CNRS Nantes University UFIP UFIP
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***  IMMUNE SYSTEM 10-MAY-15 4ZQK  ***

elNémo ID: 2105030527109398

Job options:

ID        	=	 2105030527109398
JOBID     	=	 IMMUNE SYSTEM 10-MAY-15 4ZQK
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    IMMUNE SYSTEM                           10-MAY-15   4ZQK              
TITLE     STRUCTURE OF THE COMPLEX OF HUMAN PROGRAMMED DEATH-1 (PD-1) AND ITS   
TITLE    2 LIGAND PD-L1.                                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROGRAMMED CELL DEATH 1 LIGAND 1;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: PROGRAMMED DEATH LIGAND 1,B7 HOMOLOG 1,B7-H1;               
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: PROGRAMMED CELL DEATH PROTEIN 1;                           
COMPND   8 CHAIN: B;                                                            
COMPND   9 FRAGMENT: UNP RESIDUES 33-150;                                       
COMPND  10 SYNONYM: HPD-1;                                                      
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CD274, B7H1, PDCD1L1, PDCD1LG1, PDL1;                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: PDCD1, PD1;                                                    
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 469008                                      
KEYWDS    COMPLEX, CO-STIMULATION, RECEPTOR-LIGAND COMPLEX, IMMUNE SYSTEM       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.M.ZAK,G.DUBIN,T.A.HOLAK                                             
REVDAT   3   16-DEC-15 4ZQK    1       JRNL                                     
REVDAT   2   09-DEC-15 4ZQK    1       JRNL                                     
REVDAT   1   04-NOV-15 4ZQK    0                                                
JRNL        AUTH   K.M.ZAK,R.KITEL,S.PRZETOCKA,P.GOLIK,K.GUZIK,B.MUSIELAK,      
JRNL        AUTH 2 A.DOMLING,G.DUBIN,T.A.HOLAK                                  
JRNL        TITL   STRUCTURE OF THE COMPLEX OF HUMAN PROGRAMMED DEATH 1, PD-1,  
JRNL        TITL 2 AND ITS LIGAND PD-L1.                                        
JRNL        REF    STRUCTURE                     V.  23  2341 2015              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   26602187                                                     
JRNL        DOI    10.1016/J.STR.2015.09.010                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.45 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0049                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.45                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 61.37                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 12082                          
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) : 0.209                           
REMARK   3   R VALUE            (WORKING SET) : 0.207                           
REMARK   3   FREE R VALUE                     : 0.253                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 625                             
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) : 2.45                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.51                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 863                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.89                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2250                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 49                           
REMARK   3   BIN FREE R VALUE                    : 0.2830                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1650                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 15                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 57.57                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.72000                                             
REMARK   3    B22 (A**2) : -0.72000                                             
REMARK   3    B33 (A**2) : 2.33000                                              
REMARK   3    B12 (A**2) : -0.36000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.286         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.234         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.175         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.316        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.943                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.917                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1684 ; 0.016 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  1535 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2296 ; 1.768 ; 1.951       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3514 ; 0.860 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   218 ; 7.670 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    67 ;34.544 ;24.925       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   254 ;17.366 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     5 ;12.728 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   271 ; 0.100 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1926 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   373 ; 0.001 ; 0.020       
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):   881 ; 3.231 ; 4.015       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   880 ; 3.233 ; 4.015       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1096 ; 4.885 ; 6.011       
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  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    18        A   132                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.7541  45.1745 114.2792              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2385 T22:   0.0394                                     
REMARK   3      T33:   0.0139 T12:  -0.0829                                     
REMARK   3      T13:  -0.0151 T23:   0.0102                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1247 L22:   1.9953                                     
REMARK   3      L33:   1.5961 L12:   1.1581                                     
REMARK   3      L13:   0.4526 L23:  -0.2608                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1316 S12:   0.0009 S13:   0.0248                       
REMARK   3      S21:  -0.1420 S22:   0.0472 S23:   0.0077                       
REMARK   3      S31:  -0.0151 S32:  -0.0567 S33:   0.0844                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    33        B   146                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.8712  50.2693 104.1425              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1611 T22:   0.2330                                     
REMARK   3      T33:   0.0433 T12:   0.0465                                     
REMARK   3      T13:  -0.0563 T23:   0.0150                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3530 L22:   3.2100                                     
REMARK   3      L33:   2.4375 L12:  -0.1853                                     
REMARK   3      L13:  -0.7561 L23:   1.6745                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0195 S12:   0.1309 S13:  -0.1184                       
REMARK   3      S21:   0.2490 S22:   0.0563 S23:  -0.1049                       
REMARK   3      S31:   0.3538 S32:   0.5131 S33:  -0.0368                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4ZQK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-MAY-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000209717.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-APR-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 193                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : BESSY                              
REMARK 200  BEAMLINE                       : 14.1                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91843                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12737                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.450                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 61.370                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 10.60                              
REMARK 200  R MERGE                    (I) : 0.04300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 35.2200                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.55                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 11.20                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.48000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 5.210                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: CHAIN A -3BIK, CHAIN B 3RRQ                          
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.96                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.32                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS PH 5.5, 1.84 M AMMONIUM   
REMARK 280  SULFATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       38.12233            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       76.24467            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       76.24467            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       38.12233            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1670 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10580 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASP B    85                                                      
REMARK 465     ARG B    86                                                      
REMARK 465     SER B    87                                                      
REMARK 465     GLN B    88                                                      
REMARK 465     PRO B    89                                                      
REMARK 465     GLY B    90                                                      
REMARK 465     GLN B    91                                                      
REMARK 465     ASP B    92                                                      
REMARK 465     ARG B   147                                                      
REMARK 465     ARG B   148                                                      
REMARK 465     ALA B   149                                                      
REMARK 465     GLU B   150                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  45    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  46    CG   CD   CE   NZ                                   
REMARK 470     LYS A  62    CD   CE   NZ                                        
REMARK 470     GLU A  71    CG   CD   OE1  OE2                                  
REMARK 470     ASP A  73    CG   OD1  OD2                                       
REMARK 470     LEU A  74    CG   CD1  CD2                                       
REMARK 470     LYS A  75    CG   CD   CE   NZ                                   
REMARK 470     ARG A  82    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A  83    OE1  NE2                                            
REMARK 470     LYS A  89    CG   CD   CE   NZ                                   
REMARK 470     GLN A 107    CD   OE1  NE2                                       
REMARK 470     ARG A 125    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A 129    CD   CE   NZ                                        
REMARK 470     ASN B  33    CG   OD1  ND2                                       
REMARK 470     LEU B  41    CG   CD1  CD2                                       
REMARK 470     ASN B  58    CG   OD1  ND2                                       
REMARK 470     ARG B  69    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B  96    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG B 112    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 114    NE   CZ   NH1  NH2                                  
REMARK 470     ARG B 115    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 131    CD   CE   NZ                                        
REMARK 470     LYS B 135    CE   NZ                                             
REMARK 470     ARG B 139    CZ   NH1  NH2                                       
REMARK 470     ARG B 143    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 146    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    SER B    71     O    SER B    73              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    CYS B 123   CA  -  CB  -  SG  ANGL. DEV. =   7.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A  45     -120.30    -66.37                                   
REMARK 500    TYR A 118       75.91   -175.40                                   
REMARK 500    SER B 118      134.24    -38.33                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 201                  
DBREF  4ZQK A   18   132  UNP    Q9NZQ7   PD1L1_HUMAN     18    132             
DBREF  4ZQK B   33   150  UNP    Q15116   PDCD1_HUMAN     33    150             
SEQADV 4ZQK SER B   93  UNP  Q15116    CYS    93 ENGINEERED MUTATION            
SEQRES   1 A  115  ALA PHE THR VAL THR VAL PRO LYS ASP LEU TYR VAL VAL          
SEQRES   2 A  115  GLU TYR GLY SER ASN MET THR ILE GLU CYS LYS PHE PRO          
SEQRES   3 A  115  VAL GLU LYS GLN LEU ASP LEU ALA ALA LEU ILE VAL TYR          
SEQRES   4 A  115  TRP GLU MET GLU ASP LYS ASN ILE ILE GLN PHE VAL HIS          
SEQRES   5 A  115  GLY GLU GLU ASP LEU LYS VAL GLN HIS SER SER TYR ARG          
SEQRES   6 A  115  GLN ARG ALA ARG LEU LEU LYS ASP GLN LEU SER LEU GLY          
SEQRES   7 A  115  ASN ALA ALA LEU GLN ILE THR ASP VAL LYS LEU GLN ASP          
SEQRES   8 A  115  ALA GLY VAL TYR ARG CYS MET ILE SER TYR GLY GLY ALA          
SEQRES   9 A  115  ASP TYR LYS ARG ILE THR VAL LYS VAL ASN ALA                  
SEQRES   1 B  118  ASN PRO PRO THR PHE SER PRO ALA LEU LEU VAL VAL THR          
SEQRES   2 B  118  GLU GLY ASP ASN ALA THR PHE THR CYS SER PHE SER ASN          
SEQRES   3 B  118  THR SER GLU SER PHE VAL LEU ASN TRP TYR ARG MET SER          
SEQRES   4 B  118  PRO SER ASN GLN THR ASP LYS LEU ALA ALA PHE PRO GLU          
SEQRES   5 B  118  ASP ARG SER GLN PRO GLY GLN ASP SER ARG PHE ARG VAL          
SEQRES   6 B  118  THR GLN LEU PRO ASN GLY ARG ASP PHE HIS MET SER VAL          
SEQRES   7 B  118  VAL ARG ALA ARG ARG ASN ASP SER GLY THR TYR LEU CYS          
SEQRES   8 B  118  GLY ALA ILE SER LEU ALA PRO LYS ALA GLN ILE LYS GLU          
SEQRES   9 B  118  SER LEU ARG ALA GLU LEU ARG VAL THR GLU ARG ARG ALA          
SEQRES  10 B  118  GLU                                                          
HET     NA  A 201       1                                                       
HETNAM      NA SODIUM ION                                                       
FORMUL   3   NA    NA 1+                                                        
FORMUL   4  HOH   *15(H2 O)                                                     
HELIX    1 AA1 ASP A   49  ALA A   52  5                                   4    
HELIX    2 AA2 LEU A   74  GLN A   77  5                                   4    
HELIX    3 AA3 HIS A   78  ARG A   82  5                                   5    
HELIX    4 AA4 LYS A   89  LEU A   94  5                                   6    
HELIX    5 AA5 LYS A  105  ALA A  109  5                                   5    
SHEET    1 AA1 6 LEU A  27  GLU A  31  0                                        
SHEET    2 AA1 6 ALA A 121  ASN A 131  1  O  LYS A 129   N  TYR A  28           
SHEET    3 AA1 6 GLY A 110  SER A 117 -1  N  GLY A 110   O  VAL A 128           
SHEET    4 AA1 6 ILE A  54  MET A  59 -1  N  GLU A  58   O  ARG A 113           
SHEET    5 AA1 6 LYS A  62  VAL A  68 -1  O  PHE A  67   N  VAL A  55           
SHEET    6 AA1 6 GLU A  71  GLU A  72 -1  O  GLU A  71   N  VAL A  68           
SHEET    1 AA2 3 MET A  36  LYS A  41  0                                        
SHEET    2 AA2 3 ASN A  96  ILE A 101 -1  O  ALA A  97   N  CYS A  40           
SHEET    3 AA2 3 ALA A  85  LEU A  87 -1  N  ARG A  86   O  GLN A 100           
SHEET    1 AA3 4 THR B  36  SER B  38  0                                        
SHEET    2 AA3 4 ALA B  50  SER B  55 -1  O  THR B  53   N  SER B  38           
SHEET    3 AA3 4 ASP B 105  VAL B 110 -1  O  VAL B 110   N  ALA B  50           
SHEET    4 AA3 4 PHE B  95  GLN B  99 -1  N  ARG B  96   O  SER B 109           
SHEET    1 AA4 5 LEU B  41  THR B  45  0                                        
SHEET    2 AA4 5 ALA B 140  THR B 145  1  O  ARG B 143   N  VAL B  44           
SHEET    3 AA4 5 GLY B 119  ALA B 129 -1  N  TYR B 121   O  ALA B 140           
SHEET    4 AA4 5 SER B  62  MET B  70 -1  N  SER B  62   O  LEU B 128           
SHEET    5 AA4 5 THR B  76  PHE B  82 -1  O  LEU B  79   N  TRP B  67           
SHEET    1 AA5 4 LEU B  41  THR B  45  0                                        
SHEET    2 AA5 4 ALA B 140  THR B 145  1  O  ARG B 143   N  VAL B  44           
SHEET    3 AA5 4 GLY B 119  ALA B 129 -1  N  TYR B 121   O  ALA B 140           
SHEET    4 AA5 4 GLN B 133  GLU B 136 -1  O  LYS B 135   N  ALA B 125           
SSBOND   1 CYS A   40    CYS A  114                          1555   1555  2.08  
SSBOND   2 CYS B   54    CYS B  123                          1555   1555  2.13  
CISPEP   1 GLY A  119    GLY A  120          0         0.04                     
CISPEP   2 SER B   38    PRO B   39          0        -7.36                     
CISPEP   3 PHE B   82    PRO B   83          0        -7.69                     
CISPEP   4 ALA B  129    PRO B  130          0        -3.96                     
SITE     1 AC1  2 ARG A  86  SER B  57                                          
CRYST1   70.862   70.862  114.367  90.00  90.00 120.00 P 31 2 1      6          
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      0.014112  0.008148  0.000000        0.00000                         
SCALE2      0.000000  0.016295  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008744        0.00000                         
ATOM      1  N   ALA A  18      11.475  45.257 120.093  1.00 65.94           N  
ANISOU    1  N   ALA A  18     8236   8077   8742   -928   -370   1006       N  
ATOM      2  CA  ALA A  18      10.630  45.330 118.873  1.00 65.04           C  
ANISOU    2  CA  ALA A  18     8249   7913   8550   -901   -215    873       C  
ATOM      3  C   ALA A  18       9.182  45.152 119.289  1.00 63.13           C  
ANISOU    3  C   ALA A  18     8186   7635   8167   -885   -251    823       C  
ATOM      4  O   ALA A  18       8.777  44.126 119.864  1.00 68.67           O  
ANISOU    4  O   ALA A  18     8882   8300   8908   -820   -281    865       O  
ATOM      5  CB  ALA A  18      11.022  44.272 117.837  1.00 65.58           C  
ANISOU    5  CB  ALA A  18     8213   7931   8772   -798    -44    830       C  
ATOM      6  N   PHE A  19       8.406  46.188 119.044  1.00 54.29           N  
ANISOU    6  N   PHE A  19     7214   6523   6892   -950   -258    746       N  
ATOM      7  CA  PHE A  19       6.997  46.042 119.083  1.00 50.62           C  
ANISOU    7  CA  PHE A  19     6901   6022   6310   -925   -249    677       C  
ATOM      8  C   PHE A  19       6.589  45.501 117.695  1.00 52.51           C  
ANISOU    8  C   PHE A  19     7174   6209   6568   -872    -93    599       C  
ATOM      9  O   PHE A  19       6.947  46.090 116.646  1.00 51.98           O  
ANISOU    9  O   PHE A  19     7105   6154   6489   -913    -14    562       O  
ATOM     10  CB  PHE A  19       6.378  47.388 119.351  1.00 49.82           C  
ANISOU   10  CB  PHE A  19     6922   5936   6070  -1005   -321    623       C  
ATOM     11  CG  PHE A  19       4.893  47.344 119.428  1.00 51.32           C  
ANISOU   11  CG  PHE A  19     7251   6098   6151   -978   -314    549       C  
ATOM     12  CD1 PHE A  19       4.266  47.079 120.626  1.00 51.59           C  
ANISOU   12  CD1 PHE A  19     7319   6165   6116   -975   -391    558       C  
ATOM     13  CD2 PHE A  19       4.123  47.578 118.304  1.00 50.02           C  
ANISOU   13  CD2 PHE A  19     7173   5888   5946   -967   -232    479       C  
ATOM     14  CE1 PHE A  19       2.895  47.048 120.720  1.00 50.65           C  
ANISOU   14  CE1 PHE A  19     7307   6033   5903   -952   -376    489       C  
ATOM     15  CE2 PHE A  19       2.753  47.538 118.387  1.00 48.88           C  
ANISOU   15  CE2 PHE A  19     7135   5721   5717   -941   -234    420       C  
ATOM     16  CZ  PHE A  19       2.132  47.270 119.590  1.00 49.82           C  
ANISOU   16  CZ  PHE A  19     7276   5871   5783   -929   -299    420       C  
ATOM     17  N   THR A  20       5.883  44.379 117.713  1.00 46.23           N  
ANISOU   17  N   THR A  20     6407   5363   5796   -798    -56    581       N  
ATOM     18  CA  THR A  20       5.345  43.741 116.541  1.00 48.04           C  
ANISOU   18  CA  THR A  20     6685   5541   6027   -757     76    493       C  
ATOM     19  C   THR A  20       3.900  43.348 116.857  1.00 46.53           C  
ANISOU   19  C   THR A  20     6617   5316   5747   -739     44    462       C  
ATOM     20  O   THR A  20       3.550  43.136 118.003  1.00 45.00           O  
ANISOU   20  O   THR A  20     6429   5132   5539   -735    -52    522       O  
ATOM     21  CB  THR A  20       6.121  42.469 116.168  1.00 52.57           C  
ANISOU   21  CB  THR A  20     7131   6061   6782   -673    171    492       C  
ATOM     22  OG1 THR A  20       6.356  41.732 117.351  1.00 60.31           O  
ANISOU   22  OG1 THR A  20     8035   7012   7869   -627     72    598       O  
ATOM     23  CG2 THR A  20       7.474  42.758 115.527  1.00 52.57           C  
ANISOU   23  CG2 THR A  20     6995   6103   6877   -684    252    491       C  
ATOM     24  N   VAL A  21       3.051  43.377 115.843  1.00 44.59           N  
ANISOU   24  N   VAL A  21     6468   5049   5423   -748    118    374       N  
ATOM     25  CA  VAL A  21       1.692  42.929 115.923  1.00 46.58           C  
ANISOU   25  CA  VAL A  21     6820   5271   5608   -735    106    339       C  
ATOM     26  C   VAL A  21       1.688  41.569 115.230  1.00 53.76           C  
ANISOU   26  C   VAL A  21     7707   6107   6612   -681    206    290       C  
ATOM     27  O   VAL A  21       2.514  41.299 114.349  1.00 54.46           O  
ANISOU   27  O   VAL A  21     7738   6185   6770   -667    310    240       O  
ATOM     28  CB  VAL A  21       0.739  43.878 115.194  1.00 48.89           C  
ANISOU   28  CB  VAL A  21     7227   5585   5763   -787    105    280       C  
ATOM     29  CG1 VAL A  21      -0.616  43.254 114.938  1.00 49.60           C  
ANISOU   29  CG1 VAL A  21     7399   5645   5802   -774    117    234       C  
ATOM     30  CG2 VAL A  21       0.545  45.123 116.002  1.00 51.10           C  
ANISOU   30  CG2 VAL A  21     7535   5903   5977   -825      1    308       C  
ATOM     31  N   THR A  22       0.782  40.698 115.654  1.00 55.68           N  
ANISOU   31  N   THR A  22     7989   6300   6867   -656    181    297       N  
ATOM     32  CA  THR A  22       0.668  39.356 115.054  1.00 59.19           C  
ANISOU   32  CA  THR A  22     8425   6647   7418   -610    264    240       C  
ATOM     33  C   THR A  22      -0.776  38.998 114.907  1.00 52.35           C  
ANISOU   33  C   THR A  22     7665   5759   6468   -636    249    201       C  
ATOM     34  O   THR A  22      -1.638  39.586 115.554  1.00 50.31           O  
ANISOU   34  O   THR A  22     7458   5556   6102   -669    167    242       O  
ATOM     35  CB  THR A  22       1.319  38.297 115.914  1.00 55.27           C  
ANISOU   35  CB  THR A  22     7822   6072   7108   -544    230    329       C  
ATOM     36  OG1 THR A  22       0.896  38.512 117.251  1.00 69.11           O  
ANISOU   36  OG1 THR A  22     9581   7871   8806   -569    101    450       O  
ATOM     37  CG2 THR A  22       2.791  38.421 115.865  1.00 58.30           C  
ANISOU   37  CG2 THR A  22     8072   6461   7617   -507    262    356       C  
ATOM     38  N   VAL A  23      -1.042  38.064 114.019  1.00 54.76           N  
ANISOU   38  N   VAL A  23     7999   5987   6823   -625    332    108       N  
ATOM     39  CA  VAL A  23      -2.404  37.593 113.851  1.00 57.28           C  
ANISOU   39  CA  VAL A  23     8408   6278   7078   -660    312     74       C  
ATOM     40  C   VAL A  23      -2.452  36.101 114.159  1.00 57.94           C  
ANISOU   40  C   VAL A  23     8460   6226   7330   -618    320     86       C  
ATOM     41  O   VAL A  23      -1.456  35.410 113.932  1.00 55.11           O  
ANISOU   41  O   VAL A  23     8026   5779   7135   -558    385     56       O  
ATOM     42  CB  VAL A  23      -2.945  37.878 112.438  1.00 57.96           C  
ANISOU   42  CB  VAL A  23     8584   6397   7041   -719    380    -51       C  
ATOM     43  CG1 VAL A  23      -3.334  39.344 112.312  1.00 53.84           C  
ANISOU   43  CG1 VAL A  23     8109   5989   6359   -771    325    -21       C  
ATOM     44  CG2 VAL A  23      -1.945  37.456 111.377  1.00 55.42           C  
ANISOU   44  CG2 VAL A  23     8231   6046   6780   -704    512   -164       C  
ATOM     45  N   PRO A  24      -3.603  35.608 114.681  1.00 58.70           N  
ANISOU   45  N   PRO A  24     8602   6298   7403   -649    255    133       N  
ATOM     46  CA  PRO A  24      -3.719  34.157 114.923  1.00 59.05           C  
ANISOU   46  CA  PRO A  24     8624   6192   7621   -625    252    155       C  
ATOM     47  C   PRO A  24      -3.728  33.428 113.572  1.00 57.77           C  
ANISOU   47  C   PRO A  24     8506   5929   7516   -626    361    -20       C  
ATOM     48  O   PRO A  24      -3.006  32.455 113.377  1.00 60.12           O  
ANISOU   48  O   PRO A  24     8749   6083   8009   -566    417    -65       O  
ATOM     49  CB  PRO A  24      -5.094  34.000 115.661  1.00 57.28           C  
ANISOU   49  CB  PRO A  24     8447   6003   7313   -689    163    240       C  
ATOM     50  CG  PRO A  24      -5.647  35.367 115.874  1.00 57.35           C  
ANISOU   50  CG  PRO A  24     8490   6178   7123   -727    127    250       C  
ATOM     51  CD  PRO A  24      -4.907  36.290 114.890  1.00 60.33           C  
ANISOU   51  CD  PRO A  24     8880   6602   7441   -712    193    151       C  
ATOM     52  N   LYS A  25      -4.526  33.933 112.644  1.00 55.20           N  
ANISOU   52  N   LYS A  25     8275   5681   7019   -697    389   -123       N  
ATOM     53  CA  LYS A  25      -4.547  33.426 111.288  1.00 58.57           C  
ANISOU   53  CA  LYS A  25     8758   6057   7439   -726    494   -305       C  
ATOM     54  C   LYS A  25      -4.752  34.577 110.347  1.00 51.45           C  
ANISOU   54  C   LYS A  25     7920   5309   6319   -794    521   -369       C  
ATOM     55  O   LYS A  25      -5.345  35.575 110.697  1.00 47.38           O  
ANISOU   55  O   LYS A  25     7427   4902   5672   -827    439   -281       O  
ATOM     56  CB  LYS A  25      -5.683  32.395 111.114  1.00 61.27           C  
ANISOU   56  CB  LYS A  25     9168   6300   7814   -781    465   -349       C  
ATOM     57  CG  LYS A  25      -7.047  32.950 111.473  1.00 61.29           C  
ANISOU   57  CG  LYS A  25     9222   6406   7660   -858    361   -263       C  
ATOM     58  CD  LYS A  25      -8.013  31.922 112.014  1.00 62.86           C  
ANISOU   58  CD  LYS A  25     9432   6506   7944   -897    295   -208       C  
ATOM     59  CE  LYS A  25      -8.619  31.069 110.930  1.00 66.80           C  
ANISOU   59  CE  LYS A  25    10010   6919   8451   -970    333   -362       C  
ATOM     60  NZ  LYS A  25      -9.904  30.467 111.393  1.00 68.35           N  
ANISOU   60  NZ  LYS A  25    10226   7082   8662  -1046    243   -288       N  
ATOM     61  N   ASP A  26      -4.273  34.408 109.137  1.00 51.77           N  
ANISOU   61  N   ASP A  26     7989   5356   6327   -818    637   -526       N  
ATOM     62  CA  ASP A  26      -4.367  35.391 108.069  1.00 51.64           C  
ANISOU   62  CA  ASP A  26     8036   5488   6098   -903    671   -584       C  
ATOM     63  C   ASP A  26      -5.675  35.411 107.343  1.00 53.07           C  
ANISOU   63  C   ASP A  26     8327   5718   6119  -1013    620   -629       C  
ATOM     64  O   ASP A  26      -5.961  36.359 106.600  1.00 52.47           O  
ANISOU   64  O   ASP A  26     8305   5775   5857  -1095    600   -623       O  
ATOM     65  CB  ASP A  26      -3.359  34.999 107.019  1.00 56.99           C  
ANISOU   65  CB  ASP A  26     8697   6163   6792   -904    833   -751       C  
ATOM     66  CG  ASP A  26      -1.997  35.222 107.472  1.00 60.87           C  
ANISOU   66  CG  ASP A  26     9068   6649   7412   -813    892   -709       C  
ATOM     67  OD1 ASP A  26      -1.846  35.870 108.545  1.00 62.32           O  
ANISOU   67  OD1 ASP A  26     9196   6852   7631   -770    791   -543       O  
ATOM     68  OD2 ASP A  26      -1.086  34.773 106.757  1.00 65.59           O  
ANISOU   68  OD2 ASP A  26     9619   7231   8070   -791   1041   -850       O  
ATOM     69  N   LEU A  27      -6.423  34.324 107.464  1.00 50.70           N  
ANISOU   69  N   LEU A  27     8057   5308   5898  -1026    597   -673       N  
ATOM     70  CA  LEU A  27      -7.602  34.153 106.645  1.00 51.96           C  
ANISOU   70  CA  LEU A  27     8315   5508   5921  -1143    556   -741       C  
ATOM     71  C   LEU A  27      -8.720  33.633 107.522  1.00 48.43           C  
ANISOU   71  C   LEU A  27     7862   4989   5549  -1147    444   -646       C  
ATOM     72  O   LEU A  27      -8.501  32.718 108.293  1.00 44.88           O  
ANISOU   72  O   LEU A  27     7367   4401   5284  -1084    449   -622       O  
ATOM     73  CB  LEU A  27      -7.287  33.164 105.515  1.00 54.68           C  
ANISOU   73  CB  LEU A  27     8714   5791   6270  -1192    679   -960       C  
ATOM     74  CG  LEU A  27      -8.488  32.601 104.752  1.00 58.19           C  
ANISOU   74  CG  LEU A  27     9261   6237   6613  -1322    632  -1054       C  
ATOM     75  CD1 LEU A  27      -9.113  33.663 103.860  1.00 55.85           C  
ANISOU   75  CD1 LEU A  27     9033   6136   6051  -1446    572  -1026       C  
ATOM     76  CD2 LEU A  27      -8.098  31.375 103.948  1.00 59.88           C  
ANISOU   76  CD2 LEU A  27     9519   6335   6899  -1348    759  -1291       C  
ATOM     77  N   TYR A  28      -9.886  34.261 107.446  1.00 46.01           N  
ANISOU   77  N   TYR A  28     7589   4782   5110  -1220    340   -576       N  
ATOM     78  CA  TYR A  28     -11.004  33.838 108.247  1.00 45.07           C  
ANISOU   78  CA  TYR A  28     7451   4626   5049  -1235    244   -485       C  
ATOM     79  C   TYR A  28     -12.153  33.544 107.304  1.00 48.96           C  
ANISOU   79  C   TYR A  28     8016   5153   5435  -1364    194   -555       C  
ATOM     80  O   TYR A  28     -12.421  34.311 106.351  1.00 54.75           O  
ANISOU   80  O   TYR A  28     8797   6008   5998  -1438    171   -582       O  
ATOM     81  CB  TYR A  28     -11.446  34.889 109.229  1.00 43.83           C  
ANISOU   81  CB  TYR A  28     7234   4563   4857  -1194    160   -327       C  
ATOM     82  CG  TYR A  28     -10.579  35.172 110.459  1.00 43.42           C  
ANISOU   82  CG  TYR A  28     7105   4493   4900  -1086    172   -229       C  
ATOM     83  CD1 TYR A  28      -9.376  35.835 110.348  1.00 46.64           C  
ANISOU   83  CD1 TYR A  28     7494   4927   5300  -1031    226   -239       C  
ATOM     84  CD2 TYR A  28     -11.046  34.916 111.752  1.00 44.65           C  
ANISOU   84  CD2 TYR A  28     7203   4636   5127  -1060    116   -113       C  
ATOM     85  CE1 TYR A  28      -8.629  36.172 111.478  1.00 46.42           C  
ANISOU   85  CE1 TYR A  28     7395   4899   5345   -950    217   -144       C  
ATOM     86  CE2 TYR A  28     -10.297  35.225 112.890  1.00 44.07           C  
ANISOU   86  CE2 TYR A  28     7064   4571   5108   -984    112    -18       C  
ATOM     87  CZ  TYR A  28      -9.101  35.857 112.753  1.00 45.36           C  
ANISOU   87  CZ  TYR A  28     7213   4751   5271   -929    156    -36       C  
ATOM     88  OH  TYR A  28      -8.363  36.205 113.848  1.00 49.45           O  
ANISOU   88  OH  TYR A  28     7666   5288   5832   -869    137     57       O  
ATOM     89  N   VAL A  29     -12.796  32.402 107.542  1.00 49.20           N  
ANISOU   89  N   VAL A  29     8053   5073   5567  -1404    169   -576       N  
ATOM     90  CA  VAL A  29     -14.024  32.024 106.879  1.00 49.86           C  
ANISOU   90  CA  VAL A  29     8189   5182   5575  -1536     97   -619       C  
ATOM     91  C   VAL A  29     -15.158  32.268 107.865  1.00 47.14           C  
ANISOU   91  C   VAL A  29     7770   4885   5257  -1540    -11   -454       C  
ATOM     92  O   VAL A  29     -15.159  31.764 108.984  1.00 53.50           O  
ANISOU   92  O   VAL A  29     8517   5615   6198  -1489    -15   -364       O  
ATOM     93  CB  VAL A  29     -14.002  30.568 106.386  1.00 52.08           C  
ANISOU   93  CB  VAL A  29     8530   5300   5958  -1598    143   -773       C  
ATOM     94  CG1 VAL A  29     -15.345  30.190 105.745  1.00 51.92           C  
ANISOU   94  CG1 VAL A  29     8560   5314   5854  -1755     49   -808       C  
ATOM     95  CG2 VAL A  29     -12.867  30.360 105.372  1.00 52.54           C  
ANISOU   95  CG2 VAL A  29     8650   5327   5984  -1590    276   -969       C  
ATOM     96  N   VAL A  30     -16.128  33.016 107.400  1.00 45.65           N  
ANISOU   96  N   VAL A  30     7580   4829   4937  -1610    -97   -414       N  
ATOM     97  CA  VAL A  30     -17.176  33.582 108.187  1.00 46.70           C  
ANISOU   97  CA  VAL A  30     7624   5046   5073  -1602   -185   -272       C  
ATOM     98  C   VAL A  30     -18.492  33.365 107.426  1.00 47.32           C  
ANISOU   98  C   VAL A  30     7714   5181   5083  -1740   -284   -283       C  
ATOM     99  O   VAL A  30     -18.549  33.517 106.190  1.00 47.72           O  
ANISOU   99  O   VAL A  30     7840   5281   5009  -1829   -309   -366       O  
ATOM    100  CB  VAL A  30     -16.893  35.080 108.364  1.00 52.00           C  
ANISOU  100  CB  VAL A  30     8257   5831   5671  -1520   -199   -200       C  
ATOM    101  CG1 VAL A  30     -18.054  35.814 109.007  1.00 58.56           C  
ANISOU  101  CG1 VAL A  30     8989   6757   6503  -1507   -285    -84       C  
ATOM    102  CG2 VAL A  30     -15.635  35.260 109.195  1.00 54.56           C  
ANISOU  102  CG2 VAL A  30     8561   6105   6064  -1399   -116   -182       C  
ATOM    103  N   GLU A  31     -19.546  33.011 108.148  1.00 46.31           N  
ANISOU  103  N   GLU A  31     7506   5063   5025  -1771   -344   -195       N  
ATOM    104  CA  GLU A  31     -20.794  32.690 107.495  1.00 46.08           C  
ANISOU  104  CA  GLU A  31     7471   5083   4956  -1910   -444   -197       C  
ATOM    105  C   GLU A  31     -21.558  33.951 107.274  1.00 47.46           C  
ANISOU  105  C   GLU A  31     7573   5410   5049  -1902   -534   -109       C  
ATOM    106  O   GLU A  31     -21.682  34.832 108.163  1.00 41.85           O  
ANISOU  106  O   GLU A  31     6764   4761   4377  -1793   -531    -12       O  
ATOM    107  CB  GLU A  31     -21.689  31.737 108.292  1.00 48.34           C  
ANISOU  107  CB  GLU A  31     7686   5320   5359  -1969   -475   -131       C  
ATOM    108  CG  GLU A  31     -21.090  30.421 108.754  1.00 49.21           C  
ANISOU  108  CG  GLU A  31     7843   5251   5603  -1976   -409   -172       C  
ATOM    109  CD  GLU A  31     -20.363  29.657 107.678  1.00 50.31           C  
ANISOU  109  CD  GLU A  31     8117   5263   5736  -2029   -365   -352       C  
ATOM    110  OE1 GLU A  31     -19.127  29.770 107.648  1.00 57.97           O  
ANISOU  110  OE1 GLU A  31     9132   6172   6721  -1929   -271   -417       O  
ATOM    111  OE2 GLU A  31     -21.004  28.944 106.884  1.00 49.78           O  
ANISOU  111  OE2 GLU A  31     8103   5159   5651  -2172   -418   -438       O  
ATOM    112  N   TYR A  32     -22.082  34.022 106.062  1.00 52.18           N  
ANISOU  112  N   TYR A  32     8219   6068   5538  -2024   -620   -149       N  
ATOM    113  CA  TYR A  32     -22.955  35.094 105.661  1.00 51.22           C  
ANISOU  113  CA  TYR A  32     8025   6081   5357  -2042   -741    -52       C  
ATOM    114  C   TYR A  32     -24.047  35.218 106.713  1.00 48.62           C  
ANISOU  114  C   TYR A  32     7531   5793   5147  -2002   -781     63       C  
ATOM    115  O   TYR A  32     -24.635  34.224 107.127  1.00 47.91           O  
ANISOU  115  O   TYR A  32     7407   5668   5129  -2071   -782     65       O  
ATOM    116  CB  TYR A  32     -23.578  34.753 104.298  1.00 52.28           C  
ANISOU  116  CB  TYR A  32     8226   6270   5367  -2225   -850    -99       C  
ATOM    117  CG  TYR A  32     -24.572  35.786 103.822  1.00 56.38           C  
ANISOU  117  CG  TYR A  32     8656   6925   5843  -2259  -1006     28       C  
ATOM    118  CD1 TYR A  32     -25.906  35.730 104.193  1.00 58.05           C  
ANISOU  118  CD1 TYR A  32     8723   7189   6144  -2293  -1107    125       C  
ATOM    119  CD2 TYR A  32     -24.152  36.858 103.023  1.00 61.90           C  
ANISOU  119  CD2 TYR A  32     9400   7695   6425  -2253  -1055     66       C  
ATOM    120  CE1 TYR A  32     -26.809  36.701 103.768  1.00 63.26           C  
ANISOU  120  CE1 TYR A  32     9278   7961   6798  -2308  -1258    250       C  
ATOM    121  CE2 TYR A  32     -25.032  37.830 102.572  1.00 62.35           C  
ANISOU  121  CE2 TYR A  32     9368   7855   6466  -2279  -1216    205       C  
ATOM    122  CZ  TYR A  32     -26.358  37.760 102.933  1.00 64.33           C  
ANISOU  122  CZ  TYR A  32     9468   8149   6826  -2299  -1320    295       C  
ATOM    123  OH  TYR A  32     -27.199  38.750 102.475  1.00 62.03           O  
ANISOU  123  OH  TYR A  32     9072   7948   6549  -2310  -1487    440       O  
ATOM    124  N   GLY A  33     -24.343  36.425 107.130  1.00 48.05           N  
ANISOU  124  N   GLY A  33     7355   5798   5103  -1898   -813    155       N  
ATOM    125  CA  GLY A  33     -25.468  36.622 108.032  1.00 46.38           C  
ANISOU  125  CA  GLY A  33     6971   5652   5000  -1863   -842    245       C  
ATOM    126  C   GLY A  33     -25.113  36.363 109.482  1.00 45.20           C  
ANISOU  126  C   GLY A  33     6770   5472   4932  -1765   -719    253       C  
ATOM    127  O   GLY A  33     -25.993  36.404 110.339  1.00 47.14           O  
ANISOU  127  O   GLY A  33     6873   5786   5253  -1746   -714    315       O  
ATOM    128  N   SER A  34     -23.840  36.104 109.779  1.00 41.39           N  
ANISOU  128  N   SER A  34     6393   4902   4431  -1709   -620    197       N  
ATOM    129  CA  SER A  34     -23.436  35.912 111.151  1.00 41.63           C  
ANISOU  129  CA  SER A  34     6379   4916   4521  -1627   -522    224       C  
ATOM    130  C   SER A  34     -22.669  37.163 111.698  1.00 41.37           C  
ANISOU  130  C   SER A  34     6333   4909   4476  -1479   -473    224       C  
ATOM    131  O   SER A  34     -22.468  38.109 110.991  1.00 44.68           O  
ANISOU  131  O   SER A  34     6777   5341   4857  -1444   -516    211       O  
ATOM    132  CB  SER A  34     -22.581  34.655 111.249  1.00 40.88           C  
ANISOU  132  CB  SER A  34     6389   4694   4449  -1669   -460    181       C  
ATOM    133  OG  SER A  34     -21.272  34.920 110.812  1.00 40.83           O  
ANISOU  133  OG  SER A  34     6491   4620   4402  -1608   -411    111       O  
ATOM    134  N   ASN A  35     -22.280  37.135 112.969  1.00 39.91           N  
ANISOU  134  N   ASN A  35     6108   4735   4320  -1411   -392    246       N  
ATOM    135  CA  ASN A  35     -21.424  38.141 113.570  1.00 40.29           C  
ANISOU  135  CA  ASN A  35     6159   4794   4354  -1290   -342    231       C  
ATOM    136  C   ASN A  35     -20.046  37.588 113.516  1.00 38.29           C  
ANISOU  136  C   ASN A  35     6020   4442   4087  -1281   -290    202       C  
ATOM    137  O   ASN A  35     -19.897  36.413 113.715  1.00 39.39           O  
ANISOU  137  O   ASN A  35     6188   4521   4258  -1337   -267    215       O  
ATOM    138  CB  ASN A  35     -21.867  38.379 115.005  1.00 39.27           C  
ANISOU  138  CB  ASN A  35     5916   4759   4246  -1244   -287    265       C  
ATOM    139  CG  ASN A  35     -23.354  38.686 115.061  1.00 41.81           C  
ANISOU  139  CG  ASN A  35     6097   5182   4606  -1263   -324    289       C  
ATOM    140  OD1 ASN A  35     -23.842  39.430 114.236  1.00 41.02           O  
ANISOU  140  OD1 ASN A  35     5969   5087   4528  -1244   -396    279       O  
ATOM    141  ND2 ASN A  35     -24.091  38.028 115.941  1.00 44.66           N  
ANISOU  141  ND2 ASN A  35     6365   5623   4982  -1315   -284    334       N  
ATOM    142  N   MET A  36     -19.048  38.406 113.186  1.00 39.59           N  
ANISOU  142  N   MET A  36     6243   4580   4221  -1214   -276    166       N  
ATOM    143  CA  MET A  36     -17.671  37.930 113.161  1.00 38.89           C  
ANISOU  143  CA  MET A  36     6238   4403   4134  -1194   -219    137       C  
ATOM    144  C   MET A  36     -16.772  38.664 114.110  1.00 38.49           C  
ANISOU  144  C   MET A  36     6169   4371   4084  -1102   -178    152       C  
ATOM    145  O   MET A  36     -17.016  39.811 114.444  1.00 37.60           O  
ANISOU  145  O   MET A  36     6011   4321   3955  -1048   -195    153       O  
ATOM    146  CB  MET A  36     -17.103  38.061 111.760  1.00 42.65           C  
ANISOU  146  CB  MET A  36     6809   4836   4562  -1225   -229     74       C  
ATOM    147  CG  MET A  36     -16.634  39.411 111.360  1.00 48.24           C  
ANISOU  147  CG  MET A  36     7529   5577   5222  -1175   -248     72       C  
ATOM    148  SD  MET A  36     -15.963  39.455 109.664  1.00 54.80           S  
ANISOU  148  SD  MET A  36     8473   6388   5960  -1247   -250     10       S  
ATOM    149  CE  MET A  36     -15.106  41.001 109.761  1.00 53.98           C  
ANISOU  149  CE  MET A  36     8364   6307   5838  -1171   -255     46       C  
ATOM    150  N   THR A  37     -15.691  38.006 114.493  1.00 39.07           N  
ANISOU  150  N   THR A  37     6277   4380   4189  -1086   -130    158       N  
ATOM    151  CA  THR A  37     -14.615  38.646 115.238  1.00 39.53           C  
ANISOU  151  CA  THR A  37     6328   4449   4243  -1013   -102    171       C  
ATOM    152  C   THR A  37     -13.295  38.249 114.651  1.00 40.77           C  
ANISOU  152  C   THR A  37     6544   4514   4433   -999    -64    140       C  
ATOM    153  O   THR A  37     -13.053  37.060 114.435  1.00 43.04           O  
ANISOU  153  O   THR A  37     6855   4716   4784  -1027    -40    134       O  
ATOM    154  CB  THR A  37     -14.607  38.159 116.681  1.00 41.21           C  
ANISOU  154  CB  THR A  37     6486   4701   4472  -1011    -87    244       C  
ATOM    155  OG1 THR A  37     -15.948  38.176 117.181  1.00 40.97           O  
ANISOU  155  OG1 THR A  37     6390   4761   4417  -1046   -101    268       O  
ATOM    156  CG2 THR A  37     -13.717  39.060 117.517  1.00 41.43           C  
ANISOU  156  CG2 THR A  37     6498   4775   4469   -950    -77    250       C  
ATOM    157  N   ILE A  38     -12.446  39.237 114.385  1.00 40.15           N  
ANISOU  157  N   ILE A  38     6483   4448   4326   -956    -56    116       N  
ATOM    158  CA  ILE A  38     -11.106  38.984 113.895  1.00 39.76           C  
ANISOU  158  CA  ILE A  38     6466   4333   4309   -937     -6     86       C  
ATOM    159  C   ILE A  38     -10.144  39.780 114.752  1.00 38.95           C  
ANISOU  159  C   ILE A  38     6327   4260   4212   -881     -6    123       C  
ATOM    160  O   ILE A  38     -10.506  40.833 115.225  1.00 40.56           O  
ANISOU  160  O   ILE A  38     6513   4529   4371   -865    -43    134       O  
ATOM    161  CB  ILE A  38     -10.978  39.377 112.384  1.00 39.51           C  
ANISOU  161  CB  ILE A  38     6496   4299   4216   -976      7     16       C  
ATOM    162  CG1 ILE A  38     -11.153  40.859 112.209  1.00 38.97           C  
ANISOU  162  CG1 ILE A  38     6427   4296   4083   -967    -42     36       C  
ATOM    163  CG2 ILE A  38     -11.983  38.617 111.527  1.00 38.77           C  
ANISOU  163  CG2 ILE A  38     6443   4191   4097  -1052     -7    -28       C  
ATOM    164  CD1 ILE A  38     -10.987  41.336 110.804  1.00 38.86           C  
ANISOU  164  CD1 ILE A  38     6472   4299   3994  -1023    -45      4       C  
ATOM    165  N   GLU A  39      -8.915  39.310 114.898  1.00 40.50           N  
ANISOU  165  N   GLU A  39     6510   4405   4475   -853     32    134       N  
ATOM    166  CA  GLU A  39      -8.024  39.745 115.978  1.00 44.82           C  
ANISOU  166  CA  GLU A  39     7007   4982   5041   -814     15    193       C  
ATOM    167  C   GLU A  39      -6.606  40.046 115.551  1.00 40.59           C  
ANISOU  167  C   GLU A  39     6457   4419   4546   -788     51    178       C  
ATOM    168  O   GLU A  39      -6.074  39.399 114.691  1.00 38.19           O  
ANISOU  168  O   GLU A  39     6161   4052   4297   -785    112    133       O  
ATOM    169  CB  GLU A  39      -7.902  38.609 117.009  1.00 46.96           C  
ANISOU  169  CB  GLU A  39     7234   5223   5387   -810      2    276       C  
ATOM    170  CG  GLU A  39      -9.232  38.102 117.533  1.00 50.48           C  
ANISOU  170  CG  GLU A  39     7678   5701   5801   -851    -25    310       C  
ATOM    171  CD  GLU A  39      -9.072  37.082 118.672  1.00 55.97           C  
ANISOU  171  CD  GLU A  39     8328   6382   6557   -866    -53    428       C  
ATOM    172  OE1 GLU A  39      -9.814  37.167 119.676  1.00 55.52           O  
ANISOU  172  OE1 GLU A  39     8245   6422   6427   -904    -83    488       O  
ATOM    173  OE2 GLU A  39      -8.173  36.232 118.586  1.00 58.09           O  
ANISOU  173  OE2 GLU A  39     8579   6546   6948   -842    -45    465       O  
ATOM    174  N   CYS A  40      -5.988  41.021 116.190  1.00 40.25           N  
ANISOU  174  N   CYS A  40     6387   4428   4479   -774     18    208       N  
ATOM    175  CA  CYS A  40      -4.549  41.219 116.098  1.00 41.19           C  
ANISOU  175  CA  CYS A  40     6463   4532   4654   -754     41    222       C  
ATOM    176  C   CYS A  40      -4.016  41.290 117.522  1.00 40.12           C  
ANISOU  176  C   CYS A  40     6269   4436   4539   -742    -19    306       C  
ATOM    177  O   CYS A  40      -4.655  41.880 118.386  1.00 36.44           O  
ANISOU  177  O   CYS A  40     5815   4038   3994   -760    -72    317       O  
ATOM    178  CB  CYS A  40      -4.245  42.526 115.374  1.00 45.02           C  
ANISOU  178  CB  CYS A  40     6976   5050   5078   -778     42    185       C  
ATOM    179  SG  CYS A  40      -4.618  42.471 113.597  1.00 44.76           S  
ANISOU  179  SG  CYS A  40     7012   5001   4995   -819    106    110       S  
ATOM    180  N   LYS A  41      -2.859  40.693 117.737  1.00 40.26           N  
ANISOU  180  N   LYS A  41     6218   4418   4662   -716     -9    358       N  
ATOM    181  CA  LYS A  41      -2.270  40.560 119.060  1.00 44.18           C  
ANISOU  181  CA  LYS A  41     6649   4953   5183   -717    -82    462       C  
ATOM    182  C   LYS A  41      -1.077  41.449 119.168  1.00 42.06           C  
ANISOU  182  C   LYS A  41     6332   4722   4926   -722   -104    475       C  
ATOM    183  O   LYS A  41      -0.356  41.628 118.203  1.00 38.53           O  
ANISOU  183  O   LYS A  41     5865   4241   4535   -707    -43    432       O  
ATOM    184  CB  LYS A  41      -1.809  39.102 119.345  1.00 48.16           C  
ANISOU  184  CB  LYS A  41     7087   5374   5839   -682    -84    549       C  
ATOM    185  CG  LYS A  41      -2.877  38.024 119.128  1.00 49.40           C  
ANISOU  185  CG  LYS A  41     7286   5461   6023   -685    -61    542       C  
ATOM    186  CD  LYS A  41      -4.096  38.243 120.001  1.00 54.55           C  
ANISOU  186  CD  LYS A  41     7982   6206   6540   -739   -114    576       C  
ATOM    187  CE  LYS A  41      -5.158  37.142 119.814  1.00 57.51           C  
ANISOU  187  CE  LYS A  41     8387   6515   6949   -758    -98    585       C  
ATOM    188  NZ  LYS A  41      -4.548  35.854 120.203  1.00 60.14           N  
ANISOU  188  NZ  LYS A  41     8661   6740   7449   -739   -126    698       N  
ATOM    189  N   PHE A  42      -0.845  41.961 120.367  1.00 40.49           N  
ANISOU  189  N   PHE A  42     6110   4604   4669   -756   -191    534       N  
ATOM    190  CA  PHE A  42       0.272  42.844 120.603  1.00 43.40           C  
ANISOU  190  CA  PHE A  42     6432   5014   5046   -779   -232    551       C  
ATOM    191  C   PHE A  42       0.768  42.587 121.997  1.00 45.87           C  
ANISOU  191  C   PHE A  42     6683   5396   5348   -811   -334    663       C  
ATOM    192  O   PHE A  42      -0.028  42.296 122.881  1.00 47.21           O  
ANISOU  192  O   PHE A  42     6885   5623   5430   -840   -375    695       O  
ATOM    193  CB  PHE A  42      -0.089  44.330 120.380  1.00 40.12           C  
ANISOU  193  CB  PHE A  42     6087   4634   4525   -818   -243    458       C  
ATOM    194  CG  PHE A  42      -1.197  44.842 121.253  1.00 40.68           C  
ANISOU  194  CG  PHE A  42     6221   4768   4470   -846   -286    414       C  
ATOM    195  CD1 PHE A  42      -2.538  44.528 120.971  1.00 40.50           C  
ANISOU  195  CD1 PHE A  42     6254   4732   4404   -825   -244    366       C  
ATOM    196  CD2 PHE A  42      -0.913  45.606 122.387  1.00 41.57           C  
ANISOU  196  CD2 PHE A  42     6328   4961   4505   -898   -364    411       C  
ATOM    197  CE1 PHE A  42      -3.571  44.983 121.783  1.00 37.43           C  
ANISOU  197  CE1 PHE A  42     5901   4412   3911   -845   -267    316       C  
ATOM    198  CE2 PHE A  42      -1.939  46.066 123.195  1.00 41.86           C  
ANISOU  198  CE2 PHE A  42     6415   5066   4423   -921   -381    343       C  
ATOM    199  CZ  PHE A  42      -3.276  45.760 122.886  1.00 38.85           C  
ANISOU  199  CZ  PHE A  42     6075   4672   4012   -889   -326    294       C  
ATOM    200  N   PRO A  43       2.089  42.653 122.187  1.00 49.11           N  
ANISOU  200  N   PRO A  43     6997   5814   5847   -816   -376    735       N  
ATOM    201  CA  PRO A  43       2.647  42.389 123.529  1.00 50.84           C  
ANISOU  201  CA  PRO A  43     7150   6113   6055   -861   -498    866       C  
ATOM    202  C   PRO A  43       2.182  43.445 124.530  1.00 53.83           C  
ANISOU  202  C   PRO A  43     7599   6617   6239   -950   -570    820       C  
ATOM    203  O   PRO A  43       2.242  44.654 124.248  1.00 54.54           O  
ANISOU  203  O   PRO A  43     7734   6718   6272   -977   -561    714       O  
ATOM    204  CB  PRO A  43       4.183  42.513 123.302  1.00 48.91           C  
ANISOU  204  CB  PRO A  43     6779   5852   5953   -850   -522    928       C  
ATOM    205  CG  PRO A  43       4.293  43.556 122.225  1.00 49.26           C  
ANISOU  205  CG  PRO A  43     6865   5872   5978   -853   -441    800       C  
ATOM    206  CD  PRO A  43       3.077  43.312 121.305  1.00 46.58           C  
ANISOU  206  CD  PRO A  43     6632   5468   5599   -810   -333    695       C  
ATOM    207  N   VAL A  44       1.754  42.991 125.697  1.00 60.67           N  
ANISOU  207  N   VAL A  44     8473   7574   7006  -1001   -641    898       N  
ATOM    208  CA  VAL A  44       1.452  43.879 126.814  1.00 65.91           C  
ANISOU  208  CA  VAL A  44     9189   8382   7474  -1098   -709    850       C  
ATOM    209  C   VAL A  44       2.246  43.476 128.078  1.00 67.69           C  
ANISOU  209  C   VAL A  44     9341   8723   7653  -1183   -848   1013       C  
ATOM    210  O   VAL A  44       2.236  42.319 128.487  1.00 62.82           O  
ANISOU  210  O   VAL A  44     8676   8111   7083  -1182   -890   1172       O  
ATOM    211  CB  VAL A  44      -0.051  43.858 127.117  1.00 71.15           C  
ANISOU  211  CB  VAL A  44     9940   9096   7996  -1109   -653    767       C  
ATOM    212  CG1 VAL A  44      -0.364  44.766 128.298  1.00 74.35           C  
ANISOU  212  CG1 VAL A  44    10395   9661   8195  -1207   -702    686       C  
ATOM    213  CG2 VAL A  44      -0.849  44.299 125.900  1.00 64.19           C  
ANISOU  213  CG2 VAL A  44     9121   8108   7160  -1033   -541    623       C  
ATOM    214  N   GLU A  45       2.927  44.447 128.688  1.00 74.84           N  
ANISOU  214  N   GLU A  45    10242   9719   8473  -1267   -931    981       N  
ATOM    215  CA  GLU A  45       3.715  44.196 129.902  1.00 81.77           C  
ANISOU  215  CA  GLU A  45    11053  10732   9283  -1372  -1083   1135       C  
ATOM    216  C   GLU A  45       2.802  43.823 131.075  1.00 81.80           C  
ANISOU  216  C   GLU A  45    11116  10893   9072  -1463  -1117   1172       C  
ATOM    217  O   GLU A  45       2.085  42.831 131.035  1.00 89.12           O  
ANISOU  217  O   GLU A  45    12047  11795  10021  -1428  -1076   1253       O  
ATOM    218  CB  GLU A  45       4.627  45.393 130.257  1.00 77.20           C  
ANISOU  218  CB  GLU A  45    10465  10219   8650  -1460  -1168   1072       C  
ATOM    219  N   LYS A  46       2.836  44.596 132.140  1.00 85.65           N  
ANISOU  219  N   LYS A  46    11647  11552   9344  -1593  -1191   1114       N  
ATOM    220  CA  LYS A  46       2.214  44.144 133.389  1.00 79.23           C  
ANISOU  220  CA  LYS A  46    10865  10932   8305  -1712  -1241   1188       C  
ATOM    221  C   LYS A  46       0.720  44.474 133.338  1.00 76.69           C  
ANISOU  221  C   LYS A  46    10647  10643   7850  -1692  -1095    996       C  
ATOM    222  O   LYS A  46      -0.126  43.615 133.529  1.00 73.15           O  
ANISOU  222  O   LYS A  46    10205  10230   7358  -1692  -1052   1073       O  
ATOM    223  CB  LYS A  46       2.902  44.821 134.578  1.00 72.32           C  
ANISOU  223  CB  LYS A  46     9994  10253   7232  -1878  -1380   1192       C  
ATOM    224  N   GLN A  47       0.429  45.742 133.065  1.00 73.64           N  
ANISOU  224  N   GLN A  47    10329  10231   7418  -1674  -1025    751       N  
ATOM    225  CA  GLN A  47      -0.906  46.281 132.996  1.00 67.49           C  
ANISOU  225  CA  GLN A  47     9631   9471   6543  -1644   -891    541       C  
ATOM    226  C   GLN A  47      -0.996  47.087 131.697  1.00 71.32           C  
ANISOU  226  C   GLN A  47    10140   9749   7208  -1517   -811    389       C  
ATOM    227  O   GLN A  47       0.038  47.508 131.137  1.00 76.92           O  
ANISOU  227  O   GLN A  47    10821  10354   8050  -1496   -864    408       O  
ATOM    228  CB  GLN A  47      -1.132  47.244 134.151  1.00 70.91           C  
ANISOU  228  CB  GLN A  47    10123  10091   6727  -1770   -905    369       C  
ATOM    229  CG  GLN A  47      -0.712  46.740 135.538  1.00 81.43           C  
ANISOU  229  CG  GLN A  47    11439  11665   7836  -1944  -1023    515       C  
ATOM    230  CD  GLN A  47      -0.620  47.844 136.592  1.00 81.92           C  
ANISOU  230  CD  GLN A  47    11565  11905   7657  -2085  -1053    317       C  
ATOM    231  OE1 GLN A  47      -1.055  48.965 136.359  1.00 87.05           O  
ANISOU  231  OE1 GLN A  47    12275  12492   8310  -2043   -967     50       O  
ATOM    232  NE2 GLN A  47      -0.042  47.525 137.753  1.00 81.42           N  
ANISOU  232  NE2 GLN A  47    11487  12059   7388  -2259  -1184    449       N  
ATOM    233  N   LEU A  48      -2.222  47.347 131.243  1.00 65.05           N  
ANISOU  233  N   LEU A  48     9392   8908   6418  -1443   -690    245       N  
ATOM    234  CA  LEU A  48      -2.437  48.181 130.076  1.00 60.24           C  
ANISOU  234  CA  LEU A  48     8811   8119   5959  -1339   -627    110       C  
ATOM    235  C   LEU A  48      -2.392  49.669 130.397  1.00 56.64           C  
ANISOU  235  C   LEU A  48     8409   7659   5453  -1373   -636   -102       C  
ATOM    236  O   LEU A  48      -3.271  50.170 131.100  1.00 54.95           O  
ANISOU  236  O   LEU A  48     8232   7537   5109  -1398   -583   -265       O  
ATOM    237  CB  LEU A  48      -3.791  47.868 129.423  1.00 57.98           C  
ANISOU  237  CB  LEU A  48     8539   7775   5715  -1248   -512     56       C  
ATOM    238  CG  LEU A  48      -4.097  48.528 128.074  1.00 53.22           C  
ANISOU  238  CG  LEU A  48     7960   6985   5276  -1142   -460    -34       C  
ATOM    239  CD1 LEU A  48      -3.133  48.012 127.030  1.00 53.92           C  
ANISOU  239  CD1 LEU A  48     8016   6950   5520  -1103   -488    104       C  
ATOM    240  CD2 LEU A  48      -5.528  48.309 127.617  1.00 51.63           C  
ANISOU  240  CD2 LEU A  48     7765   6760   5093  -1072   -366    -95       C  
ATOM    241  N   ASP A  49      -1.419  50.378 129.811  1.00 53.38           N  
ANISOU  241  N   ASP A  49     7994   7127   5161  -1368   -693   -108       N  
ATOM    242  CA  ASP A  49      -1.490  51.837 129.741  1.00 54.13           C  
ANISOU  242  CA  ASP A  49     8145   7139   5282  -1373   -695   -310       C  
ATOM    243  C   ASP A  49      -2.332  52.347 128.540  1.00 52.78           C  
ANISOU  243  C   ASP A  49     8000   6790   5266  -1252   -614   -394       C  
ATOM    244  O   ASP A  49      -1.856  52.394 127.410  1.00 49.95           O  
ANISOU  244  O   ASP A  49     7628   6296   5057  -1206   -623   -311       O  
ATOM    245  CB  ASP A  49      -0.098  52.407 129.670  1.00 55.29           C  
ANISOU  245  CB  ASP A  49     8276   7241   5492  -1442   -802   -266       C  
ATOM    246  CG  ASP A  49      -0.090  53.873 129.894  1.00 57.97           C  
ANISOU  246  CG  ASP A  49     8677   7511   5838  -1483   -828   -472       C  
ATOM    247  OD1 ASP A  49      -1.204  54.429 130.126  1.00 51.62           O  
ANISOU  247  OD1 ASP A  49     7924   6692   4997  -1442   -754   -660       O  
ATOM    248  OD2 ASP A  49       1.037  54.444 129.849  1.00 66.67           O  
ANISOU  248  OD2 ASP A  49     9767   8570   6994  -1556   -922   -445       O  
ATOM    249  N   LEU A  50      -3.570  52.741 128.814  1.00 55.80           N  
ANISOU  249  N   LEU A  50     8411   7186   5605  -1209   -538   -554       N  
ATOM    250  CA  LEU A  50      -4.529  53.182 127.805  1.00 56.98           C  
ANISOU  250  CA  LEU A  50     8572   7185   5895  -1097   -474   -624       C  
ATOM    251  C   LEU A  50      -4.083  54.368 127.043  1.00 57.70           C  
ANISOU  251  C   LEU A  50     8693   7089   6140  -1079   -524   -679       C  
ATOM    252  O   LEU A  50      -4.193  54.400 125.830  1.00 64.60           O  
ANISOU  252  O   LEU A  50     9564   7832   7149  -1016   -518   -603       O  
ATOM    253  CB  LEU A  50      -5.853  53.592 128.432  1.00 59.42           C  
ANISOU  253  CB  LEU A  50     8886   7547   6143  -1060   -392   -814       C  
ATOM    254  CG  LEU A  50      -7.009  52.600 128.398  1.00 63.71           C  
ANISOU  254  CG  LEU A  50     9388   8180   6640  -1011   -302   -767       C  
ATOM    255  CD1 LEU A  50      -8.322  53.374 128.589  1.00 66.88           C  
ANISOU  255  CD1 LEU A  50     9775   8562   7074   -939   -218   -976       C  
ATOM    256  CD2 LEU A  50      -6.994  51.753 127.127  1.00 59.93           C  
ANISOU  256  CD2 LEU A  50     8890   7605   6278   -952   -305   -583       C  
ATOM    257  N   ALA A  51      -3.673  55.369 127.791  1.00 58.72           N  
ANISOU  257  N   ALA A  51     8856   7214   6241  -1143   -572   -822       N  
ATOM    258  CA  ALA A  51      -3.145  56.636 127.273  1.00 62.86           C  
ANISOU  258  CA  ALA A  51     9415   7554   6914  -1154   -640   -885       C  
ATOM    259  C   ALA A  51      -1.980  56.445 126.314  1.00 58.11           C  
ANISOU  259  C   ALA A  51     8792   6882   6405  -1187   -702   -690       C  
ATOM    260  O   ALA A  51      -1.472  57.412 125.738  1.00 64.77           O  
ANISOU  260  O   ALA A  51     9658   7575   7377  -1210   -761   -698       O  
ATOM    261  CB  ALA A  51      -2.647  57.528 128.466  1.00 59.31           C  
ANISOU  261  CB  ALA A  51     9006   7148   6382  -1258   -696  -1063       C  
ATOM    262  N   ALA A  52      -1.447  55.250 126.216  1.00 53.68           N  
ANISOU  262  N   ALA A  52     8182   6429   5784  -1201   -694   -519       N  
ATOM    263  CA  ALA A  52      -0.290  55.091 125.352  1.00 51.33           C  
ANISOU  263  CA  ALA A  52     7847   6078   5578  -1231   -735   -358       C  
ATOM    264  C   ALA A  52      -0.671  54.253 124.190  1.00 44.68           C  
ANISOU  264  C   ALA A  52     6982   5199   4797  -1149   -664   -240       C  
ATOM    265  O   ALA A  52       0.209  53.782 123.456  1.00 44.39           O  
ANISOU  265  O   ALA A  52     6899   5152   4816  -1161   -664   -104       O  
ATOM    266  CB  ALA A  52       0.878  54.464 126.113  1.00 50.94           C  
ANISOU  266  CB  ALA A  52     7741   6164   5450  -1318   -796   -255       C  
ATOM    267  N   LEU A  53      -1.971  54.038 124.014  1.00 44.23           N  
ANISOU  267  N   LEU A  53     6949   5129   4729  -1069   -598   -299       N  
ATOM    268  CA  LEU A  53      -2.457  52.975 123.091  1.00 42.68           C  
ANISOU  268  CA  LEU A  53     6732   4933   4554  -1003   -530   -194       C  
ATOM    269  C   LEU A  53      -3.325  53.509 121.998  1.00 37.88           C  
ANISOU  269  C   LEU A  53     6155   4202   4035   -944   -509   -219       C  
ATOM    270  O   LEU A  53      -4.260  54.264 122.239  1.00 38.30           O  
ANISOU  270  O   LEU A  53     6233   4205   4113   -906   -511   -337       O  
ATOM    271  CB  LEU A  53      -3.256  51.924 123.850  1.00 42.65           C  
ANISOU  271  CB  LEU A  53     6710   5051   4444   -977   -479   -198       C  
ATOM    272  CG  LEU A  53      -3.762  50.737 122.995  1.00 43.99           C  
ANISOU  272  CG  LEU A  53     6861   5216   4638   -922   -416    -99       C  
ATOM    273  CD1 LEU A  53      -2.645  49.781 122.588  1.00 42.21           C  
ANISOU  273  CD1 LEU A  53     6591   5000   4448   -940   -417     42       C  
ATOM    274  CD2 LEU A  53      -4.798  49.924 123.746  1.00 47.13           C  
ANISOU  274  CD2 LEU A  53     7246   5716   4944   -906   -371   -117       C  
ATOM    275  N   ILE A  54      -3.032  53.103 120.787  1.00 36.10           N  
ANISOU  275  N   ILE A  54     5922   3934   3859   -937   -487   -109       N  
ATOM    276  CA  ILE A  54      -3.889  53.517 119.684  1.00 38.48           C  
ANISOU  276  CA  ILE A  54     6254   4140   4228   -897   -481   -105       C  
ATOM    277  C   ILE A  54      -4.222  52.258 118.888  1.00 38.58           C  
ANISOU  277  C   ILE A  54     6254   4199   4208   -870   -415    -23       C  
ATOM    278  O   ILE A  54      -3.365  51.389 118.691  1.00 38.33           O  
ANISOU  278  O   ILE A  54     6193   4216   4155   -893   -380     51       O  
ATOM    279  CB  ILE A  54      -3.174  54.545 118.781  1.00 41.79           C  
ANISOU  279  CB  ILE A  54     6695   4451   4733   -950   -536    -51       C  
ATOM    280  CG1 ILE A  54      -2.897  55.851 119.557  1.00 41.90           C  
ANISOU  280  CG1 ILE A  54     6729   4387   4804   -982   -613   -145       C  
ATOM    281  CG2 ILE A  54      -4.020  54.830 117.555  1.00 44.63           C  
ANISOU  281  CG2 ILE A  54     7083   4730   5144   -925   -544     -6       C  
ATOM    282  CD1 ILE A  54      -2.138  56.903 118.793  1.00 40.64           C  
ANISOU  282  CD1 ILE A  54     6589   4112   4741  -1053   -681    -80       C  
ATOM    283  N   VAL A  55      -5.468  52.129 118.491  1.00 35.74           N  
ANISOU  283  N   VAL A  55     5907   3821   3854   -821   -398    -47       N  
ATOM    284  CA  VAL A  55      -5.860  50.965 117.699  1.00 38.03           C  
ANISOU  284  CA  VAL A  55     6192   4145   4111   -809   -343     15       C  
ATOM    285  C   VAL A  55      -6.680  51.443 116.516  1.00 37.32           C  
ANISOU  285  C   VAL A  55     6131   3988   4061   -803   -370     38       C  
ATOM    286  O   VAL A  55      -7.623  52.219 116.675  1.00 39.86           O  
ANISOU  286  O   VAL A  55     6452   4259   4433   -764   -412    -12       O  
ATOM    287  CB  VAL A  55      -6.701  49.958 118.500  1.00 38.06           C  
ANISOU  287  CB  VAL A  55     6170   4229   4061   -774   -300    -15       C  
ATOM    288  CG1 VAL A  55      -7.090  48.761 117.647  1.00 38.52           C  
ANISOU  288  CG1 VAL A  55     6230   4301   4104   -772   -253     41       C  
ATOM    289  CG2 VAL A  55      -5.925  49.478 119.722  1.00 42.35           C  
ANISOU  289  CG2 VAL A  55     6684   4851   4554   -796   -294    -11       C  
ATOM    290  N   TYR A  56      -6.305  50.962 115.345  1.00 35.61           N  
ANISOU  290  N   TYR A  56     5934   3776   3822   -843   -345    112       N  
ATOM    291  CA  TYR A  56      -6.936  51.319 114.087  1.00 36.44           C  
ANISOU  291  CA  TYR A  56     6072   3841   3933   -867   -380    162       C  
ATOM    292  C   TYR A  56      -7.231  50.060 113.250  1.00 37.26           C  
ANISOU  292  C   TYR A  56     6188   4005   3966   -888   -319    184       C  
ATOM    293  O   TYR A  56      -6.386  49.166 113.096  1.00 41.18           O  
ANISOU  293  O   TYR A  56     6678   4542   4425   -909   -245    188       O  
ATOM    294  CB  TYR A  56      -5.962  52.240 113.365  1.00 39.41           C  
ANISOU  294  CB  TYR A  56     6472   4173   4330   -937   -416    229       C  
ATOM    295  CG  TYR A  56      -6.244  52.629 111.929  1.00 39.56           C  
ANISOU  295  CG  TYR A  56     6530   4174   4327  -1002   -457    320       C  
ATOM    296  CD1 TYR A  56      -7.340  53.394 111.596  1.00 39.93           C  
ANISOU  296  CD1 TYR A  56     6588   4151   4432   -985   -552    350       C  
ATOM    297  CD2 TYR A  56      -5.386  52.251 110.914  1.00 39.68           C  
ANISOU  297  CD2 TYR A  56     6563   4249   4263  -1087   -402    379       C  
ATOM    298  CE1 TYR A  56      -7.590  53.771 110.281  1.00 41.90           C  
ANISOU  298  CE1 TYR A  56     6874   4395   4652  -1062   -612    461       C  
ATOM    299  CE2 TYR A  56      -5.645  52.597 109.594  1.00 43.63           C  
ANISOU  299  CE2 TYR A  56     7107   4763   4709  -1171   -441    469       C  
ATOM    300  CZ  TYR A  56      -6.733  53.370 109.271  1.00 42.68           C  
ANISOU  300  CZ  TYR A  56     7005   4575   4637  -1166   -557    523       C  
ATOM    301  OH  TYR A  56      -6.956  53.720 107.928  1.00 41.24           O  
ANISOU  301  OH  TYR A  56     6866   4419   4387  -1269   -616    642       O  
ATOM    302  N   TRP A  57      -8.456  49.983 112.759  1.00 36.52           N  
ANISOU  302  N   TRP A  57     6102   3906   3865   -879   -353    190       N  
ATOM    303  CA  TRP A  57      -8.845  49.017 111.764  1.00 37.90           C  
ANISOU  303  CA  TRP A  57     6304   4127   3970   -923   -320    209       C  
ATOM    304  C   TRP A  57      -9.400  49.742 110.530  1.00 37.90           C  
ANISOU  304  C   TRP A  57     6339   4110   3950   -982   -402    282       C  
ATOM    305  O   TRP A  57     -10.175  50.717 110.620  1.00 36.10           O  
ANISOU  305  O   TRP A  57     6093   3827   3797   -952   -497    311       O  
ATOM    306  CB  TRP A  57      -9.942  48.119 112.317  1.00 36.68           C  
ANISOU  306  CB  TRP A  57     6119   3999   3817   -880   -303    165       C  
ATOM    307  CG  TRP A  57      -9.484  47.128 113.355  1.00 37.43           C  
ANISOU  307  CG  TRP A  57     6187   4123   3913   -847   -230    125       C  
ATOM    308  CD1 TRP A  57      -9.493  47.281 114.726  1.00 38.75           C  
ANISOU  308  CD1 TRP A  57     6312   4304   4109   -797   -227     94       C  
ATOM    309  CD2 TRP A  57      -9.021  45.799 113.106  1.00 38.71           C  
ANISOU  309  CD2 TRP A  57     6359   4301   4050   -869   -156    117       C  
ATOM    310  NE1 TRP A  57      -9.000  46.160 115.328  1.00 39.34           N  
ANISOU  310  NE1 TRP A  57     6369   4407   4170   -795   -171     97       N  
ATOM    311  CE2 TRP A  57      -8.706  45.227 114.365  1.00 40.15           C  
ANISOU  311  CE2 TRP A  57     6499   4496   4260   -829   -127    110       C  
ATOM    312  CE3 TRP A  57      -8.832  45.035 111.933  1.00 39.34           C  
ANISOU  312  CE3 TRP A  57     6479   4383   4086   -923   -112    108       C  
ATOM    313  CZ2 TRP A  57      -8.224  43.928 114.493  1.00 40.35           C  
ANISOU  313  CZ2 TRP A  57     6513   4512   4304   -830    -69    114       C  
ATOM    314  CZ3 TRP A  57      -8.317  43.770 112.043  1.00 41.60           C  
ANISOU  314  CZ3 TRP A  57     6757   4657   4392   -917    -36     78       C  
ATOM    315  CH2 TRP A  57      -8.013  43.210 113.327  1.00 40.92           C  
ANISOU  315  CH2 TRP A  57     6621   4560   4368   -865    -21     91       C  
ATOM    316  N   GLU A  58      -9.052  49.219 109.375  1.00 40.06           N  
ANISOU  316  N   GLU A  58     6658   4437   4126  -1067   -367    309       N  
ATOM    317  CA  GLU A  58      -9.621  49.714 108.138  1.00 45.75           C  
ANISOU  317  CA  GLU A  58     7419   5175   4790  -1150   -449    393       C  
ATOM    318  C   GLU A  58      -9.868  48.553 107.202  1.00 42.76           C  
ANISOU  318  C   GLU A  58     7082   4879   4286  -1225   -395    362       C  
ATOM    319  O   GLU A  58      -9.252  47.508 107.325  1.00 42.17           O  
ANISOU  319  O   GLU A  58     7012   4833   4179  -1220   -280    280       O  
ATOM    320  CB  GLU A  58      -8.676  50.722 107.456  1.00 47.11           C  
ANISOU  320  CB  GLU A  58     7621   5340   4938  -1230   -479    483       C  
ATOM    321  CG  GLU A  58      -7.294  50.146 107.176  1.00 51.64           C  
ANISOU  321  CG  GLU A  58     8208   5979   5435  -1280   -349    446       C  
ATOM    322  CD  GLU A  58      -6.618  50.763 105.965  1.00 62.96           C  
ANISOU  322  CD  GLU A  58     9683   7470   6770  -1414   -358    542       C  
ATOM    323  OE1 GLU A  58      -7.321  51.391 105.158  1.00 74.70           O  
ANISOU  323  OE1 GLU A  58    11205   8963   8216  -1486   -468    645       O  
ATOM    324  OE2 GLU A  58      -5.381  50.634 105.803  1.00 68.40           O  
ANISOU  324  OE2 GLU A  58    10360   8207   7424  -1455   -258    526       O  
ATOM    325  N   MET A  59     -10.713  48.776 106.213  1.00 45.59           N  
ANISOU  325  N   MET A  59     7470   5272   4580  -1301   -486    431       N  
ATOM    326  CA  MET A  59     -10.834  47.804 105.123  1.00 46.85           C  
ANISOU  326  CA  MET A  59     7688   5525   4588  -1409   -442    396       C  
ATOM    327  C   MET A  59     -11.055  48.554 103.829  1.00 46.93           C  
ANISOU  327  C   MET A  59     7748   5598   4486  -1542   -544    519       C  
ATOM    328  O   MET A  59     -11.940  49.420 103.769  1.00 45.21           O  
ANISOU  328  O   MET A  59     7503   5339   4335  -1534   -694    631       O  
ATOM    329  CB  MET A  59     -12.026  46.901 105.367  1.00 46.81           C  
ANISOU  329  CB  MET A  59     7663   5521   4602  -1382   -463    343       C  
ATOM    330  CG  MET A  59     -12.237  45.921 104.227  1.00 60.57           C  
ANISOU  330  CG  MET A  59     9474   7351   6190  -1506   -432    291       C  
ATOM    331  SD  MET A  59     -13.831  46.113 103.400  1.00 59.85           S  
ANISOU  331  SD  MET A  59     9385   7312   6043  -1597   -606    384       S  
ATOM    332  CE  MET A  59     -13.989  44.409 102.930  1.00 62.49           C  
ANISOU  332  CE  MET A  59     9777   7696   6269  -1676   -507    229       C  
ATOM    333  N   GLU A  60     -10.277  48.235 102.799  1.00 48.62           N  
ANISOU  333  N   GLU A  60     8027   5913   4535  -1666   -467    502       N  
ATOM    334  CA  GLU A  60     -10.448  48.915 101.494  1.00 57.16           C  
ANISOU  334  CA  GLU A  60     9165   7086   5468  -1826   -566    637       C  
ATOM    335  C   GLU A  60     -10.570  50.416 101.646  1.00 58.96           C  
ANISOU  335  C   GLU A  60     9362   7232   5807  -1811   -717    814       C  
ATOM    336  O   GLU A  60     -11.515  51.032 101.134  1.00 62.77           O  
ANISOU  336  O   GLU A  60     9844   7711   6294  -1861   -885    951       O  
ATOM    337  CB  GLU A  60     -11.655  48.338 100.752  1.00 56.39           C  
ANISOU  337  CB  GLU A  60     9101   7060   5267  -1911   -652    641       C  
ATOM    338  CG  GLU A  60     -11.242  46.990 100.166  1.00 58.55           C  
ANISOU  338  CG  GLU A  60     9436   7433   5379  -1989   -496    470       C  
ATOM    339  CD  GLU A  60     -12.386  46.089  99.827  1.00 63.39           C  
ANISOU  339  CD  GLU A  60    10072   8081   5934  -2038   -547    410       C  
ATOM    340  OE1 GLU A  60     -13.526  46.647  99.678  1.00 62.10           O  
ANISOU  340  OE1 GLU A  60     9882   7913   5801  -2059   -729    544       O  
ATOM    341  OE2 GLU A  60     -12.091  44.843  99.714  1.00 59.65           O  
ANISOU  341  OE2 GLU A  60     9633   7627   5402  -2053   -407    229       O  
ATOM    342  N   ASP A  61      -9.638  50.949 102.428  1.00 59.08           N  
ANISOU  342  N   ASP A  61     9343   7169   5935  -1734   -661    802       N  
ATOM    343  CA  ASP A  61      -9.484  52.367 102.692  1.00 66.83           C  
ANISOU  343  CA  ASP A  61    10299   8046   7047  -1716   -779    940       C  
ATOM    344  C   ASP A  61     -10.658  52.980 103.418  1.00 63.79           C  
ANISOU  344  C   ASP A  61     9855   7527   6856  -1595   -919    977       C  
ATOM    345  O   ASP A  61     -10.686  54.177 103.616  1.00 70.54           O  
ANISOU  345  O   ASP A  61    10686   8267   7848  -1571  -1032   1081       O  
ATOM    346  CB  ASP A  61      -9.167  53.149 101.394  1.00 73.55           C  
ANISOU  346  CB  ASP A  61    11206   8974   7766  -1898   -862   1121       C  
ATOM    347  CG  ASP A  61      -7.894  52.652 100.713  1.00 79.04           C  
ANISOU  347  CG  ASP A  61    11943   9816   8271  -2020   -698   1072       C  
ATOM    348  OD1 ASP A  61      -6.831  52.648 101.393  1.00 74.19           O  
ANISOU  348  OD1 ASP A  61    11294   9169   7728  -1960   -583    999       O  
ATOM    349  OD2 ASP A  61      -7.969  52.261  99.513  1.00 82.40           O  
ANISOU  349  OD2 ASP A  61    12431  10401   8478  -2178   -682   1102       O  
ATOM    350  N   LYS A  62     -11.632  52.192 103.830  1.00 59.86           N  
ANISOU  350  N   LYS A  62     9324   7035   6386  -1518   -912    888       N  
ATOM    351  CA  LYS A  62     -12.629  52.747 104.718  1.00 55.11           C  
ANISOU  351  CA  LYS A  62     8641   6311   5985  -1383  -1005    889       C  
ATOM    352  C   LYS A  62     -12.147  52.554 106.150  1.00 51.50           C  
ANISOU  352  C   LYS A  62     8144   5793   5633  -1249   -890    743       C  
ATOM    353  O   LYS A  62     -11.600  51.520 106.536  1.00 51.39           O  
ANISOU  353  O   LYS A  62     8143   5839   5544  -1237   -753    629       O  
ATOM    354  CB  LYS A  62     -13.984  52.118 104.477  1.00 58.16           C  
ANISOU  354  CB  LYS A  62     8993   6743   6361  -1378  -1066    886       C  
ATOM    355  CG  LYS A  62     -14.584  52.468 103.115  1.00 60.83           C  
ANISOU  355  CG  LYS A  62     9362   7142   6610  -1516  -1221   1055       C  
ATOM    356  N   ASN A  63     -12.359  53.576 106.939  1.00 51.43           N  
ANISOU  356  N   ASN A  63     8082   5657   5803  -1152   -956    748       N  
ATOM    357  CA  ASN A  63     -11.966  53.569 108.306  1.00 49.78           C  
ANISOU  357  CA  ASN A  63     7837   5398   5681  -1042   -870    617       C  
ATOM    358  C   ASN A  63     -13.034  52.934 109.212  1.00 50.47           C  
ANISOU  358  C   ASN A  63     7853   5501   5823   -936   -834    510       C  
ATOM    359  O   ASN A  63     -14.156  53.429 109.341  1.00 49.69           O  
ANISOU  359  O   ASN A  63     7687   5348   5844   -873   -919    526       O  
ATOM    360  CB  ASN A  63     -11.702  54.972 108.770  1.00 50.04           C  
ANISOU  360  CB  ASN A  63     7850   5287   5875   -996   -949    643       C  
ATOM    361  CG  ASN A  63     -10.339  55.555 108.296  1.00 56.70           C  
ANISOU  361  CG  ASN A  63     8753   6114   6675  -1097   -949    721       C  
ATOM    362  OD1 ASN A  63     -10.165  56.756 108.444  1.00 56.14           O  
ANISOU  362  OD1 ASN A  63     8677   5912   6742  -1087  -1040    772       O  
ATOM    363  ND2 ASN A  63      -9.388  54.747 107.741  1.00 52.72           N  
ANISOU  363  ND2 ASN A  63     8297   5735   6001  -1191   -847    726       N  
ATOM    364  N   ILE A  64     -12.655  51.874 109.909  1.00 46.78           N  
ANISOU  364  N   ILE A  64     7388   5104   5284   -915   -708    406       N  
ATOM    365  CA  ILE A  64     -13.642  51.181 110.726  1.00 48.19           C  
ANISOU  365  CA  ILE A  64     7501   5318   5491   -842   -669    325       C  
ATOM    366  C   ILE A  64     -13.581  51.633 112.181  1.00 43.58           C  
ANISOU  366  C   ILE A  64     6865   4695   5000   -741   -627    222       C  
ATOM    367  O   ILE A  64     -14.598  51.997 112.771  1.00 48.18           O  
ANISOU  367  O   ILE A  64     7370   5257   5681   -663   -649    175       O  
ATOM    368  CB  ILE A  64     -13.499  49.647 110.588  1.00 44.81           C  
ANISOU  368  CB  ILE A  64     7102   4986   4938   -890   -574    288       C  
ATOM    369  CG1 ILE A  64     -13.642  49.240 109.112  1.00 46.58           C  
ANISOU  369  CG1 ILE A  64     7384   5257   5058  -1002   -614    361       C  
ATOM    370  CG2 ILE A  64     -14.568  48.948 111.405  1.00 47.34           C  
ANISOU  370  CG2 ILE A  64     7351   5345   5291   -835   -544    229       C  
ATOM    371  CD1 ILE A  64     -13.106  47.858 108.761  1.00 45.82           C  
ANISOU  371  CD1 ILE A  64     7340   5226   4842  -1065   -510    307       C  
ATOM    372  N   ILE A  65     -12.395  51.582 112.755  1.00 40.94           N  
ANISOU  372  N   ILE A  65     6564   4363   4626   -749   -562    182       N  
ATOM    373  CA  ILE A  65     -12.236  51.824 114.175  1.00 40.74           C  
ANISOU  373  CA  ILE A  65     6502   4335   4641   -681   -515     77       C  
ATOM    374  C   ILE A  65     -11.090  52.762 114.324  1.00 40.70           C  
ANISOU  374  C   ILE A  65     6534   4260   4670   -699   -540     78       C  
ATOM    375  O   ILE A  65     -10.020  52.507 113.793  1.00 42.75           O  
ANISOU  375  O   ILE A  65     6840   4537   4864   -767   -521    135       O  
ATOM    376  CB  ILE A  65     -11.863  50.546 114.958  1.00 39.64           C  
ANISOU  376  CB  ILE A  65     6360   4297   4404   -689   -414     34       C  
ATOM    377  CG1 ILE A  65     -13.075  49.653 115.136  1.00 40.50           C  
ANISOU  377  CG1 ILE A  65     6419   4473   4495   -672   -386     19       C  
ATOM    378  CG2 ILE A  65     -11.318  50.921 116.348  1.00 40.44           C  
ANISOU  378  CG2 ILE A  65     6443   4411   4511   -656   -380    -51       C  
ATOM    379  CD1 ILE A  65     -14.196  50.321 115.952  1.00 40.57           C  
ANISOU  379  CD1 ILE A  65     6347   4482   4587   -595   -396    -57       C  
ATOM    380  N   GLN A  66     -11.295  53.844 115.037  1.00 47.02           N  
ANISOU  380  N   GLN A  66     7308   4980   5578   -643   -578      7       N  
ATOM    381  CA  GLN A  66     -10.169  54.665 115.439  1.00 49.22           C  
ANISOU  381  CA  GLN A  66     7620   5195   5887   -668   -597    -16       C  
ATOM    382  C   GLN A  66     -10.186  54.956 116.899  1.00 45.71           C  
ANISOU  382  C   GLN A  66     7147   4763   5459   -617   -558   -164       C  
ATOM    383  O   GLN A  66     -10.854  55.857 117.370  1.00 48.05           O  
ANISOU  383  O   GLN A  66     7410   4978   5868   -552   -588   -258       O  
ATOM    384  CB  GLN A  66     -10.071  55.947 114.641  1.00 52.18           C  
ANISOU  384  CB  GLN A  66     8017   5424   6384   -689   -707     58       C  
ATOM    385  CG  GLN A  66      -8.638  56.433 114.772  1.00 58.59           C  
ANISOU  385  CG  GLN A  66     8873   6205   7185   -760   -716     76       C  
ATOM    386  CD  GLN A  66      -8.157  57.237 113.614  1.00 62.42           C  
ANISOU  386  CD  GLN A  66     9396   6599   7721   -840   -805    218       C  
ATOM    387  OE1 GLN A  66      -7.786  58.401 113.797  1.00 67.92           O  
ANISOU  387  OE1 GLN A  66    10105   7164   8538   -854   -880    215       O  
ATOM    388  NE2 GLN A  66      -8.158  56.643 112.400  1.00 64.31           N  
ANISOU  388  NE2 GLN A  66     9659   6911   7866   -907   -800    344       N  
ATOM    389  N   PHE A  67      -9.416  54.170 117.616  1.00 45.69           N  
ANISOU  389  N   PHE A  67     7152   4866   5341   -650   -492   -186       N  
ATOM    390  CA  PHE A  67      -9.431  54.195 119.047  1.00 44.91           C  
ANISOU  390  CA  PHE A  67     7030   4830   5202   -628   -449   -315       C  
ATOM    391  C   PHE A  67      -8.147  54.757 119.577  1.00 42.67           C  
ANISOU  391  C   PHE A  67     6779   4525   4907   -684   -477   -339       C  
ATOM    392  O   PHE A  67      -7.096  54.146 119.460  1.00 46.62           O  
ANISOU  392  O   PHE A  67     7294   5081   5340   -743   -466   -257       O  
ATOM    393  CB  PHE A  67      -9.549  52.780 119.475  1.00 47.35           C  
ANISOU  393  CB  PHE A  67     7319   5286   5387   -641   -374   -288       C  
ATOM    394  CG  PHE A  67      -9.701  52.607 120.924  1.00 50.55           C  
ANISOU  394  CG  PHE A  67     7697   5796   5713   -638   -325   -394       C  
ATOM    395  CD1 PHE A  67     -10.928  52.845 121.518  1.00 52.04           C  
ANISOU  395  CD1 PHE A  67     7836   6020   5917   -582   -286   -506       C  
ATOM    396  CD2 PHE A  67      -8.640  52.204 121.689  1.00 55.02           C  
ANISOU  396  CD2 PHE A  67     8278   6442   6186   -698   -319   -377       C  
ATOM    397  CE1 PHE A  67     -11.101  52.637 122.859  1.00 54.39           C  
ANISOU  397  CE1 PHE A  67     8108   6448   6108   -597   -227   -605       C  
ATOM    398  CE2 PHE A  67      -8.804  52.009 123.059  1.00 60.05           C  
ANISOU  398  CE2 PHE A  67     8894   7205   6717   -717   -282   -461       C  
ATOM    399  CZ  PHE A  67     -10.037  52.206 123.630  1.00 53.82           C  
ANISOU  399  CZ  PHE A  67     8066   6467   5917   -673   -229   -577       C  
ATOM    400  N   VAL A  68      -8.253  55.918 120.183  1.00 44.13           N  
ANISOU  400  N   VAL A  68     6968   4626   5172   -663   -513   -461       N  
ATOM    401  CA  VAL A  68      -7.104  56.749 120.476  1.00 43.07           C  
ANISOU  401  CA  VAL A  68     6871   4428   5067   -727   -569   -483       C  
ATOM    402  C   VAL A  68      -7.194  56.995 121.958  1.00 44.20           C  
ANISOU  402  C   VAL A  68     7006   4638   5149   -725   -539   -660       C  
ATOM    403  O   VAL A  68      -8.100  57.707 122.418  1.00 39.80           O  
ANISOU  403  O   VAL A  68     6433   4023   4666   -660   -527   -813       O  
ATOM    404  CB  VAL A  68      -7.213  58.128 119.750  1.00 45.73           C  
ANISOU  404  CB  VAL A  68     7230   4558   5586   -716   -661   -478       C  
ATOM    405  CG1 VAL A  68      -6.009  59.030 120.030  1.00 44.30           C  
ANISOU  405  CG1 VAL A  68     7088   4296   5449   -798   -729   -496       C  
ATOM    406  CG2 VAL A  68      -7.375  57.922 118.265  1.00 48.04           C  
ANISOU  406  CG2 VAL A  68     7529   4806   5918   -726   -694   -302       C  
ATOM    407  N   HIS A  69      -6.322  56.317 122.714  1.00 49.21           N  
ANISOU  407  N   HIS A  69     7644   5411   5643   -795   -521   -641       N  
ATOM    408  CA  HIS A  69      -6.230  56.535 124.148  1.00 50.15           C  
ANISOU  408  CA  HIS A  69     7766   5625   5662   -829   -504   -796       C  
ATOM    409  C   HIS A  69      -7.553  56.328 124.887  1.00 50.29           C  
ANISOU  409  C   HIS A  69     7750   5733   5626   -765   -418   -934       C  
ATOM    410  O   HIS A  69      -7.837  57.011 125.823  1.00 51.56           O  
ANISOU  410  O   HIS A  69     7916   5910   5765   -766   -398  -1122       O  
ATOM    411  CB  HIS A  69      -5.676  57.955 124.355  1.00 52.53           C  
ANISOU  411  CB  HIS A  69     8108   5783   6066   -865   -580   -909       C  
ATOM    412  CG  HIS A  69      -4.319  58.141 123.736  1.00 53.37           C  
ANISOU  412  CG  HIS A  69     8234   5830   6213   -950   -660   -767       C  
ATOM    413  ND1 HIS A  69      -3.869  59.345 123.256  1.00 58.44           N  
ANISOU  413  ND1 HIS A  69     8909   6290   7005   -980   -743   -778       N  
ATOM    414  CD2 HIS A  69      -3.339  57.245 123.464  1.00 54.42           C  
ANISOU  414  CD2 HIS A  69     8345   6059   6272  -1008   -664   -602       C  
ATOM    415  CE1 HIS A  69      -2.659  59.192 122.737  1.00 56.28           C  
ANISOU  415  CE1 HIS A  69     8631   6024   6729  -1065   -789   -626       C  
ATOM    416  NE2 HIS A  69      -2.305  57.931 122.873  1.00 52.90           N  
ANISOU  416  NE2 HIS A  69     8165   5764   6169  -1076   -738   -527       N  
ATOM    417  N   GLY A  70      -8.372  55.397 124.421  1.00 52.23           N  
ANISOU  417  N   GLY A  70     7957   6036   5853   -715   -363   -848       N  
ATOM    418  CA  GLY A  70      -9.588  55.026 125.116  1.00 55.22           C  
ANISOU  418  CA  GLY A  70     8284   6530   6166   -670   -273   -950       C  
ATOM    419  C   GLY A  70     -10.818  55.762 124.687  1.00 57.57           C  
ANISOU  419  C   GLY A  70     8538   6713   6621   -563   -252  -1051       C  
ATOM    420  O   GLY A  70     -11.809  55.750 125.393  1.00 65.72           O  
ANISOU  420  O   GLY A  70     9514   7833   7622   -522   -169  -1184       O  
ATOM    421  N   GLU A  71     -10.754  56.395 123.528  1.00 62.54           N  
ANISOU  421  N   GLU A  71     9183   7156   7423   -523   -329   -978       N  
ATOM    422  CA  GLU A  71     -11.856  57.171 122.982  1.00 62.53           C  
ANISOU  422  CA  GLU A  71     9132   7015   7612   -419   -343  -1037       C  
ATOM    423  C   GLU A  71     -12.001  56.870 121.480  1.00 63.01           C  
ANISOU  423  C   GLU A  71     9194   6990   7755   -409   -410   -833       C  
ATOM    424  O   GLU A  71     -11.026  57.037 120.737  1.00 55.05           O  
ANISOU  424  O   GLU A  71     8248   5906   6762   -468   -483   -710       O  
ATOM    425  CB  GLU A  71     -11.531  58.650 123.207  1.00 61.46           C  
ANISOU  425  CB  GLU A  71     9024   6697   7629   -399   -402  -1178       C  
ATOM    426  N   GLU A  72     -13.155  56.344 121.053  1.00 67.50           N  
ANISOU  426  N   GLU A  72     9696   7598   8353   -353   -382   -792       N  
ATOM    427  CA  GLU A  72     -13.471  56.280 119.641  1.00 69.27           C  
ANISOU  427  CA  GLU A  72     9919   7734   8667   -345   -461   -627       C  
ATOM    428  C   GLU A  72     -13.687  57.724 119.165  1.00 71.62           C  
ANISOU  428  C   GLU A  72    10207   7816   9190   -286   -560   -650       C  
ATOM    429  O   GLU A  72     -14.430  58.462 119.809  1.00 66.12           O  
ANISOU  429  O   GLU A  72     9445   7057   8622   -197   -538   -809       O  
ATOM    430  CB  GLU A  72     -14.699  55.413 119.355  1.00 74.12           C  
ANISOU  430  CB  GLU A  72    10456   8443   9264   -309   -421   -584       C  
ATOM    431  CG  GLU A  72     -14.387  54.140 118.560  1.00 82.28           C  
ANISOU  431  CG  GLU A  72    11531   9566  10166   -388   -420   -421       C  
ATOM    432  CD  GLU A  72     -14.206  54.388 117.067  1.00 79.88           C  
ANISOU  432  CD  GLU A  72    11269   9159   9922   -422   -523   -267       C  
ATOM    433  OE1 GLU A  72     -13.514  53.586 116.442  1.00 85.31           O  
ANISOU  433  OE1 GLU A  72    12017   9897  10498   -500   -517   -165       O  
ATOM    434  OE2 GLU A  72     -14.738  55.360 116.500  1.00 89.20           O  
ANISOU  434  OE2 GLU A  72    12421  10212  11259   -376   -611   -243       O  
ATOM    435  N   ASP A  73     -12.995  58.123 118.085  1.00 69.18           N  
ANISOU  435  N   ASP A  73     9961   7395   8931   -343   -663   -496       N  
ATOM    436  CA  ASP A  73     -13.238  59.397 117.404  1.00 72.73           C  
ANISOU  436  CA  ASP A  73    10402   7628   9604   -305   -786   -452       C  
ATOM    437  C   ASP A  73     -14.239  59.137 116.276  1.00 77.56           C  
ANISOU  437  C   ASP A  73    10963   8229  10278   -281   -852   -301       C  
ATOM    438  O   ASP A  73     -13.841  58.696 115.198  1.00 73.09           O  
ANISOU  438  O   ASP A  73    10449   7698   9623   -370   -902   -121       O  
ATOM    439  CB  ASP A  73     -11.929  59.961 116.849  1.00 73.04           C  
ANISOU  439  CB  ASP A  73    10535   7573   9645   -407   -867   -343       C  
ATOM    440  N   LEU A  74     -15.534  59.365 116.547  1.00 90.38           N  
ANISOU  440  N   LEU A  74    12476   9822  12043   -167   -845   -382       N  
ATOM    441  CA  LEU A  74     -16.639  58.987 115.622  1.00 95.79           C  
ANISOU  441  CA  LEU A  74    13086  10530  12779   -143   -906   -249       C  
ATOM    442  C   LEU A  74     -16.648  59.862 114.363  1.00 94.70           C  
ANISOU  442  C   LEU A  74    12965  10219  12797   -168  -1085    -56       C  
ATOM    443  O   LEU A  74     -17.039  59.401 113.285  1.00 89.68           O  
ANISOU  443  O   LEU A  74    12326   9635  12111   -225  -1160    121       O  
ATOM    444  CB  LEU A  74     -18.009  59.036 116.321  1.00 93.97           C  
ANISOU  444  CB  LEU A  74    12707  10320  12677    -12   -847   -391       C  
ATOM    445  N   LYS A  75     -16.202  61.113 114.518  1.00 93.33           N  
ANISOU  445  N   LYS A  75    12814   9844  12805   -141  -1157    -89       N  
ATOM    446  CA  LYS A  75     -15.902  62.017 113.393  1.00 92.31           C  
ANISOU  446  CA  LYS A  75    12725   9539  12809   -198  -1334    117       C  
ATOM    447  C   LYS A  75     -15.208  61.315 112.207  1.00 93.76           C  
ANISOU  447  C   LYS A  75    13006   9851  12769   -362  -1373    339       C  
ATOM    448  O   LYS A  75     -15.678  61.397 111.079  1.00 91.92           O  
ANISOU  448  O   LYS A  75    12760   9600  12564   -408  -1499    536       O  
ATOM    449  CB  LYS A  75     -15.028  63.177 113.877  1.00 89.47           C  
ANISOU  449  CB  LYS A  75    12420   8985  12588   -200  -1371     40       C  
ATOM    450  N   VAL A  76     -14.119  60.592 112.473  1.00 94.13           N  
ANISOU  450  N   VAL A  76    13139  10035  12590   -450  -1263    299       N  
ATOM    451  CA  VAL A  76     -13.304  59.999 111.393  1.00 88.81           C  
ANISOU  451  CA  VAL A  76    12555   9475  11714   -604  -1276    475       C  
ATOM    452  C   VAL A  76     -13.692  58.592 110.967  1.00 91.20           C  
ANISOU  452  C   VAL A  76    12857   9983  11812   -643  -1201    501       C  
ATOM    453  O   VAL A  76     -13.146  58.080 109.977  1.00 89.80           O  
ANISOU  453  O   VAL A  76    12747   9901  11471   -767  -1207    629       O  
ATOM    454  CB  VAL A  76     -11.792  60.021 111.709  1.00 89.15           C  
ANISOU  454  CB  VAL A  76    12681   9543  11649   -690  -1211    445       C  
ATOM    455  CG1 VAL A  76     -11.251  61.448 111.617  1.00 89.52           C  
ANISOU  455  CG1 VAL A  76    12753   9380  11879   -717  -1328    501       C  
ATOM    456  CG2 VAL A  76     -11.498  59.404 113.065  1.00 85.90           C  
ANISOU  456  CG2 VAL A  76    12257   9222  11158   -632  -1066    238       C  
ATOM    457  N   GLN A  77     -14.625  57.976 111.695  1.00 89.36           N  
ANISOU  457  N   GLN A  77    12548   9818  11589   -546  -1127    376       N  
ATOM    458  CA  GLN A  77     -15.193  56.676 111.320  1.00 86.30           C  
ANISOU  458  CA  GLN A  77    12147   9598  11046   -580  -1074    399       C  
ATOM    459  C   GLN A  77     -16.129  56.794 110.097  1.00 89.39           C  
ANISOU  459  C   GLN A  77    12506   9979  11479   -617  -1213    567       C  
ATOM    460  O   GLN A  77     -17.066  57.616 110.089  1.00 90.98           O  
ANISOU  460  O   GLN A  77    12616  10064  11888   -533  -1318    596       O  
ATOM    461  CB  GLN A  77     -15.967  56.101 112.519  1.00 91.06           C  
ANISOU  461  CB  GLN A  77    12663  10269  11665   -475   -964    230       C  
ATOM    462  CG  GLN A  77     -16.722  54.796 112.288  1.00 88.16           C  
ANISOU  462  CG  GLN A  77    12264  10054  11177   -503   -915    244       C  
ATOM    463  CD  GLN A  77     -17.265  54.211 113.593  1.00 93.16           C  
ANISOU  463  CD  GLN A  77    12822  10772  11802   -425   -791     86       C  
ATOM    464  OE1 GLN A  77     -17.857  54.931 114.398  1.00 95.49           O  
ANISOU  464  OE1 GLN A  77    13029  11010  12242   -321   -778    -21       O  
ATOM    465  NE2 GLN A  77     -17.058  52.903 113.809  1.00 87.85           N  
ANISOU  465  NE2 GLN A  77    12181  10236  10962   -482   -695     69       N  
ATOM    466  N   HIS A  78     -15.864  55.976 109.074  1.00 83.28           N  
ANISOU  466  N   HIS A  78    11803   9329  10512   -746  -1217    673       N  
ATOM    467  CA  HIS A  78     -16.791  55.770 107.950  1.00 83.48           C  
ANISOU  467  CA  HIS A  78    11804   9401  10512   -810  -1336    817       C  
ATOM    468  C   HIS A  78     -18.198  55.398 108.457  1.00 81.83           C  
ANISOU  468  C   HIS A  78    11467   9216  10407   -708  -1338    752       C  
ATOM    469  O   HIS A  78     -18.382  54.311 108.999  1.00 86.13           O  
ANISOU  469  O   HIS A  78    12000   9874  10851   -698  -1216    641       O  
ATOM    470  CB  HIS A  78     -16.241  54.670 107.027  1.00 80.48           C  
ANISOU  470  CB  HIS A  78    11526   9183   9870   -963  -1284    863       C  
ATOM    471  CG  HIS A  78     -16.919  54.606 105.690  1.00 88.14           C  
ANISOU  471  CG  HIS A  78    12506  10214  10769  -1077  -1424   1030       C  
ATOM    472  ND1 HIS A  78     -18.052  53.847 105.463  1.00 88.92           N  
ANISOU  472  ND1 HIS A  78    12547  10397  10842  -1084  -1456   1029       N  
ATOM    473  CD2 HIS A  78     -16.626  55.208 104.509  1.00 84.41           C  
ANISOU  473  CD2 HIS A  78    12094   9744  10234  -1206  -1551   1214       C  
ATOM    474  CE1 HIS A  78     -18.429  53.986 104.204  1.00 85.29           C  
ANISOU  474  CE1 HIS A  78    12113   9989  10303  -1212  -1602   1198       C  
ATOM    475  NE2 HIS A  78     -17.579  54.802 103.604  1.00 87.37           N  
ANISOU  475  NE2 HIS A  78    12451  10210  10535  -1290  -1660   1317       N  
ATOM    476  N   SER A  79     -19.179  56.286 108.261  1.00 80.99           N  
ANISOU  476  N   SER A  79    11255   9002  10514   -638  -1479    831       N  
ATOM    477  CA  SER A  79     -20.451  56.264 109.038  1.00 80.08           C  
ANISOU  477  CA  SER A  79    10980   8875  10571   -499  -1462    735       C  
ATOM    478  C   SER A  79     -21.308  54.997 108.889  1.00 77.93           C  
ANISOU  478  C   SER A  79    10659   8772  10180   -543  -1423    725       C  
ATOM    479  O   SER A  79     -22.119  54.705 109.777  1.00 85.26           O  
ANISOU  479  O   SER A  79    11467   9735  11192   -444  -1344    606       O  
ATOM    480  CB  SER A  79     -21.302  57.519 108.752  1.00 80.52           C  
ANISOU  480  CB  SER A  79    10916   8761  10918   -408  -1636    837       C  
ATOM    481  OG  SER A  79     -21.992  57.417 107.522  1.00 83.82           O  
ANISOU  481  OG  SER A  79    11307   9220  11319   -499  -1807   1045       O  
ATOM    482  N   SER A  80     -21.113  54.229 107.811  1.00 72.80           N  
ANISOU  482  N   SER A  80    10102   8232   9327   -698  -1467    835       N  
ATOM    483  CA  SER A  80     -21.775  52.890 107.651  1.00 75.35           C  
ANISOU  483  CA  SER A  80    10405   8711   9514   -766  -1422    809       C  
ATOM    484  C   SER A  80     -21.361  51.791 108.671  1.00 75.99           C  
ANISOU  484  C   SER A  80    10518   8875   9480   -748  -1222    636       C  
ATOM    485  O   SER A  80     -21.993  50.746 108.764  1.00 82.55           O  
ANISOU  485  O   SER A  80    11312   9807  10245   -785  -1179    603       O  
ATOM    486  CB  SER A  80     -21.511  52.337 106.251  1.00 73.70           C  
ANISOU  486  CB  SER A  80    10311   8595   9096   -950  -1504    936       C  
ATOM    487  OG  SER A  80     -20.152  51.912 106.123  1.00 73.29           O  
ANISOU  487  OG  SER A  80    10412   8577   8858  -1027  -1390    882       O  
ATOM    488  N   TYR A  81     -20.267  52.009 109.390  1.00 72.34           N  
ANISOU  488  N   TYR A  81    10125   8369   8992   -708  -1113    544       N  
ATOM    489  CA  TYR A  81     -19.859  51.117 110.444  1.00 66.32           C  
ANISOU  489  CA  TYR A  81     9379   7673   8146   -685   -948    406       C  
ATOM    490  C   TYR A  81     -20.262  51.604 111.828  1.00 65.22           C  
ANISOU  490  C   TYR A  81     9132   7505   8144   -549   -873    281       C  
ATOM    491  O   TYR A  81     -20.050  50.881 112.791  1.00 63.79           O  
ANISOU  491  O   TYR A  81     8952   7397   7890   -538   -745    181       O  
ATOM    492  CB  TYR A  81     -18.350  50.955 110.428  1.00 62.56           C  
ANISOU  492  CB  TYR A  81     9037   7188   7544   -737   -873    383       C  
ATOM    493  CG  TYR A  81     -17.823  50.197 109.244  1.00 60.11           C  
ANISOU  493  CG  TYR A  81     8836   6940   7065   -875   -886    452       C  
ATOM    494  CD1 TYR A  81     -17.998  48.807 109.141  1.00 54.07           C  
ANISOU  494  CD1 TYR A  81     8095   6265   6183   -939   -817    411       C  
ATOM    495  CD2 TYR A  81     -17.129  50.856 108.229  1.00 59.35           C  
ANISOU  495  CD2 TYR A  81     8819   6811   6921   -950   -960    551       C  
ATOM    496  CE1 TYR A  81     -17.488  48.104 108.072  1.00 50.78           C  
ANISOU  496  CE1 TYR A  81     7781   5900   5616  -1062   -811    438       C  
ATOM    497  CE2 TYR A  81     -16.628  50.155 107.138  1.00 59.43           C  
ANISOU  497  CE2 TYR A  81     8927   6900   6753  -1086   -950    591       C  
ATOM    498  CZ  TYR A  81     -16.811  48.790 107.071  1.00 55.02           C  
ANISOU  498  CZ  TYR A  81     8392   6425   6089  -1135   -871    520       C  
ATOM    499  OH  TYR A  81     -16.288  48.134 106.000  1.00 57.95           O  
ANISOU  499  OH  TYR A  81     8861   6866   6291  -1265   -848    527       O  
ATOM    500  N   ARG A  82     -20.859  52.790 111.939  1.00 66.92           N  
ANISOU  500  N   ARG A  82     9252   7618   8557   -451   -950    284       N  
ATOM    501  CA  ARG A  82     -21.036  53.413 113.255  1.00 72.82           C  
ANISOU  501  CA  ARG A  82     9914   8326   9428   -322   -862    129       C  
ATOM    502  C   ARG A  82     -21.702  52.429 114.195  1.00 72.67           C  
ANISOU  502  C   ARG A  82     9813   8452   9345   -309   -733     29       C  
ATOM    503  O   ARG A  82     -21.333  52.308 115.364  1.00 71.76           O  
ANISOU  503  O   ARG A  82     9700   8385   9179   -276   -606   -102       O  
ATOM    504  CB  ARG A  82     -21.855  54.715 113.194  1.00 70.79           C  
ANISOU  504  CB  ARG A  82     9532   7931   9435   -204   -962    132       C  
ATOM    505  N   GLN A  83     -22.663  51.691 113.672  1.00 72.54           N  
ANISOU  505  N   GLN A  83     9728   8518   9317   -353   -771    104       N  
ATOM    506  CA  GLN A  83     -23.466  50.835 114.514  1.00 72.45           C  
ANISOU  506  CA  GLN A  83     9613   8641   9272   -348   -662     31       C  
ATOM    507  C   GLN A  83     -23.051  49.352 114.470  1.00 63.64           C  
ANISOU  507  C   GLN A  83     8594   7634   7953   -474   -599     63       C  
ATOM    508  O   GLN A  83     -23.333  48.618 115.390  1.00 64.41           O  
ANISOU  508  O   GLN A  83     8643   7836   7993   -484   -490      2       O  
ATOM    509  CB  GLN A  83     -24.947  51.021 114.129  1.00 77.33           C  
ANISOU  509  CB  GLN A  83    10054   9277  10052   -307   -742     82       C  
ATOM    510  CG  GLN A  83     -25.453  52.475 114.270  1.00 84.56           C  
ANISOU  510  CG  GLN A  83    10844  10064  11220   -159   -799     40       C  
ATOM    511  CD  GLN A  83     -26.427  52.678 115.430  1.00 78.68           C  
ANISOU  511  CD  GLN A  83     9908   9385  10602    -44   -677   -112       C  
ATOM    512  N   ARG A  84     -22.368  48.906 113.432  1.00 54.02           N  
ANISOU  512  N   ARG A  84     7506   6387   6630   -572   -663    154       N  
ATOM    513  CA  ARG A  84     -22.228  47.474 113.249  1.00 51.01           C  
ANISOU  513  CA  ARG A  84     7191   6086   6105   -683   -619    178       C  
ATOM    514  C   ARG A  84     -20.821  46.968 113.635  1.00 44.55           C  
ANISOU  514  C   ARG A  84     6507   5257   5164   -714   -530    139       C  
ATOM    515  O   ARG A  84     -20.584  45.772 113.651  1.00 41.83           O  
ANISOU  515  O   ARG A  84     6213   4954   4726   -790   -481    146       O  
ATOM    516  CB  ARG A  84     -22.686  47.044 111.831  1.00 49.14           C  
ANISOU  516  CB  ARG A  84     6984   5855   5832   -788   -739    284       C  
ATOM    517  CG  ARG A  84     -21.940  47.705 110.685  1.00 53.81           C  
ANISOU  517  CG  ARG A  84     7685   6373   6388   -827   -836    355       C  
ATOM    518  CD  ARG A  84     -22.630  47.459 109.344  1.00 52.34           C  
ANISOU  518  CD  ARG A  84     7504   6219   6165   -935   -973    463       C  
ATOM    519  NE  ARG A  84     -22.670  46.022 109.019  1.00 48.89           N  
ANISOU  519  NE  ARG A  84     7130   5853   5594  -1055   -931    441       N  
ATOM    520  CZ  ARG A  84     -21.811  45.389 108.236  1.00 44.20           C  
ANISOU  520  CZ  ARG A  84     6681   5263   4851  -1160   -911    431       C  
ATOM    521  NH1 ARG A  84     -20.822  46.032 107.635  1.00 43.74           N  
ANISOU  521  NH1 ARG A  84     6720   5167   4733  -1175   -927    457       N  
ATOM    522  NH2 ARG A  84     -21.899  44.085 108.100  1.00 42.48           N  
ANISOU  522  NH2 ARG A  84     6507   5083   4550  -1250   -864    386       N  
ATOM    523  N   ALA A  85     -19.937  47.879 114.022  1.00 43.04           N  
ANISOU  523  N   ALA A  85     6357   5003   4994   -653   -512     98       N  
ATOM    524  CA  ALA A  85     -18.538  47.573 114.281  1.00 41.70           C  
ANISOU  524  CA  ALA A  85     6299   4816   4729   -680   -450     77       C  
ATOM    525  C   ALA A  85     -18.109  48.074 115.674  1.00 42.92           C  
ANISOU  525  C   ALA A  85     6425   4984   4897   -609   -373    -15       C  
ATOM    526  O   ALA A  85     -18.479  49.141 116.099  1.00 42.81           O  
ANISOU  526  O   ALA A  85     6350   4938   4980   -531   -387    -74       O  
ATOM    527  CB  ALA A  85     -17.639  48.201 113.217  1.00 43.71           C  
ANISOU  527  CB  ALA A  85     6649   4989   4969   -710   -518    133       C  
ATOM    528  N   ARG A  86     -17.306  47.282 116.360  1.00 41.50           N  
ANISOU  528  N   ARG A  86     6293   4850   4624   -643   -297    -30       N  
ATOM    529  CA  ARG A  86     -16.775  47.670 117.658  1.00 42.79           C  
ANISOU  529  CA  ARG A  86     6446   5048   4764   -605   -235   -107       C  
ATOM    530  C   ARG A  86     -15.550  46.874 118.020  1.00 38.39           C  
ANISOU  530  C   ARG A  86     5963   4509   4116   -656   -196    -75       C  
ATOM    531  O   ARG A  86     -15.292  45.804 117.533  1.00 41.83           O  
ANISOU  531  O   ARG A  86     6437   4942   4514   -710   -189    -11       O  
ATOM    532  CB  ARG A  86     -17.821  47.577 118.760  1.00 43.30           C  
ANISOU  532  CB  ARG A  86     6403   5220   4829   -577   -170   -174       C  
ATOM    533  CG  ARG A  86     -18.195  46.178 119.141  1.00 45.09           C  
ANISOU  533  CG  ARG A  86     6609   5548   4976   -648   -120   -120       C  
ATOM    534  CD  ARG A  86     -19.409  46.218 120.047  1.00 50.63           C  
ANISOU  534  CD  ARG A  86     7184   6369   5684   -629    -56   -179       C  
ATOM    535  NE  ARG A  86     -19.522  44.967 120.820  1.00 60.12           N  
ANISOU  535  NE  ARG A  86     8372   7687   6783   -713      5   -124       N  
ATOM    536  CZ  ARG A  86     -19.036  44.738 122.054  1.00 59.63           C  
ANISOU  536  CZ  ARG A  86     8317   7725   6614   -746     69   -140       C  
ATOM    537  NH1 ARG A  86     -18.376  45.659 122.741  1.00 58.32           N  
ANISOU  537  NH1 ARG A  86     8175   7570   6414   -706     89   -234       N  
ATOM    538  NH2 ARG A  86     -19.243  43.562 122.618  1.00 63.45           N  
ANISOU  538  NH2 ARG A  86     8783   8303   7021   -835    104    -55       N  
ATOM    539  N   LEU A  87     -14.745  47.487 118.840  1.00 44.03           N  
ANISOU  539  N   LEU A  87     6693   5226   4809   -635   -178   -127       N  
ATOM    540  CA  LEU A  87     -13.524  46.876 119.357  1.00 43.34           C  
ANISOU  540  CA  LEU A  87     6654   5162   4651   -676   -154    -92       C  
ATOM    541  C   LEU A  87     -13.930  46.310 120.695  1.00 42.01           C  
ANISOU  541  C   LEU A  87     6436   5120   4406   -697    -98   -109       C  
ATOM    542  O   LEU A  87     -14.566  46.982 121.476  1.00 43.20           O  
ANISOU  542  O   LEU A  87     6534   5333   4546   -669    -70   -200       O  
ATOM    543  CB  LEU A  87     -12.463  47.976 119.482  1.00 43.85           C  
ANISOU  543  CB  LEU A  87     6759   5169   4734   -659   -184   -131       C  
ATOM    544  CG  LEU A  87     -11.032  47.579 119.762  1.00 43.33           C  
ANISOU  544  CG  LEU A  87     6732   5106   4624   -698   -182    -83       C  
ATOM    545  CD1 LEU A  87     -10.456  46.876 118.580  1.00 41.21           C  
ANISOU  545  CD1 LEU A  87     6502   4777   4378   -723   -186     -2       C  
ATOM    546  CD2 LEU A  87     -10.244  48.794 120.216  1.00 42.92           C  
ANISOU  546  CD2 LEU A  87     6698   5022   4586   -690   -215   -143       C  
ATOM    547  N   LEU A  88     -13.658  45.035 120.923  1.00 47.38           N  
ANISOU  547  N   LEU A  88     7124   5838   5040   -752    -80    -22       N  
ATOM    548  CA  LEU A  88     -13.931  44.401 122.265  1.00 45.40           C  
ANISOU  548  CA  LEU A  88     6830   5722   4697   -799    -37      0       C  
ATOM    549  C   LEU A  88     -13.009  44.969 123.310  1.00 40.80           C  
ANISOU  549  C   LEU A  88     6263   5198   4040   -811    -40    -35       C  
ATOM    550  O   LEU A  88     -11.835  44.632 123.347  1.00 39.73           O  
ANISOU  550  O   LEU A  88     6166   5028   3901   -833    -74     34       O  
ATOM    551  CB  LEU A  88     -13.773  42.889 122.210  1.00 44.66           C  
ANISOU  551  CB  LEU A  88     6746   5623   4600   -860    -38    127       C  
ATOM    552  CG  LEU A  88     -14.735  42.249 121.208  1.00 48.16           C  
ANISOU  552  CG  LEU A  88     7178   6014   5107   -869    -40    150       C  
ATOM    553  CD1 LEU A  88     -14.611  40.746 121.284  1.00 47.12           C  
ANISOU  553  CD1 LEU A  88     7055   5860   4988   -935    -42    263       C  
ATOM    554  CD2 LEU A  88     -16.164  42.694 121.482  1.00 49.36           C  
ANISOU  554  CD2 LEU A  88     7250   6257   5249   -860    -10     91       C  
ATOM    555  N   LYS A  89     -13.560  45.842 124.128  1.00 42.46           N  
ANISOU  555  N   LYS A  89     6436   5497   4199   -796     -5   -152       N  
ATOM    556  CA  LYS A  89     -12.781  46.612 125.080  1.00 47.83           C  
ANISOU  556  CA  LYS A  89     7138   6232   4802   -813    -12   -226       C  
ATOM    557  C   LYS A  89     -12.073  45.751 126.105  1.00 46.52           C  
ANISOU  557  C   LYS A  89     6979   6184   4511   -904    -23   -123       C  
ATOM    558  O   LYS A  89     -10.917  45.983 126.327  1.00 53.49           O  
ANISOU  558  O   LYS A  89     7900   7047   5377   -925    -75   -100       O  
ATOM    559  CB  LYS A  89     -13.637  47.721 125.730  1.00 49.88           C  
ANISOU  559  CB  LYS A  89     7353   6558   5041   -775     44   -409       C  
ATOM    560  N   ASP A  90     -12.722  44.723 126.654  1.00 50.37           N  
ANISOU  560  N   ASP A  90     7428   6786   4925   -965     11    -39       N  
ATOM    561  CA  ASP A  90     -12.116  43.829 127.685  1.00 48.80           C  
ANISOU  561  CA  ASP A  90     7230   6706   4607  -1067    -17     97       C  
ATOM    562  C   ASP A  90     -11.019  42.877 127.186  1.00 46.17           C  
ANISOU  562  C   ASP A  90     6925   6254   4363  -1075    -93    267       C  
ATOM    563  O   ASP A  90     -10.352  42.224 127.988  1.00 50.95           O  
ANISOU  563  O   ASP A  90     7526   6930   4903  -1150   -142    397       O  
ATOM    564  CB  ASP A  90     -13.192  43.049 128.506  1.00 53.90           C  
ANISOU  564  CB  ASP A  90     7819   7522   5139  -1149     42    152       C  
ATOM    565  CG  ASP A  90     -13.866  41.899 127.721  1.00 60.90           C  
ANISOU  565  CG  ASP A  90     8681   8325   6131  -1151     44    273       C  
ATOM    566  OD1 ASP A  90     -13.466  41.645 126.549  1.00 68.12           O  
ANISOU  566  OD1 ASP A  90     9632   9056   7195  -1090      3    305       O  
ATOM    567  OD2 ASP A  90     -14.832  41.260 128.265  1.00 60.58           O  
ANISOU  567  OD2 ASP A  90     8586   8412   6020  -1224     91    326       O  
ATOM    568  N   GLN A  91     -10.809  42.791 125.885  1.00 45.62           N  
ANISOU  568  N   GLN A  91     6879   6012   4444  -1003   -105    269       N  
ATOM    569  CA  GLN A  91      -9.662  42.039 125.344  1.00 44.16           C  
ANISOU  569  CA  GLN A  91     6711   5705   4361   -994   -158    388       C  
ATOM    570  C   GLN A  91      -8.368  42.829 125.253  1.00 42.96           C  
ANISOU  570  C   GLN A  91     6579   5509   4235   -970   -202    359       C  
ATOM    571  O   GLN A  91      -7.297  42.256 125.156  1.00 41.64           O  
ANISOU  571  O   GLN A  91     6401   5284   4136   -972   -246    462       O  
ATOM    572  CB  GLN A  91      -9.981  41.529 123.971  1.00 45.75           C  
ANISOU  572  CB  GLN A  91     6929   5760   4693   -944   -136    388       C  
ATOM    573  CG  GLN A  91     -11.136  40.567 123.940  1.00 45.86           C  
ANISOU  573  CG  GLN A  91     6921   5792   4711   -980   -109    437       C  
ATOM    574  CD  GLN A  91     -10.806  39.252 124.629  1.00 49.63           C  
ANISOU  574  CD  GLN A  91     7378   6279   5200  -1046   -143    604       C  
ATOM    575  OE1 GLN A  91      -9.817  38.594 124.305  1.00 51.72           O  
ANISOU  575  OE1 GLN A  91     7650   6431   5571  -1028   -180    683       O  
ATOM    576  NE2 GLN A  91     -11.630  38.872 125.592  1.00 49.82           N  
ANISOU  576  NE2 GLN A  91     7367   6439   5123  -1124   -131    663       N  
ATOM    577  N   LEU A  92      -8.445  44.148 125.287  1.00 44.89           N  
ANISOU  577  N   LEU A  92     6842   5771   4441   -947   -193    221       N  
ATOM    578  CA  LEU A  92      -7.205  44.956 125.139  1.00 45.24           C  
ANISOU  578  CA  LEU A  92     6906   5765   4521   -938   -241    196       C  
ATOM    579  C   LEU A  92      -6.147  44.679 126.240  1.00 47.65           C  
ANISOU  579  C   LEU A  92     7188   6162   4756  -1009   -309    290       C  
ATOM    580  O   LEU A  92      -4.956  44.616 125.916  1.00 51.33           O  
ANISOU  580  O   LEU A  92     7639   6562   5302  -1002   -356    356       O  
ATOM    581  CB  LEU A  92      -7.541  46.442 125.062  1.00 44.02           C  
ANISOU  581  CB  LEU A  92     6777   5595   4353   -910   -231     32       C  
ATOM    582  CG  LEU A  92      -8.291  46.836 123.770  1.00 43.32           C  
ANISOU  582  CG  LEU A  92     6705   5388   4368   -839   -199    -25       C  
ATOM    583  CD1 LEU A  92      -8.802  48.278 123.759  1.00 43.74           C  
ANISOU  583  CD1 LEU A  92     6771   5407   4439   -803   -198   -176       C  
ATOM    584  CD2 LEU A  92      -7.411  46.605 122.579  1.00 38.61           C  
ANISOU  584  CD2 LEU A  92     6127   4672   3873   -820   -218     46       C  
ATOM    585  N   SER A  93      -6.569  44.491 127.501  1.00 46.00           N  
ANISOU  585  N   SER A  93     6967   6115   4397  -1084   -315    305       N  
ATOM    586  CA  SER A  93      -5.602  44.248 128.616  1.00 48.19           C  
ANISOU  586  CA  SER A  93     7223   6505   4581  -1174   -401    412       C  
ATOM    587  C   SER A  93      -4.865  42.933 128.390  1.00 47.77           C  
ANISOU  587  C   SER A  93     7125   6381   4644  -1171   -455    621       C  
ATOM    588  O   SER A  93      -3.746  42.777 128.817  1.00 47.70           O  
ANISOU  588  O   SER A  93     7082   6390   4651  -1208   -542    726       O  
ATOM    589  CB  SER A  93      -6.276  44.213 129.979  1.00 46.78           C  
ANISOU  589  CB  SER A  93     7045   6539   4191  -1275   -391    398       C  
ATOM    590  OG  SER A  93      -7.339  43.251 130.011  1.00 47.87           O  
ANISOU  590  OG  SER A  93     7163   6714   4313  -1286   -337    469       O  
ATOM    591  N   LEU A  94      -5.482  42.037 127.638  1.00 48.35           N  
ANISOU  591  N   LEU A  94     7194   6357   4821  -1122   -407    668       N  
ATOM    592  CA  LEU A  94      -4.894  40.746 127.263  1.00 48.68           C  
ANISOU  592  CA  LEU A  94     7193   6286   5016  -1100   -442    836       C  
ATOM    593  C   LEU A  94      -3.975  40.807 126.031  1.00 49.81           C  
ANISOU  593  C   LEU A  94     7324   6259   5342  -1010   -427    808       C  
ATOM    594  O   LEU A  94      -3.474  39.781 125.583  1.00 49.35           O  
ANISOU  594  O   LEU A  94     7225   6086   5439   -973   -437    908       O  
ATOM    595  CB  LEU A  94      -6.016  39.707 127.013  1.00 45.10           C  
ANISOU  595  CB  LEU A  94     6745   5796   4595  -1102   -395    884       C  
ATOM    596  CG  LEU A  94      -7.140  39.585 128.068  1.00 46.56           C  
ANISOU  596  CG  LEU A  94     6933   6157   4601  -1196   -379    904       C  
ATOM    597  CD1 LEU A  94      -8.135  38.502 127.663  1.00 45.39           C  
ANISOU  597  CD1 LEU A  94     6778   5945   4521  -1201   -341    967       C  
ATOM    598  CD2 LEU A  94      -6.613  39.298 129.486  1.00 44.58           C  
ANISOU  598  CD2 LEU A  94     6653   6065   4219  -1308   -470   1057       C  
ATOM    599  N   GLY A  95      -3.773  41.990 125.463  1.00 49.87           N  
ANISOU  599  N   GLY A  95     7362   6247   5339   -978   -399    669       N  
ATOM    600  CA  GLY A  95      -2.955  42.117 124.259  1.00 48.21           C  
ANISOU  600  CA  GLY A  95     7140   5905   5274   -912   -370    640       C  
ATOM    601  C   GLY A  95      -3.658  41.637 123.004  1.00 45.34           C  
ANISOU  601  C   GLY A  95     6808   5429   4989   -856   -287    584       C  
ATOM    602  O   GLY A  95      -3.038  41.147 122.081  1.00 43.05           O  
ANISOU  602  O   GLY A  95     6497   5034   4827   -811   -252    594       O  
ATOM    603  N   ASN A  96      -4.963  41.844 122.960  1.00 44.54           N  
ANISOU  603  N   ASN A  96     6755   5362   4807   -865   -252    513       N  
ATOM    604  CA  ASN A  96      -5.774  41.403 121.857  1.00 43.74           C  
ANISOU  604  CA  ASN A  96     6686   5177   4757   -833   -192    465       C  
ATOM    605  C   ASN A  96      -6.662  42.531 121.349  1.00 42.42           C  
ANISOU  605  C   ASN A  96     6564   5028   4525   -822   -167    342       C  
ATOM    606  O   ASN A  96      -7.539  43.010 122.071  1.00 39.99           O  
ANISOU  606  O   ASN A  96     6258   4808   4128   -841   -171    301       O  
ATOM    607  CB  ASN A  96      -6.593  40.209 122.345  1.00 47.10           C  
ANISOU  607  CB  ASN A  96     7099   5615   5182   -863   -192    544       C  
ATOM    608  CG  ASN A  96      -7.479  39.616 121.297  1.00 52.84           C  
ANISOU  608  CG  ASN A  96     7857   6258   5961   -850   -143    500       C  
ATOM    609  OD1 ASN A  96      -7.206  39.686 120.093  1.00 59.06           O  
ANISOU  609  OD1 ASN A  96     8671   6956   6812   -816   -106    434       O  
ATOM    610  ND2 ASN A  96      -8.577  39.001 121.750  1.00 55.70           N  
ANISOU  610  ND2 ASN A  96     8215   6664   6286   -892   -142    537       N  
ATOM    611  N   ALA A  97      -6.435  42.938 120.090  1.00 38.54           N  
ANISOU  611  N   ALA A  97     6102   4457   4086   -795   -141    288       N  
ATOM    612  CA  ALA A  97      -7.316  43.855 119.418  1.00 36.86           C  
ANISOU  612  CA  ALA A  97     5928   4236   3843   -785   -134    204       C  
ATOM    613  C   ALA A  97      -8.302  43.108 118.543  1.00 36.95           C  
ANISOU  613  C   ALA A  97     5959   4209   3871   -787   -104    196       C  
ATOM    614  O   ALA A  97      -7.991  42.565 117.437  1.00 35.19           O  
ANISOU  614  O   ALA A  97     5761   3918   3693   -790    -73    194       O  
ATOM    615  CB  ALA A  97      -6.532  44.828 118.568  1.00 38.14           C  
ANISOU  615  CB  ALA A  97     6112   4348   4031   -780   -141    174       C  
ATOM    616  N   ALA A  98      -9.526  43.140 119.004  1.00 33.95           N  
ANISOU  616  N   ALA A  98     5566   3883   3449   -793   -108    177       N  
ATOM    617  CA  ALA A  98     -10.519  42.257 118.481  1.00 34.07           C  
ANISOU  617  CA  ALA A  98     5585   3882   3479   -812    -92    187       C  
ATOM    618  C   ALA A  98     -11.588  43.124 117.928  1.00 34.43           C  
ANISOU  618  C   ALA A  98     5633   3941   3510   -801   -109    129       C  
ATOM    619  O   ALA A  98     -12.294  43.773 118.679  1.00 34.89           O  
ANISOU  619  O   ALA A  98     5651   4063   3540   -784   -115     96       O  
ATOM    620  CB  ALA A  98     -11.060  41.358 119.597  1.00 31.87           C  
ANISOU  620  CB  ALA A  98     5265   3668   3177   -844    -86    247       C  
ATOM    621  N   LEU A  99     -11.713  43.112 116.608  1.00 33.86           N  
ANISOU  621  N   LEU A  99     5599   3809   3456   -813   -117    117       N  
ATOM    622  CA  LEU A  99     -12.768  43.813 115.897  1.00 33.94           C  
ANISOU  622  CA  LEU A  99     5606   3822   3466   -812   -156     92       C  
ATOM    623  C   LEU A  99     -13.924  42.861 115.610  1.00 36.55           C  
ANISOU  623  C   LEU A  99     5918   4172   3798   -852   -158    106       C  
ATOM    624  O   LEU A  99     -13.724  41.785 115.028  1.00 35.58           O  
ANISOU  624  O   LEU A  99     5833   4010   3678   -897   -138    117       O  
ATOM    625  CB  LEU A  99     -12.233  44.230 114.507  1.00 35.14           C  
ANISOU  625  CB  LEU A  99     5819   3921   3613   -836   -177     93       C  
ATOM    626  CG  LEU A  99     -13.231  44.792 113.529  1.00 34.66           C  
ANISOU  626  CG  LEU A  99     5763   3859   3549   -857   -240    101       C  
ATOM    627  CD1 LEU A  99     -13.801  46.057 114.079  1.00 36.24           C  
ANISOU  627  CD1 LEU A  99     5912   4060   3798   -799   -289     89       C  
ATOM    628  CD2 LEU A  99     -12.614  45.085 112.194  1.00 41.70           C  
ANISOU  628  CD2 LEU A  99     6721   4722   4400   -908   -257    119       C  
ATOM    629  N   GLN A 100     -15.119  43.329 115.914  1.00 34.51           N  
ANISOU  629  N   GLN A 100     5597   3964   3550   -837   -182     94       N  
ATOM    630  CA  GLN A 100     -16.315  42.566 115.756  1.00 36.96           C  
ANISOU  630  CA  GLN A 100     5867   4309   3868   -880   -191    113       C  
ATOM    631  C   GLN A 100     -17.296  43.327 114.914  1.00 37.81           C  
ANISOU  631  C   GLN A 100     5943   4418   4005   -875   -258    109       C  
ATOM    632  O   GLN A 100     -17.630  44.458 115.227  1.00 37.83           O  
ANISOU  632  O   GLN A 100     5894   4433   4049   -811   -280     84       O  
ATOM    633  CB  GLN A 100     -16.943  42.287 117.135  1.00 35.52           C  
ANISOU  633  CB  GLN A 100     5602   4218   3677   -874   -149    118       C  
ATOM    634  CG  GLN A 100     -18.204  41.466 117.091  1.00 39.03           C  
ANISOU  634  CG  GLN A 100     5986   4710   4135   -931   -153    150       C  
ATOM    635  CD  GLN A 100     -18.497  40.803 118.441  1.00 46.23           C  
ANISOU  635  CD  GLN A 100     6838   5715   5014   -962    -97    185       C  
ATOM    636  OE1 GLN A 100     -19.402  41.225 119.135  1.00 45.69           O  
ANISOU  636  OE1 GLN A 100     6673   5750   4937   -949    -69    161       O  
ATOM    637  NE2 GLN A 100     -17.697  39.786 118.831  1.00 45.10           N  
ANISOU  637  NE2 GLN A 100     6742   5537   4855  -1006    -79    245       N  
ATOM    638  N   ILE A 101     -17.794  42.680 113.867  1.00 41.91           N  
ANISOU  638  N   ILE A 101     6488   4923   4513   -945   -298    132       N  
ATOM    639  CA  ILE A 101     -18.762  43.296 112.957  1.00 41.07           C  
ANISOU  639  CA  ILE A 101     6348   4827   4430   -960   -387    155       C  
ATOM    640  C   ILE A 101     -19.955  42.412 112.948  1.00 39.36           C  
ANISOU  640  C   ILE A 101     6068   4660   4227  -1020   -404    176       C  
ATOM    641  O   ILE A 101     -19.793  41.216 112.755  1.00 38.21           O  
ANISOU  641  O   ILE A 101     5973   4497   4047  -1094   -378    174       O  
ATOM    642  CB  ILE A 101     -18.245  43.250 111.523  1.00 42.62           C  
ANISOU  642  CB  ILE A 101     6646   4983   4565  -1029   -434    170       C  
ATOM    643  CG1 ILE A 101     -16.873  43.895 111.442  1.00 44.59           C  
ANISOU  643  CG1 ILE A 101     6965   5187   4790   -995   -402    157       C  
ATOM    644  CG2 ILE A 101     -19.243  43.870 110.551  1.00 44.75           C  
ANISOU  644  CG2 ILE A 101     6882   5274   4848  -1064   -552    223       C  
ATOM    645  CD1 ILE A 101     -16.908  45.266 110.936  1.00 50.74           C  
ANISOU  645  CD1 ILE A 101     7738   5945   5594   -969   -482    197       C  
ATOM    646  N   THR A 102     -21.131  42.997 113.133  1.00 38.45           N  
ANISOU  646  N   THR A 102     5836   4596   4178   -988   -449    192       N  
ATOM    647  CA  THR A 102     -22.406  42.267 113.096  1.00 41.94           C  
ANISOU  647  CA  THR A 102     6188   5100   4646  -1052   -476    222       C  
ATOM    648  C   THR A 102     -23.042  42.252 111.690  1.00 44.17           C  
ANISOU  648  C   THR A 102     6484   5377   4922  -1133   -599    270       C  
ATOM    649  O   THR A 102     -22.880  43.168 110.879  1.00 41.55           O  
ANISOU  649  O   THR A 102     6180   5016   4593  -1115   -679    297       O  
ATOM    650  CB  THR A 102     -23.404  42.870 114.094  1.00 43.93           C  
ANISOU  650  CB  THR A 102     6277   5431   4985   -976   -449    210       C  
ATOM    651  OG1 THR A 102     -23.599  44.256 113.778  1.00 50.81           O  
ANISOU  651  OG1 THR A 102     7097   6270   5938   -885   -512    204       O  
ATOM    652  CG2 THR A 102     -22.826  42.805 115.525  1.00 42.24           C  
ANISOU  652  CG2 THR A 102     6055   5255   4739   -926   -328    160       C  
ATOM    653  N   ASP A 103     -23.768  41.179 111.430  1.00 44.14           N  
ANISOU  653  N   ASP A 103     6461   5405   4904  -1237   -621    288       N  
ATOM    654  CA  ASP A 103     -24.533  40.999 110.220  1.00 46.94           C  
ANISOU  654  CA  ASP A 103     6815   5780   5240  -1340   -743    332       C  
ATOM    655  C   ASP A 103     -23.691  41.004 108.992  1.00 46.80           C  
ANISOU  655  C   ASP A 103     6952   5716   5114  -1408   -787    318       C  
ATOM    656  O   ASP A 103     -23.926  41.762 108.066  1.00 50.73           O  
ANISOU  656  O   ASP A 103     7453   6231   5591  -1431   -897    371       O  
ATOM    657  CB  ASP A 103     -25.638  42.024 110.111  1.00 53.65           C  
ANISOU  657  CB  ASP A 103     7512   6681   6191  -1287   -841    394       C  
ATOM    658  CG  ASP A 103     -26.760  41.558 109.201  1.00 59.17           C  
ANISOU  658  CG  ASP A 103     8156   7435   6891  -1412   -970    457       C  
ATOM    659  OD1 ASP A 103     -26.644  40.473 108.632  1.00 58.30           O  
ANISOU  659  OD1 ASP A 103     8145   7319   6689  -1545   -980    436       O  
ATOM    660  OD2 ASP A 103     -27.768  42.266 109.077  1.00 68.40           O  
ANISOU  660  OD2 ASP A 103     9176   8648   8164  -1376  -1064    524       O  
ATOM    661  N   VAL A 104     -22.710  40.124 108.972  1.00 45.91           N  
ANISOU  661  N   VAL A 104     6961   5549   4934  -1446   -699    251       N  
ATOM    662  CA  VAL A 104     -21.785  40.072 107.882  1.00 48.24           C  
ANISOU  662  CA  VAL A 104     7398   5811   5118  -1506   -703    211       C  
ATOM    663  C   VAL A 104     -22.430  39.812 106.496  1.00 52.73           C  
ANISOU  663  C   VAL A 104     8013   6429   5594  -1657   -820    225       C  
ATOM    664  O   VAL A 104     -23.258  38.891 106.328  1.00 54.46           O  
ANISOU  664  O   VAL A 104     8210   6665   5815  -1756   -858    213       O  
ATOM    665  CB  VAL A 104     -20.718  39.045 108.193  1.00 53.48           C  
ANISOU  665  CB  VAL A 104     8156   6400   5764  -1510   -579    125       C  
ATOM    666  CG1 VAL A 104     -19.809  38.875 106.976  1.00 56.85           C  
ANISOU  666  CG1 VAL A 104     8720   6808   6072  -1584   -562     56       C  
ATOM    667  CG2 VAL A 104     -19.916  39.521 109.413  1.00 54.24           C  
ANISOU  667  CG2 VAL A 104     8218   6467   5923  -1374   -489    130       C  
ATOM    668  N   LYS A 105     -22.074  40.633 105.504  1.00 55.26           N  
ANISOU  668  N   LYS A 105     8394   6779   5823  -1690   -886    259       N  
ATOM    669  CA  LYS A 105     -22.631  40.479 104.150  1.00 56.62           C  
ANISOU  669  CA  LYS A 105     8617   7023   5872  -1852  -1010    284       C  
ATOM    670  C   LYS A 105     -21.515  40.217 103.193  1.00 53.84           C  
ANISOU  670  C   LYS A 105     8425   6676   5354  -1938   -949    200       C  
ATOM    671  O   LYS A 105     -20.375  40.169 103.572  1.00 48.88           O  
ANISOU  671  O   LYS A 105     7851   5992   4731  -1864   -819    133       O  
ATOM    672  CB  LYS A 105     -23.369  41.745 103.707  1.00 60.40           C  
ANISOU  672  CB  LYS A 105     9009   7559   6380  -1843  -1174    433       C  
ATOM    673  CG  LYS A 105     -24.507  42.213 104.588  1.00 63.41           C  
ANISOU  673  CG  LYS A 105     9204   7942   6947  -1740  -1233    512       C  
ATOM    674  CD  LYS A 105     -25.721  41.318 104.520  1.00 66.54           C  
ANISOU  674  CD  LYS A 105     9522   8392   7368  -1837  -1298    519       C  
ATOM    675  CE  LYS A 105     -26.956  42.107 104.941  1.00 71.00           C  
ANISOU  675  CE  LYS A 105     9882   8992   8103  -1758  -1404    632       C  
ATOM    676  NZ  LYS A 105     -28.096  41.196 105.269  1.00 75.67           N  
ANISOU  676  NZ  LYS A 105    10359   9634   8756  -1824  -1426    631       N  
ATOM    677  N   LEU A 106     -21.858  40.089 101.924  1.00 62.05           N  
ANISOU  677  N   LEU A 106     9534   7801   6240  -2103  -1048    207       N  
ATOM    678  CA  LEU A 106     -20.867  39.882 100.870  1.00 62.49           C  
ANISOU  678  CA  LEU A 106     9742   7898   6104  -2211   -986    117       C  
ATOM    679  C   LEU A 106     -19.852  40.956 100.749  1.00 57.82           C  
ANISOU  679  C   LEU A 106     9179   7315   5474  -2149   -948    173       C  
ATOM    680  O   LEU A 106     -18.683  40.687 100.504  1.00 56.02           O  
ANISOU  680  O   LEU A 106     9042   7078   5166  -2156   -811     67       O  
ATOM    681  CB  LEU A 106     -21.540  39.726  99.515  1.00 68.99           C  
ANISOU  681  CB  LEU A 106    10628   8845   6740  -2421  -1123    136       C  
ATOM    682  CG  LEU A 106     -21.479  38.282  99.029  1.00 77.16           C  
ANISOU  682  CG  LEU A 106    11767   9870   7679  -2553  -1048    -58       C  
ATOM    683  CD1 LEU A 106     -20.044  37.736  99.042  1.00 80.47           C  
ANISOU  683  CD1 LEU A 106    12291  10224   8062  -2510   -836   -236       C  
ATOM    684  CD2 LEU A 106     -22.381  37.439  99.895  1.00 74.61           C  
ANISOU  684  CD2 LEU A 106    11356   9465   7529  -2517  -1063    -76       C  
ATOM    685  N   GLN A 107     -20.315  42.184 100.888  1.00 58.56           N  
ANISOU  685  N   GLN A 107     9187   7424   5639  -2092  -1074    341       N  
ATOM    686  CA  GLN A 107     -19.412  43.347 100.878  1.00 60.79           C  
ANISOU  686  CA  GLN A 107     9484   7693   5921  -2028  -1058    419       C  
ATOM    687  C   GLN A 107     -18.364  43.331 102.009  1.00 56.30           C  
ANISOU  687  C   GLN A 107     8902   7021   5468  -1868   -891    337       C  
ATOM    688  O   GLN A 107     -17.305  43.877 101.835  1.00 59.28           O  
ANISOU  688  O   GLN A 107     9327   7397   5799  -1857   -830    343       O  
ATOM    689  CB  GLN A 107     -20.215  44.659 100.947  1.00 63.01           C  
ANISOU  689  CB  GLN A 107     9659   7968   6316  -1977  -1237    613       C  
ATOM    690  CG  GLN A 107     -20.794  45.120  99.616  1.00 67.61           C  
ANISOU  690  CG  GLN A 107    10271   8661   6756  -2147  -1424    755       C  
ATOM    691  N   ASP A 108     -18.629  42.689 103.153  1.00 53.03           N  
ANISOU  691  N   ASP A 108     8421   6533   5194  -1762   -821    270       N  
ATOM    692  CA  ASP A 108     -17.622  42.643 104.229  1.00 46.89           C  
ANISOU  692  CA  ASP A 108     7631   5673   4511  -1628   -680    207       C  
ATOM    693  C   ASP A 108     -16.451  41.716 103.935  1.00 45.47           C  
ANISOU  693  C   ASP A 108     7547   5477   4252  -1664   -530     74       C  
ATOM    694  O   ASP A 108     -15.485  41.704 104.656  1.00 44.74           O  
ANISOU  694  O   ASP A 108     7446   5327   4226  -1570   -425     36       O  
ATOM    695  CB  ASP A 108     -18.250  42.264 105.545  1.00 44.93           C  
ANISOU  695  CB  ASP A 108     7283   5372   4417  -1521   -656    195       C  
ATOM    696  CG  ASP A 108     -19.355  43.207 105.917  1.00 45.97           C  
ANISOU  696  CG  ASP A 108     7298   5518   4651  -1464   -776    301       C  
ATOM    697  OD1 ASP A 108     -19.143  44.426 105.897  1.00 44.90           O  
ANISOU  697  OD1 ASP A 108     7140   5366   4553  -1409   -829    375       O  
ATOM    698  OD2 ASP A 108     -20.459  42.752 106.237  1.00 48.08           O  
ANISOU  698  OD2 ASP A 108     7485   5806   4978  -1471   -819    312       O  
ATOM    699  N   ALA A 109     -16.537  40.923 102.894  1.00 45.19           N  
ANISOU  699  N   ALA A 109     7594   5491   4083  -1801   -521     -5       N  
ATOM    700  CA  ALA A 109     -15.382  40.130 102.455  1.00 45.69           C  
ANISOU  700  CA  ALA A 109     7744   5542   4076  -1835   -368   -153       C  
ATOM    701  C   ALA A 109     -14.308  41.043 101.854  1.00 48.37           C  
ANISOU  701  C   ALA A 109     8123   5944   4313  -1856   -326   -121       C  
ATOM    702  O   ALA A 109     -14.612  42.066 101.259  1.00 49.74           O  
ANISOU  702  O   ALA A 109     8302   6195   4401  -1919   -439      4       O  
ATOM    703  CB  ALA A 109     -15.820  39.113 101.416  1.00 43.45           C  
ANISOU  703  CB  ALA A 109     7545   5303   3663  -1991   -369   -270       C  
ATOM    704  N   GLY A 110     -13.069  40.601 101.942  1.00 47.81           N  
ANISOU  704  N   GLY A 110     8075   5839   4253  -1816   -168   -230       N  
ATOM    705  CA  GLY A 110     -11.929  41.369 101.569  1.00 46.36           C  
ANISOU  705  CA  GLY A 110     7906   5707   4002  -1823   -102   -205       C  
ATOM    706  C   GLY A 110     -10.829  41.315 102.627  1.00 50.55           C  
ANISOU  706  C   GLY A 110     8373   6144   4690  -1675     11   -232       C  
ATOM    707  O   GLY A 110     -10.867  40.468 103.566  1.00 50.40           O  
ANISOU  707  O   GLY A 110     8312   6020   4818  -1577     55   -289       O  
ATOM    708  N   VAL A 111      -9.884  42.254 102.469  1.00 52.20           N  
ANISOU  708  N   VAL A 111     8571   6396   4865  -1674     40   -170       N  
ATOM    709  CA  VAL A 111      -8.661  42.405 103.254  1.00 50.03           C  
ANISOU  709  CA  VAL A 111     8235   6065   4707  -1566    138   -180       C  
ATOM    710  C   VAL A 111      -8.865  43.550 104.212  1.00 47.89           C  
ANISOU  710  C   VAL A 111     7907   5750   4540  -1482     28    -37       C  
ATOM    711  O   VAL A 111      -9.253  44.631 103.805  1.00 46.33           O  
ANISOU  711  O   VAL A 111     7725   5594   4286  -1536    -80     78       O  
ATOM    712  CB  VAL A 111      -7.448  42.764 102.328  1.00 51.04           C  
ANISOU  712  CB  VAL A 111     8385   6292   4717  -1647    246   -206       C  
ATOM    713  CG1 VAL A 111      -6.171  42.961 103.115  1.00 51.23           C  
ANISOU  713  CG1 VAL A 111     8328   6267   4872  -1544    336   -204       C  
ATOM    714  CG2 VAL A 111      -7.215  41.662 101.300  1.00 50.27           C  
ANISOU  714  CG2 VAL A 111     8346   6253   4501  -1737    378   -383       C  
ATOM    715  N   TYR A 112      -8.598  43.272 105.486  1.00 48.24           N  
ANISOU  715  N   TYR A 112     7886   5705   4738  -1356     55    -50       N  
ATOM    716  CA  TYR A 112      -8.702  44.184 106.599  1.00 41.72           C  
ANISOU  716  CA  TYR A 112     7002   4831   4018  -1267    -23     40       C  
ATOM    717  C   TYR A 112      -7.292  44.470 107.064  1.00 43.90           C  
ANISOU  717  C   TYR A 112     7236   5092   4351  -1222     53     41       C  
ATOM    718  O   TYR A 112      -6.413  43.607 107.006  1.00 44.88           O  
ANISOU  718  O   TYR A 112     7343   5209   4499  -1206    170    -38       O  
ATOM    719  CB  TYR A 112      -9.473  43.530 107.786  1.00 42.31           C  
ANISOU  719  CB  TYR A 112     7031   4844   4200  -1179    -45     23       C  
ATOM    720  CG  TYR A 112     -10.947  43.431 107.547  1.00 39.99           C  
ANISOU  720  CG  TYR A 112     6748   4566   3880  -1213   -137     44       C  
ATOM    721  CD1 TYR A 112     -11.447  42.524 106.613  1.00 40.78           C  
ANISOU  721  CD1 TYR A 112     6901   4694   3899  -1301   -124    -15       C  
ATOM    722  CD2 TYR A 112     -11.831  44.292 108.143  1.00 38.42           C  
ANISOU  722  CD2 TYR A 112     6504   4359   3736  -1168   -238    114       C  
ATOM    723  CE1 TYR A 112     -12.791  42.458 106.315  1.00 39.64           C  
ANISOU  723  CE1 TYR A 112     6757   4575   3728  -1350   -222     14       C  
ATOM    724  CE2 TYR A 112     -13.204  44.222 107.840  1.00 37.71           C  
ANISOU  724  CE2 TYR A 112     6401   4292   3634  -1202   -327    141       C  
ATOM    725  CZ  TYR A 112     -13.668  43.268 106.945  1.00 38.75           C  
ANISOU  725  CZ  TYR A 112     6582   4458   3685  -1296   -322     99       C  
ATOM    726  OH  TYR A 112     -14.997  43.187 106.581  1.00 41.11           O  
ANISOU  726  OH  TYR A 112     6862   4789   3969  -1346   -421    134       O  
ATOM    727  N   ARG A 113      -7.076  45.673 107.577  1.00 44.69           N  
ANISOU  727  N   ARG A 113     7310   5176   4494  -1196    -17    125       N  
ATOM    728  CA  ARG A 113      -5.786  46.019 108.168  1.00 46.90           C  
ANISOU  728  CA  ARG A 113     7540   5442   4840  -1158     33    135       C  
ATOM    729  C   ARG A 113      -5.990  46.496 109.578  1.00 43.81           C  
ANISOU  729  C   ARG A 113     7102   4993   4552  -1069    -35    162       C  
ATOM    730  O   ARG A 113      -6.912  47.263 109.854  1.00 39.01           O  
ANISOU  730  O   ARG A 113     6502   4361   3960  -1055   -132    198       O  
ATOM    731  CB  ARG A 113      -5.190  47.149 107.390  1.00 56.02           C  
ANISOU  731  CB  ARG A 113     8713   6636   5934  -1241      9    209       C  
ATOM    732  CG  ARG A 113      -3.989  46.801 106.557  1.00 60.75           C  
ANISOU  732  CG  ARG A 113     9305   7307   6472  -1307    135    175       C  
ATOM    733  CD  ARG A 113      -3.934  47.864 105.503  1.00 66.96           C  
ANISOU  733  CD  ARG A 113    10137   8157   7148  -1431     85    271       C  
ATOM    734  NE  ARG A 113      -2.697  47.880 104.754  1.00 75.28           N  
ANISOU  734  NE  ARG A 113    11170   9301   8133  -1513    201    264       N  
ATOM    735  CZ  ARG A 113      -2.295  48.912 104.012  1.00 80.29           C  
ANISOU  735  CZ  ARG A 113    11823   9996   8687  -1632    168    373       C  
ATOM    736  NH1 ARG A 113      -3.017  50.039 103.918  1.00 73.51           N  
ANISOU  736  NH1 ARG A 113    11007   9094   7828  -1674      6    506       N  
ATOM    737  NH2 ARG A 113      -1.146  48.826 103.368  1.00 86.67           N  
ANISOU  737  NH2 ARG A 113    12597  10906   9429  -1709    297    356       N  
ATOM    738  N   CYS A 114      -5.149  46.012 110.475  1.00 40.39           N  
ANISOU  738  N   CYS A 114     6613   4542   4191  -1012     18    139       N  
ATOM    739  CA  CYS A 114      -5.128  46.495 111.837  1.00 41.28           C  
ANISOU  739  CA  CYS A 114     6684   4627   4373   -951    -39    159       C  
ATOM    740  C   CYS A 114      -3.766  47.110 112.072  1.00 38.98           C  
ANISOU  740  C   CYS A 114     6353   4340   4119   -963    -28    189       C  
ATOM    741  O   CYS A 114      -2.740  46.553 111.636  1.00 36.55           O  
ANISOU  741  O   CYS A 114     6010   4054   3822   -978     57    181       O  
ATOM    742  CB  CYS A 114      -5.275  45.332 112.817  1.00 44.84           C  
ANISOU  742  CB  CYS A 114     7098   5068   4872   -891    -10    133       C  
ATOM    743  SG  CYS A 114      -3.837  44.233 112.808  1.00 48.01           S  
ANISOU  743  SG  CYS A 114     7440   5459   5343   -872     90    123       S  
ATOM    744  N   MET A 115      -3.759  48.214 112.803  1.00 37.69           N  
ANISOU  744  N   MET A 115     6183   4153   3985   -956   -108    213       N  
ATOM    745  CA  MET A 115      -2.511  48.853 113.248  1.00 37.10           C  
ANISOU  745  CA  MET A 115     6064   4079   3954   -976   -119    242       C  
ATOM    746  C   MET A 115      -2.674  49.095 114.722  1.00 36.48           C  
ANISOU  746  C   MET A 115     5962   3990   3908   -931   -179    219       C  
ATOM    747  O   MET A 115      -3.731  49.604 115.149  1.00 33.02           O  
ANISOU  747  O   MET A 115     5555   3528   3464   -905   -234    185       O  
ATOM    748  CB  MET A 115      -2.280  50.192 112.533  1.00 36.55           C  
ANISOU  748  CB  MET A 115     6026   3984   3878  -1048   -173    292       C  
ATOM    749  CG  MET A 115      -0.971  50.923 112.868  1.00 39.27           C  
ANISOU  749  CG  MET A 115     6323   4327   4270  -1093   -191    330       C  
ATOM    750  SD  MET A 115      -0.873  51.792 114.471  1.00 41.96           S  
ANISOU  750  SD  MET A 115     6648   4620   4676  -1066   -293    297       S  
ATOM    751  CE  MET A 115      -1.976  53.124 114.076  1.00 40.32           C  
ANISOU  751  CE  MET A 115     6515   4312   4493  -1079   -391    298       C  
ATOM    752  N   ILE A 116      -1.634  48.761 115.482  1.00 36.93           N  
ANISOU  752  N   ILE A 116     5957   4075   4001   -926   -168    236       N  
ATOM    753  CA  ILE A 116      -1.599  49.072 116.885  1.00 39.13           C  
ANISOU  753  CA  ILE A 116     6216   4370   4284   -912   -232    219       C  
ATOM    754  C   ILE A 116      -0.299  49.809 117.217  1.00 39.50           C  
ANISOU  754  C   ILE A 116     6218   4422   4368   -963   -273    251       C  
ATOM    755  O   ILE A 116       0.805  49.466 116.768  1.00 38.83           O  
ANISOU  755  O   ILE A 116     6072   4357   4325   -985   -231    303       O  
ATOM    756  CB  ILE A 116      -1.752  47.815 117.777  1.00 42.57           C  
ANISOU  756  CB  ILE A 116     6613   4849   4711   -870   -211    230       C  
ATOM    757  CG1 ILE A 116      -3.099  47.117 117.519  1.00 44.10           C  
ANISOU  757  CG1 ILE A 116     6847   5037   4872   -835   -179    201       C  
ATOM    758  CG2 ILE A 116      -1.707  48.169 119.266  1.00 39.51           C  
ANISOU  758  CG2 ILE A 116     6210   4512   4290   -881   -281    217       C  
ATOM    759  CD1 ILE A 116      -2.940  45.791 116.896  1.00 48.24           C  
ANISOU  759  CD1 ILE A 116     7352   5547   5429   -816   -108    225       C  
ATOM    760  N   SER A 117      -0.470  50.832 118.018  1.00 40.13           N  
ANISOU  760  N   SER A 117     6322   4484   4440   -984   -351    209       N  
ATOM    761  CA  SER A 117       0.632  51.648 118.462  1.00 45.23           C  
ANISOU  761  CA  SER A 117     6937   5130   5119  -1048   -412    226       C  
ATOM    762  C   SER A 117       0.640  51.689 119.998  1.00 40.88           C  
ANISOU  762  C   SER A 117     6374   4633   4525  -1054   -473    180       C  
ATOM    763  O   SER A 117      -0.373  51.999 120.639  1.00 43.39           O  
ANISOU  763  O   SER A 117     6742   4949   4794  -1029   -492     92       O  
ATOM    764  CB  SER A 117       0.505  53.026 117.863  1.00 41.67           C  
ANISOU  764  CB  SER A 117     6538   4589   4704  -1094   -461    211       C  
ATOM    765  OG  SER A 117       1.240  53.878 118.619  1.00 46.44           O  
ANISOU  765  OG  SER A 117     7129   5181   5336  -1154   -538    193       O  
ATOM    766  N   TYR A 118       1.763  51.292 120.557  1.00 40.38           N  
ANISOU  766  N   TYR A 118     6236   4632   4474  -1089   -499    243       N  
ATOM    767  CA  TYR A 118       1.885  51.046 121.964  1.00 50.45           C  
ANISOU  767  CA  TYR A 118     7490   5992   5685  -1111   -560    233       C  
ATOM    768  C   TYR A 118       3.327  50.727 122.217  1.00 53.58           C  
ANISOU  768  C   TYR A 118     7785   6439   6134  -1158   -601    336       C  
ATOM    769  O   TYR A 118       3.661  49.538 122.403  1.00 61.71           O  
ANISOU  769  O   TYR A 118     8742   7516   7190  -1123   -582    425       O  
ATOM    770  CB  TYR A 118       1.040  49.809 122.389  1.00 58.81           C  
ANISOU  770  CB  TYR A 118     8549   7107   6688  -1051   -516    250       C  
ATOM    771  CG  TYR A 118       0.878  49.613 123.907  1.00 62.72           C  
ANISOU  771  CG  TYR A 118     9043   7715   7075  -1092   -578    239       C  
ATOM    772  CD1 TYR A 118       0.220  50.566 124.692  1.00 64.77           C  
ANISOU  772  CD1 TYR A 118     9366   8002   7240  -1126   -609    108       C  
ATOM    773  CD2 TYR A 118       1.354  48.440 124.554  1.00 65.62           C  
ANISOU  773  CD2 TYR A 118     9340   8161   7433  -1099   -604    361       C  
ATOM    774  CE1 TYR A 118       0.053  50.375 126.063  1.00 66.76           C  
ANISOU  774  CE1 TYR A 118     9620   8386   7359  -1181   -652     87       C  
ATOM    775  CE2 TYR A 118       1.180  48.236 125.929  1.00 58.23           C  
ANISOU  775  CE2 TYR A 118     8405   7350   6370  -1158   -668    374       C  
ATOM    776  CZ  TYR A 118       0.533  49.198 126.681  1.00 66.21           C  
ANISOU  776  CZ  TYR A 118     9487   8416   7254  -1206   -686    232       C  
ATOM    777  OH  TYR A 118       0.378  49.015 128.053  1.00 74.88           O  
ANISOU  777  OH  TYR A 118    10590   9668   8193  -1284   -739    233       O  
ATOM    778  N   GLY A 119       4.163  51.769 122.209  1.00 51.84           N  
ANISOU  778  N   GLY A 119     7550   6199   5949  -1237   -663    331       N  
ATOM    779  CA  GLY A 119       5.590  51.669 122.406  1.00 52.59           C  
ANISOU  779  CA  GLY A 119     7531   6341   6108  -1295   -714    429       C  
ATOM    780  C   GLY A 119       6.509  50.886 121.442  1.00 59.21           C  
ANISOU  780  C   GLY A 119     8253   7180   7065  -1261   -636    537       C  
ATOM    781  O   GLY A 119       7.296  50.085 121.954  1.00 72.21           O  
ANISOU  781  O   GLY A 119     9786   8888   8762  -1253   -665    630       O  
ATOM    782  N   GLY A 120       6.534  51.052 120.109  1.00 58.75           N  
ANISOU  782  N   GLY A 120     8201   7066   7057  -1245   -541    535       N  
ATOM    783  CA  GLY A 120       5.749  51.965 119.236  1.00 56.57           C  
ANISOU  783  CA  GLY A 120     8037   6711   6748  -1261   -512    469       C  
ATOM    784  C   GLY A 120       4.771  51.236 118.290  1.00 47.98           C  
ANISOU  784  C   GLY A 120     7003   5593   5633  -1180   -403    443       C  
ATOM    785  O   GLY A 120       3.752  50.822 118.758  1.00 50.01           O  
ANISOU  785  O   GLY A 120     7320   5847   5836  -1124   -406    394       O  
ATOM    786  N   ALA A 121       5.001  51.111 116.982  1.00 45.22           N  
ANISOU  786  N   ALA A 121     6640   5235   5308  -1186   -309    469       N  
ATOM    787  CA  ALA A 121       3.892  50.636 116.058  1.00 41.12           C  
ANISOU  787  CA  ALA A 121     6201   4688   4735  -1135   -230    428       C  
ATOM    788  C   ALA A 121       4.137  49.559 115.026  1.00 38.91           C  
ANISOU  788  C   ALA A 121     5878   4438   4470  -1101    -97    432       C  
ATOM    789  O   ALA A 121       5.228  49.437 114.509  1.00 38.87           O  
ANISOU  789  O   ALA A 121     5779   4473   4515  -1131    -33    468       O  
ATOM    790  CB  ALA A 121       3.302  51.803 115.307  1.00 45.34           C  
ANISOU  790  CB  ALA A 121     6829   5166   5234  -1192   -263    421       C  
ATOM    791  N   ASP A 122       3.066  48.847 114.666  1.00 36.79           N  
ANISOU  791  N   ASP A 122     5676   4149   4153  -1046    -52    384       N  
ATOM    792  CA  ASP A 122       3.095  47.831 113.625  1.00 37.99           C  
ANISOU  792  CA  ASP A 122     5813   4317   4305  -1020     74    354       C  
ATOM    793  C   ASP A 122       1.696  47.567 113.098  1.00 39.84           C  
ANISOU  793  C   ASP A 122     6157   4525   4456  -1004     84    303       C  
ATOM    794  O   ASP A 122       0.697  48.035 113.670  1.00 39.24           O  
ANISOU  794  O   ASP A 122     6148   4417   4344   -991     -3    295       O  
ATOM    795  CB  ASP A 122       3.664  46.529 114.182  1.00 43.64           C  
ANISOU  795  CB  ASP A 122     6429   5031   5122   -942    121    355       C  
ATOM    796  CG  ASP A 122       4.123  45.540 113.112  1.00 45.90           C  
ANISOU  796  CG  ASP A 122     6664   5325   5452   -916    270    304       C  
ATOM    797  OD1 ASP A 122       4.346  45.904 111.919  1.00 44.52           O  
ANISOU  797  OD1 ASP A 122     6506   5194   5215   -978    355    275       O  
ATOM    798  OD2 ASP A 122       4.273  44.372 113.506  1.00 45.92           O  
ANISOU  798  OD2 ASP A 122     6605   5287   5554   -836    302    293       O  
ATOM    799  N   TYR A 123       1.631  46.877 111.954  1.00 40.56           N  
ANISOU  799  N   TYR A 123     6262   4636   4514  -1012    191    260       N  
ATOM    800  CA  TYR A 123       0.348  46.454 111.365  1.00 40.56           C  
ANISOU  800  CA  TYR A 123     6356   4620   4434  -1008    200    211       C  
ATOM    801  C   TYR A 123       0.423  45.151 110.603  1.00 40.66           C  
ANISOU  801  C   TYR A 123     6359   4639   4452   -987    325    133       C  
ATOM    802  O   TYR A 123       1.481  44.726 110.235  1.00 43.74           O  
ANISOU  802  O   TYR A 123     6672   5053   4895   -984    425    108       O  
ATOM    803  CB  TYR A 123      -0.192  47.498 110.388  1.00 40.90           C  
ANISOU  803  CB  TYR A 123     6482   4685   4372  -1097    162    239       C  
ATOM    804  CG  TYR A 123       0.659  47.887 109.181  1.00 38.26           C  
ANISOU  804  CG  TYR A 123     6137   4424   3977  -1195    239    262       C  
ATOM    805  CD1 TYR A 123       0.623  47.180 107.995  1.00 38.31           C  
ANISOU  805  CD1 TYR A 123     6169   4492   3896  -1239    352    201       C  
ATOM    806  CD2 TYR A 123       1.413  49.042 109.213  1.00 39.90           C  
ANISOU  806  CD2 TYR A 123     6317   4644   4201  -1261    193    343       C  
ATOM    807  CE1 TYR A 123       1.337  47.608 106.860  1.00 39.54           C  
ANISOU  807  CE1 TYR A 123     6318   4744   3962  -1351    429    223       C  
ATOM    808  CE2 TYR A 123       2.159  49.462 108.122  1.00 43.23           C  
ANISOU  808  CE2 TYR A 123     6724   5147   4555  -1370    261    382       C  
ATOM    809  CZ  TYR A 123       2.101  48.745 106.932  1.00 42.91           C  
ANISOU  809  CZ  TYR A 123     6707   5190   4406  -1417    384    324       C  
ATOM    810  OH  TYR A 123       2.836  49.235 105.880  1.00 46.43           O  
ANISOU  810  OH  TYR A 123     7138   5741   4760  -1545    456    369       O  
ATOM    811  N   LYS A 124      -0.738  44.588 110.318  1.00 43.09           N  
ANISOU  811  N   LYS A 124     6742   4923   4707   -980    318     87       N  
ATOM    812  CA  LYS A 124      -0.904  43.321 109.602  1.00 44.22           C  
ANISOU  812  CA  LYS A 124     6898   5051   4851   -969    422     -9       C  
ATOM    813  C   LYS A 124      -2.181  43.357 108.780  1.00 42.01           C  
ANISOU  813  C   LYS A 124     6728   4791   4444  -1031    393    -41       C  
ATOM    814  O   LYS A 124      -3.056  44.195 109.016  1.00 42.83           O  
ANISOU  814  O   LYS A 124     6879   4899   4497  -1051    281     21       O  
ATOM    815  CB  LYS A 124      -1.092  42.162 110.595  1.00 46.64           C  
ANISOU  815  CB  LYS A 124     7164   5274   5284   -877    414    -21       C  
ATOM    816  CG  LYS A 124       0.077  41.844 111.501  1.00 47.59           C  
ANISOU  816  CG  LYS A 124     7166   5364   5553   -808    424     25       C  
ATOM    817  CD  LYS A 124       1.334  41.328 110.797  1.00 47.00           C  
ANISOU  817  CD  LYS A 124     7001   5293   5562   -791    560    -36       C  
ATOM    818  CE  LYS A 124       2.503  42.200 111.245  1.00 50.80           C  
ANISOU  818  CE  LYS A 124     7386   5826   6088   -799    535     46       C  
ATOM    819  NZ  LYS A 124       3.762  41.477 111.375  1.00 57.92           N  
ANISOU  819  NZ  LYS A 124     8142   6702   7162   -733    617     37       N  
ATOM    820  N   ARG A 125      -2.300  42.409 107.852  1.00 43.21           N  
ANISOU  820  N   ARG A 125     6911   4950   4557  -1060    489   -145       N  
ATOM    821  CA  ARG A 125      -3.472  42.242 106.980  1.00 44.14           C  
ANISOU  821  CA  ARG A 125     7129   5096   4547  -1135    462   -186       C  
ATOM    822  C   ARG A 125      -4.168  40.918 107.265  1.00 44.47           C  
ANISOU  822  C   ARG A 125     7185   5054   4657  -1090    476   -262       C  
ATOM    823  O   ARG A 125      -3.518  39.887 107.531  1.00 41.87           O  
ANISOU  823  O   ARG A 125     6802   4652   4453  -1026    563   -332       O  
ATOM    824  CB  ARG A 125      -3.014  42.183 105.495  1.00 53.04           C  
ANISOU  824  CB  ARG A 125     8297   6320   5537  -1241    573   -267       C  
ATOM    825  CG  ARG A 125      -2.321  43.439 104.946  1.00 60.72           C  
ANISOU  825  CG  ARG A 125     9263   7394   6415  -1324    571   -182       C  
ATOM    826  CD  ARG A 125      -1.659  43.202 103.567  1.00 65.45           C  
ANISOU  826  CD  ARG A 125     9882   8113   6874  -1433    718   -276       C  
ATOM    827  N   ILE A 126      -5.488  40.921 107.144  1.00 46.21           N  
ANISOU  827  N   ILE A 126     7471   5277   4810  -1130    387   -247       N  
ATOM    828  CA  ILE A 126      -6.302  39.732 107.357  1.00 44.26           C  
ANISOU  828  CA  ILE A 126     7242   4956   4617  -1115    383   -306       C  
ATOM    829  C   ILE A 126      -7.328  39.607 106.264  1.00 42.46           C  
ANISOU  829  C   ILE A 126     7104   4781   4249  -1225    352   -356       C  
ATOM    830  O   ILE A 126      -8.121  40.533 106.036  1.00 42.98           O  
ANISOU  830  O   ILE A 126     7199   4913   4221  -1276    246   -272       O  
ATOM    831  CB  ILE A 126      -7.112  39.810 108.668  1.00 44.12           C  
ANISOU  831  CB  ILE A 126     7191   4895   4679  -1053    277   -210       C  
ATOM    832  CG1 ILE A 126      -6.179  39.707 109.856  1.00 47.46           C  
ANISOU  832  CG1 ILE A 126     7530   5268   5234   -959    293   -159       C  
ATOM    833  CG2 ILE A 126      -8.191  38.713 108.681  1.00 43.80           C  
ANISOU  833  CG2 ILE A 126     7180   4800   4663  -1076    255   -252       C  
ATOM    834  CD1 ILE A 126      -6.803  40.052 111.202  1.00 47.63           C  
ANISOU  834  CD1 ILE A 126     7516   5289   5291   -914    198    -62       C  
ATOM    835  N   THR A 127      -7.393  38.427 105.666  1.00 44.89           N  
ANISOU  835  N   THR A 127     7448   5046   4561  -1259    429   -489       N  
ATOM    836  CA  THR A 127      -8.364  38.171 104.652  1.00 45.03           C  
ANISOU  836  CA  THR A 127     7553   5117   4440  -1378    394   -549       C  
ATOM    837  C   THR A 127      -9.569  37.554 105.319  1.00 46.62           C  
ANISOU  837  C   THR A 127     7751   5245   4719  -1365    301   -517       C  
ATOM    838  O   THR A 127      -9.488  36.608 106.089  1.00 51.05           O  
ANISOU  838  O   THR A 127     8275   5689   5432  -1297    329   -541       O  
ATOM    839  CB  THR A 127      -7.770  37.313 103.511  1.00 48.92           C  
ANISOU  839  CB  THR A 127     8098   5621   4868  -1448    536   -739       C  
ATOM    840  OG1 THR A 127      -6.599  37.961 103.026  1.00 51.88           O  
ANISOU  840  OG1 THR A 127     8451   6082   5179  -1456    632   -751       O  
ATOM    841  CG2 THR A 127      -8.756  37.142 102.337  1.00 48.16           C  
ANISOU  841  CG2 THR A 127     8106   5612   4582  -1606    489   -806       C  
ATOM    842  N   VAL A 128     -10.705  38.132 104.986  1.00 50.30           N  
ANISOU  842  N   VAL A 128     8247   5786   5079  -1440    182   -447       N  
ATOM    843  CA  VAL A 128     -11.999  37.589 105.304  1.00 50.62           C  
ANISOU  843  CA  VAL A 128     8285   5795   5155  -1467     92   -424       C  
ATOM    844  C   VAL A 128     -12.704  37.082 104.032  1.00 53.75           C  
ANISOU  844  C   VAL A 128     8767   6242   5413  -1617     67   -517       C  
ATOM    845  O   VAL A 128     -12.852  37.804 103.039  1.00 61.23           O  
ANISOU  845  O   VAL A 128     9762   7308   6193  -1715     23   -497       O  
ATOM    846  CB  VAL A 128     -12.869  38.649 105.970  1.00 45.98           C  
ANISOU  846  CB  VAL A 128     7640   5256   4576  -1433    -34   -272       C  
ATOM    847  CG1 VAL A 128     -14.263  38.120 106.249  1.00 48.18           C  
ANISOU  847  CG1 VAL A 128     7895   5524   4888  -1470   -122   -245       C  
ATOM    848  CG2 VAL A 128     -12.211  39.084 107.249  1.00 44.80           C  
ANISOU  848  CG2 VAL A 128     7416   5063   4543  -1304     -9   -206       C  
ATOM    849  N   LYS A 129     -13.150  35.835 104.113  1.00 53.95           N  
ANISOU  849  N   LYS A 129     8810   6176   5511  -1645     83   -607       N  
ATOM    850  CA  LYS A 129     -13.892  35.148 103.086  1.00 52.02           C  
ANISOU  850  CA  LYS A 129     8646   5958   5162  -1792     52   -712       C  
ATOM    851  C   LYS A 129     -15.270  34.861 103.701  1.00 53.42           C  
ANISOU  851  C   LYS A 129     8776   6109   5411  -1814    -75   -620       C  
ATOM    852  O   LYS A 129     -15.393  34.280 104.811  1.00 53.63           O  
ANISOU  852  O   LYS A 129     8741   6027   5608  -1733    -66   -579       O  
ATOM    853  CB  LYS A 129     -13.168  33.862 102.769  1.00 53.23           C  
ANISOU  853  CB  LYS A 129     8848   5992   5384  -1798    189   -910       C  
ATOM    854  CG  LYS A 129     -13.746  33.072 101.626  1.00 57.82           C  
ANISOU  854  CG  LYS A 129     9530   6592   5848  -1962    182  -1071       C  
ATOM    855  N   VAL A 130     -16.297  35.361 103.037  1.00 51.85           N  
ANISOU  855  N   VAL A 130     8592   6025   5085  -1924   -200   -561       N  
ATOM    856  CA  VAL A 130     -17.664  35.233 103.487  1.00 52.77           C  
ANISOU  856  CA  VAL A 130     8644   6149   5258  -1956   -326   -466       C  
ATOM    857  C   VAL A 130     -18.280  34.110 102.682  1.00 61.98           C  
ANISOU  857  C   VAL A 130     9883   7292   6373  -2113   -353   -590       C  
ATOM    858  O   VAL A 130     -18.443  34.235 101.455  1.00 57.95           O  
ANISOU  858  O   VAL A 130     9455   6883   5682  -2252   -394   -652       O  
ATOM    859  CB  VAL A 130     -18.456  36.543 103.298  1.00 52.22           C  
ANISOU  859  CB  VAL A 130     8517   6209   5114  -1970   -465   -310       C  
ATOM    860  CG1 VAL A 130     -19.949  36.299 103.505  1.00 53.61           C  
ANISOU  860  CG1 VAL A 130     8619   6413   5339  -2031   -594   -234       C  
ATOM    861  CG2 VAL A 130     -17.942  37.636 104.254  1.00 49.29           C  
ANISOU  861  CG2 VAL A 130     8068   5834   4827  -1811   -443   -200       C  
ATOM    862  N   ASN A 131     -18.574  32.998 103.377  1.00 73.99           N  
ANISOU  862  N   ASN A 131    11381   8682   8049  -2101   -331   -624       N  
ATOM    863  CA  ASN A 131     -19.234  31.814 102.787  1.00 80.28           C  
ANISOU  863  CA  ASN A 131    12241   9421   8842  -2251   -365   -743       C  
ATOM    864  C   ASN A 131     -20.736  31.986 102.868  1.00 80.80           C  
ANISOU  864  C   ASN A 131    12233   9571   8897  -2342   -527   -617       C  
ATOM    865  O   ASN A 131     -21.271  32.203 103.968  1.00 81.03           O  
ANISOU  865  O   ASN A 131    12144   9594   9051  -2260   -562   -473       O  
ATOM    866  CB  ASN A 131     -18.865  30.534 103.548  1.00 83.59           C  
ANISOU  866  CB  ASN A 131    12658   9635   9467  -2201   -281   -814       C  
ATOM    867  CG  ASN A 131     -17.770  29.729 102.866  1.00 86.33           C  
ANISOU  867  CG  ASN A 131    13110   9866   9824  -2208   -144  -1036       C  
ATOM    868  OD1 ASN A 131     -16.785  30.274 102.355  1.00 94.34           O  
ANISOU  868  OD1 ASN A 131    14163  10939  10743  -2163    -52  -1106       O  
ATOM    869  ND2 ASN A 131     -17.924  28.417 102.881  1.00 82.70           N  
ANISOU  869  ND2 ASN A 131    12690   9233   9498  -2264   -125  -1152       N  
ATOM    870  N   ALA A 132     -21.417  31.876 101.730  1.00 74.09           N  
ANISOU  870  N   ALA A 132    11444   8811   7896  -2517   -623   -672       N  
ATOM    871  CA  ALA A 132     -22.860  32.173 101.667  1.00 72.99           C  
ANISOU  871  CA  ALA A 132    11217   8777   7739  -2612   -797   -537       C  
ATOM    872  C   ALA A 132     -23.714  31.070 101.018  1.00 67.88           C  
ANISOU  872  C   ALA A 132    10622   8106   7064  -2812   -879   -634       C  
ATOM    873  O   ALA A 132     -23.275  30.418 100.039  1.00 65.38           O  
ANISOU  873  O   ALA A 132    10447   7763   6633  -2932   -837   -827       O  
ATOM    874  CB  ALA A 132     -23.042  33.502 100.925  1.00 76.61           C  
ANISOU  874  CB  ALA A 132    11663   9411   8033  -2635   -898   -432       C  
TER     875      ALA A 132                                                      
ATOM    876  N   ASN B  33      -0.321  60.859 100.007  1.00 88.83           N  
ANISOU  876  N   ASN B  33    11026  11430  11296     35   -794    329       N  
ATOM    877  CA  ASN B  33       1.065  61.288  99.659  1.00 92.11           C  
ANISOU  877  CA  ASN B  33    11543  11914  11540      8   -752    490       C  
ATOM    878  C   ASN B  33       2.093  60.204 100.010  1.00 94.06           C  
ANISOU  878  C   ASN B  33    11814  12256  11667    -52   -673    458       C  
ATOM    879  O   ASN B  33       3.014  60.458 100.838  1.00 97.03           O  
ANISOU  879  O   ASN B  33    12218  12622  12028   -135   -575    491       O  
ATOM    880  CB  ASN B  33       1.411  62.602 100.375  1.00 89.03           C  
ANISOU  880  CB  ASN B  33    11184  11406  11236    -61   -669    574       C  
ATOM    881  N   PRO B  34       1.951  58.996  99.376  1.00 87.33           N  
ANISOU  881  N   PRO B  34    10948  11499  10736      1   -723    381       N  
ATOM    882  CA  PRO B  34       2.741  57.799  99.756  1.00 78.55           C  
ANISOU  882  CA  PRO B  34     9857  10448   9542    -29   -656    327       C  
ATOM    883  C   PRO B  34       4.257  58.004  99.728  1.00 66.94           C  
ANISOU  883  C   PRO B  34     8429   9067   7937    -58   -600    425       C  
ATOM    884  O   PRO B  34       4.762  58.734  98.881  1.00 70.95           O  
ANISOU  884  O   PRO B  34     8961   9638   8358    -46   -615    529       O  
ATOM    885  CB  PRO B  34       2.328  56.725  98.700  1.00 79.84           C  
ANISOU  885  CB  PRO B  34     9999  10698   9637     46   -735    240       C  
ATOM    886  CG  PRO B  34       1.644  57.471  97.605  1.00 80.22           C  
ANISOU  886  CG  PRO B  34    10031  10783   9667    123   -861    282       C  
ATOM    887  CD  PRO B  34       1.023  58.680  98.266  1.00 86.21           C  
ANISOU  887  CD  PRO B  34    10767  11409  10581    100   -857    325       C  
ATOM    888  N   PRO B  35       4.982  57.328 100.624  1.00 58.27           N  
ANISOU  888  N   PRO B  35     7343   7975   6821    -90   -534    385       N  
ATOM    889  CA  PRO B  35       6.428  57.343 100.478  1.00 52.79           C  
ANISOU  889  CA  PRO B  35     6651   7396   6011    -98   -500    436       C  
ATOM    890  C   PRO B  35       6.930  56.643  99.202  1.00 52.61           C  
ANISOU  890  C   PRO B  35     6626   7510   5853    -32   -527    434       C  
ATOM    891  O   PRO B  35       6.191  55.917  98.544  1.00 55.48           O  
ANISOU  891  O   PRO B  35     6996   7882   6203     25   -580    374       O  
ATOM    892  CB  PRO B  35       6.924  56.639 101.752  1.00 58.69           C  
ANISOU  892  CB  PRO B  35     7415   8116   6769   -110   -459    377       C  
ATOM    893  CG  PRO B  35       5.762  55.876 102.283  1.00 57.21           C  
ANISOU  893  CG  PRO B  35     7264   7809   6663   -101   -454    296       C  
ATOM    894  CD  PRO B  35       4.517  56.500 101.758  1.00 54.34           C  
ANISOU  894  CD  PRO B  35     6867   7382   6399   -112   -488    289       C  
ATOM    895  N   THR B  36       8.169  56.917  98.820  1.00 49.83           N  
ANISOU  895  N   THR B  36     6256   7268   5408    -49   -481    481       N  
ATOM    896  CA  THR B  36       8.766  56.234  97.703  1.00 50.26           C  
ANISOU  896  CA  THR B  36     6307   7460   5332      5   -479    461       C  
ATOM    897  C   THR B  36       9.906  55.453  98.282  1.00 51.09           C  
ANISOU  897  C   THR B  36     6361   7628   5420     26   -440    394       C  
ATOM    898  O   THR B  36      10.496  55.815  99.318  1.00 52.68           O  
ANISOU  898  O   THR B  36     6530   7810   5678    -15   -416    395       O  
ATOM    899  CB  THR B  36       9.259  57.187  96.580  1.00 54.92           C  
ANISOU  899  CB  THR B  36     6920   8132   5813    -28   -436    565       C  
ATOM    900  OG1 THR B  36      10.265  58.068  97.091  1.00 67.06           O  
ANISOU  900  OG1 THR B  36     8419   9677   7384   -120   -344    612       O  
ATOM    901  CG2 THR B  36       8.112  58.039  96.069  1.00 57.72           C  
ANISOU  901  CG2 THR B  36     7344   8407   6181    -17   -500    649       C  
ATOM    902  N   PHE B  37      10.195  54.367  97.600  1.00 51.28           N  
ANISOU  902  N   PHE B  37     6380   7734   5369    101   -446    323       N  
ATOM    903  CA  PHE B  37      11.153  53.405  98.032  1.00 55.04           C  
ANISOU  903  CA  PHE B  37     6814   8260   5838    163   -431    244       C  
ATOM    904  C   PHE B  37      11.916  53.037  96.771  1.00 55.69           C  
ANISOU  904  C   PHE B  37     6857   8495   5807    197   -389    206       C  
ATOM    905  O   PHE B  37      11.324  52.504  95.852  1.00 50.59           O  
ANISOU  905  O   PHE B  37     6254   7869   5100    235   -409    170       O  
ATOM    906  CB  PHE B  37      10.419  52.192  98.616  1.00 55.45           C  
ANISOU  906  CB  PHE B  37     6928   8195   5945    233   -471    171       C  
ATOM    907  CG  PHE B  37      11.270  51.332  99.523  1.00 54.11           C  
ANISOU  907  CG  PHE B  37     6757   8014   5790    314   -474    122       C  
ATOM    908  CD1 PHE B  37      11.909  51.886 100.615  1.00 51.90           C  
ANISOU  908  CD1 PHE B  37     6451   7734   5534    295   -484    154       C  
ATOM    909  CD2 PHE B  37      11.386  49.987  99.307  1.00 55.87           C  
ANISOU  909  CD2 PHE B  37     7012   8216   6001    417   -477     39       C  
ATOM    910  CE1 PHE B  37      12.686  51.136 101.451  1.00 52.35           C  
ANISOU  910  CE1 PHE B  37     6515   7790   5584    395   -518    114       C  
ATOM    911  CE2 PHE B  37      12.151  49.212 100.167  1.00 60.72           C  
ANISOU  911  CE2 PHE B  37     7646   8801   6625    520   -496     10       C  
ATOM    912  CZ  PHE B  37      12.812  49.792 101.228  1.00 55.41           C  
ANISOU  912  CZ  PHE B  37     6948   8148   5958    518   -528     52       C  
ATOM    913  N   SER B  38      13.207  53.347  96.713  1.00 59.36           N  
ANISOU  913  N   SER B  38     7232   9075   6248    176   -323    196       N  
ATOM    914  CA  SER B  38      13.990  53.085  95.507  1.00 62.51           C  
ANISOU  914  CA  SER B  38     7586   9625   6539    190   -247    149       C  
ATOM    915  C   SER B  38      15.348  52.601  95.888  1.00 65.47           C  
ANISOU  915  C   SER B  38     7829  10096   6950    238   -211     50       C  
ATOM    916  O   SER B  38      15.744  52.778  97.040  1.00 70.69           O  
ANISOU  916  O   SER B  38     8434  10722   7702    243   -251     42       O  
ATOM    917  CB  SER B  38      14.129  54.351  94.668  1.00 62.81           C  
ANISOU  917  CB  SER B  38     7649   9719   6496     76   -159    253       C  
ATOM    918  OG  SER B  38      14.672  55.382  95.442  1.00 73.14           O  
ANISOU  918  OG  SER B  38     8897  11003   7890    -20   -113    301       O  
ATOM    919  N   PRO B  39      16.069  51.983  94.931  1.00 67.30           N  
ANISOU  919  N   PRO B  39     8005  10457   7111    282   -141    -41       N  
ATOM    920  CA  PRO B  39      15.548  51.624  93.604  1.00 63.44           C  
ANISOU  920  CA  PRO B  39     7600  10015   6490    292   -109    -53       C  
ATOM    921  C   PRO B  39      14.523  50.515  93.727  1.00 61.96           C  
ANISOU  921  C   PRO B  39     7498   9718   6325    390   -212   -106       C  
ATOM    922  O   PRO B  39      14.596  49.678  94.640  1.00 64.06           O  
ANISOU  922  O   PRO B  39     7749   9898   6693    478   -267   -164       O  
ATOM    923  CB  PRO B  39      16.783  51.109  92.871  1.00 63.40           C  
ANISOU  923  CB  PRO B  39     7484  10172   6436    324      2   -177       C  
ATOM    924  CG  PRO B  39      17.605  50.509  93.954  1.00 65.58           C  
ANISOU  924  CG  PRO B  39     7631  10436   6851    419    -45   -269       C  
ATOM    925  CD  PRO B  39      17.442  51.478  95.114  1.00 65.88           C  
ANISOU  925  CD  PRO B  39     7664  10391   6976    346   -100   -167       C  
ATOM    926  N   ALA B  40      13.561  50.521  92.818  1.00 61.47           N  
ANISOU  926  N   ALA B  40     7533   9656   6167    375   -237    -90       N  
ATOM    927  CA  ALA B  40      12.488  49.546  92.842  1.00 56.40           C  
ANISOU  927  CA  ALA B  40     6956   8912   5561    439   -323   -166       C  
ATOM    928  C   ALA B  40      12.940  48.088  92.557  1.00 54.79           C  
ANISOU  928  C   ALA B  40     6726   8727   5367    545   -298   -331       C  
ATOM    929  O   ALA B  40      12.198  47.160  92.794  1.00 51.56           O  
ANISOU  929  O   ALA B  40     6364   8199   5027    594   -345   -410       O  
ATOM    930  CB  ALA B  40      11.380  49.992  91.906  1.00 55.30           C  
ANISOU  930  CB  ALA B  40     6901   8793   5318    404   -378   -130       C  
ATOM    931  N   LEU B  41      14.150  47.886  92.063  1.00 56.76           N  
ANISOU  931  N   LEU B  41     6893   9110   5562    575   -210   -396       N  
ATOM    932  CA  LEU B  41      14.672  46.537  91.823  1.00 58.82           C  
ANISOU  932  CA  LEU B  41     7117   9379   5852    691   -180   -561       C  
ATOM    933  C   LEU B  41      16.121  46.695  92.123  1.00 60.89           C  
ANISOU  933  C   LEU B  41     7242   9740   6152    723   -111   -585       C  
ATOM    934  O   LEU B  41      16.703  47.735  91.793  1.00 62.31           O  
ANISOU  934  O   LEU B  41     7363  10044   6268    627    -36   -523       O  
ATOM    935  CB  LEU B  41      14.489  46.086  90.354  1.00 64.19           C  
ANISOU  935  CB  LEU B  41     7830  10177   6382    690   -132   -676       C  
ATOM    936  N   LEU B  42      16.720  45.709  92.765  1.00 59.72           N  
ANISOU  936  N   LEU B  42     7041   9531   6118    859   -134   -678       N  
ATOM    937  CA  LEU B  42      18.101  45.880  93.189  1.00 64.25           C  
ANISOU  937  CA  LEU B  42     7453  10206   6755    910   -101   -719       C  
ATOM    938  C   LEU B  42      18.720  44.514  93.229  1.00 67.38           C  
ANISOU  938  C   LEU B  42     7801  10571   7231   1093   -108   -875       C  
ATOM    939  O   LEU B  42      18.218  43.625  93.921  1.00 65.50           O  
ANISOU  939  O   LEU B  42     7667  10151   7070   1201   -189   -875       O  
ATOM    940  CB  LEU B  42      18.161  46.561  94.567  1.00 68.03           C  
ANISOU  940  CB  LEU B  42     7917  10612   7319    895   -191   -603       C  
ATOM    941  CG  LEU B  42      19.538  46.792  95.229  1.00 71.78           C  
ANISOU  941  CG  LEU B  42     8204  11190   7877    955   -201   -660       C  
ATOM    942  CD1 LEU B  42      20.317  47.899  94.512  1.00 70.76           C  
ANISOU  942  CD1 LEU B  42     7931  11252   7704    805    -68   -676       C  
ATOM    943  CD2 LEU B  42      19.389  47.111  96.709  1.00 67.86           C  
ANISOU  943  CD2 LEU B  42     7744  10589   7451    982   -328   -568       C  
ATOM    944  N   VAL B  43      19.793  44.334  92.457  1.00 76.31           N  
ANISOU  944  N   VAL B  43     8782  11866   8346   1125     -4  -1012       N  
ATOM    945  CA  VAL B  43      20.545  43.065  92.456  1.00 79.61           C  
ANISOU  945  CA  VAL B  43     9123  12264   8861   1321     -3  -1183       C  
ATOM    946  C   VAL B  43      21.881  43.291  93.130  1.00 76.96           C  
ANISOU  946  C   VAL B  43     8576  12029   8635   1410    -27  -1238       C  
ATOM    947  O   VAL B  43      22.570  44.251  92.780  1.00 76.24           O  
ANISOU  947  O   VAL B  43     8335  12116   8515   1288     67  -1253       O  
ATOM    948  CB  VAL B  43      20.776  42.532  91.028  1.00 79.93           C  
ANISOU  948  CB  VAL B  43     9130  12420   8818   1313    138  -1350       C  
ATOM    949  CG1 VAL B  43      21.614  41.262  91.057  1.00 82.90           C  
ANISOU  949  CG1 VAL B  43     9410  12767   9322   1527    145  -1539       C  
ATOM    950  CG2 VAL B  43      19.439  42.269  90.337  1.00 80.01           C  
ANISOU  950  CG2 VAL B  43     9335  12350   8715   1236    135  -1326       C  
ATOM    951  N   VAL B  44      22.232  42.431  94.092  1.00 75.54           N  
ANISOU  951  N   VAL B  44     8391  11732   8580   1621   -152  -1272       N  
ATOM    952  CA  VAL B  44      23.582  42.454  94.697  1.00 79.68           C  
ANISOU  952  CA  VAL B  44     8687  12367   9219   1759   -209  -1369       C  
ATOM    953  C   VAL B  44      24.129  41.043  94.978  1.00 82.50           C  
ANISOU  953  C   VAL B  44     9025  12625   9696   2046   -286  -1498       C  
ATOM    954  O   VAL B  44      23.349  40.095  95.177  1.00 77.20           O  
ANISOU  954  O   VAL B  44     8570  11733   9030   2144   -331  -1453       O  
ATOM    955  CB  VAL B  44      23.637  43.252  96.025  1.00 78.82           C  
ANISOU  955  CB  VAL B  44     8571  12239   9138   1744   -353  -1240       C  
ATOM    956  CG1 VAL B  44      23.213  44.702  95.815  1.00 78.34           C  
ANISOU  956  CG1 VAL B  44     8514  12263   8991   1473   -273  -1123       C  
ATOM    957  CG2 VAL B  44      22.791  42.586  97.104  1.00 78.77           C  
ANISOU  957  CG2 VAL B  44     8810  11985   9136   1868   -503  -1108       C  
ATOM    958  N   THR B  45      25.466  40.928  95.013  1.00 83.03           N  
ANISOU  958  N   THR B  45     8829  12846   9872   2181   -296  -1664       N  
ATOM    959  CA  THR B  45      26.141  39.678  95.370  1.00 85.31           C  
ANISOU  959  CA  THR B  45     9070  13049  10293   2492   -395  -1791       C  
ATOM    960  C   THR B  45      26.157  39.526  96.917  1.00 82.75           C  
ANISOU  960  C   THR B  45     8843  12591  10007   2677   -635  -1663       C  
ATOM    961  O   THR B  45      26.517  40.466  97.646  1.00 77.55           O  
ANISOU  961  O   THR B  45     8076  12049   9341   2619   -727  -1612       O  
ATOM    962  CB  THR B  45      27.580  39.573  94.769  1.00 91.14           C  
ANISOU  962  CB  THR B  45     9462  14015  11153   2584   -317  -2051       C  
ATOM    963  OG1 THR B  45      28.534  40.278  95.575  1.00 93.46           O  
ANISOU  963  OG1 THR B  45     9516  14466  11529   2627   -432  -2092       O  
ATOM    964  CG2 THR B  45      27.641  40.118  93.337  1.00 93.84           C  
ANISOU  964  CG2 THR B  45     9704  14538  11411   2338    -56  -2151       C  
ATOM    965  N   GLU B  46      25.733  38.354  97.401  1.00 81.65           N  
ANISOU  965  N   GLU B  46     8929  12197   9897   2889   -725  -1610       N  
ATOM    966  CA  GLU B  46      25.777  38.012  98.830  1.00 82.60           C  
ANISOU  966  CA  GLU B  46     9193  12164  10027   3106   -945  -1485       C  
ATOM    967  C   GLU B  46      27.083  38.463  99.539  1.00 84.20           C  
ANISOU  967  C   GLU B  46     9119  12575  10300   3264  -1116  -1579       C  
ATOM    968  O   GLU B  46      28.204  38.338  98.988  1.00 78.85           O  
ANISOU  968  O   GLU B  46     8135  12083   9742   3365  -1092  -1800       O  
ATOM    969  CB  GLU B  46      25.565  36.498  99.027  1.00 86.69           C  
ANISOU  969  CB  GLU B  46     9935  12396  10606   3372   -986  -1480       C  
ATOM    970  CG  GLU B  46      26.585  35.611  98.288  1.00 90.19           C  
ANISOU  970  CG  GLU B  46    10175  12896  11198   3592   -951  -1719       C  
ATOM    971  CD  GLU B  46      26.590  34.149  98.744  1.00 94.26           C  
ANISOU  971  CD  GLU B  46    10906  13111  11798   3918  -1036  -1707       C  
ATOM    972  OE1 GLU B  46      25.946  33.875  99.781  1.00 92.32           O  
ANISOU  972  OE1 GLU B  46    10964  12630  11484   3991  -1142  -1500       O  
ATOM    973  OE2 GLU B  46      27.227  33.277  98.060  1.00 92.72           O  
ANISOU  973  OE2 GLU B  46    10591  12903  11737   4098   -981  -1903       O  
ATOM    974  N   GLY B  47      26.922  38.987 100.752  1.00 82.25           N  
ANISOU  974  N   GLY B  47     8970  12303   9979   3279  -1285  -1432       N  
ATOM    975  CA  GLY B  47      28.026  39.597 101.482  1.00 88.26           C  
ANISOU  975  CA  GLY B  47     9468  13281  10784   3383  -1461  -1525       C  
ATOM    976  C   GLY B  47      28.081  41.105 101.286  1.00 91.40           C  
ANISOU  976  C   GLY B  47     9674  13903  11152   3060  -1369  -1541       C  
ATOM    977  O   GLY B  47      28.500  41.840 102.179  1.00 92.41           O  
ANISOU  977  O   GLY B  47     9698  14149  11265   3059  -1516  -1541       O  
ATOM    978  N   ASP B  48      27.648  41.589 100.128  1.00 91.80           N  
ANISOU  978  N   ASP B  48     9690  14006  11184   2786  -1127  -1556       N  
ATOM    979  CA  ASP B  48      27.582  43.032  99.930  1.00 91.82           C  
ANISOU  979  CA  ASP B  48     9570  14171  11148   2474  -1020  -1536       C  
ATOM    980  C   ASP B  48      26.451  43.680 100.711  1.00 88.64           C  
ANISOU  980  C   ASP B  48     9432  13629  10619   2323  -1067  -1305       C  
ATOM    981  O   ASP B  48      25.594  43.005 101.296  1.00 86.49           O  
ANISOU  981  O   ASP B  48     9455  13129  10277   2423  -1146  -1155       O  
ATOM    982  CB  ASP B  48      27.455  43.383  98.445  1.00 90.96           C  
ANISOU  982  CB  ASP B  48     9380  14153  11026   2240   -749  -1601       C  
ATOM    983  CG  ASP B  48      28.773  43.280  97.714  1.00 93.05           C  
ANISOU  983  CG  ASP B  48     9295  14639  11422   2292   -654  -1863       C  
ATOM    984  OD1 ASP B  48      29.829  43.301  98.387  1.00 91.69           O  
ANISOU  984  OD1 ASP B  48     8875  14594  11368   2450   -797  -2006       O  
ATOM    985  OD2 ASP B  48      28.745  43.182  96.472  1.00 91.57           O  
ANISOU  985  OD2 ASP B  48     9074  14503  11214   2176   -437  -1938       O  
ATOM    986  N   ASN B  49      26.494  45.008 100.720  1.00 83.94           N  
ANISOU  986  N   ASN B  49     8720  13167  10008   2075  -1001  -1293       N  
ATOM    987  CA  ASN B  49      25.445  45.816 101.283  1.00 78.94           C  
ANISOU  987  CA  ASN B  49     8294  12424   9274   1890  -1004  -1101       C  
ATOM    988  C   ASN B  49      24.406  46.211 100.246  1.00 81.60           C  
ANISOU  988  C   ASN B  49     8770  12691   9544   1652   -801   -997       C  
ATOM    989  O   ASN B  49      24.692  46.346  99.047  1.00 79.87           O  
ANISOU  989  O   ASN B  49     8431  12579   9339   1549   -632  -1082       O  
ATOM    990  CB  ASN B  49      26.031  47.060 101.906  1.00 81.90           C  
ANISOU  990  CB  ASN B  49     8478  12960   9680   1759  -1049  -1151       C  
ATOM    991  CG  ASN B  49      26.706  46.770 103.225  1.00 88.40           C  
ANISOU  991  CG  ASN B  49     9246  13823  10519   1991  -1307  -1208       C  
ATOM    992  OD1 ASN B  49      26.599  45.664 103.773  1.00 89.97           O  
ANISOU  992  OD1 ASN B  49     9611  13893  10681   2254  -1455  -1162       O  
ATOM    993  ND2 ASN B  49      27.409  47.756 103.743  1.00 92.50           N  
ANISOU  993  ND2 ASN B  49     9544  14516  11087   1900  -1363  -1313       N  
ATOM    994  N   ALA B  50      23.192  46.403 100.742  1.00 75.72           N  
ANISOU  994  N   ALA B  50     8282  11770   8718   1570   -824   -818       N  
ATOM    995  CA  ALA B  50      22.024  46.632  99.920  1.00 68.59           C  
ANISOU  995  CA  ALA B  50     7543  10771   7750   1392   -685   -712       C  
ATOM    996  C   ALA B  50      21.266  47.779 100.558  1.00 67.43           C  
ANISOU  996  C   ALA B  50     7488  10569   7562   1209   -694   -575       C  
ATOM    997  O   ALA B  50      20.862  47.690 101.744  1.00 66.06           O  
ANISOU  997  O   ALA B  50     7451  10280   7369   1271   -813   -496       O  
ATOM    998  CB  ALA B  50      21.160  45.380  99.887  1.00 67.59           C  
ANISOU  998  CB  ALA B  50     7647  10437   7599   1518   -705   -663       C  
ATOM    999  N   THR B  51      21.089  48.855  99.790  1.00 63.98           N  
ANISOU  999  N   THR B  51     6992  10209   7107    992   -561   -547       N  
ATOM   1000  CA  THR B  51      20.591  50.097 100.343  1.00 65.02           C  
ANISOU 1000  CA  THR B  51     7165  10309   7230    817   -557   -445       C  
ATOM   1001  C   THR B  51      19.450  50.627  99.518  1.00 64.00           C  
ANISOU 1001  C   THR B  51     7173  10099   7043    657   -449   -328       C  
ATOM   1002  O   THR B  51      19.628  51.039  98.389  1.00 58.37           O  
ANISOU 1002  O   THR B  51     6403   9475   6299    556   -322   -341       O  
ATOM   1003  CB  THR B  51      21.705  51.160 100.458  1.00 66.50           C  
ANISOU 1003  CB  THR B  51     7115  10671   7480    709   -517   -535       C  
ATOM   1004  OG1 THR B  51      22.731  50.653 101.307  1.00 66.34           O  
ANISOU 1004  OG1 THR B  51     6950  10738   7516    883   -658   -662       O  
ATOM   1005  CG2 THR B  51      21.175  52.460 101.067  1.00 64.17           C  
ANISOU 1005  CG2 THR B  51     6873  10319   7190    526   -506   -439       C  
ATOM   1006  N   PHE B  52      18.259  50.616 100.105  1.00 65.85           N  
ANISOU 1006  N   PHE B  52     7596  10164   7260    639   -501   -218       N  
ATOM   1007  CA  PHE B  52      17.154  51.303  99.489  1.00 60.57           C  
ANISOU 1007  CA  PHE B  52     7033   9423   6556    494   -431   -115       C  
ATOM   1008  C   PHE B  52      17.074  52.651 100.090  1.00 56.99           C  
ANISOU 1008  C   PHE B  52     6557   8960   6136    351   -420    -49       C  
ATOM   1009  O   PHE B  52      17.603  52.879 101.171  1.00 55.48           O  
ANISOU 1009  O   PHE B  52     6310   8785   5986    371   -487    -82       O  
ATOM   1010  CB  PHE B  52      15.883  50.578  99.758  1.00 61.06           C  
ANISOU 1010  CB  PHE B  52     7278   9309   6611    542   -477    -64       C  
ATOM   1011  CG  PHE B  52      15.851  49.223  99.161  1.00 66.41           C  
ANISOU 1011  CG  PHE B  52     7996   9966   7271    670   -476   -139       C  
ATOM   1012  CD1 PHE B  52      15.498  49.054  97.821  1.00 66.68           C  
ANISOU 1012  CD1 PHE B  52     8036  10048   7251    635   -408   -166       C  
ATOM   1013  CD2 PHE B  52      16.162  48.114  99.925  1.00 64.05           C  
ANISOU 1013  CD2 PHE B  52     7745   9591   7001    833   -543   -184       C  
ATOM   1014  CE1 PHE B  52      15.444  47.796  97.269  1.00 66.27           C  
ANISOU 1014  CE1 PHE B  52     8018   9970   7190    744   -400   -259       C  
ATOM   1015  CE2 PHE B  52      16.096  46.855  99.370  1.00 66.10           C  
ANISOU 1015  CE2 PHE B  52     8053   9800   7263    948   -528   -259       C  
ATOM   1016  CZ  PHE B  52      15.741  46.692  98.048  1.00 63.56           C  
ANISOU 1016  CZ  PHE B  52     7718   9529   6904    897   -453   -308       C  
ATOM   1017  N   THR B  53      16.386  53.534  99.393  1.00 53.97           N  
ANISOU 1017  N   THR B  53     6229   8546   5732    218   -344     38       N  
ATOM   1018  CA  THR B  53      16.063  54.821  99.949  1.00 55.40           C  
ANISOU 1018  CA  THR B  53     6424   8667   5960     83   -327    112       C  
ATOM   1019  C   THR B  53      14.544  54.934 100.029  1.00 53.42           C  
ANISOU 1019  C   THR B  53     6333   8254   5711     63   -358    207       C  
ATOM   1020  O   THR B  53      13.813  54.603  99.096  1.00 53.94           O  
ANISOU 1020  O   THR B  53     6471   8296   5728     82   -348    237       O  
ATOM   1021  CB  THR B  53      16.730  55.939  99.113  1.00 56.69           C  
ANISOU 1021  CB  THR B  53     6499   8923   6117    -59   -195    131       C  
ATOM   1022  OG1 THR B  53      18.144  55.731  99.134  1.00 55.73           O  
ANISOU 1022  OG1 THR B  53     6195   8958   6023    -41   -161      4       O  
ATOM   1023  CG2 THR B  53      16.465  57.286  99.672  1.00 57.01           C  
ANISOU 1023  CG2 THR B  53     6555   8881   6225   -199   -163    198       C  
ATOM   1024  N   CYS B  54      14.077  55.328 101.190  1.00 54.56           N  
ANISOU 1024  N   CYS B  54     6522   8294   5913     32   -402    229       N  
ATOM   1025  CA  CYS B  54      12.676  55.588 101.414  1.00 50.80           C  
ANISOU 1025  CA  CYS B  54     6165   7664   5473     -3   -415    294       C  
ATOM   1026  C   CYS B  54      12.630  57.074 101.590  1.00 50.31           C  
ANISOU 1026  C   CYS B  54     6078   7569   5467   -136   -367    351       C  
ATOM   1027  O   CYS B  54      13.312  57.588 102.459  1.00 52.98           O  
ANISOU 1027  O   CYS B  54     6355   7933   5843   -184   -365    314       O  
ATOM   1028  CB  CYS B  54      12.166  54.883 102.703  1.00 47.10           C  
ANISOU 1028  CB  CYS B  54     5784   7084   5030     55   -472    265       C  
ATOM   1029  SG  CYS B  54      10.453  55.357 103.147  1.00 51.91           S  
ANISOU 1029  SG  CYS B  54     6502   7502   5720    -18   -456    311       S  
ATOM   1030  N   SER B  55      11.839  57.759 100.777  1.00 50.31           N  
ANISOU 1030  N   SER B  55     6129   7511   5475   -185   -336    433       N  
ATOM   1031  CA  SER B  55      11.662  59.204 100.875  1.00 52.77           C  
ANISOU 1031  CA  SER B  55     6447   7750   5855   -301   -283    503       C  
ATOM   1032  C   SER B  55      10.224  59.481 101.234  1.00 56.05           C  
ANISOU 1032  C   SER B  55     6943   8007   6346   -297   -324    538       C  
ATOM   1033  O   SER B  55       9.310  58.983 100.555  1.00 51.79           O  
ANISOU 1033  O   SER B  55     6453   7440   5784   -229   -371    553       O  
ATOM   1034  CB  SER B  55      11.932  59.920  99.526  1.00 55.63           C  
ANISOU 1034  CB  SER B  55     6825   8156   6157   -348   -207    592       C  
ATOM   1035  OG  SER B  55      13.224  59.572  99.048  1.00 66.19           O  
ANISOU 1035  OG  SER B  55     8075   9649   7426   -357   -143    541       O  
ATOM   1036  N   PHE B  56      10.032  60.335 102.240  1.00 56.87           N  
ANISOU 1036  N   PHE B  56     7046   8015   6548   -374   -302    531       N  
ATOM   1037  CA  PHE B  56       8.710  60.642 102.757  1.00 61.45           C  
ANISOU 1037  CA  PHE B  56     7680   8441   7227   -377   -323    535       C  
ATOM   1038  C   PHE B  56       8.724  62.021 103.419  1.00 59.55           C  
ANISOU 1038  C   PHE B  56     7430   8103   7093   -485   -266    549       C  
ATOM   1039  O   PHE B  56       9.311  62.175 104.486  1.00 54.56           O  
ANISOU 1039  O   PHE B  56     6767   7485   6477   -542   -245    479       O  
ATOM   1040  CB  PHE B  56       8.342  59.567 103.804  1.00 62.22           C  
ANISOU 1040  CB  PHE B  56     7807   8511   7322   -333   -354    447       C  
ATOM   1041  CG  PHE B  56       6.997  59.766 104.455  1.00 63.14           C  
ANISOU 1041  CG  PHE B  56     7966   8474   7549   -353   -343    418       C  
ATOM   1042  CD1 PHE B  56       5.830  59.677 103.696  1.00 68.18           C  
ANISOU 1042  CD1 PHE B  56     8609   9050   8247   -311   -374    427       C  
ATOM   1043  CD2 PHE B  56       6.890  60.026 105.824  1.00 72.45           C  
ANISOU 1043  CD2 PHE B  56     9174   9582   8772   -412   -304    361       C  
ATOM   1044  CE1 PHE B  56       4.574  59.870 104.260  1.00 66.26           C  
ANISOU 1044  CE1 PHE B  56     8371   8671   8133   -331   -356    373       C  
ATOM   1045  CE2 PHE B  56       5.630  60.204 106.410  1.00 75.02           C  
ANISOU 1045  CE2 PHE B  56     9530   9765   9208   -441   -267    316       C  
ATOM   1046  CZ  PHE B  56       4.470  60.110 105.618  1.00 68.55           C  
ANISOU 1046  CZ  PHE B  56     8689   8882   8475   -401   -289    316       C  
ATOM   1047  N   SER B  57       8.084  63.022 102.819  1.00 64.50           N  
ANISOU 1047  N   SER B  57     8090   8626   7791   -504   -247    632       N  
ATOM   1048  CA  SER B  57       7.933  64.322 103.514  1.00 70.14           C  
ANISOU 1048  CA  SER B  57     8805   9207   8637   -601   -185    632       C  
ATOM   1049  C   SER B  57       6.459  64.425 103.909  1.00 70.04           C  
ANISOU 1049  C   SER B  57     8821   9051   8742   -557   -221    607       C  
ATOM   1050  O   SER B  57       5.584  64.308 103.070  1.00 75.25           O  
ANISOU 1050  O   SER B  57     9503   9676   9413   -470   -281    657       O  
ATOM   1051  CB  SER B  57       8.415  65.504 102.659  1.00 82.69           C  
ANISOU 1051  CB  SER B  57    10421  10752  10243   -662   -111    743       C  
ATOM   1052  OG  SER B  57       9.079  66.514 103.438  1.00 92.17           O  
ANISOU 1052  OG  SER B  57    11587  11895  11538   -798    -16    698       O  
ATOM   1053  N   ASN B  58       6.211  64.565 105.210  1.00 71.04           N  
ANISOU 1053  N   ASN B  58     8936   9110   8946   -615   -185    508       N  
ATOM   1054  CA  ASN B  58       4.883  64.528 105.783  1.00 69.59           C  
ANISOU 1054  CA  ASN B  58     8760   8802   8880   -593   -187    442       C  
ATOM   1055  C   ASN B  58       4.730  65.459 106.968  1.00 63.27           C  
ANISOU 1055  C   ASN B  58     7957   7887   8196   -691   -107    365       C  
ATOM   1056  O   ASN B  58       5.587  65.569 107.826  1.00 60.51           O  
ANISOU 1056  O   ASN B  58     7607   7589   7795   -771    -68    307       O  
ATOM   1057  CB  ASN B  58       4.555  63.139 106.276  1.00 65.73           C  
ANISOU 1057  CB  ASN B  58     8286   8365   8322   -552   -207    363       C  
ATOM   1058  N   THR B  59       3.556  66.034 107.043  1.00 55.44           N  
ANISOU 1058  N   THR B  59     6954   6747   7363   -672    -93    340       N  
ATOM   1059  CA  THR B  59       3.276  67.072 107.956  1.00 54.60           C  
ANISOU 1059  CA  THR B  59     6841   6507   7396   -754    -11    267       C  
ATOM   1060  C   THR B  59       2.534  66.521 109.181  1.00 51.37           C  
ANISOU 1060  C   THR B  59     6439   6063   7017   -788     48    122       C  
ATOM   1061  O   THR B  59       1.897  67.253 109.922  1.00 51.49           O  
ANISOU 1061  O   THR B  59     6441   5950   7173   -839    124     31       O  
ATOM   1062  CB  THR B  59       2.457  68.135 107.226  1.00 56.40           C  
ANISOU 1062  CB  THR B  59     7055   6577   7796   -696    -26    332       C  
ATOM   1063  OG1 THR B  59       2.240  69.229 108.102  1.00 77.36           O  
ANISOU 1063  OG1 THR B  59     9704   9083  10608   -778     67    252       O  
ATOM   1064  CG2 THR B  59       1.133  67.613 106.794  1.00 57.09           C  
ANISOU 1064  CG2 THR B  59     7100   6629   7964   -580    -97    303       C  
ATOM   1065  N   SER B  60       2.623  65.217 109.375  1.00 46.04           N  
ANISOU 1065  N   SER B  60     5797   5491   6206   -761     27     99       N  
ATOM   1066  CA  SER B  60       1.826  64.524 110.335  1.00 45.03           C  
ANISOU 1066  CA  SER B  60     5703   5317   6089   -786     99    -16       C  
ATOM   1067  C   SER B  60       2.266  64.849 111.761  1.00 46.40           C  
ANISOU 1067  C   SER B  60     5943   5484   6205   -889    187   -106       C  
ATOM   1068  O   SER B  60       3.467  64.948 112.048  1.00 47.39           O  
ANISOU 1068  O   SER B  60     6096   5713   6198   -919    153    -85       O  
ATOM   1069  CB  SER B  60       1.950  63.029 110.106  1.00 49.58           C  
ANISOU 1069  CB  SER B  60     6328   5988   6523   -728     62      3       C  
ATOM   1070  OG  SER B  60       0.800  62.388 110.664  1.00 59.49           O  
ANISOU 1070  OG  SER B  60     7602   7153   7848   -748    151   -100       O  
ATOM   1071  N   GLU B  61       1.289  65.013 112.636  1.00 42.57           N  
ANISOU 1071  N   GLU B  61     5474   4884   5817   -944    299   -224       N  
ATOM   1072  CA  GLU B  61       1.528  65.457 113.983  1.00 43.87           C  
ANISOU 1072  CA  GLU B  61     5707   5029   5931  -1046    393   -329       C  
ATOM   1073  C   GLU B  61       2.313  64.452 114.800  1.00 43.07           C  
ANISOU 1073  C   GLU B  61     5742   5049   5573  -1051    383   -330       C  
ATOM   1074  O   GLU B  61       3.146  64.862 115.646  1.00 43.03           O  
ANISOU 1074  O   GLU B  61     5787   5109   5453  -1107    377   -379       O  
ATOM   1075  CB  GLU B  61       0.199  65.735 114.676  1.00 47.92           C  
ANISOU 1075  CB  GLU B  61     6210   5393   6604  -1101    538   -467       C  
ATOM   1076  CG  GLU B  61      -0.536  66.860 113.973  1.00 50.31           C  
ANISOU 1076  CG  GLU B  61     6376   5567   7173  -1072    531   -477       C  
ATOM   1077  CD  GLU B  61      -1.918  67.157 114.512  1.00 55.52           C  
ANISOU 1077  CD  GLU B  61     6978   6079   8039  -1105    666   -634       C  
ATOM   1078  OE1 GLU B  61      -2.358  66.585 115.577  1.00 50.70           O  
ANISOU 1078  OE1 GLU B  61     6444   5452   7366  -1185    810   -753       O  
ATOM   1079  OE2 GLU B  61      -2.556  67.991 113.822  1.00 59.92           O  
ANISOU 1079  OE2 GLU B  61     7414   6530   8822  -1041    628   -634       O  
ATOM   1080  N   SER B  62       2.072  63.159 114.562  1.00 36.66           N  
ANISOU 1080  N   SER B  62     4993   4263   4672   -988    372   -285       N  
ATOM   1081  CA  SER B  62       2.820  62.132 115.273  1.00 38.36           C  
ANISOU 1081  CA  SER B  62     5362   4572   4640   -960    349   -262       C  
ATOM   1082  C   SER B  62       2.880  60.903 114.413  1.00 35.27           C  
ANISOU 1082  C   SER B  62     4986   4220   4196   -860    286   -172       C  
ATOM   1083  O   SER B  62       1.841  60.379 114.065  1.00 34.25           O  
ANISOU 1083  O   SER B  62     4845   3996   4172   -859    356   -193       O  
ATOM   1084  CB  SER B  62       2.115  61.802 116.644  1.00 39.76           C  
ANISOU 1084  CB  SER B  62     5704   4662   4742  -1035    511   -361       C  
ATOM   1085  OG  SER B  62       2.875  60.837 117.354  1.00 42.04           O  
ANISOU 1085  OG  SER B  62     6178   5032   4763   -985    474   -317       O  
ATOM   1086  N   PHE B  63       4.066  60.432 114.052  1.00 34.18           N  
ANISOU 1086  N   PHE B  63     4856   4219   3913   -778    158    -92       N  
ATOM   1087  CA  PHE B  63       4.127  59.351 113.122  1.00 33.60           C  
ANISOU 1087  CA  PHE B  63     4778   4175   3812   -682    102    -20       C  
ATOM   1088  C   PHE B  63       5.405  58.593 113.275  1.00 35.17           C  
ANISOU 1088  C   PHE B  63     5046   4505   3811   -588     -5     33       C  
ATOM   1089  O   PHE B  63       6.299  59.064 113.934  1.00 38.89           O  
ANISOU 1089  O   PHE B  63     5525   5067   4184   -596    -61     12       O  
ATOM   1090  CB  PHE B  63       3.986  59.909 111.684  1.00 36.19           C  
ANISOU 1090  CB  PHE B  63     4937   4525   4290   -660     37     25       C  
ATOM   1091  CG  PHE B  63       5.200  60.599 111.193  1.00 33.92           C  
ANISOU 1091  CG  PHE B  63     4562   4362   3963   -647    -58     76       C  
ATOM   1092  CD1 PHE B  63       6.205  59.897 110.606  1.00 40.44           C  
ANISOU 1092  CD1 PHE B  63     5374   5318   4673   -563   -148    132       C  
ATOM   1093  CD2 PHE B  63       5.373  61.930 111.398  1.00 40.06           C  
ANISOU 1093  CD2 PHE B  63     5275   5121   4827   -728    -38     51       C  
ATOM   1094  CE1 PHE B  63       7.377  60.519 110.196  1.00 39.72           C  
ANISOU 1094  CE1 PHE B  63     5189   5348   4556   -569   -210    156       C  
ATOM   1095  CE2 PHE B  63       6.514  62.583 110.959  1.00 39.78           C  
ANISOU 1095  CE2 PHE B  63     5157   5187   4771   -742    -95     84       C  
ATOM   1096  CZ  PHE B  63       7.517  61.872 110.362  1.00 37.19           C  
ANISOU 1096  CZ  PHE B  63     4801   5000   4328   -668   -176    132       C  
ATOM   1097  N   VAL B  64       5.487  57.400 112.667  1.00 34.67           N  
ANISOU 1097  N   VAL B  64     5022   4453   3699   -494    -37     85       N  
ATOM   1098  CA  VAL B  64       6.693  56.567 112.683  1.00 32.99           C  
ANISOU 1098  CA  VAL B  64     4860   4356   3318   -372   -148    132       C  
ATOM   1099  C   VAL B  64       6.876  56.045 111.285  1.00 33.23           C  
ANISOU 1099  C   VAL B  64     4785   4436   3403   -300   -204    174       C  
ATOM   1100  O   VAL B  64       5.923  56.034 110.518  1.00 33.62           O  
ANISOU 1100  O   VAL B  64     4781   4411   3581   -335   -152    167       O  
ATOM   1101  CB  VAL B  64       6.619  55.365 113.662  1.00 35.96           C  
ANISOU 1101  CB  VAL B  64     5472   4657   3535   -307   -109    150       C  
ATOM   1102  CG1 VAL B  64       6.619  55.810 115.168  1.00 37.06           C  
ANISOU 1102  CG1 VAL B  64     5758   4775   3549   -361    -66    111       C  
ATOM   1103  CG2 VAL B  64       5.421  54.439 113.349  1.00 36.78           C  
ANISOU 1103  CG2 VAL B  64     5659   4594   3722   -329     23    148       C  
ATOM   1104  N   LEU B  65       8.091  55.640 110.931  1.00 34.38           N  
ANISOU 1104  N   LEU B  65     4889   4720   3455   -198   -314    201       N  
ATOM   1105  CA  LEU B  65       8.332  55.084 109.623  1.00 36.69           C  
ANISOU 1105  CA  LEU B  65     5094   5069   3778   -128   -354    228       C  
ATOM   1106  C   LEU B  65       8.888  53.687 109.766  1.00 38.57           C  
ANISOU 1106  C   LEU B  65     5438   5314   3902     13   -398    243       C  
ATOM   1107  O   LEU B  65       9.901  53.480 110.430  1.00 42.01           O  
ANISOU 1107  O   LEU B  65     5906   5833   4221     99   -482    242       O  
ATOM   1108  CB  LEU B  65       9.322  55.958 108.871  1.00 40.32           C  
ANISOU 1108  CB  LEU B  65     5378   5685   4258   -142   -418    233       C  
ATOM   1109  CG  LEU B  65       9.617  55.645 107.394  1.00 44.65           C  
ANISOU 1109  CG  LEU B  65     5825   6313   4827    -94   -442    257       C  
ATOM   1110  CD1 LEU B  65       8.423  55.863 106.461  1.00 45.62           C  
ANISOU 1110  CD1 LEU B  65     5930   6352   5050   -143   -394    277       C  
ATOM   1111  CD2 LEU B  65      10.792  56.490 106.910  1.00 47.35           C  
ANISOU 1111  CD2 LEU B  65     6018   6808   5166   -123   -474    255       C  
ATOM   1112  N   ASN B  66       8.248  52.721 109.135  1.00 38.64           N  
ANISOU 1112  N   ASN B  66     5495   5235   3950     47   -351    244       N  
ATOM   1113  CA  ASN B  66       8.632  51.329 109.311  1.00 41.70           C  
ANISOU 1113  CA  ASN B  66     6016   5579   4250    181   -368    258       C  
ATOM   1114  C   ASN B  66       9.171  50.703 108.007  1.00 45.77           C  
ANISOU 1114  C   ASN B  66     6422   6182   4786    271   -420    243       C  
ATOM   1115  O   ASN B  66       8.744  51.069 106.878  1.00 45.44           O  
ANISOU 1115  O   ASN B  66     6253   6180   4831    211   -404    221       O  
ATOM   1116  CB  ASN B  66       7.433  50.523 109.835  1.00 42.28           C  
ANISOU 1116  CB  ASN B  66     6276   5437   4351    138   -233    252       C  
ATOM   1117  CG  ASN B  66       7.200  50.673 111.352  1.00 43.25           C  
ANISOU 1117  CG  ASN B  66     6588   5465   4379    101   -172    275       C  
ATOM   1118  OD1 ASN B  66       7.836  51.468 112.018  1.00 41.18           O  
ANISOU 1118  OD1 ASN B  66     6306   5304   4037    100   -244    284       O  
ATOM   1119  ND2 ASN B  66       6.219  49.923 111.877  1.00 42.54           N  
ANISOU 1119  ND2 ASN B  66     6685   5175   4302     52    -21    270       N  
ATOM   1120  N   TRP B  67      10.113  49.776 108.160  1.00 43.30           N  
ANISOU 1120  N   TRP B  67     6165   5902   4386    425   -486    251       N  
ATOM   1121  CA  TRP B  67      10.610  49.004 107.024  1.00 48.49           C  
ANISOU 1121  CA  TRP B  67     6742   6621   5062    521   -515    218       C  
ATOM   1122  C   TRP B  67      10.062  47.572 107.116  1.00 47.64           C  
ANISOU 1122  C   TRP B  67     6817   6325   4960    594   -448    212       C  
ATOM   1123  O   TRP B  67      10.264  46.901 108.160  1.00 48.72           O  
ANISOU 1123  O   TRP B  67     7145   6352   5014    688   -452    257       O  
ATOM   1124  CB  TRP B  67      12.124  48.991 107.063  1.00 51.77           C  
ANISOU 1124  CB  TRP B  67     7056   7207   5407    653   -634    204       C  
ATOM   1125  CG  TRP B  67      12.790  48.322 105.930  1.00 55.50           C  
ANISOU 1125  CG  TRP B  67     7420   7768   5899    751   -656    151       C  
ATOM   1126  CD1 TRP B  67      12.235  47.915 104.731  1.00 63.21           C  
ANISOU 1126  CD1 TRP B  67     8361   8722   6933    717   -590    114       C  
ATOM   1127  CD2 TRP B  67      14.177  48.043 105.838  1.00 60.17           C  
ANISOU 1127  CD2 TRP B  67     7901   8508   6455    898   -752    106       C  
ATOM   1128  NE1 TRP B  67      13.209  47.383 103.918  1.00 60.21           N  
ANISOU 1128  NE1 TRP B  67     7873   8461   6543    829   -624     53       N  
ATOM   1129  CE2 TRP B  67      14.408  47.448 104.583  1.00 60.45           C  
ANISOU 1129  CE2 TRP B  67     7845   8593   6528    942   -718     45       C  
ATOM   1130  CE3 TRP B  67      15.266  48.244 106.709  1.00 64.36           C  
ANISOU 1130  CE3 TRP B  67     8383   9145   6927   1001   -872     91       C  
ATOM   1131  CZ2 TRP B  67      15.677  47.020 104.192  1.00 66.55           C  
ANISOU 1131  CZ2 TRP B  67     8484   9505   7297   1085   -780    -29       C  
ATOM   1132  CZ3 TRP B  67      16.515  47.837 106.317  1.00 60.68           C  
ANISOU 1132  CZ3 TRP B  67     7766   8825   6466   1149   -952     12       C  
ATOM   1133  CH2 TRP B  67      16.716  47.226 105.068  1.00 65.38           C  
ANISOU 1133  CH2 TRP B  67     8271   9455   7114   1188   -896    -47       C  
ATOM   1134  N   TYR B  68       9.364  47.141 106.056  1.00 42.78           N  
ANISOU 1134  N   TYR B  68     6155   5667   4433    549   -386    154       N  
ATOM   1135  CA  TYR B  68       8.704  45.829 105.967  1.00 45.19           C  
ANISOU 1135  CA  TYR B  68     6607   5779   4783    578   -294    115       C  
ATOM   1136  C   TYR B  68       9.319  44.980 104.858  1.00 49.79           C  
ANISOU 1136  C   TYR B  68     7117   6423   5377    690   -328     49       C  
ATOM   1137  O   TYR B  68       9.836  45.510 103.883  1.00 51.89           O  
ANISOU 1137  O   TYR B  68     7200   6878   5636    690   -388     16       O  
ATOM   1138  CB  TYR B  68       7.194  45.948 105.724  1.00 43.95           C  
ANISOU 1138  CB  TYR B  68     6450   5501   4746    413   -179     55       C  
ATOM   1139  CG  TYR B  68       6.456  46.437 106.942  1.00 43.30           C  
ANISOU 1139  CG  TYR B  68     6484   5298   4670    309    -97     96       C  
ATOM   1140  CD1 TYR B  68       6.139  45.582 107.987  1.00 47.20           C  
ANISOU 1140  CD1 TYR B  68     7221   5582   5132    320     15    128       C  
ATOM   1141  CD2 TYR B  68       6.098  47.770 107.066  1.00 42.71           C  
ANISOU 1141  CD2 TYR B  68     6293   5308   4627    199   -116    106       C  
ATOM   1142  CE1 TYR B  68       5.494  46.048 109.137  1.00 46.27           C  
ANISOU 1142  CE1 TYR B  68     7224   5360   4996    216    112    160       C  
ATOM   1143  CE2 TYR B  68       5.443  48.237 108.180  1.00 41.61           C  
ANISOU 1143  CE2 TYR B  68     6252   5064   4495    102    -29    124       C  
ATOM   1144  CZ  TYR B  68       5.160  47.389 109.224  1.00 43.85           C  
ANISOU 1144  CZ  TYR B  68     6772   5159   4729    107     86    148       C  
ATOM   1145  OH  TYR B  68       4.549  47.911 110.347  1.00 42.32           O  
ANISOU 1145  OH  TYR B  68     6684   4875   4521      2    188    161       O  
ATOM   1146  N   ARG B  69       9.340  43.669 105.095  1.00 53.34           N  
ANISOU 1146  N   ARG B  69     7732   6703   5834    791   -278     35       N  
ATOM   1147  CA  ARG B  69       9.612  42.651 104.106  1.00 58.18           C  
ANISOU 1147  CA  ARG B  69     8315   7304   6489    879   -267    -56       C  
ATOM   1148  C   ARG B  69       8.352  41.811 104.080  1.00 58.17           C  
ANISOU 1148  C   ARG B  69     8446   7066   6591    783   -120   -123       C  
ATOM   1149  O   ARG B  69       7.733  41.649 105.123  1.00 52.75           O  
ANISOU 1149  O   ARG B  69     7941   6192   5911    729    -30    -66       O  
ATOM   1150  CB  ARG B  69      10.785  41.757 104.519  1.00 66.62           C  
ANISOU 1150  CB  ARG B  69     9478   8337   7497   1102   -329    -23       C  
ATOM   1151  N   MET B  70       7.955  41.319 102.905  1.00 56.57           N  
ANISOU 1151  N   MET B  70     8150   6877   6468    748    -88   -258       N  
ATOM   1152  CA  MET B  70       6.738  40.524 102.803  1.00 63.26           C  
ANISOU 1152  CA  MET B  70     9086   7510   7441    638     54   -364       C  
ATOM   1153  C   MET B  70       7.062  39.072 103.158  1.00 68.24           C  
ANISOU 1153  C   MET B  70     9927   7905   8096    757    141   -372       C  
ATOM   1154  O   MET B  70       8.160  38.567 102.905  1.00 67.18           O  
ANISOU 1154  O   MET B  70     9797   7820   7910    936     69   -359       O  
ATOM   1155  CB  MET B  70       6.099  40.588 101.415  1.00 64.55           C  
ANISOU 1155  CB  MET B  70     9062   7787   7676    548     41   -531       C  
ATOM   1156  CG  MET B  70       5.711  41.981 100.905  1.00 63.30           C  
ANISOU 1156  CG  MET B  70     8713   7844   7492    451    -53   -521       C  
ATOM   1157  SD  MET B  70       4.942  43.027 102.160  1.00 73.92           S  
ANISOU 1157  SD  MET B  70    10102   9115   8868    326    -13   -415       S  
ATOM   1158  CE  MET B  70       3.334  42.271 102.314  1.00 68.83           C  
ANISOU 1158  CE  MET B  70     9509   8233   8410    171    152   -574       C  
ATOM   1159  N   SER B  71       6.105  38.410 103.786  1.00 68.82           N  
ANISOU 1159  N   SER B  71    10183   7707   8259    659    308   -393       N  
ATOM   1160  CA  SER B  71       6.355  37.080 104.288  1.00 71.71           C  
ANISOU 1160  CA  SER B  71    10805   7799   8644    768    415   -367       C  
ATOM   1161  C   SER B  71       6.279  36.186 103.082  1.00 74.33           C  
ANISOU 1161  C   SER B  71    11050   8105   9087    779    449   -554       C  
ATOM   1162  O   SER B  71       5.912  36.647 101.999  1.00 71.89           O  
ANISOU 1162  O   SER B  71    10505   7989   8820    686    394   -693       O  
ATOM   1163  CB  SER B  71       5.353  36.679 105.407  1.00 70.83           C  
ANISOU 1163  CB  SER B  71    10948   7381   8582    637    624   -321       C  
ATOM   1164  OG  SER B  71       4.055  36.354 104.930  1.00 68.76           O  
ANISOU 1164  OG  SER B  71    10626   6997   8503    426    787   -505       O  
ATOM   1165  N   PRO B  72       6.665  34.918 103.241  1.00 81.35           N  
ANISOU 1165  N   PRO B  72    12137   8760  10014    905    530   -559       N  
ATOM   1166  CA  PRO B  72       6.317  33.969 102.197  1.00 85.51           C  
ANISOU 1166  CA  PRO B  72    12610   9199  10680    868    615   -772       C  
ATOM   1167  C   PRO B  72       4.822  33.982 101.825  1.00 85.72           C  
ANISOU 1167  C   PRO B  72    12554   9153  10861    605    752   -953       C  
ATOM   1168  O   PRO B  72       4.473  33.589 100.738  1.00 86.50           O  
ANISOU 1168  O   PRO B  72    12509   9301  11055    545    762  -1166       O  
ATOM   1169  CB  PRO B  72       6.793  32.652 102.791  1.00 86.54           C  
ANISOU 1169  CB  PRO B  72    13036   9006  10840   1028    720   -710       C  
ATOM   1170  CG  PRO B  72       8.077  33.060 103.460  1.00 86.48           C  
ANISOU 1170  CG  PRO B  72    13077   9120  10659   1264    546   -505       C  
ATOM   1171  CD  PRO B  72       7.760  34.405 104.088  1.00 83.40           C  
ANISOU 1171  CD  PRO B  72    12611   8909  10167   1146    478   -390       C  
ATOM   1172  N   SER B  73       3.951  34.443 102.715  1.00 89.37           N  
ANISOU 1172  N   SER B  73    13094   9512  11350    450    852   -889       N  
ATOM   1173  CA  SER B  73       2.618  34.900 102.306  1.00 85.99           C  
ANISOU 1173  CA  SER B  73    12484   9131  11056    213    914  -1065       C  
ATOM   1174  C   SER B  73       2.722  36.405 102.109  1.00 84.60           C  
ANISOU 1174  C   SER B  73    12089   9284  10773    205    722   -992       C  
ATOM   1175  O   SER B  73       3.777  36.999 102.322  1.00 79.34           O  
ANISOU 1175  O   SER B  73    11422   8778   9946    353    578   -822       O  
ATOM   1176  CB  SER B  73       1.564  34.585 103.377  1.00 87.91           C  
ANISOU 1176  CB  SER B  73    12916   9073  11413     36   1159  -1061       C  
ATOM   1177  OG  SER B  73       0.453  35.471 103.318  1.00 80.86           O  
ANISOU 1177  OG  SER B  73    11824   8288  10611   -160   1171  -1167       O  
ATOM   1178  N   ASN B  74       1.622  37.040 101.737  1.00 81.85           N  
ANISOU 1178  N   ASN B  74    11552   9024  10524     34    722  -1126       N  
ATOM   1179  CA  ASN B  74       1.618  38.480 101.663  1.00 76.85           C  
ANISOU 1179  CA  ASN B  74    10745   8649   9805     23    564  -1043       C  
ATOM   1180  C   ASN B  74       1.381  39.129 103.033  1.00 66.89           C  
ANISOU 1180  C   ASN B  74     9607   7291   8516    -36    641   -883       C  
ATOM   1181  O   ASN B  74       0.504  40.004 103.170  1.00 68.62           O  
ANISOU 1181  O   ASN B  74     9697   7569   8805   -163    642   -926       O  
ATOM   1182  CB  ASN B  74       0.589  38.960 100.630  1.00 84.13           C  
ANISOU 1182  CB  ASN B  74    11407   9726  10832    -95    493  -1248       C  
ATOM   1183  CG  ASN B  74       1.235  39.591  99.407  1.00 89.32           C  
ANISOU 1183  CG  ASN B  74    11888  10694  11356     12    275  -1249       C  
ATOM   1184  OD1 ASN B  74       2.417  39.353  99.101  1.00 93.18           O  
ANISOU 1184  OD1 ASN B  74    12424  11264  11714    157    211  -1165       O  
ATOM   1185  ND2 ASN B  74       0.452  40.399  98.686  1.00 92.23           N  
ANISOU 1185  ND2 ASN B  74    12052  11234  11755    -55    163  -1349       N  
ATOM   1186  N   GLN B  75       2.178  38.759 104.036  1.00 59.04           N  
ANISOU 1186  N   GLN B  75     8858   6165   7411     70    689   -703       N  
ATOM   1187  CA  GLN B  75       2.039  39.418 105.359  1.00 55.79           C  
ANISOU 1187  CA  GLN B  75     8580   5687   6931     24    749   -551       C  
ATOM   1188  C   GLN B  75       3.176  40.420 105.574  1.00 52.37           C  
ANISOU 1188  C   GLN B  75     8096   5487   6313    163    549   -379       C  
ATOM   1189  O   GLN B  75       4.350  40.140 105.321  1.00 54.46           O  
ANISOU 1189  O   GLN B  75     8382   5838   6471    341    430   -308       O  
ATOM   1190  CB  GLN B  75       1.893  38.394 106.520  1.00 55.24           C  
ANISOU 1190  CB  GLN B  75     8853   5283   6855     11    968   -475       C  
ATOM   1191  CG  GLN B  75       1.293  38.891 107.843  1.00 54.36           C  
ANISOU 1191  CG  GLN B  75     8896   5049   6708   -109   1113   -386       C  
ATOM   1192  CD  GLN B  75      -0.060  39.615 107.706  1.00 59.60           C  
ANISOU 1192  CD  GLN B  75     9353   5745   7548   -337   1205   -549       C  
ATOM   1193  OE1 GLN B  75      -0.128  40.830 107.388  1.00 55.95           O  
ANISOU 1193  OE1 GLN B  75     8658   5521   7081   -351   1051   -557       O  
ATOM   1194  NE2 GLN B  75      -1.143  38.889 107.966  1.00 61.14           N  
ANISOU 1194  NE2 GLN B  75     9630   5691   7911   -514   1463   -685       N  
ATOM   1195  N   THR B  76       2.819  41.602 106.050  1.00 54.50           N  
ANISOU 1195  N   THR B  76     8288   5855   6566     77    521   -332       N  
ATOM   1196  CA  THR B  76       3.813  42.634 106.357  1.00 54.38           C  
ANISOU 1196  CA  THR B  76     8221   6042   6397    174    356   -189       C  
ATOM   1197  C   THR B  76       4.523  42.365 107.664  1.00 56.99           C  
ANISOU 1197  C   THR B  76     8808   6269   6578    274    377    -34       C  
ATOM   1198  O   THR B  76       3.951  42.653 108.716  1.00 57.93           O  
ANISOU 1198  O   THR B  76     9061   6273   6677    178    490     10       O  
ATOM   1199  CB  THR B  76       3.151  44.025 106.485  1.00 53.03           C  
ANISOU 1199  CB  THR B  76     7892   5985   6270     45    330   -199       C  
ATOM   1200  OG1 THR B  76       1.966  43.950 107.304  1.00 51.65           O  
ANISOU 1200  OG1 THR B  76     7812   5615   6196   -112    519   -252       O  
ATOM   1201  CG2 THR B  76       2.759  44.505 105.146  1.00 56.82           C  
ANISOU 1201  CG2 THR B  76     8120   6628   6841      9    234   -311       C  
ATOM   1202  N   ASP B  77       5.780  41.920 107.570  1.00 53.01           N  
ANISOU 1202  N   ASP B  77     8350   5832   5961    470    254     40       N  
ATOM   1203  CA  ASP B  77       6.656  41.704 108.704  1.00 53.40           C  
ANISOU 1203  CA  ASP B  77     8616   5833   5842    619    206    185       C  
ATOM   1204  C   ASP B  77       7.672  42.811 108.942  1.00 50.86           C  
ANISOU 1204  C   ASP B  77     8157   5767   5399    697     14    253       C  
ATOM   1205  O   ASP B  77       8.521  43.067 108.125  1.00 53.01           O  
ANISOU 1205  O   ASP B  77     8234   6238   5671    784   -123    222       O  
ATOM   1206  CB  ASP B  77       7.411  40.390 108.523  1.00 61.90           C  
ANISOU 1206  CB  ASP B  77     9834   6795   6890    816    186    206       C  
ATOM   1207  CG  ASP B  77       6.481  39.199 108.567  1.00 71.46           C  
ANISOU 1207  CG  ASP B  77    11249   7694   8209    741    404    155       C  
ATOM   1208  OD1 ASP B  77       5.453  39.286 109.286  1.00 78.99           O  
ANISOU 1208  OD1 ASP B  77    12339   8483   9193    574    581    161       O  
ATOM   1209  OD2 ASP B  77       6.740  38.215 107.847  1.00 77.18           O  
ANISOU 1209  OD2 ASP B  77    11981   8339   9003    831    417     89       O  
ATOM   1210  N   LYS B  78       7.584  43.449 110.101  1.00 48.63           N  
ANISOU 1210  N   LYS B  78     7989   5474   5015    656     23    332       N  
ATOM   1211  CA  LYS B  78       8.380  44.589 110.414  1.00 47.26           C  
ANISOU 1211  CA  LYS B  78     7681   5526   4749    686   -134    366       C  
ATOM   1212  C   LYS B  78       9.820  44.169 110.603  1.00 51.20           C  
ANISOU 1212  C   LYS B  78     8203   6128   5123    924   -309    417       C  
ATOM   1213  O   LYS B  78      10.082  43.211 111.299  1.00 58.55           O  
ANISOU 1213  O   LYS B  78     9384   6908   5956   1067   -305    490       O  
ATOM   1214  CB  LYS B  78       7.850  45.241 111.705  1.00 48.80           C  
ANISOU 1214  CB  LYS B  78     8026   5656   4858    582    -62    417       C  
ATOM   1215  CG  LYS B  78       8.565  46.530 112.119  1.00 45.82           C  
ANISOU 1215  CG  LYS B  78     7508   5501   4400    580   -207    428       C  
ATOM   1216  CD  LYS B  78       8.440  46.831 113.595  1.00 45.33           C  
ANISOU 1216  CD  LYS B  78     7666   5378   4178    558   -174    487       C  
ATOM   1217  CE  LYS B  78       7.939  48.197 113.829  1.00 44.38           C  
ANISOU 1217  CE  LYS B  78     7409   5341   4112    380   -141    434       C  
ATOM   1218  NZ  LYS B  78       7.649  48.544 115.226  1.00 46.82           N  
ANISOU 1218  NZ  LYS B  78     7928   5587   4276    326    -75    464       N  
ATOM   1219  N   LEU B  79      10.741  44.894 109.975  1.00 53.65           N  
ANISOU 1219  N   LEU B  79     8252   6688   5444    966   -457    374       N  
ATOM   1220  CA  LEU B  79      12.198  44.714 110.115  1.00 53.83           C  
ANISOU 1220  CA  LEU B  79     8215   6863   5377   1182   -642    382       C  
ATOM   1221  C   LEU B  79      12.902  45.771 110.967  1.00 57.50           C  
ANISOU 1221  C   LEU B  79     8606   7505   5735   1189   -775    393       C  
ATOM   1222  O   LEU B  79      13.973  45.508 111.509  1.00 56.57           O  
ANISOU 1222  O   LEU B  79     8507   7474   5512   1383   -934    402       O  
ATOM   1223  CB  LEU B  79      12.878  44.837 108.756  1.00 50.93           C  
ANISOU 1223  CB  LEU B  79     7564   6680   5108   1209   -699    289       C  
ATOM   1224  CG  LEU B  79      12.418  43.908 107.633  1.00 54.06           C  
ANISOU 1224  CG  LEU B  79     7954   6974   5613   1208   -601    232       C  
ATOM   1225  CD1 LEU B  79      13.075  44.365 106.330  1.00 50.03           C  
ANISOU 1225  CD1 LEU B  79     7155   6690   5164   1196   -648    141       C  
ATOM   1226  CD2 LEU B  79      12.701  42.427 107.922  1.00 52.69           C  
ANISOU 1226  CD2 LEU B  79     7992   6614   5414   1409   -597    258       C  
ATOM   1227  N   ALA B  80      12.367  46.989 110.964  1.00 54.53           N  
ANISOU 1227  N   ALA B  80     8114   7200   5406    987   -723    369       N  
ATOM   1228  CA  ALA B  80      12.991  48.121 111.612  1.00 53.05           C  
ANISOU 1228  CA  ALA B  80     7817   7185   5153    954   -829    346       C  
ATOM   1229  C   ALA B  80      12.071  49.356 111.539  1.00 53.88           C  
ANISOU 1229  C   ALA B  80     7837   7288   5345    712   -720    327       C  
ATOM   1230  O   ALA B  80      11.007  49.349 110.882  1.00 52.73           O  
ANISOU 1230  O   ALA B  80     7686   7034   5316    588   -585    324       O  
ATOM   1231  CB  ALA B  80      14.336  48.437 110.994  1.00 51.35           C  
ANISOU 1231  CB  ALA B  80     7334   7207   4967   1047   -974    270       C  
ATOM   1232  N   ALA B  81      12.481  50.397 112.255  1.00 52.41           N  
ANISOU 1232  N   ALA B  81     7586   7219   5107    658   -786    298       N  
ATOM   1233  CA  ALA B  81      11.694  51.574 112.386  1.00 53.97           C  
ANISOU 1233  CA  ALA B  81     7729   7397   5380    454   -691    277       C  
ATOM   1234  C   ALA B  81      12.581  52.771 112.594  1.00 55.26           C  
ANISOU 1234  C   ALA B  81     7701   7750   5543    406   -788    209       C  
ATOM   1235  O   ALA B  81      13.716  52.655 113.035  1.00 54.66           O  
ANISOU 1235  O   ALA B  81     7581   7814   5374    530   -936    169       O  
ATOM   1236  CB  ALA B  81      10.708  51.446 113.536  1.00 50.76           C  
ANISOU 1236  CB  ALA B  81     7574   6816   4895    391   -584    313       C  
ATOM   1237  N   PHE B  82      12.035  53.920 112.210  1.00 50.24           N  
ANISOU 1237  N   PHE B  82     6944   7112   5033    226   -703    184       N  
ATOM   1238  CA  PHE B  82      12.576  55.157 112.570  1.00 48.67           C  
ANISOU 1238  CA  PHE B  82     6609   7029   4854    132   -742    115       C  
ATOM   1239  C   PHE B  82      11.479  55.930 113.257  1.00 49.24           C  
ANISOU 1239  C   PHE B  82     6776   6971   4961    -19   -627    111       C  
ATOM   1240  O   PHE B  82      10.438  56.241 112.635  1.00 46.84           O  
ANISOU 1240  O   PHE B  82     6455   6552   4791   -121   -509    138       O  
ATOM   1241  CB  PHE B  82      13.038  55.927 111.372  1.00 50.69           C  
ANISOU 1241  CB  PHE B  82     6626   7387   5247     55   -727     90       C  
ATOM   1242  CG  PHE B  82      13.670  57.220 111.727  1.00 51.30           C  
ANISOU 1242  CG  PHE B  82     6557   7567   5366    -58   -747      5       C  
ATOM   1243  CD1 PHE B  82      15.011  57.259 112.214  1.00 52.17           C  
ANISOU 1243  CD1 PHE B  82     6553   7860   5410     13   -881    -94       C  
ATOM   1244  CD2 PHE B  82      12.936  58.405 111.634  1.00 46.55           C  
ANISOU 1244  CD2 PHE B  82     5927   6878   4883   -231   -638      6       C  
ATOM   1245  CE1 PHE B  82      15.589  58.478 112.557  1.00 51.09           C  
ANISOU 1245  CE1 PHE B  82     6266   7815   5332   -115   -888   -203       C  
ATOM   1246  CE2 PHE B  82      13.514  59.612 112.011  1.00 46.90           C  
ANISOU 1246  CE2 PHE B  82     5848   6992   4980   -349   -639    -84       C  
ATOM   1247  CZ  PHE B  82      14.832  59.650 112.471  1.00 49.09           C  
ANISOU 1247  CZ  PHE B  82     6006   7450   5196   -303   -757   -194       C  
ATOM   1248  N   PRO B  83      11.719  56.266 114.532  1.00 48.08           N  
ANISOU 1248  N   PRO B  83     6719   6854   4696    -28   -670     60       N  
ATOM   1249  CA  PRO B  83      12.876  55.786 115.291  1.00 53.27           C  
ANISOU 1249  CA  PRO B  83     7412   7651   5176    125   -840     25       C  
ATOM   1250  C   PRO B  83      12.573  54.431 115.912  1.00 57.96           C  
ANISOU 1250  C   PRO B  83     8286   8135   5602    277   -850    112       C  
ATOM   1251  O   PRO B  83      11.445  53.905 115.721  1.00 56.38           O  
ANISOU 1251  O   PRO B  83     8230   7747   5444    231   -698    183       O  
ATOM   1252  CB  PRO B  83      13.007  56.815 116.389  1.00 55.33           C  
ANISOU 1252  CB  PRO B  83     7678   7967   5377     27   -861    -72       C  
ATOM   1253  CG  PRO B  83      11.618  57.268 116.637  1.00 51.08           C  
ANISOU 1253  CG  PRO B  83     7256   7244   4909   -128   -674    -49       C  
ATOM   1254  CD  PRO B  83      10.886  57.171 115.322  1.00 47.88           C  
ANISOU 1254  CD  PRO B  83     6760   6737   4696   -179   -565     19       C  
ATOM   1255  N   GLU B  84      13.546  53.889 116.650  1.00 65.22           N  
ANISOU 1255  N   GLU B  84     9281   9162   6338    456  -1023     99       N  
ATOM   1256  CA  GLU B  84      13.303  52.871 117.732  1.00 72.50           C  
ANISOU 1256  CA  GLU B  84    10544   9972   7029    595  -1042    184       C  
ATOM   1257  C   GLU B  84      14.443  51.902 117.751  1.00 72.20           C  
ANISOU 1257  C   GLU B  84    10523  10034   6876    858  -1246    204       C  
ATOM   1258  O   GLU B  84      15.572  52.321 117.592  1.00 76.52           O  
ANISOU 1258  O   GLU B  84    10833  10794   7445    924  -1418    101       O  
ATOM   1259  CB  GLU B  84      11.943  52.135 117.612  1.00 74.73           C  
ANISOU 1259  CB  GLU B  84    11055   9993   7344    529   -822    289       C  
ATOM   1260  CG  GLU B  84      11.876  50.670 118.026  1.00 80.36           C  
ANISOU 1260  CG  GLU B  84    12077  10558   7898    709   -820    406       C  
ATOM   1261  CD  GLU B  84      10.430  50.172 118.240  1.00 84.29           C  
ANISOU 1261  CD  GLU B  84    12820  10789   8419    582   -559    473       C  
ATOM   1262  OE1 GLU B  84      10.047  50.007 119.440  1.00 86.64           O  
ANISOU 1262  OE1 GLU B  84    13412  10987   8520    574   -487    516       O  
ATOM   1263  OE2 GLU B  84       9.676  49.956 117.238  1.00 62.38           O  
ANISOU 1263  OE2 GLU B  84     9943   7907   5850    485   -421    469       O  
ATOM   1264  N   SER B  93      20.293  44.270 114.748  1.00 89.24           N  
ANISOU 1264  N   SER B  93    12501  12310   9095   2703  -2154    255       N  
ATOM   1265  CA  SER B  93      20.166  43.523 113.507  1.00 90.74           C  
ANISOU 1265  CA  SER B  93    12612  12399   9466   2712  -2020    241       C  
ATOM   1266  C   SER B  93      20.922  44.212 112.368  1.00 90.86           C  
ANISOU 1266  C   SER B  93    12176  12671   9677   2615  -2020     58       C  
ATOM   1267  O   SER B  93      21.437  45.341 112.494  1.00 83.68           O  
ANISOU 1267  O   SER B  93    11012  11994   8787   2499  -2089    -54       O  
ATOM   1268  CB  SER B  93      18.686  43.363 113.079  1.00 88.77           C  
ANISOU 1268  CB  SER B  93    12562  11897   9268   2470  -1734    346       C  
ATOM   1269  OG  SER B  93      17.787  43.599 114.144  1.00 88.86           O  
ANISOU 1269  OG  SER B  93    12875  11765   9124   2365  -1663    465       O  
ATOM   1270  N   ARG B  94      20.946  43.523 111.235  1.00 89.59           N  
ANISOU 1270  N   ARG B  94    11931  12452   9659   2645  -1917     22       N  
ATOM   1271  CA  ARG B  94      21.572  44.066 110.030  1.00 93.61           C  
ANISOU 1271  CA  ARG B  94    12052  13175  10339   2539  -1867   -140       C  
ATOM   1272  C   ARG B  94      20.600  44.903 109.163  1.00 84.35           C  
ANISOU 1272  C   ARG B  94    10817  11985   9245   2199  -1636   -123       C  
ATOM   1273  O   ARG B  94      20.975  45.324 108.071  1.00 72.47           O  
ANISOU 1273  O   ARG B  94     9049  10627   7861   2092  -1558   -230       O  
ATOM   1274  CB  ARG B  94      22.264  42.965 109.210  1.00 99.39           C  
ANISOU 1274  CB  ARG B  94    12688  13898  11178   2760  -1888   -222       C  
ATOM   1275  CG  ARG B  94      21.581  41.614 109.249  1.00102.61           C  
ANISOU 1275  CG  ARG B  94    13432  13998  11557   2901  -1821    -99       C  
ATOM   1276  CD  ARG B  94      22.215  40.659 108.266  1.00106.86           C  
ANISOU 1276  CD  ARG B  94    13838  14532  12230   3075  -1806   -209       C  
ATOM   1277  NE  ARG B  94      21.439  39.426 108.239  1.00111.62           N  
ANISOU 1277  NE  ARG B  94    14771  14812  12827   3163  -1703   -100       N  
ATOM   1278  CZ  ARG B  94      20.643  39.047 107.242  1.00104.71           C  
ANISOU 1278  CZ  ARG B  94    13932  13807  12044   3008  -1493   -117       C  
ATOM   1279  NH1 ARG B  94      19.962  37.909 107.314  1.00108.27           N  
ANISOU 1279  NH1 ARG B  94    14685  13950  12502   3083  -1397    -35       N  
ATOM   1280  NH2 ARG B  94      20.534  39.790 106.163  1.00108.25           N  
ANISOU 1280  NH2 ARG B  94    14126  14430  12576   2779  -1377   -220       N  
ATOM   1281  N   PHE B  95      19.387  45.155 109.684  1.00 82.16           N  
ANISOU 1281  N   PHE B  95    10788  11534   8896   2041  -1534      6       N  
ATOM   1282  CA  PHE B  95      18.377  46.033 109.057  1.00 75.40           C  
ANISOU 1282  CA  PHE B  95     9891  10653   8106   1740  -1349     28       C  
ATOM   1283  C   PHE B  95      18.325  47.417 109.742  1.00 73.25           C  
ANISOU 1283  C   PHE B  95     9543  10494   7795   1568  -1374     20       C  
ATOM   1284  O   PHE B  95      17.717  47.606 110.809  1.00 65.77           O  
ANISOU 1284  O   PHE B  95     8806   9442   6743   1533  -1381     99       O  
ATOM   1285  CB  PHE B  95      17.013  45.336 109.093  1.00 74.31           C  
ANISOU 1285  CB  PHE B  95    10044  10238   7953   1678  -1200    140       C  
ATOM   1286  CG  PHE B  95      17.024  43.996 108.425  1.00 73.40           C  
ANISOU 1286  CG  PHE B  95    10007   9991   7890   1826  -1159    131       C  
ATOM   1287  CD1 PHE B  95      16.972  43.906 107.041  1.00 76.35           C  
ANISOU 1287  CD1 PHE B  95    10208  10421   8379   1752  -1063     47       C  
ATOM   1288  CD2 PHE B  95      17.137  42.826 109.171  1.00 81.14           C  
ANISOU 1288  CD2 PHE B  95    11244  10789   8794   2050  -1216    200       C  
ATOM   1289  CE1 PHE B  95      17.024  42.672 106.406  1.00 83.07           C  
ANISOU 1289  CE1 PHE B  95    11121  11158   9285   1886  -1022     11       C  
ATOM   1290  CE2 PHE B  95      17.184  41.579 108.547  1.00 81.47           C  
ANISOU 1290  CE2 PHE B  95    11361  10690   8905   2191  -1170    180       C  
ATOM   1291  CZ  PHE B  95      17.136  41.504 107.166  1.00 86.18           C  
ANISOU 1291  CZ  PHE B  95    11760  11353   9632   2105  -1073     72       C  
ATOM   1292  N   ARG B  96      19.007  48.372 109.117  1.00 73.85           N  
ANISOU 1292  N   ARG B  96     9321  10778   7959   1459  -1372    -87       N  
ATOM   1293  CA  ARG B  96      19.303  49.658 109.734  1.00 71.14           C  
ANISOU 1293  CA  ARG B  96     8855  10570   7607   1324  -1417   -139       C  
ATOM   1294  C   ARG B  96      18.621  50.776 108.951  1.00 70.37           C  
ANISOU 1294  C   ARG B  96     8664  10467   7605   1048  -1244   -125       C  
ATOM   1295  O   ARG B  96      18.811  50.903 107.735  1.00 69.96           O  
ANISOU 1295  O   ARG B  96     8457  10480   7646    981  -1150   -160       O  
ATOM   1296  CB  ARG B  96      20.824  49.862 109.781  1.00 74.05           C  
ANISOU 1296  CB  ARG B  96     8940  11184   8011   1437  -1567   -301       C  
ATOM   1297  CG  ARG B  96      21.578  48.873 110.674  1.00 73.21           C  
ANISOU 1297  CG  ARG B  96     8912  11104   7802   1745  -1788   -325       C  
ATOM   1298  N   VAL B  97      17.793  51.558 109.644  1.00 72.37           N  
ANISOU 1298  N   VAL B  97     9034  10635   7828    898  -1197    -69       N  
ATOM   1299  CA  VAL B  97      17.171  52.753 109.071  1.00 69.04           C  
ANISOU 1299  CA  VAL B  97     8533  10199   7500    656  -1057    -54       C  
ATOM   1300  C   VAL B  97      17.864  54.007 109.554  1.00 67.63           C  
ANISOU 1300  C   VAL B  97     8182  10160   7353    541  -1093   -148       C  
ATOM   1301  O   VAL B  97      17.994  54.210 110.736  1.00 71.04           O  
ANISOU 1301  O   VAL B  97     8679  10607   7706    569  -1188   -179       O  
ATOM   1302  CB  VAL B  97      15.701  52.885 109.477  1.00 66.69           C  
ANISOU 1302  CB  VAL B  97     8456   9697   7186    552   -960     48       C  
ATOM   1303  CG1 VAL B  97      15.099  54.134 108.828  1.00 66.65           C  
ANISOU 1303  CG1 VAL B  97     8359   9676   7292    335   -837     62       C  
ATOM   1304  CG2 VAL B  97      14.924  51.642 109.067  1.00 66.21           C  
ANISOU 1304  CG2 VAL B  97     8566   9479   7112    639   -907    119       C  
ATOM   1305  N   THR B  98      18.187  54.891 108.629  1.00 69.18           N  
ANISOU 1305  N   THR B  98     8185  10438   7661    392   -996   -190       N  
ATOM   1306  CA  THR B  98      19.031  56.056 108.885  1.00 69.06           C  
ANISOU 1306  CA  THR B  98     7965  10562   7712    267  -1003   -309       C  
ATOM   1307  C   THR B  98      18.500  57.278 108.159  1.00 63.56           C  
ANISOU 1307  C   THR B  98     7230   9799   7121     35   -830   -263       C  
ATOM   1308  O   THR B  98      18.459  57.318 106.941  1.00 70.88           O  
ANISOU 1308  O   THR B  98     8109  10726   8097    -14   -719   -218       O  
ATOM   1309  CB  THR B  98      20.445  55.763 108.346  1.00 74.35           C  
ANISOU 1309  CB  THR B  98     8382  11435   8431    349  -1052   -446       C  
ATOM   1310  OG1 THR B  98      20.971  54.643 109.053  1.00 76.90           O  
ANISOU 1310  OG1 THR B  98     8741  11814   8662    597  -1237   -490       O  
ATOM   1311  CG2 THR B  98      21.395  56.956 108.491  1.00 77.76           C  
ANISOU 1311  CG2 THR B  98     8563  12017   8965    194  -1030   -603       C  
ATOM   1312  N   GLN B  99      18.093  58.282 108.893  1.00 60.33           N  
ANISOU 1312  N   GLN B  99     6858   9327   6739   -100   -804   -272       N  
ATOM   1313  CA  GLN B  99      17.696  59.524 108.256  1.00 60.08           C  
ANISOU 1313  CA  GLN B  99     6788   9219   6820   -306   -647   -232       C  
ATOM   1314  C   GLN B  99      18.905  60.227 107.626  1.00 63.51           C  
ANISOU 1314  C   GLN B  99     6983   9796   7351   -414   -576   -341       C  
ATOM   1315  O   GLN B  99      19.946  60.361 108.267  1.00 64.83           O  
ANISOU 1315  O   GLN B  99     6985  10111   7535   -407   -658   -503       O  
ATOM   1316  CB  GLN B  99      17.128  60.425 109.294  1.00 56.53           C  
ANISOU 1316  CB  GLN B  99     6413   8673   6392   -416   -640   -251       C  
ATOM   1317  CG  GLN B  99      16.770  61.789 108.790  1.00 56.57           C  
ANISOU 1317  CG  GLN B  99     6387   8578   6530   -617   -485   -219       C  
ATOM   1318  CD  GLN B  99      15.942  62.511 109.814  1.00 56.08           C  
ANISOU 1318  CD  GLN B  99     6434   8383   6492   -699   -472   -229       C  
ATOM   1319  OE1 GLN B  99      16.309  62.571 110.994  1.00 64.13           O  
ANISOU 1319  OE1 GLN B  99     7442   9467   7458   -690   -562   -347       O  
ATOM   1320  NE2 GLN B  99      14.823  63.039 109.392  1.00 52.52           N  
ANISOU 1320  NE2 GLN B  99     6089   7755   6113   -767   -370   -118       N  
ATOM   1321  N   LEU B 100      18.757  60.696 106.389  1.00 62.07           N  
ANISOU 1321  N   LEU B 100     6786   9570   7228   -519   -420   -261       N  
ATOM   1322  CA  LEU B 100      19.822  61.475 105.720  1.00 64.80           C  
ANISOU 1322  CA  LEU B 100     6932  10019   7672   -664   -292   -352       C  
ATOM   1323  C   LEU B 100      19.795  62.993 106.010  1.00 62.87           C  
ANISOU 1323  C   LEU B 100     6657   9684   7547   -886   -174   -381       C  
ATOM   1324  O   LEU B 100      18.747  63.536 106.365  1.00 56.40           O  
ANISOU 1324  O   LEU B 100     5996   8693   6739   -934   -158   -284       O  
ATOM   1325  CB  LEU B 100      19.757  61.223 104.208  1.00 65.73           C  
ANISOU 1325  CB  LEU B 100     7077  10133   7765   -669   -162   -248       C  
ATOM   1326  CG  LEU B 100      19.905  59.729 103.877  1.00 68.39           C  
ANISOU 1326  CG  LEU B 100     7420  10561   8004   -459   -263   -255       C  
ATOM   1327  CD1 LEU B 100      19.858  59.473 102.380  1.00 66.69           C  
ANISOU 1327  CD1 LEU B 100     7233  10359   7746   -468   -133   -176       C  
ATOM   1328  CD2 LEU B 100      21.188  59.146 104.471  1.00 69.56           C  
ANISOU 1328  CD2 LEU B 100     7358  10901   8172   -355   -375   -448       C  
ATOM   1329  N   PRO B 101      20.948  63.685 105.827  1.00 66.09           N  
ANISOU 1329  N   PRO B 101     6851  10198   8061  -1030    -74   -527       N  
ATOM   1330  CA  PRO B 101      21.039  65.146 106.071  1.00 67.54           C  
ANISOU 1330  CA  PRO B 101     6996  10284   8384  -1262     65   -578       C  
ATOM   1331  C   PRO B 101      19.879  66.018 105.513  1.00 67.72           C  
ANISOU 1331  C   PRO B 101     7238  10055   8436  -1362    207   -370       C  
ATOM   1332  O   PRO B 101      19.452  66.960 106.173  1.00 67.91           O  
ANISOU 1332  O   PRO B 101     7313   9946   8546  -1471    238   -386       O  
ATOM   1333  CB  PRO B 101      22.376  65.526 105.427  1.00 69.82           C  
ANISOU 1333  CB  PRO B 101     7044  10707   8777  -1401    214   -726       C  
ATOM   1334  CG  PRO B 101      23.206  64.282 105.506  1.00 69.82           C  
ANISOU 1334  CG  PRO B 101     6881  10937   8713  -1215     62   -853       C  
ATOM   1335  CD  PRO B 101      22.269  63.105 105.493  1.00 67.68           C  
ANISOU 1335  CD  PRO B 101     6816  10619   8280   -983    -88   -689       C  
ATOM   1336  N   ASN B 102      19.347  65.707 104.332  1.00 67.49           N  
ANISOU 1336  N   ASN B 102     7343   9964   8335  -1310    277   -187       N  
ATOM   1337  CA  ASN B 102      18.217  66.500 103.795  1.00 65.87           C  
ANISOU 1337  CA  ASN B 102     7349   9530   8150  -1364    374     10       C  
ATOM   1338  C   ASN B 102      16.893  66.258 104.546  1.00 65.17           C  
ANISOU 1338  C   ASN B 102     7412   9316   8033  -1252    235     81       C  
ATOM   1339  O   ASN B 102      15.958  67.034 104.390  1.00 64.95           O  
ANISOU 1339  O   ASN B 102     7523   9096   8061  -1294    290    198       O  
ATOM   1340  CB  ASN B 102      18.040  66.285 102.286  1.00 61.87           C  
ANISOU 1340  CB  ASN B 102     6947   9008   7552  -1335    475    175       C  
ATOM   1341  CG  ASN B 102      17.518  64.899 101.953  1.00 64.84           C  
ANISOU 1341  CG  ASN B 102     7386   9465   7784  -1125    329    231       C  
ATOM   1342  OD1 ASN B 102      17.056  64.147 102.856  1.00 61.34           O  
ANISOU 1342  OD1 ASN B 102     6953   9038   7314  -1001    163    185       O  
ATOM   1343  ND2 ASN B 102      17.591  64.529 100.659  1.00 57.76           N  
ANISOU 1343  ND2 ASN B 102     6546   8615   6786  -1091    403    323       N  
ATOM   1344  N   GLY B 103      16.823  65.180 105.339  1.00 64.91           N  
ANISOU 1344  N   GLY B 103     7360   9385   7918  -1107     66      9       N  
ATOM   1345  CA  GLY B 103      15.699  64.930 106.256  1.00 62.84           C  
ANISOU 1345  CA  GLY B 103     7226   9016   7633  -1028    -39     36       C  
ATOM   1346  C   GLY B 103      14.528  64.132 105.666  1.00 62.50           C  
ANISOU 1346  C   GLY B 103     7336   8894   7516   -892    -85    181       C  
ATOM   1347  O   GLY B 103      13.886  63.359 106.354  1.00 56.99           O  
ANISOU 1347  O   GLY B 103     6712   8176   6764   -791   -182    171       O  
ATOM   1348  N   ARG B 104      14.222  64.310 104.394  1.00 58.75           N  
ANISOU 1348  N   ARG B 104     6916   8373   7032   -894    -13    308       N  
ATOM   1349  CA  ARG B 104      13.072  63.627 103.843  1.00 55.37           C  
ANISOU 1349  CA  ARG B 104     6612   7879   6547   -773    -71    414       C  
ATOM   1350  C   ARG B 104      13.470  62.221 103.356  1.00 53.86           C  
ANISOU 1350  C   ARG B 104     6395   7836   6234   -643   -138    392       C  
ATOM   1351  O   ARG B 104      12.596  61.425 103.039  1.00 54.39           O  
ANISOU 1351  O   ARG B 104     6546   7866   6252   -539   -198    438       O  
ATOM   1352  CB  ARG B 104      12.420  64.465 102.723  1.00 60.66           C  
ANISOU 1352  CB  ARG B 104     7377   8427   7244   -805      5    562       C  
ATOM   1353  CG  ARG B 104      13.082  64.325 101.338  1.00 68.06           C  
ANISOU 1353  CG  ARG B 104     8314   9463   8083   -805     76    631       C  
ATOM   1354  CD  ARG B 104      12.565  65.327 100.300  1.00 72.91           C  
ANISOU 1354  CD  ARG B 104     9056   9947   8698   -841    157    793       C  
ATOM   1355  NE  ARG B 104      13.426  66.522 100.188  1.00 88.51           N  
ANISOU 1355  NE  ARG B 104    11012  11873  10746  -1009    325    808       N  
ATOM   1356  CZ  ARG B 104      14.602  66.589  99.546  1.00 93.14           C  
ANISOU 1356  CZ  ARG B 104    11537  12569  11282  -1099    458    788       C  
ATOM   1357  NH1 ARG B 104      15.102  65.526  98.925  1.00102.02           N  
ANISOU 1357  NH1 ARG B 104    12611  13873  12278  -1024    436    752       N  
ATOM   1358  NH2 ARG B 104      15.291  67.733  99.511  1.00 95.93           N  
ANISOU 1358  NH2 ARG B 104    11875  12846  11729  -1275    634    789       N  
ATOM   1359  N   ASP B 105      14.766  61.924 103.272  1.00 50.11           N  
ANISOU 1359  N   ASP B 105     5791   7520   5727   -651   -122    305       N  
ATOM   1360  CA  ASP B 105      15.235  60.610 102.804  1.00 50.05           C  
ANISOU 1360  CA  ASP B 105     5747   7647   5622   -519   -178    268       C  
ATOM   1361  C   ASP B 105      15.860  59.748 103.908  1.00 47.25           C  
ANISOU 1361  C   ASP B 105     5325   7384   5245   -421   -293    145       C  
ATOM   1362  O   ASP B 105      16.530  60.229 104.833  1.00 47.66           O  
ANISOU 1362  O   ASP B 105     5284   7484   5340   -474   -318     47       O  
ATOM   1363  CB  ASP B 105      16.292  60.751 101.667  1.00 53.18           C  
ANISOU 1363  CB  ASP B 105     6041   8172   5991   -570    -67    252       C  
ATOM   1364  CG  ASP B 105      15.772  61.521 100.450  1.00 55.70           C  
ANISOU 1364  CG  ASP B 105     6466   8410   6285   -647     49    395       C  
ATOM   1365  OD1 ASP B 105      14.558  61.441 100.139  1.00 54.25           O  
ANISOU 1365  OD1 ASP B 105     6426   8116   6071   -588     -2    500       O  
ATOM   1366  OD2 ASP B 105      16.595  62.232  99.807  1.00 57.78           O  
ANISOU 1366  OD2 ASP B 105     6673   8721   6560   -766    195    396       O  
ATOM   1367  N   PHE B 106      15.661  58.455 103.764  1.00 49.15           N  
ANISOU 1367  N   PHE B 106     5618   7647   5409   -270   -368    146       N  
ATOM   1368  CA  PHE B 106      16.127  57.490 104.733  1.00 50.88           C  
ANISOU 1368  CA  PHE B 106     5825   7922   5584   -136   -487     63       C  
ATOM   1369  C   PHE B 106      16.743  56.342 103.958  1.00 53.90           C  
ANISOU 1369  C   PHE B 106     6156   8409   5916     -2   -508     25       C  
ATOM   1370  O   PHE B 106      16.195  55.932 102.950  1.00 58.79           O  
ANISOU 1370  O   PHE B 106     6838   8994   6507     17   -459     84       O  
ATOM   1371  CB  PHE B 106      14.943  56.962 105.524  1.00 48.13           C  
ANISOU 1371  CB  PHE B 106     5661   7420   5205    -78   -540    117       C  
ATOM   1372  CG  PHE B 106      14.189  58.012 106.282  1.00 47.37           C  
ANISOU 1372  CG  PHE B 106     5626   7207   5165   -201   -508    143       C  
ATOM   1373  CD1 PHE B 106      13.225  58.771 105.678  1.00 48.28           C  
ANISOU 1373  CD1 PHE B 106     5788   7210   5347   -296   -427    223       C  
ATOM   1374  CD2 PHE B 106      14.442  58.212 107.630  1.00 51.18           C  
ANISOU 1374  CD2 PHE B 106     6125   7696   5626   -204   -568     77       C  
ATOM   1375  CE1 PHE B 106      12.525  59.732 106.406  1.00 49.37           C  
ANISOU 1375  CE1 PHE B 106     5974   7229   5557   -397   -393    232       C  
ATOM   1376  CE2 PHE B 106      13.760  59.157 108.358  1.00 48.46           C  
ANISOU 1376  CE2 PHE B 106     5836   7245   5333   -319   -527     80       C  
ATOM   1377  CZ  PHE B 106      12.789  59.911 107.746  1.00 48.11           C  
ANISOU 1377  CZ  PHE B 106     5825   7073   5382   -416   -432    154       C  
ATOM   1378  N   HIS B 107      17.889  55.854 104.396  1.00 58.56           N  
ANISOU 1378  N   HIS B 107     6621   9133   6498     95   -585    -88       N  
ATOM   1379  CA  HIS B 107      18.403  54.594 103.893  1.00 60.23           C  
ANISOU 1379  CA  HIS B 107     6800   9415   6671    262   -625   -137       C  
ATOM   1380  C   HIS B 107      17.866  53.481 104.715  1.00 58.18           C  
ANISOU 1380  C   HIS B 107     6709   9047   6351    426   -737   -105       C  
ATOM   1381  O   HIS B 107      18.019  53.491 105.933  1.00 60.27           O  
ANISOU 1381  O   HIS B 107     7014   9299   6587    477   -839   -125       O  
ATOM   1382  CB  HIS B 107      19.914  54.516 104.021  1.00 64.46           C  
ANISOU 1382  CB  HIS B 107     7106  10143   7243    322   -672   -291       C  
ATOM   1383  CG  HIS B 107      20.642  55.262 102.968  1.00 66.31           C  
ANISOU 1383  CG  HIS B 107     7160  10498   7538    180   -523   -348       C  
ATOM   1384  ND1 HIS B 107      21.901  55.785 103.168  1.00 70.55           N  
ANISOU 1384  ND1 HIS B 107     7454  11198   8155    130   -513   -504       N  
ATOM   1385  CD2 HIS B 107      20.291  55.579 101.701  1.00 67.29           C  
ANISOU 1385  CD2 HIS B 107     7321  10602   7646     73   -367   -276       C  
ATOM   1386  CE1 HIS B 107      22.287  56.409 102.071  1.00 71.87           C  
ANISOU 1386  CE1 HIS B 107     7521  11424   8361    -22   -328   -519       C  
ATOM   1387  NE2 HIS B 107      21.333  56.290 101.163  1.00 70.25           N  
ANISOU 1387  NE2 HIS B 107     7499  11111   8082    -50   -242   -371       N  
ATOM   1388  N   MET B 108      17.247  52.533 104.042  1.00 57.64           N  
ANISOU 1388  N   MET B 108     6750   8896   6256    500   -709    -61       N  
ATOM   1389  CA  MET B 108      16.973  51.231 104.588  1.00 62.24           C  
ANISOU 1389  CA  MET B 108     7482   9375   6793    674   -785    -50       C  
ATOM   1390  C   MET B 108      18.126  50.380 104.102  1.00 64.51           C  
ANISOU 1390  C   MET B 108     7639   9787   7086    834   -828   -151       C  
ATOM   1391  O   MET B 108      18.267  50.156 102.905  1.00 68.77           O  
ANISOU 1391  O   MET B 108     8103  10382   7643    819   -745   -186       O  
ATOM   1392  CB  MET B 108      15.686  50.666 103.996  1.00 65.56           C  
ANISOU 1392  CB  MET B 108     8061   9636   7211    649   -711     17       C  
ATOM   1393  CG  MET B 108      14.403  51.046 104.709  1.00 67.00           C  
ANISOU 1393  CG  MET B 108     8405   9652   7401    551   -684     97       C  
ATOM   1394  SD  MET B 108      14.215  52.801 104.876  1.00 64.97           S  
ANISOU 1394  SD  MET B 108     8063   9436   7187    353   -643    129       S  
ATOM   1395  CE  MET B 108      12.555  52.772 105.541  1.00 53.10           C  
ANISOU 1395  CE  MET B 108     6755   7712   5708    287   -599    193       C  
ATOM   1396  N   SER B 109      18.944  49.905 105.017  1.00 70.30           N  
ANISOU 1396  N   SER B 109     8347  10566   7798    998   -961   -206       N  
ATOM   1397  CA  SER B 109      20.178  49.235 104.650  1.00 72.00           C  
ANISOU 1397  CA  SER B 109     8391  10920   8045   1164  -1019   -329       C  
ATOM   1398  C   SER B 109      20.206  47.840 105.171  1.00 71.56           C  
ANISOU 1398  C   SER B 109     8491  10750   7948   1411  -1123   -314       C  
ATOM   1399  O   SER B 109      20.119  47.638 106.386  1.00 71.88           O  
ANISOU 1399  O   SER B 109     8676  10716   7919   1512  -1243   -263       O  
ATOM   1400  CB  SER B 109      21.360  49.990 105.219  1.00 73.86           C  
ANISOU 1400  CB  SER B 109     8399  11350   8315   1163  -1109   -445       C  
ATOM   1401  OG  SER B 109      21.870  50.821 104.211  1.00 80.18           O  
ANISOU 1401  OG  SER B 109     8980  12293   9192    996   -975   -522       O  
ATOM   1402  N   VAL B 110      20.313  46.888 104.249  1.00 72.18           N  
ANISOU 1402  N   VAL B 110     8559  10803   8061   1508  -1070   -358       N  
ATOM   1403  CA  VAL B 110      20.596  45.502 104.610  1.00 82.29           C  
ANISOU 1403  CA  VAL B 110     9956  11979   9332   1772  -1164   -370       C  
ATOM   1404  C   VAL B 110      22.110  45.304 104.534  1.00 87.36           C  
ANISOU 1404  C   VAL B 110    10339  12820  10034   1950  -1271   -528       C  
ATOM   1405  O   VAL B 110      22.693  45.352 103.439  1.00 89.87           O  
ANISOU 1405  O   VAL B 110    10443  13276  10428   1913  -1178   -648       O  
ATOM   1406  CB  VAL B 110      19.938  44.466 103.673  1.00 78.68           C  
ANISOU 1406  CB  VAL B 110     9620  11373   8902   1799  -1048   -365       C  
ATOM   1407  CG1 VAL B 110      20.144  43.060 104.240  1.00 80.23           C  
ANISOU 1407  CG1 VAL B 110     9988  11404   9093   2071  -1138   -354       C  
ATOM   1408  CG2 VAL B 110      18.453  44.744 103.492  1.00 75.08           C  
ANISOU 1408  CG2 VAL B 110     9347  10760   8420   1598   -929   -257       C  
ATOM   1409  N   VAL B 111      22.735  45.085 105.690  1.00 83.48           N  
ANISOU 1409  N   VAL B 111     9865  12351   9503   2144  -1464   -537       N  
ATOM   1410  CA  VAL B 111      24.190  44.933 105.753  1.00 84.94           C  
ANISOU 1410  CA  VAL B 111     9775  12740   9759   2335  -1603   -711       C  
ATOM   1411  C   VAL B 111      24.521  43.453 105.546  1.00 83.94           C  
ANISOU 1411  C   VAL B 111     9724  12503   9665   2629  -1660   -741       C  
ATOM   1412  O   VAL B 111      23.808  42.569 106.051  1.00 77.14           O  
ANISOU 1412  O   VAL B 111     9181  11397   8730   2751  -1687   -603       O  
ATOM   1413  CB  VAL B 111      24.790  45.452 107.093  1.00 87.05           C  
ANISOU 1413  CB  VAL B 111     9995  13117   9964   2427  -1822   -737       C  
ATOM   1414  CG1 VAL B 111      26.292  45.648 106.956  1.00 91.92           C  
ANISOU 1414  CG1 VAL B 111    10227  14004  10695   2543  -1935   -969       C  
ATOM   1415  CG2 VAL B 111      24.156  46.780 107.514  1.00 86.71           C  
ANISOU 1415  CG2 VAL B 111     9983  13096   9868   2144  -1758   -670       C  
ATOM   1416  N   ARG B 112      25.573  43.190 104.773  1.00 83.27           N  
ANISOU 1416  N   ARG B 112     9352  12583   9704   2728  -1653   -929       N  
ATOM   1417  CA  ARG B 112      26.106  41.828 104.631  1.00 88.93           C  
ANISOU 1417  CA  ARG B 112    10091  13217  10481   3044  -1730   -995       C  
ATOM   1418  C   ARG B 112      24.950  40.924 104.239  1.00 84.46           C  
ANISOU 1418  C   ARG B 112     9850  12363   9877   3027  -1595   -859       C  
ATOM   1419  O   ARG B 112      24.494  40.057 104.995  1.00 79.34           O  
ANISOU 1419  O   ARG B 112     9504  11478   9165   3203  -1676   -730       O  
ATOM   1420  CB  ARG B 112      26.828  41.356 105.920  1.00 86.77           C  
ANISOU 1420  CB  ARG B 112     9858  12944  10165   3374  -2020   -995       C  
ATOM   1421  N   ALA B 113      24.469  41.172 103.031  1.00 86.12           N  
ANISOU 1421  N   ALA B 113     9999  12598  10124   2800  -1380   -896       N  
ATOM   1422  CA  ALA B 113      23.206  40.619 102.588  1.00 85.24           C  
ANISOU 1422  CA  ALA B 113    10159  12250   9976   2698  -1236   -788       C  
ATOM   1423  C   ALA B 113      23.287  39.103 102.330  1.00 89.66           C  
ANISOU 1423  C   ALA B 113    10849  12618  10601   2942  -1232   -833       C  
ATOM   1424  O   ALA B 113      24.132  38.653 101.546  1.00 80.24           O  
ANISOU 1424  O   ALA B 113     9449  11532   9507   3057  -1205  -1005       O  
ATOM   1425  CB  ALA B 113      22.757  41.351 101.334  1.00 91.01           C  
ANISOU 1425  CB  ALA B 113    10772  13095  10711   2410  -1039   -832       C  
ATOM   1426  N   ARG B 114      22.415  38.333 103.005  1.00 95.55           N  
ANISOU 1426  N   ARG B 114    11938  13070  11298   3013  -1241   -685       N  
ATOM   1427  CA  ARG B 114      22.243  36.871 102.754  1.00 95.44           C  
ANISOU 1427  CA  ARG B 114    12110  12800  11351   3203  -1194   -707       C  
ATOM   1428  C   ARG B 114      21.468  36.609 101.430  1.00 92.80           C  
ANISOU 1428  C   ARG B 114    11771  12419  11069   3004   -977   -793       C  
ATOM   1429  O   ARG B 114      20.883  37.520 100.838  1.00 89.78           O  
ANISOU 1429  O   ARG B 114    11306  12164  10644   2730   -877   -791       O  
ATOM   1430  CB  ARG B 114      21.484  36.186 103.914  1.00 94.14           C  
ANISOU 1430  CB  ARG B 114    12344  12312  11113   3303  -1233   -514       C  
ATOM   1431  CG  ARG B 114      22.193  36.117 105.262  1.00 96.80           C  
ANISOU 1431  CG  ARG B 114    12774  12638  11366   3565  -1463   -418       C  
ATOM   1432  CD  ARG B 114      21.393  35.272 106.257  1.00 97.22           C  
ANISOU 1432  CD  ARG B 114    13277  12330  11332   3663  -1450   -221       C  
ATOM   1433  N   ARG B 115      21.446  35.356 100.983  1.00 93.76           N  
ANISOU 1433  N   ARG B 115    11995  12351  11278   3153   -913   -871       N  
ATOM   1434  CA  ARG B 115      20.750  35.002  99.747  1.00 86.65           C  
ANISOU 1434  CA  ARG B 115    11094  11409  10422   2986   -725   -983       C  
ATOM   1435  C   ARG B 115      19.246  34.838  99.999  1.00 82.84           C  
ANISOU 1435  C   ARG B 115    10893  10679   9904   2799   -624   -864       C  
ATOM   1436  O   ARG B 115      18.443  35.256  99.170  1.00 73.58           O  
ANISOU 1436  O   ARG B 115     9676   9571   8710   2557   -510   -912       O  
ATOM   1437  CB  ARG B 115      21.354  33.751  99.089  1.00 86.09           C  
ANISOU 1437  CB  ARG B 115    10990  11244  10475   3204   -682  -1155       C  
ATOM   1438  N   ASN B 116      18.856  34.270 101.142  1.00 83.15           N  
ANISOU 1438  N   ASN B 116    11219  10443   9930   2907   -663   -715       N  
ATOM   1439  CA  ASN B 116      17.432  34.093 101.417  1.00 85.87           C  
ANISOU 1439  CA  ASN B 116    11818  10545  10262   2714   -536   -624       C  
ATOM   1440  C   ASN B 116      16.822  35.332 102.129  1.00 79.53           C  
ANISOU 1440  C   ASN B 116    11032   9836   9349   2513   -569   -478       C  
ATOM   1441  O   ASN B 116      15.750  35.259 102.745  1.00 76.41           O  
ANISOU 1441  O   ASN B 116    10865   9233   8935   2388   -488   -375       O  
ATOM   1442  CB  ASN B 116      17.180  32.815 102.203  1.00 88.90           C  
ANISOU 1442  CB  ASN B 116    12540  10547  10692   2890   -500   -542       C  
ATOM   1443  CG  ASN B 116      17.396  33.020 103.656  1.00 92.62           C  
ANISOU 1443  CG  ASN B 116    13203  10936  11050   3019   -626   -339       C  
ATOM   1444  OD1 ASN B 116      18.457  33.486 104.053  1.00 95.86           O  
ANISOU 1444  OD1 ASN B 116    13469  11550  11403   3188   -808   -319       O  
ATOM   1445  ND2 ASN B 116      16.375  32.755 104.458  1.00100.78           N  
ANISOU 1445  ND2 ASN B 116    14551  11695  12044   2921   -524   -200       N  
ATOM   1446  N   ASP B 117      17.547  36.446 102.063  1.00 69.92           N  
ANISOU 1446  N   ASP B 117     9570   8922   8073   2484   -674   -484       N  
ATOM   1447  CA  ASP B 117      16.962  37.755 102.256  1.00 67.68           C  
ANISOU 1447  CA  ASP B 117     9224   8777   7716   2247   -671   -407       C  
ATOM   1448  C   ASP B 117      16.232  38.212 100.997  1.00 66.80           C  
ANISOU 1448  C   ASP B 117     8983   8771   7627   2011   -552   -501       C  
ATOM   1449  O   ASP B 117      15.400  39.119 101.055  1.00 61.62           O  
ANISOU 1449  O   ASP B 117     8325   8154   6932   1803   -521   -439       O  
ATOM   1450  CB  ASP B 117      18.036  38.802 102.503  1.00 66.38           C  
ANISOU 1450  CB  ASP B 117     8827   8896   7499   2282   -805   -406       C  
ATOM   1451  CG  ASP B 117      18.519  38.860 103.930  1.00 65.75           C  
ANISOU 1451  CG  ASP B 117     8863   8772   7347   2445   -957   -290       C  
ATOM   1452  OD1 ASP B 117      17.864  38.386 104.902  1.00 67.06           O  
ANISOU 1452  OD1 ASP B 117     9325   8695   7461   2482   -951   -160       O  
ATOM   1453  OD2 ASP B 117      19.611  39.436 104.056  1.00 66.43           O  
ANISOU 1453  OD2 ASP B 117     8730   9089   7423   2529  -1082   -344       O  
ATOM   1454  N   SER B 118      16.621  37.639  99.860  1.00 65.41           N  
ANISOU 1454  N   SER B 118     8689   8660   7504   2060   -499   -657       N  
ATOM   1455  CA  SER B 118      15.934  37.851  98.612  1.00 66.09           C  
ANISOU 1455  CA  SER B 118     8691   8833   7589   1874   -397   -762       C  
ATOM   1456  C   SER B 118      14.435  37.904  98.895  1.00 65.37           C  
ANISOU 1456  C   SER B 118     8770   8559   7508   1694   -330   -701       C  
ATOM   1457  O   SER B 118      13.916  37.093  99.681  1.00 64.88           O  
ANISOU 1457  O   SER B 118     8927   8225   7500   1742   -292   -652       O  
ATOM   1458  CB  SER B 118      16.284  36.730  97.593  1.00 68.07           C  
ANISOU 1458  CB  SER B 118     8904   9053   7905   1979   -326   -947       C  
ATOM   1459  OG  SER B 118      17.639  36.843  97.131  1.00 65.78           O  
ANISOU 1459  OG  SER B 118     8402   8980   7613   2110   -363  -1039       O  
ATOM   1460  N   GLY B 119      13.757  38.897  98.304  1.00 63.73           N  
ANISOU 1460  N   GLY B 119     8466   8497   7252   1492   -314   -700       N  
ATOM   1461  CA  GLY B 119      12.304  39.045  98.473  1.00 57.35           C  
ANISOU 1461  CA  GLY B 119     7767   7549   6474   1317   -258   -675       C  
ATOM   1462  C   GLY B 119      11.786  40.457  98.315  1.00 53.96           C  
ANISOU 1462  C   GLY B 119     7237   7284   5983   1145   -293   -605       C  
ATOM   1463  O   GLY B 119      12.457  41.353  97.755  1.00 54.20           O  
ANISOU 1463  O   GLY B 119     7109   7549   5934   1127   -338   -591       O  
ATOM   1464  N   THR B 120      10.556  40.646  98.770  1.00 52.70           N  
ANISOU 1464  N   THR B 120     7168   6986   5871   1014   -257   -572       N  
ATOM   1465  CA  THR B 120       9.841  41.907  98.570  1.00 51.27           C  
ANISOU 1465  CA  THR B 120     6900   6920   5658    857   -287   -524       C  
ATOM   1466  C   THR B 120       9.863  42.792  99.807  1.00 51.06           C  
ANISOU 1466  C   THR B 120     6918   6866   5618    822   -317   -370       C  
ATOM   1467  O   THR B 120       9.740  42.314 100.921  1.00 58.24           O  
ANISOU 1467  O   THR B 120     7979   7591   6557    859   -285   -313       O  
ATOM   1468  CB  THR B 120       8.411  41.650  98.129  1.00 50.11           C  
ANISOU 1468  CB  THR B 120     6775   6674   5591    729   -238   -628       C  
ATOM   1469  OG1 THR B 120       8.462  40.905  96.934  1.00 51.57           O  
ANISOU 1469  OG1 THR B 120     6907   6917   5769    760   -225   -788       O  
ATOM   1470  CG2 THR B 120       7.692  42.922  97.788  1.00 48.39           C  
ANISOU 1470  CG2 THR B 120     6456   6584   5347    604   -292   -591       C  
ATOM   1471  N   TYR B 121      10.065  44.081  99.582  1.00 51.36           N  
ANISOU 1471  N   TYR B 121     6834   7082   5597    753   -371   -306       N  
ATOM   1472  CA  TYR B 121      10.273  45.066 100.632  1.00 49.45           C  
ANISOU 1472  CA  TYR B 121     6600   6854   5334    718   -405   -182       C  
ATOM   1473  C   TYR B 121       9.439  46.283 100.352  1.00 52.01           C  
ANISOU 1473  C   TYR B 121     6857   7236   5670    570   -413   -146       C  
ATOM   1474  O   TYR B 121       8.987  46.509  99.201  1.00 49.39           O  
ANISOU 1474  O   TYR B 121     6449   6991   5327    521   -421   -200       O  
ATOM   1475  CB  TYR B 121      11.738  45.493 100.656  1.00 54.00           C  
ANISOU 1475  CB  TYR B 121     7068   7607   5842    805   -466   -150       C  
ATOM   1476  CG  TYR B 121      12.637  44.400 101.131  1.00 56.23           C  
ANISOU 1476  CG  TYR B 121     7409   7835   6122    984   -490   -177       C  
ATOM   1477  CD1 TYR B 121      12.864  44.206 102.493  1.00 61.41           C  
ANISOU 1477  CD1 TYR B 121     8190   8379   6763   1062   -530   -101       C  
ATOM   1478  CD2 TYR B 121      13.226  43.523 100.234  1.00 55.80           C  
ANISOU 1478  CD2 TYR B 121     7300   7827   6073   1090   -476   -281       C  
ATOM   1479  CE1 TYR B 121      13.670  43.168 102.945  1.00 62.45           C  
ANISOU 1479  CE1 TYR B 121     8399   8445   6884   1261   -573   -113       C  
ATOM   1480  CE2 TYR B 121      14.035  42.492 100.668  1.00 57.44           C  
ANISOU 1480  CE2 TYR B 121     7564   7966   6297   1280   -505   -309       C  
ATOM   1481  CZ  TYR B 121      14.256  42.322 102.027  1.00 60.88           C  
ANISOU 1481  CZ  TYR B 121     8130   8285   6716   1375   -563   -217       C  
ATOM   1482  OH  TYR B 121      15.038  41.306 102.459  1.00 60.68           O  
ANISOU 1482  OH  TYR B 121     8178   8180   6697   1591   -613   -232       O  
ATOM   1483  N   LEU B 122       9.221  47.055 101.419  1.00 50.64           N  
ANISOU 1483  N   LEU B 122     6721   7008   5511    511   -416    -59       N  
ATOM   1484  CA  LEU B 122       8.467  48.295 101.358  1.00 46.80           C  
ANISOU 1484  CA  LEU B 122     6178   6549   5055    385   -423    -17       C  
ATOM   1485  C   LEU B 122       8.645  49.128 102.620  1.00 46.58           C  
ANISOU 1485  C   LEU B 122     6183   6488   5027    343   -426     68       C  
ATOM   1486  O   LEU B 122       9.069  48.618 103.636  1.00 46.16           O  
ANISOU 1486  O   LEU B 122     6231   6363   4946    404   -421     90       O  
ATOM   1487  CB  LEU B 122       6.992  48.008 101.091  1.00 46.47           C  
ANISOU 1487  CB  LEU B 122     6162   6386   5108    309   -383    -90       C  
ATOM   1488  CG  LEU B 122       6.081  47.325 102.082  1.00 45.46           C  
ANISOU 1488  CG  LEU B 122     6160   6042   5072    267   -296   -126       C  
ATOM   1489  CD1 LEU B 122       5.659  48.282 103.151  1.00 51.70           C  
ANISOU 1489  CD1 LEU B 122     6977   6772   5895    182   -270    -58       C  
ATOM   1490  CD2 LEU B 122       4.808  46.828 101.439  1.00 47.40           C  
ANISOU 1490  CD2 LEU B 122     6375   6209   5427    201   -258   -258       C  
ATOM   1491  N   CYS B 123       8.371  50.424 102.521  1.00 44.45           N  
ANISOU 1491  N   CYS B 123     5839   6273   4777    249   -439    114       N  
ATOM   1492  CA  CYS B 123       8.348  51.290 103.698  1.00 44.61           C  
ANISOU 1492  CA  CYS B 123     5888   6248   4814    186   -430    169       C  
ATOM   1493  C   CYS B 123       6.907  51.714 103.885  1.00 39.65           C  
ANISOU 1493  C   CYS B 123     5282   5494   4291     86   -382    151       C  
ATOM   1494  O   CYS B 123       6.145  51.853 102.927  1.00 40.62           O  
ANISOU 1494  O   CYS B 123     5342   5626   4466     62   -395    118       O  
ATOM   1495  CB  CYS B 123       9.354  52.483 103.653  1.00 44.81           C  
ANISOU 1495  CB  CYS B 123     5807   6418   4802    155   -467    219       C  
ATOM   1496  SG  CYS B 123       9.233  53.793 102.385  1.00 55.01           S  
ANISOU 1496  SG  CYS B 123     6983   7807   6111     72   -466    265       S  
ATOM   1497  N   GLY B 124       6.521  51.821 105.149  1.00 39.45           N  
ANISOU 1497  N   GLY B 124     5349   5351   4291     40   -329    158       N  
ATOM   1498  CA  GLY B 124       5.168  52.143 105.535  1.00 37.71           C  
ANISOU 1498  CA  GLY B 124     5145   4996   4186    -58   -258    117       C  
ATOM   1499  C   GLY B 124       5.292  53.252 106.539  1.00 41.16           C  
ANISOU 1499  C   GLY B 124     5591   5423   4625   -125   -241    157       C  
ATOM   1500  O   GLY B 124       5.870  53.066 107.627  1.00 42.00           O  
ANISOU 1500  O   GLY B 124     5802   5511   4644   -108   -226    180       O  
ATOM   1501  N   ALA B 125       4.832  54.432 106.148  1.00 38.52           N  
ANISOU 1501  N   ALA B 125     5152   5108   4377   -187   -257    164       N  
ATOM   1502  CA  ALA B 125       4.637  55.496 107.115  1.00 41.22           C  
ANISOU 1502  CA  ALA B 125     5501   5398   4763   -270   -216    169       C  
ATOM   1503  C   ALA B 125       3.340  55.282 107.844  1.00 39.18           C  
ANISOU 1503  C   ALA B 125     5298   4979   4610   -340   -107     92       C  
ATOM   1504  O   ALA B 125       2.316  55.127 107.218  1.00 41.51           O  
ANISOU 1504  O   ALA B 125     5526   5221   5024   -354    -93     31       O  
ATOM   1505  CB  ALA B 125       4.588  56.837 106.415  1.00 41.39           C  
ANISOU 1505  CB  ALA B 125     5404   5465   4857   -304   -260    207       C  
ATOM   1506  N   ILE B 126       3.373  55.373 109.157  1.00 38.73           N  
ANISOU 1506  N   ILE B 126     5350   4854   4510   -391    -29     80       N  
ATOM   1507  CA  ILE B 126       2.191  55.217 109.969  1.00 40.12           C  
ANISOU 1507  CA  ILE B 126     5591   4875   4777   -478    113     -2       C  
ATOM   1508  C   ILE B 126       1.977  56.494 110.742  1.00 38.84           C  
ANISOU 1508  C   ILE B 126     5401   4685   4669   -562    155    -26       C  
ATOM   1509  O   ILE B 126       2.804  56.820 111.609  1.00 41.85           O  
ANISOU 1509  O   ILE B 126     5865   5112   4924   -568    144      6       O  
ATOM   1510  CB  ILE B 126       2.403  54.057 111.005  1.00 41.30           C  
ANISOU 1510  CB  ILE B 126     5960   4943   4787   -466    205      8       C  
ATOM   1511  CG1 ILE B 126       2.703  52.762 110.263  1.00 40.52           C  
ANISOU 1511  CG1 ILE B 126     5900   4851   4643   -374    169     29       C  
ATOM   1512  CG2 ILE B 126       1.162  53.900 111.878  1.00 38.36           C  
ANISOU 1512  CG2 ILE B 126     5672   4398   4504   -584    398    -83       C  
ATOM   1513  CD1 ILE B 126       3.107  51.619 111.161  1.00 45.62           C  
ANISOU 1513  CD1 ILE B 126     6784   5411   5139   -324    233     71       C  
ATOM   1514  N   SER B 127       0.894  57.196 110.455  1.00 34.66           N  
ANISOU 1514  N   SER B 127     4754   4086   4331   -617    195    -97       N  
ATOM   1515  CA  SER B 127       0.514  58.317 111.252  1.00 38.84           C  
ANISOU 1515  CA  SER B 127     5261   4554   4942   -699    265   -147       C  
ATOM   1516  C   SER B 127      -0.335  57.890 112.413  1.00 37.86           C  
ANISOU 1516  C   SER B 127     5246   4298   4840   -793    450   -247       C  
ATOM   1517  O   SER B 127      -1.268  57.103 112.270  1.00 39.91           O  
ANISOU 1517  O   SER B 127     5501   4471   5193   -819    542   -324       O  
ATOM   1518  CB  SER B 127      -0.323  59.319 110.473  1.00 39.81           C  
ANISOU 1518  CB  SER B 127     5208   4641   5278   -698    227   -186       C  
ATOM   1519  OG  SER B 127       0.352  59.657 109.294  1.00 40.88           O  
ANISOU 1519  OG  SER B 127     5269   4883   5379   -615     76    -83       O  
ATOM   1520  N   LEU B 128      -0.073  58.497 113.540  1.00 37.60           N  
ANISOU 1520  N   LEU B 128     5301   4248   4737   -856    517   -266       N  
ATOM   1521  CA  LEU B 128      -0.763  58.166 114.773  1.00 40.99           C  
ANISOU 1521  CA  LEU B 128     5873   4560   5141   -956    716   -355       C  
ATOM   1522  C   LEU B 128      -1.722  59.248 115.258  1.00 44.22           C  
ANISOU 1522  C   LEU B 128     6185   4878   5740  -1056    835   -486       C  
ATOM   1523  O   LEU B 128      -2.636  58.968 116.013  1.00 48.35           O  
ANISOU 1523  O   LEU B 128     6771   5285   6316  -1152   1032   -596       O  
ATOM   1524  CB  LEU B 128       0.280  57.891 115.830  1.00 40.55           C  
ANISOU 1524  CB  LEU B 128     6033   4562   4813   -942    707   -290       C  
ATOM   1525  CG  LEU B 128       1.413  56.951 115.392  1.00 39.60           C  
ANISOU 1525  CG  LEU B 128     5991   4546   4510   -813    560   -164       C  
ATOM   1526  CD1 LEU B 128       2.487  56.870 116.499  1.00 39.83           C  
ANISOU 1526  CD1 LEU B 128     6208   4652   4274   -775    511   -117       C  
ATOM   1527  CD2 LEU B 128       0.832  55.574 115.021  1.00 39.57           C  
ANISOU 1527  CD2 LEU B 128     6067   4444   4525   -792    641   -157       C  
ATOM   1528  N   ALA B 129      -1.543  60.474 114.796  1.00 47.94           N  
ANISOU 1528  N   ALA B 129     6505   5386   6326  -1035    733   -480       N  
ATOM   1529  CA  ALA B 129      -2.390  61.578 115.222  1.00 48.02           C  
ANISOU 1529  CA  ALA B 129     6415   5297   6532  -1110    834   -606       C  
ATOM   1530  C   ALA B 129      -2.335  62.622 114.161  1.00 46.83           C  
ANISOU 1530  C   ALA B 129     6083   5165   6546  -1037    686   -562       C  
ATOM   1531  O   ALA B 129      -1.314  62.753 113.506  1.00 46.97           O  
ANISOU 1531  O   ALA B 129     6100   5286   6460   -971    537   -433       O  
ATOM   1532  CB  ALA B 129      -1.862  62.178 116.497  1.00 46.93           C  
ANISOU 1532  CB  ALA B 129     6405   5165   6261  -1190    912   -644       C  
ATOM   1533  N   PRO B 130      -3.391  63.420 114.040  1.00 49.98           N  
ANISOU 1533  N   PRO B 130     6337   5456   7197  -1049    737   -671       N  
ATOM   1534  CA  PRO B 130      -4.629  63.301 114.808  1.00 53.75           C  
ANISOU 1534  CA  PRO B 130     6783   5812   7826  -1137    935   -854       C  
ATOM   1535  C   PRO B 130      -5.426  62.132 114.262  1.00 63.59           C  
ANISOU 1535  C   PRO B 130     7974   7046   9139  -1119    960   -904       C  
ATOM   1536  O   PRO B 130      -6.249  61.567 114.983  1.00 65.15           O  
ANISOU 1536  O   PRO B 130     8201   7160   9393  -1220   1161  -1044       O  
ATOM   1537  CB  PRO B 130      -5.385  64.584 114.479  1.00 53.30           C  
ANISOU 1537  CB  PRO B 130     6539   5663   8052  -1102    913   -939       C  
ATOM   1538  CG  PRO B 130      -4.899  64.952 113.097  1.00 53.99           C  
ANISOU 1538  CG  PRO B 130     6545   5814   8155   -962    681   -782       C  
ATOM   1539  CD  PRO B 130      -3.463  64.473 113.005  1.00 52.86           C  
ANISOU 1539  CD  PRO B 130     6552   5805   7727   -958    595   -616       C  
ATOM   1540  N   LYS B 131      -5.158  61.794 112.988  1.00 66.71           N  
ANISOU 1540  N   LYS B 131     8295   7524   9527  -1003    770   -800       N  
ATOM   1541  CA  LYS B 131      -5.865  60.739 112.213  1.00 66.55           C  
ANISOU 1541  CA  LYS B 131     8190   7510   9585   -970    749   -858       C  
ATOM   1542  C   LYS B 131      -4.884  59.591 111.964  1.00 57.35           C  
ANISOU 1542  C   LYS B 131     7184   6436   8171   -943    694   -724       C  
ATOM   1543  O   LYS B 131      -3.786  59.813 111.447  1.00 62.17           O  
ANISOU 1543  O   LYS B 131     7838   7152   8631   -864    539   -568       O  
ATOM   1544  CB  LYS B 131      -6.315  61.343 110.866  1.00 63.71           C  
ANISOU 1544  CB  LYS B 131     7624   7185   9398   -835    546   -850       C  
ATOM   1545  CG  LYS B 131      -7.438  60.630 110.150  1.00 66.27           C  
ANISOU 1545  CG  LYS B 131     7780   7501   9898   -805    523   -997       C  
ATOM   1546  N   ALA B 132      -5.257  58.387 112.366  1.00 51.39           N  
ANISOU 1546  N   ALA B 132     6519   5627   7381  -1012    837   -791       N  
ATOM   1547  CA  ALA B 132      -4.411  57.226 112.184  1.00 48.56           C  
ANISOU 1547  CA  ALA B 132     6320   5323   6809   -976    801   -679       C  
ATOM   1548  C   ALA B 132      -4.506  56.760 110.753  1.00 43.20           C  
ANISOU 1548  C   ALA B 132     5505   4719   6188   -877    636   -669       C  
ATOM   1549  O   ALA B 132      -5.577  56.689 110.213  1.00 46.29           O  
ANISOU 1549  O   ALA B 132     5726   5075   6786   -884    641   -809       O  
ATOM   1550  CB  ALA B 132      -4.788  56.117 113.144  1.00 51.81           C  
ANISOU 1550  CB  ALA B 132     6911   5616   7161  -1085   1032   -744       C  
ATOM   1551  N   GLN B 133      -3.369  56.466 110.152  1.00 40.71           N  
ANISOU 1551  N   GLN B 133     5259   4520   5691   -783    489   -519       N  
ATOM   1552  CA  GLN B 133      -3.280  56.255 108.728  1.00 45.45           C  
ANISOU 1552  CA  GLN B 133     5740   5220   6308   -678    313   -492       C  
ATOM   1553  C   GLN B 133      -2.078  55.414 108.422  1.00 39.30           C  
ANISOU 1553  C   GLN B 133     5090   4529   5313   -612    247   -369       C  
ATOM   1554  O   GLN B 133      -1.082  55.556 109.039  1.00 39.94           O  
ANISOU 1554  O   GLN B 133     5294   4644   5236   -605    247   -265       O  
ATOM   1555  CB  GLN B 133      -3.004  57.567 108.039  1.00 49.37           C  
ANISOU 1555  CB  GLN B 133     6126   5797   6834   -602    154   -411       C  
ATOM   1556  CG  GLN B 133      -4.193  58.278 107.489  1.00 61.40           C  
ANISOU 1556  CG  GLN B 133     7460   7284   8587   -574    100   -519       C  
ATOM   1557  CD  GLN B 133      -3.789  59.401 106.507  1.00 69.23           C  
ANISOU 1557  CD  GLN B 133     8388   8353   9562   -462    -86   -393       C  
ATOM   1558  OE1 GLN B 133      -2.849  60.190 106.754  1.00 65.63           O  
ANISOU 1558  OE1 GLN B 133     8010   7919   9008   -465    -98   -263       O  
ATOM   1559  NE2 GLN B 133      -4.494  59.464 105.385  1.00 67.19           N  
ANISOU 1559  NE2 GLN B 133     7997   8135   9396   -364   -227   -438       N  
ATOM   1560  N   ILE B 134      -2.170  54.584 107.413  1.00 38.51           N  
ANISOU 1560  N   ILE B 134     4942   4475   5214   -556    175   -397       N  
ATOM   1561  CA  ILE B 134      -1.050  53.809 106.961  1.00 39.44           C  
ANISOU 1561  CA  ILE B 134     5153   4681   5150   -477    104   -298       C  
ATOM   1562  C   ILE B 134      -0.773  54.221 105.518  1.00 38.91           C  
ANISOU 1562  C   ILE B 134     4959   4761   5063   -381    -79   -255       C  
ATOM   1563  O   ILE B 134      -1.688  54.101 104.675  1.00 39.71           O  
ANISOU 1563  O   ILE B 134     4935   4871   5283   -364   -134   -360       O  
ATOM   1564  CB  ILE B 134      -1.457  52.320 106.918  1.00 40.25           C  
ANISOU 1564  CB  ILE B 134     5324   4697   5273   -499    200   -392       C  
ATOM   1565  CG1 ILE B 134      -1.632  51.772 108.323  1.00 42.71           C  
ANISOU 1565  CG1 ILE B 134     5819   4847   5560   -590    402   -406       C  
ATOM   1566  CG2 ILE B 134      -0.424  51.500 106.148  1.00 40.07           C  
ANISOU 1566  CG2 ILE B 134     5354   4770   5100   -395    104   -321       C  
ATOM   1567  CD1 ILE B 134      -2.486  50.542 108.381  1.00 45.68           C  
ANISOU 1567  CD1 ILE B 134     6241   5075   6039   -664    559   -539       C  
ATOM   1568  N   LYS B 135       0.451  54.627 105.220  1.00 37.71           N  
ANISOU 1568  N   LYS B 135     4841   4726   4760   -320   -166   -120       N  
ATOM   1569  CA  LYS B 135       0.869  54.973 103.831  1.00 40.65           C  
ANISOU 1569  CA  LYS B 135     5135   5241   5071   -235   -311    -60       C  
ATOM   1570  C   LYS B 135       2.084  54.180 103.352  1.00 37.87           C  
ANISOU 1570  C   LYS B 135     4843   4997   4548   -169   -345     -1       C  
ATOM   1571  O   LYS B 135       3.143  54.352 103.897  1.00 38.13           O  
ANISOU 1571  O   LYS B 135     4935   5069   4483   -165   -331     80       O  
ATOM   1572  CB  LYS B 135       1.140  56.481 103.722  1.00 45.65           C  
ANISOU 1572  CB  LYS B 135     5725   5907   5713   -235   -364     40       C  
ATOM   1573  CG  LYS B 135      -0.116  57.277 103.379  1.00 51.16           C  
ANISOU 1573  CG  LYS B 135     6316   6543   6578   -230   -409    -17       C  
ATOM   1574  CD  LYS B 135      -0.101  58.750 103.826  1.00 54.29           C  
ANISOU 1574  CD  LYS B 135     6699   6883   7047   -258   -399     52       C  
ATOM   1575  N   GLU B 136       1.920  53.349 102.313  1.00 38.91           N  
ANISOU 1575  N   GLU B 136     4943   5185   4654   -114   -397    -60       N  
ATOM   1576  CA  GLU B 136       2.935  52.397 101.859  1.00 40.29           C  
ANISOU 1576  CA  GLU B 136     5170   5444   4695    -48   -410    -44       C  
ATOM   1577  C   GLU B 136       3.520  52.769 100.526  1.00 41.24           C  
ANISOU 1577  C   GLU B 136     5234   5730   4706     15   -509      8       C  
ATOM   1578  O   GLU B 136       2.821  53.162  99.621  1.00 41.34           O  
ANISOU 1578  O   GLU B 136     5182   5785   4740     32   -585    -17       O  
ATOM   1579  CB  GLU B 136       2.323  50.999 101.675  1.00 40.81           C  
ANISOU 1579  CB  GLU B 136     5260   5434   4812    -43   -364   -179       C  
ATOM   1580  CG  GLU B 136       2.025  50.297 102.984  1.00 41.00           C  
ANISOU 1580  CG  GLU B 136     5400   5281   4898   -100   -227   -213       C  
ATOM   1581  CD  GLU B 136       1.528  48.887 102.786  1.00 45.66           C  
ANISOU 1581  CD  GLU B 136     6035   5770   5545   -106   -154   -342       C  
ATOM   1582  OE1 GLU B 136       0.900  48.619 101.704  1.00 47.83           O  
ANISOU 1582  OE1 GLU B 136     6201   6097   5877   -101   -212   -459       O  
ATOM   1583  OE2 GLU B 136       1.716  48.053 103.728  1.00 49.56           O  
ANISOU 1583  OE2 GLU B 136     6683   6122   6027   -117    -36   -331       O  
ATOM   1584  N   SER B 137       4.818  52.601 100.389  1.00 41.59           N  
ANISOU 1584  N   SER B 137     5304   5871   4625     56   -506     72       N  
ATOM   1585  CA  SER B 137       5.427  52.734  99.081  1.00 40.87           C  
ANISOU 1585  CA  SER B 137     5178   5938   4415    107   -562    102       C  
ATOM   1586  C   SER B 137       4.995  51.575  98.251  1.00 42.03           C  
ANISOU 1586  C   SER B 137     5320   6106   4543    156   -586    -18       C  
ATOM   1587  O   SER B 137       4.510  50.589  98.756  1.00 44.39           O  
ANISOU 1587  O   SER B 137     5649   6295   4922    151   -542   -115       O  
ATOM   1588  CB  SER B 137       6.923  52.623  99.228  1.00 40.36           C  
ANISOU 1588  CB  SER B 137     5118   5965   4250    134   -529    154       C  
ATOM   1589  OG  SER B 137       7.205  51.317  99.681  1.00 40.85           O  
ANISOU 1589  OG  SER B 137     5226   5980   4316    189   -499     80       O  
ATOM   1590  N   LEU B 138       5.215  51.679  96.964  1.00 45.00           N  
ANISOU 1590  N   LEU B 138     5671   6621   4804    199   -643    -17       N  
ATOM   1591  CA  LEU B 138       5.241  50.519  96.119  1.00 46.78           C  
ANISOU 1591  CA  LEU B 138     5896   6905   4971    252   -655   -138       C  
ATOM   1592  C   LEU B 138       6.335  49.538  96.601  1.00 44.83           C  
ANISOU 1592  C   LEU B 138     5685   6646   4704    291   -576   -161       C  
ATOM   1593  O   LEU B 138       7.294  49.909  97.282  1.00 46.70           O  
ANISOU 1593  O   LEU B 138     5928   6894   4921    293   -539    -72       O  
ATOM   1594  CB  LEU B 138       5.593  50.918  94.697  1.00 49.71           C  
ANISOU 1594  CB  LEU B 138     6261   7455   5173    291   -711   -110       C  
ATOM   1595  CG  LEU B 138       4.676  51.807  93.883  1.00 55.47           C  
ANISOU 1595  CG  LEU B 138     6982   8234   5861    302   -822    -77       C  
ATOM   1596  CD1 LEU B 138       5.248  51.769  92.462  1.00 57.67           C  
ANISOU 1596  CD1 LEU B 138     7297   8695   5920    353   -849    -68       C  
ATOM   1597  CD2 LEU B 138       3.225  51.326  93.879  1.00 54.92           C  
ANISOU 1597  CD2 LEU B 138     6857   8089   5921    306   -902   -230       C  
ATOM   1598  N   ARG B 139       6.150  48.286  96.252  1.00 43.71           N  
ANISOU 1598  N   ARG B 139     5558   6473   4576    330   -559   -296       N  
ATOM   1599  CA  ARG B 139       7.011  47.231  96.690  1.00 49.80           C  
ANISOU 1599  CA  ARG B 139     6375   7196   5350    393   -495   -332       C  
ATOM   1600  C   ARG B 139       8.243  47.189  95.830  1.00 47.01           C  
ANISOU 1600  C   ARG B 139     5980   7018   4863    458   -493   -327       C  
ATOM   1601  O   ARG B 139       8.129  47.299  94.643  1.00 53.62           O  
ANISOU 1601  O   ARG B 139     6786   7982   5605    459   -522   -373       O  
ATOM   1602  CB  ARG B 139       6.290  45.898  96.608  1.00 53.35           C  
ANISOU 1602  CB  ARG B 139     6866   7516   5887    402   -457   -490       C  
ATOM   1603  CG  ARG B 139       4.993  45.937  97.392  1.00 60.68           C  
ANISOU 1603  CG  ARG B 139     7819   8271   6964    313   -429   -522       C  
ATOM   1604  CD  ARG B 139       4.479  44.555  97.713  1.00 67.82           C  
ANISOU 1604  CD  ARG B 139     8798   8989   7983    303   -336   -659       C  
ATOM   1605  NE  ARG B 139       3.896  43.903  96.550  1.00 70.84           N  
ANISOU 1605  NE  ARG B 139     9115   9419   8380    295   -364   -845       N  
ATOM   1606  N   ALA B 140       9.401  47.025  96.451  1.00 42.11           N  
ANISOU 1606  N   ALA B 140     5357   6408   4233    515   -459   -282       N  
ATOM   1607  CA  ALA B 140      10.651  46.858  95.779  1.00 45.88           C  
ANISOU 1607  CA  ALA B 140     5772   7040   4619    579   -435   -308       C  
ATOM   1608  C   ALA B 140      11.120  45.402  95.932  1.00 52.04           C  
ANISOU 1608  C   ALA B 140     6584   7745   5444    696   -404   -420       C  
ATOM   1609  O   ALA B 140      10.736  44.700  96.873  1.00 48.88           O  
ANISOU 1609  O   ALA B 140     6275   7160   5138    729   -397   -425       O  
ATOM   1610  CB  ALA B 140      11.678  47.755  96.385  1.00 44.12           C  
ANISOU 1610  CB  ALA B 140     5488   6893   4381    569   -429   -207       C  
ATOM   1611  N   GLU B 141      11.961  44.947  95.013  1.00 56.07           N  
ANISOU 1611  N   GLU B 141     7032   8385   5887    761   -372   -508       N  
ATOM   1612  CA  GLU B 141      12.454  43.581  95.141  1.00 62.75           C  
ANISOU 1612  CA  GLU B 141     7906   9146   6791    890   -343   -620       C  
ATOM   1613  C   GLU B 141      13.968  43.542  95.188  1.00 60.89           C  
ANISOU 1613  C   GLU B 141     7566   9032   6536    994   -329   -634       C  
ATOM   1614  O   GLU B 141      14.652  44.258  94.472  1.00 57.05           O  
ANISOU 1614  O   GLU B 141     6970   8741   5966    953   -297   -635       O  
ATOM   1615  CB  GLU B 141      11.838  42.601  94.120  1.00 64.78           C  
ANISOU 1615  CB  GLU B 141     8194   9376   7043    897   -311   -783       C  
ATOM   1616  CG  GLU B 141      11.166  43.205  92.890  1.00 72.48           C  
ANISOU 1616  CG  GLU B 141     9137  10500   7901    797   -330   -821       C  
ATOM   1617  CD  GLU B 141       9.711  43.657  93.098  1.00 75.46           C  
ANISOU 1617  CD  GLU B 141     9560  10787   8323    694   -388   -788       C  
ATOM   1618  OE1 GLU B 141       9.404  44.778  92.634  1.00 71.34           O  
ANISOU 1618  OE1 GLU B 141     9011  10387   7709    626   -436   -704       O  
ATOM   1619  OE2 GLU B 141       8.875  42.912  93.696  1.00 73.96           O  
ANISOU 1619  OE2 GLU B 141     9435  10402   8266    681   -376   -850       O  
ATOM   1620  N   LEU B 142      14.453  42.726  96.114  1.00 62.47           N  
ANISOU 1620  N   LEU B 142     7809   9105   6820   1129   -351   -642       N  
ATOM   1621  CA  LEU B 142      15.874  42.512  96.331  1.00 65.81           C  
ANISOU 1621  CA  LEU B 142     8122   9623   7260   1269   -366   -681       C  
ATOM   1622  C   LEU B 142      16.344  41.103  95.929  1.00 64.86           C  
ANISOU 1622  C   LEU B 142     8012   9437   7195   1435   -334   -828       C  
ATOM   1623  O   LEU B 142      15.904  40.105  96.544  1.00 66.30           O  
ANISOU 1623  O   LEU B 142     8348   9391   7452   1526   -345   -830       O  
ATOM   1624  CB  LEU B 142      16.150  42.684  97.820  1.00 69.07           C  
ANISOU 1624  CB  LEU B 142     8585   9941   7716   1340   -452   -571       C  
ATOM   1625  CG  LEU B 142      17.558  42.273  98.254  1.00 71.26           C  
ANISOU 1625  CG  LEU B 142     8756  10288   8031   1532   -510   -626       C  
ATOM   1626  CD1 LEU B 142      18.625  43.091  97.520  1.00 72.87           C  
ANISOU 1626  CD1 LEU B 142     8719  10760   8208   1484   -475   -697       C  
ATOM   1627  CD2 LEU B 142      17.657  42.391  99.754  1.00 67.10           C  
ANISOU 1627  CD2 LEU B 142     8321   9659   7513   1610   -619   -514       C  
ATOM   1628  N   ARG B 143      17.244  41.023  94.944  1.00 64.20           N  
ANISOU 1628  N   ARG B 143     7777   9535   7080   1472   -277   -953       N  
ATOM   1629  CA  ARG B 143      17.868  39.743  94.520  1.00 67.19           C  
ANISOU 1629  CA  ARG B 143     8132   9871   7525   1644   -239  -1118       C  
ATOM   1630  C   ARG B 143      19.305  39.684  95.008  1.00 67.62           C  
ANISOU 1630  C   ARG B 143     8030  10019   7642   1813   -285  -1157       C  
ATOM   1631  O   ARG B 143      20.133  40.527  94.617  1.00 67.86           O  
ANISOU 1631  O   ARG B 143     7871  10279   7635   1755   -252  -1187       O  
ATOM   1632  CB  ARG B 143      17.884  39.577  92.997  1.00 67.89           C  
ANISOU 1632  CB  ARG B 143     8151  10107   7536   1577   -129  -1275       C  
ATOM   1633  N   VAL B 144      19.594  38.707  95.868  1.00 68.51           N  
ANISOU 1633  N   VAL B 144     8226   9951   7855   2023   -359  -1159       N  
ATOM   1634  CA  VAL B 144      20.971  38.443  96.309  1.00 71.73           C  
ANISOU 1634  CA  VAL B 144     8477  10437   8338   2239   -433  -1228       C  
ATOM   1635  C   VAL B 144      21.514  37.127  95.723  1.00 70.57           C  
ANISOU 1635  C   VAL B 144     8304  10221   8288   2438   -385  -1411       C  
ATOM   1636  O   VAL B 144      20.971  36.036  95.979  1.00 68.79           O  
ANISOU 1636  O   VAL B 144     8282   9735   8122   2546   -385  -1407       O  
ATOM   1637  CB  VAL B 144      21.106  38.418  97.843  1.00 72.17           C  
ANISOU 1637  CB  VAL B 144     8638  10364   8420   2380   -593  -1086       C  
ATOM   1638  CG1 VAL B 144      22.571  38.542  98.242  1.00 75.29           C  
ANISOU 1638  CG1 VAL B 144     8804  10927   8875   2568   -700  -1169       C  
ATOM   1639  CG2 VAL B 144      20.317  39.552  98.468  1.00 73.97           C  
ANISOU 1639  CG2 VAL B 144     8946  10599   8561   2177   -621   -914       C  
ATOM   1640  N   THR B 145      22.609  37.249  94.962  1.00 72.30           N  
ANISOU 1640  N   THR B 145     8271  10665   8535   2480   -327  -1579       N  
ATOM   1641  CA  THR B 145      23.207  36.125  94.207  1.00 74.03           C  
ANISOU 1641  CA  THR B 145     8416  10862   8847   2648   -251  -1793       C  
ATOM   1642  C   THR B 145      24.570  35.703  94.729  1.00 77.80           C  
ANISOU 1642  C   THR B 145     8708  11390   9462   2927   -350  -1896       C  
ATOM   1643  O   THR B 145      25.253  36.478  95.405  1.00 79.64           O  
ANISOU 1643  O   THR B 145     8788  11769   9703   2950   -454  -1849       O  
ATOM   1644  CB  THR B 145      23.405  36.507  92.720  1.00 75.16           C  
ANISOU 1644  CB  THR B 145     8404  11242   8911   2477    -71  -1953       C  
ATOM   1645  OG1 THR B 145      24.372  37.570  92.622  1.00 76.45           O  
ANISOU 1645  OG1 THR B 145     8315  11678   9055   2404    -46  -1980       O  
ATOM   1646  CG2 THR B 145      22.069  36.934  92.060  1.00 70.02           C  
ANISOU 1646  CG2 THR B 145     7924  10572   8108   2222      5  -1873       C  
ATOM   1647  N   GLU B 146      24.982  34.490  94.338  1.00 83.86           N  
ANISOU 1647  N   GLU B 146     9468  12049  10347   3136   -313  -2063       N  
ATOM   1648  CA  GLU B 146      26.208  33.821  94.828  1.00 86.69           C  
ANISOU 1648  CA  GLU B 146     9672  12401  10865   3466   -426  -2179       C  
ATOM   1649  C   GLU B 146      27.526  34.469  94.381  1.00 87.68           C  
ANISOU 1649  C   GLU B 146     9407  12860  11047   3473   -392  -2367       C  
ATOM   1650  O   GLU B 146      27.535  35.296  93.471  1.00 86.05           O  
ANISOU 1650  O   GLU B 146     9066  12876  10752   3217   -229  -2429       O  
ATOM   1651  CB  GLU B 146      26.179  32.344  94.407  1.00 89.90           C  
ANISOU 1651  CB  GLU B 146    10190  12574  11392   3670   -365  -2319       C  
TER    1652      GLU B 146                                                      
HETATM 1653 NA    NA A 201     -16.760  44.513 125.608  1.00 50.06          NA  
HETATM 1654  O   HOH A 301      -9.855  44.353 121.540  1.00 48.06           O  
HETATM 1655  O   HOH A 302      -4.997  52.478 131.912  1.00 54.19           O  
HETATM 1656  O   HOH A 303      -3.926  37.744 104.433  1.00 71.27           O  
HETATM 1657  O   HOH A 304       5.452  39.399 112.805  1.00 64.84           O  
HETATM 1658  O   HOH A 305      -9.699  34.796 121.584  1.00 65.61           O  
HETATM 1659  O   HOH A 306      -0.628  39.203 123.290  1.00 65.20           O  
HETATM 1660  O   HOH A 307     -15.970  50.495 119.597  1.00 63.84           O  
HETATM 1661  O   HOH A 308     -19.826  51.396 102.828  1.00 66.35           O  
HETATM 1662  O   HOH A 309      -5.600  62.395 124.780  1.00 64.53           O  
HETATM 1663  O   HOH B 201      -1.485  65.910 118.047  1.00 48.36           O  
HETATM 1664  O   HOH B 202      -4.663  54.284 106.232  1.00 42.30           O  
HETATM 1665  O   HOH B 203       7.223  51.577 114.742  1.00 49.96           O  
HETATM 1666  O   HOH B 204      24.974  40.188  91.764  1.00 65.07           O  
HETATM 1667  O   HOH B 205      13.293  37.476 102.530  1.00 60.32           O  
HETATM 1668  O   HOH B 206       1.687  66.580 104.110  1.00 62.51           O  
CONECT  179  743                                                                
CONECT  743  179                                                                
CONECT 1029 1496                                                                
CONECT 1496 1029                                                                
MASTER      387    0    1    5   22    0    1    6 1666    2    4   19          
END                                                                             



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