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***  BS 5DS3  ***

elNémo ID: 21050818022146608

Job options:

ID        	=	 21050818022146608
JOBID     	=	 BS 5DS3
USERID    	=	 Frankkkss
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 BS 5DS3

HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       16-SEP-15   5DS3              
TITLE     CRYSTAL STRUCTURE OF CONSTITUTIVELY ACTIVE PARP-1                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: POLY [ADP-RIBOSE] POLYMERASE 1;                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: CATALYTIC DOMAIN (UNP RESIDUES 788-1012);                  
COMPND   5 SYNONYM: PARP-1,ADP-RIBOSYLTRANSFERASE DIPHTHERIA TOXIN-LIKE 1,ARTD1,
COMPND   6 NAD(+) ADP-RIBOSYLTRANSFERASE 1,ADPRT 1,POLY[ADP-RIBOSE] SYNTHASE 1; 
COMPND   7 EC: 2.4.2.30;                                                        
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PARP1, ADPRT, PPOL;                                            
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET28                                     
KEYWDS    ADP-RIBOSYL TRANSFERASE, PARP-1, TRANSFERASE-TRANSFERASE INHIBITOR    
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.F.LANGELIER,J.M.PASCAL                                              
REVDAT   3   25-DEC-19 5DS3    1       REMARK                                   
REVDAT   2   06-SEP-17 5DS3    1       JRNL   REMARK                            
REVDAT   1   27-JUL-16 5DS3    0                                                
JRNL        AUTH   J.M.DAWICKI-MCKENNA,M.F.LANGELIER,J.E.DENIZIO,A.A.RICCIO,    
JRNL        AUTH 2 C.D.CAO,K.R.KARCH,M.MCCAULEY,J.D.STEFFEN,B.E.BLACK,          
JRNL        AUTH 3 J.M.PASCAL                                                   
JRNL        TITL   PARP-1 ACTIVATION REQUIRES LOCAL UNFOLDING OF AN             
JRNL        TITL 2 AUTOINHIBITORY DOMAIN.                                       
JRNL        REF    MOL.CELL                      V.  60   755 2015              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   26626480                                                     
JRNL        DOI    10.1016/J.MOLCEL.2015.10.013                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.58                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 10627                          
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) : 0.202                           
REMARK   3   R VALUE            (WORKING SET) : 0.200                           
REMARK   3   FREE R VALUE                     : 0.251                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 535                             
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) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.66                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 724                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.34                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3920                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 45                           
REMARK   3   BIN FREE R VALUE                    : 0.3770                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1887                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 58                                      
REMARK   3   SOLVENT ATOMS            : 27                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 59.49                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.26000                                             
REMARK   3    B22 (A**2) : -1.26000                                             
REMARK   3    B33 (A**2) : 4.08000                                              
REMARK   3    B12 (A**2) : -1.26000                                             
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): 0.456         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.287         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.224         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 23.127        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.952                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.921                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2006 ; 0.007 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  1932 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2707 ; 1.228 ; 1.970       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4468 ; 0.706 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   245 ; 6.720 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    83 ;36.768 ;24.458       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   345 ;15.700 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     8 ;13.071 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   290 ; 0.071 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2340 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   438 ; 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):   977 ; 1.150 ; 3.239       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   976 ; 1.150 ; 3.239       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1220 ; 2.057 ; 4.856       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  1221 ; 2.056 ; 4.857       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1029 ; 1.006 ; 3.361       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1022 ; 0.996 ; 3.317       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  1472 ; 1.762 ; 4.931       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  2138 ; 4.766 ;25.358       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  2137 ; 4.753 ;25.344       
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  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   765        A  1010                          
REMARK   3    RESIDUE RANGE :   A  1101        A  1104                          
REMARK   3    RESIDUE RANGE :   A  1201        A  1227                          
REMARK   3    ORIGIN FOR THE GROUP (A):   5.3590  37.2563  10.2977              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1404 T22:   0.1345                                     
REMARK   3      T33:   0.0335 T12:   0.0768                                     
REMARK   3      T13:   0.0567 T23:   0.0046                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3666 L22:   4.8228                                     
REMARK   3      L33:   1.8744 L12:   0.7058                                     
REMARK   3      L13:  -1.0878 L23:  -0.1958                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0781 S12:   0.1118 S13:  -0.0648                       
REMARK   3      S21:  -0.2827 S22:   0.0323 S23:  -0.1146                       
REMARK   3      S31:  -0.0404 S32:  -0.0426 S33:   0.0458                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.00                                          
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 5DS3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-SEP-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000213715.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-AUG-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 12.3.1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.12                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11207                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 13.80                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 11.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.71                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 13.90                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 3GJW                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.32                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20-25% PEG 3350, 0.2 M AMMONIUM          
REMARK 280  SULFATE, 0.1 M BIS-TRIS, PH 5.5, VAPOR DIFFUSION, SITTING DROP,     
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/6                                            
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       44.73233            
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       89.46467            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       67.09850            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      111.83083            
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       22.36617            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       44.73233            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       89.46467            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      111.83083            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       67.09850            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       22.36617            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   742                                                      
REMARK 465     GLY A   743                                                      
REMARK 465     SER A   744                                                      
REMARK 465     SER A   745                                                      
REMARK 465     HIS A   746                                                      
REMARK 465     HIS A   747                                                      
REMARK 465     HIS A   748                                                      
REMARK 465     HIS A   749                                                      
REMARK 465     HIS A   750                                                      
REMARK 465     HIS A   751                                                      
REMARK 465     SER A   752                                                      
REMARK 465     SER A   753                                                      
REMARK 465     GLY A   754                                                      
REMARK 465     LEU A   755                                                      
REMARK 465     VAL A   756                                                      
REMARK 465     PRO A   757                                                      
REMARK 465     ARG A   758                                                      
REMARK 465     GLY A   759                                                      
REMARK 465     SER A   760                                                      
REMARK 465     HIS A   761                                                      
REMARK 465     MET A   762                                                      
REMARK 465     THR A   763                                                      
REMARK 465     LYS A   764                                                      
REMARK 465     ALA A   823                                                      
REMARK 465     THR A   824                                                      
REMARK 465     THR A   825                                                      
REMARK 465     THR A  1011                                                      
REMARK 465     SER A  1012                                                      
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     SER A 781    CB   OG                                             
REMARK 470     SER A 783    CB   OG                                             
REMARK 470     SER A 785    CB   OG                                             
REMARK 470     LYS A 852    CG   CD   CE   NZ                                   
REMARK 470     GLN A 853    CG   CD   OE1  NE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 781     -150.31    -76.45                                   
REMARK 500    SER A 783      -91.22    102.08                                   
REMARK 500    ASP A 788       98.96     70.58                                   
REMARK 500    ASN A 827      156.79    179.52                                   
REMARK 500    ALA A 828      -73.21    109.17                                   
REMARK 500    HIS A 855      155.89    -39.64                                   
REMARK 500    ASN A 856       60.98     65.33                                   
REMARK 500    ASN A 856       60.98     65.78                                   
REMARK 500    PRO A 915       38.71    -91.02                                   
REMARK 500    ASP A 965     -123.94     51.92                                   
REMARK 500    ASN A 980      -71.41    -79.16                                   
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 1PE A 1101                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 09L A 1102                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1103                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1104                
DBREF  5DS3 A  788  1012  UNP    P09874   PARP1_HUMAN    788   1012             
SEQADV 5DS3 MET A  742  UNP  P09874              EXPRESSION TAG                 
SEQADV 5DS3 GLY A  743  UNP  P09874              EXPRESSION TAG                 
SEQADV 5DS3 SER A  744  UNP  P09874              EXPRESSION TAG                 
SEQADV 5DS3 SER A  745  UNP  P09874              EXPRESSION TAG                 
SEQADV 5DS3 HIS A  746  UNP  P09874              EXPRESSION TAG                 
SEQADV 5DS3 HIS A  747  UNP  P09874              EXPRESSION TAG                 
SEQADV 5DS3 HIS A  748  UNP  P09874              EXPRESSION TAG                 
SEQADV 5DS3 HIS A  749  UNP  P09874              EXPRESSION TAG                 
SEQADV 5DS3 HIS A  750  UNP  P09874              EXPRESSION TAG                 
SEQADV 5DS3 HIS A  751  UNP  P09874              EXPRESSION TAG                 
SEQADV 5DS3 SER A  752  UNP  P09874              EXPRESSION TAG                 
SEQADV 5DS3 SER A  753  UNP  P09874              EXPRESSION TAG                 
SEQADV 5DS3 GLY A  754  UNP  P09874              EXPRESSION TAG                 
SEQADV 5DS3 LEU A  755  UNP  P09874              EXPRESSION TAG                 
SEQADV 5DS3 VAL A  756  UNP  P09874              EXPRESSION TAG                 
SEQADV 5DS3 PRO A  757  UNP  P09874              EXPRESSION TAG                 
SEQADV 5DS3 ARG A  758  UNP  P09874              EXPRESSION TAG                 
SEQADV 5DS3 GLY A  759  UNP  P09874              EXPRESSION TAG                 
SEQADV 5DS3 SER A  760  UNP  P09874              EXPRESSION TAG                 
SEQADV 5DS3 HIS A  761  UNP  P09874              EXPRESSION TAG                 
SEQADV 5DS3 MET A  762  UNP  P09874              EXPRESSION TAG                 
SEQADV 5DS3 THR A  763  UNP  P09874              EXPRESSION TAG                 
SEQADV 5DS3 LYS A  764  UNP  P09874              EXPRESSION TAG                 
SEQADV 5DS3 SER A  765  UNP  P09874              EXPRESSION TAG                 
SEQADV 5DS3 LYS A  766  UNP  P09874              EXPRESSION TAG                 
SEQADV 5DS3 LEU A  767  UNP  P09874              EXPRESSION TAG                 
SEQADV 5DS3 PRO A  768  UNP  P09874              EXPRESSION TAG                 
SEQADV 5DS3 LYS A  769  UNP  P09874              EXPRESSION TAG                 
SEQADV 5DS3 PRO A  770  UNP  P09874              EXPRESSION TAG                 
SEQADV 5DS3 VAL A  771  UNP  P09874              EXPRESSION TAG                 
SEQADV 5DS3 GLN A  772  UNP  P09874              EXPRESSION TAG                 
SEQADV 5DS3 ASP A  773  UNP  P09874              EXPRESSION TAG                 
SEQADV 5DS3 LEU A  774  UNP  P09874              EXPRESSION TAG                 
SEQADV 5DS3 ILE A  775  UNP  P09874              EXPRESSION TAG                 
SEQADV 5DS3 LYS A  776  UNP  P09874              EXPRESSION TAG                 
SEQADV 5DS3 MET A  777  UNP  P09874              EXPRESSION TAG                 
SEQADV 5DS3 ILE A  778  UNP  P09874              EXPRESSION TAG                 
SEQADV 5DS3 PHE A  779  UNP  P09874              EXPRESSION TAG                 
SEQADV 5DS3 GLY A  780  UNP  P09874              EXPRESSION TAG                 
SEQADV 5DS3 SER A  781  UNP  P09874              EXPRESSION TAG                 
SEQADV 5DS3 GLY A  782  UNP  P09874              EXPRESSION TAG                 
SEQADV 5DS3 SER A  783  UNP  P09874              EXPRESSION TAG                 
SEQADV 5DS3 GLY A  784  UNP  P09874              EXPRESSION TAG                 
SEQADV 5DS3 SER A  785  UNP  P09874              EXPRESSION TAG                 
SEQADV 5DS3 GLY A  786  UNP  P09874              EXPRESSION TAG                 
SEQADV 5DS3 GLY A  787  UNP  P09874              EXPRESSION TAG                 
SEQRES   1 A  271  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  271  LEU VAL PRO ARG GLY SER HIS MET THR LYS SER LYS LEU          
SEQRES   3 A  271  PRO LYS PRO VAL GLN ASP LEU ILE LYS MET ILE PHE GLY          
SEQRES   4 A  271  SER GLY SER GLY SER GLY GLY ASP PRO ILE ASP VAL ASN          
SEQRES   5 A  271  TYR GLU LYS LEU LYS THR ASP ILE LYS VAL VAL ASP ARG          
SEQRES   6 A  271  ASP SER GLU GLU ALA GLU ILE ILE ARG LYS TYR VAL LYS          
SEQRES   7 A  271  ASN THR HIS ALA THR THR HIS ASN ALA TYR ASP LEU GLU          
SEQRES   8 A  271  VAL ILE ASP ILE PHE LYS ILE GLU ARG GLU GLY GLU CYS          
SEQRES   9 A  271  GLN ARG TYR LYS PRO PHE LYS GLN LEU HIS ASN ARG ARG          
SEQRES  10 A  271  LEU LEU TRP HIS GLY SER ARG THR THR ASN PHE ALA GLY          
SEQRES  11 A  271  ILE LEU SER GLN GLY LEU ARG ILE ALA PRO PRO GLU ALA          
SEQRES  12 A  271  PRO VAL THR GLY TYR MET PHE GLY LYS GLY ILE TYR PHE          
SEQRES  13 A  271  ALA ASP MET VAL SER LYS SER ALA ASN TYR CYS HIS THR          
SEQRES  14 A  271  SER GLN GLY ASP PRO ILE GLY LEU ILE LEU LEU GLY GLU          
SEQRES  15 A  271  VAL ALA LEU GLY ASN MET TYR GLU LEU LYS HIS ALA SER          
SEQRES  16 A  271  HIS ILE SER LYS LEU PRO LYS GLY LYS HIS SER VAL LYS          
SEQRES  17 A  271  GLY LEU GLY LYS THR THR PRO ASP PRO SER ALA ASN ILE          
SEQRES  18 A  271  SER LEU ASP GLY VAL ASP VAL PRO LEU GLY THR GLY ILE          
SEQRES  19 A  271  SER SER GLY VAL ASN ASP THR SER LEU LEU TYR ASN GLU          
SEQRES  20 A  271  TYR ILE VAL TYR ASP ILE ALA GLN VAL ASN LEU LYS TYR          
SEQRES  21 A  271  LEU LEU LYS LEU LYS PHE ASN PHE LYS THR SER                  
HET    1PE  A1101      16                                                       
HET    09L  A1102      32                                                       
HET    SO4  A1103       5                                                       
HET    SO4  A1104       5                                                       
HETNAM     1PE PENTAETHYLENE GLYCOL                                             
HETNAM     09L 4-(3-{[4-(CYCLOPROPYLCARBONYL)PIPERAZIN-1-YL]CARBONYL}-          
HETNAM   2 09L  4-FLUOROBENZYL)PHTHALAZIN-1(2H)-ONE                             
HETNAM     SO4 SULFATE ION                                                      
HETSYN     1PE PEG400                                                           
HETSYN     09L OLAPARIB                                                         
FORMUL   2  1PE    C10 H22 O6                                                   
FORMUL   3  09L    C24 H23 F N4 O3                                              
FORMUL   4  SO4    2(O4 S 2-)                                                   
FORMUL   6  HOH   *27(H2 O)                                                     
HELIX    1 AA1 PRO A  768  GLY A  780  1                                  13    
HELIX    2 AA2 PRO A  789  LYS A  796  1                                   8    
HELIX    3 AA3 SER A  808  THR A  821  1                                  14    
HELIX    4 AA4 GLY A  843  LYS A  849  1                                   7    
HELIX    5 AA5 PRO A  850  LYS A  852  5                                   3    
HELIX    6 AA6 ARG A  865  THR A  867  5                                   3    
HELIX    7 AA7 ASN A  868  GLY A  876  1                                   9    
HELIX    8 AA8 MET A  900  ASN A  906  1                                   7    
HELIX    9 AA9 TYR A  907  HIS A  909  5                                   3    
HELIX   10 AB1 PRO A  958  ASN A  961  5                                   4    
HELIX   11 AB2 ASP A  993  ALA A  995  5                                   3    
SHEET    1 AA1 5 THR A 799  VAL A 803  0                                        
SHEET    2 AA1 5 ASP A 830  ARG A 841 -1  O  LYS A 838   N  LYS A 802           
SHEET    3 AA1 5 VAL A 997  ASN A1008 -1  O  LYS A1006   N  GLU A 832           
SHEET    4 AA1 5 ILE A 916  ALA A 925 -1  N  ILE A 919   O  LEU A1003           
SHEET    5 AA1 5 ARG A 857  GLY A 863 -1  N  ARG A 858   O  VAL A 924           
SHEET    1 AA2 4 ILE A 895  PHE A 897  0                                        
SHEET    2 AA2 4 GLU A 988  VAL A 991 -1  O  TYR A 989   N  PHE A 897           
SHEET    3 AA2 4 SER A 947  GLY A 950 -1  N  GLY A 950   O  GLU A 988           
SHEET    4 AA2 4 MET A 929  LEU A 932  1  N  LEU A 932   O  LYS A 949           
SHEET    1 AA3 3 GLY A 974  SER A 976  0                                        
SHEET    2 AA3 3 GLY A 952  PRO A 956 -1  N  THR A 955   O  ILE A 975           
SHEET    3 AA3 3 LEU A 984  TYR A 986  1  O  LEU A 985   N  THR A 954           
SHEET    1 AA4 2 ILE A 962  LEU A 964  0                                        
SHEET    2 AA4 2 VAL A 967  VAL A 969 -1  O  VAL A 967   N  LEU A 964           
SSBOND   1 CYS A  845    CYS A  845                          1555   7555  2.06  
SITE     1 AC1  4 ARG A 865  ASN A 906  TYR A 907  HIS A 909                    
SITE     1 AC2 12 HIS A 862  GLY A 863  LEU A 877  ARG A 878                    
SITE     2 AC2 12 TYR A 889  GLY A 894  ILE A 895  TYR A 896                    
SITE     3 AC2 12 PHE A 897  SER A 904  TYR A 907  GLU A 988                    
SITE     1 AC3  4 LYS A 903  LEU A 984  LEU A 985  TYR A 986                    
SITE     1 AC4  3 ARG A 858  MET A 929  LYS A 949                               
CRYST1   93.405   93.405  134.197  90.00  90.00 120.00 P 61 2 2     12          
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      0.010706  0.006181  0.000000        0.00000                         
SCALE2      0.000000  0.012362  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007452        0.00000                         
ATOM      1  N   SER A 765      26.799  56.739  16.552  1.00 90.23           N  
ANISOU    1  N   SER A 765     8444   9430  16409  -2070    378  -2266       N  
ATOM      2  CA  SER A 765      26.238  55.363  16.406  1.00 86.07           C  
ANISOU    2  CA  SER A 765     8093   9225  15384  -1807    308  -2009       C  
ATOM      3  C   SER A 765      27.121  54.476  15.555  1.00 85.76           C  
ANISOU    3  C   SER A 765     7838   9234  15513  -1722    435  -1700       C  
ATOM      4  O   SER A 765      27.343  54.769  14.389  1.00 84.88           O  
ANISOU    4  O   SER A 765     7715   8873  15662  -1702    810  -1479       O  
ATOM      5  CB  SER A 765      24.861  55.417  15.760  1.00 82.68           C  
ANISOU    5  CB  SER A 765     8055   8702  14655  -1607    556  -1831       C  
ATOM      6  OG  SER A 765      24.428  54.118  15.389  1.00 79.28           O  
ANISOU    6  OG  SER A 765     7761   8522  13839  -1376    549  -1565       O  
ATOM      7  N   LYS A 766      27.593  53.379  16.134  1.00 86.94           N  
ANISOU    7  N   LYS A 766     7827   9701  15505  -1665    141  -1673       N  
ATOM      8  CA  LYS A 766      28.401  52.396  15.403  1.00 88.71           C  
ANISOU    8  CA  LYS A 766     7833   9976  15897  -1557    263  -1396       C  
ATOM      9  C   LYS A 766      27.534  51.455  14.529  1.00 83.52           C  
ANISOU    9  C   LYS A 766     7479   9379  14874  -1292    500  -1107       C  
ATOM     10  O   LYS A 766      28.036  50.839  13.587  1.00 83.90           O  
ANISOU   10  O   LYS A 766     7426   9377  15072  -1201    753   -882       O  
ATOM     11  CB  LYS A 766      29.309  51.627  16.394  1.00 93.45           C  
ANISOU   11  CB  LYS A 766     8095  10861  16551  -1598   -161  -1465       C  
ATOM     12  CG  LYS A 766      29.556  50.136  16.139  1.00 94.23           C  
ANISOU   12  CG  LYS A 766     8106  11153  16544  -1380   -185  -1189       C  
ATOM     13  CD  LYS A 766      28.305  49.273  16.373  1.00 91.87           C  
ANISOU   13  CD  LYS A 766     8190  11063  15654  -1165   -259  -1090       C  
ATOM     14  CE  LYS A 766      28.579  48.034  17.221  1.00 93.23           C  
ANISOU   14  CE  LYS A 766     8220  11548  15655  -1056   -625   -992       C  
ATOM     15  NZ  LYS A 766      29.781  47.265  16.790  1.00 95.63           N  
ANISOU   15  NZ  LYS A 766     8124  11824  16385  -1000   -578   -803       N  
ATOM     16  N   LEU A 767      26.240  51.358  14.834  1.00 78.61           N  
ANISOU   16  N   LEU A 767     7218   8860  13790  -1180    430  -1136       N  
ATOM     17  CA  LEU A 767      25.317  50.464  14.116  1.00 73.49           C  
ANISOU   17  CA  LEU A 767     6856   8289  12777   -949    599   -902       C  
ATOM     18  C   LEU A 767      25.359  50.604  12.588  1.00 71.20           C  
ANISOU   18  C   LEU A 767     6647   7781  12624   -893   1043   -667       C  
ATOM     19  O   LEU A 767      25.553  51.694  12.072  1.00 72.65           O  
ANISOU   19  O   LEU A 767     6815   7708  13077  -1010   1260   -669       O  
ATOM     20  CB  LEU A 767      23.870  50.702  14.586  1.00 71.37           C  
ANISOU   20  CB  LEU A 767     6941   8084  12090   -878    511   -992       C  
ATOM     21  CG  LEU A 767      23.500  50.238  16.002  1.00 70.77           C  
ANISOU   21  CG  LEU A 767     6899   8296  11691   -874    123  -1165       C  
ATOM     22  CD1 LEU A 767      22.094  50.696  16.358  1.00 68.15           C  
ANISOU   22  CD1 LEU A 767     6896   7964  11033   -826    130  -1275       C  
ATOM     23  CD2 LEU A 767      23.644  48.726  16.143  1.00 69.07           C  
ANISOU   23  CD2 LEU A 767     6632   8331  11278   -719    -11   -982       C  
ATOM     24  N   PRO A 768      25.150  49.496  11.858  1.00 68.02           N  
ANISOU   24  N   PRO A 768     6345   7479  12020   -720   1186   -465       N  
ATOM     25  CA  PRO A 768      25.149  49.583  10.392  1.00 67.39           C  
ANISOU   25  CA  PRO A 768     6381   7240  11981   -675   1607   -255       C  
ATOM     26  C   PRO A 768      24.023  50.452   9.854  1.00 65.62           C  
ANISOU   26  C   PRO A 768     6489   6887  11554   -655   1750   -188       C  
ATOM     27  O   PRO A 768      22.979  50.549  10.480  1.00 64.55           O  
ANISOU   27  O   PRO A 768     6548   6833  11145   -600   1548   -274       O  
ATOM     28  CB  PRO A 768      24.959  48.125   9.943  1.00 65.77           C  
ANISOU   28  CB  PRO A 768     6256   7209  11524   -495   1664   -128       C  
ATOM     29  CG  PRO A 768      25.302  47.282  11.133  1.00 65.78           C  
ANISOU   29  CG  PRO A 768     6055   7406  11531   -462   1304   -228       C  
ATOM     30  CD  PRO A 768      24.962  48.110  12.333  1.00 66.29           C  
ANISOU   30  CD  PRO A 768     6129   7513  11543   -570    983   -424       C  
ATOM     31  N   LYS A 769      24.226  51.055   8.690  1.00 66.70           N  
ANISOU   31  N   LYS A 769     6683   6828  11828   -693   2105    -11       N  
ATOM     32  CA  LYS A 769      23.251  51.998   8.143  1.00 66.92           C  
ANISOU   32  CA  LYS A 769     6989   6705  11733   -677   2234    104       C  
ATOM     33  C   LYS A 769      21.841  51.408   8.015  1.00 62.68           C  
ANISOU   33  C   LYS A 769     6774   6340  10700   -499   2127    171       C  
ATOM     34  O   LYS A 769      20.894  51.985   8.536  1.00 62.33           O  
ANISOU   34  O   LYS A 769     6866   6257  10559   -476   1978    100       O  
ATOM     35  CB  LYS A 769      23.735  52.591   6.809  1.00 70.41           C  
ANISOU   35  CB  LYS A 769     7456   6944  12351   -733   2649    353       C  
ATOM     36  CG  LYS A 769      22.701  53.429   6.059  1.00 71.48           C  
ANISOU   36  CG  LYS A 769     7894   6945  12320   -684   2789    566       C  
ATOM     37  CD  LYS A 769      23.349  54.200   4.910  1.00 75.68           C  
ANISOU   37  CD  LYS A 769     8414   7250  13091   -778   3193    824       C  
ATOM     38  CE  LYS A 769      22.325  54.826   3.964  1.00 76.28           C  
ANISOU   38  CE  LYS A 769     8812   7243  12926   -697   3335   1128       C  
ATOM     39  NZ  LYS A 769      21.283  55.627   4.673  1.00 75.50           N  
ANISOU   39  NZ  LYS A 769     8806   7019  12861   -658   3105   1056       N  
ATOM     40  N   PRO A 770      21.690  50.264   7.331  1.00 59.90           N  
ANISOU   40  N   PRO A 770     6529   6164  10065   -382   2213    286       N  
ATOM     41  CA  PRO A 770      20.345  49.685   7.252  1.00 56.38           C  
ANISOU   41  CA  PRO A 770     6358   5878   9183   -234   2088    326       C  
ATOM     42  C   PRO A 770      19.641  49.584   8.598  1.00 53.82           C  
ANISOU   42  C   PRO A 770     6036   5655   8757   -200   1749    129       C  
ATOM     43  O   PRO A 770      18.428  49.790   8.680  1.00 52.08           O  
ANISOU   43  O   PRO A 770     6017   5457   8313   -122   1662    147       O  
ATOM     44  CB  PRO A 770      20.604  48.288   6.691  1.00 55.81           C  
ANISOU   44  CB  PRO A 770     6300   5980   8923   -150   2177    369       C  
ATOM     45  CG  PRO A 770      21.834  48.449   5.854  1.00 58.54           C  
ANISOU   45  CG  PRO A 770     6496   6210   9533   -236   2500    459       C  
ATOM     46  CD  PRO A 770      22.658  49.530   6.494  1.00 60.85           C  
ANISOU   46  CD  PRO A 770     6539   6315  10266   -384   2469    379       C  
ATOM     47  N   VAL A 771      20.396  49.267   9.644  1.00 53.80           N  
ANISOU   47  N   VAL A 771     5803   5724   8913   -261   1559    -48       N  
ATOM     48  CA  VAL A 771      19.822  49.123  10.975  1.00 52.28           C  
ANISOU   48  CA  VAL A 771     5620   5666   8578   -245   1247   -235       C  
ATOM     49  C   VAL A 771      19.419  50.493  11.490  1.00 53.70           C  
ANISOU   49  C   VAL A 771     5837   5676   8890   -337   1207   -370       C  
ATOM     50  O   VAL A 771      18.326  50.662  12.011  1.00 52.75           O  
ANISOU   50  O   VAL A 771     5876   5596   8567   -278   1097   -446       O  
ATOM     51  CB  VAL A 771      20.792  48.440  11.960  1.00 52.74           C  
ANISOU   51  CB  VAL A 771     5419   5871   8746   -293   1027   -359       C  
ATOM     52  CG1 VAL A 771      20.206  48.405  13.360  1.00 51.71           C  
ANISOU   52  CG1 VAL A 771     5329   5900   8418   -299    715   -544       C  
ATOM     53  CG2 VAL A 771      21.095  47.024  11.498  1.00 51.72           C  
ANISOU   53  CG2 VAL A 771     5250   5874   8527   -177   1080   -225       C  
ATOM     54  N   GLN A 772      20.285  51.482  11.319  1.00 56.66           N  
ANISOU   54  N   GLN A 772     6053   5835   9640   -483   1326   -405       N  
ATOM     55  CA  GLN A 772      19.941  52.853  11.694  1.00 58.38           C  
ANISOU   55  CA  GLN A 772     6299   5824  10058   -578   1339   -538       C  
ATOM     56  C   GLN A 772      18.706  53.364  10.959  1.00 58.07           C  
ANISOU   56  C   GLN A 772     6517   5654   9890   -462   1488   -362       C  
ATOM     57  O   GLN A 772      17.882  54.053  11.550  1.00 59.25           O  
ANISOU   57  O   GLN A 772     6754   5712  10045   -454   1420   -496       O  
ATOM     58  CB  GLN A 772      21.102  53.792  11.420  1.00 61.37           C  
ANISOU   58  CB  GLN A 772     6457   5949  10911   -759   1494   -562       C  
ATOM     59  CG  GLN A 772      22.365  53.475  12.201  1.00 62.88           C  
ANISOU   59  CG  GLN A 772     6337   6243  11312   -898   1315   -752       C  
ATOM     60  CD  GLN A 772      23.430  54.518  11.971  1.00 66.23           C  
ANISOU   60  CD  GLN A 772     6522   6385  12258  -1099   1470   -801       C  
ATOM     61  OE1 GLN A 772      24.584  54.204  11.694  1.00 67.30           O  
ANISOU   61  OE1 GLN A 772     6401   6524  12644  -1173   1534   -750       O  
ATOM     62  NE2 GLN A 772      23.035  55.776  12.054  1.00 68.15           N  
ANISOU   62  NE2 GLN A 772     6831   6351  12710  -1186   1558   -894       N  
ATOM     63  N   ASP A 773      18.580  53.031   9.675  1.00 58.23           N  
ANISOU   63  N   ASP A 773     6653   5673   9797   -373   1690    -66       N  
ATOM     64  CA  ASP A 773      17.415  53.442   8.876  1.00 58.14           C  
ANISOU   64  CA  ASP A 773     6877   5577   9637   -255   1794    153       C  
ATOM     65  C   ASP A 773      16.148  52.813   9.406  1.00 55.30           C  
ANISOU   65  C   ASP A 773     6664   5409   8935   -117   1593     84       C  
ATOM     66  O   ASP A 773      15.103  53.444   9.431  1.00 54.77           O  
ANISOU   66  O   ASP A 773     6711   5235   8862    -47   1583    119       O  
ATOM     67  CB  ASP A 773      17.579  53.045   7.409  1.00 58.87           C  
ANISOU   67  CB  ASP A 773     7079   5707   9582   -203   2017    469       C  
ATOM     68  CG  ASP A 773      18.726  53.778   6.719  1.00 62.70           C  
ANISOU   68  CG  ASP A 773     7441   5973  10409   -335   2289    597       C  
ATOM     69  OD1 ASP A 773      19.002  54.943   7.071  1.00 64.93           O  
ANISOU   69  OD1 ASP A 773     7617   5984  11066   -443   2338    536       O  
ATOM     70  OD2 ASP A 773      19.353  53.185   5.813  1.00 64.33           O  
ANISOU   70  OD2 ASP A 773     7652   6265  10523   -340   2478    749       O  
ATOM     71  N   LEU A 774      16.252  51.554   9.811  1.00 53.56           N  
ANISOU   71  N   LEU A 774     6423   5455   8470    -75   1452      1       N  
ATOM     72  CA  LEU A 774      15.127  50.828  10.395  1.00 51.81           C  
ANISOU   72  CA  LEU A 774     6318   5426   7940     40   1273    -67       C  
ATOM     73  C   LEU A 774      14.697  51.451  11.723  1.00 52.58           C  
ANISOU   73  C   LEU A 774     6383   5485   8108      0   1128   -328       C  
ATOM     74  O   LEU A 774      13.509  51.641  11.970  1.00 51.72           O  
ANISOU   74  O   LEU A 774     6390   5371   7887     86   1091   -348       O  
ATOM     75  CB  LEU A 774      15.515  49.371  10.609  1.00 50.28           C  
ANISOU   75  CB  LEU A 774     6078   5483   7543     75   1174    -91       C  
ATOM     76  CG  LEU A 774      14.507  48.455  11.279  1.00 48.34           C  
ANISOU   76  CG  LEU A 774     5924   5439   7002    177   1002   -153       C  
ATOM     77  CD1 LEU A 774      13.306  48.310  10.376  1.00 48.38           C  
ANISOU   77  CD1 LEU A 774     6115   5453   6815    291   1063     14       C  
ATOM     78  CD2 LEU A 774      15.121  47.096  11.565  1.00 47.34           C  
ANISOU   78  CD2 LEU A 774     5709   5503   6773    196    919   -163       C  
ATOM     79  N   ILE A 775      15.667  51.769  12.573  1.00 54.23           N  
ANISOU   79  N   ILE A 775     6426   5674   8504   -141   1051   -542       N  
ATOM     80  CA  ILE A 775      15.371  52.392  13.857  1.00 55.56           C  
ANISOU   80  CA  ILE A 775     6576   5824   8710   -213    923   -841       C  
ATOM     81  C   ILE A 775      14.613  53.685  13.622  1.00 56.32           C  
ANISOU   81  C   ILE A 775     6749   5625   9024   -201   1070   -853       C  
ATOM     82  O   ILE A 775      13.601  53.943  14.264  1.00 56.52           O  
ANISOU   82  O   ILE A 775     6865   5647   8963   -147   1035   -991       O  
ATOM     83  CB  ILE A 775      16.649  52.701  14.671  1.00 58.43           C  
ANISOU   83  CB  ILE A 775     6731   6192   9277   -402    808  -1076       C  
ATOM     84  CG1 ILE A 775      17.422  51.422  15.023  1.00 57.82           C  
ANISOU   84  CG1 ILE A 775     6538   6402   9028   -399    630  -1047       C  
ATOM     85  CG2 ILE A 775      16.305  53.438  15.960  1.00 60.64           C  
ANISOU   85  CG2 ILE A 775     7024   6455   9561   -500    692  -1428       C  
ATOM     86  CD1 ILE A 775      16.730  50.520  16.022  1.00 56.59           C  
ANISOU   86  CD1 ILE A 775     6477   6532   8491   -324    426  -1127       C  
ATOM     87  N   LYS A 776      15.104  54.496  12.695  1.00 58.25           N  
ANISOU   87  N   LYS A 776     6950   5606   9575   -248   1257   -693       N  
ATOM     88  CA  LYS A 776      14.443  55.760  12.359  1.00 60.68           C  
ANISOU   88  CA  LYS A 776     7314   5584  10156   -224   1414   -639       C  
ATOM     89  C   LYS A 776      13.012  55.530  11.901  1.00 58.04           C  
ANISOU   89  C   LYS A 776     7148   5292   9611    -27   1423   -442       C  
ATOM     90  O   LYS A 776      12.101  56.228  12.310  1.00 58.72           O  
ANISOU   90  O   LYS A 776     7272   5222   9816     27   1448   -537       O  
ATOM     91  CB  LYS A 776      15.206  56.492  11.254  1.00 64.18           C  
ANISOU   91  CB  LYS A 776     7698   5762  10922   -289   1631   -395       C  
ATOM     92  CG  LYS A 776      16.513  57.139  11.699  1.00 68.11           C  
ANISOU   92  CG  LYS A 776     7990   6095  11793   -507   1667   -606       C  
ATOM     93  CD  LYS A 776      17.360  57.583  10.508  1.00 71.13           C  
ANISOU   93  CD  LYS A 776     8307   6270  12449   -569   1910   -313       C  
ATOM     94  CE  LYS A 776      16.727  58.738   9.740  1.00 74.11           C  
ANISOU   94  CE  LYS A 776     8778   6290  13088   -514   2125    -64       C  
ATOM     95  NZ  LYS A 776      17.252  58.815   8.347  1.00 76.17           N  
ANISOU   95  NZ  LYS A 776     9068   6469  13405   -511   2364    344       N  
ATOM     96  N   MET A 777      12.843  54.529  11.050  1.00 56.26           N  
ANISOU   96  N   MET A 777     7006   5277   9094     72   1404   -186       N  
ATOM     97  CA  MET A 777      11.552  54.166  10.470  1.00 55.22           C  
ANISOU   97  CA  MET A 777     7014   5226   8740    245   1378     22       C  
ATOM     98  C   MET A 777      10.464  53.836  11.493  1.00 52.91           C  
ANISOU   98  C   MET A 777     6753   5054   8296    322   1249   -181       C  
ATOM     99  O   MET A 777       9.315  54.221  11.310  1.00 51.98           O  
ANISOU   99  O   MET A 777     6686   4843   8220    441   1266    -87       O  
ATOM    100  CB  MET A 777      11.750  52.976   9.515  1.00 54.72           C  
ANISOU  100  CB  MET A 777     7025   5407   8359    293   1363    240       C  
ATOM    101  CG  MET A 777      10.473  52.394   8.938  1.00 54.63           C  
ANISOU  101  CG  MET A 777     7143   5537   8076    444   1290    418       C  
ATOM    102  SD  MET A 777      10.764  51.544   7.377  1.00 55.97           S  
ANISOU  102  SD  MET A 777     7430   5876   7958    468   1355    713       S  
ATOM    103  CE  MET A 777      12.210  50.579   7.790  1.00 55.91           C  
ANISOU  103  CE  MET A 777     7316   6009   7918    357   1381    528       C  
ATOM    104  N   ILE A 778      10.823  53.129  12.559  1.00 52.15           N  
ANISOU  104  N   ILE A 778     6615   5165   8033    258   1126   -435       N  
ATOM    105  CA  ILE A 778       9.828  52.633  13.499  1.00 51.79           C  
ANISOU  105  CA  ILE A 778     6614   5280   7780    326   1028   -597       C  
ATOM    106  C   ILE A 778       9.675  53.469  14.769  1.00 54.02           C  
ANISOU  106  C   ILE A 778     6864   5459   8202    250   1041   -941       C  
ATOM    107  O   ILE A 778       8.836  53.162  15.613  1.00 52.94           O  
ANISOU  107  O   ILE A 778     6771   5446   7896    296   1003  -1094       O  
ATOM    108  CB  ILE A 778      10.072  51.150  13.839  1.00 50.63           C  
ANISOU  108  CB  ILE A 778     6479   5462   7293    332    889   -604       C  
ATOM    109  CG1 ILE A 778      11.215  50.970  14.834  1.00 51.64           C  
ANISOU  109  CG1 ILE A 778     6513   5702   7405    191    787   -827       C  
ATOM    110  CG2 ILE A 778      10.321  50.360  12.557  1.00 49.77           C  
ANISOU  110  CG2 ILE A 778     6405   5430   7075    387    912   -322       C  
ATOM    111  CD1 ILE A 778      11.727  49.545  14.896  1.00 50.48           C  
ANISOU  111  CD1 ILE A 778     6341   5820   7017    206    668   -743       C  
ATOM    112  N   PHE A 779      10.458  54.539  14.887  1.00 56.76           N  
ANISOU  112  N   PHE A 779     7134   5568   8864    124   1116  -1076       N  
ATOM    113  CA  PHE A 779      10.280  55.486  15.973  1.00 59.12           C  
ANISOU  113  CA  PHE A 779     7410   5715   9337     37   1161  -1436       C  
ATOM    114  C   PHE A 779       9.806  56.845  15.475  1.00 63.55           C  
ANISOU  114  C   PHE A 779     7951   5857  10335     77   1358  -1388       C  
ATOM    115  O   PHE A 779       8.869  57.394  16.044  1.00 67.11           O  
ANISOU  115  O   PHE A 779     8425   6178  10892    133   1443  -1563       O  
ATOM    116  CB  PHE A 779      11.567  55.603  16.785  1.00 59.92           C  
ANISOU  116  CB  PHE A 779     7418   5888   9461   -173   1058  -1722       C  
ATOM    117  CG  PHE A 779      11.800  54.439  17.707  1.00 57.62           C  
ANISOU  117  CG  PHE A 779     7145   5997   8750   -206    849  -1840       C  
ATOM    118  CD1 PHE A 779      11.131  54.358  18.919  1.00 57.69           C  
ANISOU  118  CD1 PHE A 779     7233   6159   8526   -220    805  -2119       C  
ATOM    119  CD2 PHE A 779      12.678  53.422  17.363  1.00 55.49           C  
ANISOU  119  CD2 PHE A 779     6813   5942   8329   -219    718  -1657       C  
ATOM    120  CE1 PHE A 779      11.329  53.289  19.773  1.00 56.65           C  
ANISOU  120  CE1 PHE A 779     7130   6400   7993   -248    615  -2177       C  
ATOM    121  CE2 PHE A 779      12.882  52.347  18.213  1.00 54.56           C  
ANISOU  121  CE2 PHE A 779     6699   6167   7861   -234    522  -1719       C  
ATOM    122  CZ  PHE A 779      12.205  52.281  19.419  1.00 55.40           C  
ANISOU  122  CZ  PHE A 779     6898   6436   7713   -250    461  -1960       C  
ATOM    123  N   GLY A 780      10.453  57.397  14.444  1.00 66.76           N  
ANISOU  123  N   GLY A 780     8309   6039  11016     50   1451  -1146       N  
ATOM    124  CA  GLY A 780      10.015  58.659  13.797  1.00 70.68           C  
ANISOU  124  CA  GLY A 780     8786   6112  11957    108   1643   -992       C  
ATOM    125  C   GLY A 780      10.000  59.912  14.673  1.00 76.23           C  
ANISOU  125  C   GLY A 780     9422   6476  13063      6   1771  -1364       C  
ATOM    126  O   GLY A 780       9.586  59.865  15.831  1.00 77.87           O  
ANISOU  126  O   GLY A 780     9650   6780  13156    -26   1737  -1741       O  
ATOM    127  N   SER A 781      10.414  61.047  14.110  1.00 81.07           N  
ANISOU  127  N   SER A 781     9964   6680  14157    -46   1941  -1259       N  
ATOM    128  CA  SER A 781      10.584  62.287  14.876  1.00 86.12           C  
ANISOU  128  CA  SER A 781    10524   6943  15255   -180   2084  -1641       C  
ATOM    129  C   SER A 781       9.285  63.005  15.215  1.00 90.10           C  
ANISOU  129  C   SER A 781    11045   7178  16011    -33   2230  -1741       C  
ATOM    130  O   SER A 781       8.250  62.361  15.409  1.00 87.74           O  
ANISOU  130  O   SER A 781    10813   7100  15421    128   2168  -1701       O  
ATOM    131  N   GLY A 782       9.364  64.338  15.331  1.00 96.11           N  
ANISOU  131  N   GLY A 782    11723   7440  17353    -98   2440  -1894       N  
ATOM    132  CA  GLY A 782       8.193  65.218  15.530  1.00100.77           C  
ANISOU  132  CA  GLY A 782    12289   7657  18340     52   2637  -1960       C  
ATOM    133  C   GLY A 782       7.415  65.137  16.848  1.00103.24           C  
ANISOU  133  C   GLY A 782    12639   8076  18511     54   2670  -2475       C  
ATOM    134  O   GLY A 782       6.765  64.123  17.132  1.00100.57           O  
ANISOU  134  O   GLY A 782    12378   8140  17693    159   2541  -2454       O  
ATOM    135  N   SER A 783       7.467  66.216  17.637  1.00110.21           N  
ANISOU  135  N   SER A 783    13468   8583  19823    -67   2869  -2942       N  
ATOM    136  CA  SER A 783       6.651  66.377  18.868  1.00113.73           C  
ANISOU  136  CA  SER A 783    13953   9041  20218    -65   2990  -3466       C  
ATOM    137  C   SER A 783       7.398  66.128  20.170  1.00115.38           C  
ANISOU  137  C   SER A 783    14233   9545  20062   -343   2889  -4083       C  
ATOM    138  O   SER A 783       7.950  67.055  20.783  1.00117.21           O  
ANISOU  138  O   SER A 783    14423   9489  20622   -555   3009  -4549       O  
ATOM    139  N   GLY A 784       7.343  64.870  20.608  1.00112.91           N  
ANISOU  139  N   GLY A 784    14024   9803  19071   -338   2666  -4083       N  
ATOM    140  CA  GLY A 784       8.328  64.279  21.512  1.00112.50           C  
ANISOU  140  CA  GLY A 784    14034  10168  18541   -588   2438  -4436       C  
ATOM    141  C   GLY A 784       9.136  63.315  20.658  1.00108.69           C  
ANISOU  141  C   GLY A 784    13527   9983  17786   -575   2179  -3966       C  
ATOM    142  O   GLY A 784       9.236  62.118  20.954  1.00103.61           O  
ANISOU  142  O   GLY A 784    12957   9828  16579   -565   1960  -3892       O  
ATOM    143  N   SER A 785       9.665  63.859  19.562  1.00109.83           N  
ANISOU  143  N   SER A 785    13567   9800  18361   -564   2239  -3632       N  
ATOM    144  CA  SER A 785      10.469  63.125  18.581  1.00106.90           C  
ANISOU  144  CA  SER A 785    13160   9622  17833   -553   2071  -3178       C  
ATOM    145  C   SER A 785      11.702  63.899  18.122  1.00108.80           C  
ANISOU  145  C   SER A 785    13264   9561  18510   -744   2117  -3168       C  
ATOM    146  O   SER A 785      12.607  63.318  17.514  1.00108.48           O  
ANISOU  146  O   SER A 785    13173   9700  18344   -794   1990  -2903       O  
ATOM    147  N   GLY A 786      11.732  65.209  18.380  1.00111.26           N  
ANISOU  147  N   GLY A 786    13505   9391  19376   -849   2326  -3451       N  
ATOM    148  CA  GLY A 786      12.979  65.966  18.380  1.00113.20           C  
ANISOU  148  CA  GLY A 786    13605   9376  20029  -1111   2355  -3635       C  
ATOM    149  C   GLY A 786      13.746  65.588  19.636  1.00112.93           C  
ANISOU  149  C   GLY A 786    13555   9696  19656  -1367   2117  -4178       C  
ATOM    150  O   GLY A 786      13.736  66.328  20.622  1.00115.92           O  
ANISOU  150  O   GLY A 786    13929   9919  20197  -1541   2174  -4736       O  
ATOM    151  N   GLY A 787      14.395  64.421  19.595  1.00108.06           N  
ANISOU  151  N   GLY A 787    12930   9560  18565  -1388   1846  -4010       N  
ATOM    152  CA  GLY A 787      15.050  63.820  20.767  1.00106.74           C  
ANISOU  152  CA  GLY A 787    12754   9831  17968  -1588   1553  -4420       C  
ATOM    153  C   GLY A 787      15.183  62.301  20.667  1.00100.45           C  
ANISOU  153  C   GLY A 787    12007   9581  16577  -1472   1295  -4109       C  
ATOM    154  O   GLY A 787      14.570  61.672  19.797  1.00 96.16           O  
ANISOU  154  O   GLY A 787    11538   9099  15897  -1230   1357  -3646       O  
ATOM    155  N   ASP A 788      15.981  61.723  21.571  1.00 98.82           N  
ANISOU  155  N   ASP A 788    11751   9763  16033  -1649    998  -4369       N  
ATOM    156  CA  ASP A 788      16.290  60.268  21.623  1.00 92.55           C  
ANISOU  156  CA  ASP A 788    10966   9477  14719  -1568    728  -4108       C  
ATOM    157  C   ASP A 788      17.183  59.778  20.485  1.00 87.32           C  
ANISOU  157  C   ASP A 788    10145   8799  14233  -1526    704  -3662       C  
ATOM    158  O   ASP A 788      16.695  59.519  19.386  1.00 83.14           O  
ANISOU  158  O   ASP A 788     9673   8157  13758  -1321    876  -3236       O  
ATOM    159  CB  ASP A 788      15.028  59.400  21.696  1.00 89.30           C  
ANISOU  159  CB  ASP A 788    10765   9309  13854  -1319    757  -3913       C  
ATOM    160  CG  ASP A 788      14.488  59.289  23.100  1.00 91.19           C  
ANISOU  160  CG  ASP A 788    11148   9820  13677  -1390    662  -4334       C  
ATOM    161  OD1 ASP A 788      13.919  60.285  23.598  1.00 93.87           O  
ANISOU  161  OD1 ASP A 788    11554   9909  14200  -1453    850  -4706       O  
ATOM    162  OD2 ASP A 788      14.640  58.206  23.701  1.00 89.92           O  
ANISOU  162  OD2 ASP A 788    11035  10115  13014  -1384    417  -4287       O  
ATOM    163  N   PRO A 789      18.494  59.635  20.751  1.00 86.48           N  
ANISOU  163  N   PRO A 789     9828   8820  14208  -1726    491  -3768       N  
ATOM    164  CA  PRO A 789      19.401  59.179  19.701  1.00 83.86           C  
ANISOU  164  CA  PRO A 789     9321   8463  14078  -1696    509  -3375       C  
ATOM    165  C   PRO A 789      19.201  57.720  19.303  1.00 79.00           C  
ANISOU  165  C   PRO A 789     8775   8203  13038  -1480    410  -2989       C  
ATOM    166  O   PRO A 789      18.506  56.964  19.984  1.00 77.05           O  
ANISOU  166  O   PRO A 789     8682   8269  12322  -1380    267  -3031       O  
ATOM    167  CB  PRO A 789      20.790  59.387  20.309  1.00 87.34           C  
ANISOU  167  CB  PRO A 789     9490   8976  14717  -1974    275  -3652       C  
ATOM    168  CG  PRO A 789      20.569  59.388  21.774  1.00 89.99           C  
ANISOU  168  CG  PRO A 789     9908   9592  14691  -2104     12  -4110       C  
ATOM    169  CD  PRO A 789      19.212  59.979  21.990  1.00 90.02           C  
ANISOU  169  CD  PRO A 789    10174   9418  14611  -2003    239  -4269       C  
ATOM    170  N   ILE A 790      19.838  57.351  18.197  1.00 76.87           N  
ANISOU  170  N   ILE A 790     8386   7863  12956  -1421    513  -2626       N  
ATOM    171  CA  ILE A 790      19.659  56.050  17.562  1.00 72.89           C  
ANISOU  171  CA  ILE A 790     7945   7606  12143  -1214    498  -2248       C  
ATOM    172  C   ILE A 790      19.914  54.908  18.544  1.00 71.34           C  
ANISOU  172  C   ILE A 790     7714   7847  11542  -1211    167  -2328       C  
ATOM    173  O   ILE A 790      19.056  54.057  18.745  1.00 69.27           O  
ANISOU  173  O   ILE A 790     7630   7810  10877  -1047    113  -2220       O  
ATOM    174  CB  ILE A 790      20.584  55.925  16.316  1.00 73.34           C  
ANISOU  174  CB  ILE A 790     7838   7516  12512  -1211    674  -1929       C  
ATOM    175  CG1 ILE A 790      20.147  56.906  15.210  1.00 73.94           C  
ANISOU  175  CG1 ILE A 790     8007   7194  12893  -1169   1019  -1734       C  
ATOM    176  CG2 ILE A 790      20.624  54.500  15.773  1.00 70.03           C  
ANISOU  176  CG2 ILE A 790     7445   7366  11796  -1035    640  -1616       C  
ATOM    177  CD1 ILE A 790      18.743  56.683  14.674  1.00 71.03           C  
ANISOU  177  CD1 ILE A 790     7914   6830  12245   -939   1137  -1512       C  
ATOM    178  N   ASP A 791      21.080  54.913  19.173  1.00 73.28           N  
ANISOU  178  N   ASP A 791     7719   8206  11916  -1396    -62  -2506       N  
ATOM    179  CA  ASP A 791      21.488  53.812  20.036  1.00 72.65           C  
ANISOU  179  CA  ASP A 791     7565   8540  11498  -1391   -402  -2510       C  
ATOM    180  C   ASP A 791      20.575  53.599  21.242  1.00 71.67           C  
ANISOU  180  C   ASP A 791     7662   8685  10882  -1375   -580  -2727       C  
ATOM    181  O   ASP A 791      20.433  52.472  21.710  1.00 70.49           O  
ANISOU  181  O   ASP A 791     7560   8867  10355  -1272   -770  -2586       O  
ATOM    182  CB  ASP A 791      22.926  54.025  20.514  1.00 76.93           C  
ANISOU  182  CB  ASP A 791     7772   9139  12318  -1614   -645  -2676       C  
ATOM    183  CG  ASP A 791      23.950  53.932  19.379  1.00 77.85           C  
ANISOU  183  CG  ASP A 791     7625   9057  12894  -1613   -476  -2416       C  
ATOM    184  OD1 ASP A 791      25.115  54.347  19.611  1.00 81.51           O  
ANISOU  184  OD1 ASP A 791     7778   9474  13716  -1815   -608  -2561       O  
ATOM    185  OD2 ASP A 791      23.602  53.442  18.272  1.00 74.58           O  
ANISOU  185  OD2 ASP A 791     7309   8546  12481  -1423   -210  -2082       O  
ATOM    186  N   VAL A 792      19.966  54.666  21.748  1.00 72.45           N  
ANISOU  186  N   VAL A 792     7894   8631  11002  -1478   -493  -3065       N  
ATOM    187  CA  VAL A 792      19.121  54.558  22.935  1.00 72.79           C  
ANISOU  187  CA  VAL A 792     8151   8926  10580  -1487   -616  -3317       C  
ATOM    188  C   VAL A 792      17.803  53.903  22.560  1.00 68.59           C  
ANISOU  188  C   VAL A 792     7861   8432   9768  -1232   -432  -3064       C  
ATOM    189  O   VAL A 792      17.296  53.059  23.299  1.00 67.36           O  
ANISOU  189  O   VAL A 792     7835   8602   9156  -1161   -569  -3035       O  
ATOM    190  CB  VAL A 792      18.882  55.930  23.601  1.00 76.37           C  
ANISOU  190  CB  VAL A 792     8664   9176  11177  -1684   -540  -3809       C  
ATOM    191  CG1 VAL A 792      17.880  55.822  24.743  1.00 77.12           C  
ANISOU  191  CG1 VAL A 792     9011   9517  10771  -1676   -583  -4071       C  
ATOM    192  CG2 VAL A 792      20.195  56.488  24.117  1.00 80.76           C  
ANISOU  192  CG2 VAL A 792     8969   9745  11969  -1969   -778  -4105       C  
ATOM    193  N   ASN A 793      17.265  54.297  21.406  1.00 66.59           N  
ANISOU  193  N   ASN A 793     7656   7849   9794  -1104   -131  -2865       N  
ATOM    194  CA  ASN A 793      16.063  53.668  20.844  1.00 63.10           C  
ANISOU  194  CA  ASN A 793     7401   7423   9151   -864     30  -2590       C  
ATOM    195  C   ASN A 793      16.286  52.219  20.470  1.00 60.01           C  
ANISOU  195  C   ASN A 793     6980   7284   8534   -728    -82  -2241       C  
ATOM    196  O   ASN A 793      15.377  51.404  20.575  1.00 57.93           O  
ANISOU  196  O   ASN A 793     6865   7185   7961   -578    -71  -2103       O  
ATOM    197  CB  ASN A 793      15.553  54.434  19.617  1.00 62.34           C  
ANISOU  197  CB  ASN A 793     7339   6934   9413   -769    333  -2420       C  
ATOM    198  CG  ASN A 793      14.766  55.679  19.991  1.00 65.19           C  
ANISOU  198  CG  ASN A 793     7791   7025   9950   -811    504  -2707       C  
ATOM    199  OD1 ASN A 793      14.617  56.018  21.169  1.00 67.72           O  
ANISOU  199  OD1 ASN A 793     8161   7447  10123   -929    423  -3085       O  
ATOM    200  ND2 ASN A 793      14.260  56.373  18.984  1.00 65.25           N  
ANISOU  200  ND2 ASN A 793     7824   6687  10280   -715    749  -2527       N  
ATOM    201  N   TYR A 794      17.494  51.899  20.027  1.00 60.38           N  
ANISOU  201  N   TYR A 794     6820   7341   8779   -781   -169  -2106       N  
ATOM    202  CA  TYR A 794      17.832  50.528  19.686  1.00 58.63           C  
ANISOU  202  CA  TYR A 794     6539   7324   8412   -657   -260  -1800       C  
ATOM    203  C   TYR A 794      17.794  49.646  20.925  1.00 59.29           C  
ANISOU  203  C   TYR A 794     6650   7778   8098   -660   -541  -1849       C  
ATOM    204  O   TYR A 794      17.131  48.617  20.942  1.00 56.68           O  
ANISOU  204  O   TYR A 794     6435   7604   7495   -507   -543  -1652       O  
ATOM    205  CB  TYR A 794      19.212  50.471  19.039  1.00 59.85           C  
ANISOU  205  CB  TYR A 794     6429   7389   8921   -727   -271  -1685       C  
ATOM    206  CG  TYR A 794      19.716  49.075  18.817  1.00 58.56           C  
ANISOU  206  CG  TYR A 794     6160   7419   8670   -612   -369  -1415       C  
ATOM    207  CD1 TYR A 794      19.305  48.338  17.718  1.00 55.85           C  
ANISOU  207  CD1 TYR A 794     5901   7009   8307   -439   -161  -1139       C  
ATOM    208  CD2 TYR A 794      20.600  48.487  19.711  1.00 60.90           C  
ANISOU  208  CD2 TYR A 794     6265   7960   8913   -677   -677  -1441       C  
ATOM    209  CE1 TYR A 794      19.770  47.050  17.508  1.00 55.23           C  
ANISOU  209  CE1 TYR A 794     5720   7067   8196   -335   -219   -922       C  
ATOM    210  CE2 TYR A 794      21.071  47.201  19.511  1.00 60.12           C  
ANISOU  210  CE2 TYR A 794     6044   7997   8799   -555   -752  -1176       C  
ATOM    211  CZ  TYR A 794      20.651  46.490  18.409  1.00 56.99           C  
ANISOU  211  CZ  TYR A 794     5737   7495   8421   -384   -503   -932       C  
ATOM    212  OH  TYR A 794      21.113  45.221  18.213  1.00 56.14           O  
ANISOU  212  OH  TYR A 794     5506   7482   8342   -265   -547   -702       O  
ATOM    213  N   GLU A 795      18.499  50.067  21.963  1.00 63.40           N  
ANISOU  213  N   GLU A 795     7066   8438   8584   -844   -782  -2109       N  
ATOM    214  CA  GLU A 795      18.513  49.334  23.225  1.00 66.20           C  
ANISOU  214  CA  GLU A 795     7457   9176   8516   -870  -1077  -2151       C  
ATOM    215  C   GLU A 795      17.090  49.179  23.767  1.00 64.29           C  
ANISOU  215  C   GLU A 795     7509   9041   7876   -781   -970  -2208       C  
ATOM    216  O   GLU A 795      16.789  48.223  24.467  1.00 64.14           O  
ANISOU  216  O   GLU A 795     7573   9314   7482   -716  -1111  -2082       O  
ATOM    217  CB  GLU A 795      19.464  50.018  24.227  1.00 72.00           C  
ANISOU  217  CB  GLU A 795     8046  10045   9266  -1118  -1363  -2475       C  
ATOM    218  CG  GLU A 795      19.204  49.726  25.690  1.00 76.03           C  
ANISOU  218  CG  GLU A 795     8687  10947   9251  -1198  -1633  -2641       C  
ATOM    219  CD  GLU A 795      18.023  50.522  26.222  1.00 78.76           C  
ANISOU  219  CD  GLU A 795     9314  11246   9364  -1240  -1439  -2966       C  
ATOM    220  OE1 GLU A 795      18.063  51.775  26.141  1.00 82.33           O  
ANISOU  220  OE1 GLU A 795     9755  11441  10083  -1383  -1311  -3304       O  
ATOM    221  OE2 GLU A 795      17.049  49.899  26.712  1.00 78.79           O  
ANISOU  221  OE2 GLU A 795     9536  11442   8956  -1129  -1389  -2882       O  
ATOM    222  N   LYS A 796      16.216  50.111  23.412  1.00 63.26           N  
ANISOU  222  N   LYS A 796     7516   8654   7865   -770   -702  -2371       N  
ATOM    223  CA  LYS A 796      14.798  50.055  23.783  1.00 62.02           C  
ANISOU  223  CA  LYS A 796     7601   8538   7425   -671   -542  -2424       C  
ATOM    224  C   LYS A 796      14.041  48.850  23.238  1.00 57.62           C  
ANISOU  224  C   LYS A 796     7124   8050   6719   -456   -456  -2060       C  
ATOM    225  O   LYS A 796      13.019  48.452  23.786  1.00 56.88           O  
ANISOU  225  O   LYS A 796     7193   8093   6324   -385   -396  -2060       O  
ATOM    226  CB  LYS A 796      14.105  51.305  23.262  1.00 62.61           C  
ANISOU  226  CB  LYS A 796     7742   8251   7795   -673   -258  -2608       C  
ATOM    227  CG  LYS A 796      12.906  51.755  24.061  1.00 63.90           C  
ANISOU  227  CG  LYS A 796     8100   8435   7740   -667   -115  -2865       C  
ATOM    228  CD  LYS A 796      12.594  53.212  23.751  1.00 65.96           C  
ANISOU  228  CD  LYS A 796     8363   8308   8391   -722    115  -3124       C  
ATOM    229  CE  LYS A 796      13.694  54.150  24.227  1.00 69.60           C  
ANISOU  229  CE  LYS A 796     8706   8693   9044   -966     -3  -3469       C  
ATOM    230  NZ  LYS A 796      13.219  55.555  24.217  1.00 72.13           N  
ANISOU  230  NZ  LYS A 796     9059   8638   9707  -1029    244  -3789       N  
ATOM    231  N   LEU A 797      14.527  48.300  22.136  1.00 55.36           N  
ANISOU  231  N   LEU A 797     6718   7652   6661   -363   -426  -1772       N  
ATOM    232  CA  LEU A 797      13.891  47.161  21.480  1.00 52.17           C  
ANISOU  232  CA  LEU A 797     6375   7280   6168   -177   -338  -1456       C  
ATOM    233  C   LEU A 797      14.183  45.814  22.155  1.00 52.34           C  
ANISOU  233  C   LEU A 797     6368   7597   5920   -133   -541  -1269       C  
ATOM    234  O   LEU A 797      13.528  44.814  21.851  1.00 49.36           O  
ANISOU  234  O   LEU A 797     6058   7258   5436      4   -471  -1046       O  
ATOM    235  CB  LEU A 797      14.341  47.100  20.013  1.00 50.27           C  
ANISOU  235  CB  LEU A 797     6033   6809   6255   -111   -205  -1251       C  
ATOM    236  CG  LEU A 797      14.004  48.316  19.148  1.00 50.32           C  
ANISOU  236  CG  LEU A 797     6074   6507   6539   -124     11  -1325       C  
ATOM    237  CD1 LEU A 797      14.618  48.196  17.763  1.00 49.31           C  
ANISOU  237  CD1 LEU A 797     5854   6208   6672    -81    134  -1105       C  
ATOM    238  CD2 LEU A 797      12.493  48.491  19.039  1.00 49.30           C  
ANISOU  238  CD2 LEU A 797     6122   6313   6295    -14    166  -1326       C  
ATOM    239  N   LYS A 798      15.181  45.783  23.044  1.00 55.89           N  
ANISOU  239  N   LYS A 798     6704   8244   6286   -254   -802  -1348       N  
ATOM    240  CA  LYS A 798      15.565  44.565  23.755  1.00 56.39           C  
ANISOU  240  CA  LYS A 798     6719   8590   6117   -213  -1030  -1133       C  
ATOM    241  C   LYS A 798      15.742  43.418  22.765  1.00 53.67           C  
ANISOU  241  C   LYS A 798     6279   8145   5967    -50   -952   -793       C  
ATOM    242  O   LYS A 798      15.307  42.302  23.011  1.00 52.30           O  
ANISOU  242  O   LYS A 798     6162   8091   5617     58   -971   -572       O  
ATOM    243  CB  LYS A 798      14.491  44.215  24.784  1.00 57.41           C  
ANISOU  243  CB  LYS A 798     7067   8942   5801   -192  -1027  -1157       C  
ATOM    244  CG  LYS A 798      14.030  45.377  25.649  1.00 59.66           C  
ANISOU  244  CG  LYS A 798     7496   9286   5883   -337   -999  -1541       C  
ATOM    245  CD  LYS A 798      15.172  45.932  26.474  1.00 63.91           C  
ANISOU  245  CD  LYS A 798     7922   9998   6360   -533  -1291  -1756       C  
ATOM    246  CE  LYS A 798      14.697  46.907  27.548  1.00 66.90           C  
ANISOU  246  CE  LYS A 798     8476  10499   6442   -695  -1279  -2170       C  
ATOM    247  NZ  LYS A 798      15.879  47.531  28.209  1.00 70.87           N  
ANISOU  247  NZ  LYS A 798     8845  11143   6938   -913  -1581  -2421       N  
ATOM    248  N   THR A 799      16.381  43.728  21.641  1.00 53.55           N  
ANISOU  248  N   THR A 799     6125   7896   6325    -44   -838   -768       N  
ATOM    249  CA  THR A 799      16.458  42.850  20.457  1.00 52.18           C  
ANISOU  249  CA  THR A 799     5895   7573   6359     95   -677   -522       C  
ATOM    250  C   THR A 799      17.872  42.992  19.868  1.00 53.87           C  
ANISOU  250  C   THR A 799     5847   7678   6943     47   -706   -488       C  
ATOM    251  O   THR A 799      18.444  44.086  19.866  1.00 55.50           O  
ANISOU  251  O   THR A 799     5966   7801   7318    -87   -724   -675       O  
ATOM    252  CB  THR A 799      15.391  43.260  19.378  1.00 49.34           C  
ANISOU  252  CB  THR A 799     5705   6998   6040    161   -387   -545       C  
ATOM    253  OG1 THR A 799      14.069  43.122  19.903  1.00 47.95           O  
ANISOU  253  OG1 THR A 799     5730   6909   5580    208   -346   -575       O  
ATOM    254  CG2 THR A 799      15.470  42.422  18.112  1.00 47.51           C  
ANISOU  254  CG2 THR A 799     5442   6634   5975    275   -219   -343       C  
ATOM    255  N   ASP A 800      18.447  41.886  19.403  1.00 54.44           N  
ANISOU  255  N   ASP A 800     5776   7733   7175    150   -694   -261       N  
ATOM    256  CA  ASP A 800      19.688  41.940  18.631  1.00 56.09           C  
ANISOU  256  CA  ASP A 800     5732   7798   7781    129   -631   -216       C  
ATOM    257  C   ASP A 800      19.275  41.983  17.173  1.00 52.99           C  
ANISOU  257  C   ASP A 800     5448   7177   7507    195   -287   -179       C  
ATOM    258  O   ASP A 800      18.472  41.166  16.738  1.00 50.74           O  
ANISOU  258  O   ASP A 800     5311   6879   7087    313   -166    -71       O  
ATOM    259  CB  ASP A 800      20.566  40.714  18.892  1.00 58.70           C  
ANISOU  259  CB  ASP A 800     5827   8210   8265    216   -777      5       C  
ATOM    260  CG  ASP A 800      21.959  40.843  18.263  1.00 62.55           C  
ANISOU  260  CG  ASP A 800     5995   8561   9207    181   -725     29       C  
ATOM    261  OD1 ASP A 800      22.820  41.530  18.853  1.00 66.98           O  
ANISOU  261  OD1 ASP A 800     6354   9190   9905     48   -935    -74       O  
ATOM    262  OD2 ASP A 800      22.208  40.255  17.184  1.00 62.33           O  
ANISOU  262  OD2 ASP A 800     5909   8361   9412    276   -464    135       O  
ATOM    263  N   ILE A 801      19.808  42.937  16.419  1.00 53.16           N  
ANISOU  263  N   ILE A 801     5401   7026   7771    109   -132   -265       N  
ATOM    264  CA  ILE A 801      19.481  43.062  15.000  1.00 51.25           C  
ANISOU  264  CA  ILE A 801     5275   6595   7600    156    189   -210       C  
ATOM    265  C   ILE A 801      20.772  43.028  14.193  1.00 53.21           C  
ANISOU  265  C   ILE A 801     5286   6711   8218    126    348   -152       C  
ATOM    266  O   ILE A 801      21.680  43.803  14.448  1.00 55.18           O  
ANISOU  266  O   ILE A 801     5338   6913   8716      4    288   -234       O  
ATOM    267  CB  ILE A 801      18.684  44.351  14.717  1.00 49.97           C  
ANISOU  267  CB  ILE A 801     5304   6322   7357     91    295   -327       C  
ATOM    268  CG1 ILE A 801      17.532  44.482  15.718  1.00 48.82           C  
ANISOU  268  CG1 ILE A 801     5338   6307   6902    106    138   -424       C  
ATOM    269  CG2 ILE A 801      18.140  44.362  13.292  1.00 48.29           C  
ANISOU  269  CG2 ILE A 801     5254   5971   7121    157    580   -220       C  
ATOM    270  CD1 ILE A 801      16.633  45.668  15.462  1.00 48.25           C  
ANISOU  270  CD1 ILE A 801     5439   6101   6790     73    253   -528       C  
ATOM    271  N   LYS A 802      20.855  42.089  13.251  1.00 53.60           N  
ANISOU  271  N   LYS A 802     5344   6701   8319    230    558    -29       N  
ATOM    272  CA  LYS A 802      21.987  41.991  12.329  1.00 55.56           C  
ANISOU  272  CA  LYS A 802     5393   6811   8906    215    795     19       C  
ATOM    273  C   LYS A 802      21.481  41.972  10.903  1.00 53.05           C  
ANISOU  273  C   LYS A 802     5294   6384   8477    251   1139     59       C  
ATOM    274  O   LYS A 802      20.433  41.409  10.626  1.00 51.72           O  
ANISOU  274  O   LYS A 802     5359   6267   8023    334   1164     82       O  
ATOM    275  CB  LYS A 802      22.771  40.709  12.566  1.00 58.18           C  
ANISOU  275  CB  LYS A 802     5483   7176   9446    311    746    118       C  
ATOM    276  CG  LYS A 802      23.495  40.637  13.892  1.00 62.13           C  
ANISOU  276  CG  LYS A 802     5715   7804  10088    277    386    129       C  
ATOM    277  CD  LYS A 802      24.390  39.406  13.927  1.00 66.05           C  
ANISOU  277  CD  LYS A 802     5925   8281  10889    391    379    275       C  
ATOM    278  CE  LYS A 802      24.605  38.896  15.347  1.00 69.22           C  
ANISOU  278  CE  LYS A 802     6166   8875  11256    421    -39    370       C  
ATOM    279  NZ  LYS A 802      25.101  39.963  16.267  1.00 72.15           N  
ANISOU  279  NZ  LYS A 802     6400   9369  11642    258   -341    257       N  
ATOM    280  N   VAL A 803      22.239  42.573  10.000  1.00 53.49           N  
ANISOU  280  N   VAL A 803     5269   6301   8753    178   1401     73       N  
ATOM    281  CA  VAL A 803      21.913  42.530   8.585  1.00 52.45           C  
ANISOU  281  CA  VAL A 803     5344   6095   8489    199   1741    129       C  
ATOM    282  C   VAL A 803      22.332  41.187   8.006  1.00 52.87           C  
ANISOU  282  C   VAL A 803     5330   6145   8613    294   1928    150       C  
ATOM    283  O   VAL A 803      23.490  40.781   8.112  1.00 55.26           O  
ANISOU  283  O   VAL A 803     5335   6387   9273    298   1997    157       O  
ATOM    284  CB  VAL A 803      22.604  43.657   7.793  1.00 53.71           C  
ANISOU  284  CB  VAL A 803     5453   6105   8849     81   1999    163       C  
ATOM    285  CG1 VAL A 803      22.258  43.558   6.311  1.00 53.69           C  
ANISOU  285  CG1 VAL A 803     5693   6070   8633    100   2347    246       C  
ATOM    286  CG2 VAL A 803      22.187  45.010   8.346  1.00 53.58           C  
ANISOU  286  CG2 VAL A 803     5495   6040   8823    -13   1839    127       C  
ATOM    287  N   VAL A 804      21.375  40.500   7.401  1.00 51.15           N  
ANISOU  287  N   VAL A 804     5372   5978   8084    367   2010    148       N  
ATOM    288  CA  VAL A 804      21.656  39.303   6.638  1.00 51.42           C  
ANISOU  288  CA  VAL A 804     5398   5978   8160    439   2254    124       C  
ATOM    289  C   VAL A 804      22.332  39.746   5.348  1.00 54.45           C  
ANISOU  289  C   VAL A 804     5807   6273   8609    368   2652    130       C  
ATOM    290  O   VAL A 804      21.804  40.575   4.611  1.00 53.60           O  
ANISOU  290  O   VAL A 804     5935   6183   8245    304   2757    172       O  
ATOM    291  CB  VAL A 804      20.362  38.533   6.326  1.00 49.08           C  
ANISOU  291  CB  VAL A 804     5387   5763   7496    504   2217     86       C  
ATOM    292  CG1 VAL A 804      20.619  37.387   5.366  1.00 50.71           C  
ANISOU  292  CG1 VAL A 804     5623   5913   7730    550   2518      9       C  
ATOM    293  CG2 VAL A 804      19.738  38.020   7.610  1.00 47.30           C  
ANISOU  293  CG2 VAL A 804     5124   5616   7230    572   1872    101       C  
ATOM    294  N   ASP A 805      23.515  39.206   5.094  1.00 58.77           N  
ANISOU  294  N   ASP A 805     6096   6720   9514    384   2882    109       N  
ATOM    295  CA  ASP A 805      24.244  39.503   3.873  1.00 63.10           C  
ANISOU  295  CA  ASP A 805     6649   7184  10142    317   3321    108       C  
ATOM    296  C   ASP A 805      23.394  39.161   2.646  1.00 63.61           C  
ANISOU  296  C   ASP A 805     7095   7321   9750    316   3556     60       C  
ATOM    297  O   ASP A 805      22.830  38.073   2.558  1.00 61.99           O  
ANISOU  297  O   ASP A 805     7001   7158   9395    393   3532    -37       O  
ATOM    298  CB  ASP A 805      25.555  38.716   3.850  1.00 66.85           C  
ANISOU  298  CB  ASP A 805     6764   7533  11102    363   3543     68       C  
ATOM    299  CG  ASP A 805      26.502  39.186   2.764  1.00 71.99           C  
ANISOU  299  CG  ASP A 805     7345   8082  11924    276   4015     74       C  
ATOM    300  OD1 ASP A 805      26.202  40.194   2.096  1.00 73.56           O  
ANISOU  300  OD1 ASP A 805     7769   8308  11869    172   4147    141       O  
ATOM    301  OD2 ASP A 805      27.558  38.541   2.570  1.00 76.66           O  
ANISOU  301  OD2 ASP A 805     7646   8556  12925    316   4276     28       O  
ATOM    302  N   ARG A 806      23.306  40.099   1.706  1.00 66.23           N  
ANISOU  302  N   ARG A 806     7626   7670   9867    220   3771    137       N  
ATOM    303  CA  ARG A 806      22.534  39.896   0.483  1.00 69.03           C  
ANISOU  303  CA  ARG A 806     8354   8135   9736    198   3970    113       C  
ATOM    304  C   ARG A 806      22.948  38.623  -0.281  1.00 70.31           C  
ANISOU  304  C   ARG A 806     8527   8282   9903    231   4311    -64       C  
ATOM    305  O   ARG A 806      22.110  37.952  -0.874  1.00 69.12           O  
ANISOU  305  O   ARG A 806     8647   8238   9374    242   4329   -174       O  
ATOM    306  CB  ARG A 806      22.658  41.117  -0.437  1.00 74.01           C  
ANISOU  306  CB  ARG A 806     9150   8773  10197     87   4200    275       C  
ATOM    307  CG  ARG A 806      21.620  41.123  -1.557  1.00 78.25           C  
ANISOU  307  CG  ARG A 806    10108   9480  10142     59   4268    309       C  
ATOM    308  CD  ARG A 806      21.965  42.022  -2.745  1.00 84.06           C  
ANISOU  308  CD  ARG A 806    11021  10235  10682    -46   4620    482       C  
ATOM    309  NE  ARG A 806      21.348  41.501  -3.970  1.00 89.21           N  
ANISOU  309  NE  ARG A 806    12034  11081  10779    -76   4789    431       N  
ATOM    310  CZ  ARG A 806      20.040  41.538  -4.256  1.00 90.69           C  
ANISOU  310  CZ  ARG A 806    12516  11445  10495    -64   4518    478       C  
ATOM    311  NH1 ARG A 806      19.160  42.100  -3.423  1.00 88.76           N  
ANISOU  311  NH1 ARG A 806    12252  11191  10278    -10   4094    588       N  
ATOM    312  NH2 ARG A 806      19.603  41.009  -5.397  1.00 93.97           N  
ANISOU  312  NH2 ARG A 806    13240  12055  10407   -112   4675    400       N  
ATOM    313  N   ASP A 807      24.239  38.300  -0.250  1.00 72.16           N  
ANISOU  313  N   ASP A 807     8448   8371  10598    243   4580   -109       N  
ATOM    314  CA  ASP A 807      24.784  37.122  -0.937  1.00 74.18           C  
ANISOU  314  CA  ASP A 807     8660   8559  10963    282   4963   -298       C  
ATOM    315  C   ASP A 807      24.625  35.787  -0.207  1.00 70.26           C  
ANISOU  315  C   ASP A 807     8013   7992  10691    413   4789   -428       C  
ATOM    316  O   ASP A 807      24.985  34.751  -0.745  1.00 72.04           O  
ANISOU  316  O   ASP A 807     8206   8127  11037    454   5103   -607       O  
ATOM    317  CB  ASP A 807      26.267  37.346  -1.192  1.00 79.37           C  
ANISOU  317  CB  ASP A 807     8993   9061  12100    252   5352   -278       C  
ATOM    318  CG  ASP A 807      26.517  38.508  -2.115  1.00 84.03           C  
ANISOU  318  CG  ASP A 807     9745   9693  12486    115   5646   -151       C  
ATOM    319  OD1 ASP A 807      25.962  38.485  -3.234  1.00 87.70           O  
ANISOU  319  OD1 ASP A 807    10591  10292  12440     54   5877   -193       O  
ATOM    320  OD2 ASP A 807      27.262  39.442  -1.732  1.00 87.04           O  
ANISOU  320  OD2 ASP A 807     9876   9980  13215     58   5642     -5       O  
ATOM    321  N   SER A 808      24.104  35.806   1.011  1.00 65.19           N  
ANISOU  321  N   SER A 808     7278   7374  10115    475   4318   -338       N  
ATOM    322  CA  SER A 808      24.000  34.595   1.819  1.00 62.93           C  
ANISOU  322  CA  SER A 808     6826   7010  10075    602   4137   -395       C  
ATOM    323  C   SER A 808      22.984  33.621   1.236  1.00 61.79           C  
ANISOU  323  C   SER A 808     6980   6906   9591    617   4195   -570       C  
ATOM    324  O   SER A 808      22.146  33.997   0.418  1.00 60.29           O  
ANISOU  324  O   SER A 808     7141   6861   8904    530   4236   -623       O  
ATOM    325  CB  SER A 808      23.610  34.949   3.262  1.00 59.76           C  
ANISOU  325  CB  SER A 808     6301   6666   9738    643   3622   -239       C  
ATOM    326  OG  SER A 808      22.291  35.475   3.346  1.00 56.36           O  
ANISOU  326  OG  SER A 808     6190   6394   8829    599   3364   -212       O  
ATOM    327  N   GLU A 809      23.063  32.363   1.655  1.00 62.12           N  
ANISOU  327  N   GLU A 809     6869   6812   9919    725   4188   -652       N  
ATOM    328  CA  GLU A 809      22.038  31.408   1.278  1.00 61.92           C  
ANISOU  328  CA  GLU A 809     7095   6800   9630    730   4191   -827       C  
ATOM    329  C   GLU A 809      20.752  31.712   2.030  1.00 58.58           C  
ANISOU  329  C   GLU A 809     6838   6528   8889    723   3732   -718       C  
ATOM    330  O   GLU A 809      19.674  31.564   1.466  1.00 57.68           O  
ANISOU  330  O   GLU A 809     7025   6523   8366    661   3694   -833       O  
ATOM    331  CB  GLU A 809      22.472  29.958   1.503  1.00 63.60           C  
ANISOU  331  CB  GLU A 809     7089   6776  10299    847   4345   -940       C  
ATOM    332  CG  GLU A 809      21.612  28.992   0.697  1.00 64.38           C  
ANISOU  332  CG  GLU A 809     7467   6852  10141    806   4508  -1215       C  
ATOM    333  CD  GLU A 809      21.804  27.541   1.070  1.00 66.20           C  
ANISOU  333  CD  GLU A 809     7498   6814  10839    924   4602  -1310       C  
ATOM    334  OE1 GLU A 809      20.900  26.974   1.721  1.00 64.61           O  
ANISOU  334  OE1 GLU A 809     7345   6597  10604    958   4321  -1270       O  
ATOM    335  OE2 GLU A 809      22.845  26.962   0.701  1.00 69.49           O  
ANISOU  335  OE2 GLU A 809     7700   7017  11685    986   4980  -1419       O  
ATOM    336  N   GLU A 810      20.878  32.126   3.294  1.00 57.85           N  
ANISOU  336  N   GLU A 810     6541   6449   8987    780   3392   -510       N  
ATOM    337  CA  GLU A 810      19.753  32.656   4.084  1.00 56.17           C  
ANISOU  337  CA  GLU A 810     6469   6389   8484    766   2985   -397       C  
ATOM    338  C   GLU A 810      18.934  33.676   3.295  1.00 54.15           C  
ANISOU  338  C   GLU A 810     6527   6300   7745    656   2976   -414       C  
ATOM    339  O   GLU A 810      17.706  33.626   3.269  1.00 51.90           O  
ANISOU  339  O   GLU A 810     6459   6119   7140    635   2795   -439       O  
ATOM    340  CB  GLU A 810      20.269  33.373   5.343  1.00 58.10           C  
ANISOU  340  CB  GLU A 810     6470   6660   8944    797   2696   -199       C  
ATOM    341  CG  GLU A 810      20.383  32.556   6.630  1.00 59.94           C  
ANISOU  341  CG  GLU A 810     6476   6840   9456    906   2445    -83       C  
ATOM    342  CD  GLU A 810      20.698  33.448   7.846  1.00 61.09           C  
ANISOU  342  CD  GLU A 810     6458   7088   9664    896   2110     80       C  
ATOM    343  OE1 GLU A 810      21.715  34.201   7.802  1.00 63.19           O  
ANISOU  343  OE1 GLU A 810     6538   7335  10134    853   2166    109       O  
ATOM    344  OE2 GLU A 810      19.930  33.409   8.842  1.00 58.18           O  
ANISOU  344  OE2 GLU A 810     6146   6822   9138    918   1804    163       O  
ATOM    345  N   ALA A 811      19.641  34.626   2.691  1.00 54.72           N  
ANISOU  345  N   ALA A 811     6598   6387   7804    590   3164   -372       N  
ATOM    346  CA  ALA A 811      19.021  35.682   1.907  1.00 54.43           C  
ANISOU  346  CA  ALA A 811     6836   6488   7355    494   3176   -327       C  
ATOM    347  C   ALA A 811      18.339  35.134   0.665  1.00 55.52           C  
ANISOU  347  C   ALA A 811     7274   6714   7106    440   3358   -485       C  
ATOM    348  O   ALA A 811      17.249  35.563   0.316  1.00 55.13           O  
ANISOU  348  O   ALA A 811     7469   6811   6664    395   3191   -452       O  
ATOM    349  CB  ALA A 811      20.063  36.707   1.508  1.00 56.44           C  
ANISOU  349  CB  ALA A 811     6997   6701   7743    432   3394   -230       C  
ATOM    350  N   GLU A 812      19.001  34.198  -0.003  1.00 57.97           N  
ANISOU  350  N   GLU A 812     7551   6934   7541    440   3700   -666       N  
ATOM    351  CA  GLU A 812      18.443  33.528  -1.166  1.00 59.79           C  
ANISOU  351  CA  GLU A 812     8060   7246   7411    371   3892   -883       C  
ATOM    352  C   GLU A 812      17.167  32.751  -0.843  1.00 57.65           C  
ANISOU  352  C   GLU A 812     7901   7020   6981    385   3609   -984       C  
ATOM    353  O   GLU A 812      16.188  32.826  -1.578  1.00 57.85           O  
ANISOU  353  O   GLU A 812     8203   7213   6562    303   3530  -1057       O  
ATOM    354  CB  GLU A 812      19.460  32.561  -1.734  1.00 63.55           C  
ANISOU  354  CB  GLU A 812     8427   7564   8154    382   4331  -1099       C  
ATOM    355  CG  GLU A 812      19.062  32.015  -3.084  1.00 67.52           C  
ANISOU  355  CG  GLU A 812     9243   8169   8240    276   4602  -1366       C  
ATOM    356  CD  GLU A 812      19.232  33.031  -4.185  1.00 70.80           C  
ANISOU  356  CD  GLU A 812     9900   8771   8228    160   4809  -1291       C  
ATOM    357  OE1 GLU A 812      19.747  34.131  -3.895  1.00 70.73           O  
ANISOU  357  OE1 GLU A 812     9782   8760   8329    168   4782  -1033       O  
ATOM    358  OE2 GLU A 812      18.878  32.715  -5.346  1.00 75.17           O  
ANISOU  358  OE2 GLU A 812    10754   9469   8338     53   5009  -1491       O  
ATOM    359  N   ILE A 813      17.181  31.991   0.244  1.00 55.66           N  
ANISOU  359  N   ILE A 813     7426   6622   7099    485   3454   -974       N  
ATOM    360  CA  ILE A 813      15.993  31.246   0.651  1.00 53.70           C  
ANISOU  360  CA  ILE A 813     7252   6389   6762    496   3204  -1044       C  
ATOM    361  C   ILE A 813      14.834  32.195   0.901  1.00 50.49           C  
ANISOU  361  C   ILE A 813     6998   6175   6011    462   2855   -893       C  
ATOM    362  O   ILE A 813      13.718  31.948   0.457  1.00 50.08           O  
ANISOU  362  O   ILE A 813     7136   6231   5658    401   2731   -991       O  
ATOM    363  CB  ILE A 813      16.257  30.386   1.898  1.00 52.96           C  
ANISOU  363  CB  ILE A 813     6881   6106   7135    617   3091   -979       C  
ATOM    364  CG1 ILE A 813      17.183  29.231   1.529  1.00 56.24           C  
ANISOU  364  CG1 ILE A 813     7153   6295   7920    661   3443  -1157       C  
ATOM    365  CG2 ILE A 813      14.964  29.797   2.452  1.00 51.30           C  
ANISOU  365  CG2 ILE A 813     6738   5915   6835    621   2819   -992       C  
ATOM    366  CD1 ILE A 813      17.773  28.524   2.724  1.00 56.58           C  
ANISOU  366  CD1 ILE A 813     6870   6135   8491    802   3360  -1013       C  
ATOM    367  N   ILE A 814      15.111  33.293   1.588  1.00 48.46           N  
ANISOU  367  N   ILE A 814     6641   5948   5824    496   2705   -669       N  
ATOM    368  CA  ILE A 814      14.076  34.256   1.920  1.00 46.30           C  
ANISOU  368  CA  ILE A 814     6474   5813   5302    481   2401   -523       C  
ATOM    369  C   ILE A 814      13.535  34.970   0.674  1.00 47.99           C  
ANISOU  369  C   ILE A 814     6958   6193   5082    389   2443   -515       C  
ATOM    370  O   ILE A 814      12.334  35.129   0.527  1.00 48.33           O  
ANISOU  370  O   ILE A 814     7140   6358   4864    366   2222   -498       O  
ATOM    371  CB  ILE A 814      14.588  35.255   2.964  1.00 44.64           C  
ANISOU  371  CB  ILE A 814     6087   5568   5303    528   2262   -328       C  
ATOM    372  CG1 ILE A 814      14.825  34.525   4.292  1.00 43.35           C  
ANISOU  372  CG1 ILE A 814     5694   5307   5469    615   2123   -304       C  
ATOM    373  CG2 ILE A 814      13.593  36.389   3.143  1.00 43.32           C  
ANISOU  373  CG2 ILE A 814     6040   5514   4902    511   2020   -196       C  
ATOM    374  CD1 ILE A 814      15.747  35.236   5.255  1.00 43.18           C  
ANISOU  374  CD1 ILE A 814     5453   5243   5710    645   2041   -171       C  
ATOM    375  N   ARG A 815      14.408  35.385  -0.229  1.00 50.35           N  
ANISOU  375  N   ARG A 815     7320   6502   5305    337   2728   -510       N  
ATOM    376  CA  ARG A 815      13.961  36.027  -1.462  1.00 52.42           C  
ANISOU  376  CA  ARG A 815     7857   6942   5117    247   2781   -465       C  
ATOM    377  C   ARG A 815      13.123  35.093  -2.320  1.00 54.55           C  
ANISOU  377  C   ARG A 815     8337   7340   5050    176   2772   -686       C  
ATOM    378  O   ARG A 815      12.206  35.525  -3.007  1.00 55.73           O  
ANISOU  378  O   ARG A 815     8697   7680   4797    116   2613   -627       O  
ATOM    379  CB  ARG A 815      15.150  36.522  -2.278  1.00 54.93           C  
ANISOU  379  CB  ARG A 815     8205   7240   5425    195   3152   -422       C  
ATOM    380  CG  ARG A 815      15.774  37.793  -1.732  1.00 54.21           C  
ANISOU  380  CG  ARG A 815     7968   7064   5564    220   3134   -173       C  
ATOM    381  CD  ARG A 815      16.524  38.537  -2.814  1.00 56.76           C  
ANISOU  381  CD  ARG A 815     8412   7424   5731    138   3463    -64       C  
ATOM    382  NE  ARG A 815      17.595  37.704  -3.327  1.00 59.99           N  
ANISOU  382  NE  ARG A 815     8757   7761   6275    112   3867   -258       N  
ATOM    383  CZ  ARG A 815      18.797  37.564  -2.763  1.00 60.49           C  
ANISOU  383  CZ  ARG A 815     8522   7635   6826    151   4052   -282       C  
ATOM    384  NH1 ARG A 815      19.692  36.773  -3.330  1.00 62.33           N  
ANISOU  384  NH1 ARG A 815     8697   7796   7189    136   4445   -466       N  
ATOM    385  NH2 ARG A 815      19.113  38.208  -1.639  1.00 59.07           N  
ANISOU  385  NH2 ARG A 815     8091   7338   7012    203   3846   -136       N  
ATOM    386  N   LYS A 816      13.452  33.811  -2.291  1.00 56.14           N  
ANISOU  386  N   LYS A 816     8467   7427   5435    178   2938   -941       N  
ATOM    387  CA  LYS A 816      12.690  32.814  -3.027  1.00 58.68           C  
ANISOU  387  CA  LYS A 816     8963   7833   5496     93   2938  -1212       C  
ATOM    388  C   LYS A 816      11.315  32.669  -2.375  1.00 56.15           C  
ANISOU  388  C   LYS A 816     8624   7564   5145    111   2533  -1174       C  
ATOM    389  O   LYS A 816      10.304  32.527  -3.055  1.00 57.05           O  
ANISOU  389  O   LYS A 816     8918   7851   4907     21   2374  -1268       O  
ATOM    390  CB  LYS A 816      13.438  31.481  -3.031  1.00 61.30           C  
ANISOU  390  CB  LYS A 816     9182   7961   6146    105   3242  -1495       C  
ATOM    391  CG  LYS A 816      13.190  30.633  -4.263  1.00 66.98           C  
ANISOU  391  CG  LYS A 816    10136   8765   6548    -27   3446  -1843       C  
ATOM    392  CD  LYS A 816      14.128  29.426  -4.327  1.00 70.41           C  
ANISOU  392  CD  LYS A 816    10441   8946   7366     -4   3835  -2126       C  
ATOM    393  CE  LYS A 816      15.522  29.777  -4.838  1.00 73.04           C  
ANISOU  393  CE  LYS A 816    10735   9223   7793      7   4266  -2115       C  
ATOM    394  NZ  LYS A 816      15.678  29.539  -6.300  1.00 77.97           N  
ANISOU  394  NZ  LYS A 816    11650   9993   7980   -141   4611  -2403       N  
ATOM    395  N   TYR A 817      11.293  32.733  -1.048  1.00 52.93           N  
ANISOU  395  N   TYR A 817     7989   7019   5102    220   2367  -1030       N  
ATOM    396  CA  TYR A 817      10.056  32.621  -0.289  1.00 51.21           C  
ANISOU  396  CA  TYR A 817     7722   6828   4908    247   2031   -977       C  
ATOM    397  C   TYR A 817       9.132  33.765  -0.698  1.00 51.73           C  
ANISOU  397  C   TYR A 817     7928   7098   4627    216   1788   -802       C  
ATOM    398  O   TYR A 817       7.974  33.543  -1.018  1.00 51.81           O  
ANISOU  398  O   TYR A 817     8022   7228   4436    162   1579   -863       O  
ATOM    399  CB  TYR A 817      10.367  32.657   1.216  1.00 48.20           C  
ANISOU  399  CB  TYR A 817     7093   6290   4928    366   1936   -824       C  
ATOM    400  CG  TYR A 817       9.300  32.117   2.159  1.00 46.69           C  
ANISOU  400  CG  TYR A 817     6812   6066   4860    399   1696   -813       C  
ATOM    401  CD1 TYR A 817       8.011  31.800   1.722  1.00 47.54           C  
ANISOU  401  CD1 TYR A 817     7024   6276   4761    326   1529   -913       C  
ATOM    402  CD2 TYR A 817       9.573  31.976   3.520  1.00 44.70           C  
ANISOU  402  CD2 TYR A 817     6362   5697   4923    495   1626   -686       C  
ATOM    403  CE1 TYR A 817       7.047  31.332   2.609  1.00 45.95           C  
ANISOU  403  CE1 TYR A 817     6717   6031   4710    350   1343   -890       C  
ATOM    404  CE2 TYR A 817       8.616  31.516   4.408  1.00 43.27           C  
ANISOU  404  CE2 TYR A 817     6109   5493   4837    520   1444   -650       C  
ATOM    405  CZ  TYR A 817       7.358  31.199   3.944  1.00 43.97           C  
ANISOU  405  CZ  TYR A 817     6289   5657   4758    449   1321   -753       C  
ATOM    406  OH  TYR A 817       6.409  30.743   4.811  1.00 43.02           O  
ANISOU  406  OH  TYR A 817     6079   5502   4762    466   1175   -714       O  
ATOM    407  N   VAL A 818       9.670  34.982  -0.721  1.00 52.92           N  
ANISOU  407  N   VAL A 818     8088   7273   4745    248   1824   -581       N  
ATOM    408  CA  VAL A 818       8.913  36.173  -1.116  1.00 54.14           C  
ANISOU  408  CA  VAL A 818     8359   7579   4632    240   1622   -365       C  
ATOM    409  C   VAL A 818       8.434  36.100  -2.561  1.00 59.06           C  
ANISOU  409  C   VAL A 818     9235   8420   4784    129   1620   -426       C  
ATOM    410  O   VAL A 818       7.263  36.349  -2.858  1.00 60.41           O  
ANISOU  410  O   VAL A 818     9477   8741   4733    107   1341   -357       O  
ATOM    411  CB  VAL A 818       9.760  37.455  -0.976  1.00 53.44           C  
ANISOU  411  CB  VAL A 818     8235   7430   4639    280   1729   -129       C  
ATOM    412  CG1 VAL A 818       9.057  38.644  -1.620  1.00 54.27           C  
ANISOU  412  CG1 VAL A 818     8483   7669   4468    269   1573    113       C  
ATOM    413  CG2 VAL A 818      10.047  37.750   0.489  1.00 51.26           C  
ANISOU  413  CG2 VAL A 818     7724   6988   4765    373   1648    -59       C  
ATOM    414  N   LYS A 819       9.359  35.778  -3.455  1.00 62.89           N  
ANISOU  414  N   LYS A 819     9847   8932   5116     56   1934   -550       N  
ATOM    415  CA  LYS A 819       9.102  35.810  -4.883  1.00 67.85           C  
ANISOU  415  CA  LYS A 819    10752   9799   5228    -64   1978   -600       C  
ATOM    416  C   LYS A 819       7.970  34.835  -5.243  1.00 71.08           C  
ANISOU  416  C   LYS A 819    11239  10340   5427   -151   1759   -848       C  
ATOM    417  O   LYS A 819       6.984  35.211  -5.890  1.00 71.98           O  
ANISOU  417  O   LYS A 819    11491  10682   5173   -208   1488   -759       O  
ATOM    418  CB  LYS A 819      10.409  35.491  -5.619  1.00 70.00           C  
ANISOU  418  CB  LYS A 819    11118  10041   5437   -125   2429   -744       C  
ATOM    419  CG  LYS A 819      10.380  35.621  -7.130  1.00 74.82           C  
ANISOU  419  CG  LYS A 819    12049  10917   5460   -263   2559   -783       C  
ATOM    420  CD  LYS A 819       9.902  34.337  -7.793  1.00 77.87           C  
ANISOU  420  CD  LYS A 819    12577  11416   5592   -387   2573  -1189       C  
ATOM    421  CE  LYS A 819      10.819  33.888  -8.922  1.00 82.40           C  
ANISOU  421  CE  LYS A 819    13363  12069   5874   -506   3023  -1430       C  
ATOM    422  NZ  LYS A 819      11.028  34.950  -9.939  1.00 85.97           N  
ANISOU  422  NZ  LYS A 819    14068  12766   5827   -570   3112  -1162       N  
ATOM    423  N   ASN A 820       8.099  33.598  -4.771  1.00 73.72           N  
ANISOU  423  N   ASN A 820    11457  10513   6040   -157   1858  -1142       N  
ATOM    424  CA  ASN A 820       7.173  32.518  -5.135  1.00 77.74           C  
ANISOU  424  CA  ASN A 820    12024  11097   6417   -265   1715  -1442       C  
ATOM    425  C   ASN A 820       5.773  32.644  -4.520  1.00 77.83           C  
ANISOU  425  C   ASN A 820    11916  11153   6501   -238   1292  -1335       C  
ATOM    426  O   ASN A 820       4.771  32.389  -5.197  1.00 79.37           O  
ANISOU  426  O   ASN A 820    12214  11543   6400   -350   1058  -1448       O  
ATOM    427  CB  ASN A 820       7.788  31.144  -4.795  1.00 78.06           C  
ANISOU  427  CB  ASN A 820    11955  10891   6810   -273   1990  -1772       C  
ATOM    428  CG  ASN A 820       8.948  30.765  -5.722  1.00 80.60           C  
ANISOU  428  CG  ASN A 820    12423  11200   6999   -342   2426  -1992       C  
ATOM    429  OD1 ASN A 820       8.966  31.124  -6.897  1.00 84.41           O  
ANISOU  429  OD1 ASN A 820    13163  11924   6984   -455   2497  -2036       O  
ATOM    430  ND2 ASN A 820       9.911  30.022  -5.195  1.00 79.78           N  
ANISOU  430  ND2 ASN A 820    12150  10817   7343   -273   2728  -2122       N  
ATOM    431  N   THR A 821       5.706  33.047  -3.252  1.00 77.07           N  
ANISOU  431  N   THR A 821    11598  10890   6793    -99   1197  -1126       N  
ATOM    432  CA  THR A 821       4.430  33.125  -2.529  1.00 77.32           C  
ANISOU  432  CA  THR A 821    11485  10929   6963    -61    860  -1035       C  
ATOM    433  C   THR A 821       3.742  34.502  -2.698  1.00 79.69           C  
ANISOU  433  C   THR A 821    11814  11390   7075    -10    597   -712       C  
ATOM    434  O   THR A 821       3.414  35.188  -1.728  1.00 77.61           O  
ANISOU  434  O   THR A 821    11390  11034   7062    104    478   -502       O  
ATOM    435  CB  THR A 821       4.603  32.720  -1.035  1.00 73.40           C  
ANISOU  435  CB  THR A 821    10746  10180   6960     50    905  -1006       C  
ATOM    436  OG1 THR A 821       5.430  33.665  -0.329  1.00 68.71           O  
ANISOU  436  OG1 THR A 821    10078   9497   6529    168    996   -769       O  
ATOM    437  CG2 THR A 821       5.204  31.298  -0.926  1.00 72.85           C  
ANISOU  437  CG2 THR A 821    10634   9930   7114     10   1147  -1290       C  
ATOM    438  N   HIS A 822       3.479  34.867  -3.950  1.00 87.14           N  
ANISOU  438  N   HIS A 822    12962  12576   7570   -101    506   -678       N  
ATOM    439  CA  HIS A 822       3.024  36.214  -4.290  1.00 89.97           C  
ANISOU  439  CA  HIS A 822    13368  13074   7742    -46    300   -325       C  
ATOM    440  C   HIS A 822       2.252  36.237  -5.628  1.00 90.49           C  
ANISOU  440  C   HIS A 822    13628  13458   7295   -170     63   -325       C  
ATOM    441  O   HIS A 822       2.788  35.897  -6.685  1.00 87.87           O  
ANISOU  441  O   HIS A 822    13531  13283   6570   -293    221   -470       O  
ATOM    442  CB  HIS A 822       4.252  37.144  -4.301  1.00 92.76           C  
ANISOU  442  CB  HIS A 822    13784  13338   8119     20    572   -116       C  
ATOM    443  CG  HIS A 822       4.073  38.401  -5.096  1.00 99.89           C  
ANISOU  443  CG  HIS A 822    14825  14398   8728     34    463    227       C  
ATOM    444  ND1 HIS A 822       3.644  39.583  -4.531  1.00100.01           N  
ANISOU  444  ND1 HIS A 822    14715  14324   8958    161    301    552       N  
ATOM    445  CD2 HIS A 822       4.287  38.665  -6.409  1.00104.43           C  
ANISOU  445  CD2 HIS A 822    15657  15202   8817    -59    511    310       C  
ATOM    446  CE1 HIS A 822       3.587  40.517  -5.464  1.00103.10           C  
ANISOU  446  CE1 HIS A 822    15265  14862   9046    153    242    847       C  
ATOM    447  NE2 HIS A 822       3.973  39.986  -6.612  1.00105.61           N  
ANISOU  447  NE2 HIS A 822    15824  15391   8909     18    361    722       N  
ATOM    448  N   HIS A 826      -0.611  37.829 -10.012  1.00116.95           N  
ANISOU  448  N   HIS A 826    17586  18099   8750   -477  -1136    295       N  
ATOM    449  CA  HIS A 826      -1.880  38.257  -9.438  1.00117.69           C  
ANISOU  449  CA  HIS A 826    17392  18159   9163   -369  -1550    509       C  
ATOM    450  C   HIS A 826      -2.143  39.758  -9.709  1.00119.32           C  
ANISOU  450  C   HIS A 826    17596  18424   9315   -222  -1737   1086       C  
ATOM    451  O   HIS A 826      -2.378  40.121 -10.861  1.00123.46           O  
ANISOU  451  O   HIS A 826    18325  19272   9310   -296  -1948   1295       O  
ATOM    452  CB  HIS A 826      -1.953  37.888  -7.942  1.00114.14           C  
ANISOU  452  CB  HIS A 826    16637  17342   9388   -257  -1422    356       C  
ATOM    453  CG  HIS A 826      -3.097  38.529  -7.213  1.00115.52           C  
ANISOU  453  CG  HIS A 826    16506  17426   9961   -112  -1738    613       C  
ATOM    454  ND1 HIS A 826      -4.359  38.645  -7.759  1.00118.90           N  
ANISOU  454  ND1 HIS A 826    16837  18087  10253   -146  -2198    733       N  
ATOM    455  CD2 HIS A 826      -3.162  39.110  -5.990  1.00112.64           C  
ANISOU  455  CD2 HIS A 826    15904  16765  10129     65  -1650    764       C  
ATOM    456  CE1 HIS A 826      -5.152  39.265  -6.903  1.00116.62           C  
ANISOU  456  CE1 HIS A 826    16246  17627  10437     17  -2355    954       C  
ATOM    457  NE2 HIS A 826      -4.451  39.559  -5.823  1.00113.73           N  
ANISOU  457  NE2 HIS A 826    15806  16941  10464    142  -2016    963       N  
ATOM    458  N   ASN A 827      -2.064  40.616  -8.679  1.00115.89           N  
ANISOU  458  N   ASN A 827    16947  17676   9408    -24  -1646   1339       N  
ATOM    459  CA  ASN A 827      -2.589  42.005  -8.719  1.00115.98           C  
ANISOU  459  CA  ASN A 827    16860  17659   9547    140  -1864   1868       C  
ATOM    460  C   ASN A 827      -2.391  42.798  -7.405  1.00109.72           C  
ANISOU  460  C   ASN A 827    15824  16460   9402    337  -1679   2011       C  
ATOM    461  O   ASN A 827      -2.263  42.210  -6.325  1.00105.88           O  
ANISOU  461  O   ASN A 827    15175  15756   9295    357  -1518   1714       O  
ATOM    462  CB  ASN A 827      -4.095  42.012  -9.064  1.00119.19           C  
ANISOU  462  CB  ASN A 827    17094  18279   9912    143  -2400   1997       C  
ATOM    463  CG  ASN A 827      -4.387  42.468 -10.487  1.00125.84           C  
ANISOU  463  CG  ASN A 827    18160  19507  10144     74  -2699   2320       C  
ATOM    464  OD1 ASN A 827      -3.488  42.623 -11.315  1.00128.40           O  
ANISOU  464  OD1 ASN A 827    18810  19980   9993     -8  -2487   2395       O  
ATOM    465  ND2 ASN A 827      -5.663  42.685 -10.776  1.00129.44           N  
ANISOU  465  ND2 ASN A 827    18430  20139  10610    107  -3197   2527       N  
ATOM    466  N   ALA A 828      -2.390  44.132  -7.532  1.00108.44           N  
ANISOU  466  N   ALA A 828    15647  16205   9347    475  -1712   2473       N  
ATOM    467  CA  ALA A 828      -2.309  45.118  -6.421  1.00102.42           C  
ANISOU  467  CA  ALA A 828    14666  15065   9183    661  -1571   2650       C  
ATOM    468  C   ALA A 828      -0.952  45.853  -6.376  1.00100.66           C  
ANISOU  468  C   ALA A 828    14594  14648   9004    679  -1173   2782       C  
ATOM    469  O   ALA A 828      -0.875  47.033  -6.733  1.00102.50           O  
ANISOU  469  O   ALA A 828    14859  14798   9289    769  -1175   3204       O  
ATOM    470  CB  ALA A 828      -2.661  44.510  -5.059  1.00 96.79           C  
ANISOU  470  CB  ALA A 828    13691  14140   8943    703  -1518   2311       C  
ATOM    471  N   TYR A 829       0.102  45.154  -5.945  1.00 97.06           N  
ANISOU  471  N   TYR A 829    14209  14106   8562    595   -836   2437       N  
ATOM    472  CA  TYR A 829       1.468  45.712  -5.844  1.00 93.15           C  
ANISOU  472  CA  TYR A 829    13817  13424   8149    590   -444   2502       C  
ATOM    473  C   TYR A 829       2.534  44.645  -6.112  1.00 89.18           C  
ANISOU  473  C   TYR A 829    13482  13014   7386    441   -152   2153       C  
ATOM    474  O   TYR A 829       2.241  43.454  -6.139  1.00 88.39           O  
ANISOU  474  O   TYR A 829    13392  13056   7136    356   -225   1818       O  
ATOM    475  CB  TYR A 829       1.713  46.345  -4.459  1.00 90.05           C  
ANISOU  475  CB  TYR A 829    13191  12660   8364    710   -299   2473       C  
ATOM    476  CG  TYR A 829       1.280  45.487  -3.278  1.00 86.57           C  
ANISOU  476  CG  TYR A 829    12546  12136   8208    729   -349   2109       C  
ATOM    477  CD1 TYR A 829       1.941  44.296  -2.966  1.00 84.20           C  
ANISOU  477  CD1 TYR A 829    12281  11870   7838    630   -176   1735       C  
ATOM    478  CD2 TYR A 829       0.212  45.875  -2.468  1.00 85.48           C  
ANISOU  478  CD2 TYR A 829    12174  11872   8431    851   -547   2159       C  
ATOM    479  CE1 TYR A 829       1.540  43.516  -1.892  1.00 81.73           C  
ANISOU  479  CE1 TYR A 829    11793  11480   7781    649   -216   1456       C  
ATOM    480  CE2 TYR A 829      -0.192  45.104  -1.393  1.00 82.35           C  
ANISOU  480  CE2 TYR A 829    11606  11412   8270    860   -563   1855       C  
ATOM    481  CZ  TYR A 829       0.472  43.929  -1.107  1.00 81.15           C  
ANISOU  481  CZ  TYR A 829    11508  11305   8018    758   -405   1521       C  
ATOM    482  OH  TYR A 829       0.063  43.166  -0.037  1.00 79.52           O  
ANISOU  482  OH  TYR A 829    11138  11031   8042    769   -416   1267       O  
ATOM    483  N   ASP A 830       3.775  45.088  -6.284  1.00 86.61           N  
ANISOU  483  N   ASP A 830    13264  12578   7066    412    196   2229       N  
ATOM    484  CA  ASP A 830       4.904  44.198  -6.532  1.00 83.42           C  
ANISOU  484  CA  ASP A 830    12986  12218   6492    290    528   1926       C  
ATOM    485  C   ASP A 830       5.846  44.286  -5.330  1.00 77.51           C  
ANISOU  485  C   ASP A 830    12044  11151   6252    340    788   1775       C  
ATOM    486  O   ASP A 830       6.257  45.383  -4.937  1.00 76.84           O  
ANISOU  486  O   ASP A 830    11878  10852   6465    406    889   2004       O  
ATOM    487  CB  ASP A 830       5.629  44.641  -7.806  1.00 88.34           C  
ANISOU  487  CB  ASP A 830    13883  12995   6684    202    746   2153       C  
ATOM    488  CG  ASP A 830       5.799  43.521  -8.813  1.00 91.46           C  
ANISOU  488  CG  ASP A 830    14519  13694   6538     44    830   1882       C  
ATOM    489  OD1 ASP A 830       6.070  42.378  -8.388  1.00 90.44           O  
ANISOU  489  OD1 ASP A 830    14325  13527   6508     -5    939   1459       O  
ATOM    490  OD2 ASP A 830       5.668  43.792 -10.032  1.00 94.59           O  
ANISOU  490  OD2 ASP A 830    15173  14363   6404    -32    794   2095       O  
ATOM    491  N   LEU A 831       6.176  43.146  -4.733  1.00 72.23           N  
ANISOU  491  N   LEU A 831    11294  10447   5703    304    882   1397       N  
ATOM    492  CA  LEU A 831       7.067  43.140  -3.578  1.00 67.29           C  
ANISOU  492  CA  LEU A 831    10476   9560   5528    346   1083   1259       C  
ATOM    493  C   LEU A 831       8.509  42.960  -4.013  1.00 66.69           C  
ANISOU  493  C   LEU A 831    10476   9445   5415    267   1469   1186       C  
ATOM    494  O   LEU A 831       8.807  42.159  -4.885  1.00 67.51           O  
ANISOU  494  O   LEU A 831    10743   9712   5194    173   1613   1032       O  
ATOM    495  CB  LEU A 831       6.688  42.046  -2.588  1.00 64.32           C  
ANISOU  495  CB  LEU A 831     9942   9141   5355    367    977    948       C  
ATOM    496  CG  LEU A 831       5.379  42.261  -1.832  1.00 63.78           C  
ANISOU  496  CG  LEU A 831     9729   9047   5457    456    658    997       C  
ATOM    497  CD1 LEU A 831       5.027  41.003  -1.053  1.00 62.29           C  
ANISOU  497  CD1 LEU A 831     9422   8848   5397    448    597    696       C  
ATOM    498  CD2 LEU A 831       5.454  43.463  -0.900  1.00 62.13           C  
ANISOU  498  CD2 LEU A 831     9369   8618   5620    556    654   1172       C  
ATOM    499  N   GLU A 832       9.396  43.699  -3.361  1.00 65.21           N  
ANISOU  499  N   GLU A 832    10152   9032   5593    299   1642   1269       N  
ATOM    500  CA  GLU A 832      10.804  43.728  -3.689  1.00 65.80           C  
ANISOU  500  CA  GLU A 832    10238   9030   5733    232   2017   1243       C  
ATOM    501  C   GLU A 832      11.524  43.898  -2.357  1.00 61.35           C  
ANISOU  501  C   GLU A 832     9403   8218   5687    277   2067   1139       C  
ATOM    502  O   GLU A 832      11.192  44.807  -1.595  1.00 59.68           O  
ANISOU  502  O   GLU A 832     9075   7865   5736    337   1918   1265       O  
ATOM    503  CB  GLU A 832      11.048  44.910  -4.626  1.00 71.27           C  
ANISOU  503  CB  GLU A 832    11081   9733   6262    199   2150   1599       C  
ATOM    504  CG  GLU A 832      12.301  44.836  -5.485  1.00 76.70           C  
ANISOU  504  CG  GLU A 832    11875  10442   6825     97   2572   1605       C  
ATOM    505  CD  GLU A 832      13.427  45.733  -4.985  1.00 78.43           C  
ANISOU  505  CD  GLU A 832    11912  10388   7497     90   2817   1721       C  
ATOM    506  OE1 GLU A 832      13.614  45.833  -3.744  1.00 75.71           O  
ANISOU  506  OE1 GLU A 832    11316   9847   7603    143   2715   1599       O  
ATOM    507  OE2 GLU A 832      14.130  46.326  -5.843  1.00 81.85           O  
ANISOU  507  OE2 GLU A 832    12458  10815   7824     18   3116   1931       O  
ATOM    508  N   VAL A 833      12.467  43.011  -2.048  1.00 58.53           N  
ANISOU  508  N   VAL A 833     8938   7811   5489    249   2262    902       N  
ATOM    509  CA  VAL A 833      13.156  43.062  -0.757  1.00 55.42           C  
ANISOU  509  CA  VAL A 833     8277   7223   5555    286   2260    802       C  
ATOM    510  C   VAL A 833      14.280  44.082  -0.775  1.00 56.45           C  
ANISOU  510  C   VAL A 833     8310   7189   5947    241   2487    943       C  
ATOM    511  O   VAL A 833      15.047  44.123  -1.707  1.00 59.55           O  
ANISOU  511  O   VAL A 833     8784   7601   6241    172   2784    999       O  
ATOM    512  CB  VAL A 833      13.737  41.696  -0.352  1.00 54.42           C  
ANISOU  512  CB  VAL A 833     8030   7090   5554    290   2349    531       C  
ATOM    513  CG1 VAL A 833      14.464  41.802   0.983  1.00 52.24           C  
ANISOU  513  CG1 VAL A 833     7476   6650   5722    326   2302    472       C  
ATOM    514  CG2 VAL A 833      12.632  40.654  -0.260  1.00 53.61           C  
ANISOU  514  CG2 VAL A 833     8001   7111   5256    322   2137    380       C  
ATOM    515  N   ILE A 834      14.370  44.902   0.265  1.00 55.93           N  
ANISOU  515  N   ILE A 834     8069   6959   6221    266   2362    982       N  
ATOM    516  CA  ILE A 834      15.393  45.944   0.356  1.00 57.65           C  
ANISOU  516  CA  ILE A 834     8162   6988   6753    206   2550   1094       C  
ATOM    517  C   ILE A 834      16.460  45.537   1.354  1.00 57.40           C  
ANISOU  517  C   ILE A 834     7854   6855   7101    187   2586    898       C  
ATOM    518  O   ILE A 834      17.642  45.605   1.054  1.00 59.01           O  
ANISOU  518  O   ILE A 834     7942   6976   7500    120   2849    900       O  
ATOM    519  CB  ILE A 834      14.790  47.273   0.833  1.00 57.37           C  
ANISOU  519  CB  ILE A 834     8108   6808   6880    229   2388   1254       C  
ATOM    520  CG1 ILE A 834      13.757  47.780  -0.164  1.00 59.34           C  
ANISOU  520  CG1 ILE A 834     8598   7142   6804    263   2331   1512       C  
ATOM    521  CG2 ILE A 834      15.871  48.320   1.025  1.00 58.73           C  
ANISOU  521  CG2 ILE A 834     8123   6750   7439    147   2579   1329       C  
ATOM    522  CD1 ILE A 834      12.797  48.776   0.451  1.00 59.40           C  
ANISOU  522  CD1 ILE A 834     8573   7022   6974    333   2102   1622       C  
ATOM    523  N   ASP A 835      16.024  45.148   2.552  1.00 56.11           N  
ANISOU  523  N   ASP A 835     7574   6702   7041    244   2315    747       N  
ATOM    524  CA  ASP A 835      16.914  44.693   3.623  1.00 56.00           C  
ANISOU  524  CA  ASP A 835     7298   6633   7345    237   2268    583       C  
ATOM    525  C   ASP A 835      16.287  43.509   4.343  1.00 51.38           C  
ANISOU  525  C   ASP A 835     6701   6167   6652    318   2054    439       C  
ATOM    526  O   ASP A 835      15.067  43.472   4.551  1.00 48.57           O  
ANISOU  526  O   ASP A 835     6475   5886   6093    371   1861    445       O  
ATOM    527  CB  ASP A 835      17.125  45.788   4.678  1.00 59.22           C  
ANISOU  527  CB  ASP A 835     7546   6903   8050    197   2125    567       C  
ATOM    528  CG  ASP A 835      17.823  47.020   4.135  1.00 64.00           C  
ANISOU  528  CG  ASP A 835     8116   7335   8866    103   2336    703       C  
ATOM    529  OD1 ASP A 835      17.253  48.125   4.299  1.00 67.37           O  
ANISOU  529  OD1 ASP A 835     8600   7651   9344     92   2260    786       O  
ATOM    530  OD2 ASP A 835      18.932  46.892   3.555  1.00 68.50           O  
ANISOU  530  OD2 ASP A 835     8586   7855   9583     39   2597    731       O  
ATOM    531  N   ILE A 836      17.139  42.572   4.747  1.00 49.55           N  
ANISOU  531  N   ILE A 836     6290   5934   6602    330   2097    331       N  
ATOM    532  CA  ILE A 836      16.737  41.424   5.548  1.00 46.77           C  
ANISOU  532  CA  ILE A 836     5886   5659   6226    406   1913    227       C  
ATOM    533  C   ILE A 836      17.513  41.472   6.851  1.00 45.82           C  
ANISOU  533  C   ILE A 836     5502   5498   6406    402   1756    183       C  
ATOM    534  O   ILE A 836      18.743  41.443   6.838  1.00 47.15           O  
ANISOU  534  O   ILE A 836     5464   5594   6855    368   1879    178       O  
ATOM    535  CB  ILE A 836      17.040  40.097   4.827  1.00 47.15           C  
ANISOU  535  CB  ILE A 836     5951   5729   6232    437   2103    154       C  
ATOM    536  CG1 ILE A 836      16.379  40.070   3.446  1.00 47.79           C  
ANISOU  536  CG1 ILE A 836     6306   5883   5967    410   2262    171       C  
ATOM    537  CG2 ILE A 836      16.562  38.923   5.663  1.00 45.64           C  
ANISOU  537  CG2 ILE A 836     5705   5581   6053    516   1920     79       C  
ATOM    538  CD1 ILE A 836      16.757  38.871   2.605  1.00 49.20           C  
ANISOU  538  CD1 ILE A 836     6523   6072   6095    412   2507     48       C  
ATOM    539  N   PHE A 837      16.797  41.549   7.967  1.00 43.73           N  
ANISOU  539  N   PHE A 837     5239   5296   6079    431   1486    151       N  
ATOM    540  CA  PHE A 837      17.419  41.584   9.285  1.00 44.30           C  
ANISOU  540  CA  PHE A 837     5095   5384   6351    417   1289    106       C  
ATOM    541  C   PHE A 837      17.170  40.289  10.036  1.00 44.34           C  
ANISOU  541  C   PHE A 837     5051   5483   6311    502   1142    100       C  
ATOM    542  O   PHE A 837      16.041  39.800  10.103  1.00 43.41           O  
ANISOU  542  O   PHE A 837     5094   5430   5969    555   1077     99       O  
ATOM    543  CB  PHE A 837      16.870  42.737  10.122  1.00 44.01           C  
ANISOU  543  CB  PHE A 837     5099   5354   6268    368   1109     59       C  
ATOM    544  CG  PHE A 837      16.990  44.077   9.460  1.00 45.52           C  
ANISOU  544  CG  PHE A 837     5340   5412   6542    291   1247     86       C  
ATOM    545  CD1 PHE A 837      18.182  44.778   9.509  1.00 47.51           C  
ANISOU  545  CD1 PHE A 837     5402   5556   7093    192   1318     67       C  
ATOM    546  CD2 PHE A 837      15.915  44.624   8.772  1.00 45.14           C  
ANISOU  546  CD2 PHE A 837     5511   5337   6303    317   1304    154       C  
ATOM    547  CE1 PHE A 837      18.298  46.005   8.897  1.00 49.23           C  
ANISOU  547  CE1 PHE A 837     5661   5619   7423    116   1470    117       C  
ATOM    548  CE2 PHE A 837      16.025  45.844   8.142  1.00 46.63           C  
ANISOU  548  CE2 PHE A 837     5744   5382   6590    257   1438    231       C  
ATOM    549  CZ  PHE A 837      17.215  46.542   8.212  1.00 48.77           C  
ANISOU  549  CZ  PHE A 837     5838   5524   7165    154   1534    213       C  
ATOM    550  N   LYS A 838      18.226  39.741  10.618  1.00 46.15           N  
ANISOU  550  N   LYS A 838     5039   5710   6784    514   1084    116       N  
ATOM    551  CA  LYS A 838      18.086  38.640  11.553  1.00 46.32           C  
ANISOU  551  CA  LYS A 838     4986   5813   6799    593    904    161       C  
ATOM    552  C   LYS A 838      17.882  39.225  12.948  1.00 46.25           C  
ANISOU  552  C   LYS A 838     4945   5929   6697    552    610    141       C  
ATOM    553  O   LYS A 838      18.674  40.048  13.398  1.00 48.36           O  
ANISOU  553  O   LYS A 838     5065   6201   7109    468    517     96       O  
ATOM    554  CB  LYS A 838      19.327  37.755  11.505  1.00 48.61           C  
ANISOU  554  CB  LYS A 838     5012   6036   7420    641    971    221       C  
ATOM    555  CG  LYS A 838      19.133  36.415  12.177  1.00 49.37           C  
ANISOU  555  CG  LYS A 838     5049   6167   7542    749    852    316       C  
ATOM    556  CD  LYS A 838      20.319  35.495  11.937  1.00 52.34           C  
ANISOU  556  CD  LYS A 838     5153   6424   8307    820    969    385       C  
ATOM    557  CE  LYS A 838      19.908  34.036  12.087  1.00 53.18           C  
ANISOU  557  CE  LYS A 838     5268   6478   8457    940    986    469       C  
ATOM    558  NZ  LYS A 838      21.065  33.139  11.837  1.00 56.05           N  
ANISOU  558  NZ  LYS A 838     5346   6686   9264   1027   1125    536       N  
ATOM    559  N   ILE A 839      16.817  38.808  13.624  1.00 44.96           N  
ANISOU  559  N   ILE A 839     4921   5868   6291    597    480    157       N  
ATOM    560  CA  ILE A 839      16.498  39.334  14.945  1.00 45.27           C  
ANISOU  560  CA  ILE A 839     4975   6050   6175    553    239    115       C  
ATOM    561  C   ILE A 839      16.471  38.253  16.012  1.00 46.64           C  
ANISOU  561  C   ILE A 839     5085   6355   6279    617     55    236       C  
ATOM    562  O   ILE A 839      16.028  37.141  15.757  1.00 46.57           O  
ANISOU  562  O   ILE A 839     5119   6314   6260    707    130    337       O  
ATOM    563  CB  ILE A 839      15.152  40.087  14.951  1.00 43.42           C  
ANISOU  563  CB  ILE A 839     4974   5830   5693    534    264     24       C  
ATOM    564  CG1 ILE A 839      13.999  39.172  14.543  1.00 41.14           C  
ANISOU  564  CG1 ILE A 839     4836   5543   5251    621    347     87       C  
ATOM    565  CG2 ILE A 839      15.227  41.300  14.024  1.00 43.28           C  
ANISOU  565  CG2 ILE A 839     5006   5677   5762    471    414    -51       C  
ATOM    566  CD1 ILE A 839      12.647  39.818  14.698  1.00 39.99           C  
ANISOU  566  CD1 ILE A 839     4867   5423   4902    616    346     17       C  
ATOM    567  N   GLU A 840      16.970  38.591  17.198  1.00 49.44           N  
ANISOU  567  N   GLU A 840     5338   6857   6588    560   -187    227       N  
ATOM    568  CA  GLU A 840      16.874  37.746  18.387  1.00 51.28           C  
ANISOU  568  CA  GLU A 840     5543   7265   6675    605   -399    369       C  
ATOM    569  C   GLU A 840      16.316  38.592  19.528  1.00 50.63           C  
ANISOU  569  C   GLU A 840     5590   7372   6275    510   -568    241       C  
ATOM    570  O   GLU A 840      17.048  39.366  20.142  1.00 53.06           O  
ANISOU  570  O   GLU A 840     5796   7773   6589    404   -744    133       O  
ATOM    571  CB  GLU A 840      18.256  37.246  18.805  1.00 56.58           C  
ANISOU  571  CB  GLU A 840     5924   7978   7592    621   -578    509       C  
ATOM    572  CG  GLU A 840      18.860  36.123  17.972  1.00 59.67           C  
ANISOU  572  CG  GLU A 840     6152   8194   8324    740   -423    666       C  
ATOM    573  CD  GLU A 840      19.989  35.410  18.723  1.00 66.31           C  
ANISOU  573  CD  GLU A 840     6700   9107   9388    793   -656    876       C  
ATOM    574  OE1 GLU A 840      21.181  35.570  18.351  1.00 69.68           O  
ANISOU  574  OE1 GLU A 840     6859   9449  10166    781   -652    874       O  
ATOM    575  OE2 GLU A 840      19.686  34.704  19.720  1.00 69.89           O  
ANISOU  575  OE2 GLU A 840     7176   9707   9670    846   -851   1063       O  
ATOM    576  N   ARG A 841      15.030  38.460  19.819  1.00 47.83           N  
ANISOU  576  N   ARG A 841     5447   7068   5655    538   -502    227       N  
ATOM    577  CA  ARG A 841      14.456  39.187  20.942  1.00 47.93           C  
ANISOU  577  CA  ARG A 841     5592   7261   5357    453   -615     88       C  
ATOM    578  C   ARG A 841      14.970  38.586  22.235  1.00 50.44           C  
ANISOU  578  C   ARG A 841     5841   7828   5494    440   -879    229       C  
ATOM    579  O   ARG A 841      15.026  37.370  22.361  1.00 50.55           O  
ANISOU  579  O   ARG A 841     5804   7865   5537    540   -910    487       O  
ATOM    580  CB  ARG A 841      12.939  39.099  20.931  1.00 45.80           C  
ANISOU  580  CB  ARG A 841     5535   6978   4887    497   -450     60       C  
ATOM    581  CG  ARG A 841      12.255  39.684  19.702  1.00 43.68           C  
ANISOU  581  CG  ARG A 841     5344   6496   4753    518   -227    -45       C  
ATOM    582  CD  ARG A 841      10.745  39.804  19.938  1.00 42.85           C  
ANISOU  582  CD  ARG A 841     5412   6409   4458    544   -111   -100       C  
ATOM    583  NE  ARG A 841      10.476  40.382  21.260  1.00 44.82           N  
ANISOU  583  NE  ARG A 841     5738   6836   4454    469   -195   -234       N  
ATOM    584  CZ  ARG A 841       9.991  39.735  22.324  1.00 45.18           C  
ANISOU  584  CZ  ARG A 841     5856   7071   4239    477   -239   -151       C  
ATOM    585  NH1 ARG A 841       9.632  38.457  22.278  1.00 44.34           N  
ANISOU  585  NH1 ARG A 841     5746   6977   4122    561   -207     83       N  
ATOM    586  NH2 ARG A 841       9.846  40.397  23.454  1.00 47.08           N  
ANISOU  586  NH2 ARG A 841     6181   7483   4222    388   -296   -316       N  
ATOM    587  N   GLU A 842      15.328  39.429  23.201  1.00 53.24           N  
ANISOU  587  N   GLU A 842     6200   8367   5661    311  -1073     63       N  
ATOM    588  CA  GLU A 842      15.777  38.942  24.500  1.00 56.98           C  
ANISOU  588  CA  GLU A 842     6635   9134   5879    279  -1363    197       C  
ATOM    589  C   GLU A 842      14.801  37.924  25.066  1.00 55.64           C  
ANISOU  589  C   GLU A 842     6624   9076   5437    370  -1306    418       C  
ATOM    590  O   GLU A 842      13.599  38.175  25.125  1.00 53.10           O  
ANISOU  590  O   GLU A 842     6509   8740   4927    368  -1110    306       O  
ATOM    591  CB  GLU A 842      15.921  40.075  25.506  1.00 61.56           C  
ANISOU  591  CB  GLU A 842     7285   9924   6182    102  -1536    -89       C  
ATOM    592  CG  GLU A 842      17.225  40.837  25.419  1.00 65.77           C  
ANISOU  592  CG  GLU A 842     7591  10441   6956    -18  -1730   -241       C  
ATOM    593  CD  GLU A 842      17.335  41.913  26.492  1.00 71.81           C  
ANISOU  593  CD  GLU A 842     8435  11423   7427   -217  -1915   -567       C  
ATOM    594  OE1 GLU A 842      18.463  42.433  26.706  1.00 76.58           O  
ANISOU  594  OE1 GLU A 842     8834  12083   8177   -345  -2154   -685       O  
ATOM    595  OE2 GLU A 842      16.297  42.232  27.133  1.00 73.65           O  
ANISOU  595  OE2 GLU A 842     8922  11766   7293   -255  -1813   -723       O  
ATOM    596  N   GLY A 843      15.339  36.771  25.453  1.00 56.39           N  
ANISOU  596  N   GLY A 843     6599   9261   5563    454  -1467    752       N  
ATOM    597  CA  GLY A 843      14.612  35.766  26.202  1.00 56.79           C  
ANISOU  597  CA  GLY A 843     6775   9447   5353    524  -1459   1019       C  
ATOM    598  C   GLY A 843      13.656  34.899  25.419  1.00 54.13           C  
ANISOU  598  C   GLY A 843     6507   8873   5186    646  -1164   1148       C  
ATOM    599  O   GLY A 843      13.106  33.953  25.974  1.00 54.64           O  
ANISOU  599  O   GLY A 843     6643   9004   5111    707  -1137   1405       O  
ATOM    600  N   GLU A 844      13.456  35.194  24.137  1.00 51.62           N  
ANISOU  600  N   GLU A 844     6165   8284   5162    673   -949    983       N  
ATOM    601  CA  GLU A 844      12.411  34.518  23.381  1.00 50.53           C  
ANISOU  601  CA  GLU A 844     6112   7946   5138    756   -683   1034       C  
ATOM    602  C   GLU A 844      12.784  33.074  23.055  1.00 50.98           C  
ANISOU  602  C   GLU A 844     6034   7860   5476    878   -661   1337       C  
ATOM    603  O   GLU A 844      11.954  32.174  23.173  1.00 51.19           O  
ANISOU  603  O   GLU A 844     6132   7831   5485    933   -537   1497       O  
ATOM    604  CB  GLU A 844      12.051  35.284  22.105  1.00 48.59           C  
ANISOU  604  CB  GLU A 844     5899   7489   5071    739   -486    777       C  
ATOM    605  CG  GLU A 844      10.590  35.108  21.706  1.00 47.55           C  
ANISOU  605  CG  GLU A 844     5920   7264   4882    765   -264    727       C  
ATOM    606  CD  GLU A 844      10.241  35.768  20.372  1.00 46.90           C  
ANISOU  606  CD  GLU A 844     5862   6987   4969    760   -104    531       C  
ATOM    607  OE1 GLU A 844      10.951  35.537  19.362  1.00 46.06           O  
ANISOU  607  OE1 GLU A 844     5657   6732   5113    790    -64    542       O  
ATOM    608  OE2 GLU A 844       9.235  36.514  20.333  1.00 47.13           O  
ANISOU  608  OE2 GLU A 844     6008   7016   4880    730    -10    377       O  
ATOM    609  N   CYS A 845      14.028  32.855  22.659  1.00 52.19           N  
ANISOU  609  N   CYS A 845     5972   7930   5926    918   -761   1411       N  
ATOM    610  CA  CYS A 845      14.493  31.516  22.355  1.00 53.87           C  
ANISOU  610  CA  CYS A 845     6025   7972   6471   1043   -725   1683       C  
ATOM    611  C   CYS A 845      14.396  30.608  23.575  1.00 55.92           C  
ANISOU  611  C   CYS A 845     6286   8385   6576   1095   -879   2036       C  
ATOM    612  O   CYS A 845      13.991  29.445  23.455  1.00 56.51           O  
ANISOU  612  O   CYS A 845     6350   8297   6824   1188   -748   2254       O  
ATOM    613  CB  CYS A 845      15.921  31.550  21.832  1.00 56.29           C  
ANISOU  613  CB  CYS A 845     6069   8179   7139   1077   -806   1693       C  
ATOM    614  SG  CYS A 845      16.598  29.906  21.515  1.00 61.88           S  
ANISOU  614  SG  CYS A 845     6539   8640   8332   1249   -745   2023       S  
ATOM    615  N   GLN A 846      14.741  31.153  24.741  1.00 57.65           N  
ANISOU  615  N   GLN A 846     6528   8915   6460   1024  -1149   2086       N  
ATOM    616  CA AGLN A 846      14.652  30.417  26.000  0.50 60.87           C  
ANISOU  616  CA AGLN A 846     6971   9536   6620   1056  -1322   2443       C  
ATOM    617  CA BGLN A 846      14.643  30.418  26.013  0.50 61.20           C  
ANISOU  617  CA BGLN A 846     7015   9581   6656   1055  -1323   2444       C  
ATOM    618  C   GLN A 846      13.188  30.106  26.341  1.00 60.29           C  
ANISOU  618  C   GLN A 846     7146   9482   6276   1040  -1102   2473       C  
ATOM    619  O   GLN A 846      12.881  29.043  26.870  1.00 61.82           O  
ANISOU  619  O   GLN A 846     7354   9669   6465   1112  -1079   2822       O  
ATOM    620  CB AGLN A 846      15.331  31.206  27.129  0.50 63.58           C  
ANISOU  620  CB AGLN A 846     7310  10253   6592    949  -1674   2426       C  
ATOM    621  CB BGLN A 846      15.301  31.212  27.155  0.50 64.28           C  
ANISOU  621  CB BGLN A 846     7407  10350   6667    947  -1673   2425       C  
ATOM    622  CG AGLN A 846      16.845  31.385  26.969  0.50 64.91           C  
ANISOU  622  CG AGLN A 846     7178  10428   7057    962  -1942   2460       C  
ATOM    623  CG BGLN A 846      14.893  30.816  28.571  0.50 67.68           C  
ANISOU  623  CG BGLN A 846     7992  11102   6619    923  -1827   2705       C  
ATOM    624  CD AGLN A 846      17.245  32.301  25.811  0.50 61.67           C  
ANISOU  624  CD AGLN A 846     6675   9813   6941    910  -1807   2085       C  
ATOM    625  CD BGLN A 846      15.267  29.393  28.931  0.50 70.53           C  
ANISOU  625  CD BGLN A 846     8212  11409   7176   1072  -1922   3235       C  
ATOM    626  OE1AGLN A 846      16.460  33.132  25.345  0.50 57.62           O  
ANISOU  626  OE1AGLN A 846     6350   9244   6297    829  -1601   1760       O  
ATOM    627  OE1BGLN A 846      16.442  29.047  28.997  0.50 72.71           O  
ANISOU  627  OE1BGLN A 846     8229  11689   7709   1142  -2180   3453       O  
ATOM    628  NE2AGLN A 846      18.474  32.140  25.336  0.50 62.51           N  
ANISOU  628  NE2AGLN A 846     6479   9800   7470    961  -1912   2153       N  
ATOM    629  NE2BGLN A 846      14.262  28.564  29.187  0.50 70.67           N  
ANISOU  629  NE2BGLN A 846     8382  11362   7106   1123  -1710   3460       N  
ATOM    630  N   ARG A 847      12.299  31.043  26.022  1.00 59.01           N  
ANISOU  630  N   ARG A 847     7159   9326   5935    949   -930   2122       N  
ATOM    631  CA  ARG A 847      10.851  30.882  26.184  1.00 59.81           C  
ANISOU  631  CA  ARG A 847     7460   9413   5851    928   -686   2091       C  
ATOM    632  C   ARG A 847      10.270  29.837  25.224  1.00 58.72           C  
ANISOU  632  C   ARG A 847     7269   8942   6097   1018   -439   2184       C  
ATOM    633  O   ARG A 847       9.311  29.140  25.549  1.00 58.09           O  
ANISOU  633  O   ARG A 847     7276   8828   5967   1031   -281   2338       O  
ATOM    634  CB  ARG A 847      10.163  32.234  25.938  1.00 59.25           C  
ANISOU  634  CB  ARG A 847     7530   9388   5592    825   -575   1675       C  
ATOM    635  CG  ARG A 847       8.645  32.252  26.105  1.00 59.65           C  
ANISOU  635  CG  ARG A 847     7753   9430   5478    800   -319   1600       C  
ATOM    636  CD  ARG A 847       8.058  33.640  25.873  1.00 58.67           C  
ANISOU  636  CD  ARG A 847     7731   9327   5231    718   -222   1205       C  
ATOM    637  NE  ARG A 847       7.820  33.914  24.460  1.00 57.22           N  
ANISOU  637  NE  ARG A 847     7483   8870   5386    750    -94   1026       N  
ATOM    638  CZ  ARG A 847       7.360  35.070  23.974  1.00 58.12           C  
ANISOU  638  CZ  ARG A 847     7648   8929   5505    706     -8    726       C  
ATOM    639  NH1 ARG A 847       7.096  36.088  24.791  1.00 58.64           N  
ANISOU  639  NH1 ARG A 847     7821   9161   5296    627    -12    530       N  
ATOM    640  NH2 ARG A 847       7.169  35.217  22.653  1.00 57.59           N  
ANISOU  640  NH2 ARG A 847     7527   8633   5720    741     86    624       N  
ATOM    641  N   TYR A 848      10.851  29.752  24.033  1.00 58.88           N  
ANISOU  641  N   TYR A 848     7149   8720   6502   1064   -393   2069       N  
ATOM    642  CA  TYR A 848      10.396  28.831  22.998  1.00 58.99           C  
ANISOU  642  CA  TYR A 848     7115   8416   6879   1126   -165   2079       C  
ATOM    643  C   TYR A 848      10.753  27.373  23.313  1.00 65.61           C  
ANISOU  643  C   TYR A 848     7829   9113   7983   1231   -166   2460       C  
ATOM    644  O   TYR A 848      10.103  26.465  22.814  1.00 66.32           O  
ANISOU  644  O   TYR A 848     7917   8963   8318   1263     37   2506       O  
ATOM    645  CB  TYR A 848      11.000  29.272  21.664  1.00 55.96           C  
ANISOU  645  CB  TYR A 848     6643   7855   6764   1129   -108   1821       C  
ATOM    646  CG  TYR A 848      10.554  28.521  20.425  1.00 53.88           C  
ANISOU  646  CG  TYR A 848     6359   7292   6820   1162    126   1727       C  
ATOM    647  CD1 TYR A 848       9.301  28.724  19.866  1.00 51.28           C  
ANISOU  647  CD1 TYR A 848     6163   6908   6409   1104    286   1533       C  
ATOM    648  CD2 TYR A 848      11.413  27.644  19.784  1.00 55.26           C  
ANISOU  648  CD2 TYR A 848     6367   7239   7388   1243    184   1808       C  
ATOM    649  CE1 TYR A 848       8.909  28.050  18.722  1.00 49.71           C  
ANISOU  649  CE1 TYR A 848     5950   6467   6470   1110    466   1417       C  
ATOM    650  CE2 TYR A 848      11.028  26.968  18.640  1.00 53.84           C  
ANISOU  650  CE2 TYR A 848     6186   6796   7474   1252    408   1669       C  
ATOM    651  CZ  TYR A 848       9.779  27.180  18.113  1.00 50.91           C  
ANISOU  651  CZ  TYR A 848     5966   6405   6970   1176    532   1468       C  
ATOM    652  OH  TYR A 848       9.426  26.500  16.977  1.00 49.96           O  
ANISOU  652  OH  TYR A 848     5846   6050   7086   1163    722   1308       O  
ATOM    653  N   LYS A 849      11.771  27.159  24.151  1.00 74.42           N  
ANISOU  653  N   LYS A 849     8831  10371   9071   1282   -404   2737       N  
ATOM    654  CA  LYS A 849      12.261  25.807  24.501  1.00 82.25           C  
ANISOU  654  CA  LYS A 849     9670  11218  10363   1405   -437   3158       C  
ATOM    655  C   LYS A 849      11.189  24.742  24.783  1.00 88.69           C  
ANISOU  655  C   LYS A 849    10571  11889  11236   1428   -232   3386       C  
ATOM    656  O   LYS A 849      11.326  23.608  24.309  1.00 93.02           O  
ANISOU  656  O   LYS A 849    10987  12115  12240   1521    -97   3549       O  
ATOM    657  CB  LYS A 849      13.218  25.855  25.698  1.00 85.24           C  
ANISOU  657  CB  LYS A 849     9962  11880  10546   1436   -778   3480       C  
ATOM    658  CG  LYS A 849      14.621  26.279  25.342  1.00 85.29           C  
ANISOU  658  CG  LYS A 849     9738  11890  10778   1469   -981   3410       C  
ATOM    659  CD  LYS A 849      15.491  26.313  26.579  1.00 89.31           C  
ANISOU  659  CD  LYS A 849    10149  12712  11071   1484  -1365   3736       C  
ATOM    660  CE  LYS A 849      16.826  26.966  26.280  1.00 89.61           C  
ANISOU  660  CE  LYS A 849     9948  12797  11302   1479  -1589   3605       C  
ATOM    661  NZ  LYS A 849      17.593  27.201  27.527  1.00 93.88           N  
ANISOU  661  NZ  LYS A 849    10410  13711  11549   1451  -2017   3855       N  
ATOM    662  N   PRO A 850      10.153  25.075  25.592  1.00 92.96           N  
ANISOU  662  N   PRO A 850    11318  12651  11350   1342   -190   3402       N  
ATOM    663  CA  PRO A 850       9.016  24.163  25.730  1.00 93.68           C  
ANISOU  663  CA  PRO A 850    11482  12580  11531   1339     54   3564       C  
ATOM    664  C   PRO A 850       8.554  23.530  24.401  1.00 91.96           C  
ANISOU  664  C   PRO A 850    11188  11957  11794   1352    311   3358       C  
ATOM    665  O   PRO A 850       8.354  22.307  24.342  1.00 91.38           O  
ANISOU  665  O   PRO A 850    11035  11611  12075   1408    454   3596       O  
ATOM    666  CB  PRO A 850       7.928  25.070  26.318  1.00 92.58           C  
ANISOU  666  CB  PRO A 850    11562  12713  10898   1217    123   3383       C  
ATOM    667  CG  PRO A 850       8.673  26.092  27.119  1.00 93.51           C  
ANISOU  667  CG  PRO A 850    11738  13204  10585   1177   -152   3345       C  
ATOM    668  CD  PRO A 850      10.101  26.135  26.619  1.00 94.45           C  
ANISOU  668  CD  PRO A 850    11658  13252  10974   1250   -371   3346       C  
ATOM    669  N   PHE A 851       8.438  24.349  23.351  1.00 87.62           N  
ANISOU  669  N   PHE A 851    10663  11370  11259   1296    360   2926       N  
ATOM    670  CA  PHE A 851       7.862  23.915  22.075  1.00 86.20           C  
ANISOU  670  CA  PHE A 851    10454  10880  11416   1273    582   2670       C  
ATOM    671  C   PHE A 851       8.861  23.594  20.960  1.00 83.42           C  
ANISOU  671  C   PHE A 851     9954  10285  11454   1336    607   2535       C  
ATOM    672  O   PHE A 851       8.452  23.172  19.886  1.00 80.28           O  
ANISOU  672  O   PHE A 851     9546   9643  11313   1307    789   2308       O  
ATOM    673  CB  PHE A 851       6.878  24.976  21.584  1.00 85.75           C  
ANISOU  673  CB  PHE A 851    10535  10942  11103   1165    642   2303       C  
ATOM    674  CG  PHE A 851       5.729  25.209  22.526  1.00 90.30           C  
ANISOU  674  CG  PHE A 851    11236  11696  11375   1100    701   2382       C  
ATOM    675  CD1 PHE A 851       4.562  24.455  22.421  1.00 91.23           C  
ANISOU  675  CD1 PHE A 851    11358  11647  11658   1057    907   2414       C  
ATOM    676  CD2 PHE A 851       5.814  26.172  23.530  1.00 92.62           C  
ANISOU  676  CD2 PHE A 851    11636  12320  11232   1072    570   2407       C  
ATOM    677  CE1 PHE A 851       3.501  24.670  23.289  1.00 92.92           C  
ANISOU  677  CE1 PHE A 851    11667  12018  11618    997   1001   2488       C  
ATOM    678  CE2 PHE A 851       4.754  26.386  24.404  1.00 93.48           C  
ANISOU  678  CE2 PHE A 851    11866  12594  11057   1011    673   2458       C  
ATOM    679  CZ  PHE A 851       3.596  25.637  24.282  1.00 93.09           C  
ANISOU  679  CZ  PHE A 851    11806  12372  11188    979    899   2510       C  
ATOM    680  N   LYS A 852      10.155  23.770  21.210  1.00 85.28           N  
ANISOU  680  N   LYS A 852    10069  10592  11741   1414    432   2663       N  
ATOM    681  CA  LYS A 852      11.175  23.618  20.155  1.00 88.61           C  
ANISOU  681  CA  LYS A 852    10337  10804  12524   1470    483   2508       C  
ATOM    682  C   LYS A 852      11.317  22.201  19.581  1.00 93.44           C  
ANISOU  682  C   LYS A 852    10814  11017  13671   1550    692   2593       C  
ATOM    683  O   LYS A 852      11.778  22.041  18.448  1.00 92.90           O  
ANISOU  683  O   LYS A 852    10674  10738  13884   1561    839   2344       O  
ATOM    684  CB  LYS A 852      12.546  24.101  20.650  1.00 90.05           C  
ANISOU  684  CB  LYS A 852    10372  11149  12690   1535    242   2653       C  
ATOM    685  N   GLN A 853      10.936  21.186  20.364  1.00100.47           N  
ANISOU  685  N   GLN A 853    11673  11794  14705   1599    724   2939       N  
ATOM    686  CA  GLN A 853      10.986  19.774  19.934  1.00101.87           C  
ANISOU  686  CA  GLN A 853    11718  11546  15443   1672    942   3042       C  
ATOM    687  C   GLN A 853       9.581  19.204  19.655  1.00100.29           C  
ANISOU  687  C   GLN A 853    11636  11176  15293   1567   1160   2918       C  
ATOM    688  O   GLN A 853       9.367  17.989  19.680  1.00100.75           O  
ANISOU  688  O   GLN A 853    11606  10902  15770   1605   1328   3086       O  
ATOM    689  CB  GLN A 853      11.705  18.929  20.991  1.00105.72           C  
ANISOU  689  CB  GLN A 853    12036  11964  16168   1820    826   3583       C  
ATOM    690  N   LEU A 854       8.631  20.097  19.387  1.00 96.79           N  
ANISOU  690  N   LEU A 854    11368  10944  14461   1434   1154   2627       N  
ATOM    691  CA  LEU A 854       7.276  19.719  19.003  1.00 95.25           C  
ANISOU  691  CA  LEU A 854    11259  10621  14309   1316   1332   2451       C  
ATOM    692  C   LEU A 854       7.235  19.704  17.477  1.00 90.31           C  
ANISOU  692  C   LEU A 854    10638   9812  13860   1249   1467   1989       C  
ATOM    693  O   LEU A 854       7.543  20.718  16.848  1.00 88.03           O  
ANISOU  693  O   LEU A 854    10416   9709  13322   1220   1386   1726       O  
ATOM    694  CB  LEU A 854       6.271  20.747  19.556  1.00 94.92           C  
ANISOU  694  CB  LEU A 854    11379  10920  13766   1220   1243   2397       C  
ATOM    695  CG  LEU A 854       4.764  20.493  19.413  1.00 95.55           C  
ANISOU  695  CG  LEU A 854    11518  10929  13854   1097   1394   2273       C  
ATOM    696  CD1 LEU A 854       4.344  19.243  20.181  1.00 98.62           C  
ANISOU  696  CD1 LEU A 854    11839  11099  14532   1113   1537   2632       C  
ATOM    697  CD2 LEU A 854       3.968  21.712  19.877  1.00 93.02           C  
ANISOU  697  CD2 LEU A 854    11330  10955  13056   1027   1306   2182       C  
ATOM    698  N  AHIS A 855       6.864  18.554  16.910  0.50 88.54           N  
ANISOU  698  N  AHIS A 855    10350   9228  14061   1216   1677   1896       N  
ATOM    699  N  BHIS A 855       6.864  18.573  16.878  0.50 88.81           N  
ANISOU  699  N  BHIS A 855    10387   9265  14091   1214   1677   1884       N  
ATOM    700  CA AHIS A 855       6.613  18.366  15.473  0.50 83.96           C  
ANISOU  700  CA AHIS A 855     9799   8471  13628   1116   1824   1430       C  
ATOM    701  CA BHIS A 855       6.873  18.464  15.420  0.50 84.01           C  
ANISOU  701  CA BHIS A 855     9798   8493  13627   1136   1811   1426       C  
ATOM    702  C  AHIS A 855       5.883  19.532  14.781  0.50 78.90           C  
ANISOU  702  C  AHIS A 855     9315   8117  12546    990   1727   1086       C  
ATOM    703  C  BHIS A 855       5.915  19.486  14.772  0.50 79.31           C  
ANISOU  703  C  BHIS A 855     9362   8155  12616    993   1733   1089       C  
ATOM    704  O  AHIS A 855       5.167  20.306  15.434  0.50 76.56           O  
ANISOU  704  O  AHIS A 855     9095   8085  11907    956   1598   1182       O  
ATOM    705  O  BHIS A 855       5.084  20.107  15.446  0.50 77.87           O  
ANISOU  705  O  BHIS A 855     9249   8204  12132    951   1623   1193       O  
ATOM    706  CB AHIS A 855       5.772  17.100  15.326  0.50 84.75           C  
ANISOU  706  CB AHIS A 855     9843   8219  14136   1040   2025   1399       C  
ATOM    707  CB BHIS A 855       6.536  17.039  14.971  0.50 85.46           C  
ANISOU  707  CB BHIS A 855     9892   8239  14337   1098   2053   1343       C  
ATOM    708  CG AHIS A 855       4.994  16.767  16.561  0.50 84.20           C  
ANISOU  708  CG AHIS A 855     9758   8174  14057   1038   2011   1784       C  
ATOM    709  CG BHIS A 855       7.385  16.549  13.838  0.50 84.83           C  
ANISOU  709  CG BHIS A 855     9752   7897  14579   1119   2226   1041       C  
ATOM    710  ND1AHIS A 855       5.482  15.933  17.545  0.50 86.60           N  
ANISOU  710  ND1AHIS A 855     9952   8305  14647   1161   2051   2248       N  
ATOM    711  ND1BHIS A 855       8.329  17.340  13.219  0.50 82.41           N  
ANISOU  711  ND1BHIS A 855     9471   7749  14088   1162   2182    868       N  
ATOM    712  CD2AHIS A 855       3.780  17.184  16.990  0.50 81.99           C  
ANISOU  712  CD2AHIS A 855     9557   8082  13511    933   1971   1795       C  
ATOM    713  CD2BHIS A 855       7.413  15.359  13.196  0.50 86.65           C  
ANISOU  713  CD2BHIS A 855     9901   7708  15313   1092   2475    857       C  
ATOM    714  CE1AHIS A 855       4.594  15.836  18.518  0.50 86.63           C  
ANISOU  714  CE1AHIS A 855     9991   8399  14525   1121   2052   2530       C  
ATOM    715  CE1BHIS A 855       8.911  16.655  12.253  0.50 83.85           C  
ANISOU  715  CE1BHIS A 855     9594   7638  14624   1166   2409    597       C  
ATOM    716  NE2AHIS A 855       3.552  16.584  18.206  0.50 84.15           N  
ANISOU  716  NE2AHIS A 855     9784   8297  13891    981   2018   2247       N  
ATOM    717  NE2BHIS A 855       8.373  15.449  12.217  0.50 86.88           N  
ANISOU  717  NE2BHIS A 855     9916   7665  15428   1124   2588    568       N  
ATOM    718  N   ASN A 856       6.064  19.655  13.462  1.00 75.76           N  
ANISOU  718  N   ASN A 856     8963   7662  12157    925   1800    696       N  
ATOM    719  CA  ASN A 856       5.331  20.655  12.672  1.00 68.89           C  
ANISOU  719  CA  ASN A 856     8235   7035  10903    806   1706    391       C  
ATOM    720  C   ASN A 856       5.675  22.113  13.025  1.00 62.42           C  
ANISOU  720  C   ASN A 856     7491   6562   9662    853   1516    474       C  
ATOM    721  O   ASN A 856       4.809  22.886  13.431  1.00 61.84           O  
ANISOU  721  O   ASN A 856     7484   6704   9307    809   1396    505       O  
ATOM    722  CB  ASN A 856       3.812  20.409  12.757  1.00 68.65           C  
ANISOU  722  CB  ASN A 856     8224   7000  10858    678   1697    325       C  
ATOM    723  CG  ASN A 856       3.037  21.166  11.700  1.00 68.30           C  
ANISOU  723  CG  ASN A 856     8288   7136  10527    551   1607    -16       C  
ATOM    724  OD1 ASN A 856       3.550  21.450  10.626  1.00 69.30           O  
ANISOU  724  OD1 ASN A 856     8489   7293  10548    523   1621   -272       O  
ATOM    725  ND2 ASN A 856       1.796  21.511  12.009  1.00 68.82           N  
ANISOU  725  ND2 ASN A 856     8356   7328  10464    475   1517     -1       N  
ATOM    726  N   ARG A 857       6.938  22.488  12.850  1.00 57.71           N  
ANISOU  726  N   ARG A 857     6868   5997   9062    938   1509    493       N  
ATOM    727  CA  ARG A 857       7.364  23.871  13.048  1.00 53.68           C  
ANISOU  727  CA  ARG A 857     6416   5773   8204    963   1349    525       C  
ATOM    728  C   ARG A 857       7.646  24.491  11.694  1.00 50.66           C  
ANISOU  728  C   ARG A 857     6125   5440   7683    903   1399    215       C  
ATOM    729  O   ARG A 857       8.325  23.890  10.879  1.00 51.30           O  
ANISOU  729  O   ARG A 857     6172   5344   7975    909   1564     65       O  
ATOM    730  CB  ARG A 857       8.608  23.939  13.905  1.00 55.59           C  
ANISOU  730  CB  ARG A 857     6540   6040   8540   1087   1281    794       C  
ATOM    731  CG  ARG A 857       8.724  22.777  14.864  1.00 58.97           C  
ANISOU  731  CG  ARG A 857     6843   6293   9270   1168   1310   1104       C  
ATOM    732  CD  ARG A 857       9.476  23.150  16.122  1.00 60.26           C  
ANISOU  732  CD  ARG A 857     6930   6630   9334   1263   1123   1443       C  
ATOM    733  NE  ARG A 857      10.763  23.765  15.843  1.00 60.61           N  
ANISOU  733  NE  ARG A 857     6891   6739   9398   1316   1059   1404       N  
ATOM    734  CZ  ARG A 857      11.840  23.108  15.426  1.00 63.00           C  
ANISOU  734  CZ  ARG A 857     7028   6825  10084   1403   1163   1429       C  
ATOM    735  NH1 ARG A 857      11.799  21.796  15.211  1.00 65.01           N  
ANISOU  735  NH1 ARG A 857     7191   6759  10748   1451   1344   1479       N  
ATOM    736  NH2 ARG A 857      12.968  23.781  15.218  1.00 63.16           N  
ANISOU  736  NH2 ARG A 857     6954   6926  10116   1439   1105   1394       N  
ATOM    737  N   ARG A 858       7.116  25.690  11.461  1.00 46.92           N  
ANISOU  737  N   ARG A 858     5767   5200   6861    848   1276    130       N  
ATOM    738  CA  ARG A 858       7.174  26.321  10.154  1.00 45.48           C  
ANISOU  738  CA  ARG A 858     5698   5090   6493    779   1311   -123       C  
ATOM    739  C   ARG A 858       7.630  27.755  10.238  1.00 43.25           C  
ANISOU  739  C   ARG A 858     5463   5013   5956    801   1200    -70       C  
ATOM    740  O   ARG A 858       7.313  28.471  11.200  1.00 41.40           O  
ANISOU  740  O   ARG A 858     5222   4915   5591    827   1058     81       O  
ATOM    741  CB  ARG A 858       5.801  26.306   9.497  1.00 45.97           C  
ANISOU  741  CB  ARG A 858     5856   5202   6407    665   1265   -304       C  
ATOM    742  CG  ARG A 858       5.220  24.923   9.407  1.00 48.47           C  
ANISOU  742  CG  ARG A 858     6118   5302   6995    612   1369   -390       C  
ATOM    743  CD  ARG A 858       4.086  24.848   8.422  1.00 49.69           C  
ANISOU  743  CD  ARG A 858     6356   5503   7021    472   1325   -647       C  
ATOM    744  NE  ARG A 858       3.419  23.562   8.550  1.00 52.34           N  
ANISOU  744  NE  ARG A 858     6611   5619   7657    406   1409   -715       N  
ATOM    745  CZ  ARG A 858       2.318  23.217   7.896  1.00 54.69           C  
ANISOU  745  CZ  ARG A 858     6926   5912   7939    266   1361   -934       C  
ATOM    746  NH1 ARG A 858       1.744  24.062   7.046  1.00 55.06           N  
ANISOU  746  NH1 ARG A 858     7075   6187   7658    188   1207  -1083       N  
ATOM    747  NH2 ARG A 858       1.787  22.015   8.091  1.00 57.45           N  
ANISOU  747  NH2 ARG A 858     7180   6024   8623    200   1458   -990       N  
ATOM    748  N   LEU A 859       8.344  28.170   9.195  1.00 42.41           N  
ANISOU  748  N   LEU A 859     5412   4918   5784    779   1292   -212       N  
ATOM    749  CA  LEU A 859       8.758  29.553   9.036  1.00 40.95           C  
ANISOU  749  CA  LEU A 859     5280   4894   5384    779   1222   -185       C  
ATOM    750  C   LEU A 859       7.643  30.278   8.287  1.00 39.69           C  
ANISOU  750  C   LEU A 859     5271   4868   4939    700   1139   -291       C  
ATOM    751  O   LEU A 859       7.411  30.004   7.108  1.00 41.00           O  
ANISOU  751  O   LEU A 859     5537   5029   5011    628   1217   -467       O  
ATOM    752  CB  LEU A 859      10.071  29.616   8.258  1.00 41.97           C  
ANISOU  752  CB  LEU A 859     5383   4958   5605    789   1395   -258       C  
ATOM    753  CG  LEU A 859      10.788  30.955   8.298  1.00 41.51           C  
ANISOU  753  CG  LEU A 859     5323   5014   5434    796   1349   -185       C  
ATOM    754  CD1 LEU A 859      11.254  31.273   9.720  1.00 41.58           C  
ANISOU  754  CD1 LEU A 859     5187   5058   5551    862   1195     10       C  
ATOM    755  CD2 LEU A 859      11.950  30.950   7.325  1.00 42.68           C  
ANISOU  755  CD2 LEU A 859     5452   5090   5674    785   1572   -280       C  
ATOM    756  N   LEU A 860       6.950  31.191   8.975  1.00 37.71           N  
ANISOU  756  N   LEU A 860     5032   4740   4554    712    978   -186       N  
ATOM    757  CA  LEU A 860       5.714  31.811   8.457  1.00 36.20           C  
ANISOU  757  CA  LEU A 860     4933   4657   4161    660    869   -239       C  
ATOM    758  C   LEU A 860       5.739  33.317   8.560  1.00 34.64           C  
ANISOU  758  C   LEU A 860     4776   4568   3817    682    782   -158       C  
ATOM    759  O   LEU A 860       6.417  33.862   9.407  1.00 32.31           O  
ANISOU  759  O   LEU A 860     4424   4276   3574    727    771    -67       O  
ATOM    760  CB  LEU A 860       4.505  31.326   9.255  1.00 35.64           C  
ANISOU  760  CB  LEU A 860     4804   4582   4155    657    787   -199       C  
ATOM    761  CG  LEU A 860       4.156  29.848   9.177  1.00 36.68           C  
ANISOU  761  CG  LEU A 860     4887   4580   4470    618    864   -275       C  
ATOM    762  CD1 LEU A 860       3.076  29.554  10.197  1.00 36.43           C  
ANISOU  762  CD1 LEU A 860     4775   4545   4519    621    807   -178       C  
ATOM    763  CD2 LEU A 860       3.716  29.464   7.772  1.00 37.70           C  
ANISOU  763  CD2 LEU A 860     5100   4708   4515    518    879   -492       C  
ATOM    764  N   TRP A 861       4.926  33.964   7.729  1.00 35.74           N  
ANISOU  764  N   TRP A 861     5001   4789   3788    646    705   -189       N  
ATOM    765  CA  TRP A 861       4.855  35.428   7.653  1.00 35.97           C  
ANISOU  765  CA  TRP A 861     5069   4882   3713    670    635   -100       C  
ATOM    766  C   TRP A 861       3.917  36.104   8.662  1.00 35.36           C  
ANISOU  766  C   TRP A 861     4927   4830   3677    715    526    -28       C  
ATOM    767  O   TRP A 861       2.832  35.606   8.959  1.00 36.29           O  
ANISOU  767  O   TRP A 861     4996   4961   3830    710    466    -46       O  
ATOM    768  CB  TRP A 861       4.388  35.847   6.270  1.00 36.87           C  
ANISOU  768  CB  TRP A 861     5300   5075   3631    623    590   -118       C  
ATOM    769  CG  TRP A 861       5.256  35.380   5.169  1.00 38.13           C  
ANISOU  769  CG  TRP A 861     5559   5238   3688    566    729   -206       C  
ATOM    770  CD1 TRP A 861       4.976  34.400   4.279  1.00 39.63           C  
ANISOU  770  CD1 TRP A 861     5820   5458   3779    491    759   -358       C  
ATOM    771  CD2 TRP A 861       6.541  35.893   4.819  1.00 38.61           C  
ANISOU  771  CD2 TRP A 861     5657   5268   3743    568    882   -170       C  
ATOM    772  NE1 TRP A 861       6.010  34.262   3.389  1.00 41.64           N  
ANISOU  772  NE1 TRP A 861     6171   5708   3941    450    943   -430       N  
ATOM    773  CE2 TRP A 861       6.986  35.169   3.704  1.00 41.08           C  
ANISOU  773  CE2 TRP A 861     6071   5599   3938    500   1027   -301       C  
ATOM    774  CE3 TRP A 861       7.364  36.889   5.345  1.00 37.93           C  
ANISOU  774  CE3 TRP A 861     5519   5135   3757    607    923    -59       C  
ATOM    775  CZ2 TRP A 861       8.220  35.413   3.102  1.00 42.57           C  
ANISOU  775  CZ2 TRP A 861     6304   5760   4110    482   1237   -303       C  
ATOM    776  CZ3 TRP A 861       8.583  37.126   4.750  1.00 38.79           C  
ANISOU  776  CZ3 TRP A 861     5654   5209   3874    582   1104    -54       C  
ATOM    777  CH2 TRP A 861       9.000  36.399   3.645  1.00 41.00           C  
ANISOU  777  CH2 TRP A 861     6029   5509   4040    526   1270   -164       C  
ATOM    778  N   HIS A 862       4.333  37.268   9.147  1.00 34.53           N  
ANISOU  778  N   HIS A 862     4815   4718   3587    749    521     33       N  
ATOM    779  CA  HIS A 862       3.454  38.131   9.897  1.00 33.83           C  
ANISOU  779  CA  HIS A 862     4683   4638   3533    790    453     68       C  
ATOM    780  C   HIS A 862       3.667  39.580   9.522  1.00 34.11           C  
ANISOU  780  C   HIS A 862     4754   4639   3566    808    445    125       C  
ATOM    781  O   HIS A 862       4.683  40.172   9.859  1.00 34.30           O  
ANISOU  781  O   HIS A 862     4777   4619   3635    801    501    124       O  
ATOM    782  CB  HIS A 862       3.679  37.975  11.392  1.00 33.80           C  
ANISOU  782  CB  HIS A 862     4612   4636   3592    809    477     56       C  
ATOM    783  CG  HIS A 862       2.660  38.695  12.217  1.00 34.15           C  
ANISOU  783  CG  HIS A 862     4618   4691   3666    843    455     49       C  
ATOM    784  ND1 HIS A 862       1.496  38.097  12.646  1.00 34.36           N  
ANISOU  784  ND1 HIS A 862     4588   4742   3723    852    453     47       N  
ATOM    785  CD2 HIS A 862       2.611  39.973  12.658  1.00 34.92           C  
ANISOU  785  CD2 HIS A 862     4711   4755   3798    866    463     29       C  
ATOM    786  CE1 HIS A 862       0.781  38.970  13.331  1.00 35.33           C  
ANISOU  786  CE1 HIS A 862     4674   4860   3890    887    473     26       C  
ATOM    787  NE2 HIS A 862       1.441  40.114  13.361  1.00 36.02           N  
ANISOU  787  NE2 HIS A 862     4798   4906   3982    898    479      4       N  
ATOM    788  N   GLY A 863       2.696  40.154   8.832  1.00 34.95           N  
ANISOU  788  N   GLY A 863     4875   4754   3649    831    368    186       N  
ATOM    789  CA  GLY A 863       2.729  41.561   8.514  1.00 36.14           C  
ANISOU  789  CA  GLY A 863     5045   4837   3847    864    362    280       C  
ATOM    790  C   GLY A 863       2.019  42.376   9.566  1.00 37.27           C  
ANISOU  790  C   GLY A 863     5099   4910   4150    923    359    259       C  
ATOM    791  O   GLY A 863       1.074  41.913  10.204  1.00 37.59           O  
ANISOU  791  O   GLY A 863     5066   4984   4233    946    333    210       O  
ATOM    792  N   SER A 864       2.480  43.604   9.737  1.00 38.62           N  
ANISOU  792  N   SER A 864     5274   4968   4430    939    411    283       N  
ATOM    793  CA  SER A 864       1.854  44.549  10.629  1.00 38.82           C  
ANISOU  793  CA  SER A 864     5225   4892   4633    991    443    233       C  
ATOM    794  C   SER A 864       2.234  45.946  10.174  1.00 40.40           C  
ANISOU  794  C   SER A 864     5441   4927   4980   1010    485    320       C  
ATOM    795  O   SER A 864       3.190  46.131   9.421  1.00 41.21           O  
ANISOU  795  O   SER A 864     5613   5010   5033    965    513    401       O  
ATOM    796  CB  SER A 864       2.343  44.305  12.050  1.00 38.97           C  
ANISOU  796  CB  SER A 864     5224   4939   4642    952    512     58       C  
ATOM    797  OG  SER A 864       1.663  45.144  12.975  1.00 41.59           O  
ANISOU  797  OG  SER A 864     5499   5188   5115    991    574    -40       O  
ATOM    798  N   ARG A 865       1.495  46.948  10.612  1.00 41.60           N  
ANISOU  798  N   ARG A 865     5520   4938   5346   1077    518    309       N  
ATOM    799  CA  ARG A 865       1.883  48.300  10.249  1.00 42.54           C  
ANISOU  799  CA  ARG A 865     5644   4853   5666   1094    581    395       C  
ATOM    800  C   ARG A 865       3.126  48.729  11.035  1.00 41.81           C  
ANISOU  800  C   ARG A 865     5570   4684   5629   1001    687    218       C  
ATOM    801  O   ARG A 865       3.319  48.358  12.191  1.00 40.54           O  
ANISOU  801  O   ARG A 865     5393   4596   5413    955    712      4       O  
ATOM    802  CB  ARG A 865       0.714  49.299  10.338  1.00 44.29           C  
ANISOU  802  CB  ARG A 865     5762   4898   6168   1209    594    459       C  
ATOM    803  CG  ARG A 865      -0.057  49.348  11.642  1.00 44.53           C  
ANISOU  803  CG  ARG A 865     5698   4897   6323   1242    676    236       C  
ATOM    804  CD  ARG A 865      -1.582  49.391  11.419  1.00 45.58           C  
ANISOU  804  CD  ARG A 865     5696   5005   6616   1366    621    347       C  
ATOM    805  NE  ARG A 865      -2.015  50.409  10.467  1.00 47.35           N  
ANISOU  805  NE  ARG A 865     5860   5048   7083   1468    569    601       N  
ATOM    806  CZ  ARG A 865      -3.265  50.577  10.045  1.00 48.80           C  
ANISOU  806  CZ  ARG A 865     5898   5195   7447   1588    475    766       C  
ATOM    807  NH1 ARG A 865      -3.535  51.535   9.175  1.00 51.28           N  
ANISOU  807  NH1 ARG A 865     6162   5342   7979   1685    412   1041       N  
ATOM    808  NH2 ARG A 865      -4.247  49.800  10.477  1.00 48.47           N  
ANISOU  808  NH2 ARG A 865     5744   5277   7393   1614    441    683       N  
ATOM    809  N   THR A 866       3.980  49.487  10.357  1.00 42.48           N  
ANISOU  809  N   THR A 866     5688   4637   5812    964    741    326       N  
ATOM    810  CA  THR A 866       5.220  50.001  10.918  1.00 42.48           C  
ANISOU  810  CA  THR A 866     5679   4543   5918    859    829    177       C  
ATOM    811  C   THR A 866       5.068  50.562  12.330  1.00 43.34           C  
ANISOU  811  C   THR A 866     5728   4568   6168    832    879   -103       C  
ATOM    812  O   THR A 866       5.904  50.312  13.193  1.00 43.54           O  
ANISOU  812  O   THR A 866     5745   4674   6123    732    872   -303       O  
ATOM    813  CB  THR A 866       5.782  51.081   9.993  1.00 44.21           C  
ANISOU  813  CB  THR A 866     5912   4548   6336    842    917    362       C  
ATOM    814  OG1 THR A 866       6.036  50.493   8.716  1.00 44.23           O  
ANISOU  814  OG1 THR A 866     5997   4672   6134    844    891    597       O  
ATOM    815  CG2 THR A 866       7.073  51.654  10.531  1.00 45.30           C  
ANISOU  815  CG2 THR A 866     6007   4565   6638    715   1009    198       C  
ATOM    816  N   THR A 867       3.992  51.291  12.582  1.00 44.14           N  
ANISOU  816  N   THR A 867     5785   4521   6462    920    929   -124       N  
ATOM    817  CA  THR A 867       3.811  51.912  13.887  1.00 45.51           C  
ANISOU  817  CA  THR A 867     5920   4601   6771    888   1021   -426       C  
ATOM    818  C   THR A 867       3.667  50.914  15.026  1.00 44.29           C  
ANISOU  818  C   THR A 867     5788   4702   6337    847    981   -633       C  
ATOM    819  O   THR A 867       3.685  51.297  16.182  1.00 45.51           O  
ANISOU  819  O   THR A 867     5942   4845   6503    789   1052   -910       O  
ATOM    820  CB  THR A 867       2.605  52.870  13.888  1.00 47.36           C  
ANISOU  820  CB  THR A 867     6080   4596   7315   1010   1120   -406       C  
ATOM    821  OG1 THR A 867       1.518  52.263  13.188  1.00 47.41           O  
ANISOU  821  OG1 THR A 867     6056   4702   7254   1136   1032   -171       O  
ATOM    822  CG2 THR A 867       2.964  54.155  13.194  1.00 49.31           C  
ANISOU  822  CG2 THR A 867     6298   4521   7913   1021   1202   -275       C  
ATOM    823  N   ASN A 868       3.522  49.637  14.704  1.00 42.72           N  
ANISOU  823  N   ASN A 868     5616   4731   5882    870    878   -499       N  
ATOM    824  CA  ASN A 868       3.434  48.600  15.730  1.00 42.29           C  
ANISOU  824  CA  ASN A 868     5586   4912   5570    834    843   -631       C  
ATOM    825  C   ASN A 868       4.763  47.902  16.040  1.00 42.44           C  
ANISOU  825  C   ASN A 868     5635   5091   5398    727    753   -668       C  
ATOM    826  O   ASN A 868       4.847  47.132  16.990  1.00 41.19           O  
ANISOU  826  O   ASN A 868     5496   5122   5031    689    712   -758       O  
ATOM    827  CB  ASN A 868       2.404  47.549  15.306  1.00 40.69           C  
ANISOU  827  CB  ASN A 868     5369   4835   5254    919    795   -472       C  
ATOM    828  CG  ASN A 868       1.008  48.113  15.227  1.00 41.70           C  
ANISOU  828  CG  ASN A 868     5422   4838   5581   1027    867   -450       C  
ATOM    829  OD1 ASN A 868       0.710  49.121  15.833  1.00 44.47           O  
ANISOU  829  OD1 ASN A 868     5740   5035   6119   1042    988   -604       O  
ATOM    830  ND2 ASN A 868       0.154  47.473  14.467  1.00 41.78           N  
ANISOU  830  ND2 ASN A 868     5389   4906   5580   1099    793   -270       N  
ATOM    831  N   PHE A 869       5.798  48.159  15.246  1.00 44.03           N  
ANISOU  831  N   PHE A 869     5827   5216   5687    681    728   -577       N  
ATOM    832  CA  PHE A 869       7.000  47.332  15.329  1.00 44.03           C  
ANISOU  832  CA  PHE A 869     5814   5360   5553    606    643   -561       C  
ATOM    833  C   PHE A 869       7.884  47.623  16.514  1.00 44.80           C  
ANISOU  833  C   PHE A 869     5878   5520   5623    491    591   -778       C  
ATOM    834  O   PHE A 869       8.602  46.741  16.955  1.00 45.13           O  
ANISOU  834  O   PHE A 869     5893   5736   5515    451    486   -767       O  
ATOM    835  CB  PHE A 869       7.793  47.355  14.033  1.00 44.47           C  
ANISOU  835  CB  PHE A 869     5859   5334   5702    597    664   -384       C  
ATOM    836  CG  PHE A 869       7.392  46.266  13.110  1.00 43.51           C  
ANISOU  836  CG  PHE A 869     5780   5312   5438    666    644   -202       C  
ATOM    837  CD1 PHE A 869       7.940  45.018  13.243  1.00 43.28           C  
ANISOU  837  CD1 PHE A 869     5734   5435   5272    651    592   -183       C  
ATOM    838  CD2 PHE A 869       6.404  46.467  12.173  1.00 44.52           C  
ANISOU  838  CD2 PHE A 869     5954   5382   5579    744    665    -60       C  
ATOM    839  CE1 PHE A 869       7.546  43.989  12.424  1.00 42.59           C  
ANISOU  839  CE1 PHE A 869     5688   5418   5075    699    590    -63       C  
ATOM    840  CE2 PHE A 869       6.000  45.445  11.341  1.00 43.79           C  
ANISOU  840  CE2 PHE A 869     5904   5398   5334    783    628     63       C  
ATOM    841  CZ  PHE A 869       6.575  44.203  11.464  1.00 43.12           C  
ANISOU  841  CZ  PHE A 869     5814   5444   5124    754    604     40       C  
ATOM    842  N   ALA A 870       7.823  48.837  17.042  1.00 46.05           N  
ANISOU  842  N   ALA A 870     6030   5535   5932    437    654   -978       N  
ATOM    843  CA  ALA A 870       8.549  49.139  18.265  1.00 47.23           C  
ANISOU  843  CA  ALA A 870     6159   5773   6011    305    583  -1237       C  
ATOM    844  C   ALA A 870       8.004  48.256  19.379  1.00 46.89           C  
ANISOU  844  C   ALA A 870     6179   5993   5642    317    523  -1304       C  
ATOM    845  O   ALA A 870       8.779  47.653  20.133  1.00 48.62           O  
ANISOU  845  O   ALA A 870     6383   6424   5665    241    376  -1342       O  
ATOM    846  CB  ALA A 870       8.421  50.605  18.626  1.00 49.19           C  
ANISOU  846  CB  ALA A 870     6401   5793   6492    240    693  -1484       C  
ATOM    847  N   GLY A 871       6.675  48.165  19.462  1.00 44.84           N  
ANISOU  847  N   GLY A 871     5976   5721   5340    415    636  -1289       N  
ATOM    848  CA  GLY A 871       6.018  47.368  20.487  1.00 43.92           C  
ANISOU  848  CA  GLY A 871     5923   5832   4932    428    634  -1331       C  
ATOM    849  C   GLY A 871       6.245  45.896  20.256  1.00 41.55           C  
ANISOU  849  C   GLY A 871     5614   5712   4459    470    522  -1083       C  
ATOM    850  O   GLY A 871       6.512  45.146  21.183  1.00 41.55           O  
ANISOU  850  O   GLY A 871     5644   5935   4205    429    436  -1080       O  
ATOM    851  N   ILE A 872       6.153  45.493  19.002  1.00 39.92           N  
ANISOU  851  N   ILE A 872     5369   5404   4393    549    527   -871       N  
ATOM    852  CA  ILE A 872       6.299  44.096  18.623  1.00 39.36           C  
ANISOU  852  CA  ILE A 872     5285   5449   4220    593    457   -659       C  
ATOM    853  C   ILE A 872       7.706  43.560  18.903  1.00 40.20           C  
ANISOU  853  C   ILE A 872     5339   5666   4269    528    317   -617       C  
ATOM    854  O   ILE A 872       7.865  42.405  19.285  1.00 40.62           O  
ANISOU  854  O   ILE A 872     5383   5862   4189    547    248   -493       O  
ATOM    855  CB  ILE A 872       5.995  43.896  17.124  1.00 37.81           C  
ANISOU  855  CB  ILE A 872     5071   5118   4175    667    495   -491       C  
ATOM    856  CG1 ILE A 872       4.491  44.012  16.869  1.00 37.51           C  
ANISOU  856  CG1 ILE A 872     5048   5024   4180    748    580   -468       C  
ATOM    857  CG2 ILE A 872       6.481  42.535  16.655  1.00 37.21           C  
ANISOU  857  CG2 ILE A 872     4974   5125   4039    685    437   -328       C  
ATOM    858  CD1 ILE A 872       4.096  43.980  15.408  1.00 36.43           C  
ANISOU  858  CD1 ILE A 872     4902   4782   4156    807    580   -314       C  
ATOM    859  N   LEU A 873       8.726  44.374  18.680  1.00 40.33           N  
ANISOU  859  N   LEU A 873     5297   5596   4428    456    278   -699       N  
ATOM    860  CA  LEU A 873      10.070  43.899  18.899  1.00 41.60           C  
ANISOU  860  CA  LEU A 873     5362   5850   4592    398    138   -653       C  
ATOM    861  C   LEU A 873      10.408  43.907  20.392  1.00 44.55           C  
ANISOU  861  C   LEU A 873     5741   6435   4750    312     -7   -782       C  
ATOM    862  O   LEU A 873      11.083  42.994  20.875  1.00 44.87           O  
ANISOU  862  O   LEU A 873     5720   6639   4687    309   -155   -660       O  
ATOM    863  CB  LEU A 873      11.085  44.700  18.079  1.00 41.96           C  
ANISOU  863  CB  LEU A 873     5315   5727   4899    341    160   -680       C  
ATOM    864  CG  LEU A 873      10.944  44.505  16.565  1.00 40.65           C  
ANISOU  864  CG  LEU A 873     5158   5408   4876    416    293   -511       C  
ATOM    865  CD1 LEU A 873      11.950  45.357  15.803  1.00 41.30           C  
ANISOU  865  CD1 LEU A 873     5158   5326   5207    348    355   -520       C  
ATOM    866  CD2 LEU A 873      11.090  43.037  16.175  1.00 39.84           C  
ANISOU  866  CD2 LEU A 873     5033   5394   4708    487    276   -334       C  
ATOM    867  N   SER A 874       9.932  44.905  21.135  1.00 46.36           N  
ANISOU  867  N   SER A 874     6045   6666   4903    245     33  -1023       N  
ATOM    868  CA  SER A 874      10.266  44.969  22.559  1.00 49.66           C  
ANISOU  868  CA  SER A 874     6496   7320   5053    138   -109  -1181       C  
ATOM    869  C   SER A 874       9.409  44.019  23.392  1.00 49.89           C  
ANISOU  869  C   SER A 874     6634   7563   4756    192    -95  -1079       C  
ATOM    870  O   SER A 874       9.926  43.353  24.271  1.00 50.49           O  
ANISOU  870  O   SER A 874     6710   7882   4590    151   -266  -1001       O  
ATOM    871  CB  SER A 874      10.175  46.396  23.088  1.00 51.68           C  
ANISOU  871  CB  SER A 874     6796   7494   5343     21    -52  -1530       C  
ATOM    872  OG  SER A 874       8.840  46.706  23.384  1.00 53.31           O  
ANISOU  872  OG  SER A 874     7127   7661   5465     73    145  -1639       O  
ATOM    873  N   GLN A 875       8.116  43.939  23.091  1.00 50.16           N  
ANISOU  873  N   GLN A 875     6746   7506   4806    283    105  -1051       N  
ATOM    874  CA  GLN A 875       7.185  43.055  23.806  1.00 51.28           C  
ANISOU  874  CA  GLN A 875     6979   7816   4690    331    172   -944       C  
ATOM    875  C   GLN A 875       6.901  41.727  23.090  1.00 48.58           C  
ANISOU  875  C   GLN A 875     6589   7440   4426    444    185   -632       C  
ATOM    876  O   GLN A 875       6.254  40.854  23.664  1.00 48.32           O  
ANISOU  876  O   GLN A 875     6609   7532   4216    477    234   -501       O  
ATOM    877  CB  GLN A 875       5.845  43.763  23.999  1.00 53.51           C  
ANISOU  877  CB  GLN A 875     7341   8008   4980    356    408  -1124       C  
ATOM    878  CG  GLN A 875       5.924  45.060  24.773  1.00 57.22           C  
ANISOU  878  CG  GLN A 875     7872   8479   5388    246    458  -1480       C  
ATOM    879  CD  GLN A 875       6.157  44.789  26.229  1.00 62.33           C  
ANISOU  879  CD  GLN A 875     8631   9445   5604    140    380  -1579       C  
ATOM    880  OE1 GLN A 875       7.276  44.922  26.725  1.00 65.59           O  
ANISOU  880  OE1 GLN A 875     9032  10008   5880     28    161  -1651       O  
ATOM    881  NE2 GLN A 875       5.107  44.354  26.922  1.00 64.72           N  
ANISOU  881  NE2 GLN A 875     9036   9874   5680    170    551  -1560       N  
ATOM    882  N   GLY A 876       7.342  41.574  21.842  1.00 46.38           N  
ANISOU  882  N   GLY A 876     6220   6988   4413    494    167   -526       N  
ATOM    883  CA  GLY A 876       6.985  40.379  21.053  1.00 44.86           C  
ANISOU  883  CA  GLY A 876     5992   6733   4316    587    209   -294       C  
ATOM    884  C   GLY A 876       5.532  40.425  20.600  1.00 43.16           C  
ANISOU  884  C   GLY A 876     5817   6417   4162    648    377   -307       C  
ATOM    885  O   GLY A 876       4.797  41.331  20.965  1.00 43.90           O  
ANISOU  885  O   GLY A 876     5956   6488   4235    635    475   -471       O  
ATOM    886  N   LEU A 877       5.106  39.458  19.803  1.00 42.20           N  
ANISOU  886  N   LEU A 877     5663   6225   4144    710    413   -149       N  
ATOM    887  CA  LEU A 877       3.697  39.374  19.430  1.00 41.81           C  
ANISOU  887  CA  LEU A 877     5619   6104   4162    757    538   -149       C  
ATOM    888  C   LEU A 877       2.901  38.871  20.614  1.00 44.35           C  
ANISOU  888  C   LEU A 877     5977   6555   4319    750    623   -122       C  
ATOM    889  O   LEU A 877       3.301  37.906  21.279  1.00 44.62           O  
ANISOU  889  O   LEU A 877     6023   6704   4224    737    581     19       O  
ATOM    890  CB  LEU A 877       3.496  38.434  18.253  1.00 40.15           C  
ANISOU  890  CB  LEU A 877     5362   5796   4095    797    534    -21       C  
ATOM    891  CG  LEU A 877       4.046  38.932  16.918  1.00 39.37           C  
ANISOU  891  CG  LEU A 877     5251   5578   4129    804    495    -41       C  
ATOM    892  CD1 LEU A 877       4.127  37.785  15.929  1.00 38.54           C  
ANISOU  892  CD1 LEU A 877     5123   5421   4100    819    491     56       C  
ATOM    893  CD2 LEU A 877       3.191  40.051  16.346  1.00 39.58           C  
ANISOU  893  CD2 LEU A 877     5283   5513   4242    828    537   -118       C  
ATOM    894  N   ARG A 878       1.762  39.511  20.865  1.00 46.75           N  
ANISOU  894  N   ARG A 878     6287   6829   4644    763    760   -235       N  
ATOM    895  CA  ARG A 878       0.945  39.189  22.037  1.00 49.21           C  
ANISOU  895  CA  ARG A 878     6638   7266   4791    747    900   -236       C  
ATOM    896  C   ARG A 878      -0.511  38.887  21.723  1.00 48.81           C  
ANISOU  896  C   ARG A 878     6509   7127   4908    794   1053   -203       C  
ATOM    897  O   ARG A 878      -1.038  39.230  20.659  1.00 48.25           O  
ANISOU  897  O   ARG A 878     6353   6905   5073    840   1039   -224       O  
ATOM    898  CB  ARG A 878       1.024  40.319  23.050  1.00 52.06           C  
ANISOU  898  CB  ARG A 878     7082   7715   4983    696    966   -462       C  
ATOM    899  CG  ARG A 878       2.354  40.354  23.778  1.00 55.24           C  
ANISOU  899  CG  ARG A 878     7560   8285   5142    620    804   -482       C  
ATOM    900  CD  ARG A 878       2.395  41.489  24.766  1.00 59.51           C  
ANISOU  900  CD  ARG A 878     8191   8917   5501    543    868   -761       C  
ATOM    901  NE  ARG A 878       2.337  42.765  24.068  1.00 61.14           N  
ANISOU  901  NE  ARG A 878     8351   8908   5970    556    908   -967       N  
ATOM    902  CZ  ARG A 878       1.995  43.923  24.626  1.00 66.06           C  
ANISOU  902  CZ  ARG A 878     9019   9488   6590    516   1044  -1254       C  
ATOM    903  NH1 ARG A 878       1.665  43.998  25.924  1.00 69.69           N  
ANISOU  903  NH1 ARG A 878     9591  10139   6747    447   1166  -1410       N  
ATOM    904  NH2 ARG A 878       1.982  45.018  23.874  1.00 66.78           N  
ANISOU  904  NH2 ARG A 878     9049   9338   6987    542   1076  -1384       N  
ATOM    905  N   ILE A 879      -1.139  38.230  22.687  1.00 49.06           N  
ANISOU  905  N   ILE A 879     6563   7268   4809    774   1193   -134       N  
ATOM    906  CA  ILE A 879      -2.507  37.776  22.581  1.00 49.29           C  
ANISOU  906  CA  ILE A 879     6492   7229   5007    799   1358    -85       C  
ATOM    907  C   ILE A 879      -3.402  38.896  23.051  1.00 50.28           C  
ANISOU  907  C   ILE A 879     6594   7330   5177    817   1548   -287       C  
ATOM    908  O   ILE A 879      -3.281  39.341  24.191  1.00 50.88           O  
ANISOU  908  O   ILE A 879     6780   7540   5010    775   1668   -404       O  
ATOM    909  CB  ILE A 879      -2.770  36.577  23.525  1.00 51.20           C  
ANISOU  909  CB  ILE A 879     6766   7589   5095    761   1474     99       C  
ATOM    910  CG1 ILE A 879      -1.840  35.396  23.224  1.00 50.03           C  
ANISOU  910  CG1 ILE A 879     6632   7442   4933    753   1312    318       C  
ATOM    911  CG2 ILE A 879      -4.229  36.155  23.455  1.00 52.51           C  
ANISOU  911  CG2 ILE A 879     6801   7670   5479    771   1674    135       C  
ATOM    912  CD1 ILE A 879      -2.227  34.591  22.010  1.00 48.94           C  
ANISOU  912  CD1 ILE A 879     6368   7122   5105    773   1265    394       C  
ATOM    913  N   ALA A 880      -4.319  39.333  22.198  1.00 49.89           N  
ANISOU  913  N   ALA A 880     6399   7117   5440    878   1578   -331       N  
ATOM    914  CA  ALA A 880      -5.293  40.343  22.591  1.00 52.12           C  
ANISOU  914  CA  ALA A 880     6611   7331   5860    918   1785   -505       C  
ATOM    915  C   ALA A 880      -5.963  39.998  23.929  1.00 55.29           C  
ANISOU  915  C   ALA A 880     7050   7863   6095    876   2067   -536       C  
ATOM    916  O   ALA A 880      -6.264  38.838  24.195  1.00 55.14           O  
ANISOU  916  O   ALA A 880     7014   7915   6020    842   2121   -358       O  
ATOM    917  CB  ALA A 880      -6.334  40.505  21.508  1.00 51.67           C  
ANISOU  917  CB  ALA A 880     6344   7098   6188    994   1757   -461       C  
ATOM    918  N   PRO A 881      -6.204  41.013  24.776  1.00 59.36           N  
ANISOU  918  N   PRO A 881     7619   8399   6535    873   2274   -769       N  
ATOM    919  CA  PRO A 881      -6.721  40.750  26.127  1.00 63.55           C  
ANISOU  919  CA  PRO A 881     8231   9092   6821    817   2572   -823       C  
ATOM    920  C   PRO A 881      -8.084  40.054  26.105  1.00 66.07           C  
ANISOU  920  C   PRO A 881     8364   9349   7391    845   2792   -700       C  
ATOM    921  O   PRO A 881      -8.850  40.262  25.163  1.00 65.24           O  
ANISOU  921  O   PRO A 881     8036   9047   7701    923   2758   -683       O  
ATOM    922  CB  PRO A 881      -6.849  42.153  26.731  1.00 65.58           C  
ANISOU  922  CB  PRO A 881     8541   9311   7063    820   2765  -1161       C  
ATOM    923  CG  PRO A 881      -7.049  43.038  25.551  1.00 63.92           C  
ANISOU  923  CG  PRO A 881     8163   8831   7293    922   2648  -1217       C  
ATOM    924  CD  PRO A 881      -6.187  42.455  24.469  1.00 59.97           C  
ANISOU  924  CD  PRO A 881     7663   8315   6805    925   2288   -997       C  
ATOM    925  N   PRO A 882      -8.399  39.260  27.151  1.00 69.65           N  
ANISOU  925  N   PRO A 882     8897   9971   7596    777   3016   -603       N  
ATOM    926  CA  PRO A 882      -9.600  38.415  27.153  1.00 71.19           C  
ANISOU  926  CA  PRO A 882     8906  10105   8038    780   3228   -446       C  
ATOM    927  C   PRO A 882     -10.886  39.219  27.069  1.00 73.66           C  
ANISOU  927  C   PRO A 882     8992  10254   8740    850   3493   -625       C  
ATOM    928  O   PRO A 882     -11.869  38.741  26.508  1.00 73.31           O  
ANISOU  928  O   PRO A 882     8693  10074   9084    880   3538   -514       O  
ATOM    929  CB  PRO A 882      -9.520  37.689  28.498  1.00 74.05           C  
ANISOU  929  CB  PRO A 882     9454  10704   7976    686   3459   -332       C  
ATOM    930  CG  PRO A 882      -8.757  38.617  29.376  1.00 75.99           C  
ANISOU  930  CG  PRO A 882     9946  11130   7796    646   3489   -566       C  
ATOM    931  CD  PRO A 882      -7.763  39.309  28.481  1.00 72.42           C  
ANISOU  931  CD  PRO A 882     9509  10582   7422    687   3127   -670       C  
ATOM    932  N   GLU A 883     -10.854  40.431  27.621  1.00 76.65           N  
ANISOU  932  N   GLU A 883     9449  10634   9040    873   3660   -910       N  
ATOM    933  CA  GLU A 883     -12.011  41.328  27.651  1.00 80.42           C  
ANISOU  933  CA  GLU A 883     9710  10932   9913    957   3952  -1108       C  
ATOM    934  C   GLU A 883     -12.455  41.883  26.280  1.00 78.66           C  
ANISOU  934  C   GLU A 883     9209  10441  10237   1082   3730  -1084       C  
ATOM    935  O   GLU A 883     -13.629  42.208  26.101  1.00 80.26           O  
ANISOU  935  O   GLU A 883     9133  10479  10881   1162   3921  -1121       O  
ATOM    936  CB  GLU A 883     -11.787  42.480  28.665  1.00 84.55           C  
ANISOU  936  CB  GLU A 883    10412  11510  10201    937   4217  -1458       C  
ATOM    937  CG  GLU A 883     -10.439  43.218  28.618  1.00 84.24           C  
ANISOU  937  CG  GLU A 883    10605  11520   9882    903   3953  -1614       C  
ATOM    938  CD  GLU A 883     -10.348  44.307  27.549  1.00 84.32           C  
ANISOU  938  CD  GLU A 883    10465  11246  10323   1014   3767  -1715       C  
ATOM    939  OE1 GLU A 883     -11.324  44.518  26.789  1.00 85.31           O  
ANISOU  939  OE1 GLU A 883    10305  11148  10961   1131   3803  -1647       O  
ATOM    940  OE2 GLU A 883      -9.281  44.966  27.469  1.00 83.11           O  
ANISOU  940  OE2 GLU A 883    10474  11097  10007    981   3576  -1847       O  
ATOM    941  N   ALA A 884     -11.538  41.997  25.321  1.00 75.57           N  
ANISOU  941  N   ALA A 884     8880  10011   9821   1099   3335  -1006       N  
ATOM    942  CA  ALA A 884     -11.884  42.573  24.011  1.00 74.47           C  
ANISOU  942  CA  ALA A 884     8515   9650  10128   1211   3106   -955       C  
ATOM    943  C   ALA A 884     -12.951  41.745  23.266  1.00 74.84           C  
ANISOU  943  C   ALA A 884     8270   9628  10536   1236   3036   -753       C  
ATOM    944  O   ALA A 884     -13.062  40.534  23.476  1.00 73.42           O  
ANISOU  944  O   ALA A 884     8101   9560  10232   1149   3054   -610       O  
ATOM    945  CB  ALA A 884     -10.639  42.743  23.148  1.00 71.48           C  
ANISOU  945  CB  ALA A 884     8290   9274   9595   1204   2726   -890       C  
ATOM    946  N   PRO A 885     -13.739  42.399  22.389  1.00 75.43           N  
ANISOU  946  N   PRO A 885     8068   9511  11079   1352   2944   -732       N  
ATOM    947  CA  PRO A 885     -14.806  41.684  21.699  1.00 74.66           C  
ANISOU  947  CA  PRO A 885     7661   9361  11344   1362   2853   -567       C  
ATOM    948  C   PRO A 885     -14.286  40.846  20.539  1.00 71.69           C  
ANISOU  948  C   PRO A 885     7322   9042  10871   1305   2435   -384       C  
ATOM    949  O   PRO A 885     -13.261  41.170  19.916  1.00 67.96           O  
ANISOU  949  O   PRO A 885     7038   8588  10195   1312   2177   -365       O  
ATOM    950  CB  PRO A 885     -15.722  42.804  21.194  1.00 77.44           C  
ANISOU  950  CB  PRO A 885     7710   9500  12212   1517   2865   -602       C  
ATOM    951  CG  PRO A 885     -14.954  44.084  21.358  1.00 78.19           C  
ANISOU  951  CG  PRO A 885     7987   9507  12213   1587   2896   -756       C  
ATOM    952  CD  PRO A 885     -13.573  43.756  21.843  1.00 75.84           C  
ANISOU  952  CD  PRO A 885     8079   9387  11349   1469   2847   -817       C  
ATOM    953  N   VAL A 886     -15.041  39.801  20.234  1.00 72.58           N  
ANISOU  953  N   VAL A 886     7240   9170  11167   1243   2391   -269       N  
ATOM    954  CA  VAL A 886     -14.570  38.694  19.407  1.00 70.12           C  
ANISOU  954  CA  VAL A 886     6994   8929  10719   1144   2089   -143       C  
ATOM    955  C   VAL A 886     -14.565  38.990  17.896  1.00 70.18           C  
ANISOU  955  C   VAL A 886     6901   8893  10869   1187   1677    -71       C  
ATOM    956  O   VAL A 886     -13.981  38.233  17.105  1.00 67.83           O  
ANISOU  956  O   VAL A 886     6710   8658  10401   1107   1418    -10       O  
ATOM    957  CB  VAL A 886     -15.395  37.420  19.726  1.00 71.45           C  
ANISOU  957  CB  VAL A 886     6989   9107  11049   1037   2231    -71       C  
ATOM    958  CG1 VAL A 886     -16.680  37.344  18.895  1.00 73.28           C  
ANISOU  958  CG1 VAL A 886     6824   9244  11776   1052   2092    -31       C  
ATOM    959  CG2 VAL A 886     -14.539  36.183  19.553  1.00 70.21           C  
ANISOU  959  CG2 VAL A 886     7036   9027  10614    915   2098     14       C  
ATOM    960  N   THR A 887     -15.215  40.084  17.499  1.00 72.40           N  
ANISOU  960  N   THR A 887     6979   9067  11462   1314   1628    -72       N  
ATOM    961  CA  THR A 887     -15.191  40.531  16.107  1.00 71.58           C  
ANISOU  961  CA  THR A 887     6802   8941  11452   1369   1236     33       C  
ATOM    962  C   THR A 887     -13.794  41.050  15.793  1.00 67.50           C  
ANISOU  962  C   THR A 887     6616   8457  10570   1380   1112     28       C  
ATOM    963  O   THR A 887     -13.152  41.691  16.636  1.00 66.37           O  
ANISOU  963  O   THR A 887     6652   8284  10278   1412   1329    -75       O  
ATOM    964  CB  THR A 887     -16.200  41.665  15.848  1.00 75.47           C  
ANISOU  964  CB  THR A 887     6986   9288  12402   1526   1228     78       C  
ATOM    965  OG1 THR A 887     -15.808  42.820  16.597  1.00 76.45           O  
ANISOU  965  OG1 THR A 887     7225   9300  12520   1630   1483    -26       O  
ATOM    966  CG2 THR A 887     -17.622  41.251  16.256  1.00 78.66           C  
ANISOU  966  CG2 THR A 887     7010   9639  13236   1525   1398     72       C  
ATOM    967  N   GLY A 888     -13.326  40.762  14.584  1.00 64.82           N  
ANISOU  967  N   GLY A 888     6355   8185  10087   1340    772    125       N  
ATOM    968  CA  GLY A 888     -11.958  41.073  14.199  1.00 61.14           C  
ANISOU  968  CA  GLY A 888     6192   7758   9278   1329    664    132       C  
ATOM    969  C   GLY A 888     -11.010  39.970  14.626  1.00 58.34           C  
ANISOU  969  C   GLY A 888     6068   7508   8588   1203    731     71       C  
ATOM    970  O   GLY A 888      -9.781  40.106  14.482  1.00 57.12           O  
ANISOU  970  O   GLY A 888     6155   7389   8157   1183    683     61       O  
ATOM    971  N   TYR A 889     -11.574  38.880  15.160  1.00 56.34           N  
ANISOU  971  N   TYR A 889     5721   7288   8397   1122    851     48       N  
ATOM    972  CA  TYR A 889     -10.805  37.680  15.487  1.00 52.81           C  
ANISOU  972  CA  TYR A 889     5449   6911   7702   1009    898     36       C  
ATOM    973  C   TYR A 889     -11.511  36.471  14.904  1.00 53.74           C  
ANISOU  973  C   TYR A 889     5410   7034   7973    906    787     60       C  
ATOM    974  O   TYR A 889     -12.248  35.764  15.581  1.00 54.61           O  
ANISOU  974  O   TYR A 889     5381   7117   8248    854    966     61       O  
ATOM    975  CB  TYR A 889     -10.617  37.543  16.985  1.00 51.83           C  
ANISOU  975  CB  TYR A 889     5415   6809   7468    999   1215     -4       C  
ATOM    976  CG  TYR A 889      -9.910  38.725  17.576  1.00 50.20           C  
ANISOU  976  CG  TYR A 889     5364   6603   7103   1071   1312    -79       C  
ATOM    977  CD1 TYR A 889     -10.605  39.680  18.302  1.00 51.86           C  
ANISOU  977  CD1 TYR A 889     5474   6753   7475   1147   1528   -166       C  
ATOM    978  CD2 TYR A 889      -8.553  38.907  17.389  1.00 47.27           C  
ANISOU  978  CD2 TYR A 889     5225   6277   6457   1058   1200    -86       C  
ATOM    979  CE1 TYR A 889      -9.961  40.780  18.837  1.00 51.24           C  
ANISOU  979  CE1 TYR A 889     5538   6654   7275   1196   1624   -279       C  
ATOM    980  CE2 TYR A 889      -7.901  40.000  17.930  1.00 46.98           C  
ANISOU  980  CE2 TYR A 889     5313   6230   6305   1102   1279   -180       C  
ATOM    981  CZ  TYR A 889      -8.617  40.934  18.642  1.00 48.35           C  
ANISOU  981  CZ  TYR A 889     5398   6337   6633   1166   1485   -286       C  
ATOM    982  OH  TYR A 889      -7.989  42.021  19.170  1.00 48.62           O  
ANISOU  982  OH  TYR A 889     5555   6339   6578   1193   1571   -421       O  
ATOM    983  N   MET A 890     -11.261  36.263  13.617  1.00 54.04           N  
ANISOU  983  N   MET A 890     5478   7107   7948    867    499     69       N  
ATOM    984  CA  MET A 890     -11.888  35.226  12.832  1.00 54.86           C  
ANISOU  984  CA  MET A 890     5440   7220   8181    752    333     45       C  
ATOM    985  C   MET A 890     -11.677  33.859  13.476  1.00 52.77           C  
ANISOU  985  C   MET A 890     5222   6916   7912    640    512     16       C  
ATOM    986  O   MET A 890     -12.557  33.005  13.436  1.00 54.24           O  
ANISOU  986  O   MET A 890     5211   7054   8343    544    524     -8       O  
ATOM    987  CB  MET A 890     -11.285  35.261  11.432  1.00 56.98           C  
ANISOU  987  CB  MET A 890     5841   7564   8245    718     32     31       C  
ATOM    988  CG  MET A 890     -12.078  34.526  10.375  1.00 62.79           C  
ANISOU  988  CG  MET A 890     6415   8343   9098    601   -220    -23       C  
ATOM    989  SD  MET A 890     -11.229  34.563   8.782  1.00 67.37           S  
ANISOU  989  SD  MET A 890     7220   9050   9325    547   -525    -60       S  
ATOM    990  CE  MET A 890     -12.611  34.344   7.648  1.00 71.57           C  
ANISOU  990  CE  MET A 890     7477   9682  10032    454   -889    -88       C  
ATOM    991  N   PHE A 891     -10.507  33.653  14.070  1.00 48.91           N  
ANISOU  991  N   PHE A 891     4975   6434   7174    649    645     34       N  
ATOM    992  CA  PHE A 891     -10.211  32.400  14.738  1.00 47.84           C  
ANISOU  992  CA  PHE A 891     4890   6246   7039    565    817     62       C  
ATOM    993  C   PHE A 891      -9.761  32.657  16.178  1.00 46.88           C  
ANISOU  993  C   PHE A 891     4886   6153   6770    625   1079    143       C  
ATOM    994  O   PHE A 891      -8.850  32.013  16.699  1.00 45.64           O  
ANISOU  994  O   PHE A 891     4889   5998   6452    604   1162    208       O  
ATOM    995  CB  PHE A 891      -9.162  31.627  13.938  1.00 46.52           C  
ANISOU  995  CB  PHE A 891     4891   6063   6720    503    688     18       C  
ATOM    996  CG  PHE A 891      -9.623  31.219  12.560  1.00 47.59           C  
ANISOU  996  CG  PHE A 891     4936   6193   6950    410    448    -97       C  
ATOM    997  CD1 PHE A 891     -10.442  30.117  12.384  1.00 49.16           C  
ANISOU  997  CD1 PHE A 891     4963   6305   7409    282    454   -159       C  
ATOM    998  CD2 PHE A 891      -9.222  31.930  11.431  1.00 47.59           C  
ANISOU  998  CD2 PHE A 891     5031   6283   6766    436    217   -147       C  
ATOM    999  CE1 PHE A 891     -10.857  29.735  11.119  1.00 50.70           C  
ANISOU  999  CE1 PHE A 891     5083   6519   7661    172    210   -305       C  
ATOM   1000  CE2 PHE A 891      -9.635  31.546  10.157  1.00 48.82           C  
ANISOU 1000  CE2 PHE A 891     5131   6478   6939    335    -18   -261       C  
ATOM   1001  CZ  PHE A 891     -10.455  30.447  10.004  1.00 50.15           C  
ANISOU 1001  CZ  PHE A 891     5128   6575   7349    198    -34   -358       C  
ATOM   1002  N   GLY A 892     -10.420  33.605  16.826  1.00 47.62           N  
ANISOU 1002  N   GLY A 892     4894   6272   6926    697   1209    136       N  
ATOM   1003  CA  GLY A 892     -10.172  33.882  18.230  1.00 48.08           C  
ANISOU 1003  CA  GLY A 892     5060   6384   6823    732   1474    175       C  
ATOM   1004  C   GLY A 892      -8.927  34.712  18.483  1.00 46.42           C  
ANISOU 1004  C   GLY A 892     5086   6253   6298    794   1426    145       C  
ATOM   1005  O   GLY A 892      -8.218  35.115  17.563  1.00 43.13           O  
ANISOU 1005  O   GLY A 892     4748   5833   5806    818   1211    109       O  
ATOM   1006  N   LYS A 893      -8.668  34.959  19.759  1.00 47.93           N  
ANISOU 1006  N   LYS A 893     5389   6523   6296    806   1636    155       N  
ATOM   1007  CA  LYS A 893      -7.599  35.858  20.164  1.00 48.27           C  
ANISOU 1007  CA  LYS A 893     5629   6649   6062    848   1604     90       C  
ATOM   1008  C   LYS A 893      -6.287  35.097  20.225  1.00 47.30           C  
ANISOU 1008  C   LYS A 893     5676   6583   5712    809   1493    187       C  
ATOM   1009  O   LYS A 893      -5.913  34.563  21.253  1.00 49.61           O  
ANISOU 1009  O   LYS A 893     6068   6968   5813    778   1606    282       O  
ATOM   1010  CB  LYS A 893      -7.923  36.521  21.518  1.00 50.47           C  
ANISOU 1010  CB  LYS A 893     5957   7010   6207    862   1870     14       C  
ATOM   1011  CG  LYS A 893      -9.326  37.121  21.600  1.00 52.16           C  
ANISOU 1011  CG  LYS A 893     5962   7142   6711    906   2053    -73       C  
ATOM   1012  CD  LYS A 893      -9.301  38.530  22.150  1.00 53.38           C  
ANISOU 1012  CD  LYS A 893     6170   7299   6810    967   2180   -260       C  
ATOM   1013  CE  LYS A 893     -10.701  39.055  22.399  1.00 56.32           C  
ANISOU 1013  CE  LYS A 893     6317   7577   7504   1021   2423   -344       C  
ATOM   1014  NZ  LYS A 893     -11.320  38.454  23.614  1.00 59.23           N  
ANISOU 1014  NZ  LYS A 893     6685   8035   7783    963   2765   -325       N  
ATOM   1015  N   GLY A 894      -5.594  35.042  19.101  1.00 45.78           N  
ANISOU 1015  N   GLY A 894     5508   6338   5546    815   1274    178       N  
ATOM   1016  CA  GLY A 894      -4.318  34.357  19.022  1.00 44.01           C  
ANISOU 1016  CA  GLY A 894     5407   6137   5175    793   1174    259       C  
ATOM   1017  C   GLY A 894      -3.330  35.180  18.226  1.00 42.35           C  
ANISOU 1017  C   GLY A 894     5275   5921   4891    824   1004    180       C  
ATOM   1018  O   GLY A 894      -3.526  36.374  18.017  1.00 42.49           O  
ANISOU 1018  O   GLY A 894     5287   5932   4924    863    984     79       O  
ATOM   1019  N   ILE A 895      -2.272  34.519  17.779  1.00 40.95           N  
ANISOU 1019  N   ILE A 895     5159   5726   4671    808    907    236       N  
ATOM   1020  CA  ILE A 895      -1.259  35.125  16.953  1.00 38.91           C  
ANISOU 1020  CA  ILE A 895     4965   5454   4364    824    776    180       C  
ATOM   1021  C   ILE A 895      -1.357  34.458  15.599  1.00 37.86           C  
ANISOU 1021  C   ILE A 895     4796   5234   4354    799    696    165       C  
ATOM   1022  O   ILE A 895      -1.193  33.238  15.493  1.00 37.85           O  
ANISOU 1022  O   ILE A 895     4776   5178   4423    765    719    216       O  
ATOM   1023  CB  ILE A 895       0.133  34.907  17.536  1.00 39.00           C  
ANISOU 1023  CB  ILE A 895     5057   5521   4237    823    745    241       C  
ATOM   1024  CG1 ILE A 895       0.187  35.455  18.960  1.00 41.16           C  
ANISOU 1024  CG1 ILE A 895     5383   5923   4332    822    807    240       C  
ATOM   1025  CG2 ILE A 895       1.170  35.624  16.694  1.00 38.60           C  
ANISOU 1025  CG2 ILE A 895     5048   5444   4171    832    643    177       C  
ATOM   1026  CD1 ILE A 895       1.447  35.057  19.692  1.00 42.54           C  
ANISOU 1026  CD1 ILE A 895     5612   6189   4361    811    740    339       C  
ATOM   1027  N   TYR A 896      -1.590  35.283  14.578  1.00 36.27           N  
ANISOU 1027  N   TYR A 896     4591   5015   4172    812    604     96       N  
ATOM   1028  CA  TYR A 896      -1.969  34.839  13.245  1.00 35.95           C  
ANISOU 1028  CA  TYR A 896     4524   4937   4197    775    509     57       C  
ATOM   1029  C   TYR A 896      -0.803  34.958  12.253  1.00 35.48           C  
ANISOU 1029  C   TYR A 896     4572   4872   4036    765    450     31       C  
ATOM   1030  O   TYR A 896      -0.175  36.005  12.135  1.00 35.47           O  
ANISOU 1030  O   TYR A 896     4630   4888   3957    800    429     39       O  
ATOM   1031  CB  TYR A 896      -3.100  35.714  12.720  1.00 36.11           C  
ANISOU 1031  CB  TYR A 896     4462   4968   4289    800    427     39       C  
ATOM   1032  CG  TYR A 896      -4.456  35.527  13.366  1.00 36.50           C  
ANISOU 1032  CG  TYR A 896     4356   5006   4503    801    489     46       C  
ATOM   1033  CD1 TYR A 896      -4.659  35.789  14.711  1.00 36.46           C  
ANISOU 1033  CD1 TYR A 896     4332   5014   4508    834    650     65       C  
ATOM   1034  CD2 TYR A 896      -5.555  35.144  12.601  1.00 37.15           C  
ANISOU 1034  CD2 TYR A 896     4305   5078   4731    761    388     24       C  
ATOM   1035  CE1 TYR A 896      -5.910  35.656  15.283  1.00 37.19           C  
ANISOU 1035  CE1 TYR A 896     4274   5091   4765    835    751     69       C  
ATOM   1036  CE2 TYR A 896      -6.800  35.002  13.166  1.00 38.22           C  
ANISOU 1036  CE2 TYR A 896     4262   5192   5067    760    457     33       C  
ATOM   1037  CZ  TYR A 896      -6.970  35.262  14.507  1.00 38.05           C  
ANISOU 1037  CZ  TYR A 896     4222   5167   5068    801    660     59       C  
ATOM   1038  OH  TYR A 896      -8.215  35.120  15.057  1.00 39.30           O  
ANISOU 1038  OH  TYR A 896     4193   5297   5439    797    773     66       O  
ATOM   1039  N   PHE A 897      -0.541  33.887  11.521  1.00 35.23           N  
ANISOU 1039  N   PHE A 897     4557   4800   4027    709    447    -13       N  
ATOM   1040  CA  PHE A 897       0.519  33.870  10.536  1.00 35.25           C  
ANISOU 1040  CA  PHE A 897     4658   4795   3940    691    440    -58       C  
ATOM   1041  C   PHE A 897      -0.019  33.449   9.173  1.00 36.18           C  
ANISOU 1041  C   PHE A 897     4802   4930   4015    618    362   -161       C  
ATOM   1042  O   PHE A 897      -1.140  32.949   9.083  1.00 37.49           O  
ANISOU 1042  O   PHE A 897     4884   5094   4264    573    303   -203       O  
ATOM   1043  CB  PHE A 897       1.587  32.899  10.985  1.00 34.82           C  
ANISOU 1043  CB  PHE A 897     4608   4667   3953    692    546    -43       C  
ATOM   1044  CG  PHE A 897       2.307  33.338  12.218  1.00 34.13           C  
ANISOU 1044  CG  PHE A 897     4508   4606   3854    749    576     59       C  
ATOM   1045  CD1 PHE A 897       1.815  33.014  13.471  1.00 34.09           C  
ANISOU 1045  CD1 PHE A 897     4448   4618   3886    766    607    143       C  
ATOM   1046  CD2 PHE A 897       3.486  34.073  12.123  1.00 33.44           C  
ANISOU 1046  CD2 PHE A 897     4461   4536   3707    772    574     69       C  
ATOM   1047  CE1 PHE A 897       2.482  33.416  14.609  1.00 34.15           C  
ANISOU 1047  CE1 PHE A 897     4462   4689   3823    802    610    225       C  
ATOM   1048  CE2 PHE A 897       4.167  34.473  13.259  1.00 33.18           C  
ANISOU 1048  CE2 PHE A 897     4406   4545   3654    804    567    138       C  
ATOM   1049  CZ  PHE A 897       3.660  34.144  14.508  1.00 33.90           C  
ANISOU 1049  CZ  PHE A 897     4463   4683   3734    817    572    211       C  
ATOM   1050  N   ALA A 898       0.775  33.661   8.125  1.00 35.63           N  
ANISOU 1050  N   ALA A 898     4844   4885   3807    595    365   -208       N  
ATOM   1051  CA  ALA A 898       0.448  33.163   6.782  1.00 37.34           C  
ANISOU 1051  CA  ALA A 898     5126   5148   3912    505    304   -336       C  
ATOM   1052  C   ALA A 898       1.643  32.440   6.153  1.00 38.04           C  
ANISOU 1052  C   ALA A 898     5311   5181   3959    464    453   -448       C  
ATOM   1053  O   ALA A 898       2.799  32.721   6.492  1.00 36.81           O  
ANISOU 1053  O   ALA A 898     5176   4980   3828    518    570   -387       O  
ATOM   1054  CB  ALA A 898       0.000  34.314   5.889  1.00 37.89           C  
ANISOU 1054  CB  ALA A 898     5258   5345   3793    510    154   -270       C  
ATOM   1055  N   ASP A 899       1.359  31.516   5.235  1.00 40.34           N  
ANISOU 1055  N   ASP A 899     5648   5473   4206    361    455   -631       N  
ATOM   1056  CA  ASP A 899       2.408  30.873   4.447  1.00 42.31           C  
ANISOU 1056  CA  ASP A 899     6000   5670   4404    313    626   -782       C  
ATOM   1057  C   ASP A 899       2.613  31.533   3.092  1.00 44.23           C  
ANISOU 1057  C   ASP A 899     6416   6073   4316    256    596   -833       C  
ATOM   1058  O   ASP A 899       3.416  31.055   2.298  1.00 46.37           O  
ANISOU 1058  O   ASP A 899     6793   6326   4499    201    763   -985       O  
ATOM   1059  CB  ASP A 899       2.183  29.350   4.304  1.00 44.34           C  
ANISOU 1059  CB  ASP A 899     6216   5789   4841    227    715   -994       C  
ATOM   1060  CG  ASP A 899       0.898  28.984   3.575  1.00 46.49           C  
ANISOU 1060  CG  ASP A 899     6495   6148   5019     98    544  -1157       C  
ATOM   1061  OD1 ASP A 899       0.269  29.855   2.954  1.00 47.66           O  
ANISOU 1061  OD1 ASP A 899     6699   6489   4918     74    349  -1111       O  
ATOM   1062  OD2 ASP A 899       0.516  27.799   3.625  1.00 48.24           O  
ANISOU 1062  OD2 ASP A 899     6649   6233   5445     17    596  -1325       O  
ATOM   1063  N   MET A 900       1.907  32.627   2.826  1.00 45.66           N  
ANISOU 1063  N   MET A 900     6623   6403   4322    272    403   -693       N  
ATOM   1064  CA  MET A 900       2.130  33.393   1.599  1.00 49.31           C  
ANISOU 1064  CA  MET A 900     7257   7027   4449    232    367   -660       C  
ATOM   1065  C   MET A 900       2.200  34.888   1.858  1.00 47.50           C  
ANISOU 1065  C   MET A 900     7023   6837   4186    332    296   -391       C  
ATOM   1066  O   MET A 900       1.238  35.492   2.313  1.00 48.12           O  
ANISOU 1066  O   MET A 900     7001   6938   4342    385    114   -262       O  
ATOM   1067  CB  MET A 900       1.070  33.048   0.540  1.00 54.84           C  
ANISOU 1067  CB  MET A 900     8026   7898   4911    110    162   -787       C  
ATOM   1068  CG  MET A 900       1.197  31.600   0.071  1.00 58.64           C  
ANISOU 1068  CG  MET A 900     8551   8326   5403    -17    279  -1112       C  
ATOM   1069  SD  MET A 900       0.241  31.125  -1.369  1.00 68.22           S  
ANISOU 1069  SD  MET A 900     9892   9771   6258   -210     63  -1347       S  
ATOM   1070  CE  MET A 900       1.100  31.964  -2.701  1.00 69.62           C  
ANISOU 1070  CE  MET A 900    10354  10166   5930   -244    145  -1284       C  
ATOM   1071  N   VAL A 901       3.348  35.478   1.532  1.00 46.66           N  
ANISOU 1071  N   VAL A 901     7013   6717   3995    352    464   -319       N  
ATOM   1072  CA  VAL A 901       3.658  36.869   1.884  1.00 45.45           C  
ANISOU 1072  CA  VAL A 901     6842   6536   3887    440    456    -84       C  
ATOM   1073  C   VAL A 901       2.594  37.891   1.452  1.00 46.39           C  
ANISOU 1073  C   VAL A 901     6978   6763   3884    467    224    105       C  
ATOM   1074  O   VAL A 901       2.375  38.878   2.137  1.00 44.48           O  
ANISOU 1074  O   VAL A 901     6645   6445   3810    557    173    267       O  
ATOM   1075  CB  VAL A 901       5.063  37.279   1.347  1.00 45.91           C  
ANISOU 1075  CB  VAL A 901     7006   6569   3866    425    691    -46       C  
ATOM   1076  CG1 VAL A 901       5.118  37.263  -0.175  1.00 48.59           C  
ANISOU 1076  CG1 VAL A 901     7554   7073   3832    331    727    -66       C  
ATOM   1077  CG2 VAL A 901       5.484  38.636   1.887  1.00 44.75           C  
ANISOU 1077  CG2 VAL A 901     6806   6338   3856    501    708    164       C  
ATOM   1078  N   SER A 902       1.936  37.647   0.323  1.00 49.82           N  
ANISOU 1078  N   SER A 902     7519   7372   4037    389     80     80       N  
ATOM   1079  CA  SER A 902       0.909  38.556  -0.184  1.00 51.70           C  
ANISOU 1079  CA  SER A 902     7753   7728   4160    421   -176    295       C  
ATOM   1080  C   SER A 902      -0.207  38.746   0.838  1.00 50.36           C  
ANISOU 1080  C   SER A 902     7360   7477   4297    506   -342    343       C  
ATOM   1081  O   SER A 902      -0.660  39.868   1.068  1.00 50.49           O  
ANISOU 1081  O   SER A 902     7300   7449   4434    605   -437    564       O  
ATOM   1082  CB  SER A 902       0.325  38.014  -1.482  1.00 55.40           C  
ANISOU 1082  CB  SER A 902     8355   8433   4262    300   -348    216       C  
ATOM   1083  OG  SER A 902      -0.402  36.826  -1.225  1.00 56.03           O  
ANISOU 1083  OG  SER A 902     8332   8520   4435    228   -442    -33       O  
ATOM   1084  N   LYS A 903      -0.635  37.645   1.453  1.00 49.07           N  
ANISOU 1084  N   LYS A 903     7085   7272   4284    467   -344    138       N  
ATOM   1085  CA  LYS A 903      -1.615  37.693   2.534  1.00 47.85           C  
ANISOU 1085  CA  LYS A 903     6715   7030   4434    537   -431    160       C  
ATOM   1086  C   LYS A 903      -1.118  38.586   3.664  1.00 44.99           C  
ANISOU 1086  C   LYS A 903     6289   6510   4294    654   -287    271       C  
ATOM   1087  O   LYS A 903      -1.783  39.552   4.028  1.00 44.95           O  
ANISOU 1087  O   LYS A 903     6179   6460   4437    744   -371    418       O  
ATOM   1088  CB  LYS A 903      -1.914  36.273   3.041  1.00 48.75           C  
ANISOU 1088  CB  LYS A 903     6743   7099   4678    463   -386    -68       C  
ATOM   1089  CG  LYS A 903      -2.795  36.145   4.288  1.00 48.82           C  
ANISOU 1089  CG  LYS A 903     6538   7007   5003    520   -397    -57       C  
ATOM   1090  CD  LYS A 903      -4.267  36.402   4.033  1.00 51.54           C  
ANISOU 1090  CD  LYS A 903     6722   7428   5432    524   -640      5       C  
ATOM   1091  CE  LYS A 903      -5.073  36.406   5.335  1.00 52.05           C  
ANISOU 1091  CE  LYS A 903     6570   7378   5827    591   -584     25       C  
ATOM   1092  NZ  LYS A 903      -6.372  37.162   5.233  1.00 53.82           N  
ANISOU 1092  NZ  LYS A 903     6601   7638   6207    654   -780    157       N  
ATOM   1093  N   SER A 904       0.053  38.268   4.209  1.00 42.69           N  
ANISOU 1093  N   SER A 904     6049   6130   4041    647    -76    188       N  
ATOM   1094  CA  SER A 904       0.609  39.028   5.326  1.00 40.29           C  
ANISOU 1094  CA  SER A 904     5688   5697   3922    729     43    248       C  
ATOM   1095  C   SER A 904       0.862  40.487   4.982  1.00 41.04           C  
ANISOU 1095  C   SER A 904     5827   5754   4011    786     36    430       C  
ATOM   1096  O   SER A 904       0.729  41.360   5.832  1.00 40.46           O  
ANISOU 1096  O   SER A 904     5670   5574   4129    859     63    483       O  
ATOM   1097  CB  SER A 904       1.911  38.402   5.802  1.00 39.29           C  
ANISOU 1097  CB  SER A 904     5597   5508   3820    701    230    146       C  
ATOM   1098  OG  SER A 904       1.664  37.308   6.667  1.00 39.43           O  
ANISOU 1098  OG  SER A 904     5527   5494   3958    690    258     37       O  
ATOM   1099  N   ALA A 905       1.222  40.752   3.732  1.00 42.54           N  
ANISOU 1099  N   ALA A 905     6156   6024   3983    746     19    521       N  
ATOM   1100  CA  ALA A 905       1.689  42.084   3.329  1.00 43.77           C  
ANISOU 1100  CA  ALA A 905     6371   6117   4140    788     60    723       C  
ATOM   1101  C   ALA A 905       0.589  43.164   3.296  1.00 44.66           C  
ANISOU 1101  C   ALA A 905     6395   6189   4384    883   -103    925       C  
ATOM   1102  O   ALA A 905       0.879  44.357   3.385  1.00 45.85           O  
ANISOU 1102  O   ALA A 905     6540   6206   4674    942    -43   1081       O  
ATOM   1103  CB  ALA A 905       2.377  41.994   1.975  1.00 45.95           C  
ANISOU 1103  CB  ALA A 905     6836   6507   4113    711    117    786       C  
ATOM   1104  N   ASN A 906      -0.664  42.746   3.160  1.00 44.95           N  
ANISOU 1104  N   ASN A 906     6340   6319   4418    897   -302    921       N  
ATOM   1105  CA  ASN A 906      -1.791  43.666   3.263  1.00 46.06           C  
ANISOU 1105  CA  ASN A 906     6336   6400   4764   1005   -455   1101       C  
ATOM   1106  C   ASN A 906      -1.969  44.265   4.654  1.00 44.71           C  
ANISOU 1106  C   ASN A 906     6012   6027   4948   1094   -332   1038       C  
ATOM   1107  O   ASN A 906      -2.582  45.319   4.796  1.00 46.06           O  
ANISOU 1107  O   ASN A 906     6075   6074   5351   1199   -372   1190       O  
ATOM   1108  CB  ASN A 906      -3.078  42.962   2.880  1.00 47.43           C  
ANISOU 1108  CB  ASN A 906     6402   6723   4896    986   -697   1081       C  
ATOM   1109  CG  ASN A 906      -3.085  42.515   1.439  1.00 49.96           C  
ANISOU 1109  CG  ASN A 906     6875   7270   4836    890   -867   1139       C  
ATOM   1110  OD1 ASN A 906      -2.702  43.267   0.527  1.00 51.19           O  
ANISOU 1110  OD1 ASN A 906     7167   7475   4806    900   -899   1361       O  
ATOM   1111  ND2 ASN A 906      -3.522  41.281   1.219  1.00 50.13           N  
ANISOU 1111  ND2 ASN A 906     6883   7430   4733    785   -964    936       N  
ATOM   1112  N   TYR A 907      -1.442  43.597   5.675  1.00 42.28           N  
ANISOU 1112  N   TYR A 907     5697   5687   4681   1052   -179    818       N  
ATOM   1113  CA  TYR A 907      -1.589  44.066   7.045  1.00 41.61           C  
ANISOU 1113  CA  TYR A 907     5497   5456   4856   1112    -55    721       C  
ATOM   1114  C   TYR A 907      -0.551  45.114   7.415  1.00 41.83           C  
ANISOU 1114  C   TYR A 907     5582   5329   4979   1124     96    733       C  
ATOM   1115  O   TYR A 907      -0.528  45.593   8.549  1.00 41.21           O  
ANISOU 1115  O   TYR A 907     5436   5135   5085   1153    208    618       O  
ATOM   1116  CB  TYR A 907      -1.556  42.877   8.001  1.00 39.96           C  
ANISOU 1116  CB  TYR A 907     5255   5305   4620   1058     17    515       C  
ATOM   1117  CG  TYR A 907      -2.765  41.996   7.813  1.00 41.00           C  
ANISOU 1117  CG  TYR A 907     5279   5533   4764   1046   -111    493       C  
ATOM   1118  CD1 TYR A 907      -4.003  42.351   8.353  1.00 41.93           C  
ANISOU 1118  CD1 TYR A 907     5215   5599   5118   1120   -140    512       C  
ATOM   1119  CD2 TYR A 907      -2.693  40.838   7.054  1.00 41.35           C  
ANISOU 1119  CD2 TYR A 907     5388   5706   4618    954   -191    440       C  
ATOM   1120  CE1 TYR A 907      -5.120  41.558   8.158  1.00 42.97           C  
ANISOU 1120  CE1 TYR A 907     5212   5810   5303   1097   -261    494       C  
ATOM   1121  CE2 TYR A 907      -3.807  40.036   6.864  1.00 42.32           C  
ANISOU 1121  CE2 TYR A 907     5394   5902   4782    920   -318    397       C  
ATOM   1122  CZ  TYR A 907      -5.011  40.402   7.415  1.00 43.43           C  
ANISOU 1122  CZ  TYR A 907     5337   5996   5168    989   -361    434       C  
ATOM   1123  OH  TYR A 907      -6.110  39.601   7.213  1.00 46.71           O  
ANISOU 1123  OH  TYR A 907     5605   6478   5663    943   -488    391       O  
ATOM   1124  N   CYS A 908       0.304  45.458   6.451  1.00 42.68           N  
ANISOU 1124  N   CYS A 908     5818   5442   4956   1088    111    860       N  
ATOM   1125  CA  CYS A 908       1.240  46.572   6.572  1.00 42.74           C  
ANISOU 1125  CA  CYS A 908     5863   5279   5095   1089    247    912       C  
ATOM   1126  C   CYS A 908       0.551  47.906   6.291  1.00 44.50           C  
ANISOU 1126  C   CYS A 908     6020   5333   5554   1191    211   1119       C  
ATOM   1127  O   CYS A 908       1.075  48.962   6.630  1.00 45.00           O  
ANISOU 1127  O   CYS A 908     6070   5192   5835   1205    336   1135       O  
ATOM   1128  CB  CYS A 908       2.399  46.398   5.583  1.00 43.15           C  
ANISOU 1128  CB  CYS A 908     6064   5393   4935   1007    312    993       C  
ATOM   1129  SG  CYS A 908       3.367  44.887   5.792  1.00 42.06           S  
ANISOU 1129  SG  CYS A 908     5982   5401   4595    903    390    772       S  
ATOM   1130  N   HIS A 909      -0.608  47.862   5.643  1.00 45.89           N  
ANISOU 1130  N   HIS A 909     6138   5581   5715   1261     32   1283       N  
ATOM   1131  CA  HIS A 909      -1.328  49.075   5.255  1.00 48.60           C  
ANISOU 1131  CA  HIS A 909     6395   5763   6308   1380    -31   1538       C  
ATOM   1132  C   HIS A 909      -0.428  50.143   4.642  1.00 51.12           C  
ANISOU 1132  C   HIS A 909     6817   5925   6681   1374     73   1748       C  
ATOM   1133  O   HIS A 909      -0.582  51.327   4.937  1.00 53.31           O  
ANISOU 1133  O   HIS A 909     7008   5939   7308   1458    152   1844       O  
ATOM   1134  CB  HIS A 909      -2.066  49.647   6.459  1.00 48.23           C  
ANISOU 1134  CB  HIS A 909     6163   5519   6642   1473     52   1402       C  
ATOM   1135  CG  HIS A 909      -3.237  48.828   6.869  1.00 47.47           C  
ANISOU 1135  CG  HIS A 909     5926   5547   6562   1505    -54   1297       C  
ATOM   1136  ND1 HIS A 909      -3.126  47.746   7.712  1.00 45.24           N  
ANISOU 1136  ND1 HIS A 909     5652   5389   6148   1426     10   1029       N  
ATOM   1137  CD2 HIS A 909      -4.540  48.908   6.525  1.00 49.42           C  
ANISOU 1137  CD2 HIS A 909     6004   5811   6962   1603   -222   1446       C  
ATOM   1138  CE1 HIS A 909      -4.316  47.200   7.880  1.00 45.76           C  
ANISOU 1138  CE1 HIS A 909     5566   5530   6290   1466    -87   1007       C  
ATOM   1139  NE2 HIS A 909      -5.192  47.891   7.175  1.00 48.34           N  
ANISOU 1139  NE2 HIS A 909     5770   5796   6798   1571   -234   1244       N  
ATOM   1140  N   THR A 910       0.497  49.726   3.783  1.00 52.03           N  
ANISOU 1140  N   THR A 910     7107   6181   6479   1274     99   1814       N  
ATOM   1141  CA  THR A 910       1.428  50.654   3.168  1.00 54.75           C  
ANISOU 1141  CA  THR A 910     7553   6386   6862   1249    235   2022       C  
ATOM   1142  C   THR A 910       0.731  51.322   2.002  1.00 58.94           C  
ANISOU 1142  C   THR A 910     8113   6930   7351   1333     79   2433       C  
ATOM   1143  O   THR A 910      -0.117  50.716   1.352  1.00 58.46           O  
ANISOU 1143  O   THR A 910     8062   7099   7050   1353   -149   2529       O  
ATOM   1144  CB  THR A 910       2.706  49.965   2.653  1.00 54.67           C  
ANISOU 1144  CB  THR A 910     7710   6521   6538   1110    362   1948       C  
ATOM   1145  OG1 THR A 910       2.414  49.275   1.439  1.00 57.96           O  
ANISOU 1145  OG1 THR A 910     8264   7206   6552   1078    226   2091       O  
ATOM   1146  CG2 THR A 910       3.266  48.975   3.670  1.00 50.93           C  
ANISOU 1146  CG2 THR A 910     7200   6110   6041   1037    441   1577       C  
ATOM   1147  N   SER A 911       1.123  52.567   1.746  1.00 63.19           N  
ANISOU 1147  N   SER A 911     8658   7218   8131   1372    199   2681       N  
ATOM   1148  CA  SER A 911       0.451  53.452   0.804  1.00 68.36           C  
ANISOU 1148  CA  SER A 911     9307   7808   8855   1482     65   3133       C  
ATOM   1149  C   SER A 911       1.339  53.746  -0.392  1.00 71.54           C  
ANISOU 1149  C   SER A 911     9923   8279   8980   1404    156   3439       C  
ATOM   1150  O   SER A 911       2.551  53.528  -0.345  1.00 71.45           O  
ANISOU 1150  O   SER A 911    10020   8264   8862   1277    382   3287       O  
ATOM   1151  CB  SER A 911       0.150  54.774   1.499  1.00 70.41           C  
ANISOU 1151  CB  SER A 911     9390   7656   9703   1603    173   3212       C  
ATOM   1152  OG  SER A 911       1.347  55.319   2.048  1.00 70.06           O  
ANISOU 1152  OG  SER A 911     9379   7372   9869   1513    461   3051       O  
ATOM   1153  N   GLN A 912       0.739  54.270  -1.453  1.00 75.57           N  
ANISOU 1153  N   GLN A 912    10482   8847   9384   1483    -15   3891       N  
ATOM   1154  CA  GLN A 912       1.507  54.742  -2.597  1.00 78.97           C  
ANISOU 1154  CA  GLN A 912    11119   9315   9568   1421     95   4256       C  
ATOM   1155  C   GLN A 912       2.456  55.876  -2.191  1.00 79.71           C  
ANISOU 1155  C   GLN A 912    11177   8999  10107   1408    419   4324       C  
ATOM   1156  O   GLN A 912       3.532  56.024  -2.772  1.00 80.30           O  
ANISOU 1156  O   GLN A 912    11412   9079  10018   1296    641   4436       O  
ATOM   1157  CB  GLN A 912       0.573  55.217  -3.703  1.00 84.25           C  
ANISOU 1157  CB  GLN A 912    11824  10106  10080   1528   -182   4779       C  
ATOM   1158  CG  GLN A 912      -0.339  54.132  -4.249  1.00 85.24           C  
ANISOU 1158  CG  GLN A 912    11987  10659   9739   1511   -532   4725       C  
ATOM   1159  CD  GLN A 912      -0.782  54.407  -5.677  1.00 92.24           C  
ANISOU 1159  CD  GLN A 912    13027  11800  10220   1533   -780   5245       C  
ATOM   1160  OE1 GLN A 912      -1.152  55.535  -6.032  1.00 97.50           O  
ANISOU 1160  OE1 GLN A 912    13629  12272  11144   1667   -848   5729       O  
ATOM   1161  NE2 GLN A 912      -0.742  53.376  -6.511  1.00 93.47           N  
ANISOU 1161  NE2 GLN A 912    13389  12391   9732   1398   -915   5153       N  
ATOM   1162  N   GLY A 913       2.052  56.659  -1.186  1.00 79.71           N  
ANISOU 1162  N   GLY A 913    10961   8642  10683   1513    462   4229       N  
ATOM   1163  CA  GLY A 913       2.846  57.780  -0.668  1.00 80.17           C  
ANISOU 1163  CA  GLY A 913    10951   8267  11243   1492    756   4229       C  
ATOM   1164  C   GLY A 913       4.078  57.379   0.125  1.00 76.98           C  
ANISOU 1164  C   GLY A 913    10558   7827  10861   1326    997   3780       C  
ATOM   1165  O   GLY A 913       5.130  57.985  -0.028  1.00 78.33           O  
ANISOU 1165  O   GLY A 913    10769   7800  11192   1230   1245   3852       O  
ATOM   1166  N   ASP A 914       3.946  56.377   0.993  1.00 73.60           N  
ANISOU 1166  N   ASP A 914    10076   7581  10305   1290    921   3337       N  
ATOM   1167  CA  ASP A 914       5.101  55.799   1.700  1.00 71.00           C  
ANISOU 1167  CA  ASP A 914     9755   7290   9930   1137   1092   2936       C  
ATOM   1168  C   ASP A 914       5.081  54.267   1.519  1.00 65.88           C  
ANISOU 1168  C   ASP A 914     9201   7053   8776   1082    965   2739       C  
ATOM   1169  O   ASP A 914       4.602  53.533   2.385  1.00 62.58           O  
ANISOU 1169  O   ASP A 914     8700   6739   8336   1101    856   2431       O  
ATOM   1170  CB  ASP A 914       5.113  56.206   3.190  1.00 71.20           C  
ANISOU 1170  CB  ASP A 914     9602   7062  10386   1137   1164   2555       C  
ATOM   1171  CG  ASP A 914       6.378  55.713   3.938  1.00 70.85           C  
ANISOU 1171  CG  ASP A 914     9546   7057  10316    974   1305   2179       C  
ATOM   1172  OD1 ASP A 914       7.437  55.511   3.287  1.00 72.17           O  
ANISOU 1172  OD1 ASP A 914     9799   7294  10327    864   1435   2265       O  
ATOM   1173  OD2 ASP A 914       6.309  55.526   5.181  1.00 68.89           O  
ANISOU 1173  OD2 ASP A 914     9193   6779  10202    956   1287   1807       O  
ATOM   1174  N   PRO A 915       5.613  53.786   0.383  1.00 64.36           N  
ANISOU 1174  N   PRO A 915     9187   7083   8184   1007   1007   2916       N  
ATOM   1175  CA  PRO A 915       5.417  52.413  -0.041  1.00 61.91           C  
ANISOU 1175  CA  PRO A 915     8983   7142   7396    966    881   2781       C  
ATOM   1176  C   PRO A 915       6.491  51.440   0.451  1.00 58.15           C  
ANISOU 1176  C   PRO A 915     8509   6758   6825    845   1033   2420       C  
ATOM   1177  O   PRO A 915       6.884  50.543  -0.286  1.00 57.94           O  
ANISOU 1177  O   PRO A 915     8618   6970   6426    771   1074   2387       O  
ATOM   1178  CB  PRO A 915       5.471  52.544  -1.557  1.00 64.99           C  
ANISOU 1178  CB  PRO A 915     9578   7701   7413    942    882   3164       C  
ATOM   1179  CG  PRO A 915       6.529  53.575  -1.759  1.00 67.24           C  
ANISOU 1179  CG  PRO A 915     9881   7725   7940    887   1168   3353       C  
ATOM   1180  CD  PRO A 915       6.427  54.526  -0.598  1.00 66.93           C  
ANISOU 1180  CD  PRO A 915     9631   7311   8486    949   1207   3252       C  
ATOM   1181  N   ILE A 916       6.949  51.616   1.685  1.00 55.41           N  
ANISOU 1181  N   ILE A 916     8009   6227   6817    826   1112   2150       N  
ATOM   1182  CA  ILE A 916       7.888  50.693   2.312  1.00 52.42           C  
ANISOU 1182  CA  ILE A 916     7587   5930   6398    733   1204   1825       C  
ATOM   1183  C   ILE A 916       7.175  50.008   3.474  1.00 48.71           C  
ANISOU 1183  C   ILE A 916     7009   5526   5970    782   1037   1542       C  
ATOM   1184  O   ILE A 916       6.417  50.650   4.194  1.00 47.62           O  
ANISOU 1184  O   ILE A 916     6776   5247   6069    856    956   1516       O  
ATOM   1185  CB  ILE A 916       9.146  51.418   2.836  1.00 53.26           C  
ANISOU 1185  CB  ILE A 916     7593   5801   6841    644   1417   1744       C  
ATOM   1186  CG1 ILE A 916       9.780  52.278   1.741  1.00 56.99           C  
ANISOU 1186  CG1 ILE A 916     8154   6154   7345    595   1618   2063       C  
ATOM   1187  CG2 ILE A 916      10.169  50.421   3.357  1.00 51.57           C  
ANISOU 1187  CG2 ILE A 916     7315   5695   6583    556   1489   1461       C  
ATOM   1188  CD1 ILE A 916      10.599  51.496   0.742  1.00 58.10           C  
ANISOU 1188  CD1 ILE A 916     8422   6495   7158    511   1779   2113       C  
ATOM   1189  N   GLY A 917       7.417  48.710   3.656  1.00 46.29           N  
ANISOU 1189  N   GLY A 917     6716   5417   5452    741   1011   1337       N  
ATOM   1190  CA  GLY A 917       6.702  47.941   4.670  1.00 43.91           C  
ANISOU 1190  CA  GLY A 917     6331   5199   5154    783    866   1113       C  
ATOM   1191  C   GLY A 917       7.592  46.976   5.407  1.00 42.30           C  
ANISOU 1191  C   GLY A 917     6069   5061   4940    719    923    869       C  
ATOM   1192  O   GLY A 917       8.635  46.588   4.904  1.00 43.20           O  
ANISOU 1192  O   GLY A 917     6216   5210   4988    650   1056    864       O  
ATOM   1193  N   LEU A 918       7.172  46.580   6.604  1.00 40.92           N  
ANISOU 1193  N   LEU A 918     5801   4906   4839    745    831    684       N  
ATOM   1194  CA  LEU A 918       7.909  45.606   7.388  1.00 39.20           C  
ANISOU 1194  CA  LEU A 918     5519   4764   4609    701    845    496       C  
ATOM   1195  C   LEU A 918       7.080  44.343   7.574  1.00 38.26           C  
ANISOU 1195  C   LEU A 918     5413   4801   4324    737    739    423       C  
ATOM   1196  O   LEU A 918       5.904  44.416   7.890  1.00 37.62           O  
ANISOU 1196  O   LEU A 918     5317   4736   4238    794    636    425       O  
ATOM   1197  CB  LEU A 918       8.288  46.201   8.739  1.00 39.20           C  
ANISOU 1197  CB  LEU A 918     5406   4668   4818    678    835    345       C  
ATOM   1198  CG  LEU A 918       9.271  47.381   8.696  1.00 40.94           C  
ANISOU 1198  CG  LEU A 918     5581   4709   5265    610    946    363       C  
ATOM   1199  CD1 LEU A 918       9.495  47.990  10.084  1.00 41.00           C  
ANISOU 1199  CD1 LEU A 918     5485   4637   5454    569    906    161       C  
ATOM   1200  CD2 LEU A 918      10.589  46.969   8.057  1.00 41.02           C  
ANISOU 1200  CD2 LEU A 918     5572   4739   5274    538   1067    400       C  
ATOM   1201  N   ILE A 919       7.699  43.187   7.337  1.00 39.10           N  
ANISOU 1201  N   ILE A 919     5529   4995   4331    703    785    362       N  
ATOM   1202  CA  ILE A 919       7.063  41.898   7.571  1.00 39.49           C  
ANISOU 1202  CA  ILE A 919     5573   5151   4277    721    712    281       C  
ATOM   1203  C   ILE A 919       8.033  41.013   8.325  1.00 39.31           C  
ANISOU 1203  C   ILE A 919     5465   5136   4334    701    759    183       C  
ATOM   1204  O   ILE A 919       9.228  41.030   8.049  1.00 39.76           O  
ANISOU 1204  O   ILE A 919     5492   5153   4462    664    869    183       O  
ATOM   1205  CB  ILE A 919       6.662  41.205   6.264  1.00 41.68           C  
ANISOU 1205  CB  ILE A 919     5963   5520   4352    702    718    313       C  
ATOM   1206  CG1 ILE A 919       5.845  42.155   5.392  1.00 45.18           C  
ANISOU 1206  CG1 ILE A 919     6489   5978   4699    722    644    466       C  
ATOM   1207  CG2 ILE A 919       5.798  39.989   6.549  1.00 40.99           C  
ANISOU 1207  CG2 ILE A 919     5852   5507   4213    711    630    217       C  
ATOM   1208  CD1 ILE A 919       5.241  41.515   4.153  1.00 47.47           C  
ANISOU 1208  CD1 ILE A 919     6895   6407   4731    690    585    489       C  
ATOM   1209  N   LEU A 920       7.507  40.251   9.281  1.00 38.54           N  
ANISOU 1209  N   LEU A 920     5313   5085   4244    728    679    124       N  
ATOM   1210  CA  LEU A 920       8.295  39.297  10.048  1.00 38.50           C  
ANISOU 1210  CA  LEU A 920     5219   5094   4313    725    692     81       C  
ATOM   1211  C   LEU A 920       8.238  37.915   9.431  1.00 38.82           C  
ANISOU 1211  C   LEU A 920     5279   5146   4324    727    747     58       C  
ATOM   1212  O   LEU A 920       7.260  37.553   8.755  1.00 38.01           O  
ANISOU 1212  O   LEU A 920     5253   5074   4114    722    727     39       O  
ATOM   1213  CB  LEU A 920       7.759  39.166  11.466  1.00 38.88           C  
ANISOU 1213  CB  LEU A 920     5213   5192   4367    749    593     59       C  
ATOM   1214  CG  LEU A 920       7.801  40.424  12.320  1.00 39.62           C  
ANISOU 1214  CG  LEU A 920     5286   5275   4492    736    548     19       C  
ATOM   1215  CD1 LEU A 920       6.684  40.381  13.346  1.00 39.42           C  
ANISOU 1215  CD1 LEU A 920     5266   5310   4400    763    494    -15       C  
ATOM   1216  CD2 LEU A 920       9.164  40.565  12.978  1.00 40.77           C  
ANISOU 1216  CD2 LEU A 920     5339   5426   4725    694    527     -6       C  
ATOM   1217  N   LEU A 921       9.304  37.157   9.680  1.00 38.37           N  
ANISOU 1217  N   LEU A 921     5134   5054   4390    730    812     50       N  
ATOM   1218  CA  LEU A 921       9.299  35.720   9.530  1.00 38.37           C  
ANISOU 1218  CA  LEU A 921     5108   5021   4447    745    868     19       C  
ATOM   1219  C   LEU A 921       9.543  35.133  10.901  1.00 37.14           C  
ANISOU 1219  C   LEU A 921     4832   4870   4408    787    787     87       C  
ATOM   1220  O   LEU A 921      10.562  35.397  11.523  1.00 36.50           O  
ANISOU 1220  O   LEU A 921     4645   4790   4430    797    758    134       O  
ATOM   1221  CB  LEU A 921      10.393  35.274   8.575  1.00 40.66           C  
ANISOU 1221  CB  LEU A 921     5382   5239   4827    729   1046    -26       C  
ATOM   1222  CG  LEU A 921      10.072  35.420   7.095  1.00 42.04           C  
ANISOU 1222  CG  LEU A 921     5712   5435   4825    676   1154   -102       C  
ATOM   1223  CD1 LEU A 921      11.317  35.148   6.275  1.00 43.83           C  
ANISOU 1223  CD1 LEU A 921     5916   5594   5142    656   1379   -154       C  
ATOM   1224  CD2 LEU A 921       8.967  34.446   6.702  1.00 43.13           C  
ANISOU 1224  CD2 LEU A 921     5926   5591   4867    657   1122   -193       C  
ATOM   1225  N   GLY A 922       8.587  34.357  11.385  1.00 37.39           N  
ANISOU 1225  N   GLY A 922     4875   4914   4418    804    742    105       N  
ATOM   1226  CA  GLY A 922       8.710  33.699  12.680  1.00 37.53           C  
ANISOU 1226  CA  GLY A 922     4801   4949   4509    843    675    212       C  
ATOM   1227  C   GLY A 922       8.659  32.197  12.544  1.00 37.70           C  
ANISOU 1227  C   GLY A 922     4775   4859   4689    868    755    243       C  
ATOM   1228  O   GLY A 922       7.985  31.667  11.668  1.00 36.74           O  
ANISOU 1228  O   GLY A 922     4715   4674   4570    837    832    143       O  
ATOM   1229  N   GLU A 923       9.406  31.519  13.405  1.00 39.55           N  
ANISOU 1229  N   GLU A 923     4891   5064   5071    920    728    383       N  
ATOM   1230  CA  GLU A 923       9.301  30.080  13.563  1.00 41.17           C  
ANISOU 1230  CA  GLU A 923     5031   5134   5474    958    799    465       C  
ATOM   1231  C   GLU A 923       8.098  29.855  14.471  1.00 41.66           C  
ANISOU 1231  C   GLU A 923     5140   5264   5425    948    738    556       C  
ATOM   1232  O   GLU A 923       8.061  30.354  15.598  1.00 41.19           O  
ANISOU 1232  O   GLU A 923     5080   5349   5221    958    623    672       O  
ATOM   1233  CB  GLU A 923      10.565  29.518  14.194  1.00 42.76           C  
ANISOU 1233  CB  GLU A 923     5068   5281   5897   1034    772    637       C  
ATOM   1234  CG  GLU A 923      10.610  28.005  14.219  1.00 45.81           C  
ANISOU 1234  CG  GLU A 923     5365   5466   6574   1090    879    736       C  
ATOM   1235  CD  GLU A 923      11.825  27.457  14.964  1.00 49.40           C  
ANISOU 1235  CD  GLU A 923     5625   5867   7278   1188    818    969       C  
ATOM   1236  OE1 GLU A 923      12.869  28.152  15.025  1.00 49.91           O  
ANISOU 1236  OE1 GLU A 923     5597   6009   7357   1202    741    979       O  
ATOM   1237  OE2 GLU A 923      11.736  26.318  15.490  1.00 51.72           O  
ANISOU 1237  OE2 GLU A 923     5839   6030   7782   1250    843   1161       O  
ATOM   1238  N   VAL A 924       7.103  29.135  13.962  1.00 42.05           N  
ANISOU 1238  N   VAL A 924     5226   5215   5533    912    824    481       N  
ATOM   1239  CA  VAL A 924       5.881  28.880  14.701  1.00 42.23           C  
ANISOU 1239  CA  VAL A 924     5271   5277   5494    891    807    555       C  
ATOM   1240  C   VAL A 924       5.787  27.385  14.977  1.00 44.26           C  
ANISOU 1240  C   VAL A 924     5450   5352   6013    910    904    680       C  
ATOM   1241  O   VAL A 924       5.853  26.571  14.056  1.00 45.29           O  
ANISOU 1241  O   VAL A 924     5556   5298   6352    889   1015    559       O  
ATOM   1242  CB  VAL A 924       4.634  29.367  13.929  1.00 41.40           C  
ANISOU 1242  CB  VAL A 924     5242   5208   5278    820    809    375       C  
ATOM   1243  CG1 VAL A 924       3.412  29.368  14.840  1.00 41.80           C  
ANISOU 1243  CG1 VAL A 924     5288   5324   5270    802    800    456       C  
ATOM   1244  CG2 VAL A 924       4.852  30.768  13.370  1.00 40.13           C  
ANISOU 1244  CG2 VAL A 924     5153   5166   4928    810    738    264       C  
ATOM   1245  N   ALA A 925       5.648  27.027  16.249  1.00 46.04           N  
ANISOU 1245  N   ALA A 925     5641   5623   6227    946    875    922       N  
ATOM   1246  CA  ALA A 925       5.502  25.626  16.645  1.00 48.63           C  
ANISOU 1246  CA  ALA A 925     5891   5761   6824    969    975   1105       C  
ATOM   1247  C   ALA A 925       4.016  25.253  16.660  1.00 48.66           C  
ANISOU 1247  C   ALA A 925     5918   5717   6851    890   1062   1058       C  
ATOM   1248  O   ALA A 925       3.316  25.443  17.658  1.00 48.65           O  
ANISOU 1248  O   ALA A 925     5942   5840   6702    879   1056   1205       O  
ATOM   1249  CB  ALA A 925       6.145  25.385  18.003  1.00 50.82           C  
ANISOU 1249  CB  ALA A 925     6120   6123   7064   1047    895   1442       C  
ATOM   1250  N   LEU A 926       3.553  24.710  15.538  1.00 48.30           N  
ANISOU 1250  N   LEU A 926     5859   5497   6995    823   1150    837       N  
ATOM   1251  CA  LEU A 926       2.128  24.501  15.292  1.00 47.45           C  
ANISOU 1251  CA  LEU A 926     5746   5354   6926    724   1198    722       C  
ATOM   1252  C   LEU A 926       1.597  23.242  15.958  1.00 49.90           C  
ANISOU 1252  C   LEU A 926     5971   5469   7519    705   1332    912       C  
ATOM   1253  O   LEU A 926       0.432  23.188  16.332  1.00 50.73           O  
ANISOU 1253  O   LEU A 926     6050   5596   7627    639   1376    936       O  
ATOM   1254  CB  LEU A 926       1.868  24.424  13.785  1.00 46.23           C  
ANISOU 1254  CB  LEU A 926     5613   5117   6833    638   1204    390       C  
ATOM   1255  CG  LEU A 926       2.158  25.711  13.016  1.00 43.58           C  
ANISOU 1255  CG  LEU A 926     5373   4976   6207    639   1084    221       C  
ATOM   1256  CD1 LEU A 926       2.302  25.479  11.526  1.00 43.53           C  
ANISOU 1256  CD1 LEU A 926     5413   4895   6229    567   1108    -62       C  
ATOM   1257  CD2 LEU A 926       1.055  26.712  13.293  1.00 43.32           C  
ANISOU 1257  CD2 LEU A 926     5359   5130   5967    611    985    212       C  
ATOM   1258  N   GLY A 927       2.442  22.225  16.091  1.00 51.95           N  
ANISOU 1258  N   GLY A 927     6167   5515   8056    764   1415   1058       N  
ATOM   1259  CA  GLY A 927       1.996  20.927  16.576  1.00 54.66           C  
ANISOU 1259  CA  GLY A 927     6419   5604   8744    745   1569   1245       C  
ATOM   1260  C   GLY A 927       0.823  20.355  15.787  1.00 55.46           C  
ANISOU 1260  C   GLY A 927     6475   5531   9066    599   1666    988       C  
ATOM   1261  O   GLY A 927       0.763  20.466  14.561  1.00 54.76           O  
ANISOU 1261  O   GLY A 927     6409   5406   8989    526   1640    640       O  
ATOM   1262  N   ASN A 928      -0.114  19.745  16.505  1.00 57.23           N  
ANISOU 1262  N   ASN A 928     6631   5659   9452    546   1775   1165       N  
ATOM   1263  CA  ASN A 928      -1.290  19.136  15.909  1.00 58.60           C  
ANISOU 1263  CA  ASN A 928     6721   5655   9888    391   1864    948       C  
ATOM   1264  C   ASN A 928      -2.264  20.262  15.590  1.00 55.44           C  
ANISOU 1264  C   ASN A 928     6349   5528   9186    319   1731    744       C  
ATOM   1265  O   ASN A 928      -2.744  20.951  16.489  1.00 54.19           O  
ANISOU 1265  O   ASN A 928     6206   5575   8805    350   1718    922       O  
ATOM   1266  CB  ASN A 928      -1.879  18.107  16.890  1.00 63.00           C  
ANISOU 1266  CB  ASN A 928     7177   6000  10758    365   2054   1262       C  
ATOM   1267  CG  ASN A 928      -2.965  17.232  16.274  1.00 66.68           C  
ANISOU 1267  CG  ASN A 928     7515   6197  11622    190   2172   1041       C  
ATOM   1268  OD1 ASN A 928      -3.491  17.524  15.204  1.00 67.75           O  
ANISOU 1268  OD1 ASN A 928     7639   6374  11728     76   2074    652       O  
ATOM   1269  ND2 ASN A 928      -3.320  16.157  16.968  1.00 70.12           N  
ANISOU 1269  ND2 ASN A 928     7848   6359  12434    160   2375   1303       N  
ATOM   1270  N   MET A 929      -2.513  20.480  14.301  1.00 53.97           N  
ANISOU 1270  N   MET A 929     6172   5350   8981    228   1633    374       N  
ATOM   1271  CA  MET A 929      -3.346  21.603  13.855  1.00 51.67           C  
ANISOU 1271  CA  MET A 929     5895   5315   8419    179   1470    197       C  
ATOM   1272  C   MET A 929      -4.808  21.209  13.868  1.00 52.21           C  
ANISOU 1272  C   MET A 929     5811   5311   8715     41   1507    128       C  
ATOM   1273  O   MET A 929      -5.137  20.052  13.674  1.00 54.12           O  
ANISOU 1273  O   MET A 929     5953   5286   9322    -62   1622     64       O  
ATOM   1274  CB  MET A 929      -2.963  22.046  12.436  1.00 51.12           C  
ANISOU 1274  CB  MET A 929     5913   5323   8187    140   1325   -131       C  
ATOM   1275  CG  MET A 929      -1.493  22.397  12.283  1.00 50.49           C  
ANISOU 1275  CG  MET A 929     5959   5289   7935    260   1317    -94       C  
ATOM   1276  SD  MET A 929      -1.037  22.999  10.646  1.00 50.72           S  
ANISOU 1276  SD  MET A 929     6112   5435   7721    210   1194   -445       S  
ATOM   1277  CE  MET A 929      -0.929  21.456   9.733  1.00 53.51           C  
ANISOU 1277  CE  MET A 929     6432   5469   8430     84   1344   -727       C  
ATOM   1278  N   TYR A 930      -5.677  22.187  14.097  1.00 50.69           N  
ANISOU 1278  N   TYR A 930     5580   5337   8344     41   1418    135       N  
ATOM   1279  CA  TYR A 930      -7.118  21.994  14.025  1.00 51.87           C  
ANISOU 1279  CA  TYR A 930     5544   5449   8714    -86   1426     52       C  
ATOM   1280  C   TYR A 930      -7.532  22.697  12.763  1.00 51.36           C  
ANISOU 1280  C   TYR A 930     5471   5536   8507   -148   1176   -245       C  
ATOM   1281  O   TYR A 930      -7.370  23.907  12.665  1.00 49.61           O  
ANISOU 1281  O   TYR A 930     5329   5544   7976    -55   1044   -232       O  
ATOM   1282  CB  TYR A 930      -7.795  22.623  15.248  1.00 51.16           C  
ANISOU 1282  CB  TYR A 930     5396   5495   8545    -25   1531    294       C  
ATOM   1283  CG  TYR A 930      -9.281  22.338  15.424  1.00 52.62           C  
ANISOU 1283  CG  TYR A 930     5349   5614   9030   -146   1610    270       C  
ATOM   1284  CD1 TYR A 930      -9.824  21.078  15.137  1.00 54.66           C  
ANISOU 1284  CD1 TYR A 930     5452   5603   9712   -301   1703    194       C  
ATOM   1285  CD2 TYR A 930     -10.133  23.314  15.942  1.00 51.21           C  
ANISOU 1285  CD2 TYR A 930     5084   5616   8755   -106   1622    326       C  
ATOM   1286  CE1 TYR A 930     -11.169  20.821  15.328  1.00 56.03           C  
ANISOU 1286  CE1 TYR A 930     5383   5708  10198   -422   1783    178       C  
ATOM   1287  CE2 TYR A 930     -11.474  23.057  16.135  1.00 53.08           C  
ANISOU 1287  CE2 TYR A 930     5074   5785   9307   -211   1717    315       C  
ATOM   1288  CZ  TYR A 930     -11.986  21.810  15.829  1.00 55.59           C  
ANISOU 1288  CZ  TYR A 930     5231   5849  10039   -373   1791    247       C  
ATOM   1289  OH  TYR A 930     -13.326  21.557  16.022  1.00 57.66           O  
ANISOU 1289  OH  TYR A 930     5215   6036  10656   -490   1890    235       O  
ATOM   1290  N   GLU A 931      -8.049  21.948  11.795  1.00 53.88           N  
ANISOU 1290  N   GLU A 931     5696   5728   9047   -311   1106   -509       N  
ATOM   1291  CA  GLU A 931      -8.236  22.479  10.443  1.00 54.40           C  
ANISOU 1291  CA  GLU A 931     5796   5954   8917   -381    841   -797       C  
ATOM   1292  C   GLU A 931      -9.664  22.910  10.192  1.00 55.25           C  
ANISOU 1292  C   GLU A 931     5695   6177   9118   -471    671   -871       C  
ATOM   1293  O   GLU A 931     -10.569  22.113  10.290  1.00 57.56           O  
ANISOU 1293  O   GLU A 931     5786   6317   9765   -610    723   -937       O  
ATOM   1294  CB  GLU A 931      -7.778  21.453   9.419  1.00 56.76           C  
ANISOU 1294  CB  GLU A 931     6155   6083   9326   -513    842  -1091       C  
ATOM   1295  CG  GLU A 931      -6.371  20.966   9.727  1.00 56.78           C  
ANISOU 1295  CG  GLU A 931     6315   5931   9326   -407   1039   -995       C  
ATOM   1296  CD  GLU A 931      -5.644  20.426   8.518  1.00 59.57           C  
ANISOU 1296  CD  GLU A 931     6792   6201   9639   -488   1028  -1317       C  
ATOM   1297  OE1 GLU A 931      -6.308  19.892   7.601  1.00 63.45           O  
ANISOU 1297  OE1 GLU A 931     7226   6645  10235   -676    937  -1639       O  
ATOM   1298  OE2 GLU A 931      -4.398  20.530   8.485  1.00 59.81           O  
ANISOU 1298  OE2 GLU A 931     6971   6217   9536   -372   1118  -1266       O  
ATOM   1299  N   LEU A 932      -9.846  24.185   9.873  1.00 54.67           N  
ANISOU 1299  N   LEU A 932     5651   6358   8762   -387    472   -847       N  
ATOM   1300  CA  LEU A 932     -11.170  24.795   9.739  1.00 56.72           C  
ANISOU 1300  CA  LEU A 932     5685   6741   9124   -424    303   -856       C  
ATOM   1301  C   LEU A 932     -11.309  25.503   8.397  1.00 57.98           C  
ANISOU 1301  C   LEU A 932     5887   7116   9025   -457    -39  -1025       C  
ATOM   1302  O   LEU A 932     -10.348  26.095   7.899  1.00 56.85           O  
ANISOU 1302  O   LEU A 932     5976   7090   8532   -374   -106  -1026       O  
ATOM   1303  CB  LEU A 932     -11.404  25.817  10.852  1.00 54.84           C  
ANISOU 1303  CB  LEU A 932     5405   6593   8839   -257    418   -595       C  
ATOM   1304  CG  LEU A 932     -11.177  25.324  12.283  1.00 54.29           C  
ANISOU 1304  CG  LEU A 932     5344   6383   8901   -202    755   -378       C  
ATOM   1305  CD1 LEU A 932     -11.298  26.505  13.238  1.00 52.76           C  
ANISOU 1305  CD1 LEU A 932     5161   6328   8557    -45    846   -186       C  
ATOM   1306  CD2 LEU A 932     -12.143  24.198  12.647  1.00 56.48           C  
ANISOU 1306  CD2 LEU A 932     5385   6460   9615   -351    905   -385       C  
ATOM   1307  N   LYS A 933     -12.510  25.436   7.830  1.00 61.29           N  
ANISOU 1307  N   LYS A 933     6072   7591   9624   -583   -257  -1146       N  
ATOM   1308  CA  LYS A 933     -12.841  26.122   6.588  1.00 63.45           C  
ANISOU 1308  CA  LYS A 933     6348   8100   9656   -621   -628  -1260       C  
ATOM   1309  C   LYS A 933     -13.602  27.419   6.851  1.00 64.29           C  
ANISOU 1309  C   LYS A 933     6289   8358   9777   -479   -764  -1047       C  
ATOM   1310  O   LYS A 933     -13.830  28.198   5.928  1.00 65.98           O  
ANISOU 1310  O   LYS A 933     6509   8777   9781   -462  -1074  -1049       O  
ATOM   1311  CB  LYS A 933     -13.689  25.205   5.701  1.00 67.63           C  
ANISOU 1311  CB  LYS A 933     6704   8616  10374   -867   -842  -1548       C  
ATOM   1312  CG  LYS A 933     -12.929  23.994   5.183  1.00 68.61           C  
ANISOU 1312  CG  LYS A 933     7009   8591  10467  -1021   -736  -1826       C  
ATOM   1313  CD  LYS A 933     -13.829  22.845   4.768  1.00 72.42           C  
ANISOU 1313  CD  LYS A 933     7269   8944  11302  -1282   -821  -2114       C  
ATOM   1314  CE  LYS A 933     -12.984  21.629   4.409  1.00 73.60           C  
ANISOU 1314  CE  LYS A 933     7603   8877  11483  -1412   -632  -2390       C  
ATOM   1315  NZ  LYS A 933     -13.741  20.575   3.679  1.00 77.97           N  
ANISOU 1315  NZ  LYS A 933     7995   9333  12295  -1703   -769  -2771       N  
ATOM   1316  N   HIS A 934     -14.009  27.644   8.101  1.00 64.47           N  
ANISOU 1316  N   HIS A 934     6164   8276  10054   -377   -520   -859       N  
ATOM   1317  CA  HIS A 934     -14.813  28.816   8.460  1.00 65.02           C  
ANISOU 1317  CA  HIS A 934     6038   8438  10227   -240   -585   -683       C  
ATOM   1318  C   HIS A 934     -14.419  29.358   9.829  1.00 61.39           C  
ANISOU 1318  C   HIS A 934     5652   7905   9767    -70   -243   -485       C  
ATOM   1319  O   HIS A 934     -13.865  28.640  10.654  1.00 60.81           O  
ANISOU 1319  O   HIS A 934     5689   7704   9712    -85     39   -456       O  
ATOM   1320  CB  HIS A 934     -16.304  28.463   8.462  1.00 69.61           C  
ANISOU 1320  CB  HIS A 934     6216   8981  11251   -352   -681   -727       C  
ATOM   1321  CG  HIS A 934     -16.782  27.845   7.186  1.00 74.21           C  
ANISOU 1321  CG  HIS A 934     6698   9646  11853   -554  -1039   -954       C  
ATOM   1322  ND1 HIS A 934     -17.061  26.499   7.072  1.00 77.50           N  
ANISOU 1322  ND1 HIS A 934     7016   9915  12512   -773   -990  -1165       N  
ATOM   1323  CD2 HIS A 934     -17.017  28.383   5.965  1.00 76.69           C  
ANISOU 1323  CD2 HIS A 934     7003  10181  11955   -582  -1457  -1008       C  
ATOM   1324  CE1 HIS A 934     -17.461  26.236   5.839  1.00 80.47           C  
ANISOU 1324  CE1 HIS A 934     7327  10425  12820   -941  -1367  -1381       C  
ATOM   1325  NE2 HIS A 934     -17.440  27.361   5.147  1.00 80.51           N  
ANISOU 1325  NE2 HIS A 934     7392  10674  12523   -828  -1666  -1278       N  
ATOM   1326  N   ALA A 935     -14.729  30.628  10.062  1.00 59.97           N  
ANISOU 1326  N   ALA A 935     5405   7807   9573     87   -275   -349       N  
ATOM   1327  CA  ALA A 935     -14.381  31.303  11.307  1.00 57.05           C  
ANISOU 1327  CA  ALA A 935     5117   7395   9165    241     29   -207       C  
ATOM   1328  C   ALA A 935     -15.016  30.602  12.502  1.00 57.34           C  
ANISOU 1328  C   ALA A 935     4986   7301   9497    195    356   -165       C  
ATOM   1329  O   ALA A 935     -16.177  30.227  12.460  1.00 59.74           O  
ANISOU 1329  O   ALA A 935     4981   7554  10161    113    338   -194       O  
ATOM   1330  CB  ALA A 935     -14.833  32.751  11.249  1.00 57.21           C  
ANISOU 1330  CB  ALA A 935     5032   7485   9221    399    -64   -108       C  
ATOM   1331  N   SER A 936     -14.238  30.430  13.563  1.00 55.37           N  
ANISOU 1331  N   SER A 936     4938   7008   9090    243    649    -84       N  
ATOM   1332  CA  SER A 936     -14.709  29.830  14.809  1.00 55.92           C  
ANISOU 1332  CA  SER A 936     4908   6979   9357    211    999      3       C  
ATOM   1333  C   SER A 936     -15.028  30.903  15.841  1.00 55.86           C  
ANISOU 1333  C   SER A 936     4869   7020   9334    349   1228     87       C  
ATOM   1334  O   SER A 936     -15.946  30.743  16.636  1.00 58.44           O  
ANISOU 1334  O   SER A 936     4994   7292   9919    330   1483    135       O  
ATOM   1335  CB  SER A 936     -13.619  28.931  15.377  1.00 54.94           C  
ANISOU 1335  CB  SER A 936     5039   6797   9038    177   1170     71       C  
ATOM   1336  OG  SER A 936     -12.404  29.660  15.551  1.00 52.19           O  
ANISOU 1336  OG  SER A 936     4976   6549   8305    296   1145    107       O  
ATOM   1337  N   HIS A 937     -14.238  31.972  15.835  1.00 53.56           N  
ANISOU 1337  N   HIS A 937     4782   6819   8748    478   1166     89       N  
ATOM   1338  CA  HIS A 937     -14.324  33.054  16.806  1.00 54.29           C  
ANISOU 1338  CA  HIS A 937     4902   6948   8776    604   1389    119       C  
ATOM   1339  C   HIS A 937     -14.002  32.667  18.238  1.00 54.68           C  
ANISOU 1339  C   HIS A 937     5094   7011   8669    592   1749    194       C  
ATOM   1340  O   HIS A 937     -14.340  33.396  19.151  1.00 56.20           O  
ANISOU 1340  O   HIS A 937     5270   7232   8850    663   1994    187       O  
ATOM   1341  CB  HIS A 937     -15.696  33.721  16.773  1.00 57.74           C  
ANISOU 1341  CB  HIS A 937     5000   7344   9595    656   1426     98       C  
ATOM   1342  CG  HIS A 937     -15.988  34.401  15.485  1.00 59.42           C  
ANISOU 1342  CG  HIS A 937     5083   7575   9919    706   1057     71       C  
ATOM   1343  ND1 HIS A 937     -15.316  35.537  15.081  1.00 58.51           N  
ANISOU 1343  ND1 HIS A 937     5127   7502   9599    827    912     76       N  
ATOM   1344  CD2 HIS A 937     -16.862  34.100  14.496  1.00 62.06           C  
ANISOU 1344  CD2 HIS A 937     5145   7901  10533    643    788     57       C  
ATOM   1345  CE1 HIS A 937     -15.769  35.909  13.897  1.00 59.70           C  
ANISOU 1345  CE1 HIS A 937     5124   7675   9885    847    577     97       C  
ATOM   1346  NE2 HIS A 937     -16.706  35.054  13.520  1.00 62.23           N  
ANISOU 1346  NE2 HIS A 937     5182   7982  10481    735    478     79       N  
ATOM   1347  N   ILE A 938     -13.347  31.536  18.459  1.00 54.08           N  
ANISOU 1347  N   ILE A 938     5164   6916   8468    506   1791    271       N  
ATOM   1348  CA  ILE A 938     -13.067  31.124  19.827  1.00 53.98           C  
ANISOU 1348  CA  ILE A 938     5286   6937   8284    493   2111    396       C  
ATOM   1349  C   ILE A 938     -11.612  30.765  19.932  1.00 52.30           C  
ANISOU 1349  C   ILE A 938     5367   6776   7725    501   2019    465       C  
ATOM   1350  O   ILE A 938     -10.968  30.451  18.932  1.00 50.96           O  
ANISOU 1350  O   ILE A 938     5255   6567   7541    483   1768    420       O  
ATOM   1351  CB  ILE A 938     -13.985  29.979  20.297  1.00 56.21           C  
ANISOU 1351  CB  ILE A 938     5379   7111   8863    380   2346    501       C  
ATOM   1352  CG1 ILE A 938     -13.718  28.697  19.504  1.00 55.85           C  
ANISOU 1352  CG1 ILE A 938     5310   6935   8974    267   2183    524       C  
ATOM   1353  CG2 ILE A 938     -15.439  30.408  20.178  1.00 58.18           C  
ANISOU 1353  CG2 ILE A 938     5290   7309   9503    377   2435    424       C  
ATOM   1354  CD1 ILE A 938     -14.731  27.601  19.741  1.00 58.42           C  
ANISOU 1354  CD1 ILE A 938     5395   7105   9694    135   2380    597       C  
ATOM   1355  N   SER A 939     -11.099  30.839  21.154  1.00 53.03           N  
ANISOU 1355  N   SER A 939     5641   6970   7535    526   2225    570       N  
ATOM   1356  CA  SER A 939      -9.669  30.744  21.403  1.00 51.53           C  
ANISOU 1356  CA  SER A 939     5713   6864   7000    554   2123    642       C  
ATOM   1357  C   SER A 939      -9.329  29.410  22.019  1.00 52.44           C  
ANISOU 1357  C   SER A 939     5890   6935   7098    493   2244    870       C  
ATOM   1358  O   SER A 939      -8.191  29.184  22.434  1.00 52.19           O  
ANISOU 1358  O   SER A 939     6048   6975   6804    518   2186    988       O  
ATOM   1359  CB  SER A 939      -9.247  31.860  22.351  1.00 51.82           C  
ANISOU 1359  CB  SER A 939     5917   7073   6699    621   2218    593       C  
ATOM   1360  OG  SER A 939      -9.855  33.080  21.967  1.00 51.98           O  
ANISOU 1360  OG  SER A 939     5833   7084   6830    680   2196    402       O  
ATOM   1361  N   LYS A 940     -10.317  28.523  22.053  1.00 54.27           N  
ANISOU 1361  N   LYS A 940     5938   7034   7647    411   2405    946       N  
ATOM   1362  CA  LYS A 940     -10.239  27.296  22.821  1.00 56.30           C  
ANISOU 1362  CA  LYS A 940     6226   7223   7941    350   2600   1205       C  
ATOM   1363  C   LYS A 940     -10.249  26.097  21.891  1.00 55.94           C  
ANISOU 1363  C   LYS A 940     6059   6939   8254    271   2495   1216       C  
ATOM   1364  O   LYS A 940     -11.174  25.923  21.100  1.00 57.61           O  
ANISOU 1364  O   LYS A 940     6051   7025   8811    199   2454   1067       O  
ATOM   1365  CB  LYS A 940     -11.409  27.252  23.805  1.00 59.77           C  
ANISOU 1365  CB  LYS A 940     6553   7687   8468    304   2954   1297       C  
ATOM   1366  CG  LYS A 940     -11.228  28.183  24.999  1.00 61.12           C  
ANISOU 1366  CG  LYS A 940     6908   8102   8213    364   3129   1317       C  
ATOM   1367  CD  LYS A 940     -10.596  27.484  26.202  1.00 64.26           C  
ANISOU 1367  CD  LYS A 940     7515   8610   8290    346   3290   1627       C  
ATOM   1368  CE  LYS A 940      -9.392  26.590  25.861  1.00 63.63           C  
ANISOU 1368  CE  LYS A 940     7542   8452   8180    360   3057   1807       C  
ATOM   1369  NZ  LYS A 940      -8.937  25.760  27.018  1.00 66.79           N  
ANISOU 1369  NZ  LYS A 940     8096   8930   8351    345   3214   2182       N  
ATOM   1370  N   LEU A 941      -9.216  25.272  21.992  1.00 55.22           N  
ANISOU 1370  N   LEU A 941     6100   6781   8098    281   2447   1382       N  
ATOM   1371  CA  LEU A 941      -9.027  24.152  21.085  1.00 55.19           C  
ANISOU 1371  CA  LEU A 941     6011   6529   8428    214   2357   1353       C  
ATOM   1372  C   LEU A 941      -9.431  22.844  21.716  1.00 57.73           C  
ANISOU 1372  C   LEU A 941     6250   6651   9033    133   2609   1609       C  
ATOM   1373  O   LEU A 941      -9.398  22.727  22.930  1.00 60.17           O  
ANISOU 1373  O   LEU A 941     6646   7051   9165    159   2816   1889       O  
ATOM   1374  CB  LEU A 941      -7.559  24.053  20.714  1.00 53.83           C  
ANISOU 1374  CB  LEU A 941     6011   6361   8081    290   2164   1368       C  
ATOM   1375  CG  LEU A 941      -7.057  25.259  19.935  1.00 50.95           C  
ANISOU 1375  CG  LEU A 941     5725   6151   7479    356   1918   1122       C  
ATOM   1376  CD1 LEU A 941      -5.550  25.189  19.780  1.00 49.46           C  
ANISOU 1376  CD1 LEU A 941     5695   5982   7115    433   1777   1174       C  
ATOM   1377  CD2 LEU A 941      -7.763  25.338  18.587  1.00 50.51           C  
ANISOU 1377  CD2 LEU A 941     5523   6005   7662    283   1774    841       C  
ATOM   1378  N   PRO A 942      -9.802  21.845  20.894  1.00 58.40           N  
ANISOU 1378  N   PRO A 942     6174   6462   9554     25   2597   1516       N  
ATOM   1379  CA  PRO A 942      -9.996  20.494  21.420  1.00 61.18           C  
ANISOU 1379  CA  PRO A 942     6452   6559  10233    -50   2835   1776       C  
ATOM   1380  C   PRO A 942      -8.701  19.935  21.983  1.00 61.65           C  
ANISOU 1380  C   PRO A 942     6698   6584  10140     48   2841   2073       C  
ATOM   1381  O   PRO A 942      -7.635  20.479  21.719  1.00 59.85           O  
ANISOU 1381  O   PRO A 942     6622   6492   9626    153   2631   2008       O  
ATOM   1382  CB  PRO A 942     -10.427  19.695  20.192  1.00 61.63           C  
ANISOU 1382  CB  PRO A 942     6322   6331  10761   -185   2747   1512       C  
ATOM   1383  CG  PRO A 942     -11.014  20.706  19.278  1.00 60.05           C  
ANISOU 1383  CG  PRO A 942     6036   6292  10485   -206   2524   1161       C  
ATOM   1384  CD  PRO A 942     -10.180  21.934  19.474  1.00 57.15           C  
ANISOU 1384  CD  PRO A 942     5883   6218   9612    -49   2376   1160       C  
ATOM   1385  N   LYS A 943      -8.799  18.854  22.745  1.00 65.41           N  
ANISOU 1385  N   LYS A 943     7144   6870  10837     14   3081   2415       N  
ATOM   1386  CA  LYS A 943      -7.653  18.286  23.447  1.00 67.02           C  
ANISOU 1386  CA  LYS A 943     7500   7048  10916    119   3094   2786       C  
ATOM   1387  C   LYS A 943      -6.620  17.728  22.455  1.00 65.73           C  
ANISOU 1387  C   LYS A 943     7336   6660  10975    161   2908   2652       C  
ATOM   1388  O   LYS A 943      -6.973  17.029  21.500  1.00 65.97           O  
ANISOU 1388  O   LYS A 943     7221   6394  11447     59   2921   2419       O  
ATOM   1389  CB  LYS A 943      -8.122  17.195  24.419  1.00 71.79           C  
ANISOU 1389  CB  LYS A 943     8049   7461  11767     65   3413   3216       C  
ATOM   1390  CG  LYS A 943      -7.044  16.686  25.369  1.00 74.52           C  
ANISOU 1390  CG  LYS A 943     8552   7836  11926    186   3428   3698       C  
ATOM   1391  CD  LYS A 943      -7.213  15.195  25.677  1.00 79.51           C  
ANISOU 1391  CD  LYS A 943     9075   8069  13067    136   3674   4065       C  
ATOM   1392  CE  LYS A 943      -5.876  14.464  25.843  1.00 81.08           C  
ANISOU 1392  CE  LYS A 943     9341   8118  13345    273   3567   4393       C  
ATOM   1393  NZ  LYS A 943      -4.927  14.645  24.697  1.00 77.77           N  
ANISOU 1393  NZ  LYS A 943     8911   7618  13017    343   3291   4039       N  
ATOM   1394  N   GLY A 944      -5.349  18.060  22.680  1.00 64.17           N  
ANISOU 1394  N   GLY A 944     7294   6612  10474    302   2741   2773       N  
ATOM   1395  CA  GLY A 944      -4.263  17.590  21.825  1.00 63.21           C  
ANISOU 1395  CA  GLY A 944     7168   6293  10553    362   2597   2665       C  
ATOM   1396  C   GLY A 944      -4.102  18.357  20.523  1.00 60.19           C  
ANISOU 1396  C   GLY A 944     6793   5985  10089    343   2387   2182       C  
ATOM   1397  O   GLY A 944      -3.400  17.908  19.626  1.00 61.01           O  
ANISOU 1397  O   GLY A 944     6877   5896  10406    357   2318   2012       O  
ATOM   1398  N   LYS A 945      -4.754  19.508  20.408  1.00 57.78           N  
ANISOU 1398  N   LYS A 945     6516   5952   9486    313   2302   1969       N  
ATOM   1399  CA  LYS A 945      -4.558  20.407  19.283  1.00 54.30           C  
ANISOU 1399  CA  LYS A 945     6107   5634   8888    313   2087   1583       C  
ATOM   1400  C   LYS A 945      -3.869  21.636  19.833  1.00 52.86           C  
ANISOU 1400  C   LYS A 945     6078   5783   8223    428   1953   1645       C  
ATOM   1401  O   LYS A 945      -4.235  22.134  20.899  1.00 53.38           O  
ANISOU 1401  O   LYS A 945     6192   6045   8042    449   2029   1824       O  
ATOM   1402  CB  LYS A 945      -5.887  20.821  18.673  1.00 53.66           C  
ANISOU 1402  CB  LYS A 945     5910   5585   8891    192   2072   1303       C  
ATOM   1403  CG  LYS A 945      -6.705  19.672  18.133  1.00 55.97           C  
ANISOU 1403  CG  LYS A 945     6027   5567   9672     42   2185   1195       C  
ATOM   1404  CD  LYS A 945      -6.111  19.135  16.848  1.00 55.71           C  
ANISOU 1404  CD  LYS A 945     5996   5345   9824      0   2074    907       C  
ATOM   1405  CE  LYS A 945      -6.953  17.998  16.307  1.00 58.56           C  
ANISOU 1405  CE  LYS A 945     6180   5389  10679   -176   2181    746       C  
ATOM   1406  NZ  LYS A 945      -6.657  17.749  14.876  1.00 58.60           N  
ANISOU 1406  NZ  LYS A 945     6197   5293  10775   -258   2041    339       N  
ATOM   1407  N   HIS A 946      -2.872  22.122  19.109  1.00 51.53           N  
ANISOU 1407  N   HIS A 946     5983   5671   7924    490   1775   1482       N  
ATOM   1408  CA  HIS A 946      -2.048  23.216  19.581  1.00 50.45           C  
ANISOU 1408  CA  HIS A 946     5975   5808   7386    588   1640   1530       C  
ATOM   1409  C   HIS A 946      -2.174  24.455  18.722  1.00 47.83           C  
ANISOU 1409  C   HIS A 946     5680   5630   6860    580   1489   1214       C  
ATOM   1410  O   HIS A 946      -1.691  25.516  19.102  1.00 47.65           O  
ANISOU 1410  O   HIS A 946     5752   5825   6526    640   1394   1211       O  
ATOM   1411  CB  HIS A 946      -0.591  22.769  19.617  1.00 51.65           C  
ANISOU 1411  CB  HIS A 946     6161   5891   7573    683   1568   1677       C  
ATOM   1412  CG  HIS A 946      -0.372  21.519  20.400  1.00 55.19           C  
ANISOU 1412  CG  HIS A 946     6558   6157   8254    713   1698   2034       C  
ATOM   1413  ND1 HIS A 946      -0.834  21.364  21.690  1.00 57.99           N  
ANISOU 1413  ND1 HIS A 946     6943   6619   8470    714   1802   2354       N  
ATOM   1414  CD2 HIS A 946       0.248  20.359  20.078  1.00 57.77           C  
ANISOU 1414  CD2 HIS A 946     6804   6186   8958    745   1758   2137       C  
ATOM   1415  CE1 HIS A 946      -0.508  20.161  22.129  1.00 61.16           C  
ANISOU 1415  CE1 HIS A 946     7287   6803   9146    748   1904   2677       C  
ATOM   1416  NE2 HIS A 946       0.154  19.532  21.171  1.00 61.29           N  
ANISOU 1416  NE2 HIS A 946     7225   6554   9508    773   1879   2550       N  
ATOM   1417  N   SER A 947      -2.815  24.330  17.568  1.00 47.43           N  
ANISOU 1417  N   SER A 947     5557   5469   6994    499   1459    954       N  
ATOM   1418  CA  SER A 947      -2.962  25.457  16.663  1.00 46.03           C  
ANISOU 1418  CA  SER A 947     5414   5431   6644    494   1303    697       C  
ATOM   1419  C   SER A 947      -4.163  25.267  15.729  1.00 47.03           C  
ANISOU 1419  C   SER A 947     5423   5480   6964    382   1275    479       C  
ATOM   1420  O   SER A 947      -4.770  24.193  15.696  1.00 50.04           O  
ANISOU 1420  O   SER A 947     5695   5674   7643    294   1380    485       O  
ATOM   1421  CB  SER A 947      -1.689  25.617  15.835  1.00 44.70           C  
ANISOU 1421  CB  SER A 947     5332   5251   6399    540   1194    591       C  
ATOM   1422  OG  SER A 947      -1.451  24.440  15.089  1.00 45.87           O  
ANISOU 1422  OG  SER A 947     5434   5165   6826    488   1251    505       O  
ATOM   1423  N   VAL A 948      -4.490  26.320  14.982  1.00 44.68           N  
ANISOU 1423  N   VAL A 948     5139   5323   6513    381   1123    301       N  
ATOM   1424  CA  VAL A 948      -5.530  26.273  13.974  1.00 45.28           C  
ANISOU 1424  CA  VAL A 948     5104   5374   6726    279   1023     95       C  
ATOM   1425  C   VAL A 948      -4.920  26.571  12.620  1.00 44.44           C  
ANISOU 1425  C   VAL A 948     5094   5309   6481    263    854   -107       C  
ATOM   1426  O   VAL A 948      -4.126  27.508  12.469  1.00 42.64           O  
ANISOU 1426  O   VAL A 948     4989   5206   6004    348    783    -93       O  
ATOM   1427  CB  VAL A 948      -6.646  27.305  14.250  1.00 45.21           C  
ANISOU 1427  CB  VAL A 948     4995   5506   6676    297    980     98       C  
ATOM   1428  CG1 VAL A 948      -7.397  27.670  12.972  1.00 45.78           C  
ANISOU 1428  CG1 VAL A 948     4981   5627   6785    230    769   -103       C  
ATOM   1429  CG2 VAL A 948      -7.613  26.772  15.287  1.00 46.92           C  
ANISOU 1429  CG2 VAL A 948     5065   5652   7108    259   1175    232       C  
ATOM   1430  N   LYS A 949      -5.292  25.765  11.639  1.00 45.85           N  
ANISOU 1430  N   LYS A 949     5220   5382   6817    140    804   -305       N  
ATOM   1431  CA  LYS A 949      -5.013  26.094  10.272  1.00 45.93           C  
ANISOU 1431  CA  LYS A 949     5321   5477   6652     95    637   -520       C  
ATOM   1432  C   LYS A 949      -6.305  26.488   9.598  1.00 47.70           C  
ANISOU 1432  C   LYS A 949     5424   5809   6891      8    444   -640       C  
ATOM   1433  O   LYS A 949      -7.203  25.662   9.447  1.00 50.23           O  
ANISOU 1433  O   LYS A 949     5593   6028   7464   -118    437   -746       O  
ATOM   1434  CB  LYS A 949      -4.398  24.927   9.536  1.00 47.35           C  
ANISOU 1434  CB  LYS A 949     5554   5483   6951      6    710   -705       C  
ATOM   1435  CG  LYS A 949      -3.891  25.357   8.177  1.00 48.10           C  
ANISOU 1435  CG  LYS A 949     5794   5702   6777    -29    580   -916       C  
ATOM   1436  CD  LYS A 949      -3.589  24.173   7.299  1.00 50.83           C  
ANISOU 1436  CD  LYS A 949     6177   5883   7250   -157    656  -1188       C  
ATOM   1437  CE  LYS A 949      -2.953  24.622   6.007  1.00 51.60           C  
ANISOU 1437  CE  LYS A 949     6455   6127   7021   -189    575  -1385       C  
ATOM   1438  NZ  LYS A 949      -2.225  23.488   5.385  1.00 54.04           N  
ANISOU 1438  NZ  LYS A 949     6832   6240   7459   -269    752  -1633       N  
ATOM   1439  N   GLY A 950      -6.399  27.755   9.205  1.00 46.99           N  
ANISOU 1439  N   GLY A 950     5378   5912   6561     76    280   -609       N  
ATOM   1440  CA  GLY A 950      -7.460  28.204   8.309  1.00 48.79           C  
ANISOU 1440  CA  GLY A 950     5503   6268   6765      7     36   -709       C  
ATOM   1441  C   GLY A 950      -7.127  27.681   6.927  1.00 50.58           C  
ANISOU 1441  C   GLY A 950     5844   6531   6841   -119    -90   -949       C  
ATOM   1442  O   GLY A 950      -6.026  27.909   6.421  1.00 49.49           O  
ANISOU 1442  O   GLY A 950     5909   6435   6458    -82    -59   -980       O  
ATOM   1443  N   LEU A 951      -8.060  26.949   6.326  1.00 53.14           N  
ANISOU 1443  N   LEU A 951     6035   6836   7316   -281   -218  -1137       N  
ATOM   1444  CA  LEU A 951      -7.795  26.269   5.064  1.00 54.45           C  
ANISOU 1444  CA  LEU A 951     6317   7028   7343   -437   -313  -1426       C  
ATOM   1445  C   LEU A 951      -8.157  27.177   3.917  1.00 55.64           C  
ANISOU 1445  C   LEU A 951     6525   7454   7160   -464   -627  -1463       C  
ATOM   1446  O   LEU A 951      -9.324  27.521   3.745  1.00 57.47           O  
ANISOU 1446  O   LEU A 951     6565   7794   7474   -504   -863  -1434       O  
ATOM   1447  CB  LEU A 951      -8.585  24.966   4.983  1.00 57.19           C  
ANISOU 1447  CB  LEU A 951     6493   7206   8027   -627   -298  -1647       C  
ATOM   1448  CG  LEU A 951      -8.089  23.867   5.925  1.00 56.62           C  
ANISOU 1448  CG  LEU A 951     6397   6827   8290   -619     29  -1616       C  
ATOM   1449  CD1 LEU A 951      -9.157  22.795   6.103  1.00 59.68           C  
ANISOU 1449  CD1 LEU A 951     6547   7027   9101   -791     51  -1749       C  
ATOM   1450  CD2 LEU A 951      -6.786  23.275   5.414  1.00 56.23           C  
ANISOU 1450  CD2 LEU A 951     6566   6670   8127   -626    189  -1774       C  
ATOM   1451  N   GLY A 952      -7.153  27.566   3.136  1.00 55.45           N  
ANISOU 1451  N   GLY A 952     6752   7542   6773   -439   -625  -1504       N  
ATOM   1452  CA  GLY A 952      -7.360  28.449   1.982  1.00 57.15           C  
ANISOU 1452  CA  GLY A 952     7068   8035   6610   -461   -909  -1495       C  
ATOM   1453  C   GLY A 952      -7.554  27.696   0.689  1.00 60.24           C  
ANISOU 1453  C   GLY A 952     7551   8542   6794   -678  -1067  -1824       C  
ATOM   1454  O   GLY A 952      -7.351  26.490   0.648  1.00 61.00           O  
ANISOU 1454  O   GLY A 952     7658   8468   7050   -807   -910  -2095       O  
ATOM   1455  N   LYS A 953      -7.951  28.413  -0.363  1.00 63.58           N  
ANISOU 1455  N   LYS A 953     8043   9252   6861   -722  -1377  -1799       N  
ATOM   1456  CA  LYS A 953      -8.026  27.852  -1.729  1.00 68.37           C  
ANISOU 1456  CA  LYS A 953     8801  10047   7128   -939  -1553  -2118       C  
ATOM   1457  C   LYS A 953      -6.632  27.632  -2.324  1.00 68.25           C  
ANISOU 1457  C   LYS A 953     9113  10030   6789   -956  -1288  -2270       C  
ATOM   1458  O   LYS A 953      -6.376  26.620  -2.979  1.00 70.76           O  
ANISOU 1458  O   LYS A 953     9546  10316   7020  -1136  -1201  -2645       O  
ATOM   1459  CB  LYS A 953      -8.805  28.778  -2.661  1.00 71.63           C  
ANISOU 1459  CB  LYS A 953     9208  10805   7203   -964  -1982  -1979       C  
ATOM   1460  CG  LYS A 953     -10.295  28.824  -2.403  1.00 74.55           C  
ANISOU 1460  CG  LYS A 953     9228  11214   7881  -1002  -2302  -1914       C  
ATOM   1461  CD  LYS A 953     -11.024  29.473  -3.575  1.00 79.91           C  
ANISOU 1461  CD  LYS A 953     9911  12261   8187  -1076  -2777  -1840       C  
ATOM   1462  CE  LYS A 953     -12.531  29.242  -3.512  1.00 83.68           C  
ANISOU 1462  CE  LYS A 953    10010  12789   8993  -1174  -3130  -1871       C  
ATOM   1463  NZ  LYS A 953     -13.102  29.677  -2.202  1.00 81.17           N  
ANISOU 1463  NZ  LYS A 953     9375  12245   9221   -985  -3009  -1600       N  
ATOM   1464  N   THR A 954      -5.747  28.600  -2.098  1.00 65.51           N  
ANISOU 1464  N   THR A 954     8898   9702   6290   -773  -1146  -1992       N  
ATOM   1465  CA  THR A 954      -4.376  28.554  -2.580  1.00 65.52           C  
ANISOU 1465  CA  THR A 954     9173   9694   6027   -762   -867  -2079       C  
ATOM   1466  C   THR A 954      -3.387  28.175  -1.463  1.00 62.37           C  
ANISOU 1466  C   THR A 954     8732   8979   5987   -630   -488  -2027       C  
ATOM   1467  O   THR A 954      -3.502  28.619  -0.321  1.00 58.74           O  
ANISOU 1467  O   THR A 954     8112   8396   5810   -477   -454  -1768       O  
ATOM   1468  CB  THR A 954      -3.992  29.908  -3.200  1.00 65.91           C  
ANISOU 1468  CB  THR A 954     9396   9985   5659   -668   -968  -1798       C  
ATOM   1469  OG1 THR A 954      -4.715  30.077  -4.421  1.00 69.60           O  
ANISOU 1469  OG1 THR A 954     9956  10771   5715   -814  -1303  -1872       O  
ATOM   1470  CG2 THR A 954      -2.502  29.997  -3.495  1.00 65.46           C  
ANISOU 1470  CG2 THR A 954     9578   9882   5409   -627   -624  -1826       C  
ATOM   1471  N   THR A 955      -2.413  27.350  -1.830  1.00 64.04           N  
ANISOU 1471  N   THR A 955     9088   9070   6172   -694   -206  -2283       N  
ATOM   1472  CA  THR A 955      -1.415  26.824  -0.913  1.00 61.63           C  
ANISOU 1472  CA  THR A 955     8734   8467   6214   -584    136  -2256       C  
ATOM   1473  C   THR A 955      -0.081  26.766  -1.665  1.00 63.03           C  
ANISOU 1473  C   THR A 955     9135   8651   6162   -590    409  -2390       C  
ATOM   1474  O   THR A 955      -0.068  26.558  -2.885  1.00 66.41           O  
ANISOU 1474  O   THR A 955     9750   9245   6236   -742    391  -2651       O  
ATOM   1475  CB  THR A 955      -1.834  25.418  -0.421  1.00 62.59           C  
ANISOU 1475  CB  THR A 955     8698   8319   6764   -675    236  -2483       C  
ATOM   1476  OG1 THR A 955      -1.175  25.115   0.807  1.00 60.48           O  
ANISOU 1476  OG1 THR A 955     8312   7780   6885   -524    474  -2301       O  
ATOM   1477  CG2 THR A 955      -1.514  24.325  -1.456  1.00 66.40           C  
ANISOU 1477  CG2 THR A 955     9317   8740   7169   -862    383  -2933       C  
ATOM   1478  N   PRO A 956       1.046  26.955  -0.960  1.00 60.97           N  
ANISOU 1478  N   PRO A 956     8851   8224   6089   -434    663  -2220       N  
ATOM   1479  CA  PRO A 956       2.339  26.778  -1.629  1.00 62.54           C  
ANISOU 1479  CA  PRO A 956     9214   8387   6160   -440    967  -2365       C  
ATOM   1480  C   PRO A 956       2.530  25.320  -2.051  1.00 65.55           C  
ANISOU 1480  C   PRO A 956     9613   8569   6723   -568   1188  -2775       C  
ATOM   1481  O   PRO A 956       1.997  24.423  -1.400  1.00 66.71           O  
ANISOU 1481  O   PRO A 956     9594   8501   7251   -590   1177  -2850       O  
ATOM   1482  CB  PRO A 956       3.360  27.174  -0.555  1.00 59.30           C  
ANISOU 1482  CB  PRO A 956     8691   7807   6034   -245   1144  -2085       C  
ATOM   1483  CG  PRO A 956       2.591  27.906   0.487  1.00 56.69           C  
ANISOU 1483  CG  PRO A 956     8210   7514   5814   -145    901  -1776       C  
ATOM   1484  CD  PRO A 956       1.206  27.337   0.452  1.00 58.02           C  
ANISOU 1484  CD  PRO A 956     8298   7705   6039   -257    684  -1904       C  
ATOM   1485  N   ASP A 957       3.257  25.086  -3.136  1.00 68.02           N  
ANISOU 1485  N   ASP A 957    10125   8939   6778   -658   1407  -3043       N  
ATOM   1486  CA  ASP A 957       3.407  23.733  -3.658  1.00 71.70           C  
ANISOU 1486  CA  ASP A 957    10628   9212   7402   -798   1638  -3492       C  
ATOM   1487  C   ASP A 957       4.269  22.907  -2.706  1.00 70.55           C  
ANISOU 1487  C   ASP A 957    10291   8657   7856   -660   1949  -3455       C  
ATOM   1488  O   ASP A 957       5.452  23.195  -2.532  1.00 70.41           O  
ANISOU 1488  O   ASP A 957    10266   8559   7927   -527   2193  -3321       O  
ATOM   1489  CB  ASP A 957       4.026  23.744  -5.061  1.00 75.21           C  
ANISOU 1489  CB  ASP A 957    11352   9833   7388   -928   1840  -3802       C  
ATOM   1490  CG  ASP A 957       4.106  22.350  -5.686  1.00 79.52           C  
ANISOU 1490  CG  ASP A 957    11954  10183   8075  -1099   2090  -4342       C  
ATOM   1491  OD1 ASP A 957       3.446  21.410  -5.194  1.00 79.77           O  
ANISOU 1491  OD1 ASP A 957    11822   9979   8506  -1154   2031  -4491       O  
ATOM   1492  OD2 ASP A 957       4.834  22.190  -6.686  1.00 82.92           O  
ANISOU 1492  OD2 ASP A 957    12596  10681   8226  -1185   2373  -4631       O  
ATOM   1493  N   PRO A 958       3.681  21.871  -2.089  1.00 70.70           N  
ANISOU 1493  N   PRO A 958    10138   8411   8311   -694   1938  -3553       N  
ATOM   1494  CA  PRO A 958       4.436  21.092  -1.117  1.00 69.62           C  
ANISOU 1494  CA  PRO A 958     9806   7886   8761   -548   2198  -3443       C  
ATOM   1495  C   PRO A 958       5.669  20.399  -1.692  1.00 71.75           C  
ANISOU 1495  C   PRO A 958    10126   7936   9200   -537   2620  -3712       C  
ATOM   1496  O   PRO A 958       6.596  20.100  -0.951  1.00 71.41           O  
ANISOU 1496  O   PRO A 958     9922   7631   9578   -366   2831  -3527       O  
ATOM   1497  CB  PRO A 958       3.417  20.056  -0.635  1.00 70.99           C  
ANISOU 1497  CB  PRO A 958     9826   7833   9311   -640   2114  -3555       C  
ATOM   1498  CG  PRO A 958       2.447  19.939  -1.759  1.00 74.13           C  
ANISOU 1498  CG  PRO A 958    10373   8443   9348   -885   1935  -3935       C  
ATOM   1499  CD  PRO A 958       2.318  21.341  -2.260  1.00 72.52           C  
ANISOU 1499  CD  PRO A 958    10329   8673   8551   -870   1691  -3754       C  
ATOM   1500  N   SER A 959       5.690  20.149  -2.994  1.00 74.88           N  
ANISOU 1500  N   SER A 959    10736   8442   9270   -715   2745  -4145       N  
ATOM   1501  CA  SER A 959       6.847  19.511  -3.607  1.00 77.65           C  
ANISOU 1501  CA  SER A 959    11142   8585   9773   -712   3195  -4443       C  
ATOM   1502  C   SER A 959       8.064  20.443  -3.694  1.00 76.13           C  
ANISOU 1502  C   SER A 959    10990   8514   9420   -563   3369  -4206       C  
ATOM   1503  O   SER A 959       9.153  20.011  -4.053  1.00 77.85           O  
ANISOU 1503  O   SER A 959    11200   8541   9836   -520   3770  -4381       O  
ATOM   1504  CB  SER A 959       6.490  18.969  -4.997  1.00 82.55           C  
ANISOU 1504  CB  SER A 959    12008   9315  10042   -971   3299  -5021       C  
ATOM   1505  OG  SER A 959       6.217  20.016  -5.907  1.00 82.60           O  
ANISOU 1505  OG  SER A 959    12272   9794   9317  -1075   3104  -5019       O  
ATOM   1506  N   ALA A 960       7.888  21.720  -3.377  1.00 73.57           N  
ANISOU 1506  N   ALA A 960    10692   8484   8775   -489   3089  -3819       N  
ATOM   1507  CA  ALA A 960       9.022  22.652  -3.336  1.00 72.84           C  
ANISOU 1507  CA  ALA A 960    10600   8477   8597   -352   3236  -3562       C  
ATOM   1508  C   ALA A 960       9.440  23.009  -1.914  1.00 69.22           C  
ANISOU 1508  C   ALA A 960     9877   7876   8546   -137   3134  -3109       C  
ATOM   1509  O   ALA A 960      10.478  23.648  -1.718  1.00 67.80           O  
ANISOU 1509  O   ALA A 960     9634   7703   8423    -18   3264  -2902       O  
ATOM   1510  CB  ALA A 960       8.705  23.914  -4.121  1.00 72.68           C  
ANISOU 1510  CB  ALA A 960    10818   8880   7916   -433   3047  -3464       C  
ATOM   1511  N   ASN A 961       8.645  22.599  -0.930  1.00 68.29           N  
ANISOU 1511  N   ASN A 961     9606   7638   8702    -99   2907  -2963       N  
ATOM   1512  CA  ASN A 961       8.942  22.916   0.451  1.00 67.13           C  
ANISOU 1512  CA  ASN A 961     9237   7397   8871     84   2784  -2543       C  
ATOM   1513  C   ASN A 961      10.270  22.294   0.844  1.00 67.69           C  
ANISOU 1513  C   ASN A 961     9119   7165   9433    226   3093  -2496       C  
ATOM   1514  O   ASN A 961      10.555  21.141   0.519  1.00 68.98           O  
ANISOU 1514  O   ASN A 961     9234   7047   9927    204   3363  -2759       O  
ATOM   1515  CB  ASN A 961       7.826  22.448   1.399  1.00 68.29           C  
ANISOU 1515  CB  ASN A 961     9266   7459   9221     84   2541  -2414       C  
ATOM   1516  CG  ASN A 961       6.489  23.159   1.153  1.00 69.77           C  
ANISOU 1516  CG  ASN A 961     9577   7944   8988    -30   2207  -2406       C  
ATOM   1517  OD1 ASN A 961       6.392  24.154   0.395  1.00 70.79           O  
ANISOU 1517  OD1 ASN A 961     9877   8362   8658    -84   2105  -2417       O  
ATOM   1518  ND2 ASN A 961       5.439  22.646   1.798  1.00 69.75           N  
ANISOU 1518  ND2 ASN A 961     9472   7859   9171    -64   2042  -2363       N  
ATOM   1519  N   ILE A 962      11.087  23.092   1.518  1.00 66.03           N  
ANISOU 1519  N   ILE A 962     8789   7009   9288    368   3050  -2169       N  
ATOM   1520  CA  ILE A 962      12.378  22.647   2.006  1.00 67.46           C  
ANISOU 1520  CA  ILE A 962     8741   6935   9952    521   3278  -2052       C  
ATOM   1521  C   ILE A 962      12.399  22.840   3.518  1.00 65.80           C  
ANISOU 1521  C   ILE A 962     8323   6698   9980    666   3022  -1630       C  
ATOM   1522  O   ILE A 962      11.421  23.289   4.105  1.00 62.74           O  
ANISOU 1522  O   ILE A 962     7987   6473   9376    639   2726  -1474       O  
ATOM   1523  CB  ILE A 962      13.548  23.355   1.280  1.00 68.05           C  
ANISOU 1523  CB  ILE A 962     8845   7098   9912    537   3514  -2099       C  
ATOM   1524  CG1 ILE A 962      13.510  24.884   1.459  1.00 65.95           C  
ANISOU 1524  CG1 ILE A 962     8655   7149   9255    537   3274  -1845       C  
ATOM   1525  CG2 ILE A 962      13.505  23.020  -0.197  1.00 71.23           C  
ANISOU 1525  CG2 ILE A 962     9477   7531  10055    384   3804  -2534       C  
ATOM   1526  CD1 ILE A 962      14.518  25.434   2.447  1.00 64.40           C  
ANISOU 1526  CD1 ILE A 962     8214   6913   9340    685   3215  -1515       C  
ATOM   1527  N   SER A 963      13.510  22.468   4.135  1.00 69.40           N  
ANISOU 1527  N   SER A 963     8536   6949  10882    816   3142  -1452       N  
ATOM   1528  CA  SER A 963      13.615  22.370   5.574  1.00 69.79           C  
ANISOU 1528  CA  SER A 963     8378   6943  11196    952   2922  -1064       C  
ATOM   1529  C   SER A 963      14.949  22.964   6.008  1.00 71.77           C  
ANISOU 1529  C   SER A 963     8431   7219  11618   1076   2929   -840       C  
ATOM   1530  O   SER A 963      15.989  22.320   5.881  1.00 75.88           O  
ANISOU 1530  O   SER A 963     8755   7499  12575   1171   3168   -856       O  
ATOM   1531  CB  SER A 963      13.511  20.890   5.975  1.00 73.43           C  
ANISOU 1531  CB  SER A 963     8690   7045  12162   1013   3046  -1053       C  
ATOM   1532  OG  SER A 963      13.607  20.687   7.374  1.00 74.21           O  
ANISOU 1532  OG  SER A 963     8598   7093  12503   1146   2840   -641       O  
ATOM   1533  N   LEU A 964      14.925  24.218   6.453  1.00 72.04           N  
ANISOU 1533  N   LEU A 964     8507   7533  11332   1066   2683   -660       N  
ATOM   1534  CA  LEU A 964      15.998  24.753   7.283  1.00 73.54           C  
ANISOU 1534  CA  LEU A 964     8470   7760  11708   1176   2571   -384       C  
ATOM   1535  C   LEU A 964      15.900  24.035   8.627  1.00 76.58           C  
ANISOU 1535  C   LEU A 964     8676   8045  12373   1290   2374    -77       C  
ATOM   1536  O   LEU A 964      14.816  23.580   9.001  1.00 78.45           O  
ANISOU 1536  O   LEU A 964     9017   8276  12515   1258   2270    -47       O  
ATOM   1537  CB  LEU A 964      15.830  26.257   7.514  1.00 71.08           C  
ANISOU 1537  CB  LEU A 964     8264   7756  10986   1115   2340   -291       C  
ATOM   1538  CG  LEU A 964      16.219  27.216   6.392  1.00 73.14           C  
ANISOU 1538  CG  LEU A 964     8651   8134  11003   1026   2504   -469       C  
ATOM   1539  CD1 LEU A 964      16.064  28.682   6.816  1.00 70.28           C  
ANISOU 1539  CD1 LEU A 964     8352   8019  10330    983   2260   -331       C  
ATOM   1540  CD2 LEU A 964      17.649  26.933   5.946  1.00 76.80           C  
ANISOU 1540  CD2 LEU A 964     8907   8428  11846   1087   2794   -514       C  
ATOM   1541  N   ASP A 965      17.013  23.931   9.355  1.00 79.24           N  
ANISOU 1541  N   ASP A 965     8738   8313  13056   1418   2318    169       N  
ATOM   1542  CA  ASP A 965      16.984  23.435  10.736  1.00 79.51           C  
ANISOU 1542  CA  ASP A 965     8613   8324  13273   1526   2071    531       C  
ATOM   1543  C   ASP A 965      16.233  22.097  10.749  1.00 78.99           C  
ANISOU 1543  C   ASP A 965     8575   7999  13438   1548   2195    519       C  
ATOM   1544  O   ASP A 965      16.619  21.166  10.042  1.00 84.43           O  
ANISOU 1544  O   ASP A 965     9178   8385  14515   1586   2492    357       O  
ATOM   1545  CB  ASP A 965      16.312  24.490  11.626  1.00 77.40           C  
ANISOU 1545  CB  ASP A 965     8478   8389  12539   1463   1729    680       C  
ATOM   1546  CG  ASP A 965      16.551  25.902  11.120  1.00 77.76           C  
ANISOU 1546  CG  ASP A 965     8624   8660  12260   1370   1695    528       C  
ATOM   1547  OD1 ASP A 965      17.731  26.324  11.098  1.00 79.70           O  
ANISOU 1547  OD1 ASP A 965     8682   8909  12691   1409   1710    574       O  
ATOM   1548  OD2 ASP A 965      15.566  26.574  10.716  1.00 75.24           O  
ANISOU 1548  OD2 ASP A 965     8552   8494  11541   1259   1663    371       O  
ATOM   1549  N   GLY A 966      15.185  22.001  11.560  1.00 74.09           N  
ANISOU 1549  N   GLY A 966     8062   7477  12609   1518   1993    681       N  
ATOM   1550  CA  GLY A 966      14.076  21.090  11.300  1.00 72.53           C  
ANISOU 1550  CA  GLY A 966     7986   7105  12466   1456   2113    557       C  
ATOM   1551  C   GLY A 966      12.802  21.913  11.127  1.00 67.58           C  
ANISOU 1551  C   GLY A 966     7621   6746  11310   1306   1979    405       C  
ATOM   1552  O   GLY A 966      11.715  21.443  11.458  1.00 66.67           O  
ANISOU 1552  O   GLY A 966     7583   6597  11152   1255   1940    438       O  
ATOM   1553  N   VAL A 967      12.948  23.145  10.624  1.00 62.54           N  
ANISOU 1553  N   VAL A 967     7095   6356  10309   1241   1917    261       N  
ATOM   1554  CA  VAL A 967      11.830  24.067  10.397  1.00 58.47           C  
ANISOU 1554  CA  VAL A 967     6803   6091   9322   1117   1784    135       C  
ATOM   1555  C   VAL A 967      11.471  24.126   8.916  1.00 58.02           C  
ANISOU 1555  C   VAL A 967     6912   6019   9112    999   1962   -238       C  
ATOM   1556  O   VAL A 967      12.309  24.461   8.082  1.00 58.14           O  
ANISOU 1556  O   VAL A 967     6934   6033   9122    993   2113   -385       O  
ATOM   1557  CB  VAL A 967      12.176  25.500  10.841  1.00 55.79           C  
ANISOU 1557  CB  VAL A 967     6487   6033   8677   1119   1584    244       C  
ATOM   1558  CG1 VAL A 967      11.059  26.460  10.479  1.00 52.77           C  
ANISOU 1558  CG1 VAL A 967     6315   5863   7872   1008   1481    107       C  
ATOM   1559  CG2 VAL A 967      12.448  25.556  12.334  1.00 56.38           C  
ANISOU 1559  CG2 VAL A 967     6432   6191   8797   1205   1368    582       C  
ATOM   1560  N   ASP A 968      10.211  23.844   8.611  1.00 56.91           N  
ANISOU 1560  N   ASP A 968     6904   5892   8826    897   1933   -381       N  
ATOM   1561  CA  ASP A 968       9.718  23.821   7.247  1.00 58.07           C  
ANISOU 1561  CA  ASP A 968     7220   6060   8784    765   2050   -733       C  
ATOM   1562  C   ASP A 968       9.571  25.243   6.678  1.00 54.23           C  
ANISOU 1562  C   ASP A 968     6890   5868   7843    705   1932   -785       C  
ATOM   1563  O   ASP A 968       8.962  26.107   7.301  1.00 51.51           O  
ANISOU 1563  O   ASP A 968     6578   5712   7281    707   1712   -625       O  
ATOM   1564  CB  ASP A 968       8.380  23.081   7.231  1.00 61.79           C  
ANISOU 1564  CB  ASP A 968     7740   6460   9276    668   2004   -841       C  
ATOM   1565  CG  ASP A 968       7.730  23.051   5.858  1.00 67.50           C  
ANISOU 1565  CG  ASP A 968     8639   7248   9758    507   2059  -1215       C  
ATOM   1566  OD1 ASP A 968       8.261  22.354   4.940  1.00 72.20           O  
ANISOU 1566  OD1 ASP A 968     9264   7682  10485    463   2301  -1489       O  
ATOM   1567  OD2 ASP A 968       6.663  23.711   5.713  1.00 68.97           O  
ANISOU 1567  OD2 ASP A 968     8928   7650   9627    423   1855  -1235       O  
ATOM   1568  N   VAL A 969      10.157  25.482   5.503  1.00 52.99           N  
ANISOU 1568  N   VAL A 969     6830   5738   7564    654   2106   -998       N  
ATOM   1569  CA  VAL A 969       9.966  26.732   4.761  1.00 49.91           C  
ANISOU 1569  CA  VAL A 969     6612   5603   6746    583   2028  -1045       C  
ATOM   1570  C   VAL A 969       9.124  26.458   3.517  1.00 50.09           C  
ANISOU 1570  C   VAL A 969     6831   5699   6501    436   2065  -1341       C  
ATOM   1571  O   VAL A 969       9.622  25.912   2.539  1.00 51.16           O  
ANISOU 1571  O   VAL A 969     7037   5757   6645    379   2308  -1592       O  
ATOM   1572  CB  VAL A 969      11.301  27.346   4.325  1.00 50.39           C  
ANISOU 1572  CB  VAL A 969     6650   5680   6815    622   2203  -1029       C  
ATOM   1573  CG1 VAL A 969      11.075  28.727   3.740  1.00 49.18           C  
ANISOU 1573  CG1 VAL A 969     6661   5773   6252    561   2105   -995       C  
ATOM   1574  CG2 VAL A 969      12.257  27.415   5.501  1.00 50.20           C  
ANISOU 1574  CG2 VAL A 969     6393   5565   7116    755   2165   -773       C  
ATOM   1575  N   PRO A 970       7.833  26.830   3.557  1.00 48.91           N  
ANISOU 1575  N   PRO A 970     6761   5705   6115    370   1821  -1323       N  
ATOM   1576  CA  PRO A 970       6.915  26.520   2.467  1.00 50.37           C  
ANISOU 1576  CA  PRO A 970     7104   5982   6052    218   1784  -1592       C  
ATOM   1577  C   PRO A 970       7.015  27.561   1.368  1.00 50.67           C  
ANISOU 1577  C   PRO A 970     7338   6268   5645    154   1761  -1633       C  
ATOM   1578  O   PRO A 970       6.195  28.469   1.294  1.00 50.95           O  
ANISOU 1578  O   PRO A 970     7438   6506   5415    133   1519  -1510       O  
ATOM   1579  CB  PRO A 970       5.548  26.587   3.155  1.00 48.76           C  
ANISOU 1579  CB  PRO A 970     6840   5838   5846    200   1512  -1485       C  
ATOM   1580  CG  PRO A 970       5.720  27.674   4.166  1.00 45.83           C  
ANISOU 1580  CG  PRO A 970     6397   5556   5460    321   1379  -1163       C  
ATOM   1581  CD  PRO A 970       7.161  27.605   4.621  1.00 45.78           C  
ANISOU 1581  CD  PRO A 970     6301   5419   5673    428   1565  -1060       C  
ATOM   1582  N   LEU A 971       8.029  27.437   0.530  1.00 51.98           N  
ANISOU 1582  N   LEU A 971     7589   6407   5751    130   2031  -1783       N  
ATOM   1583  CA  LEU A 971       8.277  28.416  -0.514  1.00 52.75           C  
ANISOU 1583  CA  LEU A 971     7883   6733   5425     71   2061  -1782       C  
ATOM   1584  C   LEU A 971       7.953  27.861  -1.901  1.00 57.06           C  
ANISOU 1584  C   LEU A 971     8646   7388   5643    -96   2160  -2126       C  
ATOM   1585  O   LEU A 971       8.449  28.358  -2.925  1.00 58.37           O  
ANISOU 1585  O   LEU A 971     8998   7711   5467   -158   2308  -2184       O  
ATOM   1586  CB  LEU A 971       9.722  28.923  -0.431  1.00 52.39           C  
ANISOU 1586  CB  LEU A 971     7778   6618   5508    160   2308  -1658       C  
ATOM   1587  CG  LEU A 971      10.847  27.929  -0.187  1.00 53.01           C  
ANISOU 1587  CG  LEU A 971     7700   6425   6016    224   2623  -1776       C  
ATOM   1588  CD1 LEU A 971      10.842  26.824  -1.222  1.00 56.57           C  
ANISOU 1588  CD1 LEU A 971     8272   6800   6422    110   2874  -2168       C  
ATOM   1589  CD2 LEU A 971      12.162  28.668  -0.219  1.00 53.36           C  
ANISOU 1589  CD2 LEU A 971     7677   6455   6141    293   2823  -1633       C  
ATOM   1590  N   GLY A 972       7.116  26.827  -1.939  1.00 58.40           N  
ANISOU 1590  N   GLY A 972     8800   7482   5906   -184   2085  -2362       N  
ATOM   1591  CA  GLY A 972       6.558  26.384  -3.199  1.00 61.54           C  
ANISOU 1591  CA  GLY A 972     9408   8033   5939   -374   2084  -2706       C  
ATOM   1592  C   GLY A 972       5.743  27.516  -3.788  1.00 61.44           C  
ANISOU 1592  C   GLY A 972     9553   8374   5417   -434   1769  -2545       C  
ATOM   1593  O   GLY A 972       5.192  28.348  -3.067  1.00 58.87           O  
ANISOU 1593  O   GLY A 972     9124   8112   5129   -342   1504  -2226       O  
ATOM   1594  N   THR A 973       5.674  27.558  -5.107  1.00 65.18           N  
ANISOU 1594  N   THR A 973    10278   9078   5408   -587   1806  -2759       N  
ATOM   1595  CA  THR A 973       4.849  28.537  -5.786  1.00 65.88           C  
ANISOU 1595  CA  THR A 973    10522   9517   4992   -653   1482  -2597       C  
ATOM   1596  C   THR A 973       3.377  28.220  -5.486  1.00 65.82           C  
ANISOU 1596  C   THR A 973    10399   9562   5045   -718   1087  -2635       C  
ATOM   1597  O   THR A 973       3.008  27.053  -5.344  1.00 66.72           O  
ANISOU 1597  O   THR A 973    10432   9515   5402   -806   1118  -2942       O  
ATOM   1598  CB  THR A 973       5.152  28.553  -7.296  1.00 70.10           C  
ANISOU 1598  CB  THR A 973    11373  10313   4949   -819   1622  -2825       C  
ATOM   1599  OG1 THR A 973       4.673  29.775  -7.854  1.00 70.99           O  
ANISOU 1599  OG1 THR A 973    11628  10751   4593   -827   1349  -2517       O  
ATOM   1600  CG2 THR A 973       4.526  27.368  -8.015  1.00 73.77           C  
ANISOU 1600  CG2 THR A 973    11938  10825   5265  -1029   1590  -3310       C  
ATOM   1601  N   GLY A 974       2.554  29.259  -5.356  1.00 64.95           N  
ANISOU 1601  N   GLY A 974    10256   9645   4775   -668    737  -2316       N  
ATOM   1602  CA  GLY A 974       1.143  29.093  -5.001  1.00 64.62           C  
ANISOU 1602  CA  GLY A 974    10057   9650   4844   -709    362  -2303       C  
ATOM   1603  C   GLY A 974       0.373  28.246  -6.003  1.00 68.87           C  
ANISOU 1603  C   GLY A 974    10701  10353   5112   -940    205  -2686       C  
ATOM   1604  O   GLY A 974       0.336  28.559  -7.188  1.00 72.35           O  
ANISOU 1604  O   GLY A 974    11379  11094   5017  -1060    118  -2760       O  
ATOM   1605  N   ILE A 975      -0.225  27.158  -5.528  1.00 69.18           N  
ANISOU 1605  N   ILE A 975    10570  10198   5517  -1014    176  -2934       N  
ATOM   1606  CA  ILE A 975      -1.078  26.315  -6.363  1.00 73.46           C  
ANISOU 1606  CA  ILE A 975    11164  10868   5880  -1255     -9  -3329       C  
ATOM   1607  C   ILE A 975      -2.427  26.096  -5.692  1.00 73.15           C  
ANISOU 1607  C   ILE A 975    10845  10777   6170  -1279   -340  -3273       C  
ATOM   1608  O   ILE A 975      -2.622  26.456  -4.522  1.00 69.25           O  
ANISOU 1608  O   ILE A 975    10131  10113   6066  -1106   -355  -2961       O  
ATOM   1609  CB  ILE A 975      -0.435  24.944  -6.644  1.00 75.99           C  
ANISOU 1609  CB  ILE A 975    11555  10948   6368  -1382    352  -3815       C  
ATOM   1610  CG1 ILE A 975      -0.331  24.110  -5.353  1.00 73.36           C  
ANISOU 1610  CG1 ILE A 975    10952  10178   6743  -1279    545  -3802       C  
ATOM   1611  CG2 ILE A 975       0.926  25.128  -7.310  1.00 76.95           C  
ANISOU 1611  CG2 ILE A 975    11928  11104   6203  -1357    730  -3890       C  
ATOM   1612  CD1 ILE A 975      -0.315  22.614  -5.593  1.00 76.39           C  
ANISOU 1612  CD1 ILE A 975    11319  10301   7402  -1448    758  -4299       C  
ATOM   1613  N   SER A 976      -3.349  25.497  -6.439  1.00 77.42           N  
ANISOU 1613  N   SER A 976    11393  11470   6551  -1506   -594  -3591       N  
ATOM   1614  CA  SER A 976      -4.683  25.205  -5.939  1.00 78.09           C  
ANISOU 1614  CA  SER A 976    11192  11514   6962  -1566   -908  -3585       C  
ATOM   1615  C   SER A 976      -4.625  24.079  -4.905  1.00 77.04           C  
ANISOU 1615  C   SER A 976    10849  10945   7476  -1554   -638  -3732       C  
ATOM   1616  O   SER A 976      -3.971  23.063  -5.121  1.00 78.45           O  
ANISOU 1616  O   SER A 976    11119  10912   7776  -1646   -332  -4083       O  
ATOM   1617  CB  SER A 976      -5.595  24.819  -7.094  1.00 83.42           C  
ANISOU 1617  CB  SER A 976    11930  12479   7285  -1840  -1258  -3926       C  
ATOM   1618  OG  SER A 976      -6.938  24.821  -6.675  1.00 84.12           O  
ANISOU 1618  OG  SER A 976    11712  12589   7659  -1880  -1622  -3836       O  
ATOM   1619  N   SER A 977      -5.305  24.273  -3.780  1.00 75.04           N  
ANISOU 1619  N   SER A 977    10315  10550   7646  -1436   -733  -3448       N  
ATOM   1620  CA  SER A 977      -5.260  23.324  -2.668  1.00 74.00           C  
ANISOU 1620  CA  SER A 977     9981  10015   8120  -1397   -475  -3477       C  
ATOM   1621  C   SER A 977      -6.249  22.179  -2.799  1.00 78.76           C  
ANISOU 1621  C   SER A 977    10410  10483   9028  -1627   -577  -3824       C  
ATOM   1622  O   SER A 977      -6.129  21.183  -2.098  1.00 78.89           O  
ANISOU 1622  O   SER A 977    10299  10138   9536  -1639   -322  -3919       O  
ATOM   1623  CB  SER A 977      -5.547  24.048  -1.353  1.00 69.82           C  
ANISOU 1623  CB  SER A 977     9243   9404   7880  -1177   -495  -3018       C  
ATOM   1624  OG  SER A 977      -6.881  24.525  -1.304  1.00 69.99           O  
ANISOU 1624  OG  SER A 977     9065   9594   7931  -1216   -853  -2899       O  
ATOM   1625  N   GLY A 978      -7.250  22.337  -3.657  1.00 84.06           N  
ANISOU 1625  N   GLY A 978    11057  11441   9440  -1810   -965  -3987       N  
ATOM   1626  CA  GLY A 978      -8.296  21.329  -3.812  1.00 89.31           C  
ANISOU 1626  CA  GLY A 978    11521  12003  10409  -2055  -1116  -4326       C  
ATOM   1627  C   GLY A 978      -9.431  21.437  -2.805  1.00 89.49           C  
ANISOU 1627  C   GLY A 978    11176  11920  10904  -2005  -1270  -4063       C  
ATOM   1628  O   GLY A 978     -10.438  20.749  -2.936  1.00 93.45           O  
ANISOU 1628  O   GLY A 978    11463  12367  11673  -2212  -1444  -4300       O  
ATOM   1629  N   VAL A 979      -9.278  22.300  -1.805  1.00 87.41           N  
ANISOU 1629  N   VAL A 979    10832  11627  10751  -1743  -1192  -3593       N  
ATOM   1630  CA  VAL A 979     -10.295  22.483  -0.766  1.00 87.84           C  
ANISOU 1630  CA  VAL A 979    10551  11582  11241  -1673  -1272  -3324       C  
ATOM   1631  C   VAL A 979     -11.521  23.181  -1.359  1.00 91.91           C  
ANISOU 1631  C   VAL A 979    10897  12422  11600  -1751  -1751  -3277       C  
ATOM   1632  O   VAL A 979     -11.417  24.290  -1.889  1.00 91.52           O  
ANISOU 1632  O   VAL A 979    10972  12678  11124  -1651  -1972  -3081       O  
ATOM   1633  CB  VAL A 979      -9.750  23.311   0.424  1.00 83.13           C  
ANISOU 1633  CB  VAL A 979     9948  10901  10733  -1376  -1056  -2866       C  
ATOM   1634  CG1 VAL A 979     -10.857  23.621   1.430  1.00 82.50           C  
ANISOU 1634  CG1 VAL A 979     9541  10765  11040  -1307  -1129  -2602       C  
ATOM   1635  CG2 VAL A 979      -8.591  22.586   1.103  1.00 80.91           C  
ANISOU 1635  CG2 VAL A 979     9785  10303  10655  -1293   -623  -2869       C  
ATOM   1636  N   ASN A 980     -12.679  22.531  -1.250  1.00 96.71           N  
ANISOU 1636  N   ASN A 980    11201  12947  12594  -1927  -1907  -3433       N  
ATOM   1637  CA  ASN A 980     -13.898  22.994  -1.915  1.00101.01           C  
ANISOU 1637  CA  ASN A 980    11537  13791  13049  -2043  -2400  -3447       C  
ATOM   1638  C   ASN A 980     -14.565  24.144  -1.158  1.00 99.00           C  
ANISOU 1638  C   ASN A 980    11041  13616  12957  -1817  -2519  -2980       C  
ATOM   1639  O   ASN A 980     -14.529  25.298  -1.589  1.00 99.21           O  
ANISOU 1639  O   ASN A 980    11153  13923  12619  -1683  -2753  -2737       O  
ATOM   1640  CB  ASN A 980     -14.901  21.833  -2.093  1.00104.92           C  
ANISOU 1640  CB  ASN A 980    11757  14153  13955  -2339  -2526  -3818       C  
ATOM   1641  CG  ASN A 980     -14.336  20.668  -2.898  1.00108.13           C  
ANISOU 1641  CG  ASN A 980    12386  14460  14238  -2590  -2412  -4345       C  
ATOM   1642  OD1 ASN A 980     -15.000  19.645  -3.069  1.00112.64           O  
ANISOU 1642  OD1 ASN A 980    12768  14877  15154  -2850  -2466  -4701       O  
ATOM   1643  ND2 ASN A 980     -13.115  20.814  -3.397  1.00106.74           N  
ANISOU 1643  ND2 ASN A 980    12598  14353  13603  -2522  -2233  -4414       N  
ATOM   1644  N   ASP A 981     -15.149  23.815  -0.014  1.00 97.56           N  
ANISOU 1644  N   ASP A 981    10563  13166  13338  -1773  -2322  -2855       N  
ATOM   1645  CA  ASP A 981     -16.079  24.693   0.665  1.00 97.00           C  
ANISOU 1645  CA  ASP A 981    10180  13143  13529  -1621  -2437  -2512       C  
ATOM   1646  C   ASP A 981     -15.317  25.574   1.650  1.00 91.95           C  
ANISOU 1646  C   ASP A 981     9679  12426  12833  -1320  -2128  -2141       C  
ATOM   1647  O   ASP A 981     -15.178  25.219   2.820  1.00 90.96           O  
ANISOU 1647  O   ASP A 981     9482  12036  13042  -1242  -1765  -2031       O  
ATOM   1648  CB  ASP A 981     -17.135  23.825   1.370  1.00 99.49           C  
ANISOU 1648  CB  ASP A 981    10102  13214  14485  -1758  -2348  -2598       C  
ATOM   1649  CG  ASP A 981     -18.303  24.629   1.915  1.00100.40           C  
ANISOU 1649  CG  ASP A 981     9829  13391  14928  -1646  -2495  -2311       C  
ATOM   1650  OD1 ASP A 981     -19.420  24.494   1.368  1.00103.70           O  
ANISOU 1650  OD1 ASP A 981     9930  13926  15544  -1810  -2855  -2432       O  
ATOM   1651  OD2 ASP A 981     -18.105  25.384   2.892  1.00 97.05           O  
ANISOU 1651  OD2 ASP A 981     9401  12893  14579  -1400  -2248  -1983       O  
ATOM   1652  N   THR A 982     -14.814  26.719   1.183  1.00 89.54           N  
ANISOU 1652  N   THR A 982     9574  12351  12096  -1163  -2271  -1947       N  
ATOM   1653  CA  THR A 982     -14.012  27.597   2.051  1.00 84.03           C  
ANISOU 1653  CA  THR A 982     9021  11580  11325   -899  -1992  -1637       C  
ATOM   1654  C   THR A 982     -14.057  29.101   1.724  1.00 82.79           C  
ANISOU 1654  C   THR A 982     8899  11647  10909   -713  -2212  -1341       C  
ATOM   1655  O   THR A 982     -14.151  29.527   0.572  1.00 84.04           O  
ANISOU 1655  O   THR A 982     9147  12064  10721   -765  -2551  -1355       O  
ATOM   1656  CB  THR A 982     -12.540  27.128   2.113  1.00 81.55           C  
ANISOU 1656  CB  THR A 982     9060  11148  10775   -879  -1675  -1736       C  
ATOM   1657  OG1 THR A 982     -11.857  27.808   3.180  1.00 76.32           O  
ANISOU 1657  OG1 THR A 982     8476  10380  10143   -651  -1392  -1458       O  
ATOM   1658  CG2 THR A 982     -11.824  27.374   0.773  1.00 82.83           C  
ANISOU 1658  CG2 THR A 982     9527  11546  10395   -941  -1855  -1869       C  
ATOM   1659  N   SER A 983     -13.958  29.890   2.787  1.00 79.75           N  
ANISOU 1659  N   SER A 983     8455  11149  10695   -498  -1993  -1070       N  
ATOM   1660  CA  SER A 983     -14.064  31.339   2.733  1.00 79.50           C  
ANISOU 1660  CA  SER A 983     8407  11239  10559   -299  -2126   -773       C  
ATOM   1661  C   SER A 983     -12.731  31.999   2.374  1.00 76.46           C  
ANISOU 1661  C   SER A 983     8394  10921   9733   -197  -2034   -682       C  
ATOM   1662  O   SER A 983     -12.708  33.046   1.726  1.00 76.97           O  
ANISOU 1662  O   SER A 983     8522  11147   9574   -105  -2245   -490       O  
ATOM   1663  CB  SER A 983     -14.514  31.836   4.106  1.00 78.37           C  
ANISOU 1663  CB  SER A 983     8044  10914  10817   -133  -1874   -582       C  
ATOM   1664  OG  SER A 983     -15.205  30.800   4.793  1.00 79.60           O  
ANISOU 1664  OG  SER A 983     7967  10911  11366   -249  -1725   -716       O  
ATOM   1665  N   LEU A 984     -11.633  31.370   2.795  1.00 72.17           N  
ANISOU 1665  N   LEU A 984     8076  10241   9104   -214  -1716   -801       N  
ATOM   1666  CA  LEU A 984     -10.293  31.939   2.680  1.00 68.74           C  
ANISOU 1666  CA  LEU A 984     7952   9822   8342   -113  -1558   -716       C  
ATOM   1667  C   LEU A 984      -9.614  31.692   1.331  1.00 69.21           C  
ANISOU 1667  C   LEU A 984     8282  10056   7958   -234  -1684   -869       C  
ATOM   1668  O   LEU A 984      -9.598  30.570   0.833  1.00 70.64           O  
ANISOU 1668  O   LEU A 984     8509  10236   8095   -416  -1691  -1155       O  
ATOM   1669  CB  LEU A 984      -9.400  31.341   3.759  1.00 66.63           C  
ANISOU 1669  CB  LEU A 984     7772   9334   8207    -73  -1173   -763       C  
ATOM   1670  CG  LEU A 984      -9.902  31.358   5.195  1.00 65.33           C  
ANISOU 1670  CG  LEU A 984     7399   9001   8419     17   -973   -647       C  
ATOM   1671  CD1 LEU A 984      -8.882  30.679   6.092  1.00 63.19           C  
ANISOU 1671  CD1 LEU A 984     7259   8558   8192     38   -641   -676       C  
ATOM   1672  CD2 LEU A 984     -10.155  32.788   5.637  1.00 65.31           C  
ANISOU 1672  CD2 LEU A 984     7329   9036   8450    199  -1001   -402       C  
ATOM   1673  N   LEU A 985      -9.044  32.750   0.759  1.00 68.35           N  
ANISOU 1673  N   LEU A 985     8355  10084   7531   -138  -1752   -683       N  
ATOM   1674  CA  LEU A 985      -8.175  32.650  -0.413  1.00 69.52           C  
ANISOU 1674  CA  LEU A 985     8808  10393   7214   -229  -1777   -789       C  
ATOM   1675  C   LEU A 985      -6.870  31.952  -0.051  1.00 66.01           C  
ANISOU 1675  C   LEU A 985     8554   9778   6748   -242  -1401   -955       C  
ATOM   1676  O   LEU A 985      -6.327  31.179  -0.847  1.00 65.92           O  
ANISOU 1676  O   LEU A 985     8726   9818   6501   -383  -1342  -1207       O  
ATOM   1677  CB  LEU A 985      -7.822  34.046  -0.944  1.00 70.71           C  
ANISOU 1677  CB  LEU A 985     9092  10686   7086   -100  -1879   -483       C  
ATOM   1678  CG  LEU A 985      -8.924  34.886  -1.597  1.00 74.83           C  
ANISOU 1678  CG  LEU A 985     9474  11410   7546    -70  -2285   -255       C  
ATOM   1679  CD1 LEU A 985      -8.463  36.333  -1.765  1.00 74.79           C  
ANISOU 1679  CD1 LEU A 985     9575  11434   7407    104  -2283    106       C  
ATOM   1680  CD2 LEU A 985      -9.343  34.295  -2.937  1.00 79.14           C  
ANISOU 1680  CD2 LEU A 985    10110  12239   7718   -276  -2600   -434       C  
ATOM   1681  N   TYR A 986      -6.367  32.261   1.145  1.00 61.57           N  
ANISOU 1681  N   TYR A 986     7941   9019   6432    -92  -1150   -811       N  
ATOM   1682  CA  TYR A 986      -5.099  31.743   1.620  1.00 58.61           C  
ANISOU 1682  CA  TYR A 986     7705   8482   6083    -69   -820   -897       C  
ATOM   1683  C   TYR A 986      -5.209  31.163   3.018  1.00 54.82           C  
ANISOU 1683  C   TYR A 986     7055   7776   5997    -17   -627   -887       C  
ATOM   1684  O   TYR A 986      -5.950  31.661   3.859  1.00 53.23           O  
ANISOU 1684  O   TYR A 986     6674   7538   6011     68   -667   -729       O  
ATOM   1685  CB  TYR A 986      -4.055  32.858   1.665  1.00 58.18           C  
ANISOU 1685  CB  TYR A 986     7803   8443   5857     64   -702   -690       C  
ATOM   1686  CG  TYR A 986      -3.839  33.610   0.366  1.00 61.98           C  
ANISOU 1686  CG  TYR A 986     8472   9141   5937     36   -849   -616       C  
ATOM   1687  CD1 TYR A 986      -3.120  33.038  -0.679  1.00 64.78           C  
ANISOU 1687  CD1 TYR A 986     9046   9588   5977    -86   -770   -813       C  
ATOM   1688  CD2 TYR A 986      -4.318  34.907   0.200  1.00 62.64           C  
ANISOU 1688  CD2 TYR A 986     8516   9324   5961    138  -1037   -334       C  
ATOM   1689  CE1 TYR A 986      -2.908  33.725  -1.860  1.00 67.86           C  
ANISOU 1689  CE1 TYR A 986     9632  10200   5951   -120   -881   -722       C  
ATOM   1690  CE2 TYR A 986      -4.110  35.600  -0.977  1.00 65.66           C  
ANISOU 1690  CE2 TYR A 986     9077   9902   5968    117  -1167   -211       C  
ATOM   1691  CZ  TYR A 986      -3.405  35.007  -2.006  1.00 68.54           C  
ANISOU 1691  CZ  TYR A 986     9680  10391   5970    -17  -1090   -398       C  
ATOM   1692  OH  TYR A 986      -3.195  35.689  -3.191  1.00 72.06           O  
ANISOU 1692  OH  TYR A 986    10329  11060   5990    -49  -1200   -256       O  
ATOM   1693  N   ASN A 987      -4.417  30.127   3.260  1.00 53.92           N  
ANISOU 1693  N   ASN A 987     7007   7508   5972    -63   -396  -1042       N  
ATOM   1694  CA  ASN A 987      -4.184  29.605   4.599  1.00 51.22           C  
ANISOU 1694  CA  ASN A 987     6558   6957   5944      5   -179   -974       C  
ATOM   1695  C   ASN A 987      -3.872  30.669   5.632  1.00 48.21           C  
ANISOU 1695  C   ASN A 987     6153   6570   5592    172   -111   -718       C  
ATOM   1696  O   ASN A 987      -3.225  31.673   5.337  1.00 47.13           O  
ANISOU 1696  O   ASN A 987     6135   6519   5252    247   -127   -616       O  
ATOM   1697  CB  ASN A 987      -2.991  28.657   4.593  1.00 50.93           C  
ANISOU 1697  CB  ASN A 987     6633   6766   5949    -17     63  -1102       C  
ATOM   1698  CG  ASN A 987      -3.246  27.400   3.811  1.00 54.10           C  
ANISOU 1698  CG  ASN A 987     7043   7096   6414   -189     74  -1402       C  
ATOM   1699  OD1 ASN A 987      -4.377  26.917   3.725  1.00 55.66           O  
ANISOU 1699  OD1 ASN A 987     7102   7287   6756   -297    -57  -1503       O  
ATOM   1700  ND2 ASN A 987      -2.184  26.847   3.243  1.00 55.65           N  
ANISOU 1700  ND2 ASN A 987     7388   7221   6536   -222    249  -1567       N  
ATOM   1701  N   GLU A 988      -4.317  30.415   6.854  1.00 46.57           N  
ANISOU 1701  N   GLU A 988     5799   6254   5641    217    -16   -626       N  
ATOM   1702  CA  GLU A 988      -3.943  31.210   8.000  1.00 44.33           C  
ANISOU 1702  CA  GLU A 988     5505   5952   5384    353     88   -436       C  
ATOM   1703  C   GLU A 988      -3.561  30.231   9.094  1.00 43.34           C  
ANISOU 1703  C   GLU A 988     5340   5677   5447    360    289   -401       C  
ATOM   1704  O   GLU A 988      -4.077  29.117   9.134  1.00 43.89           O  
ANISOU 1704  O   GLU A 988     5321   5642   5710    272    333   -481       O  
ATOM   1705  CB  GLU A 988      -5.106  32.073   8.461  1.00 45.83           C  
ANISOU 1705  CB  GLU A 988     5545   6199   5667    408     -5   -329       C  
ATOM   1706  CG  GLU A 988      -5.705  32.970   7.382  1.00 48.77           C  
ANISOU 1706  CG  GLU A 988     5907   6706   5916    408   -242   -316       C  
ATOM   1707  CD  GLU A 988      -6.791  33.895   7.924  1.00 49.47           C  
ANISOU 1707  CD  GLU A 988     5814   6811   6170    494   -305   -191       C  
ATOM   1708  OE1 GLU A 988      -7.461  34.575   7.100  1.00 51.78           O  
ANISOU 1708  OE1 GLU A 988     6044   7199   6429    505   -523   -141       O  
ATOM   1709  OE2 GLU A 988      -6.966  33.936   9.169  1.00 47.09           O  
ANISOU 1709  OE2 GLU A 988     5431   6429   6030    551   -130   -137       O  
ATOM   1710  N   TYR A 989      -2.653  30.644   9.972  1.00 41.24           N  
ANISOU 1710  N   TYR A 989     5134   5400   5132    457    400   -272       N  
ATOM   1711  CA  TYR A 989      -2.180  29.782  11.052  1.00 41.08           C  
ANISOU 1711  CA  TYR A 989     5088   5267   5252    479    564   -182       C  
ATOM   1712  C   TYR A 989      -2.251  30.542  12.357  1.00 39.73           C  
ANISOU 1712  C   TYR A 989     4896   5160   5037    565    615    -22       C  
ATOM   1713  O   TYR A 989      -1.787  31.671  12.458  1.00 38.39           O  
ANISOU 1713  O   TYR A 989     4792   5080   4712    629    572      6       O  
ATOM   1714  CB  TYR A 989      -0.740  29.327  10.814  1.00 40.82           C  
ANISOU 1714  CB  TYR A 989     5153   5165   5191    500    644   -195       C  
ATOM   1715  CG  TYR A 989      -0.533  28.581   9.528  1.00 40.98           C  
ANISOU 1715  CG  TYR A 989     5220   5117   5233    412    645   -394       C  
ATOM   1716  CD1 TYR A 989      -0.312  29.264   8.345  1.00 41.00           C  
ANISOU 1716  CD1 TYR A 989     5329   5231   5017    385    554   -508       C  
ATOM   1717  CD2 TYR A 989      -0.527  27.192   9.501  1.00 42.49           C  
ANISOU 1717  CD2 TYR A 989     5359   5124   5659    350    758   -470       C  
ATOM   1718  CE1 TYR A 989      -0.106  28.583   7.155  1.00 42.84           C  
ANISOU 1718  CE1 TYR A 989     5633   5429   5212    289    575   -720       C  
ATOM   1719  CE2 TYR A 989      -0.323  26.500   8.316  1.00 44.02           C  
ANISOU 1719  CE2 TYR A 989     5607   5246   5870    255    786   -707       C  
ATOM   1720  CZ  TYR A 989      -0.118  27.204   7.149  1.00 43.96           C  
ANISOU 1720  CZ  TYR A 989     5724   5387   5590    220    693   -844       C  
ATOM   1721  OH  TYR A 989       0.061  26.544   5.973  1.00 46.37           O  
ANISOU 1721  OH  TYR A 989     6109   5654   5854    111    733  -1104       O  
ATOM   1722  N   ILE A 990      -2.835  29.916  13.366  1.00 40.25           N  
ANISOU 1722  N   ILE A 990     4876   5177   5241    556    723     72       N  
ATOM   1723  CA  ILE A 990      -3.099  30.618  14.599  1.00 39.03           C  
ANISOU 1723  CA  ILE A 990     4709   5107   5011    617    792    189       C  
ATOM   1724  C   ILE A 990      -2.648  29.779  15.776  1.00 38.96           C  
ANISOU 1724  C   ILE A 990     4714   5061   5027    630    930    357       C  
ATOM   1725  O   ILE A 990      -3.034  28.640  15.890  1.00 39.99           O  
ANISOU 1725  O   ILE A 990     4773   5071   5349    578   1016    410       O  
ATOM   1726  CB  ILE A 990      -4.586  30.956  14.733  1.00 39.75           C  
ANISOU 1726  CB  ILE A 990     4665   5219   5217    595    806    162       C  
ATOM   1727  CG1 ILE A 990      -5.087  31.735  13.506  1.00 39.39           C  
ANISOU 1727  CG1 ILE A 990     4584   5214   5166    589    627     40       C  
ATOM   1728  CG2 ILE A 990      -4.803  31.790  15.982  1.00 40.41           C  
ANISOU 1728  CG2 ILE A 990     4758   5393   5203    659    917    240       C  
ATOM   1729  CD1 ILE A 990      -5.557  30.895  12.339  1.00 40.18           C  
ANISOU 1729  CD1 ILE A 990     4620   5259   5386    488    517    -75       C  
ATOM   1730  N   VAL A 991      -1.801  30.360  16.615  1.00 38.22           N  
ANISOU 1730  N   VAL A 991     4709   5070   4743    692    935    447       N  
ATOM   1731  CA  VAL A 991      -1.429  29.790  17.897  1.00 39.28           C  
ANISOU 1731  CA  VAL A 991     4867   5233   4822    712   1031    646       C  
ATOM   1732  C   VAL A 991      -1.937  30.683  19.029  1.00 39.90           C  
ANISOU 1732  C   VAL A 991     4980   5473   4706    729   1101    673       C  
ATOM   1733  O   VAL A 991      -2.128  31.876  18.846  1.00 38.80           O  
ANISOU 1733  O   VAL A 991     4861   5406   4473    749   1056    533       O  
ATOM   1734  CB  VAL A 991       0.086  29.630  18.042  1.00 39.14           C  
ANISOU 1734  CB  VAL A 991     4915   5230   4723    759    958    733       C  
ATOM   1735  CG1 VAL A 991       0.586  28.550  17.106  1.00 39.50           C  
ANISOU 1735  CG1 VAL A 991     4917   5087   5001    747    960    716       C  
ATOM   1736  CG2 VAL A 991       0.818  30.941  17.790  1.00 38.41           C  
ANISOU 1736  CG2 VAL A 991     4893   5251   4449    790    842    614       C  
ATOM   1737  N   TYR A 992      -2.140  30.088  20.200  1.00 41.81           N  
ANISOU 1737  N   TYR A 992     5233   5760   4890    720   1230    856       N  
ATOM   1738  CA  TYR A 992      -2.809  30.751  21.315  1.00 42.61           C  
ANISOU 1738  CA  TYR A 992     5372   6012   4806    716   1361    866       C  
ATOM   1739  C   TYR A 992      -1.917  30.872  22.533  1.00 43.63           C  
ANISOU 1739  C   TYR A 992     5633   6323   4621    732   1348   1005       C  
ATOM   1740  O   TYR A 992      -2.390  31.178  23.610  1.00 45.87           O  
ANISOU 1740  O   TYR A 992     5976   6751   4700    713   1485   1040       O  
ATOM   1741  CB  TYR A 992      -4.105  29.999  21.640  1.00 44.05           C  
ANISOU 1741  CB  TYR A 992     5446   6117   5173    667   1563    950       C  
ATOM   1742  CG  TYR A 992      -5.025  29.956  20.437  1.00 43.93           C  
ANISOU 1742  CG  TYR A 992     5275   5950   5462    636   1528    790       C  
ATOM   1743  CD1 TYR A 992      -5.037  28.858  19.589  1.00 44.36           C  
ANISOU 1743  CD1 TYR A 992     5249   5828   5777    589   1482    805       C  
ATOM   1744  CD2 TYR A 992      -5.849  31.033  20.120  1.00 43.42           C  
ANISOU 1744  CD2 TYR A 992     5140   5921   5434    652   1524    615       C  
ATOM   1745  CE1 TYR A 992      -5.856  28.824  18.474  1.00 44.13           C  
ANISOU 1745  CE1 TYR A 992     5086   5698   5983    541   1410    638       C  
ATOM   1746  CE2 TYR A 992      -6.662  31.006  19.003  1.00 43.24           C  
ANISOU 1746  CE2 TYR A 992     4965   5792   5671    624   1440    495       C  
ATOM   1747  CZ  TYR A 992      -6.661  29.898  18.186  1.00 43.68           C  
ANISOU 1747  CZ  TYR A 992     4956   5710   5928    560   1370    500       C  
ATOM   1748  OH  TYR A 992      -7.465  29.846  17.073  1.00 44.75           O  
ANISOU 1748  OH  TYR A 992     4947   5772   6283    510   1253    364       O  
ATOM   1749  N   ASP A 993      -0.625  30.645  22.338  1.00 44.03           N  
ANISOU 1749  N   ASP A 993     5722   6375   4630    762   1182   1075       N  
ATOM   1750  CA  ASP A 993       0.381  30.733  23.391  1.00 46.83           C  
ANISOU 1750  CA  ASP A 993     6177   6917   4700    774   1096   1218       C  
ATOM   1751  C   ASP A 993       1.606  31.402  22.783  1.00 45.57           C  
ANISOU 1751  C   ASP A 993     6022   6766   4524    801    890   1093       C  
ATOM   1752  O   ASP A 993       2.154  30.912  21.795  1.00 43.88           O  
ANISOU 1752  O   ASP A 993     5737   6391   4544    828    821   1096       O  
ATOM   1753  CB  ASP A 993       0.741  29.332  23.912  1.00 49.40           C  
ANISOU 1753  CB  ASP A 993     6480   7196   5091    791   1116   1554       C  
ATOM   1754  CG  ASP A 993       1.706  29.360  25.110  1.00 52.78           C  
ANISOU 1754  CG  ASP A 993     7003   7858   5191    803    994   1758       C  
ATOM   1755  OD1 ASP A 993       2.426  30.372  25.317  1.00 53.02           O  
ANISOU 1755  OD1 ASP A 993     7094   8055   4995    795    840   1608       O  
ATOM   1756  OD2 ASP A 993       1.755  28.343  25.843  1.00 55.40           O  
ANISOU 1756  OD2 ASP A 993     7341   8204   5502    816   1040   2085       O  
ATOM   1757  N   ILE A 994       2.029  32.515  23.375  1.00 47.15           N  
ANISOU 1757  N   ILE A 994     6305   7145   4462    781    815    967       N  
ATOM   1758  CA  ILE A 994       3.170  33.297  22.864  1.00 46.55           C  
ANISOU 1758  CA  ILE A 994     6221   7076   4389    788    637    833       C  
ATOM   1759  C   ILE A 994       4.477  32.493  22.797  1.00 47.16           C  
ANISOU 1759  C   ILE A 994     6235   7133   4549    823    483   1028       C  
ATOM   1760  O   ILE A 994       5.351  32.799  21.973  1.00 48.16           O  
ANISOU 1760  O   ILE A 994     6301   7176   4819    839    384    941       O  
ATOM   1761  CB  ILE A 994       3.412  34.579  23.702  1.00 47.95           C  
ANISOU 1761  CB  ILE A 994     6491   7447   4278    738    587    655       C  
ATOM   1762  CG1 ILE A 994       3.734  34.235  25.172  1.00 51.18           C  
ANISOU 1762  CG1 ILE A 994     6988   8106   4351    703    540    819       C  
ATOM   1763  CG2 ILE A 994       2.201  35.497  23.620  1.00 47.15           C  
ANISOU 1763  CG2 ILE A 994     6421   7311   4181    723    757    434       C  
ATOM   1764  CD1 ILE A 994       4.149  35.420  26.022  1.00 52.69           C  
ANISOU 1764  CD1 ILE A 994     7279   8509   4231    628    459    609       C  
ATOM   1765  N   ALA A 995       4.602  31.479  23.659  1.00 47.66           N  
ANISOU 1765  N   ALA A 995     6300   7264   4545    840    477   1308       N  
ATOM   1766  CA  ALA A 995       5.778  30.617  23.694  1.00 48.03           C  
ANISOU 1766  CA  ALA A 995     6255   7272   4721    895    337   1544       C  
ATOM   1767  C   ALA A 995       5.898  29.682  22.472  1.00 46.83           C  
ANISOU 1767  C   ALA A 995     5985   6824   4982    948    411   1572       C  
ATOM   1768  O   ALA A 995       6.903  28.977  22.335  1.00 48.04           O  
ANISOU 1768  O   ALA A 995     6034   6891   5328   1008    328   1737       O  
ATOM   1769  CB  ALA A 995       5.779  29.798  24.980  1.00 50.68           C  
ANISOU 1769  CB  ALA A 995     6629   7756   4871    906    315   1881       C  
ATOM   1770  N   GLN A 996       4.882  29.657  21.606  1.00 44.35           N  
ANISOU 1770  N   GLN A 996     5679   6359   4812    925    565   1405       N  
ATOM   1771  CA  GLN A 996       4.919  28.862  20.375  1.00 43.22           C  
ANISOU 1771  CA  GLN A 996     5451   5957   5013    946    639   1356       C  
ATOM   1772  C   GLN A 996       5.505  29.642  19.203  1.00 41.18           C  
ANISOU 1772  C   GLN A 996     5182   5649   4815    941    588   1113       C  
ATOM   1773  O   GLN A 996       5.572  29.127  18.091  1.00 39.19           O  
ANISOU 1773  O   GLN A 996     4886   5214   4788    944    656   1020       O  
ATOM   1774  CB  GLN A 996       3.513  28.379  20.000  1.00 43.50           C  
ANISOU 1774  CB  GLN A 996     5488   5870   5167    902    803   1295       C  
ATOM   1775  CG  GLN A 996       2.899  27.376  20.973  1.00 46.04           C  
ANISOU 1775  CG  GLN A 996     5799   6170   5522    899    913   1558       C  
ATOM   1776  CD  GLN A 996       1.504  26.905  20.559  1.00 46.16           C  
ANISOU 1776  CD  GLN A 996     5777   6046   5713    837   1079   1478       C  
ATOM   1777  OE1 GLN A 996       0.528  27.156  21.250  1.00 47.60           O  
ANISOU 1777  OE1 GLN A 996     5989   6329   5767    799   1176   1507       O  
ATOM   1778  NE2 GLN A 996       1.410  26.228  19.424  1.00 46.48           N  
ANISOU 1778  NE2 GLN A 996     5744   5858   6055    817   1118   1357       N  
ATOM   1779  N   VAL A 997       5.918  30.885  19.457  1.00 41.60           N  
ANISOU 1779  N   VAL A 997     5281   5862   4661    923    485   1003       N  
ATOM   1780  CA  VAL A 997       6.436  31.783  18.421  1.00 40.09           C  
ANISOU 1780  CA  VAL A 997     5089   5631   4510    910    454    799       C  
ATOM   1781  C   VAL A 997       7.879  32.173  18.718  1.00 41.13           C  
ANISOU 1781  C   VAL A 997     5157   5832   4639    924    322    839       C  
ATOM   1782  O   VAL A 997       8.195  32.618  19.815  1.00 43.37           O  
ANISOU 1782  O   VAL A 997     5454   6290   4733    907    204    897       O  
ATOM   1783  CB  VAL A 997       5.614  33.087  18.347  1.00 39.35           C  
ANISOU 1783  CB  VAL A 997     5081   5619   4249    867    464    612       C  
ATOM   1784  CG1 VAL A 997       6.132  33.990  17.229  1.00 38.32           C  
ANISOU 1784  CG1 VAL A 997     4955   5428   4175    854    446    452       C  
ATOM   1785  CG2 VAL A 997       4.130  32.787  18.166  1.00 39.07           C  
ANISOU 1785  CG2 VAL A 997     5070   5537   4236    853    575    581       C  
ATOM   1786  N   ASN A 998       8.744  32.010  17.727  1.00 41.21           N  
ANISOU 1786  N   ASN A 998     5090   5711   4856    945    347    792       N  
ATOM   1787  CA  ASN A 998      10.106  32.484  17.808  1.00 42.37           C  
ANISOU 1787  CA  ASN A 998     5139   5896   5062    949    242    799       C  
ATOM   1788  C   ASN A 998      10.443  33.294  16.571  1.00 41.12           C  
ANISOU 1788  C   ASN A 998     4992   5652   4976    917    320    608       C  
ATOM   1789  O   ASN A 998      10.670  32.738  15.511  1.00 41.45           O  
ANISOU 1789  O   ASN A 998     5008   5546   5195    937    446    569       O  
ATOM   1790  CB  ASN A 998      11.059  31.304  17.940  1.00 44.59           C  
ANISOU 1790  CB  ASN A 998     5265   6084   5593   1023    223    998       C  
ATOM   1791  CG  ASN A 998      12.452  31.719  18.365  1.00 46.05           C  
ANISOU 1791  CG  ASN A 998     5301   6348   5846   1030     63   1059       C  
ATOM   1792  OD1 ASN A 998      13.405  30.979  18.162  1.00 47.83           O  
ANISOU 1792  OD1 ASN A 998     5356   6461   6354   1097     67   1180       O  
ATOM   1793  ND2 ASN A 998      12.574  32.893  18.969  1.00 46.33           N  
ANISOU 1793  ND2 ASN A 998     5379   6564   5658    958    -74    964       N  
ATOM   1794  N   LEU A 999      10.457  34.614  16.714  1.00 41.06           N  
ANISOU 1794  N   LEU A 999     5036   5735   4831    861    261    486       N  
ATOM   1795  CA  LEU A 999      10.712  35.514  15.592  1.00 40.54           C  
ANISOU 1795  CA  LEU A 999     4995   5588   4820    826    342    343       C  
ATOM   1796  C   LEU A 999      12.159  35.391  15.151  1.00 41.74           C  
ANISOU 1796  C   LEU A 999     5001   5669   5187    832    360    368       C  
ATOM   1797  O   LEU A 999      13.064  35.417  15.986  1.00 42.72           O  
ANISOU 1797  O   LEU A 999     4996   5864   5371    829    226    439       O  
ATOM   1798  CB  LEU A 999      10.427  36.958  15.994  1.00 40.87           C  
ANISOU 1798  CB  LEU A 999     5102   5705   4719    767    282    226       C  
ATOM   1799  CG  LEU A 999       8.993  37.257  16.449  1.00 40.58           C  
ANISOU 1799  CG  LEU A 999     5186   5726   4507    766    294    179       C  
ATOM   1800  CD1 LEU A 999       8.843  38.733  16.777  1.00 40.87           C  
ANISOU 1800  CD1 LEU A 999     5267   5787   4474    714    270     38       C  
ATOM   1801  CD2 LEU A 999       7.983  36.847  15.379  1.00 39.76           C  
ANISOU 1801  CD2 LEU A 999     5147   5530   4430    794    404    171       C  
ATOM   1802  N   LYS A1000      12.368  35.243  13.843  1.00 41.25           N  
ANISOU 1802  N   LYS A1000     4952   5480   5237    834    526    309       N  
ATOM   1803  CA  LYS A1000      13.702  35.018  13.283  1.00 42.04           C  
ANISOU 1803  CA  LYS A1000     4905   5488   5580    845    614    321       C  
ATOM   1804  C   LYS A1000      14.186  36.161  12.406  1.00 40.98           C  
ANISOU 1804  C   LYS A1000     4793   5315   5462    780    715    225       C  
ATOM   1805  O   LYS A1000      15.326  36.593  12.548  1.00 41.12           O  
ANISOU 1805  O   LYS A1000     4655   5315   5652    754    700    235       O  
ATOM   1806  CB  LYS A1000      13.728  33.717  12.466  1.00 43.71           C  
ANISOU 1806  CB  LYS A1000     5101   5563   5941    898    789    325       C  
ATOM   1807  CG  LYS A1000      13.449  32.452  13.261  1.00 45.75           C  
ANISOU 1807  CG  LYS A1000     5299   5796   6285    968    727    456       C  
ATOM   1808  CD  LYS A1000      14.178  32.492  14.587  1.00 48.86           C  
ANISOU 1808  CD  LYS A1000     5536   6289   6738    998    519    623       C  
ATOM   1809  CE  LYS A1000      14.530  31.116  15.097  1.00 52.39           C  
ANISOU 1809  CE  LYS A1000     5841   6648   7414   1093    504    815       C  
ATOM   1810  NZ  LYS A1000      15.876  30.671  14.633  1.00 56.02           N  
ANISOU 1810  NZ  LYS A1000     6078   6965   8241   1151    595    851       N  
ATOM   1811  N   TYR A1001      13.333  36.631  11.493  1.00 39.12           N  
ANISOU 1811  N   TYR A1001     4734   5064   5065    752    812    152       N  
ATOM   1812  CA  TYR A1001      13.713  37.685  10.564  1.00 39.17           C  
ANISOU 1812  CA  TYR A1001     4786   5024   5073    695    930    109       C  
ATOM   1813  C   TYR A1001      12.690  38.810  10.467  1.00 38.69           C  
ANISOU 1813  C   TYR A1001     4876   4997   4826    664    875     87       C  
ATOM   1814  O   TYR A1001      11.510  38.631  10.775  1.00 38.73           O  
ANISOU 1814  O   TYR A1001     4974   5057   4684    691    790     82       O  
ATOM   1815  CB  TYR A1001      13.928  37.118   9.170  1.00 39.61           C  
ANISOU 1815  CB  TYR A1001     4904   5009   5137    694   1158     74       C  
ATOM   1816  CG  TYR A1001      14.891  35.965   9.104  1.00 40.54           C  
ANISOU 1816  CG  TYR A1001     4866   5046   5491    737   1272     74       C  
ATOM   1817  CD1 TYR A1001      16.261  36.179   9.039  1.00 42.48           C  
ANISOU 1817  CD1 TYR A1001     4923   5224   5990    726   1368     94       C  
ATOM   1818  CD2 TYR A1001      14.431  34.658   9.070  1.00 40.22           C  
ANISOU 1818  CD2 TYR A1001     4844   4969   5469    788   1302     53       C  
ATOM   1819  CE1 TYR A1001      17.150  35.120   8.959  1.00 43.79           C  
ANISOU 1819  CE1 TYR A1001     4913   5291   6432    783   1489    102       C  
ATOM   1820  CE2 TYR A1001      15.307  33.594   8.986  1.00 41.61           C  
ANISOU 1820  CE2 TYR A1001     4862   5028   5919    841   1431     56       C  
ATOM   1821  CZ  TYR A1001      16.662  33.826   8.936  1.00 43.51           C  
ANISOU 1821  CZ  TYR A1001     4907   5205   6418    848   1524     85       C  
ATOM   1822  OH  TYR A1001      17.517  32.756   8.878  1.00 45.52           O  
ANISOU 1822  OH  TYR A1001     4972   5321   7000    919   1659     98       O  
ATOM   1823  N   LEU A1002      13.176  39.974  10.042  1.00 38.96           N  
ANISOU 1823  N   LEU A1002     4911   4976   4914    610    938     87       N  
ATOM   1824  CA  LEU A1002      12.350  41.135   9.762  1.00 38.52           C  
ANISOU 1824  CA  LEU A1002     4979   4901   4755    591    922     96       C  
ATOM   1825  C   LEU A1002      12.771  41.631   8.406  1.00 39.51           C  
ANISOU 1825  C   LEU A1002     5173   4957   4882    555   1108    157       C  
ATOM   1826  O   LEU A1002      13.943  41.870   8.186  1.00 40.54           O  
ANISOU 1826  O   LEU A1002     5199   5020   5181    508   1225    165       O  
ATOM   1827  CB  LEU A1002      12.591  42.223  10.809  1.00 39.69           C  
ANISOU 1827  CB  LEU A1002     5049   5023   5007    547    817     43       C  
ATOM   1828  CG  LEU A1002      11.789  43.523  10.702  1.00 40.30           C  
ANISOU 1828  CG  LEU A1002     5220   5027   5065    537    813     42       C  
ATOM   1829  CD1 LEU A1002      10.298  43.254  10.662  1.00 39.52           C  
ANISOU 1829  CD1 LEU A1002     5237   4985   4791    607    753     62       C  
ATOM   1830  CD2 LEU A1002      12.095  44.442  11.874  1.00 41.50           C  
ANISOU 1830  CD2 LEU A1002     5286   5145   5336    479    722    -76       C  
ATOM   1831  N   LEU A1003      11.826  41.751   7.489  1.00 39.50           N  
ANISOU 1831  N   LEU A1003     5336   4981   4688    571   1134    212       N  
ATOM   1832  CA  LEU A1003      12.119  42.180   6.137  1.00 41.64           C  
ANISOU 1832  CA  LEU A1003     5713   5226   4880    534   1306    301       C  
ATOM   1833  C   LEU A1003      11.604  43.584   5.917  1.00 42.95           C  
ANISOU 1833  C   LEU A1003     5948   5323   5045    528   1277    420       C  
ATOM   1834  O   LEU A1003      10.500  43.907   6.315  1.00 43.15           O  
ANISOU 1834  O   LEU A1003     6010   5364   5020    575   1126    433       O  
ATOM   1835  CB  LEU A1003      11.430  41.270   5.130  1.00 42.04           C  
ANISOU 1835  CB  LEU A1003     5916   5382   4674    546   1338    292       C  
ATOM   1836  CG  LEU A1003      12.165  40.003   4.739  1.00 42.64           C  
ANISOU 1836  CG  LEU A1003     5964   5473   4763    533   1491    186       C  
ATOM   1837  CD1 LEU A1003      12.248  39.026   5.905  1.00 41.07           C  
ANISOU 1837  CD1 LEU A1003     5615   5261   4728    581   1387     96       C  
ATOM   1838  CD2 LEU A1003      11.447  39.388   3.547  1.00 43.71           C  
ANISOU 1838  CD2 LEU A1003     6288   5712   4604    511   1536    151       C  
ATOM   1839  N   LYS A1004      12.396  44.406   5.248  1.00 44.98           N  
ANISOU 1839  N   LYS A1004     6212   5488   5388    473   1444    521       N  
ATOM   1840  CA  LYS A1004      11.958  45.722   4.830  1.00 45.52           C  
ANISOU 1840  CA  LYS A1004     6356   5459   5479    471   1453    684       C  
ATOM   1841  C   LYS A1004      11.683  45.625   3.339  1.00 46.89           C  
ANISOU 1841  C   LYS A1004     6720   5721   5374    464   1559    850       C  
ATOM   1842  O   LYS A1004      12.571  45.280   2.558  1.00 47.65           O  
ANISOU 1842  O   LYS A1004     6852   5844   5408    407   1769    866       O  
ATOM   1843  CB  LYS A1004      13.050  46.720   5.142  1.00 47.40           C  
ANISOU 1843  CB  LYS A1004     6466   5518   6025    397   1575    696       C  
ATOM   1844  CG  LYS A1004      12.776  48.151   4.732  1.00 50.28           C  
ANISOU 1844  CG  LYS A1004     6883   5715   6502    387   1629    880       C  
ATOM   1845  CD  LYS A1004      13.996  48.943   5.131  1.00 52.55           C  
ANISOU 1845  CD  LYS A1004     7008   5815   7141    287   1761    836       C  
ATOM   1846  CE  LYS A1004      13.933  50.394   4.744  1.00 55.69           C  
ANISOU 1846  CE  LYS A1004     7432   5986   7741    259   1864   1020       C  
ATOM   1847  NZ  LYS A1004      15.105  51.099   5.346  1.00 57.76           N  
ANISOU 1847  NZ  LYS A1004     7496   6052   8395    140   1963    909       N  
ATOM   1848  N   LEU A1005      10.443  45.903   2.957  1.00 47.76           N  
ANISOU 1848  N   LEU A1005     6946   5890   5309    521   1410    970       N  
ATOM   1849  CA  LEU A1005       9.955  45.624   1.609  1.00 50.37           C  
ANISOU 1849  CA  LEU A1005     7472   6376   5290    513   1426   1109       C  
ATOM   1850  C   LEU A1005       9.462  46.866   0.876  1.00 52.38           C  
ANISOU 1850  C   LEU A1005     7824   6575   5501    536   1405   1412       C  
ATOM   1851  O   LEU A1005       8.718  47.664   1.427  1.00 51.19           O  
ANISOU 1851  O   LEU A1005     7604   6309   5534    606   1262   1492       O  
ATOM   1852  CB  LEU A1005       8.807  44.624   1.684  1.00 49.92           C  
ANISOU 1852  CB  LEU A1005     7451   6484   5029    556   1214    996       C  
ATOM   1853  CG  LEU A1005       9.214  43.232   2.161  1.00 49.76           C  
ANISOU 1853  CG  LEU A1005     7368   6523   5016    534   1251    739       C  
ATOM   1854  CD1 LEU A1005       8.222  42.712   3.191  1.00 49.24           C  
ANISOU 1854  CD1 LEU A1005     7206   6476   5024    594   1037    621       C  
ATOM   1855  CD2 LEU A1005       9.348  42.259   1.008  1.00 51.17           C  
ANISOU 1855  CD2 LEU A1005     7696   6854   4889    475   1356    670       C  
ATOM   1856  N   LYS A1006       9.880  47.001  -0.377  1.00 55.57           N  
ANISOU 1856  N   LYS A1006     8390   7058   5663    480   1566   1588       N  
ATOM   1857  CA  LYS A1006       9.351  48.011  -1.272  1.00 58.53           C  
ANISOU 1857  CA  LYS A1006     8895   7430   5912    504   1531   1935       C  
ATOM   1858  C   LYS A1006       8.088  47.466  -1.917  1.00 59.37           C  
ANISOU 1858  C   LYS A1006     9130   7781   5646    542   1275   1991       C  
ATOM   1859  O   LYS A1006       8.086  46.366  -2.465  1.00 59.63           O  
ANISOU 1859  O   LYS A1006     9273   8030   5350    484   1281   1833       O  
ATOM   1860  CB  LYS A1006      10.375  48.345  -2.357  1.00 62.01           C  
ANISOU 1860  CB  LYS A1006     9474   7883   6204    412   1832   2118       C  
ATOM   1861  CG  LYS A1006       9.923  49.386  -3.377  1.00 66.35           C  
ANISOU 1861  CG  LYS A1006    10182   8442   6585    431   1818   2544       C  
ATOM   1862  CD  LYS A1006       9.505  50.685  -2.705  1.00 66.59           C  
ANISOU 1862  CD  LYS A1006    10070   8184   7047    517   1722   2734       C  
ATOM   1863  CE  LYS A1006       9.613  51.883  -3.639  1.00 71.16           C  
ANISOU 1863  CE  LYS A1006    10763   8657   7616    516   1843   3192       C  
ATOM   1864  NZ  LYS A1006       8.527  51.929  -4.652  1.00 74.05           N  
ANISOU 1864  NZ  LYS A1006    11310   9252   7570    576   1614   3506       N  
ATOM   1865  N   PHE A1007       7.017  48.243  -1.839  1.00 59.93           N  
ANISOU 1865  N   PHE A1007     9166   7800   5804    637   1051   2204       N  
ATOM   1866  CA  PHE A1007       5.777  47.932  -2.527  1.00 60.76           C  
ANISOU 1866  CA  PHE A1007     9360   8130   5594    675    772   2321       C  
ATOM   1867  C   PHE A1007       5.779  48.771  -3.801  1.00 65.78           C  
ANISOU 1867  C   PHE A1007    10177   8837   5977    665    795   2736       C  
ATOM   1868  O   PHE A1007       5.919  49.993  -3.740  1.00 66.71           O  
ANISOU 1868  O   PHE A1007    10249   8729   6368    721    864   3019       O  
ATOM   1869  CB  PHE A1007       4.562  48.307  -1.664  1.00 58.43           C  
ANISOU 1869  CB  PHE A1007     8879   7727   5594    800    513   2334       C  
ATOM   1870  CG  PHE A1007       4.339  47.417  -0.466  1.00 54.22           C  
ANISOU 1870  CG  PHE A1007     8192   7175   5234    809    464   1965       C  
ATOM   1871  CD1 PHE A1007       5.330  47.231   0.498  1.00 51.85           C  
ANISOU 1871  CD1 PHE A1007     7803   6729   5166    772    661   1728       C  
ATOM   1872  CD2 PHE A1007       3.111  46.802  -0.265  1.00 53.29           C  
ANISOU 1872  CD2 PHE A1007     8000   7181   5066    854    210   1880       C  
ATOM   1873  CE1 PHE A1007       5.109  46.427   1.616  1.00 48.07           C  
ANISOU 1873  CE1 PHE A1007     7196   6248   4817    784    607   1439       C  
ATOM   1874  CE2 PHE A1007       2.883  46.006   0.854  1.00 49.99           C  
ANISOU 1874  CE2 PHE A1007     7446   6737   4811    860    190   1580       C  
ATOM   1875  CZ  PHE A1007       3.884  45.817   1.793  1.00 47.41           C  
ANISOU 1875  CZ  PHE A1007     7062   6281   4671    828    388   1373       C  
ATOM   1876  N   ASN A1008       5.625  48.123  -4.950  1.00 69.50           N  
ANISOU 1876  N   ASN A1008    10861   9617   5926    588    743   2776       N  
ATOM   1877  CA  ASN A1008       5.548  48.832  -6.227  1.00 75.48           C  
ANISOU 1877  CA  ASN A1008    11826  10510   6342    570    733   3198       C  
ATOM   1878  C   ASN A1008       4.142  48.726  -6.807  1.00 79.36           C  
ANISOU 1878  C   ASN A1008    12356  11247   6547    621    317   3371       C  
ATOM   1879  O   ASN A1008       3.736  47.670  -7.285  1.00 80.23           O  
ANISOU 1879  O   ASN A1008    12569  11655   6260    540    170   3158       O  
ATOM   1880  CB  ASN A1008       6.597  48.286  -7.191  1.00 77.30           C  
ANISOU 1880  CB  ASN A1008    12297  10929   6142    421   1037   3128       C  
ATOM   1881  CG  ASN A1008       8.013  48.528  -6.695  1.00 75.76           C  
ANISOU 1881  CG  ASN A1008    12024  10476   6283    376   1448   3018       C  
ATOM   1882  OD1 ASN A1008       8.451  49.668  -6.579  1.00 77.09           O  
ANISOU 1882  OD1 ASN A1008    12137  10402   6751    407   1592   3294       O  
ATOM   1883  ND2 ASN A1008       8.731  47.455  -6.388  1.00 73.90           N  
ANISOU 1883  ND2 ASN A1008    11759  10274   6043    301   1631   2617       N  
ATOM   1884  N   PHE A1009       3.401  49.829  -6.744  1.00 82.61           N  
ANISOU 1884  N   PHE A1009    12663  11517   7206    753    126   3751       N  
ATOM   1885  CA  PHE A1009       1.972  49.836  -7.050  1.00 85.59           C  
ANISOU 1885  CA  PHE A1009    12977  12067   7474    835   -307   3928       C  
ATOM   1886  C   PHE A1009       1.734  50.048  -8.543  1.00 92.74           C  
ANISOU 1886  C   PHE A1009    14137  13297   7800    785   -463   4321       C  
ATOM   1887  O   PHE A1009       2.662  49.957  -9.346  1.00 95.51           O  
ANISOU 1887  O   PHE A1009    14744  13783   7761    664   -207   4375       O  
ATOM   1888  CB  PHE A1009       1.282  50.961  -6.263  1.00 85.61           C  
ANISOU 1888  CB  PHE A1009    12718  11734   8073   1021   -423   4166       C  
ATOM   1889  CG  PHE A1009       1.215  50.735  -4.777  1.00 81.28           C  
ANISOU 1889  CG  PHE A1009    11920  10927   8032   1073   -346   3779       C  
ATOM   1890  CD1 PHE A1009       0.114  50.108  -4.208  1.00 79.46           C  
ANISOU 1890  CD1 PHE A1009    11509  10771   7909   1126   -610   3570       C  
ATOM   1891  CD2 PHE A1009       2.229  51.193  -3.941  1.00 79.25           C  
ANISOU 1891  CD2 PHE A1009    11603  10360   8148   1063    -15   3638       C  
ATOM   1892  CE1 PHE A1009       0.036  49.915  -2.841  1.00 75.87           C  
ANISOU 1892  CE1 PHE A1009    10848  10101   7877   1169   -520   3240       C  
ATOM   1893  CE2 PHE A1009       2.156  51.004  -2.571  1.00 75.81           C  
ANISOU 1893  CE2 PHE A1009    10960   9726   8118   1102     35   3293       C  
ATOM   1894  CZ  PHE A1009       1.060  50.360  -2.019  1.00 74.27           C  
ANISOU 1894  CZ  PHE A1009    10616   9621   7982   1157   -204   3101       C  
ATOM   1895  N   LYS A1010       0.480  50.323  -8.905  1.00 97.12           N  
ANISOU 1895  N   LYS A1010    14613  13989   8296    876   -884   4600       N  
ATOM   1896  CA  LYS A1010       0.121  50.799 -10.236  1.00103.55           C  
ANISOU 1896  CA  LYS A1010    15631  15087   8626    866  -1101   5093       C  
ATOM   1897  C   LYS A1010      -0.326  52.253 -10.100  1.00106.40           C  
ANISOU 1897  C   LYS A1010    15826  15147   9452   1063  -1195   5645       C  
ATOM   1898  O   LYS A1010      -0.905  52.831 -11.024  1.00112.85           O  
ANISOU 1898  O   LYS A1010    16721  16138  10019   1117  -1466   6155       O  
ATOM   1899  CB  LYS A1010      -1.009  49.962 -10.851  1.00106.28           C  
ANISOU 1899  CB  LYS A1010    15995  15854   8529    810  -1571   5013       C  
ATOM   1900  CG  LYS A1010      -1.143  48.544 -10.317  1.00102.69           C  
ANISOU 1900  CG  LYS A1010    15478  15511   8026    697  -1588   4377       C  
ATOM   1901  CD  LYS A1010       0.060  47.676 -10.639  1.00101.67           C  
ANISOU 1901  CD  LYS A1010    15615  15502   7511    509  -1206   4003       C  
ATOM   1902  CE  LYS A1010       0.111  46.481  -9.701  1.00 97.22           C  
ANISOU 1902  CE  LYS A1010    14907  14853   7178    453  -1118   3405       C  
ATOM   1903  NZ  LYS A1010       0.715  45.293 -10.358  1.00 98.19           N  
ANISOU 1903  NZ  LYS A1010    15280  15240   6786    251   -952   3014       N  
TER    1904      LYS A1010                                                      
HETATM 1905  OH2 1PE A1101      -4.720  49.941  16.657  1.00 71.02           O  
ANISOU 1905  OH2 1PE A1101     8577   8076  10330   1470   1392   -631       O  
HETATM 1906  C12 1PE A1101      -3.460  50.399  16.184  1.00 68.56           C  
ANISOU 1906  C12 1PE A1101     8393   7710   9946   1403   1300   -598       C  
HETATM 1907  C22 1PE A1101      -2.910  49.511  15.123  1.00 66.33           C  
ANISOU 1907  C22 1PE A1101     8178   7594   9430   1367   1068   -356       C  
HETATM 1908  OH3 1PE A1101      -3.977  48.976  14.353  1.00 68.14           O  
ANISOU 1908  OH3 1PE A1101     8285   7875   9727   1453    950   -145       O  
HETATM 1909  C13 1PE A1101      -4.990  47.181  13.165  1.00 71.46           C  
ANISOU 1909  C13 1PE A1101     8616   8574   9960   1462    669    122       C  
HETATM 1910  C23 1PE A1101      -3.727  47.686  13.797  1.00 68.17           C  
ANISOU 1910  C23 1PE A1101     8354   8109   9438   1390    785    -34       C  
HETATM 1911  OH4 1PE A1101      -4.872  47.114  11.745  1.00 72.66           O  
ANISOU 1911  OH4 1PE A1101     8792   8764  10052   1474    450    361       O  
HETATM 1912  C14 1PE A1101      -5.923  45.081  11.018  1.00 75.91           C  
ANISOU 1912  C14 1PE A1101     9110   9469  10260   1408    213    438       C  
HETATM 1913  C24 1PE A1101      -4.634  45.798  11.259  1.00 73.36           C  
ANISOU 1913  C24 1PE A1101     8955   9063   9854   1384    321    386       C  
HETATM 1914  OH5 1PE A1101      -6.262  45.135   9.635  1.00 80.16           O  
ANISOU 1914  OH5 1PE A1101     9623  10061  10772   1430    -27    650       O  
HETATM 1915  C15 1PE A1101      -7.967  45.007   7.935  1.00 84.70           C  
ANISOU 1915  C15 1PE A1101     9957  10757  11469   1493   -451    953       C  
HETATM 1916  C25 1PE A1101      -7.569  44.643   9.335  1.00 82.46           C  
ANISOU 1916  C25 1PE A1101     9711  10418  11200   1455   -171    707       C  
HETATM 1917  OH6 1PE A1101      -7.017  44.501   6.998  1.00 84.83           O  
ANISOU 1917  OH6 1PE A1101    10202  10920  11109   1389   -558    987       O  
HETATM 1918  C16 1PE A1101      -6.326  44.243   4.711  1.00 82.76           C  
ANISOU 1918  C16 1PE A1101    10203  10918  10323   1284   -881   1221       C  
HETATM 1919  C26 1PE A1101      -7.481  44.473   5.648  1.00 85.30           C  
ANISOU 1919  C26 1PE A1101    10249  11118  11040   1381   -850   1185       C  
HETATM 1920  OH7 1PE A1101      -6.055  42.862   4.534  1.00 78.93           O  
ANISOU 1920  OH7 1PE A1101     9811  10593   9584   1141   -895   1022       O  
HETATM 1921  CAJ 09L A1102      -1.039  43.569  21.423  1.00 48.36           C  
ANISOU 1921  CAJ 09L A1102     6423   6689   5261    848   1245   -863       C  
HETATM 1922  CAK 09L A1102      -2.154  42.608  21.257  1.00 48.31           C  
ANISOU 1922  CAK 09L A1102     6331   6704   5319    898   1316   -712       C  
HETATM 1923  CAI 09L A1102      -1.449  43.140  20.036  1.00 46.60           C  
ANISOU 1923  CAI 09L A1102     6094   6351   5258    922   1144   -664       C  
HETATM 1924  CAL 09L A1102      -0.529  42.182  19.312  1.00 44.31           C  
ANISOU 1924  CAL 09L A1102     5833   6120   4883    895    962   -493       C  
HETATM 1925  OAB 09L A1102       0.568  41.902  19.760  1.00 44.98           O  
ANISOU 1925  OAB 09L A1102     5993   6307   4790    834    886   -496       O  
HETATM 1926  NAE 09L A1102      -0.966  41.654  18.155  1.00 42.05           N  
ANISOU 1926  NAE 09L A1102     5476   5768   4733    938    887   -350       N  
HETATM 1927  CAM 09L A1102      -2.223  41.910  17.441  1.00 40.90           C  
ANISOU 1927  CAM 09L A1102     5212   5517   4811   1007    909   -309       C  
HETATM 1928  CAO 09L A1102      -3.012  40.627  17.290  1.00 40.08           C  
ANISOU 1928  CAO 09L A1102     5035   5471   4723    999    906   -205       C  
HETATM 1929  CAN 09L A1102      -0.158  40.639  17.475  1.00 40.17           C  
ANISOU 1929  CAN 09L A1102     5266   5572   4424    909    761   -222       C  
HETATM 1930  CAP 09L A1102      -0.938  39.360  17.383  1.00 39.41           C  
ANISOU 1930  CAP 09L A1102     5113   5512   4346    909    779   -120       C  
HETATM 1931  NAF 09L A1102      -2.187  39.594  16.656  1.00 38.67           N  
ANISOU 1931  NAF 09L A1102     4912   5336   4441    954    782   -108       N  
HETATM 1932  CAQ 09L A1102      -2.422  38.900  15.527  1.00 37.80           C  
ANISOU 1932  CAQ 09L A1102     4761   5203   4398    946    675    -31       C  
HETATM 1933  OAC 09L A1102      -1.649  38.060  15.108  1.00 37.21           O  
ANISOU 1933  OAC 09L A1102     4742   5150   4246    905    616     11       O  
HETATM 1934  CAR 09L A1102      -3.660  39.189  14.739  1.00 37.58           C  
ANISOU 1934  CAR 09L A1102     4606   5119   4553    984    621     -7       C  
HETATM 1935  CAS 09L A1102      -3.486  39.576  13.412  1.00 36.49           C  
ANISOU 1935  CAS 09L A1102     4485   4951   4428    996    468     42       C  
HETATM 1936  CAU 09L A1102      -4.957  38.986  15.174  1.00 39.23           C  
ANISOU 1936  CAU 09L A1102     4670   5317   4918   1000    700    -13       C  
HETATM 1937  FAA 09L A1102      -5.172  38.693  16.473  1.00 39.32           F  
ANISOU 1937  FAA 09L A1102     4679   5368   4891    985    883    -49       F  
HETATM 1938  CAX 09L A1102      -6.042  39.094  14.346  1.00 40.25           C  
ANISOU 1938  CAX 09L A1102     4645   5407   5239   1027    601     26       C  
HETATM 1939  CAW 09L A1102      -5.837  39.456  13.027  1.00 39.80           C  
ANISOU 1939  CAW 09L A1102     4612   5342   5166   1038    405     85       C  
HETATM 1940  CAT 09L A1102      -4.564  39.722  12.548  1.00 37.75           C  
ANISOU 1940  CAT 09L A1102     4524   5093   4725   1023    353     96       C  
HETATM 1941  CAV 09L A1102      -4.358  40.236  11.140  1.00 37.88           C  
ANISOU 1941  CAV 09L A1102     4585   5111   4694   1035    178    183       C  
HETATM 1942  CAY 09L A1102      -3.126  39.684  10.459  1.00 36.91           C  
ANISOU 1942  CAY 09L A1102     4628   5039   4355    966    145    176       C  
HETATM 1943  CAZ 09L A1102      -3.130  38.360   9.810  1.00 37.44           C  
ANISOU 1943  CAZ 09L A1102     4719   5175   4331    879     81    133       C  
HETATM 1944  CBB 09L A1102      -4.256  37.541   9.782  1.00 38.76           C  
ANISOU 1944  CBB 09L A1102     4754   5364   4607    840     25     99       C  
HETATM 1945  CBE 09L A1102      -4.209  36.322   9.127  1.00 39.39           C  
ANISOU 1945  CBE 09L A1102     4862   5481   4623    741    -25     22       C  
HETATM 1946  CBF 09L A1102      -3.055  35.912   8.494  1.00 38.82           C  
ANISOU 1946  CBF 09L A1102     4949   5424   4376    694     -1    -23       C  
HETATM 1947  CBD 09L A1102      -1.924  36.708   8.522  1.00 37.66           C  
ANISOU 1947  CBD 09L A1102     4921   5263   4123    740     65     27       C  
HETATM 1948  CBA 09L A1102      -1.950  37.931   9.189  1.00 36.95           C  
ANISOU 1948  CBA 09L A1102     4802   5136   4101    826     97    106       C  
HETATM 1949  CBC 09L A1102      -0.764  38.786   9.239  1.00 36.17           C  
ANISOU 1949  CBC 09L A1102     4807   5002   3934    854    167    142       C  
HETATM 1950  OAD 09L A1102       0.336  38.439   8.824  1.00 37.06           O  
ANISOU 1950  OAD 09L A1102     5018   5120   3941    814    218    119       O  
HETATM 1951  NAH 09L A1102      -0.924  39.965   9.855  1.00 35.86           N  
ANISOU 1951  NAH 09L A1102     4728   4902   3995    923    198    184       N  
HETATM 1952  NAG 09L A1102      -2.084  40.441  10.470  1.00 36.84           N  
ANISOU 1952  NAG 09L A1102     4725   4991   4281    981    195    191       N  
HETATM 1953  S   SO4 A1103      -7.949  35.602   2.606  1.00 73.90           S  
HETATM 1954  O1  SO4 A1103      -7.243  36.558   1.716  1.00 71.50           O  
HETATM 1955  O2  SO4 A1103      -9.059  35.002   1.851  1.00 71.79           O  
HETATM 1956  O3  SO4 A1103      -7.058  34.503   3.063  1.00 74.50           O  
HETATM 1957  O4  SO4 A1103      -8.480  36.331   3.784  1.00 73.89           O  
HETATM 1958  S   SO4 A1104       0.327  20.765   5.271  1.00104.82           S  
HETATM 1959  O1  SO4 A1104       1.684  20.424   4.770  1.00103.42           O  
HETATM 1960  O2  SO4 A1104      -0.674  20.351   4.259  1.00104.36           O  
HETATM 1961  O3  SO4 A1104       0.057  20.066   6.551  1.00101.67           O  
HETATM 1962  O4  SO4 A1104       0.238  22.230   5.485  1.00102.76           O  
HETATM 1963  O   HOH A1201      16.648  49.602   6.571  1.00 43.97           O  
HETATM 1964  O   HOH A1202      -6.734  33.696  23.526  1.00 43.40           O  
HETATM 1965  O   HOH A1203     -10.382  28.745  17.036  1.00 51.03           O  
HETATM 1966  O   HOH A1204       6.858  37.074  19.290  1.00 34.10           O  
HETATM 1967  O   HOH A1205       2.915  50.443   8.092  1.00 43.94           O  
HETATM 1968  O   HOH A1206      -0.954  32.071   3.880  1.00 36.70           O  
HETATM 1969  O   HOH A1207      -1.976  30.000   1.429  1.00 56.53           O  
HETATM 1970  O   HOH A1208       6.895  51.273  15.792  1.00 44.03           O  
HETATM 1971  O   HOH A1209      12.595  42.091  23.033  1.00 48.68           O  
HETATM 1972  O   HOH A1210      13.389  36.527  18.664  1.00 43.91           O  
HETATM 1973  O   HOH A1211       8.990  32.167  22.669  1.00 43.41           O  
HETATM 1974  O   HOH A1212       1.184  42.014  27.788  1.00 59.09           O  
HETATM 1975  O   HOH A1213       2.814  53.739   4.500  1.00 46.57           O  
HETATM 1976  O   HOH A1214      16.918  51.581   3.268  1.00 53.63           O  
HETATM 1977  O   HOH A1215       4.717  47.866   7.834  1.00 32.30           O  
HETATM 1978  O   HOH A1216       5.349  38.228  23.175  1.00 39.02           O  
HETATM 1979  O   HOH A1217      20.297  39.076  15.475  1.00 46.48           O  
HETATM 1980  O   HOH A1218       5.012  50.278  18.635  1.00 44.90           O  
HETATM 1981  O   HOH A1219      -4.853  38.398  19.589  1.00 52.10           O  
HETATM 1982  O   HOH A1220      19.846  42.546   3.793  1.00 37.90           O  
HETATM 1983  O   HOH A1221      25.807  31.759   2.336  1.00 46.49           O  
HETATM 1984  O   HOH A1222       5.059  35.676  20.535  1.00 50.12           O  
HETATM 1985  O   HOH A1223      12.634  23.935  -3.786  1.00 57.99           O  
HETATM 1986  O   HOH A1224      -4.923  42.409  19.037  1.00 51.59           O  
HETATM 1987  O   HOH A1225       0.568  32.905  26.218  1.00 39.32           O  
HETATM 1988  O   HOH A1226     -15.028  24.296   9.615  1.00 45.65           O  
HETATM 1989  O   HOH A1227       2.460  52.543   9.891  1.00 37.15           O  
CONECT 1905 1906                                                                
CONECT 1906 1905 1907                                                           
CONECT 1907 1906 1908                                                           
CONECT 1908 1907 1910                                                           
CONECT 1909 1910 1911                                                           
CONECT 1910 1908 1909                                                           
CONECT 1911 1909 1913                                                           
CONECT 1912 1913 1914                                                           
CONECT 1913 1911 1912                                                           
CONECT 1914 1912 1916                                                           
CONECT 1915 1916 1917                                                           
CONECT 1916 1914 1915                                                           
CONECT 1917 1915 1919                                                           
CONECT 1918 1919 1920                                                           
CONECT 1919 1917 1918                                                           
CONECT 1920 1918                                                                
CONECT 1921 1922 1923                                                           
CONECT 1922 1921 1923                                                           
CONECT 1923 1921 1922 1924                                                      
CONECT 1924 1923 1925 1926                                                      
CONECT 1925 1924                                                                
CONECT 1926 1924 1927 1929                                                      
CONECT 1927 1926 1928                                                           
CONECT 1928 1927 1931                                                           
CONECT 1929 1926 1930                                                           
CONECT 1930 1929 1931                                                           
CONECT 1931 1928 1930 1932                                                      
CONECT 1932 1931 1933 1934                                                      
CONECT 1933 1932                                                                
CONECT 1934 1932 1935 1936                                                      
CONECT 1935 1934 1940                                                           
CONECT 1936 1934 1937 1938                                                      
CONECT 1937 1936                                                                
CONECT 1938 1936 1939                                                           
CONECT 1939 1938 1940                                                           
CONECT 1940 1935 1939 1941                                                      
CONECT 1941 1940 1942                                                           
CONECT 1942 1941 1943 1952                                                      
CONECT 1943 1942 1944 1948                                                      
CONECT 1944 1943 1945                                                           
CONECT 1945 1944 1946                                                           
CONECT 1946 1945 1947                                                           
CONECT 1947 1946 1948                                                           
CONECT 1948 1943 1947 1949                                                      
CONECT 1949 1948 1950 1951                                                      
CONECT 1950 1949                                                                
CONECT 1951 1949 1952                                                           
CONECT 1952 1942 1951                                                           
CONECT 1953 1954 1955 1956 1957                                                 
CONECT 1954 1953                                                                
CONECT 1955 1953                                                                
CONECT 1956 1953                                                                
CONECT 1957 1953                                                                
CONECT 1958 1959 1960 1961 1962                                                 
CONECT 1959 1958                                                                
CONECT 1960 1958                                                                
CONECT 1961 1958                                                                
CONECT 1962 1958                                                                
MASTER      380    0    4   11   14    0    6    6 1972    1   58   21          
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.