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***  HYDROLASE 20-MAR-08 3CM3  ***

elNémo ID: 191008170021129713

Job options:

ID        	=	 191008170021129713
JOBID     	=	 HYDROLASE 20-MAR-08 3CM3
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    HYDROLASE                               20-MAR-08   3CM3              
TITLE     HIGH RESOLUTION CRYSTAL STRUCTURE OF THE VACCINIA VIRUS               
TITLE    2 DUAL-SPECIFICITY PHOSPHATASE VH1                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DUAL SPECIFICITY PROTEIN PHOSPHATASE;                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: LATE PROTEIN H1;                                            
COMPND   5 EC: 3.1.3.48, 3.1.3.-;                                               
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: VACCINIA VIRUS;                                 
SOURCE   3 STRAIN: WESTERN RESERVE / WR;                                        
SOURCE   4 GENE: H1 ORF;                                                        
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET14B                                    
KEYWDS    DUAL-SPECIFICITY PHOSPHATASE, VACCINIA VIRUS, VH1,                    
KEYWDS   2 HYDROLASE, LATE PROTEIN, PROTEIN PHOSPHATASE                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.C.KOKSAL,G.CINGOLANI                                                
REVDAT   2   28-APR-09 3CM3    1       JRNL                                     
REVDAT   1   10-FEB-09 3CM3    0                                                
JRNL        AUTH   A.C.KOKSAL,J.D.NARDOZZI,G.CINGOLANI                          
JRNL        TITL   DIMERIC QUATERNARY STRUCTURE OF THE PROTOTYPICAL             
JRNL        TITL 2 DUAL SPECIFICITY PHOSPHATASE VH1.                            
JRNL        REF    J.BIOL.CHEM.                  V. 284 10129 2009              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   19211553                                                     
JRNL        DOI    10.1074/JBC.M808362200                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.32 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ENGH & HUBER                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.32                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 14.11                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 33998                          
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) : 0.172                           
REMARK   3   R VALUE            (WORKING SET) : 0.171                           
REMARK   3   FREE R VALUE                     : 0.185                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1800                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.32                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1248                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 46.10                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3620                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 65                           
REMARK   3   BIN FREE R VALUE                    : 0.3840                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1366                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 13                                      
REMARK   3   SOLVENT ATOMS            : 300                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.33                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.35                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.071         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.057         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.971                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.963                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1411 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1916 ; 1.186 ; 1.976       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   176 ; 5.494 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    61 ;36.513 ;23.934       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   254 ;15.109 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     7 ;17.492 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   216 ; 0.076 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1049 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   724 ; 0.257 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):   978 ; 0.320 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   215 ; 0.242 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    62 ; 0.207 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    40 ; 0.229 ; 0.200       
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):   853 ; 2.158 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1398 ; 3.819 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   558 ; 3.739 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   515 ; 6.064 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3CM3 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-APR-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB046940.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-OCT-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : F1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.918                              
REMARK 200  MONOCHROMATOR                  : SI 111                             
REMARK 200  OPTICS                         : HORIZONTAL BENT SI(111),           
REMARK 200                                   ASYMMETRICALLY CUT WITH WATER      
REMARK 200                                   COOLED CU BLOCK. RH-COATED SI      
REMARK 200                                   MIRROR FOR VERTICAL FOCUSING.      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC Q-270                         
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35905                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.320                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.9                               
REMARK 200  DATA REDUNDANCY                : 15.700                             
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05700                            
REMARK 200   FOR THE DATA SET  : 65.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.32                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.37                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 51.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.40                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.35700                            
REMARK 200   FOR SHELL         : 2.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2RF6                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.18                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 62% PEG 400, 0.1M TRIS PH 8 ,            
REMARK 280  BATCH, TEMPERATURE 297K                                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       67.49350            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       67.49350            
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        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       31.90800            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       19.34500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       31.90800            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       19.34500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       67.49350            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       31.90800            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       19.34500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       67.49350            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       31.90800            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       19.34500            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: ONE COPY OF THE BIOLOGICALLY RELEVANT MONOMER IS PRESENT     
REMARK 300 IN THE ASYMMETRIC UNIT                                               
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3230 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15430 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A1243  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A1325  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A1373  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   998                                                      
REMARK 465     PRO A   999                                                      
REMARK 465     GLU A  1000                                                      
REMARK 465     ILE A  1001                                                      
REMARK 465     ARG A  1002                                                      
REMARK 465     MET A  1003                                                      
REMARK 465     ASP A  1004                                                      
REMARK 465     LYS A  1005                                                      
REMARK 465     LYS A  1006                                                      
REMARK 465     ASP A  1171                                                      
REMARK 465     LYS A  1172                                                      
REMARK 465     ASN A  1173                                                      
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    THR A1027      -53.99   -121.78                                   
REMARK 500    SER A1112     -151.55   -128.88                                   
REMARK 500    VAL A1116      -54.11   -121.11                                   
REMARK 500    ASN A1117      -67.46   -101.60                                   
REMARK 500    VAL A1155       57.66     30.91                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1294        DISTANCE =  5.78 ANGSTROMS                       
REMARK 525    HOH A1404        DISTANCE =  6.50 ANGSTROMS                       
REMARK 525    HOH A1440        DISTANCE =  5.03 ANGSTROMS                       
REMARK 525    HOH A1442        DISTANCE =  5.22 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1                   
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 1174                
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 2                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2RF6   RELATED DB: PDB                                   
REMARK 900 VACCINIA VIRUS DUAL-SPECIFICITY PHOSPHATASE VH1                      
REMARK 900 RELATED ID: 3CEO   RELATED DB: PDB                                   
REMARK 900 VACCINIA VIRUS DUAL-SPECIFICITY PHOSPHATASE VH1 BOUND TO             
REMARK 900 XENON GAS                                                            
DBREF  3CM3 A 1003  1173  UNP    P07239   DUSP_VACCV       1    171             
SEQADV 3CM3 GLY A  998  UNP  P07239              EXPRESSION TAG                 
SEQADV 3CM3 PRO A  999  UNP  P07239              EXPRESSION TAG                 
SEQADV 3CM3 GLU A 1000  UNP  P07239              EXPRESSION TAG                 
SEQADV 3CM3 ILE A 1001  UNP  P07239              EXPRESSION TAG                 
SEQADV 3CM3 ARG A 1002  UNP  P07239              EXPRESSION TAG                 
SEQADV 3CM3 SER A 1112  UNP  P07239    CYS   110 ENGINEERED                     
SEQRES   1 A  176  GLY PRO GLU ILE ARG MET ASP LYS LYS SER LEU TYR LYS          
SEQRES   2 A  176  TYR LEU LEU LEU ARG SER THR GLY ASP MET HIS LYS ALA          
SEQRES   3 A  176  LYS SER PRO THR ILE MET THR ARG VAL THR ASN ASN VAL          
SEQRES   4 A  176  TYR LEU GLY ASN TYR LYS ASN ALA MET ASP ALA PRO SER          
SEQRES   5 A  176  SER GLU VAL LYS PHE LYS TYR VAL LEU ASN LEU THR MET          
SEQRES   6 A  176  ASP LYS TYR THR LEU PRO ASN SER ASN ILE ASN ILE ILE          
SEQRES   7 A  176  HIS ILE PRO LEU VAL ASP ASP THR THR THR ASP ILE SER          
SEQRES   8 A  176  LYS TYR PHE ASP ASP VAL THR ALA PHE LEU SER LYS CYS          
SEQRES   9 A  176  ASP GLN ARG ASN GLU PRO VAL LEU VAL HIS SER ALA ALA          
SEQRES  10 A  176  GLY VAL ASN ARG SER GLY ALA MET ILE LEU ALA TYR LEU          
SEQRES  11 A  176  MET SER LYS ASN LYS GLU SER LEU PRO MET LEU TYR PHE          
SEQRES  12 A  176  LEU TYR VAL TYR HIS SER MET ARG ASP LEU ARG GLY ALA          
SEQRES  13 A  176  PHE VAL GLU ASN PRO SER PHE LYS ARG GLN ILE ILE GLU          
SEQRES  14 A  176  LYS TYR VAL ILE ASP LYS ASN                                  
HET    PO4  A   1       5                                                       
HET    BME  A1174       4                                                       
HET    BME  A   2       4                                                       
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     BME BETA-MERCAPTOETHANOL                                             
FORMUL   2  PO4    O4 P 3-                                                      
FORMUL   3  BME    2(C2 H6 O S)                                                 
FORMUL   5  HOH   *300(H2 O)                                                    
HELIX    1   1 SER A 1007  THR A 1017  1                                  11    
HELIX    2   2 ASN A 1040  ASP A 1046  1                                   7    
HELIX    3   3 ALA A 1047  SER A 1050  5                                   4    
HELIX    4   4 ILE A 1087  LYS A 1089  5                                   3    
HELIX    5   5 TYR A 1090  ASN A 1105  1                                  16    
HELIX    6   6 ASN A 1117  ASN A 1131  1                                  15    
HELIX    7   7 LEU A 1135  GLY A 1152  1                                  18    
HELIX    8   8 ASN A 1157  VAL A 1169  1                                  13    
SHEET    1   A 5 THR A1030  ARG A1031  0                                        
SHEET    2   A 5 VAL A1036  GLY A1039 -1  O  LEU A1038   N  THR A1030           
SHEET    3   A 5 VAL A1108  HIS A1111  1  O  VAL A1110   N  TYR A1037           
SHEET    4   A 5 TYR A1056  ASN A1059  1  N  LEU A1058   O  LEU A1109           
SHEET    5   A 5 ASN A1073  HIS A1076  1  O  ILE A1075   N  VAL A1057           
SITE     1 AC1  8 ASP A1081  SER A1112  ALA A1113  ALA A1114                    
SITE     2 AC1  8 GLY A1115  ASN A1117  ARG A1118  HOH A1199                    
SITE     1 AC2  5 ASN A1117  GLU A1156  ASN A1157  HOH A1251                    
SITE     2 AC2  5 HOH A1391                                                     
SITE     1 AC3  3 ASN A1131  LYS A1132  SER A1134                               
CRYST1   63.816   38.690  134.987  90.00  90.00  90.00 C 2 2 21      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015670  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.025846  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007408        0.00000                         
ATOM      1  N   SER A1007      23.183 -12.243   7.340  1.00 44.49           N  
ANISOU    1  N   SER A1007     8216   3592   5095   1023   1280    164       N  
ATOM      2  CA  SER A1007      21.716 -12.220   7.558  1.00 43.59           C  
ANISOU    2  CA  SER A1007     8036   3596   4931    834   1225     87       C  
ATOM      3  C   SER A1007      21.163 -10.798   7.556  1.00 42.26           C  
ANISOU    3  C   SER A1007     7731   3589   4738    820    900   -142       C  
ATOM      4  O   SER A1007      20.211 -10.492   6.830  1.00 41.39           O  
ANISOU    4  O   SER A1007     7764   3474   4487    658    806   -126       O  
ATOM      5  CB  SER A1007      21.378 -12.924   8.872  1.00 44.08           C  
ANISOU    5  CB  SER A1007     8223   3643   4881    833   1322     81       C  
ATOM      6  OG  SER A1007      21.891 -14.249   8.855  1.00 44.41           O  
ANISOU    6  OG  SER A1007     7896   3876   5102    678   1747    337       O  
ATOM      7  N   LEU A1008      21.763  -9.925   8.369  1.00 42.33           N  
ANISOU    7  N   LEU A1008     7350   3720   5012    759    406   -263       N  
ATOM      8  CA  LEU A1008      21.334  -8.523   8.461  1.00 41.98           C  
ANISOU    8  CA  LEU A1008     6830   3948   5173    513    240   -274       C  
ATOM      9  C   LEU A1008      21.441  -7.823   7.107  1.00 39.42           C  
ANISOU    9  C   LEU A1008     5795   3722   5461     59    181     -5       C  
ATOM     10  O   LEU A1008      20.696  -6.897   6.781  1.00 38.54           O  
ANISOU   10  O   LEU A1008     5314   3657   5673   -135    164    153       O  
ATOM     11  CB  LEU A1008      22.160  -7.770   9.514  1.00 44.48           C  
ANISOU   11  CB  LEU A1008     7426   4363   5113    635    125   -485       C  
ATOM     12  CG  LEU A1008      21.858  -8.020  10.999  1.00 50.00           C  
ANISOU   12  CG  LEU A1008     8524   5324   5149    551      6   -427       C  
ATOM     13  CD1 LEU A1008      22.859  -7.267  11.891  1.00 54.59           C  
ANISOU   13  CD1 LEU A1008     9429   6126   5188    560   -313   -527       C  
ATOM     14  CD2 LEU A1008      20.410  -7.636  11.363  1.00 53.72           C  
ANISOU   14  CD2 LEU A1008     9136   5931   5345    395     93   -153       C  
ATOM     15  N   TYR A1009      22.388  -8.300   6.305  1.00 37.60           N  
ANISOU   15  N   TYR A1009     4841   3722   5722   -395    273    436       N  
ATOM     16  CA  TYR A1009      22.604  -7.778   4.968  1.00 36.44           C  
ANISOU   16  CA  TYR A1009     4217   3923   5705   -489    399    785       C  
ATOM     17  C   TYR A1009      21.475  -8.159   3.995  1.00 34.46           C  
ANISOU   17  C   TYR A1009     3806   3657   5630   -487    679    891       C  
ATOM     18  O   TYR A1009      20.937  -7.287   3.301  1.00 34.03           O  
ANISOU   18  O   TYR A1009     3440   3614   5874   -467    876   1000       O  
ATOM     19  CB  TYR A1009      23.987  -8.247   4.515  1.00 37.35           C  
ANISOU   19  CB  TYR A1009     4318   4250   5625   -478    186    957       C  
ATOM     20  CG  TYR A1009      24.576  -7.492   3.353  1.00 37.20           C  
ANISOU   20  CG  TYR A1009     4244   4611   5278   -421   -137   1150       C  
ATOM     21  CD1 TYR A1009      24.371  -6.124   3.190  1.00 37.62           C  
ANISOU   21  CD1 TYR A1009     4332   4863   5098   -496   -450   1194       C  
ATOM     22  CD2 TYR A1009      25.360  -8.165   2.425  1.00 36.76           C  
ANISOU   22  CD2 TYR A1009     4153   4863   4949   -467   -390   1333       C  
ATOM     23  CE1 TYR A1009      24.921  -5.445   2.108  1.00 37.68           C  
ANISOU   23  CE1 TYR A1009     4419   4971   4924   -744   -702   1314       C  
ATOM     24  CE2 TYR A1009      25.913  -7.500   1.347  1.00 37.22           C  
ANISOU   24  CE2 TYR A1009     4499   5036   4607   -658   -661   1412       C  
ATOM     25  CZ  TYR A1009      25.691  -6.147   1.197  1.00 37.60           C  
ANISOU   25  CZ  TYR A1009     4544   5052   4690   -912   -772   1342       C  
ATOM     26  OH  TYR A1009      26.249  -5.509   0.122  1.00 39.04           O  
ANISOU   26  OH  TYR A1009     4874   5281   4679  -1133   -732   1421       O  
ATOM     27  N   LYS A1010      21.090  -9.440   3.972  1.00 30.45           N  
ANISOU   27  N   LYS A1010     3280   3388   4902   -186   1049    601       N  
ATOM     28  CA  LYS A1010      19.977  -9.930   3.157  1.00 27.79           C  
ANISOU   28  CA  LYS A1010     3384   3183   3991     31    991    153       C  
ATOM     29  C   LYS A1010      18.679  -9.227   3.576  1.00 24.44           C  
ANISOU   29  C   LYS A1010     2779   3140   3366    -93   1054    -27       C  
ATOM     30  O   LYS A1010      17.820  -8.854   2.764  1.00 24.09           O  
ANISOU   30  O   LYS A1010     2867   3145   3143    -49   1093   -173       O  
ATOM     31  CB  LYS A1010      19.820 -11.439   3.344  1.00 28.79           C  
ANISOU   31  CB  LYS A1010     3743   3167   4029    137    829    120       C  
ATOM     32  CG  LYS A1010      19.274 -12.183   2.133  1.00 33.33           C  
ANISOU   32  CG  LYS A1010     4706   3370   4589    285     74   -104       C  
ATOM     33  CD  LYS A1010      18.705 -13.550   2.516  1.00 38.32           C  
ANISOU   33  CD  LYS A1010     5404   3574   5580    357   -723   -285       C  
ATOM     34  CE  LYS A1010      19.780 -14.482   3.067  1.00 40.07           C  
ANISOU   34  CE  LYS A1010     5457   3634   6132    395   -873   -208       C  
ATOM     35  NZ  LYS A1010      19.278 -15.893   3.007  1.00 41.44           N  
ANISOU   35  NZ  LYS A1010     5435   3720   6589    315  -1045   -153       N  
ATOM     36  N   TYR A1011      18.542  -9.040   4.879  1.00 22.01           N  
ANISOU   36  N   TYR A1011     2266   3070   3027   -346    794   -263       N  
ATOM     37  CA  TYR A1011      17.431  -8.298   5.473  1.00 20.62           C  
ANISOU   37  CA  TYR A1011     1912   3201   2723   -496    496   -339       C  
ATOM     38  C   TYR A1011      17.342  -6.888   4.890  1.00 20.56           C  
ANISOU   38  C   TYR A1011     1852   3127   2831   -461    249   -340       C  
ATOM     39  O   TYR A1011      16.295  -6.441   4.426  1.00 21.05           O  
ANISOU   39  O   TYR A1011     1817   3364   2815   -432    217   -419       O  
ATOM     40  CB  TYR A1011      17.612  -8.268   6.997  1.00 21.04           C  
ANISOU   40  CB  TYR A1011     1946   3316   2734   -489    342   -445       C  
ATOM     41  CG  TYR A1011      16.783  -7.222   7.718  1.00 21.17           C  
ANISOU   41  CG  TYR A1011     2008   3431   2606   -540    417   -522       C  
ATOM     42  CD1 TYR A1011      15.425  -7.417   7.966  1.00 22.32           C  
ANISOU   42  CD1 TYR A1011     2313   3424   2741   -766    684   -718       C  
ATOM     43  CD2 TYR A1011      17.361  -6.043   8.183  1.00 22.45           C  
ANISOU   43  CD2 TYR A1011     2213   3592   2725   -529     93   -640       C  
ATOM     44  CE1 TYR A1011      14.674  -6.447   8.644  1.00 23.41           C  
ANISOU   44  CE1 TYR A1011     2655   3289   2949   -775    891   -785       C  
ATOM     45  CE2 TYR A1011      16.626  -5.070   8.849  1.00 23.11           C  
ANISOU   45  CE2 TYR A1011     2426   3388   2967   -715    392   -644       C  
ATOM     46  CZ  TYR A1011      15.276  -5.275   9.082  1.00 23.60           C  
ANISOU   46  CZ  TYR A1011     2572   3228   3167   -744    692   -776       C  
ATOM     47  OH  TYR A1011      14.553  -4.304   9.753  1.00 25.16           O  
ANISOU   47  OH  TYR A1011     3032   3334   3194   -709    869   -662       O  
ATOM     48  N   LEU A1012      18.464  -6.178   4.897  1.00 20.33           N  
ANISOU   48  N   LEU A1012     1800   3034   2890   -599     43    -87       N  
ATOM     49  CA  LEU A1012      18.478  -4.801   4.399  1.00 21.01           C  
ANISOU   49  CA  LEU A1012     1658   3136   3188   -485    -82    107       C  
ATOM     50  C   LEU A1012      18.076  -4.684   2.934  1.00 20.09           C  
ANISOU   50  C   LEU A1012     1641   2908   3084   -438    153     17       C  
ATOM     51  O   LEU A1012      17.345  -3.764   2.549  1.00 19.44           O  
ANISOU   51  O   LEU A1012     1448   3059   2879   -375    -20   -109       O  
ATOM     52  CB  LEU A1012      19.873  -4.173   4.578  1.00 22.64           C  
ANISOU   52  CB  LEU A1012     1886   3160   3555   -597   -284    274       C  
ATOM     53  CG  LEU A1012      20.184  -3.318   5.801  1.00 27.44           C  
ANISOU   53  CG  LEU A1012     2307   4129   3991   -688   -780    368       C  
ATOM     54  CD1 LEU A1012      19.322  -3.659   6.999  1.00 30.89           C  
ANISOU   54  CD1 LEU A1012     3131   4598   4007   -939  -1062    485       C  
ATOM     55  CD2 LEU A1012      21.682  -3.373   6.124  1.00 28.98           C  
ANISOU   55  CD2 LEU A1012     2318   4038   4654   -662  -1368    465       C  
ATOM     56  N   LEU A1013      18.561  -5.620   2.120  1.00 20.25           N  
ANISOU   56  N   LEU A1013     1430   2964   3300   -434    394   -164       N  
ATOM     57  CA  LEU A1013      18.340  -5.547   0.673  1.00 19.43           C  
ANISOU   57  CA  LEU A1013     1221   2836   3327   -434    631   -296       C  
ATOM     58  C   LEU A1013      16.918  -5.903   0.275  1.00 18.78           C  
ANISOU   58  C   LEU A1013     1269   2745   3120   -412    653   -225       C  
ATOM     59  O   LEU A1013      16.395  -5.315  -0.681  1.00 18.98           O  
ANISOU   59  O   LEU A1013     1171   2971   3070   -344    675    -91       O  
ATOM     60  CB  LEU A1013      19.375  -6.396  -0.075  1.00 20.50           C  
ANISOU   60  CB  LEU A1013     1141   2933   3716   -386    666   -388       C  
ATOM     61  CG  LEU A1013      20.809  -5.863   0.013  1.00 22.36           C  
ANISOU   61  CG  LEU A1013     1208   3314   3973   -509    710   -573       C  
ATOM     62  CD1 LEU A1013      21.757  -6.870  -0.607  1.00 25.73           C  
ANISOU   62  CD1 LEU A1013     1194   3819   4765   -421    754   -952       C  
ATOM     63  CD2 LEU A1013      20.918  -4.517  -0.676  1.00 23.69           C  
ANISOU   63  CD2 LEU A1013     1316   3718   3968   -675    570   -463       C  
ATOM     64  N   LEU A1014      16.304  -6.830   1.022  1.00 18.27           N  
ANISOU   64  N   LEU A1014     1307   2933   2702   -630    693   -348       N  
ATOM     65  CA  LEU A1014      14.889  -7.151   0.792  1.00 18.82           C  
ANISOU   65  CA  LEU A1014     1499   2975   2678   -678    631   -505       C  
ATOM     66  C   LEU A1014      14.012  -5.994   1.233  1.00 18.60           C  
ANISOU   66  C   LEU A1014     1488   3088   2493   -631    395   -688       C  
ATOM     67  O   LEU A1014      13.097  -5.589   0.511  1.00 19.82           O  
ANISOU   67  O   LEU A1014     1445   3440   2644   -537    226   -736       O  
ATOM     68  CB  LEU A1014      14.473  -8.446   1.490  1.00 19.45           C  
ANISOU   68  CB  LEU A1014     1703   2973   2716   -724    728   -524       C  
ATOM     69  CG  LEU A1014      15.042  -9.718   0.855  1.00 20.59           C  
ANISOU   69  CG  LEU A1014     1852   3086   2885   -586    715   -496       C  
ATOM     70  CD1 LEU A1014      14.845 -10.925   1.761  1.00 23.30           C  
ANISOU   70  CD1 LEU A1014     2630   3127   3097   -684    702   -450       C  
ATOM     71  CD2 LEU A1014      14.391  -9.961  -0.499  1.00 21.37           C  
ANISOU   71  CD2 LEU A1014     1562   3574   2985   -741    666   -617       C  
ATOM     72  N   ARG A1015      14.295  -5.441   2.414  1.00 18.33           N  
ANISOU   72  N   ARG A1015     1439   3199   2328   -595    405   -746       N  
ATOM     73  CA  ARG A1015      13.552  -4.267   2.876  1.00 19.23           C  
ANISOU   73  CA  ARG A1015     1518   3366   2423   -395    364   -851       C  
ATOM     74  C   ARG A1015      13.692  -3.112   1.887  1.00 19.25           C  
ANISOU   74  C   ARG A1015     1509   3330   2477   -208    219   -878       C  
ATOM     75  O   ARG A1015      12.766  -2.317   1.713  1.00 20.80           O  
ANISOU   75  O   ARG A1015     1365   3637   2901    -93     74   -907       O  
ATOM     76  CB  ARG A1015      14.033  -3.804   4.254  1.00 19.86           C  
ANISOU   76  CB  ARG A1015     1623   3546   2377   -333    483   -829       C  
ATOM     77  CG  ARG A1015      13.618  -4.681   5.409  1.00 19.49           C  
ANISOU   77  CG  ARG A1015     1315   3382   2707   -230    496   -586       C  
ATOM     78  CD  ARG A1015      12.189  -4.338   5.822  1.00 21.63           C  
ANISOU   78  CD  ARG A1015     1474   3531   3215   -140    746   -293       C  
ATOM     79  NE  ARG A1015      11.763  -5.069   7.013  1.00 24.10           N  
ANISOU   79  NE  ARG A1015     1974   3650   3533   -240    590   -175       N  
ATOM     80  CZ  ARG A1015      11.262  -6.306   6.998  1.00 25.97           C  
ANISOU   80  CZ  ARG A1015     2433   3679   3756   -163    829   -228       C  
ATOM     81  NH1 ARG A1015      11.123  -6.966   5.849  1.00 26.45           N  
ANISOU   81  NH1 ARG A1015     2220   3882   3946    -54    560   -491       N  
ATOM     82  NH2 ARG A1015      10.915  -6.890   8.139  1.00 28.74           N  
ANISOU   82  NH2 ARG A1015     2836   3989   4095   -333    816      5       N  
ATOM     83  N   SER A1016      14.861  -3.017   1.259  1.00 18.28           N  
ANISOU   83  N   SER A1016     1412   3192   2338   -208     52   -772       N  
ATOM     84  CA  SER A1016      15.174  -1.901   0.381  1.00 18.14           C  
ANISOU   84  CA  SER A1016     1474   3041   2378   -229   -153   -714       C  
ATOM     85  C   SER A1016      14.520  -2.030  -0.993  1.00 18.62           C  
ANISOU   85  C   SER A1016     1612   3129   2333   -240    -98   -693       C  
ATOM     86  O   SER A1016      14.470  -1.063  -1.759  1.00 20.16           O  
ANISOU   86  O   SER A1016     2044   3194   2421   -219   -229   -627       O  
ATOM     87  CB  SER A1016      16.690  -1.765   0.229  1.00 18.16           C  
ANISOU   87  CB  SER A1016     1474   3064   2363   -259    -73   -649       C  
ATOM     88  OG  SER A1016      17.258  -1.282   1.429  1.00 19.88           O  
ANISOU   88  OG  SER A1016     1473   3255   2824   -333   -518   -548       O  
ATOM     89  N   THR A1017      14.017  -3.222  -1.304  1.00 18.90           N  
ANISOU   89  N   THR A1017     1479   3294   2407   -205   -252   -772       N  
ATOM     90  CA  THR A1017      13.371  -3.432  -2.604  1.00 19.63           C  
ANISOU   90  CA  THR A1017     1250   3639   2569    -37   -186   -798       C  
ATOM     91  C   THR A1017      11.878  -3.734  -2.488  1.00 22.21           C  
ANISOU   91  C   THR A1017     1280   4275   2883    126    -34   -886       C  
ATOM     92  O   THR A1017      11.291  -4.458  -3.310  1.00 22.54           O  
ANISOU   92  O   THR A1017     1132   4429   3003    -93    -46   -900       O  
ATOM     93  CB  THR A1017      14.118  -4.494  -3.420  1.00 19.24           C  
ANISOU   93  CB  THR A1017     1191   3569   2549     27   -230   -697       C  
ATOM     94  OG1 THR A1017      14.310  -5.664  -2.631  1.00 20.92           O  
ANISOU   94  OG1 THR A1017     1852   3447   2648     57   -318   -627       O  
ATOM     95  CG2 THR A1017      15.484  -3.953  -3.845  1.00 19.98           C  
ANISOU   95  CG2 THR A1017      982   3973   2637    -54   -194   -614       C  
ATOM     96  N   GLY A1018      11.267  -3.160  -1.460  1.00 25.57           N  
ANISOU   96  N   GLY A1018     1349   4981   3384    450    109   -895       N  
ATOM     97  CA  GLY A1018       9.812  -3.133  -1.365  1.00 29.05           C  
ANISOU   97  CA  GLY A1018     1509   5475   4052    617    186   -749       C  
ATOM     98  C   GLY A1018       9.203  -4.108  -0.388  1.00 30.47           C  
ANISOU   98  C   GLY A1018     1703   5519   4356    489    -31   -741       C  
ATOM     99  O   GLY A1018       7.992  -4.157  -0.233  1.00 31.07           O  
ANISOU   99  O   GLY A1018     1683   5792   4329    549     35   -627       O  
ATOM    100  N   ASP A1019      10.049  -4.871   0.291  1.00 30.58           N  
ANISOU  100  N   ASP A1019     1834   5177   4609    366   -302   -891       N  
ATOM    101  CA  ASP A1019       9.591  -5.824   1.293  1.00 31.86           C  
ANISOU  101  CA  ASP A1019     2125   5120   4859    208   -513   -882       C  
ATOM    102  C   ASP A1019       9.420  -5.129   2.645  1.00 32.65           C  
ANISOU  102  C   ASP A1019     2298   5309   4798    -41   -284   -898       C  
ATOM    103  O   ASP A1019      10.106  -5.462   3.617  1.00 33.37           O  
ANISOU  103  O   ASP A1019     2475   5364   4838    -81   -403   -776       O  
ATOM    104  CB  ASP A1019      10.589  -6.977   1.399  1.00 32.67           C  
ANISOU  104  CB  ASP A1019     2266   5044   5102    353   -754   -847       C  
ATOM    105  CG  ASP A1019       9.922  -8.315   1.620  1.00 35.72           C  
ANISOU  105  CG  ASP A1019     2606   5149   5817    408   -935   -520       C  
ATOM    106  OD1 ASP A1019       8.675  -8.381   1.625  1.00 40.17           O  
ANISOU  106  OD1 ASP A1019     2883   5475   6904    359   -930     52       O  
ATOM    107  OD2 ASP A1019      10.655  -9.309   1.788  1.00 37.19           O  
ANISOU  107  OD2 ASP A1019     2639   5320   6172    533   -472   -293       O  
ATOM    108  N   MET A1020       8.515  -4.150   2.686  1.00 33.80           N  
ANISOU  108  N   MET A1020     2196   5766   4881   -379    324  -1062       N  
ATOM    109  CA  MET A1020       8.201  -3.408   3.907  1.00 36.03           C  
ANISOU  109  CA  MET A1020     2398   6219   5073   -662    900  -1193       C  
ATOM    110  C   MET A1020       6.725  -3.584   4.233  1.00 35.57           C  
ANISOU  110  C   MET A1020     2257   6348   4910   -538    842  -1436       C  
ATOM    111  O   MET A1020       5.913  -3.787   3.331  1.00 36.84           O  
ANISOU  111  O   MET A1020     2451   6736   4809   -241    828  -1500       O  
ATOM    112  CB  MET A1020       8.497  -1.915   3.724  1.00 36.98           C  
ANISOU  112  CB  MET A1020     2511   6190   5349   -807    944  -1181       C  
ATOM    113  CG  MET A1020       9.956  -1.574   3.451  1.00 39.78           C  
ANISOU  113  CG  MET A1020     2730   6657   5727  -1058   1102   -560       C  
ATOM    114  SD  MET A1020      10.187   0.131   2.896  1.00 37.05           S  
ANISOU  114  SD  MET A1020     2205   6790   5083   -966    445   -394       S  
ATOM    115  CE  MET A1020       9.710   1.045   4.359  1.00 38.64           C  
ANISOU  115  CE  MET A1020     2572   7181   4928   -581    680   -186       C  
ATOM    116  N   HIS A1021       6.377  -3.495   5.514  1.00 34.13           N  
ANISOU  116  N   HIS A1021     1897   6115   4956   -767    781  -1594       N  
ATOM    117  CA  HIS A1021       4.967  -3.519   5.914  1.00 33.82           C  
ANISOU  117  CA  HIS A1021     1606   5917   5328   -960    579  -1536       C  
ATOM    118  C   HIS A1021       4.347  -2.137   5.753  1.00 33.67           C  
ANISOU  118  C   HIS A1021     1473   5957   5363  -1036    214  -1712       C  
ATOM    119  O   HIS A1021       5.060  -1.133   5.768  1.00 34.06           O  
ANISOU  119  O   HIS A1021     1474   5896   5572  -1141    331  -1773       O  
ATOM    120  CB  HIS A1021       4.812  -3.980   7.368  1.00 33.83           C  
ANISOU  120  CB  HIS A1021     1615   5806   5432  -1061    649  -1500       C  
ATOM    121  CG  HIS A1021       5.461  -3.073   8.371  1.00 35.75           C  
ANISOU  121  CG  HIS A1021     1923   5565   6097   -732    397  -1674       C  
ATOM    122  ND1 HIS A1021       4.796  -2.045   9.006  1.00 38.16           N  
ANISOU  122  ND1 HIS A1021     2213   5400   6887   -537    219  -1852       N  
ATOM    123  CD2 HIS A1021       6.728  -3.039   8.850  1.00 36.72           C  
ANISOU  123  CD2 HIS A1021     2071   5188   6692   -636    131  -1921       C  
ATOM    124  CE1 HIS A1021       5.617  -1.420   9.830  1.00 39.04           C  
ANISOU  124  CE1 HIS A1021     2560   5070   7203   -410    104  -1993       C  
ATOM    125  NE2 HIS A1021       6.802  -2.003   9.752  1.00 38.17           N  
ANISOU  125  NE2 HIS A1021     2383   5004   7116   -463    109  -2020       N  
ATOM    126  N   LYS A1022       3.023  -2.075   5.607  1.00 34.26           N  
ANISOU  126  N   LYS A1022     1483   6291   5245   -864   -270  -1817       N  
ATOM    127  CA  LYS A1022       2.320  -0.795   5.610  1.00 35.95           C  
ANISOU  127  CA  LYS A1022     1867   6751   5040   -485   -732  -1791       C  
ATOM    128  C   LYS A1022       2.526  -0.107   6.958  1.00 33.73           C  
ANISOU  128  C   LYS A1022     1903   6377   4535   -562   -560  -1665       C  
ATOM    129  O   LYS A1022       2.576  -0.773   7.994  1.00 34.00           O  
ANISOU  129  O   LYS A1022     2072   6352   4496   -671   -252  -1615       O  
ATOM    130  CB  LYS A1022       0.820  -0.983   5.369  1.00 38.34           C  
ANISOU  130  CB  LYS A1022     1941   7225   5400   -322  -1084  -1744       C  
ATOM    131  CG  LYS A1022       0.027   0.324   5.298  1.00 44.81           C  
ANISOU  131  CG  LYS A1022     2319   8553   6154    401  -1289  -1263       C  
ATOM    132  CD  LYS A1022      -1.190   0.306   6.219  1.00 52.86           C  
ANISOU  132  CD  LYS A1022     2624  10339   7120   1162  -1418   -544       C  
ATOM    133  CE  LYS A1022      -2.291  -0.594   5.668  1.00 54.96           C  
ANISOU  133  CE  LYS A1022     2361  11181   7342   1571  -1410   -333       C  
ATOM    134  NZ  LYS A1022      -2.980   0.029   4.467  1.00 57.76           N  
ANISOU  134  NZ  LYS A1022     2858  11706   7383   1764  -1289   -259       N  
ATOM    135  N   ALA A1023       2.655   1.215   6.943  1.00 31.62           N  
ANISOU  135  N   ALA A1023     1808   6129   4077   -610   -348  -1453       N  
ATOM    136  CA  ALA A1023       2.866   1.979   8.169  1.00 29.59           C  
ANISOU  136  CA  ALA A1023     1474   5921   3849   -793    -98  -1263       C  
ATOM    137  C   ALA A1023       1.743   1.778   9.181  1.00 28.94           C  
ANISOU  137  C   ALA A1023     1233   5787   3977   -908    -20  -1162       C  
ATOM    138  O   ALA A1023       0.552   1.746   8.820  1.00 29.53           O  
ANISOU  138  O   ALA A1023     1146   5981   4092   -913   -148  -1079       O  
ATOM    139  CB  ALA A1023       3.046   3.459   7.856  1.00 29.89           C  
ANISOU  139  CB  ALA A1023     1747   5956   3652   -856     24  -1177       C  
ATOM    140  N   LYS A1024       2.140   1.618  10.441  1.00 28.48           N  
ANISOU  140  N   LYS A1024     1054   5655   4113   -842    175  -1307       N  
ATOM    141  CA  LYS A1024       1.193   1.603  11.551  1.00 29.17           C  
ANISOU  141  CA  LYS A1024     1189   5521   4372   -763    313  -1342       C  
ATOM    142  C   LYS A1024       1.667   2.519  12.684  1.00 27.80           C  
ANISOU  142  C   LYS A1024      961   5350   4253   -612    394  -1421       C  
ATOM    143  O   LYS A1024       2.868   2.626  12.959  1.00 27.14           O  
ANISOU  143  O   LYS A1024      724   5170   4417   -727    498  -1483       O  
ATOM    144  CB  LYS A1024       0.877   0.178  12.026  1.00 30.86           C  
ANISOU  144  CB  LYS A1024     1527   5687   4510   -790    230  -1216       C  
ATOM    145  CG  LYS A1024       1.951  -0.563  12.789  1.00 37.50           C  
ANISOU  145  CG  LYS A1024     2867   6258   5123   -772   -379   -815       C  
ATOM    146  CD  LYS A1024       1.691  -0.548  14.304  1.00 44.81           C  
ANISOU  146  CD  LYS A1024     4266   6941   5820   -674   -926   -226       C  
ATOM    147  CE  LYS A1024       2.874  -1.170  15.046  1.00 46.58           C  
ANISOU  147  CE  LYS A1024     4541   7045   6111   -573  -1155    -31       C  
ATOM    148  NZ  LYS A1024       3.055  -0.630  16.423  1.00 46.50           N  
ANISOU  148  NZ  LYS A1024     4343   7031   6294   -434  -1137    -62       N  
ATOM    149  N   SER A1025       0.722   3.211  13.310  1.00 27.12           N  
ANISOU  149  N   SER A1025     1017   4992   4293   -474    478  -1342       N  
ATOM    150  CA  SER A1025       1.045   4.230  14.309  1.00 27.36           C  
ANISOU  150  CA  SER A1025     1298   4809   4287   -542    571   -988       C  
ATOM    151  C   SER A1025       1.682   3.638  15.557  1.00 25.25           C  
ANISOU  151  C   SER A1025     1263   4499   3831   -766    736   -886       C  
ATOM    152  O   SER A1025       1.158   2.679  16.134  1.00 27.10           O  
ANISOU  152  O   SER A1025     1559   4702   4034  -1027    700   -793       O  
ATOM    153  CB  SER A1025      -0.231   4.973  14.714  1.00 28.47           C  
ANISOU  153  CB  SER A1025     1474   4798   4544   -317    619  -1022       C  
ATOM    154  OG  SER A1025      -0.814   5.648  13.606  1.00 33.15           O  
ANISOU  154  OG  SER A1025     2011   5174   5411   -197    507   -493       O  
ATOM    155  N   PRO A1026       2.805   4.205  16.000  1.00 24.05           N  
ANISOU  155  N   PRO A1026     1393   4379   3366   -929    785   -640       N  
ATOM    156  CA  PRO A1026       3.391   3.754  17.253  1.00 24.50           C  
ANISOU  156  CA  PRO A1026     1728   4345   3235   -948    878   -559       C  
ATOM    157  C   PRO A1026       2.484   4.093  18.435  1.00 25.82           C  
ANISOU  157  C   PRO A1026     2157   4347   3307  -1171   1032   -553       C  
ATOM    158  O   PRO A1026       1.745   5.076  18.404  1.00 27.09           O  
ANISOU  158  O   PRO A1026     2301   4616   3375  -1001   1096   -553       O  
ATOM    159  CB  PRO A1026       4.703   4.546  17.342  1.00 23.89           C  
ANISOU  159  CB  PRO A1026     1492   4460   3127   -930    772   -551       C  
ATOM    160  CG  PRO A1026       4.945   5.078  15.983  1.00 23.76           C  
ANISOU  160  CG  PRO A1026     1315   4372   3339   -798    652   -403       C  
ATOM    161  CD  PRO A1026       3.614   5.245  15.344  1.00 22.80           C  
ANISOU  161  CD  PRO A1026     1132   4282   3249   -833    776   -582       C  
ATOM    162  N   THR A1027       2.570   3.296  19.486  1.00 28.48           N  
ANISOU  162  N   THR A1027     2856   4415   3551  -1456   1150   -406       N  
ATOM    163  CA  THR A1027       1.749   3.516  20.668  1.00 31.11           C  
ANISOU  163  CA  THR A1027     3355   4541   3925  -1650   1132   -307       C  
ATOM    164  C   THR A1027       2.619   3.709  21.898  1.00 30.14           C  
ANISOU  164  C   THR A1027     3436   4230   3785  -1404   1186   -351       C  
ATOM    165  O   THR A1027       2.490   4.698  22.630  1.00 31.69           O  
ANISOU  165  O   THR A1027     3740   4244   4056  -1229    876   -531       O  
ATOM    166  CB  THR A1027       0.766   2.328  20.904  1.00 32.58           C  
ANISOU  166  CB  THR A1027     3479   4731   4169  -1833   1096   -197       C  
ATOM    167  OG1 THR A1027       1.489   1.091  20.919  1.00 36.29           O  
ANISOU  167  OG1 THR A1027     4320   4763   4706  -1914    820    -87       O  
ATOM    168  CG2 THR A1027      -0.269   2.256  19.794  1.00 34.64           C  
ANISOU  168  CG2 THR A1027     3528   5169   4465  -2010   1049   -274       C  
ATOM    169  N   ILE A1028       3.504   2.744  22.127  1.00 29.61           N  
ANISOU  169  N   ILE A1028     3463   4086   3702  -1272   1333   -260       N  
ATOM    170  CA  ILE A1028       4.366   2.773  23.294  1.00 29.34           C  
ANISOU  170  CA  ILE A1028     3497   3914   3736  -1172   1447     59       C  
ATOM    171  C   ILE A1028       5.685   3.471  22.992  1.00 27.43           C  
ANISOU  171  C   ILE A1028     3384   3855   3185  -1075   1324    -15       C  
ATOM    172  O   ILE A1028       6.198   3.447  21.872  1.00 27.83           O  
ANISOU  172  O   ILE A1028     3422   4117   3034  -1127   1412    -41       O  
ATOM    173  CB  ILE A1028       4.623   1.359  23.883  1.00 30.74           C  
ANISOU  173  CB  ILE A1028     3643   3932   4104  -1158   1465    131       C  
ATOM    174  CG1 ILE A1028       5.357   0.456  22.886  1.00 33.34           C  
ANISOU  174  CG1 ILE A1028     3867   4151   4650   -842   1393    326       C  
ATOM    175  CG2 ILE A1028       3.308   0.737  24.355  1.00 32.45           C  
ANISOU  175  CG2 ILE A1028     3772   3995   4564  -1163   1562    472       C  
ATOM    176  CD1 ILE A1028       5.969  -0.795  23.507  1.00 35.77           C  
ANISOU  176  CD1 ILE A1028     3946   4587   5059   -383   1220    553       C  
ATOM    177  N   MET A1029       6.197   4.136  24.020  1.00 25.83           N  
ANISOU  177  N   MET A1029     3185   3662   2969   -636    925     46       N  
ATOM    178  CA  MET A1029       7.531   4.715  24.016  1.00 24.73           C  
ANISOU  178  CA  MET A1029     3120   3386   2890   -292    599     76       C  
ATOM    179  C   MET A1029       8.556   3.657  23.634  1.00 23.67           C  
ANISOU  179  C   MET A1029     2921   3217   2856    -93    412    193       C  
ATOM    180  O   MET A1029       8.382   2.480  23.942  1.00 24.72           O  
ANISOU  180  O   MET A1029     2890   3208   3294    -74    496    322       O  
ATOM    181  CB  MET A1029       7.834   5.225  25.421  1.00 26.43           C  
ANISOU  181  CB  MET A1029     3388   3610   3046   -251    412   -126       C  
ATOM    182  CG  MET A1029       8.792   6.386  25.489  1.00 27.62           C  
ANISOU  182  CG  MET A1029     3680   3819   2996   -263    472   -151       C  
ATOM    183  SD  MET A1029       8.811   7.070  27.157  1.00 24.41           S  
ANISOU  183  SD  MET A1029     2524   4205   2545     51    476   -164       S  
ATOM    184  CE  MET A1029       8.728   5.599  28.178  1.00 27.97           C  
ANISOU  184  CE  MET A1029     3824   3871   2933    -82    342   -346       C  
ATOM    185  N   THR A1030       9.627   4.077  22.969  1.00 22.04           N  
ANISOU  185  N   THR A1030     2903   2962   2511     87    285     98       N  
ATOM    186  CA  THR A1030      10.718   3.164  22.660  1.00 22.32           C  
ANISOU  186  CA  THR A1030     3181   2937   2362    285    172    -20       C  
ATOM    187  C   THR A1030      12.021   3.691  23.253  1.00 21.34           C  
ANISOU  187  C   THR A1030     3057   2872   2178    405    208     98       C  
ATOM    188  O   THR A1030      12.376   4.852  23.035  1.00 21.73           O  
ANISOU  188  O   THR A1030     3097   2870   2289    329    186    151       O  
ATOM    189  CB  THR A1030      10.868   3.013  21.130  1.00 22.88           C  
ANISOU  189  CB  THR A1030     3364   2955   2372    285    173   -172       C  
ATOM    190  OG1 THR A1030       9.693   2.409  20.575  1.00 24.99           O  
ANISOU  190  OG1 THR A1030     3808   3129   2558    120    -30   -114       O  
ATOM    191  CG2 THR A1030      12.076   2.156  20.777  1.00 24.61           C  
ANISOU  191  CG2 THR A1030     3689   3170   2492    476    252    -98       C  
ATOM    192  N   ARG A1031      12.725   2.841  23.995  1.00 22.39           N  
ANISOU  192  N   ARG A1031     3253   3086   2169    601    115    173       N  
ATOM    193  CA  ARG A1031      14.070   3.151  24.456  1.00 23.26           C  
ANISOU  193  CA  ARG A1031     3425   3262   2149    750     97    228       C  
ATOM    194  C   ARG A1031      15.027   2.913  23.294  1.00 23.42           C  
ANISOU  194  C   ARG A1031     3474   3176   2249    696    219    148       C  
ATOM    195  O   ARG A1031      15.159   1.796  22.799  1.00 24.53           O  
ANISOU  195  O   ARG A1031     3533   3224   2563    693    270     87       O  
ATOM    196  CB  ARG A1031      14.467   2.278  25.643  1.00 23.78           C  
ANISOU  196  CB  ARG A1031     3560   3359   2117    908     41    285       C  
ATOM    197  CG  ARG A1031      15.796   2.664  26.277  1.00 25.82           C  
ANISOU  197  CG  ARG A1031     4065   3607   2140   1018   -230    357       C  
ATOM    198  CD  ARG A1031      16.122   1.771  27.464  1.00 28.55           C  
ANISOU  198  CD  ARG A1031     4659   4029   2158   1544   -263    509       C  
ATOM    199  NE  ARG A1031      17.212   2.303  28.276  1.00 30.12           N  
ANISOU  199  NE  ARG A1031     4778   4629   2037   1902   -208    518       N  
ATOM    200  CZ  ARG A1031      17.817   1.627  29.259  1.00 31.37           C  
ANISOU  200  CZ  ARG A1031     4938   4863   2117   2178   -142    639       C  
ATOM    201  NH1 ARG A1031      17.452   0.383  29.555  1.00 33.10           N  
ANISOU  201  NH1 ARG A1031     5260   4902   2416   2274    -49    640       N  
ATOM    202  NH2 ARG A1031      18.796   2.192  29.957  1.00 32.35           N  
ANISOU  202  NH2 ARG A1031     4946   5156   2187   2318   -320    595       N  
ATOM    203  N   VAL A1032      15.695   3.970  22.848  1.00 23.60           N  
ANISOU  203  N   VAL A1032     3517   3237   2213    732    377    230       N  
ATOM    204  CA  VAL A1032      16.581   3.864  21.695  1.00 25.03           C  
ANISOU  204  CA  VAL A1032     3722   3420   2368    872    533    296       C  
ATOM    205  C   VAL A1032      18.026   3.629  22.123  1.00 24.78           C  
ANISOU  205  C   VAL A1032     3777   3407   2230   1115    467    228       C  
ATOM    206  O   VAL A1032      18.724   2.792  21.554  1.00 25.88           O  
ANISOU  206  O   VAL A1032     3989   3537   2308   1238    230     92       O  
ATOM    207  CB  VAL A1032      16.502   5.112  20.797  1.00 25.43           C  
ANISOU  207  CB  VAL A1032     3655   3522   2486    860    640    447       C  
ATOM    208  CG1 VAL A1032      15.056   5.414  20.435  1.00 25.75           C  
ANISOU  208  CG1 VAL A1032     3666   3571   2545    794    584    386       C  
ATOM    209  CG2 VAL A1032      17.148   6.303  21.485  1.00 26.23           C  
ANISOU  209  CG2 VAL A1032     3623   3736   2606    776    850    485       C  
ATOM    210  N   THR A1033      18.463   4.373  23.132  1.00 24.78           N  
ANISOU  210  N   THR A1033     3675   3578   2161   1400    406    261       N  
ATOM    211  CA  THR A1033      19.783   4.176  23.732  1.00 24.79           C  
ANISOU  211  CA  THR A1033     3512   3799   2108   1544    458    373       C  
ATOM    212  C   THR A1033      19.611   4.058  25.247  1.00 24.89           C  
ANISOU  212  C   THR A1033     3264   4070   2124   1597    443    329       C  
ATOM    213  O   THR A1033      18.477   3.965  25.743  1.00 25.48           O  
ANISOU  213  O   THR A1033     3194   4334   2152   1649    491    392       O  
ATOM    214  CB  THR A1033      20.755   5.333  23.401  1.00 24.72           C  
ANISOU  214  CB  THR A1033     3564   3747   2081   1532    472    331       C  
ATOM    215  OG1 THR A1033      20.293   6.536  24.029  1.00 24.91           O  
ANISOU  215  OG1 THR A1033     3370   3901   2194   1562    427    170       O  
ATOM    216  CG2 THR A1033      20.879   5.541  21.883  1.00 25.07           C  
ANISOU  216  CG2 THR A1033     3542   3883   2099   1524    643    388       C  
ATOM    217  N   ASN A1034      20.712   4.067  25.993  1.00 25.29           N  
ANISOU  217  N   ASN A1034     3079   4284   2247   1699    355    215       N  
ATOM    218  CA  ASN A1034      20.618   3.994  27.448  1.00 25.21           C  
ANISOU  218  CA  ASN A1034     2951   4323   2304   1676    161    137       C  
ATOM    219  C   ASN A1034      19.669   5.052  28.017  1.00 25.21           C  
ANISOU  219  C   ASN A1034     3032   4440   2107   1817    208    164       C  
ATOM    220  O   ASN A1034      18.836   4.745  28.875  1.00 25.96           O  
ANISOU  220  O   ASN A1034     3088   4571   2205   1875    315    219       O  
ATOM    221  CB  ASN A1034      21.984   4.106  28.120  1.00 25.64           C  
ANISOU  221  CB  ASN A1034     2854   4356   2531   1544     73    137       C  
ATOM    222  CG  ASN A1034      22.691   2.771  28.236  1.00 27.43           C  
ANISOU  222  CG  ASN A1034     2996   4313   3113   1221   -381    -10       C  
ATOM    223  OD1 ASN A1034      22.328   1.788  27.591  1.00 28.98           O  
ANISOU  223  OD1 ASN A1034     2736   4383   3892    878   -461    -82       O  
ATOM    224  ND2 ASN A1034      23.714   2.724  29.077  1.00 29.63           N  
ANISOU  224  ND2 ASN A1034     2912   4584   3763    939   -670     76       N  
ATOM    225  N   ASN A1035      19.790   6.287  27.531  1.00 24.07           N  
ANISOU  225  N   ASN A1035     2840   4383   1923   1858     -3     62       N  
ATOM    226  CA  ASN A1035      19.006   7.393  28.098  1.00 23.48           C  
ANISOU  226  CA  ASN A1035     2705   4408   1808   1771   -185    -35       C  
ATOM    227  C   ASN A1035      18.076   8.130  27.142  1.00 21.79           C  
ANISOU  227  C   ASN A1035     2462   4086   1729   1518   -203    -62       C  
ATOM    228  O   ASN A1035      17.318   9.001  27.590  1.00 22.34           O  
ANISOU  228  O   ASN A1035     2508   4189   1791   1562   -153    -76       O  
ATOM    229  CB  ASN A1035      19.922   8.419  28.761  1.00 24.36           C  
ANISOU  229  CB  ASN A1035     2752   4634   1869   1861   -307    -93       C  
ATOM    230  CG  ASN A1035      20.632   7.841  29.956  1.00 26.85           C  
ANISOU  230  CG  ASN A1035     2924   5213   2064   1973   -417    109       C  
ATOM    231  OD1 ASN A1035      20.079   7.797  31.046  1.00 29.45           O  
ANISOU  231  OD1 ASN A1035     3355   5658   2176   1976   -333    219       O  
ATOM    232  ND2 ASN A1035      21.854   7.378  29.733  1.00 29.77           N  
ANISOU  232  ND2 ASN A1035     3023   5651   2639   2073   -443     82       N  
ATOM    233  N   VAL A1036      18.146   7.795  25.858  1.00 19.70           N  
ANISOU  233  N   VAL A1036     2060   3756   1668   1216    -54     87       N  
ATOM    234  CA  VAL A1036      17.313   8.479  24.867  1.00 17.87           C  
ANISOU  234  CA  VAL A1036     1693   3416   1682    882    -17    159       C  
ATOM    235  C   VAL A1036      16.114   7.628  24.451  1.00 18.05           C  
ANISOU  235  C   VAL A1036     1764   3197   1897    803    136    152       C  
ATOM    236  O   VAL A1036      16.246   6.470  24.046  1.00 18.78           O  
ANISOU  236  O   VAL A1036     1932   3219   1985    877    137    148       O  
ATOM    237  CB  VAL A1036      18.128   8.923  23.629  1.00 17.75           C  
ANISOU  237  CB  VAL A1036     1579   3461   1703    772    -20    186       C  
ATOM    238  CG1 VAL A1036      17.259   9.671  22.633  1.00 17.13           C  
ANISOU  238  CG1 VAL A1036     1588   3323   1597    649   -193    197       C  
ATOM    239  CG2 VAL A1036      19.300   9.803  24.049  1.00 17.65           C  
ANISOU  239  CG2 VAL A1036     1172   3596   1939    758    -92    -31       C  
ATOM    240  N   TYR A1037      14.932   8.245  24.558  1.00 17.40           N  
ANISOU  240  N   TYR A1037     1588   3192   1832    736    120     68       N  
ATOM    241  CA  TYR A1037      13.660   7.583  24.264  1.00 17.61           C  
ANISOU  241  CA  TYR A1037     1747   3125   1817    522    186      6       C  
ATOM    242  C   TYR A1037      12.937   8.320  23.134  1.00 15.89           C  
ANISOU  242  C   TYR A1037     1488   2842   1708    408    175   -137       C  
ATOM    243  O   TYR A1037      13.147   9.522  22.934  1.00 15.68           O  
ANISOU  243  O   TYR A1037     1154   2854   1949    252    120   -109       O  
ATOM    244  CB  TYR A1037      12.766   7.535  25.518  1.00 18.45           C  
ANISOU  244  CB  TYR A1037     1939   3321   1752    524    229     76       C  
ATOM    245  CG  TYR A1037      13.310   6.665  26.635  1.00 20.62           C  
ANISOU  245  CG  TYR A1037     2468   3517   1851    680    401    197       C  
ATOM    246  CD1 TYR A1037      12.720   5.447  26.961  1.00 22.65           C  
ANISOU  246  CD1 TYR A1037     2946   3684   1975    706    489    337       C  
ATOM    247  CD2 TYR A1037      14.425   7.060  27.375  1.00 21.91           C  
ANISOU  247  CD2 TYR A1037     2655   3759   1912    847    344    241       C  
ATOM    248  CE1 TYR A1037      13.225   4.643  27.987  1.00 24.00           C  
ANISOU  248  CE1 TYR A1037     3248   3939   1932    847    471    417       C  
ATOM    249  CE2 TYR A1037      14.944   6.269  28.395  1.00 23.67           C  
ANISOU  249  CE2 TYR A1037     3129   3941   1923    957    535    476       C  
ATOM    250  CZ  TYR A1037      14.335   5.057  28.708  1.00 24.23           C  
ANISOU  250  CZ  TYR A1037     3336   3939   1932    970    482    480       C  
ATOM    251  OH  TYR A1037      14.843   4.257  29.721  1.00 26.78           O  
ANISOU  251  OH  TYR A1037     3729   4147   2298   1018    502    644       O  
ATOM    252  N   LEU A1038      12.106   7.575  22.398  1.00 15.76           N  
ANISOU  252  N   LEU A1038     1464   2698   1826    197    164    -98       N  
ATOM    253  CA  LEU A1038      11.323   8.114  21.275  1.00 15.83           C  
ANISOU  253  CA  LEU A1038     1333   2741   1941    164    172    -82       C  
ATOM    254  C   LEU A1038       9.834   7.890  21.541  1.00 15.88           C  
ANISOU  254  C   LEU A1038     1386   2583   2064     57    241   -108       C  
ATOM    255  O   LEU A1038       9.450   6.782  21.916  1.00 17.25           O  
ANISOU  255  O   LEU A1038     1630   2669   2257     98    388    -17       O  
ATOM    256  CB  LEU A1038      11.727   7.420  19.966  1.00 15.99           C  
ANISOU  256  CB  LEU A1038     1324   2777   1976    295     74    -82       C  
ATOM    257  CG  LEU A1038      10.886   7.673  18.702  1.00 14.71           C  
ANISOU  257  CG  LEU A1038      891   2791   1905     81    175    -71       C  
ATOM    258  CD1 LEU A1038      10.781   9.143  18.343  1.00 15.69           C  
ANISOU  258  CD1 LEU A1038     1080   2851   2029    195    395     49       C  
ATOM    259  CD2 LEU A1038      11.474   6.877  17.540  1.00 15.78           C  
ANISOU  259  CD2 LEU A1038     1221   2748   2027    175    436   -131       C  
ATOM    260  N   GLY A1039       9.018   8.924  21.343  1.00 15.65           N  
ANISOU  260  N   GLY A1039     1158   2671   2116    -31    331    -73       N  
ATOM    261  CA  GLY A1039       7.616   8.850  21.725  1.00 16.64           C  
ANISOU  261  CA  GLY A1039     1208   2867   2247   -115    461    -68       C  
ATOM    262  C   GLY A1039       6.701   9.784  20.963  1.00 15.71           C  
ANISOU  262  C   GLY A1039     1009   2842   2117   -296    505   -175       C  
ATOM    263  O   GLY A1039       7.149  10.631  20.186  1.00 15.60           O  
ANISOU  263  O   GLY A1039      956   2973   2000   -175    529   -162       O  
ATOM    264  N   ASN A1040       5.401   9.613  21.201  1.00 16.29           N  
ANISOU  264  N   ASN A1040      895   3111   2185   -355    612   -388       N  
ATOM    265  CA  ASN A1040       4.389  10.498  20.658  1.00 16.59           C  
ANISOU  265  CA  ASN A1040      781   3312   2212   -472    706   -458       C  
ATOM    266  C   ASN A1040       3.883  11.458  21.745  1.00 16.94           C  
ANISOU  266  C   ASN A1040      787   3429   2222   -307    723   -408       C  
ATOM    267  O   ASN A1040       4.439  11.541  22.852  1.00 17.08           O  
ANISOU  267  O   ASN A1040      876   3470   2143   -359    710   -458       O  
ATOM    268  CB  ASN A1040       3.257   9.672  20.040  1.00 17.02           C  
ANISOU  268  CB  ASN A1040      856   3422   2187   -599    709   -419       C  
ATOM    269  CG  ASN A1040       2.533   8.825  21.069  1.00 18.37           C  
ANISOU  269  CG  ASN A1040     1061   3679   2240   -788    863   -375       C  
ATOM    270  OD1 ASN A1040       2.685   9.005  22.284  1.00 20.29           O  
ANISOU  270  OD1 ASN A1040     1365   4065   2280   -710    798   -193       O  
ATOM    271  ND2 ASN A1040       1.724   7.897  20.571  1.00 21.96           N  
ANISOU  271  ND2 ASN A1040     1622   3964   2759  -1168    710   -203       N  
ATOM    272  N   TYR A1041       2.829  12.203  21.432  1.00 17.21           N  
ANISOU  272  N   TYR A1041      619   3558   2362   -237    842   -274       N  
ATOM    273  CA ATYR A1041       2.318  13.197  22.369  0.50 18.26           C  
ANISOU  273  CA ATYR A1041      867   3698   2372    -60    812   -186       C  
ATOM    274  CA BTYR A1041       2.309  13.199  22.361  0.50 18.24           C  
ANISOU  274  CA BTYR A1041      900   3677   2354    -62    790   -197       C  
ATOM    275  C   TYR A1041       1.783  12.576  23.659  1.00 18.55           C  
ANISOU  275  C   TYR A1041      996   3698   2354   -241    834   -208       C  
ATOM    276  O   TYR A1041       2.062  13.069  24.758  1.00 18.17           O  
ANISOU  276  O   TYR A1041      725   3799   2380   -285    834   -258       O  
ATOM    277  CB ATYR A1041       1.249  14.085  21.720  0.50 19.19           C  
ANISOU  277  CB ATYR A1041      970   3873   2449     91    768   -174       C  
ATOM    278  CB BTYR A1041       1.225  14.032  21.676  0.50 19.14           C  
ANISOU  278  CB BTYR A1041     1014   3817   2442     97    715   -215       C  
ATOM    279  CG ATYR A1041       1.065  15.382  22.469  0.50 20.88           C  
ANISOU  279  CG ATYR A1041     1217   4124   2594    421    516   -241       C  
ATOM    280  CG BTYR A1041       0.408  14.879  22.612  0.50 20.72           C  
ANISOU  280  CG BTYR A1041     1243   4174   2453    460    597   -296       C  
ATOM    281  CD1ATYR A1041       2.043  16.372  22.427  0.50 24.43           C  
ANISOU  281  CD1ATYR A1041     1956   4415   2910    252    524   -381       C  
ATOM    282  CD1BTYR A1041       0.869  16.118  23.045  0.50 23.02           C  
ANISOU  282  CD1BTYR A1041     1588   4359   2799    649    644   -428       C  
ATOM    283  CD2ATYR A1041      -0.070  15.613  23.237  0.50 23.74           C  
ANISOU  283  CD2ATYR A1041     1720   4458   2842    533    544   -421       C  
ATOM    284  CD2BTYR A1041      -0.841  14.448  23.051  0.50 22.46           C  
ANISOU  284  CD2BTYR A1041     1377   4487   2671    595    737   -386       C  
ATOM    285  CE1ATYR A1041       1.887  17.558  23.122  0.50 26.41           C  
ANISOU  285  CE1ATYR A1041     2152   4620   3264    182    671   -597       C  
ATOM    286  CE1BTYR A1041       0.110  16.906  23.902  0.50 24.32           C  
ANISOU  286  CE1BTYR A1041     1641   4386   3212    816    929   -467       C  
ATOM    287  CE2ATYR A1041      -0.234  16.800  23.934  0.50 25.83           C  
ANISOU  287  CE2ATYR A1041     1941   4566   3307    450    608   -601       C  
ATOM    288  CE2BTYR A1041      -1.601  15.225  23.912  0.50 23.59           C  
ANISOU  288  CE2BTYR A1041     1492   4426   3046    864    983   -403       C  
ATOM    289  CZ ATYR A1041       0.748  17.770  23.870  0.50 27.41           C  
ANISOU  289  CZ ATYR A1041     2202   4706   3508    280    723   -684       C  
ATOM    290  CZ BTYR A1041      -1.127  16.453  24.334  0.50 25.09           C  
ANISOU  290  CZ BTYR A1041     1791   4347   3395    900   1093   -381       C  
ATOM    291  OH ATYR A1041       0.591  18.944  24.564  0.50 29.19           O  
ANISOU  291  OH ATYR A1041     2313   4813   3962    118    728   -829       O  
ATOM    292  OH BTYR A1041      -1.887  17.223  25.190  0.50 25.88           O  
ANISOU  292  OH BTYR A1041     1993   4142   3698    988   1421   -318       O  
ATOM    293  N   LYS A1042       1.020  11.495  23.541  1.00 19.06           N  
ANISOU  293  N   LYS A1042     1042   3758   2442   -489    806   -247       N  
ATOM    294  CA  LYS A1042       0.528  10.800  24.734  1.00 20.22           C  
ANISOU  294  CA  LYS A1042     1386   3831   2467   -790    891   -386       C  
ATOM    295  C   LYS A1042       1.678  10.362  25.634  1.00 19.20           C  
ANISOU  295  C   LYS A1042     1500   3607   2187   -652    926   -364       C  
ATOM    296  O   LYS A1042       1.616  10.499  26.857  1.00 20.16           O  
ANISOU  296  O   LYS A1042     1404   4027   2228   -740    961   -392       O  
ATOM    297  CB  LYS A1042      -0.330   9.591  24.334  1.00 21.89           C  
ANISOU  297  CB  LYS A1042     1571   3894   2854   -929    850   -401       C  
ATOM    298  CG  LYS A1042      -0.797   8.743  25.523  1.00 26.76           C  
ANISOU  298  CG  LYS A1042     2311   4259   3596  -1500   1032   -427       C  
ATOM    299  CD  LYS A1042      -2.112   8.040  25.246  1.00 34.34           C  
ANISOU  299  CD  LYS A1042     3316   5109   4623  -2166   1190   -491       C  
ATOM    300  CE  LYS A1042      -2.525   7.166  26.421  1.00 36.89           C  
ANISOU  300  CE  LYS A1042     3702   5353   4960  -2483   1238   -489       C  
ATOM    301  NZ  LYS A1042      -2.532   7.883  27.734  1.00 37.59           N  
ANISOU  301  NZ  LYS A1042     3603   5648   5030  -2469   1360   -511       N  
ATOM    302  N   ASN A1043       2.755   9.855  25.023  1.00 18.59           N  
ANISOU  302  N   ASN A1043     1623   3425   2017   -467    930   -230       N  
ATOM    303  CA  ASN A1043       3.910   9.452  25.807  1.00 18.14           C  
ANISOU  303  CA  ASN A1043     1788   3095   2010   -348    873   -219       C  
ATOM    304  C   ASN A1043       4.485  10.651  26.576  1.00 17.43           C  
ANISOU  304  C   ASN A1043     1743   3000   1879   -320    860   -164       C  
ATOM    305  O   ASN A1043       4.966  10.500  27.711  1.00 18.63           O  
ANISOU  305  O   ASN A1043     1851   3233   1993   -353    715    -63       O  
ATOM    306  CB  ASN A1043       5.006   8.845  24.918  1.00 18.46           C  
ANISOU  306  CB  ASN A1043     1949   3088   1976   -320    921   -263       C  
ATOM    307  CG  ASN A1043       4.577   7.588  24.166  1.00 19.82           C  
ANISOU  307  CG  ASN A1043     2132   3059   2338   -471   1076   -241       C  
ATOM    308  OD1 ASN A1043       3.698   6.814  24.590  1.00 23.49           O  
ANISOU  308  OD1 ASN A1043     2721   3422   2782   -834   1289   -175       O  
ATOM    309  ND2 ASN A1043       5.230   7.357  23.043  1.00 21.05           N  
ANISOU  309  ND2 ASN A1043     2806   3032   2161   -509   1216   -317       N  
ATOM    310  N   ALA A1044       4.440  11.841  25.959  1.00 16.59           N  
ANISOU  310  N   ALA A1044     1263   2978   2064   -206    854   -203       N  
ATOM    311  CA  ALA A1044       4.961  13.040  26.648  1.00 16.89           C  
ANISOU  311  CA  ALA A1044     1262   2996   2161   -161    876   -274       C  
ATOM    312  C   ALA A1044       4.076  13.386  27.849  1.00 17.61           C  
ANISOU  312  C   ALA A1044     1084   3368   2240   -274    886   -467       C  
ATOM    313  O   ALA A1044       4.560  13.723  28.939  1.00 18.47           O  
ANISOU  313  O   ALA A1044     1168   3576   2273   -322    820   -469       O  
ATOM    314  CB  ALA A1044       5.056  14.211  25.693  1.00 16.99           C  
ANISOU  314  CB  ALA A1044     1206   2935   2316    -35    693   -184       C  
ATOM    315  N   MET A1045       2.765  13.301  27.647  1.00 18.92           N  
ANISOU  315  N   MET A1045     1124   3740   2325   -372   1032   -568       N  
ATOM    316  CA  MET A1045       1.820  13.582  28.734  1.00 20.47           C  
ANISOU  316  CA  MET A1045     1253   4149   2374   -366   1039   -610       C  
ATOM    317  C   MET A1045       1.975  12.598  29.893  1.00 21.18           C  
ANISOU  317  C   MET A1045     1553   4129   2365   -493   1128   -577       C  
ATOM    318  O   MET A1045       1.778  12.966  31.048  1.00 22.17           O  
ANISOU  318  O   MET A1045     1712   4262   2450   -564   1212   -630       O  
ATOM    319  CB  MET A1045       0.385  13.598  28.201  1.00 21.53           C  
ANISOU  319  CB  MET A1045     1289   4415   2477   -348    951   -666       C  
ATOM    320  CG  MET A1045       0.104  14.683  27.167  1.00 21.67           C  
ANISOU  320  CG  MET A1045      775   4620   2838   -388    693   -612       C  
ATOM    321  SD  MET A1045       0.587  16.361  27.598  1.00 26.38           S  
ANISOU  321  SD  MET A1045     1492   4747   3783    282    597   -934       S  
ATOM    322  CE  MET A1045       2.169  16.532  26.750  1.00 25.37           C  
ANISOU  322  CE  MET A1045     1133   4424   4083   -140    432   -671       C  
ATOM    323  N   ASP A1046       2.352  11.361  29.570  1.00 21.77           N  
ANISOU  323  N   ASP A1046     1897   3968   2406   -749   1186   -452       N  
ATOM    324  CA  ASP A1046       2.556  10.312  30.567  1.00 22.83           C  
ANISOU  324  CA  ASP A1046     2150   4054   2469   -869   1199   -274       C  
ATOM    325  C   ASP A1046       3.967  10.279  31.139  1.00 23.32           C  
ANISOU  325  C   ASP A1046     2293   3973   2592   -842   1067   -182       C  
ATOM    326  O   ASP A1046       4.257   9.492  32.050  1.00 24.36           O  
ANISOU  326  O   ASP A1046     2329   4241   2685   -903   1023   -113       O  
ATOM    327  CB  ASP A1046       2.222   8.940  29.969  1.00 23.87           C  
ANISOU  327  CB  ASP A1046     2398   4072   2599   -948   1186   -197       C  
ATOM    328  CG  ASP A1046       0.752   8.796  29.631  1.00 25.17           C  
ANISOU  328  CG  ASP A1046     2381   4645   2538  -1164   1412   -342       C  
ATOM    329  OD1 ASP A1046      -0.068   9.513  30.247  1.00 29.86           O  
ANISOU  329  OD1 ASP A1046     2763   5508   3075  -1127   1576   -505       O  
ATOM    330  OD2 ASP A1046       0.415   7.978  28.743  1.00 26.57           O  
ANISOU  330  OD2 ASP A1046     2529   4702   2865  -1286   1324   -355       O  
ATOM    331  N   ALA A1047       4.831  11.146  30.622  1.00 22.61           N  
ANISOU  331  N   ALA A1047     2221   3984   2386   -781    986   -197       N  
ATOM    332  CA  ALA A1047       6.226  11.200  31.042  1.00 22.15           C  
ANISOU  332  CA  ALA A1047     2310   3885   2222   -595    913   -109       C  
ATOM    333  C   ALA A1047       6.403  11.304  32.559  1.00 23.00           C  
ANISOU  333  C   ALA A1047     2698   3880   2161   -502    850   -118       C  
ATOM    334  O   ALA A1047       7.154  10.526  33.142  1.00 23.48           O  
ANISOU  334  O   ALA A1047     2718   4002   2203   -392    878    -82       O  
ATOM    335  CB  ALA A1047       6.971  12.326  30.330  1.00 22.10           C  
ANISOU  335  CB  ALA A1047     2230   3901   2266   -615    776     10       C  
ATOM    336  N   PRO A1048       5.718  12.257  33.207  1.00 24.16           N  
ANISOU  336  N   PRO A1048     2971   4065   2143   -375    860   -227       N  
ATOM    337  CA  PRO A1048       5.928  12.421  34.655  1.00 25.88           C  
ANISOU  337  CA  PRO A1048     3431   4237   2167   -163    882   -230       C  
ATOM    338  C   PRO A1048       5.686  11.160  35.496  1.00 27.51           C  
ANISOU  338  C   PRO A1048     3795   4402   2257    120    996    -38       C  
ATOM    339  O   PRO A1048       6.316  10.990  36.547  1.00 28.55           O  
ANISOU  339  O   PRO A1048     3943   4666   2240    204    974    -35       O  
ATOM    340  CB  PRO A1048       4.924  13.524  35.024  1.00 25.82           C  
ANISOU  340  CB  PRO A1048     3433   4203   2175   -197    895   -274       C  
ATOM    341  CG  PRO A1048       4.807  14.326  33.746  1.00 25.01           C  
ANISOU  341  CG  PRO A1048     3249   4144   2108   -351    763   -359       C  
ATOM    342  CD  PRO A1048       4.773  13.264  32.685  1.00 24.06           C  
ANISOU  342  CD  PRO A1048     3009   3930   2201   -436    776   -285       C  
ATOM    343  N   SER A1049       4.813  10.266  35.034  1.00 27.83           N  
ANISOU  343  N   SER A1049     3759   4327   2489    263   1190    216       N  
ATOM    344  CA ASER A1049       4.483   9.049  35.777  0.50 28.62           C  
ANISOU  344  CA ASER A1049     3957   4347   2572    285   1305    320       C  
ATOM    345  CA BSER A1049       4.461   9.048  35.763  0.50 28.79           C  
ANISOU  345  CA BSER A1049     3905   4347   2685    305   1208    438       C  
ATOM    346  C   SER A1049       5.167   7.794  35.242  1.00 28.90           C  
ANISOU  346  C   SER A1049     4117   4298   2567    302   1342    436       C  
ATOM    347  O   SER A1049       4.951   6.686  35.759  1.00 28.92           O  
ANISOU  347  O   SER A1049     4052   4287   2651    261   1404    449       O  
ATOM    348  CB ASER A1049       2.971   8.824  35.803  0.50 28.69           C  
ANISOU  348  CB ASER A1049     3901   4314   2687    263   1324    361       C  
ATOM    349  CB BSER A1049       2.945   8.853  35.708  0.50 29.08           C  
ANISOU  349  CB BSER A1049     3822   4379   2849    274   1208    511       C  
ATOM    350  OG ASER A1049       2.346   9.783  36.633  0.50 29.61           O  
ANISOU  350  OG ASER A1049     3853   4623   2773    219   1366    205       O  
ATOM    351  OG BSER A1049       2.565   7.633  36.313  0.50 30.66           O  
ANISOU  351  OG BSER A1049     3919   4474   3257    247    917    700       O  
ATOM    352  N   SER A1050       5.994   7.983  34.215  1.00 29.64           N  
ANISOU  352  N   SER A1050     4462   4329   2469    206   1491    368       N  
ATOM    353  CA  SER A1050       6.733   6.889  33.599  1.00 30.90           C  
ANISOU  353  CA  SER A1050     4708   4462   2569    208   1289    386       C  
ATOM    354  C   SER A1050       7.679   6.160  34.547  1.00 32.23           C  
ANISOU  354  C   SER A1050     4942   4535   2768     54   1171    592       C  
ATOM    355  O   SER A1050       8.201   6.747  35.494  1.00 32.55           O  
ANISOU  355  O   SER A1050     4787   4738   2842     73   1168    568       O  
ATOM    356  CB  SER A1050       7.592   7.432  32.447  1.00 29.90           C  
ANISOU  356  CB  SER A1050     4625   4417   2319    296   1365    313       C  
ATOM    357  OG  SER A1050       8.520   6.459  32.001  1.00 31.06           O  
ANISOU  357  OG  SER A1050     4539   4674   2590    434   1111    370       O  
ATOM    358  N   GLU A1051       7.907   4.878  34.262  1.00 34.10           N  
ANISOU  358  N   GLU A1051     5278   4375   3303   -171    744    882       N  
ATOM    359  CA  GLU A1051       8.893   4.072  34.983  1.00 35.15           C  
ANISOU  359  CA  GLU A1051     5605   4329   3420   -241    548   1096       C  
ATOM    360  C   GLU A1051      10.280   4.721  34.903  1.00 33.70           C  
ANISOU  360  C   GLU A1051     5375   4401   3030    -65    509   1146       C  
ATOM    361  O   GLU A1051      11.125   4.517  35.782  1.00 34.43           O  
ANISOU  361  O   GLU A1051     5493   4638   2949    -93    423   1199       O  
ATOM    362  CB  GLU A1051       8.938   2.649  34.423  1.00 36.14           C  
ANISOU  362  CB  GLU A1051     5849   4223   3659   -353    540   1168       C  
ATOM    363  CG  GLU A1051       7.623   1.888  34.559  1.00 39.64           C  
ANISOU  363  CG  GLU A1051     6452   4426   4185   -555    623   1031       C  
ATOM    364  CD  GLU A1051       7.346   1.498  35.995  1.00 43.57           C  
ANISOU  364  CD  GLU A1051     7099   4767   4690   -754   1014    979       C  
ATOM    365  OE1 GLU A1051       6.515   2.162  36.653  1.00 45.67           O  
ANISOU  365  OE1 GLU A1051     7257   5077   5019   -768   1074    803       O  
ATOM    366  OE2 GLU A1051       7.977   0.524  36.468  1.00 45.62           O  
ANISOU  366  OE2 GLU A1051     7529   5041   4765   -619   1092   1053       O  
ATOM    367  N   VAL A1052      10.486   5.496  33.846  1.00 31.35           N  
ANISOU  367  N   VAL A1052     4924   4345   2642    337    653    925       N  
ATOM    368  CA  VAL A1052      11.722   6.227  33.593  1.00 30.26           C  
ANISOU  368  CA  VAL A1052     4706   4305   2486    529    610    767       C  
ATOM    369  C   VAL A1052      11.668   7.595  34.259  1.00 31.01           C  
ANISOU  369  C   VAL A1052     4881   4541   2361    494    384    666       C  
ATOM    370  O   VAL A1052      10.680   8.317  34.106  1.00 31.45           O  
ANISOU  370  O   VAL A1052     4913   4553   2484    540    399    571       O  
ATOM    371  CB  VAL A1052      11.942   6.416  32.071  1.00 29.32           C  
ANISOU  371  CB  VAL A1052     4474   4277   2390    606    759    662       C  
ATOM    372  CG1 VAL A1052      13.241   7.160  31.777  1.00 28.96           C  
ANISOU  372  CG1 VAL A1052     4248   4239   2515    644    825    696       C  
ATOM    373  CG2 VAL A1052      11.917   5.070  31.360  1.00 30.35           C  
ANISOU  373  CG2 VAL A1052     4596   4239   2696    662    623    584       C  
ATOM    374  N   LYS A1053      12.720   7.952  34.991  1.00 32.74           N  
ANISOU  374  N   LYS A1053     5141   4845   2453    350    -54    772       N  
ATOM    375  CA  LYS A1053      12.800   9.283  35.610  1.00 33.63           C  
ANISOU  375  CA  LYS A1053     5138   5134   2504    261   -450    758       C  
ATOM    376  C   LYS A1053      13.408  10.310  34.651  1.00 29.46           C  
ANISOU  376  C   LYS A1053     4250   4758   2187    423   -230    505       C  
ATOM    377  O   LYS A1053      14.600  10.606  34.707  1.00 29.49           O  
ANISOU  377  O   LYS A1053     4099   4917   2187    573   -274    425       O  
ATOM    378  CB  LYS A1053      13.576   9.244  36.940  1.00 36.36           C  
ANISOU  378  CB  LYS A1053     5647   5483   2685    186   -658    908       C  
ATOM    379  CG  LYS A1053      14.676   8.177  37.070  1.00 42.95           C  
ANISOU  379  CG  LYS A1053     6121   6704   3495    227  -1058    895       C  
ATOM    380  CD  LYS A1053      15.928   8.465  36.240  1.00 49.58           C  
ANISOU  380  CD  LYS A1053     6603   8191   4045    428  -1154    732       C  
ATOM    381  CE  LYS A1053      17.036   7.462  36.528  1.00 51.67           C  
ANISOU  381  CE  LYS A1053     6664   8790   4178    516  -1181    544       C  
ATOM    382  NZ  LYS A1053      18.236   7.688  35.670  1.00 52.59           N  
ANISOU  382  NZ  LYS A1053     6751   9114   4117    507  -1212    509       N  
ATOM    383  N   PHE A1054      12.587  10.870  33.768  1.00 24.67           N  
ANISOU  383  N   PHE A1054     3258   4237   1878    379    -10    137       N  
ATOM    384  CA  PHE A1054      13.109  11.819  32.777  1.00 21.19           C  
ANISOU  384  CA  PHE A1054     2381   3941   1728    328     76   -120       C  
ATOM    385  C   PHE A1054      13.603  13.106  33.417  1.00 20.72           C  
ANISOU  385  C   PHE A1054     2034   4041   1797    340    107   -304       C  
ATOM    386  O   PHE A1054      12.924  13.681  34.286  1.00 21.90           O  
ANISOU  386  O   PHE A1054     2117   4131   2073    406    153   -410       O  
ATOM    387  CB  PHE A1054      12.036  12.167  31.737  1.00 19.93           C  
ANISOU  387  CB  PHE A1054     2148   3740   1684    346    153   -141       C  
ATOM    388  CG  PHE A1054      11.725  11.013  30.836  1.00 19.62           C  
ANISOU  388  CG  PHE A1054     2184   3537   1735    285    153    -87       C  
ATOM    389  CD1 PHE A1054      12.622  10.648  29.841  1.00 19.09           C  
ANISOU  389  CD1 PHE A1054     2336   3269   1648    482    305     40       C  
ATOM    390  CD2 PHE A1054      10.553  10.285  30.979  1.00 20.12           C  
ANISOU  390  CD2 PHE A1054     2380   3404   1861    207    419    -31       C  
ATOM    391  CE1 PHE A1054      12.347   9.570  29.006  1.00 20.27           C  
ANISOU  391  CE1 PHE A1054     2354   3400   1949    399    366    -62       C  
ATOM    392  CE2 PHE A1054      10.263   9.212  30.150  1.00 20.71           C  
ANISOU  392  CE2 PHE A1054     2511   3366   1993     63    507    -37       C  
ATOM    393  CZ  PHE A1054      11.164   8.850  29.150  1.00 21.72           C  
ANISOU  393  CZ  PHE A1054     2842   3355   2055    137    562      0       C  
ATOM    394  N   LYS A1055      14.773  13.557  32.970  1.00 20.09           N  
ANISOU  394  N   LYS A1055     1738   4126   1770    370    -70   -282       N  
ATOM    395  CA  LYS A1055      15.242  14.898  33.297  1.00 19.99           C  
ANISOU  395  CA  LYS A1055     1500   4235   1861    272   -252   -296       C  
ATOM    396  C   LYS A1055      14.719  15.891  32.261  1.00 18.40           C  
ANISOU  396  C   LYS A1055     1189   4038   1764    293   -197   -333       C  
ATOM    397  O   LYS A1055      14.354  17.030  32.598  1.00 18.95           O  
ANISOU  397  O   LYS A1055     1164   4104   1932    241    -31   -438       O  
ATOM    398  CB  LYS A1055      16.772  14.965  33.378  1.00 20.97           C  
ANISOU  398  CB  LYS A1055     1527   4336   2106    315   -326   -285       C  
ATOM    399  CG  LYS A1055      17.284  16.355  33.729  1.00 23.84           C  
ANISOU  399  CG  LYS A1055     1737   4717   2606    109   -582   -417       C  
ATOM    400  CD  LYS A1055      18.752  16.374  34.121  1.00 27.22           C  
ANISOU  400  CD  LYS A1055     1773   5044   3524     31   -678   -662       C  
ATOM    401  CE  LYS A1055      19.153  17.785  34.533  1.00 29.92           C  
ANISOU  401  CE  LYS A1055     1817   5292   4259   -285   -684   -794       C  
ATOM    402  NZ  LYS A1055      20.544  17.822  35.076  1.00 33.20           N  
ANISOU  402  NZ  LYS A1055     2319   5572   4722   -197   -750   -974       N  
ATOM    403  N   TYR A1056      14.669  15.444  31.008  1.00 17.19           N  
ANISOU  403  N   TYR A1056      981   3874   1676    148   -141   -230       N  
ATOM    404  CA  TYR A1056      14.303  16.300  29.890  1.00 16.24           C  
ANISOU  404  CA  TYR A1056      770   3664   1738    131    -71   -262       C  
ATOM    405  C   TYR A1056      13.226  15.666  29.028  1.00 15.16           C  
ANISOU  405  C   TYR A1056      664   3334   1761    219    -98   -259       C  
ATOM    406  O   TYR A1056      13.153  14.442  28.909  1.00 16.05           O  
ANISOU  406  O   TYR A1056      847   3258   1993    263   -125   -175       O  
ATOM    407  CB  TYR A1056      15.520  16.540  28.995  1.00 16.38           C  
ANISOU  407  CB  TYR A1056      585   3869   1770     92      6   -285       C  
ATOM    408  CG  TYR A1056      16.623  17.357  29.625  1.00 17.51           C  
ANISOU  408  CG  TYR A1056      675   4110   1867     70     -6   -511       C  
ATOM    409  CD1 TYR A1056      16.473  18.727  29.822  1.00 18.87           C  
ANISOU  409  CD1 TYR A1056      833   4320   2017     97     57   -820       C  
ATOM    410  CD2 TYR A1056      17.820  16.767  29.998  1.00 19.48           C  
ANISOU  410  CD2 TYR A1056     1084   4316   2002    195   -207   -544       C  
ATOM    411  CE1 TYR A1056      17.471  19.485  30.395  1.00 20.50           C  
ANISOU  411  CE1 TYR A1056     1075   4435   2280    109    -65   -750       C  
ATOM    412  CE2 TYR A1056      18.826  17.516  30.564  1.00 20.02           C  
ANISOU  412  CE2 TYR A1056      971   4528   2108    -35   -131   -820       C  
ATOM    413  CZ  TYR A1056      18.653  18.874  30.753  1.00 20.72           C  
ANISOU  413  CZ  TYR A1056      863   4623   2386    107   -141   -825       C  
ATOM    414  OH  TYR A1056      19.667  19.617  31.315  1.00 23.83           O  
ANISOU  414  OH  TYR A1056     1324   4949   2779   -252   -307   -746       O  
ATOM    415  N   VAL A1057      12.400  16.517  28.422  1.00 15.04           N  
ANISOU  415  N   VAL A1057      604   3269   1843    263    -93   -344       N  
ATOM    416  CA  VAL A1057      11.561  16.144  27.281  1.00 14.89           C  
ANISOU  416  CA  VAL A1057      623   3264   1771    109     -5   -302       C  
ATOM    417  C   VAL A1057      11.859  17.145  26.157  1.00 14.16           C  
ANISOU  417  C   VAL A1057      482   3125   1773    -23     43   -370       C  
ATOM    418  O   VAL A1057      11.823  18.373  26.398  1.00 15.59           O  
ANISOU  418  O   VAL A1057      759   3190   1976    -87     35   -395       O  
ATOM    419  CB  VAL A1057      10.062  16.165  27.662  1.00 15.50           C  
ANISOU  419  CB  VAL A1057      705   3336   1849     -3     31   -274       C  
ATOM    420  CG1 VAL A1057       9.175  16.008  26.421  1.00 16.66           C  
ANISOU  420  CG1 VAL A1057      498   3804   2029    313     49   -392       C  
ATOM    421  CG2 VAL A1057       9.749  15.047  28.638  1.00 16.87           C  
ANISOU  421  CG2 VAL A1057     1123   3289   1999    -70    219   -205       C  
ATOM    422  N   LEU A1058      12.158  16.612  24.966  1.00 13.51           N  
ANISOU  422  N   LEU A1058      426   2969   1738    -15      6   -280       N  
ATOM    423  CA  LEU A1058      12.355  17.447  23.801  1.00 13.34           C  
ANISOU  423  CA  LEU A1058      260   2998   1808     88     65   -230       C  
ATOM    424  C   LEU A1058      11.042  17.431  22.993  1.00 12.88           C  
ANISOU  424  C   LEU A1058      263   2883   1747     52    112   -210       C  
ATOM    425  O   LEU A1058      10.702  16.444  22.356  1.00 13.17           O  
ANISOU  425  O   LEU A1058      269   2880   1853      0    160   -240       O  
ATOM    426  CB  LEU A1058      13.550  16.932  22.981  1.00 14.47           C  
ANISOU  426  CB  LEU A1058      306   3172   2020    113    162   -283       C  
ATOM    427  CG  LEU A1058      13.865  17.721  21.731  1.00 16.30           C  
ANISOU  427  CG  LEU A1058      307   3503   2381    194    295    -60       C  
ATOM    428  CD1 LEU A1058      14.176  19.165  22.074  1.00 20.08           C  
ANISOU  428  CD1 LEU A1058     1246   3709   2673    252    599    -97       C  
ATOM    429  CD2 LEU A1058      15.092  17.060  21.074  1.00 19.02           C  
ANISOU  429  CD2 LEU A1058      421   4025   2779    296    606     38       C  
ATOM    430  N   ASN A1059      10.344  18.555  23.078  1.00 13.42           N  
ANISOU  430  N   ASN A1059      269   2935   1896     74    148    -54       N  
ATOM    431  CA  ASN A1059       9.053  18.750  22.429  1.00 13.06           C  
ANISOU  431  CA  ASN A1059      281   2944   1738     92    186   -118       C  
ATOM    432  C   ASN A1059       9.293  19.376  21.052  1.00 12.83           C  
ANISOU  432  C   ASN A1059      286   2754   1835    105    210    -74       C  
ATOM    433  O   ASN A1059       9.641  20.548  20.957  1.00 13.51           O  
ANISOU  433  O   ASN A1059      306   2795   2034     93    294    -43       O  
ATOM    434  CB  ASN A1059       8.207  19.687  23.289  1.00 13.61           C  
ANISOU  434  CB  ASN A1059      281   3025   1863    172    148   -215       C  
ATOM    435  CG  ASN A1059       6.924  20.139  22.593  1.00 13.59           C  
ANISOU  435  CG  ASN A1059      346   3124   1692    252    306   -125       C  
ATOM    436  OD1 ASN A1059       6.456  19.491  21.650  1.00 14.91           O  
ANISOU  436  OD1 ASN A1059      377   3402   1888    217    401   -249       O  
ATOM    437  ND2 ASN A1059       6.388  21.267  23.040  1.00 15.20           N  
ANISOU  437  ND2 ASN A1059      410   3055   2310     76    555   -204       N  
ATOM    438  N   LEU A1060       9.076  18.578  20.012  1.00 13.22           N  
ANISOU  438  N   LEU A1060      276   2991   1755     57    175   -126       N  
ATOM    439  CA  LEU A1060       9.279  19.005  18.636  1.00 14.22           C  
ANISOU  439  CA  LEU A1060      284   3124   1995    283     48   -206       C  
ATOM    440  C   LEU A1060       7.978  19.475  17.990  1.00 14.55           C  
ANISOU  440  C   LEU A1060      302   3269   1958    353     98    -92       C  
ATOM    441  O   LEU A1060       7.965  19.838  16.815  1.00 14.86           O  
ANISOU  441  O   LEU A1060      289   3346   2011    285    109   -118       O  
ATOM    442  CB  LEU A1060       9.864  17.858  17.807  1.00 14.16           C  
ANISOU  442  CB  LEU A1060      298   3025   2055    349     26   -170       C  
ATOM    443  CG  LEU A1060      11.384  17.697  17.741  1.00 20.88           C  
ANISOU  443  CG  LEU A1060      593   3483   3858    417    -31   -715       C  
ATOM    444  CD1 LEU A1060      12.085  18.546  18.787  1.00 19.64           C  
ANISOU  444  CD1 LEU A1060      483   3379   3600    571   -206   -586       C  
ATOM    445  CD2 LEU A1060      11.767  16.233  17.879  1.00 19.00           C  
ANISOU  445  CD2 LEU A1060      408   3424   3388    623    -54   -803       C  
ATOM    446  N   THR A1061       6.882  19.463  18.745  1.00 15.20           N  
ANISOU  446  N   THR A1061      344   3194   2238    423    219   -142       N  
ATOM    447  CA  THR A1061       5.604  19.940  18.191  1.00 16.25           C  
ANISOU  447  CA  THR A1061      357   3416   2401    502    226      0       C  
ATOM    448  C   THR A1061       5.564  21.461  18.216  1.00 16.50           C  
ANISOU  448  C   THR A1061      386   3418   2465    582    238     15       C  
ATOM    449  O   THR A1061       6.392  22.110  18.869  1.00 17.13           O  
ANISOU  449  O   THR A1061      337   3452   2720    493    148     68       O  
ATOM    450  CB  THR A1061       4.365  19.400  18.955  1.00 16.31           C  
ANISOU  450  CB  THR A1061      313   3459   2423    393    149    -63       C  
ATOM    451  OG1 THR A1061       4.255  20.051  20.229  1.00 17.05           O  
ANISOU  451  OG1 THR A1061      296   3612   2569    266    216   -119       O  
ATOM    452  CG2 THR A1061       4.439  17.899  19.121  1.00 16.82           C  
ANISOU  452  CG2 THR A1061      315   3479   2596    446     23    -11       C  
ATOM    453  N   MET A1062       4.550  22.048  17.572  1.00 17.17           N  
ANISOU  453  N   MET A1062      456   3503   2565    762    263    109       N  
ATOM    454  CA  MET A1062       4.501  23.505  17.496  1.00 18.33           C  
ANISOU  454  CA  MET A1062      611   3671   2682    854    284     68       C  
ATOM    455  C   MET A1062       4.006  24.157  18.790  1.00 19.51           C  
ANISOU  455  C   MET A1062      886   3731   2795    917    377     31       C  
ATOM    456  O   MET A1062       4.286  25.331  19.035  1.00 21.58           O  
ANISOU  456  O   MET A1062     1360   3770   3070    816    524    -65       O  
ATOM    457  CB  MET A1062       3.626  23.964  16.318  1.00 18.54           C  
ANISOU  457  CB  MET A1062      531   3797   2718    974    186    126       C  
ATOM    458  CG  MET A1062       4.263  23.666  14.975  1.00 19.83           C  
ANISOU  458  CG  MET A1062      746   3955   2833    833    119     37       C  
ATOM    459  SD  MET A1062       5.766  24.624  14.686  1.00 21.54           S  
ANISOU  459  SD  MET A1062      741   4246   3197    680    153    260       S  
ATOM    460  CE  MET A1062       5.055  26.247  14.367  1.00 24.35           C  
ANISOU  460  CE  MET A1062      855   4336   4059    675    417    163       C  
ATOM    461  N  AASP A1063       3.285  23.403  19.620  0.50 19.66           N  
ANISOU  461  N  AASP A1063      759   3975   2736    834    472     38       N  
ATOM    462  N  BASP A1063       3.327  23.402  19.639  0.50 19.66           N  
ANISOU  462  N  BASP A1063      758   3975   2736    834    472     38       N  
ATOM    463  CA AASP A1063       2.675  23.958  20.839  0.50 20.18           C  
ANISOU  463  CA AASP A1063      921   3982   2763    737    586      6       C  
ATOM    464  CA BASP A1063       2.711  24.021  20.802  0.50 20.17           C  
ANISOU  464  CA BASP A1063      919   3982   2763    737    586      6       C  
ATOM    465  C  AASP A1063       3.593  23.854  22.058  0.50 19.32           C  
ANISOU  465  C  AASP A1063      876   3743   2723    706    749      6       C  
ATOM    466  C  BASP A1063       3.489  23.844  22.108  0.50 19.33           C  
ANISOU  466  C  BASP A1063      878   3745   2723    706    746      6       C  
ATOM    467  O  AASP A1063       4.143  22.787  22.343  0.50 19.24           O  
ANISOU  467  O  AASP A1063      816   3720   2773    706    789    -17       O  
ATOM    468  O  BASP A1063       3.861  22.731  22.482  0.50 19.36           O  
ANISOU  468  O  BASP A1063      847   3727   2781    706    771    -19       O  
ATOM    469  CB AASP A1063       1.322  23.286  21.135  0.50 20.71           C  
ANISOU  469  CB AASP A1063      974   4151   2745    680    579     31       C  
ATOM    470  CB BASP A1063       1.241  23.622  20.908  0.50 20.69           C  
ANISOU  470  CB BASP A1063      962   4156   2743    680    575     31       C  
ATOM    471  CG AASP A1063       0.621  23.877  22.360  0.50 20.44           C  
ANISOU  471  CG AASP A1063      988   4038   2739    324    502     96       C  
ATOM    472  CG BASP A1063       0.425  24.144  19.737  0.50 20.97           C  
ANISOU  472  CG BASP A1063     1067   4088   2811    351    496     54       C  
ATOM    473  OD1AASP A1063       0.327  25.092  22.362  0.50 21.35           O  
ANISOU  473  OD1AASP A1063      991   4201   2921    296    423    230       O  
ATOM    474  OD1BASP A1063      -0.007  25.316  19.798  0.50 21.49           O  
ANISOU  474  OD1BASP A1063     1115   4111   2939    513    181    228       O  
ATOM    475  OD2AASP A1063       0.346  23.121  23.319  0.50 22.12           O  
ANISOU  475  OD2AASP A1063     1333   4162   2908     87    425    109       O  
ATOM    476  OD2BASP A1063       0.238  23.397  18.749  0.50 21.25           O  
ANISOU  476  OD2BASP A1063      935   4158   2980    205    366     65       O  
ATOM    477  N   LYS A1064       3.742  24.967  22.776  1.00 19.06           N  
ANISOU  477  N   LYS A1064      943   3521   2777    449    917     71       N  
ATOM    478  CA  LYS A1064       4.563  25.007  23.985  1.00 20.33           C  
ANISOU  478  CA  LYS A1064     1429   3393   2903     31    987    147       C  
ATOM    479  C   LYS A1064       3.780  24.632  25.242  1.00 20.33           C  
ANISOU  479  C   LYS A1064     1630   3192   2901     20   1120    175       C  
ATOM    480  O   LYS A1064       3.382  25.498  26.032  1.00 22.68           O  
ANISOU  480  O   LYS A1064     2185   3298   3136     52   1251    124       O  
ATOM    481  CB  LYS A1064       5.193  26.403  24.141  1.00 21.33           C  
ANISOU  481  CB  LYS A1064     1479   3470   3156   -126    992     87       C  
ATOM    482  CG  LYS A1064       6.323  26.480  25.168  1.00 24.80           C  
ANISOU  482  CG  LYS A1064     1967   3826   3630   -186    803   -186       C  
ATOM    483  CD  LYS A1064       6.808  27.906  25.352  1.00 28.42           C  
ANISOU  483  CD  LYS A1064     2335   4097   4368   -350    736   -307       C  
ATOM    484  CE  LYS A1064       7.377  28.511  24.061  1.00 31.73           C  
ANISOU  484  CE  LYS A1064     2847   4338   4870   -272    798   -284       C  
ATOM    485  NZ  LYS A1064       8.621  27.833  23.592  1.00 32.14           N  
ANISOU  485  NZ  LYS A1064     2784   4314   5113   -339    768   -498       N  
ATOM    486  N   TYR A1065       3.587  23.344  25.450  1.00 18.35           N  
ANISOU  486  N   TYR A1065     1061   3082   2829    -15   1000    247       N  
ATOM    487  CA  TYR A1065       2.849  22.870  26.617  1.00 17.78           C  
ANISOU  487  CA  TYR A1065     1034   3039   2682     68    939    192       C  
ATOM    488  C   TYR A1065       3.729  22.921  27.867  1.00 18.03           C  
ANISOU  488  C   TYR A1065     1042   3115   2694     12    988    137       C  
ATOM    489  O   TYR A1065       4.970  23.048  27.780  1.00 18.69           O  
ANISOU  489  O   TYR A1065      972   3282   2847    -40    872     82       O  
ATOM    490  CB  TYR A1065       2.283  21.452  26.367  1.00 17.17           C  
ANISOU  490  CB  TYR A1065      681   3027   2815     87    803    228       C  
ATOM    491  CG  TYR A1065       3.354  20.395  26.276  1.00 16.69           C  
ANISOU  491  CG  TYR A1065      723   3104   2515    181    627    175       C  
ATOM    492  CD1 TYR A1065       3.901  19.788  27.413  1.00 16.44           C  
ANISOU  492  CD1 TYR A1065      462   3395   2388    317    625    131       C  
ATOM    493  CD2 TYR A1065       3.848  20.001  25.039  1.00 15.81           C  
ANISOU  493  CD2 TYR A1065      377   3294   2337    186    493    194       C  
ATOM    494  CE1 TYR A1065       4.900  18.831  27.323  1.00 16.82           C  
ANISOU  494  CE1 TYR A1065      482   3583   2327    296    577     63       C  
ATOM    495  CE2 TYR A1065       4.845  19.041  24.940  1.00 15.58           C  
ANISOU  495  CE2 TYR A1065      308   3292   2318     96    333    131       C  
ATOM    496  CZ  TYR A1065       5.355  18.457  26.073  1.00 16.68           C  
ANISOU  496  CZ  TYR A1065      620   3443   2275    247    599    173       C  
ATOM    497  OH  TYR A1065       6.364  17.524  25.985  1.00 15.76           O  
ANISOU  497  OH  TYR A1065      329   3420   2240    229    236     17       O  
ATOM    498  N   THR A1066       3.095  22.781  29.025  1.00 18.93           N  
ANISOU  498  N   THR A1066     1421   3167   2606     68   1062    118       N  
ATOM    499  CA  THR A1066       3.788  22.629  30.289  1.00 19.73           C  
ANISOU  499  CA  THR A1066     1527   3282   2687    141   1180     82       C  
ATOM    500  C   THR A1066       3.369  21.325  30.965  1.00 18.67           C  
ANISOU  500  C   THR A1066     1322   3303   2469      5   1005    103       C  
ATOM    501  O   THR A1066       2.313  20.746  30.639  1.00 19.44           O  
ANISOU  501  O   THR A1066     1384   3434   2569   -102    952     57       O  
ATOM    502  CB  THR A1066       3.508  23.811  31.243  1.00 20.54           C  
ANISOU  502  CB  THR A1066     1720   3346   2739    109   1185     37       C  
ATOM    503  OG1 THR A1066       2.105  23.854  31.531  1.00 23.21           O  
ANISOU  503  OG1 THR A1066     2017   3585   3215    377   1420     31       O  
ATOM    504  CG2 THR A1066       3.923  25.135  30.622  1.00 22.66           C  
ANISOU  504  CG2 THR A1066     2099   3373   3138    153   1456     35       C  
ATOM    505  N   LEU A1067       4.212  20.864  31.881  1.00 18.09           N  
ANISOU  505  N   LEU A1067     1351   3240   2284     81    850    -13       N  
ATOM    506  CA  LEU A1067       3.894  19.777  32.794  1.00 17.24           C  
ANISOU  506  CA  LEU A1067     1098   3188   2266     65    631   -197       C  
ATOM    507  C   LEU A1067       4.128  20.305  34.208  1.00 17.92           C  
ANISOU  507  C   LEU A1067     1305   3237   2266     63    658   -197       C  
ATOM    508  O   LEU A1067       5.129  19.968  34.852  1.00 19.03           O  
ANISOU  508  O   LEU A1067     1263   3630   2336    -43    590   -258       O  
ATOM    509  CB  LEU A1067       4.787  18.558  32.509  1.00 17.21           C  
ANISOU  509  CB  LEU A1067     1150   3203   2187    120    584   -252       C  
ATOM    510  CG  LEU A1067       4.658  17.945  31.111  1.00 17.52           C  
ANISOU  510  CG  LEU A1067      935   3348   2374     35    438   -294       C  
ATOM    511  CD1 LEU A1067       5.829  17.004  30.836  1.00 19.69           C  
ANISOU  511  CD1 LEU A1067     1342   3463   2675    357    438   -388       C  
ATOM    512  CD2 LEU A1067       3.318  17.227  30.924  1.00 20.43           C  
ANISOU  512  CD2 LEU A1067     1331   3495   2937   -109    186   -318       C  
ATOM    513  N   PRO A1068       3.201  21.148  34.688  1.00 18.93           N  
ANISOU  513  N   PRO A1068     1342   3357   2495     49    838   -271       N  
ATOM    514  CA  PRO A1068       3.458  21.994  35.860  1.00 19.50           C  
ANISOU  514  CA  PRO A1068     1418   3294   2698   -103    934   -296       C  
ATOM    515  C   PRO A1068       3.580  21.232  37.172  1.00 19.79           C  
ANISOU  515  C   PRO A1068     1392   3499   2628   -230    942   -315       C  
ATOM    516  O   PRO A1068       4.112  21.788  38.147  1.00 21.01           O  
ANISOU  516  O   PRO A1068     1428   3716   2840   -342    776   -333       O  
ATOM    517  CB  PRO A1068       2.237  22.924  35.907  1.00 20.58           C  
ANISOU  517  CB  PRO A1068     1523   3388   2908    -30   1018   -401       C  
ATOM    518  CG  PRO A1068       1.151  22.127  35.259  1.00 20.13           C  
ANISOU  518  CG  PRO A1068     1525   3495   2628     -6    926   -313       C  
ATOM    519  CD  PRO A1068       1.834  21.345  34.167  1.00 19.31           C  
ANISOU  519  CD  PRO A1068     1287   3474   2576     70    895   -219       C  
ATOM    520  N   ASN A1069       3.110  19.987  37.194  1.00 18.75           N  
ANISOU  520  N   ASN A1069     1052   3481   2592   -197    876    -63       N  
ATOM    521  CA  ASN A1069       3.225  19.168  38.403  1.00 19.53           C  
ANISOU  521  CA  ASN A1069     1186   3655   2581   -183    741     76       C  
ATOM    522  C   ASN A1069       4.465  18.281  38.421  1.00 19.72           C  
ANISOU  522  C   ASN A1069     1272   3621   2599   -185    634    104       C  
ATOM    523  O   ASN A1069       4.653  17.484  39.327  1.00 21.60           O  
ANISOU  523  O   ASN A1069     1659   3865   2682   -140    619    219       O  
ATOM    524  CB  ASN A1069       1.940  18.360  38.556  1.00 19.24           C  
ANISOU  524  CB  ASN A1069     1076   3562   2671   -120    842    153       C  
ATOM    525  CG  ASN A1069       0.724  19.271  38.472  1.00 19.35           C  
ANISOU  525  CG  ASN A1069     1115   3601   2635    -62    793     68       C  
ATOM    526  OD1 ASN A1069       0.606  20.199  39.262  1.00 20.67           O  
ANISOU  526  OD1 ASN A1069     1168   4077   2610     35    665   -119       O  
ATOM    527  ND2 ASN A1069      -0.148  19.023  37.496  1.00 20.12           N  
ANISOU  527  ND2 ASN A1069      734   3711   3201    -71    652   -218       N  
ATOM    528  N   SER A1070       5.340  18.456  37.431  1.00 19.56           N  
ANISOU  528  N   SER A1070     1106   3734   2592   -230    403   -160       N  
ATOM    529  CA  SER A1070       6.534  17.640  37.251  1.00 19.89           C  
ANISOU  529  CA  SER A1070     1036   3840   2682   -274    237   -410       C  
ATOM    530  C   SER A1070       7.772  18.520  37.305  1.00 20.04           C  
ANISOU  530  C   SER A1070     1036   3986   2594   -263      6   -467       C  
ATOM    531  O   SER A1070       7.683  19.712  37.021  1.00 21.05           O  
ANISOU  531  O   SER A1070     1069   3858   3070   -386    219   -463       O  
ATOM    532  CB  SER A1070       6.454  17.000  35.874  1.00 20.59           C  
ANISOU  532  CB  SER A1070     1186   3810   2829   -130     -6   -595       C  
ATOM    533  OG  SER A1070       7.605  16.285  35.544  1.00 23.24           O  
ANISOU  533  OG  SER A1070     1421   4413   2996   -252    307   -675       O  
ATOM    534  N   ASN A1071       8.918  17.931  37.632  1.00 19.97           N  
ANISOU  534  N   ASN A1071      921   4453   2213   -170    -51   -560       N  
ATOM    535  CA  ASN A1071      10.172  18.683  37.614  1.00 20.71           C  
ANISOU  535  CA  ASN A1071     1054   4805   2011     -3   -120   -579       C  
ATOM    536  C   ASN A1071      10.912  18.495  36.294  1.00 19.30           C  
ANISOU  536  C   ASN A1071     1097   4352   1884    -38      0   -582       C  
ATOM    537  O   ASN A1071      12.077  18.860  36.186  1.00 19.63           O  
ANISOU  537  O   ASN A1071      945   4557   1958    -57    -20   -634       O  
ATOM    538  CB  ASN A1071      11.065  18.313  38.808  1.00 23.16           C  
ANISOU  538  CB  ASN A1071     1368   5307   2124    -10   -170   -386       C  
ATOM    539  CG  ASN A1071      11.522  16.853  38.787  1.00 28.00           C  
ANISOU  539  CG  ASN A1071     2020   6211   2407    658   -392   -185       C  
ATOM    540  OD1 ASN A1071      11.282  16.106  37.835  1.00 31.09           O  
ANISOU  540  OD1 ASN A1071     2533   6521   2757    903   -581    -26       O  
ATOM    541  ND2 ASN A1071      12.188  16.439  39.861  1.00 34.74           N  
ANISOU  541  ND2 ASN A1071     3160   7171   2870   1027   -652     80       N  
ATOM    542  N   ILE A1072      10.237  17.948  35.287  1.00 18.58           N  
ANISOU  542  N   ILE A1072     1162   4117   1779   -109    208   -631       N  
ATOM    543  CA  ILE A1072      10.858  17.738  33.971  1.00 18.45           C  
ANISOU  543  CA  ILE A1072     1186   3986   1840   -208    263   -604       C  
ATOM    544  C   ILE A1072      11.157  19.082  33.313  1.00 18.09           C  
ANISOU  544  C   ILE A1072     1000   3984   1888   -173    370   -640       C  
ATOM    545  O   ILE A1072      10.345  20.009  33.408  1.00 18.64           O  
ANISOU  545  O   ILE A1072      918   3925   2239   -250    412   -627       O  
ATOM    546  CB  ILE A1072       9.946  16.887  33.045  1.00 18.39           C  
ANISOU  546  CB  ILE A1072     1221   3887   1878   -153    216   -590       C  
ATOM    547  CG1 ILE A1072       9.886  15.440  33.545  1.00 19.83           C  
ANISOU  547  CG1 ILE A1072     1474   3921   2140   -252    241   -474       C  
ATOM    548  CG2 ILE A1072      10.395  16.977  31.586  1.00 19.49           C  
ANISOU  548  CG2 ILE A1072     1315   4266   1826   -370    250   -553       C  
ATOM    549  CD1 ILE A1072       8.786  14.599  32.902  1.00 20.79           C  
ANISOU  549  CD1 ILE A1072     1588   3790   2520   -229     27   -335       C  
ATOM    550  N   ASN A1073      12.334  19.197  32.684  1.00 18.03           N  
ANISOU  550  N   ASN A1073      798   4140   1914   -184    285   -606       N  
ATOM    551  CA  ASN A1073      12.642  20.377  31.885  1.00 18.87           C  
ANISOU  551  CA  ASN A1073      961   4047   2161   -230    250   -595       C  
ATOM    552  C   ASN A1073      12.234  20.088  30.456  1.00 17.25           C  
ANISOU  552  C   ASN A1073     1080   3395   2081    -93    238   -516       C  
ATOM    553  O   ASN A1073      12.747  19.141  29.855  1.00 16.70           O  
ANISOU  553  O   ASN A1073      890   3341   2116    -38    119   -533       O  
ATOM    554  CB  ASN A1073      14.135  20.705  31.938  1.00 20.97           C  
ANISOU  554  CB  ASN A1073     1025   4481   2460   -487    241   -648       C  
ATOM    555  CG  ASN A1073      14.515  22.007  31.235  1.00 27.48           C  
ANISOU  555  CG  ASN A1073     1764   5284   3395   -991      0   -362       C  
ATOM    556  OD1 ASN A1073      13.932  22.404  30.227  1.00 33.59           O  
ANISOU  556  OD1 ASN A1073     2476   6118   4169  -1377    -10    -62       O  
ATOM    557  ND2 ASN A1073      15.531  22.680  31.771  1.00 34.28           N  
ANISOU  557  ND2 ASN A1073     2603   5866   4557  -1357   -197   -282       N  
ATOM    558  N   ILE A1074      11.289  20.891  29.946  1.00 16.39           N  
ANISOU  558  N   ILE A1074      986   3176   2064     52    381   -390       N  
ATOM    559  CA  ILE A1074      10.748  20.698  28.598  1.00 16.22           C  
ANISOU  559  CA  ILE A1074      830   3097   2237     48    460   -359       C  
ATOM    560  C   ILE A1074      11.443  21.684  27.647  1.00 15.84           C  
ANISOU  560  C   ILE A1074      938   2980   2099     -5    439   -445       C  
ATOM    561  O   ILE A1074      11.278  22.905  27.773  1.00 17.92           O  
ANISOU  561  O   ILE A1074     1288   3018   2504    -24    644   -458       O  
ATOM    562  CB  ILE A1074       9.212  20.889  28.528  1.00 16.35           C  
ANISOU  562  CB  ILE A1074      761   3106   2345    103    518   -403       C  
ATOM    563  CG1 ILE A1074       8.504  20.010  29.556  1.00 19.34           C  
ANISOU  563  CG1 ILE A1074     1102   3515   2732    107    520   -252       C  
ATOM    564  CG2 ILE A1074       8.705  20.596  27.116  1.00 17.44           C  
ANISOU  564  CG2 ILE A1074      786   3231   2608    -41    296   -296       C  
ATOM    565  CD1 ILE A1074       7.134  20.499  29.937  1.00 20.62           C  
ANISOU  565  CD1 ILE A1074      805   3980   3048     65    571   -489       C  
ATOM    566  N   ILE A1075      12.226  21.138  26.724  1.00 15.47           N  
ANISOU  566  N   ILE A1075      761   3088   2029   -120    307   -419       N  
ATOM    567  CA  ILE A1075      12.890  21.944  25.714  1.00 16.32           C  
ANISOU  567  CA  ILE A1075      636   3404   2161   -225    208   -284       C  
ATOM    568  C   ILE A1075      12.022  21.974  24.468  1.00 15.17           C  
ANISOU  568  C   ILE A1075      474   3106   2184   -195    272   -208       C  
ATOM    569  O   ILE A1075      11.664  20.929  23.926  1.00 15.96           O  
ANISOU  569  O   ILE A1075      505   3199   2361   -147     98   -252       O  
ATOM    570  CB  ILE A1075      14.263  21.359  25.362  1.00 17.27           C  
ANISOU  570  CB  ILE A1075      588   3688   2284   -227    217   -216       C  
ATOM    571  CG1 ILE A1075      15.135  21.280  26.617  1.00 21.44           C  
ANISOU  571  CG1 ILE A1075     1316   4140   2689   -432   -130   -248       C  
ATOM    572  CG2 ILE A1075      14.939  22.197  24.279  1.00 18.95           C  
ANISOU  572  CG2 ILE A1075      780   4023   2398   -366    326   -164       C  
ATOM    573  CD1 ILE A1075      16.016  20.067  26.649  1.00 28.66           C  
ANISOU  573  CD1 ILE A1075     2682   4753   3454   -719   -307   -230       C  
ATOM    574  N   HIS A1076      11.676  23.178  24.029  1.00 15.63           N  
ANISOU  574  N   HIS A1076      514   3106   2319   -159    318   -120       N  
ATOM    575  CA  HIS A1076      10.763  23.335  22.910  1.00 15.70           C  
ANISOU  575  CA  HIS A1076      549   3046   2370     17    474    -68       C  
ATOM    576  C   HIS A1076      11.518  23.741  21.653  1.00 15.26           C  
ANISOU  576  C   HIS A1076      443   2921   2435     10    474    -98       C  
ATOM    577  O   HIS A1076      12.110  24.825  21.595  1.00 16.59           O  
ANISOU  577  O   HIS A1076      691   2926   2685   -193    500    -46       O  
ATOM    578  CB  HIS A1076       9.696  24.374  23.237  1.00 15.76           C  
ANISOU  578  CB  HIS A1076      357   3138   2492      3    480   -173       C  
ATOM    579  CG  HIS A1076       8.581  24.421  22.242  1.00 16.39           C  
ANISOU  579  CG  HIS A1076      500   3222   2506     74    476    -81       C  
ATOM    580  ND1 HIS A1076       7.802  25.542  22.048  1.00 17.73           N  
ANISOU  580  ND1 HIS A1076      741   3321   2675    151    588     -3       N  
ATOM    581  CD2 HIS A1076       8.119  23.487  21.377  1.00 16.39           C  
ANISOU  581  CD2 HIS A1076      406   3291   2529     85    397    -13       C  
ATOM    582  CE1 HIS A1076       6.896  25.292  21.119  1.00 17.83           C  
ANISOU  582  CE1 HIS A1076      744   3413   2617    474    408     31       C  
ATOM    583  NE2 HIS A1076       7.059  24.049  20.703  1.00 17.25           N  
ANISOU  583  NE2 HIS A1076      535   3312   2707    346    392     82       N  
ATOM    584  N   ILE A1077      11.493  22.863  20.655  1.00 14.82           N  
ANISOU  584  N   ILE A1077      359   2980   2293     49    460    -81       N  
ATOM    585  CA  ILE A1077      11.993  23.202  19.323  1.00 16.72           C  
ANISOU  585  CA  ILE A1077      802   3091   2458    183    570   -118       C  
ATOM    586  C   ILE A1077      10.830  23.020  18.348  1.00 15.59           C  
ANISOU  586  C   ILE A1077      834   2754   2335    152    597    -43       C  
ATOM    587  O   ILE A1077      10.599  21.919  17.855  1.00 15.56           O  
ANISOU  587  O   ILE A1077      697   2732   2484    114    603     24       O  
ATOM    588  CB  ILE A1077      13.187  22.317  18.901  1.00 18.44           C  
ANISOU  588  CB  ILE A1077     1005   3370   2632    239    538   -125       C  
ATOM    589  CG1 ILE A1077      14.331  22.416  19.921  1.00 21.16           C  
ANISOU  589  CG1 ILE A1077      878   4097   3064    627    546   -324       C  
ATOM    590  CG2 ILE A1077      13.669  22.724  17.520  1.00 20.81           C  
ANISOU  590  CG2 ILE A1077     1226   3828   2851    204    776   -263       C  
ATOM    591  CD1 ILE A1077      15.527  21.532  19.603  1.00 24.35           C  
ANISOU  591  CD1 ILE A1077     1103   4535   3614    798    630   -317       C  
ATOM    592  N   PRO A1078      10.082  24.097  18.092  1.00 16.61           N  
ANISOU  592  N   PRO A1078      846   2809   2655    197    498   -129       N  
ATOM    593  CA  PRO A1078       8.858  23.954  17.294  1.00 17.29           C  
ANISOU  593  CA  PRO A1078      980   2969   2619    241    412   -230       C  
ATOM    594  C   PRO A1078       9.158  23.680  15.827  1.00 17.59           C  
ANISOU  594  C   PRO A1078     1018   3068   2599    252    454   -208       C  
ATOM    595  O   PRO A1078       9.865  24.470  15.185  1.00 19.28           O  
ANISOU  595  O   PRO A1078     1412   3188   2725     49    494    -76       O  
ATOM    596  CB  PRO A1078       8.152  25.297  17.468  1.00 17.97           C  
ANISOU  596  CB  PRO A1078     1084   2991   2754    252    392   -247       C  
ATOM    597  CG  PRO A1078       9.180  26.247  17.960  1.00 17.19           C  
ANISOU  597  CG  PRO A1078      842   2860   2831    270    405   -181       C  
ATOM    598  CD  PRO A1078      10.226  25.437  18.670  1.00 17.06           C  
ANISOU  598  CD  PRO A1078      922   2791   2768    175    458    -93       C  
ATOM    599  N   LEU A1079       8.650  22.554  15.332  1.00 15.63           N  
ANISOU  599  N   LEU A1079      368   3242   2328    329    348   -205       N  
ATOM    600  CA  LEU A1079       8.786  22.173  13.933  1.00 16.17           C  
ANISOU  600  CA  LEU A1079      359   3440   2345    452    208   -152       C  
ATOM    601  C   LEU A1079       7.425  21.774  13.397  1.00 15.33           C  
ANISOU  601  C   LEU A1079      370   3398   2056    472    266   -114       C  
ATOM    602  O   LEU A1079       6.560  21.348  14.157  1.00 16.02           O  
ANISOU  602  O   LEU A1079      326   3720   2039    432    195     97       O  
ATOM    603  CB  LEU A1079       9.734  20.984  13.794  1.00 16.49           C  
ANISOU  603  CB  LEU A1079      355   3384   2527    410    131   -160       C  
ATOM    604  CG  LEU A1079      11.161  21.187  14.290  1.00 18.33           C  
ANISOU  604  CG  LEU A1079      322   3797   2845    419    228     57       C  
ATOM    605  CD1 LEU A1079      11.847  19.837  14.402  1.00 19.45           C  
ANISOU  605  CD1 LEU A1079      293   3851   3246    320    207    296       C  
ATOM    606  CD2 LEU A1079      11.901  22.100  13.329  1.00 21.85           C  
ANISOU  606  CD2 LEU A1079      893   3914   3495    230    348    249       C  
ATOM    607  N   VAL A1080       7.263  21.904  12.085  1.00 15.82           N  
ANISOU  607  N   VAL A1080      395   3596   2018    383    219    -63       N  
ATOM    608  CA  VAL A1080       6.085  21.383  11.388  1.00 16.27           C  
ANISOU  608  CA  VAL A1080      518   3574   2090    511    109    -38       C  
ATOM    609  C   VAL A1080       6.434  20.090  10.640  1.00 15.97           C  
ANISOU  609  C   VAL A1080      392   3560   2116    535     74    -12       C  
ATOM    610  O   VAL A1080       7.499  19.969  10.028  1.00 17.00           O  
ANISOU  610  O   VAL A1080      436   3759   2265    573    196    -63       O  
ATOM    611  CB  VAL A1080       5.481  22.418  10.409  1.00 17.46           C  
ANISOU  611  CB  VAL A1080      821   3564   2249    524     31     -3       C  
ATOM    612  CG1 VAL A1080       4.240  21.846   9.737  1.00 19.03           C  
ANISOU  612  CG1 VAL A1080      766   3907   2558    584   -120      5       C  
ATOM    613  CG2 VAL A1080       5.111  23.710  11.135  1.00 19.43           C  
ANISOU  613  CG2 VAL A1080     1280   3583   2520    581    186     12       C  
ATOM    614  N   ASP A1081       5.539  19.107  10.674  1.00 15.65           N  
ANISOU  614  N   ASP A1081      331   3630   1985    509     31     -5       N  
ATOM    615  CA  ASP A1081       5.693  17.888   9.883  1.00 15.85           C  
ANISOU  615  CA  ASP A1081      443   3763   1817    571     54     43       C  
ATOM    616  C   ASP A1081       5.130  18.142   8.492  1.00 17.12           C  
ANISOU  616  C   ASP A1081      571   4142   1791    798     73     65       C  
ATOM    617  O   ASP A1081       3.948  17.885   8.230  1.00 18.48           O  
ANISOU  617  O   ASP A1081      434   4481   2108    863    -68     98       O  
ATOM    618  CB  ASP A1081       5.002  16.702  10.554  1.00 15.96           C  
ANISOU  618  CB  ASP A1081      331   3689   2043    516     24     41       C  
ATOM    619  CG  ASP A1081       5.144  15.409   9.770  1.00 15.78           C  
ANISOU  619  CG  ASP A1081      309   3765   1921    443    -24     41       C  
ATOM    620  OD1 ASP A1081       6.001  15.325   8.835  1.00 17.87           O  
ANISOU  620  OD1 ASP A1081      557   4205   2027    551    274    -31       O  
ATOM    621  OD2 ASP A1081       4.441  14.435  10.120  1.00 17.70           O  
ANISOU  621  OD2 ASP A1081      308   3772   2646    421    105      0       O  
ATOM    622  N   ASP A1082       5.949  18.697   7.611  1.00 18.82           N  
ANISOU  622  N   ASP A1082      930   4431   1788   1164    129    159       N  
ATOM    623  CA  ASP A1082       5.527  18.915   6.236  1.00 22.20           C  
ANISOU  623  CA  ASP A1082     1356   5156   1923   1824    241    373       C  
ATOM    624  C   ASP A1082       6.715  18.741   5.312  1.00 23.91           C  
ANISOU  624  C   ASP A1082     1570   5697   1817   2011    252    487       C  
ATOM    625  O   ASP A1082       7.840  18.548   5.771  1.00 22.05           O  
ANISOU  625  O   ASP A1082     1212   5281   1885   1629     91    368       O  
ATOM    626  CB  ASP A1082       4.906  20.304   6.064  1.00 24.70           C  
ANISOU  626  CB  ASP A1082     1914   5144   2328   1905    285    469       C  
ATOM    627  CG  ASP A1082       5.907  21.423   6.272  1.00 28.61           C  
ANISOU  627  CG  ASP A1082     2433   5120   3316   2046    529    612       C  
ATOM    628  OD1 ASP A1082       7.116  21.187   6.077  1.00 32.19           O  
ANISOU  628  OD1 ASP A1082     2772   5008   4449   1985    930    815       O  
ATOM    629  OD2 ASP A1082       5.484  22.542   6.630  1.00 32.66           O  
ANISOU  629  OD2 ASP A1082     2813   5310   4286   2081    842    724       O  
ATOM    630  N   THR A1083       6.470  18.787   4.010  1.00 28.33           N  
ANISOU  630  N   THR A1083     1967   7041   1756   2388    252    540       N  
ATOM    631  CA  THR A1083       7.529  18.440   3.066  1.00 32.64           C  
ANISOU  631  CA  THR A1083     2610   7911   1879   2691    417    617       C  
ATOM    632  C   THR A1083       8.364  19.672   2.674  1.00 33.91           C  
ANISOU  632  C   THR A1083     2694   8093   2097   2930    520    908       C  
ATOM    633  O   THR A1083       9.265  19.568   1.836  1.00 34.76           O  
ANISOU  633  O   THR A1083     2554   8403   2249   3064    617    986       O  
ATOM    634  CB  THR A1083       6.991  17.650   1.846  1.00 33.50           C  
ANISOU  634  CB  THR A1083     2775   8011   1941   2709    296    502       C  
ATOM    635  OG1 THR A1083       5.870  18.328   1.284  1.00 34.07           O  
ANISOU  635  OG1 THR A1083     2894   7997   2055   2608    285    456       O  
ATOM    636  CG2 THR A1083       6.532  16.253   2.278  1.00 35.03           C  
ANISOU  636  CG2 THR A1083     3152   8008   2149   2748    337    386       C  
ATOM    637  N   THR A1084       8.108  20.804   3.339  1.00 36.15           N  
ANISOU  637  N   THR A1084     3251   7713   2772   3237    850   1280       N  
ATOM    638  CA  THR A1084       8.807  22.071   3.073  1.00 38.29           C  
ANISOU  638  CA  THR A1084     3943   7135   3472   3337   1168   1551       C  
ATOM    639  C   THR A1084       9.799  22.536   4.169  1.00 36.95           C  
ANISOU  639  C   THR A1084     3847   6420   3772   3000   1448   1578       C  
ATOM    640  O   THR A1084      10.773  23.229   3.871  1.00 38.69           O  
ANISOU  640  O   THR A1084     4122   6402   4176   2937   1553   1805       O  
ATOM    641  CB  THR A1084       7.802  23.206   2.702  1.00 39.78           C  
ANISOU  641  CB  THR A1084     4194   7322   3598   3452   1133   1597       C  
ATOM    642  OG1 THR A1084       8.376  24.055   1.699  1.00 41.75           O  
ANISOU  642  OG1 THR A1084     4629   7336   3898   3330   1023   1624       O  
ATOM    643  CG2 THR A1084       7.408  24.039   3.927  1.00 39.99           C  
ANISOU  643  CG2 THR A1084     4259   7206   3731   3646    930   1518       C  
ATOM    644  N   THR A1085       9.582  22.110   5.411  1.00 33.95           N  
ANISOU  644  N   THR A1085     3583   5618   3700   2583   1462   1230       N  
ATOM    645  CA  THR A1085      10.409  22.547   6.541  1.00 30.96           C  
ANISOU  645  CA  THR A1085     3253   4884   3625   1967   1456    811       C  
ATOM    646  C   THR A1085      11.836  21.992   6.512  1.00 27.45           C  
ANISOU  646  C   THR A1085     3097   4004   3330   1553   1401    570       C  
ATOM    647  O   THR A1085      12.042  20.815   6.228  1.00 26.52           O  
ANISOU  647  O   THR A1085     2989   3819   3269   1473   1368    586       O  
ATOM    648  CB  THR A1085       9.769  22.156   7.889  1.00 32.57           C  
ANISOU  648  CB  THR A1085     3337   5464   3576   2108   1490    780       C  
ATOM    649  OG1 THR A1085       8.697  23.056   8.191  1.00 34.81           O  
ANISOU  649  OG1 THR A1085     3576   5727   3925   2117   1395    701       O  
ATOM    650  CG2 THR A1085      10.799  22.206   9.009  1.00 33.37           C  
ANISOU  650  CG2 THR A1085     3307   5539   3833   1958   1532    789       C  
ATOM    651  N  AASP A1086      12.783  22.838   6.500  0.50 26.21           N  
ANISOU  651  N  AASP A1086     3125   3614   3219   1324   1230    526       N  
ATOM    652  N  BASP A1086      12.812  22.844   6.827  0.50 26.36           N  
ANISOU  652  N  BASP A1086     3140   3580   3294   1254   1411    485       N  
ATOM    653  CA AASP A1086      14.099  22.434   6.969  0.50 24.01           C  
ANISOU  653  CA AASP A1086     2858   3264   3000   1026   1168    474       C  
ATOM    654  CA BASP A1086      14.211  22.424   6.927  0.50 24.42           C  
ANISOU  654  CA BASP A1086     3034   3143   3102    864   1303    460       C  
ATOM    655  C  AASP A1086      14.021  21.979   8.419  0.50 21.54           C  
ANISOU  655  C  AASP A1086     2405   3082   2696    719    838    274       C  
ATOM    656  C  BASP A1086      14.615  22.031   8.345  0.50 22.57           C  
ANISOU  656  C  BASP A1086     2694   3041   2842    476   1026    241       C  
ATOM    657  O  AASP A1086      13.553  22.715   9.288  0.50 19.63           O  
ANISOU  657  O  AASP A1086     1693   3023   2743    700    785    296       O  
ATOM    658  O  BASP A1086      15.071  22.866   9.127  0.50 22.27           O  
ANISOU  658  O  BASP A1086     2560   2975   2926    153   1062    230       O  
ATOM    659  CB AASP A1086      15.106  23.575   6.822  0.50 25.56           C  
ANISOU  659  CB AASP A1086     3161   3366   3185   1076   1386    489       C  
ATOM    660  CB BASP A1086      15.152  23.521   6.427  0.50 25.52           C  
ANISOU  660  CB BASP A1086     3264   3143   3289    952   1500    540       C  
ATOM    661  CG AASP A1086      16.498  23.182   7.267  0.50 27.04           C  
ANISOU  661  CG AASP A1086     3316   3528   3429    939   1518    597       C  
ATOM    662  CG BASP A1086      16.612  23.218   6.730  0.50 25.97           C  
ANISOU  662  CG BASP A1086     3472   2842   3555    847   1430    768       C  
ATOM    663  OD1AASP A1086      17.026  23.821   8.198  0.50 29.52           O  
ANISOU  663  OD1AASP A1086     3576   4056   3585    829   1676    579       O  
ATOM    664  OD1BASP A1086      16.981  22.027   6.745  0.50 27.24           O  
ANISOU  664  OD1BASP A1086     3576   2888   3885    762   1656    847       O  
ATOM    665  OD2AASP A1086      17.061  22.229   6.691  0.50 29.27           O  
ANISOU  665  OD2AASP A1086     3431   3984   3707   1098   1553    533       O  
ATOM    666  OD2BASP A1086      17.392  24.168   6.950  0.50 26.62           O  
ANISOU  666  OD2BASP A1086     3562   2833   3720    684   1518    855       O  
ATOM    667  N   ILE A1087      14.467  20.754   8.667  1.00 18.79           N  
ANISOU  667  N   ILE A1087     1720   3000   2421    373    533    153       N  
ATOM    668  CA  ILE A1087      14.739  20.281  10.026  1.00 17.74           C  
ANISOU  668  CA  ILE A1087     1166   3228   2347    -12    131     43       C  
ATOM    669  C   ILE A1087      16.247  20.152  10.237  1.00 16.48           C  
ANISOU  669  C   ILE A1087      900   3176   2187    -35    192   -147       C  
ATOM    670  O   ILE A1087      16.716  20.108  11.374  1.00 16.21           O  
ANISOU  670  O   ILE A1087      719   3226   2213   -208     80   -184       O  
ATOM    671  CB  ILE A1087      14.003  18.962  10.338  1.00 18.11           C  
ANISOU  671  CB  ILE A1087     1150   3361   2370   -135   -142    175       C  
ATOM    672  CG1 ILE A1087      14.447  17.827   9.405  1.00 18.88           C  
ANISOU  672  CG1 ILE A1087     1230   3289   2655   -269   -522    318       C  
ATOM    673  CG2 ILE A1087      12.491  19.197  10.325  1.00 20.90           C  
ANISOU  673  CG2 ILE A1087     1321   3786   2833   -196   -164    148       C  
ATOM    674  CD1 ILE A1087      14.136  16.452   9.960  1.00 22.96           C  
ANISOU  674  CD1 ILE A1087     1967   3598   3160   -482   -785    553       C  
ATOM    675  N   SER A1088      17.000  20.104   9.135  1.00 17.09           N  
ANISOU  675  N   SER A1088      891   3251   2352    -76    318   -294       N  
ATOM    676  CA  SER A1088      18.441  19.878   9.226  1.00 18.12           C  
ANISOU  676  CA  SER A1088      973   3388   2524   -102    478   -388       C  
ATOM    677  C   SER A1088      19.154  21.004   9.972  1.00 17.58           C  
ANISOU  677  C   SER A1088      988   3192   2500   -142    414   -252       C  
ATOM    678  O   SER A1088      20.217  20.756  10.538  1.00 17.77           O  
ANISOU  678  O   SER A1088      833   3409   2511    -80    441   -270       O  
ATOM    679  CB  SER A1088      19.043  19.685   7.830  1.00 18.83           C  
ANISOU  679  CB  SER A1088      986   3535   2633    -20    494   -408       C  
ATOM    680  OG  SER A1088      19.201  20.918   7.159  1.00 23.03           O  
ANISOU  680  OG  SER A1088     1824   3939   2987     17    899   -329       O  
ATOM    681  N   LYS A1089      18.577  22.211  10.002  1.00 17.93           N  
ANISOU  681  N   LYS A1089     1104   3055   2655   -136    357   -147       N  
ATOM    682  CA  LYS A1089      19.216  23.331  10.719  1.00 19.03           C  
ANISOU  682  CA  LYS A1089     1518   2978   2736   -164    263    -46       C  
ATOM    683  C   LYS A1089      19.460  23.020  12.200  1.00 17.34           C  
ANISOU  683  C   LYS A1089     1092   2867   2628   -260    344    -87       C  
ATOM    684  O   LYS A1089      20.329  23.640  12.827  1.00 18.54           O  
ANISOU  684  O   LYS A1089     1194   3097   2752   -522    417    -97       O  
ATOM    685  CB  LYS A1089      18.421  24.643  10.570  1.00 20.47           C  
ANISOU  685  CB  LYS A1089     1850   3084   2845      6    124    -74       C  
ATOM    686  CG  LYS A1089      17.061  24.659  11.240  1.00 25.29           C  
ANISOU  686  CG  LYS A1089     2542   3919   3147    447    -13   -285       C  
ATOM    687  CD  LYS A1089      16.360  26.017  11.138  1.00 32.49           C  
ANISOU  687  CD  LYS A1089     3542   5194   3607   1357   -152   -241       C  
ATOM    688  CE  LYS A1089      15.317  26.050  10.037  1.00 36.94           C  
ANISOU  688  CE  LYS A1089     4210   6003   3824   1720   -125   -326       C  
ATOM    689  NZ  LYS A1089      15.813  26.660   8.765  1.00 38.74           N  
ANISOU  689  NZ  LYS A1089     4350   6621   3747   1964     76   -285       N  
ATOM    690  N   TYR A1090      18.706  22.074  12.759  1.00 16.07           N  
ANISOU  690  N   TYR A1090      629   2949   2529   -322    324   -104       N  
ATOM    691  CA  TYR A1090      18.829  21.728  14.176  1.00 15.20           C  
ANISOU  691  CA  TYR A1090      346   2951   2477   -328    372   -263       C  
ATOM    692  C   TYR A1090      19.570  20.429  14.448  1.00 14.36           C  
ANISOU  692  C   TYR A1090      318   2928   2210   -344    239   -329       C  
ATOM    693  O   TYR A1090      19.777  20.088  15.608  1.00 15.13           O  
ANISOU  693  O   TYR A1090      350   3203   2196   -240    206   -271       O  
ATOM    694  CB  TYR A1090      17.428  21.612  14.808  1.00 16.74           C  
ANISOU  694  CB  TYR A1090      410   3176   2773   -342    526   -285       C  
ATOM    695  CG  TYR A1090      16.603  22.867  14.683  1.00 20.77           C  
ANISOU  695  CG  TYR A1090      858   3400   3634   -142    832   -186       C  
ATOM    696  CD1 TYR A1090      16.870  23.985  15.465  1.00 26.44           C  
ANISOU  696  CD1 TYR A1090     2117   3750   4178    386    930   -361       C  
ATOM    697  CD2 TYR A1090      15.531  22.934  13.783  1.00 24.91           C  
ANISOU  697  CD2 TYR A1090     1149   3734   4582    175    922     76       C  
ATOM    698  CE1 TYR A1090      16.095  25.148  15.356  1.00 29.65           C  
ANISOU  698  CE1 TYR A1090     2484   3966   4816    612   1203   -272       C  
ATOM    699  CE2 TYR A1090      14.758  24.087  13.666  1.00 27.88           C  
ANISOU  699  CE2 TYR A1090     1392   3905   5296    185   1115    282       C  
ATOM    700  CZ  TYR A1090      15.038  25.184  14.458  1.00 29.45           C  
ANISOU  700  CZ  TYR A1090     1835   4029   5324    560   1500    -12       C  
ATOM    701  OH  TYR A1090      14.291  26.325  14.330  1.00 33.81           O  
ANISOU  701  OH  TYR A1090     2356   4329   6161    588   1465     38       O  
ATOM    702  N   PHE A1091      19.977  19.687  13.409  1.00 14.51           N  
ANISOU  702  N   PHE A1091      306   2969   2238   -186    252   -324       N  
ATOM    703  CA  PHE A1091      20.632  18.396  13.637  1.00 15.09           C  
ANISOU  703  CA  PHE A1091      421   2994   2319    -98    142   -397       C  
ATOM    704  C   PHE A1091      21.870  18.495  14.548  1.00 16.11           C  
ANISOU  704  C   PHE A1091      509   3156   2457   -114    136   -436       C  
ATOM    705  O   PHE A1091      22.010  17.716  15.488  1.00 16.38           O  
ANISOU  705  O   PHE A1091      375   3393   2457   -146     87   -383       O  
ATOM    706  CB  PHE A1091      21.050  17.745  12.320  1.00 15.88           C  
ANISOU  706  CB  PHE A1091      487   3088   2458   -109    120   -460       C  
ATOM    707  CG  PHE A1091      19.915  17.161  11.496  1.00 15.26           C  
ANISOU  707  CG  PHE A1091      388   2910   2500    120   -164   -456       C  
ATOM    708  CD1 PHE A1091      18.665  16.863  12.038  1.00 16.77           C  
ANISOU  708  CD1 PHE A1091      377   2896   3097     98   -307   -269       C  
ATOM    709  CD2 PHE A1091      20.139  16.892  10.139  1.00 18.25           C  
ANISOU  709  CD2 PHE A1091      649   3558   2727    417   -197   -736       C  
ATOM    710  CE1 PHE A1091      17.653  16.300  11.234  1.00 16.67           C  
ANISOU  710  CE1 PHE A1091      294   2966   3073    131   -324   -366       C  
ATOM    711  CE2 PHE A1091      19.148  16.342   9.331  1.00 19.29           C  
ANISOU  711  CE2 PHE A1091      995   3546   2788    509   -482   -630       C  
ATOM    712  CZ  PHE A1091      17.894  16.049   9.883  1.00 19.54           C  
ANISOU  712  CZ  PHE A1091      865   3321   3237    184   -344   -535       C  
ATOM    713  N   ASP A1092      22.770  19.437  14.269  1.00 17.24           N  
ANISOU  713  N   ASP A1092      491   3467   2594   -152    184   -454       N  
ATOM    714  CA  ASP A1092      23.997  19.491  15.066  1.00 18.86           C  
ANISOU  714  CA  ASP A1092      593   3903   2669   -285    197   -518       C  
ATOM    715  C   ASP A1092      23.732  19.721  16.553  1.00 18.20           C  
ANISOU  715  C   ASP A1092      571   3725   2619   -293    273   -465       C  
ATOM    716  O   ASP A1092      24.244  18.996  17.418  1.00 18.52           O  
ANISOU  716  O   ASP A1092      412   3869   2754   -293    357   -456       O  
ATOM    717  CB  ASP A1092      24.938  20.556  14.514  1.00 19.74           C  
ANISOU  717  CB  ASP A1092      634   4120   2748   -384    197   -494       C  
ATOM    718  CG  ASP A1092      25.602  20.148  13.215  1.00 23.75           C  
ANISOU  718  CG  ASP A1092      763   5188   3072   -549    381   -670       C  
ATOM    719  OD1 ASP A1092      25.514  18.966  12.822  1.00 28.53           O  
ANISOU  719  OD1 ASP A1092     1278   5924   3637   -241    520   -996       O  
ATOM    720  OD2 ASP A1092      26.223  21.021  12.571  1.00 29.05           O  
ANISOU  720  OD2 ASP A1092     1148   6503   3388  -1133    653   -702       O  
ATOM    721  N   ASP A1093      22.912  20.717  16.879  1.00 17.96           N  
ANISOU  721  N   ASP A1093      480   3704   2639   -307    357   -423       N  
ATOM    722  CA  ASP A1093      22.655  21.023  18.285  1.00 18.55           C  
ANISOU  722  CA  ASP A1093      794   3495   2759   -357    241   -447       C  
ATOM    723  C   ASP A1093      21.803  19.958  18.970  1.00 16.11           C  
ANISOU  723  C   ASP A1093      295   3467   2360   -219    160   -408       C  
ATOM    724  O   ASP A1093      21.999  19.655  20.143  1.00 16.72           O  
ANISOU  724  O   ASP A1093      350   3639   2362   -346     26   -368       O  
ATOM    725  CB  ASP A1093      22.037  22.413  18.442  1.00 21.11           C  
ANISOU  725  CB  ASP A1093     1272   3501   3249   -377    410   -527       C  
ATOM    726  CG  ASP A1093      23.070  23.530  18.276  1.00 26.65           C  
ANISOU  726  CG  ASP A1093     2099   3564   4462   -614    428   -571       C  
ATOM    727  OD1 ASP A1093      24.271  23.243  18.064  1.00 30.59           O  
ANISOU  727  OD1 ASP A1093     2453   3878   5289   -921    388   -768       O  
ATOM    728  OD2 ASP A1093      22.672  24.707  18.364  1.00 32.41           O  
ANISOU  728  OD2 ASP A1093     3075   3713   5526   -706    732   -507       O  
ATOM    729  N   VAL A1094      20.841  19.377  18.252  1.00 15.26           N  
ANISOU  729  N   VAL A1094      276   3300   2221   -140      0   -366       N  
ATOM    730  CA  VAL A1094      20.019  18.331  18.869  1.00 15.15           C  
ANISOU  730  CA  VAL A1094      253   3368   2133     -7      0   -274       C  
ATOM    731  C   VAL A1094      20.870  17.093  19.164  1.00 14.88           C  
ANISOU  731  C   VAL A1094      253   3433   1967    -31     17   -406       C  
ATOM    732  O   VAL A1094      20.816  16.544  20.260  1.00 15.72           O  
ANISOU  732  O   VAL A1094      265   3806   1903    194     28   -287       O  
ATOM    733  CB  VAL A1094      18.769  17.970  18.036  1.00 15.00           C  
ANISOU  733  CB  VAL A1094      258   3197   2243      6    -97   -213       C  
ATOM    734  CG1 VAL A1094      18.101  16.693  18.567  1.00 15.18           C  
ANISOU  734  CG1 VAL A1094      263   3167   2338     80   -126    -86       C  
ATOM    735  CG2 VAL A1094      17.785  19.140  18.053  1.00 15.64           C  
ANISOU  735  CG2 VAL A1094      285   3181   2474    295     61   -155       C  
ATOM    736  N   THR A1095      21.669  16.659  18.189  1.00 15.56           N  
ANISOU  736  N   THR A1095      253   3638   2020     26      0   -562       N  
ATOM    737  CA  THR A1095      22.445  15.446  18.403  1.00 16.87           C  
ANISOU  737  CA  THR A1095      255   3817   2335     77    -19   -644       C  
ATOM    738  C   THR A1095      23.516  15.664  19.492  1.00 17.67           C  
ANISOU  738  C   THR A1095      258   3977   2477    131    -35   -719       C  
ATOM    739  O   THR A1095      23.776  14.753  20.276  1.00 18.54           O  
ANISOU  739  O   THR A1095      271   4158   2617    219   -142   -658       O  
ATOM    740  CB  THR A1095      23.109  14.920  17.100  1.00 16.88           C  
ANISOU  740  CB  THR A1095      263   3822   2328    103     17   -610       C  
ATOM    741  OG1 THR A1095      24.003  15.902  16.564  1.00 18.21           O  
ANISOU  741  OG1 THR A1095      263   4144   2511     18    146   -615       O  
ATOM    742  CG2 THR A1095      22.027  14.618  16.059  1.00 17.33           C  
ANISOU  742  CG2 THR A1095      258   3982   2345    132    -56   -665       C  
ATOM    743  N   ALA A1096      24.074  16.866  19.593  1.00 18.34           N  
ANISOU  743  N   ALA A1096      256   4235   2476     27    -82   -697       N  
ATOM    744  CA  ALA A1096      25.042  17.155  20.665  1.00 19.03           C  
ANISOU  744  CA  ALA A1096      291   4426   2515   -109   -172   -640       C  
ATOM    745  C   ALA A1096      24.346  17.106  22.029  1.00 19.09           C  
ANISOU  745  C   ALA A1096      282   4469   2502     76   -184   -577       C  
ATOM    746  O   ALA A1096      24.883  16.601  23.013  1.00 20.48           O  
ANISOU  746  O   ALA A1096      527   4724   2529     82   -238   -573       O  
ATOM    747  CB  ALA A1096      25.683  18.506  20.441  1.00 19.92           C  
ANISOU  747  CB  ALA A1096      304   4575   2691   -263   -252   -538       C  
ATOM    748  N   PHE A1097      23.109  17.603  22.086  1.00 18.08           N  
ANISOU  748  N   PHE A1097      263   4198   2410    102   -136   -635       N  
ATOM    749  CA  PHE A1097      22.359  17.580  23.330  1.00 17.92           C  
ANISOU  749  CA  PHE A1097      373   4061   2372    285    -93   -586       C  
ATOM    750  C   PHE A1097      21.999  16.149  23.740  1.00 17.23           C  
ANISOU  750  C   PHE A1097      355   3977   2213    425   -159   -538       C  
ATOM    751  O   PHE A1097      22.147  15.763  24.910  1.00 17.79           O  
ANISOU  751  O   PHE A1097      339   4226   2195    489   -285   -555       O  
ATOM    752  CB  PHE A1097      21.102  18.451  23.205  1.00 17.87           C  
ANISOU  752  CB  PHE A1097      282   4056   2450    252    125   -496       C  
ATOM    753  CG  PHE A1097      20.082  18.217  24.299  1.00 20.56           C  
ANISOU  753  CG  PHE A1097      754   4399   2657    353    520   -397       C  
ATOM    754  CD1 PHE A1097      20.363  18.555  25.618  1.00 25.57           C  
ANISOU  754  CD1 PHE A1097     1729   5062   2924    557    819   -269       C  
ATOM    755  CD2 PHE A1097      18.835  17.662  23.984  1.00 22.53           C  
ANISOU  755  CD2 PHE A1097      749   4666   3147    342    988   -120       C  
ATOM    756  CE1 PHE A1097      19.405  18.341  26.623  1.00 27.35           C  
ANISOU  756  CE1 PHE A1097     2063   5296   3034    995    948     12       C  
ATOM    757  CE2 PHE A1097      17.888  17.435  24.986  1.00 26.57           C  
ANISOU  757  CE2 PHE A1097     1692   5012   3393    763   1216     60       C  
ATOM    758  CZ  PHE A1097      18.181  17.768  26.304  1.00 27.36           C  
ANISOU  758  CZ  PHE A1097     2046   5249   3102    868   1429    120       C  
ATOM    759  N   LEU A1098      21.533  15.359  22.776  1.00 16.50           N  
ANISOU  759  N   LEU A1098      366   3777   2125    610   -186   -461       N  
ATOM    760  CA  LEU A1098      21.228  13.955  23.080  1.00 16.83           C  
ANISOU  760  CA  LEU A1098      388   3889   2117    666   -217   -368       C  
ATOM    761  C   LEU A1098      22.488  13.177  23.527  1.00 18.22           C  
ANISOU  761  C   LEU A1098      416   4250   2257    768   -241   -388       C  
ATOM    762  O   LEU A1098      22.408  12.380  24.456  1.00 19.00           O  
ANISOU  762  O   LEU A1098      483   4420   2318    872   -361   -241       O  
ATOM    763  CB  LEU A1098      20.547  13.305  21.889  1.00 16.18           C  
ANISOU  763  CB  LEU A1098      386   3679   2081    658   -173   -368       C  
ATOM    764  CG  LEU A1098      19.162  13.897  21.579  1.00 15.12           C  
ANISOU  764  CG  LEU A1098      307   3531   1906    422    -21   -192       C  
ATOM    765  CD1 LEU A1098      18.617  13.198  20.353  1.00 15.30           C  
ANISOU  765  CD1 LEU A1098      340   3472   2000    513     47   -260       C  
ATOM    766  CD2 LEU A1098      18.193  13.795  22.779  1.00 15.28           C  
ANISOU  766  CD2 LEU A1098      280   3513   2011    287    -52   -154       C  
ATOM    767  N  ASER A1099      23.627  13.424  22.880  0.50 19.83           N  
ANISOU  767  N  ASER A1099      405   4708   2422    741   -313   -425       N  
ATOM    768  N  BSER A1099      23.621  13.422  22.870  0.50 19.58           N  
ANISOU  768  N  BSER A1099      408   4668   2362    754   -305   -447       N  
ATOM    769  CA ASER A1099      24.885  12.804  23.277  0.50 21.42           C  
ANISOU  769  CA ASER A1099      406   5148   2585    688   -344   -487       C  
ATOM    770  CA BSER A1099      24.877  12.809  23.267  0.50 20.62           C  
ANISOU  770  CA BSER A1099      405   4953   2477    749   -315   -520       C  
ATOM    771  C  ASER A1099      25.260  13.144  24.714  0.50 21.63           C  
ANISOU  771  C  ASER A1099      444   5152   2623    674   -430   -507       C  
ATOM    772  C  BSER A1099      25.208  13.129  24.723  0.50 21.26           C  
ANISOU  772  C  BSER A1099      439   5119   2518    687   -390   -502       C  
ATOM    773  O  ASER A1099      25.777  12.300  25.446  0.50 22.48           O  
ANISOU  773  O  ASER A1099      726   5141   2675    649   -505   -522       O  
ATOM    774  O  BSER A1099      25.634  12.256  25.479  0.50 22.31           O  
ANISOU  774  O  BSER A1099      728   5145   2603    675   -467   -496       O  
ATOM    775  CB ASER A1099      25.970  13.256  22.315  0.50 21.97           C  
ANISOU  775  CB ASER A1099      372   5296   2680    697   -287   -463       C  
ATOM    776  CB BSER A1099      25.975  13.310  22.341  0.50 20.68           C  
ANISOU  776  CB BSER A1099      388   4992   2476    722   -313   -549       C  
ATOM    777  OG ASER A1099      25.861  12.537  21.101  0.50 24.89           O  
ANISOU  777  OG ASER A1099      592   6014   2851    658   -274   -493       O  
ATOM    778  OG BSER A1099      27.217  12.741  22.718  0.50 20.67           O  
ANISOU  778  OG BSER A1099      421   4834   2599    842   -274   -579       O  
ATOM    779  N   LYS A1100      24.994  14.382  25.117  1.00 21.75           N  
ANISOU  779  N   LYS A1100      531   5223   2509    723   -485   -509       N  
ATOM    780  CA  LYS A1100      25.268  14.835  26.479  1.00 23.27           C  
ANISOU  780  CA  LYS A1100      841   5457   2545    807   -498   -568       C  
ATOM    781  C   LYS A1100      24.335  14.143  27.474  1.00 22.89           C  
ANISOU  781  C   LYS A1100      802   5483   2413    988   -500   -520       C  
ATOM    782  O   LYS A1100      24.761  13.751  28.564  1.00 24.04           O  
ANISOU  782  O   LYS A1100      986   5702   2444    851   -542   -480       O  
ATOM    783  CB  LYS A1100      25.190  16.361  26.550  1.00 24.45           C  
ANISOU  783  CB  LYS A1100     1087   5522   2680    781   -546   -693       C  
ATOM    784  CG  LYS A1100      25.571  16.991  27.882  1.00 29.27           C  
ANISOU  784  CG  LYS A1100     1958   5946   3219    487   -515   -878       C  
ATOM    785  CD  LYS A1100      25.968  18.456  27.705  1.00 36.42           C  
ANISOU  785  CD  LYS A1100     3023   6560   4255    142   -562   -763       C  
ATOM    786  CE  LYS A1100      24.790  19.421  27.798  1.00 40.63           C  
ANISOU  786  CE  LYS A1100     3616   7031   4791     -6   -680   -315       C  
ATOM    787  NZ  LYS A1100      23.813  19.245  26.686  1.00 44.34           N  
ANISOU  787  NZ  LYS A1100     3847   7562   5440   -197   -856    -19       N  
ATOM    788  N   CYS A1101      23.062  13.965  27.101  1.00 22.32           N  
ANISOU  788  N   CYS A1101      886   5256   2337   1040   -476   -531       N  
ATOM    789  CA  CYS A1101      22.146  13.223  27.965  1.00 21.76           C  
ANISOU  789  CA  CYS A1101     1085   4924   2257   1186   -522   -612       C  
ATOM    790  C   CYS A1101      22.649  11.795  28.202  1.00 23.32           C  
ANISOU  790  C   CYS A1101     1562   5088   2211   1553   -535   -670       C  
ATOM    791  O   CYS A1101      22.616  11.296  29.331  1.00 24.32           O  
ANISOU  791  O   CYS A1101     1736   5278   2228   1595   -627   -597       O  
ATOM    792  CB  CYS A1101      20.750  13.209  27.368  1.00 21.30           C  
ANISOU  792  CB  CYS A1101      917   4841   2334   1023   -527   -529       C  
ATOM    793  SG  CYS A1101      19.951  14.828  27.403  1.00 20.73           S  
ANISOU  793  SG  CYS A1101      797   4596   2484    688   -296   -463       S  
ATOM    794  N   ASP A1102      23.143  11.152  27.146  1.00 25.12           N  
ANISOU  794  N   ASP A1102     2026   5289   2231   1888   -737   -869       N  
ATOM    795  CA  ASP A1102      23.702   9.807  27.299  1.00 26.89           C  
ANISOU  795  CA  ASP A1102     2249   5594   2372   2152   -973   -986       C  
ATOM    796  C   ASP A1102      24.986   9.774  28.138  1.00 28.63           C  
ANISOU  796  C   ASP A1102     2345   5942   2590   2248  -1208  -1022       C  
ATOM    797  O   ASP A1102      25.195   8.847  28.919  1.00 29.89           O  
ANISOU  797  O   ASP A1102     2368   6140   2847   2275  -1181   -930       O  
ATOM    798  CB  ASP A1102      23.899   9.138  25.926  1.00 26.74           C  
ANISOU  798  CB  ASP A1102     2333   5493   2334   2150   -961   -996       C  
ATOM    799  CG  ASP A1102      22.729   8.239  25.535  1.00 27.50           C  
ANISOU  799  CG  ASP A1102     2487   5615   2345   2073   -767  -1049       C  
ATOM    800  OD1 ASP A1102      22.398   8.148  24.330  1.00 26.64           O  
ANISOU  800  OD1 ASP A1102     2222   5442   2459   1985   -979   -913       O  
ATOM    801  OD2 ASP A1102      22.150   7.594  26.442  1.00 28.08           O  
ANISOU  801  OD2 ASP A1102     2347   5895   2426   1985   -780   -860       O  
ATOM    802  N   GLN A1103      25.827  10.795  27.992  1.00 29.62           N  
ANISOU  802  N   GLN A1103     2203   6248   2802   2328  -1404  -1080       N  
ATOM    803  CA  GLN A1103      27.069  10.883  28.771  1.00 32.70           C  
ANISOU  803  CA  GLN A1103     2585   6657   3183   2213  -1597  -1089       C  
ATOM    804  C   GLN A1103      26.765  11.063  30.259  1.00 32.82           C  
ANISOU  804  C   GLN A1103     2542   6998   2930   2291  -1597  -1133       C  
ATOM    805  O   GLN A1103      27.431  10.483  31.115  1.00 33.98           O  
ANISOU  805  O   GLN A1103     2711   7185   3016   2372  -1497  -1052       O  
ATOM    806  CB  GLN A1103      27.926  12.054  28.285  1.00 33.30           C  
ANISOU  806  CB  GLN A1103     2495   6664   3494   2099  -1718  -1080       C  
ATOM    807  CG  GLN A1103      28.528  11.886  26.902  1.00 40.41           C  
ANISOU  807  CG  GLN A1103     3542   6674   5138   1779  -2055   -964       C  
ATOM    808  CD  GLN A1103      29.079  13.191  26.346  1.00 46.96           C  
ANISOU  808  CD  GLN A1103     4304   6765   6772   1492  -2414   -790       C  
ATOM    809  OE1 GLN A1103      30.064  13.729  26.855  1.00 49.68           O  
ANISOU  809  OE1 GLN A1103     4745   6966   7164   1445  -2186  -1075       O  
ATOM    810  NE2 GLN A1103      28.442  13.705  25.297  1.00 49.86           N  
ANISOU  810  NE2 GLN A1103     4343   7024   7577   1535  -2460   -661       N  
ATOM    811  N   ARG A1104      25.754  11.877  30.547  1.00 33.01           N  
ANISOU  811  N   ARG A1104     2707   7092   2745   2283  -1541   -986       N  
ATOM    812  CA  ARG A1104      25.420  12.254  31.916  1.00 32.86           C  
ANISOU  812  CA  ARG A1104     2842   6987   2657   2117  -1497   -913       C  
ATOM    813  C   ARG A1104      24.373  11.354  32.577  1.00 32.77           C  
ANISOU  813  C   ARG A1104     3230   6638   2585   2301  -1324   -728       C  
ATOM    814  O   ARG A1104      24.023  11.562  33.745  1.00 33.11           O  
ANISOU  814  O   ARG A1104     3296   6771   2515   2292  -1358   -781       O  
ATOM    815  CB  ARG A1104      24.952  13.718  31.964  1.00 32.85           C  
ANISOU  815  CB  ARG A1104     2766   6998   2716   1923  -1483   -935       C  
ATOM    816  CG  ARG A1104      25.995  14.730  31.517  1.00 34.68           C  
ANISOU  816  CG  ARG A1104     2851   7415   2910   1348  -1368   -895       C  
ATOM    817  CD  ARG A1104      25.432  16.142  31.417  1.00 36.46           C  
ANISOU  817  CD  ARG A1104     3027   7710   3115    571  -1014  -1014       C  
ATOM    818  NE  ARG A1104      24.868  16.630  32.674  1.00 40.66           N  
ANISOU  818  NE  ARG A1104     3671   8177   3601    175   -719  -1289       N  
ATOM    819  CZ  ARG A1104      25.492  17.416  33.547  1.00 43.53           C  
ANISOU  819  CZ  ARG A1104     4282   8467   3790     76   -640  -1465       C  
ATOM    820  NH1 ARG A1104      26.736  17.827  33.321  1.00 45.80           N  
ANISOU  820  NH1 ARG A1104     4557   8827   4018   -370   -732  -1489       N  
ATOM    821  NH2 ARG A1104      24.880  17.802  34.664  1.00 45.42           N  
ANISOU  821  NH2 ARG A1104     4785   8564   3907    421   -555  -1500       N  
ATOM    822  N   ASN A1105      23.879  10.349  31.851  1.00 32.21           N  
ANISOU  822  N   ASN A1105     3452   6291   2495   2431  -1145   -430       N  
ATOM    823  CA  ASN A1105      22.814   9.469  32.359  1.00 32.57           C  
ANISOU  823  CA  ASN A1105     3761   6147   2467   2441   -957   -124       C  
ATOM    824  C   ASN A1105      21.582  10.270  32.782  1.00 30.66           C  
ANISOU  824  C   ASN A1105     3508   5867   2275   2090   -850   -216       C  
ATOM    825  O   ASN A1105      21.035  10.076  33.876  1.00 31.30           O  
ANISOU  825  O   ASN A1105     3689   5964   2238   2061   -877   -185       O  
ATOM    826  CB  ASN A1105      23.284   8.559  33.503  1.00 34.23           C  
ANISOU  826  CB  ASN A1105     4065   6438   2502   2662   -851    -15       C  
ATOM    827  CG  ASN A1105      23.890   7.257  33.004  1.00 36.90           C  
ANISOU  827  CG  ASN A1105     4526   6832   2662   3079   -754    262       C  
ATOM    828  OD1 ASN A1105      23.533   6.733  31.941  1.00 39.10           O  
ANISOU  828  OD1 ASN A1105     4498   7368   2989   3497   -727    252       O  
ATOM    829  ND2 ASN A1105      24.821   6.720  33.784  1.00 40.39           N  
ANISOU  829  ND2 ASN A1105     4798   7368   3181   3402   -727    270       N  
ATOM    830  N   GLU A1106      21.161  11.166  31.893  1.00 27.37           N  
ANISOU  830  N   GLU A1106     2818   5422   2159   1685   -724   -331       N  
ATOM    831  CA  GLU A1106      19.993  11.999  32.128  1.00 24.21           C  
ANISOU  831  CA  GLU A1106     2132   4949   2117   1119   -584   -405       C  
ATOM    832  C   GLU A1106      18.941  11.619  31.100  1.00 22.55           C  
ANISOU  832  C   GLU A1106     2098   4539   1932    917   -434   -142       C  
ATOM    833  O   GLU A1106      19.070  11.999  29.942  1.00 22.81           O  
ANISOU  833  O   GLU A1106     2035   4690   1941    820   -320   -131       O  
ATOM    834  CB  GLU A1106      20.357  13.483  32.037  1.00 23.59           C  
ANISOU  834  CB  GLU A1106     1870   4978   2113   1014   -592   -480       C  
ATOM    835  CG  GLU A1106      21.342  13.892  33.127  1.00 24.78           C  
ANISOU  835  CG  GLU A1106     1587   5440   2387    671   -626   -631       C  
ATOM    836  CD  GLU A1106      21.872  15.308  33.009  1.00 26.12           C  
ANISOU  836  CD  GLU A1106     1553   5655   2714    529   -604   -697       C  
ATOM    837  OE1 GLU A1106      21.783  15.901  31.906  1.00 26.04           O  
ANISOU  837  OE1 GLU A1106     1448   5619   2827    590   -627   -737       O  
ATOM    838  OE2 GLU A1106      22.401  15.807  34.035  1.00 27.49           O  
ANISOU  838  OE2 GLU A1106     1605   5989   2851    518   -898   -688       O  
ATOM    839  N   PRO A1107      17.948  10.816  31.508  1.00 22.19           N  
ANISOU  839  N   PRO A1107     2125   4347   1958    856   -335    135       N  
ATOM    840  CA  PRO A1107      16.952  10.343  30.544  1.00 20.80           C  
ANISOU  840  CA  PRO A1107     2046   4034   1823    790   -241    164       C  
ATOM    841  C   PRO A1107      16.202  11.481  29.858  1.00 18.92           C  
ANISOU  841  C   PRO A1107     1676   3837   1676    772   -135    -35       C  
ATOM    842  O   PRO A1107      15.828  12.472  30.500  1.00 18.98           O  
ANISOU  842  O   PRO A1107     1711   3774   1726    697    -98   -118       O  
ATOM    843  CB  PRO A1107      16.010   9.484  31.386  1.00 21.48           C  
ANISOU  843  CB  PRO A1107     1982   4169   2011    825   -164    218       C  
ATOM    844  CG  PRO A1107      16.834   9.062  32.554  1.00 23.65           C  
ANISOU  844  CG  PRO A1107     2441   4489   2055    790   -241    421       C  
ATOM    845  CD  PRO A1107      17.716  10.250  32.849  1.00 23.00           C  
ANISOU  845  CD  PRO A1107     2275   4462   2002    850   -388    294       C  
ATOM    846  N   VAL A1108      16.008  11.330  28.552  1.00 17.43           N  
ANISOU  846  N   VAL A1108     1472   3555   1597    631   -131    -54       N  
ATOM    847  CA  VAL A1108      15.337  12.347  27.748  1.00 16.24           C  
ANISOU  847  CA  VAL A1108     1118   3388   1664    540    -93   -120       C  
ATOM    848  C   VAL A1108      14.373  11.663  26.789  1.00 15.32           C  
ANISOU  848  C   VAL A1108     1080   3197   1544    469     20   -131       C  
ATOM    849  O   VAL A1108      14.706  10.665  26.149  1.00 16.43           O  
ANISOU  849  O   VAL A1108     1286   3262   1693    498     19   -137       O  
ATOM    850  CB  VAL A1108      16.349  13.217  26.953  1.00 15.93           C  
ANISOU  850  CB  VAL A1108     1023   3294   1737    504    -24   -120       C  
ATOM    851  CG1 VAL A1108      17.301  12.348  26.147  1.00 17.57           C  
ANISOU  851  CG1 VAL A1108      885   3932   1860    678    -49   -285       C  
ATOM    852  CG2 VAL A1108      15.656  14.220  26.015  1.00 16.51           C  
ANISOU  852  CG2 VAL A1108      865   3488   1921    386   -215    -54       C  
ATOM    853  N   LEU A1109      13.157  12.205  26.729  1.00 15.12           N  
ANISOU  853  N   LEU A1109      913   3068   1763    329     57    -73       N  
ATOM    854  CA  LEU A1109      12.159  11.726  25.778  1.00 14.14           C  
ANISOU  854  CA  LEU A1109      925   2912   1536    164    230   -115       C  
ATOM    855  C   LEU A1109      12.076  12.694  24.598  1.00 13.40           C  
ANISOU  855  C   LEU A1109      733   2822   1536    146    285   -115       C  
ATOM    856  O   LEU A1109      11.778  13.877  24.815  1.00 14.04           O  
ANISOU  856  O   LEU A1109      753   2739   1841    120    307   -137       O  
ATOM    857  CB  LEU A1109      10.783  11.608  26.455  1.00 15.12           C  
ANISOU  857  CB  LEU A1109      979   2930   1835     15    274    -87       C  
ATOM    858  CG  LEU A1109       9.603  11.315  25.508  1.00 15.87           C  
ANISOU  858  CG  LEU A1109      957   3169   1902    -17    383   -283       C  
ATOM    859  CD1 LEU A1109       9.735   9.965  24.822  1.00 17.43           C  
ANISOU  859  CD1 LEU A1109     1482   3235   1905    -74    331   -203       C  
ATOM    860  CD2 LEU A1109       8.278  11.381  26.259  1.00 16.99           C  
ANISOU  860  CD2 LEU A1109      913   3425   2117     -6    522   -208       C  
ATOM    861  N   VAL A1110      12.361  12.194  23.388  1.00 12.93           N  
ANISOU  861  N   VAL A1110      509   2973   1430    148    252    -59       N  
ATOM    862  CA  VAL A1110      12.215  12.977  22.169  1.00 13.05           C  
ANISOU  862  CA  VAL A1110      287   3142   1528    171    172    -28       C  
ATOM    863  C   VAL A1110      10.844  12.649  21.576  1.00 12.29           C  
ANISOU  863  C   VAL A1110      299   2739   1632    161    217    -83       C  
ATOM    864  O   VAL A1110      10.566  11.487  21.287  1.00 13.30           O  
ANISOU  864  O   VAL A1110      289   2759   2004    153    199   -170       O  
ATOM    865  CB  VAL A1110      13.339  12.629  21.147  1.00 13.55           C  
ANISOU  865  CB  VAL A1110      293   3415   1439    225    164    -24       C  
ATOM    866  CG1 VAL A1110      13.184  13.504  19.903  1.00 14.43           C  
ANISOU  866  CG1 VAL A1110      282   3614   1585     31    195    153       C  
ATOM    867  CG2 VAL A1110      14.718  12.835  21.794  1.00 15.29           C  
ANISOU  867  CG2 VAL A1110      255   3621   1932     89      8     59       C  
ATOM    868  N   HIS A1111       9.994  13.654  21.409  1.00 12.41           N  
ANISOU  868  N   HIS A1111      271   2716   1729     85    142    -86       N  
ATOM    869  CA  HIS A1111       8.645  13.364  20.929  1.00 12.61           C  
ANISOU  869  CA  HIS A1111      282   2806   1703    -54    200    -15       C  
ATOM    870  C   HIS A1111       8.125  14.365  19.923  1.00 11.93           C  
ANISOU  870  C   HIS A1111      299   2620   1614     40    244   -118       C  
ATOM    871  O   HIS A1111       8.560  15.512  19.864  1.00 12.80           O  
ANISOU  871  O   HIS A1111      269   2635   1958    115    128    -39       O  
ATOM    872  CB  HIS A1111       7.643  13.211  22.091  1.00 12.84           C  
ANISOU  872  CB  HIS A1111      337   2840   1703    -38    346    -74       C  
ATOM    873  CG  HIS A1111       7.092  14.511  22.588  1.00 13.20           C  
ANISOU  873  CG  HIS A1111      339   2903   1773     27    357   -124       C  
ATOM    874  ND1 HIS A1111       5.947  15.084  22.072  1.00 13.68           N  
ANISOU  874  ND1 HIS A1111      390   3000   1808    -49    460    -54       N  
ATOM    875  CD2 HIS A1111       7.543  15.360  23.540  1.00 13.83           C  
ANISOU  875  CD2 HIS A1111      370   2930   1955      0    439   -304       C  
ATOM    876  CE1 HIS A1111       5.720  16.230  22.686  1.00 14.00           C  
ANISOU  876  CE1 HIS A1111      340   3199   1781     10    359   -175       C  
ATOM    877  NE2 HIS A1111       6.665  16.417  23.590  1.00 13.86           N  
ANISOU  877  NE2 HIS A1111      368   3055   1844      0    425   -185       N  
ATOM    878  N   SER A1112       7.131  13.907  19.160  1.00 13.40           N  
ANISOU  878  N   SER A1112      256   3109   1722    -48     65   -130       N  
ATOM    879  CA  SER A1112       6.340  14.779  18.306  1.00 14.44           C  
ANISOU  879  CA  SER A1112      280   3373   1835    -43    204    -91       C  
ATOM    880  C   SER A1112       4.865  14.512  18.601  1.00 15.48           C  
ANISOU  880  C   SER A1112      277   3635   1968   -118    187    -59       C  
ATOM    881  O   SER A1112       4.536  14.112  19.708  1.00 16.65           O  
ANISOU  881  O   SER A1112      273   4032   2021   -166    151    -13       O  
ATOM    882  CB  SER A1112       6.687  14.525  16.838  1.00 14.65           C  
ANISOU  882  CB  SER A1112      255   3395   1915    -26     51    -50       C  
ATOM    883  OG  SER A1112       6.707  13.134  16.576  1.00 15.24           O  
ANISOU  883  OG  SER A1112      289   3481   2020    186    197   -183       O  
ATOM    884  N   ALA A1113       4.004  14.721  17.617  1.00 16.37           N  
ANISOU  884  N   ALA A1113      302   3907   2011    -97    286   -238       N  
ATOM    885  CA  ALA A1113       2.583  14.404  17.811  1.00 17.29           C  
ANISOU  885  CA  ALA A1113      294   3923   2352    -74    291   -335       C  
ATOM    886  C   ALA A1113       2.363  12.903  17.637  1.00 17.43           C  
ANISOU  886  C   ALA A1113      286   3998   2339   -135    252   -368       C  
ATOM    887  O   ALA A1113       1.832  12.227  18.530  1.00 17.63           O  
ANISOU  887  O   ALA A1113      329   4007   2363    -92    399   -373       O  
ATOM    888  CB  ALA A1113       1.735  15.193  16.839  1.00 17.76           C  
ANISOU  888  CB  ALA A1113      285   4101   2363   -108    252   -320       C  
ATOM    889  N   ALA A1114       2.778  12.383  16.484  1.00 16.78           N  
ANISOU  889  N   ALA A1114      311   3819   2247   -209    320   -394       N  
ATOM    890  CA  ALA A1114       2.620  10.971  16.175  1.00 16.95           C  
ANISOU  890  CA  ALA A1114      329   3810   2300   -305    349   -417       C  
ATOM    891  C   ALA A1114       3.785  10.090  16.616  1.00 16.02           C  
ANISOU  891  C   ALA A1114      337   3564   2187   -384    322   -450       C  
ATOM    892  O   ALA A1114       3.663   8.862  16.613  1.00 16.87           O  
ANISOU  892  O   ALA A1114      435   3540   2433   -520    531   -467       O  
ATOM    893  CB  ALA A1114       2.353  10.781  14.689  1.00 16.95           C  
ANISOU  893  CB  ALA A1114      340   3804   2297   -406    320   -306       C  
ATOM    894  N   GLY A1115       4.918  10.695  16.971  1.00 15.16           N  
ANISOU  894  N   GLY A1115      324   3355   2081   -296    310   -379       N  
ATOM    895  CA  GLY A1115       6.106   9.918  17.296  1.00 14.90           C  
ANISOU  895  CA  GLY A1115      306   3379   1976    -86    296   -351       C  
ATOM    896  C   GLY A1115       6.717   9.197  16.100  1.00 13.89           C  
ANISOU  896  C   GLY A1115      328   3025   1923   -207    329   -225       C  
ATOM    897  O   GLY A1115       7.319   8.128  16.245  1.00 14.66           O  
ANISOU  897  O   GLY A1115      447   3052   2072   -208    348   -160       O  
ATOM    898  N   VAL A1116       6.560   9.793  14.919  1.00 14.05           N  
ANISOU  898  N   VAL A1116      284   3253   1800   -161    195   -216       N  
ATOM    899  CA  VAL A1116       6.996   9.176  13.670  1.00 14.16           C  
ANISOU  899  CA  VAL A1116      428   3093   1861   -250    175   -186       C  
ATOM    900  C   VAL A1116       8.018  10.032  12.913  1.00 13.47           C  
ANISOU  900  C   VAL A1116      291   2967   1860    -49    225   -120       C  
ATOM    901  O   VAL A1116       9.107   9.550  12.555  1.00 13.92           O  
ANISOU  901  O   VAL A1116      284   3055   1949     87    217    -23       O  
ATOM    902  CB  VAL A1116       5.776   8.881  12.752  1.00 14.06           C  
ANISOU  902  CB  VAL A1116      320   3100   1923   -274    175   -270       C  
ATOM    903  CG1 VAL A1116       6.225   8.426  11.376  1.00 14.88           C  
ANISOU  903  CG1 VAL A1116      397   3264   1993   -313    285   -307       C  
ATOM    904  CG2 VAL A1116       4.884   7.828  13.383  1.00 16.56           C  
ANISOU  904  CG2 VAL A1116      577   3537   2178   -460    295   -219       C  
ATOM    905  N   ASN A1117       7.660  11.289  12.656  1.00 13.24           N  
ANISOU  905  N   ASN A1117      364   2991   1676      6     76      3       N  
ATOM    906  CA  ASN A1117       8.381  12.093  11.674  1.00 12.59           C  
ANISOU  906  CA  ASN A1117      263   2882   1638    162     -6   -106       C  
ATOM    907  C   ASN A1117       9.349  13.081  12.278  1.00 12.84           C  
ANISOU  907  C   ASN A1117      259   2910   1709    120    -20   -227       C  
ATOM    908  O   ASN A1117      10.562  12.911  12.112  1.00 13.12           O  
ANISOU  908  O   ASN A1117      281   2982   1721    272     10   -120       O  
ATOM    909  CB  ASN A1117       7.435  12.787  10.698  1.00 13.08           C  
ANISOU  909  CB  ASN A1117      262   3089   1615    156     -5    -60       C  
ATOM    910  CG  ASN A1117       6.878  11.841   9.664  1.00 13.98           C  
ANISOU  910  CG  ASN A1117      315   3181   1817    375     70   -342       C  
ATOM    911  OD1 ASN A1117       7.531  10.896   9.243  1.00 14.87           O  
ANISOU  911  OD1 ASN A1117      271   3364   2014    227     23   -254       O  
ATOM    912  ND2 ASN A1117       5.628  12.089   9.253  1.00 16.78           N  
ANISOU  912  ND2 ASN A1117      299   3840   2237    305   -225   -276       N  
ATOM    913  N   ARG A1118       8.889  14.107  12.980  1.00 12.34           N  
ANISOU  913  N   ARG A1118      259   2799   1632    107     31   -186       N  
ATOM    914  CA  ARG A1118       9.831  15.103  13.527  1.00 11.82           C  
ANISOU  914  CA  ARG A1118      267   2594   1629    103    109    -38       C  
ATOM    915  C   ARG A1118      10.729  14.424  14.542  1.00 11.50           C  
ANISOU  915  C   ARG A1118      273   2554   1544     98     85     19       C  
ATOM    916  O   ARG A1118      11.985  14.620  14.525  1.00 12.70           O  
ANISOU  916  O   ARG A1118      260   2824   1743     56     92     61       O  
ATOM    917  CB  ARG A1118       9.085  16.270  14.170  1.00 12.41           C  
ANISOU  917  CB  ARG A1118      291   2671   1755    226    152    -49       C  
ATOM    918  CG  ARG A1118       8.391  17.142  13.130  1.00 13.79           C  
ANISOU  918  CG  ARG A1118      318   3057   1862    408     94     37       C  
ATOM    919  CD  ARG A1118       7.344  18.039  13.758  1.00 14.75           C  
ANISOU  919  CD  ARG A1118      335   2939   2329    230    364     71       C  
ATOM    920  NE  ARG A1118       6.150  17.256  14.113  1.00 14.64           N  
ANISOU  920  NE  ARG A1118      289   3224   2047    309     71     10       N  
ATOM    921  CZ  ARG A1118       5.031  17.806  14.599  1.00 15.22           C  
ANISOU  921  CZ  ARG A1118      322   3240   2222    443     74    125       C  
ATOM    922  NH1 ARG A1118       4.963  19.116  14.800  1.00 15.41           N  
ANISOU  922  NH1 ARG A1118      291   3323   2241    328    -77      0       N  
ATOM    923  NH2 ARG A1118       4.005  17.005  14.898  1.00 15.72           N  
ANISOU  923  NH2 ARG A1118      282   3528   2161    231    151     20       N  
ATOM    924  N   SER A1119      10.156  13.633  15.434  1.00 11.45           N  
ANISOU  924  N   SER A1119      265   2585   1499    145     71    125       N  
ATOM    925  CA  SER A1119      10.934  12.938  16.469  1.00 11.91           C  
ANISOU  925  CA  SER A1119      395   2560   1571     85    219     87       C  
ATOM    926  C   SER A1119      11.746  11.812  15.867  1.00 11.82           C  
ANISOU  926  C   SER A1119      267   2563   1660    131     93     -6       C  
ATOM    927  O   SER A1119      12.937  11.641  16.210  1.00 12.43           O  
ANISOU  927  O   SER A1119      267   2777   1676    164     57     -6       O  
ATOM    928  CB  SER A1119       9.971  12.429  17.552  1.00 12.27           C  
ANISOU  928  CB  SER A1119      412   2590   1659    -20    260     43       C  
ATOM    929  OG  SER A1119       8.938  11.641  16.963  1.00 13.78           O  
ANISOU  929  OG  SER A1119      342   2858   2037   -193    366    -38       O  
ATOM    930  N   GLY A1120      11.152  11.004  14.989  1.00 11.82           N  
ANISOU  930  N   GLY A1120      260   2603   1626     40     92    -39       N  
ATOM    931  CA  GLY A1120      11.886   9.920  14.345  1.00 11.99           C  
ANISOU  931  CA  GLY A1120      465   2442   1648   -113    263     52       C  
ATOM    932  C   GLY A1120      13.092  10.479  13.621  1.00 11.38           C  
ANISOU  932  C   GLY A1120      276   2493   1553    -74    163     81       C  
ATOM    933  O   GLY A1120      14.188   9.884  13.680  1.00 12.31           O  
ANISOU  933  O   GLY A1120      264   2655   1756    108     99     44       O  
ATOM    934  N   ALA A1121      12.954  11.606  12.950  1.00 11.12           N  
ANISOU  934  N   ALA A1121      295   2474   1456   -104    197    164       N  
ATOM    935  CA  ALA A1121      14.095  12.179  12.199  1.00 11.08           C  
ANISOU  935  CA  ALA A1121      274   2477   1460   -151    103    135       C  
ATOM    936  C   ALA A1121      15.212  12.605  13.140  1.00 11.54           C  
ANISOU  936  C   ALA A1121      253   2526   1604     15     14    -52       C  
ATOM    937  O   ALA A1121      16.399  12.400  12.813  1.00 12.42           O  
ANISOU  937  O   ALA A1121      287   2703   1729    276     64    -20       O  
ATOM    938  CB  ALA A1121      13.644  13.347  11.355  1.00 11.84           C  
ANISOU  938  CB  ALA A1121      289   2732   1476     -8    204    311       C  
ATOM    939  N   MET A1122      14.917  13.200  14.285  1.00 11.24           N  
ANISOU  939  N   MET A1122      260   2472   1536    121    -40   -153       N  
ATOM    940  CA  MET A1122      15.965  13.604  15.234  1.00 11.44           C  
ANISOU  940  CA  MET A1122      256   2486   1605    -50     58    -99       C  
ATOM    941  C   MET A1122      16.610  12.395  15.832  1.00 11.75           C  
ANISOU  941  C   MET A1122      258   2538   1668     30     76    -20       C  
ATOM    942  O   MET A1122      17.847  12.420  16.058  1.00 13.24           O  
ANISOU  942  O   MET A1122      260   2964   1807    123     41   -117       O  
ATOM    943  CB  MET A1122      15.404  14.526  16.324  1.00 12.27           C  
ANISOU  943  CB  MET A1122      263   2612   1787    -40     74   -186       C  
ATOM    944  CG  MET A1122      14.919  15.862  15.774  1.00 13.75           C  
ANISOU  944  CG  MET A1122      273   2624   2329   -100    182    -93       C  
ATOM    945  SD  MET A1122      16.263  16.729  14.907  1.00 15.59           S  
ANISOU  945  SD  MET A1122      255   3012   2654     38     65     95       S  
ATOM    946  CE  MET A1122      15.391  18.232  14.405  1.00 20.03           C  
ANISOU  946  CE  MET A1122      522   3023   4065     15   -208    463       C  
ATOM    947  N   ILE A1123      15.878  11.314  16.068  1.00 11.60           N  
ANISOU  947  N   ILE A1123      273   2476   1659    164    104    108       N  
ATOM    948  CA  ILE A1123      16.482  10.081  16.570  1.00 11.88           C  
ANISOU  948  CA  ILE A1123      430   2486   1597     93    142    -13       C  
ATOM    949  C   ILE A1123      17.366   9.450  15.505  1.00 11.83           C  
ANISOU  949  C   ILE A1123      265   2651   1580    145     59    -79       C  
ATOM    950  O   ILE A1123      18.488   8.978  15.797  1.00 12.75           O  
ANISOU  950  O   ILE A1123      275   2794   1775    235      0      0       O  
ATOM    951  CB  ILE A1123      15.387   9.069  17.012  1.00 12.79           C  
ANISOU  951  CB  ILE A1123      544   2517   1800     74    263     93       C  
ATOM    952  CG1 ILE A1123      14.682   9.552  18.287  1.00 15.14           C  
ANISOU  952  CG1 ILE A1123      934   3079   1738    175    240    -34       C  
ATOM    953  CG2 ILE A1123      15.937   7.664  17.147  1.00 14.38           C  
ANISOU  953  CG2 ILE A1123      780   2592   2090    192    263    131       C  
ATOM    954  CD1 ILE A1123      15.587   9.710  19.505  1.00 15.91           C  
ANISOU  954  CD1 ILE A1123     1001   3212   1831    372      6    172       C  
ATOM    955  N   LEU A1124      16.929   9.438  14.254  1.00 11.85           N  
ANISOU  955  N   LEU A1124      273   2707   1521    201     48   -174       N  
ATOM    956  CA  LEU A1124      17.764   8.899  13.172  1.00 12.19           C  
ANISOU  956  CA  LEU A1124      412   2666   1553    130     43   -151       C  
ATOM    957  C   LEU A1124      19.036   9.725  13.049  1.00 12.01           C  
ANISOU  957  C   LEU A1124      276   2547   1738    227     18    -97       C  
ATOM    958  O   LEU A1124      20.155   9.163  12.895  1.00 13.29           O  
ANISOU  958  O   LEU A1124      348   2790   1911    461    115    -87       O  
ATOM    959  CB  LEU A1124      16.971   8.891  11.865  1.00 11.72           C  
ANISOU  959  CB  LEU A1124      260   2725   1468    134     -5   -158       C  
ATOM    960  CG  LEU A1124      17.572   8.208  10.652  1.00 15.17           C  
ANISOU  960  CG  LEU A1124      579   3508   1676    562   -186   -322       C  
ATOM    961  CD1 LEU A1124      18.275   6.891  10.947  1.00 18.57           C  
ANISOU  961  CD1 LEU A1124     1288   3528   2240    612   -230   -216       C  
ATOM    962  CD2 LEU A1124      16.574   8.036   9.516  1.00 14.35           C  
ANISOU  962  CD2 LEU A1124      265   3607   1580    196    -57   -434       C  
ATOM    963  N   ALA A1125      18.926  11.044  13.103  1.00 12.04           N  
ANISOU  963  N   ALA A1125      260   2514   1800    123      8    -65       N  
ATOM    964  CA  ALA A1125      20.114  11.918  13.069  1.00 12.17           C  
ANISOU  964  CA  ALA A1125      256   2657   1710     93      3     20       C  
ATOM    965  C   ALA A1125      21.047  11.590  14.229  1.00 12.85           C  
ANISOU  965  C   ALA A1125      276   2946   1659    247     -5     -7       C  
ATOM    966  O   ALA A1125      22.278  11.475  14.042  1.00 14.23           O  
ANISOU  966  O   ALA A1125      311   3140   1957    388     91    -27       O  
ATOM    967  CB  ALA A1125      19.714  13.372  13.172  1.00 12.67           C  
ANISOU  967  CB  ALA A1125      254   2576   1982     43    -21    -38       C  
ATOM    968  N   TYR A1126      20.511  11.391  15.416  1.00 12.97           N  
ANISOU  968  N   TYR A1126      311   3084   1532    401     -6    107       N  
ATOM    969  CA  TYR A1126      21.338  11.075  16.584  1.00 13.85           C  
ANISOU  969  CA  TYR A1126      434   3215   1615    553     -5      0       C  
ATOM    970  C   TYR A1126      22.086   9.791  16.323  1.00 14.71           C  
ANISOU  970  C   TYR A1126      434   3305   1852    636    -31   -137       C  
ATOM    971  O   TYR A1126      23.318   9.728  16.511  1.00 16.15           O  
ANISOU  971  O   TYR A1126      408   3718   2011    727   -119   -304       O  
ATOM    972  CB  TYR A1126      20.478  10.957  17.838  1.00 14.61           C  
ANISOU  972  CB  TYR A1126      663   3395   1492    697      6     46       C  
ATOM    973  CG  TYR A1126      21.262  10.603  19.091  1.00 14.93           C  
ANISOU  973  CG  TYR A1126      692   3339   1640    916   -197     19       C  
ATOM    974  CD1 TYR A1126      22.457  11.257  19.403  1.00 17.35           C  
ANISOU  974  CD1 TYR A1126      944   3734   1914    856   -362   -186       C  
ATOM    975  CD2 TYR A1126      20.819   9.622  19.967  1.00 16.21           C  
ANISOU  975  CD2 TYR A1126      974   3501   1685   1115   -109    120       C  
ATOM    976  CE1 TYR A1126      23.173  10.933  20.555  1.00 18.35           C  
ANISOU  976  CE1 TYR A1126     1316   4007   1650   1067   -394    -82       C  
ATOM    977  CE2 TYR A1126      21.529   9.294  21.124  1.00 18.23           C  
ANISOU  977  CE2 TYR A1126     1360   3783   1782   1120   -115    115       C  
ATOM    978  CZ  TYR A1126      22.709   9.953  21.421  1.00 18.75           C  
ANISOU  978  CZ  TYR A1126     1421   4011   1692   1111   -292   -142       C  
ATOM    979  OH  TYR A1126      23.425   9.622  22.559  1.00 22.28           O  
ANISOU  979  OH  TYR A1126     1624   4874   1967   1216   -337      6       O  
ATOM    980  N   LEU A1127      21.388   8.746  15.890  1.00 14.44           N  
ANISOU  980  N   LEU A1127      419   3224   1844    701    -41   -129       N  
ATOM    981  CA  LEU A1127      22.063   7.468  15.662  1.00 15.89           C  
ANISOU  981  CA  LEU A1127      832   3185   2020    706     31    -93       C  
ATOM    982  C   LEU A1127      23.111   7.561  14.560  1.00 14.84           C  
ANISOU  982  C   LEU A1127      518   3046   2073    744    -48   -153       C  
ATOM    983  O   LEU A1127      24.214   6.999  14.710  1.00 16.30           O  
ANISOU  983  O   LEU A1127      553   3287   2354    922   -219    -74       O  
ATOM    984  CB  LEU A1127      21.048   6.365  15.381  1.00 16.30           C  
ANISOU  984  CB  LEU A1127      848   3192   2152    700     91    -34       C  
ATOM    985  CG  LEU A1127      20.119   6.037  16.561  1.00 19.19           C  
ANISOU  985  CG  LEU A1127     1324   3650   2317    731    348     98       C  
ATOM    986  CD1 LEU A1127      19.009   5.105  16.128  1.00 22.03           C  
ANISOU  986  CD1 LEU A1127     1659   3670   3041    627    553      6       C  
ATOM    987  CD2 LEU A1127      20.897   5.437  17.738  1.00 23.27           C  
ANISOU  987  CD2 LEU A1127     1993   4192   2657    832    485    390       C  
ATOM    988  N   MET A1128      22.831   8.288  13.484  1.00 14.87           N  
ANISOU  988  N   MET A1128      394   3255   2000    649    -46   -227       N  
ATOM    989  CA  MET A1128      23.828   8.464  12.435  1.00 15.33           C  
ANISOU  989  CA  MET A1128      497   3300   2029    465    -49   -373       C  
ATOM    990  C   MET A1128      25.027   9.207  13.017  1.00 15.53           C  
ANISOU  990  C   MET A1128      342   3418   2140    527    -51   -516       C  
ATOM    991  O   MET A1128      26.198   8.886  12.671  1.00 17.14           O  
ANISOU  991  O   MET A1128      390   3842   2280    684    -26   -684       O  
ATOM    992  CB  MET A1128      23.271   9.259  11.254  1.00 14.71           C  
ANISOU  992  CB  MET A1128      311   3258   2020    417    -35   -285       C  
ATOM    993  CG  MET A1128      22.174   8.552  10.453  1.00 15.33           C  
ANISOU  993  CG  MET A1128      260   3425   2140    116    -77   -254       C  
ATOM    994  SD  MET A1128      22.579   6.918   9.816  1.00 15.80           S  
ANISOU  994  SD  MET A1128      304   3413   2286    263     43   -215       S  
ATOM    995  CE  MET A1128      23.885   7.300   8.613  1.00 17.51           C  
ANISOU  995  CE  MET A1128      399   3573   2682    148    274   -162       C  
ATOM    996  N   SER A1129      24.796  10.180  13.884  1.00 16.25           N  
ANISOU  996  N   SER A1129      348   3594   2231    555   -164   -658       N  
ATOM    997  CA  SER A1129      25.874  11.029  14.410  1.00 18.04           C  
ANISOU  997  CA  SER A1129      456   3968   2430    604   -285   -797       C  
ATOM    998  C   SER A1129      26.783  10.204  15.299  1.00 19.20           C  
ANISOU  998  C   SER A1129      427   4280   2587    798   -324   -744       C  
ATOM    999  O   SER A1129      27.987  10.494  15.396  1.00 21.59           O  
ANISOU  999  O   SER A1129      375   4781   3048    666   -366   -794       O  
ATOM   1000  CB  SER A1129      25.347  12.239  15.192  1.00 17.67           C  
ANISOU 1000  CB  SER A1129      359   3925   2428    563   -326   -864       C  
ATOM   1001  OG  SER A1129      24.861  11.875  16.477  1.00 20.04           O  
ANISOU 1001  OG  SER A1129      353   4695   2567    656   -195   -807       O  
ATOM   1002  N   LYS A1130      26.229   9.181  15.942  1.00 20.20           N  
ANISOU 1002  N   LYS A1130      568   4514   2592   1110   -395   -606       N  
ATOM   1003  CA  LYS A1130      26.978   8.364  16.895  1.00 22.76           C  
ANISOU 1003  CA  LYS A1130     1168   4820   2657   1421   -386   -640       C  
ATOM   1004  C   LYS A1130      27.735   7.264  16.173  1.00 22.13           C  
ANISOU 1004  C   LYS A1130      864   4760   2786   1359   -315   -653       C  
ATOM   1005  O   LYS A1130      28.651   6.665  16.747  1.00 22.88           O  
ANISOU 1005  O   LYS A1130      752   4935   3007   1492   -414   -557       O  
ATOM   1006  CB  LYS A1130      26.025   7.767  17.935  1.00 24.04           C  
ANISOU 1006  CB  LYS A1130     1544   5095   2495   1544   -361   -568       C  
ATOM   1007  CG  LYS A1130      25.729   8.687  19.102  1.00 29.75           C  
ANISOU 1007  CG  LYS A1130     2416   6050   2836   2002   -487   -913       C  
ATOM   1008  CD  LYS A1130      26.651   8.383  20.288  1.00 38.03           C  
ANISOU 1008  CD  LYS A1130     3700   7458   3291   2257   -631  -1482       C  
ATOM   1009  CE  LYS A1130      26.523   9.404  21.408  1.00 41.31           C  
ANISOU 1009  CE  LYS A1130     4099   7746   3851   2404   -608  -1826       C  
ATOM   1010  NZ  LYS A1130      27.609  10.435  21.343  1.00 44.20           N  
ANISOU 1010  NZ  LYS A1130     4663   7846   4284   2345   -326  -2016       N  
ATOM   1011  N   ASN A1131      27.379   6.998  14.920  1.00 21.56           N  
ANISOU 1011  N   ASN A1131      640   4726   2827   1315   -229   -750       N  
ATOM   1012  CA  ASN A1131      28.062   5.957  14.152  1.00 21.38           C  
ANISOU 1012  CA  ASN A1131      661   4650   2811   1132   -153   -719       C  
ATOM   1013  C   ASN A1131      29.427   6.410  13.661  1.00 20.85           C  
ANISOU 1013  C   ASN A1131      601   4508   2813   1115   -274   -590       C  
ATOM   1014  O   ASN A1131      29.512   7.325  12.842  1.00 21.40           O  
ANISOU 1014  O   ASN A1131      562   4591   2976   1055   -472   -403       O  
ATOM   1015  CB  ASN A1131      27.216   5.516  12.954  1.00 20.91           C  
ANISOU 1015  CB  ASN A1131      544   4627   2775   1111    -54   -762       C  
ATOM   1016  CG  ASN A1131      28.009   4.668  11.969  1.00 20.44           C  
ANISOU 1016  CG  ASN A1131      493   4318   2953    955     25   -736       C  
ATOM   1017  OD1 ASN A1131      28.637   3.679  12.354  1.00 22.84           O  
ANISOU 1017  OD1 ASN A1131     1129   4140   3409    715     38   -825       O  
ATOM   1018  ND2 ASN A1131      27.997   5.062  10.700  1.00 20.89           N  
ANISOU 1018  ND2 ASN A1131      368   4672   2899    649    120   -671       N  
ATOM   1019  N   LYS A1132      30.484   5.754  14.159  1.00 20.37           N  
ANISOU 1019  N   LYS A1132      500   4329   2910    983   -272   -483       N  
ATOM   1020  CA  LYS A1132      31.873   6.003  13.735  1.00 20.99           C  
ANISOU 1020  CA  LYS A1132      527   4286   3163    908   -274   -604       C  
ATOM   1021  C   LYS A1132      32.470   4.767  13.052  1.00 20.29           C  
ANISOU 1021  C   LYS A1132      518   4158   3034   1000   -262   -439       C  
ATOM   1022  O   LYS A1132      33.600   4.807  12.531  1.00 22.30           O  
ANISOU 1022  O   LYS A1132      848   4350   3276    974    -19   -377       O  
ATOM   1023  CB  LYS A1132      32.731   6.401  14.940  1.00 22.10           C  
ANISOU 1023  CB  LYS A1132      706   4370   3321    832   -322   -662       C  
ATOM   1024  CG  LYS A1132      32.185   7.560  15.761  1.00 26.75           C  
ANISOU 1024  CG  LYS A1132     1412   4798   3953    498   -450  -1212       C  
ATOM   1025  CD  LYS A1132      33.124   7.939  16.890  1.00 34.43           C  
ANISOU 1025  CD  LYS A1132     2791   5482   4809    153   -441  -1534       C  
ATOM   1026  CE  LYS A1132      33.815   9.268  16.603  1.00 38.65           C  
ANISOU 1026  CE  LYS A1132     3495   5881   5310     23   -208  -1586       C  
ATOM   1027  NZ  LYS A1132      34.854   9.568  17.634  1.00 41.36           N  
ANISOU 1027  NZ  LYS A1132     3948   6168   5598     31    -52  -1430       N  
ATOM   1028  N   GLU A1133      31.713   3.670  13.068  1.00 21.01           N  
ANISOU 1028  N   GLU A1133      743   4214   3025   1067   -337   -571       N  
ATOM   1029  CA  GLU A1133      32.227   2.344  12.714  1.00 21.55           C  
ANISOU 1029  CA  GLU A1133      864   4280   3043   1180   -505   -627       C  
ATOM   1030  C   GLU A1133      31.814   1.881  11.319  1.00 21.18           C  
ANISOU 1030  C   GLU A1133      719   4311   3018   1312   -456   -675       C  
ATOM   1031  O   GLU A1133      32.641   1.338  10.570  1.00 22.64           O  
ANISOU 1031  O   GLU A1133      898   4487   3219   1303   -373   -768       O  
ATOM   1032  CB  GLU A1133      31.763   1.299  13.737  1.00 22.57           C  
ANISOU 1032  CB  GLU A1133     1112   4435   3030   1221   -493   -549       C  
ATOM   1033  CG  GLU A1133      32.320   1.477  15.141  1.00 23.21           C  
ANISOU 1033  CG  GLU A1133      903   4758   3156   1348   -603   -640       C  
ATOM   1034  CD  GLU A1133      33.593   0.682  15.369  1.00 23.54           C  
ANISOU 1034  CD  GLU A1133      798   5120   3027   1316   -230   -913       C  
ATOM   1035  OE1 GLU A1133      33.731  -0.408  14.781  1.00 26.77           O  
ANISOU 1035  OE1 GLU A1133     1225   5303   3643   1588   -542   -970       O  
ATOM   1036  OE2 GLU A1133      34.435   1.145  16.159  1.00 22.31           O  
ANISOU 1036  OE2 GLU A1133      439   4586   3452    831   -393   -568       O  
ATOM   1037  N   SER A1134      30.537   2.075  10.986  1.00 20.85           N  
ANISOU 1037  N   SER A1134      588   4257   3077   1054   -390   -688       N  
ATOM   1038  CA  SER A1134      29.943   1.431   9.817  1.00 21.39           C  
ANISOU 1038  CA  SER A1134      621   4508   3000    864   -164   -630       C  
ATOM   1039  C   SER A1134      29.787   2.371   8.627  1.00 20.53           C  
ANISOU 1039  C   SER A1134      427   4494   2881    841    -10   -709       C  
ATOM   1040  O   SER A1134      29.643   3.576   8.810  1.00 20.50           O  
ANISOU 1040  O   SER A1134      428   4582   2779    858    -28   -696       O  
ATOM   1041  CB  SER A1134      28.569   0.864  10.215  1.00 21.71           C  
ANISOU 1041  CB  SER A1134      688   4539   3021    702   -204   -535       C  
ATOM   1042  OG  SER A1134      28.680  -0.130  11.229  1.00 26.07           O  
ANISOU 1042  OG  SER A1134     1191   5216   3497    640    -87   -197       O  
ATOM   1043  N   LEU A1135      29.814   1.826   7.412  1.00 20.77           N  
ANISOU 1043  N   LEU A1135      456   4519   2915    784     49   -749       N  
ATOM   1044  CA  LEU A1135      29.584   2.638   6.214  1.00 20.53           C  
ANISOU 1044  CA  LEU A1135      456   4503   2842    680    219   -719       C  
ATOM   1045  C   LEU A1135      28.234   3.331   6.363  1.00 18.80           C  
ANISOU 1045  C   LEU A1135      306   4106   2730    386    135   -487       C  
ATOM   1046  O   LEU A1135      27.245   2.658   6.610  1.00 18.79           O  
ANISOU 1046  O   LEU A1135      480   3937   2721    274    108   -361       O  
ATOM   1047  CB  LEU A1135      29.598   1.776   4.943  1.00 22.63           C  
ANISOU 1047  CB  LEU A1135      776   4798   3025    658    193   -872       C  
ATOM   1048  CG  LEU A1135      30.868   0.957   4.693  1.00 27.13           C  
ANISOU 1048  CG  LEU A1135     1298   5403   3607    702    384  -1230       C  
ATOM   1049  CD1 LEU A1135      30.627  -0.114   3.643  1.00 30.37           C  
ANISOU 1049  CD1 LEU A1135     1949   5752   3837    803    293  -1419       C  
ATOM   1050  CD2 LEU A1135      32.035   1.858   4.284  1.00 31.32           C  
ANISOU 1050  CD2 LEU A1135     1527   6165   4208    496    397  -1474       C  
ATOM   1051  N   PRO A1136      28.205   4.660   6.233  1.00 17.99           N  
ANISOU 1051  N   PRO A1136      285   3935   2614    217    189   -310       N  
ATOM   1052  CA  PRO A1136      26.963   5.409   6.468  1.00 17.65           C  
ANISOU 1052  CA  PRO A1136      264   3844   2597    180     57   -245       C  
ATOM   1053  C   PRO A1136      25.777   4.871   5.677  1.00 17.43           C  
ANISOU 1053  C   PRO A1136      284   3896   2441     98      0   -164       C  
ATOM   1054  O   PRO A1136      24.676   4.794   6.234  1.00 17.20           O  
ANISOU 1054  O   PRO A1136      264   3727   2545    161     80   -208       O  
ATOM   1055  CB  PRO A1136      27.326   6.823   6.026  1.00 18.11           C  
ANISOU 1055  CB  PRO A1136      259   3856   2766    136    -41   -186       C  
ATOM   1056  CG  PRO A1136      28.777   6.924   6.339  1.00 18.68           C  
ANISOU 1056  CG  PRO A1136      260   3932   2906      0    138   -170       C  
ATOM   1057  CD  PRO A1136      29.357   5.561   6.024  1.00 18.65           C  
ANISOU 1057  CD  PRO A1136      276   4029   2781     90    220   -331       C  
ATOM   1058  N   MET A1137      25.964   4.503   4.413  1.00 17.90           N  
ANISOU 1058  N   MET A1137      331   4077   2395    -15    -43   -170       N  
ATOM   1059  CA  MET A1137      24.809   4.032   3.613  1.00 19.83           C  
ANISOU 1059  CA  MET A1137      734   4419   2381   -142    -57   -153       C  
ATOM   1060  C   MET A1137      24.192   2.783   4.245  1.00 18.70           C  
ANISOU 1060  C   MET A1137      579   4018   2509     57    148   -296       C  
ATOM   1061  O   MET A1137      22.962   2.652   4.356  1.00 18.80           O  
ANISOU 1061  O   MET A1137      460   3971   2712    109    208   -384       O  
ATOM   1062  CB  MET A1137      25.214   3.765   2.159  1.00 22.36           C  
ANISOU 1062  CB  MET A1137     1307   4888   2301   -340   -174   -120       C  
ATOM   1063  CG  MET A1137      24.155   2.988   1.399  1.00 27.32           C  
ANISOU 1063  CG  MET A1137     2117   5799   2465   -706   -230   -153       C  
ATOM   1064  SD  MET A1137      24.675   2.420  -0.217  0.50 31.00           S  
ANISOU 1064  SD  MET A1137     3253   5971   2554   -856   -107   -315       S  
ATOM   1065  CE  MET A1137      26.432   2.167   0.041  1.00 34.11           C  
ANISOU 1065  CE  MET A1137     3634   6610   2718   -837   -142   -401       C  
ATOM   1066  N   LEU A1138      25.037   1.857   4.686  1.00 19.23           N  
ANISOU 1066  N   LEU A1138      708   3822   2775    195    225   -359       N  
ATOM   1067  CA  LEU A1138      24.575   0.610   5.278  1.00 19.86           C  
ANISOU 1067  CA  LEU A1138      939   3625   2982    410    357   -467       C  
ATOM   1068  C   LEU A1138      23.963   0.875   6.640  1.00 18.00           C  
ANISOU 1068  C   LEU A1138      601   3395   2845    410    271   -364       C  
ATOM   1069  O   LEU A1138      22.923   0.316   6.982  1.00 18.87           O  
ANISOU 1069  O   LEU A1138      697   3476   2996    263    324   -322       O  
ATOM   1070  CB  LEU A1138      25.727  -0.387   5.430  1.00 22.00           C  
ANISOU 1070  CB  LEU A1138     1254   3704   3400    540    518   -627       C  
ATOM   1071  CG  LEU A1138      26.264  -1.026   4.151  1.00 27.00           C  
ANISOU 1071  CG  LEU A1138     2184   4079   3995    688    925   -860       C  
ATOM   1072  CD1 LEU A1138      27.491  -1.871   4.474  1.00 31.02           C  
ANISOU 1072  CD1 LEU A1138     2657   4307   4823    961   1347  -1080       C  
ATOM   1073  CD2 LEU A1138      25.191  -1.887   3.498  1.00 31.25           C  
ANISOU 1073  CD2 LEU A1138     2985   4438   4449    649    952  -1132       C  
ATOM   1074  N   TYR A1139      24.602   1.735   7.432  1.00 17.45           N  
ANISOU 1074  N   TYR A1139      627   3343   2660    471     87   -219       N  
ATOM   1075  CA  TYR A1139      24.096   2.031   8.770  1.00 17.16           C  
ANISOU 1075  CA  TYR A1139      557   3433   2529    557    -63    -65       C  
ATOM   1076  C   TYR A1139      22.729   2.725   8.683  1.00 16.16           C  
ANISOU 1076  C   TYR A1139      460   3233   2448    434    -93      0       C  
ATOM   1077  O   TYR A1139      21.816   2.433   9.483  1.00 17.41           O  
ANISOU 1077  O   TYR A1139      571   3370   2675    386    -38     98       O  
ATOM   1078  CB  TYR A1139      25.103   2.868   9.579  1.00 18.01           C  
ANISOU 1078  CB  TYR A1139      719   3713   2412    584   -152     19       C  
ATOM   1079  CG  TYR A1139      24.776   2.836  11.054  1.00 18.44           C  
ANISOU 1079  CG  TYR A1139      597   4065   2345    610   -175    109       C  
ATOM   1080  CD1 TYR A1139      24.939   1.656  11.787  1.00 20.16           C  
ANISOU 1080  CD1 TYR A1139      864   4352   2442    538   -174    322       C  
ATOM   1081  CD2 TYR A1139      24.296   3.959  11.716  1.00 18.37           C  
ANISOU 1081  CD2 TYR A1139      329   4244   2406    511   -150      0       C  
ATOM   1082  CE1 TYR A1139      24.621   1.608  13.133  1.00 22.71           C  
ANISOU 1082  CE1 TYR A1139     1747   4415   2465    531   -219    197       C  
ATOM   1083  CE2 TYR A1139      23.987   3.925  13.078  1.00 20.44           C  
ANISOU 1083  CE2 TYR A1139      900   4345   2522    522    -59    -15       C  
ATOM   1084  CZ  TYR A1139      24.141   2.743  13.775  1.00 21.59           C  
ANISOU 1084  CZ  TYR A1139     1421   4377   2407    384   -241     40       C  
ATOM   1085  OH  TYR A1139      23.835   2.684  15.109  1.00 24.93           O  
ANISOU 1085  OH  TYR A1139     2108   4634   2730    269    -82     43       O  
ATOM   1086  N   PHE A1140      22.583   3.646   7.737  1.00 15.12           N  
ANISOU 1086  N   PHE A1140      291   2996   2458    252   -126     31       N  
ATOM   1087  CA  PHE A1140      21.316   4.355   7.511  1.00 13.71           C  
ANISOU 1087  CA  PHE A1140      285   2739   2187     76   -153     10       C  
ATOM   1088  C   PHE A1140      20.213   3.358   7.200  1.00 13.51           C  
ANISOU 1088  C   PHE A1140      346   2750   2037      0    -76    -26       C  
ATOM   1089  O   PHE A1140      19.125   3.416   7.789  1.00 14.09           O  
ANISOU 1089  O   PHE A1140      262   2949   2142     96     98      6       O  
ATOM   1090  CB  PHE A1140      21.468   5.343   6.349  1.00 14.06           C  
ANISOU 1090  CB  PHE A1140      269   2829   2242     27   -173     99       C  
ATOM   1091  CG  PHE A1140      20.162   5.931   5.859  1.00 13.37           C  
ANISOU 1091  CG  PHE A1140      256   2838   1987     14    -71    -17       C  
ATOM   1092  CD1 PHE A1140      19.494   6.919   6.589  1.00 13.62           C  
ANISOU 1092  CD1 PHE A1140      260   2842   2071     14   -110    -89       C  
ATOM   1093  CD2 PHE A1140      19.632   5.489   4.648  1.00 14.76           C  
ANISOU 1093  CD2 PHE A1140      408   3165   2037    -74    -96   -130       C  
ATOM   1094  CE1 PHE A1140      18.279   7.465   6.105  1.00 14.25           C  
ANISOU 1094  CE1 PHE A1140      322   3106   1985     65     82     24       C  
ATOM   1095  CE2 PHE A1140      18.435   6.006   4.173  1.00 16.06           C  
ANISOU 1095  CE2 PHE A1140      900   3041   2161     46   -259    -35       C  
ATOM   1096  CZ  PHE A1140      17.766   6.991   4.909  1.00 15.32           C  
ANISOU 1096  CZ  PHE A1140      719   2985   2117    -27     65     20       C  
ATOM   1097  N   LEU A1141      20.451   2.436   6.279  1.00 13.80           N  
ANISOU 1097  N   LEU A1141      460   2621   2161    -49    -43    -62       N  
ATOM   1098  CA  LEU A1141      19.422   1.449   5.940  1.00 14.71           C  
ANISOU 1098  CA  LEU A1141      597   2569   2425    -60     20    -65       C  
ATOM   1099  C   LEU A1141      19.090   0.554   7.131  1.00 15.68           C  
ANISOU 1099  C   LEU A1141      577   2736   2644      0     86     86       C  
ATOM   1100  O   LEU A1141      17.926   0.233   7.387  1.00 16.70           O  
ANISOU 1100  O   LEU A1141      483   2858   3005   -114    219      5       O  
ATOM   1101  CB  LEU A1141      19.823   0.601   4.731  1.00 15.68           C  
ANISOU 1101  CB  LEU A1141      776   2648   2533   -137    104   -175       C  
ATOM   1102  CG  LEU A1141      19.924   1.383   3.411  1.00 17.12           C  
ANISOU 1102  CG  LEU A1141      912   2912   2680    109    175   -175       C  
ATOM   1103  CD1 LEU A1141      20.446   0.468   2.325  1.00 19.02           C  
ANISOU 1103  CD1 LEU A1141      926   3370   2930     35    461   -467       C  
ATOM   1104  CD2 LEU A1141      18.568   1.985   3.011  1.00 19.10           C  
ANISOU 1104  CD2 LEU A1141      802   3179   3276    -38     31   -109       C  
ATOM   1105  N   TYR A1142      20.119   0.141   7.871  1.00 16.82           N  
ANISOU 1105  N   TYR A1142      716   2890   2786    225     86    284       N  
ATOM   1106  CA  TYR A1142      19.924  -0.708   9.033  1.00 18.61           C  
ANISOU 1106  CA  TYR A1142     1035   3115   2921    410    175    397       C  
ATOM   1107  C   TYR A1142      19.088  -0.011  10.102  1.00 18.24           C  
ANISOU 1107  C   TYR A1142     1057   3037   2836    313    164    320       C  
ATOM   1108  O   TYR A1142      18.099  -0.594  10.595  1.00 19.04           O  
ANISOU 1108  O   TYR A1142      986   3059   3188    173    322    296       O  
ATOM   1109  CB  TYR A1142      21.268  -1.174   9.631  1.00 20.94           C  
ANISOU 1109  CB  TYR A1142     1366   3431   3158    688    186    644       C  
ATOM   1110  CG  TYR A1142      21.042  -1.905  10.940  1.00 25.78           C  
ANISOU 1110  CG  TYR A1142     2002   4178   3616   1194    450   1118       C  
ATOM   1111  CD1 TYR A1142      20.528  -3.201  10.929  1.00 31.30           C  
ANISOU 1111  CD1 TYR A1142     3003   4584   4307   1439    847   1571       C  
ATOM   1112  CD2 TYR A1142      21.289  -1.307  12.173  1.00 31.06           C  
ANISOU 1112  CD2 TYR A1142     2973   4989   3840   1606    595   1473       C  
ATOM   1113  CE1 TYR A1142      20.287  -3.890  12.110  1.00 35.87           C  
ANISOU 1113  CE1 TYR A1142     3901   5113   4616   1500   1124   1825       C  
ATOM   1114  CE2 TYR A1142      21.049  -1.990  13.365  1.00 35.28           C  
ANISOU 1114  CE2 TYR A1142     3828   5414   4162   1694   1000   1720       C  
ATOM   1115  CZ  TYR A1142      20.550  -3.282  13.323  1.00 37.19           C  
ANISOU 1115  CZ  TYR A1142     4147   5478   4505   1648   1313   1869       C  
ATOM   1116  OH  TYR A1142      20.309  -3.976  14.488  1.00 40.20           O  
ANISOU 1116  OH  TYR A1142     4623   5849   4802   1756   1553   1897       O  
ATOM   1117  N   VAL A1143      19.474   1.204  10.472  1.00 17.65           N  
ANISOU 1117  N   VAL A1143      794   3113   2800    270    164    120       N  
ATOM   1118  CA  VAL A1143      18.756   1.932  11.523  1.00 17.14           C  
ANISOU 1118  CA  VAL A1143      684   3359   2469    153     71     43       C  
ATOM   1119  C   VAL A1143      17.327   2.216  11.051  1.00 15.15           C  
ANISOU 1119  C   VAL A1143      522   3021   2213      6    142     74       C  
ATOM   1120  O   VAL A1143      16.380   2.042  11.824  1.00 15.53           O  
ANISOU 1120  O   VAL A1143      666   3086   2150      6    185     31       O  
ATOM   1121  CB  VAL A1143      19.453   3.249  11.969  1.00 18.19           C  
ANISOU 1121  CB  VAL A1143      689   3625   2596    193    -31   -173       C  
ATOM   1122  CG1 VAL A1143      18.501   4.073  12.869  1.00 19.56           C  
ANISOU 1122  CG1 VAL A1143      850   3935   2646    196     17   -252       C  
ATOM   1123  CG2 VAL A1143      20.772   2.943  12.678  1.00 21.82           C  
ANISOU 1123  CG2 VAL A1143      948   4528   2813    241   -109   -109       C  
ATOM   1124  N   TYR A1144      17.185   2.656   9.796  1.00 14.00           N  
ANISOU 1124  N   TYR A1144      406   2845   2069     59     91     49       N  
ATOM   1125  CA  TYR A1144      15.871   2.990   9.271  1.00 13.74           C  
ANISOU 1125  CA  TYR A1144      479   2651   2090    -24    148    -74       C  
ATOM   1126  C   TYR A1144      14.945   1.790   9.412  1.00 13.79           C  
ANISOU 1126  C   TYR A1144      666   2624   1949    -71    340   -164       C  
ATOM   1127  O   TYR A1144      13.857   1.878  10.008  1.00 14.34           O  
ANISOU 1127  O   TYR A1144      392   2879   2178    -71    386   -237       O  
ATOM   1128  CB  TYR A1144      15.936   3.480   7.800  1.00 13.42           C  
ANISOU 1128  CB  TYR A1144      269   2770   2060     -1    171    -18       C  
ATOM   1129  CG  TYR A1144      14.523   3.844   7.396  1.00 13.58           C  
ANISOU 1129  CG  TYR A1144      269   2969   1920     45    156   -174       C  
ATOM   1130  CD1 TYR A1144      14.017   5.083   7.783  1.00 13.87           C  
ANISOU 1130  CD1 TYR A1144      333   2944   1992    250     82   -129       C  
ATOM   1131  CD2 TYR A1144      13.695   2.960   6.714  1.00 15.46           C  
ANISOU 1131  CD2 TYR A1144      300   3373   2201    375      0   -496       C  
ATOM   1132  CE1 TYR A1144      12.713   5.435   7.488  1.00 15.53           C  
ANISOU 1132  CE1 TYR A1144      593   3359   1949    450    -68   -241       C  
ATOM   1133  CE2 TYR A1144      12.370   3.310   6.411  1.00 16.21           C  
ANISOU 1133  CE2 TYR A1144      291   3607   2258    355    -63   -688       C  
ATOM   1134  CZ  TYR A1144      11.901   4.549   6.804  1.00 14.83           C  
ANISOU 1134  CZ  TYR A1144      405   3328   1903    296    -93   -335       C  
ATOM   1135  OH  TYR A1144      10.597   4.909   6.522  1.00 18.25           O  
ANISOU 1135  OH  TYR A1144      304   4056   2574    362   -241   -564       O  
ATOM   1136  N   HIS A1145      15.340   0.671   8.824  1.00 14.69           N  
ANISOU 1136  N   HIS A1145      917   2502   2161   -175    480   -228       N  
ATOM   1137  CA  HIS A1145      14.439  -0.485   8.772  1.00 16.21           C  
ANISOU 1137  CA  HIS A1145     1254   2517   2389   -184    653   -230       C  
ATOM   1138  C   HIS A1145      14.230  -1.155  10.117  1.00 17.03           C  
ANISOU 1138  C   HIS A1145     1316   2687   2469   -184    772   -151       C  
ATOM   1139  O   HIS A1145      13.114  -1.596  10.417  1.00 18.52           O  
ANISOU 1139  O   HIS A1145     1360   2908   2768   -362    913   -219       O  
ATOM   1140  CB  HIS A1145      14.882  -1.466   7.688  1.00 16.78           C  
ANISOU 1140  CB  HIS A1145     1392   2560   2422   -305    631   -335       C  
ATOM   1141  CG  HIS A1145      14.593  -0.951   6.318  1.00 18.16           C  
ANISOU 1141  CG  HIS A1145     1509   2869   2522   -318    489   -377       C  
ATOM   1142  ND1 HIS A1145      13.314  -0.734   5.858  1.00 19.58           N  
ANISOU 1142  ND1 HIS A1145     1420   3217   2804   -405    386   -549       N  
ATOM   1143  CD2 HIS A1145      15.420  -0.580   5.306  1.00 18.79           C  
ANISOU 1143  CD2 HIS A1145     1576   3088   2477   -511    355   -296       C  
ATOM   1144  CE1 HIS A1145      13.362  -0.258   4.621  1.00 20.03           C  
ANISOU 1144  CE1 HIS A1145     1594   3298   2718   -390    294   -548       C  
ATOM   1145  NE2 HIS A1145      14.632  -0.158   4.260  1.00 19.34           N  
ANISOU 1145  NE2 HIS A1145     1527   3402   2417   -463    229   -465       N  
ATOM   1146  N   SER A1146      15.269  -1.220  10.941  1.00 17.75           N  
ANISOU 1146  N   SER A1146     1473   2768   2504     73    776    -54       N  
ATOM   1147  CA  SER A1146      15.132  -1.851  12.246  1.00 18.58           C  
ANISOU 1147  CA  SER A1146     1615   2763   2680    296    829     60       C  
ATOM   1148  C   SER A1146      14.224  -1.016  13.157  1.00 17.62           C  
ANISOU 1148  C   SER A1146     1532   2644   2520    102    939      0       C  
ATOM   1149  O   SER A1146      13.400  -1.583  13.884  1.00 18.70           O  
ANISOU 1149  O   SER A1146     1597   2815   2694    -48   1089     46       O  
ATOM   1150  CB  SER A1146      16.487  -2.131  12.901  1.00 20.01           C  
ANISOU 1150  CB  SER A1146     1835   2964   2802    428    715     87       C  
ATOM   1151  OG  SER A1146      17.208  -0.939  13.151  1.00 22.64           O  
ANISOU 1151  OG  SER A1146     1851   3357   3393    511    478     98       O  
ATOM   1152  N   MET A1147      14.351   0.311  13.104  1.00 16.66           N  
ANISOU 1152  N   MET A1147     1177   2612   2540     74    763   -164       N  
ATOM   1153  CA  MET A1147      13.469   1.186  13.884  1.00 16.08           C  
ANISOU 1153  CA  MET A1147      873   2725   2513    -26    564   -252       C  
ATOM   1154  C   MET A1147      12.029   1.120  13.385  1.00 16.41           C  
ANISOU 1154  C   MET A1147      840   2933   2460   -153    599   -307       C  
ATOM   1155  O   MET A1147      11.078   1.118  14.172  1.00 17.64           O  
ANISOU 1155  O   MET A1147      891   3271   2542   -197    619   -357       O  
ATOM   1156  CB  MET A1147      13.964   2.638  13.845  1.00 16.00           C  
ANISOU 1156  CB  MET A1147      812   2716   2551      0    447   -237       C  
ATOM   1157  CG  MET A1147      15.200   2.944  14.702  1.00 18.11           C  
ANISOU 1157  CG  MET A1147      969   3260   2651    104    162   -184       C  
ATOM   1158  SD  MET A1147      14.935   2.658  16.481  1.00 24.07           S  
ANISOU 1158  SD  MET A1147     2442   4047   2655     31    119    -31       S  
ATOM   1159  CE  MET A1147      13.679   3.863  16.862  1.00 25.03           C  
ANISOU 1159  CE  MET A1147     1360   5788   2363    781    357   -293       C  
ATOM   1160  N   ARG A1148      11.863   1.082  12.074  1.00 16.68           N  
ANISOU 1160  N   ARG A1148      867   2975   2496   -219    568   -390       N  
ATOM   1161  CA  ARG A1148      10.523   1.031  11.499  1.00 17.53           C  
ANISOU 1161  CA  ARG A1148     1044   2978   2639   -271    560   -320       C  
ATOM   1162  C   ARG A1148       9.817  -0.274  11.854  1.00 18.40           C  
ANISOU 1162  C   ARG A1148     1224   2933   2833   -443    846   -480       C  
ATOM   1163  O   ARG A1148       8.603  -0.291  12.147  1.00 19.26           O  
ANISOU 1163  O   ARG A1148     1025   3296   2998   -489    979   -482       O  
ATOM   1164  CB  ARG A1148      10.582   1.214   9.982  1.00 17.34           C  
ANISOU 1164  CB  ARG A1148      943   3084   2560   -109    516   -322       C  
ATOM   1165  CG  ARG A1148       9.200   1.483   9.396  1.00 19.17           C  
ANISOU 1165  CG  ARG A1148     1000   3391   2894    -98    130   -241       C  
ATOM   1166  CD  ARG A1148       9.312   1.750   7.923  1.00 20.36           C  
ANISOU 1166  CD  ARG A1148     1071   3731   2935     76    -81   -428       C  
ATOM   1167  NE  ARG A1148       8.051   2.218   7.363  1.00 21.34           N  
ANISOU 1167  NE  ARG A1148      991   3973   3143   -153   -296   -500       N  
ATOM   1168  CZ  ARG A1148       7.118   1.429   6.852  1.00 23.26           C  
ANISOU 1168  CZ  ARG A1148     1604   4138   3095   -606    -63   -416       C  
ATOM   1169  NH1 ARG A1148       7.275   0.112   6.809  1.00 25.20           N  
ANISOU 1169  NH1 ARG A1148     1976   4135   3463   -723    241   -340       N  
ATOM   1170  NH2 ARG A1148       6.018   1.971   6.366  1.00 23.35           N  
ANISOU 1170  NH2 ARG A1148     1000   4888   2984   -588    -30   -353       N  
ATOM   1171  N   ASP A1149      10.565  -1.377  11.829  1.00 20.64           N  
ANISOU 1171  N   ASP A1149     1756   2851   3237   -606   1049   -568       N  
ATOM   1172  CA  ASP A1149      10.003  -2.677  12.192  1.00 23.37           C  
ANISOU 1172  CA  ASP A1149     2425   2930   3526   -653   1092   -540       C  
ATOM   1173  C   ASP A1149       9.552  -2.697  13.654  1.00 24.16           C  
ANISOU 1173  C   ASP A1149     2635   3109   3436   -656   1067   -294       C  
ATOM   1174  O   ASP A1149       8.533  -3.300  14.000  1.00 24.97           O  
ANISOU 1174  O   ASP A1149     2536   3458   3494   -696   1067   -186       O  
ATOM   1175  CB  ASP A1149      11.026  -3.788  11.927  1.00 24.80           C  
ANISOU 1175  CB  ASP A1149     2660   2874   3887   -706   1119   -627       C  
ATOM   1176  CG  ASP A1149      11.193  -4.102  10.447  1.00 27.73           C  
ANISOU 1176  CG  ASP A1149     2960   3143   4433   -702   1251   -900       C  
ATOM   1177  OD1 ASP A1149      10.468  -3.520   9.603  1.00 31.16           O  
ANISOU 1177  OD1 ASP A1149     3576   3734   4528   -741   1392   -806       O  
ATOM   1178  OD2 ASP A1149      12.064  -4.932  10.111  1.00 31.22           O  
ANISOU 1178  OD2 ASP A1149     3100   3411   5353   -675   1579  -1225       O  
ATOM   1179  N   LEU A1150      10.318  -2.014  14.500  1.00 23.53           N  
ANISOU 1179  N   LEU A1150     2533   3172   3237   -379   1000   -108       N  
ATOM   1180  CA  LEU A1150      10.049  -1.943  15.934  1.00 24.05           C  
ANISOU 1180  CA  LEU A1150     2691   3249   3197   -170    904     82       C  
ATOM   1181  C   LEU A1150       8.884  -1.018  16.269  1.00 23.69           C  
ANISOU 1181  C   LEU A1150     2508   3203   3289   -142   1058     24       C  
ATOM   1182  O   LEU A1150       8.024  -1.367  17.097  1.00 24.94           O  
ANISOU 1182  O   LEU A1150     2606   3486   3384   -114   1238    208       O  
ATOM   1183  CB  LEU A1150      11.308  -1.481  16.685  1.00 24.92           C  
ANISOU 1183  CB  LEU A1150     2942   3321   3206   -131    776     15       C  
ATOM   1184  CG  LEU A1150      11.201  -1.342  18.209  1.00 28.06           C  
ANISOU 1184  CG  LEU A1150     3790   3659   3212    -87    467    142       C  
ATOM   1185  CD1 LEU A1150      10.763  -2.651  18.860  1.00 30.46           C  
ANISOU 1185  CD1 LEU A1150     4370   3937   3267    -34    280    197       C  
ATOM   1186  CD2 LEU A1150      12.525  -0.851  18.774  1.00 30.45           C  
ANISOU 1186  CD2 LEU A1150     4359   3952   3257    -31    -10    204       C  
ATOM   1187  N   ARG A1151       8.844   0.146  15.629  1.00 21.55           N  
ANISOU 1187  N   ARG A1151     1949   3122   3118   -208    820   -259       N  
ATOM   1188  CA  ARG A1151       7.869   1.193  15.929  1.00 20.98           C  
ANISOU 1188  CA  ARG A1151     1641   3312   3018   -208    684   -571       C  
ATOM   1189  C   ARG A1151       6.575   1.066  15.132  1.00 20.63           C  
ANISOU 1189  C   ARG A1151     1351   3504   2985   -401    798   -688       C  
ATOM   1190  O   ARG A1151       5.533   1.491  15.625  1.00 22.41           O  
ANISOU 1190  O   ARG A1151     1339   3968   3206   -230    886   -851       O  
ATOM   1191  CB  ARG A1151       8.468   2.577  15.647  1.00 20.95           C  
ANISOU 1191  CB  ARG A1151     1483   3185   3291   -195    469   -643       C  
ATOM   1192  CG  ARG A1151       9.780   2.900  16.356  1.00 22.57           C  
ANISOU 1192  CG  ARG A1151     1606   3576   3395     51    324   -714       C  
ATOM   1193  CD  ARG A1151       9.551   3.568  17.691  1.00 21.03           C  
ANISOU 1193  CD  ARG A1151     1439   3677   2876    388    313   -390       C  
ATOM   1194  NE  ARG A1151       8.734   4.787  17.638  1.00 17.77           N  
ANISOU 1194  NE  ARG A1151     1050   3355   2347    208    472   -195       N  
ATOM   1195  CZ  ARG A1151       7.951   5.172  18.651  1.00 18.11           C  
ANISOU 1195  CZ  ARG A1151     1430   2991   2460   -208    571   -160       C  
ATOM   1196  NH1 ARG A1151       7.881   4.417  19.755  1.00 20.47           N  
ANISOU 1196  NH1 ARG A1151     2178   3244   2356   -109    573   -120       N  
ATOM   1197  NH2 ARG A1151       7.238   6.293  18.554  1.00 16.43           N  
ANISOU 1197  NH2 ARG A1151     1008   2980   2255   -175    573   -329       N  
ATOM   1198  N   GLY A1152       6.648   0.516  13.924  1.00 19.38           N  
ANISOU 1198  N   GLY A1152      992   3553   2818   -498    828   -635       N  
ATOM   1199  CA  GLY A1152       5.479   0.429  13.031  1.00 19.57           C  
ANISOU 1199  CA  GLY A1152      894   3698   2842   -636    675   -568       C  
ATOM   1200  C   GLY A1152       5.498   1.486  11.935  1.00 18.31           C  
ANISOU 1200  C   GLY A1152      612   3625   2720   -546    557   -621       C  
ATOM   1201  O   GLY A1152       5.059   1.234  10.807  1.00 19.75           O  
ANISOU 1201  O   GLY A1152      663   3984   2858   -679    460   -652       O  
ATOM   1202  N   ALA A1153       6.002   2.667  12.280  1.00 18.39           N  
ANISOU 1202  N   ALA A1153      571   3684   2732   -582    377   -498       N  
ATOM   1203  CA  ALA A1153       6.195   3.756  11.334  1.00 17.22           C  
ANISOU 1203  CA  ALA A1153      379   3562   2603   -445    208   -460       C  
ATOM   1204  C   ALA A1153       7.353   4.613  11.840  1.00 16.22           C  
ANISOU 1204  C   ALA A1153      439   3357   2365   -416    164   -430       C  
ATOM   1205  O   ALA A1153       7.494   4.820  13.042  1.00 17.23           O  
ANISOU 1205  O   ALA A1153      693   3553   2299   -505    262   -390       O  
ATOM   1206  CB  ALA A1153       4.921   4.591  11.201  1.00 18.59           C  
ANISOU 1206  CB  ALA A1153      421   3844   2797   -359    103   -483       C  
ATOM   1207  N   PHE A1154       8.178   5.104  10.921  1.00 15.01           N  
ANISOU 1207  N   PHE A1154      289   3177   2236   -315     90   -329       N  
ATOM   1208  CA  PHE A1154       9.435   5.761  11.289  1.00 13.87           C  
ANISOU 1208  CA  PHE A1154      267   2863   2140   -186     44   -205       C  
ATOM   1209  C   PHE A1154       9.854   6.618  10.107  1.00 13.36           C  
ANISOU 1209  C   PHE A1154      262   2828   1985   -150      8   -283       C  
ATOM   1210  O   PHE A1154      10.002   6.113   8.997  1.00 14.14           O  
ANISOU 1210  O   PHE A1154      263   2974   2134     -5    137   -345       O  
ATOM   1211  CB  PHE A1154      10.494   4.718  11.675  1.00 14.09           C  
ANISOU 1211  CB  PHE A1154      284   2949   2122   -153     96   -120       C  
ATOM   1212  CG  PHE A1154      11.793   5.307  12.167  1.00 13.49           C  
ANISOU 1212  CG  PHE A1154      465   2587   2073   -140    228   -135       C  
ATOM   1213  CD1 PHE A1154      11.868   5.965  13.390  1.00 12.71           C  
ANISOU 1213  CD1 PHE A1154      263   2453   2113   -136     55   -115       C  
ATOM   1214  CD2 PHE A1154      12.943   5.184  11.408  1.00 13.30           C  
ANISOU 1214  CD2 PHE A1154      320   2714   2019    -87    296    -71       C  
ATOM   1215  CE1 PHE A1154      13.064   6.499  13.844  1.00 13.66           C  
ANISOU 1215  CE1 PHE A1154      518   2565   2108     19    329   -160       C  
ATOM   1216  CE2 PHE A1154      14.143   5.715  11.859  1.00 13.17           C  
ANISOU 1216  CE2 PHE A1154      306   2648   2048    -65    305   -153       C  
ATOM   1217  CZ  PHE A1154      14.201   6.369  13.076  1.00 13.14           C  
ANISOU 1217  CZ  PHE A1154      333   2498   2159     -1    390    -57       C  
ATOM   1218  N   VAL A1155      10.039   7.909  10.358  1.00 13.22           N  
ANISOU 1218  N   VAL A1155      262   2851   1908   -146     43   -217       N  
ATOM   1219  CA  VAL A1155      10.333   8.875   9.307  1.00 13.67           C  
ANISOU 1219  CA  VAL A1155      264   3066   1862   -170     44    -87       C  
ATOM   1220  C   VAL A1155       9.734   8.571   7.940  1.00 14.04           C  
ANISOU 1220  C   VAL A1155      359   3131   1844   -181    131   -186       C  
ATOM   1221  O   VAL A1155      10.446   8.458   6.946  1.00 14.77           O  
ANISOU 1221  O   VAL A1155      259   3310   2044     -6    103   -190       O  
ATOM   1222  CB  VAL A1155      11.855   9.070   9.163  1.00 13.68           C  
ANISOU 1222  CB  VAL A1155      264   3177   1755   -164     59     17       C  
ATOM   1223  CG1 VAL A1155      12.149  10.387   8.469  1.00 15.32           C  
ANISOU 1223  CG1 VAL A1155      513   3300   2008    -98    142    163       C  
ATOM   1224  CG2 VAL A1155      12.524   9.024  10.530  1.00 14.09           C  
ANISOU 1224  CG2 VAL A1155      335   3174   1844   -131    120    -12       C  
ATOM   1225  N   GLU A1156       8.412   8.444   7.902  1.00 14.46           N  
ANISOU 1225  N   GLU A1156      258   3321   1914   -115    -17   -153       N  
ATOM   1226  CA  GLU A1156       7.692   8.304   6.643  1.00 15.42           C  
ANISOU 1226  CA  GLU A1156      265   3690   1903   -202      0   -258       C  
ATOM   1227  C   GLU A1156       7.804   9.525   5.733  1.00 15.40           C  
ANISOU 1227  C   GLU A1156      254   3779   1819    -57     -8   -201       C  
ATOM   1228  O   GLU A1156       7.679   9.413   4.516  1.00 17.35           O  
ANISOU 1228  O   GLU A1156      754   3901   1938    -93    -74   -195       O  
ATOM   1229  CB  GLU A1156       6.222   7.961   6.906  1.00 16.18           C  
ANISOU 1229  CB  GLU A1156      280   3822   2046   -307     35   -297       C  
ATOM   1230  CG  GLU A1156       6.019   6.853   7.929  1.00 17.90           C  
ANISOU 1230  CG  GLU A1156      472   3862   2467   -353     17   -346       C  
ATOM   1231  CD  GLU A1156       6.546   5.512   7.455  1.00 20.00           C  
ANISOU 1231  CD  GLU A1156      795   4032   2772   -439   -120   -526       C  
ATOM   1232  OE1 GLU A1156       6.276   5.140   6.296  1.00 22.40           O  
ANISOU 1232  OE1 GLU A1156      872   4598   3041   -388   -241   -763       O  
ATOM   1233  OE2 GLU A1156       7.228   4.824   8.244  1.00 19.97           O  
ANISOU 1233  OE2 GLU A1156      752   4041   2793   -494    170   -461       O  
ATOM   1234  N   ASN A1157       8.046  10.686   6.332  1.00 15.50           N  
ANISOU 1234  N   ASN A1157      254   3781   1853     45     27   -147       N  
ATOM   1235  CA  ASN A1157       8.144  11.946   5.589  1.00 15.38           C  
ANISOU 1235  CA  ASN A1157      263   3824   1758    118     88   -126       C  
ATOM   1236  C   ASN A1157       9.379  11.894   4.674  1.00 15.20           C  
ANISOU 1236  C   ASN A1157      295   3785   1694    175     38   -208       C  
ATOM   1237  O   ASN A1157      10.500  11.840   5.169  1.00 15.75           O  
ANISOU 1237  O   ASN A1157      262   4005   1717    182     -6   -131       O  
ATOM   1238  CB  ASN A1157       8.210  13.106   6.593  1.00 15.21           C  
ANISOU 1238  CB  ASN A1157      326   3761   1694    297    252    -63       C  
ATOM   1239  CG  ASN A1157       8.334  14.472   5.937  1.00 15.78           C  
ANISOU 1239  CG  ASN A1157      453   3785   1756    544    203    -17       C  
ATOM   1240  OD1 ASN A1157       8.961  14.633   4.883  1.00 18.14           O  
ANISOU 1240  OD1 ASN A1157     1005   3878   2008    535    537    103       O  
ATOM   1241  ND2 ASN A1157       7.773  15.479   6.606  1.00 15.67           N  
ANISOU 1241  ND2 ASN A1157      350   3813   1791    575     52   -136       N  
ATOM   1242  N   PRO A1158       9.185  11.852   3.349  1.00 16.48           N  
ANISOU 1242  N   PRO A1158      496   4142   1622    131      0   -115       N  
ATOM   1243  CA  PRO A1158      10.350  11.688   2.468  1.00 17.26           C  
ANISOU 1243  CA  PRO A1158      819   4088   1650    263    126    -76       C  
ATOM   1244  C   PRO A1158      11.292  12.887   2.459  1.00 16.34           C  
ANISOU 1244  C   PRO A1158      652   3855   1703    487    237    115       C  
ATOM   1245  O   PRO A1158      12.476  12.711   2.157  1.00 16.53           O  
ANISOU 1245  O   PRO A1158      427   3973   1879    588    151      5       O  
ATOM   1246  CB  PRO A1158       9.725  11.476   1.085  1.00 18.60           C  
ANISOU 1246  CB  PRO A1158     1007   4386   1676    226     87    -98       C  
ATOM   1247  CG  PRO A1158       8.367  12.086   1.179  1.00 19.58           C  
ANISOU 1247  CG  PRO A1158     1106   4623   1712    104   -153   -197       C  
ATOM   1248  CD  PRO A1158       7.910  11.913   2.595  1.00 16.77           C  
ANISOU 1248  CD  PRO A1158      577   4117   1676    115   -120    -20       C  
ATOM   1249  N   SER A1159      10.799  14.088   2.764  1.00 15.77           N  
ANISOU 1249  N   SER A1159      597   3709   1684    606    152    230       N  
ATOM   1250  CA ASER A1159      11.662  15.274   2.850  0.50 15.49           C  
ANISOU 1250  CA ASER A1159      636   3528   1720    634    216    364       C  
ATOM   1251  CA BSER A1159      11.675  15.252   2.822  0.50 15.30           C  
ANISOU 1251  CA BSER A1159      575   3560   1676    593    197    364       C  
ATOM   1252  C   SER A1159      12.608  15.170   4.038  1.00 14.66           C  
ANISOU 1252  C   SER A1159      544   3413   1612    621    219    218       C  
ATOM   1253  O   SER A1159      13.788  15.554   3.963  1.00 14.86           O  
ANISOU 1253  O   SER A1159      553   3303   1790    454    261    197       O  
ATOM   1254  CB ASER A1159      10.868  16.576   2.968  0.50 16.22           C  
ANISOU 1254  CB ASER A1159      708   3567   1886    640    219    452       C  
ATOM   1255  CB BSER A1159      10.847  16.538   2.793  0.50 15.89           C  
ANISOU 1255  CB BSER A1159      597   3625   1817    586    175    414       C  
ATOM   1256  OG ASER A1159      11.745  17.666   3.258  0.50 17.47           O  
ANISOU 1256  OG ASER A1159      750   3621   2266    820    342    469       O  
ATOM   1257  OG BSER A1159      10.100  16.606   1.579  0.50 15.63           O  
ANISOU 1257  OG BSER A1159      353   3655   1932    535    249    593       O  
ATOM   1258  N   PHE A1160      12.117  14.651   5.150  1.00 14.35           N  
ANISOU 1258  N   PHE A1160      500   3420   1534    540    205    175       N  
ATOM   1259  CA  PHE A1160      12.967  14.476   6.326  1.00 13.11           C  
ANISOU 1259  CA  PHE A1160      388   3127   1465    489    252     30       C  
ATOM   1260  C   PHE A1160      14.016  13.402   6.032  1.00 12.99           C  
ANISOU 1260  C   PHE A1160      318   2976   1641    335    171    -60       C  
ATOM   1261  O   PHE A1160      15.194  13.562   6.378  1.00 13.24           O  
ANISOU 1261  O   PHE A1160      287   3084   1659    290     79     68       O  
ATOM   1262  CB  PHE A1160      12.118  14.077   7.537  1.00 13.31           C  
ANISOU 1262  CB  PHE A1160      379   3185   1492    518    209     46       C  
ATOM   1263  CG  PHE A1160      11.265  15.195   8.104  1.00 13.56           C  
ANISOU 1263  CG  PHE A1160      337   3179   1634    469    115     80       C  
ATOM   1264  CD1 PHE A1160      11.256  16.472   7.546  1.00 14.65           C  
ANISOU 1264  CD1 PHE A1160      434   3183   1948    678    226    113       C  
ATOM   1265  CD2 PHE A1160      10.486  14.958   9.210  1.00 14.06           C  
ANISOU 1265  CD2 PHE A1160      366   3476   1500    474      6    -52       C  
ATOM   1266  CE1 PHE A1160      10.455  17.484   8.094  1.00 14.87           C  
ANISOU 1266  CE1 PHE A1160      560   3210   1879    634    137    196       C  
ATOM   1267  CE2 PHE A1160       9.680  15.952   9.758  1.00 13.77           C  
ANISOU 1267  CE2 PHE A1160      328   3416   1489    461     98     34       C  
ATOM   1268  CZ  PHE A1160       9.680  17.211   9.215  1.00 14.71           C  
ANISOU 1268  CZ  PHE A1160      372   3517   1699    617     92    219       C  
ATOM   1269  N   LYS A1161      13.616  12.306   5.389  1.00 12.88           N  
ANISOU 1269  N   LYS A1161      403   2752   1738    291    313    -76       N  
ATOM   1270  CA  LYS A1161      14.591  11.267   5.002  1.00 13.43           C  
ANISOU 1270  CA  LYS A1161      693   2594   1815    173    403     65       C  
ATOM   1271  C   LYS A1161      15.644  11.847   4.082  1.00 12.49           C  
ANISOU 1271  C   LYS A1161      579   2544   1624    241    285    151       C  
ATOM   1272  O   LYS A1161      16.840  11.547   4.243  1.00 12.93           O  
ANISOU 1272  O   LYS A1161      326   2689   1897    366    186    115       O  
ATOM   1273  CB  LYS A1161      13.931  10.072   4.319  1.00 14.32           C  
ANISOU 1273  CB  LYS A1161      805   2680   1956     24    518    -68       C  
ATOM   1274  CG  LYS A1161      13.158   9.217   5.300  1.00 18.69           C  
ANISOU 1274  CG  LYS A1161     1524   3095   2483   -364    656    -68       C  
ATOM   1275  CD  LYS A1161      12.722   7.915   4.699  1.00 21.76           C  
ANISOU 1275  CD  LYS A1161     1753   3445   3070   -653    575   -296       C  
ATOM   1276  CE  LYS A1161      11.544   8.133   3.784  1.00 24.97           C  
ANISOU 1276  CE  LYS A1161     1949   3822   3716   -759    259   -445       C  
ATOM   1277  NZ  LYS A1161      10.552   7.040   3.999  1.00 25.44           N  
ANISOU 1277  NZ  LYS A1161     1500   3921   4246   -820    303   -666       N  
ATOM   1278  N   ARG A1162      15.228  12.667   3.131  1.00 12.06           N  
ANISOU 1278  N   ARG A1162      438   2599   1544    153    226    274       N  
ATOM   1279  CA  ARG A1162      16.176  13.289   2.188  1.00 12.25           C  
ANISOU 1279  CA  ARG A1162      710   2524   1421     52    207    219       C  
ATOM   1280  C   ARG A1162      17.216  14.101   2.959  1.00 11.93           C  
ANISOU 1280  C   ARG A1162      540   2457   1536    194    263     24       C  
ATOM   1281  O   ARG A1162      18.417  14.040   2.656  1.00 12.93           O  
ANISOU 1281  O   ARG A1162      340   2829   1744    252    307     35       O  
ATOM   1282  CB  ARG A1162      15.455  14.215   1.215  1.00 12.87           C  
ANISOU 1282  CB  ARG A1162      864   2599   1427     86    218    320       C  
ATOM   1283  CG  ARG A1162      16.381  14.864   0.168  1.00 14.02           C  
ANISOU 1283  CG  ARG A1162     1086   2689   1553     98    263    438       C  
ATOM   1284  CD  ARG A1162      15.773  16.115  -0.432  1.00 16.03           C  
ANISOU 1284  CD  ARG A1162     1351   2621   2117    115    377    480       C  
ATOM   1285  NE  ARG A1162      15.878  17.258   0.484  1.00 16.82           N  
ANISOU 1285  NE  ARG A1162     1404   2685   2301    280    205    342       N  
ATOM   1286  CZ  ARG A1162      14.853  17.965   0.947  1.00 15.46           C  
ANISOU 1286  CZ  ARG A1162     1023   2781   2071     41     13    291       C  
ATOM   1287  NH1 ARG A1162      13.592  17.641   0.624  1.00 18.03           N  
ANISOU 1287  NH1 ARG A1162      864   3379   2608    -65   -147    527       N  
ATOM   1288  NH2 ARG A1162      15.065  18.987   1.752  1.00 17.65           N  
ANISOU 1288  NH2 ARG A1162     1676   3021   2008     15     17    164       N  
ATOM   1289  N   GLN A1163      16.770  14.861   3.951  1.00 12.32           N  
ANISOU 1289  N   GLN A1163      603   2417   1659    241    208   -113       N  
ATOM   1290  CA  GLN A1163      17.668  15.710   4.753  1.00 12.31           C  
ANISOU 1290  CA  GLN A1163      675   2290   1712    239    164    -38       C  
ATOM   1291  C   GLN A1163      18.657  14.885   5.565  1.00 12.52           C  
ANISOU 1291  C   GLN A1163      522   2356   1879    219    148     46       C  
ATOM   1292  O   GLN A1163      19.836  15.263   5.690  1.00 13.84           O  
ANISOU 1292  O   GLN A1163      439   2745   2073    -74    205     43       O  
ATOM   1293  CB  GLN A1163      16.868  16.659   5.638  1.00 12.54           C  
ANISOU 1293  CB  GLN A1163      665   2442   1657    284     65    -87       C  
ATOM   1294  CG  GLN A1163      16.171  17.712   4.786  1.00 13.50           C  
ANISOU 1294  CG  GLN A1163      675   2596   1859    438    126      0       C  
ATOM   1295  CD  GLN A1163      15.263  18.590   5.618  1.00 14.05           C  
ANISOU 1295  CD  GLN A1163      849   2714   1773    666    -59   -115       C  
ATOM   1296  OE1 GLN A1163      15.714  19.227   6.580  1.00 16.73           O  
ANISOU 1296  OE1 GLN A1163     1402   2989   1967    522   -109   -296       O  
ATOM   1297  NE2 GLN A1163      13.970  18.657   5.244  1.00 15.99           N  
ANISOU 1297  NE2 GLN A1163      777   3260   2037    715     92     93       N  
ATOM   1298  N   ILE A1164      18.229  13.758   6.111  1.00 12.06           N  
ANISOU 1298  N   ILE A1164      410   2381   1791    285    173    163       N  
ATOM   1299  CA  ILE A1164      19.122  12.845   6.808  1.00 12.76           C  
ANISOU 1299  CA  ILE A1164      439   2504   1905    351    159    135       C  
ATOM   1300  C   ILE A1164      20.155  12.293   5.828  1.00 13.08           C  
ANISOU 1300  C   ILE A1164      392   2630   1946    247    186     -3       C  
ATOM   1301  O   ILE A1164      21.360  12.235   6.152  1.00 13.75           O  
ANISOU 1301  O   ILE A1164      285   2966   1972    140    211     57       O  
ATOM   1302  CB  ILE A1164      18.360  11.675   7.463  1.00 13.19           C  
ANISOU 1302  CB  ILE A1164      497   2617   1897    417    153    208       C  
ATOM   1303  CG1 ILE A1164      17.485  12.214   8.607  1.00 14.54           C  
ANISOU 1303  CG1 ILE A1164      509   3145   1870    388    208     87       C  
ATOM   1304  CG2 ILE A1164      19.328  10.586   7.945  1.00 14.43           C  
ANISOU 1304  CG2 ILE A1164      364   2861   2256    500    241    397       C  
ATOM   1305  CD1 ILE A1164      18.270  12.566   9.848  1.00 17.86           C  
ANISOU 1305  CD1 ILE A1164     1097   3643   2046    423      3    -54       C  
ATOM   1306  N   ILE A1165      19.716  11.869   4.651  1.00 12.68           N  
ANISOU 1306  N   ILE A1165      340   2671   1808     93    280     26       N  
ATOM   1307  CA  ILE A1165      20.642  11.315   3.662  1.00 13.20           C  
ANISOU 1307  CA  ILE A1165      504   2642   1870    124    248     57       C  
ATOM   1308  C   ILE A1165      21.676  12.353   3.253  1.00 13.49           C  
ANISOU 1308  C   ILE A1165      348   2669   2109    142    403     96       C  
ATOM   1309  O   ILE A1165      22.887  12.043   3.126  1.00 14.94           O  
ANISOU 1309  O   ILE A1165      372   3152   2152    307    414    115       O  
ATOM   1310  CB  ILE A1165      19.871  10.786   2.422  1.00 12.96           C  
ANISOU 1310  CB  ILE A1165      285   2795   1842     92    212     -8       C  
ATOM   1311  CG1 ILE A1165      19.092   9.519   2.808  1.00 13.98           C  
ANISOU 1311  CG1 ILE A1165      447   2829   2037     15     87   -104       C  
ATOM   1312  CG2 ILE A1165      20.813  10.508   1.251  1.00 15.49           C  
ANISOU 1312  CG2 ILE A1165      744   3125   2016    208    384   -148       C  
ATOM   1313  CD1 ILE A1165      17.922   9.222   1.872  1.00 15.36           C  
ANISOU 1313  CD1 ILE A1165      362   2982   2492    140   -194   -295       C  
ATOM   1314  N   GLU A1166      21.242  13.581   3.006  1.00 14.05           N  
ANISOU 1314  N   GLU A1166      491   2655   2194     10    491    230       N  
ATOM   1315  CA  GLU A1166      22.167  14.666   2.625  1.00 15.72           C  
ANISOU 1315  CA  GLU A1166      810   2894   2266    -87    500    136       C  
ATOM   1316  C   GLU A1166      23.228  14.922   3.701  1.00 16.32           C  
ANISOU 1316  C   GLU A1166      662   3142   2395   -137    500    -15       C  
ATOM   1317  O   GLU A1166      24.429  15.048   3.403  1.00 18.77           O  
ANISOU 1317  O   GLU A1166      614   3833   2685   -130    621   -142       O  
ATOM   1318  CB  GLU A1166      21.384  15.947   2.337  1.00 16.51           C  
ANISOU 1318  CB  GLU A1166     1001   2799   2474   -197    520    315       C  
ATOM   1319  CG  GLU A1166      20.546  15.850   1.079  1.00 17.77           C  
ANISOU 1319  CG  GLU A1166      891   3282   2578     93    571    537       C  
ATOM   1320  CD  GLU A1166      19.459  16.915   0.990  1.00 21.46           C  
ANISOU 1320  CD  GLU A1166     1676   3364   3115    164    368    754       C  
ATOM   1321  OE1 GLU A1166      19.162  17.598   1.999  1.00 23.81           O  
ANISOU 1321  OE1 GLU A1166     1727   3797   3524    617    599    653       O  
ATOM   1322  OE2 GLU A1166      18.897  17.074  -0.113  1.00 23.76           O  
ANISOU 1322  OE2 GLU A1166     1949   3546   3531    -74    -86   1013       O  
ATOM   1323  N   LYS A1167      22.798  14.994   4.961  1.00 16.60           N  
ANISOU 1323  N   LYS A1167      814   3194   2301    -41    388    -65       N  
ATOM   1324  CA  LYS A1167      23.703  15.331   6.059  1.00 16.87           C  
ANISOU 1324  CA  LYS A1167      867   3109   2433   -102    335   -126       C  
ATOM   1325  C   LYS A1167      24.689  14.210   6.403  1.00 16.31           C  
ANISOU 1325  C   LYS A1167      541   3203   2451    -35    333   -104       C  
ATOM   1326  O   LYS A1167      25.896  14.451   6.572  1.00 17.98           O  
ANISOU 1326  O   LYS A1167      357   3619   2854   -186    322   -104       O  
ATOM   1327  CB  LYS A1167      22.878  15.682   7.305  1.00 17.64           C  
ANISOU 1327  CB  LYS A1167     1130   3212   2360     57    285   -228       C  
ATOM   1328  CG  LYS A1167      23.685  15.898   8.577  1.00 21.59           C  
ANISOU 1328  CG  LYS A1167     1747   3781   2675   -219     49   -454       C  
ATOM   1329  CD  LYS A1167      24.322  17.271   8.631  1.00 26.41           C  
ANISOU 1329  CD  LYS A1167     2492   4359   3183   -496      5   -715       C  
ATOM   1330  CE  LYS A1167      24.840  17.568  10.036  1.00 26.97           C  
ANISOU 1330  CE  LYS A1167     2416   4514   3318   -644      0   -886       C  
ATOM   1331  NZ  LYS A1167      25.630  18.831  10.084  1.00 29.39           N  
ANISOU 1331  NZ  LYS A1167     2734   4877   3553   -687    241   -841       N  
ATOM   1332  N   TYR A1168      24.192  12.983   6.495  1.00 15.80           N  
ANISOU 1332  N   TYR A1168      410   3134   2460    120    368    -63       N  
ATOM   1333  CA  TYR A1168      24.966  11.898   7.090  1.00 16.26           C  
ANISOU 1333  CA  TYR A1168      527   3298   2353    261    274   -147       C  
ATOM   1334  C   TYR A1168      25.478  10.857   6.103  1.00 16.33           C  
ANISOU 1334  C   TYR A1168      395   3528   2283    443    285   -185       C  
ATOM   1335  O   TYR A1168      26.368  10.078   6.467  1.00 18.30           O  
ANISOU 1335  O   TYR A1168      562   3860   2531    688     65   -307       O  
ATOM   1336  CB  TYR A1168      24.142  11.210   8.193  1.00 15.89           C  
ANISOU 1336  CB  TYR A1168      593   3296   2148    274    274   -120       C  
ATOM   1337  CG  TYR A1168      23.803  12.153   9.321  1.00 15.31           C  
ANISOU 1337  CG  TYR A1168      289   3228   2299    197    197   -197       C  
ATOM   1338  CD1 TYR A1168      24.767  12.525  10.253  1.00 16.07           C  
ANISOU 1338  CD1 TYR A1168      362   3384   2361    197      3   -292       C  
ATOM   1339  CD2 TYR A1168      22.505  12.676   9.459  1.00 15.27           C  
ANISOU 1339  CD2 TYR A1168      311   3330   2161    241    262    -93       C  
ATOM   1340  CE1 TYR A1168      24.495  13.396  11.278  1.00 15.94           C  
ANISOU 1340  CE1 TYR A1168      285   3362   2409     83    243   -289       C  
ATOM   1341  CE2 TYR A1168      22.226  13.542  10.479  1.00 15.06           C  
ANISOU 1341  CE2 TYR A1168      478   3093   2152   -102    131   -115       C  
ATOM   1342  CZ  TYR A1168      23.200  13.902  11.400  1.00 15.10           C  
ANISOU 1342  CZ  TYR A1168      262   3111   2363     87     98   -296       C  
ATOM   1343  OH  TYR A1168      22.901  14.782  12.419  1.00 16.98           O  
ANISOU 1343  OH  TYR A1168      256   3535   2659    -52     77   -610       O  
ATOM   1344  N   VAL A1169      24.945  10.833   4.884  1.00 16.94           N  
ANISOU 1344  N   VAL A1169      342   3785   2308    328    324   -214       N  
ATOM   1345  CA  VAL A1169      25.348   9.824   3.904  1.00 19.42           C  
ANISOU 1345  CA  VAL A1169      645   4219   2515    537    388   -164       C  
ATOM   1346  C   VAL A1169      26.101  10.414   2.709  1.00 22.34           C  
ANISOU 1346  C   VAL A1169      804   4820   2863    494    894     27       C  
ATOM   1347  O   VAL A1169      27.180   9.937   2.362  1.00 23.60           O  
ANISOU 1347  O   VAL A1169      646   5317   3003    798    850    -31       O  
ATOM   1348  CB  VAL A1169      24.158   8.967   3.410  1.00 18.33           C  
ANISOU 1348  CB  VAL A1169      638   3844   2480    573    194   -263       C  
ATOM   1349  CG1 VAL A1169      24.650   7.899   2.431  1.00 20.33           C  
ANISOU 1349  CG1 VAL A1169      895   4162   2666    724     31   -410       C  
ATOM   1350  CG2 VAL A1169      23.450   8.323   4.584  1.00 19.34           C  
ANISOU 1350  CG2 VAL A1169     1053   3671   2623    507     97   -196       C  
ATOM   1351  N  AILE A1170      25.536  11.445   2.090  0.50 25.94           N  
ANISOU 1351  N  AILE A1170     1238   5400   3219    381   1167    408       N  
ATOM   1352  N  BILE A1170      25.537  11.439   2.079  0.50 25.94           N  
ANISOU 1352  N  BILE A1170     1237   5400   3219    383   1167    408       N  
ATOM   1353  CA AILE A1170      26.162  12.092   0.940  0.50 32.66           C  
ANISOU 1353  CA AILE A1170     2319   6280   3810    -57   1448    728       C  
ATOM   1354  CA BILE A1170      26.180  12.076   0.932  0.50 32.66           C  
ANISOU 1354  CA BILE A1170     2319   6280   3810    -57   1448    728       C  
ATOM   1355  C  AILE A1170      27.315  12.971   1.403  0.50 36.82           C  
ANISOU 1355  C  AILE A1170     2773   6977   4239   -584   1456    697       C  
ATOM   1356  C  BILE A1170      27.270  13.027   1.419  0.50 36.81           C  
ANISOU 1356  C  BILE A1170     2773   6977   4237   -584   1456    697       C  
ATOM   1357  O  AILE A1170      27.122  13.890   2.196  0.50 40.85           O  
ANISOU 1357  O  AILE A1170     3231   7713   4578  -1010   1526    513       O  
ATOM   1358  O  BILE A1170      27.016  13.900   2.250  0.50 40.85           O  
ANISOU 1358  O  BILE A1170     3231   7713   4578  -1010   1526    515       O  
ATOM   1359  CB AILE A1170      25.158  12.967   0.147  0.50 32.66           C  
ANISOU 1359  CB AILE A1170     2469   6171   3768    -17   1410    929       C  
ATOM   1360  CB BILE A1170      25.170  12.863   0.065  0.50 32.66           C  
ANISOU 1360  CB BILE A1170     2469   6171   3767    -17   1411    929       C  
ATOM   1361  CG1AILE A1170      23.922  12.148  -0.273  0.50 33.07           C  
ANISOU 1361  CG1AILE A1170     2574   6165   3826    197   1360    820       C  
ATOM   1362  CG1BILE A1170      24.114  11.919  -0.515  0.50 33.06           C  
ANISOU 1362  CG1BILE A1170     2569   6165   3826    197   1360    820       C  
ATOM   1363  CG2AILE A1170      25.846  13.613  -1.066  0.50 34.05           C  
ANISOU 1363  CG2AILE A1170     2576   6557   3806    120   1571   1014       C  
ATOM   1364  CG2BILE A1170      25.898  13.617  -1.052  0.50 34.05           C  
ANISOU 1364  CG2BILE A1170     2574   6557   3806    120   1571   1014       C  
ATOM   1365  CD1AILE A1170      24.248  10.789  -0.885  0.50 32.94           C  
ANISOU 1365  CD1AILE A1170     2585   6082   3849    362   1149    807       C  
ATOM   1366  CD1BILE A1170      22.939  12.636  -1.178  0.50 33.14           C  
ANISOU 1366  CD1BILE A1170     2594   6093   3903    384   1106    807       C  
TER    1367      ILE A1170                                                      
HETATM 1368  P   PO4 A   1       5.072  13.619  13.693  1.00 13.65           P  
ANISOU 1368  P   PO4 A   1      320   3075   1791    -46    274    -34       P  
HETATM 1369  O1  PO4 A   1       6.106  14.649  13.264  1.00 13.51           O  
ANISOU 1369  O1  PO4 A   1      291   2935   1905    230    175     60       O  
HETATM 1370  O2  PO4 A   1       4.360  13.130  12.425  1.00 14.95           O  
ANISOU 1370  O2  PO4 A   1      410   3366   1905     82    489   -328       O  
HETATM 1371  O3  PO4 A   1       5.643  12.397  14.359  1.00 13.69           O  
ANISOU 1371  O3  PO4 A   1      384   2831   1985   -285    412      3       O  
HETATM 1372  O4  PO4 A   1       4.038  14.233  14.641  1.00 14.45           O  
ANISOU 1372  O4  PO4 A   1      318   3348   1826    164    285   -164       O  
HETATM 1373  C1  BME A1174       4.781  11.652   4.964  0.50 27.69           C  
ANISOU 1373  C1  BME A1174     3370   3418   3734     13     48    -35       C  
HETATM 1374  C2  BME A1174       4.822  11.780   6.481  0.50 29.48           C  
ANISOU 1374  C2  BME A1174     3522   3774   3905     -3    -40    242       C  
HETATM 1375  O1  BME A1174       4.809  12.940   4.394  0.50 30.81           O  
ANISOU 1375  O1  BME A1174     3704   4007   3995    -87   -109   -142       O  
HETATM 1376  S2  BME A1174       3.897  10.470   7.314  0.50 37.46           S  
ANISOU 1376  S2  BME A1174     4505   4910   4816    -82      0    -65       S  
HETATM 1377  C1  BME A   2      31.941   5.668   9.642  1.00 45.25           C  
ANISOU 1377  C1  BME A   2     5758   5799   5636    126   -161    -81       C  
HETATM 1378  C2  BME A   2      32.113   7.084   9.118  1.00 46.23           C  
ANISOU 1378  C2  BME A   2     5881   5896   5787    115   -184    -15       C  
HETATM 1379  O1  BME A   2      32.848   4.826   8.968  1.00 44.94           O  
ANISOU 1379  O1  BME A   2     5651   5741   5683    153   -160    -51       O  
HETATM 1380  S2  BME A   2      30.905   8.216   9.837  1.00 49.10           S  
ANISOU 1380  S2  BME A   2     6111   6334   6211    114    -65   -137       S  
HETATM 1381  O   HOH A1175      22.648  -5.597   8.297  1.00 36.79           O  
ANISOU 1381  O   HOH A1175     4517   4819   4643    -43   -119     35       O  
HETATM 1382  O   HOH A1176      25.181   8.246  23.385  1.00 38.19           O  
ANISOU 1382  O   HOH A1176     4528   5008   4975      6   -131    -13       O  
HETATM 1383  O   HOH A1177      10.298  -1.929   0.772  1.00 38.08           O  
ANISOU 1383  O   HOH A1177     4611   5008   4848     48    -12    -54       O  
HETATM 1384  O   HOH A1178      20.996   2.776  29.976  1.00 35.56           O  
ANISOU 1384  O   HOH A1178     4359   4657   4496     87   -108    -71       O  
HETATM 1385  O   HOH A1179      22.824  18.903  28.988  1.00 39.30           O  
ANISOU 1385  O   HOH A1179     4884   5163   4884    -57     43    -35       O  
HETATM 1386  O   HOH A1180      20.332   6.040  37.438  1.00 35.00           O  
ANISOU 1386  O   HOH A1180     4074   4754   4472     93    -76    -52       O  
HETATM 1387  O   HOH A1181       8.556  28.226  27.113  1.00 37.96           O  
ANISOU 1387  O   HOH A1181     4616   4910   4896      0     97     20       O  
HETATM 1388  O   HOH A1182       8.576  -4.758   7.515  1.00 37.60           O  
ANISOU 1388  O   HOH A1182     4548   4898   4839     65    -63    -38       O  
HETATM 1389  O   HOH A1183      16.328 -14.416   3.423  1.00 35.16           O  
ANISOU 1389  O   HOH A1183     4189   4665   4507    -85    -43    -10       O  
HETATM 1390  O   HOH A1184       8.982  27.703  21.295  1.00 38.67           O  
ANISOU 1390  O   HOH A1184     4702   4970   5019    -49     26     49       O  
HETATM 1391  O   HOH A1185      11.882  -7.740   3.809  1.00 40.22           O  
ANISOU 1391  O   HOH A1185     5138   5174   4970    -38     30     54       O  
HETATM 1392  O   HOH A1186      -2.145  14.681  26.957  1.00 38.54           O  
ANISOU 1392  O   HOH A1186     4747   5076   4819     35     13     43       O  
HETATM 1393  O   HOH A1187      14.138  22.403  34.616  1.00 38.20           O  
ANISOU 1393  O   HOH A1187     4665   5102   4749      0     26     49       O  
HETATM 1394  O   HOH A1188      10.296  13.719  35.223  1.00 40.24           O  
ANISOU 1394  O   HOH A1188     5044   5199   5044    -63     91   -108       O  
HETATM 1395  O   HOH A1189       7.939  25.195   6.494  1.00 39.60           O  
ANISOU 1395  O   HOH A1189     4855   5212   4978     -3    -81    -51       O  
HETATM 1396  O   HOH A1190       1.749  26.482  28.080  1.00 38.98           O  
ANISOU 1396  O   HOH A1190     4881   4995   4934     -6     35     76       O  
HETATM 1397  O   HOH A1191      35.341   9.788  14.757  1.00 39.69           O  
ANISOU 1397  O   HOH A1191     4925   5041   5112     43     -6     26       O  
HETATM 1398  O   HOH A1192      14.746  25.685  20.914  1.00 36.41           O  
ANISOU 1398  O   HOH A1192     4363   4708   4763     62    118    -63       O  
HETATM 1399  O   HOH A1193      24.346  -0.195  26.947  1.00 38.76           O  
ANISOU 1399  O   HOH A1193     4805   4988   4934      0    103    -57       O  
HETATM 1400  O   HOH A1194       6.857  22.869  25.455  1.00 19.27           O  
ANISOU 1400  O   HOH A1194      868   3639   2813    240    502   -436       O  
HETATM 1401  O   HOH A1195      34.800  -0.048  11.826  1.00 21.38           O  
ANISOU 1401  O   HOH A1195      528   4429   3165   1001    311    -27       O  
HETATM 1402  O   HOH A1196       2.358  17.922  35.117  1.00 20.63           O  
ANISOU 1402  O   HOH A1196     1693   3804   2343   -412    724    219       O  
HETATM 1403  O   HOH A1197       8.782   6.113  15.071  1.00 16.02           O  
ANISOU 1403  O   HOH A1197      629   3382   2074   -109    452   -270       O  
HETATM 1404  O   HOH A1198       9.555  10.684  34.609  1.00 28.19           O  
ANISOU 1404  O   HOH A1198     2754   4598   3359    282    513   -582       O  
HETATM 1405  O   HOH A1199       1.497  14.484  13.350  1.00 24.30           O  
ANISOU 1405  O   HOH A1199      518   5296   3418    710    199   -649       O  
HETATM 1406  O   HOH A1200       5.114   6.284  20.544  1.00 22.44           O  
ANISOU 1406  O   HOH A1200     1924   3865   2736   -625   1136   -275       O  
HETATM 1407  O   HOH A1201      -0.069  22.867  38.698  1.00 26.53           O  
ANISOU 1407  O   HOH A1201     1686   4356   4038   -397   1577    247       O  
HETATM 1408  O   HOH A1202      26.906   7.774  10.147  1.00 20.77           O  
ANISOU 1408  O   HOH A1202      419   4641   2833    401     27   -489       O  
HETATM 1409  O   HOH A1203      27.027  18.131  17.125  1.00 38.65           O  
ANISOU 1409  O   HOH A1203     2669   7250   4765   1234   1553    186       O  
HETATM 1410  O   HOH A1204       2.148   6.730  27.079  1.00 27.33           O  
ANISOU 1410  O   HOH A1204     2881   4359   3145   -575   1071    500       O  
HETATM 1411  O   HOH A1205      30.244   3.700  16.184  1.00 32.35           O  
ANISOU 1411  O   HOH A1205     1492   6441   4356   1080     27   1519       O  
HETATM 1412  O   HOH A1206       1.443   7.514  17.555  1.00 23.79           O  
ANISOU 1412  O   HOH A1206     1124   4539   3375   -763    643   -252       O  
HETATM 1413  O   HOH A1207      14.512  18.116  35.198  1.00 32.56           O  
ANISOU 1413  O   HOH A1207     2477   6269   3625    731   -304  -1823       O  
HETATM 1414  O   HOH A1208      28.049   9.883   8.557  1.00 25.71           O  
ANISOU 1414  O   HOH A1208     1437   4928   3402    714   -592   -193       O  
HETATM 1415  O   HOH A1209       6.163   8.225  28.772  1.00 26.66           O  
ANISOU 1415  O   HOH A1209     2842   4356   2933     51    864    281       O  
HETATM 1416  O   HOH A1210      22.177  22.776  14.910  1.00 22.04           O  
ANISOU 1416  O   HOH A1210      746   4198   3429   -340    260     52       O  
HETATM 1417  O   HOH A1211      24.973  15.618  13.983  1.00 25.12           O  
ANISOU 1417  O   HOH A1211      560   5223   3761   -678   -170   -683       O  
HETATM 1418  O   HOH A1212      22.576  21.214  11.953  1.00 26.39           O  
ANISOU 1418  O   HOH A1212     1291   4905   3831   -615    165    427       O  
HETATM 1419  O   HOH A1213       8.922  24.252  26.825  1.00 22.01           O  
ANISOU 1419  O   HOH A1213     1165   3914   3282   -140    696   -505       O  
HETATM 1420  O   HOH A1214      17.814  18.868  -1.812  1.00 21.18           O  
ANISOU 1420  O   HOH A1214     1238   3544   3264   -219    -20    166       O  
HETATM 1421  O   HOH A1215      10.542  19.064   5.020  1.00 22.88           O  
ANISOU 1421  O   HOH A1215     1421   4605   2666   1133    458    559       O  
HETATM 1422  O   HOH A1216       8.434   4.924   4.521  1.00 26.56           O  
ANISOU 1422  O   HOH A1216      935   5533   3625    -40    505   -344       O  
HETATM 1423  O   HOH A1217      -3.978   6.156  29.168  1.00 41.47           O  
ANISOU 1423  O   HOH A1217     5640   5978   4138  -2344   2222   -577       O  
HETATM 1424  O   HOH A1218       6.438  22.509  32.975  1.00 24.95           O  
ANISOU 1424  O   HOH A1218     1351   4785   3343   -636    714   -339       O  
HETATM 1425  O   HOH A1219       7.019  24.578  28.724  1.00 23.58           O  
ANISOU 1425  O   HOH A1219     1360   4176   3425     -5    876   -307       O  
HETATM 1426  O   HOH A1220      27.565  16.513  23.201  1.00 34.37           O  
ANISOU 1426  O   HOH A1220     1509   7699   3849    540   -264   -926       O  
HETATM 1427  O   HOH A1221      12.145  26.275  15.829  1.00 28.79           O  
ANISOU 1427  O   HOH A1221     1942   4805   4189   -114    868   -416       O  
HETATM 1428  O   HOH A1222       9.990  26.674  25.896  1.00 35.29           O  
ANISOU 1428  O   HOH A1222     3533   4629   5248  -1142   1720   -531       O  
HETATM 1429  O   HOH A1223      11.850  15.909  -0.678  1.00 26.07           O  
ANISOU 1429  O   HOH A1223     2035   5005   2865   -410    -76    511       O  
HETATM 1430  O   HOH A1224      10.458  23.169  31.568  1.00 27.76           O  
ANISOU 1430  O   HOH A1224     1967   4720   3862    -24    120  -1525       O  
HETATM 1431  O   HOH A1225       0.363   6.372  22.695  1.00 44.54           O  
ANISOU 1431  O   HOH A1225     5378   6923   4623  -2451   1606    518       O  
HETATM 1432  O   HOH A1226      24.505   4.799  16.401  1.00 30.77           O  
ANISOU 1432  O   HOH A1226     3743   4695   3255   1720   -731     98       O  
HETATM 1433  O   HOH A1227      28.395   5.334   2.735  1.00 28.21           O  
ANISOU 1433  O   HOH A1227     1465   6190   3064     31    474   -524       O  
HETATM 1434  O   HOH A1228      12.709  25.472   8.831  1.00 38.00           O  
ANISOU 1434  O   HOH A1228     3467   3964   7009    394   1523   -443       O  
HETATM 1435  O   HOH A1229       9.396  -0.184  21.439  1.00 37.81           O  
ANISOU 1435  O   HOH A1229     5345   4232   4790    175      0    -49       O  
HETATM 1436  O   HOH A1230      22.198  16.477  29.233  1.00 28.07           O  
ANISOU 1436  O   HOH A1230     1481   6054   3129    649   -186   -241       O  
HETATM 1437  O   HOH A1231       4.010   5.658   4.910  1.00 39.83           O  
ANISOU 1437  O   HOH A1231     3364   6832   4935   -564  -1598    263       O  
HETATM 1438  O   HOH A1232       1.194  21.054  18.653  1.00 33.60           O  
ANISOU 1438  O   HOH A1232     3170   5486   4110   1524    626   -794       O  
HETATM 1439  O   HOH A1233      20.575  17.961   5.369  1.00 27.49           O  
ANISOU 1439  O   HOH A1233     3050   3583   3813   -283   1280   -351       O  
HETATM 1440  O   HOH A1234      16.620  21.469   3.931  1.00 27.53           O  
ANISOU 1440  O   HOH A1234     2790   3777   3892   -118   1023   -315       O  
HETATM 1441  O   HOH A1235       0.666  17.055  13.499  1.00 42.92           O  
ANISOU 1441  O   HOH A1235     3941   5518   6847   1518   -546   -207       O  
HETATM 1442  O   HOH A1236      30.209  -1.177   7.429  1.00 38.12           O  
ANISOU 1442  O   HOH A1236     5166   4826   4490   1955   1106     86       O  
HETATM 1443  O   HOH A1237      12.617  25.592  25.336  1.00 31.05           O  
ANISOU 1443  O   HOH A1237     3210   3993   4593   -803    254   -820       O  
HETATM 1444  O   HOH A1238      23.527  24.076  11.173  1.00 45.30           O  
ANISOU 1444  O   HOH A1238     5938   5594   5680   1976   -696    489       O  
HETATM 1445  O   HOH A1239      28.738  15.951  20.790  1.00 36.39           O  
ANISOU 1445  O   HOH A1239     2754   5848   5224   -148    680    -68       O  
HETATM 1446  O   HOH A1240      23.383   3.412  24.991  1.00 33.76           O  
ANISOU 1446  O   HOH A1240     2583   6649   3596    750    401    575       O  
HETATM 1447  O   HOH A1241      13.943  -8.629   5.098  1.00 40.10           O  
ANISOU 1447  O   HOH A1241     4447   5942   4848   -260   2064   -511       O  
HETATM 1448  O   HOH A1242      27.172  10.085  24.609  1.00 33.43           O  
ANISOU 1448  O   HOH A1242     2556   6337   3810    741   -759   -297       O  
HETATM 1449  O   HOH A1243      10.997  19.345   0.000  0.50 30.21           O  
ANISOU 1449  O   HOH A1243      964   7307   3206      0      0  -1018       O  
HETATM 1450  O   HOH A1244       7.975  21.028  34.421  1.00 34.34           O  
ANISOU 1450  O   HOH A1244     2578   5526   4942    636   1377   1439       O  
HETATM 1451  O   HOH A1245       2.468  15.335  36.389  1.00 35.39           O  
ANISOU 1451  O   HOH A1245     2915   4713   5817    794   1314   1089       O  
HETATM 1452  O   HOH A1246      16.865   5.360  31.014  1.00 46.69           O  
ANISOU 1452  O   HOH A1246     5708   5802   6230    175     31   -454       O  
HETATM 1453  O   HOH A1247      26.378  12.749  18.580  1.00 30.98           O  
ANISOU 1453  O   HOH A1247     1676   6035   4059    159   -621  -1243       O  
HETATM 1454  O   HOH A1248      -0.332  10.773  20.966  1.00 32.00           O  
ANISOU 1454  O   HOH A1248     2637   5684   3837   -296     -5   -890       O  
HETATM 1455  O   HOH A1249      11.824  13.301  36.898  1.00 44.93           O  
ANISOU 1455  O   HOH A1249     5422   5586   6065    353   2169   1076       O  
HETATM 1456  O   HOH A1250      20.347  26.214  18.304  1.00 43.13           O  
ANISOU 1456  O   HOH A1250     3765   6757   5866   1009    187  -1992       O  
HETATM 1457  O   HOH A1251       4.324  14.598   6.541  1.00 41.61           O  
ANISOU 1457  O   HOH A1251     3589   6941   5281   -850   -294    -76       O  
HETATM 1458  O   HOH A1252       8.621  24.245  10.740  1.00 29.74           O  
ANISOU 1458  O   HOH A1252     1949   4954   4393    -43    604    992       O  
HETATM 1459  O   HOH A1253      11.778   0.135  24.369  1.00 36.76           O  
ANISOU 1459  O   HOH A1253     5389   3567   5011    -60    754    996       O  
HETATM 1460  O   HOH A1254       9.888  -0.758  35.513  1.00 31.51           O  
ANISOU 1460  O   HOH A1254     2374   5138   4458    320   -785    537       O  
HETATM 1461  O   HOH A1255       4.780   3.763  26.575  1.00 35.74           O  
ANISOU 1461  O   HOH A1255     4313   5249   4018   -243   1656    438       O  
HETATM 1462  O   HOH A1256      23.282  21.301  22.028  1.00 32.04           O  
ANISOU 1462  O   HOH A1256     3463   4887   3822   -608   -631   -597       O  
HETATM 1463  O   HOH A1257       7.941  14.365  37.260  1.00 40.08           O  
ANISOU 1463  O   HOH A1257     4440   6524   4266    644   -974    135       O  
HETATM 1464  O   HOH A1258       1.722  14.849  10.450  1.00 31.15           O  
ANISOU 1464  O   HOH A1258     1482   6000   4352    381     54   -573       O  
HETATM 1465  O   HOH A1259       1.723  19.389  21.108  1.00 31.25           O  
ANISOU 1465  O   HOH A1259     1203   5579   5091   -531   1272  -1142       O  
HETATM 1466  O   HOH A1260      13.879  -0.704  22.992  1.00 44.41           O  
ANISOU 1466  O   HOH A1260     6211   4956   5705   -207    533    364       O  
HETATM 1467  O   HOH A1261      25.482 -11.939   5.879  1.00 50.43           O  
ANISOU 1467  O   HOH A1261     5870   6710   6582   -326    511   2029       O  
HETATM 1468  O   HOH A1262      18.477  26.238  19.621  1.00 43.72           O  
ANISOU 1468  O   HOH A1262     6011   6503   4099  -1537   -780  -1202       O  
HETATM 1469  O   HOH A1263       5.501   1.916  19.505  1.00 42.46           O  
ANISOU 1469  O   HOH A1263     4794   6147   5191  -2256   1379    392       O  
HETATM 1470  O   HOH A1264      19.222   6.496  33.257  1.00 47.53           O  
ANISOU 1470  O   HOH A1264     5065   6294   6699   1596    877   2458       O  
HETATM 1471  O   HOH A1265       2.919  27.620  21.884  1.00 35.66           O  
ANISOU 1471  O   HOH A1265     3609   5141   4801   2123     27    886       O  
HETATM 1472  O   HOH A1266      17.790  26.660   6.901  1.00 37.21           O  
ANISOU 1472  O   HOH A1266     5885   4978   3273  -1622   -241    -17       O  
HETATM 1473  O   HOH A1267      29.388  10.115  12.889  1.00 32.49           O  
ANISOU 1473  O   HOH A1267     2585   5198   4562   1193    593    175       O  
HETATM 1474  O   HOH A1268      -0.461  13.107  14.399  1.00 42.40           O  
ANISOU 1474  O   HOH A1268     4370   6230   5511   -719    623   1084       O  
HETATM 1475  O   HOH A1269       5.386  24.449  34.654  1.00 34.98           O  
ANISOU 1475  O   HOH A1269     3864   4711   4715  -1391   1879   -684       O  
HETATM 1476  O   HOH A1270      34.451   7.195  11.435  1.00 37.54           O  
ANISOU 1476  O   HOH A1270     3368   6226   4668   -313   -120    860       O  
HETATM 1477  O   HOH A1271      29.092  18.998  20.837  1.00 49.68           O  
ANISOU 1477  O   HOH A1271     3580   7092   8205  -1164   -820    -76       O  
HETATM 1478  O   HOH A1272      20.373  20.791  35.414  1.00 37.23           O  
ANISOU 1478  O   HOH A1272     4827   5253   4065    -60   -428   -825       O  
HETATM 1479  O   HOH A1273       3.450   6.899  32.517  1.00 34.85           O  
ANISOU 1479  O   HOH A1273     4663   4496   4083   -737   -630    339       O  
HETATM 1480  O   HOH A1274      26.656  21.693  18.206  1.00 48.01           O  
ANISOU 1480  O   HOH A1274     5396   7203   5641   -597    988    218       O  
HETATM 1481  O   HOH A1275      18.687  23.923  20.216  1.00 45.95           O  
ANISOU 1481  O   HOH A1275     5824   7257   4379    882    653   -978       O  
HETATM 1482  O   HOH A1276      10.114  25.187  12.410  1.00 40.92           O  
ANISOU 1482  O   HOH A1276     5004   6298   4246  -1093   1569    926       O  
HETATM 1483  O   HOH A1277      12.289  13.441  -1.370  1.00 40.23           O  
ANISOU 1483  O   HOH A1277     1977   6140   7166   1225    485    109       O  
HETATM 1484  O   HOH A1278       5.331  -2.750  14.826  1.00 47.31           O  
ANISOU 1484  O   HOH A1278     5396   5572   7008   -549   -851    649       O  
HETATM 1485  O   HOH A1279       6.985   3.981  31.046  1.00 41.57           O  
ANISOU 1485  O   HOH A1279     5098   6043   4654   1254  -1243    640       O  
HETATM 1486  O   HOH A1280      25.298   8.891  36.418  1.00 41.35           O  
ANISOU 1486  O   HOH A1280     4277   6682   4751   1127  -1203    -35       O  
HETATM 1487  O   HOH A1281      29.884   7.424  19.008  1.00 38.76           O  
ANISOU 1487  O   HOH A1281     3497   6348   4881   2353  -1956  -1625       O  
HETATM 1488  O   HOH A1282       0.820  17.106  19.696  1.00 35.34           O  
ANISOU 1488  O   HOH A1282     2211   6219   4996   -417    644    -57       O  
HETATM 1489  O   HOH A1283      12.189  25.757   4.768  1.00 50.06           O  
ANISOU 1489  O   HOH A1283     6593   6481   5946   -197    584   1516       O  
HETATM 1490  O   HOH A1284      -1.312  19.848  25.688  1.00 27.43           O  
ANISOU 1490  O   HOH A1284     2099   5267   3055     98    476   -104       O  
HETATM 1491  O   HOH A1285      24.215  20.345  24.312  1.00 39.40           O  
ANISOU 1491  O   HOH A1285     3655   6898   4417  -2081  -1622   -197       O  
HETATM 1492  O   HOH A1286      11.109  -1.502   7.684  1.00 36.26           O  
ANISOU 1492  O   HOH A1286     3495   5842   4442  -2064   1527  -1456       O  
HETATM 1493  O   HOH A1287       2.152  11.565  33.908  1.00 41.22           O  
ANISOU 1493  O   HOH A1287     5677   6534   3452  -1546   1659   -115       O  
HETATM 1494  O   HOH A1288      24.875  -5.025   7.853  1.00 49.77           O  
ANISOU 1494  O   HOH A1288     6017   7469   5425    230    208  -1032       O  
HETATM 1495  O   HOH A1289      23.178  21.842  37.325  1.00 45.43           O  
ANISOU 1495  O   HOH A1289     5137   6545   5580   1428   2861   1230       O  
HETATM 1496  O   HOH A1290       7.881  24.098  31.215  1.00 26.99           O  
ANISOU 1496  O   HOH A1290     2152   4711   3393   -467   1105   -416       O  
HETATM 1497  O   HOH A1291      12.594  26.235  12.075  1.00 42.32           O  
ANISOU 1497  O   HOH A1291     5102   5167   5812   -230   -706   1668       O  
HETATM 1498  O   HOH A1292      24.740   5.496  24.008  1.00 60.68           O  
ANISOU 1498  O   HOH A1292     7354   7455   8248    570    983  -1922       O  
HETATM 1499  O   HOH A1293      20.676  25.244  16.245  1.00 43.67           O  
ANISOU 1499  O   HOH A1293     5770   6423   4399    357  -1243   -929       O  
HETATM 1500  O   HOH A1294       7.950  11.326  -2.275  1.00 44.53           O  
ANISOU 1500  O   HOH A1294     5508   6933   4480    271  -1333   -943       O  
HETATM 1501  O   HOH A1295      11.493  27.410  21.793  1.00 35.95           O  
ANISOU 1501  O   HOH A1295     3368   3943   6348   -152   1269   -544       O  
HETATM 1502  O   HOH A1296      18.949  12.597  35.675  1.00 49.13           O  
ANISOU 1502  O   HOH A1296     7734   8062   2870   1186    375   -864       O  
HETATM 1503  O   HOH A1297       2.588  10.806  10.971  1.00 40.48           O  
ANISOU 1503  O   HOH A1297     5184   6251   3944    540   -219    834       O  
HETATM 1504  O   HOH A1298      10.686 -11.520   2.279  1.00 42.88           O  
ANISOU 1504  O   HOH A1298     5271   5878   5144    794   -877    529       O  
HETATM 1505  O   HOH A1299      16.993  25.440  32.647  1.00 42.06           O  
ANISOU 1505  O   HOH A1299     5554   5230   5195   -405    185  -1412       O  
HETATM 1506  O   HOH A1300      19.906   4.074  33.666  1.00 44.02           O  
ANISOU 1506  O   HOH A1300     4688   6262   5777    891   -516   2002       O  
HETATM 1507  O   HOH A1301      13.956  14.116  -2.989  1.00 34.06           O  
ANISOU 1507  O   HOH A1301     6125   3752   3063   -750   -463    -38       O  
HETATM 1508  O   HOH A1302      18.937  21.910  21.262  1.00 42.39           O  
ANISOU 1508  O   HOH A1302     4485   7171   4451   -147    544  -1286       O  
HETATM 1509  O   HOH A1303      20.506  27.029  14.580  1.00 42.68           O  
ANISOU 1509  O   HOH A1303     4582   4388   7246   -126  -1729    575       O  
HETATM 1510  O   HOH A1304      14.076  16.778  -3.541  1.00 37.69           O  
ANISOU 1510  O   HOH A1304     3869   6359   4092  -1641  -2029   2144       O  
HETATM 1511  O   HOH A1305      26.922  15.574  18.190  1.00 37.07           O  
ANISOU 1511  O   HOH A1305     1544   5982   6557  -1035    658  -1921       O  
HETATM 1512  O   HOH A1306       5.204  27.585  18.095  1.00 32.06           O  
ANISOU 1512  O   HOH A1306     3176   4431   4573    175   -560   -485       O  
HETATM 1513  O   HOH A1307      16.233  20.552  34.976  1.00 56.40           O  
ANISOU 1513  O   HOH A1307     7009   7149   7271  -1541   -326  -1133       O  
HETATM 1514  O   HOH A1308      -1.256   1.524  15.930  1.00 47.26           O  
ANISOU 1514  O   HOH A1308     4559   6129   7268  -1674   1155   -456       O  
HETATM 1515  O   HOH A1309      30.833  10.461  16.911  1.00 51.40           O  
ANISOU 1515  O   HOH A1309     5461   6496   7573  -1199    230   -302       O  
HETATM 1516  O   HOH A1310       7.309  28.654  16.191  1.00 47.33           O  
ANISOU 1516  O   HOH A1310     5921   5920   6144   1272    566   2125       O  
HETATM 1517  O   HOH A1311      24.732  24.691  15.253  1.00 50.64           O  
ANISOU 1517  O   HOH A1311     6564   6593   6082    164   -674   1571       O  
HETATM 1518  O   HOH A1312      13.571  -4.242  14.694  1.00 34.99           O  
ANISOU 1518  O   HOH A1312     3998   4007   5288    438   1745    218       O  
HETATM 1519  O   HOH A1313      23.255  20.572   9.350  1.00 49.90           O  
ANISOU 1519  O   HOH A1313     6575   6261   6122    794    -20    942       O  
HETATM 1520  O   HOH A1314      16.702  11.240  36.290  1.00 41.59           O  
ANISOU 1520  O   HOH A1314     5059   7245   3499    891   -340    -17       O  
HETATM 1521  O   HOH A1315       4.146  20.210   2.820  1.00 37.07           O  
ANISOU 1521  O   HOH A1315     2522   7950   3612   1303   -593    445       O  
HETATM 1522  O   HOH A1316       8.762  -2.118   7.196  1.00 42.09           O  
ANISOU 1522  O   HOH A1316     3790   6065   6136  -1835   -239    807       O  
HETATM 1523  O   HOH A1317      27.849   1.903  14.334  1.00 50.40           O  
ANISOU 1523  O   HOH A1317     5741   7098   6312   -575    152   -419       O  
HETATM 1524  O   HOH A1318       2.151  25.966  33.710  1.00 44.33           O  
ANISOU 1524  O   HOH A1318     6984   5084   4774   1164   3115   -238       O  
HETATM 1525  O   HOH A1319       8.702  -7.732  -2.519  1.00 43.32           O  
ANISOU 1525  O   HOH A1319     5497   6309   4652   -109    271  -1684       O  
HETATM 1526  O   HOH A1320       0.420  20.851  23.294  1.00 36.95           O  
ANISOU 1526  O   HOH A1320     4259   5989   3792    983    553   -626       O  
HETATM 1527  O   HOH A1321      -1.924   3.087  12.267  1.00 47.14           O  
ANISOU 1527  O   HOH A1321     4081   7077   6754    -31    868  -2426       O  
HETATM 1528  O   HOH A1322       3.570  27.731  27.443  1.00 42.16           O  
ANISOU 1528  O   HOH A1322     5497   5155   5368   -882   1562  -1252       O  
HETATM 1529  O   HOH A1323       3.142   3.040   4.431  1.00 37.95           O  
ANISOU 1529  O   HOH A1323     3222   6779   4420  -1727   -452    285       O  
HETATM 1530  O   HOH A1324      28.059  -7.298  -1.215  1.00 41.97           O  
ANISOU 1530  O   HOH A1324     3373   7026   5546  -1571   -608   -357       O  
HETATM 1531  O   HOH A1325      12.312   0.000   0.000  0.50 45.50           O  
ANISOU 1531  O   HOH A1325     5726   5501   6061      0      0    109       O  
HETATM 1532  O   HOH A1326       1.818  -4.987   6.139  1.00 52.01           O  
ANISOU 1532  O   HOH A1326     4386   7667   7710  -1391   1145  -1939       O  
HETATM 1533  O   HOH A1327      -0.268   5.059  30.095  1.00 56.31           O  
ANISOU 1533  O   HOH A1327     6915   7393   7088   -379    762   -259       O  
HETATM 1534  O   HOH A1328      15.211  24.333  34.215  1.00 50.43           O  
ANISOU 1534  O   HOH A1328     6273   6355   6535   1207    854   -328       O  
HETATM 1535  O   HOH A1329       8.524  15.572  39.127  1.00 39.77           O  
ANISOU 1535  O   HOH A1329     4345   5062   5702     87    785    186       O  
HETATM 1536  O   HOH A1330      22.545  14.178  36.424  1.00 49.07           O  
ANISOU 1536  O   HOH A1330     8190   6194   4259    882  -1544   -518       O  
HETATM 1537  O   HOH A1331      13.803   1.920  30.583  1.00 37.47           O  
ANISOU 1537  O   HOH A1331     5503   4744   3991    131   1473    197       O  
HETATM 1538  O   HOH A1332       9.445  12.038  36.894  1.00 53.31           O  
ANISOU 1538  O   HOH A1332     7426   6955   5874  -1102   -463  -2953       O  
HETATM 1539  O   HOH A1333      22.991   3.973  31.479  1.00 53.92           O  
ANISOU 1539  O   HOH A1333     6363   6830   7293  -1430    476   1456       O  
HETATM 1540  O   HOH A1334      -2.715  12.347  27.171  1.00 54.74           O  
ANISOU 1540  O   HOH A1334     7414   6710   6675   -430  -1111   -630       O  
HETATM 1541  O   HOH A1335      27.330   3.604  17.256  1.00 46.97           O  
ANISOU 1541  O   HOH A1335     3977   8475   5393   1361    172   -188       O  
HETATM 1542  O   HOH A1336      29.115  11.725  18.520  1.00 41.24           O  
ANISOU 1542  O   HOH A1336     2687   6219   6765   -148  -1726    395       O  
HETATM 1543  O   HOH A1337      -4.448   2.101  10.325  1.00 52.05           O  
ANISOU 1543  O   HOH A1337     6226   7346   6205   -421   1351   -375       O  
HETATM 1544  O   HOH A1338      24.670 -14.104   8.565  1.00 44.47           O  
ANISOU 1544  O   HOH A1338     5112   5299   6485    263   -339  -1480       O  
HETATM 1545  O   HOH A1339      15.738  -1.052  28.257  1.00 45.68           O  
ANISOU 1545  O   HOH A1339     4834   6219   6301    750  -1067    943       O  
HETATM 1546  O   HOH A1340       7.268  -0.429  19.725  1.00 42.19           O  
ANISOU 1546  O   HOH A1340     6190   6108   3734   -746   1907   -161       O  
HETATM 1547  O   HOH A1341      20.690   2.549  32.149  1.00 51.62           O  
ANISOU 1547  O   HOH A1341     7871   6345   5399   -649  -1896   -434       O  
HETATM 1548  O   HOH A1342      -0.899   4.961  19.122  1.00 40.43           O  
ANISOU 1548  O   HOH A1342     3251   6438   5672    192   1765    -40       O  
HETATM 1549  O   HOH A1343      14.382 -10.861   6.112  1.00 41.11           O  
ANISOU 1549  O   HOH A1343     5802   4713   5105  -1439   1339   -608       O  
HETATM 1550  O   HOH A1344      -0.263  16.178  36.365  1.00 48.17           O  
ANISOU 1550  O   HOH A1344     6183   5777   6344    842    573   1995       O  
HETATM 1551  O   HOH A1345      24.974 -10.257   9.088  1.00 48.08           O  
ANISOU 1551  O   HOH A1345     3350   7210   7710  -1212   1905   -908       O  
HETATM 1552  O   HOH A1346      22.924  27.781  14.020  1.00 45.94           O  
ANISOU 1552  O   HOH A1346     4838   5472   7145     76    502    661       O  
HETATM 1553  O   HOH A1347      19.389   0.843  16.656  1.00 48.43           O  
ANISOU 1553  O   HOH A1347     6772   4679   6952    535   1576   1492       O  
HETATM 1554  O   HOH A1348      -4.033  -2.128   8.786  1.00 46.99           O  
ANISOU 1554  O   HOH A1348     4120   6786   6948    939   1852  -1404       O  
HETATM 1555  O   HOH A1349      16.053 -11.883   4.833  1.00 48.50           O  
ANISOU 1555  O   HOH A1349     7684   4289   6456   -436    706    697       O  
HETATM 1556  O   HOH A1350      24.711 -11.581  10.942  1.00 43.65           O  
ANISOU 1556  O   HOH A1350     7591   4751   4244   -491    361    834       O  
HETATM 1557  O   HOH A1351      -3.023  11.943  21.905  1.00 57.73           O  
ANISOU 1557  O   HOH A1351     7020   8518   6398  -1168   -370    197       O  
HETATM 1558  O   HOH A1352      10.593  28.826  15.161  1.00 49.35           O  
ANISOU 1558  O   HOH A1352     7275   5296   6179   -416   1879   -126       O  
HETATM 1559  O   HOH A1353      13.134  -9.857   7.748  1.00 45.32           O  
ANISOU 1559  O   HOH A1353     4715   5619   6887    864    -38  -1127       O  
HETATM 1560  O   HOH A1354      20.159  16.424  37.318  1.00 45.28           O  
ANISOU 1560  O   HOH A1354     4356   7825   5023   -763  -1349   -518       O  
HETATM 1561  O   HOH A1355      23.024 -16.039   1.684  1.00 45.03           O  
ANISOU 1561  O   HOH A1355     4327   5734   7048   -232  -1560    137       O  
HETATM 1562  O   HOH A1356      17.974  15.002  37.299  1.00 42.88           O  
ANISOU 1562  O   HOH A1356     4930   6804   4560   1123    595    922       O  
HETATM 1563  O   HOH A1357      15.445  15.796  37.055  1.00 47.15           O  
ANISOU 1563  O   HOH A1357     5568   7199   5149   -634  -1133    649       O  
HETATM 1564  O   HOH A1358      18.719  18.610  38.276  1.00 39.75           O  
ANISOU 1564  O   HOH A1358     4945   5533   4627   -966   -184   -388       O  
HETATM 1565  O   HOH A1359      18.310  -9.835  10.927  1.00 41.73           O  
ANISOU 1565  O   HOH A1359     6758   4368   4729   -272   -516   1518       O  
HETATM 1566  O   HOH A1360       3.309  14.282  38.426  1.00 44.85           O  
ANISOU 1566  O   HOH A1360     5676   6241   5123   -220   1023   1080       O  
HETATM 1567  O   HOH A1361       2.816  12.059  37.932  1.00 55.50           O  
ANISOU 1567  O   HOH A1361     7056   7940   6093   1162   1437  -1993       O  
HETATM 1568  O   HOH A1362       0.514  10.380  34.980  1.00 49.52           O  
ANISOU 1568  O   HOH A1362     6473   6567   5776    741    697   -199       O  
HETATM 1569  O   HOH A1363      -4.409   3.437  13.568  1.00 54.60           O  
ANISOU 1569  O   HOH A1363     5536   8177   7034  -3296   -333    939       O  
HETATM 1570  O   HOH A1364       1.365   3.487  29.707  1.00 49.89           O  
ANISOU 1570  O   HOH A1364     6603   6413   5939    -27    781   1263       O  
HETATM 1571  O   HOH A1365       0.483  24.964  30.077  1.00 40.90           O  
ANISOU 1571  O   HOH A1365     3276   6516   5748    -71    961   -627       O  
HETATM 1572  O   HOH A1366       5.789  28.689  21.165  1.00 58.42           O  
ANISOU 1572  O   HOH A1366     8011   6434   7753   -684   -996   1106       O  
HETATM 1573  O   HOH A1367       8.802  26.698  14.172  1.00 44.58           O  
ANISOU 1573  O   HOH A1367     5249   6614   5077    496    -17   1577       O  
HETATM 1574  O   HOH A1368      28.724  -1.326  21.595  1.00 60.18           O  
ANISOU 1574  O   HOH A1368     6796   8712   7358    590  -1194   -417       O  
HETATM 1575  O   HOH A1369      29.053  14.778  29.570  1.00 44.96           O  
ANISOU 1575  O   HOH A1369     3998   7680   5404    577    331    -17       O  
HETATM 1576  O   HOH A1370      12.253  18.646  -2.519  1.00 34.27           O  
ANISOU 1576  O   HOH A1370     3763   6294   2964  -2073    575    599       O  
HETATM 1577  O   HOH A1371      33.371   1.678   7.700  1.00 41.49           O  
ANISOU 1577  O   HOH A1371     1738   7616   6412    114   -856   -754       O  
HETATM 1578  O   HOH A1372       4.293   5.884  28.378  1.00 40.53           O  
ANISOU 1578  O   HOH A1372     5349   5544   4505   -636   1967     13       O  
HETATM 1579  O   HOH A1373       0.000  17.424  33.744  0.50 51.54           O  
ANISOU 1579  O   HOH A1373     6837   5429   7318      0   -425      0       O  
HETATM 1580  O   HOH A1374      24.197   6.168  28.863  1.00 46.74           O  
ANISOU 1580  O   HOH A1374     5472   6571   5716   -644   -204   1377       O  
HETATM 1581  O   HOH A1375      26.821  19.490  24.439  1.00 49.12           O  
ANISOU 1581  O   HOH A1375     6158   6958   5546  -1798  -1446   1541       O  
HETATM 1582  O   HOH A1376      13.433  26.643  17.921  1.00 48.43           O  
ANISOU 1582  O   HOH A1376     5892   6740   5770   -736    465   -276       O  
HETATM 1583  O   HOH A1377      16.532  -5.022  13.482  1.00 93.25           O  
ANISOU 1583  O   HOH A1377    11836  11352  12243    -54    265    142       O  
HETATM 1584  O   HOH A1378       0.820  13.436  35.422  1.00 51.77           O  
ANISOU 1584  O   HOH A1378     6995   8654   4023   -759   2301  -2325       O  
HETATM 1585  O   HOH A1379      25.444   1.755  26.734  1.00 67.32           O  
ANISOU 1585  O   HOH A1379     8676   8287   8614   -939    375   1049       O  
HETATM 1586  O   HOH A1380       5.572  13.103  38.717  1.00 52.77           O  
ANISOU 1586  O   HOH A1380     6394   7713   5945    450   -803     43       O  
HETATM 1587  O   HOH A1381      19.163  21.609  33.167  1.00 45.13           O  
ANISOU 1587  O   HOH A1381     5281   5551   6315    366   -126  -1084       O  
HETATM 1588  O   HOH A1382      -5.901   7.739  28.167  1.00 42.83           O  
ANISOU 1588  O   HOH A1382     4638   7372   4262   -656   1412   -608       O  
HETATM 1589  O   HOH A1383      21.078   0.292  25.203  1.00 60.86           O  
ANISOU 1589  O   HOH A1383     9820   8281   5023   -220   1296  -2275       O  
HETATM 1590  O   HOH A1384      21.107  21.659  40.044  1.00 44.59           O  
ANISOU 1590  O   HOH A1384     4887   6244   5813  -1202  -1467    -20       O  
HETATM 1591  O   HOH A1385      19.500  21.922  24.408  1.00 54.57           O  
ANISOU 1591  O   HOH A1385     6327   5899   8507   1323   -302   -493       O  
HETATM 1592  O   HOH A1386      27.350   7.577  25.785  1.00 48.09           O  
ANISOU 1592  O   HOH A1386     5655   6237   6380   1746    287    656       O  
HETATM 1593  O   HOH A1387       5.046  11.458  -0.271  1.00 66.43           O  
ANISOU 1593  O   HOH A1387     7835   8766   8640   -544   -478   -859       O  
HETATM 1594  O   HOH A1388      34.658   9.818  11.645  1.00 67.16           O  
ANISOU 1594  O   HOH A1388     9143   7710   8665   1168   1146   -388       O  
HETATM 1595  O   HOH A1389       9.583  29.754  17.605  1.00 42.38           O  
ANISOU 1595  O   HOH A1389     4232   4778   7092   -207   2092   -649       O  
HETATM 1596  O   HOH A1390       7.343  -6.675   5.722  1.00 51.43           O  
ANISOU 1596  O   HOH A1390     6223   6499   6819   -375    410   -643       O  
HETATM 1597  O   HOH A1391       2.483   8.085   7.111  1.00 49.81           O  
ANISOU 1597  O   HOH A1391     5544   6460   6923    684    921    408       O  
HETATM 1598  O   HOH A1392      19.481  29.447  14.838  1.00 64.19           O  
ANISOU 1598  O   HOH A1392     8798   7095   8496     43   -487   2265       O  
HETATM 1599  O   HOH A1393       9.155  -0.112  24.281  1.00 44.53           O  
ANISOU 1599  O   HOH A1393     6057   5152   5712    593   -568    992       O  
HETATM 1600  O   HOH A1394      29.397  -9.341   0.443  1.00 49.19           O  
ANISOU 1600  O   HOH A1394     6189   7807   4693    -52   -772     87       O  
HETATM 1601  O   HOH A1395      21.884  23.994  21.923  1.00 48.92           O  
ANISOU 1601  O   HOH A1395     6399   7335   4855    627   -151     76       O  
HETATM 1602  O   HOH A1396       3.969   4.846  30.769  1.00 48.35           O  
ANISOU 1602  O   HOH A1396     6255   5263   6851  -1642    104    741       O  
HETATM 1603  O   HOH A1397      -2.905   0.125  14.438  1.00 60.22           O  
ANISOU 1603  O   HOH A1397     7382   8367   7131   -263   -741   -882       O  
HETATM 1604  O   HOH A1398      -4.178  15.587  26.756  1.00 55.51           O  
ANISOU 1604  O   HOH A1398     6154   7882   7056   -724   -658   -428       O  
HETATM 1605  O   HOH A1399      17.477   0.414  18.854  1.00 58.75           O  
ANISOU 1605  O   HOH A1399     6190   8651   7483   2152   -891     74       O  
HETATM 1606  O   HOH A1400      30.299  -3.079  19.372  1.00 75.94           O  
ANISOU 1606  O   HOH A1400     9046  10204   9603   -209   -780   -188       O  
HETATM 1607  O   HOH A1401      29.615  17.800  27.302  1.00 61.79           O  
ANISOU 1607  O   HOH A1401     7738   7418   8323   -964     34   -333       O  
HETATM 1608  O   HOH A1402       4.009   3.647  35.152  1.00 62.65           O  
ANISOU 1608  O   HOH A1402     8155   7508   8140    891   1211    662       O  
HETATM 1609  O   HOH A1403      20.883 -10.747  11.577  1.00 56.66           O  
ANISOU 1609  O   HOH A1403     6668   6485   8374   -171   -432   -571       O  
HETATM 1610  O   HOH A1404      11.520  -3.581  22.417  1.00 61.18           O  
ANISOU 1610  O   HOH A1404     7932   8245   7070   -432  -1429    304       O  
HETATM 1611  O   HOH A1405       1.083   6.125  10.115  1.00 51.70           O  
ANISOU 1611  O   HOH A1405     6341   6312   6990   1668    736    -76       O  
HETATM 1612  O   HOH A1406      17.353  -0.129  16.245  1.00 55.11           O  
ANISOU 1612  O   HOH A1406     6894   6998   7049    604   -982   -878       O  
HETATM 1613  O   HOH A1407      27.240   1.119  23.265  1.00 57.17           O  
ANISOU 1613  O   HOH A1407     7045   7103   7573    -80   -671  -1659       O  
HETATM 1614  O   HOH A1408      -3.015   6.695  15.235  1.00 77.22           O  
ANISOU 1614  O   HOH A1408     9570   9480  10290    671   -662     -3       O  
HETATM 1615  O   HOH A1409      22.591  18.583  36.720  1.00 59.19           O  
ANISOU 1615  O   HOH A1409     7253   7947   7289   1142   -153   -243       O  
HETATM 1616  O   HOH A1410      29.139   8.237  30.974  1.00 50.15           O  
ANISOU 1616  O   HOH A1410     6315   7505   5235   -886    -43   -230       O  
HETATM 1617  O   HOH A1411       0.300  26.446  26.404  1.00 48.44           O  
ANISOU 1617  O   HOH A1411     6241   6215   5950   -794    864   -458       O  
HETATM 1618  O   HOH A1412       1.271  12.727   7.301  1.00 83.97           O  
ANISOU 1618  O   HOH A1412    10635   9879  11390     54    104   -252       O  
HETATM 1619  O   HOH A1413      24.978   5.304  26.281  1.00 62.20           O  
ANISOU 1619  O   HOH A1413     6937   8007   8689     87     43    772       O  
HETATM 1620  O   HOH A1414      10.013  27.315  29.495  1.00 58.85           O  
ANISOU 1620  O   HOH A1414     7182   8019   7160  -1747     93   -555       O  
HETATM 1621  O   HOH A1415       8.023  29.682  20.543  1.00 57.08           O  
ANISOU 1621  O   HOH A1415     5715   7572   8399    -17   -218  -1421       O  
HETATM 1622  O   HOH A1416       7.833   9.145  37.343  1.00 51.51           O  
ANISOU 1622  O   HOH A1416     6420   8137   5016   -706    -38    285       O  
HETATM 1623  O   HOH A1417      -0.693   8.991  16.272  1.00 46.97           O  
ANISOU 1623  O   HOH A1417     3440   6948   7458    252    131    137       O  
HETATM 1624  O   HOH A1418       9.089  25.774   8.413  1.00 59.71           O  
ANISOU 1624  O   HOH A1418     7910   7153   7623   -136   -447    351       O  
HETATM 1625  O   HOH A1419      22.869  19.155   5.464  1.00 54.45           O  
ANISOU 1625  O   HOH A1419     6079   6779   7831  -2309   -436    917       O  
HETATM 1626  O   HOH A1420      27.521  20.568  35.149  1.00 54.52           O  
ANISOU 1626  O   HOH A1420     6237   6559   7918   1404  -1150   -886       O  
HETATM 1627  O   HOH A1421      25.367  18.818   5.360  1.00 43.22           O  
ANISOU 1627  O   HOH A1421     4859   5497   6064   -828   -287   1324       O  
HETATM 1628  O   HOH A1422      -0.474   8.285  13.737  1.00 51.47           O  
ANISOU 1628  O   HOH A1422     5920   6326   7311  -1861   -793    527       O  
HETATM 1629  O   HOH A1423      19.379  19.540   4.208  1.00 58.93           O  
ANISOU 1629  O   HOH A1423     7505   7828   7056    775   1062    705       O  
HETATM 1630  O   HOH A1424      28.187   1.969  25.170  1.00 58.78           O  
ANISOU 1630  O   HOH A1424     7433   7990   6909    621   -148    494       O  
HETATM 1631  O   HOH A1425      29.386   0.984  21.340  1.00 41.82           O  
ANISOU 1631  O   HOH A1425     4158   6685   5048   1280  -1058    337       O  
HETATM 1632  O   HOH A1426      23.111 -11.283   5.112  1.00 41.20           O  
ANISOU 1632  O   HOH A1426     5788   4598   5270    860   -577    974       O  
HETATM 1633  O   HOH A1427       6.305  27.206  28.748  1.00 35.14           O  
ANISOU 1633  O   HOH A1427     3661   4697   4995   -649    974    454       O  
HETATM 1634  O   HOH A1428       6.094  20.598   1.444  1.00 37.16           O  
ANISOU 1634  O   HOH A1428     3817   6363   3941    644   -810   -957       O  
HETATM 1635  O   HOH A1429      22.529  26.042  12.583  1.00 43.14           O  
ANISOU 1635  O   HOH A1429     6140   5360   4891   -922  -1208   1023       O  
HETATM 1636  O   HOH A1430      28.387  15.083   3.856  1.00 63.38           O  
ANISOU 1636  O   HOH A1430     8039   8222   7820    364    109   -604       O  
HETATM 1637  O   HOH A1431      25.004  -2.587  10.824  1.00 59.37           O  
ANISOU 1637  O   HOH A1431     6111   7386   9060    315   -242    198       O  
HETATM 1638  O   HOH A1432      20.279 -15.183   6.686  1.00 55.02           O  
ANISOU 1638  O   HOH A1432     7810   6158   6937   -794    952   -170       O  
HETATM 1639  O   HOH A1433       3.040  18.056   3.525  1.00 61.03           O  
ANISOU 1639  O   HOH A1433     7324   9042   6822    465  -1518    627       O  
HETATM 1640  O   HOH A1434      26.244  22.146  20.833  1.00 48.08           O  
ANISOU 1640  O   HOH A1434     6352   6693   5223  -1711    507    -20       O  
HETATM 1641  O   HOH A1435      30.296  -1.961  11.334  1.00 50.07           O  
ANISOU 1641  O   HOH A1435     5766   6007   7250   1638  -1162  -1026       O  
HETATM 1642  O   HOH A1436      30.146  10.057  20.071  1.00 48.32           O  
ANISOU 1642  O   HOH A1436     5457   6424   6477    526  -1172    -54       O  
HETATM 1643  O   HOH A1437      28.622   6.680  28.565  1.00 46.88           O  
ANISOU 1643  O   HOH A1437     5580   7045   5188   -697    913    237       O  
HETATM 1644  O   HOH A1438      29.024  -8.145  -3.428  1.00 55.24           O  
ANISOU 1644  O   HOH A1438     6538   6934   7516  -2205   -710    126       O  
HETATM 1645  O   HOH A1439      27.044  17.354  13.620  1.00 55.89           O  
ANISOU 1645  O   HOH A1439     6796   7856   6585   -656      0    485       O  
HETATM 1646  O   HOH A1440      29.954  14.989  16.518  1.00 65.60           O  
ANISOU 1646  O   HOH A1440     8658   8539   7728    207    -65    803       O  
HETATM 1647  O   HOH A1441      13.170  24.303  28.555  1.00 53.76           O  
ANISOU 1647  O   HOH A1441     7044   6625   6757    296      6  -1001       O  
HETATM 1648  O   HOH A1442      27.522  -5.222  11.198  1.00 50.44           O  
ANISOU 1648  O   HOH A1442     5895   6233   7038  -1014    882   -368       O  
HETATM 1649  O   HOH A1443      33.875  -0.753   6.683  1.00 57.64           O  
ANISOU 1649  O   HOH A1443     7289   7275   7336    907    346   -194       O  
HETATM 1650  O   HOH A1444      34.408   3.461   5.044  1.00 56.77           O  
ANISOU 1650  O   HOH A1444     6369   7983   7218   1819   -474   -197       O  
HETATM 1651  O   HOH A1445      10.605  -9.827   8.295  1.00 61.96           O  
ANISOU 1651  O   HOH A1445     7620   6994   8927    -10    812   -601       O  
HETATM 1652  O   HOH A1446      11.514   1.481  29.781  1.00 51.35           O  
ANISOU 1652  O   HOH A1446     6011   6510   6991   -584   -575    781       O  
HETATM 1653  O   HOH A1447       0.348  10.853  11.465  1.00 51.72           O  
ANISOU 1653  O   HOH A1447     5970   7713   5968  -1667   -366   -680       O  
HETATM 1654  O   HOH A1448       7.912  26.254  11.908  1.00 65.30           O  
ANISOU 1654  O   HOH A1448     8420   8011   8381   -648    408  -1136       O  
HETATM 1655  O   HOH A1449       6.819  -8.437  -0.041  1.00 67.67           O  
ANISOU 1655  O   HOH A1449     7609   9398   8705   -658   -590    904       O  
HETATM 1656  O   HOH A1450      20.777   1.770  21.409  1.00 79.31           O  
ANISOU 1656  O   HOH A1450    10499   9940   9695    445     15   -535       O  
HETATM 1657  O   HOH A1451      11.330  28.637  19.244  1.00 85.97           O  
ANISOU 1657  O   HOH A1451    10707  10381  11576   -900    120   -151       O  
HETATM 1658  O   HOH A1452      27.756   9.476  34.726  1.00 51.33           O  
ANISOU 1658  O   HOH A1452     5795   6430   7279   -640    -43    297       O  
HETATM 1659  O   HOH A1453      21.109  10.749  36.202  1.00 55.76           O  
ANISOU 1659  O   HOH A1453     7210   7900   6075   -608   -524   -869       O  
HETATM 1660  O   HOH A1454      26.863   5.178  29.906  1.00 56.54           O  
ANISOU 1660  O   HOH A1454     7153   6075   8256   -619   -480   1360       O  
HETATM 1661  O   HOH A1455       4.983  -5.033  -1.210  1.00 71.08           O  
ANISOU 1661  O   HOH A1455     9404   9150   8452   -221  -1193    838       O  
HETATM 1662  O   HOH A1456      30.748  -6.131  18.543  1.00 61.36           O  
ANISOU 1662  O   HOH A1456     8342   7329   7644   -487   -403   -204       O  
HETATM 1663  O   HOH A1457      18.184  23.733  30.354  1.00 75.75           O  
ANISOU 1663  O   HOH A1457     9937   8751  10094   -114   -507    513       O  
HETATM 1664  O   HOH A1458      30.010   0.895  17.931  1.00104.49           O  
ANISOU 1664  O   HOH A1458    13538  12991  13171    322      6    983       O  
HETATM 1665  O   HOH A1459      12.848  -6.855  11.943  1.00 60.32           O  
ANISOU 1665  O   HOH A1459     7677   8284   6959    165   1093  -1123       O  
HETATM 1666  O   HOH A1460      24.290  14.730  38.259  1.00 60.39           O  
ANISOU 1666  O   HOH A1460     7275   7249   8421    652   -610    183       O  
HETATM 1667  O   HOH A1461      28.694  -4.498   1.841  1.00 58.32           O  
ANISOU 1667  O   HOH A1461     6822   7846   7491    263  -1212  -1613       O  
HETATM 1668  O   HOH A1462      29.541  11.919   5.621  1.00 63.94           O  
ANISOU 1668  O   HOH A1462     6757   9488   8051    -70     24   -586       O  
HETATM 1669  O   HOH A1463      15.349  25.788  28.068  1.00 67.28           O  
ANISOU 1669  O   HOH A1463     8816   8234   8514    -82    414    353       O  
HETATM 1670  O   HOH A1464      24.314   4.328  19.709  1.00 61.14           O  
ANISOU 1670  O   HOH A1464     7070   7792   8367    412    740    489       O  
HETATM 1671  O   HOH A1465      21.617  -2.312  17.294  1.00 83.94           O  
ANISOU 1671  O   HOH A1465     9860  11167  10865   -329   -217    108       O  
HETATM 1672  O   HOH A1466      28.393  11.545  10.867  1.00 45.78           O  
ANISOU 1672  O   HOH A1466     3853   7055   6485    109    303   -662       O  
HETATM 1673  O   HOH A1467      16.185  -2.835  16.999  1.00 74.59           O  
ANISOU 1673  O   HOH A1467     9243   9567   9530   -705    715   -671       O  
HETATM 1674  O   HOH A1468      -2.525   6.846  12.689  1.00113.76           O  
ANISOU 1674  O   HOH A1468    14328  14364  14529     -6    -48   1316       O  
HETATM 1675  O   HOH A1469      21.634   0.477  16.718  1.00 74.99           O  
ANISOU 1675  O   HOH A1469     9656   9509   9329     76    154   -405       O  
HETATM 1676  O   HOH A1470       4.708  -4.528  12.545  1.00 62.15           O  
ANISOU 1676  O   HOH A1470     7544   7950   8119    269    441   1207       O  
HETATM 1677  O   HOH A1471      20.745  24.458  24.672  1.00 63.73           O  
ANISOU 1677  O   HOH A1471     8633   6883   8697    272   -379   -710       O  
HETATM 1678  O   HOH A1472       4.844  -2.213  21.020  1.00 75.57           O  
ANISOU 1678  O   HOH A1472     9416   9437   9862  -1133    445    406       O  
HETATM 1679  O   HOH A1473      -2.451   3.616  28.450  1.00 65.14           O  
ANISOU 1679  O   HOH A1473     8608   7659   8482   1237  -1142    500       O  
HETATM 1680  O   HOH A1474      31.675  19.029  24.964  1.00 57.70           O  
ANISOU 1680  O   HOH A1474     6420   8216   7286    340    798    856       O  
CONECT 1368 1369 1370 1371 1372                                                 
CONECT 1369 1368                                                                
CONECT 1370 1368                                                                
CONECT 1371 1368                                                                
CONECT 1372 1368                                                                
CONECT 1373 1374 1375                                                           
CONECT 1374 1373 1376                                                           
CONECT 1375 1373                                                                
CONECT 1376 1374                                                                
CONECT 1377 1378 1379                                                           
CONECT 1378 1377 1380                                                           
CONECT 1379 1377                                                                
CONECT 1380 1378                                                                
MASTER      342    0    3    8    5    0    5    6 1679    1   13   14          
END                                                                             



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