12741   -332  -1019   1720       O  
ATOM   4137  N   ALA B 151      71.585  25.608 141.899  1.00 89.85           N  
ANISOU 4137  N   ALA B 151    12148   8582  13408    117   -666   1472       N  
ATOM   4138  CA  ALA B 151      72.197  24.687 140.936  1.00 90.38           C  
ANISOU 4138  CA  ALA B 151    12023   8487  13830    201   -596   1389       C  
ATOM   4139  C   ALA B 151      72.645  25.399 139.656  1.00 90.27           C  
ANISOU 4139  C   ALA B 151    11986   8442  13870    275   -292   1200       C  
ATOM   4140  O   ALA B 151      73.713  25.086 139.125  1.00 91.40           O  
ANISOU 4140  O   ALA B 151    11939   8421  14366    297   -239   1111       O  
ATOM   4141  CB  ALA B 151      71.243  23.547 140.601  1.00 89.56           C  
ANISOU 4141  CB  ALA B 151    11937   8398  13690    246   -597   1409       C  
ATOM   4142  N   VAL B 152      71.844  26.354 139.176  1.00 88.97           N  
ANISOU 4142  N   VAL B 152    12007   8423  13372    302    -96   1143       N  
ATOM   4143  CA  VAL B 152      72.185  27.114 137.963  1.00 88.69           C  
ANISOU 4143  CA  VAL B 152    11982   8378  13338    349    184    987       C  
ATOM   4144  C   VAL B 152      73.265  28.171 138.242  1.00 89.92           C  
ANISOU 4144  C   VAL B 152    12092   8479  13591    313    207    951       C  
ATOM   4145  O   VAL B 152      74.147  28.398 137.402  1.00 91.22           O  
ANISOU 4145  O   VAL B 152    12159   8545  13954    332    374    819       O  
ATOM   4146  CB  VAL B 152      70.936  27.763 137.314  1.00 86.72           C  
ANISOU 4146  CB  VAL B 152    11934   8292  12720    387    365    968       C  
ATOM   4147  CG1 VAL B 152      71.319  28.556 136.070  1.00 86.56           C  
ANISOU 4147  CG1 VAL B 152    11934   8263  12691    412    634    834       C  
ATOM   4148  CG2 VAL B 152      69.912  26.703 136.930  1.00 86.19           C  
ANISOU 4148  CG2 VAL B 152    11900   8277  12569    418    355    988       C  
ATOM   4149  N   GLU B 153      73.188  28.818 139.407  1.00 90.33           N  
ANISOU 4149  N   GLU B 153    12222   8601  13498    245     55   1054       N  
ATOM   4150  CA  GLU B 153      74.206  29.793 139.842  1.00 91.87           C  
ANISOU 4150  CA  GLU B 153    12374   8752  13777    189     48   1029       C  
ATOM   4151  C   GLU B 153      75.619  29.201 139.909  1.00 94.50           C  
ANISOU 4151  C   GLU B 153    12463   8901  14540    170    -64   1007       C  
ATOM   4152  O   GLU B 153      76.594  29.876 139.562  1.00 95.42           O  
ANISOU 4152  O   GLU B 153    12500   8940  14813    167     47    909       O  
ATOM   4153  CB  GLU B 153      73.838  30.400 141.202  1.00 91.49           C  
ANISOU 4153  CB  GLU B 153    12449   8814  13499     82   -117   1143       C  
ATOM   4154  CG  GLU B 153      72.733  31.443 141.136  1.00 89.77           C  
ANISOU 4154  CG  GLU B 153    12444   8741  12921     92     53   1123       C  
ATOM   4155  CD  GLU B 153      72.234  31.891 142.505  1.00 89.72           C  
ANISOU 4155  CD  GLU B 153    12561   8840  12686    -36    -86   1212       C  
ATOM   4156  OE1 GLU B 153      72.608  31.286 143.534  1.00 90.63           O  
ANISOU 4156  OE1 GLU B 153    12623   8942  12867   -147   -344   1313       O  
ATOM   4157  OE2 GLU B 153      71.454  32.865 142.554  1.00 88.99           O  
ANISOU 4157  OE2 GLU B 153    12620   8840  12352    -40     66   1182       O  
ATOM   4158  N   ARG B 154      75.718  27.952 140.366  1.00 95.93           N  
ANISOU 4158  N   ARG B 154    12517   9002  14928    157   -286   1105       N  
ATOM   4159  CA  ARG B 154      76.987  27.212 140.364  1.00 98.32           C  
ANISOU 4159  CA  ARG B 154    12549   9097  15707    153   -401   1097       C  
ATOM   4160  C   ARG B 154      77.560  27.082 138.959  1.00 98.93           C  
ANISOU 4160  C   ARG B 154    12506   9048  16034    233   -115    892       C  
ATOM   4161  O   ARG B 154      78.729  27.378 138.743  1.00100.10           O  
ANISOU 4161  O   ARG B 154    12493   9062  16475    223    -63    805       O  
ATOM   4162  CB  ARG B 154      76.823  25.822 140.992  1.00 99.33           C  
ANISOU 4162  CB  ARG B 154    12567   9153  16021    135   -674   1249       C  
ATOM   4163  CG  ARG B 154      76.854  25.855 142.516  1.00100.02           C  
ANISOU 4163  CG  ARG B 154    12689   9300  16013      5  -1019   1463       C  
ATOM   4164  CD  ARG B 154      76.672  24.478 143.138  1.00101.36           C  
ANISOU 4164  CD  ARG B 154    12758   9395  16359    -24  -1303   1639       C  
ATOM   4165  NE  ARG B 154      75.262  24.145 143.353  1.00100.07           N  
ANISOU 4165  NE  ARG B 154    12801   9387  15832    -28  -1309   1701       N  
ATOM   4166  CZ  ARG B 154      74.817  23.038 143.953  1.00100.83           C  
ANISOU 4166  CZ  ARG B 154    12876   9462  15972    -67  -1539   1861       C  
ATOM   4167  NH1 ARG B 154      75.663  22.115 144.414  1.00102.95           N  
ANISOU 4167  NH1 ARG B 154    12917   9551  16649   -102  -1802   1998       N  
ATOM   4168  NH2 ARG B 154      73.505  22.850 144.094  1.00 99.61           N  
ANISOU 4168  NH2 ARG B 154    12920   9458  15466    -72  -1508   1892       N  
ATOM   4169  N   ALA B 155      76.730  26.642 138.019  1.00 98.47           N  
ANISOU 4169  N   ALA B 155    12528   9035  15848    293     71    811       N  
ATOM   4170  CA  ALA B 155      77.134  26.506 136.614  1.00 99.49           C  
ANISOU 4170  CA  ALA B 155    12581   9072  16148    332    371    602       C  
ATOM   4171  C   ALA B 155      77.424  27.853 135.940  1.00 99.70           C  
ANISOU 4171  C   ALA B 155    12714   9157  16008    324    621    478       C  
ATOM   4172  O   ALA B 155      78.306  27.934 135.083  1.00101.59           O  
ANISOU 4172  O   ALA B 155    12835   9274  16489    318    824    309       O  
ATOM   4173  CB  ALA B 155      76.076  25.743 135.829  1.00 98.48           C  
ANISOU 4173  CB  ALA B 155    12541   9012  15864    367    494    558       C  
ATOM   4174  N   TRP B 156      76.687  28.896 136.327  1.00 98.41           N  
ANISOU 4174  N   TRP B 156    12767   9169  15454    317    617    558       N  
ATOM   4175  CA  TRP B 156      76.899  30.259 135.798  1.00 97.61           C  
ANISOU 4175  CA  TRP B 156    12775   9121  15189    308    834    471       C  
ATOM   4176  C   TRP B 156      78.266  30.829 136.235  1.00 98.98           C  
ANISOU 4176  C   TRP B 156    12803   9174  15630    267    796    428       C  
ATOM   4177  O   TRP B 156      79.016  31.401 135.418  1.00 99.41           O  
ANISOU 4177  O   TRP B 156    12816   9159  15796    259   1019    280       O  
ATOM   4178  CB  TRP B 156      75.747  31.173 136.254  1.00 95.81           C  
ANISOU 4178  CB  TRP B 156    12785   9084  14534    311    818    581       C  
ATOM   4179  CG  TRP B 156      75.537  32.411 135.435  1.00 94.97           C  
ANISOU 4179  CG  TRP B 156    12823   9048  14213    321   1070    512       C  
ATOM   4180  CD1 TRP B 156      75.559  33.699 135.885  1.00 94.38           C  
ANISOU 4180  CD1 TRP B 156    12847   9025  13986    300   1105    540       C  
ATOM   4181  CD2 TRP B 156      75.244  32.480 134.032  1.00 94.73           C  
ANISOU 4181  CD2 TRP B 156    12859   9042  14092    337   1317    416       C  
ATOM   4182  NE1 TRP B 156      75.314  34.568 134.849  1.00 94.02           N  
ANISOU 4182  NE1 TRP B 156    12914   9020  13786    317   1350    481       N  
ATOM   4183  CE2 TRP B 156      75.112  33.849 133.701  1.00 93.99           C  
ANISOU 4183  CE2 TRP B 156    12901   9010  13800    332   1474    413       C  
ATOM   4184  CE3 TRP B 156      75.086  31.520 133.021  1.00 95.22           C  
ANISOU 4184  CE3 TRP B 156    12881   9080  14218    338   1424    331       C  
ATOM   4185  CZ2 TRP B 156      74.840  34.285 132.397  1.00 93.95           C  
ANISOU 4185  CZ2 TRP B 156    12996   9048  13652    323   1710    352       C  
ATOM   4186  CZ3 TRP B 156      74.802  31.956 131.721  1.00 95.26           C  
ANISOU 4186  CZ3 TRP B 156    12997   9143  14055    313   1671    251       C  
ATOM   4187  CH2 TRP B 156      74.688  33.328 131.425  1.00 94.66           C  
ANISOU 4187  CH2 TRP B 156    13059   9132  13775    304   1798    275       C  
ATOM   4188  N   ALA B 157      78.584  30.649 137.519  1.00 99.89           N  
ANISOU 4188  N   ALA B 157    12842   9268  15842    224    510    561       N  
ATOM   4189  CA  ALA B 157      79.893  31.018 138.076  1.00101.76           C  
ANISOU 4189  CA  ALA B 157    12914   9387  16363    170    411    549       C  
ATOM   4190  C   ALA B 157      81.020  30.127 137.544  1.00104.05           C  
ANISOU 4190  C   ALA B 157    12922   9452  17158    188    435    444       C  
ATOM   4191  O   ALA B 157      82.088  30.625 137.189  1.00104.47           O  
ANISOU 4191  O   ALA B 157    12853   9393  17444    171    557    321       O  
ATOM   4192  CB  ALA B 157      79.855  30.963 139.598  1.00102.05           C  
ANISOU 4192  CB  ALA B 157    12952   9476  16343     88     72    739       C  
ATOM   4193  N   ALA B 158      80.769  28.818 137.478  1.00105.61           N  
ANISOU 4193  N   ALA B 158    13011   9574  17540    219    335    484       N  
ATOM   4194  CA  ALA B 158      81.716  27.847 136.904  1.00107.78           C  
ANISOU 4194  CA  ALA B 158    13005   9612  18332    240    388    370       C  
ATOM   4195  C   ALA B 158      82.037  28.158 135.442  1.00108.19           C  
ANISOU 4195  C   ALA B 158    13057   9610  18438    254    784    114       C  
ATOM   4196  O   ALA B 158      83.190  28.052 135.022  1.00110.51           O  
ANISOU 4196  O   ALA B 158    13133   9713  19142    239    895    -29       O  
ATOM   4197  CB  ALA B 158      81.171  26.430 137.028  1.00108.14           C  
ANISOU 4197  CB  ALA B 158    12971   9602  18514    272    246    453       C  
ATOM   4198  N   ALA B 159      81.011  28.532 134.677  1.00106.36           N  
ANISOU 4198  N   ALA B 159    13069   9546  17797    267    991     64       N  
ATOM   4199  CA  ALA B 159      81.204  29.087 133.334  1.00105.93           C  
ANISOU 4199  CA  ALA B 159    13081   9493  17672    243   1357   -147       C  
ATOM   4200  C   ALA B 159      81.920  30.437 133.406  1.00105.95           C  
ANISOU 4200  C   ALA B 159    13123   9506  17626    213   1445   -190       C  
ATOM   4201  O   ALA B 159      82.687  30.776 132.504  1.00107.33           O  
ANISOU 4201  O   ALA B 159    13238   9589  17953    174   1706   -381       O  
ATOM   4202  CB  ALA B 159      79.872  29.233 132.613  1.00104.07           C  
ANISOU 4202  CB  ALA B 159    13106   9453  16982    251   1501   -138       C  
ATOM   4203  N   GLY B 160      81.647  31.205 134.466  1.00104.89           N  
ANISOU 4203  N   GLY B 160    13095   9484  17272    214   1246    -26       N  
ATOM   4204  CA  GLY B 160      82.365  32.455 134.738  1.00105.00           C  
ANISOU 4204  CA  GLY B 160    13128   9499  17268    178   1293    -55       C  
ATOM   4205  C   GLY B 160      81.615  33.644 134.184  1.00103.27           C  
ANISOU 4205  C   GLY B 160    13174   9443  16620    178   1502    -69       C  
ATOM   4206  O   GLY B 160      82.199  34.490 133.504  1.00103.73           O  
ANISOU 4206  O   GLY B 160    13254   9467  16691    149   1730   -196       O  
ATOM   4207  N   SER B 161      80.318  33.702 134.490  1.00101.33           N  
ANISOU 4207  N   SER B 161    13122   9364  16014    207   1419     68       N  
ATOM   4208  CA  SER B 161      79.437  34.760 134.000  1.00 99.51           C  
ANISOU 4208  CA  SER B 161    13133   9281  15395    217   1588     90       C  
ATOM   4209  C   SER B 161      78.834  35.524 135.175  1.00 98.19           C  
ANISOU 4209  C   SER B 161    13089   9227  14990    213   1425    238       C  
ATOM   4210  O   SER B 161      78.498  34.932 136.204  1.00 97.97           O  
ANISOU 4210  O   SER B 161    13034   9230  14957    206   1177    355       O  
ATOM   4211  CB  SER B 161      78.335  34.157 133.138  1.00 98.52           C  
ANISOU 4211  CB  SER B 161    13123   9246  15063    246   1678    102       C  
ATOM   4212  OG  SER B 161      78.869  33.552 131.977  1.00 99.66           O  
ANISOU 4212  OG  SER B 161    13177   9296  15391    217   1874    -62       O  
ATOM   4213  N   MET B 162      78.704  36.839 135.007  1.00 97.43           N  
ANISOU 4213  N   MET B 162    13128   9186  14705    203   1577    228       N  
ATOM   4214  CA  MET B 162      78.252  37.733 136.075  1.00 96.67           C  
ANISOU 4214  CA  MET B 162    13140   9174  14413    179   1482    326       C  
ATOM   4215  C   MET B 162      76.731  37.859 136.096  1.00 93.75           C  
ANISOU 4215  C   MET B 162    12952   8943  13722    221   1483    437       C  
ATOM   4216  O   MET B 162      76.055  37.560 135.108  1.00 92.66           O  
ANISOU 4216  O   MET B 162    12882   8846  13478    269   1595    439       O  
ATOM   4217  CB  MET B 162      78.870  39.127 135.898  1.00 98.44           C  
ANISOU 4217  CB  MET B 162    13405   9366  14629    148   1663    253       C  
ATOM   4218  CG  MET B 162      80.391  39.162 135.791  1.00100.92           C  
ANISOU 4218  CG  MET B 162    13540   9541  15264    104   1697    127       C  
ATOM   4219  SD  MET B 162      81.261  38.547 137.252  1.00103.55           S  
ANISOU 4219  SD  MET B 162    13682   9814  15847     34   1370    176       S  
ATOM   4220  CE  MET B 162      81.404  36.789 136.910  1.00104.12           C  
ANISOU 4220  CE  MET B 162    13577   9798  16185     77   1237    181       C  
ATOM   4221  N   GLY B 163      76.206  38.305 137.235  1.00 91.87           N  
ANISOU 4221  N   GLY B 163    12790   8777  13337    185   1362    523       N  
ATOM   4222  CA  GLY B 163      74.783  38.607 137.379  1.00 89.81           C  
ANISOU 4222  CA  GLY B 163    12690   8632  12800    217   1381    615       C  
ATOM   4223  C   GLY B 163      73.900  37.376 137.443  1.00 88.18           C  
ANISOU 4223  C   GLY B 163    12490   8486  12525    251   1239    693       C  
ATOM   4224  O   GLY B 163      74.385  36.259 137.644  1.00 88.69           O  
ANISOU 4224  O   GLY B 163    12434   8504  12758    239   1086    692       O  
ATOM   4225  N   GLU B 164      72.596  37.592 137.263  1.00 85.82           N  
ANISOU 4225  N   GLU B 164    12323   8282  12003    294   1291    763       N  
ATOM   4226  CA  GLU B 164      71.611  36.511 137.306  1.00 83.77           C  
ANISOU 4226  CA  GLU B 164    12086   8091  11649    326   1174    837       C  
ATOM   4227  C   GLU B 164      71.783  35.588 136.099  1.00 83.47           C  
ANISOU 4227  C   GLU B 164    11986   8024  11703    373   1230    792       C  
ATOM   4228  O   GLU B 164      72.104  36.063 135.006  1.00 83.51           O  
ANISOU 4228  O   GLU B 164    12004   8002  11723    390   1416    729       O  
ATOM   4229  CB  GLU B 164      70.186  37.070 137.313  1.00 82.24           C  
ANISOU 4229  CB  GLU B 164    12033   7994  11219    361   1239    914       C  
ATOM   4230  CG  GLU B 164      69.113  36.047 137.675  1.00 81.36           C  
ANISOU 4230  CG  GLU B 164    11950   7961  10999    375   1099    991       C  
ATOM   4231  CD  GLU B 164      67.697  36.546 137.446  1.00 80.35           C  
ANISOU 4231  CD  GLU B 164    11936   7915  10678    423   1183   1061       C  
ATOM   4232  OE1 GLU B 164      67.510  37.730 137.093  1.00 80.32           O  
ANISOU 4232  OE1 GLU B 164    11986   7898  10633    445   1339   1065       O  
ATOM   4233  OE2 GLU B 164      66.757  35.738 137.611  1.00 79.32           O  
ANISOU 4233  OE2 GLU B 164    11831   7850  10456    439   1090   1117       O  
ATOM   4234  N   PRO B 165      71.584  34.268 136.291  1.00 83.35           N  
ANISOU 4234  N   PRO B 165    11906   8011  11750    378   1079    817       N  
ATOM   4235  CA  PRO B 165      71.597  33.346 135.155  1.00 83.41           C  
ANISOU 4235  CA  PRO B 165    11863   7996  11831    408   1153    759       C  
ATOM   4236  C   PRO B 165      70.560  33.644 134.063  1.00 82.91           C  
ANISOU 4236  C   PRO B 165    11929   8032  11540    442   1308    781       C  
ATOM   4237  O   PRO B 165      69.339  33.640 134.319  1.00 81.74           O  
ANISOU 4237  O   PRO B 165    11877   7985  11194    470   1253    880       O  
ATOM   4238  CB  PRO B 165      71.311  31.993 135.802  1.00 83.47           C  
ANISOU 4238  CB  PRO B 165    11800   7999  11913    406    946    811       C  
ATOM   4239  CG  PRO B 165      71.857  32.117 137.178  1.00 83.86           C  
ANISOU 4239  CG  PRO B 165    11799   8012  12051    352    754    866       C  
ATOM   4240  CD  PRO B 165      71.618  33.543 137.578  1.00 83.55           C  
ANISOU 4240  CD  PRO B 165    11880   8034  11831    331    835    885       C  
ATOM   4241  N   VAL B 166      71.079  33.931 132.868  1.00 84.33           N  
ANISOU 4241  N   VAL B 166    12107   8180  11755    425   1498    692       N  
ATOM   4242  CA  VAL B 166      70.304  33.960 131.634  1.00 84.93           C  
ANISOU 4242  CA  VAL B 166    12283   8342  11643    421   1633    705       C  
ATOM   4243  C   VAL B 166      70.411  32.577 130.992  1.00 86.23           C  
ANISOU 4243  C   VAL B 166    12371   8489  11901    391   1640    617       C  
ATOM   4244  O   VAL B 166      71.521  32.058 130.813  1.00 87.85           O  
ANISOU 4244  O   VAL B 166    12446   8575  12357    356   1686    486       O  
ATOM   4245  CB  VAL B 166      70.839  35.017 130.646  1.00 85.54           C  
ANISOU 4245  CB  VAL B 166    12416   8400  11686    380   1843    655       C  
ATOM   4246  CG1 VAL B 166      70.021  35.017 129.353  1.00 85.58           C  
ANISOU 4246  CG1 VAL B 166    12535   8509  11473    344   1955    694       C  
ATOM   4247  CG2 VAL B 166      70.834  36.395 131.298  1.00 85.61           C  
ANISOU 4247  CG2 VAL B 166    12481   8399  11646    408   1853    727       C  
ATOM   4248  N   ILE B 167      69.264  31.995 130.642  1.00 86.09           N  
ANISOU 4248  N   ILE B 167    12424   8579  11705    401   1604    682       N  
ATOM   4249  CA  ILE B 167      69.195  30.617 130.135  1.00 86.89           C  
ANISOU 4249  CA  ILE B 167    12459   8672  11883    369   1605    601       C  
ATOM   4250  C   ILE B 167      68.065  30.434 129.126  1.00 86.66           C  
ANISOU 4250  C   ILE B 167    12550   8785  11592    334   1672    643       C  
ATOM   4251  O   ILE B 167      67.141  31.255 129.052  1.00 85.83           O  
ANISOU 4251  O   ILE B 167    12567   8787  11258    360   1657    776       O  
ATOM   4252  CB  ILE B 167      69.029  29.576 131.282  1.00 86.90           C  
ANISOU 4252  CB  ILE B 167    12365   8631  12018    414   1390    644       C  
ATOM   4253  CG1 ILE B 167      67.861  29.929 132.229  1.00 85.95           C  
ANISOU 4253  CG1 ILE B 167    12346   8618  11690    468   1235    807       C  
ATOM   4254  CG2 ILE B 167      70.317  29.436 132.088  1.00 87.73           C  
ANISOU 4254  CG2 ILE B 167    12316   8580  12435    415   1311    590       C  
ATOM   4255  CD1 ILE B 167      66.539  29.273 131.888  1.00 85.56           C  
ANISOU 4255  CD1 ILE B 167    12371   8689  11449    479   1200    869       C  
ATOM   4256  N   LYS B 168      68.161  29.357 128.342  1.00 87.50           N  
ANISOU 4256  N   LYS B 168    12610   8884  11752    267   1749    526       N  
ATOM   4257  CA  LYS B 168      67.037  28.889 127.532  1.00 87.14           C  
ANISOU 4257  CA  LYS B 168    12661   8980  11468    219   1772    563       C  
ATOM   4258  C   LYS B 168      65.981  28.368 128.495  1.00 85.59           C  
ANISOU 4258  C   LYS B 168    12469   8841  11210    307   1567    690       C  
ATOM   4259  O   LYS B 168      66.241  27.424 129.247  1.00 85.52           O  
ANISOU 4259  O   LYS B 168    12350   8747  11394    341   1460    655       O  
ATOM   4260  CB  LYS B 168      67.449  27.782 126.543  1.00 88.13           C  
ANISOU 4260  CB  LYS B 168    12726   9072  11685    104   1919    378       C  
ATOM   4261  CG  LYS B 168      66.263  27.079 125.881  1.00 87.82           C  
ANISOU 4261  CG  LYS B 168    12770   9181  11416     46   1912    409       C  
ATOM   4262  CD  LYS B 168      66.528  26.630 124.451  1.00 89.33           C  
ANISOU 4262  CD  LYS B 168    12992   9407  11540   -133   2134    240       C  
ATOM   4263  CE  LYS B 168      65.226  26.256 123.756  1.00 89.31           C  
ANISOU 4263  CE  LYS B 168    13109   9593  11231   -208   2108    314       C  
ATOM   4264  NZ  LYS B 168      65.371  26.152 122.278  1.00 90.98           N  
ANISOU 4264  NZ  LYS B 168    13405   9886  11276   -425   2324    186       N  
ATOM   4265  N   CYS B 169      64.802  28.989 128.464  1.00 84.26           N  
ANISOU 4265  N   CYS B 169    12420   8804  10788    338   1513    842       N  
ATOM   4266  CA  CYS B 169      63.737  28.678 129.408  1.00 82.62           C  
ANISOU 4266  CA  CYS B 169    12227   8653  10510    415   1338    962       C  
ATOM   4267  C   CYS B 169      63.175  27.272 129.191  1.00 83.29           C  
ANISOU 4267  C   CYS B 169    12280   8778  10587    388   1292    918       C  
ATOM   4268  O   CYS B 169      62.442  27.023 128.232  1.00 83.40           O  
ANISOU 4268  O   CYS B 169    12359   8905  10424    328   1348    926       O  
ATOM   4269  CB  CYS B 169      62.614  29.715 129.312  1.00 81.22           C  
ANISOU 4269  CB  CYS B 169    12163   8588  10106    450   1318   1123       C  
ATOM   4270  SG  CYS B 169      61.232  29.434 130.446  1.00 79.12           S  
ANISOU 4270  SG  CYS B 169    11916   8388   9758    531   1139   1250       S  
ATOM   4271  N   GLU B 170      63.549  26.366 130.092  1.00 83.85           N  
ANISOU 4271  N   GLU B 170    12249   8754  10857    420   1185    879       N  
ATOM   4272  CA  GLU B 170      63.082  24.987 130.090  1.00 84.16           C  
ANISOU 4272  CA  GLU B 170    12240   8800  10936    404   1128    842       C  
ATOM   4273  C   GLU B 170      62.518  24.675 131.465  1.00 83.36           C  
ANISOU 4273  C   GLU B 170    12128   8693  10849    473    926    953       C  
ATOM   4274  O   GLU B 170      63.047  25.142 132.477  1.00 83.21           O  
ANISOU 4274  O   GLU B 170    12082   8602  10930    506    835    999       O  
ATOM   4275  CB  GLU B 170      64.245  24.048 129.784  1.00 85.88           C  
ANISOU 4275  CB  GLU B 170    12316   8868  11446    356   1205    675       C  
ATOM   4276  CG  GLU B 170      64.786  24.184 128.367  1.00 87.97           C  
ANISOU 4276  CG  GLU B 170    12592   9137  11693    251   1437    527       C  
ATOM   4277  CD  GLU B 170      66.171  23.586 128.194  1.00 90.07           C  
ANISOU 4277  CD  GLU B 170    12697   9214  12311    209   1543    347       C  
ATOM   4278  OE1 GLU B 170      67.081  23.951 128.972  1.00 90.36           O  
ANISOU 4278  OE1 GLU B 170    12645   9125  12564    264   1476    360       O  
ATOM   4279  OE2 GLU B 170      66.356  22.762 127.269  1.00 91.88           O  
ANISOU 4279  OE2 GLU B 170    12881   9416  12610    111   1700    186       O  
ATOM   4280  N   PHE B 171      61.459  23.870 131.497  1.00 83.20           N  
ANISOU 4280  N   PHE B 171    12136   8753  10722    474    860    991       N  
ATOM   4281  CA  PHE B 171      60.778  23.516 132.745  1.00 82.42           C  
ANISOU 4281  CA  PHE B 171    12047   8665  10602    516    681   1094       C  
ATOM   4282  C   PHE B 171      61.716  22.812 133.724  1.00 83.22           C  
ANISOU 4282  C   PHE B 171    12035   8617  10966    515    558   1081       C  
ATOM   4283  O   PHE B 171      61.847  23.224 134.877  1.00 82.67           O  
ANISOU 4283  O   PHE B 171    11978   8522  10909    526    431   1164       O  
ATOM   4284  CB  PHE B 171      59.573  22.623 132.445  1.00 81.80           C  
ANISOU 4284  CB  PHE B 171    12003   8687  10390    505    654   1111       C  
ATOM   4285  CG  PHE B 171      58.707  22.347 133.638  1.00 80.72           C  
ANISOU 4285  CG  PHE B 171    11899   8581  10189    534    495   1214       C  
ATOM   4286  CD1 PHE B 171      57.685  23.222 133.985  1.00 79.94           C  
ANISOU 4286  CD1 PHE B 171    11894   8585   9892    563    476   1311       C  
ATOM   4287  CD2 PHE B 171      58.906  21.207 134.408  1.00 81.14           C  
ANISOU 4287  CD2 PHE B 171    11883   8551  10395    522    371   1214       C  
ATOM   4288  CE1 PHE B 171      56.878  22.969 135.080  1.00 79.64           C  
ANISOU 4288  CE1 PHE B 171    11891   8574   9794    567    356   1384       C  
ATOM   4289  CE2 PHE B 171      58.108  20.949 135.504  1.00 80.91           C  
ANISOU 4289  CE2 PHE B 171    11900   8557  10284    522    231   1308       C  
ATOM   4290  CZ  PHE B 171      57.088  21.832 135.843  1.00 80.13           C  
ANISOU 4290  CZ  PHE B 171    11905   8570   9971    539    234   1382       C  
ATOM   4291  N   GLU B 172      62.375  21.762 133.240  1.00 85.10           N  
ANISOU 4291  N   GLU B 172    12158   8752  11423    488    598    976       N  
ATOM   4292  CA  GLU B 172      63.323  20.989 134.051  1.00 86.97           C  
ANISOU 4292  CA  GLU B 172    12253   8820  11970    486    470    976       C  
ATOM   4293  C   GLU B 172      64.573  21.775 134.496  1.00 87.58           C  
ANISOU 4293  C   GLU B 172    12266   8790  12219    488    449    975       C  
ATOM   4294  O   GLU B 172      65.259  21.350 135.426  1.00 88.90           O  
ANISOU 4294  O   GLU B 172    12331   8837  12610    482    287   1029       O  
ATOM   4295  CB  GLU B 172      63.737  19.682 133.343  1.00 88.58           C  
ANISOU 4295  CB  GLU B 172    12323   8910  12421    457    547    848       C  
ATOM   4296  CG  GLU B 172      64.545  19.828 132.053  1.00 90.23           C  
ANISOU 4296  CG  GLU B 172    12474   9064  12742    412    784    669       C  
ATOM   4297  CD  GLU B 172      63.707  19.682 130.794  1.00 90.78           C  
ANISOU 4297  CD  GLU B 172    12640   9275  12576    355    961    580       C  
ATOM   4298  OE1 GLU B 172      62.683  20.390 130.657  1.00 89.77           O  
ANISOU 4298  OE1 GLU B 172    12665   9325  12119    365    949    672       O  
ATOM   4299  OE2 GLU B 172      64.079  18.855 129.941  1.00 92.38           O  
ANISOU 4299  OE2 GLU B 172    12757   9405  12935    288   1112    418       O  
ATOM   4300  N   LYS B 173      64.869  22.895 133.831  1.00 87.11           N  
ANISOU 4300  N   LYS B 173    12263   8773  12062    488    602    923       N  
ATOM   4301  CA  LYS B 173      65.983  23.763 134.220  1.00 87.32           C  
ANISOU 4301  CA  LYS B 173    12241   8714  12222    488    598    916       C  
ATOM   4302  C   LYS B 173      65.667  24.651 135.429  1.00 85.76           C  
ANISOU 4302  C   LYS B 173    12133   8576  11872    496    458   1049       C  
ATOM   4303  O   LYS B 173      66.569  24.951 136.217  1.00 85.46           O  
ANISOU 4303  O   LYS B 173    12031   8452  11988    476    360   1076       O  
ATOM   4304  CB  LYS B 173      66.426  24.633 133.032  1.00 88.16           C  
ANISOU 4304  CB  LYS B 173    12380   8837  12279    472    828    807       C  
ATOM   4305  CG  LYS B 173      67.748  25.373 133.225  1.00 89.41           C  
ANISOU 4305  CG  LYS B 173    12459   8880  12632    464    862    759       C  
ATOM   4306  CD  LYS B 173      68.931  24.423 133.370  1.00 91.41           C  
ANISOU 4306  CD  LYS B 173    12506   8939  13285    448    821    675       C  
ATOM   4307  CE  LYS B 173      70.254  25.161 133.328  1.00 93.01           C  
ANISOU 4307  CE  LYS B 173    12619   9027  13693    433    891    601       C  
ATOM   4308  NZ  LYS B 173      71.402  24.251 133.604  1.00 95.00           N  
ANISOU 4308  NZ  LYS B 173    12641   9070  14384    423    821    542       N  
ATOM   4309  N   VAL B 174      64.407  25.075 135.566  1.00 83.89           N  
ANISOU 4309  N   VAL B 174    12038   8484  11350    511    457   1124       N  
ATOM   4310  CA  VAL B 174      63.992  25.968 136.670  1.00 82.50           C  
ANISOU 4310  CA  VAL B 174    11955   8367  11022    500    369   1222       C  
ATOM   4311  C   VAL B 174      63.167  25.285 137.768  1.00 81.73           C  
ANISOU 4311  C   VAL B 174    11898   8314  10841    470    192   1318       C  
ATOM   4312  O   VAL B 174      63.360  25.582 138.945  1.00 81.34           O  
ANISOU 4312  O   VAL B 174    11872   8255  10779    413     66   1382       O  
ATOM   4313  CB  VAL B 174      63.259  27.245 136.165  1.00 81.86           C  
ANISOU 4313  CB  VAL B 174    11994   8390  10717    531    517   1235       C  
ATOM   4314  CG1 VAL B 174      64.109  27.971 135.128  1.00 82.60           C  
ANISOU 4314  CG1 VAL B 174    12063   8441  10878    540    686   1154       C  
ATOM   4315  CG2 VAL B 174      61.862  26.944 135.619  1.00 81.07           C  
ANISOU 4315  CG2 VAL B 174    11970   8409  10424    559    551   1272       C  
ATOM   4316  N   ILE B 175      62.257  24.383 137.393  1.00 81.17           N  
ANISOU 4316  N   ILE B 175    11842   8296  10700    488    186   1325       N  
ATOM   4317  CA  ILE B 175      61.426  23.671 138.371  1.00 80.80           C  
ANISOU 4317  CA  ILE B 175    11839   8291  10569    452     31   1410       C  
ATOM   4318  C   ILE B 175      62.156  22.407 138.827  1.00 81.84           C  
ANISOU 4318  C   ILE B 175    11851   8301  10941    418   -129   1433       C  
ATOM   4319  O   ILE B 175      62.677  21.652 138.003  1.00 82.68           O  
ANISOU 4319  O   ILE B 175    11846   8323  11242    447    -75   1359       O  
ATOM   4320  CB  ILE B 175      60.035  23.300 137.796  1.00 79.91           C  
ANISOU 4320  CB  ILE B 175    11795   8292  10273    485     94   1412       C  
ATOM   4321  CG1 ILE B 175      59.281  24.551 137.306  1.00 79.24           C  
ANISOU 4321  CG1 ILE B 175    11804   8309   9991    522    235   1415       C  
ATOM   4322  CG2 ILE B 175      59.200  22.541 138.826  1.00 79.43           C  
ANISOU 4322  CG2 ILE B 175    11778   8267  10132    439    -54   1489       C  
ATOM   4323  CD1 ILE B 175      58.816  25.505 138.386  1.00 78.87           C  
ANISOU 4323  CD1 ILE B 175    11843   8301   9823    492    208   1471       C  
ATOM   4324  N   SER B 176      62.189  22.189 140.143  1.00 81.79           N  
ANISOU 4324  N   SER B 176    11865   8281  10928    342   -322   1536       N  
ATOM   4325  CA  SER B 176      62.837  21.017 140.738  1.00 81.99           C  
ANISOU 4325  CA  SER B 176    11777   8186  11189    296   -520   1605       C  
ATOM   4326  C   SER B 176      61.993  19.767 140.491  1.00 81.10           C  
ANISOU 4326  C   SER B 176    11655   8082  11075    314   -545   1615       C  
ATOM   4327  O   SER B 176      60.795  19.766 140.776  1.00 79.51           O  
ANISOU 4327  O   SER B 176    11576   8001  10630    297   -541   1647       O  
ATOM   4328  CB  SER B 176      63.028  21.232 142.246  1.00 82.92           C  
ANISOU 4328  CB  SER B 176    11948   8312  11243    175   -733   1734       C  
ATOM   4329  OG  SER B 176      63.606  20.099 142.871  1.00 84.57           O  
ANISOU 4329  OG  SER B 176    12048   8403  11679    118   -959   1840       O  
ATOM   4330  N   MET B 177      62.613  18.713 139.960  1.00 81.51           N  
ANISOU 4330  N   MET B 177    11554   7997  11416    343   -558   1578       N  
ATOM   4331  CA  MET B 177      61.916  17.433 139.755  1.00 81.25           C  
ANISOU 4331  CA  MET B 177    11495   7950  11425    351   -583   1582       C  
ATOM   4332  C   MET B 177      61.509  16.780 141.073  1.00 81.34           C  
ANISOU 4332  C   MET B 177    11549   7960  11395    268   -824   1744       C  
ATOM   4333  O   MET B 177      60.445  16.168 141.153  1.00 81.32           O  
ANISOU 4333  O   MET B 177    11618   8028  11249    258   -831   1764       O  
ATOM   4334  CB  MET B 177      62.755  16.460 138.916  1.00 82.20           C  
ANISOU 4334  CB  MET B 177    11424   7897  11911    387   -520   1488       C  
ATOM   4335  CG  MET B 177      62.811  16.838 137.446  1.00 81.89           C  
ANISOU 4335  CG  MET B 177    11374   7891  11847    437   -247   1305       C  
ATOM   4336  SD  MET B 177      61.206  16.698 136.633  1.00 80.74           S  
ANISOU 4336  SD  MET B 177    11375   7941  11360    450   -100   1246       S  
ATOM   4337  CE  MET B 177      61.229  18.193 135.629  1.00 80.47           C  
ANISOU 4337  CE  MET B 177    11434   8028  11110    473    113   1158       C  
ATOM   4338  N   GLU B 178      62.343  16.938 142.099  1.00 81.65           N  
ANISOU 4338  N   GLU B 178    11552   7925  11543    192  -1022   1863       N  
ATOM   4339  CA  GLU B 178      62.011  16.504 143.465  1.00 81.82           C  
ANISOU 4339  CA  GLU B 178    11645   7967  11473     69  -1267   2036       C  
ATOM   4340  C   GLU B 178      60.679  17.099 143.939  1.00 79.63           C  
ANISOU 4340  C   GLU B 178    11582   7885  10788     16  -1211   2038       C  
ATOM   4341  O   GLU B 178      59.812  16.376 144.449  1.00 79.62           O  
ANISOU 4341  O   GLU B 178    11651   7927  10672    -41  -1293   2105       O  
ATOM   4342  CB  GLU B 178      63.142  16.880 144.426  1.00 83.55           C  
ANISOU 4342  CB  GLU B 178    11814   8112  11818    -28  -1475   2157       C  
ATOM   4343  CG  GLU B 178      64.407  16.058 144.205  1.00 85.65           C  
ANISOU 4343  CG  GLU B 178    11842   8155  12546      4  -1591   2198       C  
ATOM   4344  CD  GLU B 178      65.628  16.633 144.891  1.00 87.34           C  
ANISOU 4344  CD  GLU B 178    11979   8297  12906    -70  -1759   2288       C  
ATOM   4345  OE1 GLU B 178      65.934  17.823 144.666  1.00 86.95           O  
ANISOU 4345  OE1 GLU B 178    11980   8316  12739    -54  -1627   2195       O  
ATOM   4346  OE2 GLU B 178      66.295  15.884 145.637  1.00 89.29           O  
ANISOU 4346  OE2 GLU B 178    12109   8413  13403   -148  -2029   2460       O  
ATOM   4347  N   TYR B 179      60.518  18.406 143.736  1.00 77.48           N  
ANISOU 4347  N   TYR B 179    11399   7714  10324     36  -1058   1958       N  
ATOM   4348  CA  TYR B 179      59.243  19.098 143.983  1.00 75.85           C  
ANISOU 4348  CA  TYR B 179    11364   7671   9783      9   -949   1927       C  
ATOM   4349  C   TYR B 179      58.091  18.465 143.191  1.00 74.05           C  
ANISOU 4349  C   TYR B 179    11154   7501   9477     90   -832   1867       C  
ATOM   4350  O   TYR B 179      57.040  18.155 143.755  1.00 73.78           O  
ANISOU 4350  O   TYR B 179    11220   7548   9264     30   -863   1903       O  
ATOM   4351  CB  TYR B 179      59.359  20.607 143.671  1.00 75.30           C  
ANISOU 4351  CB  TYR B 179    11347   7663   9599     45   -778   1843       C  
ATOM   4352  CG  TYR B 179      58.028  21.298 143.442  1.00 74.40           C  
ANISOU 4352  CG  TYR B 179    11353   7682   9233     75   -607   1782       C  
ATOM   4353  CD1 TYR B 179      57.224  21.681 144.516  1.00 74.56           C  
ANISOU 4353  CD1 TYR B 179    11504   7786   9037    -43   -630   1812       C  
ATOM   4354  CD2 TYR B 179      57.565  21.554 142.149  1.00 73.62           C  
ANISOU 4354  CD2 TYR B 179    11230   7619   9122    205   -424   1697       C  
ATOM   4355  CE1 TYR B 179      55.992  22.296 144.304  1.00 73.91           C  
ANISOU 4355  CE1 TYR B 179    11503   7800   8778    -10   -467   1753       C  
ATOM   4356  CE2 TYR B 179      56.340  22.169 141.933  1.00 72.73           C  
ANISOU 4356  CE2 TYR B 179    11203   7613   8816    235   -292   1666       C  
ATOM   4357  CZ  TYR B 179      55.556  22.540 143.013  1.00 73.04           C  
ANISOU 4357  CZ  TYR B 179    11349   7714   8688    137   -310   1691       C  
ATOM   4358  OH  TYR B 179      54.341  23.156 142.805  1.00 72.23           O  
ANISOU 4358  OH  TYR B 179    11304   7694   8446    170   -171   1656       O  
ATOM   4359  N   MET B 180      58.301  18.265 141.893  1.00 73.09           N  
ANISOU 4359  N   MET B 180    10940   7345   9486    207   -694   1771       N  
ATOM   4360  CA  MET B 180      57.250  17.728 141.018  1.00 72.16           C  
ANISOU 4360  CA  MET B 180    10837   7296   9283    271   -574   1705       C  
ATOM   4361  C   MET B 180      56.824  16.306 141.385  1.00 72.82           C  
ANISOU 4361  C   MET B 180    10894   7338   9436    232   -696   1759       C  
ATOM   4362  O   MET B 180      55.632  15.994 141.375  1.00 72.44           O  
ANISOU 4362  O   MET B 180    10921   7384   9215    226   -662   1753       O  
ATOM   4363  CB  MET B 180      57.679  17.790 139.546  1.00 71.94           C  
ANISOU 4363  CB  MET B 180    10722   7241   9370    363   -401   1584       C  
ATOM   4364  CG  MET B 180      57.380  19.117 138.868  1.00 70.99           C  
ANISOU 4364  CG  MET B 180    10670   7223   9077    411   -234   1529       C  
ATOM   4365  SD  MET B 180      55.676  19.210 138.286  1.00 69.83           S  
ANISOU 4365  SD  MET B 180    10620   7244   8668    441   -128   1513       S  
ATOM   4366  CE  MET B 180      54.916  20.245 139.524  1.00 69.45           C  
ANISOU 4366  CE  MET B 180    10694   7271   8421    397   -167   1587       C  
ATOM   4367  N   VAL B 181      57.797  15.460 141.717  1.00 74.07           N  
ANISOU 4367  N   VAL B 181    10936   7343   9864    204   -842   1819       N  
ATOM   4368  CA  VAL B 181      57.539  14.062 142.064  1.00 74.69           C  
ANISOU 4368  CA  VAL B 181    10967   7346  10064    167   -969   1886       C  
ATOM   4369  C   VAL B 181      57.039  13.926 143.505  1.00 74.77           C  
ANISOU 4369  C   VAL B 181    11096   7403   9909     36  -1162   2035       C  
ATOM   4370  O   VAL B 181      55.929  13.421 143.736  1.00 74.25           O  
ANISOU 4370  O   VAL B 181    11116   7414   9681      3  -1160   2047       O  
ATOM   4371  CB  VAL B 181      58.791  13.188 141.821  1.00 76.13           C  
ANISOU 4371  CB  VAL B 181    10951   7317  10656    189  -1047   1899       C  
ATOM   4372  CG1 VAL B 181      58.595  11.765 142.343  1.00 77.34           C  
ANISOU 4372  CG1 VAL B 181    11047   7365  10972    141  -1208   2002       C  
ATOM   4373  CG2 VAL B 181      59.126  13.167 140.330  1.00 75.98           C  
ANISOU 4373  CG2 VAL B 181    10829   7259  10780    288   -816   1718       C  
ATOM   4374  N   TYR B 182      57.847  14.378 144.464  1.00 75.39           N  
ANISOU 4374  N   TYR B 182    11184   7441  10018    -54  -1323   2143       N  
ATOM   4375  CA  TYR B 182      57.537  14.161 145.886  1.00 76.05           C  
ANISOU 4375  CA  TYR B 182    11382   7561   9952   -224  -1529   2297       C  
ATOM   4376  C   TYR B 182      56.397  15.060 146.365  1.00 74.95           C  
ANISOU 4376  C   TYR B 182    11437   7604   9436   -294  -1421   2249       C  
ATOM   4377  O   TYR B 182      55.424  14.579 146.949  1.00 74.55           O  
ANISOU 4377  O   TYR B 182    11490   7619   9215   -382  -1458   2288       O  
ATOM   4378  CB  TYR B 182      58.772  14.360 146.779  1.00 77.35           C  
ANISOU 4378  CB  TYR B 182    11499   7637  10253   -333  -1752   2437       C  
ATOM   4379  CG  TYR B 182      59.990  13.525 146.404  1.00 78.37           C  
ANISOU 4379  CG  TYR B 182    11406   7556  10815   -270  -1873   2495       C  
ATOM   4380  CD1 TYR B 182      59.878  12.163 146.107  1.00 78.88           C  
ANISOU 4380  CD1 TYR B 182    11359   7497  11114   -229  -1929   2533       C  
ATOM   4381  CD2 TYR B 182      61.265  14.096 146.371  1.00 78.91           C  
ANISOU 4381  CD2 TYR B 182    11362   7535  11083   -258  -1924   2507       C  
ATOM   4382  CE1 TYR B 182      60.991  11.406 145.766  1.00 80.17           C  
ANISOU 4382  CE1 TYR B 182    11295   7441  11723   -172  -2019   2575       C  
ATOM   4383  CE2 TYR B 182      62.385  13.339 146.042  1.00 80.23           C  
ANISOU 4383  CE2 TYR B 182    11303   7490  11689   -202  -2025   2553       C  
ATOM   4384  CZ  TYR B 182      62.243  11.999 145.738  1.00 80.81           C  
ANISOU 4384  CZ  TYR B 182    11258   7431  12013   -158  -2067   2584       C  
ATOM   4385  OH  TYR B 182      63.350  11.254 145.412  1.00 82.29           O  
ANISOU 4385  OH  TYR B 182    11199   7382  12684   -104  -2148   2618       O  
ATOM   4386  N   PHE B 183      56.508  16.358 146.102  1.00 74.54           N  
ANISOU 4386  N   PHE B 183    11424   7619   9276   -257  -1275   2159       N  
ATOM   4387  CA  PHE B 183      55.516  17.313 146.599  1.00 74.31           C  
ANISOU 4387  CA  PHE B 183    11556   7734   8945   -327  -1158   2106       C  
ATOM   4388  C   PHE B 183      54.252  17.312 145.736  1.00 73.12           C  
ANISOU 4388  C   PHE B 183    11428   7667   8686   -214   -961   1998       C  
ATOM   4389  O   PHE B 183      53.190  16.918 146.199  1.00 72.70           O  
ANISOU 4389  O   PHE B 183    11461   7680   8479   -281   -959   2005       O  
ATOM   4390  CB  PHE B 183      56.118  18.715 146.712  1.00 74.23           C  
ANISOU 4390  CB  PHE B 183    11569   7747   8886   -339  -1079   2057       C  
ATOM   4391  CG  PHE B 183      55.325  19.647 147.580  1.00 74.19           C  
ANISOU 4391  CG  PHE B 183    11723   7854   8612   -470   -995   2020       C  
ATOM   4392  CD1 PHE B 183      55.364  19.532 148.964  1.00 75.28           C  
ANISOU 4392  CD1 PHE B 183    11971   8021   8609   -699  -1147   2105       C  
ATOM   4393  CD2 PHE B 183      54.540  20.644 147.013  1.00 73.38           C  
ANISOU 4393  CD2 PHE B 183    11652   7820   8407   -380   -761   1899       C  
ATOM   4394  CE1 PHE B 183      54.631  20.393 149.766  1.00 75.64           C  
ANISOU 4394  CE1 PHE B 183    12163   8164   8412   -845  -1035   2039       C  
ATOM   4395  CE2 PHE B 183      53.808  21.508 147.810  1.00 73.61           C  
ANISOU 4395  CE2 PHE B 183    11805   7926   8236   -502   -657   1845       C  
ATOM   4396  CZ  PHE B 183      53.859  21.388 149.191  1.00 74.68           C  
ANISOU 4396  CZ  PHE B 183    12056   8091   8228   -740   -779   1899       C  
ATOM   4397  N   ASN B 184      54.370  17.719 144.477  1.00 72.59           N  
ANISOU 4397  N   ASN B 184    11282   7598   8701    -56   -805   1904       N  
ATOM   4398  CA  ASN B 184      53.194  17.874 143.616  1.00 71.87           C  
ANISOU 4398  CA  ASN B 184    11209   7598   8498     38   -632   1819       C  
ATOM   4399  C   ASN B 184      52.496  16.530 143.322  1.00 71.63           C  
ANISOU 4399  C   ASN B 184    11153   7569   8493     52   -669   1825       C  
ATOM   4400  O   ASN B 184      51.303  16.357 143.628  1.00 72.48           O  
ANISOU 4400  O   ASN B 184    11336   7758   8444     15   -636   1816       O  
ATOM   4401  CB  ASN B 184      53.580  18.593 142.317  1.00 71.65           C  
ANISOU 4401  CB  ASN B 184    11111   7571   8542    173   -480   1739       C  
ATOM   4402  CG  ASN B 184      52.403  18.789 141.382  1.00 71.34           C  
ANISOU 4402  CG  ASN B 184    11084   7632   8388    255   -331   1679       C  
ATOM   4403  OD1 ASN B 184      52.416  18.316 140.245  1.00 71.40           O  
ANISOU 4403  OD1 ASN B 184    11024   7641   8461    330   -272   1634       O  
ATOM   4404  ND2 ASN B 184      51.369  19.475 141.861  1.00 71.78           N  
ANISOU 4404  ND2 ASN B 184    11222   7768   8281    226   -269   1676       N  
ATOM   4405  N   PHE B 185      53.239  15.575 142.767  1.00 70.72           N  
ANISOU 4405  N   PHE B 185    10923   7351   8594     98   -727   1830       N  
ATOM   4406  CA  PHE B 185      52.645  14.322 142.287  1.00 69.49           C  
ANISOU 4406  CA  PHE B 185    10724   7185   8492    122   -726   1810       C  
ATOM   4407  C   PHE B 185      52.250  13.363 143.422  1.00 69.22           C  
ANISOU 4407  C   PHE B 185    10744   7124   8433      5   -891   1913       C  
ATOM   4408  O   PHE B 185      51.075  12.957 143.512  1.00 68.32           O  
ANISOU 4408  O   PHE B 185    10693   7089   8174    -16   -854   1895       O  
ATOM   4409  CB  PHE B 185      53.578  13.649 141.269  1.00 70.05           C  
ANISOU 4409  CB  PHE B 185    10646   7139   8829    198   -695   1755       C  
ATOM   4410  CG  PHE B 185      53.047  12.361 140.693  1.00 70.19           C  
ANISOU 4410  CG  PHE B 185    10607   7133   8926    214   -668   1710       C  
ATOM   4411  CD1 PHE B 185      51.749  12.281 140.188  1.00 69.33           C  
ANISOU 4411  CD1 PHE B 185    10561   7159   8622    232   -561   1648       C  
ATOM   4412  CD2 PHE B 185      53.858  11.230 140.627  1.00 70.75           C  
ANISOU 4412  CD2 PHE B 185    10549   7038   9293    209   -744   1725       C  
ATOM   4413  CE1 PHE B 185      51.268  11.095 139.652  1.00 69.36           C  
ANISOU 4413  CE1 PHE B 185    10514   7146   8693    234   -529   1596       C  
ATOM   4414  CE2 PHE B 185      53.382  10.048 140.088  1.00 71.02           C  
ANISOU 4414  CE2 PHE B 185    10527   7039   9416    217   -698   1668       C  
ATOM   4415  CZ  PHE B 185      52.087   9.979 139.601  1.00 70.27           C  
ANISOU 4415  CZ  PHE B 185    10509   7094   9094    225   -589   1599       C  
ATOM   4416  N   PHE B 186      53.211  13.016 144.284  1.00 69.75           N  
ANISOU 4416  N   PHE B 186    10783   7081   8637    -77  -1079   2029       N  
ATOM   4417  CA  PHE B 186      52.955  12.054 145.377  1.00 70.14           C  
ANISOU 4417  CA  PHE B 186    10883   7092   8672   -211  -1265   2158       C  
ATOM   4418  C   PHE B 186      52.045  12.577 146.496  1.00 69.68           C  
ANISOU 4418  C   PHE B 186    11006   7159   8308   -358  -1283   2192       C  
ATOM   4419  O   PHE B 186      51.278  11.796 147.055  1.00 69.84           O  
ANISOU 4419  O   PHE B 186    11094   7201   8240   -448  -1344   2240       O  
ATOM   4420  CB  PHE B 186      54.257  11.513 146.002  1.00 71.28           C  
ANISOU 4420  CB  PHE B 186    10937   7077   9068   -276  -1495   2306       C  
ATOM   4421  CG  PHE B 186      55.097  10.646 145.088  1.00 71.69           C  
ANISOU 4421  CG  PHE B 186    10790   6961   9487   -162  -1494   2280       C  
ATOM   4422  CD1 PHE B 186      54.560   9.966 143.985  1.00 71.03           C  
ANISOU 4422  CD1 PHE B 186    10638   6870   9479    -57  -1334   2154       C  
ATOM   4423  CD2 PHE B 186      56.448  10.472 145.372  1.00 72.89           C  
ANISOU 4423  CD2 PHE B 186    10813   6951   9928   -179  -1656   2381       C  
ATOM   4424  CE1 PHE B 186      55.364   9.169 143.182  1.00 71.81           C  
ANISOU 4424  CE1 PHE B 186    10551   6802   9929     20  -1306   2107       C  
ATOM   4425  CE2 PHE B 186      57.252   9.672 144.572  1.00 73.67           C  
ANISOU 4425  CE2 PHE B 186    10708   6869  10410    -83  -1637   2343       C  
ATOM   4426  CZ  PHE B 186      56.711   9.020 143.477  1.00 73.15           C  
ANISOU 4426  CZ  PHE B 186    10584   6796  10414     12  -1449   2195       C  
ATOM   4427  N   VAL B 187      52.124  13.865 146.831  1.00 69.03           N  
ANISOU 4427  N   VAL B 187    11000   7152   8076   -394  -1215   2157       N  
ATOM   4428  CA  VAL B 187      51.255  14.440 147.878  1.00 69.17           C  
ANISOU 4428  CA  VAL B 187    11185   7280   7815   -552  -1187   2153       C  
ATOM   4429  C   VAL B 187      49.981  15.087 147.321  1.00 67.86           C  
ANISOU 4429  C   VAL B 187    11059   7225   7496   -472   -954   2013       C  
ATOM   4430  O   VAL B 187      48.901  14.874 147.863  1.00 67.71           O  
ANISOU 4430  O   VAL B 187    11134   7273   7316   -564   -916   1992       O  
ATOM   4431  CB  VAL B 187      52.011  15.453 148.778  1.00 69.86           C  
ANISOU 4431  CB  VAL B 187    11343   7380   7820   -686  -1247   2192       C  
ATOM   4432  CG1 VAL B 187      51.074  16.088 149.807  1.00 70.05           C  
ANISOU 4432  CG1 VAL B 187    11540   7516   7560   -869  -1169   2149       C  
ATOM   4433  CG2 VAL B 187      53.182  14.774 149.477  1.00 71.43           C  
ANISOU 4433  CG2 VAL B 187    11504   7475   8160   -798  -1517   2363       C  
ATOM   4434  N   TRP B 188      50.103  15.871 146.255  1.00 67.26           N  
ANISOU 4434  N   TRP B 188    10909   7164   7482   -312   -805   1925       N  
ATOM   4435  CA  TRP B 188      48.985  16.706 145.783  1.00 67.06           C  
ANISOU 4435  CA  TRP B 188    10909   7233   7335   -244   -604   1819       C  
ATOM   4436  C   TRP B 188      48.262  16.226 144.520  1.00 66.59           C  
ANISOU 4436  C   TRP B 188    10769   7208   7321    -96   -511   1763       C  
ATOM   4437  O   TRP B 188      47.235  16.807 144.156  1.00 66.48           O  
ANISOU 4437  O   TRP B 188    10766   7272   7222    -49   -374   1701       O  
ATOM   4438  CB  TRP B 188      49.452  18.164 145.630  1.00 66.83           C  
ANISOU 4438  CB  TRP B 188    10879   7212   7301   -205   -497   1774       C  
ATOM   4439  CG  TRP B 188      49.804  18.768 146.944  1.00 67.71           C  
ANISOU 4439  CG  TRP B 188    11093   7322   7309   -383   -544   1797       C  
ATOM   4440  CD1 TRP B 188      51.047  19.096 147.401  1.00 68.51           C  
ANISOU 4440  CD1 TRP B 188    11194   7370   7466   -448   -649   1851       C  
ATOM   4441  CD2 TRP B 188      48.892  19.077 147.995  1.00 68.21           C  
ANISOU 4441  CD2 TRP B 188    11279   7446   7191   -547   -483   1759       C  
ATOM   4442  NE1 TRP B 188      50.960  19.614 148.671  1.00 69.45           N  
ANISOU 4442  NE1 TRP B 188    11438   7525   7425   -653   -663   1852       N  
ATOM   4443  CE2 TRP B 188      49.648  19.608 149.062  1.00 69.55           C  
ANISOU 4443  CE2 TRP B 188    11531   7605   7288   -724   -552   1788       C  
ATOM   4444  CE3 TRP B 188      47.499  18.985 148.128  1.00 68.13           C  
ANISOU 4444  CE3 TRP B 188    11312   7495   7077   -572   -365   1692       C  
ATOM   4445  CZ2 TRP B 188      49.060  20.047 150.251  1.00 70.89           C  
ANISOU 4445  CZ2 TRP B 188    11839   7828   7268   -942   -491   1739       C  
ATOM   4446  CZ3 TRP B 188      46.912  19.405 149.313  1.00 69.42           C  
ANISOU 4446  CZ3 TRP B 188    11599   7697   7078   -774   -299   1640       C  
ATOM   4447  CH2 TRP B 188      47.697  19.928 150.365  1.00 70.87           C  
ANISOU 4447  CH2 TRP B 188    11877   7874   7174   -967   -355   1659       C  
ATOM   4448  N   VAL B 189      48.770  15.181 143.862  1.00 66.89           N  
ANISOU 4448  N   VAL B 189    10721   7186   7505    -36   -582   1783       N  
ATOM   4449  CA  VAL B 189      48.021  14.538 142.759  1.00 66.20           C  
ANISOU 4449  CA  VAL B 189    10573   7143   7436     57   -502   1724       C  
ATOM   4450  C   VAL B 189      47.496  13.142 143.135  1.00 66.48           C  
ANISOU 4450  C   VAL B 189    10618   7158   7480     -6   -588   1751       C  
ATOM   4451  O   VAL B 189      46.280  12.941 143.152  1.00 66.03           O  
ANISOU 4451  O   VAL B 189    10601   7182   7305    -21   -529   1716       O  
ATOM   4452  CB  VAL B 189      48.830  14.486 141.442  1.00 65.83           C  
ANISOU 4452  CB  VAL B 189    10416   7058   7538    171   -449   1678       C  
ATOM   4453  CG1 VAL B 189      48.029  13.811 140.333  1.00 65.45           C  
ANISOU 4453  CG1 VAL B 189    10319   7072   7474    228   -366   1611       C  
ATOM   4454  CG2 VAL B 189      49.237  15.890 141.005  1.00 65.55           C  
ANISOU 4454  CG2 VAL B 189    10379   7049   7478    231   -354   1655       C  
ATOM   4455  N   LEU B 190      48.381  12.188 143.437  1.00 66.91           N  
ANISOU 4455  N   LEU B 190    10629   7097   7696    -44   -727   1819       N  
ATOM   4456  CA  LEU B 190      47.944  10.779 143.604  1.00 67.55           C  
ANISOU 4456  CA  LEU B 190    10696   7136   7830    -88   -799   1846       C  
ATOM   4457  C   LEU B 190      46.853  10.522 144.663  1.00 67.55           C  
ANISOU 4457  C   LEU B 190    10820   7200   7642   -215   -835   1882       C  
ATOM   4458  O   LEU B 190      45.867   9.814 144.369  1.00 68.04           O  
ANISOU 4458  O   LEU B 190    10883   7307   7659   -208   -783   1836       O  
ATOM   4459  CB  LEU B 190      49.136   9.836 143.849  1.00 68.99           C  
ANISOU 4459  CB  LEU B 190    10793   7152   8266   -113   -957   1936       C  
ATOM   4460  CG  LEU B 190      49.995   9.467 142.642  1.00 69.67           C  
ANISOU 4460  CG  LEU B 190    10724   7143   8601      0   -894   1864       C  
ATOM   4461  CD1 LEU B 190      51.174   8.612 143.078  1.00 71.19           C  
ANISOU 4461  CD1 LEU B 190    10814   7144   9089    -32  -1061   1968       C  
ATOM   4462  CD2 LEU B 190      49.185   8.746 141.571  1.00 69.44           C  
ANISOU 4462  CD2 LEU B 190    10649   7163   8572     58   -758   1747       C  
ATOM   4463  N   PRO B 191      47.010  11.084 145.883  1.00 67.27           N  
ANISOU 4463  N   PRO B 191    10893   7174   7491   -349   -913   1953       N  
ATOM   4464  CA  PRO B 191      45.981  10.828 146.901  1.00 67.46           C  
ANISOU 4464  CA  PRO B 191    11046   7259   7326   -500   -926   1969       C  
ATOM   4465  C   PRO B 191      44.588  11.381 146.557  1.00 66.50           C  
ANISOU 4465  C   PRO B 191    10955   7258   7053   -460   -734   1845       C  
ATOM   4466  O   PRO B 191      43.607  10.649 146.729  1.00 66.94           O  
ANISOU 4466  O   PRO B 191    11044   7347   7042   -509   -714   1823       O  
ATOM   4467  CB  PRO B 191      46.564  11.443 148.186  1.00 68.36           C  
ANISOU 4467  CB  PRO B 191    11270   7365   7337   -674  -1031   2054       C  
ATOM   4468  CG  PRO B 191      48.014  11.613 147.920  1.00 68.64           C  
ANISOU 4468  CG  PRO B 191    11215   7304   7559   -613  -1138   2122       C  
ATOM   4469  CD  PRO B 191      48.159  11.812 146.441  1.00 67.52           C  
ANISOU 4469  CD  PRO B 191    10938   7156   7559   -398  -1003   2021       C  
ATOM   4470  N   PRO B 192      44.495  12.639 146.058  1.00 65.45           N  
ANISOU 4470  N   PRO B 192    10798   7179   6888   -372   -599   1770       N  
ATOM   4471  CA  PRO B 192      43.203  13.070 145.520  1.00 64.43           C  
ANISOU 4471  CA  PRO B 192    10652   7143   6684   -307   -435   1671       C  
ATOM   4472  C   PRO B 192      42.629  12.130 144.462  1.00 63.46           C  
ANISOU 4472  C   PRO B 192    10443   7045   6621   -206   -413   1637       C  
ATOM   4473  O   PRO B 192      41.455  11.780 144.548  1.00 62.82           O  
ANISOU 4473  O   PRO B 192    10380   7022   6465   -236   -356   1592       O  
ATOM   4474  CB  PRO B 192      43.520  14.433 144.913  1.00 64.07           C  
ANISOU 4474  CB  PRO B 192    10559   7116   6667   -201   -332   1634       C  
ATOM   4475  CG  PRO B 192      44.597  14.965 145.776  1.00 64.63           C  
ANISOU 4475  CG  PRO B 192    10690   7131   6734   -292   -405   1686       C  
ATOM   4476  CD  PRO B 192      45.421  13.783 146.185  1.00 65.31           C  
ANISOU 4476  CD  PRO B 192    10783   7140   6889   -361   -591   1781       C  
ATOM   4477  N   LEU B 193      43.457  11.714 143.501  1.00 62.99           N  
ANISOU 4477  N   LEU B 193    10292   6942   6699   -107   -449   1647       N  
ATOM   4478  CA  LEU B 193      43.013  10.809 142.427  1.00 62.79           C  
ANISOU 4478  CA  LEU B 193    10186   6942   6728    -35   -414   1597       C  
ATOM   4479  C   LEU B 193      42.491   9.493 142.980  1.00 62.49           C  
ANISOU 4479  C   LEU B 193    10179   6876   6688   -122   -480   1614       C  
ATOM   4480  O   LEU B 193      41.368   9.081 142.648  1.00 62.36           O  
ANISOU 4480  O   LEU B 193    10154   6934   6606   -119   -415   1556       O  
ATOM   4481  CB  LEU B 193      44.138  10.528 141.424  1.00 63.35           C  
ANISOU 4481  CB  LEU B 193    10159   6948   6960     47   -425   1586       C  
ATOM   4482  CG  LEU B 193      44.588  11.688 140.532  1.00 63.53           C  
ANISOU 4482  CG  LEU B 193    10140   7010   6985    140   -340   1556       C  
ATOM   4483  CD1 LEU B 193      45.828  11.267 139.754  1.00 64.11           C  
ANISOU 4483  CD1 LEU B 193    10128   6995   7235    184   -349   1535       C  
ATOM   4484  CD2 LEU B 193      43.479  12.150 139.591  1.00 63.18           C  
ANISOU 4484  CD2 LEU B 193    10073   7097   6833    197   -229   1502       C  
ATOM   4485  N   LEU B 194      43.290   8.853 143.835  1.00 62.20           N  
ANISOU 4485  N   LEU B 194    10174   6731   6728   -208   -618   1703       N  
ATOM   4486  CA  LEU B 194      42.881   7.579 144.438  1.00 62.25           C  
ANISOU 4486  CA  LEU B 194    10214   6691   6747   -304   -699   1746       C  
ATOM   4487  C   LEU B 194      41.628   7.736 145.312  1.00 61.69           C  
ANISOU 4487  C   LEU B 194    10258   6706   6473   -417   -655   1726       C  
ATOM   4488  O   LEU B 194      40.687   6.927 145.223  1.00 61.42           O  
ANISOU 4488  O   LEU B 194    10228   6703   6406   -442   -620   1685       O  
ATOM   4489  CB  LEU B 194      44.038   6.961 145.235  1.00 63.41           C  
ANISOU 4489  CB  LEU B 194    10367   6693   7032   -385   -884   1882       C  
ATOM   4490  CG  LEU B 194      45.274   6.548 144.421  1.00 63.74           C  
ANISOU 4490  CG  LEU B 194    10267   6610   7339   -284   -925   1893       C  
ATOM   4491  CD1 LEU B 194      46.374   6.050 145.346  1.00 64.88           C  
ANISOU 4491  CD1 LEU B 194    10405   6603   7642   -373  -1132   2054       C  
ATOM   4492  CD2 LEU B 194      44.932   5.496 143.375  1.00 63.79           C  
ANISOU 4492  CD2 LEU B 194    10171   6592   7473   -213   -843   1802       C  
ATOM   4493  N   LEU B 195      41.600   8.795 146.117  1.00 61.50           N  
ANISOU 4493  N   LEU B 195    10324   6720   6324   -492   -635   1736       N  
ATOM   4494  CA  LEU B 195      40.431   9.117 146.951  1.00 61.79           C  
ANISOU 4494  CA  LEU B 195    10464   6830   6180   -614   -551   1686       C  
ATOM   4495  C   LEU B 195      39.167   9.319 146.112  1.00 60.67           C  
ANISOU 4495  C   LEU B 195    10256   6782   6013   -515   -393   1568       C  
ATOM   4496  O   LEU B 195      38.113   8.780 146.442  1.00 60.49           O  
ANISOU 4496  O   LEU B 195    10269   6795   5918   -587   -348   1524       O  
ATOM   4497  CB  LEU B 195      40.714  10.361 147.810  1.00 62.21           C  
ANISOU 4497  CB  LEU B 195    10606   6901   6130   -708   -519   1686       C  
ATOM   4498  CG  LEU B 195      39.660  10.828 148.812  1.00 63.04           C  
ANISOU 4498  CG  LEU B 195    10826   7065   6062   -872   -406   1613       C  
ATOM   4499  CD1 LEU B 195      39.251   9.697 149.746  1.00 64.01           C  
ANISOU 4499  CD1 LEU B 195    11058   7174   6088  -1059   -490   1662       C  
ATOM   4500  CD2 LEU B 195      40.191  12.015 149.602  1.00 63.70           C  
ANISOU 4500  CD2 LEU B 195    10988   7148   6066   -977   -375   1608       C  
ATOM   4501  N   MET B 196      39.284  10.082 145.027  1.00 59.91           N  
ANISOU 4501  N   MET B 196    10060   6722   5978   -359   -319   1527       N  
ATOM   4502  CA  MET B 196      38.183  10.286 144.070  1.00 59.42           C  
ANISOU 4502  CA  MET B 196     9912   6750   5912   -261   -204   1446       C  
ATOM   4503  C   MET B 196      37.745   8.984 143.414  1.00 59.30           C  
ANISOU 4503  C   MET B 196     9846   6751   5931   -239   -228   1423       C  
ATOM   4504  O   MET B 196      36.543   8.700 143.338  1.00 59.08           O  
ANISOU 4504  O   MET B 196     9804   6788   5853   -258   -163   1364       O  
ATOM   4505  CB  MET B 196      38.581  11.278 142.978  1.00 58.96           C  
ANISOU 4505  CB  MET B 196     9765   6723   5913   -117   -155   1441       C  
ATOM   4506  CG  MET B 196      38.475  12.731 143.386  1.00 59.13           C  
ANISOU 4506  CG  MET B 196     9804   6751   5910   -114    -72   1431       C  
ATOM   4507  SD  MET B 196      38.793  13.791 141.966  1.00 59.07           S  
ANISOU 4507  SD  MET B 196     9685   6782   5976     53    -24   1444       S  
ATOM   4508  CE  MET B 196      40.586  13.783 141.898  1.00 58.65           C  
ANISOU 4508  CE  MET B 196     9652   6646   5985     70   -113   1498       C  
ATOM   4509  N   VAL B 197      38.722   8.206 142.934  1.00 59.28           N  
ANISOU 4509  N   VAL B 197     9805   6683   6033   -205   -310   1458       N  
ATOM   4510  CA  VAL B 197      38.462   6.866 142.377  1.00 59.13           C  
ANISOU 4510  CA  VAL B 197     9737   6653   6074   -204   -325   1427       C  
ATOM   4511  C   VAL B 197      37.707   5.992 143.381  1.00 59.57           C  
ANISOU 4511  C   VAL B 197     9872   6691   6071   -330   -355   1438       C  
ATOM   4512  O   VAL B 197      36.786   5.278 142.998  1.00 59.32           O  
ANISOU 4512  O   VAL B 197     9810   6707   6020   -336   -306   1375       O  
ATOM   4513  CB  VAL B 197      39.766   6.165 141.911  1.00 59.42           C  
ANISOU 4513  CB  VAL B 197     9714   6578   6282   -169   -396   1459       C  
ATOM   4514  CG1 VAL B 197      39.554   4.673 141.646  1.00 59.84           C  
ANISOU 4514  CG1 VAL B 197     9726   6581   6427   -201   -411   1429       C  
ATOM   4515  CG2 VAL B 197      40.313   6.844 140.659  1.00 59.25           C  
ANISOU 4515  CG2 VAL B 197     9608   6596   6305    -58   -331   1413       C  
ATOM   4516  N   LEU B 198      38.083   6.059 144.657  1.00 60.30           N  
ANISOU 4516  N   LEU B 198    10070   6718   6120   -448   -434   1517       N  
ATOM   4517  CA  LEU B 198      37.353   5.324 145.699  1.00 61.26           C  
ANISOU 4517  CA  LEU B 198    10291   6828   6154   -601   -459   1534       C  
ATOM   4518  C   LEU B 198      35.938   5.877 145.925  1.00 60.99           C  
ANISOU 4518  C   LEU B 198    10288   6900   5983   -639   -319   1434       C  
ATOM   4519  O   LEU B 198      34.956   5.118 145.952  1.00 61.35           O  
ANISOU 4519  O   LEU B 198    10337   6977   5997   -685   -276   1382       O  
ATOM   4520  CB  LEU B 198      38.149   5.332 147.011  1.00 62.55           C  
ANISOU 4520  CB  LEU B 198    10575   6910   6279   -752   -591   1658       C  
ATOM   4521  CG  LEU B 198      37.840   4.191 147.982  1.00 63.94           C  
ANISOU 4521  CG  LEU B 198    10848   7033   6411   -923   -682   1730       C  
ATOM   4522  CD1 LEU B 198      38.406   2.870 147.461  1.00 64.45           C  
ANISOU 4522  CD1 LEU B 198    10825   6986   6675   -868   -784   1793       C  
ATOM   4523  CD2 LEU B 198      38.381   4.517 149.370  1.00 65.02           C  
ANISOU 4523  CD2 LEU B 198    11133   7136   6433  -1118   -796   1845       C  
ATOM   4524  N   ILE B 199      35.837   7.195 146.074  1.00 60.81           N  
ANISOU 4524  N   ILE B 199    10274   6921   5907   -620   -240   1402       N  
ATOM   4525  CA  ILE B 199      34.551   7.884 146.282  1.00 61.17           C  
ANISOU 4525  CA  ILE B 199    10318   7041   5880   -648    -91   1300       C  
ATOM   4526  C   ILE B 199      33.525   7.502 145.222  1.00 60.85           C  
ANISOU 4526  C   ILE B 199    10159   7074   5885   -545    -24   1227       C  
ATOM   4527  O   ILE B 199      32.381   7.216 145.564  1.00 61.39           O  
ANISOU 4527  O   ILE B 199    10237   7176   5909   -615     52   1157       O  
ATOM   4528  CB  ILE B 199      34.717   9.431 146.335  1.00 61.08           C  
ANISOU 4528  CB  ILE B 199    10292   7044   5872   -604     -6   1276       C  
ATOM   4529  CG1 ILE B 199      35.369   9.851 147.659  1.00 61.74           C  
ANISOU 4529  CG1 ILE B 199    10518   7076   5864   -772    -35   1313       C  
ATOM   4530  CG2 ILE B 199      33.370  10.148 146.209  1.00 61.22           C  
ANISOU 4530  CG2 ILE B 199    10243   7117   5899   -582    155   1170       C  
ATOM   4531  CD1 ILE B 199      36.095  11.176 147.584  1.00 61.45           C  
ANISOU 4531  CD1 ILE B 199    10462   7025   5858   -714     -2   1321       C  
ATOM   4532  N   TYR B 200      33.923   7.484 143.954  1.00 60.50           N  
ANISOU 4532  N   TYR B 200    10007   7058   5921   -399    -52   1240       N  
ATOM   4533  CA  TYR B 200      32.989   7.125 142.870  1.00 60.22           C  
ANISOU 4533  CA  TYR B 200     9861   7110   5909   -324     -6   1180       C  
ATOM   4534  C   TYR B 200      32.529   5.672 142.971  1.00 60.61           C  
ANISOU 4534  C   TYR B 200     9929   7152   5948   -397    -29   1149       C  
ATOM   4535  O   TYR B 200      31.323   5.418 142.966  1.00 60.97           O  
ANISOU 4535  O   TYR B 200     9945   7255   5962   -428     36   1081       O  
ATOM   4536  CB  TYR B 200      33.545   7.464 141.477  1.00 59.54           C  
ANISOU 4536  CB  TYR B 200     9673   7069   5878   -191    -25   1198       C  
ATOM   4537  CG  TYR B 200      33.405   8.935 141.144  1.00 59.10           C  
ANISOU 4537  CG  TYR B 200     9565   7055   5836   -110     24   1215       C  
ATOM   4538  CD1 TYR B 200      32.142   9.520 140.993  1.00 59.26           C  
ANISOU 4538  CD1 TYR B 200     9511   7140   5862    -91     98   1180       C  
ATOM   4539  CD2 TYR B 200      34.524   9.752 141.000  1.00 58.94           C  
ANISOU 4539  CD2 TYR B 200     9554   6993   5845    -54      0   1269       C  
ATOM   4540  CE1 TYR B 200      32.004  10.870 140.710  1.00 59.30           C  
ANISOU 4540  CE1 TYR B 200     9451   7158   5921    -15    141   1210       C  
ATOM   4541  CE2 TYR B 200      34.393  11.106 140.710  1.00 58.99           C  
ANISOU 4541  CE2 TYR B 200     9510   7022   5878     16     49   1291       C  
ATOM   4542  CZ  TYR B 200      33.135  11.656 140.567  1.00 59.15           C  
ANISOU 4542  CZ  TYR B 200     9454   7097   5921     37    118   1267       C  
ATOM   4543  OH  TYR B 200      33.012  12.996 140.271  1.00 59.66           O  
ANISOU 4543  OH  TYR B 200     9452   7163   6053    112    163   1303       O  
ATOM   4544  N   LEU B 201      33.463   4.737 143.128  1.00 61.01           N  
ANISOU 4544  N   LEU B 201    10020   7116   6044   -429   -119   1201       N  
ATOM   4545  CA  LEU B 201      33.110   3.326 143.395  1.00 62.23           C  
ANISOU 4545  CA  LEU B 201    10201   7230   6210   -513   -145   1187       C  
ATOM   4546  C   LEU B 201      32.061   3.225 144.506  1.00 62.84           C  
ANISOU 4546  C   LEU B 201    10369   7321   6184   -646    -96   1157       C  
ATOM   4547  O   LEU B 201      31.029   2.551 144.346  1.00 62.69           O  
ANISOU 4547  O   LEU B 201    10324   7347   6146   -679    -40   1085       O  
ATOM   4548  CB  LEU B 201      34.356   2.500 143.759  1.00 63.05           C  
ANISOU 4548  CB  LEU B 201    10342   7196   6414   -549   -265   1280       C  
ATOM   4549  CG  LEU B 201      35.311   2.167 142.592  1.00 62.79           C  
ANISOU 4549  CG  LEU B 201    10203   7125   6528   -440   -285   1273       C  
ATOM   4550  CD1 LEU B 201      36.699   1.788 143.085  1.00 63.23           C  
ANISOU 4550  CD1 LEU B 201    10276   7023   6723   -461   -407   1382       C  
ATOM   4551  CD2 LEU B 201      34.753   1.056 141.712  1.00 63.14           C  
ANISOU 4551  CD2 LEU B 201    10169   7194   6625   -432   -229   1181       C  
ATOM   4552  N   GLU B 202      32.307   3.935 145.608  1.00 63.71           N  
ANISOU 4552  N   GLU B 202    10586   7399   6223   -737   -102   1199       N  
ATOM   4553  CA  GLU B 202      31.315   4.030 146.696  1.00 65.32           C  
ANISOU 4553  CA  GLU B 202    10884   7619   6313   -891    -21   1146       C  
ATOM   4554  C   GLU B 202      29.978   4.633 146.228  1.00 65.73           C  
ANISOU 4554  C   GLU B 202    10840   7765   6370   -837    128   1022       C  
ATOM   4555  O   GLU B 202      28.909   4.108 146.561  1.00 66.57           O  
ANISOU 4555  O   GLU B 202    10959   7894   6440   -923    201    947       O  
ATOM   4556  CB  GLU B 202      31.883   4.830 147.879  1.00 66.02           C  
ANISOU 4556  CB  GLU B 202    11104   7667   6314  -1018    -35   1196       C  
ATOM   4557  CG  GLU B 202      31.126   4.697 149.189  1.00 67.36           C  
ANISOU 4557  CG  GLU B 202    11414   7834   6343  -1243     34   1152       C  
ATOM   4558  CD  GLU B 202      31.138   3.298 149.767  1.00 68.12           C  
ANISOU 4558  CD  GLU B 202    11608   7880   6395  -1383    -64   1222       C  
ATOM   4559  OE1 GLU B 202      32.134   2.558 149.590  1.00 67.92           O  
ANISOU 4559  OE1 GLU B 202    11579   7780   6444  -1351   -226   1349       O  
ATOM   4560  OE2 GLU B 202      30.133   2.930 150.413  1.00 69.44           O  
ANISOU 4560  OE2 GLU B 202    11846   8067   6469  -1530     26   1148       O  
ATOM   4561  N   VAL B 203      30.037   5.711 145.444  1.00 65.88           N  
ANISOU 4561  N   VAL B 203    10753   7828   6449   -698    165   1010       N  
ATOM   4562  CA  VAL B 203      28.820   6.370 144.924  1.00 66.64           C  
ANISOU 4562  CA  VAL B 203    10726   7998   6593   -633    280    924       C  
ATOM   4563  C   VAL B 203      27.992   5.395 144.087  1.00 67.27           C  
ANISOU 4563  C   VAL B 203    10715   8145   6697   -598    275    879       C  
ATOM   4564  O   VAL B 203      26.785   5.339 144.241  1.00 68.09           O  
ANISOU 4564  O   VAL B 203    10773   8284   6813   -639    365    796       O  
ATOM   4565  CB  VAL B 203      29.144   7.658 144.113  1.00 66.41           C  
ANISOU 4565  CB  VAL B 203    10592   7997   6643   -484    289    957       C  
ATOM   4566  CG1 VAL B 203      27.924   8.178 143.356  1.00 66.77           C  
ANISOU 4566  CG1 VAL B 203    10478   8114   6775   -403    361    907       C  
ATOM   4567  CG2 VAL B 203      29.706   8.743 145.028  1.00 66.62           C  
ANISOU 4567  CG2 VAL B 203    10697   7959   6655   -535    335    969       C  
ATOM   4568  N   PHE B 204      28.648   4.633 143.217  1.00 67.65           N  
ANISOU 4568  N   PHE B 204    10735   8206   6762   -534    183    921       N  
ATOM   4569  CA  PHE B 204      27.979   3.599 142.422  1.00 68.73           C  
ANISOU 4569  CA  PHE B 204    10798   8404   6909   -526    182    868       C  
ATOM   4570  C   PHE B 204      27.421   2.504 143.342  1.00 70.27           C  
ANISOU 4570  C   PHE B 204    11082   8555   7062   -666    208    824       C  
ATOM   4571  O   PHE B 204      26.219   2.151 143.259  1.00 70.64           O  
ANISOU 4571  O   PHE B 204    11076   8657   7104   -703    277    740       O  
ATOM   4572  CB  PHE B 204      28.932   2.987 141.384  1.00 68.30           C  
ANISOU 4572  CB  PHE B 204    10707   8353   6890   -460    105    900       C  
ATOM   4573  CG  PHE B 204      29.367   3.947 140.298  1.00 67.67           C  
ANISOU 4573  CG  PHE B 204    10539   8338   6831   -342     87    934       C  
ATOM   4574  CD1 PHE B 204      28.443   4.504 139.424  1.00 67.88           C  
ANISOU 4574  CD1 PHE B 204    10451   8485   6855   -290    112    912       C  
ATOM   4575  CD2 PHE B 204      30.708   4.277 140.134  1.00 66.98           C  
ANISOU 4575  CD2 PHE B 204    10482   8191   6776   -293     35    997       C  
ATOM   4576  CE1 PHE B 204      28.837   5.382 138.418  1.00 67.39           C  
ANISOU 4576  CE1 PHE B 204    10318   8485   6801   -201     82    965       C  
ATOM   4577  CE2 PHE B 204      31.114   5.155 139.133  1.00 66.63           C  
ANISOU 4577  CE2 PHE B 204    10368   8207   6740   -199     25   1028       C  
ATOM   4578  CZ  PHE B 204      30.177   5.714 138.281  1.00 66.92           C  
ANISOU 4578  CZ  PHE B 204    10304   8367   6755   -158     46   1017       C  
ATOM   4579  N   TYR B 205      28.284   1.993 144.228  1.00 75.06           N  
ANISOU 4579  N   TYR B 205     8230   9242  11046   -822    288  -1523       N  
ATOM   4580  CA  TYR B 205      27.873   0.969 145.204  1.00 76.94           C  
ANISOU 4580  CA  TYR B 205     8415   9279  11540   -816    239  -1396       C  
ATOM   4581  C   TYR B 205      26.600   1.359 145.959  1.00 75.80           C  
ANISOU 4581  C   TYR B 205     8453   9098  11248   -868    237  -1301       C  
ATOM   4582  O   TYR B 205      25.664   0.567 146.046  1.00 75.94           O  
ANISOU 4582  O   TYR B 205     8432   8990  11432   -826    247  -1347       O  
ATOM   4583  CB  TYR B 205      28.995   0.650 146.206  1.00 79.04           C  
ANISOU 4583  CB  TYR B 205     8603   9484  11945   -869    145  -1144       C  
ATOM   4584  CG  TYR B 205      28.514  -0.131 147.415  1.00 80.80           C  
ANISOU 4584  CG  TYR B 205     8802   9548  12349   -911     71   -929       C  
ATOM   4585  CD1 TYR B 205      28.107  -1.461 147.290  1.00 82.47           C  
ANISOU 4585  CD1 TYR B 205     8830   9564  12938   -823     80   -990       C  
ATOM   4586  CD2 TYR B 205      28.435   0.466 148.678  1.00 80.86           C  
ANISOU 4586  CD2 TYR B 205     8964   9611  12146  -1060      2   -674       C  
ATOM   4587  CE1 TYR B 205      27.654  -2.181 148.386  1.00 83.67           C  
ANISOU 4587  CE1 TYR B 205     8947   9579  13265   -866      4   -768       C  
ATOM   4588  CE2 TYR B 205      27.982  -0.247 149.781  1.00 82.11           C  
ANISOU 4588  CE2 TYR B 205     9093   9661  12444  -1126    -70   -466       C  
ATOM   4589  CZ  TYR B 205      27.600  -1.571 149.632  1.00 83.62           C  
ANISOU 4589  CZ  TYR B 205     9093   9657  13020  -1021    -79   -496       C  
ATOM   4590  OH  TYR B 205      27.145  -2.278 150.725  1.00 84.97           O  
ANISOU 4590  OH  TYR B 205     9221   9728  13335  -1092   -160   -263       O  
ATOM   4591  N   LEU B 206      26.566   2.575 146.493  1.00 74.80           N  
ANISOU 4591  N   LEU B 206     8518   9073  10830   -963    241  -1181       N  
ATOM   4592  CA  LEU B 206      25.371   3.077 147.208  1.00 74.08           C  
ANISOU 4592  CA  LEU B 206     8601   8943  10603  -1026    276  -1112       C  
ATOM   4593  C   LEU B 206      24.120   3.079 146.338  1.00 73.78           C  
ANISOU 4593  C   LEU B 206     8571   8894  10566   -945    347  -1282       C  
ATOM   4594  O   LEU B 206      23.075   2.569 146.753  1.00 73.63           O  
ANISOU 4594  O   LEU B 206     8573   8761  10643   -935    355  -1268       O  
ATOM   4595  CB  LEU B 206      25.608   4.489 147.772  1.00 73.36           C  
ANISOU 4595  CB  LEU B 206     8698   8956  10220  -1152    313  -1008       C  
ATOM   4596  CG  LEU B 206      26.554   4.519 148.972  1.00 73.93           C  
ANISOU 4596  CG  LEU B 206     8797   9051  10241  -1296    239   -800       C  
ATOM   4597  CD1 LEU B 206      27.234   5.872 149.094  1.00 73.55           C  
ANISOU 4597  CD1 LEU B 206     8881   9140   9924  -1406    281   -766       C  
ATOM   4598  CD2 LEU B 206      25.827   4.168 150.260  1.00 74.39           C  
ANISOU 4598  CD2 LEU B 206     8928   9025  10309  -1411    223   -658       C  
ATOM   4599  N   ILE B 207      24.231   3.628 145.128  1.00 74.21           N  
ANISOU 4599  N   ILE B 207     8597   9087  10513   -901    391  -1424       N  
ATOM   4600  CA  ILE B 207      23.088   3.761 144.210  1.00 74.45           C  
ANISOU 4600  CA  ILE B 207     8618   9163  10506   -856    445  -1551       C  
ATOM   4601  C   ILE B 207      22.582   2.383 143.790  1.00 76.18           C  
ANISOU 4601  C   ILE B 207     8690   9292  10962   -789    435  -1698       C  
ATOM   4602  O   ILE B 207      21.368   2.144 143.818  1.00 75.75           O  
ANISOU 4602  O   ILE B 207     8659   9174  10946   -775    456  -1715       O  
ATOM   4603  CB  ILE B 207      23.431   4.625 142.964  1.00 74.10           C  
ANISOU 4603  CB  ILE B 207     8542   9331  10281   -856    476  -1640       C  
ATOM   4604  CG1 ILE B 207      23.685   6.075 143.379  1.00 73.10           C  
ANISOU 4604  CG1 ILE B 207     8563   9261   9949   -921    508  -1491       C  
ATOM   4605  CG2 ILE B 207      22.321   4.582 141.919  1.00 74.43           C  
ANISOU 4605  CG2 ILE B 207     8524   9461  10296   -835    508  -1751       C  
ATOM   4606  CD1 ILE B 207      24.363   6.932 142.340  1.00 73.25           C  
ANISOU 4606  CD1 ILE B 207     8541   9484   9806   -932    518  -1527       C  
ATOM   4607  N   ARG B 208      23.499   1.480 143.419  1.00 78.48           N  
ANISOU 4607  N   ARG B 208     8820   9563  11434   -753    416  -1808       N  
ATOM   4608  CA  ARG B 208      23.085   0.122 143.031  1.00 80.67           C  
ANISOU 4608  CA  ARG B 208     8939   9725  11985   -699    433  -1975       C  
ATOM   4609  C   ARG B 208      22.386  -0.626 144.188  1.00 80.89           C  
ANISOU 4609  C   ARG B 208     8991   9535  12209   -687    394  -1834       C  
ATOM   4610  O   ARG B 208      21.368  -1.305 143.978  1.00 80.86           O  
ANISOU 4610  O   ARG B 208     8946   9452  12325   -659    416  -1931       O  
ATOM   4611  CB  ARG B 208      24.267  -0.658 142.454  1.00 83.18           C  
ANISOU 4611  CB  ARG B 208     9062  10031  12512   -668    454  -2127       C  
ATOM   4612  CG  ARG B 208      24.656  -0.131 141.066  1.00 84.51           C  
ANISOU 4612  CG  ARG B 208     9180  10440  12489   -695    514  -2338       C  
ATOM   4613  CD  ARG B 208      26.112  -0.345 140.711  1.00 86.59           C  
ANISOU 4613  CD  ARG B 208     9310  10731  12858   -685    537  -2416       C  
ATOM   4614  NE  ARG B 208      26.404   0.145 139.358  1.00 87.64           N  
ANISOU 4614  NE  ARG B 208     9392  11122  12783   -734    600  -2629       N  
ATOM   4615  CZ  ARG B 208      27.624   0.272 138.824  1.00 89.45           C  
ANISOU 4615  CZ  ARG B 208     9527  11450  13008   -745    634  -2718       C  
ATOM   4616  NH1 ARG B 208      28.723  -0.055 139.512  1.00 90.25           N  
ANISOU 4616  NH1 ARG B 208     9562  11403  13323   -702    609  -2602       N  
ATOM   4617  NH2 ARG B 208      27.751   0.735 137.580  1.00 90.12           N  
ANISOU 4617  NH2 ARG B 208     9569  11802  12868   -815    689  -2907       N  
ATOM   4618  N   LYS B 209      22.907  -0.458 145.403  1.00 81.50           N  
ANISOU 4618  N   LYS B 209     9134   9539  12290   -731    332  -1598       N  
ATOM   4619  CA  LYS B 209      22.279  -1.033 146.605  1.00 82.23           C  
ANISOU 4619  CA  LYS B 209     9259   9468  12515   -757    284  -1422       C  
ATOM   4620  C   LYS B 209      20.911  -0.409 146.891  1.00 81.74           C  
ANISOU 4620  C   LYS B 209     9368   9415  12273   -788    324  -1395       C  
ATOM   4621  O   LYS B 209      19.951  -1.131 147.170  1.00 82.16           O  
ANISOU 4621  O   LYS B 209     9399   9345  12473   -764    323  -1397       O  
ATOM   4622  CB  LYS B 209      23.190  -0.896 147.834  1.00 82.55           C  
ANISOU 4622  CB  LYS B 209     9327   9492  12545   -847    203  -1156       C  
ATOM   4623  CG  LYS B 209      22.779  -1.789 148.999  1.00 83.71           C  
ANISOU 4623  CG  LYS B 209     9431   9483  12889   -887    133   -960       C  
ATOM   4624  CD  LYS B 209      23.826  -1.872 150.094  1.00 84.84           C  
ANISOU 4624  CD  LYS B 209     9532   9641  13060   -998     30   -676       C  
ATOM   4625  CE  LYS B 209      23.844  -0.643 150.991  1.00 84.04           C  
ANISOU 4625  CE  LYS B 209     9654   9691  12584  -1168     30   -530       C  
ATOM   4626  NZ  LYS B 209      22.618  -0.521 151.834  1.00 83.65           N  
ANISOU 4626  NZ  LYS B 209     9746   9607  12428  -1253     57   -467       N  
ATOM   4627  N   GLN B 210      20.814   0.918 146.815  1.00 81.73           N  
ANISOU 4627  N   GLN B 210     9521   9544  11987   -839    370  -1366       N  
ATOM   4628  CA  GLN B 210      19.523   1.607 147.003  1.00 81.50           C  
ANISOU 4628  CA  GLN B 210     9630   9505  11828   -863    436  -1341       C  
ATOM   4629  C   GLN B 210      18.488   1.219 145.942  1.00 81.80           C  
ANISOU 4629  C   GLN B 210     9591   9554  11934   -785    468  -1502       C  
ATOM   4630  O   GLN B 210      17.316   1.036 146.266  1.00 81.23           O  
ANISOU 4630  O   GLN B 210     9560   9392  11909   -780    492  -1474       O  
ATOM   4631  CB  GLN B 210      19.701   3.129 147.057  1.00 81.26           C  
ANISOU 4631  CB  GLN B 210     9746   9586  11540   -930    502  -1281       C  
ATOM   4632  CG  GLN B 210      20.278   3.618 148.373  1.00 82.12           C  
ANISOU 4632  CG  GLN B 210     9978   9677  11543  -1059    499  -1118       C  
ATOM   4633  CD  GLN B 210      20.221   5.129 148.525  1.00 82.63           C  
ANISOU 4633  CD  GLN B 210    10195   9808  11392  -1140    605  -1085       C  
ATOM   4634  OE1 GLN B 210      19.228   5.776 148.168  1.00 83.26           O  
ANISOU 4634  OE1 GLN B 210    10323   9864  11446  -1115    699  -1116       O  
ATOM   4635  NE2 GLN B 210      21.288   5.702 149.067  1.00 83.19           N  
ANISOU 4635  NE2 GLN B 210    10328   9951  11329  -1245    595  -1010       N  
ATOM   4636  N   LEU B 211      18.925   1.087 144.689  1.00 83.04           N  
ANISOU 4636  N   LEU B 211     9629   9835  12084   -744    470  -1670       N  
ATOM   4637  CA  LEU B 211      18.069   0.532 143.625  1.00 84.15           C  
ANISOU 4637  CA  LEU B 211     9664  10023  12285   -709    491  -1845       C  
ATOM   4638  C   LEU B 211      17.655  -0.905 143.957  1.00 85.80           C  
ANISOU 4638  C   LEU B 211     9773  10050  12775   -670    470  -1912       C  
ATOM   4639  O   LEU B 211      16.472  -1.252 143.845  1.00 85.94           O  
ANISOU 4639  O   LEU B 211     9787  10021  12843   -660    484  -1944       O  
ATOM   4640  CB  LEU B 211      18.766   0.573 142.258  1.00 84.42           C  
ANISOU 4640  CB  LEU B 211     9574  10256  12243   -716    505  -2036       C  
ATOM   4641  CG  LEU B 211      18.902   1.944 141.579  1.00 83.35           C  
ANISOU 4641  CG  LEU B 211     9495  10339  11832   -760    523  -1984       C  
ATOM   4642  CD1 LEU B 211      19.885   1.873 140.417  1.00 84.24           C  
ANISOU 4642  CD1 LEU B 211     9481  10651  11876   -784    529  -2162       C  
ATOM   4643  CD2 LEU B 211      17.560   2.492 141.112  1.00 82.77           C  
ANISOU 4643  CD2 LEU B 211     9443  10345  11658   -782    544  -1930       C  
ATOM   4644  N   ALA B1001      18.624  -1.725 144.375  1.00 87.58           N  
ANISOU 4644  N   ALA B1001     9904  10163  13207   -649    436  -1911       N  
ATOM   4645  CA  ALA B1001      18.344  -3.109 144.783  1.00 89.73           C  
ANISOU 4645  CA  ALA B1001    10055  10228  13807   -610    418  -1938       C  
ATOM   4646  C   ALA B1001      17.314  -3.208 145.922  1.00 90.71           C  
ANISOU 4646  C   ALA B1001    10286  10219  13958   -625    387  -1749       C  
ATOM   4647  O   ALA B1001      16.422  -4.063 145.888  1.00 91.53           O  
ANISOU 4647  O   ALA B1001    10327  10208  14239   -596    393  -1812       O  
ATOM   4648  CB  ALA B1001      19.630  -3.826 145.168  1.00 90.79           C  
ANISOU 4648  CB  ALA B1001    10052  10252  14189   -589    383  -1892       C  
ATOM   4649  N   ASP B1002      17.432  -2.327 146.916  1.00 91.80           N  
ANISOU 4649  N   ASP B1002    10583  10381  13915   -688    367  -1535       N  
ATOM   4650  CA  ASP B1002      16.502  -2.302 148.065  1.00 92.90           C  
ANISOU 4650  CA  ASP B1002    10835  10419  14041   -736    359  -1364       C  
ATOM   4651  C   ASP B1002      15.052  -1.994 147.678  1.00 93.28           C  
ANISOU 4651  C   ASP B1002    10951  10473  14015   -716    421  -1431       C  
ATOM   4652  O   ASP B1002      14.123  -2.622 148.206  1.00 93.61           O  
ANISOU 4652  O   ASP B1002    10992  10391  14184   -712    414  -1385       O  
ATOM   4653  CB  ASP B1002      16.976  -1.307 149.136  1.00 93.02           C  
ANISOU 4653  CB  ASP B1002    11009  10493  13840   -849    357  -1167       C  
ATOM   4654  CG  ASP B1002      18.245  -1.767 149.855  1.00 94.49           C  
ANISOU 4654  CG  ASP B1002    11119  10662  14120   -902    267  -1017       C  
ATOM   4655  OD1 ASP B1002      18.876  -2.759 149.426  1.00 95.15           O  
ANISOU 4655  OD1 ASP B1002    11015  10676  14462   -829    219  -1069       O  
ATOM   4656  OD2 ASP B1002      18.612  -1.125 150.862  1.00 95.60           O  
ANISOU 4656  OD2 ASP B1002    11375  10862  14087  -1032    254   -845       O  
ATOM   4657  N   LEU B1003      14.857  -1.039 146.765  1.00 94.81           N  
ANISOU 4657  N   LEU B1003    11188  10814  14019   -709    476  -1514       N  
ATOM   4658  CA  LEU B1003      13.511  -0.721 146.261  1.00 96.60           C  
ANISOU 4658  CA  LEU B1003    11441  11066  14196   -694    526  -1548       C  
ATOM   4659  C   LEU B1003      12.869  -1.901 145.528  1.00 98.92           C  
ANISOU 4659  C   LEU B1003    11590  11324  14672   -647    504  -1708       C  
ATOM   4660  O   LEU B1003      11.692  -2.192 145.750  1.00 98.39           O  
ANISOU 4660  O   LEU B1003    11537  11175  14672   -638    516  -1678       O  
ATOM   4661  CB  LEU B1003      13.532   0.497 145.334  1.00 96.79           C  
ANISOU 4661  CB  LEU B1003    11491  11273  14010   -707    573  -1567       C  
ATOM   4662  CG  LEU B1003      13.867   1.841 145.969  1.00 96.41           C  
ANISOU 4662  CG  LEU B1003    11590  11245  13794   -760    631  -1422       C  
ATOM   4663  CD1 LEU B1003      14.068   2.886 144.876  1.00 96.84           C  
ANISOU 4663  CD1 LEU B1003    11618  11482  13692   -763    660  -1439       C  
ATOM   4664  CD2 LEU B1003      12.795   2.271 146.959  1.00 95.87           C  
ANISOU 4664  CD2 LEU B1003    11643  11043  13740   -795    709  -1295       C  
ATOM   4665  N   GLU B1004      13.642  -2.574 144.672  1.00102.66           N  
ANISOU 4665  N   GLU B1004    11920  11854  15232   -627    486  -1891       N  
ATOM   4666  CA  GLU B1004      13.163  -3.787 143.988  1.00105.63           C  
ANISOU 4666  CA  GLU B1004    12143  12184  15807   -607    490  -2089       C  
ATOM   4667  C   GLU B1004      12.942  -4.942 144.979  1.00106.58           C  
ANISOU 4667  C   GLU B1004    12219  12054  16221   -572    458  -2025       C  
ATOM   4668  O   GLU B1004      12.013  -5.744 144.804  1.00107.11           O  
ANISOU 4668  O   GLU B1004    12221  12039  16437   -561    466  -2108       O  
ATOM   4669  CB  GLU B1004      14.119  -4.233 142.868  1.00108.29           C  
ANISOU 4669  CB  GLU B1004    12327  12631  16187   -618    515  -2336       C  
ATOM   4670  CG  GLU B1004      14.431  -3.197 141.788  1.00109.20           C  
ANISOU 4670  CG  GLU B1004    12453  13025  16010   -672    537  -2404       C  
ATOM   4671  CD  GLU B1004      13.202  -2.626 141.101  1.00110.00           C  
ANISOU 4671  CD  GLU B1004    12577  13291  15924   -724    542  -2387       C  
ATOM   4672  OE1 GLU B1004      12.205  -3.361 140.925  1.00111.48           O  
ANISOU 4672  OE1 GLU B1004    12708  13430  16218   -736    546  -2463       O  
ATOM   4673  OE2 GLU B1004      13.240  -1.434 140.728  1.00109.66           O  
ANISOU 4673  OE2 GLU B1004    12593  13427  15644   -757    540  -2279       O  
ATOM   4674  N   ASP B1005      13.792  -5.019 146.009  1.00107.18           N  
ANISOU 4674  N   ASP B1005    12320  12025  16379   -571    416  -1859       N  
ATOM   4675  CA  ASP B1005      13.606  -5.980 147.105  1.00108.45           C  
ANISOU 4675  CA  ASP B1005    12435  11971  16797   -561    367  -1715       C  
ATOM   4676  C   ASP B1005      12.274  -5.736 147.831  1.00107.88           C  
ANISOU 4676  C   ASP B1005    12493  11852  16645   -586    370  -1582       C  
ATOM   4677  O   ASP B1005      11.477  -6.665 147.998  1.00108.54           O  
ANISOU 4677  O   ASP B1005    12506  11799  16934   -561    358  -1598       O  
ATOM   4678  CB  ASP B1005      14.783  -5.917 148.092  1.00109.13           C  
ANISOU 4678  CB  ASP B1005    12523  12017  16922   -595    305  -1507       C  
ATOM   4679  CG  ASP B1005      14.756  -7.038 149.123  1.00111.57           C  
ANISOU 4679  CG  ASP B1005    12726  12124  17538   -599    235  -1330       C  
ATOM   4680  OD1 ASP B1005      14.664  -8.220 148.726  1.00114.36           O  
ANISOU 4680  OD1 ASP B1005    12895  12325  18229   -536    243  -1446       O  
ATOM   4681  OD2 ASP B1005      14.843  -6.737 150.333  1.00111.75           O  
ANISOU 4681  OD2 ASP B1005    12840  12150  17469   -682    178  -1072       O  
ATOM   4682  N   ASN B1006      12.031  -4.487 148.234  1.00107.85           N  
ANISOU 4682  N   ASN B1006    12666  11948  16363   -637    401  -1463       N  
ATOM   4683  CA  ASN B1006      10.750  -4.112 148.870  1.00107.63           C  
ANISOU 4683  CA  ASN B1006    12758  11874  16260   -667    439  -1356       C  
ATOM   4684  C   ASN B1006       9.545  -4.304 147.946  1.00108.12           C  
ANISOU 4684  C   ASN B1006    12773  11951  16353   -620    473  -1488       C  
ATOM   4685  O   ASN B1006       8.494  -4.776 148.386  1.00108.02           O  
ANISOU 4685  O   ASN B1006    12768  11831  16444   -616    476  -1439       O  
ATOM   4686  CB  ASN B1006      10.779  -2.659 149.366  1.00107.25           C  
ANISOU 4686  CB  ASN B1006    12889  11916  15944   -738    507  -1243       C  
ATOM   4687  CG  ASN B1006      11.667  -2.470 150.589  1.00107.69           C  
ANISOU 4687  CG  ASN B1006    13017  11961  15936   -837    479  -1081       C  
ATOM   4688  OD1 ASN B1006      11.706  -3.314 151.488  1.00109.41           O  
ANISOU 4688  OD1 ASN B1006    13196  12085  16290   -878    415   -964       O  
ATOM   4689  ND2 ASN B1006      12.379  -1.350 150.632  1.00107.15           N  
ANISOU 4689  ND2 ASN B1006    13048  12006  15658   -894    523  -1057       N  
ATOM   4690  N   TRP B1007       9.704  -3.933 146.675  1.00109.36           N  
ANISOU 4690  N   TRP B1007    12876  12265  16410   -604    493  -1640       N  
ATOM   4691  CA  TRP B1007       8.652  -4.104 145.656  1.00110.38           C  
ANISOU 4691  CA  TRP B1007    12933  12469  16536   -595    510  -1759       C  
ATOM   4692  C   TRP B1007       8.315  -5.574 145.427  1.00112.93           C  
ANISOU 4692  C   TRP B1007    13115  12677  17114   -573    483  -1906       C  
ATOM   4693  O   TRP B1007       7.135  -5.927 145.346  1.00113.47           O  
ANISOU 4693  O   TRP B1007    13166  12705  17241   -573    487  -1910       O  
ATOM   4694  CB  TRP B1007       9.080  -3.450 144.334  1.00110.13           C  
ANISOU 4694  CB  TRP B1007    12848  12675  16321   -621    524  -1880       C  
ATOM   4695  CG  TRP B1007       8.094  -3.565 143.203  1.00110.15           C  
ANISOU 4695  CG  TRP B1007    12757  12820  16274   -657    527  -1982       C  
ATOM   4696  CD1 TRP B1007       8.270  -4.232 142.022  1.00111.21           C  
ANISOU 4696  CD1 TRP B1007    12743  13096  16413   -706    521  -2220       C  
ATOM   4697  CD2 TRP B1007       6.785  -2.989 143.144  1.00109.81           C  
ANISOU 4697  CD2 TRP B1007    12747  12809  16166   -672    543  -1843       C  
ATOM   4698  NE1 TRP B1007       7.150  -4.105 141.230  1.00111.65           N  
ANISOU 4698  NE1 TRP B1007    12741  13302  16376   -769    515  -2227       N  
ATOM   4699  CE2 TRP B1007       6.224  -3.343 141.892  1.00110.53           C  
ANISOU 4699  CE2 TRP B1007    12701  13087  16206   -737    521  -1978       C  
ATOM   4700  CE3 TRP B1007       6.031  -2.195 144.021  1.00108.75           C  
ANISOU 4700  CE3 TRP B1007    12732  12566  16022   -650    586  -1621       C  
ATOM   4701  CZ2 TRP B1007       4.937  -2.942 141.506  1.00110.34           C  
ANISOU 4701  CZ2 TRP B1007    12647  13149  16128   -774    517  -1857       C  
ATOM   4702  CZ3 TRP B1007       4.759  -1.791 143.631  1.00108.61           C  
ANISOU 4702  CZ3 TRP B1007    12682  12600  15986   -667    604  -1518       C  
ATOM   4703  CH2 TRP B1007       4.221  -2.177 142.392  1.00109.57           C  
ANISOU 4703  CH2 TRP B1007    12656  12911  16063   -724    557  -1615       C  
ATOM   4704  N   GLU B1008       9.345  -6.420 145.328  1.00115.68           N  
ANISOU 4704  N   GLU B1008    13350  12960  17640   -555    464  -2024       N  
ATOM   4705  CA  GLU B1008       9.140  -7.864 145.166  1.00118.08           C  
ANISOU 4705  CA  GLU B1008    13497  13110  18257   -533    462  -2174       C  
ATOM   4706  C   GLU B1008       8.608  -8.517 146.448  1.00117.39           C  
ANISOU 4706  C   GLU B1008    13432  12795  18376   -507    420  -1982       C  
ATOM   4707  O   GLU B1008       7.782  -9.429 146.370  1.00118.36           O  
ANISOU 4707  O   GLU B1008    13473  12805  18694   -496    423  -2053       O  
ATOM   4708  CB  GLU B1008      10.420  -8.564 144.696  1.00120.65           C  
ANISOU 4708  CB  GLU B1008    13668  13398  18775   -520    483  -2351       C  
ATOM   4709  CG  GLU B1008      10.174  -9.971 144.162  1.00123.91           C  
ANISOU 4709  CG  GLU B1008    13888  13672  19518   -517    529  -2593       C  
ATOM   4710  CD  GLU B1008      11.401 -10.621 143.548  1.00126.85           C  
ANISOU 4710  CD  GLU B1008    14084  14000  20111   -513    593  -2816       C  
ATOM   4711  OE1 GLU B1008      12.479  -9.985 143.480  1.00127.37           O  
ANISOU 4711  OE1 GLU B1008    14174  14160  20057   -509    589  -2780       O  
ATOM   4712  OE2 GLU B1008      11.281 -11.792 143.123  1.00128.91           O  
ANISOU 4712  OE2 GLU B1008    14170  14117  20690   -519    662  -3042       O  
ATOM   4713  N   THR B1009       9.076  -8.058 147.613  1.00116.11           N  
ANISOU 4713  N   THR B1009    13372  12585  18159   -518    383  -1741       N  
ATOM   4714  CA  THR B1009       8.542  -8.520 148.907  1.00116.17           C  
ANISOU 4714  CA  THR B1009    13414  12430  18295   -531    339  -1524       C  
ATOM   4715  C   THR B1009       7.032  -8.276 149.021  1.00116.07           C  
ANISOU 4715  C   THR B1009    13492  12415  18193   -540    370  -1492       C  
ATOM   4716  O   THR B1009       6.278  -9.175 149.422  1.00117.14           O  
ANISOU 4716  O   THR B1009    13568  12405  18532   -528    347  -1457       O  
ATOM   4717  CB  THR B1009       9.252  -7.829 150.094  1.00115.34           C  
ANISOU 4717  CB  THR B1009    13425  12352  18044   -597    305  -1278       C  
ATOM   4718  OG1 THR B1009      10.659  -8.091 150.028  1.00115.75           O  
ANISOU 4718  OG1 THR B1009    13376  12404  18200   -591    265  -1273       O  
ATOM   4719  CG2 THR B1009       8.715  -8.327 151.441  1.00115.53           C  
ANISOU 4719  CG2 THR B1009    13472  12252  18170   -652    258  -1048       C  
ATOM   4720  N   LEU B1010       6.606  -7.069 148.651  1.00115.74           N  
ANISOU 4720  N   LEU B1010    13574  12522  17877   -560    426  -1491       N  
ATOM   4721  CA  LEU B1010       5.194  -6.681 148.722  1.00115.81           C  
ANISOU 4721  CA  LEU B1010    13657  12531  17815   -567    470  -1436       C  
ATOM   4722  C   LEU B1010       4.294  -7.499 147.787  1.00117.63           C  
ANISOU 4722  C   LEU B1010    13762  12753  18177   -539    461  -1596       C  
ATOM   4723  O   LEU B1010       3.168  -7.843 148.162  1.00117.33           O  
ANISOU 4723  O   LEU B1010    13733  12624  18221   -535    465  -1532       O  
ATOM   4724  CB  LEU B1010       5.030  -5.180 148.440  1.00114.63           C  
ANISOU 4724  CB  LEU B1010    13625  12526  17401   -591    542  -1385       C  
ATOM   4725  CG  LEU B1010       3.720  -4.541 148.931  1.00114.27           C  
ANISOU 4725  CG  LEU B1010    13674  12435  17308   -608    617  -1255       C  
ATOM   4726  CD1 LEU B1010       3.700  -4.418 150.452  1.00114.09           C  
ANISOU 4726  CD1 LEU B1010    13771  12294  17283   -667    652  -1098       C  
ATOM   4727  CD2 LEU B1010       3.498  -3.186 148.274  1.00113.92           C  
ANISOU 4727  CD2 LEU B1010    13672  12521  17089   -615    692  -1224       C  
ATOM   4728  N   ASN B1011       4.783  -7.820 146.588  1.00120.15           N  
ANISOU 4728  N   ASN B1011    13963  13178  18507   -538    457  -1812       N  
ATOM   4729  CA  ASN B1011       4.046  -8.700 145.665  1.00122.78           C  
ANISOU 4729  CA  ASN B1011    14163  13527  18960   -551    458  -2006       C  
ATOM   4730  C   ASN B1011       4.092 -10.177 146.092  1.00124.72           C  
ANISOU 4730  C   ASN B1011    14289  13545  19553   -522    436  -2076       C  
ATOM   4731  O   ASN B1011       3.066 -10.863 146.046  1.00125.28           O  
ANISOU 4731  O   ASN B1011    14308  13537  19753   -527    434  -2112       O  
ATOM   4732  CB  ASN B1011       4.558  -8.547 144.222  1.00124.22           C  
ANISOU 4732  CB  ASN B1011    14251  13932  19015   -603    480  -2241       C  
ATOM   4733  CG  ASN B1011       4.184  -7.207 143.596  1.00123.68           C  
ANISOU 4733  CG  ASN B1011    14252  14104  18636   -647    489  -2153       C  
ATOM   4734  OD1 ASN B1011       3.166  -6.600 143.940  1.00122.82           O  
ANISOU 4734  OD1 ASN B1011    14217  13989  18456   -641    494  -1969       O  
ATOM   4735  ND2 ASN B1011       5.002  -6.748 142.653  1.00124.31           N  
ANISOU 4735  ND2 ASN B1011    14288  14391  18553   -694    499  -2274       N  
ATOM   4736  N   ASP B1012       5.269 -10.656 146.502  1.00126.00           N  
ANISOU 4736  N   ASP B1012    14390  13595  19888   -495    421  -2076       N  
ATOM   4737  CA  ASP B1012       5.445 -12.059 146.926  1.00127.92           C  
ANISOU 4737  CA  ASP B1012    14481  13594  20528   -463    405  -2107       C  
ATOM   4738  C   ASP B1012       4.533 -12.469 148.091  1.00128.23           C  
ANISOU 4738  C   ASP B1012    14562  13467  20691   -450    356  -1878       C  
ATOM   4739  O   ASP B1012       3.966 -13.564 148.073  1.00130.13           O  
ANISOU 4739  O   ASP B1012    14681  13548  21212   -437    356  -1946       O  
ATOM   4740  CB  ASP B1012       6.913 -12.353 147.291  1.00128.82           C  
ANISOU 4740  CB  ASP B1012    14509  13616  20818   -437    388  -2064       C  
ATOM   4741  CG  ASP B1012       7.826 -12.458 146.067  1.00130.48           C  
ANISOU 4741  CG  ASP B1012    14603  13918  21052   -446    458  -2358       C  
ATOM   4742  OD1 ASP B1012       7.388 -12.139 144.939  1.00130.81           O  
ANISOU 4742  OD1 ASP B1012    14653  14149  20900   -496    511  -2583       O  
ATOM   4743  OD2 ASP B1012       9.000 -12.853 146.240  1.00131.40           O  
ANISOU 4743  OD2 ASP B1012    14610  13933  21383   -418    461  -2353       O  
ATOM   4744  N   ASN B1013       4.384 -11.595 149.085  1.00127.19           N  
ANISOU 4744  N   ASN B1013    14596  13377  20353   -470    329  -1623       N  
ATOM   4745  CA  ASN B1013       3.532 -11.891 150.248  1.00127.40           C  
ANISOU 4745  CA  ASN B1013    14673  13279  20455   -486    294  -1402       C  
ATOM   4746  C   ASN B1013       2.021 -11.812 149.969  1.00127.38           C  
ANISOU 4746  C   ASN B1013    14716  13291  20389   -486    328  -1440       C  
ATOM   4747  O   ASN B1013       1.227 -12.435 150.692  1.00127.49           O  
ANISOU 4747  O   ASN B1013    14715  13171  20553   -489    303  -1324       O  
ATOM   4748  CB  ASN B1013       3.928 -11.005 151.437  1.00126.53           C  
ANISOU 4748  CB  ASN B1013    14716  13223  20137   -547    278  -1148       C  
ATOM   4749  CG  ASN B1013       5.254 -11.419 152.061  1.00127.54           C  
ANISOU 4749  CG  ASN B1013    14759  13295  20402   -569    209  -1019       C  
ATOM   4750  OD1 ASN B1013       5.961 -12.289 151.545  1.00128.96           O  
ANISOU 4750  OD1 ASN B1013    14762  13380  20856   -518    187  -1125       O  
ATOM   4751  ND2 ASN B1013       5.603 -10.788 153.177  1.00127.13           N  
ANISOU 4751  ND2 ASN B1013    14824  13309  20171   -661    185   -789       N  
ATOM   4752  N   LEU B1014       1.620 -11.088 148.919  1.00127.88           N  
ANISOU 4752  N   LEU B1014    14817  13524  20246   -491    376  -1580       N  
ATOM   4753  CA  LEU B1014       0.221 -11.125 148.447  1.00128.99           C  
ANISOU 4753  CA  LEU B1014    14953  13695  20360   -498    397  -1621       C  
ATOM   4754  C   LEU B1014      -0.180 -12.505 147.904  1.00131.42           C  
ANISOU 4754  C   LEU B1014    15093  13896  20945   -494    380  -1805       C  
ATOM   4755  O   LEU B1014      -1.351 -12.882 147.989  1.00132.21           O  
ANISOU 4755  O   LEU B1014    15179  13940  21112   -500    375  -1776       O  
ATOM   4756  CB  LEU B1014      -0.048 -10.052 147.381  1.00128.58           C  
ANISOU 4756  CB  LEU B1014    14939  13875  20040   -526    436  -1690       C  
ATOM   4757  CG  LEU B1014      -0.174  -8.604 147.864  1.00127.26           C  
ANISOU 4757  CG  LEU B1014    14929  13785  19637   -532    485  -1496       C  
ATOM   4758  CD1 LEU B1014      -0.099  -7.650 146.681  1.00126.98           C  
ANISOU 4758  CD1 LEU B1014    14878  13978  19387   -558    507  -1558       C  
ATOM   4759  CD2 LEU B1014      -1.460  -8.388 148.651  1.00126.96           C  
ANISOU 4759  CD2 LEU B1014    14963  13650  19623   -532    522  -1321       C  
ATOM   4760  N   LYS B1015       0.784 -13.244 147.350  1.00133.54           N  
ANISOU 4760  N   LYS B1015    15227  14125  21388   -491    385  -2002       N  
ATOM   4761  CA  LYS B1015       0.560 -14.635 146.930  1.00135.53           C  
ANISOU 4761  CA  LYS B1015    15299  14227  21969   -496    399  -2203       C  
ATOM   4762  C   LYS B1015       0.431 -15.556 148.148  1.00136.73           C  
ANISOU 4762  C   LYS B1015    15400  14107  22445   -450    352  -2012       C  
ATOM   4763  O   LYS B1015      -0.366 -16.496 148.137  1.00136.46           O  
ANISOU 4763  O   LYS B1015    15270  13935  22641   -452    352  -2068       O  
ATOM   4764  CB  LYS B1015       1.696 -15.128 146.025  1.00136.49           C  
ANISOU 4764  CB  LYS B1015    15275  14359  22225   -513    454  -2485       C  
ATOM   4765  CG  LYS B1015       1.871 -14.343 144.731  1.00136.06           C  
ANISOU 4765  CG  LYS B1015    15242  14602  21853   -588    498  -2693       C  
ATOM   4766  CD  LYS B1015       3.246 -14.571 144.123  1.00137.09           C  
ANISOU 4766  CD  LYS B1015    15264  14748  22074   -599    557  -2912       C  
ATOM   4767  CE  LYS B1015       3.508 -13.626 142.962  1.00136.71           C  
ANISOU 4767  CE  LYS B1015    15253  15029  21659   -684    587  -3062       C  
ATOM   4768  NZ  LYS B1015       4.915 -13.716 142.487  1.00137.34           N  
ANISOU 4768  NZ  LYS B1015    15247  15130  21803   -690    647  -3246       N  
ATOM   4769  N   VAL B1016       1.222 -15.277 149.187  1.00138.56           N  
ANISOU 4769  N   VAL B1016    15683  14280  22682   -428    306  -1774       N  
ATOM   4770  CA  VAL B1016       1.161 -16.010 150.459  1.00141.43           C  
ANISOU 4770  CA  VAL B1016    15998  14437  23302   -415    239  -1519       C  
ATOM   4771  C   VAL B1016      -0.171 -15.755 151.172  1.00143.34           C  
ANISOU 4771  C   VAL B1016    16361  14683  23416   -439    221  -1343       C  
ATOM   4772  O   VAL B1016      -0.797 -16.702 151.653  1.00145.42           O  
ANISOU 4772  O   VAL B1016    16535  14777  23939   -432    188  -1266       O  
ATOM   4773  CB  VAL B1016       2.349 -15.654 151.397  1.00140.82           C  
ANISOU 4773  CB  VAL B1016    15947  14360  23195   -430    184  -1281       C  
ATOM   4774  CG1 VAL B1016       2.194 -16.313 152.769  1.00141.35           C  
ANISOU 4774  CG1 VAL B1016    15963  14275  23468   -459     98   -964       C  
ATOM   4775  CG2 VAL B1016       3.676 -16.061 150.765  1.00142.02           C  
ANISOU 4775  CG2 VAL B1016    15943  14465  23552   -397    204  -1432       C  
ATOM   4776  N   ILE B1017      -0.599 -14.490 151.238  1.00144.71           N  
ANISOU 4776  N   ILE B1017    16723  15036  23223   -466    253  -1279       N  
ATOM   4777  CA  ILE B1017      -1.895 -14.150 151.864  1.00145.97           C  
ANISOU 4777  CA  ILE B1017    16993  15197  23271   -490    267  -1131       C  
ATOM   4778  C   ILE B1017      -3.087 -14.752 151.100  1.00147.81           C  
ANISOU 4778  C   ILE B1017    17149  15394  23618   -471    282  -1278       C  
ATOM   4779  O   ILE B1017      -4.003 -15.299 151.722  1.00149.92           O  
ANISOU 4779  O   ILE B1017    17402  15545  24015   -475    262  -1165       O  
ATOM   4780  CB  ILE B1017      -2.078 -12.617 152.035  1.00145.40           C  
ANISOU 4780  CB  ILE B1017    17114  15294  22836   -523    334  -1048       C  
ATOM   4781  CG1 ILE B1017      -1.079 -12.085 153.070  1.00145.92           C  
ANISOU 4781  CG1 ILE B1017    17270  15389  22785   -579    323   -875       C  
ATOM   4782  CG2 ILE B1017      -3.503 -12.266 152.470  1.00144.50           C  
ANISOU 4782  CG2 ILE B1017    17085  15166  22652   -541    382   -940       C  
ATOM   4783  CD1 ILE B1017      -0.882 -10.584 153.039  1.00144.94           C  
ANISOU 4783  CD1 ILE B1017    17308  15422  22339   -613    407   -859       C  
ATOM   4784  N   GLU B1018      -3.071 -14.650 149.769  1.00148.42           N  
ANISOU 4784  N   GLU B1018    17170  15591  23629   -471    314  -1522       N  
ATOM   4785  CA  GLU B1018      -4.168 -15.171 148.929  1.00148.56           C  
ANISOU 4785  CA  GLU B1018    17107  15627  23711   -492    325  -1676       C  
ATOM   4786  C   GLU B1018      -4.318 -16.701 148.954  1.00149.39           C  
ANISOU 4786  C   GLU B1018    17042  15518  24199   -484    305  -1786       C  
ATOM   4787  O   GLU B1018      -5.423 -17.209 148.753  1.00149.76           O  
ANISOU 4787  O   GLU B1018    17044  15527  24328   -504    303  -1824       O  
ATOM   4788  CB  GLU B1018      -4.029 -14.688 147.474  1.00148.95           C  
ANISOU 4788  CB  GLU B1018    17122  15907  23562   -540    359  -1906       C  
ATOM   4789  CG  GLU B1018      -4.419 -13.228 147.252  1.00147.87           C  
ANISOU 4789  CG  GLU B1018    17114  15980  23087   -556    380  -1777       C  
ATOM   4790  CD  GLU B1018      -5.918 -12.962 147.343  1.00147.36           C  
ANISOU 4790  CD  GLU B1018    17080  15935  22974   -570    383  -1640       C  
ATOM   4791  OE1 GLU B1018      -6.717 -13.923 147.390  1.00147.59           O  
ANISOU 4791  OE1 GLU B1018    17030  15857  23190   -580    361  -1681       O  
ATOM   4792  OE2 GLU B1018      -6.299 -11.773 147.367  1.00146.17           O  
ANISOU 4792  OE2 GLU B1018    17019  15895  22622   -570    417  -1485       O  
ATOM   4793  N   LYS B1019      -3.218 -17.419 149.192  1.00149.47           N  
ANISOU 4793  N   LYS B1019    16943  15380  24465   -457    295  -1825       N  
ATOM   4794  CA  LYS B1019      -3.229 -18.883 149.279  1.00150.53           C  
ANISOU 4794  CA  LYS B1019    16885  15265  25041   -443    293  -1910       C  
ATOM   4795  C   LYS B1019      -2.584 -19.351 150.591  1.00151.98           C  
ANISOU 4795  C   LYS B1019    17022  15249  25473   -403    227  -1625       C  
ATOM   4796  O   LYS B1019      -1.558 -20.038 150.587  1.00153.12           O  
ANISOU 4796  O   LYS B1019    17008  15245  25922   -379    232  -1667       O  
ATOM   4797  CB  LYS B1019      -2.516 -19.491 148.064  1.00150.61           C  
ANISOU 4797  CB  LYS B1019    16735  15268  25222   -470    372  -2276       C  
ATOM   4798  CG  LYS B1019      -3.191 -19.195 146.730  1.00149.49           C  
ANISOU 4798  CG  LYS B1019    16604  15356  24839   -558    428  -2560       C  
ATOM   4799  CD  LYS B1019      -2.336 -19.626 145.546  1.00150.36           C  
ANISOU 4799  CD  LYS B1019    16571  15512  25044   -622    527  -2941       C  
ATOM   4800  CE  LYS B1019      -2.283 -21.139 145.394  1.00152.54           C  
ANISOU 4800  CE  LYS B1019    16627  15509  25821   -635    603  -3164       C  
ATOM   4801  NZ  LYS B1019      -1.444 -21.547 144.235  1.00154.26           N  
ANISOU 4801  NZ  LYS B1019    16699  15767  26146   -718    738  -3578       N  
ATOM   4802  N   ALA B1020      -3.204 -18.964 151.707  1.00152.48           N  
ANISOU 4802  N   ALA B1020    17207  15321  25406   -414    170  -1327       N  
ATOM   4803  CA  ALA B1020      -2.766 -19.352 153.057  1.00154.19           C  
ANISOU 4803  CA  ALA B1020    17383  15406  25794   -423     90  -1005       C  
ATOM   4804  C   ALA B1020      -3.839 -20.196 153.748  1.00154.93           C  
ANISOU 4804  C   ALA B1020    17416  15343  26106   -432     47   -852       C  
ATOM   4805  O   ALA B1020      -5.033 -19.905 153.632  1.00154.87           O  
ANISOU 4805  O   ALA B1020    17508  15399  25934   -443     73   -882       O  
ATOM   4806  CB  ALA B1020      -2.448 -18.115 153.891  1.00153.59           C  
ANISOU 4806  CB  ALA B1020    17507  15511  25338   -475     71   -781       C  
ATOM   4807  N   ASP B1021      -3.407 -21.225 154.478  1.00155.90           N  
ANISOU 4807  N   ASP B1021    17360  15261  26611   -430    -21   -664       N  
ATOM   4808  CA  ASP B1021      -4.326 -22.115 155.200  1.00156.19           C  
ANISOU 4808  CA  ASP B1021    17310  15137  26896   -443    -74   -484       C  
ATOM   4809  C   ASP B1021      -4.666 -21.529 156.564  1.00156.34           C  
ANISOU 4809  C   ASP B1021    17472  15274  26655   -530   -140   -129       C  
ATOM   4810  O   ASP B1021      -5.838 -21.333 156.890  1.00155.92           O  
ANISOU 4810  O   ASP B1021    17524  15264  26454   -558   -126    -78       O  
ATOM   4811  CB  ASP B1021      -3.726 -23.521 155.374  1.00157.17           C  
ANISOU 4811  CB  ASP B1021    17142  14973  27599   -411   -115   -410       C  
ATOM   4812  CG  ASP B1021      -3.521 -24.255 154.055  1.00156.81           C  
ANISOU 4812  CG  ASP B1021    16932  14775  27871   -350    -10   -807       C  
ATOM   4813  OD1 ASP B1021      -3.872 -23.708 152.986  1.00154.25           O  
ANISOU 4813  OD1 ASP B1021    16720  14602  27283   -351     75  -1132       O  
ATOM   4814  OD2 ASP B1021      -2.996 -25.385 154.094  1.00157.54           O  
ANISOU 4814  OD2 ASP B1021    16767  14600  28491   -318     -7   -790       O  
ATOM   4815  N   ASN B1022      -3.627 -21.257 157.363  1.00157.84           N  
ANISOU 4815  N   ASN B1022    17656  15527  26787   -591   -205    111       N  
ATOM   4816  CA  ASN B1022      -3.779 -20.791 158.753  1.00158.22           C  
ANISOU 4816  CA  ASN B1022    17812  15710  26593   -726   -267    455       C  
ATOM   4817  C   ASN B1022      -3.442 -19.294 158.892  1.00157.21           C  
ANISOU 4817  C   ASN B1022    17929  15841  25961   -795   -204    425       C  
ATOM   4818  O   ASN B1022      -2.521 -18.773 158.235  1.00155.85           O  
ANISOU 4818  O   ASN B1022    17783  15734  25696   -754   -174    276       O  
ATOM   4819  CB  ASN B1022      -2.897 -21.626 159.720  1.00159.98           C  
ANISOU 4819  CB  ASN B1022    17824  15846  27115   -798   -403    814       C  
ATOM   4820  CG  ASN B1022      -3.243 -21.398 161.181  1.00160.12           C  
ANISOU 4820  CG  ASN B1022    17912  16012  26912   -979   -477   1180       C  
ATOM   4821  OD1 ASN B1022      -4.348 -20.969 161.511  1.00159.02           O  
ANISOU 4821  OD1 ASN B1022    17933  15958  26526  -1029   -421   1160       O  
ATOM   4822  ND2 ASN B1022      -2.295 -21.690 162.066  1.00161.50           N  
ANISOU 4822  ND2 ASN B1022    17952  16231  27176  -1095   -601   1523       N  
ATOM   4823  N   ALA B1023      -4.175 -18.622 159.784  1.00157.82           N  
ANISOU 4823  N   ALA B1023    18175  16055  25732   -911   -173    565       N  
ATOM   4824  CA  ALA B1023      -3.979 -17.192 160.079  1.00157.81           C  
ANISOU 4824  CA  ALA B1023    18403  16278  25278  -1004    -84    544       C  
ATOM   4825  C   ALA B1023      -2.527 -16.820 160.422  1.00159.57           C  
ANISOU 4825  C   ALA B1023    18618  16616  25394  -1084   -138    659       C  
ATOM   4826  O   ALA B1023      -2.082 -15.708 160.114  1.00159.64           O  
ANISOU 4826  O   ALA B1023    18779  16765  25111  -1097    -57    530       O  
ATOM   4827  CB  ALA B1023      -4.910 -16.756 161.204  1.00157.30           C  
ANISOU 4827  CB  ALA B1023    18473  16314  24979  -1155    -33    704       C  
ATOM   4828  N   ALA B1024      -1.802 -17.750 161.050  1.00161.58           N  
ANISOU 4828  N   ALA B1024    18678  16808  25905  -1140   -278    921       N  
ATOM   4829  CA  ALA B1024      -0.363 -17.600 161.312  1.00162.21           C  
ANISOU 4829  CA  ALA B1024    18692  16975  25964  -1208   -355   1065       C  
ATOM   4830  C   ALA B1024       0.476 -17.380 160.045  1.00161.35           C  
ANISOU 4830  C   ALA B1024    18556  16814  25935  -1051   -310    791       C  
ATOM   4831  O   ALA B1024       1.469 -16.651 160.089  1.00160.02           O  
ANISOU 4831  O   ALA B1024    18452  16787  25560  -1105   -310    808       O  
ATOM   4832  CB  ALA B1024       0.164 -18.804 162.082  1.00164.89           C  
ANISOU 4832  CB  ALA B1024    18765  17214  26669  -1274   -522   1424       C  
ATOM   4833  N   GLN B1025       0.083 -18.004 158.930  1.00161.38           N  
ANISOU 4833  N   GLN B1025    18463  16633  26220   -879   -268    534       N  
ATOM   4834  CA  GLN B1025       0.751 -17.771 157.636  1.00160.77           C  
ANISOU 4834  CA  GLN B1025    18367  16536  26182   -753   -203    229       C  
ATOM   4835  C   GLN B1025       0.463 -16.359 157.104  1.00159.94           C  
ANISOU 4835  C   GLN B1025    18513  16629  25626   -753    -90     20       C  
ATOM   4836  O   GLN B1025       1.356 -15.689 156.565  1.00160.12           O  
ANISOU 4836  O   GLN B1025    18584  16752  25502   -734    -59    -95       O  
ATOM   4837  CB  GLN B1025       0.329 -18.817 156.596  1.00159.61           C  
ANISOU 4837  CB  GLN B1025    18048  16169  26426   -617   -169    -15       C  
ATOM   4838  CG  GLN B1025       0.693 -20.250 156.962  1.00160.97           C  
ANISOU 4838  CG  GLN B1025    17931  16091  27137   -595   -253    159       C  
ATOM   4839  CD  GLN B1025       0.292 -21.259 155.899  1.00161.16           C  
ANISOU 4839  CD  GLN B1025    17785  15888  27560   -480   -183   -137       C  
ATOM   4840  OE1 GLN B1025      -0.679 -21.063 155.167  1.00159.00           O  
ANISOU 4840  OE1 GLN B1025    17613  15651  27145   -447   -105   -396       O  
ATOM   4841  NE2 GLN B1025       1.038 -22.353 155.818  1.00162.94           N  
ANISOU 4841  NE2 GLN B1025    17732  15873  28303   -433   -204    -94       N  
ATOM   4842  N   VAL B1026      -0.783 -15.917 157.282  1.00159.30           N  
ANISOU 4842  N   VAL B1026    18577  16595  25355   -777    -25     -6       N  
ATOM   4843  CA  VAL B1026      -1.229 -14.589 156.855  1.00156.90           C  
ANISOU 4843  CA  VAL B1026    18483  16447  24684   -779     92   -160       C  
ATOM   4844  C   VAL B1026      -0.558 -13.489 157.691  1.00156.02           C  
ANISOU 4844  C   VAL B1026    18528  16510  24241   -912    121    -24       C  
ATOM   4845  O   VAL B1026      -0.105 -12.487 157.138  1.00154.67           O  
ANISOU 4845  O   VAL B1026    18462  16452  23852   -895    191   -157       O  
ATOM   4846  CB  VAL B1026      -2.775 -14.470 156.922  1.00156.55           C  
ANISOU 4846  CB  VAL B1026    18518  16376  24586   -773    161   -187       C  
ATOM   4847  CG1 VAL B1026      -3.246 -13.057 156.580  1.00155.97           C  
ANISOU 4847  CG1 VAL B1026    18633  16440  24188   -781    293   -293       C  
ATOM   4848  CG2 VAL B1026      -3.426 -15.483 155.984  1.00156.42           C  
ANISOU 4848  CG2 VAL B1026    18354  16214  24864   -660    139   -351       C  
ATOM   4849  N   LYS B1027      -0.487 -13.689 159.009  1.00156.88           N  
ANISOU 4849  N   LYS B1027    18641  16655  24311  -1063     66    240       N  
ATOM   4850  CA  LYS B1027       0.151 -12.729 159.930  1.00157.37           C  
ANISOU 4850  CA  LYS B1027    18841  16906  24045  -1243     95    372       C  
ATOM   4851  C   LYS B1027       1.644 -12.529 159.631  1.00157.98           C  
ANISOU 4851  C   LYS B1027    18870  17052  24103  -1239     35    378       C  
ATOM   4852  O   LYS B1027       2.133 -11.386 159.577  1.00157.74           O  
ANISOU 4852  O   LYS B1027    18988  17166  23781  -1296    115    302       O  
ATOM   4853  CB  LYS B1027      -0.036 -13.185 161.383  1.00158.18           C  
ANISOU 4853  CB  LYS B1027    18915  17062  24121  -1442     26    673       C  
ATOM   4854  CG  LYS B1027       0.358 -12.152 162.428  1.00158.36           C  
ANISOU 4854  CG  LYS B1027    19101  17313  23752  -1687     89    780       C  
ATOM   4855  CD  LYS B1027      -0.215 -12.497 163.797  1.00158.93           C  
ANISOU 4855  CD  LYS B1027    19174  17471  23740  -1912     62   1025       C  
ATOM   4856  CE  LYS B1027      -0.032 -11.363 164.790  1.00158.77           C  
ANISOU 4856  CE  LYS B1027    19340  17694  23288  -2190    181   1054       C  
ATOM   4857  NZ  LYS B1027      -0.820 -11.596 166.031  1.00159.62           N  
ANISOU 4857  NZ  LYS B1027    19470  17901  23276  -2425    202   1228       N  
ATOM   4858  N   ASP B1028       2.346 -13.649 159.438  1.00158.61           N  
ANISOU 4858  N   ASP B1028    18728  17011  24524  -1171    -94    468       N  
ATOM   4859  CA  ASP B1028       3.765 -13.654 159.047  1.00157.87           C  
ANISOU 4859  CA  ASP B1028    18539  16939  24502  -1141   -153    472       C  
ATOM   4860  C   ASP B1028       4.024 -12.942 157.713  1.00155.80           C  
ANISOU 4860  C   ASP B1028    18352  16701  24140  -1002    -55    148       C  
ATOM   4861  O   ASP B1028       5.085 -12.342 157.531  1.00156.84           O  
ANISOU 4861  O   ASP B1028    18514  16939  24138  -1023    -56    131       O  
ATOM   4862  CB  ASP B1028       4.307 -15.092 158.979  1.00159.52           C  
ANISOU 4862  CB  ASP B1028    18459  16954  25198  -1069   -279    606       C  
ATOM   4863  CG  ASP B1028       4.592 -15.684 160.353  1.00161.04           C  
ANISOU 4863  CG  ASP B1028    18531  17178  25479  -1242   -418   1022       C  
ATOM   4864  OD1 ASP B1028       3.824 -15.430 161.307  1.00160.85           O  
ANISOU 4864  OD1 ASP B1028    18621  17264  25231  -1394   -415   1168       O  
ATOM   4865  OD2 ASP B1028       5.594 -16.416 160.475  1.00161.88           O  
ANISOU 4865  OD2 ASP B1028    18411  17204  25891  -1236   -529   1215       O  
ATOM   4866  N   ALA B1029       3.066 -13.021 156.786  1.00153.36           N  
ANISOU 4866  N   ALA B1029    18061  16314  23891   -878     21    -88       N  
ATOM   4867  CA  ALA B1029       3.126 -12.253 155.535  1.00150.12           C  
ANISOU 4867  CA  ALA B1029    17726  15974  23335   -782    112   -369       C  
ATOM   4868  C   ALA B1029       2.844 -10.765 155.782  1.00147.46           C  
ANISOU 4868  C   ALA B1029    17620  15806  22600   -859    217   -378       C  
ATOM   4869  O   ALA B1029       3.626  -9.900 155.365  1.00147.29           O  
ANISOU 4869  O   ALA B1029    17667  15899  22394   -861    254   -455       O  
ATOM   4870  CB  ALA B1029       2.147 -12.817 154.517  1.00149.92           C  
ANISOU 4870  CB  ALA B1029    17631  15849  23482   -667    150   -585       C  
ATOM   4871  N   LEU B1030       1.734 -10.485 156.468  1.00145.38           N  
ANISOU 4871  N   LEU B1030    17462  15540  22234   -925    277   -302       N  
ATOM   4872  CA  LEU B1030       1.298  -9.108 156.760  1.00143.18           C  
ANISOU 4872  CA  LEU B1030    17383  15374  21645  -1003    417   -322       C  
ATOM   4873  C   LEU B1030       2.323  -8.288 157.546  1.00141.99           C  
ANISOU 4873  C   LEU B1030    17336  15362  21249  -1154    437   -222       C  
ATOM   4874  O   LEU B1030       2.554  -7.118 157.220  1.00142.10           O  
ANISOU 4874  O   LEU B1030    17469  15466  21057  -1165    543   -320       O  
ATOM   4875  CB  LEU B1030      -0.041  -9.106 157.516  1.00143.61           C  
ANISOU 4875  CB  LEU B1030    17505  15377  21681  -1066    490   -246       C  
ATOM   4876  CG  LEU B1030      -1.295  -9.470 156.711  1.00143.42           C  
ANISOU 4876  CG  LEU B1030    17429  15249  21815   -936    519   -358       C  
ATOM   4877  CD1 LEU B1030      -2.456  -9.772 157.646  1.00143.77           C  
ANISOU 4877  CD1 LEU B1030    17504  15225  21895  -1009    558   -239       C  
ATOM   4878  CD2 LEU B1030      -1.672  -8.365 155.732  1.00142.44           C  
ANISOU 4878  CD2 LEU B1030    17376  15182  21560   -865    635   -507       C  
ATOM   4879  N   THR B1031       2.927  -8.893 158.572  1.00141.28           N  
ANISOU 4879  N   THR B1031    17188  15299  21190  -1283    332    -13       N  
ATOM   4880  CA  THR B1031       3.960  -8.207 159.373  1.00140.58           C  
ANISOU 4880  CA  THR B1031    17181  15376  20857  -1465    331    103       C  
ATOM   4881  C   THR B1031       5.207  -7.846 158.542  1.00138.30           C  
ANISOU 4881  C   THR B1031    16861  15140  20546  -1385    296     12       C  
ATOM   4882  O   THR B1031       5.754  -6.738 158.674  1.00138.70           O  
ANISOU 4882  O   THR B1031    17043  15321  20335  -1476    376    -26       O  
ATOM   4883  CB  THR B1031       4.376  -9.037 160.606  1.00142.64           C  
ANISOU 4883  CB  THR B1031    17343  15684  21167  -1641    193    397       C  
ATOM   4884  OG1 THR B1031       4.700 -10.374 160.206  1.00145.13           O  
ANISOU 4884  OG1 THR B1031    17430  15854  21860  -1508     37    481       O  
ATOM   4885  CG2 THR B1031       3.250  -9.080 161.634  1.00142.90           C  
ANISOU 4885  CG2 THR B1031    17451  15737  21106  -1793    255    493       C  
ATOM   4886  N   LYS B1032       5.633  -8.774 157.683  1.00136.13           N  
ANISOU 4886  N   LYS B1032    16408  14756  20557  -1223    195    -39       N  
ATOM   4887  CA  LYS B1032       6.744  -8.536 156.748  1.00134.93           C  
ANISOU 4887  CA  LYS B1032    16205  14640  20420  -1131    175   -160       C  
ATOM   4888  C   LYS B1032       6.388  -7.502 155.670  1.00133.04           C  
ANISOU 4888  C   LYS B1032    16082  14453  20014  -1037    301   -404       C  
ATOM   4889  O   LYS B1032       7.230  -6.671 155.308  1.00132.46           O  
ANISOU 4889  O   LYS B1032    16066  14488  19773  -1047    331   -464       O  
ATOM   4890  CB  LYS B1032       7.203  -9.848 156.098  1.00135.39           C  
ANISOU 4890  CB  LYS B1032    16026  14548  20865   -997     72   -187       C  
ATOM   4891  CG  LYS B1032       7.902 -10.790 157.066  1.00136.63           C  
ANISOU 4891  CG  LYS B1032    16021  14656  21235  -1084    -67    101       C  
ATOM   4892  CD  LYS B1032       8.162 -12.156 156.453  1.00137.22           C  
ANISOU 4892  CD  LYS B1032    15836  14521  21780   -943   -132     65       C  
ATOM   4893  CE  LYS B1032       8.743 -13.117 157.479  1.00138.57           C  
ANISOU 4893  CE  LYS B1032    15810  14620  22220  -1031   -275    414       C  
ATOM   4894  NZ  LYS B1032       8.623 -14.540 157.058  1.00139.41           N  
ANISOU 4894  NZ  LYS B1032    15654  14464  22849   -902   -312    396       N  
ATOM   4895  N   MET B1033       5.154  -7.561 155.161  1.00131.28           N  
ANISOU 4895  N   MET B1033    15874  14159  19845   -955    366   -518       N  
ATOM   4896  CA  MET B1033       4.628  -6.515 154.261  1.00128.58           C  
ANISOU 4896  CA  MET B1033    15626  13878  19347   -894    483   -681       C  
ATOM   4897  C   MET B1033       4.624  -5.138 154.929  1.00126.23           C  
ANISOU 4897  C   MET B1033    15513  13674  18774  -1014    608   -630       C  
ATOM   4898  O   MET B1033       5.001  -4.140 154.304  1.00125.81           O  
ANISOU 4898  O   MET B1033    15518  13704  18579   -993    676   -716       O  
ATOM   4899  CB  MET B1033       3.209  -6.850 153.780  1.00128.46           C  
ANISOU 4899  CB  MET B1033    15582  13779  19448   -815    521   -753       C  
ATOM   4900  CG  MET B1033       3.162  -7.885 152.673  1.00129.03           C  
ANISOU 4900  CG  MET B1033    15484  13796  19744   -698    446   -902       C  
ATOM   4901  SD  MET B1033       1.492  -8.213 152.082  1.00129.00           S  
ANISOU 4901  SD  MET B1033    15444  13731  19838   -637    484   -977       S  
ATOM   4902  CE  MET B1033       1.194  -6.780 151.050  1.00128.01           C  
ANISOU 4902  CE  MET B1033    15391  13765  19481   -617    582  -1059       C  
ATOM   4903  N   ARG B1034       4.201  -5.099 156.193  1.00124.55           N  
ANISOU 4903  N   ARG B1034    15381  13447  18494  -1156    648   -496       N  
ATOM   4904  CA  ARG B1034       4.208  -3.866 156.985  1.00123.30           C  
ANISOU 4904  CA  ARG B1034    15393  13368  18086  -1315    798   -473       C  
ATOM   4905  C   ARG B1034       5.637  -3.356 157.169  1.00122.44           C  
ANISOU 4905  C   ARG B1034    15320  13391  17811  -1406    764   -446       C  
ATOM   4906  O   ARG B1034       5.944  -2.212 156.801  1.00121.97           O  
ANISOU 4906  O   ARG B1034    15350  13390  17603  -1414    873   -536       O  
ATOM   4907  CB  ARG B1034       3.538  -4.087 158.349  1.00124.08           C  
ANISOU 4907  CB  ARG B1034    15552  13455  18136  -1489    844   -350       C  
ATOM   4908  CG  ARG B1034       3.069  -2.819 159.025  1.00124.29           C  
ANISOU 4908  CG  ARG B1034    15748  13516  17958  -1644   1069   -399       C  
ATOM   4909  CD  ARG B1034       2.212  -3.149 160.236  1.00125.58           C  
ANISOU 4909  CD  ARG B1034    15954  13665  18094  -1811   1130   -312       C  
ATOM   4910  NE  ARG B1034       1.885  -1.949 160.996  1.00125.83           N  
ANISOU 4910  NE  ARG B1034    16143  13736  17931  -2003   1376   -388       N  
ATOM   4911  CZ  ARG B1034       2.711  -1.312 161.830  1.00126.80           C  
ANISOU 4911  CZ  ARG B1034    16364  14010  17803  -2244   1441   -381       C  
ATOM   4912  NH1 ARG B1034       3.962  -1.734 162.028  1.00126.97           N  
ANISOU 4912  NH1 ARG B1034    16340  14173  17728  -2318   1257   -264       N  
ATOM   4913  NH2 ARG B1034       2.289  -0.223 162.465  1.00128.27           N  
ANISOU 4913  NH2 ARG B1034    16685  14203  17847  -2423   1706   -498       N  
ATOM   4914  N   ALA B1035       6.510  -4.225 157.689  1.00122.08           N  
ANISOU 4914  N   ALA B1035    15183  13384  17818  -1470    607   -304       N  
ATOM   4915  CA  ALA B1035       7.940  -3.906 157.851  1.00121.43           C  
ANISOU 4915  CA  ALA B1035    15101  13429  17609  -1554    543   -245       C  
ATOM   4916  C   ALA B1035       8.584  -3.411 156.546  1.00119.04           C  
ANISOU 4916  C   ALA B1035    14773  13143  17311  -1396    552   -406       C  
ATOM   4917  O   ALA B1035       9.380  -2.462 156.557  1.00117.70           O  
ANISOU 4917  O   ALA B1035    14688  13083  16946  -1469    601   -429       O  
ATOM   4918  CB  ALA B1035       8.695  -5.115 158.385  1.00122.88           C  
ANISOU 4918  CB  ALA B1035    15121  13613  17951  -1600    352    -38       C  
ATOM   4919  N   ALA B1036       8.228  -4.056 155.434  1.00118.07           N  
ANISOU 4919  N   ALA B1036    14532  12926  17401  -1202    508   -521       N  
ATOM   4920  CA  ALA B1036       8.641  -3.608 154.100  1.00116.67           C  
ANISOU 4920  CA  ALA B1036    14323  12791  17214  -1069    527   -689       C  
ATOM   4921  C   ALA B1036       8.050  -2.241 153.734  1.00115.24           C  
ANISOU 4921  C   ALA B1036    14276  12656  16851  -1072    683   -774       C  
ATOM   4922  O   ALA B1036       8.727  -1.430 153.099  1.00115.24           O  
ANISOU 4922  O   ALA B1036    14302  12748  16736  -1051    714   -841       O  
ATOM   4923  CB  ALA B1036       8.262  -4.643 153.048  1.00117.16           C  
ANISOU 4923  CB  ALA B1036    14224  12765  17523   -910    463   -811       C  
ATOM   4924  N   ALA B1037       6.796  -1.995 154.125  1.00114.61           N  
ANISOU 4924  N   ALA B1037    14263  12503  16777  -1096    786   -760       N  
ATOM   4925  CA  ALA B1037       6.152  -0.690 153.890  1.00114.10           C  
ANISOU 4925  CA  ALA B1037    14300  12443  16609  -1104    958   -808       C  
ATOM   4926  C   ALA B1037       6.810   0.445 154.684  1.00115.12           C  
ANISOU 4926  C   ALA B1037    14570  12638  16532  -1263   1074   -783       C  
ATOM   4927  O   ALA B1037       7.013   1.546 154.150  1.00115.04           O  
ANISOU 4927  O   ALA B1037    14601  12663  16444  -1247   1174   -837       O  
ATOM   4928  CB  ALA B1037       4.661  -0.758 154.198  1.00113.99           C  
ANISOU 4928  CB  ALA B1037    14305  12313  16693  -1097   1052   -787       C  
ATOM   4929  N   LEU B1038       7.141   0.171 155.948  1.00116.62           N  
ANISOU 4929  N   LEU B1038    14822  12856  16632  -1436   1061   -694       N  
ATOM   4930  CA  LEU B1038       7.857   1.135 156.799  1.00116.96           C  
ANISOU 4930  CA  LEU B1038    14996  12994  16449  -1638   1165   -682       C  
ATOM   4931  C   LEU B1038       9.273   1.427 156.291  1.00116.14           C  
ANISOU 4931  C   LEU B1038    14868  13006  16250  -1621   1076   -690       C  
ATOM   4932  O   LEU B1038       9.743   2.562 156.399  1.00116.37           O  
ANISOU 4932  O   LEU B1038    14996  13094  16123  -1714   1196   -738       O  
ATOM   4933  CB  LEU B1038       7.923   0.643 158.251  1.00118.81           C  
ANISOU 4933  CB  LEU B1038    15275  13285  16580  -1865   1140   -562       C  
ATOM   4934  CG  LEU B1038       6.595   0.520 159.006  1.00119.49           C  
ANISOU 4934  CG  LEU B1038    15411  13283  16704  -1945   1264   -558       C  
ATOM   4935  CD1 LEU B1038       6.806  -0.213 160.325  1.00120.86           C  
ANISOU 4935  CD1 LEU B1038    15586  13558  16775  -2172   1178   -402       C  
ATOM   4936  CD2 LEU B1038       5.961   1.886 159.237  1.00119.27           C  
ANISOU 4936  CD2 LEU B1038    15516  13204  16595  -2035   1546   -688       C  
ATOM   4937  N   ASP B1039       9.947   0.404 155.756  1.00114.79           N  
ANISOU 4937  N   ASP B1039    14560  12856  16196  -1509    882   -649       N  
ATOM   4938  CA  ASP B1039      11.244   0.584 155.082  1.00112.83           C  
ANISOU 4938  CA  ASP B1039    14263  12704  15903  -1460    798   -672       C  
ATOM   4939  C   ASP B1039      11.083   1.384 153.786  1.00110.72           C  
ANISOU 4939  C   ASP B1039    13989  12440  15637  -1314    872   -809       C  
ATOM   4940  O   ASP B1039      11.863   2.303 153.511  1.00110.21           O  
ANISOU 4940  O   ASP B1039    13973  12462  15437  -1344    915   -840       O  
ATOM   4941  CB  ASP B1039      11.895  -0.770 154.776  1.00112.63           C  
ANISOU 4941  CB  ASP B1039    14063  12662  16068  -1367    605   -615       C  
ATOM   4942  CG  ASP B1039      13.324  -0.633 154.250  1.00111.98           C  
ANISOU 4942  CG  ASP B1039    13920  12677  15950  -1341    526   -624       C  
ATOM   4943  OD1 ASP B1039      14.180  -0.084 154.973  1.00112.31           O  
ANISOU 4943  OD1 ASP B1039    14032  12825  15813  -1497    524   -530       O  
ATOM   4944  OD2 ASP B1039      13.591  -1.073 153.105  1.00111.23           O  
ANISOU 4944  OD2 ASP B1039    13703  12561  15996  -1179    474   -733       O  
ATOM   4945  N   ALA B1040      10.065   1.029 152.999  1.00109.40           N  
ANISOU 4945  N   ALA B1040    13751  12194  15619  -1174    879   -873       N  
ATOM   4946  CA  ALA B1040       9.787   1.699 151.727  1.00108.37           C  
ANISOU 4946  CA  ALA B1040    13582  12097  15494  -1057    928   -962       C  
ATOM   4947  C   ALA B1040       9.391   3.159 151.910  1.00107.58           C  
ANISOU 4947  C   ALA B1040    13595  11983  15298  -1120   1113   -952       C  
ATOM   4948  O   ALA B1040       9.723   3.983 151.070  1.00105.87           O  
ANISOU 4948  O   ALA B1040    13357  11834  15032  -1075   1146   -979       O  
ATOM   4949  CB  ALA B1040       8.707   0.957 150.954  1.00108.55           C  
ANISOU 4949  CB  ALA B1040    13496  12063  15683   -935    890  -1008       C  
ATOM   4950  N   GLN B1041       8.699   3.472 153.009  1.00108.49           N  
ANISOU 4950  N   GLN B1041    13814  12005  15401  -1235   1245   -914       N  
ATOM   4951  CA  GLN B1041       8.337   4.860 153.317  1.00108.78           C  
ANISOU 4951  CA  GLN B1041    13950  11988  15393  -1317   1465   -927       C  
ATOM   4952  C   GLN B1041       9.550   5.774 153.557  1.00109.34           C  
ANISOU 4952  C   GLN B1041    14103  12151  15290  -1429   1514   -949       C  
ATOM   4953  O   GLN B1041       9.489   6.962 153.228  1.00110.01           O  
ANISOU 4953  O   GLN B1041    14212  12205  15380  -1432   1664   -972       O  
ATOM   4954  CB  GLN B1041       7.387   4.924 154.519  1.00109.66           C  
ANISOU 4954  CB  GLN B1041    14153  11982  15530  -1447   1621   -918       C  
ATOM   4955  CG  GLN B1041       6.731   6.289 154.697  1.00110.11           C  
ANISOU 4955  CG  GLN B1041    14272  11924  15639  -1504   1891   -956       C  
ATOM   4956  CD  GLN B1041       5.668   6.301 155.781  1.00110.56           C  
ANISOU 4956  CD  GLN B1041    14399  11854  15753  -1626   2070   -975       C  
ATOM   4957  OE1 GLN B1041       4.682   5.571 155.707  1.00109.65           O  
ANISOU 4957  OE1 GLN B1041    14224  11665  15773  -1542   2028   -936       O  
ATOM   4958  NE2 GLN B1041       5.861   7.141 156.792  1.00111.46           N  
ANISOU 4958  NE2 GLN B1041    14639  11950  15760  -1840   2283  -1052       N  
ATOM   4959  N   LYS B1042      10.631   5.225 154.119  1.00110.13           N  
ANISOU 4959  N   LYS B1042    14227  12357  15258  -1522   1389   -924       N  
ATOM   4960  CA  LYS B1042      11.844   6.012 154.405  1.00110.73           C  
ANISOU 4960  CA  LYS B1042    14378  12541  15152  -1648   1417   -934       C  
ATOM   4961  C   LYS B1042      12.588   6.450 153.135  1.00108.66           C  
ANISOU 4961  C   LYS B1042    14041  12355  14889  -1510   1353   -961       C  
ATOM   4962  O   LYS B1042      12.712   5.710 152.150  1.00107.07           O  
ANISOU 4962  O   LYS B1042    13714  12192  14773  -1351   1203   -966       O  
ATOM   4963  CB  LYS B1042      12.795   5.246 155.338  1.00112.69           C  
ANISOU 4963  CB  LYS B1042    14642  12901  15273  -1796   1277   -853       C  
ATOM   4964  CG  LYS B1042      12.241   5.014 156.732  1.00114.79           C  
ANISOU 4964  CG  LYS B1042    14993  13152  15467  -2005   1350   -810       C  
ATOM   4965  CD  LYS B1042      13.154   4.107 157.540  1.00116.22           C  
ANISOU 4965  CD  LYS B1042    15138  13467  15553  -2145   1165   -665       C  
ATOM   4966  CE  LYS B1042      12.524   3.710 158.866  1.00117.87           C  
ANISOU 4966  CE  LYS B1042    15402  13692  15689  -2361   1207   -593       C  
ATOM   4967  NZ  LYS B1042      13.405   2.788 159.634  1.00119.15           N  
ANISOU 4967  NZ  LYS B1042    15490  13999  15779  -2507   1002   -392       N  
ATOM   4968  N   ARG B1062       3.873   9.156 151.195  1.00126.55           N  
ANISOU 4968  N   ARG B1062    15929  13699  18454  -1063   2230   -688       N  
ATOM   4969  CA  ARG B1062       3.578   9.145 152.625  1.00127.76           C  
ANISOU 4969  CA  ARG B1062    16227  13717  18598  -1207   2410   -788       C  
ATOM   4970  C   ARG B1062       2.154   8.655 152.880  1.00126.35           C  
ANISOU 4970  C   ARG B1062    15997  13399  18608  -1167   2471   -742       C  
ATOM   4971  O   ARG B1062       1.938   7.726 153.665  1.00127.22           O  
ANISOU 4971  O   ARG B1062    16182  13513  18640  -1225   2419   -796       O  
ATOM   4972  CB  ARG B1062       3.746  10.546 153.225  1.00130.73           C  
ANISOU 4972  CB  ARG B1062    16672  13954  19043  -1332   2708   -847       C  
ATOM   4973  CG  ARG B1062       5.109  11.185 152.989  1.00132.33           C  
ANISOU 4973  CG  ARG B1062    16923  14278  19078  -1381   2676   -887       C  
ATOM   4974  CD  ARG B1062       5.074  12.701 153.141  1.00135.59           C  
ANISOU 4974  CD  ARG B1062    17333  14522  19662  -1451   2974   -907       C  
ATOM   4975  NE  ARG B1062       6.250  13.327 152.532  1.00137.74           N  
ANISOU 4975  NE  ARG B1062    17597  14915  19822  -1444   2905   -893       N  
ATOM   4976  CZ  ARG B1062       6.433  14.641 152.369  1.00140.46           C  
ANISOU 4976  CZ  ARG B1062    17905  15142  20321  -1475   3113   -880       C  
ATOM   4977  NH1 ARG B1062       5.516  15.525 152.770  1.00142.59           N  
ANISOU 4977  NH1 ARG B1062    18132  15144  20899  -1516   3428   -887       N  
ATOM   4978  NH2 ARG B1062       7.553  15.080 151.795  1.00140.06           N  
ANISOU 4978  NH2 ARG B1062    17847  15227  20139  -1465   3015   -859       N  
ATOM   4979  N   HIS B1063       1.190   9.276 152.199  1.00123.57           N  
ANISOU 4979  N   HIS B1063    15501  12930  18517  -1070   2570   -614       N  
ATOM   4980  CA  HIS B1063      -0.222   8.966 152.409  1.00121.26           C  
ANISOU 4980  CA  HIS B1063    15143  12488  18443  -1030   2654   -548       C  
ATOM   4981  C   HIS B1063      -0.691   7.684 151.707  1.00118.64           C  
ANISOU 4981  C   HIS B1063    14717  12278  18080   -917   2386   -480       C  
ATOM   4982  O   HIS B1063      -1.613   7.012 152.188  1.00120.87           O  
ANISOU 4982  O   HIS B1063    15003  12476  18445   -916   2401   -477       O  
ATOM   4983  CB  HIS B1063      -1.111  10.145 152.017  1.00121.32           C  
ANISOU 4983  CB  HIS B1063    15006  12301  18789   -980   2879   -407       C  
ATOM   4984  CG  HIS B1063      -2.480  10.059 152.603  1.00120.85           C  
ANISOU 4984  CG  HIS B1063    14909  12031  18975   -983   3058   -377       C  
ATOM   4985  ND1 HIS B1063      -2.741  10.362 153.922  1.00120.60           N  
ANISOU 4985  ND1 HIS B1063    15009  11825  18986  -1129   3334   -534       N  
ATOM   4986  CD2 HIS B1063      -3.653   9.652 152.067  1.00120.47           C  
ANISOU 4986  CD2 HIS B1063    14707  11938  19127   -876   2998   -215       C  
ATOM   4987  CE1 HIS B1063      -4.024  10.167 154.166  1.00122.07           C  
ANISOU 4987  CE1 HIS B1063    15122  11850  19407  -1098   3447   -472       C  
ATOM   4988  NE2 HIS B1063      -4.596   9.730 153.059  1.00121.50           N  
ANISOU 4988  NE2 HIS B1063    14876  11849  19438   -938   3239   -269       N  
ATOM   4989  N   GLY B1064      -0.071   7.344 150.579  1.00115.01           N  
ANISOU 4989  N   GLY B1064    14172  12020  17505   -838   2156   -440       N  
ATOM   4990  CA  GLY B1064      -0.253   6.019 149.976  1.00112.56           C  
ANISOU 4990  CA  GLY B1064    13795  11849  17122   -769   1907   -445       C  
ATOM   4991  C   GLY B1064       0.206   4.931 150.943  1.00110.27           C  
ANISOU 4991  C   GLY B1064    13641  11565  16690   -829   1828   -585       C  
ATOM   4992  O   GLY B1064      -0.472   3.918 151.116  1.00109.60           O  
ANISOU 4992  O   GLY B1064    13532  11452  16656   -804   1747   -588       O  
ATOM   4993  N   PHE B1065       1.349   5.161 151.583  1.00108.53           N  
ANISOU 4993  N   PHE B1065    13548  11384  16304   -918   1850   -675       N  
ATOM   4994  CA  PHE B1065       1.856   4.291 152.653  1.00106.14           C  
ANISOU 4994  CA  PHE B1065    13361  11092  15872  -1011   1790   -757       C  
ATOM   4995  C   PHE B1065       0.977   4.310 153.912  1.00105.71           C  
ANISOU 4995  C   PHE B1065    13395  10886  15884  -1118   1967   -763       C  
ATOM   4996  O   PHE B1065       0.839   3.276 154.571  1.00106.22           O  
ANISOU 4996  O   PHE B1065    13489  10954  15915  -1160   1877   -771       O  
ATOM   4997  CB  PHE B1065       3.315   4.635 153.019  1.00105.34           C  
ANISOU 4997  CB  PHE B1065    13359  11096  15570  -1106   1770   -820       C  
ATOM   4998  CG  PHE B1065       4.314   4.275 151.950  1.00103.76           C  
ANISOU 4998  CG  PHE B1065    13078  11058  15285  -1017   1570   -838       C  
ATOM   4999  CD1 PHE B1065       4.474   2.953 151.549  1.00103.03           C  
ANISOU 4999  CD1 PHE B1065    12907  11033  15207   -947   1365   -864       C  
ATOM   5000  CD2 PHE B1065       5.096   5.256 151.337  1.00103.01           C  
ANISOU 5000  CD2 PHE B1065    12976  11043  15117  -1010   1601   -840       C  
ATOM   5001  CE1 PHE B1065       5.372   2.615 150.543  1.00102.18           C  
ANISOU 5001  CE1 PHE B1065    12714  11067  15041   -878   1214   -914       C  
ATOM   5002  CE2 PHE B1065       6.008   4.922 150.347  1.00102.46           C  
ANISOU 5002  CE2 PHE B1065    12830  11136  14964   -941   1430   -870       C  
ATOM   5003  CZ  PHE B1065       6.146   3.600 149.949  1.00102.08           C  
ANISOU 5003  CZ  PHE B1065    12703  11153  14929   -879   1244   -918       C  
ATOM   5004  N   ASP B1066       0.390   5.466 154.253  1.00104.36           N  
ANISOU 5004  N   ASP B1066    13251  10575  15823  -1171   2227   -759       N  
ATOM   5005  CA  ASP B1066      -0.633   5.535 155.319  1.00103.81           C  
ANISOU 5005  CA  ASP B1066    13238  10347  15855  -1270   2432   -780       C  
ATOM   5006  C   ASP B1066      -1.826   4.632 154.973  1.00103.94           C  
ANISOU 5006  C   ASP B1066    13150  10307  16035  -1152   2337   -697       C  
ATOM   5007  O   ASP B1066      -2.209   3.762 155.766  1.00103.52           O  
ANISOU 5007  O   ASP B1066    13143  10238  15951  -1214   2302   -713       O  
ATOM   5008  CB  ASP B1066      -1.154   6.968 155.546  1.00104.27           C  
ANISOU 5008  CB  ASP B1066    13300  10226  16090  -1323   2761   -799       C  
ATOM   5009  CG  ASP B1066      -0.104   7.922 156.122  1.00103.20           C  
ANISOU 5009  CG  ASP B1066    13287  10119  15805  -1485   2915   -917       C  
ATOM   5010  OD1 ASP B1066       0.921   7.462 156.665  1.00102.24           O  
ANISOU 5010  OD1 ASP B1066    13274  10156  15416  -1602   2794   -982       O  
ATOM   5011  OD2 ASP B1066      -0.318   9.153 156.042  1.00100.79           O  
ANISOU 5011  OD2 ASP B1066    12955   9667  15672  -1504   3167   -933       O  
ATOM   5012  N   ILE B1067      -2.395   4.845 153.783  1.00104.82           N  
ANISOU 5012  N   ILE B1067    13109  10406  16311  -1000   2288   -592       N  
ATOM   5013  CA  ILE B1067      -3.543   4.054 153.296  1.00105.65           C  
ANISOU 5013  CA  ILE B1067    13092  10478  16568   -896   2189   -501       C  
ATOM   5014  C   ILE B1067      -3.203   2.559 153.212  1.00106.19           C  
ANISOU 5014  C   ILE B1067    13163  10670  16515   -869   1928   -546       C  
ATOM   5015  O   ILE B1067      -4.031   1.718 153.554  1.00106.47           O  
ANISOU 5015  O   ILE B1067    13179  10645  16630   -859   1890   -527       O  
ATOM   5016  CB  ILE B1067      -4.077   4.575 151.928  1.00105.27           C  
ANISOU 5016  CB  ILE B1067    12859  10458  16680   -772   2152   -353       C  
ATOM   5017  CG1 ILE B1067      -4.735   5.954 152.108  1.00106.25           C  
ANISOU 5017  CG1 ILE B1067    12936  10391  17043   -785   2438   -262       C  
ATOM   5018  CG2 ILE B1067      -5.090   3.601 151.311  1.00105.49           C  
ANISOU 5018  CG2 ILE B1067    12758  10517  16804   -688   1998   -270       C  
ATOM   5019  CD1 ILE B1067      -4.887   6.748 150.830  1.00106.70           C  
ANISOU 5019  CD1 ILE B1067    12805  10498  17238   -697   2410    -79       C  
ATOM   5020  N   LEU B1068      -1.993   2.236 152.761  1.00107.90           N  
ANISOU 5020  N   LEU B1068    13388  11040  16566   -858   1760   -606       N  
ATOM   5021  CA  LEU B1068      -1.534   0.839 152.685  1.00109.42           C  
ANISOU 5021  CA  LEU B1068    13560  11319  16694   -834   1537   -659       C  
ATOM   5022  C   LEU B1068      -1.347   0.225 154.078  1.00110.71           C  
ANISOU 5022  C   LEU B1068    13834  11430  16798   -951   1549   -678       C  
ATOM   5023  O   LEU B1068      -2.027  -0.746 154.426  1.00111.47           O  
ANISOU 5023  O   LEU B1068    13900  11469  16982   -942   1485   -652       O  
ATOM   5024  CB  LEU B1068      -0.246   0.745 151.859  1.00109.77           C  
ANISOU 5024  CB  LEU B1068    13571  11524  16610   -800   1389   -722       C  
ATOM   5025  CG  LEU B1068       0.406  -0.634 151.682  1.00109.93           C  
ANISOU 5025  CG  LEU B1068    13542  11612  16614   -772   1184   -793       C  
ATOM   5026  CD1 LEU B1068       0.832  -0.847 150.234  1.00110.00           C  
ANISOU 5026  CD1 LEU B1068    13424  11765  16603   -692   1058   -862       C  
ATOM   5027  CD2 LEU B1068       1.596  -0.819 152.618  1.00110.18           C  
ANISOU 5027  CD2 LEU B1068    13668  11665  16527   -865   1153   -811       C  
ATOM   5028  N   VAL B1069      -0.463   0.816 154.882  1.00112.12           N  
ANISOU 5028  N   VAL B1069    14132  11642  16823  -1079   1631   -709       N  
ATOM   5029  CA  VAL B1069      -0.167   0.318 156.242  1.00113.90           C  
ANISOU 5029  CA  VAL B1069    14455  11876  16945  -1241   1634   -699       C  
ATOM   5030  C   VAL B1069      -1.445   0.246 157.102  1.00115.03           C  
ANISOU 5030  C   VAL B1069    14632  11896  17178  -1312   1781   -671       C  
ATOM   5031  O   VAL B1069      -1.597  -0.680 157.906  1.00116.82           O  
ANISOU 5031  O   VAL B1069    14867  12129  17387  -1390   1704   -625       O  
ATOM   5032  CB  VAL B1069       0.934   1.160 156.949  1.00115.24           C  
ANISOU 5032  CB  VAL B1069    14747  12130  16906  -1409   1726   -738       C  
ATOM   5033  CG1 VAL B1069       1.085   0.777 158.425  1.00116.68           C  
ANISOU 5033  CG1 VAL B1069    15022  12356  16952  -1631   1751   -706       C  
ATOM   5034  CG2 VAL B1069       2.276   1.000 156.236  1.00114.33           C  
ANISOU 5034  CG2 VAL B1069    14593  12144  16702  -1348   1550   -749       C  
ATOM   5035  N   GLY B1070      -2.351   1.212 156.919  1.00115.56           N  
ANISOU 5035  N   GLY B1070    14697  11847  17363  -1286   1993   -684       N  
ATOM   5036  CA  GLY B1070      -3.688   1.153 157.519  1.00116.04           C  
ANISOU 5036  CA  GLY B1070    14757  11769  17561  -1319   2144   -660       C  
ATOM   5037  C   GLY B1070      -4.476  -0.096 157.128  1.00115.60           C  
ANISOU 5037  C   GLY B1070    14595  11687  17640  -1197   1964   -589       C  
ATOM   5038  O   GLY B1070      -5.114  -0.730 157.977  1.00115.43           O  
ANISOU 5038  O   GLY B1070    14595  11617  17643  -1272   1982   -561       O  
ATOM   5039  N   GLN B1071      -4.427  -0.450 155.843  1.00115.28           N  
ANISOU 5039  N   GLN B1071    14434  11691  17675  -1031   1796   -567       N  
ATOM   5040  CA  GLN B1071      -5.084  -1.666 155.339  1.00115.43           C  
ANISOU 5040  CA  GLN B1071    14341  11698  17817   -927   1621   -529       C  
ATOM   5041  C   GLN B1071      -4.372  -2.949 155.792  1.00117.27           C  
ANISOU 5041  C   GLN B1071    14576  11986  17992   -962   1428   -540       C  
ATOM   5042  O   GLN B1071      -5.025  -3.977 156.014  1.00117.98           O  
ANISOU 5042  O   GLN B1071    14612  12020  18194   -943   1344   -502       O  
ATOM   5043  CB  GLN B1071      -5.212  -1.628 153.813  1.00114.02           C  
ANISOU 5043  CB  GLN B1071    14026  11585  17708   -786   1515   -523       C  
ATOM   5044  CG  GLN B1071      -6.250  -0.626 153.328  1.00113.67           C  
ANISOU 5044  CG  GLN B1071    13917  11470  17802   -740   1671   -436       C  
ATOM   5045  CD  GLN B1071      -6.124  -0.289 151.854  1.00113.15           C  
ANISOU 5045  CD  GLN B1071    13718  11529  17743   -652   1575   -399       C  
ATOM   5046  OE1 GLN B1071      -5.379  -0.932 151.107  1.00112.99           O  
ANISOU 5046  OE1 GLN B1071    13652  11654  17624   -622   1392   -473       O  
ATOM   5047  NE2 GLN B1071      -6.873   0.720 151.422  1.00113.51           N  
ANISOU 5047  NE2 GLN B1071    13682  11523  17922   -622   1705   -275       N  
ATOM   5048  N   ILE B1072      -3.045  -2.885 155.920  1.00118.42           N  
ANISOU 5048  N   ILE B1072    14766  12232  17993  -1014   1359   -573       N  
ATOM   5049  CA  ILE B1072      -2.261  -3.973 156.527  1.00118.95           C  
ANISOU 5049  CA  ILE B1072    14820  12340  18033  -1073   1196   -538       C  
ATOM   5050  C   ILE B1072      -2.632  -4.153 158.008  1.00120.65           C  
ANISOU 5050  C   ILE B1072    15118  12529  18194  -1246   1269   -453       C  
ATOM   5051  O   ILE B1072      -2.714  -5.285 158.486  1.00122.62           O  
ANISOU 5051  O   ILE B1072    15307  12759  18522  -1269   1139   -370       O  
ATOM   5052  CB  ILE B1072      -0.732  -3.765 156.350  1.00118.63           C  
ANISOU 5052  CB  ILE B1072    14797  12417  17858  -1099   1116   -568       C  
ATOM   5053  CG1 ILE B1072      -0.357  -3.935 154.873  1.00117.81           C  
ANISOU 5053  CG1 ILE B1072    14583  12355  17823   -940   1012   -659       C  
ATOM   5054  CG2 ILE B1072       0.067  -4.749 157.204  1.00119.74           C  
ANISOU 5054  CG2 ILE B1072    14912  12592  17990  -1194    972   -474       C  
ATOM   5055  CD1 ILE B1072       1.065  -3.551 154.526  1.00117.60           C  
ANISOU 5055  CD1 ILE B1072    14568  12441  17671   -949    961   -704       C  
ATOM   5056  N   ASP B1073      -2.855  -3.047 158.721  1.00121.62           N  
ANISOU 5056  N   ASP B1073    15364  12654  18191  -1381   1486   -477       N  
ATOM   5057  CA  ASP B1073      -3.366  -3.103 160.102  1.00123.34           C  
ANISOU 5057  CA  ASP B1073    15661  12867  18334  -1580   1600   -428       C  
ATOM   5058  C   ASP B1073      -4.816  -3.626 160.161  1.00124.25           C  
ANISOU 5058  C   ASP B1073    15722  12853  18633  -1516   1638   -392       C  
ATOM   5059  O   ASP B1073      -5.149  -4.427 161.043  1.00124.41           O  
ANISOU 5059  O   ASP B1073    15736  12881  18652  -1620   1587   -305       O  
ATOM   5060  CB  ASP B1073      -3.268  -1.734 160.788  1.00124.29           C  
ANISOU 5060  CB  ASP B1073    15921  13012  18290  -1760   1867   -516       C  
ATOM   5061  CG  ASP B1073      -1.825  -1.307 161.065  1.00124.44           C  
ANISOU 5061  CG  ASP B1073    16009  13187  18084  -1891   1829   -533       C  
ATOM   5062  OD1 ASP B1073      -1.006  -2.145 161.510  1.00124.57           O  
ANISOU 5062  OD1 ASP B1073    15997  13323  18009  -1973   1633   -428       O  
ATOM   5063  OD2 ASP B1073      -1.510  -0.116 160.848  1.00124.06           O  
ANISOU 5063  OD2 ASP B1073    16031  13136  17971  -1917   1998   -637       O  
ATOM   5064  N   ASP B1074      -5.662  -3.174 159.231  1.00124.53           N  
ANISOU 5064  N   ASP B1074    15706  12782  18827  -1356   1719   -435       N  
ATOM   5065  CA  ASP B1074      -7.038  -3.700 159.100  1.00125.69           C  
ANISOU 5065  CA  ASP B1074    15778  12809  19169  -1272   1732   -389       C  
ATOM   5066  C   ASP B1074      -7.080  -5.194 158.751  1.00128.28           C  
ANISOU 5066  C   ASP B1074    15992  13137  19609  -1177   1478   -330       C  
ATOM   5067  O   ASP B1074      -8.000  -5.900 159.170  1.00129.11           O  
ANISOU 5067  O   ASP B1074    16061  13171  19824  -1185   1463   -268       O  
ATOM   5068  CB  ASP B1074      -7.849  -2.916 158.055  1.00124.35           C  
ANISOU 5068  CB  ASP B1074    15541  12550  19153  -1126   1840   -405       C  
ATOM   5069  CG  ASP B1074      -8.355  -1.582 158.573  1.00124.25           C  
ANISOU 5069  CG  ASP B1074    15601  12446  19162  -1213   2149   -439       C  
ATOM   5070  OD1 ASP B1074      -7.734  -1.005 159.486  1.00124.59           O  
ANISOU 5070  OD1 ASP B1074    15765  12530  19041  -1387   2286   -506       O  
ATOM   5071  OD2 ASP B1074      -9.386  -1.106 158.056  1.00124.18           O  
ANISOU 5071  OD2 ASP B1074    15511  12320  19349  -1119   2264   -397       O  
ATOM   5072  N   ALA B1075      -6.103  -5.664 157.974  1.00130.92           N  
ANISOU 5072  N   ALA B1075    16263  13541  19939  -1092   1296   -359       N  
ATOM   5073  CA  ALA B1075      -5.934  -7.100 157.718  1.00132.72           C  
ANISOU 5073  CA  ALA B1075    16371  13751  20303  -1024   1078   -328       C  
ATOM   5074  C   ALA B1075      -5.442  -7.812 158.981  1.00134.22           C  
ANISOU 5074  C   ALA B1075    16579  13967  20449  -1172   1004   -209       C  
ATOM   5075  O   ALA B1075      -6.085  -8.749 159.464  1.00133.71           O  
ANISOU 5075  O   ALA B1075    16455  13836  20513  -1189    939   -120       O  
ATOM   5076  CB  ALA B1075      -4.967  -7.331 156.565  1.00133.18           C  
ANISOU 5076  CB  ALA B1075    16348  13870  20382   -914    945   -419       C  
ATOM   5077  N   LEU B1076      -4.319  -7.333 159.521  1.00136.27           N  
ANISOU 5077  N   LEU B1076    16913  14339  20525  -1295   1011   -187       N  
ATOM   5078  CA  LEU B1076      -3.709  -7.868 160.756  1.00139.19           C  
ANISOU 5078  CA  LEU B1076    17289  14787  20808  -1482    932    -34       C  
ATOM   5079  C   LEU B1076      -4.734  -8.025 161.889  1.00141.40           C  
ANISOU 5079  C   LEU B1076    17614  15053  21058  -1633   1022     57       C  
ATOM   5080  O   LEU B1076      -4.771  -9.066 162.556  1.00142.27           O  
ANISOU 5080  O   LEU B1076    17640  15167  21246  -1704    888    219       O  
ATOM   5081  CB  LEU B1076      -2.550  -6.969 161.214  1.00139.61           C  
ANISOU 5081  CB  LEU B1076    17446  14993  20607  -1635    984    -39       C  
ATOM   5082  CG  LEU B1076      -1.646  -7.448 162.357  1.00141.33           C  
ANISOU 5082  CG  LEU B1076    17647  15349  20701  -1852    869    146       C  
ATOM   5083  CD1 LEU B1076      -0.805  -8.636 161.918  1.00141.73           C  
ANISOU 5083  CD1 LEU B1076    17520  15366  20966  -1739    625    258       C  
ATOM   5084  CD2 LEU B1076      -0.752  -6.312 162.833  1.00141.46           C  
ANISOU 5084  CD2 LEU B1076    17797  15529  20422  -2037    977    106       C  
ATOM   5085  N   LYS B1077      -5.575  -7.001 162.064  1.00142.64           N  
ANISOU 5085  N   LYS B1077    17883  15183  21131  -1678   1255    -39       N  
ATOM   5086  CA  LYS B1077      -6.715  -7.032 163.002  1.00144.46           C  
ANISOU 5086  CA  LYS B1077    18154  15379  21353  -1806   1390      2       C  
ATOM   5087  C   LYS B1077      -7.531  -8.336 162.951  1.00145.79           C  
ANISOU 5087  C   LYS B1077    18197  15448  21749  -1711   1242    111       C  
ATOM   5088  O   LYS B1077      -8.004  -8.802 163.989  1.00146.98           O  
ANISOU 5088  O   LYS B1077    18349  15629  21865  -1869   1249    226       O  
ATOM   5089  CB  LYS B1077      -7.635  -5.827 162.750  1.00144.12           C  
ANISOU 5089  CB  LYS B1077    18193  15243  21323  -1774   1666   -139       C  
ATOM   5090  CG  LYS B1077      -8.812  -5.681 163.708  1.00144.78           C  
ANISOU 5090  CG  LYS B1077    18324  15278  21407  -1915   1861   -133       C  
ATOM   5091  CD  LYS B1077      -9.494  -4.331 163.538  1.00144.30           C  
ANISOU 5091  CD  LYS B1077    18331  15112  21384  -1907   2171   -275       C  
ATOM   5092  CE  LYS B1077     -10.858  -4.291 164.211  1.00144.67           C  
ANISOU 5092  CE  LYS B1077    18383  15056  21527  -1981   2369   -279       C  
ATOM   5093  NZ  LYS B1077     -10.782  -4.517 165.681  1.00145.84           N  
ANISOU 5093  NZ  LYS B1077    18610  15341  21459  -2287   2440   -256       N  
ATOM   5094  N   LEU B1078      -7.691  -8.911 161.755  1.00146.53           N  
ANISOU 5094  N   LEU B1078    18177  15434  22060  -1478   1115     69       N  
ATOM   5095  CA  LEU B1078      -8.358 -10.211 161.599  1.00148.05           C  
ANISOU 5095  CA  LEU B1078    18236  15522  22492  -1385    967    151       C  
ATOM   5096  C   LEU B1078      -7.485 -11.361 162.116  1.00150.79           C  
ANISOU 5096  C   LEU B1078    18478  15905  22911  -1448    755    311       C  
ATOM   5097  O   LEU B1078      -7.974 -12.236 162.844  1.00151.78           O  
ANISOU 5097  O   LEU B1078    18535  15997  23135  -1519    683    463       O  
ATOM   5098  CB  LEU B1078      -8.725 -10.477 160.135  1.00146.35           C  
ANISOU 5098  CB  LEU B1078    17925  15209  22470  -1155    906     32       C  
ATOM   5099  CG  LEU B1078      -9.626  -9.453 159.437  1.00144.88           C  
ANISOU 5099  CG  LEU B1078    17786  14988  22273  -1073   1076    -70       C  
ATOM   5100  CD1 LEU B1078      -9.528  -9.585 157.922  1.00144.39           C  
ANISOU 5100  CD1 LEU B1078    17626  14920  22315   -900    986   -179       C  
ATOM   5101  CD2 LEU B1078     -11.062  -9.603 159.904  1.00144.71           C  
ANISOU 5101  CD2 LEU B1078    17759  14872  22350  -1091   1171    -10       C  
ATOM   5102  N   ALA B1079      -6.198 -11.340 161.753  1.00152.44           N  
ANISOU 5102  N   ALA B1079    18657  16175  23088  -1427    659    298       N  
ATOM   5103  CA  ALA B1079      -5.256 -12.432 162.076  1.00153.13           C  
ANISOU 5103  CA  ALA B1079    18600  16267  23314  -1460    455    466       C  
ATOM   5104  C   ALA B1079      -5.129 -12.752 163.573  1.00153.76           C  
ANISOU 5104  C   ALA B1079    18677  16460  23283  -1707    407    721       C  
ATOM   5105  O   ALA B1079      -4.805 -13.884 163.937  1.00154.02           O  
ANISOU 5105  O   ALA B1079    18545  16455  23518  -1729    232    924       O  
ATOM   5106  CB  ALA B1079      -3.881 -12.136 161.488  1.00153.53           C  
ANISOU 5106  CB  ALA B1079    18634  16377  23321  -1413    396    405       C  
ATOM   5107  N   ASN B1080      -5.371 -11.754 164.425  1.00153.63           N  
ANISOU 5107  N   ASN B1080    18825  16588  22957  -1910    571    711       N  
ATOM   5108  CA  ASN B1080      -5.440 -11.956 165.875  1.00155.29           C  
ANISOU 5108  CA  ASN B1080    19048  16953  23002  -2197    559    928       C  
ATOM   5109  C   ASN B1080      -6.637 -12.824 166.273  1.00155.97           C  
ANISOU 5109  C   ASN B1080    19057  16942  23260  -2192    532   1034       C  
ATOM   5110  O   ASN B1080      -6.515 -13.664 167.168  1.00158.22           O  
ANISOU 5110  O   ASN B1080    19234  17302  23580  -2350    393   1296       O  
ATOM   5111  CB  ASN B1080      -5.498 -10.612 166.613  1.00155.44           C  
ANISOU 5111  CB  ASN B1080    19268  17143  22646  -2432    793    820       C  
ATOM   5112  CG  ASN B1080      -4.216  -9.809 166.469  1.00154.84           C  
ANISOU 5112  CG  ASN B1080    19261  17198  22369  -2498    804    762       C  
ATOM   5113  OD1 ASN B1080      -3.471  -9.964 165.499  1.00152.89           O  
ANISOU 5113  OD1 ASN B1080    18947  16877  22265  -2298    693    716       O  
ATOM   5114  ND2 ASN B1080      -3.955  -8.941 167.439  1.00156.05           N  
ANISOU 5114  ND2 ASN B1080    19549  17557  22186  -2795    949    747       N  
ATOM   5115  N   GLU B1081      -7.780 -12.620 165.613  1.00154.21           N  
ANISOU 5115  N   GLU B1081    18876  16564  23150  -2023    656    857       N  
ATOM   5116  CA  GLU B1081      -8.957 -13.472 165.824  1.00154.65           C  
ANISOU 5116  CA  GLU B1081    18851  16504  23402  -1984    626    940       C  
ATOM   5117  C   GLU B1081      -8.785 -14.831 165.148  1.00154.76           C  
ANISOU 5117  C   GLU B1081    18660  16355  23784  -1794    403   1025       C  
ATOM   5118  O   GLU B1081      -9.004 -15.871 165.775  1.00156.22           O  
ANISOU 5118  O   GLU B1081    18715  16512  24129  -1859    273   1242       O  
ATOM   5119  CB  GLU B1081     -10.235 -12.794 165.315  1.00153.56           C  
ANISOU 5119  CB  GLU B1081    18808  16256  23282  -1871    830    741       C  
ATOM   5120  CG  GLU B1081     -10.615 -11.534 166.082  1.00154.39           C  
ANISOU 5120  CG  GLU B1081    19088  16469  23101  -2067   1096    650       C  
ATOM   5121  CD  GLU B1081     -12.106 -11.224 166.029  1.00154.63           C  
ANISOU 5121  CD  GLU B1081    19155  16377  23219  -2013   1283    562       C  
ATOM   5122  OE1 GLU B1081     -12.763 -11.557 165.020  1.00153.70           O  
ANISOU 5122  OE1 GLU B1081    18962  16098  23339  -1778   1238    507       O  
ATOM   5123  OE2 GLU B1081     -12.619 -10.646 167.008  1.00156.01           O  
ANISOU 5123  OE2 GLU B1081    19426  16626  23223  -2224   1484    545       O  
ATOM   5124  N   GLY B1082      -8.401 -14.805 163.872  1.00153.49           N  
ANISOU 5124  N   GLY B1082    18463  16090  23767  -1575    374    846       N  
ATOM   5125  CA  GLY B1082      -8.156 -16.019 163.088  1.00153.15           C  
ANISOU 5125  CA  GLY B1082    18223  15880  24087  -1401    206    853       C  
ATOM   5126  C   GLY B1082      -9.268 -16.282 162.092  1.00151.97           C  
ANISOU 5126  C   GLY B1082    18045  15575  24120  -1217    250    672       C  
ATOM   5127  O   GLY B1082     -10.009 -17.258 162.217  1.00152.32           O  
ANISOU 5127  O   GLY B1082    17977  15498  24398  -1186    183    751       O  
ATOM   5128  N   LYS B1083      -9.376 -15.393 161.106  1.00150.49           N  
ANISOU 5128  N   LYS B1083    17948  15407  23821  -1112    358    447       N  
ATOM   5129  CA  LYS B1083     -10.300 -15.554 159.980  1.00149.41           C  
ANISOU 5129  CA  LYS B1083    17769  15170  23827   -954    386    276       C  
ATOM   5130  C   LYS B1083      -9.580 -15.207 158.675  1.00149.37           C  
ANISOU 5130  C   LYS B1083    17746  15195  23812   -838    379     69       C  
ATOM   5131  O   LYS B1083      -9.276 -14.039 158.411  1.00147.93           O  
ANISOU 5131  O   LYS B1083    17682  15122  23403   -846    479     -7       O  
ATOM   5132  CB  LYS B1083     -11.535 -14.668 160.167  1.00148.04           C  
ANISOU 5132  CB  LYS B1083    17717  15019  23509   -978    553    257       C  
ATOM   5133  CG  LYS B1083     -12.663 -14.979 159.194  1.00147.26           C  
ANISOU 5133  CG  LYS B1083    17547  14830  23574   -850    558    155       C  
ATOM   5134  CD  LYS B1083     -13.777 -13.949 159.258  1.00146.31           C  
ANISOU 5134  CD  LYS B1083    17526  14727  23338   -860    735    150       C  
ATOM   5135  CE  LYS B1083     -14.860 -14.263 158.239  1.00145.98           C  
ANISOU 5135  CE  LYS B1083    17391  14621  23453   -747    717     83       C  
ATOM   5136  NZ  LYS B1083     -15.977 -13.283 158.282  1.00145.89           N  
ANISOU 5136  NZ  LYS B1083    17438  14605  23385   -748    889    118       N  
ATOM   5137  N   VAL B1084      -9.318 -16.233 157.862  1.00150.96           N  
ANISOU 5137  N   VAL B1084    17789  15297  24270   -743    273    -28       N  
ATOM   5138  CA  VAL B1084      -8.600 -16.078 156.591  1.00151.33           C  
ANISOU 5138  CA  VAL B1084    17793  15383  24322   -656    265   -245       C  
ATOM   5139  C   VAL B1084      -9.517 -15.474 155.522  1.00151.24           C  
ANISOU 5139  C   VAL B1084    17817  15435  24214   -598    342   -403       C  
ATOM   5140  O   VAL B1084      -9.130 -14.518 154.843  1.00152.05           O  
ANISOU 5140  O   VAL B1084    17983  15661  24126   -581    397   -502       O  
ATOM   5141  CB  VAL B1084      -8.018 -17.426 156.089  1.00151.98           C  
ANISOU 5141  CB  VAL B1084    17674  15327  24743   -599    159   -328       C  
ATOM   5142  CG1 VAL B1084      -7.323 -17.259 154.737  1.00151.55           C  
ANISOU 5142  CG1 VAL B1084    17573  15331  24674   -536    175   -591       C  
ATOM   5143  CG2 VAL B1084      -7.055 -18.008 157.120  1.00152.97           C  
ANISOU 5143  CG2 VAL B1084    17726  15389  25007   -658     70   -116       C  
ATOM   5144  N   LYS B1085     -10.730 -16.028 155.398  1.00151.59           N  
ANISOU 5144  N   LYS B1085    17804  15401  24392   -578    337   -398       N  
ATOM   5145  CA  LYS B1085     -11.709 -15.607 154.383  1.00151.25           C  
ANISOU 5145  CA  LYS B1085    17755  15425  24289   -541    386   -505       C  
ATOM   5146  C   LYS B1085     -11.762 -14.093 154.219  1.00151.62           C  
ANISOU 5146  C   LYS B1085    17928  15607  24072   -549    498   -478       C  
ATOM   5147  O   LYS B1085     -11.520 -13.574 153.124  1.00152.68           O  
ANISOU 5147  O   LYS B1085    18040  15861  24107   -524    505   -598       O  
ATOM   5148  CB  LYS B1085     -13.118 -16.132 154.722  1.00150.81           C  
ANISOU 5148  CB  LYS B1085    17661  15273  24363   -545    389   -414       C  
ATOM   5149  CG  LYS B1085     -13.300 -17.650 154.659  1.00151.36           C  
ANISOU 5149  CG  LYS B1085    17580  15196  24734   -532    288   -460       C  
ATOM   5150  CD  LYS B1085     -13.002 -18.215 153.280  1.00151.68           C  
ANISOU 5150  CD  LYS B1085    17493  15265  24873   -507    246   -716       C  
ATOM   5151  CE  LYS B1085     -13.574 -19.613 153.105  1.00153.22           C  
ANISOU 5151  CE  LYS B1085    17534  15305  25377   -507    187   -788       C  
ATOM   5152  NZ  LYS B1085     -13.372 -20.110 151.717  1.00154.08           N  
ANISOU 5152  NZ  LYS B1085    17521  15465  25556   -524    180  -1083       N  
ATOM   5153  N   GLU B1086     -12.037 -13.399 155.322  1.00152.51           N  
ANISOU 5153  N   GLU B1086    18161  15702  24082   -600    594   -324       N  
ATOM   5154  CA  GLU B1086     -12.135 -11.932 155.325  1.00152.40           C  
ANISOU 5154  CA  GLU B1086    18260  15772  23873   -615    739   -293       C  
ATOM   5155  C   GLU B1086     -10.824 -11.251 154.911  1.00151.80           C  
ANISOU 5155  C   GLU B1086    18231  15806  23640   -615    739   -377       C  
ATOM   5156  O   GLU B1086     -10.853 -10.249 154.189  1.00152.07           O  
ANISOU 5156  O   GLU B1086    18283  15927  23566   -590    809   -410       O  
ATOM   5157  CB  GLU B1086     -12.598 -11.416 156.700  1.00152.60           C  
ANISOU 5157  CB  GLU B1086    18401  15743  23835   -703    872   -154       C  
ATOM   5158  CG  GLU B1086     -12.857  -9.910 156.788  1.00151.97           C  
ANISOU 5158  CG  GLU B1086    18421  15699  23622   -727   1069   -136       C  
ATOM   5159  CD  GLU B1086     -13.825  -9.391 155.737  1.00150.96           C  
ANISOU 5159  CD  GLU B1086    18215  15574  23569   -643   1116   -132       C  
ATOM   5160  OE1 GLU B1086     -14.894 -10.009 155.543  1.00151.22           O  
ANISOU 5160  OE1 GLU B1086    18162  15548  23745   -611   1078    -86       O  
ATOM   5161  OE2 GLU B1086     -13.515  -8.358 155.106  1.00147.73           O  
ANISOU 5161  OE2 GLU B1086    17816  15234  23078   -619   1186   -153       O  
ATOM   5162  N   ALA B1087      -9.686 -11.814 155.328  1.00151.08           N  
ANISOU 5162  N   ALA B1087    18136  15709  23556   -643    654   -391       N  
ATOM   5163  CA  ALA B1087      -8.363 -11.261 154.976  1.00150.26           C  
ANISOU 5163  CA  ALA B1087    18068  15707  23316   -645    644   -466       C  
ATOM   5164  C   ALA B1087      -8.121 -11.149 153.459  1.00150.29           C  
ANISOU 5164  C   ALA B1087    17989  15805  23307   -572    605   -632       C  
ATOM   5165  O   ALA B1087      -7.335 -10.301 153.020  1.00151.17           O  
ANISOU 5165  O   ALA B1087    18146  16026  23263   -571    636   -683       O  
ATOM   5166  CB  ALA B1087      -7.246 -12.063 155.635  1.00150.42           C  
ANISOU 5166  CB  ALA B1087    18056  15693  23404   -685    540   -423       C  
ATOM   5167  N   GLN B1088      -8.796 -11.989 152.669  1.00151.35           N  
ANISOU 5167  N   GLN B1088    18000  15915  23590   -534    540   -719       N  
ATOM   5168  CA  GLN B1088      -8.760 -11.875 151.202  1.00152.10           C  
ANISOU 5168  CA  GLN B1088    18006  16144  23637   -512    512   -878       C  
ATOM   5169  C   GLN B1088      -9.434 -10.590 150.686  1.00151.75           C  
ANISOU 5169  C   GLN B1088    18000  16222  23435   -515    596   -801       C  
ATOM   5170  O   GLN B1088      -9.053 -10.079 149.628  1.00152.60           O  
ANISOU 5170  O   GLN B1088    18064  16492  23423   -521    583   -881       O  
ATOM   5171  CB  GLN B1088      -9.392 -13.109 150.540  1.00153.63           C  
ANISOU 5171  CB  GLN B1088    18054  16297  24019   -511    436  -1000       C  
ATOM   5172  CG  GLN B1088      -8.619 -14.402 150.780  1.00154.97           C  
ANISOU 5172  CG  GLN B1088    18136  16332  24411   -502    366  -1103       C  
ATOM   5173  CD  GLN B1088      -9.436 -15.654 150.514  1.00156.14           C  
ANISOU 5173  CD  GLN B1088    18153  16371  24799   -507    320  -1187       C  
ATOM   5174  OE1 GLN B1088     -10.396 -15.637 149.744  1.00156.92           O  
ANISOU 5174  OE1 GLN B1088    18204  16555  24861   -534    324  -1245       O  
ATOM   5175  NE2 GLN B1088      -9.050 -16.754 151.151  1.00156.78           N  
ANISOU 5175  NE2 GLN B1088    18160  16264  25143   -492    275  -1177       N  
ATOM   5176  N   ALA B1089     -10.422 -10.074 151.425  1.00151.22           N  
ANISOU 5176  N   ALA B1089    17994  16075  23387   -517    687   -636       N  
ATOM   5177  CA  ALA B1089     -11.055  -8.786 151.092  1.00150.42           C  
ANISOU 5177  CA  ALA B1089    17909  16039  23205   -513    795   -524       C  
ATOM   5178  C   ALA B1089     -10.079  -7.611 151.233  1.00149.61           C  
ANISOU 5178  C   ALA B1089    17903  15994  22946   -523    879   -513       C  
ATOM   5179  O   ALA B1089     -10.125  -6.675 150.440  1.00149.67           O  
ANISOU 5179  O   ALA B1089    17873  16111  22884   -515    917   -474       O  
ATOM   5180  CB  ALA B1089     -12.295  -8.550 151.947  1.00150.33           C  
ANISOU 5180  CB  ALA B1089    17929  15890  23297   -516    904   -367       C  
ATOM   5181  N   ALA B1090      -9.210  -7.668 152.244  1.00148.77           N  
ANISOU 5181  N   ALA B1090    17909  15824  22791   -553    903   -530       N  
ATOM   5182  CA  ALA B1090      -8.145  -6.674 152.427  1.00148.00           C  
ANISOU 5182  CA  ALA B1090    17908  15788  22537   -580    972   -542       C  
ATOM   5183  C   ALA B1090      -7.068  -6.785 151.341  1.00147.76           C  
ANISOU 5183  C   ALA B1090    17816  15904  22420   -554    863   -670       C  
ATOM   5184  O   ALA B1090      -6.583  -5.765 150.841  1.00148.17           O  
ANISOU 5184  O   ALA B1090    17888  16056  22353   -554    913   -668       O  
ATOM   5185  CB  ALA B1090      -7.521  -6.812 153.809  1.00147.67           C  
ANISOU 5185  CB  ALA B1090    17986  15675  22447   -654   1008   -513       C  
ATOM   5186  N   ALA B1091      -6.704  -8.019 150.984  1.00147.29           N  
ANISOU 5186  N   ALA B1091    17671  15847  22442   -540    730   -787       N  
ATOM   5187  CA  ALA B1091      -5.712  -8.289 149.929  1.00147.59           C  
ANISOU 5187  CA  ALA B1091    17633  16016  22429   -529    645   -949       C  
ATOM   5188  C   ALA B1091      -6.073  -7.655 148.577  1.00148.34           C  
ANISOU 5188  C   ALA B1091    17644  16294  22422   -535    643   -980       C  
ATOM   5189  O   ALA B1091      -5.204  -7.095 147.898  1.00149.50           O  
ANISOU 5189  O   ALA B1091    17784  16585  22433   -546    634  -1044       O  
ATOM   5190  CB  ALA B1091      -5.510  -9.789 149.768  1.00148.68           C  
ANISOU 5190  CB  ALA B1091    17663  16083  22744   -520    541  -1082       C  
ATOM   5191  N   GLU B1092      -7.348  -7.746 148.198  1.00149.73           N  
ANISOU 5191  N   GLU B1092    17747  16481  22661   -541    643   -913       N  
ATOM   5192  CA  GLU B1092      -7.853  -7.088 146.979  1.00151.05           C  
ANISOU 5192  CA  GLU B1092    17810  16846  22733   -574    631   -870       C  
ATOM   5193  C   GLU B1092      -7.744  -5.560 147.038  1.00150.08           C  
ANISOU 5193  C   GLU B1092    17742  16763  22519   -562    732   -703       C  
ATOM   5194  O   GLU B1092      -7.453  -4.921 146.025  1.00150.12           O  
ANISOU 5194  O   GLU B1092    17671  16964  22402   -595    705   -688       O  
ATOM   5195  CB  GLU B1092      -9.310  -7.476 146.707  1.00153.14           C  
ANISOU 5195  CB  GLU B1092    17977  17104  23104   -592    609   -783       C  
ATOM   5196  CG  GLU B1092      -9.507  -8.928 146.300  1.00155.06           C  
ANISOU 5196  CG  GLU B1092    18128  17353  23434   -629    510   -969       C  
ATOM   5197  CD  GLU B1092     -10.967  -9.282 146.081  1.00156.94           C  
ANISOU 5197  CD  GLU B1092    18273  17589  23767   -658    488   -872       C  
ATOM   5198  OE1 GLU B1092     -11.680  -8.504 145.411  1.00158.28           O  
ANISOU 5198  OE1 GLU B1092    18362  17907  23870   -697    490   -713       O  
ATOM   5199  OE2 GLU B1092     -11.402 -10.346 146.573  1.00158.22           O  
ANISOU 5199  OE2 GLU B1092    18427  17603  24085   -645    462   -933       O  
ATOM   5200  N   GLN B1093      -7.987  -4.987 148.217  1.00149.12           N  
ANISOU 5200  N   GLN B1093    17737  16459  22462   -533    857   -583       N  
ATOM   5201  CA  GLN B1093      -7.874  -3.536 148.435  1.00148.20           C  
ANISOU 5201  CA  GLN B1093    17675  16325  22309   -528    996   -449       C  
ATOM   5202  C   GLN B1093      -6.408  -3.077 148.440  1.00146.01           C  
ANISOU 5202  C   GLN B1093    17480  16119  21876   -539    996   -544       C  
ATOM   5203  O   GLN B1093      -6.085  -2.017 147.888  1.00146.73           O  
ANISOU 5203  O   GLN B1093    17546  16305  21897   -543   1041   -476       O  
ATOM   5204  CB  GLN B1093      -8.557  -3.118 149.750  1.00148.00           C  
ANISOU 5204  CB  GLN B1093    17752  16078  22403   -525   1165   -345       C  
ATOM   5205  CG  GLN B1093     -10.054  -3.418 149.831  1.00147.93           C  
ANISOU 5205  CG  GLN B1093    17661  15977  22568   -509   1193   -226       C  
ATOM   5206  CD  GLN B1093     -10.932  -2.380 149.152  1.00148.39           C  
ANISOU 5206  CD  GLN B1093    17591  16059  22729   -493   1273    -27       C  
ATOM   5207  OE1 GLN B1093     -10.520  -1.717 148.199  1.00149.03           O  
ANISOU 5207  OE1 GLN B1093    17591  16296  22738   -499   1235     24       O  
ATOM   5208  NE2 GLN B1093     -12.159  -2.246 149.638  1.00148.41           N  
ANISOU 5208  NE2 GLN B1093    17557  15909  22920   -478   1382    107       N  
ATOM   5209  N   LEU B1094      -5.534  -3.876 149.059  1.00142.68           N  
ANISOU 5209  N   LEU B1094    17139  15651  21421   -546    941   -677       N  
ATOM   5210  CA  LEU B1094      -4.084  -3.611 149.051  1.00140.03           C  
ANISOU 5210  CA  LEU B1094    16865  15390  20947   -560    919   -768       C  
ATOM   5211  C   LEU B1094      -3.492  -3.549 147.636  1.00138.82           C  
ANISOU 5211  C   LEU B1094    16602  15452  20689   -561    825   -859       C  
ATOM   5212  O   LEU B1094      -2.622  -2.715 147.366  1.00139.28           O  
ANISOU 5212  O   LEU B1094    16692  15602  20624   -570    851   -860       O  
ATOM   5213  CB  LEU B1094      -3.329  -4.655 149.890  1.00139.34           C  
ANISOU 5213  CB  LEU B1094    16834  15218  20890   -573    853   -856       C  
ATOM   5214  CG  LEU B1094      -3.512  -4.589 151.408  1.00139.14           C  
ANISOU 5214  CG  LEU B1094    16933  15040  20891   -621    940   -764       C  
ATOM   5215  CD1 LEU B1094      -3.020  -5.870 152.065  1.00139.32           C  
ANISOU 5215  CD1 LEU B1094    16944  14996  20995   -637    831   -797       C  
ATOM   5216  CD2 LEU B1094      -2.798  -3.387 151.986  1.00139.17           C  
ANISOU 5216  CD2 LEU B1094    17063  15062  20752   -679   1060   -726       C  
ATOM   5217  N   LYS B1095      -3.962  -4.426 146.747  1.00137.14           N  
ANISOU 5217  N   LYS B1095    16260  15331  20515   -571    725   -944       N  
ATOM   5218  CA  LYS B1095      -3.578  -4.379 145.324  1.00135.47           C  
ANISOU 5218  CA  LYS B1095    15926  15367  20179   -615    647  -1039       C  
ATOM   5219  C   LYS B1095      -4.069  -3.103 144.619  1.00133.54           C  
ANISOU 5219  C   LYS B1095    15618  15268  19852   -641    684   -850       C  
ATOM   5220  O   LYS B1095      -3.363  -2.556 143.761  1.00132.87           O  
ANISOU 5220  O   LYS B1095    15482  15382  19618   -680    653   -872       O  
ATOM   5221  CB  LYS B1095      -4.078  -5.622 144.580  1.00136.54           C  
ANISOU 5221  CB  LYS B1095    15932  15575  20370   -660    555  -1193       C  
ATOM   5222  CG  LYS B1095      -3.345  -6.894 144.979  1.00137.15           C  
ANISOU 5222  CG  LYS B1095    16019  15529  20561   -641    517  -1402       C  
ATOM   5223  CD  LYS B1095      -3.938  -8.127 144.321  1.00138.60           C  
ANISOU 5223  CD  LYS B1095    16071  15742  20846   -693    459  -1571       C  
ATOM   5224  CE  LYS B1095      -3.264  -9.387 144.837  1.00138.90           C  
ANISOU 5224  CE  LYS B1095    16097  15596  21083   -660    443  -1745       C  
ATOM   5225  NZ  LYS B1095      -3.814 -10.618 144.209  1.00140.39           N  
ANISOU 5225  NZ  LYS B1095    16148  15783  21408   -718    412  -1942       N  
ATOM   5226  N   THR B1096      -5.270  -2.644 144.982  1.00131.33           N  
ANISOU 5226  N   THR B1096    15322  14883  19691   -621    753   -651       N  
ATOM   5227  CA  THR B1096      -5.806  -1.366 144.493  1.00130.02           C  
ANISOU 5227  CA  THR B1096    15075  14793  19533   -632    811   -413       C  
ATOM   5228  C   THR B1096      -4.969  -0.193 145.006  1.00127.74           C  
ANISOU 5228  C   THR B1096    14892  14430  19212   -603    929   -358       C  
ATOM   5229  O   THR B1096      -4.622   0.700 144.231  1.00128.21           O  
ANISOU 5229  O   THR B1096    14874  14643  19195   -628    924   -259       O  
ATOM   5230  CB  THR B1096      -7.282  -1.146 144.910  1.00130.04           C  
ANISOU 5230  CB  THR B1096    15028  14645  19735   -607    889   -206       C  
ATOM   5231  OG1 THR B1096      -8.033  -2.346 144.700  1.00130.53           O  
ANISOU 5231  OG1 THR B1096    15025  14731  19838   -632    790   -280       O  
ATOM   5232  CG2 THR B1096      -7.918  -0.007 144.109  1.00130.47           C  
ANISOU 5232  CG2 THR B1096    14920  14811  19842   -632    915     69       C  
ATOM   5233  N   THR B1097      -4.652  -0.206 146.303  1.00124.59           N  
ANISOU 5233  N   THR B1097    14660  13812  18864   -570   1032   -416       N  
ATOM   5234  CA  THR B1097      -3.772   0.805 146.916  1.00122.40           C  
ANISOU 5234  CA  THR B1097    14504  13464  18537   -570   1153   -407       C  
ATOM   5235  C   THR B1097      -2.382   0.823 146.270  1.00121.79           C  
ANISOU 5235  C   THR B1097    14433  13572  18269   -589   1057   -532       C  
ATOM   5236  O   THR B1097      -1.854   1.899 145.965  1.00121.40           O  
ANISOU 5236  O   THR B1097    14379  13583  18162   -598   1112   -460       O  
ATOM   5237  CB  THR B1097      -3.634   0.571 148.440  1.00120.61           C  
ANISOU 5237  CB  THR B1097    14452  13025  18350   -581   1258   -474       C  
ATOM   5238  OG1 THR B1097      -4.917   0.721 149.060  1.00120.32           O  
ANISOU 5238  OG1 THR B1097    14409  12814  18490   -574   1382   -361       O  
ATOM   5239  CG2 THR B1097      -2.650   1.532 149.086  1.00119.98           C  
ANISOU 5239  CG2 THR B1097    14501  12903  18184   -619   1378   -496       C  
ATOM   5240  N   ARG B1098      -1.811  -0.368 146.070  1.00121.65           N  
ANISOU 5240  N   ARG B1098    14411  13626  18182   -594    927   -715       N  
ATOM   5241  CA  ARG B1098      -0.502  -0.536 145.427  1.00121.20           C  
ANISOU 5241  CA  ARG B1098    14341  13736  17971   -613    840   -862       C  
ATOM   5242  C   ARG B1098      -0.456   0.147 144.060  1.00120.84           C  
ANISOU 5242  C   ARG B1098    14160  13939  17813   -652    794   -801       C  
ATOM   5243  O   ARG B1098       0.397   1.017 143.812  1.00121.16           O  
ANISOU 5243  O   ARG B1098    14220  14065  17747   -662    819   -773       O  
ATOM   5244  CB  ARG B1098      -0.176  -2.030 145.287  1.00122.28           C  
ANISOU 5244  CB  ARG B1098    14441  13884  18135   -615    729  -1066       C  
ATOM   5245  CG  ARG B1098       1.174  -2.335 144.657  1.00123.81           C  
ANISOU 5245  CG  ARG B1098    14604  14221  18217   -634    661  -1243       C  
ATOM   5246  CD  ARG B1098       1.548  -3.803 144.793  1.00124.83           C  
ANISOU 5246  CD  ARG B1098    14694  14274  18461   -625    595  -1437       C  
ATOM   5247  NE  ARG B1098       0.575  -4.686 144.146  1.00126.12           N  
ANISOU 5247  NE  ARG B1098    14736  14476  18705   -653    550  -1520       N  
ATOM   5248  CZ  ARG B1098       0.482  -4.918 142.832  1.00127.33           C  
ANISOU 5248  CZ  ARG B1098    14754  14855  18768   -729    505  -1650       C  
ATOM   5249  NH1 ARG B1098       1.303  -4.326 141.956  1.00127.30           N  
ANISOU 5249  NH1 ARG B1098    14709  15072  18585   -781    494  -1708       N  
ATOM   5250  NH2 ARG B1098      -0.461  -5.749 142.389  1.00129.14           N  
ANISOU 5250  NH2 ARG B1098    14885  15110  19073   -776    471  -1725       N  
ATOM   5251  N   ASN B1099      -1.395  -0.244 143.197  1.00120.63           N  
ANISOU 5251  N   ASN B1099    13988  14042  17804   -691    724   -763       N  
ATOM   5252  CA  ASN B1099      -1.497   0.305 141.840  1.00121.69           C  
ANISOU 5252  CA  ASN B1099    13959  14464  17814   -770    658   -671       C  
ATOM   5253  C   ASN B1099      -1.933   1.772 141.819  1.00121.17           C  
ANISOU 5253  C   ASN B1099    13849  14376  17812   -756    744   -373       C  
ATOM   5254  O   ASN B1099      -1.565   2.507 140.901  1.00120.95           O  
ANISOU 5254  O   ASN B1099    13716  14567  17671   -812    704   -272       O  
ATOM   5255  CB  ASN B1099      -2.460  -0.529 140.987  1.00123.48           C  
ANISOU 5255  CB  ASN B1099    14031  14853  18031   -851    558   -694       C  
ATOM   5256  CG  ASN B1099      -1.973  -1.954 140.774  1.00124.37           C  
ANISOU 5256  CG  ASN B1099    14145  15007  18101   -888    490  -1015       C  
ATOM   5257  OD1 ASN B1099      -1.246  -2.509 141.600  1.00123.33           O  
ANISOU 5257  OD1 ASN B1099    14134  14685  18037   -817    520  -1172       O  
ATOM   5258  ND2 ASN B1099      -2.386  -2.559 139.669  1.00126.34           N  
ANISOU 5258  ND2 ASN B1099    14242  15504  18254  -1015    404  -1107       N  
ATOM   5259  N   ALA B1100      -2.716   2.186 142.816  1.00120.73           N  
ANISOU 5259  N   ALA B1100    13859  14053  17958   -690    872   -234       N  
ATOM   5260  CA  ALA B1100      -3.141   3.587 142.948  1.00121.07           C  
ANISOU 5260  CA  ALA B1100    13855  14000  18144   -667   1003     32       C  
ATOM   5261  C   ALA B1100      -1.981   4.501 143.329  1.00120.21           C  
ANISOU 5261  C   ALA B1100    13858  13838  17977   -651   1096     -2       C  
ATOM   5262  O   ALA B1100      -1.726   5.490 142.638  1.00120.73           O  
ANISOU 5262  O   ALA B1100    13821  14022  18029   -674   1103    157       O  
ATOM   5263  CB  ALA B1100      -4.266   3.728 143.971  1.00121.08           C  
ANISOU 5263  CB  ALA B1100    13897  13708  18397   -614   1152    141       C  
ATOM   5264  N   TYR B1101      -1.286   4.165 144.419  1.00119.43           N  
ANISOU 5264  N   TYR B1101    13957  13577  17844   -626   1159   -192       N  
ATOM   5265  CA  TYR B1101      -0.247   5.041 144.984  1.00119.00           C  
ANISOU 5265  CA  TYR B1101    14026  13447  17738   -629   1267   -228       C  
ATOM   5266  C   TYR B1101       1.194   4.556 144.798  1.00118.13           C  
ANISOU 5266  C   TYR B1101    13991  13485  17405   -648   1156   -428       C  
ATOM   5267  O   TYR B1101       2.053   5.339 144.392  1.00118.85           O  
ANISOU 5267  O   TYR B1101    14076  13678  17401   -665   1163   -406       O  
ATOM   5268  CB  TYR B1101      -0.507   5.258 146.475  1.00119.13           C  
ANISOU 5268  CB  TYR B1101    14205  13179  17877   -626   1453   -261       C  
ATOM   5269  CG  TYR B1101      -1.796   5.984 146.779  1.00120.49           C  
ANISOU 5269  CG  TYR B1101    14310  13160  18311   -610   1626    -76       C  
ATOM   5270  CD1 TYR B1101      -2.991   5.284 146.934  1.00120.54           C  
ANISOU 5270  CD1 TYR B1101    14264  13088  18446   -587   1612    -29       C  
ATOM   5271  CD2 TYR B1101      -1.817   7.367 146.940  1.00121.37           C  
ANISOU 5271  CD2 TYR B1101    14399  13144  18571   -617   1820     49       C  
ATOM   5272  CE1 TYR B1101      -4.182   5.944 147.215  1.00121.58           C  
ANISOU 5272  CE1 TYR B1101    14316  13029  18847   -568   1782    147       C  
ATOM   5273  CE2 TYR B1101      -3.000   8.043 147.225  1.00122.60           C  
ANISOU 5273  CE2 TYR B1101    14466  13087  19027   -598   2007    218       C  
ATOM   5274  CZ  TYR B1101      -4.181   7.327 147.354  1.00122.78           C  
ANISOU 5274  CZ  TYR B1101    14432  13044  19172   -572   1986    272       C  
ATOM   5275  OH  TYR B1101      -5.357   7.974 147.656  1.00123.76           O  
ANISOU 5275  OH  TYR B1101    14457  12945  19620   -550   2182    442       O  
ATOM   5276  N   ILE B1102       1.456   3.280 145.080  1.00117.57           N  
ANISOU 5276  N   ILE B1102    13972  13415  17281   -644   1060   -608       N  
ATOM   5277  CA  ILE B1102       2.830   2.817 145.338  1.00117.59           C  
ANISOU 5277  CA  ILE B1102    14067  13463  17149   -654   1000   -784       C  
ATOM   5278  C   ILE B1102       3.714   2.779 144.081  1.00120.02           C  
ANISOU 5278  C   ILE B1102    14272  14029  17299   -675    886   -864       C  
ATOM   5279  O   ILE B1102       4.920   3.042 144.177  1.00120.69           O  
ANISOU 5279  O   ILE B1102    14419  14160  17277   -684    882   -936       O  
ATOM   5280  CB  ILE B1102       2.853   1.455 146.090  1.00116.25           C  
ANISOU 5280  CB  ILE B1102    13954  13182  17032   -643    942   -919       C  
ATOM   5281  CG1 ILE B1102       2.035   1.528 147.395  1.00116.18           C  
ANISOU 5281  CG1 ILE B1102    14052  12945  17145   -649   1059   -838       C  
ATOM   5282  CG2 ILE B1102       4.287   1.026 146.404  1.00115.38           C  
ANISOU 5282  CG2 ILE B1102    13908  13100  16830   -655    885  -1050       C  
ATOM   5283  CD1 ILE B1102       2.411   2.651 148.345  1.00115.89           C  
ANISOU 5283  CD1 ILE B1102    14151  12803  17077   -696   1217   -779       C  
ATOM   5284  N   GLN B1103       3.127   2.479 142.920  1.00122.56           N  
ANISOU 5284  N   GLN B1103    14434  14538  17594   -704    801   -852       N  
ATOM   5285  CA  GLN B1103       3.865   2.530 141.636  1.00124.24           C  
ANISOU 5285  CA  GLN B1103    14532  15042  17631   -763    707   -926       C  
ATOM   5286  C   GLN B1103       4.588   3.866 141.398  1.00123.72           C  
ANISOU 5286  C   GLN B1103    14475  15057  17476   -774    752   -798       C  
ATOM   5287  O   GLN B1103       5.719   3.884 140.887  1.00124.39           O  
ANISOU 5287  O   GLN B1103    14551  15300  17410   -802    704   -913       O  
ATOM   5288  CB  GLN B1103       2.941   2.254 140.439  1.00127.18           C  
ANISOU 5288  CB  GLN B1103    14718  15641  17963   -840    623   -876       C  
ATOM   5289  CG  GLN B1103       2.624   0.790 140.195  1.00128.69           C  
ANISOU 5289  CG  GLN B1103    14861  15862  18173   -872    553  -1095       C  
ATOM   5290  CD  GLN B1103       2.028   0.533 138.822  1.00131.17           C  
ANISOU 5290  CD  GLN B1103    14982  16490  18365  -1005    462  -1100       C  
ATOM   5291  OE1 GLN B1103       2.569   0.976 137.803  1.00131.87           O  
ANISOU 5291  OE1 GLN B1103    14973  16865  18266  -1102    415  -1102       O  
ATOM   5292  NE2 GLN B1103       0.910  -0.200 138.788  1.00132.33           N  
ANISOU 5292  NE2 GLN B1103    15068  16606  18601  -1031    435  -1101       N  
ATOM   5293  N   LYS B1104       3.933   4.969 141.772  1.00123.61           N  
ANISOU 5293  N   LYS B1104    14467  14917  17579   -752    858   -567       N  
ATOM   5294  CA  LYS B1104       4.493   6.313 141.608  1.00125.17           C  
ANISOU 5294  CA  LYS B1104    14659  15147  17750   -760    926   -423       C  
ATOM   5295  C   LYS B1104       5.821   6.467 142.356  1.00124.86           C  
ANISOU 5295  C   LYS B1104    14787  15027  17624   -746    970   -567       C  
ATOM   5296  O   LYS B1104       6.831   6.855 141.762  1.00125.25           O  
ANISOU 5296  O   LYS B1104    14813  15246  17530   -773    925   -597       O  
ATOM   5297  CB  LYS B1104       3.489   7.374 142.086  1.00126.45           C  
ANISOU 5297  CB  LYS B1104    14797  15106  18140   -733   1076   -174       C  
ATOM   5298  CG  LYS B1104       3.921   8.812 141.817  1.00127.16           C  
ANISOU 5298  CG  LYS B1104    14838  15208  18267   -744   1160      4       C  
ATOM   5299  CD  LYS B1104       2.787   9.803 141.972  1.00128.13           C  
ANISOU 5299  CD  LYS B1104    14855  15149  18678   -723   1305    280       C  
ATOM   5300  CE  LYS B1104       3.284  11.200 141.654  1.00129.15           C  
ANISOU 5300  CE  LYS B1104    14911  15278  18880   -735   1391    460       C  
ATOM   5301  NZ  LYS B1104       2.202  12.210 141.756  1.00130.86           N  
ANISOU 5301  NZ  LYS B1104    14984  15288  19447   -711   1552    750       N  
ATOM   5302  N   TYR B1105       5.811   6.142 143.649  1.00133.10           N  
ANISOU 5302  N   TYR B1105    19341  16652  14579  -1813  -1140   1859       N  
ATOM   5303  CA  TYR B1105       7.008   6.220 144.497  1.00132.96           C  
ANISOU 5303  CA  TYR B1105    19351  16706  14458  -1860  -1106   1849       C  
ATOM   5304  C   TYR B1105       8.137   5.368 143.922  1.00130.27           C  
ANISOU 5304  C   TYR B1105    19176  16281  14037  -1769  -1224   1995       C  
ATOM   5305  O   TYR B1105       9.254   5.853 143.745  1.00129.22           O  
ANISOU 5305  O   TYR B1105    19065  16107  13925  -1679  -1204   1999       O  
ATOM   5306  CB  TYR B1105       6.687   5.784 145.937  1.00135.66           C  
ANISOU 5306  CB  TYR B1105    19659  17228  14658  -2086  -1070   1802       C  
ATOM   5307  CG  TYR B1105       7.791   6.072 146.944  1.00137.63           C  
ANISOU 5307  CG  TYR B1105    19904  17578  14809  -2170  -1020   1774       C  
ATOM   5308  CD1 TYR B1105       7.907   7.330 147.548  1.00137.95           C  
ANISOU 5308  CD1 TYR B1105    19804  17691  14919  -2206   -866   1608       C  
ATOM   5309  CD2 TYR B1105       8.714   5.084 147.305  1.00138.58           C  
ANISOU 5309  CD2 TYR B1105    20151  17718  14782  -2222  -1129   1913       C  
ATOM   5310  CE1 TYR B1105       8.911   7.596 148.472  1.00138.37           C  
ANISOU 5310  CE1 TYR B1105    19854  17847  14872  -2295   -820   1582       C  
ATOM   5311  CE2 TYR B1105       9.723   5.342 148.228  1.00138.59           C  
ANISOU 5311  CE2 TYR B1105    20146  17814  14695  -2310  -1096   1903       C  
ATOM   5312  CZ  TYR B1105       9.817   6.598 148.811  1.00138.63           C  
ANISOU 5312  CZ  TYR B1105    20022  17904  14746  -2350   -939   1738       C  
ATOM   5313  OH  TYR B1105      10.814   6.856 149.726  1.00137.94           O  
ANISOU 5313  OH  TYR B1105    19930  17919  14561  -2448   -905   1728       O  
ATOM   5314  N   LEU B1106       7.820   4.114 143.606  1.00128.19           N  
ANISOU 5314  N   LEU B1106    19018  15985  13700  -1792  -1343   2105       N  
ATOM   5315  CA  LEU B1106       8.774   3.186 142.983  1.00126.82           C  
ANISOU 5315  CA  LEU B1106    18988  15713  13484  -1708  -1457   2228       C  
ATOM   5316  C   LEU B1106       9.372   3.757 141.696  1.00125.30           C  
ANISOU 5316  C   LEU B1106    18825  15392  13392  -1521  -1451   2231       C  
ATOM   5317  O   LEU B1106      10.596   3.841 141.568  1.00126.13           O  
ANISOU 5317  O   LEU B1106    18978  15453  13491  -1450  -1456   2252       O  
ATOM   5318  CB  LEU B1106       8.097   1.848 142.680  1.00127.52           C  
ANISOU 5318  CB  LEU B1106    19160  15769  13520  -1753  -1575   2323       C  
ATOM   5319  CG  LEU B1106       8.939   0.734 142.059  1.00127.30           C  
ANISOU 5319  CG  LEU B1106    19265  15628  13473  -1684  -1696   2433       C  
ATOM   5320  CD1 LEU B1106       9.884   0.153 143.090  1.00127.46           C  
ANISOU 5320  CD1 LEU B1106    19316  15691  13420  -1777  -1748   2497       C  
ATOM   5321  CD2 LEU B1106       8.057  -0.361 141.457  1.00127.45           C  
ANISOU 5321  CD2 LEU B1106    19347  15594  13482  -1699  -1794   2498       C  
ATOM   5322  N   GLU B 220       8.506   4.146 140.759  1.00123.43           N  
ANISOU 5322  N   GLU B 220    18555  15099  13243  -1456  -1446   2215       N  
ATOM   5323  CA  GLU B 220       8.950   4.667 139.453  1.00121.79           C  
ANISOU 5323  CA  GLU B 220    18375  14783  13115  -1307  -1454   2233       C  
ATOM   5324  C   GLU B 220       9.758   5.972 139.569  1.00119.90           C  
ANISOU 5324  C   GLU B 220    18061  14545  12950  -1239  -1361   2167       C  
ATOM   5325  O   GLU B 220      10.805   6.135 138.910  1.00119.07           O  
ANISOU 5325  O   GLU B 220    18016  14376  12850  -1140  -1372   2193       O  
ATOM   5326  CB  GLU B 220       7.751   4.859 138.512  1.00123.15           C  
ANISOU 5326  CB  GLU B 220    18512  14910  13368  -1283  -1481   2246       C  
ATOM   5327  CG  GLU B 220       7.136   3.550 138.018  1.00123.85           C  
ANISOU 5327  CG  GLU B 220    18700  14971  13386  -1317  -1584   2323       C  
ATOM   5328  CD  GLU B 220       5.807   3.737 137.298  1.00124.46           C  
ANISOU 5328  CD  GLU B 220    18728  15023  13537  -1323  -1610   2337       C  
ATOM   5329  OE1 GLU B 220       5.573   4.836 136.748  1.00124.99           O  
ANISOU 5329  OE1 GLU B 220    18708  15056  13724  -1267  -1577   2317       O  
ATOM   5330  OE2 GLU B 220       4.995   2.781 137.272  1.00124.26           O  
ANISOU 5330  OE2 GLU B 220    18746  15006  13460  -1386  -1674   2377       O  
ATOM   5331  N   ARG B 221       9.286   6.889 140.416  1.00118.83           N  
ANISOU 5331  N   ARG B 221    17790  14482  12877  -1300  -1265   2070       N  
ATOM   5332  CA  ARG B 221       9.986   8.166 140.639  1.00117.53           C  
ANISOU 5332  CA  ARG B 221    17537  14320  12797  -1247  -1169   1993       C  
ATOM   5333  C   ARG B 221      11.327   7.962 141.356  1.00114.36           C  
ANISOU 5333  C   ARG B 221    17196  13961  12293  -1260  -1154   1999       C  
ATOM   5334  O   ARG B 221      12.332   8.588 140.991  1.00114.48           O  
ANISOU 5334  O   ARG B 221    17221  13930  12345  -1163  -1128   1996       O  
ATOM   5335  CB  ARG B 221       9.105   9.169 141.405  1.00119.57           C  
ANISOU 5335  CB  ARG B 221    17618  14642  13171  -1319  -1060   1863       C  
ATOM   5336  CG  ARG B 221       7.850   9.641 140.659  1.00121.28           C  
ANISOU 5336  CG  ARG B 221    17738  14791  13549  -1290  -1072   1852       C  
ATOM   5337  CD  ARG B 221       8.100  10.371 139.340  1.00121.53           C  
ANISOU 5337  CD  ARG B 221    17765  14699  13709  -1151  -1113   1914       C  
ATOM   5338  NE  ARG B 221       8.251  11.819 139.487  1.00122.48           N  
ANISOU 5338  NE  ARG B 221    17731  14791  14013  -1108  -1025   1825       N  
ATOM   5339  CZ  ARG B 221       8.329  12.683 138.471  1.00122.90           C  
ANISOU 5339  CZ  ARG B 221    17735  14740  14217  -1010  -1057   1873       C  
ATOM   5340  NH1 ARG B 221       8.273  12.271 137.202  1.00122.93           N  
ANISOU 5340  NH1 ARG B 221    17839  14675  14193   -955  -1171   2007       N  
ATOM   5341  NH2 ARG B 221       8.465  13.984 138.723  1.00123.33           N  
ANISOU 5341  NH2 ARG B 221    17637  14765  14458   -979   -978   1787       N  
ATOM   5342  N   ALA B 222      11.350   7.081 142.355  1.00111.30           N  
ANISOU 5342  N   ALA B 222    16847  13661  11780  -1386  -1179   2018       N  
ATOM   5343  CA  ALA B 222      12.603   6.691 143.019  1.00109.10           C  
ANISOU 5343  CA  ALA B 222    16633  13414  11405  -1415  -1199   2057       C  
ATOM   5344  C   ALA B 222      13.578   6.052 142.029  1.00106.95           C  
ANISOU 5344  C   ALA B 222    16487  13019  11131  -1289  -1287   2151       C  
ATOM   5345  O   ALA B 222      14.750   6.433 141.981  1.00106.65           O  
ANISOU 5345  O   ALA B 222    16467  12951  11103  -1220  -1266   2150       O  
ATOM   5346  CB  ALA B 222      12.332   5.755 144.182  1.00109.53           C  
ANISOU 5346  CB  ALA B 222    16706  13579  11330  -1594  -1241   2093       C  
ATOM   5347  N   ARG B 223      13.080   5.097 141.240  1.00105.66           N  
ANISOU 5347  N   ARG B 223    16401  12787  10958  -1265  -1378   2219       N  
ATOM   5348  CA  ARG B 223      13.845   4.503 140.131  1.00104.45           C  
ANISOU 5348  CA  ARG B 223    16353  12514  10818  -1152  -1448   2278       C  
ATOM   5349  C   ARG B 223      14.448   5.595 139.242  1.00101.86           C  
ANISOU 5349  C   ARG B 223    16004  12133  10565  -1023  -1386   2236       C  
ATOM   5350  O   ARG B 223      15.674   5.640 139.043  1.00101.52           O  
ANISOU 5350  O   ARG B 223    16003  12045  10524   -955  -1383   2241       O  
ATOM   5351  CB  ARG B 223      12.973   3.585 139.263  1.00105.97           C  
ANISOU 5351  CB  ARG B 223    16606  12650  11006  -1149  -1528   2325       C  
ATOM   5352  CG  ARG B 223      12.806   2.157 139.757  1.00107.67           C  
ANISOU 5352  CG  ARG B 223    16886  12863  11158  -1239  -1628   2396       C  
ATOM   5353  CD  ARG B 223      11.869   1.383 138.836  1.00108.99           C  
ANISOU 5353  CD  ARG B 223    17106  12976  11329  -1232  -1695   2428       C  
ATOM   5354  NE  ARG B 223      11.409   0.113 139.404  1.00110.79           N  
ANISOU 5354  NE  ARG B 223    17374  13214  11507  -1336  -1788   2494       N  
ATOM   5355  CZ  ARG B 223      10.524  -0.708 138.830  1.00112.03           C  
ANISOU 5355  CZ  ARG B 223    17574  13335  11657  -1356  -1854   2527       C  
ATOM   5356  NH1 ARG B 223       9.973  -0.410 137.649  1.00111.82           N  
ANISOU 5356  NH1 ARG B 223    17557  13266  11660  -1287  -1839   2502       N  
ATOM   5357  NH2 ARG B 223      10.189  -1.852 139.432  1.00112.99           N  
ANISOU 5357  NH2 ARG B 223    17726  13463  11739  -1457  -1944   2594       N  
ATOM   5358  N   SER B 224      13.584   6.476 138.728  1.00 99.52           N  
ANISOU 5358  N   SER B 224    15634  11838  10341   -998  -1344   2201       N  
ATOM   5359  CA  SER B 224      14.038   7.528 137.807  1.00 97.54           C  
ANISOU 5359  CA  SER B 224    15357  11535  10168   -892  -1305   2183       C  
ATOM   5360  C   SER B 224      15.068   8.472 138.452  1.00 95.37           C  
ANISOU 5360  C   SER B 224    15028  11288   9919   -861  -1223   2129       C  
ATOM   5361  O   SER B 224      16.129   8.734 137.865  1.00 94.75           O  
ANISOU 5361  O   SER B 224    14992  11160   9846   -775  -1218   2138       O  
ATOM   5362  CB  SER B 224      12.859   8.322 137.231  1.00 98.00           C  
ANISOU 5362  CB  SER B 224    15324  11581  10327   -887  -1294   2173       C  
ATOM   5363  OG  SER B 224      12.297   9.199 138.187  1.00 98.77           O  
ANISOU 5363  OG  SER B 224    15285  11738  10504   -938  -1213   2095       O  
ATOM   5364  N   THR B 225      14.770   8.953 139.660  1.00 93.41           N  
ANISOU 5364  N   THR B 225    14685  11124   9680   -941  -1155   2065       N  
ATOM   5365  CA  THR B 225      15.682   9.874 140.363  1.00 91.76           C  
ANISOU 5365  CA  THR B 225    14416  10953   9492   -929  -1069   2003       C  
ATOM   5366  C   THR B 225      17.007   9.219 140.784  1.00 90.18           C  
ANISOU 5366  C   THR B 225    14307  10756   9200   -927  -1099   2044       C  
ATOM   5367  O   THR B 225      18.050   9.868 140.717  1.00 89.08           O  
ANISOU 5367  O   THR B 225    14163  10598   9086   -858  -1058   2025       O  
ATOM   5368  CB  THR B 225      15.015  10.544 141.583  1.00 92.01           C  
ANISOU 5368  CB  THR B 225    14314  11090   9553  -1040   -976   1901       C  
ATOM   5369  OG1 THR B 225      14.455   9.546 142.435  1.00 93.24           O  
ANISOU 5369  OG1 THR B 225    14497  11329   9601  -1177  -1010   1918       O  
ATOM   5370  CG2 THR B 225      13.920  11.510 141.135  1.00 92.17           C  
ANISOU 5370  CG2 THR B 225    14209  11080   9731  -1015   -930   1840       C  
ATOM   5371  N   LEU B 226      16.970   7.950 141.198  1.00 89.53           N  
ANISOU 5371  N   LEU B 226    14300  10688   9029  -1002  -1179   2107       N  
ATOM   5372  CA  LEU B 226      18.205   7.177 141.461  1.00 89.18           C  
ANISOU 5372  CA  LEU B 226    14337  10613   8933   -995  -1237   2167       C  
ATOM   5373  C   LEU B 226      19.016   6.938 140.176  1.00 89.27           C  
ANISOU 5373  C   LEU B 226    14428  10503   8987   -858  -1272   2192       C  
ATOM   5374  O   LEU B 226      20.238   7.135 140.160  1.00 89.09           O  
ANISOU 5374  O   LEU B 226    14424  10446   8978   -799  -1258   2190       O  
ATOM   5375  CB  LEU B 226      17.909   5.832 142.139  1.00 89.50           C  
ANISOU 5375  CB  LEU B 226    14428  10678   8898  -1114  -1335   2244       C  
ATOM   5376  CG  LEU B 226      17.583   5.878 143.640  1.00 90.10           C  
ANISOU 5376  CG  LEU B 226    14443  10897   8893  -1287  -1313   2236       C  
ATOM   5377  CD1 LEU B 226      16.908   4.594 144.120  1.00 90.60           C  
ANISOU 5377  CD1 LEU B 226    14548  10989   8885  -1416  -1418   2320       C  
ATOM   5378  CD2 LEU B 226      18.827   6.158 144.475  1.00 90.06           C  
ANISOU 5378  CD2 LEU B 226    14429  10932   8857  -1319  -1297   2247       C  
ATOM   5379  N   GLN B 227      18.336   6.516 139.110  1.00 89.75           N  
ANISOU 5379  N   GLN B 227    14530  10505   9063   -821  -1314   2210       N  
ATOM   5380  CA  GLN B 227      19.000   6.313 137.813  1.00 89.86           C  
ANISOU 5380  CA  GLN B 227    14614  10424   9102   -717  -1335   2214       C  
ATOM   5381  C   GLN B 227      19.554   7.616 137.205  1.00 89.68           C  
ANISOU 5381  C   GLN B 227    14552  10396   9126   -629  -1259   2171       C  
ATOM   5382  O   GLN B 227      20.560   7.591 136.476  1.00 90.13           O  
ANISOU 5382  O   GLN B 227    14656  10396   9191   -556  -1256   2162       O  
ATOM   5383  CB  GLN B 227      18.074   5.598 136.829  1.00 90.51           C  
ANISOU 5383  CB  GLN B 227    14746  10466   9175   -723  -1394   2238       C  
ATOM   5384  CG  GLN B 227      17.884   4.125 137.167  1.00 91.49           C  
ANISOU 5384  CG  GLN B 227    14930  10562   9270   -785  -1483   2284       C  
ATOM   5385  CD  GLN B 227      16.781   3.456 136.369  1.00 92.52           C  
ANISOU 5385  CD  GLN B 227    15098  10669   9385   -810  -1536   2304       C  
ATOM   5386  OE1 GLN B 227      16.379   3.937 135.308  1.00 93.17           O  
ANISOU 5386  OE1 GLN B 227    15184  10741   9475   -772  -1518   2288       O  
ATOM   5387  NE2 GLN B 227      16.287   2.331 136.879  1.00 93.18           N  
ANISOU 5387  NE2 GLN B 227    15210  10746   9446   -885  -1611   2348       N  
ATOM   5388  N   LYS B 228      18.910   8.743 137.510  1.00 89.83           N  
ANISOU 5388  N   LYS B 228    14475  10468   9187   -642  -1199   2140       N  
ATOM   5389  CA  LYS B 228      19.463  10.061 137.152  1.00 90.20           C  
ANISOU 5389  CA  LYS B 228    14466  10509   9297   -569  -1131   2105       C  
ATOM   5390  C   LYS B 228      20.752  10.384 137.931  1.00 89.05           C  
ANISOU 5390  C   LYS B 228    14312  10379   9140   -547  -1082   2077       C  
ATOM   5391  O   LYS B 228      21.717  10.915 137.358  1.00 88.87           O  
ANISOU 5391  O   LYS B 228    14304  10321   9139   -468  -1055   2067       O  
ATOM   5392  CB  LYS B 228      18.411  11.164 137.321  1.00 92.05           C  
ANISOU 5392  CB  LYS B 228    14578  10775   9621   -591  -1084   2073       C  
ATOM   5393  CG  LYS B 228      17.406  11.178 136.172  1.00 93.54           C  
ANISOU 5393  CG  LYS B 228    14766  10923   9849   -584  -1138   2119       C  
ATOM   5394  CD  LYS B 228      16.117  11.915 136.490  1.00 94.68           C  
ANISOU 5394  CD  LYS B 228    14783  11087  10103   -627  -1115   2093       C  
ATOM   5395  CE  LYS B 228      15.130  11.754 135.341  1.00 95.41           C  
ANISOU 5395  CE  LYS B 228    14886  11135  10228   -631  -1192   2161       C  
ATOM   5396  NZ  LYS B 228      13.928  12.623 135.472  1.00 96.39           N  
ANISOU 5396  NZ  LYS B 228    14864  11251  10506   -659  -1178   2143       N  
ATOM   5397  N   GLU B 229      20.764  10.056 139.226  1.00 88.21           N  
ANISOU 5397  N   GLU B 229    14184  10336   8995   -631  -1075   2069       N  
ATOM   5398  CA  GLU B 229      22.002  10.118 140.036  1.00 87.17           C  
ANISOU 5398  CA  GLU B 229    14058  10225   8838   -634  -1052   2063       C  
ATOM   5399  C   GLU B 229      23.100   9.213 139.471  1.00 86.06           C  
ANISOU 5399  C   GLU B 229    14014   9997   8686   -572  -1115   2107       C  
ATOM   5400  O   GLU B 229      24.269   9.607 139.417  1.00 86.14           O  
ANISOU 5400  O   GLU B 229    14030   9981   8716   -510  -1085   2092       O  
ATOM   5401  CB  GLU B 229      21.740   9.757 141.512  1.00 87.43           C  
ANISOU 5401  CB  GLU B 229    14056  10354   8806   -772  -1055   2067       C  
ATOM   5402  CG  GLU B 229      21.274  10.911 142.385  1.00 87.77           C  
ANISOU 5402  CG  GLU B 229    13982  10499   8867   -837   -952   1981       C  
ATOM   5403  CD  GLU B 229      22.331  11.974 142.600  1.00 87.57           C  
ANISOU 5403  CD  GLU B 229    13912  10482   8877   -782   -873   1931       C  
ATOM   5404  OE1 GLU B 229      23.515  11.620 142.817  1.00 87.47           O  
ANISOU 5404  OE1 GLU B 229    13955  10450   8829   -763   -903   1974       O  
ATOM   5405  OE2 GLU B 229      21.968  13.173 142.556  1.00 87.55           O  
ANISOU 5405  OE2 GLU B 229    13810  10496   8956   -758   -785   1849       O  
ATOM   5406  N   LEU B 230      22.715   8.009 139.043  1.00 84.87           N  
ANISOU 5406  N   LEU B 230    13932   9797   8518   -591  -1198   2150       N  
ATOM   5407  CA  LEU B 230      23.645   7.093 138.371  1.00 83.74           C  
ANISOU 5407  CA  LEU B 230    13866   9554   8398   -533  -1252   2168       C  
ATOM   5408  C   LEU B 230      24.175   7.663 137.053  1.00 82.66           C  
ANISOU 5408  C   LEU B 230    13749   9367   8288   -430  -1206   2121       C  
ATOM   5409  O   LEU B 230      25.381   7.573 136.785  1.00 82.22           O  
ANISOU 5409  O   LEU B 230    13718   9258   8263   -371  -1195   2099       O  
ATOM   5410  CB  LEU B 230      22.985   5.732 138.124  1.00 83.93           C  
ANISOU 5410  CB  LEU B 230    13943   9530   8414   -580  -1344   2209       C  
ATOM   5411  CG  LEU B 230      23.883   4.596 137.627  1.00 84.08           C  
ANISOU 5411  CG  LEU B 230    14022   9433   8489   -541  -1406   2214       C  
ATOM   5412  CD1 LEU B 230      24.744   4.113 138.770  1.00 84.16           C  
ANISOU 5412  CD1 LEU B 230    14017   9426   8533   -583  -1459   2268       C  
ATOM   5413  CD2 LEU B 230      23.070   3.453 137.043  1.00 84.64           C  
ANISOU 5413  CD2 LEU B 230    14141   9454   8564   -572  -1477   2229       C  
ATOM   5414  N   LYS B 231      23.278   8.242 136.247  1.00 82.24           N  
ANISOU 5414  N   LYS B 231    13683   9336   8228   -421  -1184   2110       N  
ATOM   5415  CA  LYS B 231      23.648   8.776 134.923  1.00 81.58           C  
ANISOU 5415  CA  LYS B 231    13621   9224   8151   -356  -1155   2084       C  
ATOM   5416  C   LYS B 231      24.717   9.880 134.992  1.00 80.94           C  
ANISOU 5416  C   LYS B 231    13502   9153   8097   -293  -1086   2054       C  
ATOM   5417  O   LYS B 231      25.658   9.888 134.191  1.00 80.89           O  
ANISOU 5417  O   LYS B 231    13534   9111   8090   -242  -1068   2024       O  
ATOM   5418  CB  LYS B 231      22.418   9.297 134.174  1.00 81.40           C  
ANISOU 5418  CB  LYS B 231    13574   9230   8125   -379  -1164   2106       C  
ATOM   5419  CG  LYS B 231      22.662   9.566 132.690  1.00 81.68           C  
ANISOU 5419  CG  LYS B 231    13646   9246   8139   -352  -1164   2101       C  
ATOM   5420  CD  LYS B 231      21.578  10.431 132.068  1.00 81.99           C  
ANISOU 5420  CD  LYS B 231    13635   9315   8200   -378  -1179   2148       C  
ATOM   5421  CE  LYS B 231      21.992  10.921 130.688  1.00 82.40           C  
ANISOU 5421  CE  LYS B 231    13715   9370   8222   -372  -1180   2160       C  
ATOM   5422  NZ  LYS B 231      21.096  12.005 130.200  1.00 82.84           N  
ANISOU 5422  NZ  LYS B 231    13697   9446   8332   -397  -1207   2229       N  
ATOM   5423  N   ILE B 232      24.567  10.804 135.940  1.00 80.40           N  
ANISOU 5423  N   ILE B 232    13355   9138   8054   -304  -1041   2050       N  
ATOM   5424  CA  ILE B 232      25.524  11.913 136.088  1.00 79.91           C  
ANISOU 5424  CA  ILE B 232    13249   9087   8025   -248   -973   2021       C  
ATOM   5425  C   ILE B 232      26.876  11.389 136.597  1.00 78.31           C  
ANISOU 5425  C   ILE B 232    13084   8856   7815   -223   -971   2009       C  
ATOM   5426  O   ILE B 232      27.943  11.713 136.035  1.00 77.60           O  
ANISOU 5426  O   ILE B 232    13012   8733   7738   -157   -941   1984       O  
ATOM   5427  CB  ILE B 232      24.986  13.027 137.024  1.00 81.04           C  
ANISOU 5427  CB  ILE B 232    13285   9292   8213   -277   -916   2000       C  
ATOM   5428  CG1 ILE B 232      23.699  13.641 136.447  1.00 82.69           C  
ANISOU 5428  CG1 ILE B 232    13435   9507   8475   -292   -922   2011       C  
ATOM   5429  CG2 ILE B 232      26.031  14.129 137.211  1.00 80.41           C  
ANISOU 5429  CG2 ILE B 232    13160   9220   8172   -220   -847   1966       C  
ATOM   5430  CD1 ILE B 232      22.937  14.527 137.409  1.00 83.47           C  
ANISOU 5430  CD1 ILE B 232    13410   9655   8646   -337   -867   1967       C  
ATOM   5431  N   ALA B 233      26.814  10.569 137.648  1.00 77.17           N  
ANISOU 5431  N   ALA B 233    12945   8721   7652   -285  -1013   2035       N  
ATOM   5432  CA  ALA B 233      28.005   9.940 138.246  1.00 75.88           C  
ANISOU 5432  CA  ALA B 233    12806   8520   7503   -280  -1040   2049       C  
ATOM   5433  C   ALA B 233      28.965   9.352 137.208  1.00 74.44           C  
ANISOU 5433  C   ALA B 233    12682   8241   7360   -205  -1054   2023       C  
ATOM   5434  O   ALA B 233      30.174   9.568 137.293  1.00 74.09           O  
ANISOU 5434  O   ALA B 233    12633   8166   7352   -155  -1029   2003       O  
ATOM   5435  CB  ALA B 233      27.591   8.868 139.244  1.00 76.47           C  
ANISOU 5435  CB  ALA B 233    12891   8606   7558   -379  -1120   2109       C  
ATOM   5436  N   LYS B 234      28.421   8.632 136.228  1.00 73.03           N  
ANISOU 5436  N   LYS B 234    12551   8020   7176   -205  -1088   2012       N  
ATOM   5437  CA  LYS B 234      29.225   8.082 135.130  1.00 72.11           C  
ANISOU 5437  CA  LYS B 234    12481   7824   7094   -152  -1084   1955       C  
ATOM   5438  C   LYS B 234      29.911   9.185 134.313  1.00 71.08           C  
ANISOU 5438  C   LYS B 234    12342   7716   6949    -91  -1003   1904       C  
ATOM   5439  O   LYS B 234      31.110   9.082 134.001  1.00 71.66           O  
ANISOU 5439  O   LYS B 234    12423   7739   7063    -42   -975   1853       O  
ATOM   5440  CB  LYS B 234      28.368   7.209 134.211  1.00 72.63           C  
ANISOU 5440  CB  LYS B 234    12594   7862   7139   -185  -1125   1942       C  
ATOM   5441  CG  LYS B 234      27.894   5.908 134.843  1.00 73.05           C  
ANISOU 5441  CG  LYS B 234    12662   7866   7225   -239  -1214   1985       C  
ATOM   5442  CD  LYS B 234      27.008   5.118 133.894  1.00 73.44           C  
ANISOU 5442  CD  LYS B 234    12757   7894   7252   -272  -1246   1964       C  
ATOM   5443  CE  LYS B 234      26.570   3.797 134.506  1.00 74.18           C  
ANISOU 5443  CE  LYS B 234    12863   7929   7393   -325  -1342   2010       C  
ATOM   5444  NZ  LYS B 234      25.695   3.006 133.599  1.00 74.70           N  
ANISOU 5444  NZ  LYS B 234    12972   7972   7438   -359  -1372   1985       N  
ATOM   5445  N   SER B 235      29.153  10.238 133.984  1.00 69.71           N  
ANISOU 5445  N   SER B 235    12142   7612   6730    -99   -972   1923       N  
ATOM   5446  CA  SER B 235      29.693  11.389 133.244  1.00 68.34           C  
ANISOU 5446  CA  SER B 235    11951   7466   6546    -56   -910   1898       C  
ATOM   5447  C   SER B 235      30.835  12.050 134.007  1.00 67.58           C  
ANISOU 5447  C   SER B 235    11818   7370   6488     -5   -862   1884       C  
ATOM   5448  O   SER B 235      31.927  12.301 133.456  1.00 67.04           O  
ANISOU 5448  O   SER B 235    11761   7281   6428     41   -821   1839       O  
ATOM   5449  CB  SER B 235      28.597  12.423 132.967  1.00 67.87           C  
ANISOU 5449  CB  SER B 235    11847   7465   6472    -80   -907   1943       C  
ATOM   5450  OG  SER B 235      27.439  11.818 132.416  1.00 68.30           O  
ANISOU 5450  OG  SER B 235    11931   7524   6496   -135   -960   1970       O  
ATOM   5451  N   LEU B 236      30.580  12.311 135.289  1.00 67.10           N  
ANISOU 5451  N   LEU B 236    11710   7341   6444    -27   -864   1916       N  
ATOM   5452  CA  LEU B 236      31.589  12.921 136.154  1.00 66.42           C  
ANISOU 5452  CA  LEU B 236    11584   7266   6384      2   -823   1907       C  
ATOM   5453  C   LEU B 236      32.807  12.013 136.368  1.00 66.55           C  
ANISOU 5453  C   LEU B 236    11634   7212   6438     27   -848   1894       C  
ATOM   5454  O   LEU B 236      33.933  12.502 136.474  1.00 66.86           O  
ANISOU 5454  O   LEU B 236    11658   7240   6506     76   -807   1871       O  
ATOM   5455  CB  LEU B 236      30.969  13.334 137.485  1.00 66.30           C  
ANISOU 5455  CB  LEU B 236    11508   7318   6364    -56   -816   1932       C  
ATOM   5456  CG  LEU B 236      29.910  14.441 137.409  1.00 66.12           C  
ANISOU 5456  CG  LEU B 236    11418   7352   6353    -72   -775   1924       C  
ATOM   5457  CD1 LEU B 236      29.177  14.574 138.732  1.00 66.24           C  
ANISOU 5457  CD1 LEU B 236    11371   7436   6361   -156   -763   1922       C  
ATOM   5458  CD2 LEU B 236      30.525  15.773 136.997  1.00 65.62           C  
ANISOU 5458  CD2 LEU B 236    11309   7293   6329     -8   -710   1898       C  
ATOM   5459  N   ALA B 237      32.581  10.700 136.419  1.00 66.77           N  
ANISOU 5459  N   ALA B 237    11698   7184   6485     -6   -919   1911       N  
ATOM   5460  CA  ALA B 237      33.673   9.720 136.484  1.00 67.05           C  
ANISOU 5460  CA  ALA B 237    11750   7122   6601     17   -957   1896       C  
ATOM   5461  C   ALA B 237      34.517   9.749 135.211  1.00 67.05           C  
ANISOU 5461  C   ALA B 237    11774   7072   6631     83   -904   1806       C  
ATOM   5462  O   ALA B 237      35.751   9.843 135.284  1.00 67.05           O  
ANISOU 5462  O   ALA B 237    11756   7025   6693    132   -878   1772       O  
ATOM   5463  CB  ALA B 237      33.126   8.320 136.721  1.00 67.63           C  
ANISOU 5463  CB  ALA B 237    11847   7137   6712    -37  -1052   1934       C  
ATOM   5464  N   LEU B 238      33.846   9.693 134.054  1.00 67.27           N  
ANISOU 5464  N   LEU B 238    11836   7117   6606     72   -887   1766       N  
ATOM   5465  CA  LEU B 238      34.524   9.801 132.745  1.00 67.34           C  
ANISOU 5465  CA  LEU B 238    11867   7110   6608    101   -826   1671       C  
ATOM   5466  C   LEU B 238      35.471  11.006 132.665  1.00 66.49           C  
ANISOU 5466  C   LEU B 238    11733   7041   6488    152   -753   1652       C  
ATOM   5467  O   LEU B 238      36.583  10.905 132.128  1.00 66.49           O  
ANISOU 5467  O   LEU B 238    11733   7001   6526    187   -708   1571       O  
ATOM   5468  CB  LEU B 238      33.503   9.881 131.605  1.00 67.68           C  
ANISOU 5468  CB  LEU B 238    11946   7207   6558     52   -821   1660       C  
ATOM   5469  CG  LEU B 238      34.064  10.061 130.185  1.00 68.55           C  
ANISOU 5469  CG  LEU B 238    12082   7338   6622     42   -759   1566       C  
ATOM   5470  CD1 LEU B 238      35.026   8.935 129.828  1.00 69.50           C  
ANISOU 5470  CD1 LEU B 238    12210   7365   6830     55   -739   1447       C  
ATOM   5471  CD2 LEU B 238      32.939  10.141 129.168  1.00 69.09           C  
ANISOU 5471  CD2 LEU B 238    12186   7475   6588    -32   -775   1584       C  
ATOM   5472  N   ILE B 239      35.018  12.138 133.197  1.00 65.53           N  
ANISOU 5472  N   ILE B 239    11580   6993   6324    153   -739   1716       N  
ATOM   5473  CA  ILE B 239      35.862  13.328 133.295  1.00 64.86           C  
ANISOU 5473  CA  ILE B 239    11461   6941   6239    200   -677   1709       C  
ATOM   5474  C   ILE B 239      37.132  13.051 134.125  1.00 64.16           C  
ANISOU 5474  C   ILE B 239    11352   6796   6228    244   -672   1692       C  
ATOM   5475  O   ILE B 239      38.241  13.441 133.722  1.00 64.07           O  
ANISOU 5475  O   ILE B 239    11334   6770   6239    290   -619   1639       O  
ATOM   5476  CB  ILE B 239      35.055  14.530 133.838  1.00 64.84           C  
ANISOU 5476  CB  ILE B 239    11411   7013   6212    188   -667   1772       C  
ATOM   5477  CG1 ILE B 239      34.064  14.997 132.768  1.00 65.26           C  
ANISOU 5477  CG1 ILE B 239    11472   7109   6214    154   -674   1793       C  
ATOM   5478  CG2 ILE B 239      35.964  15.688 134.249  1.00 64.62           C  
ANISOU 5478  CG2 ILE B 239    11336   7008   6206    237   -608   1766       C  
ATOM   5479  CD1 ILE B 239      32.870  15.747 133.299  1.00 65.25           C  
ANISOU 5479  CD1 ILE B 239    11413   7150   6226    126   -690   1852       C  
ATOM   5480  N   LEU B 240      36.970  12.365 135.258  1.00 63.68           N  
ANISOU 5480  N   LEU B 240    11279   6706   6210    217   -733   1744       N  
ATOM   5481  CA  LEU B 240      38.116  11.987 136.090  1.00 63.44           C  
ANISOU 5481  CA  LEU B 240    11223   6614   6264    239   -754   1753       C  
ATOM   5482  C   LEU B 240      39.064  11.044 135.346  1.00 63.67           C  
ANISOU 5482  C   LEU B 240    11265   6533   6393    277   -758   1675       C  
ATOM   5483  O   LEU B 240      40.289  11.247 135.346  1.00 63.43           O  
ANISOU 5483  O   LEU B 240    11210   6461   6428    327   -724   1635       O  
ATOM   5484  CB  LEU B 240      37.643  11.338 137.401  1.00 63.48           C  
ANISOU 5484  CB  LEU B 240    11213   6618   6285    171   -840   1844       C  
ATOM   5485  CG  LEU B 240      38.711  10.917 138.411  1.00 63.74           C  
ANISOU 5485  CG  LEU B 240    11215   6595   6405    164   -893   1891       C  
ATOM   5486  CD1 LEU B 240      39.533  12.111 138.862  1.00 63.24           C  
ANISOU 5486  CD1 LEU B 240    11119   6589   6321    197   -826   1887       C  
ATOM   5487  CD2 LEU B 240      38.031  10.243 139.577  1.00 64.01           C  
ANISOU 5487  CD2 LEU B 240    11240   6651   6426     63   -990   1994       C  
ATOM   5488  N   PHE B 241      38.488  10.025 134.709  1.00 64.17           N  
ANISOU 5488  N   PHE B 241    11357   6547   6475    250   -793   1642       N  
ATOM   5489  CA  PHE B 241      39.263   9.096 133.886  1.00 65.26           C  
ANISOU 5489  CA  PHE B 241    11495   6579   6721    275   -781   1534       C  
ATOM   5490  C   PHE B 241      40.057   9.840 132.816  1.00 65.08           C  
ANISOU 5490  C   PHE B 241    11475   6589   6661    312   -675   1426       C  
ATOM   5491  O   PHE B 241      41.261   9.609 132.664  1.00 65.42           O  
ANISOU 5491  O   PHE B 241    11486   6558   6812    354   -643   1348       O  
ATOM   5492  CB  PHE B 241      38.356   8.050 133.230  1.00 66.08           C  
ANISOU 5492  CB  PHE B 241    11631   6649   6826    228   -818   1499       C  
ATOM   5493  CG  PHE B 241      39.091   7.085 132.344  1.00 67.20           C  
ANISOU 5493  CG  PHE B 241    11759   6682   7090    242   -792   1359       C  
ATOM   5494  CD1 PHE B 241      39.845   6.056 132.896  1.00 68.13           C  
ANISOU 5494  CD1 PHE B 241    11826   6651   7410    263   -855   1349       C  
ATOM   5495  CD2 PHE B 241      39.041   7.210 130.962  1.00 67.81           C  
ANISOU 5495  CD2 PHE B 241    11865   6805   7092    220   -706   1234       C  
ATOM   5496  CE1 PHE B 241      40.530   5.164 132.085  1.00 69.60           C  
ANISOU 5496  CE1 PHE B 241    11978   6720   7745    277   -822   1196       C  
ATOM   5497  CE2 PHE B 241      39.725   6.320 130.144  1.00 69.37           C  
ANISOU 5497  CE2 PHE B 241    12039   6910   7406    218   -664   1074       C  
ATOM   5498  CZ  PHE B 241      40.468   5.292 130.707  1.00 70.11           C  
ANISOU 5498  CZ  PHE B 241    12070   6840   7725    253   -717   1045       C  
ATOM   5499  N   LEU B 242      39.379  10.737 132.095  1.00 64.46           N  
ANISOU 5499  N   LEU B 242    11428   6622   6439    288   -627   1429       N  
ATOM   5500  CA  LEU B 242      40.031  11.541 131.054  1.00 64.23           C  
ANISOU 5500  CA  LEU B 242    11405   6649   6350    298   -536   1349       C  
ATOM   5501  C   LEU B 242      41.131  12.443 131.626  1.00 63.52           C  
ANISOU 5501  C   LEU B 242    11277   6563   6292    360   -496   1363       C  
ATOM   5502  O   LEU B 242      42.214  12.550 131.033  1.00 63.85           O  
ANISOU 5502  O   LEU B 242    11306   6586   6366    385   -431   1266       O  
ATOM   5503  CB  LEU B 242      39.004  12.365 130.269  1.00 63.97           C  
ANISOU 5503  CB  LEU B 242    11404   6731   6169    245   -523   1389       C  
ATOM   5504  CG  LEU B 242      38.095  11.540 129.351  1.00 64.91           C  
ANISOU 5504  CG  LEU B 242    11566   6860   6235    171   -544   1351       C  
ATOM   5505  CD1 LEU B 242      36.825  12.297 128.991  1.00 64.70           C  
ANISOU 5505  CD1 LEU B 242    11558   6931   6091    117   -573   1446       C  
ATOM   5506  CD2 LEU B 242      38.833  11.108 128.092  1.00 66.02           C  
ANISOU 5506  CD2 LEU B 242    11722   7001   6362    134   -473   1201       C  
ATOM   5507  N   PHE B 243      40.854  13.065 132.778  1.00 62.43           N  
ANISOU 5507  N   PHE B 243    11117   6455   6148    375   -530   1470       N  
ATOM   5508  CA  PHE B 243      41.857  13.879 133.471  1.00 61.67           C  
ANISOU 5508  CA  PHE B 243    10983   6364   6084    427   -498   1489       C  
ATOM   5509  C   PHE B 243      43.099  13.055 133.812  1.00 61.85           C  
ANISOU 5509  C   PHE B 243    10977   6274   6248    465   -511   1441       C  
ATOM   5510  O   PHE B 243      44.226  13.428 133.452  1.00 61.44           O  
ANISOU 5510  O   PHE B 243    10905   6205   6233    509   -450   1373       O  
ATOM   5511  CB  PHE B 243      41.270  14.493 134.744  1.00 61.35           C  
ANISOU 5511  CB  PHE B 243    10917   6375   6017    412   -533   1597       C  
ATOM   5512  CG  PHE B 243      42.212  15.424 135.458  1.00 61.40           C  
ANISOU 5512  CG  PHE B 243    10884   6402   6043    452   -495   1614       C  
ATOM   5513  CD1 PHE B 243      42.253  16.773 135.130  1.00 61.18           C  
ANISOU 5513  CD1 PHE B 243    10839   6447   5956    473   -431   1611       C  
ATOM   5514  CD2 PHE B 243      43.058  14.955 136.460  1.00 61.72           C  
ANISOU 5514  CD2 PHE B 243    10896   6385   6168    462   -533   1642       C  
ATOM   5515  CE1 PHE B 243      43.117  17.637 135.786  1.00 60.92           C  
ANISOU 5515  CE1 PHE B 243    10769   6434   5944    509   -393   1621       C  
ATOM   5516  CE2 PHE B 243      43.927  15.813 137.116  1.00 61.24           C  
ANISOU 5516  CE2 PHE B 243    10800   6349   6117    490   -499   1659       C  
ATOM   5517  CZ  PHE B 243      43.957  17.155 136.777  1.00 60.87           C  
ANISOU 5517  CZ  PHE B 243    10741   6379   6006    517   -423   1641       C  
ATOM   5518  N   ALA B 244      42.872  11.932 134.497  1.00 62.45           N  
ANISOU 5518  N   ALA B 244    11043   6268   6415    444   -597   1482       N  
ATOM   5519  CA  ALA B 244      43.961  11.030 134.906  1.00 63.13           C  
ANISOU 5519  CA  ALA B 244    11085   6221   6678    472   -639   1458       C  
ATOM   5520  C   ALA B 244      44.754  10.502 133.710  1.00 63.85           C  
ANISOU 5520  C   ALA B 244    11164   6236   6859    502   -574   1298       C  
ATOM   5521  O   ALA B 244      45.996  10.501 133.718  1.00 63.80           O  
ANISOU 5521  O   ALA B 244    11111   6161   6969    549   -544   1239       O  
ATOM   5522  CB  ALA B 244      43.410   9.870 135.716  1.00 63.72           C  
ANISOU 5522  CB  ALA B 244    11151   6221   6838    425   -760   1543       C  
ATOM   5523  N   LEU B 245      44.021  10.083 132.680  1.00 64.38           N  
ANISOU 5523  N   LEU B 245    11268   6324   6867    463   -547   1222       N  
ATOM   5524  CA  LEU B 245      44.627   9.546 131.462  1.00 65.67           C  
ANISOU 5524  CA  LEU B 245    11419   6438   7094    462   -470   1044       C  
ATOM   5525  C   LEU B 245      45.436  10.613 130.718  1.00 65.23           C  
ANISOU 5525  C   LEU B 245    11365   6466   6954    478   -357    963       C  
ATOM   5526  O   LEU B 245      46.537  10.333 130.236  1.00 65.97           O  
ANISOU 5526  O   LEU B 245    11414   6494   7156    501   -293    827       O  
ATOM   5527  CB  LEU B 245      43.555   8.947 130.542  1.00 66.65           C  
ANISOU 5527  CB  LEU B 245    11589   6594   7139    393   -466    988       C  
ATOM   5528  CG  LEU B 245      44.032   7.962 129.469  1.00 68.43           C  
ANISOU 5528  CG  LEU B 245    11788   6742   7468    367   -405    790       C  
ATOM   5529  CD1 LEU B 245      44.472   6.642 130.094  1.00 69.29           C  
ANISOU 5529  CD1 LEU B 245    11827   6659   7838    399   -481    766       C  
ATOM   5530  CD2 LEU B 245      42.933   7.721 128.441  1.00 68.89           C  
ANISOU 5530  CD2 LEU B 245    11906   6887   7382    280   -382    741       C  
ATOM   5531  N   SER B 246      44.892  11.829 130.641  1.00 63.81           N  
ANISOU 5531  N   SER B 246    11225   6422   6595    464   -335   1046       N  
ATOM   5532  CA  SER B 246      45.614  12.969 130.059  1.00 63.15           C  
ANISOU 5532  CA  SER B 246    11141   6424   6427    474   -246   1004       C  
ATOM   5533  C   SER B 246      46.859  13.356 130.864  1.00 62.82           C  
ANISOU 5533  C   SER B 246    11048   6326   6492    550   -234   1016       C  
ATOM   5534  O   SER B 246      47.917  13.625 130.277  1.00 62.60           O  
ANISOU 5534  O   SER B 246    10996   6297   6490    567   -154    910       O  
ATOM   5535  CB  SER B 246      44.699  14.192 129.942  1.00 62.24           C  
ANISOU 5535  CB  SER B 246    11063   6443   6139    444   -250   1115       C  
ATOM   5536  OG  SER B 246      43.589  13.936 129.107  1.00 62.64           O  
ANISOU 5536  OG  SER B 246    11159   6553   6088    366   -264   1113       O  
ATOM   5537  N   TRP B 247      46.733  13.369 132.197  1.00 62.72           N  
ANISOU 5537  N   TRP B 247    11017   6276   6536    582   -313   1143       N  
ATOM   5538  CA  TRP B 247      47.804  13.891 133.075  1.00 62.81           C  
ANISOU 5538  CA  TRP B 247    10984   6258   6622    639   -313   1184       C  
ATOM   5539  C   TRP B 247      48.899  12.909 133.514  1.00 64.08           C  
ANISOU 5539  C   TRP B 247    11083   6266   6998    676   -348   1140       C  
ATOM   5540  O   TRP B 247      50.046  13.334 133.696  1.00 63.90           O  
ANISOU 5540  O   TRP B 247    11019   6216   7042    723   -312   1114       O  
ATOM   5541  CB  TRP B 247      47.206  14.583 134.310  1.00 61.79           C  
ANISOU 5541  CB  TRP B 247    10858   6191   6427    632   -369   1337       C  
ATOM   5542  CG  TRP B 247      46.806  15.989 134.021  1.00 60.94           C  
ANISOU 5542  CG  TRP B 247    10770   6211   6173    629   -310   1365       C  
ATOM   5543  CD1 TRP B 247      45.542  16.474 133.850  1.00 60.58           C  
ANISOU 5543  CD1 TRP B 247    10752   6249   6014    587   -320   1419       C  
ATOM   5544  CD2 TRP B 247      47.688  17.092 133.838  1.00 60.49           C  
ANISOU 5544  CD2 TRP B 247    10695   6198   6089    668   -239   1343       C  
ATOM   5545  NE1 TRP B 247      45.585  17.819 133.580  1.00 60.01           N  
ANISOU 5545  NE1 TRP B 247    10672   6261   5865    599   -266   1436       N  
ATOM   5546  CE2 TRP B 247      46.892  18.226 133.569  1.00 59.97           C  
ANISOU 5546  CE2 TRP B 247    10643   6237   5903    647   -216   1391       C  
ATOM   5547  CE3 TRP B 247      49.078  17.237 133.885  1.00 60.77           C  
ANISOU 5547  CE3 TRP B 247    10696   6187   6205    719   -198   1289       C  
ATOM   5548  CZ2 TRP B 247      47.444  19.492 133.342  1.00 59.59           C  
ANISOU 5548  CZ2 TRP B 247    10578   6249   5814    673   -156   1392       C  
ATOM   5549  CZ3 TRP B 247      49.627  18.491 133.661  1.00 60.25           C  
ANISOU 5549  CZ3 TRP B 247    10622   6192   6078    745   -131   1285       C  
ATOM   5550  CH2 TRP B 247      48.813  19.604 133.396  1.00 59.61           C  
ANISOU 5550  CH2 TRP B 247    10557   6215   5877    721   -113   1339       C  
ATOM   5551  N   LEU B 248      48.565  11.623 133.679  1.00 65.30           N  
ANISOU 5551  N   LEU B 248    11220   6312   7276    655   -425   1137       N  
ATOM   5552  CA  LEU B 248      49.539  10.639 134.207  1.00 66.55           C  
ANISOU 5552  CA  LEU B 248    11301   6300   7683    686   -488   1122       C  
ATOM   5553  C   LEU B 248      50.857  10.470 133.417  1.00 67.46           C  
ANISOU 5553  C   LEU B 248    11355   6330   7945    732   -400    948       C  
ATOM   5554  O   LEU B 248      51.922  10.318 134.037  1.00 67.85           O  
ANISOU 5554  O   LEU B 248    11334   6275   8169    775   -435    967       O  
ATOM   5555  CB  LEU B 248      48.875   9.272 134.438  1.00 67.72           C  
ANISOU 5555  CB  LEU B 248    11436   6338   7955    649   -594   1150       C  
ATOM   5556  CG  LEU B 248      48.050   9.170 135.733  1.00 67.57           C  
ANISOU 5556  CG  LEU B 248    11437   6348   7888    601   -722   1351       C  
ATOM   5557  CD1 LEU B 248      47.154   7.938 135.722  1.00 68.51           C  
ANISOU 5557  CD1 LEU B 248    11561   6392   8077    552   -812   1372       C  
ATOM   5558  CD2 LEU B 248      48.941   9.171 136.973  1.00 67.87           C  
ANISOU 5558  CD2 LEU B 248    11416   6321   8050    608   -812   1472       C  
ATOM   5559  N   PRO B 249      50.800  10.490 132.069  1.00 68.12           N  
ANISOU 5559  N   PRO B 249    11460   6462   7960    711   -286    778       N  
ATOM   5560  CA  PRO B 249      52.029  10.412 131.262  1.00 69.55           C  
ANISOU 5560  CA  PRO B 249    11580   6588   8257    736   -180    588       C  
ATOM   5561  C   PRO B 249      53.121  11.436 131.630  1.00 69.59           C  
ANISOU 5561  C   PRO B 249    11560   6625   8256    790   -137    615       C  
ATOM   5562  O   PRO B 249      54.273  11.047 131.892  1.00 70.54           O  
ANISOU 5562  O   PRO B 249    11593   6613   8594    838   -140    557       O  
ATOM   5563  CB  PRO B 249      51.519  10.647 129.834  1.00 69.60           C  
ANISOU 5563  CB  PRO B 249    11641   6722   8081    666    -64    447       C  
ATOM   5564  CG  PRO B 249      50.141  10.084 129.851  1.00 69.26           C  
ANISOU 5564  CG  PRO B 249    11653   6699   7964    616   -136    517       C  
ATOM   5565  CD  PRO B 249      49.595  10.372 131.222  1.00 68.10           C  
ANISOU 5565  CD  PRO B 249    11526   6553   7794    645   -259    743       C  
ATOM   5566  N   LEU B 250      52.750  12.718 131.677  1.00 68.73           N  
ANISOU 5566  N   LEU B 250    11518   6677   7918    782   -106    706       N  
ATOM   5567  CA  LEU B 250      53.693  13.796 132.015  1.00 68.36           C  
ANISOU 5567  CA  LEU B 250    11454   6674   7844    829    -64    738       C  
ATOM   5568  C   LEU B 250      54.298  13.630 133.420  1.00 68.47           C  
ANISOU 5568  C   LEU B 250    11414   6586   8013    878   -165    866       C  
ATOM   5569  O   LEU B 250      55.451  14.017 133.654  1.00 68.20           O  
ANISOU 5569  O   LEU B 250    11331   6516   8065    925   -136    846       O  
ATOM   5570  CB  LEU B 250      53.019  15.166 131.886  1.00 67.36           C  
ANISOU 5570  CB  LEU B 250    11399   6725   7467    807    -30    827       C  
ATOM   5571  CG  LEU B 250      53.915  16.413 131.937  1.00 66.78           C  
ANISOU 5571  CG  LEU B 250    11316   6720   7336    844     33    837       C  
ATOM   5572  CD1 LEU B 250      54.803  16.517 130.707  1.00 67.54           C  
ANISOU 5572  CD1 LEU B 250    11393   6837   7430    830    152    658       C  
ATOM   5573  CD2 LEU B 250      53.067  17.665 132.066  1.00 65.68           C  
ANISOU 5573  CD2 LEU B 250    11230   6724   7000    824     32    956       C  
ATOM   5574  N   HIS B 251      53.520  13.059 134.343  1.00 68.94           N  
ANISOU 5574  N   HIS B 251    11483   6608   8102    854   -286   1004       N  
ATOM   5575  CA  HIS B 251      54.025  12.689 135.670  1.00 69.49           C  
ANISOU 5575  CA  HIS B 251    11499   6580   8324    865   -406   1138       C  
ATOM   5576  C   HIS B 251      54.992  11.515 135.583  1.00 71.04           C  
ANISOU 5576  C   HIS B 251    11597   6574   8821    895   -447   1056       C  
ATOM   5577  O   HIS B 251      56.117  11.604 136.095  1.00 71.48           O  
ANISOU 5577  O   HIS B 251    11583   6549   9024    933   -471   1078       O  
ATOM   5578  CB  HIS B 251      52.879  12.381 136.638  1.00 69.35           C  
ANISOU 5578  CB  HIS B 251    11517   6594   8238    804   -525   1305       C  
ATOM   5579  CG  HIS B 251      52.102  13.593 137.043  1.00 68.37           C  
ANISOU 5579  CG  HIS B 251    11457   6647   7872    776   -495   1396       C  
ATOM   5580  ND1 HIS B 251      52.684  14.664 137.687  1.00 67.82           N  
ANISOU 5580  ND1 HIS B 251    11379   6648   7740    793   -470   1454       N  
ATOM   5581  CD2 HIS B 251      50.794  13.907 136.893  1.00 68.22           C  
ANISOU 5581  CD2 HIS B 251    11501   6738   7680    733   -486   1429       C  
ATOM   5582  CE1 HIS B 251      51.768  15.587 137.916  1.00 67.25           C  
ANISOU 5582  CE1 HIS B 251    11355   6718   7479    761   -441   1509       C  
ATOM   5583  NE2 HIS B 251      50.614  15.155 137.439  1.00 67.40           N  
ANISOU 5583  NE2 HIS B 251    11414   6759   7432    726   -452   1497       N  
ATOM   5584  N   ILE B 252      54.583  10.442 134.902  1.00 71.92           N  
ANISOU 5584  N   ILE B 252    11690   6596   9037    877   -451    952       N  
ATOM   5585  CA  ILE B 252      55.483   9.295 134.696  1.00 73.87           C  
ANISOU 5585  CA  ILE B 252    11824   6632   9610    906   -478    840       C  
ATOM   5586  C   ILE B 252      56.828   9.780 134.125  1.00 74.27           C  
ANISOU 5586  C   ILE B 252    11813   6658   9747    961   -359    686       C  
ATOM   5587  O   ILE B 252      57.899   9.369 134.607  1.00 75.24           O  
ANISOU 5587  O   ILE B 252    11831   6623  10132   1002   -414    690       O  
ATOM   5588  CB  ILE B 252      54.858   8.200 133.790  1.00 75.03           C  
ANISOU 5588  CB  ILE B 252    11959   6706   9840    876   -457    694       C  
ATOM   5589  CG1 ILE B 252      53.687   7.511 134.500  1.00 74.91           C  
ANISOU 5589  CG1 ILE B 252    11981   6673   9808    826   -601    858       C  
ATOM   5590  CG2 ILE B 252      55.898   7.144 133.397  1.00 76.91           C  
ANISOU 5590  CG2 ILE B 252    12058   6723  10438    910   -447    524       C  
ATOM   5591  CD1 ILE B 252      52.734   6.792 133.563  1.00 75.33           C  
ANISOU 5591  CD1 ILE B 252    12067   6731   9824    784   -562    738       C  
ATOM   5592  N   LEU B 253      56.759  10.667 133.128  1.00 73.36           N  
ANISOU 5592  N   LEU B 253    11760   6698   9413    954   -207    564       N  
ATOM   5593  CA  LEU B 253      57.956  11.306 132.569  1.00 73.73           C  
ANISOU 5593  CA  LEU B 253    11765   6762   9487    991    -85    427       C  
ATOM   5594  C   LEU B 253      58.794  12.067 133.612  1.00 73.15           C  
ANISOU 5594  C   LEU B 253    11667   6684   9440   1041   -135    570       C  
ATOM   5595  O   LEU B 253      60.027  12.012 133.566  1.00 73.63           O  
ANISOU 5595  O   LEU B 253    11639   6647   9689   1086   -101    484       O  
ATOM   5596  CB  LEU B 253      57.586  12.244 131.412  1.00 73.31           C  
ANISOU 5596  CB  LEU B 253    11797   6908   9149    948     61    321       C  
ATOM   5597  CG  LEU B 253      57.165  11.601 130.089  1.00 74.45           C  
ANISOU 5597  CG  LEU B 253    11947   7073   9267    881    157    115       C  
ATOM   5598  CD1 LEU B 253      56.559  12.663 129.185  1.00 73.67           C  
ANISOU 5598  CD1 LEU B 253    11950   7197   8842    815    252    100       C  
ATOM   5599  CD2 LEU B 253      58.337  10.901 129.410  1.00 76.21           C  
ANISOU 5599  CD2 LEU B 253    12053   7166   9737    891    252   -130       C  
ATOM   5600  N   ASN B 254      58.135  12.771 134.537  1.00 72.18           N  
ANISOU 5600  N   ASN B 254    11617   6669   9138   1025   -210    775       N  
ATOM   5601  CA  ASN B 254      58.847  13.482 135.617  1.00 71.76           C  
ANISOU 5601  CA  ASN B 254    11544   6626   9096   1054   -264    918       C  
ATOM   5602  C   ASN B 254      59.487  12.530 136.620  1.00 72.92           C  
ANISOU 5602  C   ASN B 254    11593   6584   9527   1061   -412   1018       C  
ATOM   5603  O   ASN B 254      60.586  12.796 137.113  1.00 72.58           O  
ANISOU 5603  O   ASN B 254    11487   6483   9607   1096   -431   1050       O  
ATOM   5604  CB  ASN B 254      57.919  14.452 136.361  1.00 70.44           C  
ANISOU 5604  CB  ASN B 254    11466   6625   8669   1017   -296   1089       C  
ATOM   5605  CG  ASN B 254      57.545  15.660 135.528  1.00 69.17           C  
ANISOU 5605  CG  ASN B 254    11380   6638   8260   1017   -166   1025       C  
ATOM   5606  OD1 ASN B 254      58.006  15.820 134.400  1.00 69.56           O  
ANISOU 5606  OD1 ASN B 254    11423   6703   8301   1033    -53    865       O  
ATOM   5607  ND2 ASN B 254      56.703  16.522 136.087  1.00 67.84           N  
ANISOU 5607  ND2 ASN B 254    11274   6603   7899    988   -183   1149       N  
ATOM   5608  N   CYS B 255      58.788  11.435 136.921  1.00 74.25           N  
ANISOU 5608  N   CYS B 255    11748   6660   9803   1022   -526   1078       N  
ATOM   5609  CA  CYS B 255      59.318  10.389 137.797  1.00 75.98           C  
ANISOU 5609  CA  CYS B 255    11863   6681  10322   1013   -691   1186       C  
ATOM   5610  C   CYS B 255      60.517   9.680 137.167  1.00 77.89           C  
ANISOU 5610  C   CYS B 255    11973   6723  10897   1074   -654   1010       C  
ATOM   5611  O   CYS B 255      61.569   9.561 137.809  1.00 78.58           O  
ANISOU 5611  O   CYS B 255    11966   6688  11202   1098   -732   1077       O  
ATOM   5612  CB  CYS B 255      58.231   9.372 138.159  1.00 76.35           C  
ANISOU 5612  CB  CYS B 255    11925   6678  10406    949   -820   1285       C  
ATOM   5613  SG  CYS B 255      56.927  10.055 139.209  1.00 74.66           S  
ANISOU 5613  SG  CYS B 255    11832   6673   9862    859   -893   1512       S  
ATOM   5614  N   ILE B 256      60.372   9.233 135.917  1.00 78.90           N  
ANISOU 5614  N   ILE B 256    12088   6821  11069   1089   -533    779       N  
ATOM   5615  CA  ILE B 256      61.485   8.535 135.248  1.00 81.23           C  
ANISOU 5615  CA  ILE B 256    12243   6925  11695   1137   -475    569       C  
ATOM   5616  C   ILE B 256      62.705   9.436 135.006  1.00 81.35           C  
ANISOU 5616  C   ILE B 256    12223   6976  11709   1189   -361    477       C  
ATOM   5617  O   ILE B 256      63.825   8.950 135.082  1.00 82.62           O  
ANISOU 5617  O   ILE B 256    12245   6952  12191   1232   -381    406       O  
ATOM   5618  CB  ILE B 256      61.078   7.761 133.958  1.00 82.38           C  
ANISOU 5618  CB  ILE B 256    12368   7031  11902   1120   -361    313       C  
ATOM   5619  CG1 ILE B 256      60.680   8.711 132.823  1.00 81.46           C  
ANISOU 5619  CG1 ILE B 256    12363   7144  11442   1094   -167    162       C  
ATOM   5620  CG2 ILE B 256      59.992   6.728 134.268  1.00 82.89           C  
ANISOU 5620  CG2 ILE B 256    12445   7021  12029   1075   -492    407       C  
ATOM   5621  CD1 ILE B 256      59.964   8.038 131.669  1.00 82.30           C  
ANISOU 5621  CD1 ILE B 256    12484   7267  11517   1041    -74    -38       C  
ATOM   5622  N   THR B 257      62.502  10.730 134.757  1.00 80.79           N  
ANISOU 5622  N   THR B 257    12266   7128  11300   1185   -253    488       N  
ATOM   5623  CA  THR B 257      63.633  11.674 134.662  1.00 81.35           C  
ANISOU 5623  CA  THR B 257    12313   7245  11351   1230   -161    436       C  
ATOM   5624  C   THR B 257      64.336  11.876 136.013  1.00 81.97           C  
ANISOU 5624  C   THR B 257    12343   7250  11551   1254   -304    650       C  
ATOM   5625  O   THR B 257      65.572  11.929 136.067  1.00 82.96           O  
ANISOU 5625  O   THR B 257    12368   7272  11878   1302   -286    592       O  
ATOM   5626  CB  THR B 257      63.215  13.052 134.103  1.00 79.65           C  
ANISOU 5626  CB  THR B 257    12227   7283  10754   1213    -28    417       C  
ATOM   5627  OG1 THR B 257      62.080  13.544 134.823  1.00 78.50           O  
ANISOU 5627  OG1 THR B 257    12191   7267  10368   1177   -110    624       O  
ATOM   5628  CG2 THR B 257      62.881  12.956 132.616  1.00 80.21           C  
ANISOU 5628  CG2 THR B 257    12324   7430  10719   1175    129    181       C  
ATOM   5629  N   LEU B 258      63.550  11.982 137.088  1.00 81.92           N  
ANISOU 5629  N   LEU B 258    12402   7304  11418   1208   -443    890       N  
ATOM   5630  CA  LEU B 258      64.093  12.095 138.449  1.00 82.47           C  
ANISOU 5630  CA  LEU B 258    12431   7323  11579   1195   -596   1114       C  
ATOM   5631  C   LEU B 258      64.858  10.843 138.853  1.00 85.33           C  
ANISOU 5631  C   LEU B 258    12639   7419  12361   1204   -740   1143       C  
ATOM   5632  O   LEU B 258      66.035  10.921 139.193  1.00 86.19           O  
ANISOU 5632  O   LEU B 258    12652   7424  12670   1240   -772   1161       O  
ATOM   5633  CB  LEU B 258      62.981  12.357 139.476  1.00 81.15           C  
ANISOU 5633  CB  LEU B 258    12361   7288  11181   1113   -708   1343       C  
ATOM   5634  CG  LEU B 258      63.388  12.402 140.957  1.00 81.19           C  
ANISOU 5634  CG  LEU B 258    12332   7271  11245   1056   -880   1590       C  
ATOM   5635  CD1 LEU B 258      64.434  13.480 141.195  1.00 80.74           C  
ANISOU 5635  CD1 LEU B 258    12264   7276  11136   1095   -815   1593       C  
ATOM   5636  CD2 LEU B 258      62.177  12.633 141.844  1.00 80.38           C  
ANISOU 5636  CD2 LEU B 258    12325   7322  10891    954   -961   1774       C  
ATOM   5637  N   PHE B 259      64.179   9.698 138.817  1.00 87.59           N  
ANISOU 5637  N   PHE B 259    12896   7591  12793   1171   -833   1156       N  
ATOM   5638  CA  PHE B 259      64.766   8.439 139.300  1.00 90.70           C  
ANISOU 5638  CA  PHE B 259    13134   7714  13612   1168  -1005   1220       C  
ATOM   5639  C   PHE B 259      65.823   7.878 138.351  1.00 94.08           C  
ANISOU 5639  C   PHE B 259    13414   7944  14388   1247   -908    959       C  
ATOM   5640  O   PHE B 259      66.849   7.369 138.807  1.00 95.57           O  
ANISOU 5640  O   PHE B 259    13453   7924  14934   1270  -1017   1004       O  
ATOM   5641  CB  PHE B 259      63.681   7.387 139.567  1.00 90.76           C  
ANISOU 5641  CB  PHE B 259    13152   7657  13676   1102  -1142   1318       C  
ATOM   5642  CG  PHE B 259      62.646   7.819 140.576  1.00 88.91           C  
ANISOU 5642  CG  PHE B 259    13043   7605  13130   1007  -1246   1570       C  
ATOM   5643  CD1 PHE B 259      63.025   8.308 141.826  1.00 88.39           C  
ANISOU 5643  CD1 PHE B 259    12981   7594  13008    948  -1373   1809       C  
ATOM   5644  CD2 PHE B 259      61.289   7.728 140.283  1.00 87.87           C  
ANISOU 5644  CD2 PHE B 259    13023   7598  12766    965  -1213   1560       C  
ATOM   5645  CE1 PHE B 259      62.074   8.708 142.753  1.00 87.28           C  
ANISOU 5645  CE1 PHE B 259    12947   7635  12578    842  -1452   2013       C  
ATOM   5646  CE2 PHE B 259      60.333   8.125 141.207  1.00 86.82           C  
ANISOU 5646  CE2 PHE B 259    12993   7634  12359    872  -1297   1769       C  
ATOM   5647  CZ  PHE B 259      60.725   8.614 142.445  1.00 86.53           C  
ANISOU 5647  CZ  PHE B 259    12954   7657  12264    806  -1411   1987       C  
ATOM   5648  N   CYS B 260      65.571   7.978 137.044  1.00 96.35           N  
ANISOU 5648  N   CYS B 260    13735   8300  14574   1274   -707    688       N  
ATOM   5649  CA  CYS B 260      66.519   7.552 136.008  1.00 99.45           C  
ANISOU 5649  CA  CYS B 260    13992   8545  15246   1330   -570    390       C  
ATOM   5650  C   CYS B 260      66.945   8.731 135.103  1.00 98.96           C  
ANISOU 5650  C   CYS B 260    13999   8679  14922   1355   -340    201       C  
ATOM   5651  O   CYS B 260      66.401   8.905 134.010  1.00 97.86           O  
ANISOU 5651  O   CYS B 260    13930   8669  14583   1331   -177      8       O  
ATOM   5652  CB  CYS B 260      65.912   6.415 135.176  1.00101.70           C  
ANISOU 5652  CB  CYS B 260    14227   8720  15692   1311   -534    200       C  
ATOM   5653  SG  CYS B 260      67.082   5.671 134.017  1.00105.94           S  
ANISOU 5653  SG  CYS B 260    14559   9041  16650   1359   -377   -187       S  
ATOM   5654  N   PRO B 261      67.914   9.555 135.562  1.00 99.69           N  
ANISOU 5654  N   PRO B 261    14072   8798  15005   1393   -335    270       N  
ATOM   5655  CA  PRO B 261      68.467  10.597 134.680  1.00 99.75           C  
ANISOU 5655  CA  PRO B 261    14121   8963  14815   1415   -124     83       C  
ATOM   5656  C   PRO B 261      69.296  10.033 133.511  1.00102.33           C  
ANISOU 5656  C   PRO B 261    14312   9168  15401   1435     34   -256       C  
ATOM   5657  O   PRO B 261      69.473  10.713 132.498  1.00101.34           O  
ANISOU 5657  O   PRO B 261    14232   9199  15072   1419    230   -455       O  
ATOM   5658  CB  PRO B 261      69.344  11.429 135.626  1.00 98.92           C  
ANISOU 5658  CB  PRO B 261    14007   8875  14703   1449   -191    261       C  
ATOM   5659  CG  PRO B 261      69.735  10.485 136.709  1.00 99.92           C  
ANISOU 5659  CG  PRO B 261    14008   8764  15191   1455   -412    440       C  
ATOM   5660  CD  PRO B 261      68.570   9.556 136.886  1.00 99.99           C  
ANISOU 5660  CD  PRO B 261    14046   8727  15218   1404   -524    521       C  
ATOM   5661  N   SER B 262      69.799   8.808 133.669  1.00105.70           N  
ANISOU 5661  N   SER B 262    14562   9318  16280   1459    -51   -322       N  
ATOM   5662  CA  SER B 262      70.515   8.092 132.608  1.00108.47           C  
ANISOU 5662  CA  SER B 262    14755   9522  16936   1470     95   -670       C  
ATOM   5663  C   SER B 262      69.608   7.668 131.437  1.00109.14           C  
ANISOU 5663  C   SER B 262    14892   9699  16877   1403    238   -902       C  
ATOM   5664  O   SER B 262      70.074   7.590 130.297  1.00111.05           O  
ANISOU 5664  O   SER B 262    15069   9961  17164   1376    439  -1226       O  
ATOM   5665  CB  SER B 262      71.216   6.859 133.196  1.00110.81           C  
ANISOU 5665  CB  SER B 262    14832   9470  17797   1513    -62   -654       C  
ATOM   5666  OG  SER B 262      72.101   6.270 132.262  1.00113.22           O  
ANISOU 5666  OG  SER B 262    14955   9617  18443   1530     88  -1005       O  
ATOM   5667  N   CYS B 263      68.331   7.393 131.722  1.00107.97           N  
ANISOU 5667  N   CYS B 263    14857   9613  16552   1364    138   -742       N  
ATOM   5668  CA  CYS B 263      67.353   6.971 130.702  1.00107.82           C  
ANISOU 5668  CA  CYS B 263    14898   9686  16379   1293    248   -924       C  
ATOM   5669  C   CYS B 263      67.120   8.025 129.615  1.00107.07           C  
ANISOU 5669  C   CYS B 263    14936   9883  15861   1231    460  -1075       C  
ATOM   5670  O   CYS B 263      66.936   9.205 129.922  1.00105.70           O  
ANISOU 5670  O   CYS B 263    14897   9906  15354   1233    458   -901       O  
ATOM   5671  CB  CYS B 263      65.998   6.645 131.350  1.00106.23           C  
ANISOU 5671  CB  CYS B 263    14811   9520  16030   1265     85   -676       C  
ATOM   5672  SG  CYS B 263      65.953   5.172 132.399  1.00107.11           S  
ANISOU 5672  SG  CYS B 263    14775   9302  16617   1293   -170   -514       S  
ATOM   5673  N   HIS B 264      67.133   7.586 128.355  1.00108.78           N  
ANISOU 5673  N   HIS B 264    15105  10125  16099   1162    639  -1399       N  
ATOM   5674  CA  HIS B 264      66.733   8.421 127.215  1.00108.16           C  
ANISOU 5674  CA  HIS B 264    15153  10332  15608   1064    825  -1539       C  
ATOM   5675  C   HIS B 264      65.247   8.202 126.956  1.00106.74           C  
ANISOU 5675  C   HIS B 264    15107  10272  15175    993    788  -1461       C  
ATOM   5676  O   HIS B 264      64.769   7.071 127.015  1.00107.45           O  
ANISOU 5676  O   HIS B 264    15137  10209  15481    989    722  -1504       O  
ATOM   5677  CB  HIS B 264      67.544   8.065 125.958  1.00111.02           C  
ANISOU 5677  CB  HIS B 264    15390  10683  16106    995   1048  -1944       C  
ATOM   5678  CG  HIS B 264      67.178   8.869 124.746  1.00111.10           C  
ANISOU 5678  CG  HIS B 264    15522  10995  15693    862   1231  -2087       C  
ATOM   5679  ND1 HIS B 264      67.533  10.193 124.593  1.00109.90           N  
ANISOU 5679  ND1 HIS B 264    15464  11052  15240    845   1295  -2012       N  
ATOM   5680  CD2 HIS B 264      66.496   8.530 123.626  1.00112.10           C  
ANISOU 5680  CD2 HIS B 264    15687  11252  15651    726   1355  -2291       C  
ATOM   5681  CE1 HIS B 264      67.079  10.637 123.434  1.00110.22           C  
ANISOU 5681  CE1 HIS B 264    15594  11336  14947    700   1439  -2150       C  
ATOM   5682  NE2 HIS B 264      66.447   9.647 122.827  1.00111.60           N  
ANISOU 5682  NE2 HIS B 264    15740  11475  15186    621   1480  -2320       N  
ATOM   5683  N   LYS B 265      64.526   9.288 126.677  1.00104.58           N  
ANISOU 5683  N   LYS B 265    15006  10264  14462    939    822  -1341       N  
ATOM   5684  CA  LYS B 265      63.094   9.238 126.367  1.00103.57           C  
ANISOU 5684  CA  LYS B 265    15012  10275  14063    864    792  -1259       C  
ATOM   5685  C   LYS B 265      62.788  10.137 125.167  1.00102.74           C  
ANISOU 5685  C   LYS B 265    15014  10449  13572    742    951  -1369       C  
ATOM   5686  O   LYS B 265      62.963  11.354 125.263  1.00100.32           O  
ANISOU 5686  O   LYS B 265    14787  10297  13030    747    965  -1244       O  
ATOM   5687  CB  LYS B 265      62.264   9.663 127.580  1.00101.88           C  
ANISOU 5687  CB  LYS B 265    14906  10084  13719    924    603   -902       C  
ATOM   5688  CG  LYS B 265      62.032   8.533 128.573  1.00102.83           C  
ANISOU 5688  CG  LYS B 265    14951   9969  14148    984    428   -781       C  
ATOM   5689  CD  LYS B 265      60.932   7.574 128.119  1.00103.32           C  
ANISOU 5689  CD  LYS B 265    15036  10010  14209    921    409   -844       C  
ATOM   5690  CE  LYS B 265      61.175   6.165 128.641  1.00104.59           C  
ANISOU 5690  CE  LYS B 265    15050   9882  14806    965    296   -873       C  
ATOM   5691  NZ  LYS B 265      60.159   5.201 128.146  1.00105.29           N  
ANISOU 5691  NZ  LYS B 265    15151   9942  14911    903    287   -956       N  
ATOM   5692  N   PRO B 266      62.342   9.543 124.032  1.00104.40           N  
ANISOU 5692  N   PRO B 266    15221  10724  13721    619   1065  -1600       N  
ATOM   5693  CA  PRO B 266      62.078  10.289 122.795  1.00104.19           C  
ANISOU 5693  CA  PRO B 266    15284  10968  13335    467   1212  -1716       C  
ATOM   5694  C   PRO B 266      61.235  11.553 122.961  1.00101.15           C  
ANISOU 5694  C   PRO B 266    15068  10798  12566    447   1140  -1437       C  
ATOM   5695  O   PRO B 266      60.320  11.591 123.785  1.00 99.38           O  
ANISOU 5695  O   PRO B 266    14917  10546  12296    509    989  -1189       O  
ATOM   5696  CB  PRO B 266      61.329   9.271 121.932  1.00106.02           C  
ANISOU 5696  CB  PRO B 266    15505  11208  13569    350   1271  -1912       C  
ATOM   5697  CG  PRO B 266      61.896   7.964 122.343  1.00107.77           C  
ANISOU 5697  CG  PRO B 266    15559  11139  14249    432   1250  -2064       C  
ATOM   5698  CD  PRO B 266      62.190   8.087 123.813  1.00106.49           C  
ANISOU 5698  CD  PRO B 266    15375  10801  14283    605   1069  -1789       C  
ATOM   5699  N   SER B 267      61.549  12.566 122.158  1.00100.67           N  
ANISOU 5699  N   SER B 267    15057  10948  12244    350   1249  -1487       N  
ATOM   5700  CA  SER B 267      60.855  13.847 122.203  1.00 98.80           C  
ANISOU 5700  CA  SER B 267    14958  10909  11669    321   1189  -1240       C  
ATOM   5701  C   SER B 267      59.372  13.759 121.836  1.00 98.40           C  
ANISOU 5701  C   SER B 267    15016  10972  11397    230   1127  -1132       C  
ATOM   5702  O   SER B 267      58.581  14.498 122.399  1.00 97.23           O  
ANISOU 5702  O   SER B 267    14959  10884  11099    269   1011   -871       O  
ATOM   5703  CB  SER B 267      61.562  14.866 121.310  1.00 99.14           C  
ANISOU 5703  CB  SER B 267    15018  11148  11502    214   1317  -1331       C  
ATOM   5704  OG  SER B 267      62.897  15.057 121.744  1.00 99.31           O  
ANISOU 5704  OG  SER B 267    14946  11067  11720    310   1364  -1401       O  
ATOM   5705  N   ILE B 268      58.993  12.854 120.934  1.00100.14           N  
ANISOU 5705  N   ILE B 268    15219  11215  11614    108   1202  -1337       N  
ATOM   5706  CA  ILE B 268      57.575  12.717 120.535  1.00100.08           C  
ANISOU 5706  CA  ILE B 268    15311  11316  11398     12   1142  -1240       C  
ATOM   5707  C   ILE B 268      56.711  12.318 121.744  1.00 98.54           C  
ANISOU 5707  C   ILE B 268    15143  10971  11323    150    969  -1012       C  
ATOM   5708  O   ILE B 268      55.615  12.866 121.933  1.00 97.42           O  
ANISOU 5708  O   ILE B 268    15103  10926  10985    135    871   -793       O  
ATOM   5709  CB  ILE B 268      57.355  11.726 119.353  1.00102.16           C  
ANISOU 5709  CB  ILE B 268    15543  11627  11646   -153   1261  -1523       C  
ATOM   5710  CG1 ILE B 268      58.165  12.160 118.133  1.00104.06           C  
ANISOU 5710  CG1 ILE B 268    15759  12050  11729   -324   1440  -1754       C  
ATOM   5711  CG2 ILE B 268      55.868  11.646 118.979  1.00101.44           C  
ANISOU 5711  CG2 ILE B 268    15560  11652  11329   -253   1186  -1397       C  
ATOM   5712  CD1 ILE B 268      58.099  11.220 116.948  1.00106.99           C  
ANISOU 5712  CD1 ILE B 268    16082  12484  12083   -511   1585  -2073       C  
ATOM   5713  N   LEU B 269      57.227  11.402 122.568  1.00 98.34           N  
ANISOU 5713  N   LEU B 269    15022  10713  11630    274    927  -1057       N  
ATOM   5714  CA  LEU B 269      56.530  10.968 123.778  1.00 97.12           C  
ANISOU 5714  CA  LEU B 269    14881  10415  11602    389    759   -843       C  
ATOM   5715  C   LEU B 269      56.394  12.119 124.784  1.00 95.27           C  
ANISOU 5715  C   LEU B 269    14712  10229  11256    479    656   -559       C  
ATOM   5716  O   LEU B 269      55.358  12.244 125.437  1.00 94.05           O  
ANISOU 5716  O   LEU B 269    14626  10088  11021    505    537   -352       O  
ATOM   5717  CB  LEU B 269      57.233   9.763 124.418  1.00 98.00           C  
ANISOU 5717  CB  LEU B 269    14860  10262  12110    485    725   -943       C  
ATOM   5718  CG  LEU B 269      56.993   8.388 123.779  1.00 99.59           C  
ANISOU 5718  CG  LEU B 269    14991  10359  12487    422    772  -1170       C  
ATOM   5719  CD1 LEU B 269      57.192   8.337 122.270  1.00101.18           C  
ANISOU 5719  CD1 LEU B 269    15182  10705  12553    263    961  -1463       C  
ATOM   5720  CD2 LEU B 269      57.895   7.369 124.459  1.00100.60           C  
ANISOU 5720  CD2 LEU B 269    14964  10208  13052    527    729  -1256       C  
ATOM   5721  N   THR B 270      57.432  12.954 124.888  1.00 95.21           N  
ANISOU 5721  N   THR B 270    14677  10251  11246    519    709   -566       N  
ATOM   5722  CA  THR B 270      57.375  14.182 125.693  1.00 93.67           C  
ANISOU 5722  CA  THR B 270    14539  10125  10925    585    638   -329       C  
ATOM   5723  C   THR B 270      56.336  15.162 125.149  1.00 93.61           C  
ANISOU 5723  C   THR B 270    14642  10324  10600    497    629   -205       C  
ATOM   5724  O   THR B 270      55.565  15.735 125.913  1.00 91.85           O  
ANISOU 5724  O   THR B 270    14474  10127  10296    541    526     12       O  
ATOM   5725  CB  THR B 270      58.748  14.891 125.754  1.00 93.22           C  
ANISOU 5725  CB  THR B 270    14427  10067  10922    631    712   -385       C  
ATOM   5726  OG1 THR B 270      59.724  14.004 126.311  1.00 94.08           O  
ANISOU 5726  OG1 THR B 270    14420   9969  11356    717    704   -483       O  
ATOM   5727  CG2 THR B 270      58.685  16.158 126.604  1.00 91.38           C  
ANISOU 5727  CG2 THR B 270    14247   9903  10570    698    641   -150       C  
ATOM   5728  N   TYR B 271      56.328  15.338 123.830  1.00 96.75           N  
ANISOU 5728  N   TYR B 271    15063  10866  10829    360    735   -347       N  
ATOM   5729  CA  TYR B 271      55.452  16.302 123.160  1.00 98.26           C  
ANISOU 5729  CA  TYR B 271    15347  11257  10728    252    722   -230       C  
ATOM   5730  C   TYR B 271      53.974  15.893 123.190  1.00 96.12           C  
ANISOU 5730  C   TYR B 271    15138  11003  10377    214    629   -118       C  
ATOM   5731  O   TYR B 271      53.122  16.736 123.477  1.00 95.11           O  
ANISOU 5731  O   TYR B 271    15070  10951  10114    216    544     86       O  
ATOM   5732  CB  TYR B 271      55.925  16.587 121.717  1.00103.23           C  
ANISOU 5732  CB  TYR B 271    15980  12053  11189     86    855   -407       C  
ATOM   5733  CG  TYR B 271      56.910  17.747 121.599  1.00106.59           C  
ANISOU 5733  CG  TYR B 271    16394  12563  11542     88    909   -388       C  
ATOM   5734  CD1 TYR B 271      56.476  19.065 121.732  1.00107.76           C  
ANISOU 5734  CD1 TYR B 271    16601  12823  11516     82    838   -166       C  
ATOM   5735  CD2 TYR B 271      58.269  17.529 121.343  1.00110.10           C  
ANISOU 5735  CD2 TYR B 271    16757  12967  12106     94   1030   -597       C  
ATOM   5736  CE1 TYR B 271      57.362  20.129 121.622  1.00110.25           C  
ANISOU 5736  CE1 TYR B 271    16904  13213  11772     82    882   -142       C  
ATOM   5737  CE2 TYR B 271      59.163  18.591 121.231  1.00112.05           C  
ANISOU 5737  CE2 TYR B 271    16996  13296  12282     93   1079   -578       C  
ATOM   5738  CZ  TYR B 271      58.708  19.892 121.377  1.00113.45           C  
ANISOU 5738  CZ  TYR B 271    17240  13587  12277     88   1002   -345       C  
ATOM   5739  OH  TYR B 271      59.579  20.963 121.262  1.00120.40           O  
ANISOU 5739  OH  TYR B 271    18110  14546  13091     84   1044   -318       O  
ATOM   5740  N   ILE B 272      53.664  14.623 122.910  1.00 95.30           N  
ANISOU 5740  N   ILE B 272    15014  10823  10373    180    643   -256       N  
ATOM   5741  CA  ILE B 272      52.257  14.152 122.990  1.00 93.77           C  
ANISOU 5741  CA  ILE B 272    14877  10633  10117    148    551   -151       C  
ATOM   5742  C   ILE B 272      51.700  14.205 124.422  1.00 90.98           C  
ANISOU 5742  C   ILE B 272    14533  10171   9864    284    414     65       C  
ATOM   5743  O   ILE B 272      50.514  14.501 124.624  1.00 90.16           O  
ANISOU 5743  O   ILE B 272    14490  10123   9643    265    330    226       O  
ATOM   5744  CB  ILE B 272      52.032  12.736 122.384  1.00 95.60           C  
ANISOU 5744  CB  ILE B 272    15079  10799  10442     79    596   -353       C  
ATOM   5745  CG1 ILE B 272      52.728  11.637 123.208  1.00 96.16           C  
ANISOU 5745  CG1 ILE B 272    15055  10638  10843    201    580   -445       C  
ATOM   5746  CG2 ILE B 272      52.441  12.702 120.911  1.00 97.35           C  
ANISOU 5746  CG2 ILE B 272    15296  11164  10528    -92    740   -580       C  
ATOM   5747  CD1 ILE B 272      52.705  10.268 122.561  1.00 97.79           C  
ANISOU 5747  CD1 ILE B 272    15205  10760  11188    136    641   -680       C  
ATOM   5748  N   ALA B 273      52.559  13.922 125.403  1.00 89.50           N  
ANISOU 5748  N   ALA B 273    14280   9833   9891    405    393     65       N  
ATOM   5749  CA  ALA B 273      52.207  14.074 126.818  1.00 87.60           C  
ANISOU 5749  CA  ALA B 273    14042   9511   9729    511    272    267       C  
ATOM   5750  C   ALA B 273      51.821  15.515 127.137  1.00 85.39           C  
ANISOU 5750  C   ALA B 273    13812   9356   9273    521    242    448       C  
ATOM   5751  O   ALA B 273      50.822  15.751 127.804  1.00 85.39           O  
ANISOU 5751  O   ALA B 273    13848   9372   9222    536    154    608       O  
ATOM   5752  CB  ALA B 273      53.357  13.628 127.710  1.00 87.74           C  
ANISOU 5752  CB  ALA B 273    13975   9364   9996    614    256    238       C  
ATOM   5753  N   ILE B 274      52.610  16.466 126.641  1.00 83.87           N  
ANISOU 5753  N   ILE B 274    13615   9250   9000    507    319    411       N  
ATOM   5754  CA  ILE B 274      52.345  17.897 126.834  1.00 81.88           C  
ANISOU 5754  CA  ILE B 274    13396   9109   8604    512    296    567       C  
ATOM   5755  C   ILE B 274      51.111  18.358 126.049  1.00 81.00           C  
ANISOU 5755  C   ILE B 274    13347   9130   8299    407    268    645       C  
ATOM   5756  O   ILE B 274      50.323  19.155 126.559  1.00 80.71           O  
ANISOU 5756  O   ILE B 274    13329   9130   8205    426    199    811       O  
ATOM   5757  CB  ILE B 274      53.599  18.744 126.499  1.00 82.03           C  
ANISOU 5757  CB  ILE B 274    13387   9176   8604    521    381    506       C  
ATOM   5758  CG1 ILE B 274      54.673  18.484 127.560  1.00 81.93           C  
ANISOU 5758  CG1 ILE B 274    13311   9027   8792    640    377    490       C  
ATOM   5759  CG2 ILE B 274      53.286  20.237 126.440  1.00 81.15           C  
ANISOU 5759  CG2 ILE B 274    13304   9186   8341    503    361    654       C  
ATOM   5760  CD1 ILE B 274      56.076  18.862 127.152  1.00 82.60           C  
ANISOU 5760  CD1 ILE B 274    13350   9119   8913    651    475    369       C  
ATOM   5761  N   PHE B 275      50.941  17.860 124.825  1.00 80.85           N  
ANISOU 5761  N   PHE B 275    13350   9179   8189    288    321    522       N  
ATOM   5762  CA  PHE B 275      49.720  18.131 124.056  1.00 80.04           C  
ANISOU 5762  CA  PHE B 275    13303   9194   7911    172    279    602       C  
ATOM   5763  C   PHE B 275      48.468  17.566 124.742  1.00 78.13           C  
ANISOU 5763  C   PHE B 275    13083   8889   7712    206    180    708       C  
ATOM   5764  O   PHE B 275      47.410  18.192 124.694  1.00 77.25           O  
ANISOU 5764  O   PHE B 275    13002   8845   7502    169    110    854       O  
ATOM   5765  CB  PHE B 275      49.816  17.592 122.619  1.00 82.14           C  
ANISOU 5765  CB  PHE B 275    13588   9557   8063     14    359    434       C  
ATOM   5766  CG  PHE B 275      50.770  18.355 121.723  1.00 83.53           C  
ANISOU 5766  CG  PHE B 275    13756   9855   8126    -73    450    356       C  
ATOM   5767  CD1 PHE B 275      50.750  19.752 121.654  1.00 83.11           C  
ANISOU 5767  CD1 PHE B 275    13715   9898   7962    -91    413    516       C  
ATOM   5768  CD2 PHE B 275      51.662  17.669 120.899  1.00 85.49           C  
ANISOU 5768  CD2 PHE B 275    13974  10123   8382   -154    573    116       C  
ATOM   5769  CE1 PHE B 275      51.621  20.439 120.816  1.00 83.82           C  
ANISOU 5769  CE1 PHE B 275    13798  10107   7941   -187    488    454       C  
ATOM   5770  CE2 PHE B 275      52.533  18.354 120.059  1.00 86.30           C  
ANISOU 5770  CE2 PHE B 275    14068  10354   8366   -255    662     36       C  
ATOM   5771  CZ  PHE B 275      52.513  19.740 120.018  1.00 85.31           C  
ANISOU 5771  CZ  PHE B 275    13965  10330   8117   -273    615    214       C  
ATOM   5772  N   LEU B 276      48.588  16.394 125.369  1.00 76.90           N  
ANISOU 5772  N   LEU B 276    12903   8599   7713    271    168    637       N  
ATOM   5773  CA  LEU B 276      47.472  15.801 126.131  1.00 75.35           C  
ANISOU 5773  CA  LEU B 276    12724   8338   7566    303     71    739       C  
ATOM   5774  C   LEU B 276      46.997  16.671 127.301  1.00 73.40           C  
ANISOU 5774  C   LEU B 276    12474   8088   7328    379     -4    926       C  
ATOM   5775  O   LEU B 276      45.787  16.811 127.526  1.00 72.92           O  
ANISOU 5775  O   LEU B 276    12438   8056   7212    356    -73   1039       O  
ATOM   5776  CB  LEU B 276      47.834  14.399 126.650  1.00 75.69           C  
ANISOU 5776  CB  LEU B 276    12731   8227   7801    355     60    641       C  
ATOM   5777  CG  LEU B 276      47.578  13.241 125.679  1.00 76.96           C  
ANISOU 5777  CG  LEU B 276    12898   8372   7969    269     98    481       C  
ATOM   5778  CD1 LEU B 276      48.370  12.004 126.083  1.00 77.68           C  
ANISOU 5778  CD1 LEU B 276    12920   8290   8302    328    108    349       C  
ATOM   5779  CD2 LEU B 276      46.091  12.927 125.577  1.00 76.73           C  
ANISOU 5779  CD2 LEU B 276    12923   8383   7847    211     22    574       C  
ATOM   5780  N   THR B 277      47.950  17.252 128.032  1.00 72.13           N  
ANISOU 5780  N   THR B 277    12274   7891   7238    461     14    945       N  
ATOM   5781  CA  THR B 277      47.648  18.073 129.211  1.00 70.33           C  
ANISOU 5781  CA  THR B 277    12030   7662   7029    524    -39   1093       C  
ATOM   5782  C   THR B 277      46.955  19.374 128.845  1.00 70.30           C  
ANISOU 5782  C   THR B 277    12039   7769   6903    485    -49   1196       C  
ATOM   5783  O   THR B 277      45.970  19.747 129.482  1.00 70.15           O  
ANISOU 5783  O   THR B 277    12014   7759   6878    492   -108   1307       O  
ATOM   5784  CB  THR B 277      48.910  18.420 130.019  1.00 69.40           C  
ANISOU 5784  CB  THR B 277    11867   7490   7011    608    -11   1083       C  
ATOM   5785  OG1 THR B 277      49.853  19.113 129.189  1.00 68.92           O  
ANISOU 5785  OG1 THR B 277    11799   7486   6902    597     70   1011       O  
ATOM   5786  CG2 THR B 277      49.532  17.156 130.599  1.00 69.79           C  
ANISOU 5786  CG2 THR B 277    11886   7406   7224    650    -31   1018       C  
ATOM   5787  N   HIS B 278      47.476  20.064 127.831  1.00 71.07           N  
ANISOU 5787  N   HIS B 278    12141   7945   6914    437      4   1160       N  
ATOM   5788  CA  HIS B 278      46.824  21.270 127.300  1.00 71.03           C  
ANISOU 5788  CA  HIS B 278    12140   8039   6808    381    -22   1269       C  
ATOM   5789  C   HIS B 278      45.489  20.912 126.644  1.00 70.89           C  
ANISOU 5789  C   HIS B 278    12157   8065   6711    288    -81   1316       C  
ATOM   5790  O   HIS B 278      44.508  21.641 126.786  1.00 69.99           O  
ANISOU 5790  O   HIS B 278    12030   7979   6584    272   -144   1443       O  
ATOM   5791  CB  HIS B 278      47.730  22.008 126.305  1.00 72.31           C  
ANISOU 5791  CB  HIS B 278    12301   8283   6887    326     37   1227       C  
ATOM   5792  CG  HIS B 278      49.020  22.480 126.902  1.00 73.04           C  
ANISOU 5792  CG  HIS B 278    12357   8339   7054    415     92   1189       C  
ATOM   5793  ND1 HIS B 278      50.212  22.470 126.209  1.00 74.20           N  
ANISOU 5793  ND1 HIS B 278    12502   8517   7174    389    175   1073       N  
ATOM   5794  CD2 HIS B 278      49.309  22.956 128.137  1.00 72.98           C  
ANISOU 5794  CD2 HIS B 278    12311   8271   7145    519     80   1246       C  
ATOM   5795  CE1 HIS B 278      51.176  22.929 126.988  1.00 74.01           C  
ANISOU 5795  CE1 HIS B 278    12439   8444   7235    484    204   1070       C  
ATOM   5796  NE2 HIS B 278      50.654  23.231 128.163  1.00 73.22           N  
ANISOU 5796  NE2 HIS B 278    12319   8292   7208    561    146   1176       N  
ATOM   5797  N   GLY B 279      45.469  19.786 125.931  1.00 71.52           N  
ANISOU 5797  N   GLY B 279    12274   8145   6754    226    -57   1207       N  
ATOM   5798  CA  GLY B 279      44.254  19.241 125.326  1.00 71.94           C  
ANISOU 5798  CA  GLY B 279    12365   8234   6734    135   -109   1235       C  
ATOM   5799  C   GLY B 279      43.144  18.915 126.314  1.00 71.23           C  
ANISOU 5799  C   GLY B 279    12269   8078   6714    187   -186   1327       C  
ATOM   5800  O   GLY B 279      41.960  19.103 126.002  1.00 71.65           O  
ANISOU 5800  O   GLY B 279    12335   8174   6713    126   -249   1418       O  
ATOM   5801  N   ASN B 280      43.515  18.450 127.509  1.00 70.43           N  
ANISOU 5801  N   ASN B 280    12145   7881   6734    288   -186   1309       N  
ATOM   5802  CA  ASN B 280      42.542  18.172 128.584  1.00 69.65           C  
ANISOU 5802  CA  ASN B 280    12035   7732   6694    325   -254   1393       C  
ATOM   5803  C   ASN B 280      41.607  19.355 128.894  1.00 69.05           C  
ANISOU 5803  C   ASN B 280    11928   7705   6600    320   -299   1525       C  
ATOM   5804  O   ASN B 280      40.452  19.149 129.270  1.00 68.42           O  
ANISOU 5804  O   ASN B 280    11846   7618   6529    302   -355   1588       O  
ATOM   5805  CB  ASN B 280      43.263  17.729 129.865  1.00 69.12           C  
ANISOU 5805  CB  ASN B 280    11939   7575   6746    413   -251   1375       C  
ATOM   5806  CG  ASN B 280      42.312  17.176 130.913  1.00 68.49           C  
ANISOU 5806  CG  ASN B 280    11854   7455   6711    420   -321   1444       C  
ATOM   5807  OD1 ASN B 280      42.143  17.760 131.981  1.00 67.87           O  
ANISOU 5807  OD1 ASN B 280    11740   7381   6663    451   -338   1514       O  
ATOM   5808  ND2 ASN B 280      41.672  16.052 130.603  1.00 68.63           N  
ANISOU 5808  ND2 ASN B 280    11905   7442   6728    379   -357   1417       N  
ATOM   5809  N   SER B 281      42.097  20.582 128.721  1.00 69.78           N  
ANISOU 5809  N   SER B 281    11989   7839   6682    332   -274   1562       N  
ATOM   5810  CA  SER B 281      41.263  21.784 128.866  1.00 70.34           C  
ANISOU 5810  CA  SER B 281    12011   7942   6770    322   -316   1678       C  
ATOM   5811  C   SER B 281      40.128  21.900 127.829  1.00 71.61           C  
ANISOU 5811  C   SER B 281    12187   8155   6864    222   -380   1751       C  
ATOM   5812  O   SER B 281      39.155  22.615 128.070  1.00 71.70           O  
ANISOU 5812  O   SER B 281    12147   8165   6927    213   -434   1847       O  
ATOM   5813  CB  SER B 281      42.126  23.052 128.831  1.00 69.92           C  
ANISOU 5813  CB  SER B 281    11914   7913   6736    353   -281   1700       C  
ATOM   5814  OG  SER B 281      43.066  23.079 129.895  1.00 68.90           O  
ANISOU 5814  OG  SER B 281    11762   7738   6675    441   -231   1652       O  
ATOM   5815  N   ALA B 282      40.253  21.214 126.691  1.00 73.03           N  
ANISOU 5815  N   ALA B 282    12427   8380   6940    138   -373   1699       N  
ATOM   5816  CA  ALA B 282      39.200  21.188 125.661  1.00 74.28           C  
ANISOU 5816  CA  ALA B 282    12608   8599   7016     21   -439   1770       C  
ATOM   5817  C   ALA B 282      38.100  20.133 125.876  1.00 74.47           C  
ANISOU 5817  C   ALA B 282    12660   8590   7043      3   -483   1767       C  
ATOM   5818  O   ALA B 282      37.003  20.273 125.338  1.00 74.64           O  
ANISOU 5818  O   ALA B 282    12681   8645   7031    -75   -555   1856       O  
ATOM   5819  CB  ALA B 282      39.827  20.997 124.285  1.00 75.51           C  
ANISOU 5819  CB  ALA B 282    12813   8843   7032    -92   -406   1709       C  
ATOM   5820  N   MET B 283      38.382  19.094 126.660  1.00 74.56           N  
ANISOU 5820  N   MET B 283    12691   8535   7104     70   -451   1678       N  
ATOM   5821  CA  MET B 283      37.527  17.891 126.706  1.00 74.90           C  
ANISOU 5821  CA  MET B 283    12771   8548   7137     41   -486   1655       C  
ATOM   5822  C   MET B 283      36.208  18.113 127.462  1.00 75.12           C  
ANISOU 5822  C   MET B 283    12764   8555   7223     54   -555   1759       C  
ATOM   5823  O   MET B 283      35.119  17.785 126.945  1.00 76.53           O  
ANISOU 5823  O   MET B 283    12962   8756   7359    -16   -612   1805       O  
ATOM   5824  CB  MET B 283      38.294  16.710 127.321  1.00 74.12           C  
ANISOU 5824  CB  MET B 283    12691   8370   7099    102   -444   1539       C  
ATOM   5825  CG  MET B 283      39.596  16.367 126.600  1.00 74.46           C  
ANISOU 5825  CG  MET B 283    12754   8418   7119     91   -367   1408       C  
ATOM   5826  SD  MET B 283      40.393  14.892 127.240  1.00 74.76           S  
ANISOU 5826  SD  MET B 283    12791   8333   7280    155   -339   1278       S  
ATOM   5827  CE  MET B 283      41.971  14.955 126.393  1.00 74.99           C  
ANISOU 5827  CE  MET B 283    12812   8377   7303    146   -233   1124       C  
ATOM   5828  N   ASN B 284      36.312  18.685 128.664  1.00 74.26           N  
ANISOU 5828  N   ASN B 284    12599   8408   7207    135   -545   1787       N  
ATOM   5829  CA  ASN B 284      35.159  18.856 129.570  1.00 73.93           C  
ANISOU 5829  CA  ASN B 284    12509   8347   7232    145   -589   1852       C  
ATOM   5830  C   ASN B 284      33.898  19.446 128.891  1.00 74.22           C  
ANISOU 5830  C   ASN B 284    12517   8415   7267     77   -656   1949       C  
ATOM   5831  O   ASN B 284      32.831  18.797 128.912  1.00 74.66           O  
ANISOU 5831  O   ASN B 284    12585   8464   7315     38   -704   1973       O  
ATOM   5832  CB  ASN B 284      35.555  19.634 130.844  1.00 73.70           C  
ANISOU 5832  CB  ASN B 284    12411   8297   7293    217   -553   1854       C  
ATOM   5833  CG  ASN B 284      36.363  18.794 131.826  1.00 73.64           C  
ANISOU 5833  CG  ASN B 284    12425   8251   7301    263   -522   1790       C  
ATOM   5834  OD1 ASN B 284      36.381  17.564 131.749  1.00 73.44           O  
ANISOU 5834  OD1 ASN B 284    12455   8196   7253    248   -541   1753       O  
ATOM   5835  ND2 ASN B 284      37.037  19.462 132.759  1.00 73.61           N  
ANISOU 5835  ND2 ASN B 284    12374   8244   7350    313   -481   1781       N  
ATOM   5836  N   PRO B 285      34.019  20.634 128.249  1.00 73.98           N  
ANISOU 5836  N   PRO B 285    12443   8415   7250     55   -670   2015       N  
ATOM   5837  CA  PRO B 285      32.892  21.168 127.469  1.00 74.49           C  
ANISOU 5837  CA  PRO B 285    12474   8501   7326    -23   -754   2126       C  
ATOM   5838  C   PRO B 285      32.313  20.183 126.456  1.00 75.14           C  
ANISOU 5838  C   PRO B 285    12634   8623   7290   -121   -800   2133       C  
ATOM   5839  O   PRO B 285      31.090  20.109 126.320  1.00 74.86           O  
ANISOU 5839  O   PRO B 285    12578   8582   7282   -169   -871   2206       O  
ATOM   5840  CB  PRO B 285      33.505  22.365 126.734  1.00 75.00           C  
ANISOU 5840  CB  PRO B 285    12503   8599   7394    -49   -764   2189       C  
ATOM   5841  CG  PRO B 285      34.627  22.801 127.604  1.00 74.32           C  
ANISOU 5841  CG  PRO B 285    12391   8487   7360     49   -682   2119       C  
ATOM   5842  CD  PRO B 285      35.180  21.547 128.206  1.00 73.71           C  
ANISOU 5842  CD  PRO B 285    12383   8391   7230     96   -621   2002       C  
ATOM   5843  N   ILE B 286      33.180  19.432 125.771  1.00 75.90           N  
ANISOU 5843  N   ILE B 286    12813   8757   7267   -155   -755   2047       N  
ATOM   5844  CA  ILE B 286      32.732  18.471 124.754  1.00 77.18           C  
ANISOU 5844  CA  ILE B 286    13049   8965   7308   -262   -783   2027       C  
ATOM   5845  C   ILE B 286      31.996  17.300 125.404  1.00 77.25           C  
ANISOU 5845  C   ILE B 286    13084   8922   7344   -235   -795   1985       C  
ATOM   5846  O   ILE B 286      30.922  16.921 124.931  1.00 77.88           O  
ANISOU 5846  O   ILE B 286    13181   9020   7387   -310   -859   2037       O  
ATOM   5847  CB  ILE B 286      33.892  17.965 123.856  1.00 77.84           C  
ANISOU 5847  CB  ILE B 286    13198   9104   7271   -316   -713   1912       C  
ATOM   5848  CG1 ILE B 286      34.462  19.123 123.030  1.00 78.50           C  
ANISOU 5848  CG1 ILE B 286    13262   9264   7300   -382   -718   1974       C  
ATOM   5849  CG2 ILE B 286      33.419  16.848 122.923  1.00 78.71           C  
ANISOU 5849  CG2 ILE B 286    13379   9260   7266   -431   -725   1857       C  
ATOM   5850  CD1 ILE B 286      35.785  18.820 122.355  1.00 79.24           C  
ANISOU 5850  CD1 ILE B 286    13401   9413   7294   -421   -627   1842       C  
ATOM   5851  N   VAL B 287      32.563  16.736 126.474  1.00 76.83           N  
ANISOU 5851  N   VAL B 287    13032   8805   7353   -138   -743   1903       N  
ATOM   5852  CA  VAL B 287      31.894  15.624 127.185  1.00 76.88           C  
ANISOU 5852  CA  VAL B 287    13059   8760   7390   -119   -765   1877       C  
ATOM   5853  C   VAL B 287      30.573  16.054 127.862  1.00 76.79           C  
ANISOU 5853  C   VAL B 287    12991   8738   7448   -117   -824   1974       C  
ATOM   5854  O   VAL B 287      29.592  15.284 127.848  1.00 77.38           O  
ANISOU 5854  O   VAL B 287    13087   8804   7507   -158   -870   1990       O  
ATOM   5855  CB  VAL B 287      32.839  14.854 128.155  1.00 76.24           C  
ANISOU 5855  CB  VAL B 287    12988   8612   7365    -38   -715   1785       C  
ATOM   5856  CG1 VAL B 287      33.358  15.728 129.278  1.00 75.38           C  
ANISOU 5856  CG1 VAL B 287    12818   8485   7337     42   -686   1808       C  
ATOM   5857  CG2 VAL B 287      32.149  13.618 128.730  1.00 76.42           C  
ANISOU 5857  CG2 VAL B 287    13036   8586   7412    -44   -755   1772       C  
ATOM   5858  N   TYR B 288      30.530  17.276 128.411  1.00 76.49           N  
ANISOU 5858  N   TYR B 288    12870   8697   7493    -76   -819   2028       N  
ATOM   5859  CA  TYR B 288      29.259  17.819 128.937  1.00 76.58           C  
ANISOU 5859  CA  TYR B 288    12805   8696   7596    -84   -866   2103       C  
ATOM   5860  C   TYR B 288      28.172  17.853 127.856  1.00 77.77           C  
ANISOU 5860  C   TYR B 288    12959   8872   7715   -176   -949   2190       C  
ATOM   5861  O   TYR B 288      27.034  17.446 128.099  1.00 77.40           O  
ANISOU 5861  O   TYR B 288    12899   8812   7698   -203   -994   2220       O  
ATOM   5862  CB  TYR B 288      29.414  19.237 129.517  1.00 76.34           C  
ANISOU 5862  CB  TYR B 288    12667   8653   7684    -36   -842   2133       C  
ATOM   5863  CG  TYR B 288      30.344  19.381 130.709  1.00 75.99           C  
ANISOU 5863  CG  TYR B 288    12601   8592   7677     40   -765   2058       C  
ATOM   5864  CD1 TYR B 288      30.363  18.440 131.741  1.00 75.38           C  
ANISOU 5864  CD1 TYR B 288    12551   8503   7585     57   -742   2002       C  
ATOM   5865  CD2 TYR B 288      31.189  20.487 130.821  1.00 76.21           C  
ANISOU 5865  CD2 TYR B 288    12577   8620   7757     85   -723   2056       C  
ATOM   5866  CE1 TYR B 288      31.213  18.582 132.825  1.00 74.65           C  
ANISOU 5866  CE1 TYR B 288    12437   8406   7520    106   -684   1950       C  
ATOM   5867  CE2 TYR B 288      32.041  20.637 131.904  1.00 75.48           C  
ANISOU 5867  CE2 TYR B 288    12465   8520   7694    146   -654   1992       C  
ATOM   5868  CZ  TYR B 288      32.051  19.678 132.902  1.00 74.90           C  
ANISOU 5868  CZ  TYR B 288    12420   8441   7595    151   -637   1942       C  
ATOM   5869  OH  TYR B 288      32.892  19.825 133.975  1.00 75.40           O  
ANISOU 5869  OH  TYR B 288    12463   8506   7678    190   -582   1894       O  
ATOM   5870  N   ALA B 289      28.535  18.337 126.670  1.00 79.32           N  
ANISOU 5870  N   ALA B 289    13175   9113   7850   -236   -972   2237       N  
ATOM   5871  CA  ALA B 289      27.602  18.450 125.546  1.00 80.98           C  
ANISOU 5871  CA  ALA B 289    13389   9360   8017   -348  -1065   2341       C  
ATOM   5872  C   ALA B 289      27.070  17.089 125.102  1.00 82.11           C  
ANISOU 5872  C   ALA B 289    13621   9525   8051   -412  -1084   2302       C  
ATOM   5873  O   ALA B 289      25.871  16.936 124.861  1.00 82.63           O  
ANISOU 5873  O   ALA B 289    13671   9590   8132   -470  -1160   2377       O  
ATOM   5874  CB  ALA B 289      28.266  19.158 124.376  1.00 81.47           C  
ANISOU 5874  CB  ALA B 289    13464   9487   8004   -424  -1084   2395       C  
ATOM   5875  N   PHE B 290      27.966  16.111 124.995  1.00 83.14           N  
ANISOU 5875  N   PHE B 290    13834   9665   8089   -402  -1017   2180       N  
ATOM   5876  CA  PHE B 290      27.583  14.747 124.622  1.00 84.86           C  
ANISOU 5876  CA  PHE B 290    14130   9889   8222   -456  -1025   2119       C  
ATOM   5877  C   PHE B 290      26.756  14.044 125.703  1.00 85.96           C  
ANISOU 5877  C   PHE B 290    14257   9966   8437   -402  -1043   2113       C  
ATOM   5878  O   PHE B 290      25.712  13.464 125.391  1.00 86.43           O  
ANISOU 5878  O   PHE B 290    14337  10032   8468   -464  -1101   2149       O  
ATOM   5879  CB  PHE B 290      28.812  13.897 124.261  1.00 85.03           C  
ANISOU 5879  CB  PHE B 290    14220   9917   8168   -455   -943   1973       C  
ATOM   5880  CG  PHE B 290      29.250  14.039 122.828  1.00 85.77           C  
ANISOU 5880  CG  PHE B 290    14356  10105   8126   -578   -932   1952       C  
ATOM   5881  CD1 PHE B 290      28.454  13.554 121.797  1.00 86.58           C  
ANISOU 5881  CD1 PHE B 290    14503  10274   8119   -716   -982   1977       C  
ATOM   5882  CD2 PHE B 290      30.463  14.648 122.507  1.00 85.76           C  
ANISOU 5882  CD2 PHE B 290    14350  10139   8095   -572   -869   1906       C  
ATOM   5883  CE1 PHE B 290      28.854  13.678 120.472  1.00 87.82           C  
ANISOU 5883  CE1 PHE B 290    14699  10541   8127   -861   -969   1955       C  
ATOM   5884  CE2 PHE B 290      30.867  14.775 121.186  1.00 86.78           C  
ANISOU 5884  CE2 PHE B 290    14516  10374   8081   -710   -854   1881       C  
ATOM   5885  CZ  PHE B 290      30.061  14.289 120.166  1.00 87.93           C  
ANISOU 5885  CZ  PHE B 290    14705  10596   8106   -863   -903   1905       C  
ATOM   5886  N   ARG B 291      27.208  14.103 126.960  1.00 86.77           N  
ANISOU 5886  N   ARG B 291    14324  10015   8627   -301   -998   2073       N  
ATOM   5887  CA  ARG B 291      26.573  13.311 128.033  1.00 87.53           C  
ANISOU 5887  CA  ARG B 291    14415  10067   8773   -270  -1012   2059       C  
ATOM   5888  C   ARG B 291      25.478  14.030 128.833  1.00 89.10           C  
ANISOU 5888  C   ARG B 291    14527  10260   9066   -261  -1044   2133       C  
ATOM   5889  O   ARG B 291      24.398  13.467 129.040  1.00 89.46           O  
ANISOU 5889  O   ARG B 291    14573  10299   9118   -297  -1089   2159       O  
ATOM   5890  CB  ARG B 291      27.634  12.750 128.981  1.00 86.77           C  
ANISOU 5890  CB  ARG B 291    14333   9925   8708   -197   -958   1976       C  
ATOM   5891  CG  ARG B 291      28.551  11.740 128.314  1.00 87.08           C  
ANISOU 5891  CG  ARG B 291    14445   9944   8696   -207   -930   1881       C  
ATOM   5892  CD  ARG B 291      29.431  11.036 129.321  1.00 86.92           C  
ANISOU 5892  CD  ARG B 291    14426   9856   8742   -142   -904   1820       C  
ATOM   5893  NE  ARG B 291      28.669  10.142 130.194  1.00 87.15           N  
ANISOU 5893  NE  ARG B 291    14458   9848   8806   -152   -956   1847       N  
ATOM   5894  CZ  ARG B 291      28.236   8.925 129.867  1.00 87.83           C  
ANISOU 5894  CZ  ARG B 291    14590   9899   8881   -193   -996   1819       C  
ATOM   5895  NH1 ARG B 291      28.454   8.410 128.655  1.00 89.13           N  
ANISOU 5895  NH1 ARG B 291    14801  10064   8998   -233   -980   1748       N  
ATOM   5896  NH2 ARG B 291      27.565   8.207 130.771  1.00 87.49           N  
ANISOU 5896  NH2 ARG B 291    14542   9826   8872   -206  -1049   1859       N  
ATOM   5897  N   ILE B 292      25.755  15.255 129.283  1.00 90.76           N  
ANISOU 5897  N   ILE B 292    14655  10469   9358   -217  -1015   2155       N  
ATOM   5898  CA  ILE B 292      24.826  15.992 130.157  1.00 92.12           C  
ANISOU 5898  CA  ILE B 292    14721  10629   9650   -206  -1023   2189       C  
ATOM   5899  C   ILE B 292      23.755  16.723 129.338  1.00 95.24           C  
ANISOU 5899  C   ILE B 292    15055  11024  10105   -261  -1096   2288       C  
ATOM   5900  O   ILE B 292      24.053  17.674 128.613  1.00 94.69           O  
ANISOU 5900  O   ILE B 292    14950  10959  10065   -270  -1116   2345       O  
ATOM   5901  CB  ILE B 292      25.552  16.981 131.102  1.00 90.84           C  
ANISOU 5901  CB  ILE B 292    14481  10459   9574   -140   -954   2152       C  
ATOM   5902  CG1 ILE B 292      26.647  16.250 131.894  1.00 89.84           C  
ANISOU 5902  CG1 ILE B 292    14412  10331   9390    -99   -898   2075       C  
ATOM   5903  CG2 ILE B 292      24.549  17.633 132.056  1.00 90.79           C  
ANISOU 5903  CG2 ILE B 292    14355  10443   9698   -145   -945   2152       C  
ATOM   5904  CD1 ILE B 292      27.353  17.085 132.941  1.00 89.21           C  
ANISOU 5904  CD1 ILE B 292    14263  10254   9376    -48   -830   2034       C  
ATOM   5905  N   GLN B 293      22.513  16.258 129.486  1.00 99.76           N  
ANISOU 5905  N   GLN B 293    15610  11589  10702   -303  -1144   2316       N  
ATOM   5906  CA  GLN B 293      21.325  16.796 128.786  1.00103.14           C  
ANISOU 5906  CA  GLN B 293    15972  12005  11208   -363  -1229   2418       C  
ATOM   5907  C   GLN B 293      21.065  18.305 128.932  1.00103.41           C  
ANISOU 5907  C   GLN B 293    15859  12001  11430   -342  -1241   2469       C  
ATOM   5908  O   GLN B 293      20.699  18.966 127.960  1.00104.87           O  
ANISOU 5908  O   GLN B 293    16003  12175  11666   -391  -1323   2580       O  
ATOM   5909  CB  GLN B 293      20.071  16.024 129.241  1.00105.54           C  
ANISOU 5909  CB  GLN B 293    16269  12302  11530   -397  -1261   2416       C  
ATOM   5910  CG  GLN B 293      19.738  16.157 130.739  1.00106.31           C  
ANISOU 5910  CG  GLN B 293    16282  12386  11725   -360  -1196   2339       C  
ATOM   5911  CD  GLN B 293      19.000  14.952 131.308  1.00107.38           C  
ANISOU 5911  CD  GLN B 293    16465  12536  11798   -396  -1205   2307       C  
ATOM   5912  OE1 GLN B 293      18.249  14.276 130.602  1.00109.32           O  
ANISOU 5912  OE1 GLN B 293    16761  12783  11992   -448  -1274   2359       O  
ATOM   5913  NE2 GLN B 293      19.207  14.680 132.598  1.00107.56           N  
ANISOU 5913  NE2 GLN B 293    16470  12576  11819   -381  -1140   2227       N  
ATOM   5914  N   LYS B 294      21.249  18.836 130.138  1.00103.37           N  
ANISOU 5914  N   LYS B 294    15767  11974  11533   -281  -1163   2391       N  
ATOM   5915  CA  LYS B 294      20.920  20.236 130.442  1.00103.94           C  
ANISOU 5915  CA  LYS B 294    15675  11995  11822   -258  -1160   2409       C  
ATOM   5916  C   LYS B 294      21.909  21.231 129.828  1.00103.91           C  
ANISOU 5916  C   LYS B 294    15653  11981  11846   -232  -1166   2457       C  
ATOM   5917  O   LYS B 294      21.534  22.360 129.520  1.00104.72           O  
ANISOU 5917  O   LYS B 294    15629  12028  12128   -239  -1216   2529       O  
ATOM   5918  CB  LYS B 294      20.837  20.445 131.959  1.00104.42           C  
ANISOU 5918  CB  LYS B 294    15649  12052  11974   -220  -1059   2283       C  
ATOM   5919  CG  LYS B 294      19.659  19.736 132.617  1.00105.48           C  
ANISOU 5919  CG  LYS B 294    15758  12196  12123   -264  -1058   2242       C  
ATOM   5920  CD  LYS B 294      19.954  19.338 134.059  1.00105.67           C  
ANISOU 5920  CD  LYS B 294    15781  12267  12099   -259   -954   2114       C  
ATOM   5921  CE  LYS B 294      20.720  18.023 134.124  1.00105.43           C  
ANISOU 5921  CE  LYS B 294    15920  12288  11851   -261   -952   2106       C  
ATOM   5922  NZ  LYS B 294      20.963  17.572 135.523  1.00105.33           N  
ANISOU 5922  NZ  LYS B 294    15907  12326  11785   -282   -877   2012       N  
ATOM   5923  N   PHE B 295      23.167  20.817 129.673  1.00103.61           N  
ANISOU 5923  N   PHE B 295    15730  11988  11647   -206  -1118   2417       N  
ATOM   5924  CA  PHE B 295      24.174  21.622 128.966  1.00104.13           C  
ANISOU 5924  CA  PHE B 295    15801  12061  11702   -195  -1124   2463       C  
ATOM   5925  C   PHE B 295      23.929  21.637 127.450  1.00105.37           C  
ANISOU 5925  C   PHE B 295    16003  12244  11788   -287  -1233   2595       C  
ATOM   5926  O   PHE B 295      24.084  22.679 126.801  1.00106.25           O  
ANISOU 5926  O   PHE B 295    16049  12340  11979   -314  -1291   2693       O  
ATOM   5927  CB  PHE B 295      25.598  21.120 129.266  1.00102.86           C  
ANISOU 5927  CB  PHE B 295    15744  11941  11397   -143  -1034   2369       C  
ATOM   5928  CG  PHE B 295      26.154  21.591 130.588  1.00101.86           C  
ANISOU 5928  CG  PHE B 295    15551  11796  11352    -66   -938   2273       C  
ATOM   5929  CD1 PHE B 295      26.395  22.945 130.817  1.00101.92           C  
ANISOU 5929  CD1 PHE B 295    15439  11769  11515    -31   -919   2283       C  
ATOM   5930  CD2 PHE B 295      26.469  20.680 131.595  1.00101.18           C  
ANISOU 5930  CD2 PHE B 295    15521  11731  11190    -41   -872   2176       C  
ATOM   5931  CE1 PHE B 295      26.917  23.381 132.028  1.00101.01           C  
ANISOU 5931  CE1 PHE B 295    15264  11649  11465     25   -824   2184       C  
ATOM   5932  CE2 PHE B 295      26.990  21.110 132.809  1.00100.57           C  
ANISOU 5932  CE2 PHE B 295    15385  11655  11169      4   -789   2095       C  
ATOM   5933  CZ  PHE B 295      27.217  22.461 133.026  1.00100.37           C  
ANISOU 5933  CZ  PHE B 295    15245  11604  11285     37   -758   2091       C  
ATOM   5934  N   ARG B 296      23.565  20.477 126.899  1.00105.81           N  
ANISOU 5934  N   ARG B 296    16169  12343  11691   -348  -1265   2599       N  
ATOM   5935  CA  ARG B 296      23.249  20.329 125.471  1.00107.20           C  
ANISOU 5935  CA  ARG B 296    16398  12565  11766   -466  -1365   2713       C  
ATOM   5936  C   ARG B 296      22.140  21.277 125.018  1.00108.59           C  
ANISOU 5936  C   ARG B 296    16449  12695  12115   -526  -1488   2868       C  
ATOM   5937  O   ARG B 296      22.287  21.958 123.999  1.00110.73           O  
ANISOU 5937  O   ARG B 296    16703  12989  12379   -608  -1574   2995       O  
ATOM   5938  CB  ARG B 296      22.860  18.874 125.163  1.00108.15           C  
ANISOU 5938  CB  ARG B 296    16639  12729  11724   -518  -1369   2669       C  
ATOM   5939  CG  ARG B 296      22.285  18.618 123.778  1.00110.04           C  
ANISOU 5939  CG  ARG B 296    16927  13025  11856   -660  -1474   2780       C  
ATOM   5940  CD  ARG B 296      22.297  17.132 123.463  1.00111.37           C  
ANISOU 5940  CD  ARG B 296    17228  13243  11843   -703  -1444   2692       C  
ATOM   5941  NE  ARG B 296      23.541  16.706 122.823  1.00112.80           N  
ANISOU 5941  NE  ARG B 296    17508  13491  11858   -734  -1379   2606       N  
ATOM   5942  CZ  ARG B 296      23.778  15.477 122.356  1.00113.93           C  
ANISOU 5942  CZ  ARG B 296    17759  13677  11850   -785  -1343   2510       C  
ATOM   5943  NH1 ARG B 296      22.873  14.502 122.474  1.00114.24           N  
ANISOU 5943  NH1 ARG B 296    17832  13701  11870   -807  -1370   2495       N  
ATOM   5944  NH2 ARG B 296      24.944  15.215 121.771  1.00114.51           N  
ANISOU 5944  NH2 ARG B 296    17900  13807  11801   -816  -1274   2417       N  
ATOM   5945  N   VAL B 297      21.043  21.317 125.777  1.00108.33           N  
ANISOU 5945  N   VAL B 297    16320  12596  12242   -495  -1501   2860       N  
ATOM   5946  CA  VAL B 297      19.906  22.193 125.456  1.00109.79           C  
ANISOU 5946  CA  VAL B 297    16360  12711  12643   -542  -1620   2997       C  
ATOM   5947  C   VAL B 297      20.283  23.680 125.584  1.00110.47           C  
ANISOU 5947  C   VAL B 297    16302  12728  12942   -503  -1636   3048       C  
ATOM   5948  O   VAL B 297      19.815  24.506 124.794  1.00112.21           O  
ANISOU 5948  O   VAL B 297    16430  12906  13295   -575  -1767   3211       O  
ATOM   5949  CB  VAL B 297      18.648  21.843 126.296  1.00109.23           C  
ANISOU 5949  CB  VAL B 297    16211  12584  12706   -518  -1613   2949       C  
ATOM   5950  CG1 VAL B 297      18.767  22.330 127.731  1.00108.83           C  
ANISOU 5950  CG1 VAL B 297    16052  12481  12818   -414  -1496   2808       C  
ATOM   5951  CG2 VAL B 297      17.390  22.405 125.645  1.00110.57           C  
ANISOU 5951  CG2 VAL B 297    16261  12690  13060   -596  -1760   3107       C  
ATOM   5952  N   THR B 298      21.146  24.004 126.547  1.00109.33           N  
ANISOU 5952  N   THR B 298    16136  12571  12831   -400  -1512   2918       N  
ATOM   5953  CA  THR B 298      21.617  25.375 126.745  1.00110.12           C  
ANISOU 5953  CA  THR B 298    16104  12607  13129   -355  -1510   2942       C  
ATOM   5954  C   THR B 298      22.580  25.834 125.639  1.00111.66           C  
ANISOU 5954  C   THR B 298    16360  12851  13213   -411  -1569   3054       C  
ATOM   5955  O   THR B 298      22.360  26.898 125.037  1.00113.08           O  
ANISOU 5955  O   THR B 298    16428  12977  13561   -459  -1681   3201       O  
ATOM   5956  CB  THR B 298      22.289  25.538 128.123  1.00108.68           C  
ANISOU 5956  CB  THR B 298    15889  12411  12991   -242  -1354   2762       C  
ATOM   5957  OG1 THR B 298      21.410  25.041 129.143  1.00108.33           O  
ANISOU 5957  OG1 THR B 298    15797  12347  13015   -218  -1295   2654       O  
ATOM   5958  CG2 THR B 298      22.612  26.999 128.411  1.00109.06           C  
ANISOU 5958  CG2 THR B 298    15776  12379  13282   -195  -1348   2773       C  
ATOM   5959  N   PHE B 299      23.618  25.035 125.357  1.00112.05           N  
ANISOU 5959  N   PHE B 299    16576  13001  12995   -416  -1499   2987       N  
ATOM   5960  CA  PHE B 299      24.617  25.390 124.317  1.00113.18           C  
ANISOU 5960  CA  PHE B 299    16786  13214  13003   -483  -1534   3066       C  
ATOM   5961  C   PHE B 299      23.964  25.709 122.964  1.00116.44           C  
ANISOU 5961  C   PHE B 299    17183  13652  13407   -639  -1705   3272       C  
ATOM   5962  O   PHE B 299      24.351  26.676 122.286  1.00117.03           O  
ANISOU 5962  O   PHE B 299    17206  13730  13531   -701  -1785   3401       O  
ATOM   5963  CB  PHE B 299      25.669  24.280 124.101  1.00111.71           C  
ANISOU 5963  CB  PHE B 299    16779  13132  12533   -485  -1436   2947       C  
ATOM   5964  CG  PHE B 299      26.518  23.951 125.313  1.00109.65           C  
ANISOU 5964  CG  PHE B 299    16545  12855  12261   -351  -1286   2770       C  
ATOM   5965  CD1 PHE B 299      26.790  24.887 126.316  1.00108.95           C  
ANISOU 5965  CD1 PHE B 299    16341  12697  12355   -250  -1231   2725       C  
ATOM   5966  CD2 PHE B 299      27.078  22.681 125.429  1.00108.46           C  
ANISOU 5966  CD2 PHE B 299    16530  12759  11920   -336  -1205   2648       C  
ATOM   5967  CE1 PHE B 299      27.582  24.550 127.408  1.00107.54           C  
ANISOU 5967  CE1 PHE B 299    16194  12520  12146   -150  -1103   2575       C  
ATOM   5968  CE2 PHE B 299      27.871  22.343 126.516  1.00107.45           C  
ANISOU 5968  CE2 PHE B 299    16425  12615  11786   -229  -1089   2509       C  
ATOM   5969  CZ  PHE B 299      28.123  23.278 127.509  1.00106.81           C  
ANISOU 5969  CZ  PHE B 299    16239  12481  11864   -141  -1040   2478       C  
ATOM   5970  N   LEU B 300      22.979  24.892 122.585  1.00118.49           N  
ANISOU 5970  N   LEU B 300    17485  13933  13601   -713  -1766   3311       N  
ATOM   5971  CA  LEU B 300      22.147  25.155 121.407  1.00121.08           C  
ANISOU 5971  CA  LEU B 300    17783  14280  13941   -873  -1942   3519       C  
ATOM   5972  C   LEU B 300      21.459  26.516 121.494  1.00122.71           C  
ANISOU 5972  C   LEU B 300    17786  14357  14480   -870  -2066   3672       C  
ATOM   5973  O   LEU B 300      21.460  27.271 120.517  1.00124.54           O  
ANISOU 5973  O   LEU B 300    17972  14601  14745   -993  -2210   3866       O  
ATOM   5974  CB  LEU B 300      21.087  24.061 121.232  1.00121.82           C  
ANISOU 5974  CB  LEU B 300    17937  14397  13951   -930  -1976   3516       C  
ATOM   5975  CG  LEU B 300      21.593  22.683 120.791  1.00121.59           C  
ANISOU 5975  CG  LEU B 300    18100  14494  13603   -982  -1897   3404       C  
ATOM   5976  CD1 LEU B 300      20.521  21.625 121.012  1.00121.38           C  
ANISOU 5976  CD1 LEU B 300    18111  14458  13549   -989  -1905   3366       C  
ATOM   5977  CD2 LEU B 300      22.043  22.697 119.336  1.00122.78           C  
ANISOU 5977  CD2 LEU B 300    18335  14774  13540  -1168  -1975   3514       C  
ATOM   5978  N   LYS B 301      20.880  26.823 122.659  1.00123.14           N  
ANISOU 5978  N   LYS B 301    17710  14289  14786   -742  -2012   3582       N  
ATOM   5979  CA  LYS B 301      20.178  28.096 122.854  1.00124.32           C  
ANISOU 5979  CA  LYS B 301    17639  14292  15306   -726  -2113   3692       C  
ATOM   5980  C   LYS B 301      21.126  29.288 122.767  1.00124.03           C  
ANISOU 5980  C   LYS B 301    17527  14221  15378   -703  -2124   3742       C  
ATOM   5981  O   LYS B 301      20.811  30.279 122.108  1.00125.32           O  
ANISOU 5981  O   LYS B 301    17563  14313  15737   -781  -2285   3939       O  
ATOM   5982  CB  LYS B 301      19.417  28.118 124.190  1.00124.13           C  
ANISOU 5982  CB  LYS B 301    17487  14157  15517   -602  -2020   3538       C  
ATOM   5983  CG  LYS B 301      18.430  29.273 124.326  1.00125.83           C  
ANISOU 5983  CG  LYS B 301    17454  14205  16148   -600  -2131   3637       C  
ATOM   5984  CD  LYS B 301      17.227  28.913 125.203  1.00126.03           C  
ANISOU 5984  CD  LYS B 301    17380  14155  16348   -552  -2085   3525       C  
ATOM   5985  CE  LYS B 301      16.208  28.075 124.438  1.00126.81           C  
ANISOU 5985  CE  LYS B 301    17544  14291  16347   -659  -2204   3646       C  
ATOM   5986  NZ  LYS B 301      15.341  27.261 125.337  1.00126.30           N  
ANISOU 5986  NZ  LYS B 301    17472  14217  16297   -611  -2110   3491       N  
ATOM   5987  N   ILE B 302      22.290  29.176 123.408  1.00122.21           N  
ANISOU 5987  N   ILE B 302    17372  14037  15023   -603  -1963   3576       N  
ATOM   5988  CA  ILE B 302      23.315  30.226 123.339  1.00121.95           C  
ANISOU 5988  CA  ILE B 302    17288  13986  15060   -577  -1957   3608       C  
ATOM   5989  C   ILE B 302      23.814  30.383 121.894  1.00123.14           C  
ANISOU 5989  C   ILE B 302    17523  14238  15025   -738  -2086   3799       C  
ATOM   5990  O   ILE B 302      23.930  31.514 121.400  1.00124.12           O  
ANISOU 5990  O   ILE B 302    17534  14307  15316   -792  -2207   3963       O  
ATOM   5991  CB  ILE B 302      24.493  29.957 124.311  1.00120.17           C  
ANISOU 5991  CB  ILE B 302    17142  13803  14712   -446  -1757   3389       C  
ATOM   5992  CG1 ILE B 302      24.012  30.027 125.769  1.00119.07           C  
ANISOU 5992  CG1 ILE B 302    16892  13571  14776   -317  -1641   3215       C  
ATOM   5993  CG2 ILE B 302      25.626  30.964 124.100  1.00120.38           C  
ANISOU 5993  CG2 ILE B 302    17138  13829  14770   -433  -1755   3430       C  
ATOM   5994  CD1 ILE B 302      24.922  29.325 126.757  1.00117.13           C  
ANISOU 5994  CD1 ILE B 302    16757  13393  14351   -219  -1455   3004       C  
ATOM   5995  N   TRP B 303      24.084  29.256 121.227  1.00123.86           N  
ANISOU 5995  N   TRP B 303    17803  14477  14781   -825  -2061   3775       N  
ATOM   5996  CA  TRP B 303      24.500  29.256 119.813  1.00125.60           C  
ANISOU 5996  CA  TRP B 303    18115  14826  14781  -1013  -2169   3933       C  
ATOM   5997  C   TRP B 303      23.475  29.965 118.930  1.00127.44           C  
ANISOU 5997  C   TRP B 303    18229  15010  15180  -1166  -2401   4205       C  
ATOM   5998  O   TRP B 303      23.813  30.934 118.235  1.00129.45           O  
ANISOU 5998  O   TRP B 303    18420  15269  15495  -1266  -2525   4384       O  
ATOM   5999  CB  TRP B 303      24.723  27.821 119.309  1.00125.81           C  
ANISOU 5999  CB  TRP B 303    18342  15006  14453  -1088  -2095   3832       C  
ATOM   6000  CG  TRP B 303      25.111  27.721 117.847  1.00127.32           C  
ANISOU 6000  CG  TRP B 303    18631  15355  14388  -1309  -2187   3963       C  
ATOM   6001  CD1 TRP B 303      26.157  28.352 117.227  1.00127.84           C  
ANISOU 6001  CD1 TRP B 303    18719  15502  14352  -1390  -2198   4019       C  
ATOM   6002  CD2 TRP B 303      24.466  26.933 116.837  1.00128.59           C  
ANISOU 6002  CD2 TRP B 303    18880  15627  14349  -1494  -2273   4045       C  
ATOM   6003  NE1 TRP B 303      26.198  28.009 115.897  1.00129.17           N  
ANISOU 6003  NE1 TRP B 303    18982  15834  14261  -1625  -2282   4127       N  
ATOM   6004  CE2 TRP B 303      25.173  27.140 115.629  1.00129.71           C  
ANISOU 6004  CE2 TRP B 303    19093  15924  14265  -1695  -2329   4143       C  
ATOM   6005  CE3 TRP B 303      23.358  26.072 116.833  1.00128.85           C  
ANISOU 6005  CE3 TRP B 303    18938  15650  14366  -1520  -2306   4042       C  
ATOM   6006  CZ2 TRP B 303      24.810  26.515 114.428  1.00130.89           C  
ANISOU 6006  CZ2 TRP B 303    19337  16228  14166  -1931  -2412   4230       C  
ATOM   6007  CZ3 TRP B 303      22.995  25.448 115.634  1.00129.77           C  
ANISOU 6007  CZ3 TRP B 303    19150  15907  14246  -1740  -2393   4134       C  
ATOM   6008  CH2 TRP B 303      23.722  25.676 114.450  1.00130.89           C  
ANISOU 6008  CH2 TRP B 303    19361  16211  14159  -1948  -2443   4223       C  
ATOM   6009  N   ASN B 304      22.229  29.491 118.993  1.00127.31           N  
ANISOU 6009  N   ASN B 304    18176  14944  15250  -1185  -2465   4240       N  
ATOM   6010  CA  ASN B 304      21.119  30.056 118.210  1.00128.60           C  
ANISOU 6010  CA  ASN B 304    18218  15048  15596  -1329  -2697   4502       C  
ATOM   6011  C   ASN B 304      20.886  31.540 118.521  1.00129.60           C  
ANISOU 6011  C   ASN B 304    18111  14993  16136  -1278  -2806   4630       C  
ATOM   6012  O   ASN B 304      20.799  32.359 117.605  1.00131.02           O  
ANISOU 6012  O   ASN B 304    18214  15163  16403  -1428  -3001   4881       O  
ATOM   6013  CB  ASN B 304      19.824  29.268 118.465  1.00128.17           C  
ANISOU 6013  CB  ASN B 304    18151  14949  15598  -1320  -2718   4478       C  
ATOM   6014  CG  ASN B 304      18.787  29.466 117.373  1.00130.40           C  
ANISOU 6014  CG  ASN B 304    18375  15230  15940  -1518  -2957   4753       C  
ATOM   6015  OD1 ASN B 304      18.460  30.592 117.001  1.00131.59           O  
ANISOU 6015  OD1 ASN B 304    18360  15279  16357  -1584  -3135   4968       O  
ATOM   6016  ND2 ASN B 304      18.252  28.362 116.862  1.00130.88           N  
ANISOU 6016  ND2 ASN B 304    18564  15398  15765  -1620  -2971   4752       N  
ATOM   6017  N   ASP B 305      20.794  31.876 119.807  1.00128.27           N  
ANISOU 6017  N   ASP B 305    17825  14685  16224  -1081  -2681   4456       N  
ATOM   6018  CA  ASP B 305      20.483  33.250 120.223  1.00128.39           C  
ANISOU 6018  CA  ASP B 305    17595  14507  16679  -1019  -2764   4535       C  
ATOM   6019  C   ASP B 305      21.640  34.247 120.064  1.00128.58           C  
ANISOU 6019  C   ASP B 305    17588  14530  16736  -1013  -2769   4584       C  
ATOM   6020  O   ASP B 305      21.382  35.442 119.898  1.00130.24           O  
ANISOU 6020  O   ASP B 305    17602  14598  17285  -1036  -2916   4747       O  
ATOM   6021  CB  ASP B 305      19.966  33.284 121.669  1.00126.56           C  
ANISOU 6021  CB  ASP B 305    17238  14139  16711   -831  -2615   4307       C  
ATOM   6022  CG  ASP B 305      18.653  32.535 121.845  1.00125.91           C  
ANISOU 6022  CG  ASP B 305    17132  14022  16683   -843  -2640   4287       C  
ATOM   6023  OD1 ASP B 305      18.251  31.780 120.931  1.00125.69           O  
ANISOU 6023  OD1 ASP B 305    17226  14097  16433   -978  -2739   4413       O  
ATOM   6024  OD2 ASP B 305      18.024  32.697 122.911  1.00125.20           O  
ANISOU 6024  OD2 ASP B 305    16901  13811  16855   -725  -2552   4134       O  
ATOM   6025  N   HIS B 306      22.893  33.781 120.119  1.00126.25           N  
ANISOU 6025  N   HIS B 306    17471  14380  16118   -982  -2617   4447       N  
ATOM   6026  CA  HIS B 306      24.047  34.699 120.056  1.00125.18           C  
ANISOU 6026  CA  HIS B 306    17310  14247  16005   -964  -2602   4471       C  
ATOM   6027  C   HIS B 306      25.083  34.420 118.951  1.00125.39           C  
ANISOU 6027  C   HIS B 306    17517  14470  15655  -1116  -2626   4557       C  
ATOM   6028  O   HIS B 306      25.537  35.367 118.305  1.00127.11           O  
ANISOU 6028  O   HIS B 306    17673  14685  15935  -1211  -2750   4735       O  
ATOM   6029  CB  HIS B 306      24.727  34.784 121.428  1.00122.93           C  
ANISOU 6029  CB  HIS B 306    17007  13910  15791   -753  -2379   4201       C  
ATOM   6030  CG  HIS B 306      23.844  35.344 122.504  1.00122.48           C  
ANISOU 6030  CG  HIS B 306    16738  13661  16137   -626  -2352   4112       C  
ATOM   6031  ND1 HIS B 306      23.916  36.656 122.920  1.00122.96           N  
ANISOU 6031  ND1 HIS B 306    16588  13563  16565   -563  -2386   4137       N  
ATOM   6032  CD2 HIS B 306      22.866  34.769 123.243  1.00121.75           C  
ANISOU 6032  CD2 HIS B 306    16603  13514  16142   -561  -2288   3986       C  
ATOM   6033  CE1 HIS B 306      23.024  36.864 123.873  1.00122.75           C  
ANISOU 6033  CE1 HIS B 306    16394  13392  16850   -466  -2334   4014       C  
ATOM   6034  NE2 HIS B 306      22.373  35.735 124.088  1.00121.95           N  
ANISOU 6034  NE2 HIS B 306    16393  13357  16586   -466  -2275   3924       N  
ATOM   6035  N   PHE B 307      25.451  33.154 118.726  1.00124.27           N  
ANISOU 6035  N   PHE B 307    17584  14494  15138  -1148  -2511   4428       N  
ATOM   6036  CA  PHE B 307      26.540  32.811 117.781  1.00123.77           C  
ANISOU 6036  CA  PHE B 307    17690  14625  14710  -1284  -2488   4445       C  
ATOM   6037  C   PHE B 307      26.064  32.175 116.461  1.00125.71           C  
ANISOU 6037  C   PHE B 307    18038  15021  14702  -1527  -2619   4601       C  
ATOM   6038  O   PHE B 307      26.832  31.490 115.779  1.00124.55           O  
ANISOU 6038  O   PHE B 307    18057  15057  14206  -1639  -2550   4538       O  
ATOM   6039  CB  PHE B 307      27.566  31.908 118.478  1.00120.82           C  
ANISOU 6039  CB  PHE B 307    17468  14331  14107  -1148  -2243   4158       C  
ATOM   6040  CG  PHE B 307      28.387  32.615 119.512  1.00118.30           C  
ANISOU 6040  CG  PHE B 307    17076  13920  13952   -965  -2123   4031       C  
ATOM   6041  CD1 PHE B 307      29.584  33.228 119.165  1.00117.46           C  
ANISOU 6041  CD1 PHE B 307    16994  13875  13757   -995  -2103   4053       C  
ATOM   6042  CD2 PHE B 307      27.970  32.663 120.837  1.00117.09           C  
ANISOU 6042  CD2 PHE B 307    16829  13629  14029   -777  -2025   3884       C  
ATOM   6043  CE1 PHE B 307      30.351  33.881 120.121  1.00116.43           C  
ANISOU 6043  CE1 PHE B 307    16798  13662  13775   -830  -1991   3935       C  
ATOM   6044  CE2 PHE B 307      28.729  33.313 121.797  1.00115.90           C  
ANISOU 6044  CE2 PHE B 307    16611  13406  14016   -626  -1910   3760       C  
ATOM   6045  CZ  PHE B 307      29.922  33.924 121.440  1.00115.61           C  
ANISOU 6045  CZ  PHE B 307    16603  13424  13899   -647  -1895   3789       C  
ATOM   6046  N   ARG B 308      24.810  32.431 116.090  1.00128.51           N  
ANISOU 6046  N   ARG B 308    18287  15300  15242  -1620  -2807   4800       N  
ATOM   6047  CA  ARG B 308      24.241  31.888 114.859  1.00131.91           C  
ANISOU 6047  CA  ARG B 308    18799  15868  15451  -1866  -2950   4969       C  
ATOM   6048  C   ARG B 308      24.564  32.804 113.678  1.00135.02           C  
ANISOU 6048  C   ARG B 308    19156  16342  15801  -2102  -3149   5248       C  
ATOM   6049  O   ARG B 308      24.580  34.034 113.822  1.00136.19           O  
ANISOU 6049  O   ARG B 308    19139  16358  16250  -2075  -3266   5400       O  
ATOM   6050  CB  ARG B 308      22.724  31.724 115.003  1.00133.24           C  
ANISOU 6050  CB  ARG B 308    18865  15917  15840  -1866  -3072   5067       C  
ATOM   6051  CG  ARG B 308      22.096  30.717 114.051  1.00134.57           C  
ANISOU 6051  CG  ARG B 308    19161  16236  15734  -2066  -3143   5139       C  
ATOM   6052  CD  ARG B 308      22.506  29.287 114.383  1.00133.31           C  
ANISOU 6052  CD  ARG B 308    19193  16191  15267  -1990  -2918   4852       C  
ATOM   6053  NE  ARG B 308      21.582  28.304 113.813  1.00134.28           N  
ANISOU 6053  NE  ARG B 308    19394  16392  15231  -2121  -2975   4888       N  
ATOM   6054  CZ  ARG B 308      21.519  27.954 112.524  1.00135.81           C  
ANISOU 6054  CZ  ARG B 308    19683  16767  15149  -2390  -3081   5022       C  
ATOM   6055  NH1 ARG B 308      22.331  28.496 111.614  1.00137.50           N  
ANISOU 6055  NH1 ARG B 308    19931  17117  15196  -2576  -3144   5140       N  
ATOM   6056  NH2 ARG B 308      20.629  27.044 112.137  1.00135.93           N  
ANISOU 6056  NH2 ARG B 308    19762  16838  15045  -2488  -3121   5034       N  
ATOM   6057  N   CYS B 309      24.811  32.196 112.518  1.00137.04           N  
ANISOU 6057  N   CYS B 309    19560  16819  15688  -2346  -3187   5310       N  
ATOM   6058  CA  CYS B 309      25.127  32.935 111.289  1.00139.92           C  
ANISOU 6058  CA  CYS B 309    19913  17308  15941  -2623  -3378   5580       C  
ATOM   6059  C   CYS B 309      23.842  33.504 110.669  1.00141.82           C  
ANISOU 6059  C   CYS B 309    20014  17470  16401  -2793  -3672   5917       C  
ATOM   6060  O   CYS B 309      23.425  33.112 109.580  1.00142.40           O  
ANISOU 6060  O   CYS B 309    20157  17703  16245  -3064  -3805   6079       O  
ATOM   6061  CB  CYS B 309      25.880  32.031 110.301  1.00140.95           C  
ANISOU 6061  CB  CYS B 309    20251  17723  15579  -2841  -3290   5491       C  
ATOM   6062  SG  CYS B 309      26.601  32.879 108.867  1.00144.22           S  
ANISOU 6062  SG  CYS B 309    20679  18342  15775  -3195  -3467   5760       S  
TER    6063      CYS B 309                                                      
HETATM 6064  O4  DU1 A1201      52.632  56.381 141.281  1.00 60.89           O  
HETATM 6065  C3  DU1 A1201      53.092  57.489 141.071  1.00 58.99           C  
HETATM 6066  N1  DU1 A1201      54.241  57.935 141.723  1.00 60.21           N  
HETATM 6067  C14 DU1 A1201      54.739  59.205 141.449  1.00 58.78           C  
HETATM 6068  C22 DU1 A1201      54.124  60.036 140.552  1.00 57.54           C  
HETATM 6069  N4  DU1 A1201      54.897  61.167 140.563  1.00 56.77           N  
HETATM 6070  C15 DU1 A1201      55.910  60.971 141.444  1.00 56.90           C  
HETATM 6071  C16 DU1 A1201      56.974  61.968 141.733  1.00 56.94           C  
HETATM 6072  C21 DU1 A1201      56.419  63.357 142.071  1.00 56.59           C  
HETATM 6073  C20 DU1 A1201      57.523  64.320 142.504  1.00 56.46           C  
HETATM 6074  C19 DU1 A1201      58.880  63.915 141.946  1.00 56.42           C  
HETATM 6075  C18 DU1 A1201      58.749  63.350 140.542  1.00 56.71           C  
HETATM 6076  C17 DU1 A1201      57.917  62.069 140.527  1.00 56.73           C  
HETATM 6077  N3  DU1 A1201      55.847  59.780 142.000  1.00 57.84           N  
HETATM 6078  C23 DU1 A1201      52.955  59.668 139.845  1.00 57.21           C  
HETATM 6079  O3  DU1 A1201      52.364  60.373 139.033  1.00 56.07           O  
HETATM 6080  N   DU1 A1201      52.492  58.368 140.164  1.00 57.32           N  
HETATM 6081  C2  DU1 A1201      51.292  57.890 139.453  1.00 55.89           C  
HETATM 6082  C1  DU1 A1201      50.003  58.368 140.053  1.00 55.32           C  
HETATM 6083  C   DU1 A1201      48.813  57.763 139.327  1.00 54.88           C  
HETATM 6084  C4  DU1 A1201      54.903  57.018 142.666  1.00 61.90           C  
HETATM 6085  C5  DU1 A1201      54.273  57.020 144.043  1.00 64.75           C  
HETATM 6086  C6  DU1 A1201      54.879  55.986 144.968  1.00 67.52           C  
HETATM 6087  N2  DU1 A1201      56.038  56.504 145.684  1.00 70.55           N  
HETATM 6088  C7  DU1 A1201      56.350  56.105 146.923  1.00 73.59           C  
HETATM 6089  O2  DU1 A1201      55.669  55.283 147.534  1.00 76.81           O  
HETATM 6090  C8  DU1 A1201      57.554  56.719 147.568  1.00 73.81           C  
HETATM 6091  C13 DU1 A1201      57.962  58.025 147.299  1.00 74.48           C  
HETATM 6092  C12 DU1 A1201      59.067  58.571 147.928  1.00 76.49           C  
HETATM 6093  C11 DU1 A1201      59.769  57.813 148.852  1.00 76.85           C  
HETATM 6094  S   DU1 A1201      61.183  58.480 149.680  1.00 79.44           S  
HETATM 6095  O1  DU1 A1201      61.626  59.622 148.910  1.00 82.41           O  
HETATM 6096  O   DU1 A1201      62.126  57.392 149.841  1.00 79.67           O  
HETATM 6097  C10 DU1 A1201      59.375  56.519 149.147  1.00 75.20           C  
HETATM 6098  C9  DU1 A1201      58.270  55.981 148.511  1.00 74.78           C  
HETATM 6099  C1  OLA A1202      29.207  43.942 135.216  1.00 83.80           C  
HETATM 6100  O1  OLA A1202      28.631  42.972 134.676  1.00 84.55           O  
HETATM 6101  O2  OLA A1202      28.790  44.486 136.263  1.00 84.61           O  
HETATM 6102  C2  OLA A1202      30.459  44.490 134.571  1.00 82.45           C  
HETATM 6103  C3  OLA A1202      31.564  43.442 134.577  1.00 81.35           C  
HETATM 6104  C4  OLA A1202      32.892  44.068 134.175  1.00 80.37           C  
HETATM 6105  C5  OLA A1202      33.910  42.997 133.806  1.00 80.07           C  
HETATM 6106  C6  OLA A1202      35.282  43.613 133.543  1.00 80.62           C  
HETATM 6107  C7  OLA A1202      36.041  42.858 132.456  1.00 81.64           C  
HETATM 6108  C8  OLA A1202      37.312  43.584 132.022  1.00 82.50           C  
HETATM 6109  C9  OLA A1202      38.523  43.032 132.751  1.00 83.24           C  
HETATM 6110  C10 OLA A1202      39.754  43.040 132.225  1.00 84.73           C  
HETATM 6111  C11 OLA A1202      40.036  43.603 130.850  1.00 86.14           C  
HETATM 6112  C12 OLA A1202      41.526  43.571 130.539  1.00 86.32           C  
HETATM 6113  C13 OLA A1202      41.835  44.513 129.380  1.00 86.55           C  
HETATM 6114  C14 OLA A1202      43.114  44.100 128.665  1.00 87.34           C  
HETATM 6115  C15 OLA A1202      43.490  45.104 127.582  1.00 87.81           C  
HETATM 6116  C16 OLA A1202      44.943  44.916 127.159  1.00 88.54           C  
HETATM 6117  C17 OLA A1202      45.342  45.914 126.077  1.00 88.74           C  
HETATM 6118  C18 OLA A1202      45.744  47.242 126.679  1.00 87.90           C  
HETATM 6119  C1  OLA A1203      30.068  45.160 139.185  1.00 62.83           C  
HETATM 6120  O1  OLA A1203      29.890  46.282 139.700  1.00 64.92           O  
HETATM 6121  O2  OLA A1203      29.302  44.194 139.391  1.00 64.76           O  
HETATM 6122  C2  OLA A1203      31.248  44.964 138.266  1.00 61.18           C  
HETATM 6123  C3  OLA A1203      32.567  45.154 139.007  1.00 59.27           C  
HETATM 6124  C4  OLA A1203      33.718  45.065 138.011  1.00 58.36           C  
HETATM 6125  C5  OLA A1203      35.068  44.868 138.685  1.00 57.53           C  
HETATM 6126  C6  OLA A1203      36.096  44.384 137.668  1.00 57.19           C  
HETATM 6127  C7  OLA A1203      37.495  44.371 138.269  1.00 57.18           C  
HETATM 6128  C8  OLA A1203      38.557  44.066 137.218  1.00 57.57           C  
HETATM 6129  C9  OLA A1203      39.832  43.666 137.925  1.00 59.05           C  
HETATM 6130  C10 OLA A1203      40.960  44.357 137.757  1.00 60.42           C  
HETATM 6131  C11 OLA A1203      42.233  43.954 138.474  1.00 61.20           C  
HETATM 6132  C12 OLA A1203      42.710  45.092 139.374  1.00 61.44           C  
HETATM 6133  C13 OLA A1203      44.205  44.988 139.670  1.00 61.45           C  
HETATM 6134  C14 OLA A1203      45.045  45.647 138.577  1.00 61.19           C  
HETATM 6135  C15 OLA A1203      46.450  45.051 138.510  1.00 61.56           C  
HETATM 6136  C16 OLA A1203      47.208  45.536 137.279  1.00 61.82           C  
HETATM 6137  C17 OLA A1203      48.510  44.764 137.078  1.00 61.78           C  
HETATM 6138  C18 OLA A1203      49.409  45.440 136.062  1.00 61.25           C  
HETATM 6139  C1  OLA A1204      63.424  53.947 165.201  1.00 71.50           C  
HETATM 6140  O1  OLA A1204      63.640  53.288 164.161  1.00 72.34           O  
HETATM 6141  O2  OLA A1204      64.296  54.667 165.738  1.00 71.90           O  
HETATM 6142  C2  OLA A1204      62.052  53.865 165.833  1.00 70.01           C  
HETATM 6143  C3  OLA A1204      61.018  54.502 164.913  1.00 67.84           C  
HETATM 6144  C4  OLA A1204      59.612  54.411 165.488  1.00 66.99           C  
HETATM 6145  C5  OLA A1204      58.611  55.153 164.603  1.00 66.29           C  
HETATM 6146  C6  OLA A1204      57.269  54.431 164.548  1.00 66.62           C  
HETATM 6147  C7  OLA A1204      56.317  55.103 163.566  1.00 66.47           C  
HETATM 6148  C8  OLA A1204      54.938  54.447 163.588  1.00 66.16           C  
HETATM 6149  C9  OLA A1204      54.036  55.146 162.594  1.00 66.65           C  
HETATM 6150  C10 OLA A1204      52.774  54.764 162.386  1.00 66.67           C  
HETATM 6151  C11 OLA A1204      52.156  53.604 163.133  1.00 66.58           C  
HETATM 6152  C12 OLA A1204      50.711  53.417 162.686  1.00 65.71           C  
HETATM 6153  C1  OLA A1205      62.587  57.452 153.660  1.00 60.10           C  
HETATM 6154  O1  OLA A1205      61.850  56.457 153.471  1.00 60.00           O  
HETATM 6155  O2  OLA A1205      63.825  57.393 153.493  1.00 59.78           O  
HETATM 6156  C2  OLA A1205      61.995  58.780 154.103  1.00 60.12           C  
HETATM 6157  C3  OLA A1205      60.514  58.671 154.463  1.00 60.42           C  
HETATM 6158  C4  OLA A1205      59.925  60.019 154.873  1.00 61.15           C  
HETATM 6159  C5  OLA A1205      58.476  59.868 155.334  1.00 62.46           C  
HETATM 6160  C6  OLA A1205      57.968  61.103 156.075  1.00 63.68           C  
HETATM 6161  C7  OLA A1205      56.752  60.765 156.934  1.00 64.49           C  
HETATM 6162  C8  OLA A1205      56.219  62.004 157.649  1.00 65.77           C  
HETATM 6163  C9  OLA A1205      55.324  62.804 156.728  1.00 66.51           C  
HETATM 6164  C10 OLA A1205      54.071  63.085 157.082  1.00 66.30           C  
HETATM 6165  O4  DU1 B1201      54.338  22.563 132.835  1.00 85.23           O  
HETATM 6166  C3  DU1 B1201      55.002  21.542 132.877  1.00 82.53           C  
HETATM 6167  N1  DU1 B1201      55.977  21.269 131.918  1.00 82.84           N  
HETATM 6168  C14 DU1 B1201      56.722  20.095 132.010  1.00 81.80           C  
HETATM 6169  C22 DU1 B1201      56.516  19.197 133.020  1.00 80.44           C  
HETATM 6170  N4  DU1 B1201      57.417  18.197 132.770  1.00 79.34           N  
HETATM 6171  C15 DU1 B1201      58.105  18.528 131.648  1.00 79.21           C  
HETATM 6172  C16 DU1 B1201      59.176  17.671 131.072  1.00 77.97           C  
HETATM 6173  C21 DU1 B1201      58.617  16.319 130.607  1.00 77.85           C  
HETATM 6174  C20 DU1 B1201      59.699  15.249 130.478  1.00 77.14           C  
HETATM 6175  C19 DU1 B1201      61.075  15.863 130.311  1.00 76.98           C  
HETATM 6176  C18 DU1 B1201      61.467  16.664 131.541  1.00 77.20           C  
HETATM 6177  C17 DU1 B1201      60.286  17.452 132.107  1.00 76.99           C  
HETATM 6178  N3  DU1 B1201      57.707  19.685 131.158  1.00 81.74           N  
HETATM 6179  C23 DU1 B1201      55.551  19.392 134.030  1.00 80.60           C  
HETATM 6180  O3  DU1 B1201      55.328  18.617 134.952  1.00 82.30           O  
HETATM 6181  N   DU1 B1201      54.824  20.596 133.890  1.00 80.96           N  
HETATM 6182  C2  DU1 B1201      53.811  20.892 134.921  1.00 80.22           C  
HETATM 6183  C1  DU1 B1201      52.473  20.248 134.672  1.00 79.90           C  
HETATM 6184  C   DU1 B1201      51.465  20.706 135.712  1.00 78.79           C  
HETATM 6185  C4  DU1 B1201      56.195  22.263 130.854  1.00 83.04           C  
HETATM 6186  C5  DU1 B1201      55.140  22.221 129.764  1.00 83.48           C  
HETATM 6187  C6  DU1 B1201      55.304  23.333 128.747  1.00 83.97           C  
HETATM 6188  N2  DU1 B1201      56.291  22.985 127.733  1.00 84.94           N  
HETATM 6189  C7  DU1 B1201      56.126  23.266 126.436  1.00 86.51           C  
HETATM 6190  O2  DU1 B1201      55.120  23.829 126.010  1.00 87.18           O  
HETATM 6191  C8  DU1 B1201      57.205  22.828 125.494  1.00 87.68           C  
HETATM 6192  C13 DU1 B1201      57.868  21.615 125.677  1.00 88.32           C  
HETATM 6193  C12 DU1 B1201      58.848  21.199 124.793  1.00 89.43           C  
HETATM 6194  C11 DU1 B1201      59.163  21.992 123.700  1.00 89.31           C  
HETATM 6195  S   DU1 B1201      60.402  21.478 122.547  1.00 90.08           S  
HETATM 6196  O1  DU1 B1201      61.104  20.363 123.146  1.00 91.02           O  
HETATM 6197  O   DU1 B1201      61.182  22.651 122.221  1.00 90.31           O  
HETATM 6198  C10 DU1 B1201      58.505  23.194 123.487  1.00 88.78           C  
HETATM 6199  C9  DU1 B1201      57.528  23.603 124.380  1.00 88.85           C  
HETATM 6200  C1  OLA B1202      32.096  31.516 144.658  1.00 84.89           C  
HETATM 6201  O1  OLA B1202      31.712  31.079 143.551  1.00 84.27           O  
HETATM 6202  O2  OLA B1202      31.344  32.143 145.435  1.00 85.87           O  
HETATM 6203  C2  OLA B1202      33.529  31.275 145.073  1.00 84.82           C  
HETATM 6204  C3  OLA B1202      34.223  32.605 145.350  1.00 85.38           C  
HETATM 6205  C4  OLA B1202      35.716  32.422 145.618  1.00 85.94           C  
HETATM 6206  C5  OLA B1202      36.558  32.753 144.391  1.00 86.38           C  
HETATM 6207  C6  OLA B1202      38.051  32.633 144.681  1.00 87.03           C  
HETATM 6208  C7  OLA B1202      38.626  33.942 145.216  1.00 87.64           C  
HETATM 6209  C8  OLA B1202      40.029  33.757 145.788  1.00 87.97           C  
HETATM 6210  C9  OLA B1202      41.020  33.530 144.665  1.00 88.20           C  
HETATM 6211  C10 OLA B1202      42.334  33.438 144.884  1.00 88.04           C  
HETATM 6212  C11 OLA B1202      42.926  33.554 146.272  1.00 88.10           C  
HETATM 6213  C12 OLA B1202      44.446  33.431 146.205  1.00 88.54           C  
HETATM 6214  C13 OLA B1202      45.100  33.978 147.470  1.00 89.61           C  
HETATM 6215  C14 OLA B1202      46.624  33.897 147.400  1.00 90.58           C  
HETATM 6216  C15 OLA B1202      47.183  32.812 148.315  1.00 91.40           C  
HETATM 6217  C16 OLA B1202      48.708  32.825 148.303  1.00 92.07           C  
HETATM 6218  C17 OLA B1202      49.285  31.711 149.172  1.00 92.21           C  
HETATM 6219  C18 OLA B1202      50.610  32.116 149.784  1.00 92.48           C  
HETATM 6220  C1  OLA B1203      33.748  30.406 140.483  1.00 70.56           C  
HETATM 6221  O1  OLA B1203      33.126  31.235 139.788  1.00 71.37           O  
HETATM 6222  O2  OLA B1203      33.180  29.669 141.316  1.00 70.82           O  
HETATM 6223  C2  OLA B1203      35.244  30.281 140.305  1.00 70.61           C  
HETATM 6224  C3  OLA B1203      35.942  31.620 140.524  1.00 71.77           C  
HETATM 6225  C4  OLA B1203      37.434  31.408 140.771  1.00 72.97           C  
HETATM 6226  C5  OLA B1203      38.263  32.659 140.487  1.00 73.01           C  
HETATM 6227  C6  OLA B1203      39.758  32.363 140.617  1.00 73.60           C  
HETATM 6228  C7  OLA B1203      40.636  33.494 140.074  1.00 74.82           C  
HETATM 6229  C8  OLA B1203      41.860  32.985 139.311  1.00 74.81           C  
HETATM 6230  C9  OLA B1203      41.444  32.514 137.927  1.00 74.29           C  
HETATM 6231  C10 OLA B1203      42.186  32.639 136.818  1.00 72.57           C  
HETATM 6232  C11 OLA B1203      43.553  33.288 136.770  1.00 72.27           C  
HETATM 6233  C12 OLA B1203      44.615  32.442 137.470  1.00 71.93           C  
HETATM 6234  C13 OLA B1203      45.984  32.659 136.823  1.00 72.02           C  
HETATM 6235  C14 OLA B1203      47.162  32.313 137.737  1.00 72.10           C  
HETATM 6236  C15 OLA B1203      48.225  33.409 137.708  1.00 72.57           C  
HETATM 6237  C16 OLA B1203      49.512  32.967 138.399  1.00 73.07           C  
HETATM 6238  C17 OLA B1203      50.568  34.069 138.370  1.00 73.28           C  
HETATM 6239  C18 OLA B1203      51.908  33.565 138.865  1.00 72.69           C  
HETATM 6240  C1  OLA B1204      57.517  30.107 112.861  1.00 84.81           C  
HETATM 6241  O1  OLA B1204      58.209  29.103 112.580  1.00 83.92           O  
HETATM 6242  O2  OLA B1204      57.700  30.791 113.892  1.00 84.41           O  
HETATM 6243  C2  OLA B1204      56.409  30.512 111.912  1.00 84.65           C  
HETATM 6244  C3  OLA B1204      55.243  29.526 111.990  1.00 83.68           C  
HETATM 6245  C4  OLA B1204      53.917  30.207 112.318  1.00 83.25           C  
HETATM 6246  C5  OLA B1204      52.832  29.173 112.604  1.00 82.38           C  
HETATM 6247  C6  OLA B1204      51.480  29.828 112.870  1.00 82.53           C  
HETATM 6248  C7  OLA B1204      50.339  28.849 112.608  1.00 82.61           C  
HETATM 6249  C8  OLA B1204      49.013  29.341 113.184  1.00 82.68           C  
HETATM 6250  C9  OLA B1204      48.494  30.513 112.377  1.00 82.63           C  
HETATM 6251  C10 OLA B1204      47.302  31.065 112.617  1.00 82.27           C  
HETATM 6252  C11 OLA B1204      46.388  30.560 113.711  1.00 81.07           C  
CONECT  570 1244                                                                
CONECT 1244  570                                                                
CONECT 2571 2590                                                                
CONECT 2590 2571                                                                
CONECT 2657 6094                                                                
CONECT 3596 4270                                                                
CONECT 4270 3596                                                                
CONECT 5653 5672                                                                
CONECT 5672 5653                                                                
CONECT 5739 6195                                                                
CONECT 6064 6065                                                                
CONECT 6065 6064 6066 6080                                                      
CONECT 6066 6065 6067 6084                                                      
CONECT 6067 6066 6068 6077                                                      
CONECT 6068 6067 6069 6078                                                      
CONECT 6069 6068 6070                                                           
CONECT 6070 6069 6071 6077                                                      
CONECT 6071 6070 6072 6076                                                      
CONECT 6072 6071 6073                                                           
CONECT 6073 6072 6074                                                           
CONECT 6074 6073 6075                                                           
CONECT 6075 6074 6076                                                           
CONECT 6076 6071 6075                                                           
CONECT 6077 6067 6070                                                           
CONECT 6078 6068 6079 6080                                                      
CONECT 6079 6078                                                                
CONECT 6080 6065 6078 6081                                                      
CONECT 6081 6080 6082                                                           
CONECT 6082 6081 6083                                                           
CONECT 6083 6082                                                                
CONECT 6084 6066 6085                                                           
CONECT 6085 6084 6086                                                           
CONECT 6086 6085 6087                                                           
CONECT 6087 6086 6088                                                           
CONECT 6088 6087 6089 6090                                                      
CONECT 6089 6088                                                                
CONECT 6090 6088 6091 6098                                                      
CONECT 6091 6090 6092                                                           
CONECT 6092 6091 6093                                                           
CONECT 6093 6092 6094 6097                                                      
CONECT 6094 2657 6093 6095 6096                                                 
CONECT 6095 6094                                                                
CONECT 6096 6094                                                                
CONECT 6097 6093 6098                                                           
CONECT 6098 6090 6097                                                           
CONECT 6099 6100 6101 6102                                                      
CONECT 6100 6099                                                                
CONECT 6101 6099                                                                
CONECT 6102 6099 6103                                                           
CONECT 6103 6102 6104                                                           
CONECT 6104 6103 6105                                                           
CONECT 6105 6104 6106                                                           
CONECT 6106 6105 6107                                                           
CONECT 6107 6106 6108                                                           
CONECT 6108 6107 6109                                                           
CONECT 6109 6108 6110                                                           
CONECT 6110 6109 6111                                                           
CONECT 6111 6110 6112                                                           
CONECT 6112 6111 6113                                                           
CONECT 6113 6112 6114                                                           
CONECT 6114 6113 6115                                                           
CONECT 6115 6114 6116                                                           
CONECT 6116 6115 6117                                                           
CONECT 6117 6116 6118                                                           
CONECT 6118 6117                                                                
CONECT 6119 6120 6121 6122                                                      
CONECT 6120 6119                                                                
CONECT 6121 6119                                                                
CONECT 6122 6119 6123                                                           
CONECT 6123 6122 6124                                                           
CONECT 6124 6123 6125                                                           
CONECT 6125 6124 6126                                                           
CONECT 6126 6125 6127                                                           
CONECT 6127 6126 6128                                                           
CONECT 6128 6127 6129                                                           
CONECT 6129 6128 6130                                                           
CONECT 6130 6129 6131                                                           
CONECT 6131 6130 6132                                                           
CONECT 6132 6131 6133                                                           
CONECT 6133 6132 6134                                                           
CONECT 6134 6133 6135                                                           
CONECT 6135 6134 6136                                                           
CONECT 6136 6135 6137                                                           
CONECT 6137 6136 6138                                                           
CONECT 6138 6137                                                                
CONECT 6139 6140 6141 6142                                                      
CONECT 6140 6139                                                                
CONECT 6141 6139                                                                
CONECT 6142 6139 6143                                                           
CONECT 6143 6142 6144                                                           
CONECT 6144 6143 6145                                                           
CONECT 6145 6144 6146                                                           
CONECT 6146 6145 6147                                                           
CONECT 6147 6146 6148                                                           
CONECT 6148 6147 6149                                                           
CONECT 6149 6148 6150                                                           
CONECT 6150 6149 6151                                                           
CONECT 6151 6150 6152                                                           
CONECT 6152 6151                                                                
CONECT 6153 6154 6155 6156                                                      
CONECT 6154 6153                                                                
CONECT 6155 6153                                                                
CONECT 6156 6153 6157                                                           
CONECT 6157 6156 6158                                                           
CONECT 6158 6157 6159                                                           
CONECT 6159 6158 6160                                                           
CONECT 6160 6159 6161                                                           
CONECT 6161 6160 6162                                                           
CONECT 6162 6161 6163                                                           
CONECT 6163 6162 6164                                                           
CONECT 6164 6163                                                                
CONECT 6165 6166                                                                
CONECT 6166 6165 6167 6181                                                      
CONECT 6167 6166 6168 6185                                                      
CONECT 6168 6167 6169 6178                                                      
CONECT 6169 6168 6170 6179                                                      
CONECT 6170 6169 6171                                                           
CONECT 6171 6170 6172 6178                                                      
CONECT 6172 6171 6173 6177                                                      
CONECT 6173 6172 6174                                                           
CONECT 6174 6173 6175                                                           
CONECT 6175 6174 6176                                                           
CONECT 6176 6175 6177                                                           
CONECT 6177 6172 6176                                                           
CONECT 6178 6168 6171                                                           
CONECT 6179 6169 6180 6181                                                      
CONECT 6180 6179                                                                
CONECT 6181 6166 6179 6182                                                      
CONECT 6182 6181 6183                                                           
CONECT 6183 6182 6184                                                           
CONECT 6184 6183                                                                
CONECT 6185 6167 6186                                                           
CONECT 6186 6185 6187                                                           
CONECT 6187 6186 6188                                                           
CONECT 6188 6187 6189                                                           
CONECT 6189 6188 6190 6191                                                      
CONECT 6190 6189                                                                
CONECT 6191 6189 6192 6199                                                      
CONECT 6192 6191 6193                                                           
CONECT 6193 6192 6194                                                           
CONECT 6194 6193 6195 6198                                                      
CONECT 6195 5739 6194 6196 6197                                                 
CONECT 6196 6195                                                                
CONECT 6197 6195                                                                
CONECT 6198 6194 6199                                                           
CONECT 6199 6191 6198                                                           
CONECT 6200 6201 6202 6203                                                      
CONECT 6201 6200                                                                
CONECT 6202 6200                                                                
CONECT 6203 6200 6204                                                           
CONECT 6204 6203 6205                                                           
CONECT 6205 6204 6206                                                           
CONECT 6206 6205 6207                                                           
CONECT 6207 6206 6208                                                           
CONECT 6208 6207 6209                                                           
CONECT 6209 6208 6210                                                           
CONECT 6210 6209 6211                                                           
CONECT 6211 6210 6212                                                           
CONECT 6212 6211 6213                                                           
CONECT 6213 6212 6214                                                           
CONECT 6214 6213 6215                                                           
CONECT 6215 6214 6216                                                           
CONECT 6216 6215 6217                                                           
CONECT 6217 6216 6218                                                           
CONECT 6218 6217 6219                                                           
CONECT 6219 6218                                                                
CONECT 6220 6221 6222 6223                                                      
CONECT 6221 6220                                                                
CONECT 6222 6220                                                                
CONECT 6223 6220 6224                                                           
CONECT 6224 6223 6225                                                           
CONECT 6225 6224 6226                                                           
CONECT 6226 6225 6227                                                           
CONECT 6227 6226 6228                                                           
CONECT 6228 6227 6229                                                           
CONECT 6229 6228 6230                                                           
CONECT 6230 6229 6231                                                           
CONECT 6231 6230 6232                                                           
CONECT 6232 6231 6233                                                           
CONECT 6233 6232 6234                                                           
CONECT 6234 6233 6235                                                           
CONECT 6235 6234 6236                                                           
CONECT 6236 6235 6237                                                           
CONECT 6237 6236 6238                                                           
CONECT 6238 6237 6239                                                           
CONECT 6239 6238                                                                
CONECT 6240 6241 6242 6243                                                      
CONECT 6241 6240                                                                
CONECT 6242 6240                                                                
CONECT 6243 6240 6244                                                           
CONECT 6244 6243 6245                                                           
CONECT 6245 6244 6246                                                           
CONECT 6246 6245 6247                                                           
CONECT 6247 6246 6248                                                           
CONECT 6248 6247 6249                                                           
CONECT 6249 6248 6250                                                           
CONECT 6250 6249 6251                                                           
CONECT 6251 6250 6252                                                           
CONECT 6252 6251                                                                
MASTER      373    0    9   39    4    0   14    6 6250    2  199   64          
END