Welcome to PDBbind-CN database

Browse entries in the PDBbind-CN Database

HEADER    HYDROLASE                               11-JAN-08   2VLA              
TITLE     CRYSTAL STRUCTURE OF RESTRICTION ENDONUCLEASE BPUJI RECOGNITION DOMAIN
TITLE    2 IN COMPLEX WITH COGNATE DNA                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RESTRICTION ENDONUCLEASE R.BPUJI;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RECOGNITION DOMAIN, RESIDUES 1-285;                        
COMPND   5 SYNONYM: BPUJI;                                                      
COMPND   6 EC: 3.1.21.4;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: 5'-D(*GP*GP*TP*AP*CP*CP*CP*GP*TP*GP *GP*A)-3';             
COMPND  10 CHAIN: L;                                                            
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: 5'-D(*TP*CP*CP*AP*CP*GP*GP*GP*TP*AP *CP*C)-3';             
COMPND  14 CHAIN: M;                                                            
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS PUMILUS;                               
SOURCE   3 ORGANISM_TAXID: 1408;                                                
SOURCE   4 STRAIN: RFL1458;                                                     
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: ER2267;                                    
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PAL-BPUJI;                                
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 SYNTHETIC: YES;                                                      
SOURCE  11 MOL_ID: 3;                                                           
SOURCE  12 SYNTHETIC: YES                                                       
KEYWDS    RESTRICTION ENDONUCLEASE, HYDROLASE, ENDONUCLEASE, DNA RECOGNITION,   
KEYWDS   2 HELIX-TURN-HELIX                                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.SUKACKAITE,S.GRAZULIS,M.BOCHTLER,V.SIKSNYS                          
REVDAT   5   24-JUL-19 2VLA    1       REMARK                                   
REVDAT   4   16-JUN-09 2VLA    1       REMARK                                   
REVDAT   3   24-FEB-09 2VLA    1       VERSN                                    
REVDAT   2   13-MAY-08 2VLA    1       JRNL                                     
REVDAT   1   06-MAY-08 2VLA    0                                                
JRNL        AUTH   R.SUKACKAITE,S.GRAZULIS,M.BOCHTLER,V.SIKSNYS                 
JRNL        TITL   THE RECOGNITION DOMAIN OF THE BPUJI RESTRICTION ENDONUCLEASE 
JRNL        TITL 2 IN COMPLEX WITH COGNATE DNA AT 1.3-A RESOLUTION.             
JRNL        REF    J.MOL.BIOL.                   V. 378  1084 2008              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   18433771                                                     
JRNL        DOI    10.1016/J.JMB.2008.03.041                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 83.62                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 91374                          
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) : 0.140                           
REMARK   3   R VALUE            (WORKING SET) : 0.138                           
REMARK   3   FREE R VALUE                     : 0.166                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 10116                           
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) : 1.29                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.33                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6144                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2070                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 697                          
REMARK   3   BIN FREE R VALUE                    : 0.2420                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2289                                    
REMARK   3   NUCLEIC ACID ATOMS       : 486                                     
REMARK   3   HETEROGEN ATOMS          : 19                                      
REMARK   3   SOLVENT ATOMS            : 461                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 13.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 13.91                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.48000                                              
REMARK   3    B22 (A**2) : -1.99000                                             
REMARK   3    B33 (A**2) : -1.48000                                             
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): 0.044         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.043         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.032         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.727         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.977                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.970                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3074 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1981 ; 0.000 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4268 ; 1.099 ; 2.164       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4867 ; 0.780 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   315 ; 6.505 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   134 ;35.140 ;25.448       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   468 ;13.589 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    12 ;19.495 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   452 ; 0.073 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3141 ; 0.010 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   513 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   640 ; 0.229 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2227 ; 0.225 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1493 ; 0.201 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1406 ; 0.090 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   289 ; 0.165 ; 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):     8 ; 0.258 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    55 ; 0.245 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    31 ; 0.145 ; 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):  1503 ; 3.119 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2462 ; 3.951 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1702 ; 5.414 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1806 ; 6.777 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 2VLA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-JAN-08.                  
REMARK 100 THE DEPOSITION ID IS D_1290034983.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-NOV-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : X12                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 101561                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 55.990                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.300                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY                : 10.80                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.37                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.31000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: MLPHARE                                               
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM TARTRATE, 20% PEG3350,    
REMARK 280  PH 6.6                                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       28.14600            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       83.75650            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.14600            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       83.75650            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4650 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14890 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.6 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, L, M                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASN A   281                                                      
REMARK 465     SER A   282                                                      
REMARK 465     HIS A   283                                                      
REMARK 465     LYS A   284                                                      
REMARK 465     SER A   285                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     MET A   1    CB   CG   SD   CE                                   
REMARK 470     LYS A  41    CG   CD   CE   NZ                                   
REMARK 470     LYS A  46    CD   CE   NZ                                        
REMARK 470     ASP A  84    CB   CG   OD1  OD2                                  
REMARK 470     GLU A  85    CB   CG   CD   OE1  OE2                             
REMARK 470     LYS A 132    CD   CE   NZ                                        
REMARK 470     ARG A 235    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A 267    CE   NZ                                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NZ   LYS A   176     O    HOH A  2232              2.11            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500     DT L 103   O4' -  C1' -  N1  ANGL. DEV. =  -5.3 DEGREES          
REMARK 500     DC L 105   O4' -  C1' -  N1  ANGL. DEV. =   2.4 DEGREES          
REMARK 500     DG M 206   O4' -  C1' -  N9  ANGL. DEV. =   2.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ILE A  72      -61.77   -103.70                                   
REMARK 500    GLN A 134      104.36   -162.32                                   
REMARK 500    GLN A 134      102.27   -163.35                                   
REMARK 500    VAL A 164      -67.65   -121.84                                   
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 A2023        DISTANCE =  6.49 ANGSTROMS                       
REMARK 525    HOH A2062        DISTANCE =  6.43 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG6 A 1281                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 1282                 
DBREF  2VLA A    1   285  UNP    A3FMN7   A3FMN7_BACPU     1    285             
DBREF  2VLA L  101   112  PDB    2VLA     2VLA           101    112             
DBREF  2VLA M  201   212  PDB    2VLA     2VLA           201    212             
SEQRES   1 A  285  MET ASN TYR ASN PRO GLU GLU GLN PHE ARG CYS THR ILE          
SEQRES   2 A  285  ILE ARG GLY LYS ALA LYS ASN MET LEU ASP ASN LEU LEU          
SEQRES   3 A  285  PRO ALA TYR ALA ASN ILE ILE ASP ASP ILE CYS PRO CYS          
SEQRES   4 A  285  ASP LYS ALA SER PHE VAL LYS ASP PHE ASN ASN ARG LEU          
SEQRES   5 A  285  ILE GLU ILE LEU GLY GLU GLU THR THR LYS LYS THR LEU          
SEQRES   6 A  285  ASP ASN HIS ARG THR GLU ILE ALA GLY LYS LEU PHE GLY          
SEQRES   7 A  285  MET PHE TYR GLU ASP ASP GLU VAL ILE PHE PRO SER GLY          
SEQRES   8 A  285  ARG THR ASN LYS TYR ILE GLU ASP SER ASP GLN PRO ALA          
SEQRES   9 A  285  PHE PHE LYS ASP ILE CYS PHE LYS PHE GLN PHE PRO ASN          
SEQRES  10 A  285  GLY MET ASP LYS LEU ASP LYS VAL ILE GLU LYS VAL GLY          
SEQRES  11 A  285  ALA LYS ILE GLN ILE ARG GLN PHE PRO TYR ILE LEU GLN          
SEQRES  12 A  285  VAL LEU LEU THR ALA ASP ASN ASN ASN ILE GLN LEU SER          
SEQRES  13 A  285  LYS ASP ASP ILE ALA TYR TYR VAL LEU ASN SER LEU GLN          
SEQRES  14 A  285  VAL LEU GLN GLY LYS ILE LYS PRO ILE GLU VAL ILE GLU          
SEQRES  15 A  285  LYS ILE ILE GLU ASP ARG SER ASN ASP ILE THR LYS LYS          
SEQRES  16 A  285  VAL ARG HIS PRO GLY LYS GLU THR SER TYR SER MET GLN          
SEQRES  17 A  285  HIS ILE ARG GLU GLN LEU ASN TYR LEU GLU LEU ALA ASN          
SEQRES  18 A  285  LEU ILE ARG ILE ASP GLY ASN LEU VAL LYS LEU ASN TYR          
SEQRES  19 A  285  ARG GLU ALA GLU ASN ILE ASN TYR ILE ALA GLN PHE TRP          
SEQRES  20 A  285  GLY ASN LYS PRO GLU PHE ASN ALA TYR LYS TYR ASP PHE          
SEQRES  21 A  285  THR SER GLU ASP ASP LYS LYS SER PHE PHE LYS ASP TRP          
SEQRES  22 A  285  GLN GLN TYR TYR SER ASN VAL ASN SER HIS LYS SER              
SEQRES   1 L   12   DG  DG  DT  DA  DC  DC  DC  DG  DT  DG  DG  DA              
SEQRES   1 M   12   DT  DC  DC  DA  DC  DG  DG  DG  DT  DA  DC  DC              
HET    PG6  A1281      18                                                       
HET     NA  A1282       1                                                       
HETNAM     PG6 1-(2-METHOXY-ETHOXY)-2-{2-[2-(2-METHOXY-ETHOXY]-                 
HETNAM   2 PG6  ETHOXY}-ETHANE                                                  
HETNAM      NA SODIUM ION                                                       
FORMUL   4  PG6    C12 H26 O6                                                   
FORMUL   5   NA    NA 1+                                                        
FORMUL   6  HOH   *461(H2 O)                                                    
HELIX    1   1 MET A   21  ILE A   36  1                                  16    
HELIX    2   2 LYS A   41  LEU A   56  1                                  16    
HELIX    3   3 LYS A   62  ILE A   72  1                                  11    
HELIX    4   4 GLY A   91  ASP A   99  1                                   9    
HELIX    5   5 GLN A  102  LYS A  112  1                                  11    
HELIX    6   6 LEU A  122  ALA A  131  1                                  10    
HELIX    7   7 GLN A  137  ASN A  151  1                                  15    
HELIX    8   8 ASP A  158  VAL A  164  1                                   7    
HELIX    9   9 LEU A  168  GLN A  172  1                                   5    
HELIX   10  10 PRO A  177  ASN A  190  1                                  14    
HELIX   11  11 THR A  203  ALA A  220  1                                  18    
HELIX   12  12 ALA A  237  GLN A  245  1                                   9    
HELIX   13  13 GLU A  263  SER A  278  1                                  16    
SHEET    1  AA 3 CYS A  39  ASP A  40  0                                        
SHEET    2  AA 3 VAL A  86  PRO A  89 -1  O  ILE A  87   N  CYS A  39           
SHEET    3  AA 3 PHE A  80  ASP A  83 -1  O  TYR A  81   N  PHE A  88           
SHEET    1  AB 2 ILE A 223  ILE A 225  0                                        
SHEET    2  AB 2 VAL A 230  LEU A 232 -1  O  LYS A 231   N  ARG A 224           
LINK        NA    NA A1282                 O   GLY A 173     1555   1555  2.57  
CISPEP   1 CYS A   37    PRO A   38          0        -5.33                     
CISPEP   2 PHE A  115    PRO A  116          0        -6.05                     
SITE     1 AC1  8 GLN A 134  GLN A 172  GLY A 173  ILE A 175                    
SITE     2 AC1  8 TRP A 247  ASN A 249  LYS A 250   NA A1282                    
SITE     1 AC2  2 GLY A 173  PG6 A1281                                          
CRYST1   56.292  167.513   43.846  90.00  90.00  90.00 P 21 21 2     4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.017765  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005970  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.022807        0.00000                         
ATOM      1  N   MET A   1      17.711  41.027 -17.094  1.00 33.72           N  
ANISOU    1  N   MET A   1     3523   4500   4789    263    301    489       N  
ATOM      2  CA  MET A   1      17.797  41.673 -18.431  1.00 32.79           C  
ANISOU    2  CA  MET A   1     3268   4504   4685    102    392     16       C  
ATOM      3  C   MET A   1      16.963  40.914 -19.447  1.00 30.82           C  
ANISOU    3  C   MET A   1     2722   4177   4809   -276    555    426       C  
ATOM      4  O   MET A   1      16.795  39.699 -19.345  1.00 36.60           O  
ANISOU    4  O   MET A   1     3121   4736   6048   -205    226     87       O  
ATOM      5  N   ASN A   2      16.437  41.638 -20.424  1.00 28.48           N  
ANISOU    5  N   ASN A   2     2356   4257   4205   -489    926    323       N  
ATOM      6  CA  ASN A   2      15.675  41.038 -21.484  1.00 28.69           C  
ANISOU    6  CA  ASN A   2     2876   3852   4170   -321    823    418       C  
ATOM      7  C   ASN A   2      14.466  40.310 -20.934  1.00 23.66           C  
ANISOU    7  C   ASN A   2     1737   3586   3666   -392    965    220       C  
ATOM      8  O   ASN A   2      14.106  39.252 -21.420  1.00 26.06           O  
ANISOU    8  O   ASN A   2     1792   4066   4041   -256   1422    -67       O  
ATOM      9  CB  ASN A   2      16.547  40.069 -22.288  1.00 32.65           C  
ANISOU    9  CB  ASN A   2     3180   4449   4773   -207    813    148       C  
ATOM     10  CG  ASN A   2      17.605  40.781 -23.112  1.00 36.47           C  
ANISOU   10  CG  ASN A   2     3953   4720   5183   -275    835    351       C  
ATOM     11  OD1 ASN A   2      17.376  41.880 -23.623  1.00 39.93           O  
ANISOU   11  OD1 ASN A   2     3858   5705   5607     82   1115    577       O  
ATOM     12  ND2 ASN A   2      18.768  40.153 -23.252  1.00 45.26           N  
ANISOU   12  ND2 ASN A   2     4642   5989   6566    422    137    219       N  
ATOM     13  N   TYR A   3      13.845  40.894 -19.909  1.00 23.08           N  
ANISOU   13  N   TYR A   3     2261   3241   3266   -530    735    419       N  
ATOM     14  CA  TYR A   3      12.615  40.354 -19.351  1.00 19.46           C  
ANISOU   14  CA  TYR A   3     1537   3045   2812   -398    267    394       C  
ATOM     15  C   TYR A   3      11.557  40.263 -20.418  1.00 19.19           C  
ANISOU   15  C   TYR A   3     1395   3165   2730   -203    691    622       C  
ATOM     16  O   TYR A   3      11.219  41.260 -21.061  1.00 20.71           O  
ANISOU   16  O   TYR A   3     1695   3331   2841   -210    658    944       O  
ATOM     17  CB  TYR A   3      12.134  41.243 -18.212  1.00 16.30           C  
ANISOU   17  CB  TYR A   3      511   2929   2753   -591    500    277       C  
ATOM     18  CG  TYR A   3      10.737  40.910 -17.673  1.00 13.96           C  
ANISOU   18  CG  TYR A   3      420   2463   2421   -457    334    286       C  
ATOM     19  CD1 TYR A   3      10.382  39.616 -17.339  1.00 15.55           C  
ANISOU   19  CD1 TYR A   3      871   2821   2214   -199     97    183       C  
ATOM     20  CD2 TYR A   3       9.826  41.918 -17.431  1.00 15.26           C  
ANISOU   20  CD2 TYR A   3      969   2476   2352   -121     88     46       C  
ATOM     21  CE1 TYR A   3       9.092  39.334 -16.818  1.00 15.18           C  
ANISOU   21  CE1 TYR A   3     1157   2546   2062   -608     63    453       C  
ATOM     22  CE2 TYR A   3       8.594  41.658 -16.908  1.00 16.34           C  
ANISOU   22  CE2 TYR A   3      818   2984   2404   -193    167    109       C  
ATOM     23  CZ  TYR A   3       8.236  40.377 -16.581  1.00 13.80           C  
ANISOU   23  CZ  TYR A   3      343   2803   2094   -413    190    109       C  
ATOM     24  OH  TYR A   3       6.964  40.157 -16.061  1.00 15.14           O  
ANISOU   24  OH  TYR A   3      372   3119   2262   -128    455    353       O  
ATOM     25  N   ASN A   4      11.060  39.048 -20.638  1.00 17.81           N  
ANISOU   25  N   ASN A   4      781   3434   2550   -132    686    425       N  
ATOM     26  CA  ASN A   4       9.987  38.829 -21.570  1.00 20.94           C  
ANISOU   26  CA  ASN A   4     1939   3513   2502   -139    540    506       C  
ATOM     27  C   ASN A   4       8.931  37.993 -20.928  1.00 19.29           C  
ANISOU   27  C   ASN A   4     1517   3193   2619    -38    684    412       C  
ATOM     28  O   ASN A   4       9.057  36.772 -20.856  1.00 20.54           O  
ANISOU   28  O   ASN A   4     1509   3491   2803     89    836    245       O  
ATOM     29  CB  ASN A   4      10.496  38.135 -22.831  1.00 21.36           C  
ANISOU   29  CB  ASN A   4     1526   4159   2430   -385    888    277       C  
ATOM     30  CG  ASN A   4       9.408  37.929 -23.853  1.00 28.53           C  
ANISOU   30  CG  ASN A   4     3250   4906   2683   -105    379    117       C  
ATOM     31  OD1 ASN A   4       8.289  38.442 -23.704  1.00 30.27           O  
ANISOU   31  OD1 ASN A   4     2879   5204   3417   -531   1309    462       O  
ATOM     32  ND2 ASN A   4       9.719  37.183 -24.905  1.00 37.06           N  
ANISOU   32  ND2 ASN A   4     4087   6558   3435   -254    899   -214       N  
ATOM     33  N   PRO A   5       7.866  38.638 -20.454  1.00 16.72           N  
ANISOU   33  N   PRO A   5     1116   3112   2123     -4    357    255       N  
ATOM     34  CA  PRO A   5       6.773  37.915 -19.792  1.00 15.98           C  
ANISOU   34  CA  PRO A   5      801   2852   2416   -391    411    271       C  
ATOM     35  C   PRO A   5       5.963  37.058 -20.741  1.00 16.80           C  
ANISOU   35  C   PRO A   5     1457   2909   2015   -266    424    280       C  
ATOM     36  O   PRO A   5       5.126  36.302 -20.304  1.00 19.11           O  
ANISOU   36  O   PRO A   5     1362   3105   2793   -592    678    341       O  
ATOM     37  CB  PRO A   5       5.923  39.039 -19.200  1.00 17.29           C  
ANISOU   37  CB  PRO A   5     1305   2861   2402   -310    -28     28       C  
ATOM     38  CG  PRO A   5       6.184  40.204 -20.066  1.00 18.88           C  
ANISOU   38  CG  PRO A   5     1547   3154   2471    123    441    106       C  
ATOM     39  CD  PRO A   5       7.639  40.090 -20.459  1.00 18.64           C  
ANISOU   39  CD  PRO A   5     1589   3147   2343   -393    298    277       C  
ATOM     40  N   GLU A   6       6.203  37.176 -22.040  1.00 19.94           N  
ANISOU   40  N   GLU A   6     2341   2865   2371   -586    231     93       N  
ATOM     41  CA  GLU A   6       5.460  36.374 -23.000  1.00 20.51           C  
ANISOU   41  CA  GLU A   6     2209   3227   2355   -328    245     -1       C  
ATOM     42  C   GLU A   6       5.679  34.880 -22.763  1.00 18.60           C  
ANISOU   42  C   GLU A   6     2093   3056   1916   -491     43     -7       C  
ATOM     43  O   GLU A   6       4.833  34.086 -23.082  1.00 20.88           O  
ANISOU   43  O   GLU A   6     1846   3672   2415   -941   -474    169       O  
ATOM     44  CB  GLU A   6       5.811  36.764 -24.448  1.00 24.41           C  
ANISOU   44  CB  GLU A   6     3068   3571   2636   -356    -18   -150       C  
ATOM     45  CG  GLU A   6       4.962  37.926 -24.971  1.00 30.83           C  
ANISOU   45  CG  GLU A   6     3868   4024   3821   -351    -92    267       C  
ATOM     46  CD  GLU A   6       5.231  38.283 -26.438  1.00 37.24           C  
ANISOU   46  CD  GLU A   6     4849   4655   4643    -24    199    180       C  
ATOM     47  OE1 GLU A   6       5.800  37.447 -27.179  1.00 45.89           O  
ANISOU   47  OE1 GLU A   6     6330   6215   4889    124    819     77       O  
ATOM     48  OE2 GLU A   6       4.844  39.399 -26.849  1.00 43.94           O  
ANISOU   48  OE2 GLU A   6     5460   5413   5822     52    -86    761       O  
ATOM     49  N   GLU A   7       6.834  34.506 -22.212  1.00 17.48           N  
ANISOU   49  N   GLU A   7     1475   3102   2062   -642     87     43       N  
ATOM     50  CA  GLU A   7       7.071  33.116 -21.789  1.00 15.50           C  
ANISOU   50  CA  GLU A   7      847   3190   1850   -333   -157   -154       C  
ATOM     51  C   GLU A   7       6.273  32.817 -20.513  1.00 13.55           C  
ANISOU   51  C   GLU A   7      726   2872   1550   -186   -166   -290       C  
ATOM     52  O   GLU A   7       6.574  33.318 -19.448  1.00 14.61           O  
ANISOU   52  O   GLU A   7      411   3387   1752   -215     52   -111       O  
ATOM     53  CB  GLU A   7       8.558  32.868 -21.553  1.00 16.56           C  
ANISOU   53  CB  GLU A   7      723   3562   2006   -379   -113    292       C  
ATOM     54  CG  GLU A   7       9.409  32.996 -22.796  1.00 23.47           C  
ANISOU   54  CG  GLU A   7     2280   4050   2584   -217    336     79       C  
ATOM     55  CD  GLU A   7      10.912  32.818 -22.520  1.00 23.88           C  
ANISOU   55  CD  GLU A   7     1706   4659   2706   -224   1310    264       C  
ATOM     56  OE1 GLU A   7      11.295  32.518 -21.367  1.00 30.56           O  
ANISOU   56  OE1 GLU A   7     3424   4516   3670    155      6   -196       O  
ATOM     57  OE2 GLU A   7      11.712  32.968 -23.474  1.00 40.94           O  
ANISOU   57  OE2 GLU A   7     3773   6775   5006    339   1003    277       O  
ATOM     58  N   GLN A   8       5.231  32.036 -20.659  1.00 12.95           N  
ANISOU   58  N   GLN A   8      651   2863   1403   -356   -182   -138       N  
ATOM     59  CA  GLN A   8       4.311  31.798 -19.568  1.00 12.87           C  
ANISOU   59  CA  GLN A   8      906   2577   1407    -79    269   -165       C  
ATOM     60  C   GLN A   8       4.401  30.356 -19.106  1.00 13.97           C  
ANISOU   60  C   GLN A   8     1189   2567   1549      8      5   -200       C  
ATOM     61  O   GLN A   8       4.715  29.467 -19.887  1.00 14.63           O  
ANISOU   61  O   GLN A   8      881   2930   1745    -24    269   -195       O  
ATOM     62  CB  GLN A   8       2.866  32.114 -20.025  1.00 14.30           C  
ANISOU   62  CB  GLN A   8     1021   2668   1744   -437    -59   -264       C  
ATOM     63  CG  GLN A   8       2.587  33.595 -20.256  1.00 13.61           C  
ANISOU   63  CG  GLN A   8      424   3098   1649   -177    212      0       C  
ATOM     64  CD  GLN A   8       2.309  34.349 -18.951  1.00 12.97           C  
ANISOU   64  CD  GLN A   8      950   2349   1626    -52    167     80       C  
ATOM     65  OE1 GLN A   8       1.317  34.096 -18.284  1.00 13.65           O  
ANISOU   65  OE1 GLN A   8      825   2845   1515   -229    178    -19       O  
ATOM     66  NE2 GLN A   8       3.203  35.283 -18.591  1.00 13.50           N  
ANISOU   66  NE2 GLN A   8     1041   2404   1681   -176    218    205       N  
ATOM     67  N   PHE A   9       4.106  30.122 -17.826  1.00 11.44           N  
ANISOU   67  N   PHE A   9      318   2447   1583     23    147   -105       N  
ATOM     68  CA  PHE A   9       4.247  28.791 -17.250  1.00 11.90           C  
ANISOU   68  CA  PHE A   9      297   2567   1657     14    243   -314       C  
ATOM     69  C   PHE A   9       3.320  28.628 -16.073  1.00 11.13           C  
ANISOU   69  C   PHE A   9      267   2334   1625    -13    141   -135       C  
ATOM     70  O   PHE A   9       3.443  29.336 -15.086  1.00 12.48           O  
ANISOU   70  O   PHE A   9      257   2805   1680    -53     66   -227       O  
ATOM     71  CB  PHE A   9       5.716  28.558 -16.817  1.00 12.84           C  
ANISOU   71  CB  PHE A   9      363   2510   2006   -123    432   -162       C  
ATOM     72  CG  PHE A   9       5.982  27.169 -16.250  1.00 15.88           C  
ANISOU   72  CG  PHE A   9      961   2867   2203    212    262   -152       C  
ATOM     73  CD1 PHE A   9       5.761  26.901 -14.916  1.00 18.12           C  
ANISOU   73  CD1 PHE A   9     1538   2756   2587    522    759    212       C  
ATOM     74  CD2 PHE A   9       6.450  26.154 -17.059  1.00 17.59           C  
ANISOU   74  CD2 PHE A   9     1539   2659   2483   -465    463     62       C  
ATOM     75  CE1 PHE A   9       5.992  25.640 -14.397  1.00 19.85           C  
ANISOU   75  CE1 PHE A   9     1159   3199   3183    369    790    249       C  
ATOM     76  CE2 PHE A   9       6.692  24.898 -16.549  1.00 18.21           C  
ANISOU   76  CE2 PHE A   9     1561   2864   2491    280     87   -235       C  
ATOM     77  CZ  PHE A   9       6.453  24.639 -15.216  1.00 18.32           C  
ANISOU   77  CZ  PHE A   9     1453   2782   2726    412    281    416       C  
ATOM     78  N   ARG A  10       2.355  27.717 -16.204  1.00 12.05           N  
ANISOU   78  N   ARG A  10      669   2468   1441     12     34   -125       N  
ATOM     79  CA  ARG A  10       1.410  27.448 -15.131  1.00 10.56           C  
ANISOU   79  CA  ARG A  10      445   2302   1265    124   -120    -12       C  
ATOM     80  C   ARG A  10       2.099  26.684 -14.018  1.00 11.03           C  
ANISOU   80  C   ARG A  10      338   2438   1414    115    196   -213       C  
ATOM     81  O   ARG A  10       2.637  25.590 -14.237  1.00 12.60           O  
ANISOU   81  O   ARG A  10      635   2401   1750    167    -36   -238       O  
ATOM     82  CB  ARG A  10       0.210  26.665 -15.676  1.00 12.01           C  
ANISOU   82  CB  ARG A  10      728   2484   1351    153    104    -38       C  
ATOM     83  CG  ARG A  10      -0.862  26.376 -14.631  1.00 11.59           C  
ANISOU   83  CG  ARG A  10      396   2534   1472    232   -251    -44       C  
ATOM     84  CD  ARG A  10      -2.095  25.769 -15.232  1.00 11.97           C  
ANISOU   84  CD  ARG A  10      437   2520   1589    281   -285      2       C  
ATOM     85  NE  ARG A  10      -3.156  25.634 -14.248  1.00 11.05           N  
ANISOU   85  NE  ARG A  10      338   2234   1625    214     83     35       N  
ATOM     86  CZ  ARG A  10      -3.428  24.537 -13.544  1.00 11.93           C  
ANISOU   86  CZ  ARG A  10      728   2015   1787    -48   -189     76       C  
ATOM     87  NH1 ARG A  10      -2.716  23.446 -13.683  1.00 11.16           N  
ANISOU   87  NH1 ARG A  10      348   2214   1678   -100     74    168       N  
ATOM     88  NH2 ARG A  10      -4.460  24.526 -12.699  1.00 11.53           N  
ANISOU   88  NH2 ARG A  10      412   2333   1636   -118   -187     90       N  
ATOM     89  N   CYS A  11       2.090  27.269 -12.830  1.00 11.04           N  
ANISOU   89  N   CYS A  11      278   2355   1561    103    161      2       N  
ATOM     90  CA  CYS A  11       2.830  26.755 -11.706  1.00 10.70           C  
ANISOU   90  CA  CYS A  11      258   2259   1548     80     47    -32       C  
ATOM     91  C   CYS A  11       1.925  26.764 -10.468  1.00 11.15           C  
ANISOU   91  C   CYS A  11      432   2224   1577     53   -175     15       C  
ATOM     92  O   CYS A  11       1.766  27.778  -9.812  1.00 10.98           O  
ANISOU   92  O   CYS A  11      289   2249   1633    130    189    -73       O  
ATOM     93  CB  CYS A  11       4.128  27.599 -11.477  1.00 11.09           C  
ANISOU   93  CB  CYS A  11      294   2641   1275    -60    203   -109       C  
ATOM     94  SG  CYS A  11       5.247  26.968 -10.277  1.00 16.03           S  
ANISOU   94  SG  CYS A  11      300   3767   2023     95   -205   -172       S  
ATOM     95  N   THR A  12       1.296  25.633 -10.209  1.00 10.64           N  
ANISOU   95  N   THR A  12      274   2163   1606    191     37   -123       N  
ATOM     96  CA  THR A  12       0.204  25.618  -9.254  1.00 10.54           C  
ANISOU   96  CA  THR A  12      357   2162   1484    179    328     12       C  
ATOM     97  C   THR A  12       0.668  25.465  -7.824  1.00 10.35           C  
ANISOU   97  C   THR A  12      259   2191   1481     51    -79     24       C  
ATOM     98  O   THR A  12       1.863  25.073  -7.548  1.00 10.73           O  
ANISOU   98  O   THR A  12      259   2276   1540     82    -63     51       O  
ATOM     99  CB  THR A  12      -0.813  24.487  -9.535  1.00 14.46           C  
ANISOU   99  CB  THR A  12     1165   2367   1963   -174   -354   -125       C  
ATOM    100  OG1 THR A  12      -0.169  23.228  -9.445  1.00 15.50           O  
ANISOU  100  OG1 THR A  12      952   2601   2336   -219   -175    -88       O  
ATOM    101  CG2 THR A  12      -1.433  24.636 -10.896  1.00 15.24           C  
ANISOU  101  CG2 THR A  12      840   3082   1867   -295   -425     14       C  
ATOM    102  N   ILE A  13      -0.263  25.789  -6.905  1.00 10.46           N  
ANISOU  102  N   ILE A  13      272   2334   1365    110    126     76       N  
ATOM    103  CA  ILE A  13      -0.238  25.287  -5.559  1.00 10.01           C  
ANISOU  103  CA  ILE A  13      272   2013   1519     16    154    145       C  
ATOM    104  C   ILE A  13      -1.520  24.489  -5.356  1.00  9.64           C  
ANISOU  104  C   ILE A  13      261   2150   1249    -70     69    138       C  
ATOM    105  O   ILE A  13      -2.450  24.577  -6.163  1.00 11.22           O  
ANISOU  105  O   ILE A  13      367   2268   1626    235   -331    115       O  
ATOM    106  CB  ILE A  13      -0.111  26.409  -4.502  1.00 10.36           C  
ANISOU  106  CB  ILE A  13      290   2116   1526    264     35    256       C  
ATOM    107  CG1 ILE A  13      -1.346  27.336  -4.514  1.00 10.20           C  
ANISOU  107  CG1 ILE A  13      376   2027   1471   -228     -6    -28       C  
ATOM    108  CG2 ILE A  13       1.194  27.237  -4.735  1.00 11.35           C  
ANISOU  108  CG2 ILE A  13      430   1982   1899   -179     71     83       C  
ATOM    109  CD1 ILE A  13      -1.572  28.051  -3.208  1.00 12.00           C  
ANISOU  109  CD1 ILE A  13      346   2372   1842   -106    364    159       C  
ATOM    110  N   ILE A  14      -1.542  23.703  -4.302  1.00  9.62           N  
ANISOU  110  N   ILE A  14      254   2056   1343     23    -33    152       N  
ATOM    111  CA  ILE A  14      -2.674  22.871  -3.938  1.00 10.03           C  
ANISOU  111  CA  ILE A  14      549   1690   1572     47    369    109       C  
ATOM    112  C   ILE A  14      -3.919  23.728  -3.822  1.00  9.70           C  
ANISOU  112  C   ILE A  14      437   1821   1425   -370   -134    -12       C  
ATOM    113  O   ILE A  14      -3.874  24.872  -3.370  1.00 10.29           O  
ANISOU  113  O   ILE A  14      258   2072   1578    -40    -72   -141       O  
ATOM    114  CB  ILE A  14      -2.377  22.112  -2.628  1.00 10.59           C  
ANISOU  114  CB  ILE A  14      296   1949   1776   -101    232     72       C  
ATOM    115  CG1 ILE A  14      -1.423  20.927  -2.932  1.00 13.39           C  
ANISOU  115  CG1 ILE A  14      287   2857   1941    299     27    190       C  
ATOM    116  CG2 ILE A  14      -3.676  21.616  -1.937  1.00 10.53           C  
ANISOU  116  CG2 ILE A  14      273   2081   1645    -90    139    179       C  
ATOM    117  CD1 ILE A  14      -0.834  20.296  -1.727  1.00 14.48           C  
ANISOU  117  CD1 ILE A  14      803   2684   2012    172    191    363       C  
ATOM    118  N   ARG A  15      -5.029  23.192  -4.332  1.00  8.83           N  
ANISOU  118  N   ARG A  15      256   1636   1462     65     -3    -94       N  
ATOM    119  CA  ARG A  15      -6.299  23.910  -4.330  1.00  8.31           C  
ANISOU  119  CA  ARG A  15      304   1494   1357    143    205     98       C  
ATOM    120  C   ARG A  15      -6.937  23.901  -2.937  1.00  9.49           C  
ANISOU  120  C   ARG A  15      269   1720   1617      0   -147     87       C  
ATOM    121  O   ARG A  15      -6.963  22.886  -2.274  1.00 10.70           O  
ANISOU  121  O   ARG A  15      296   2188   1582    150    212    126       O  
ATOM    122  CB  ARG A  15      -7.218  23.287  -5.374  1.00  9.18           C  
ANISOU  122  CB  ARG A  15      305   1792   1390    207    -16    -83       C  
ATOM    123  CG  ARG A  15      -8.520  24.073  -5.605  1.00  9.43           C  
ANISOU  123  CG  ARG A  15      278   2010   1295    186     87    129       C  
ATOM    124  CD  ARG A  15      -9.247  23.642  -6.883  1.00  9.81           C  
ANISOU  124  CD  ARG A  15      366   2105   1257    458     -9     -8       C  
ATOM    125  NE  ARG A  15      -8.514  24.082  -8.062  1.00 10.07           N  
ANISOU  125  NE  ARG A  15      348   2178   1299    157    286    -81       N  
ATOM    126  CZ  ARG A  15      -8.947  23.957  -9.295  1.00  8.94           C  
ANISOU  126  CZ  ARG A  15      255   2090   1052     44    -32    -41       C  
ATOM    127  NH1 ARG A  15     -10.139  23.407  -9.539  1.00 11.00           N  
ANISOU  127  NH1 ARG A  15      295   2237   1645    -67   -232    -83       N  
ATOM    128  NH2 ARG A  15      -8.222  24.389 -10.302  1.00 11.21           N  
ANISOU  128  NH2 ARG A  15      312   2482   1462    -90   -264    150       N  
ATOM    129  N   GLY A  16      -7.388  25.070  -2.500  1.00  9.91           N  
ANISOU  129  N   GLY A  16      256   1905   1604    -65     25     37       N  
ATOM    130  CA  GLY A  16      -7.839  25.237  -1.120  1.00 10.37           C  
ANISOU  130  CA  GLY A  16      334   1959   1647   -194    286     -6       C  
ATOM    131  C   GLY A  16      -9.118  24.512  -0.735  1.00  9.94           C  
ANISOU  131  C   GLY A  16      260   1863   1653     15     94   -140       C  
ATOM    132  O   GLY A  16      -9.940  24.161  -1.609  1.00 10.69           O  
ANISOU  132  O   GLY A  16      291   2271   1497     90    197   -149       O  
ATOM    133  N   LYS A  17      -9.241  24.248   0.555  1.00  9.67           N  
ANISOU  133  N   LYS A  17      267   2090   1316     91    102     29       N  
ATOM    134  CA  LYS A  17     -10.465  23.701   1.121  1.00 11.25           C  
ANISOU  134  CA  LYS A  17      407   2319   1545   -231    421   -133       C  
ATOM    135  C   LYS A  17     -10.913  24.385   2.405  1.00 11.42           C  
ANISOU  135  C   LYS A  17      880   1844   1616    155    243    -24       C  
ATOM    136  O   LYS A  17     -11.998  24.095   2.900  1.00 12.18           O  
ANISOU  136  O   LYS A  17      414   2456   1756   -155    425   -164       O  
ATOM    137  CB  LYS A  17     -10.323  22.202   1.401  1.00 11.21           C  
ANISOU  137  CB  LYS A  17      369   2207   1683    -84    402    -52       C  
ATOM    138  CG  LYS A  17      -9.838  21.375   0.229  1.00 12.48           C  
ANISOU  138  CG  LYS A  17      551   2370   1820    150    311    -79       C  
ATOM    139  CD  LYS A  17      -9.599  19.943   0.654  1.00 11.29           C  
ANISOU  139  CD  LYS A  17      330   2396   1561   -170    263   -121       C  
ATOM    140  CE  LYS A  17      -8.692  19.227  -0.300  1.00 11.34           C  
ANISOU  140  CE  LYS A  17      320   2076   1912     88    -78    212       C  
ATOM    141  NZ  LYS A  17      -9.342  18.911  -1.617  1.00 12.26           N  
ANISOU  141  NZ  LYS A  17      333   2343   1979     54   -114   -246       N  
ATOM    142  N   ALA A  18     -10.102  25.285   2.954  1.00 10.33           N  
ANISOU  142  N   ALA A  18      348   2065   1510    101    322   -195       N  
ATOM    143  CA  ALA A  18     -10.316  25.761   4.321  1.00 11.94           C  
ANISOU  143  CA  ALA A  18      632   2176   1729    105    -29    -72       C  
ATOM    144  C   ALA A  18     -10.570  27.271   4.450  1.00 10.94           C  
ANISOU  144  C   ALA A  18      275   2217   1662     91   -166   -199       C  
ATOM    145  O   ALA A  18     -10.737  27.764   5.546  1.00 14.40           O  
ANISOU  145  O   ALA A  18      836   2718   1914    342    -49   -493       O  
ATOM    146  CB  ALA A  18      -9.133  25.357   5.214  1.00 14.56           C  
ANISOU  146  CB  ALA A  18      922   2825   1784    498   -378   -151       C  
ATOM    147  N   LYS A  19     -10.609  27.986   3.343  1.00 11.35           N  
ANISOU  147  N   LYS A  19      292   2306   1711    -19     82   -171       N  
ATOM    148  CA  LYS A  19     -10.757  29.457   3.397  1.00 11.73           C  
ANISOU  148  CA  LYS A  19      297   2151   2006    -11    276   -188       C  
ATOM    149  C   LYS A  19     -12.114  29.895   3.977  1.00 12.23           C  
ANISOU  149  C   LYS A  19      255   2496   1892    -36    -53   -223       C  
ATOM    150  O   LYS A  19     -12.157  30.702   4.904  1.00 12.97           O  
ANISOU  150  O   LYS A  19      281   2474   2171    204    107   -264       O  
ATOM    151  CB  LYS A  19     -10.559  30.072   2.006  1.00 13.12           C  
ANISOU  151  CB  LYS A  19      553   2290   2141    -97    213   -158       C  
ATOM    152  CG  LYS A  19     -10.465  31.589   1.998  1.00 14.59           C  
ANISOU  152  CG  LYS A  19      463   2665   2413    112   -367    -90       C  
ATOM    153  CD  LYS A  19      -9.131  32.024   2.601  1.00 16.82           C  
ANISOU  153  CD  LYS A  19     1310   2367   2712     41   -119   -119       C  
ATOM    154  CE  LYS A  19      -8.826  33.513   2.417  1.00 17.40           C  
ANISOU  154  CE  LYS A  19     1092   3206   2312    273    -57    -24       C  
ATOM    155  NZ  LYS A  19      -9.781  34.358   3.173  1.00 17.09           N  
ANISOU  155  NZ  LYS A  19      935   2870   2687    226    276   -243       N  
ATOM    156  N   ASN A  20     -13.195  29.395   3.408  1.00 11.74           N  
ANISOU  156  N   ASN A  20      380   2161   1920    247    -75   -434       N  
ATOM    157  CA  ASN A  20     -14.548  29.819   3.827  1.00 13.41           C  
ANISOU  157  CA  ASN A  20      607   2346   2140    424     52   -199       C  
ATOM    158  C   ASN A  20     -14.795  29.618   5.313  1.00 13.00           C  
ANISOU  158  C   ASN A  20      283   2350   2304     15    244   -353       C  
ATOM    159  O   ASN A  20     -15.504  30.411   5.941  1.00 15.83           O  
ANISOU  159  O   ASN A  20      603   2790   2619    459    470   -344       O  
ATOM    160  CB  ASN A  20     -15.619  29.045   3.046  1.00 13.33           C  
ANISOU  160  CB  ASN A  20      308   2588   2168    280    138   -499       C  
ATOM    161  CG  ASN A  20     -15.808  29.557   1.636  1.00 15.21           C  
ANISOU  161  CG  ASN A  20      388   2617   2772    336    372   -580       C  
ATOM    162  OD1 ASN A  20     -15.345  30.643   1.289  1.00 15.56           O  
ANISOU  162  OD1 ASN A  20      336   3091   2485    397    207   -269       O  
ATOM    163  ND2 ASN A  20     -16.565  28.780   0.806  1.00 18.76           N  
ANISOU  163  ND2 ASN A  20      298   3385   3441    246   -356  -1087       N  
ATOM    164  N   MET A  21     -14.276  28.521   5.860  1.00 13.38           N  
ANISOU  164  N   MET A  21      391   2419   2274    208    154   -103       N  
ATOM    165  CA  MET A  21     -14.494  28.164   7.258  1.00 15.39           C  
ANISOU  165  CA  MET A  21      631   2800   2416     29   -128     -1       C  
ATOM    166  C   MET A  21     -13.208  28.128   8.073  1.00 12.67           C  
ANISOU  166  C   MET A  21      309   2570   1933    -61    301     42       C  
ATOM    167  O   MET A  21     -13.105  27.393   9.047  1.00 13.28           O  
ANISOU  167  O   MET A  21      287   2693   2064    -32    246    -13       O  
ATOM    168  CB  MET A  21     -15.181  26.793   7.346  1.00 15.52           C  
ANISOU  168  CB  MET A  21      275   2987   2634   -247    -25    258       C  
ATOM    169  CG  MET A  21     -16.565  26.772   6.737  1.00 22.95           C  
ANISOU  169  CG  MET A  21     1762   3274   3684   -360   -294    -30       C  
ATOM    170  SD  MET A  21     -17.551  25.441   7.377  1.00 35.04           S  
ANISOU  170  SD  MET A  21     2898   4482   5934  -1074   -156    517       S  
ATOM    171  CE  MET A  21     -17.343  25.771   9.144  1.00 32.86           C  
ANISOU  171  CE  MET A  21     2728   5460   4297   -952    958   -129       C  
ATOM    172  N   LEU A  22     -12.244  28.953   7.686  1.00 12.60           N  
ANISOU  172  N   LEU A  22      339   2408   2040     95    256    -72       N  
ATOM    173  CA  LEU A  22     -10.888  28.865   8.244  1.00 11.62           C  
ANISOU  173  CA  LEU A  22      256   2272   1886     43     60   -153       C  
ATOM    174  C   LEU A  22     -10.882  28.999   9.778  1.00 13.05           C  
ANISOU  174  C   LEU A  22      374   2408   2174   -104    435    -82       C  
ATOM    175  O   LEU A  22     -10.171  28.283  10.478  1.00 12.19           O  
ANISOU  175  O   LEU A  22      285   2557   1788    -46    218     46       O  
ATOM    176  CB  LEU A  22     -10.003  29.943   7.635  1.00 11.91           C  
ANISOU  176  CB  LEU A  22      260   2431   1831     -3   -108   -138       C  
ATOM    177  CG  LEU A  22      -8.503  29.841   7.976  1.00 13.69           C  
ANISOU  177  CG  LEU A  22      559   2868   1773   -233   -155     81       C  
ATOM    178  CD1 LEU A  22      -7.922  28.475   7.562  1.00 13.57           C  
ANISOU  178  CD1 LEU A  22      273   2558   2322    116    183    224       C  
ATOM    179  CD2 LEU A  22      -7.735  30.970   7.302  1.00 17.65           C  
ANISOU  179  CD2 LEU A  22      481   3175   3047   -652    386    400       C  
ATOM    180  N   ASP A  23     -11.709  29.876  10.309  1.00 13.69           N  
ANISOU  180  N   ASP A  23      357   2882   1962    248    334   -342       N  
ATOM    181  CA  ASP A  23     -11.632  30.164  11.706  1.00 15.89           C  
ANISOU  181  CA  ASP A  23      922   2655   2457    286    520   -289       C  
ATOM    182  C   ASP A  23     -12.170  29.003  12.560  1.00 15.03           C  
ANISOU  182  C   ASP A  23      891   2619   2198    -26    343   -252       C  
ATOM    183  O   ASP A  23     -11.844  28.904  13.739  1.00 17.28           O  
ANISOU  183  O   ASP A  23     1158   3269   2139    280    167   -168       O  
ATOM    184  CB  ASP A  23     -12.350  31.499  12.018  1.00 17.57           C  
ANISOU  184  CB  ASP A  23      672   3408   2593    482    845   -314       C  
ATOM    185  CG  ASP A  23     -11.546  32.724  11.495  1.00 24.65           C  
ANISOU  185  CG  ASP A  23     2522   3442   3401   -200   -446   -178       C  
ATOM    186  OD1 ASP A  23     -10.636  33.191  12.207  1.00 35.06           O  
ANISOU  186  OD1 ASP A  23     2568   5745   5005  -1140    182   -518       O  
ATOM    187  OD2 ASP A  23     -11.743  33.122  10.319  1.00 30.04           O  
ANISOU  187  OD2 ASP A  23     2520   4106   4784    182    909    -79       O  
ATOM    188  N   ASN A  24     -12.950  28.106  11.945  1.00 13.55           N  
ANISOU  188  N   ASN A  24      309   2826   2011    -76    313   -195       N  
ATOM    189  CA  ASN A  24     -13.292  26.823  12.567  1.00 15.01           C  
ANISOU  189  CA  ASN A  24      517   3092   2092   -325    274   -265       C  
ATOM    190  C   ASN A  24     -12.348  25.671  12.191  1.00 14.86           C  
ANISOU  190  C   ASN A  24      966   2734   1944   -140    224    143       C  
ATOM    191  O   ASN A  24     -12.002  24.838  13.030  1.00 15.89           O  
ANISOU  191  O   ASN A  24      897   3146   1995   -361    376     95       O  
ATOM    192  CB  ASN A  24     -14.730  26.426  12.200  1.00 19.57           C  
ANISOU  192  CB  ASN A  24      999   3643   2793   -537    697    -33       C  
ATOM    193  CG  ASN A  24     -15.728  27.120  13.013  1.00 28.50           C  
ANISOU  193  CG  ASN A  24     2569   4934   3326    -84    501   -259       C  
ATOM    194  OD1 ASN A  24     -15.516  27.359  14.193  1.00 35.07           O  
ANISOU  194  OD1 ASN A  24     2961   6359   4005    469    725   -717       O  
ATOM    195  ND2 ASN A  24     -16.857  27.445  12.407  1.00 31.34           N  
ANISOU  195  ND2 ASN A  24     2349   4580   4978    141    624    670       N  
ATOM    196  N   LEU A  25     -11.969  25.597  10.929  1.00 13.75           N  
ANISOU  196  N   LEU A  25      656   2723   1842   -323    131    112       N  
ATOM    197  CA  LEU A  25     -11.173  24.473  10.463  1.00 12.98           C  
ANISOU  197  CA  LEU A  25      318   2576   2036   -192    290     46       C  
ATOM    198  C   LEU A  25      -9.719  24.488  10.964  1.00 12.49           C  
ANISOU  198  C   LEU A  25      832   2182   1731   -306    104    -46       C  
ATOM    199  O   LEU A  25      -9.175  23.446  11.254  1.00 13.45           O  
ANISOU  199  O   LEU A  25      627   2660   1821   -381    122    183       O  
ATOM    200  CB  LEU A  25     -11.206  24.402   8.936  1.00 12.51           C  
ANISOU  200  CB  LEU A  25      544   2417   1792   -166     38    256       C  
ATOM    201  CG  LEU A  25     -12.417  23.757   8.317  1.00 15.06           C  
ANISOU  201  CG  LEU A  25      819   2617   2284   -314   -188    -74       C  
ATOM    202  CD1 LEU A  25     -12.411  23.988   6.836  1.00 13.59           C  
ANISOU  202  CD1 LEU A  25      552   2865   1746   -415     68   -299       C  
ATOM    203  CD2 LEU A  25     -12.452  22.254   8.656  1.00 18.46           C  
ANISOU  203  CD2 LEU A  25     1738   2626   2648   -635   -199    -44       C  
ATOM    204  N   LEU A  26      -9.108  25.653  11.053  1.00 11.66           N  
ANISOU  204  N   LEU A  26      255   2307   1866     65    -30    -21       N  
ATOM    205  CA  LEU A  26      -7.703  25.681  11.466  1.00 11.66           C  
ANISOU  205  CA  LEU A  26      425   2350   1655   -243    181    -78       C  
ATOM    206  C   LEU A  26      -7.534  25.200  12.918  1.00 13.01           C  
ANISOU  206  C   LEU A  26      811   2288   1843   -285    228    -87       C  
ATOM    207  O   LEU A  26      -6.723  24.331  13.193  1.00 12.97           O  
ANISOU  207  O   LEU A  26      933   2309   1687   -205    193     59       O  
ATOM    208  CB  LEU A  26      -7.044  27.062  11.246  1.00 11.80           C  
ANISOU  208  CB  LEU A  26      444   2497   1541    -52    -16    -60       C  
ATOM    209  CG  LEU A  26      -5.523  27.102  11.441  1.00 12.57           C  
ANISOU  209  CG  LEU A  26      301   2758   1714   -192   -226     73       C  
ATOM    210  CD1 LEU A  26      -4.858  26.148  10.462  1.00 20.10           C  
ANISOU  210  CD1 LEU A  26     1221   2661   3753   -514    252    -72       C  
ATOM    211  CD2 LEU A  26      -5.003  28.524  11.282  1.00 16.19           C  
ANISOU  211  CD2 LEU A  26     1513   2668   1971   -406    230     84       C  
ATOM    212  N   PRO A  27      -8.373  25.698  13.841  1.00 12.13           N  
ANISOU  212  N   PRO A  27      493   2573   1543    -89    145    -52       N  
ATOM    213  CA  PRO A  27      -8.318  25.104  15.171  1.00 13.87           C  
ANISOU  213  CA  PRO A  27      559   2754   1955    -59    128     10       C  
ATOM    214  C   PRO A  27      -8.649  23.617  15.187  1.00 12.76           C  
ANISOU  214  C   PRO A  27      398   2787   1661    -96     75    -42       C  
ATOM    215  O   PRO A  27      -8.075  22.874  15.972  1.00 15.27           O  
ANISOU  215  O   PRO A  27     1034   2970   1797   -275    341    221       O  
ATOM    216  CB  PRO A  27      -9.373  25.895  15.940  1.00 14.74           C  
ANISOU  216  CB  PRO A  27      923   2985   1691   -259     13   -105       C  
ATOM    217  CG  PRO A  27      -9.453  27.175  15.255  1.00 15.13           C  
ANISOU  217  CG  PRO A  27      659   3028   2061     98    255   -209       C  
ATOM    218  CD  PRO A  27      -9.244  26.878  13.811  1.00 13.32           C  
ANISOU  218  CD  PRO A  27      788   2741   1531   -237    -19   -279       C  
ATOM    219  N   ALA A  28      -9.610  23.183  14.369  1.00 14.61           N  
ANISOU  219  N   ALA A  28     1139   2627   1784   -293    128   -108       N  
ATOM    220  CA  ALA A  28      -9.939  21.777  14.321  1.00 14.10           C  
ANISOU  220  CA  ALA A  28      579   2831   1945   -232    121   -100       C  
ATOM    221  C   ALA A  28      -8.761  20.927  13.850  1.00 13.78           C  
ANISOU  221  C   ALA A  28      991   2608   1634   -274     95     20       C  
ATOM    222  O   ALA A  28      -8.398  19.945  14.510  1.00 15.14           O  
ANISOU  222  O   ALA A  28     1145   2866   1740   -437    218    145       O  
ATOM    223  CB  ALA A  28     -11.177  21.537  13.445  1.00 16.77           C  
ANISOU  223  CB  ALA A  28     1160   2864   2347   -724    -79   -170       C  
ATOM    224  N   TYR A  29      -8.141  21.308  12.734  1.00 13.03           N  
ANISOU  224  N   TYR A  29     1093   2409   1446   -261    112     20       N  
ATOM    225  CA  TYR A  29      -6.998  20.560  12.232  1.00 13.10           C  
ANISOU  225  CA  TYR A  29      925   2382   1670   -262    -57   -141       C  
ATOM    226  C   TYR A  29      -5.946  20.459  13.364  1.00 12.09           C  
ANISOU  226  C   TYR A  29      866   2111   1616   -279    206     13       C  
ATOM    227  O   TYR A  29      -5.391  19.399  13.622  1.00 13.55           O  
ANISOU  227  O   TYR A  29      947   2403   1795   -252    -31     48       O  
ATOM    228  CB  TYR A  29      -6.352  21.258  11.048  1.00 12.34           C  
ANISOU  228  CB  TYR A  29      878   2305   1504   -242     34     44       C  
ATOM    229  CG  TYR A  29      -7.126  21.333   9.747  1.00 12.36           C  
ANISOU  229  CG  TYR A  29      640   2364   1691   -186   -133   -124       C  
ATOM    230  CD1 TYR A  29      -8.007  20.331   9.336  1.00 12.56           C  
ANISOU  230  CD1 TYR A  29     1135   2208   1429    367    268    180       C  
ATOM    231  CD2 TYR A  29      -6.892  22.380   8.879  1.00 12.32           C  
ANISOU  231  CD2 TYR A  29      553   2376   1752   -346    -52     48       C  
ATOM    232  CE1 TYR A  29      -8.680  20.433   8.100  1.00 12.73           C  
ANISOU  232  CE1 TYR A  29     1155   2137   1544   -206    130     -6       C  
ATOM    233  CE2 TYR A  29      -7.513  22.475   7.670  1.00 10.86           C  
ANISOU  233  CE2 TYR A  29      360   2211   1553    -46    -76     24       C  
ATOM    234  CZ  TYR A  29      -8.391  21.507   7.262  1.00 11.18           C  
ANISOU  234  CZ  TYR A  29      256   2414   1575    -78     23   -103       C  
ATOM    235  OH  TYR A  29      -8.996  21.674   6.034  1.00 12.64           O  
ANISOU  235  OH  TYR A  29      703   2473   1624   -255   -129     29       O  
ATOM    236  N   ALA A  30      -5.642  21.590  13.991  1.00 11.87           N  
ANISOU  236  N   ALA A  30      373   2470   1667     59     66    113       N  
ATOM    237  CA  ALA A  30      -4.552  21.648  14.954  1.00 13.16           C  
ANISOU  237  CA  ALA A  30      977   2540   1483   -116   -124    178       C  
ATOM    238  C   ALA A  30      -4.863  20.807  16.188  1.00 13.28           C  
ANISOU  238  C   ALA A  30      800   2490   1753   -385    -68     56       C  
ATOM    239  O   ALA A  30      -3.997  20.098  16.703  1.00 16.21           O  
ANISOU  239  O   ALA A  30     1594   2934   1630   -300   -346    326       O  
ATOM    240  CB  ALA A  30      -4.285  23.082  15.348  1.00 13.62           C  
ANISOU  240  CB  ALA A  30      894   2632   1649   -515   -111    120       C  
ATOM    241  N   ASN A  31      -6.084  20.914  16.681  1.00 14.01           N  
ANISOU  241  N   ASN A  31      835   2867   1618   -208    103    210       N  
ATOM    242  CA  ASN A  31      -6.468  20.216  17.906  1.00 14.23           C  
ANISOU  242  CA  ASN A  31      984   2651   1768   -262    -84    104       C  
ATOM    243  C   ASN A  31      -6.592  18.739  17.677  1.00 15.66           C  
ANISOU  243  C   ASN A  31     1498   2726   1723   -232     81     64       C  
ATOM    244  O   ASN A  31      -6.226  17.945  18.532  1.00 17.30           O  
ANISOU  244  O   ASN A  31     1962   2779   1830   -330    -47    161       O  
ATOM    245  CB  ASN A  31      -7.754  20.796  18.486  1.00 15.52           C  
ANISOU  245  CB  ASN A  31     1459   2677   1759   -297    368     32       C  
ATOM    246  CG  ASN A  31      -7.504  22.071  19.266  1.00 16.15           C  
ANISOU  246  CG  ASN A  31     1662   2738   1735   -553     97    -78       C  
ATOM    247  OD1 ASN A  31      -6.482  22.197  19.956  1.00 21.56           O  
ANISOU  247  OD1 ASN A  31     1859   3396   2934   -233   -533   -577       O  
ATOM    248  ND2 ASN A  31      -8.397  23.018  19.151  1.00 17.60           N  
ANISOU  248  ND2 ASN A  31     1538   2995   2154    -74    109    223       N  
ATOM    249  N   ILE A  32      -7.118  18.359  16.515  1.00 15.17           N  
ANISOU  249  N   ILE A  32     1391   2750   1622   -485     74    185       N  
ATOM    250  CA  ILE A  32      -7.175  16.952  16.161  1.00 15.65           C  
ANISOU  250  CA  ILE A  32     1428   2764   1752   -435    -58     23       C  
ATOM    251  C   ILE A  32      -5.756  16.372  16.149  1.00 15.28           C  
ANISOU  251  C   ILE A  32     1467   2584   1752   -333    127    175       C  
ATOM    252  O   ILE A  32      -5.483  15.345  16.773  1.00 17.68           O  
ANISOU  252  O   ILE A  32     2262   2516   1939   -318    102    160       O  
ATOM    253  CB  ILE A  32      -7.837  16.734  14.802  1.00 16.72           C  
ANISOU  253  CB  ILE A  32     1899   2591   1862   -621    168    -45       C  
ATOM    254  CG1 ILE A  32      -9.331  17.090  14.888  1.00 18.49           C  
ANISOU  254  CG1 ILE A  32     2052   2773   2198   -394     27    -10       C  
ATOM    255  CG2 ILE A  32      -7.623  15.272  14.341  1.00 17.99           C  
ANISOU  255  CG2 ILE A  32     1632   3000   2201   -453   -194   -230       C  
ATOM    256  CD1 ILE A  32     -10.047  17.184  13.529  1.00 19.75           C  
ANISOU  256  CD1 ILE A  32     2200   3143   2159   -670   -165    226       C  
ATOM    257  N   ILE A  33      -4.861  17.025  15.435  1.00 15.17           N  
ANISOU  257  N   ILE A  33     1268   2479   2017   -214    216    237       N  
ATOM    258  CA  ILE A  33      -3.490  16.541  15.321  1.00 15.90           C  
ANISOU  258  CA  ILE A  33     1646   2532   1864    -38   -133     90       C  
ATOM    259  C   ILE A  33      -2.785  16.493  16.686  1.00 16.83           C  
ANISOU  259  C   ILE A  33     1646   2619   2128    -63    168    184       C  
ATOM    260  O   ILE A  33      -2.174  15.488  17.046  1.00 20.08           O  
ANISOU  260  O   ILE A  33     2644   2961   2022    330    170    383       O  
ATOM    261  CB  ILE A  33      -2.699  17.397  14.324  1.00 14.84           C  
ANISOU  261  CB  ILE A  33     1069   2730   1836    -78    243     55       C  
ATOM    262  CG1 ILE A  33      -3.209  17.137  12.908  1.00 15.22           C  
ANISOU  262  CG1 ILE A  33      893   2788   2099   -167    228     39       C  
ATOM    263  CG2 ILE A  33      -1.205  17.095  14.403  1.00 16.83           C  
ANISOU  263  CG2 ILE A  33     1061   3050   2280    215    -16    203       C  
ATOM    264  CD1 ILE A  33      -2.783  18.195  11.897  1.00 14.82           C  
ANISOU  264  CD1 ILE A  33      739   2869   2020   -349    110    184       C  
ATOM    265  N   ASP A  34      -2.925  17.555  17.463  1.00 16.86           N  
ANISOU  265  N   ASP A  34     1787   2853   1763     65   -272     64       N  
ATOM    266  CA  ASP A  34      -2.270  17.626  18.765  1.00 17.99           C  
ANISOU  266  CA  ASP A  34     2049   2876   1908     52   -126    163       C  
ATOM    267  C   ASP A  34      -2.784  16.507  19.697  1.00 20.91           C  
ANISOU  267  C   ASP A  34     2574   3176   2194    -85   -326    172       C  
ATOM    268  O   ASP A  34      -2.016  15.914  20.463  1.00 22.40           O  
ANISOU  268  O   ASP A  34     2875   3603   2033    -12   -270    320       O  
ATOM    269  CB  ASP A  34      -2.528  18.993  19.384  1.00 18.96           C  
ANISOU  269  CB  ASP A  34     2114   3193   1896    371   -192     74       C  
ATOM    270  CG  ASP A  34      -1.828  19.182  20.675  1.00 20.45           C  
ANISOU  270  CG  ASP A  34     2106   3747   1914     65    154     25       C  
ATOM    271  OD1 ASP A  34      -0.595  19.011  20.709  1.00 25.05           O  
ANISOU  271  OD1 ASP A  34     2032   4501   2985   -153   -495    124       O  
ATOM    272  OD2 ASP A  34      -2.496  19.567  21.644  1.00 21.97           O  
ANISOU  272  OD2 ASP A  34     2359   3999   1989    123   -188    252       O  
ATOM    273  N   ASP A  35      -4.087  16.220  19.612  1.00 19.32           N  
ANISOU  273  N   ASP A  35     2240   3035   2064   -333    -91    289       N  
ATOM    274  CA  ASP A  35      -4.711  15.222  20.476  1.00 22.55           C  
ANISOU  274  CA  ASP A  35     2859   3497   2212   -170   -133    363       C  
ATOM    275  C   ASP A  35      -4.282  13.800  20.123  1.00 21.49           C  
ANISOU  275  C   ASP A  35     2754   3230   2179   -151    -64    542       C  
ATOM    276  O   ASP A  35      -3.964  12.998  21.017  1.00 24.40           O  
ANISOU  276  O   ASP A  35     3193   3597   2481   -277    -99    775       O  
ATOM    277  CB  ASP A  35      -6.221  15.311  20.377  1.00 21.16           C  
ANISOU  277  CB  ASP A  35     2365   3305   2367   -158    142    494       C  
ATOM    278  CG  ASP A  35      -6.793  16.493  21.135  1.00 27.91           C  
ANISOU  278  CG  ASP A  35     3324   4154   3125   -200    223    -33       C  
ATOM    279  OD1 ASP A  35      -6.036  17.154  21.893  1.00 30.37           O  
ANISOU  279  OD1 ASP A  35     3751   4640   3147   -134    322   -399       O  
ATOM    280  OD2 ASP A  35      -8.014  16.751  20.983  1.00 27.23           O  
ANISOU  280  OD2 ASP A  35     2766   4445   3134    170   1139    439       O  
ATOM    281  N   ILE A  36      -4.327  13.456  18.832  1.00 21.01           N  
ANISOU  281  N   ILE A  36     2682   3078   2221   -105    230    482       N  
ATOM    282  CA  ILE A  36      -4.185  12.064  18.430  1.00 20.86           C  
ANISOU  282  CA  ILE A  36     2502   3003   2420    -29    188    428       C  
ATOM    283  C   ILE A  36      -2.736  11.669  18.136  1.00 23.40           C  
ANISOU  283  C   ILE A  36     2863   3124   2902     92    226    251       C  
ATOM    284  O   ILE A  36      -2.404  10.489  18.148  1.00 27.09           O  
ANISOU  284  O   ILE A  36     3239   3356   3698    337    384    662       O  
ATOM    285  CB  ILE A  36      -5.119  11.691  17.220  1.00 22.93           C  
ANISOU  285  CB  ILE A  36     2887   2849   2976   -120    220    389       C  
ATOM    286  CG1 ILE A  36      -4.640  12.339  15.917  1.00 20.75           C  
ANISOU  286  CG1 ILE A  36     1999   3204   2678   -240     38   -167       C  
ATOM    287  CG2 ILE A  36      -6.563  12.096  17.519  1.00 24.38           C  
ANISOU  287  CG2 ILE A  36     2451   3420   3391   -138    172    393       C  
ATOM    288  CD1 ILE A  36      -5.485  11.942  14.673  1.00 20.00           C  
ANISOU  288  CD1 ILE A  36     1271   3331   2996   -195    134    -34       C  
ATOM    289  N   CYS A  37      -1.871  12.653  17.927  1.00 21.96           N  
ANISOU  289  N   CYS A  37     2497   3087   2760    155   -185    158       N  
ATOM    290  CA  CYS A  37      -0.442  12.374  17.670  1.00 24.17           C  
ANISOU  290  CA  CYS A  37     2544   3616   3021    328   -394     18       C  
ATOM    291  C   CYS A  37       0.395  12.560  18.938  1.00 27.85           C  
ANISOU  291  C   CYS A  37     2966   4091   3522    330   -539   -254       C  
ATOM    292  O   CYS A  37      -0.014  13.279  19.844  1.00 31.68           O  
ANISOU  292  O   CYS A  37     3382   4970   3683    352   -541   -565       O  
ATOM    293  CB  CYS A  37       0.087  13.285  16.564  1.00 22.52           C  
ANISOU  293  CB  CYS A  37     2095   3080   3380     42   -337    -63       C  
ATOM    294  SG  CYS A  37      -0.786  13.125  15.017  1.00 22.34           S  
ANISOU  294  SG  CYS A  37     2599   3180   2709    164    227    247       S  
ATOM    295  N   PRO A  38       1.578  11.893  19.004  1.00 29.41           N  
ANISOU  295  N   PRO A  38     3159   4411   3602    307   -557    -23       N  
ATOM    296  CA  PRO A  38       2.047  10.933  18.005  1.00 27.55           C  
ANISOU  296  CA  PRO A  38     2824   4108   3536    280   -352     96       C  
ATOM    297  C   PRO A  38       1.228   9.648  17.990  1.00 29.14           C  
ANISOU  297  C   PRO A  38     3556   4038   3478    293   -186    289       C  
ATOM    298  O   PRO A  38       0.753   9.199  19.035  1.00 29.71           O  
ANISOU  298  O   PRO A  38     3727   4470   3089    428   -213    365       O  
ATOM    299  CB  PRO A  38       3.497  10.639  18.447  1.00 27.19           C  
ANISOU  299  CB  PRO A  38     2460   4263   3607    390   -350    135       C  
ATOM    300  CG  PRO A  38       3.526  10.956  19.875  1.00 33.59           C  
ANISOU  300  CG  PRO A  38     4029   4707   4027    276   -381    -83       C  
ATOM    301  CD  PRO A  38       2.556  12.074  20.091  1.00 31.24           C  
ANISOU  301  CD  PRO A  38     3760   4412   3696    251   -468    -73       C  
ATOM    302  N   CYS A  39       1.071   9.063  16.810  1.00 27.58           N  
ANISOU  302  N   CYS A  39     3631   3829   3018    165   -272    208       N  
ATOM    303  CA  CYS A  39       0.396   7.782  16.676  1.00 29.47           C  
ANISOU  303  CA  CYS A  39     3911   3597   3688     59    -60    316       C  
ATOM    304  C   CYS A  39       0.757   7.083  15.366  1.00 27.93           C  
ANISOU  304  C   CYS A  39     3751   3189   3670    -17     75    235       C  
ATOM    305  O   CYS A  39       1.374   7.675  14.479  1.00 26.14           O  
ANISOU  305  O   CYS A  39     3413   2778   3740    -34    124    151       O  
ATOM    306  CB  CYS A  39      -1.119   7.963  16.765  1.00 30.78           C  
ANISOU  306  CB  CYS A  39     4103   3953   3636    270   -209    344       C  
ATOM    307  SG  CYS A  39      -1.851   8.860  15.388  1.00 31.15           S  
ANISOU  307  SG  CYS A  39     4242   3829   3764    455   -813    639       S  
ATOM    308  N   ASP A  40       0.375   5.811  15.265  1.00 28.15           N  
ANISOU  308  N   ASP A  40     3730   2997   3967   -163    168    403       N  
ATOM    309  CA  ASP A  40       0.585   5.030  14.059  1.00 30.37           C  
ANISOU  309  CA  ASP A  40     3999   3140   4401   -194     37    204       C  
ATOM    310  C   ASP A  40      -0.243   5.578  12.910  1.00 29.82           C  
ANISOU  310  C   ASP A  40     4065   3141   4124   -163    146    239       C  
ATOM    311  O   ASP A  40      -1.317   6.146  13.125  1.00 29.74           O  
ANISOU  311  O   ASP A  40     3731   3335   4232   -512    104    123       O  
ATOM    312  CB  ASP A  40       0.204   3.556  14.309  1.00 32.06           C  
ANISOU  312  CB  ASP A  40     4312   3302   4567   -215    130    379       C  
ATOM    313  CG  ASP A  40      -1.275   3.379  14.626  1.00 39.73           C  
ANISOU  313  CG  ASP A  40     5368   4457   5269   -220     68    202       C  
ATOM    314  OD1 ASP A  40      -1.689   3.712  15.761  1.00 47.36           O  
ANISOU  314  OD1 ASP A  40     6530   5296   6166    255    529    311       O  
ATOM    315  OD2 ASP A  40      -2.020   2.899  13.744  1.00 44.44           O  
ANISOU  315  OD2 ASP A  40     5837   5529   5518    -27   -229     51       O  
ATOM    316  N   LYS A  41       0.245   5.377  11.684  1.00 29.87           N  
ANISOU  316  N   LYS A  41     3856   3253   4239     93    260    246       N  
ATOM    317  CA  LYS A  41      -0.401   5.934  10.492  1.00 30.51           C  
ANISOU  317  CA  LYS A  41     4029   3663   3901   -134     77    166       C  
ATOM    318  C   LYS A  41      -1.838   5.445  10.344  1.00 30.37           C  
ANISOU  318  C   LYS A  41     4108   3320   4109   -127     10    300       C  
ATOM    319  O   LYS A  41      -2.751   6.237  10.087  1.00 31.60           O  
ANISOU  319  O   LYS A  41     4415   3420   4171   -369    230    511       O  
ATOM    320  CB  LYS A  41       0.406   5.579   9.235  1.00 32.83           C  
ANISOU  320  CB  LYS A  41     4358   3850   4266   -118    110    132       C  
ATOM    321  N   ALA A  42      -2.045   4.142  10.507  1.00 32.25           N  
ANISOU  321  N   ALA A  42     4244   3661   4348     16   -115    378       N  
ATOM    322  CA  ALA A  42      -3.388   3.563  10.374  1.00 32.18           C  
ANISOU  322  CA  ALA A  42     4305   3622   4297   -148      9    371       C  
ATOM    323  C   ALA A  42      -4.369   4.234  11.329  1.00 31.13           C  
ANISOU  323  C   ALA A  42     4157   3553   4116   -170    -82    448       C  
ATOM    324  O   ALA A  42      -5.494   4.597  10.943  1.00 31.93           O  
ANISOU  324  O   ALA A  42     4727   3310   4092    -58    277    732       O  
ATOM    325  CB  ALA A  42      -3.345   2.068  10.630  1.00 32.85           C  
ANISOU  325  CB  ALA A  42     4225   3541   4715    -83    -85    558       C  
ATOM    326  N   SER A  43      -3.948   4.386  12.579  1.00 31.16           N  
ANISOU  326  N   SER A  43     4436   3422   3980   -334    126    447       N  
ATOM    327  CA  SER A  43      -4.772   5.014  13.588  1.00 29.71           C  
ANISOU  327  CA  SER A  43     4023   3495   3770   -253      4    373       C  
ATOM    328  C   SER A  43      -5.022   6.478  13.242  1.00 28.05           C  
ANISOU  328  C   SER A  43     3750   3414   3495   -223     61    580       C  
ATOM    329  O   SER A  43      -6.107   7.011  13.487  1.00 27.67           O  
ANISOU  329  O   SER A  43     3590   3529   3393   -216    377    694       O  
ATOM    330  CB  SER A  43      -4.094   4.911  14.955  1.00 31.67           C  
ANISOU  330  CB  SER A  43     4339   3748   3943    -52     54    529       C  
ATOM    331  OG  SER A  43      -3.982   3.556  15.368  1.00 35.69           O  
ANISOU  331  OG  SER A  43     5040   4033   4485      4    -21    364       O  
ATOM    332  N   PHE A  44      -4.012   7.123  12.665  1.00 25.51           N  
ANISOU  332  N   PHE A  44     3047   3312   3332   -368   -153    487       N  
ATOM    333  CA  PHE A  44      -4.103   8.547  12.325  1.00 23.28           C  
ANISOU  333  CA  PHE A  44     2766   3136   2943   -180     56    370       C  
ATOM    334  C   PHE A  44      -5.218   8.814  11.324  1.00 20.96           C  
ANISOU  334  C   PHE A  44     2740   2707   2516   -351    149    374       C  
ATOM    335  O   PHE A  44      -6.016   9.725  11.504  1.00 20.82           O  
ANISOU  335  O   PHE A  44     2186   3140   2585   -393    -45    355       O  
ATOM    336  CB  PHE A  44      -2.780   9.040  11.757  1.00 21.33           C  
ANISOU  336  CB  PHE A  44     2283   2820   3001   -208    -18    299       C  
ATOM    337  CG  PHE A  44      -2.777  10.506  11.411  1.00 21.12           C  
ANISOU  337  CG  PHE A  44     2361   2806   2855   -211   -368    342       C  
ATOM    338  CD1 PHE A  44      -2.865  11.467  12.401  1.00 23.59           C  
ANISOU  338  CD1 PHE A  44     3047   3137   2778   -158   -289    613       C  
ATOM    339  CD2 PHE A  44      -2.699  10.916  10.098  1.00 20.39           C  
ANISOU  339  CD2 PHE A  44     2257   2819   2668   -639   -218    323       C  
ATOM    340  CE1 PHE A  44      -2.867  12.811  12.079  1.00 24.55           C  
ANISOU  340  CE1 PHE A  44     3400   3201   2727   -171   -290    269       C  
ATOM    341  CE2 PHE A  44      -2.690  12.261   9.773  1.00 18.55           C  
ANISOU  341  CE2 PHE A  44     1483   3114   2451   -503   -409    583       C  
ATOM    342  CZ  PHE A  44      -2.789  13.201  10.753  1.00 20.07           C  
ANISOU  342  CZ  PHE A  44     2136   2920   2567   -294   -306    312       C  
ATOM    343  N   VAL A  45      -5.275   8.005  10.278  1.00 22.01           N  
ANISOU  343  N   VAL A  45     2551   3018   2791   -248    109    285       N  
ATOM    344  CA  VAL A  45      -6.285   8.172   9.241  1.00 22.73           C  
ANISOU  344  CA  VAL A  45     2916   2997   2720   -106    -39    153       C  
ATOM    345  C   VAL A  45      -7.678   8.085   9.824  1.00 22.31           C  
ANISOU  345  C   VAL A  45     3004   2756   2714   -226   -158    303       C  
ATOM    346  O   VAL A  45      -8.517   8.941   9.568  1.00 21.44           O  
ANISOU  346  O   VAL A  45     2405   2858   2882   -494   -309    232       O  
ATOM    347  CB  VAL A  45      -6.121   7.109   8.123  1.00 25.67           C  
ANISOU  347  CB  VAL A  45     3119   3724   2909     -9    -72    219       C  
ATOM    348  CG1 VAL A  45      -7.297   7.161   7.149  1.00 25.18           C  
ANISOU  348  CG1 VAL A  45     3514   3163   2888     26    345    185       C  
ATOM    349  CG2 VAL A  45      -4.794   7.321   7.392  1.00 26.47           C  
ANISOU  349  CG2 VAL A  45     3811   3335   2909    388    763    159       C  
ATOM    350  N   LYS A  46      -7.924   7.051  10.615  1.00 23.70           N  
ANISOU  350  N   LYS A  46     3288   2960   2754   -318   -118    287       N  
ATOM    351  CA  LYS A  46      -9.256   6.799  11.137  1.00 25.07           C  
ANISOU  351  CA  LYS A  46     3268   3195   3060   -276    158    293       C  
ATOM    352  C   LYS A  46      -9.656   7.881  12.117  1.00 23.19           C  
ANISOU  352  C   LYS A  46     3146   2765   2897   -427    112    506       C  
ATOM    353  O   LYS A  46     -10.754   8.447  12.026  1.00 25.01           O  
ANISOU  353  O   LYS A  46     3064   3172   3265   -559    104    418       O  
ATOM    354  CB  LYS A  46      -9.311   5.424  11.819  1.00 27.13           C  
ANISOU  354  CB  LYS A  46     3499   3229   3579   -213    200    234       C  
ATOM    355  CG  LYS A  46     -10.601   5.159  12.596  1.00 32.65           C  
ANISOU  355  CG  LYS A  46     3909   4288   4206   -401    201      5       C  
ATOM    356  N   ASP A  47      -8.758   8.182  13.047  1.00 23.17           N  
ANISOU  356  N   ASP A  47     2914   2972   2916   -568    142    396       N  
ATOM    357  CA  ASP A  47      -9.052   9.112  14.119  1.00 23.61           C  
ANISOU  357  CA  ASP A  47     2750   3142   3077   -650    266    341       C  
ATOM    358  C   ASP A  47      -9.176  10.550  13.609  1.00 19.51           C  
ANISOU  358  C   ASP A  47     1935   2879   2597   -557    349     99       C  
ATOM    359  O   ASP A  47     -10.034  11.312  14.063  1.00 22.95           O  
ANISOU  359  O   ASP A  47     2900   3088   2731   -931    506     81       O  
ATOM    360  CB  ASP A  47      -7.983   9.014  15.203  1.00 25.07           C  
ANISOU  360  CB  ASP A  47     3041   3223   3259   -725    286    473       C  
ATOM    361  CG  ASP A  47      -8.041   7.689  15.966  1.00 32.03           C  
ANISOU  361  CG  ASP A  47     4078   4087   4004   -457     32    671       C  
ATOM    362  OD1 ASP A  47      -9.104   7.018  15.928  1.00 36.70           O  
ANISOU  362  OD1 ASP A  47     5538   4198   4208  -1268     13   1013       O  
ATOM    363  OD2 ASP A  47      -7.029   7.321  16.590  1.00 36.06           O  
ANISOU  363  OD2 ASP A  47     5184   4474   4042   -229   -307   1386       O  
ATOM    364  N   PHE A  48      -8.334  10.916  12.653  1.00 18.98           N  
ANISOU  364  N   PHE A  48     2061   2878   2269   -584    200    201       N  
ATOM    365  CA  PHE A  48      -8.424  12.236  12.053  1.00 17.63           C  
ANISOU  365  CA  PHE A  48     1670   2772   2256   -547    197     88       C  
ATOM    366  C   PHE A  48      -9.782  12.420  11.367  1.00 16.50           C  
ANISOU  366  C   PHE A  48     1821   2355   2093   -466    282    138       C  
ATOM    367  O   PHE A  48     -10.481  13.392  11.610  1.00 18.19           O  
ANISOU  367  O   PHE A  48     1908   2803   2199   -768    484    -37       O  
ATOM    368  CB  PHE A  48      -7.292  12.453  11.046  1.00 17.21           C  
ANISOU  368  CB  PHE A  48     1829   2638   2071   -460    268    167       C  
ATOM    369  CG  PHE A  48      -7.300  13.809  10.422  1.00 14.90           C  
ANISOU  369  CG  PHE A  48     1252   2476   1932   -395    141     31       C  
ATOM    370  CD1 PHE A  48      -8.131  14.083   9.346  1.00 15.91           C  
ANISOU  370  CD1 PHE A  48     1363   2596   2085   -482    179   -237       C  
ATOM    371  CD2 PHE A  48      -6.455  14.814  10.896  1.00 16.58           C  
ANISOU  371  CD2 PHE A  48     1712   2734   1853   -252     61    266       C  
ATOM    372  CE1 PHE A  48      -8.149  15.332   8.766  1.00 17.50           C  
ANISOU  372  CE1 PHE A  48     1630   2501   2517    132    369    -78       C  
ATOM    373  CE2 PHE A  48      -6.477  16.072  10.331  1.00 18.36           C  
ANISOU  373  CE2 PHE A  48     2374   2508   2092   -319    346   -140       C  
ATOM    374  CZ  PHE A  48      -7.318  16.331   9.256  1.00 15.58           C  
ANISOU  374  CZ  PHE A  48     1020   2400   2498    105   1000     57       C  
ATOM    375  N   ASN A  49     -10.138  11.475  10.507  1.00 19.09           N  
ANISOU  375  N   ASN A  49     2430   2704   2117   -670    171     83       N  
ATOM    376  CA  ASN A  49     -11.378  11.562   9.743  1.00 18.57           C  
ANISOU  376  CA  ASN A  49     1864   2861   2329   -571    330    147       C  
ATOM    377  C   ASN A  49     -12.612  11.570  10.648  1.00 18.39           C  
ANISOU  377  C   ASN A  49     1764   2821   2400   -394    168    112       C  
ATOM    378  O   ASN A  49     -13.555  12.305  10.410  1.00 20.35           O  
ANISOU  378  O   ASN A  49     2124   3071   2535   -679    147     31       O  
ATOM    379  CB  ASN A  49     -11.487  10.393   8.774  1.00 19.20           C  
ANISOU  379  CB  ASN A  49     2319   2933   2040   -415     29   -109       C  
ATOM    380  CG  ASN A  49     -10.617  10.559   7.550  1.00 19.28           C  
ANISOU  380  CG  ASN A  49     2154   2935   2234   -464    -65     -1       C  
ATOM    381  OD1 ASN A  49      -9.732  11.418   7.507  1.00 20.09           O  
ANISOU  381  OD1 ASN A  49     2562   2923   2148   -865    105   -165       O  
ATOM    382  ND2 ASN A  49     -10.863   9.724   6.536  1.00 18.14           N  
ANISOU  382  ND2 ASN A  49     1860   2948   2082   -191   -356    -68       N  
ATOM    383  N   ASN A  50     -12.593  10.741  11.686  1.00 18.84           N  
ANISOU  383  N   ASN A  50     1648   3032   2476   -527    150    -54       N  
ATOM    384  CA  ASN A  50     -13.711  10.672  12.620  1.00 20.63           C  
ANISOU  384  CA  ASN A  50     1858   3220   2758   -759    178    147       C  
ATOM    385  C   ASN A  50     -13.951  11.983  13.362  1.00 20.33           C  
ANISOU  385  C   ASN A  50     1502   3548   2673   -674    221    -35       C  
ATOM    386  O   ASN A  50     -15.093  12.323  13.671  1.00 23.04           O  
ANISOU  386  O   ASN A  50     1945   3585   3221   -801    524   -201       O  
ATOM    387  CB  ASN A  50     -13.517   9.523  13.620  1.00 21.90           C  
ANISOU  387  CB  ASN A  50     1523   3524   3270   -848    144    266       C  
ATOM    388  CG  ASN A  50     -13.833   8.159  13.015  1.00 31.49           C  
ANISOU  388  CG  ASN A  50     3542   4132   4291   -527   -238    384       C  
ATOM    389  OD1 ASN A  50     -14.508   8.063  11.993  1.00 37.01           O  
ANISOU  389  OD1 ASN A  50     4495   4441   5125  -1482   -470    308       O  
ATOM    390  ND2 ASN A  50     -13.340   7.103  13.647  1.00 30.31           N  
ANISOU  390  ND2 ASN A  50     2479   4024   5010    -57    651    728       N  
ATOM    391  N   ARG A  51     -12.878  12.721  13.647  1.00 18.15           N  
ANISOU  391  N   ARG A  51     1625   3117   2154   -767    393    239       N  
ATOM    392  CA  ARG A  51     -13.010  14.036  14.263  1.00 18.77           C  
ANISOU  392  CA  ARG A  51     1881   3188   2063   -665    170     12       C  
ATOM    393  C   ARG A  51     -13.424  15.109  13.238  1.00 18.12           C  
ANISOU  393  C   ARG A  51     1802   3074   2007   -472    292   -170       C  
ATOM    394  O   ARG A  51     -14.302  15.931  13.511  1.00 18.89           O  
ANISOU  394  O   ARG A  51      906   3844   2427   -725    297   -147       O  
ATOM    395  CB  ARG A  51     -11.701  14.449  14.958  1.00 20.05           C  
ANISOU  395  CB  ARG A  51     2150   3307   2160   -728    -57    -43       C  
ATOM    396  CG  ARG A  51     -11.364  13.656  16.232  1.00 27.14           C  
ANISOU  396  CG  ARG A  51     3733   3525   3051   -708    267     81       C  
ATOM    397  CD  ARG A  51     -11.893  14.330  17.516  1.00 32.23           C  
ANISOU  397  CD  ARG A  51     4123   4173   3948   -180    423     98       C  
ATOM    398  NE  ARG A  51     -11.395  15.707  17.726  1.00 29.13           N  
ANISOU  398  NE  ARG A  51     3075   4913   3079   -476    456    139       N  
ATOM    399  CZ  ARG A  51     -10.307  16.031  18.443  1.00 32.55           C  
ANISOU  399  CZ  ARG A  51     4156   4503   3708   -331    279     34       C  
ATOM    400  NH1 ARG A  51      -9.558  15.090  19.010  1.00 28.89           N  
ANISOU  400  NH1 ARG A  51     2923   4866   3186   -158    739    -19       N  
ATOM    401  NH2 ARG A  51      -9.967  17.304  18.582  1.00 32.77           N  
ANISOU  401  NH2 ARG A  51     4333   5162   2953   -744    594   -221       N  
ATOM    402  N   LEU A  52     -12.800  15.101  12.059  1.00 18.72           N  
ANISOU  402  N   LEU A  52     1693   3200   2219   -517    596    -23       N  
ATOM    403  CA  LEU A  52     -13.030  16.180  11.079  1.00 17.35           C  
ANISOU  403  CA  LEU A  52     1415   3071   2104   -323    337    -42       C  
ATOM    404  C   LEU A  52     -14.469  16.161  10.566  1.00 15.22           C  
ANISOU  404  C   LEU A  52     1054   2641   2085   -583    397    -59       C  
ATOM    405  O   LEU A  52     -15.064  17.215  10.301  1.00 18.00           O  
ANISOU  405  O   LEU A  52     1267   3188   2381   -604    622     31       O  
ATOM    406  CB  LEU A  52     -12.031  16.090   9.901  1.00 16.76           C  
ANISOU  406  CB  LEU A  52     1176   2988   2203   -475    408   -132       C  
ATOM    407  CG  LEU A  52     -12.180  17.209   8.856  1.00 16.57           C  
ANISOU  407  CG  LEU A  52      494   3425   2376   -349    651     40       C  
ATOM    408  CD1 LEU A  52     -11.996  18.594   9.492  1.00 19.36           C  
ANISOU  408  CD1 LEU A  52     1040   3170   3143    267   1067     97       C  
ATOM    409  CD2 LEU A  52     -11.192  17.015   7.710  1.00 17.45           C  
ANISOU  409  CD2 LEU A  52      706   3492   2429   -259    925    408       C  
ATOM    410  N   ILE A  53     -15.046  14.980  10.463  1.00 19.43           N  
ANISOU  410  N   ILE A  53     1328   3409   2644   -393    194    157       N  
ATOM    411  CA  ILE A  53     -16.390  14.878   9.901  1.00 19.26           C  
ANISOU  411  CA  ILE A  53     1098   3493   2727   -348    371     23       C  
ATOM    412  C   ILE A  53     -17.454  15.605  10.785  1.00 19.79           C  
ANISOU  412  C   ILE A  53      963   3853   2703   -213    305    -71       C  
ATOM    413  O   ILE A  53     -18.518  16.013  10.304  1.00 23.35           O  
ANISOU  413  O   ILE A  53     1641   4371   2857   -413    347    124       O  
ATOM    414  CB  ILE A  53     -16.812  13.420   9.664  1.00 21.15           C  
ANISOU  414  CB  ILE A  53     1590   3527   2915   -562    618    141       C  
ATOM    415  CG1 ILE A  53     -18.015  13.381   8.706  1.00 20.21           C  
ANISOU  415  CG1 ILE A  53     1359   3352   2968   -570    269     49       C  
ATOM    416  CG2 ILE A  53     -17.169  12.732  11.001  1.00 23.87           C  
ANISOU  416  CG2 ILE A  53     2617   3747   2704   -728    685    124       C  
ATOM    417  CD1 ILE A  53     -18.364  11.989   8.203  1.00 23.53           C  
ANISOU  417  CD1 ILE A  53     1444   4057   3439   -261    374   -293       C  
ATOM    418  N   GLU A  54     -17.138  15.780  12.059  1.00 21.69           N  
ANISOU  418  N   GLU A  54     1226   4178   2837   -479    458   -205       N  
ATOM    419  CA  GLU A  54     -17.994  16.547  12.963  1.00 23.03           C  
ANISOU  419  CA  GLU A  54     1659   4140   2950   -332    414   -161       C  
ATOM    420  C   GLU A  54     -18.008  18.035  12.621  1.00 23.15           C  
ANISOU  420  C   GLU A  54     1481   4062   3252    104    745   -428       C  
ATOM    421  O   GLU A  54     -18.981  18.734  12.913  1.00 29.82           O  
ANISOU  421  O   GLU A  54     2262   4702   4364     -2    788   -248       O  
ATOM    422  CB  GLU A  54     -17.559  16.338  14.411  1.00 26.16           C  
ANISOU  422  CB  GLU A  54     2520   4357   3059   -398    409   -305       C  
ATOM    423  CG  GLU A  54     -17.755  14.916  14.897  1.00 28.83           C  
ANISOU  423  CG  GLU A  54     2708   4634   3611   -462    855     66       C  
ATOM    424  CD  GLU A  54     -19.224  14.465  14.813  1.00 39.08           C  
ANISOU  424  CD  GLU A  54     3641   5657   5551   -189    511     27       C  
ATOM    425  OE1 GLU A  54     -20.121  15.265  15.179  1.00 47.53           O  
ANISOU  425  OE1 GLU A  54     5758   5973   6326    348    718    349       O  
ATOM    426  OE2 GLU A  54     -19.475  13.316  14.379  1.00 41.15           O  
ANISOU  426  OE2 GLU A  54     3586   6286   5762   -252   1094    -17       O  
ATOM    427  N   ILE A  55     -16.951  18.510  11.968  1.00 20.97           N  
ANISOU  427  N   ILE A  55     1148   3925   2892   -371    367   -258       N  
ATOM    428  CA  ILE A  55     -16.865  19.899  11.558  1.00 21.24           C  
ANISOU  428  CA  ILE A  55     1515   3802   2751    -96    866   -582       C  
ATOM    429  C   ILE A  55     -17.476  20.105  10.167  1.00 19.96           C  
ANISOU  429  C   ILE A  55     1039   3552   2991    105    416   -446       C  
ATOM    430  O   ILE A  55     -18.165  21.097   9.917  1.00 25.00           O  
ANISOU  430  O   ILE A  55     1627   4297   3574    163    541   -754       O  
ATOM    431  CB  ILE A  55     -15.393  20.381  11.530  1.00 21.52           C  
ANISOU  431  CB  ILE A  55      847   4050   3278   -236    589   -330       C  
ATOM    432  CG1 ILE A  55     -14.746  20.171  12.900  1.00 26.00           C  
ANISOU  432  CG1 ILE A  55     2106   4279   3491   -648    446   -320       C  
ATOM    433  CG2 ILE A  55     -15.323  21.841  11.113  1.00 25.47           C  
ANISOU  433  CG2 ILE A  55     1764   3835   4075   -309    924   -707       C  
ATOM    434  CD1 ILE A  55     -15.420  20.934  14.017  1.00 31.85           C  
ANISOU  434  CD1 ILE A  55     2991   4888   4221   -140   -170   -691       C  
ATOM    435  N   LEU A  56     -17.181  19.179   9.253  1.00 20.35           N  
ANISOU  435  N   LEU A  56     1538   3500   2693   -268    467   -335       N  
ATOM    436  CA  LEU A  56     -17.562  19.342   7.856  1.00 16.30           C  
ANISOU  436  CA  LEU A  56      415   3328   2447   -434    507   -275       C  
ATOM    437  C   LEU A  56     -19.014  18.899   7.608  1.00 20.11           C  
ANISOU  437  C   LEU A  56     1299   3466   2873   -368    442   -173       C  
ATOM    438  O   LEU A  56     -19.653  19.397   6.706  1.00 20.44           O  
ANISOU  438  O   LEU A  56      542   4157   3064   -219    603    -67       O  
ATOM    439  CB  LEU A  56     -16.597  18.569   6.947  1.00 19.30           C  
ANISOU  439  CB  LEU A  56     1401   3487   2445   -382    104   -247       C  
ATOM    440  CG  LEU A  56     -15.177  19.113   6.850  1.00 16.44           C  
ANISOU  440  CG  LEU A  56      856   3064   2324   -226    -48    -55       C  
ATOM    441  CD1 LEU A  56     -14.396  18.299   5.844  1.00 17.60           C  
ANISOU  441  CD1 LEU A  56     1271   2875   2537   -204    789   -387       C  
ATOM    442  CD2 LEU A  56     -15.197  20.588   6.463  1.00 18.41           C  
ANISOU  442  CD2 LEU A  56     1004   3040   2950   -297    852   -240       C  
ATOM    443  N   GLY A  57     -19.503  17.957   8.411  1.00 21.34           N  
ANISOU  443  N   GLY A  57     1060   3871   3176      8    243   -211       N  
ATOM    444  CA  GLY A  57     -20.902  17.513   8.321  1.00 21.03           C  
ANISOU  444  CA  GLY A  57     1169   3806   3014   -284    524   -248       C  
ATOM    445  C   GLY A  57     -21.007  16.047   7.941  1.00 21.86           C  
ANISOU  445  C   GLY A  57     1661   3504   3139   -401    560   -308       C  
ATOM    446  O   GLY A  57     -20.156  15.522   7.216  1.00 19.73           O  
ANISOU  446  O   GLY A  57      711   3878   2907   -432    614   -490       O  
ATOM    447  N   GLU A  58     -22.100  15.411   8.344  1.00 23.67           N  
ANISOU  447  N   GLU A  58     1812   3863   3317   -891    748   -128       N  
ATOM    448  CA  GLU A  58     -22.226  13.949   8.268  1.00 25.24           C  
ANISOU  448  CA  GLU A  58     2344   3954   3290   -462    835    -14       C  
ATOM    449  C   GLU A  58     -22.333  13.420   6.822  1.00 22.58           C  
ANISOU  449  C   GLU A  58     1598   3636   3343   -553    462    -93       C  
ATOM    450  O   GLU A  58     -22.114  12.245   6.572  1.00 26.94           O  
ANISOU  450  O   GLU A  58     2128   4112   3993   -604    588   -286       O  
ATOM    451  CB  GLU A  58     -23.447  13.488   9.078  1.00 25.35           C  
ANISOU  451  CB  GLU A  58     2008   4116   3508   -518    790     95       C  
ATOM    452  CG  GLU A  58     -24.773  13.910   8.480  1.00 30.30           C  
ANISOU  452  CG  GLU A  58     2905   4719   3889   -539    437    275       C  
ATOM    453  CD  GLU A  58     -25.962  13.528   9.348  1.00 42.10           C  
ANISOU  453  CD  GLU A  58     4402   6151   5441   -313    554    445       C  
ATOM    454  OE1 GLU A  58     -25.793  12.702  10.273  1.00 46.48           O  
ANISOU  454  OE1 GLU A  58     5019   6684   5957   -279    885    769       O  
ATOM    455  OE2 GLU A  58     -27.062  14.058   9.104  1.00 48.81           O  
ANISOU  455  OE2 GLU A  58     4530   7241   6772   -108    296    140       O  
ATOM    456  N  AGLU A  59     -22.628  14.316   5.896  0.50 21.55           N  
ANISOU  456  N  AGLU A  59     1236   3706   3245   -318    483    -74       N  
ATOM    457  N  BGLU A  59     -22.656  14.298   5.882  0.50 20.68           N  
ANISOU  457  N  BGLU A  59     1029   3660   3168   -356    480    -93       N  
ATOM    458  CA AGLU A  59     -22.810  13.955   4.503  0.50 21.87           C  
ANISOU  458  CA AGLU A  59     1655   3574   3080   -221    312   -168       C  
ATOM    459  CA BGLU A  59     -22.801  13.891   4.478  0.50 20.15           C  
ANISOU  459  CA BGLU A  59     1263   3473   2916   -252    393   -182       C  
ATOM    460  C  AGLU A  59     -21.474  13.901   3.734  0.50 19.93           C  
ANISOU  460  C  AGLU A  59     1353   3437   2780   -421    307   -232       C  
ATOM    461  C  BGLU A  59     -21.471  13.949   3.703  0.50 19.08           C  
ANISOU  461  C  BGLU A  59     1151   3387   2711   -450    357   -239       C  
ATOM    462  O  AGLU A  59     -21.426  13.433   2.606  0.50 24.48           O  
ANISOU  462  O  AGLU A  59     2096   4021   3183   -194    218   -256       O  
ATOM    463  O  BGLU A  59     -21.429  13.639   2.520  0.50 24.09           O  
ANISOU  463  O  BGLU A  59     1988   3969   3195   -211    142   -296       O  
ATOM    464  CB AGLU A  59     -23.754  14.953   3.834  0.50 24.57           C  
ANISOU  464  CB AGLU A  59     2208   3800   3327   -295     93    -46       C  
ATOM    465  CB BGLU A  59     -23.839  14.767   3.773  0.50 21.39           C  
ANISOU  465  CB BGLU A  59     1477   3636   3014   -384    228    -42       C  
ATOM    466  CG AGLU A  59     -23.245  16.408   3.838  0.50 28.70           C  
ANISOU  466  CG AGLU A  59     3070   3941   3893   -260    180    -49       C  
ATOM    467  CG BGLU A  59     -25.256  14.618   4.312  0.50 18.14           C  
ANISOU  467  CG BGLU A  59      553   3560   2777   -591    732   -184       C  
ATOM    468  CD AGLU A  59     -23.334  17.086   5.220  0.50 23.49           C  
ANISOU  468  CD AGLU A  59     1890   3057   3975   -326    456     46       C  
ATOM    469  CD BGLU A  59     -25.733  13.187   4.293  0.50 28.48           C  
ANISOU  469  CD BGLU A  59     2950   3944   3926   -255    595     -8       C  
ATOM    470  OE1AGLU A  59     -23.227  16.393   6.245  0.50 28.43           O  
ANISOU  470  OE1AGLU A  59     1519   5381   3900   -317   -306   -243       O  
ATOM    471  OE1BGLU A  59     -25.076  12.339   3.651  0.50 34.90           O  
ANISOU  471  OE1BGLU A  59     2757   5360   5140   -535    580     70       O  
ATOM    472  OE2AGLU A  59     -23.485  18.316   5.259  0.50 32.89           O  
ANISOU  472  OE2AGLU A  59     2664   4460   5370   -266    359   -779       O  
ATOM    473  OE2BGLU A  59     -26.764  12.905   4.921  0.50 31.09           O  
ANISOU  473  OE2BGLU A  59     1917   5322   4574   -307    574   -100       O  
ATOM    474  N   THR A  60     -20.404  14.368   4.374  1.00 19.14           N  
ANISOU  474  N   THR A  60     1142   3375   2755   -226    281   -263       N  
ATOM    475  CA  THR A  60     -19.058  14.447   3.741  1.00 17.92           C  
ANISOU  475  CA  THR A  60      960   3086   2762   -246    347   -133       C  
ATOM    476  C   THR A  60     -18.548  13.048   3.403  1.00 17.13           C  
ANISOU  476  C   THR A  60     1010   3017   2479   -549    584     20       C  
ATOM    477  O   THR A  60     -18.549  12.161   4.250  1.00 18.58           O  
ANISOU  477  O   THR A  60     1417   3133   2510   -518    531     36       O  
ATOM    478  CB  THR A  60     -18.079  15.133   4.693  1.00 17.03           C  
ANISOU  478  CB  THR A  60      960   2973   2536   -419    772     81       C  
ATOM    479  OG1 THR A  60     -18.614  16.399   5.102  1.00 19.61           O  
ANISOU  479  OG1 THR A  60      774   3255   3420   -398    452   -391       O  
ATOM    480  CG2 THR A  60     -16.701  15.356   4.012  1.00 15.98           C  
ANISOU  480  CG2 THR A  60      692   3105   2272   -610    829   -201       C  
ATOM    481  N   THR A  61     -18.096  12.858   2.164  1.00 16.75           N  
ANISOU  481  N   THR A  61     1075   2801   2486   -514    415   -123       N  
ATOM    482  CA  THR A  61     -17.538  11.579   1.759  1.00 16.09           C  
ANISOU  482  CA  THR A  61     1170   2546   2395   -279    173    108       C  
ATOM    483  C   THR A  61     -16.176  11.322   2.402  1.00 14.36           C  
ANISOU  483  C   THR A  61      961   2358   2137   -427    343    -49       C  
ATOM    484  O   THR A  61     -15.434  12.262   2.740  1.00 15.39           O  
ANISOU  484  O   THR A  61      954   2566   2326   -664    150    -95       O  
ATOM    485  CB  THR A  61     -17.375  11.474   0.222  1.00 15.59           C  
ANISOU  485  CB  THR A  61     1001   2493   2428   -514     70   -140       C  
ATOM    486  OG1 THR A  61     -16.406  12.435  -0.233  1.00 15.05           O  
ANISOU  486  OG1 THR A  61      759   2707   2251   -587    136    -23       O  
ATOM    487  CG2 THR A  61     -18.741  11.666  -0.501  1.00 17.29           C  
ANISOU  487  CG2 THR A  61      897   3038   2631   -705   -547    -86       C  
ATOM    488  N   LYS A  62     -15.811  10.056   2.498  1.00 15.26           N  
ANISOU  488  N   LYS A  62      890   2337   2571   -583    195    161       N  
ATOM    489  CA  LYS A  62     -14.466   9.687   2.942  1.00 16.69           C  
ANISOU  489  CA  LYS A  62     1436   2814   2089    -87    321    -15       C  
ATOM    490  C   LYS A  62     -13.404  10.325   2.071  1.00 14.49           C  
ANISOU  490  C   LYS A  62     1288   2294   1921   -365    128     15       C  
ATOM    491  O   LYS A  62     -12.375  10.744   2.563  1.00 15.66           O  
ANISOU  491  O   LYS A  62     1310   2418   2221   -456   -231     -4       O  
ATOM    492  CB  LYS A  62     -14.292   8.179   2.932  1.00 17.85           C  
ANISOU  492  CB  LYS A  62     1486   2804   2490   -214     50    -14       C  
ATOM    493  CG  LYS A  62     -12.888   7.734   3.326  1.00 20.45           C  
ANISOU  493  CG  LYS A  62     1731   3044   2995    -56    124    122       C  
ATOM    494  CD  LYS A  62     -12.805   6.241   3.477  1.00 24.09           C  
ANISOU  494  CD  LYS A  62     2007   3164   3980    174    231     65       C  
ATOM    495  CE  LYS A  62     -11.380   5.795   3.776  1.00 28.37           C  
ANISOU  495  CE  LYS A  62     2671   3678   4430    516    323    245       C  
ATOM    496  NZ  LYS A  62     -10.514   5.908   2.582  1.00 30.44           N  
ANISOU  496  NZ  LYS A  62     1860   4093   5610    201   1021    838       N  
ATOM    497  N   LYS A  63     -13.646  10.380   0.768  1.00 13.54           N  
ANISOU  497  N   LYS A  63      516   2350   2278   -412    157    -77       N  
ATOM    498  CA  LYS A  63     -12.672  10.951  -0.160  1.00 13.30           C  
ANISOU  498  CA  LYS A  63      592   2324   2134   -161    109     10       C  
ATOM    499  C   LYS A  63     -12.342  12.405   0.226  1.00 13.04           C  
ANISOU  499  C   LYS A  63      855   2095   2002     15    234    -25       C  
ATOM    500  O   LYS A  63     -11.183  12.821   0.237  1.00 12.58           O  
ANISOU  500  O   LYS A  63      498   2297   1982   -264      5    -32       O  
ATOM    501  CB  LYS A  63     -13.197  10.885  -1.602  1.00 13.27           C  
ANISOU  501  CB  LYS A  63      667   2223   2148   -197     85    -12       C  
ATOM    502  CG  LYS A  63     -12.235  11.490  -2.665  1.00 12.78           C  
ANISOU  502  CG  LYS A  63      443   2242   2168   -101     17   -184       C  
ATOM    503  CD  LYS A  63     -10.840  10.822  -2.641  1.00 13.48           C  
ANISOU  503  CD  LYS A  63      799   2552   1769    -74    -89   -105       C  
ATOM    504  CE  LYS A  63     -10.007  11.174  -3.866  1.00 12.99           C  
ANISOU  504  CE  LYS A  63      630   2081   2225    328    223    -78       C  
ATOM    505  NZ  LYS A  63     -10.480  10.544  -5.092  1.00 14.08           N  
ANISOU  505  NZ  LYS A  63     1296   2187   1864   -361    213   -315       N  
ATOM    506  N   THR A  64     -13.368  13.164   0.538  1.00 12.17           N  
ANISOU  506  N   THR A  64      307   2340   1975   -242    -44   -196       N  
ATOM    507  CA  THR A  64     -13.196  14.549   0.942  1.00 11.26           C  
ANISOU  507  CA  THR A  64      312   2226   1738    -17    295   -106       C  
ATOM    508  C   THR A  64     -12.445  14.657   2.242  1.00 11.79           C  
ANISOU  508  C   THR A  64      842   2019   1616   -213    375    -66       C  
ATOM    509  O   THR A  64     -11.533  15.476   2.372  1.00 11.42           O  
ANISOU  509  O   THR A  64      260   2110   1966   -114    -23     67       O  
ATOM    510  CB  THR A  64     -14.569  15.226   1.045  1.00 11.99           C  
ANISOU  510  CB  THR A  64      380   2144   2032   -243    427   -123       C  
ATOM    511  OG1 THR A  64     -15.113  15.275  -0.261  1.00 12.87           O  
ANISOU  511  OG1 THR A  64      401   2481   2006    -83    -17    -78       O  
ATOM    512  CG2 THR A  64     -14.492  16.623   1.635  1.00 12.06           C  
ANISOU  512  CG2 THR A  64      311   1959   2312     63    339     16       C  
ATOM    513  N   LEU A  65     -12.801  13.821   3.212  1.00 12.50           N  
ANISOU  513  N   LEU A  65      587   2321   1840   -364    204   -132       N  
ATOM    514  CA  LEU A  65     -12.077  13.804   4.479  1.00 12.31           C  
ANISOU  514  CA  LEU A  65      651   2288   1739   -214    202    -13       C  
ATOM    515  C   LEU A  65     -10.585  13.483   4.253  1.00 12.05           C  
ANISOU  515  C   LEU A  65      669   2078   1828   -300     17   -131       C  
ATOM    516  O   LEU A  65      -9.702  14.151   4.805  1.00 12.26           O  
ANISOU  516  O   LEU A  65      666   2286   1707   -398    170   -125       O  
ATOM    517  CB  LEU A  65     -12.720  12.791   5.449  1.00 13.56           C  
ANISOU  517  CB  LEU A  65      889   2518   1742   -218    -18     27       C  
ATOM    518  CG  LEU A  65     -14.152  13.108   5.910  1.00 16.04           C  
ANISOU  518  CG  LEU A  65      892   3027   2174    -42    518     10       C  
ATOM    519  CD1 LEU A  65     -14.744  11.890   6.604  1.00 17.88           C  
ANISOU  519  CD1 LEU A  65     1384   2783   2625   -940    556     42       C  
ATOM    520  CD2 LEU A  65     -14.144  14.312   6.824  1.00 16.51           C  
ANISOU  520  CD2 LEU A  65      526   3079   2668   -380    689   -138       C  
ATOM    521  N   ASP A  66     -10.318  12.440   3.469  1.00 11.39           N  
ANISOU  521  N   ASP A  66      317   2240   1771   -320    -74     65       N  
ATOM    522  CA  ASP A  66      -8.960  12.062   3.143  1.00 11.24           C  
ANISOU  522  CA  ASP A  66      299   2171   1798    -52    -98     44       C  
ATOM    523  C   ASP A  66      -8.221  13.224   2.475  1.00 11.65           C  
ANISOU  523  C   ASP A  66      544   1981   1901   -287    -70     82       C  
ATOM    524  O   ASP A  66      -7.068  13.515   2.803  1.00 11.55           O  
ANISOU  524  O   ASP A  66      258   2331   1798   -105     12     93       O  
ATOM    525  CB  ASP A  66      -8.956  10.848   2.183  1.00 12.70           C  
ANISOU  525  CB  ASP A  66      689   2191   1945   -173    229    113       C  
ATOM    526  CG  ASP A  66      -9.323   9.529   2.870  1.00 13.75           C  
ANISOU  526  CG  ASP A  66      751   2406   2067    -79    -92   -248       C  
ATOM    527  OD1 ASP A  66      -9.221   9.435   4.107  1.00 17.69           O  
ANISOU  527  OD1 ASP A  66     2048   2503   2168   -380    -59     97       O  
ATOM    528  OD2 ASP A  66      -9.650   8.571   2.145  1.00 15.47           O  
ANISOU  528  OD2 ASP A  66     1355   2216   2306   -312   -116    -84       O  
ATOM    529  N   ASN A  67      -8.867  13.884   1.536  1.00 11.82           N  
ANISOU  529  N   ASN A  67      636   2040   1812    -46    149    -33       N  
ATOM    530  CA  ASN A  67      -8.221  14.971   0.822  1.00 10.11           C  
ANISOU  530  CA  ASN A  67      265   1944   1630    130    -63   -128       C  
ATOM    531  C   ASN A  67      -7.908  16.153   1.761  1.00  9.81           C  
ANISOU  531  C   ASN A  67      367   1962   1399     79    119      8       C  
ATOM    532  O   ASN A  67      -6.821  16.759   1.669  1.00 10.67           O  
ANISOU  532  O   ASN A  67      270   2030   1752   -167     46    -24       O  
ATOM    533  CB  ASN A  67      -9.076  15.452  -0.364  1.00 11.15           C  
ANISOU  533  CB  ASN A  67      315   2146   1775    146     42     56       C  
ATOM    534  CG  ASN A  67      -9.073  14.487  -1.550  1.00 10.43           C  
ANISOU  534  CG  ASN A  67      262   2114   1587     10   -107     35       C  
ATOM    535  OD1 ASN A  67      -8.230  13.588  -1.663  1.00 10.95           O  
ANISOU  535  OD1 ASN A  67      281   2051   1826     77      5    -33       O  
ATOM    536  ND2 ASN A  67      -9.957  14.745  -2.490  1.00 10.47           N  
ANISOU  536  ND2 ASN A  67      254   2111   1610    -29    -36    130       N  
ATOM    537  N   HIS A  68      -8.822  16.488   2.665  1.00 10.51           N  
ANISOU  537  N   HIS A  68      292   2243   1459     52    205   -210       N  
ATOM    538  CA  HIS A  68      -8.493  17.487   3.680  1.00 10.37           C  
ANISOU  538  CA  HIS A  68      329   2061   1550    293    197     27       C  
ATOM    539  C   HIS A  68      -7.212  17.067   4.426  1.00 10.24           C  
ANISOU  539  C   HIS A  68      388   2034   1466     56    200    -53       C  
ATOM    540  O   HIS A  68      -6.299  17.883   4.656  1.00 11.10           O  
ANISOU  540  O   HIS A  68      295   2104   1817   -222     34    -17       O  
ATOM    541  CB  HIS A  68      -9.642  17.664   4.684  1.00 10.30           C  
ANISOU  541  CB  HIS A  68      288   2158   1468   -118    197   -270       C  
ATOM    542  CG  HIS A  68     -10.664  18.664   4.271  1.00 11.41           C  
ANISOU  542  CG  HIS A  68      321   2176   1839    -31    -25   -157       C  
ATOM    543  ND1 HIS A  68     -10.740  19.915   4.839  1.00 11.70           N  
ANISOU  543  ND1 HIS A  68      313   2309   1822     69    297    -96       N  
ATOM    544  CD2 HIS A  68     -11.708  18.573   3.403  1.00 11.24           C  
ANISOU  544  CD2 HIS A  68      711   2034   1526   -485    242   -486       C  
ATOM    545  CE1 HIS A  68     -11.781  20.556   4.331  1.00 10.93           C  
ANISOU  545  CE1 HIS A  68      362   1808   1981    101    399   -250       C  
ATOM    546  NE2 HIS A  68     -12.364  19.770   3.435  1.00 11.07           N  
ANISOU  546  NE2 HIS A  68      396   2002   1808   -202    461   -344       N  
ATOM    547  N   ARG A  69      -7.175  15.816   4.859  1.00 11.11           N  
ANISOU  547  N   ARG A  69      546   2015   1658    -43   -184    128       N  
ATOM    548  CA  ARG A  69      -6.068  15.343   5.675  1.00  9.95           C  
ANISOU  548  CA  ARG A  69      269   2254   1258     48    121     -6       C  
ATOM    549  C   ARG A  69      -4.762  15.436   4.920  1.00 11.72           C  
ANISOU  549  C   ARG A  69      946   1950   1554     65     12   -123       C  
ATOM    550  O   ARG A  69      -3.753  15.970   5.442  1.00 11.26           O  
ANISOU  550  O   ARG A  69      510   2217   1550   -122    -89   -132       O  
ATOM    551  CB  ARG A  69      -6.297  13.903   6.107  1.00 12.54           C  
ANISOU  551  CB  ARG A  69      894   2365   1506    109    252    123       C  
ATOM    552  CG  ARG A  69      -5.388  13.450   7.206  1.00 12.72           C  
ANISOU  552  CG  ARG A  69      761   2249   1822   -237    113     98       C  
ATOM    553  CD  ARG A  69      -5.597  12.002   7.562  1.00 16.21           C  
ANISOU  553  CD  ARG A  69     1321   2663   2174   -146   -346    425       C  
ATOM    554  NE  ARG A  69      -5.228  11.143   6.459  1.00 17.31           N  
ANISOU  554  NE  ARG A  69     2021   2455   2100   -182   -166    -58       N  
ATOM    555  CZ  ARG A  69      -6.091  10.492   5.695  1.00 18.28           C  
ANISOU  555  CZ  ARG A  69     2179   2388   2375     15     66    271       C  
ATOM    556  NH1 ARG A  69      -7.382  10.550   5.958  1.00 20.37           N  
ANISOU  556  NH1 ARG A  69     2184   2700   2856   -640   -306    167       N  
ATOM    557  NH2 ARG A  69      -5.650   9.770   4.660  1.00 18.82           N  
ANISOU  557  NH2 ARG A  69     2118   2557   2473    -11    -95     13       N  
ATOM    558  N   THR A  70      -4.739  14.921   3.696  1.00 10.95           N  
ANISOU  558  N   THR A  70      518   2259   1383      4    -27    -62       N  
ATOM    559  CA  THR A  70      -3.475  14.838   2.984  1.00 11.31           C  
ANISOU  559  CA  THR A  70      489   2207   1599    133     21    -97       C  
ATOM    560  C   THR A  70      -3.094  16.145   2.331  1.00 10.46           C  
ANISOU  560  C   THR A  70      481   1717   1775   -282     33     81       C  
ATOM    561  O   THR A  70      -1.941  16.576   2.439  1.00 10.41           O  
ANISOU  561  O   THR A  70      278   2058   1620   -153    131    -44       O  
ATOM    562  CB  THR A  70      -3.436  13.686   1.957  1.00 12.22           C  
ANISOU  562  CB  THR A  70      562   2364   1714      0     55    -49       C  
ATOM    563  OG1 THR A  70      -4.287  13.984   0.842  1.00 11.87           O  
ANISOU  563  OG1 THR A  70      644   2144   1720     53    -48     39       O  
ATOM    564  CG2 THR A  70      -3.859  12.362   2.617  1.00 12.91           C  
ANISOU  564  CG2 THR A  70     1356   1839   1707    -94    -30    102       C  
ATOM    565  N   GLU A  71      -4.040  16.794   1.666  1.00 11.12           N  
ANISOU  565  N   GLU A  71      417   2108   1699     74    205    114       N  
ATOM    566  CA  GLU A  71      -3.731  17.972   0.863  1.00  9.81           C  
ANISOU  566  CA  GLU A  71      274   1937   1512    102    127   -165       C  
ATOM    567  C   GLU A  71      -3.542  19.214   1.684  1.00  8.83           C  
ANISOU  567  C   GLU A  71      263   1811   1280    114    -35     53       C  
ATOM    568  O   GLU A  71      -2.676  20.056   1.356  1.00 10.11           O  
ANISOU  568  O   GLU A  71      266   1927   1645    -40    132    -75       O  
ATOM    569  CB  GLU A  71      -4.813  18.249  -0.167  1.00 10.53           C  
ANISOU  569  CB  GLU A  71      276   2058   1664   -154    108    149       C  
ATOM    570  CG  GLU A  71      -5.060  17.151  -1.191  1.00 11.10           C  
ANISOU  570  CG  GLU A  71      485   2044   1686    152     29    221       C  
ATOM    571  CD  GLU A  71      -5.941  17.652  -2.336  1.00 10.16           C  
ANISOU  571  CD  GLU A  71      258   1989   1611    -61    -56    -72       C  
ATOM    572  OE1 GLU A  71      -5.474  18.523  -3.098  1.00 12.25           O  
ANISOU  572  OE1 GLU A  71      638   2207   1808   -197   -228     -2       O  
ATOM    573  OE2 GLU A  71      -7.136  17.207  -2.444  1.00 11.31           O  
ANISOU  573  OE2 GLU A  71      258   2345   1693   -107     -2   -147       O  
ATOM    574  N   ILE A  72      -4.377  19.389   2.709  1.00 10.24           N  
ANISOU  574  N   ILE A  72      281   2210   1397   -216     84   -131       N  
ATOM    575  CA  ILE A  72      -4.448  20.675   3.410  1.00 10.16           C  
ANISOU  575  CA  ILE A  72      284   2278   1298     -1    179     67       C  
ATOM    576  C   ILE A  72      -3.726  20.595   4.743  1.00 11.18           C  
ANISOU  576  C   ILE A  72      769   2088   1390     13    223    -92       C  
ATOM    577  O   ILE A  72      -2.718  21.261   4.945  1.00 10.79           O  
ANISOU  577  O   ILE A  72      314   2242   1543   -185    158   -105       O  
ATOM    578  CB  ILE A  72      -5.924  21.192   3.576  1.00 10.13           C  
ANISOU  578  CB  ILE A  72      300   2259   1291    -27    220    -68       C  
ATOM    579  CG1 ILE A  72      -6.613  21.263   2.204  1.00 11.01           C  
ANISOU  579  CG1 ILE A  72      300   2435   1448   -112    235   -358       C  
ATOM    580  CG2 ILE A  72      -5.906  22.546   4.254  1.00 11.92           C  
ANISOU  580  CG2 ILE A  72      293   2383   1851    261     73   -312       C  
ATOM    581  CD1 ILE A  72      -5.931  22.201   1.169  1.00 11.97           C  
ANISOU  581  CD1 ILE A  72      272   2622   1652    197     75    151       C  
ATOM    582  N   ALA A  73      -4.183  19.742   5.626  1.00 10.22           N  
ANISOU  582  N   ALA A  73      269   2150   1461   -150    -65    -82       N  
ATOM    583  CA  ALA A  73      -3.507  19.590   6.907  1.00 10.68           C  
ANISOU  583  CA  ALA A  73      617   1981   1457     24    190   -170       C  
ATOM    584  C   ALA A  73      -2.053  19.099   6.705  1.00 11.93           C  
ANISOU  584  C   ALA A  73      914   1969   1647   -224    111    -37       C  
ATOM    585  O   ALA A  73      -1.134  19.615   7.328  1.00 12.72           O  
ANISOU  585  O   ALA A  73      654   2520   1660   -335     19   -149       O  
ATOM    586  CB  ALA A  73      -4.288  18.630   7.812  1.00 12.75           C  
ANISOU  586  CB  ALA A  73      620   2684   1539   -250    222    253       C  
ATOM    587  N   GLY A  74      -1.858  18.138   5.815  1.00 10.57           N  
ANISOU  587  N   GLY A  74      254   2320   1442    -41    -13     27       N  
ATOM    588  CA  GLY A  74      -0.526  17.582   5.560  1.00 10.56           C  
ANISOU  588  CA  GLY A  74      256   2290   1464     58    -42     63       C  
ATOM    589  C   GLY A  74       0.348  18.484   4.674  1.00 10.52           C  
ANISOU  589  C   GLY A  74      273   1993   1729    -44    165     85       C  
ATOM    590  O   GLY A  74       1.336  19.083   5.139  1.00 12.76           O  
ANISOU  590  O   GLY A  74      283   2716   1846   -185   -151   -136       O  
ATOM    591  N   LYS A  75      -0.001  18.591   3.401  1.00 10.64           N  
ANISOU  591  N   LYS A  75      265   2227   1549   -150    -42     71       N  
ATOM    592  CA  LYS A  75       0.883  19.260   2.446  1.00 10.55           C  
ANISOU  592  CA  LYS A  75      260   2091   1656    113      1    105       C  
ATOM    593  C   LYS A  75       0.826  20.789   2.532  1.00 10.26           C  
ANISOU  593  C   LYS A  75      339   2013   1545    -20    -96     24       C  
ATOM    594  O   LYS A  75       1.828  21.440   2.863  1.00 11.88           O  
ANISOU  594  O   LYS A  75      324   2139   2050     93   -340     86       O  
ATOM    595  CB  LYS A  75       0.593  18.804   1.037  1.00 11.06           C  
ANISOU  595  CB  LYS A  75      266   2323   1611     28    132    113       C  
ATOM    596  CG  LYS A  75       0.869  17.351   0.806  1.00 13.23           C  
ANISOU  596  CG  LYS A  75      628   2517   1878   -126     37   -318       C  
ATOM    597  CD  LYS A  75       2.357  17.077   0.680  1.00 14.77           C  
ANISOU  597  CD  LYS A  75      845   2256   2510    247    163    225       C  
ATOM    598  CE  LYS A  75       2.641  15.637   0.243  1.00 15.32           C  
ANISOU  598  CE  LYS A  75      458   3091   2271    404    369    -69       C  
ATOM    599  NZ  LYS A  75       4.059  15.434  -0.168  1.00 15.28           N  
ANISOU  599  NZ  LYS A  75      617   2739   2449    219    311    190       N  
ATOM    600  N   LEU A  76      -0.334  21.389   2.272  1.00  9.99           N  
ANISOU  600  N   LEU A  76      256   2057   1482     39     55     68       N  
ATOM    601  CA  LEU A  76      -0.361  22.830   2.054  1.00 10.11           C  
ANISOU  601  CA  LEU A  76      289   2311   1238     16   -189    -21       C  
ATOM    602  C   LEU A  76      -0.076  23.596   3.352  1.00 10.43           C  
ANISOU  602  C   LEU A  76      281   2047   1633    186    125    136       C  
ATOM    603  O   LEU A  76       0.618  24.616   3.336  1.00 10.62           O  
ANISOU  603  O   LEU A  76      261   2206   1566    104    -52     44       O  
ATOM    604  CB  LEU A  76      -1.685  23.273   1.445  1.00 11.29           C  
ANISOU  604  CB  LEU A  76      343   2406   1537   -104   -337    154       C  
ATOM    605  CG  LEU A  76      -1.807  24.753   1.089  1.00 10.66           C  
ANISOU  605  CG  LEU A  76      289   2334   1426    118   -184     18       C  
ATOM    606  CD1 LEU A  76      -0.790  25.150   0.024  1.00 12.03           C  
ANISOU  606  CD1 LEU A  76      352   2438   1779   -163    337    293       C  
ATOM    607  CD2 LEU A  76      -3.275  25.048   0.613  1.00 13.06           C  
ANISOU  607  CD2 LEU A  76      499   2509   1952    149   -629     54       C  
ATOM    608  N   PHE A  77      -0.682  23.170   4.464  1.00 10.07           N  
ANISOU  608  N   PHE A  77      258   2172   1394     62     63     37       N  
ATOM    609  CA  PHE A  77      -0.466  23.874   5.726  1.00 10.81           C  
ANISOU  609  CA  PHE A  77      259   2281   1567    103     30     45       C  
ATOM    610  C   PHE A  77       0.688  23.307   6.568  1.00 10.66           C  
ANISOU  610  C   PHE A  77      379   2044   1624    -48    -80    -17       C  
ATOM    611  O   PHE A  77       1.072  23.904   7.548  1.00 12.33           O  
ANISOU  611  O   PHE A  77      393   2412   1878    144   -218   -278       O  
ATOM    612  CB  PHE A  77      -1.718  23.889   6.578  1.00 10.21           C  
ANISOU  612  CB  PHE A  77      364   2081   1431     38     96    -26       C  
ATOM    613  CG  PHE A  77      -2.856  24.763   6.031  1.00 10.87           C  
ANISOU  613  CG  PHE A  77      476   2076   1578     26    -75    -77       C  
ATOM    614  CD1 PHE A  77      -2.703  25.517   4.874  1.00 12.04           C  
ANISOU  614  CD1 PHE A  77      598   2177   1797    446   -157   -128       C  
ATOM    615  CD2 PHE A  77      -4.077  24.824   6.708  1.00 11.14           C  
ANISOU  615  CD2 PHE A  77      297   2357   1578     11    172    -12       C  
ATOM    616  CE1 PHE A  77      -3.758  26.293   4.403  1.00 10.88           C  
ANISOU  616  CE1 PHE A  77      298   2096   1737    -10    260    -79       C  
ATOM    617  CE2 PHE A  77      -5.107  25.600   6.244  1.00 13.22           C  
ANISOU  617  CE2 PHE A  77      547   2325   2149    125   -229   -137       C  
ATOM    618  CZ  PHE A  77      -4.958  26.333   5.091  1.00 11.66           C  
ANISOU  618  CZ  PHE A  77      522   2185   1721    176   -176   -189       C  
ATOM    619  N   GLY A  78       1.199  22.135   6.202  1.00 10.23           N  
ANISOU  619  N   GLY A  78      305   1983   1596   -200   -207     80       N  
ATOM    620  CA  GLY A  78       2.366  21.561   6.890  1.00 10.21           C  
ANISOU  620  CA  GLY A  78      326   2051   1502     61   -131     -3       C  
ATOM    621  C   GLY A  78       2.144  21.340   8.385  1.00 11.12           C  
ANISOU  621  C   GLY A  78      583   2076   1565   -174   -255    -76       C  
ATOM    622  O   GLY A  78       2.979  21.739   9.204  1.00 12.07           O  
ANISOU  622  O   GLY A  78      393   2589   1604     12   -352    -32       O  
ATOM    623  N   MET A  79       1.069  20.636   8.739  1.00 11.46           N  
ANISOU  623  N   MET A  79      679   2041   1631     16   -255    109       N  
ATOM    624  CA  MET A  79       0.646  20.560  10.122  1.00 11.25           C  
ANISOU  624  CA  MET A  79      483   2220   1568     99     -5    186       C  
ATOM    625  C   MET A  79       1.071  19.274  10.835  1.00 11.68           C  
ANISOU  625  C   MET A  79      693   2254   1488    -73   -111     96       C  
ATOM    626  O   MET A  79       0.954  19.172  12.051  1.00 12.39           O  
ANISOU  626  O   MET A  79      577   2588   1539    -33   -246    273       O  
ATOM    627  CB  MET A  79      -0.871  20.758  10.228  1.00 12.08           C  
ANISOU  627  CB  MET A  79      702   2390   1497    114    238    109       C  
ATOM    628  CG  MET A  79      -1.314  22.128   9.750  1.00 11.58           C  
ANISOU  628  CG  MET A  79      284   2627   1489    267     51    205       C  
ATOM    629  SD  MET A  79      -3.040  22.471   9.990  1.00 12.22           S  
ANISOU  629  SD  MET A  79      437   2596   1609      0    101     88       S  
ATOM    630  CE  MET A  79      -3.004  22.873  11.736  1.00 14.19           C  
ANISOU  630  CE  MET A  79      796   2772   1822   -161    -46     61       C  
ATOM    631  N   PHE A  80       1.522  18.293  10.077  1.00 11.73           N  
ANISOU  631  N   PHE A  80      524   2233   1700    127   -247    238       N  
ATOM    632  CA  PHE A  80       2.068  17.062  10.651  1.00 13.61           C  
ANISOU  632  CA  PHE A  80     1150   2324   1696     65    106      2       C  
ATOM    633  C   PHE A  80       3.144  16.486   9.743  1.00 13.23           C  
ANISOU  633  C   PHE A  80      840   2257   1929     38    -64    124       C  
ATOM    634  O   PHE A  80       3.298  16.910   8.616  1.00 13.27           O  
ANISOU  634  O   PHE A  80      516   2708   1816    305     49    157       O  
ATOM    635  CB  PHE A  80       0.946  16.022  10.890  1.00 13.97           C  
ANISOU  635  CB  PHE A  80     1140   2225   1941    357   -168    111       C  
ATOM    636  CG  PHE A  80       0.255  15.548   9.628  1.00 13.40           C  
ANISOU  636  CG  PHE A  80      961   2280   1851     -6   -191    219       C  
ATOM    637  CD1 PHE A  80       0.764  14.489   8.884  1.00 16.63           C  
ANISOU  637  CD1 PHE A  80     1774   2545   1997    131   -544     28       C  
ATOM    638  CD2 PHE A  80      -0.951  16.098   9.239  1.00 12.82           C  
ANISOU  638  CD2 PHE A  80      797   2380   1690    123    -66    -21       C  
ATOM    639  CE1 PHE A  80       0.082  14.012   7.758  1.00 14.90           C  
ANISOU  639  CE1 PHE A  80     1124   2294   2241    230   -385    -77       C  
ATOM    640  CE2 PHE A  80      -1.613  15.638   8.093  1.00 12.66           C  
ANISOU  640  CE2 PHE A  80      413   2428   1969    155    429    246       C  
ATOM    641  CZ  PHE A  80      -1.097  14.597   7.368  1.00 14.00           C  
ANISOU  641  CZ  PHE A  80     1435   2078   1804     77   -357    197       C  
ATOM    642  N   TYR A  81       3.894  15.523  10.265  1.00 14.82           N  
ANISOU  642  N   TYR A  81     1068   2525   2038    633   -196    131       N  
ATOM    643  CA  TYR A  81       4.928  14.843   9.491  1.00 16.19           C  
ANISOU  643  CA  TYR A  81     1092   2616   2442    242     77    319       C  
ATOM    644  C   TYR A  81       5.078  13.440  10.023  1.00 18.49           C  
ANISOU  644  C   TYR A  81     1665   2637   2724    312    135    151       C  
ATOM    645  O   TYR A  81       4.548  13.113  11.084  1.00 19.83           O  
ANISOU  645  O   TYR A  81     1796   2686   3051    506   -258    353       O  
ATOM    646  CB  TYR A  81       6.265  15.600   9.557  1.00 16.43           C  
ANISOU  646  CB  TYR A  81     1207   2659   2376    512   -132    210       C  
ATOM    647  CG  TYR A  81       6.938  15.548  10.911  1.00 18.83           C  
ANISOU  647  CG  TYR A  81     1066   3352   2732    283    110    450       C  
ATOM    648  CD1 TYR A  81       6.595  16.438  11.912  1.00 19.56           C  
ANISOU  648  CD1 TYR A  81     1921   2972   2538    195   -752    131       C  
ATOM    649  CD2 TYR A  81       7.924  14.612  11.178  1.00 20.59           C  
ANISOU  649  CD2 TYR A  81     1609   3389   2823    323   -429    -38       C  
ATOM    650  CE1 TYR A  81       7.206  16.397  13.142  1.00 21.69           C  
ANISOU  650  CE1 TYR A  81     1847   3094   3297    496   -480   -187       C  
ATOM    651  CE2 TYR A  81       8.534  14.555  12.404  1.00 21.05           C  
ANISOU  651  CE2 TYR A  81     1067   3622   3307    734   -498    143       C  
ATOM    652  CZ  TYR A  81       8.179  15.451  13.382  1.00 19.99           C  
ANISOU  652  CZ  TYR A  81     1569   3270   2755    438   -416     92       C  
ATOM    653  OH  TYR A  81       8.800  15.398  14.614  1.00 24.17           O  
ANISOU  653  OH  TYR A  81     1820   3814   3548    106  -1186    724       O  
ATOM    654  N   GLU A  82       5.768  12.602   9.269  1.00 21.35           N  
ANISOU  654  N   GLU A  82     1937   2815   3359    542    307    185       N  
ATOM    655  CA  GLU A  82       5.999  11.219   9.672  1.00 24.07           C  
ANISOU  655  CA  GLU A  82     2321   3071   3751    457    295    117       C  
ATOM    656  C   GLU A  82       7.464  10.975   9.949  1.00 27.56           C  
ANISOU  656  C   GLU A  82     2539   3583   4347    662    374    443       C  
ATOM    657  O   GLU A  82       8.329  11.487   9.237  1.00 28.91           O  
ANISOU  657  O   GLU A  82     2117   3723   5142    785    500    464       O  
ATOM    658  CB  GLU A  82       5.526  10.264   8.583  1.00 26.36           C  
ANISOU  658  CB  GLU A  82     2664   3364   3986    267    512    191       C  
ATOM    659  CG  GLU A  82       6.042   8.838   8.757  1.00 29.52           C  
ANISOU  659  CG  GLU A  82     3480   3439   4296    360    232     80       C  
ATOM    660  CD  GLU A  82       5.482   7.887   7.730  1.00 35.58           C  
ANISOU  660  CD  GLU A  82     4801   4075   4642    197   -168   -303       C  
ATOM    661  OE1 GLU A  82       4.523   8.268   7.022  1.00 39.09           O  
ANISOU  661  OE1 GLU A  82     5263   4518   5068    668   -192    417       O  
ATOM    662  OE2 GLU A  82       5.994   6.749   7.633  1.00 43.70           O  
ANISOU  662  OE2 GLU A  82     5702   4739   6162    443   -402    -12       O  
ATOM    663  N   ASP A  83       7.740  10.198  10.987  1.00 27.67           N  
ANISOU  663  N   ASP A  83     2168   3631   4713    865    267    426       N  
ATOM    664  CA  ASP A  83       9.094   9.698  11.229  1.00 29.67           C  
ANISOU  664  CA  ASP A  83     2773   3728   4770    905     63    477       C  
ATOM    665  C   ASP A  83       9.043   8.305  11.835  1.00 34.34           C  
ANISOU  665  C   ASP A  83     3891   4044   5111    774    183    372       C  
ATOM    666  O   ASP A  83       8.313   8.061  12.803  1.00 34.17           O  
ANISOU  666  O   ASP A  83     3695   4078   5208   1179   -144    735       O  
ATOM    667  CB  ASP A  83       9.856  10.630  12.157  1.00 32.80           C  
ANISOU  667  CB  ASP A  83     3299   4159   5003    787     -9    361       C  
ATOM    668  CG  ASP A  83      11.311  10.228  12.311  1.00 39.40           C  
ANISOU  668  CG  ASP A  83     3871   5526   5574    691     -6    306       C  
ATOM    669  OD1 ASP A  83      12.061  10.306  11.307  1.00 41.29           O  
ANISOU  669  OD1 ASP A  83     3535   5977   6174   1221   -177    323       O  
ATOM    670  OD2 ASP A  83      11.701   9.824  13.428  1.00 49.68           O  
ANISOU  670  OD2 ASP A  83     5601   6840   6435    385    -90    642       O  
ATOM    671  N   ASP A  84       9.823   7.392  11.264  1.00 36.72           N  
ANISOU  671  N   ASP A  84     4166   4381   5404    826    200    318       N  
ATOM    672  CA  ASP A  84       9.820   5.998  11.706  1.00 38.23           C  
ANISOU  672  CA  ASP A  84     4661   4473   5388    395    286    252       C  
ATOM    673  C   ASP A  84       8.399   5.491  11.949  1.00 38.39           C  
ANISOU  673  C   ASP A  84     4843   4448   5295    154     77    258       C  
ATOM    674  O   ASP A  84       8.114   4.898  12.985  1.00 39.93           O  
ANISOU  674  O   ASP A  84     5175   4572   5425    409     64    374       O  
ATOM    675  N   GLU A  85       7.506   5.761  11.004  1.00 37.08           N  
ANISOU  675  N   GLU A  85     4615   4399   5074    219    -21    214       N  
ATOM    676  CA  GLU A  85       6.197   5.117  10.980  1.00 36.62           C  
ANISOU  676  CA  GLU A  85     4611   4312   4991    113    158     74       C  
ATOM    677  C   GLU A  85       5.238   5.669  12.042  1.00 34.10           C  
ANISOU  677  C   GLU A  85     4191   3882   4881     94    222     85       C  
ATOM    678  O   GLU A  85       4.207   5.055  12.341  1.00 37.09           O  
ANISOU  678  O   GLU A  85     4458   4143   5492     96    412   -126       O  
ATOM    679  N   VAL A  86       5.579   6.819  12.612  1.00 31.72           N  
ANISOU  679  N   VAL A  86     3926   3567   4558    190    120    257       N  
ATOM    680  CA  VAL A  86       4.688   7.499  13.540  1.00 27.84           C  
ANISOU  680  CA  VAL A  86     3493   3085   3998    299      4    339       C  
ATOM    681  C   VAL A  86       4.411   8.931  13.047  1.00 26.81           C  
ANISOU  681  C   VAL A  86     3015   3042   4128    440    -85    450       C  
ATOM    682  O   VAL A  86       5.296   9.592  12.511  1.00 25.16           O  
ANISOU  682  O   VAL A  86     2174   3010   4372    521   -253    588       O  
ATOM    683  CB  VAL A  86       5.292   7.546  14.962  1.00 29.54           C  
ANISOU  683  CB  VAL A  86     3542   3287   4394    566    -73    533       C  
ATOM    684  CG1 VAL A  86       4.348   8.241  15.922  1.00 32.19           C  
ANISOU  684  CG1 VAL A  86     4535   3645   4048    485   -109    354       C  
ATOM    685  CG2 VAL A  86       5.613   6.116  15.455  1.00 31.13           C  
ANISOU  685  CG2 VAL A  86     3891   3365   4572    221     54    636       C  
ATOM    686  N   ILE A  87       3.166   9.379  13.191  1.00 25.13           N  
ANISOU  686  N   ILE A  87     2774   2994   3780    267      1    387       N  
ATOM    687  CA  ILE A  87       2.775  10.727  12.770  1.00 21.23           C  
ANISOU  687  CA  ILE A  87     2422   2829   2816     98   -293    319       C  
ATOM    688  C   ILE A  87       2.840  11.683  13.939  1.00 20.83           C  
ANISOU  688  C   ILE A  87     2292   2658   2963    159   -410    461       C  
ATOM    689  O   ILE A  87       2.317  11.391  15.017  1.00 21.16           O  
ANISOU  689  O   ILE A  87     2077   2866   3096     88   -180    481       O  
ATOM    690  CB  ILE A  87       1.341  10.744  12.188  1.00 21.11           C  
ANISOU  690  CB  ILE A  87     2450   3007   2562    -27    -27    222       C  
ATOM    691  CG1 ILE A  87       1.208   9.695  11.078  1.00 22.17           C  
ANISOU  691  CG1 ILE A  87     2454   2812   3158   -196    -34    -64       C  
ATOM    692  CG2 ILE A  87       0.997  12.131  11.669  1.00 17.95           C  
ANISOU  692  CG2 ILE A  87     1523   2751   2546    119   -367     26       C  
ATOM    693  CD1 ILE A  87       2.282   9.794   9.999  1.00 26.23           C  
ANISOU  693  CD1 ILE A  87     2762   3877   3325   -307    557   -341       C  
ATOM    694  N   PHE A  88       3.531  12.810  13.732  1.00 20.02           N  
ANISOU  694  N   PHE A  88     2124   2700   2781    144   -390    413       N  
ATOM    695  CA  PHE A  88       3.749  13.815  14.774  1.00 18.76           C  
ANISOU  695  CA  PHE A  88     1794   2724   2608   -145   -354    323       C  
ATOM    696  C   PHE A  88       3.143  15.150  14.366  1.00 18.04           C  
ANISOU  696  C   PHE A  88     1870   2634   2348   -137   -391     67       C  
ATOM    697  O   PHE A  88       3.112  15.476  13.184  1.00 16.70           O  
ANISOU  697  O   PHE A  88     1295   2975   2075     54   -286    219       O  
ATOM    698  CB  PHE A  88       5.254  14.030  14.982  1.00 21.22           C  
ANISOU  698  CB  PHE A  88     1943   2996   3122    157   -706    289       C  
ATOM    699  CG  PHE A  88       5.980  12.822  15.526  1.00 23.98           C  
ANISOU  699  CG  PHE A  88     1896   3524   3691    147   -641    411       C  
ATOM    700  CD1 PHE A  88       6.063  12.606  16.890  1.00 29.29           C  
ANISOU  700  CD1 PHE A  88     3926   3232   3968    281   -762    391       C  
ATOM    701  CD2 PHE A  88       6.568  11.920  14.678  1.00 28.67           C  
ANISOU  701  CD2 PHE A  88     3034   3544   4313    636   -457    507       C  
ATOM    702  CE1 PHE A  88       6.724  11.491  17.394  1.00 28.86           C  
ANISOU  702  CE1 PHE A  88     3017   3514   4432    811  -1033    262       C  
ATOM    703  CE2 PHE A  88       7.248  10.806  15.177  1.00 32.04           C  
ANISOU  703  CE2 PHE A  88     3924   3684   4564    329   -550    491       C  
ATOM    704  CZ  PHE A  88       7.319  10.599  16.529  1.00 33.16           C  
ANISOU  704  CZ  PHE A  88     4091   3989   4517    533   -753    459       C  
ATOM    705  N   PRO A  89       2.758  15.972  15.352  1.00 17.12           N  
ANISOU  705  N   PRO A  89     1757   2821   1925   -198   -452    326       N  
ATOM    706  CA  PRO A  89       2.443  17.370  15.050  1.00 17.22           C  
ANISOU  706  CA  PRO A  89     1971   2678   1891    -62   -364    266       C  
ATOM    707  C   PRO A  89       3.680  18.115  14.598  1.00 16.06           C  
ANISOU  707  C   PRO A  89     1597   2542   1961    173   -234    180       C  
ATOM    708  O   PRO A  89       4.751  17.874  15.120  1.00 17.47           O  
ANISOU  708  O   PRO A  89     1307   3076   2252     76   -517    368       O  
ATOM    709  CB  PRO A  89       1.951  17.927  16.391  1.00 18.91           C  
ANISOU  709  CB  PRO A  89     2112   2885   2188     -1   -245     -7       C  
ATOM    710  CG  PRO A  89       1.740  16.727  17.274  1.00 22.52           C  
ANISOU  710  CG  PRO A  89     2687   3402   2465   -138     43     21       C  
ATOM    711  CD  PRO A  89       2.658  15.681  16.790  1.00 19.82           C  
ANISOU  711  CD  PRO A  89     2297   3023   2208   -241   -275    185       C  
ATOM    712  N   SER A  90       3.546  19.003  13.629  1.00 14.25           N  
ANISOU  712  N   SER A  90     1070   2548   1795   -132   -468    177       N  
ATOM    713  CA  SER A  90       4.711  19.768  13.150  1.00 15.10           C  
ANISOU  713  CA  SER A  90     1302   2420   2012    -36   -365     89       C  
ATOM    714  C   SER A  90       5.035  20.930  14.066  1.00 15.37           C  
ANISOU  714  C   SER A  90     1543   2556   1738     97   -446    200       C  
ATOM    715  O   SER A  90       4.233  21.308  14.921  1.00 14.96           O  
ANISOU  715  O   SER A  90     1139   2779   1765   -165   -400     18       O  
ATOM    716  CB  SER A  90       4.457  20.309  11.763  1.00 13.80           C  
ANISOU  716  CB  SER A  90     1169   2315   1757    183   -246    195       C  
ATOM    717  OG  SER A  90       3.437  21.290  11.808  1.00 13.04           O  
ANISOU  717  OG  SER A  90      828   2314   1810     96   -349     29       O  
ATOM    718  N   GLY A  91       6.203  21.524  13.853  1.00 15.42           N  
ANISOU  718  N   GLY A  91     1224   2629   2002    249   -209    138       N  
ATOM    719  CA  GLY A  91       6.576  22.765  14.540  1.00 13.59           C  
ANISOU  719  CA  GLY A  91      617   2589   1955     35   -181    106       C  
ATOM    720  C   GLY A  91       5.537  23.872  14.330  1.00 12.79           C  
ANISOU  720  C   GLY A  91      298   2708   1851    -43   -202     23       C  
ATOM    721  O   GLY A  91       5.250  24.645  15.245  1.00 14.09           O  
ANISOU  721  O   GLY A  91      936   2766   1652     13   -377     31       O  
ATOM    722  N   ARG A  92       5.017  23.989  13.114  1.00 13.02           N  
ANISOU  722  N   ARG A  92      882   2705   1359    101   -164     -6       N  
ATOM    723  CA  ARG A  92       4.063  25.044  12.828  1.00 11.98           C  
ANISOU  723  CA  ARG A  92      339   2253   1959    -23      9     45       C  
ATOM    724  C   ARG A  92       2.784  24.843  13.623  1.00 11.32           C  
ANISOU  724  C   ARG A  92      322   2349   1631   -115   -296     37       C  
ATOM    725  O   ARG A  92       2.233  25.801  14.202  1.00 13.01           O  
ANISOU  725  O   ARG A  92      797   2560   1584   -124   -193   -160       O  
ATOM    726  CB  ARG A  92       3.745  25.102  11.335  1.00 11.20           C  
ANISOU  726  CB  ARG A  92      548   2317   1391    256   -137    -76       C  
ATOM    727  CG  ARG A  92       2.906  26.300  10.959  1.00 12.50           C  
ANISOU  727  CG  ARG A  92      347   2460   1940    114    235    221       C  
ATOM    728  CD  ARG A  92       2.650  26.400   9.469  1.00 12.04           C  
ANISOU  728  CD  ARG A  92      522   2560   1493    341   -121    163       C  
ATOM    729  NE  ARG A  92       3.870  26.762   8.744  1.00 13.01           N  
ANISOU  729  NE  ARG A  92      640   2606   1697    161      2      5       N  
ATOM    730  CZ  ARG A  92       4.357  26.098   7.695  1.00 13.26           C  
ANISOU  730  CZ  ARG A  92      336   2544   2157    260     76    -71       C  
ATOM    731  NH1 ARG A  92       3.746  25.011   7.246  1.00 16.45           N  
ANISOU  731  NH1 ARG A  92     1408   2486   2355   -169    805   -178       N  
ATOM    732  NH2 ARG A  92       5.457  26.517   7.101  1.00 18.24           N  
ANISOU  732  NH2 ARG A  92      942   2921   3066   -216    792   -109       N  
ATOM    733  N   THR A  93       2.342  23.598  13.711  1.00 11.72           N  
ANISOU  733  N   THR A  93      531   2363   1560     90    -69    -33       N  
ATOM    734  CA  THR A  93       1.171  23.276  14.522  1.00 11.65           C  
ANISOU  734  CA  THR A  93      520   2448   1459    -69     81    141       C  
ATOM    735  C   THR A  93       1.446  23.556  15.994  1.00 13.65           C  
ANISOU  735  C   THR A  93     1072   2363   1751    173      9     96       C  
ATOM    736  O   THR A  93       0.621  24.178  16.677  1.00 13.34           O  
ANISOU  736  O   THR A  93      853   2752   1463   -103     17    -54       O  
ATOM    737  CB  THR A  93       0.761  21.819  14.340  1.00 12.97           C  
ANISOU  737  CB  THR A  93      360   2709   1857    -98   -122    187       C  
ATOM    738  OG1 THR A  93       0.290  21.639  13.017  1.00 12.78           O  
ANISOU  738  OG1 THR A  93      635   2678   1541      5   -214    159       O  
ATOM    739  CG2 THR A  93      -0.369  21.409  15.339  1.00 14.37           C  
ANISOU  739  CG2 THR A  93      751   2756   1952   -292    149   -127       C  
ATOM    740  N   ASN A  94       2.608  23.098  16.480  1.00 14.38           N  
ANISOU  740  N   ASN A  94     1504   2581   1379     48    -40     94       N  
ATOM    741  CA  ASN A  94       2.976  23.282  17.877  1.00 14.14           C  
ANISOU  741  CA  ASN A  94      931   2717   1723   -309    -70    142       C  
ATOM    742  C   ASN A  94       2.948  24.779  18.266  1.00 13.68           C  
ANISOU  742  C   ASN A  94     1021   2734   1442   -351   -238    -81       C  
ATOM    743  O   ASN A  94       2.490  25.138  19.345  1.00 16.31           O  
ANISOU  743  O   ASN A  94     1441   3281   1473   -132   -158    -55       O  
ATOM    744  CB  ASN A  94       4.365  22.689  18.154  1.00 16.18           C  
ANISOU  744  CB  ASN A  94     1330   2903   1914   -242   -518     55       C  
ATOM    745  CG  ASN A  94       4.374  21.147  18.135  1.00 17.33           C  
ANISOU  745  CG  ASN A  94      930   3362   2290    282    134     77       C  
ATOM    746  OD1 ASN A  94       3.332  20.507  18.320  1.00 21.20           O  
ANISOU  746  OD1 ASN A  94     1564   3629   2859   -263   -258    313       O  
ATOM    747  ND2 ASN A  94       5.554  20.559  17.927  1.00 22.43           N  
ANISOU  747  ND2 ASN A  94     2740   3646   2136    945   -640   -169       N  
ATOM    748  N   LYS A  95       3.456  25.634  17.393  1.00 13.87           N  
ANISOU  748  N   LYS A  95     1024   2621   1623    -45   -185    192       N  
ATOM    749  CA  LYS A  95       3.497  27.060  17.681  1.00 14.05           C  
ANISOU  749  CA  LYS A  95     1267   2675   1396    -38   -246    146       C  
ATOM    750  C   LYS A  95       2.080  27.648  17.763  1.00 13.78           C  
ANISOU  750  C   LYS A  95     1353   2445   1437   -300   -423   -118       C  
ATOM    751  O   LYS A  95       1.765  28.410  18.663  1.00 14.27           O  
ANISOU  751  O   LYS A  95     1167   2651   1603   -509   -139   -281       O  
ATOM    752  CB  LYS A  95       4.328  27.797  16.628  1.00 14.30           C  
ANISOU  752  CB  LYS A  95      678   2910   1845   -316   -550    170       C  
ATOM    753  CG  LYS A  95       4.356  29.301  16.791  1.00 15.04           C  
ANISOU  753  CG  LYS A  95      738   3016   1960   -200   -354   -111       C  
ATOM    754  CD  LYS A  95       5.446  29.930  15.891  1.00 16.40           C  
ANISOU  754  CD  LYS A  95      630   3305   2293   -493    251    103       C  
ATOM    755  CE  LYS A  95       5.422  31.451  15.981  1.00 21.80           C  
ANISOU  755  CE  LYS A  95     1897   3574   2811   -382   -489    272       C  
ATOM    756  NZ  LYS A  95       4.122  32.037  15.544  1.00 21.94           N  
ANISOU  756  NZ  LYS A  95     1704   3817   2815   -878   -573    381       N  
ATOM    757  N   TYR A  96       1.234  27.279  16.814  1.00 12.22           N  
ANISOU  757  N   TYR A  96      486   2590   1565   -174    -86   -140       N  
ATOM    758  CA  TYR A  96      -0.138  27.777  16.763  1.00 12.10           C  
ANISOU  758  CA  TYR A  96      780   2395   1423   -158     14     65       C  
ATOM    759  C   TYR A  96      -0.940  27.310  17.980  1.00 12.90           C  
ANISOU  759  C   TYR A  96      929   2354   1617   -245   -250   -143       C  
ATOM    760  O   TYR A  96      -1.744  28.066  18.532  1.00 14.36           O  
ANISOU  760  O   TYR A  96     1103   2801   1552   -399     85   -253       O  
ATOM    761  CB  TYR A  96      -0.778  27.321  15.449  1.00 12.20           C  
ANISOU  761  CB  TYR A  96      750   2561   1323    -39     25    -62       C  
ATOM    762  CG  TYR A  96      -2.242  27.656  15.300  1.00 11.99           C  
ANISOU  762  CG  TYR A  96      326   2598   1630   -138    201    -54       C  
ATOM    763  CD1 TYR A  96      -2.677  28.978  15.167  1.00 13.02           C  
ANISOU  763  CD1 TYR A  96      831   2736   1379   -481   -119     72       C  
ATOM    764  CD2 TYR A  96      -3.198  26.650  15.264  1.00 14.09           C  
ANISOU  764  CD2 TYR A  96     1242   2451   1658   -386   -175     -3       C  
ATOM    765  CE1 TYR A  96      -4.035  29.266  15.011  1.00 14.55           C  
ANISOU  765  CE1 TYR A  96     1125   2546   1856   -262   -273    -44       C  
ATOM    766  CE2 TYR A  96      -4.554  26.934  15.113  1.00 14.45           C  
ANISOU  766  CE2 TYR A  96      633   2939   1916   -250   -263    172       C  
ATOM    767  CZ  TYR A  96      -4.962  28.227  14.998  1.00 13.21           C  
ANISOU  767  CZ  TYR A  96      496   3031   1489   -355   -235    278       C  
ATOM    768  OH  TYR A  96      -6.311  28.471  14.846  1.00 17.11           O  
ANISOU  768  OH  TYR A  96      318   4074   2106    -30   -113    340       O  
ATOM    769  N   ILE A  97      -0.688  26.080  18.411  1.00 13.46           N  
ANISOU  769  N   ILE A  97     1217   2629   1264   -355    186     52       N  
ATOM    770  CA  ILE A  97      -1.316  25.533  19.616  1.00 13.51           C  
ANISOU  770  CA  ILE A  97      947   2719   1464   -248    -35     49       C  
ATOM    771  C   ILE A  97      -0.933  26.398  20.856  1.00 14.13           C  
ANISOU  771  C   ILE A  97     1289   2529   1548   -529    169    -10       C  
ATOM    772  O   ILE A  97      -1.749  26.593  21.756  1.00 14.25           O  
ANISOU  772  O   ILE A  97      806   3072   1535   -549    169   -183       O  
ATOM    773  CB  ILE A  97      -0.885  24.039  19.832  1.00 14.56           C  
ANISOU  773  CB  ILE A  97     1190   2774   1567   -694    -46    105       C  
ATOM    774  CG1 ILE A  97      -1.597  23.106  18.826  1.00 15.49           C  
ANISOU  774  CG1 ILE A  97     1150   3024   1711    -81    275     81       C  
ATOM    775  CG2 ILE A  97      -1.124  23.593  21.284  1.00 18.87           C  
ANISOU  775  CG2 ILE A  97     2463   3000   1704    -71    137    474       C  
ATOM    776  CD1 ILE A  97      -3.027  22.909  19.085  1.00 18.73           C  
ANISOU  776  CD1 ILE A  97     1375   3466   2275   -100    403     90       C  
ATOM    777  N   GLU A  98       0.285  26.944  20.867  1.00 13.09           N  
ANISOU  777  N   GLU A  98      942   2573   1457   -486     -5   -184       N  
ATOM    778  CA  GLU A  98       0.716  27.816  21.971  1.00 13.09           C  
ANISOU  778  CA  GLU A  98     1130   2514   1328   -196    248    -38       C  
ATOM    779  C   GLU A  98       0.227  29.264  21.831  1.00 14.34           C  
ANISOU  779  C   GLU A  98     1071   2944   1432   -354   -166    -27       C  
ATOM    780  O   GLU A  98      -0.053  29.920  22.833  1.00 14.03           O  
ANISOU  780  O   GLU A  98      982   2862   1486   -243    -58   -155       O  
ATOM    781  CB  GLU A  98       2.264  27.821  22.124  1.00 15.76           C  
ANISOU  781  CB  GLU A  98     1435   2861   1690   -366     30   -101       C  
ATOM    782  CG  GLU A  98       2.880  26.501  22.590  1.00 14.69           C  
ANISOU  782  CG  GLU A  98      585   2995   2000   -321    112   -450       C  
ATOM    783  CD  GLU A  98       2.804  26.255  24.122  1.00 18.40           C  
ANISOU  783  CD  GLU A  98     1797   3416   1775    278     67   -504       C  
ATOM    784  OE1 GLU A  98       1.927  26.824  24.819  1.00 14.94           O  
ANISOU  784  OE1 GLU A  98     1046   2932   1699     70     65   -263       O  
ATOM    785  OE2 GLU A  98       3.627  25.466  24.617  1.00 20.25           O  
ANISOU  785  OE2 GLU A  98     1629   3674   2389    672    124     96       O  
ATOM    786  N   ASP A  99       0.213  29.803  20.611  1.00 16.86           N  
ANISOU  786  N   ASP A  99     2117   2823   1464   -167   -332    -71       N  
ATOM    787  CA  ASP A  99      -0.020  31.249  20.466  1.00 18.17           C  
ANISOU  787  CA  ASP A  99     2445   2796   1659   -145   -289     -5       C  
ATOM    788  C   ASP A  99      -1.324  31.684  19.820  1.00 16.20           C  
ANISOU  788  C   ASP A  99     1966   2631   1558   -138    -24     22       C  
ATOM    789  O   ASP A  99      -1.667  32.860  19.894  1.00 17.52           O  
ANISOU  789  O   ASP A  99     2020   2814   1821   -111     91   -249       O  
ATOM    790  CB  ASP A  99       1.180  31.965  19.823  1.00 18.85           C  
ANISOU  790  CB  ASP A  99     2450   2552   2160   -474   -322     37       C  
ATOM    791  CG  ASP A  99       1.377  31.633  18.353  1.00 18.55           C  
ANISOU  791  CG  ASP A  99     2018   2718   2308   -678   -455    305       C  
ATOM    792  OD1 ASP A  99       0.469  31.095  17.689  1.00 14.99           O  
ANISOU  792  OD1 ASP A  99      511   3148   2035   -201     18    -61       O  
ATOM    793  OD2 ASP A  99       2.443  31.987  17.836  1.00 20.59           O  
ANISOU  793  OD2 ASP A  99     1822   3358   2642   -565      4   -142       O  
ATOM    794  N   SER A 100      -2.065  30.740  19.222  1.00 15.41           N  
ANISOU  794  N   SER A 100     1689   2409   1754    -98    -30     57       N  
ATOM    795  CA  SER A 100      -3.362  31.041  18.571  1.00 15.10           C  
ANISOU  795  CA  SER A 100     1249   2721   1768   -141    531     93       C  
ATOM    796  C   SER A 100      -3.263  32.183  17.529  1.00 15.14           C  
ANISOU  796  C   SER A 100     1166   2795   1791    131    284      0       C  
ATOM    797  O   SER A 100      -4.248  32.875  17.262  1.00 17.76           O  
ANISOU  797  O   SER A 100     1060   3204   2482    246    563    279       O  
ATOM    798  CB  SER A 100      -4.415  31.392  19.607  1.00 18.63           C  
ANISOU  798  CB  SER A 100     1538   3172   2365    -53    100    150       C  
ATOM    799  OG  SER A 100      -5.706  31.160  19.093  1.00 23.48           O  
ANISOU  799  OG  SER A 100     1792   3705   3424    186    460    140       O  
ATOM    800  N   ASP A 101      -2.096  32.339  16.923  1.00 13.87           N  
ANISOU  800  N   ASP A 101      903   2637   1727   -189    277      0       N  
ATOM    801  CA  ASP A 101      -1.842  33.487  16.062  1.00 12.72           C  
ANISOU  801  CA  ASP A 101      633   2619   1579   -196    240   -139       C  
ATOM    802  C   ASP A 101      -1.979  33.065  14.612  1.00 12.16           C  
ANISOU  802  C   ASP A 101      768   2430   1422    -37    147    -47       C  
ATOM    803  O   ASP A 101      -1.057  32.532  14.016  1.00 12.49           O  
ANISOU  803  O   ASP A 101      469   2728   1545    -98    176    -64       O  
ATOM    804  CB  ASP A 101      -0.440  34.031  16.344  1.00 13.13           C  
ANISOU  804  CB  ASP A 101      740   2599   1649   -319    257   -118       C  
ATOM    805  CG  ASP A 101      -0.170  35.367  15.674  1.00 14.85           C  
ANISOU  805  CG  ASP A 101     1438   2600   1604   -422   -181   -370       C  
ATOM    806  OD1 ASP A 101      -0.773  35.650  14.627  1.00 15.34           O  
ANISOU  806  OD1 ASP A 101     1219   3048   1561    -99    170    -26       O  
ATOM    807  OD2 ASP A 101       0.739  36.105  16.165  1.00 20.10           O  
ANISOU  807  OD2 ASP A 101     1947   3279   2412   -628   -430    -85       O  
ATOM    808  N   GLN A 102      -3.164  33.272  14.062  1.00 12.33           N  
ANISOU  808  N   GLN A 102      675   2580   1428    -67    -39    -24       N  
ATOM    809  CA  GLN A 102      -3.468  32.823  12.724  1.00 11.34           C  
ANISOU  809  CA  GLN A 102      283   2536   1489   -122     13    -21       C  
ATOM    810  C   GLN A 102      -2.644  33.585  11.664  1.00 10.98           C  
ANISOU  810  C   GLN A 102      528   2257   1386     36   -124   -205       C  
ATOM    811  O   GLN A 102      -2.093  32.975  10.766  1.00 10.83           O  
ANISOU  811  O   GLN A 102      259   2390   1463    -99     47   -206       O  
ATOM    812  CB  GLN A 102      -4.974  32.910  12.450  1.00 13.71           C  
ANISOU  812  CB  GLN A 102      616   2712   1879    -42    157   -205       C  
ATOM    813  CG  GLN A 102      -5.374  32.415  11.096  1.00 13.71           C  
ANISOU  813  CG  GLN A 102      429   2767   2013   -199     89   -225       C  
ATOM    814  CD  GLN A 102      -6.833  32.576  10.854  1.00 15.62           C  
ANISOU  814  CD  GLN A 102      720   3160   2054   -190    342    130       C  
ATOM    815  OE1 GLN A 102      -7.653  31.968  11.536  1.00 19.76           O  
ANISOU  815  OE1 GLN A 102     1033   3765   2708   -587    179     -7       O  
ATOM    816  NE2 GLN A 102      -7.182  33.451   9.917  1.00 16.42           N  
ANISOU  816  NE2 GLN A 102      526   3457   2255   -187    160    148       N  
ATOM    817  N   PRO A 103      -2.551  34.920  11.780  1.00 11.79           N  
ANISOU  817  N   PRO A 103      715   2352   1410    -30    236   -138       N  
ATOM    818  CA  PRO A 103      -1.698  35.606  10.823  1.00 12.01           C  
ANISOU  818  CA  PRO A 103      707   2344   1510     36    246    -81       C  
ATOM    819  C   PRO A 103      -0.248  35.106  10.844  1.00 10.50           C  
ANISOU  819  C   PRO A 103      423   2198   1368   -236    179    -49       C  
ATOM    820  O   PRO A 103       0.368  34.994   9.805  1.00 12.07           O  
ANISOU  820  O   PRO A 103      537   2540   1506     53      0     16       O  
ATOM    821  CB  PRO A 103      -1.782  37.076  11.263  1.00 12.30           C  
ANISOU  821  CB  PRO A 103      264   2624   1784    134     76     82       C  
ATOM    822  CG  PRO A 103      -3.093  37.179  11.935  1.00 14.07           C  
ANISOU  822  CG  PRO A 103      875   2491   1979    -13    349   -303       C  
ATOM    823  CD  PRO A 103      -3.254  35.861  12.656  1.00 12.29           C  
ANISOU  823  CD  PRO A 103      453   2504   1712     51    243   -180       C  
ATOM    824  N   ALA A 104       0.275  34.774  12.022  1.00 11.77           N  
ANISOU  824  N   ALA A 104      656   2274   1542     26    174    -64       N  
ATOM    825  CA  ALA A 104       1.654  34.273  12.112  1.00 11.01           C  
ANISOU  825  CA  ALA A 104      489   2336   1359   -162    233     96       C  
ATOM    826  C   ALA A 104       1.796  32.898  11.489  1.00 11.69           C  
ANISOU  826  C   ALA A 104      725   2369   1346    -32    336   -290       C  
ATOM    827  O   ALA A 104       2.807  32.599  10.905  1.00 11.61           O  
ANISOU  827  O   ALA A 104      281   2606   1524    148    148   -102       O  
ATOM    828  CB  ALA A 104       2.126  34.245  13.549  1.00 12.29           C  
ANISOU  828  CB  ALA A 104      497   2627   1543   -218   -291   -121       C  
ATOM    829  N   PHE A 105       0.773  32.075  11.592  1.00 11.14           N  
ANISOU  829  N   PHE A 105      267   2387   1577   -114   -101    -73       N  
ATOM    830  CA  PHE A 105       0.745  30.779  10.953  1.00 10.33           C  
ANISOU  830  CA  PHE A 105      264   2210   1449    -65   -102    -39       C  
ATOM    831  C   PHE A 105       0.918  30.957   9.446  1.00 10.86           C  
ANISOU  831  C   PHE A 105      689   1970   1465     72     10   -161       C  
ATOM    832  O   PHE A 105       1.725  30.279   8.813  1.00 10.57           O  
ANISOU  832  O   PHE A 105      266   2325   1422   -121    -77   -126       O  
ATOM    833  CB  PHE A 105      -0.596  30.093  11.285  1.00 10.14           C  
ANISOU  833  CB  PHE A 105      255   2157   1438    -61    -16    -27       C  
ATOM    834  CG  PHE A 105      -0.750  28.700  10.734  1.00  9.91           C  
ANISOU  834  CG  PHE A 105      276   2245   1242    -53    146     55       C  
ATOM    835  CD1 PHE A 105      -1.305  28.497   9.491  1.00 10.25           C  
ANISOU  835  CD1 PHE A 105      268   2308   1316     78    116     81       C  
ATOM    836  CD2 PHE A 105      -0.476  27.596  11.522  1.00 10.65           C  
ANISOU  836  CD2 PHE A 105      284   2404   1359   -200   -100   -165       C  
ATOM    837  CE1 PHE A 105      -1.527  27.214   9.012  1.00 12.34           C  
ANISOU  837  CE1 PHE A 105      291   2633   1764   -235    162   -146       C  
ATOM    838  CE2 PHE A 105      -0.676  26.319  11.054  1.00 11.08           C  
ANISOU  838  CE2 PHE A 105      268   2319   1621     69    134    134       C  
ATOM    839  CZ  PHE A 105      -1.232  26.122   9.802  1.00 11.06           C  
ANISOU  839  CZ  PHE A 105      293   2151   1755   -149    226   -286       C  
ATOM    840  N   PHE A 106       0.182  31.895   8.865  1.00 10.17           N  
ANISOU  840  N   PHE A 106      270   2245   1349    -38    135    -13       N  
ATOM    841  CA  PHE A 106       0.264  32.128   7.436  1.00 10.29           C  
ANISOU  841  CA  PHE A 106      390   2106   1414   -180   -219     20       C  
ATOM    842  C   PHE A 106       1.493  32.918   7.014  1.00 10.16           C  
ANISOU  842  C   PHE A 106      379   2226   1255     62    115   -125       C  
ATOM    843  O   PHE A 106       2.023  32.699   5.933  1.00 10.53           O  
ANISOU  843  O   PHE A 106      260   2388   1351     75     65    -80       O  
ATOM    844  CB  PHE A 106      -1.032  32.722   6.913  1.00  9.91           C  
ANISOU  844  CB  PHE A 106      331   2080   1351    -71   -289     31       C  
ATOM    845  CG  PHE A 106      -2.126  31.728   6.868  1.00 10.40           C  
ANISOU  845  CG  PHE A 106      273   2199   1477     57    149     25       C  
ATOM    846  CD1 PHE A 106      -2.097  30.734   5.930  1.00 12.09           C  
ANISOU  846  CD1 PHE A 106      649   2418   1524   -304    125   -403       C  
ATOM    847  CD2 PHE A 106      -3.100  31.683   7.862  1.00 10.63           C  
ANISOU  847  CD2 PHE A 106      410   2161   1465   -122     73   -140       C  
ATOM    848  CE1 PHE A 106      -3.047  29.744   5.933  1.00 12.00           C  
ANISOU  848  CE1 PHE A 106      343   2246   1968    266   -331   -211       C  
ATOM    849  CE2 PHE A 106      -4.008  30.684   7.887  1.00 10.97           C  
ANISOU  849  CE2 PHE A 106      260   2276   1630    106     47     47       C  
ATOM    850  CZ  PHE A 106      -4.003  29.723   6.923  1.00 13.18           C  
ANISOU  850  CZ  PHE A 106      607   2470   1928   -346     41   -273       C  
ATOM    851  N  ALYS A 107       1.985  33.803   7.886  0.50 10.63           N  
ANISOU  851  N  ALYS A 107      337   2356   1344   -246    228    -69       N  
ATOM    852  N  BLYS A 107       1.999  33.767   7.889  0.50 10.14           N  
ANISOU  852  N  BLYS A 107      304   2242   1304   -238    161    -64       N  
ATOM    853  CA ALYS A 107       3.288  34.456   7.639  0.50 12.73           C  
ANISOU  853  CA ALYS A 107      733   2403   1700   -144     43     10       C  
ATOM    854  CA BLYS A 107       3.250  34.449   7.601  0.50 11.27           C  
ANISOU  854  CA BLYS A 107      555   2162   1561   -179    -58     25       C  
ATOM    855  C  ALYS A 107       4.355  33.399   7.436  0.50 12.01           C  
ANISOU  855  C  ALYS A 107      660   2418   1482   -368   -232     89       C  
ATOM    856  C  BLYS A 107       4.392  33.444   7.484  0.50 11.44           C  
ANISOU  856  C  BLYS A 107      619   2238   1488   -354   -261    113       C  
ATOM    857  O  ALYS A 107       5.159  33.486   6.507  0.50 11.93           O  
ANISOU  857  O  ALYS A 107      269   2884   1380     73    120   -154       O  
ATOM    858  O  BLYS A 107       5.279  33.613   6.659  0.50 12.32           O  
ANISOU  858  O  BLYS A 107      384   2557   1741   -341    348    -21       O  
ATOM    859  CB ALYS A 107       3.678  35.363   8.811  0.50 16.04           C  
ANISOU  859  CB ALYS A 107     1406   2678   2011   -256    227     16       C  
ATOM    860  CB BLYS A 107       3.544  35.466   8.680  0.50 11.63           C  
ANISOU  860  CB BLYS A 107      592   2347   1480   -340   -204    125       C  
ATOM    861  CG ALYS A 107       3.007  36.735   8.802  0.50 16.38           C  
ANISOU  861  CG ALYS A 107     1669   2756   1796   -220     48    128       C  
ATOM    862  CG BLYS A 107       4.774  36.275   8.443  0.50 12.20           C  
ANISOU  862  CG BLYS A 107      356   2320   1958   -462    -42    158       C  
ATOM    863  CD ALYS A 107       3.354  37.540  10.055  0.50 18.87           C  
ANISOU  863  CD ALYS A 107     1867   2833   2468   -205    116    -64       C  
ATOM    864  CD BLYS A 107       4.979  37.269   9.557  0.50 13.53           C  
ANISOU  864  CD BLYS A 107      549   2088   2501   -652    470   -266       C  
ATOM    865  CE ALYS A 107       2.708  38.944  10.035  0.50 21.13           C  
ANISOU  865  CE ALYS A 107     2898   2821   2307   -526    -95   -271       C  
ATOM    866  CE BLYS A 107       5.490  36.589  10.822  0.50 15.66           C  
ANISOU  866  CE BLYS A 107      820   2757   2370   -451    277   -199       C  
ATOM    867  NZ ALYS A 107       1.338  38.959  10.580  0.50 18.72           N  
ANISOU  867  NZ ALYS A 107     1678   4012   1421   -432   -965   -818       N  
ATOM    868  NZ BLYS A 107       5.436  37.489  12.007  0.50 25.58           N  
ANISOU  868  NZ BLYS A 107     2349   3969   3401    -80    -68   -480       N  
ATOM    869  N   ASP A 108       4.355  32.391   8.298  1.00 11.20           N  
ANISOU  869  N   ASP A 108      263   2256   1737   -136    -31    -16       N  
ATOM    870  CA  ASP A 108       5.370  31.348   8.253  1.00 12.06           C  
ANISOU  870  CA  ASP A 108      361   2424   1797    -27   -231    143       C  
ATOM    871  C   ASP A 108       5.246  30.512   6.979  1.00 11.22           C  
ANISOU  871  C   ASP A 108      418   2495   1350   -124    355   -111       C  
ATOM    872  O   ASP A 108       6.248  30.188   6.346  1.00 11.75           O  
ANISOU  872  O   ASP A 108      271   2549   1642    136    115    -37       O  
ATOM    873  CB  ASP A 108       5.259  30.454   9.489  1.00 13.12           C  
ANISOU  873  CB  ASP A 108      866   2327   1790    156   -217     55       C  
ATOM    874  CG  ASP A 108       6.407  29.464   9.600  1.00 15.84           C  
ANISOU  874  CG  ASP A 108     1081   2737   2198   -552    -33    432       C  
ATOM    875  OD1 ASP A 108       7.573  29.916   9.863  1.00 18.49           O  
ANISOU  875  OD1 ASP A 108      341   3677   3007   -379   -377    186       O  
ATOM    876  OD2 ASP A 108       6.174  28.250   9.405  1.00 17.07           O  
ANISOU  876  OD2 ASP A 108      447   3273   2764     15   -277    253       O  
ATOM    877  N   ILE A 109       4.019  30.155   6.606  1.00 11.72           N  
ANISOU  877  N   ILE A 109      405   2425   1622   -291   -141    -42       N  
ATOM    878  CA  ILE A 109       3.780  29.514   5.335  1.00 11.03           C  
ANISOU  878  CA  ILE A 109      254   2212   1724    -37     19    186       C  
ATOM    879  C   ILE A 109       4.365  30.338   4.167  1.00 10.76           C  
ANISOU  879  C   ILE A 109      324   2305   1458    111    -89    -96       C  
ATOM    880  O   ILE A 109       5.048  29.786   3.288  1.00 11.16           O  
ANISOU  880  O   ILE A 109      286   2281   1672     96    193   -155       O  
ATOM    881  CB  ILE A 109       2.265  29.249   5.133  1.00 10.51           C  
ANISOU  881  CB  ILE A 109      314   2263   1416     91    -23   -206       C  
ATOM    882  CG1 ILE A 109       1.855  28.019   5.969  1.00 11.17           C  
ANISOU  882  CG1 ILE A 109      336   2525   1382    -93    -40     52       C  
ATOM    883  CG2 ILE A 109       1.917  29.082   3.660  1.00 11.42           C  
ANISOU  883  CG2 ILE A 109      327   2398   1613      1    314   -222       C  
ATOM    884  CD1 ILE A 109       0.316  27.750   6.041  1.00 12.94           C  
ANISOU  884  CD1 ILE A 109      285   2540   2091   -208    163    -48       C  
ATOM    885  N   CYS A 110       4.140  31.647   4.182  1.00 10.83           N  
ANISOU  885  N   CYS A 110      283   2329   1501    248     14     18       N  
ATOM    886  CA  CYS A 110       4.586  32.501   3.093  1.00 10.24           C  
ANISOU  886  CA  CYS A 110      305   2147   1435    130   -221     63       C  
ATOM    887  C   CYS A 110       6.109  32.598   3.108  1.00 10.54           C  
ANISOU  887  C   CYS A 110      329   2430   1245    197   -231     99       C  
ATOM    888  O   CYS A 110       6.751  32.624   2.046  1.00 11.75           O  
ANISOU  888  O   CYS A 110      260   2594   1609    -94     61     48       O  
ATOM    889  CB  CYS A 110       3.962  33.890   3.190  1.00 10.71           C  
ANISOU  889  CB  CYS A 110      364   2257   1447    -68    350    204       C  
ATOM    890  SG  CYS A 110       2.188  33.931   2.780  1.00 12.54           S  
ANISOU  890  SG  CYS A 110      279   2730   1753    190    139    130       S  
ATOM    891  N   PHE A 111       6.690  32.594   4.297  1.00 11.27           N  
ANISOU  891  N   PHE A 111      302   2325   1653   -129     48    107       N  
ATOM    892  CA  PHE A 111       8.155  32.667   4.441  1.00 11.38           C  
ANISOU  892  CA  PHE A 111      355   2063   1903   -326    -51     48       C  
ATOM    893  C   PHE A 111       8.837  31.438   3.858  1.00 10.80           C  
ANISOU  893  C   PHE A 111      301   2287   1514    -67   -242     55       C  
ATOM    894  O   PHE A 111       9.940  31.542   3.256  1.00 13.52           O  
ANISOU  894  O   PHE A 111      378   2666   2091   -259    437   -151       O  
ATOM    895  CB  PHE A 111       8.514  32.832   5.893  1.00 12.38           C  
ANISOU  895  CB  PHE A 111      278   2599   1826   -104   -172   -106       C  
ATOM    896  CG  PHE A 111       9.989  33.031   6.115  1.00 13.45           C  
ANISOU  896  CG  PHE A 111      428   2717   1965   -371   -231    120       C  
ATOM    897  CD1 PHE A 111      10.603  34.264   5.834  1.00 17.61           C  
ANISOU  897  CD1 PHE A 111      559   3546   2587   -686    688   -367       C  
ATOM    898  CD2 PHE A 111      10.777  31.987   6.510  1.00 18.70           C  
ANISOU  898  CD2 PHE A 111      943   3351   2810     54   -292   -296       C  
ATOM    899  CE1 PHE A 111      11.985  34.426   5.978  1.00 21.21           C  
ANISOU  899  CE1 PHE A 111     1796   3251   3011   -537    449     32       C  
ATOM    900  CE2 PHE A 111      12.157  32.156   6.659  1.00 24.82           C  
ANISOU  900  CE2 PHE A 111     1868   3987   3574    224   -134   -244       C  
ATOM    901  CZ  PHE A 111      12.739  33.388   6.387  1.00 17.71           C  
ANISOU  901  CZ  PHE A 111      317   4165   2244   -411   -189   -141       C  
ATOM    902  N   LYS A 112       8.240  30.272   4.073  1.00 10.83           N  
ANISOU  902  N   LYS A 112      259   2266   1588   -103     40      2       N  
ATOM    903  CA  LYS A 112       8.822  28.992   3.696  1.00 12.10           C  
ANISOU  903  CA  LYS A 112      419   2320   1856    -22   -124    -62       C  
ATOM    904  C   LYS A 112       8.490  28.504   2.293  1.00 11.77           C  
ANISOU  904  C   LYS A 112      354   2230   1886    177   -216     58       C  
ATOM    905  O   LYS A 112       9.183  27.640   1.752  1.00 12.52           O  
ANISOU  905  O   LYS A 112      282   2486   1990    156   -182    -86       O  
ATOM    906  CB  LYS A 112       8.425  27.919   4.702  1.00 13.29           C  
ANISOU  906  CB  LYS A 112      490   2493   2067    367   -281   -377       C  
ATOM    907  CG  LYS A 112       8.974  28.167   6.099  1.00 18.62           C  
ANISOU  907  CG  LYS A 112     1925   2941   2207    139   -258    -70       C  
ATOM    908  CD  LYS A 112      10.271  27.459   6.340  1.00 26.32           C  
ANISOU  908  CD  LYS A 112     2592   4251   3156    103   -936   -207       C  
ATOM    909  CE  LYS A 112      10.637  27.473   7.823  1.00 32.36           C  
ANISOU  909  CE  LYS A 112     3551   4919   3824    150   -971    376       C  
ATOM    910  NZ  LYS A 112      10.166  26.240   8.550  1.00 35.51           N  
ANISOU  910  NZ  LYS A 112     3153   5414   4925    157  -1376    141       N  
ATOM    911  N   PHE A 113       7.413  29.010   1.712  1.00 10.97           N  
ANISOU  911  N   PHE A 113      321   2378   1469    279    196      3       N  
ATOM    912  CA  PHE A 113       6.954  28.527   0.425  1.00 10.58           C  
ANISOU  912  CA  PHE A 113      326   2197   1496    288    179    -92       C  
ATOM    913  C   PHE A 113       8.040  28.767  -0.625  1.00 10.28           C  
ANISOU  913  C   PHE A 113      262   2022   1621    108     60    -43       C  
ATOM    914  O   PHE A 113       8.748  29.784  -0.578  1.00 11.26           O  
ANISOU  914  O   PHE A 113      254   2104   1920    -21     35   -175       O  
ATOM    915  CB  PHE A 113       5.635  29.230   0.001  1.00 10.82           C  
ANISOU  915  CB  PHE A 113      270   2184   1657    114   -123    -32       C  
ATOM    916  CG  PHE A 113       4.522  28.272  -0.441  1.00 11.46           C  
ANISOU  916  CG  PHE A 113      664   2305   1386    124     16    -25       C  
ATOM    917  CD1 PHE A 113       4.621  27.535  -1.593  1.00 13.34           C  
ANISOU  917  CD1 PHE A 113      275   3144   1650   -107   -155    -57       C  
ATOM    918  CD2 PHE A 113       3.379  28.164   0.291  1.00 12.67           C  
ANISOU  918  CD2 PHE A 113      984   2437   1390   -114    243   -104       C  
ATOM    919  CE1 PHE A 113       3.584  26.704  -1.999  1.00 13.02           C  
ANISOU  919  CE1 PHE A 113      502   2644   1800    120    170   -405       C  
ATOM    920  CE2 PHE A 113       2.343  27.359  -0.130  1.00 12.72           C  
ANISOU  920  CE2 PHE A 113      405   2524   1901   -147     59   -364       C  
ATOM    921  CZ  PHE A 113       2.453  26.643  -1.257  1.00 12.19           C  
ANISOU  921  CZ  PHE A 113      436   2324   1871     83    -59   -320       C  
ATOM    922  N   GLN A 114       8.094  27.894  -1.614  1.00 10.21           N  
ANISOU  922  N   GLN A 114      264   2169   1444    -99    -75   -137       N  
ATOM    923  CA  GLN A 114       8.962  28.063  -2.736  1.00 10.39           C  
ANISOU  923  CA  GLN A 114      291   2263   1394    109      9     26       C  
ATOM    924  C   GLN A 114       8.500  27.189  -3.860  1.00 10.02           C  
ANISOU  924  C   GLN A 114      356   1949   1500    124    -32     79       C  
ATOM    925  O   GLN A 114       7.669  26.269  -3.648  1.00 10.39           O  
ANISOU  925  O   GLN A 114      280   1951   1716    150    141    -10       O  
ATOM    926  CB  GLN A 114      10.394  27.668  -2.340  1.00 11.20           C  
ANISOU  926  CB  GLN A 114      282   2347   1626    175   -155   -179       C  
ATOM    927  CG  GLN A 114      10.459  26.290  -1.740  1.00 12.06           C  
ANISOU  927  CG  GLN A 114      294   2266   2021    174   -222    -88       C  
ATOM    928  CD  GLN A 114      11.894  25.785  -1.608  1.00 12.40           C  
ANISOU  928  CD  GLN A 114      491   2343   1878    101   -535    -24       C  
ATOM    929  OE1 GLN A 114      12.626  26.204  -0.711  1.00 13.00           O  
ANISOU  929  OE1 GLN A 114      315   2552   2072    335   -156     -6       O  
ATOM    930  NE2 GLN A 114      12.289  24.878  -2.493  1.00 13.19           N  
ANISOU  930  NE2 GLN A 114      295   2604   2109    143   -256   -107       N  
ATOM    931  N   PHE A 115       9.037  27.439  -5.058  1.00 10.61           N  
ANISOU  931  N   PHE A 115      284   2152   1592    241     42     76       N  
ATOM    932  CA  PHE A 115       8.967  26.484  -6.157  1.00 10.82           C  
ANISOU  932  CA  PHE A 115      433   2277   1400     99    451     58       C  
ATOM    933  C   PHE A 115      10.422  26.170  -6.563  1.00 10.53           C  
ANISOU  933  C   PHE A 115      322   1889   1787     54    233   -287       C  
ATOM    934  O   PHE A 115      11.258  27.076  -6.588  1.00 12.52           O  
ANISOU  934  O   PHE A 115      259   2245   2250     51   -106   -232       O  
ATOM    935  CB  PHE A 115       8.266  27.067  -7.369  1.00 11.05           C  
ANISOU  935  CB  PHE A 115      338   2365   1492    217    282     28       C  
ATOM    936  CG  PHE A 115       6.825  27.512  -7.121  1.00 10.57           C  
ANISOU  936  CG  PHE A 115      313   2238   1464     96    259    -17       C  
ATOM    937  CD1 PHE A 115       5.827  26.604  -6.728  1.00 12.02           C  
ANISOU  937  CD1 PHE A 115      560   2313   1694     23    -66    324       C  
ATOM    938  CD2 PHE A 115       6.475  28.822  -7.310  1.00 11.72           C  
ANISOU  938  CD2 PHE A 115      283   2347   1820   -189   -157    133       C  
ATOM    939  CE1 PHE A 115       4.457  27.028  -6.578  1.00 12.90           C  
ANISOU  939  CE1 PHE A 115      326   2368   2205    -67    -11   -119       C  
ATOM    940  CE2 PHE A 115       5.103  29.241  -7.158  1.00 12.79           C  
ANISOU  940  CE2 PHE A 115      303   2200   2355     -2    324     -9       C  
ATOM    941  CZ  PHE A 115       4.132  28.325  -6.772  1.00 13.09           C  
ANISOU  941  CZ  PHE A 115      353   2275   2342    127    449    183       C  
ATOM    942  N   PRO A 116      10.728  24.897  -6.858  1.00 11.36           N  
ANISOU  942  N   PRO A 116      339   2122   1852    -65    367    -41       N  
ATOM    943  CA  PRO A 116       9.854  23.741  -6.719  1.00 11.39           C  
ANISOU  943  CA  PRO A 116      364   2103   1858    168     60    -13       C  
ATOM    944  C   PRO A 116       9.667  23.369  -5.273  1.00 11.78           C  
ANISOU  944  C   PRO A 116      309   2224   1941    206    207   -300       C  
ATOM    945  O   PRO A 116      10.329  23.923  -4.390  1.00 12.64           O  
ANISOU  945  O   PRO A 116      266   2737   1798    -28    141   -110       O  
ATOM    946  CB  PRO A 116      10.636  22.605  -7.467  1.00 13.38           C  
ANISOU  946  CB  PRO A 116      360   2465   2259    199    426     45       C  
ATOM    947  CG  PRO A 116      11.782  23.298  -8.159  1.00 14.01           C  
ANISOU  947  CG  PRO A 116      405   2235   2682    382    455     98       C  
ATOM    948  CD  PRO A 116      12.068  24.511  -7.344  1.00 13.28           C  
ANISOU  948  CD  PRO A 116      522   2339   2183    412    630    158       C  
ATOM    949  N   ASN A 117       8.768  22.427  -5.019  1.00 11.15           N  
ANISOU  949  N   ASN A 117      253   2316   1668      1      8      3       N  
ATOM    950  CA  ASN A 117       8.537  21.960  -3.691  1.00 11.43           C  
ANISOU  950  CA  ASN A 117      277   2153   1914    178    -52   -161       C  
ATOM    951  C   ASN A 117       8.027  20.518  -3.665  1.00 12.10           C  
ANISOU  951  C   ASN A 117      443   2349   1804    254     71    -31       C  
ATOM    952  O   ASN A 117       7.752  19.912  -4.720  1.00 12.31           O  
ANISOU  952  O   ASN A 117      433   2354   1890    125     61     -2       O  
ATOM    953  CB  ASN A 117       7.558  22.906  -2.973  1.00 11.15           C  
ANISOU  953  CB  ASN A 117      264   2281   1691     67   -113    -78       C  
ATOM    954  CG  ASN A 117       6.183  22.934  -3.635  1.00 10.68           C  
ANISOU  954  CG  ASN A 117      289   1951   1815   -149    187     11       C  
ATOM    955  OD1 ASN A 117       5.544  21.887  -3.777  1.00 11.45           O  
ANISOU  955  OD1 ASN A 117      253   2035   2061     31      2    148       O  
ATOM    956  ND2 ASN A 117       5.756  24.125  -4.108  1.00 10.72           N  
ANISOU  956  ND2 ASN A 117      268   2122   1679    140     90     91       N  
ATOM    957  N   GLY A 118       7.880  19.974  -2.471  1.00 11.46           N  
ANISOU  957  N   GLY A 118      325   2350   1676    303   -202    -30       N  
ATOM    958  CA  GLY A 118       7.409  18.607  -2.306  1.00 11.39           C  
ANISOU  958  CA  GLY A 118      330   2293   1702    137    155    120       C  
ATOM    959  C   GLY A 118       5.944  18.491  -1.981  1.00 11.61           C  
ANISOU  959  C   GLY A 118      755   1871   1784    122    143     67       C  
ATOM    960  O   GLY A 118       5.489  17.441  -1.536  1.00 13.24           O  
ANISOU  960  O   GLY A 118      693   2210   2127    218    138    161       O  
ATOM    961  N   MET A 119       5.181  19.544  -2.244  1.00 11.78           N  
ANISOU  961  N   MET A 119      522   1906   2047     10   -120    131       N  
ATOM    962  CA  MET A 119       3.695  19.440  -2.173  1.00 12.22           C  
ANISOU  962  CA  MET A 119      378   2336   1927     22     79    219       C  
ATOM    963  C   MET A 119       3.120  18.805  -3.426  1.00 10.95           C  
ANISOU  963  C   MET A 119      261   2233   1665    109     57     24       C  
ATOM    964  O   MET A 119       2.057  18.153  -3.383  1.00 13.90           O  
ANISOU  964  O   MET A 119      379   2645   2256   -229   -125      0       O  
ATOM    965  CB  MET A 119       3.065  20.808  -1.974  1.00 12.00           C  
ANISOU  965  CB  MET A 119      256   2533   1770    -78      0    198       C  
ATOM    966  CG  MET A 119       3.474  21.468  -0.734  1.00 11.28           C  
ANISOU  966  CG  MET A 119      377   1981   1928     15    -38    110       C  
ATOM    967  SD  MET A 119       2.436  22.818  -0.368  1.00 16.22           S  
ANISOU  967  SD  MET A 119     1032   3119   2011    673    123     58       S  
ATOM    968  CE  MET A 119       3.380  23.724   0.741  1.00 14.49           C  
ANISOU  968  CE  MET A 119      368   2678   2456    349   -240    178       C  
ATOM    969  N   ASP A 120       3.762  19.077  -4.560  1.00 12.10           N  
ANISOU  969  N   ASP A 120      266   2518   1811    117     91      0       N  
ATOM    970  CA  ASP A 120       3.268  18.662  -5.853  1.00 12.13           C  
ANISOU  970  CA  ASP A 120      398   2416   1792    400     93    -43       C  
ATOM    971  C   ASP A 120       3.426  17.153  -6.063  1.00 12.62           C  
ANISOU  971  C   ASP A 120      571   2132   2092    221    216     34       C  
ATOM    972  O   ASP A 120       4.364  16.524  -5.540  1.00 14.23           O  
ANISOU  972  O   ASP A 120      693   2419   2296    377    -38    124       O  
ATOM    973  CB  ASP A 120       4.032  19.388  -6.976  1.00 13.06           C  
ANISOU  973  CB  ASP A 120      305   2508   2149     50      5    -57       C  
ATOM    974  CG  ASP A 120       3.875  20.905  -6.923  1.00 14.13           C  
ANISOU  974  CG  ASP A 120      454   2708   2205    163     -6     88       C  
ATOM    975  OD1 ASP A 120       2.867  21.400  -6.374  1.00 14.96           O  
ANISOU  975  OD1 ASP A 120      632   2658   2394    127    164   -167       O  
ATOM    976  OD2 ASP A 120       4.769  21.605  -7.453  1.00 16.81           O  
ANISOU  976  OD2 ASP A 120      830   2494   3064    296    259    234       O  
ATOM    977  N   LYS A 121       2.643  16.635  -6.992  1.00 12.27           N  
ANISOU  977  N   LYS A 121      311   2236   2111    191    262   -109       N  
ATOM    978  CA  LYS A 121       2.760  15.264  -7.461  1.00 13.12           C  
ANISOU  978  CA  LYS A 121      333   2304   2345    388   -119      0       C  
ATOM    979  C   LYS A 121       4.088  15.131  -8.237  1.00 12.27           C  
ANISOU  979  C   LYS A 121      281   2025   2353    216    -87   -163       C  
ATOM    980  O   LYS A 121       4.521  16.076  -8.878  1.00 13.49           O  
ANISOU  980  O   LYS A 121      741   2207   2175    207    204    -69       O  
ATOM    981  CB  LYS A 121       1.566  14.920  -8.354  1.00 14.29           C  
ANISOU  981  CB  LYS A 121      578   2419   2431    -54    -81    180       C  
ATOM    982  CG  LYS A 121       1.439  13.438  -8.719  1.00 15.92           C  
ANISOU  982  CG  LYS A 121     1111   2474   2462    261    -14   -236       C  
ATOM    983  CD  LYS A 121       0.179  13.215  -9.512  1.00 17.24           C  
ANISOU  983  CD  LYS A 121     1111   2690   2747    338   -148    -42       C  
ATOM    984  CE  LYS A 121      -0.023  11.758  -9.949  1.00 17.60           C  
ANISOU  984  CE  LYS A 121     1166   2625   2896    447     15   -326       C  
ATOM    985  NZ  LYS A 121      -0.314  10.845  -8.813  1.00 17.25           N  
ANISOU  985  NZ  LYS A 121     1660   2435   2457     -3    331   -103       N  
ATOM    986  N   LEU A 122       4.701  13.961  -8.199  1.00 13.26           N  
ANISOU  986  N   LEU A 122      634   2183   2221     80    224      8       N  
ATOM    987  CA  LEU A 122       6.055  13.803  -8.772  1.00 14.12           C  
ANISOU  987  CA  LEU A 122      861   2317   2183     92    110   -171       C  
ATOM    988  C   LEU A 122       6.163  14.279 -10.226  1.00 13.17           C  
ANISOU  988  C   LEU A 122      831   2074   2099      4      9   -145       C  
ATOM    989  O   LEU A 122       7.165  14.859 -10.607  1.00 14.98           O  
ANISOU  989  O   LEU A 122      777   2415   2498     35    388      9       O  
ATOM    990  CB  LEU A 122       6.523  12.358  -8.677  1.00 13.79           C  
ANISOU  990  CB  LEU A 122      442   2404   2394    341    253     23       C  
ATOM    991  CG  LEU A 122       8.000  12.146  -9.095  1.00 15.93           C  
ANISOU  991  CG  LEU A 122      477   2740   2836    352    680     75       C  
ATOM    992  CD1 LEU A 122       8.932  12.833  -8.107  1.00 22.28           C  
ANISOU  992  CD1 LEU A 122     1462   3765   3237    344    -41   -169       C  
ATOM    993  CD2 LEU A 122       8.335  10.659  -9.211  1.00 22.80           C  
ANISOU  993  CD2 LEU A 122     1992   2707   3963    496    716     48       C  
ATOM    994  N   ASP A 123       5.155  14.002 -11.054  1.00 15.15           N  
ANISOU  994  N   ASP A 123     1078   2515   2164     42    217   -114       N  
ATOM    995  CA  ASP A 123       5.255  14.405 -12.457  1.00 16.77           C  
ANISOU  995  CA  ASP A 123     1654   2356   2361    249     41   -172       C  
ATOM    996  C   ASP A 123       5.314  15.932 -12.573  1.00 15.53           C  
ANISOU  996  C   ASP A 123     1354   2615   1930     75     37    -19       C  
ATOM    997  O   ASP A 123       6.048  16.475 -13.415  1.00 16.27           O  
ANISOU  997  O   ASP A 123     1562   2461   2158    259    309   -143       O  
ATOM    998  CB  ASP A 123       4.123  13.811 -13.320  1.00 15.30           C  
ANISOU  998  CB  ASP A 123      863   2570   2379    202    180   -168       C  
ATOM    999  CG  ASP A 123       2.749  14.151 -12.818  1.00 17.42           C  
ANISOU  999  CG  ASP A 123     1272   2998   2349    158   -348    -55       C  
ATOM   1000  OD1 ASP A 123       2.562  14.240 -11.601  1.00 21.37           O  
ANISOU 1000  OD1 ASP A 123     2010   3439   2667    -82    -84   -150       O  
ATOM   1001  OD2 ASP A 123       1.823  14.274 -13.667  1.00 21.38           O  
ANISOU 1001  OD2 ASP A 123     1835   3304   2983    168      6    -99       O  
ATOM   1002  N   LYS A 124       4.586  16.621 -11.691  1.00 14.33           N  
ANISOU 1002  N   LYS A 124     1018   2391   2036     87    135   -114       N  
ATOM   1003  CA  LYS A 124       4.590  18.068 -11.666  1.00 14.31           C  
ANISOU 1003  CA  LYS A 124      678   2621   2138    159     97   -173       C  
ATOM   1004  C   LYS A 124       5.949  18.617 -11.110  1.00 14.11           C  
ANISOU 1004  C   LYS A 124     1119   2162   2080    131    273     15       C  
ATOM   1005  O   LYS A 124       6.461  19.628 -11.587  1.00 13.93           O  
ANISOU 1005  O   LYS A 124      756   2336   2200    166    284     96       O  
ATOM   1006  CB  LYS A 124       3.403  18.580 -10.847  1.00 14.95           C  
ANISOU 1006  CB  LYS A 124     1194   2116   2367    410    140   -239       C  
ATOM   1007  CG  LYS A 124       2.054  18.075 -11.355  1.00 19.48           C  
ANISOU 1007  CG  LYS A 124     1595   3025   2778    358     80     88       C  
ATOM   1008  CD  LYS A 124       1.673  18.694 -12.680  1.00 22.50           C  
ANISOU 1008  CD  LYS A 124     1312   4077   3158    234    141   -425       C  
ATOM   1009  CE  LYS A 124       0.196  18.506 -12.975  1.00 28.16           C  
ANISOU 1009  CE  LYS A 124     2292   4724   3683    137   -520   -166       C  
ATOM   1010  NZ  LYS A 124      -0.078  18.437 -14.435  1.00 36.78           N  
ANISOU 1010  NZ  LYS A 124     5103   5334   3537    518   -209    -83       N  
ATOM   1011  N   VAL A 125       6.502  17.949 -10.104  1.00 13.15           N  
ANISOU 1011  N   VAL A 125      578   2289   2127    182    309      7       N  
ATOM   1012  CA  VAL A 125       7.850  18.275  -9.617  1.00 13.67           C  
ANISOU 1012  CA  VAL A 125      768   2307   2117    385    249   -219       C  
ATOM   1013  C   VAL A 125       8.883  18.198 -10.747  1.00 13.03           C  
ANISOU 1013  C   VAL A 125      508   2155   2286    188    277   -203       C  
ATOM   1014  O   VAL A 125       9.635  19.132 -10.970  1.00 14.89           O  
ANISOU 1014  O   VAL A 125      826   2373   2457    -28    236    -82       O  
ATOM   1015  CB  VAL A 125       8.296  17.314  -8.474  1.00 13.03           C  
ANISOU 1015  CB  VAL A 125      283   2535   2133    233    102    -78       C  
ATOM   1016  CG1 VAL A 125       9.763  17.598  -8.080  1.00 14.73           C  
ANISOU 1016  CG1 VAL A 125      287   3098   2210    283    103    -21       C  
ATOM   1017  CG2 VAL A 125       7.375  17.427  -7.262  1.00 14.94           C  
ANISOU 1017  CG2 VAL A 125      356   2865   2454     60    470   -107       C  
ATOM   1018  N   ILE A 126       8.868  17.094 -11.475  1.00 14.90           N  
ANISOU 1018  N   ILE A 126      596   2518   2546      8    565   -173       N  
ATOM   1019  CA  ILE A 126       9.781  16.885 -12.574  1.00 16.22           C  
ANISOU 1019  CA  ILE A 126     1141   2553   2467     71    595   -240       C  
ATOM   1020  C   ILE A 126       9.613  17.969 -13.651  1.00 16.00           C  
ANISOU 1020  C   ILE A 126     1313   2535   2230    180    418   -235       C  
ATOM   1021  O   ILE A 126      10.574  18.438 -14.204  1.00 17.59           O  
ANISOU 1021  O   ILE A 126     1099   2863   2719    133    928   -289       O  
ATOM   1022  CB  ILE A 126       9.586  15.463 -13.175  1.00 17.29           C  
ANISOU 1022  CB  ILE A 126     1286   2692   2589     19    554   -177       C  
ATOM   1023  CG1 ILE A 126      10.090  14.413 -12.178  1.00 17.81           C  
ANISOU 1023  CG1 ILE A 126      716   3271   2778    266    873   -200       C  
ATOM   1024  CG2 ILE A 126      10.286  15.326 -14.521  1.00 18.31           C  
ANISOU 1024  CG2 ILE A 126     1387   2934   2633    316   1178   -437       C  
ATOM   1025  CD1 ILE A 126       9.759  12.975 -12.547  1.00 19.67           C  
ANISOU 1025  CD1 ILE A 126     1888   2552   3032    366    617   -337       C  
ATOM   1026  N  AGLU A 127       8.374  18.371 -13.916  0.50 16.13           N  
ANISOU 1026  N  AGLU A 127     1330   2565   2232    126    303   -164       N  
ATOM   1027  N  BGLU A 127       8.377  18.384 -13.906  0.50 16.30           N  
ANISOU 1027  N  BGLU A 127     1384   2565   2243    142    320   -157       N  
ATOM   1028  CA AGLU A 127       8.121  19.458 -14.869  0.50 17.11           C  
ANISOU 1028  CA AGLU A 127     1791   2577   2130    -91    277   -156       C  
ATOM   1029  CA BGLU A 127       8.133  19.460 -14.871  0.50 17.18           C  
ANISOU 1029  CA BGLU A 127     1842   2580   2105    -84    283   -132       C  
ATOM   1030  C  AGLU A 127       8.772  20.771 -14.396  0.50 16.00           C  
ANISOU 1030  C  AGLU A 127     1551   2523   2006    -34    445   -125       C  
ATOM   1031  C  BGLU A 127       8.762  20.782 -14.399  0.50 16.06           C  
ANISOU 1031  C  BGLU A 127     1575   2517   2008    -23    445   -125       C  
ATOM   1032  O  AGLU A 127       9.418  21.469 -15.173  0.50 18.69           O  
ANISOU 1032  O  AGLU A 127     2111   2709   2280   -174    488   -114       O  
ATOM   1033  O  BGLU A 127       9.375  21.502 -15.183  0.50 18.53           O  
ANISOU 1033  O  BGLU A 127     2085   2630   2325   -152    475   -156       O  
ATOM   1034  CB AGLU A 127       6.618  19.661 -15.074  0.50 18.66           C  
ANISOU 1034  CB AGLU A 127     1955   2659   2473    163    182   -150       C  
ATOM   1035  CB BGLU A 127       6.638  19.650 -15.107  0.50 18.36           C  
ANISOU 1035  CB BGLU A 127     1959   2627   2390    172    220   -135       C  
ATOM   1036  CG AGLU A 127       5.950  18.592 -15.945  0.50 19.37           C  
ANISOU 1036  CG AGLU A 127     1882   2735   2742    -51    221   -195       C  
ATOM   1037  CG BGLU A 127       6.313  20.584 -16.270  0.50 20.48           C  
ANISOU 1037  CG BGLU A 127     2374   2889   2519    -39     92    125       C  
ATOM   1038  CD AGLU A 127       4.439  18.749 -16.019  0.50 25.94           C  
ANISOU 1038  CD AGLU A 127     2909   3271   3675   -127   -234    -14       C  
ATOM   1039  CD BGLU A 127       4.922  21.206 -16.171  0.50 23.11           C  
ANISOU 1039  CD BGLU A 127     2276   3409   3093   -331   -143    269       C  
ATOM   1040  OE1AGLU A 127       3.937  19.838 -15.681  0.50 27.35           O  
ANISOU 1040  OE1AGLU A 127     2377   3713   4301   -386    -64   -314       O  
ATOM   1041  OE1BGLU A 127       4.216  20.953 -15.171  0.50 27.77           O  
ANISOU 1041  OE1BGLU A 127     2415   4524   3613     -1    -86     77       O  
ATOM   1042  OE2AGLU A 127       3.757  17.781 -16.427  0.50 27.38           O  
ANISOU 1042  OE2AGLU A 127     2588   3545   4269   -557   -543   -144       O  
ATOM   1043  OE2BGLU A 127       4.545  21.962 -17.090  0.50 21.26           O  
ANISOU 1043  OE2BGLU A 127     2327   2553   3197    247     22    230       O  
ATOM   1044  N   LYS A 128       8.598  21.097 -13.121  1.00 15.88           N  
ANISOU 1044  N   LYS A 128     1360   2389   2285   -100    321    -93       N  
ATOM   1045  CA  LYS A 128       9.089  22.357 -12.600  1.00 14.96           C  
ANISOU 1045  CA  LYS A 128     1044   2549   2089     49    310    -28       C  
ATOM   1046  C   LYS A 128      10.616  22.360 -12.531  1.00 15.25           C  
ANISOU 1046  C   LYS A 128     1011   2383   2397   -225    282     26       C  
ATOM   1047  O   LYS A 128      11.254  23.323 -12.911  1.00 15.56           O  
ANISOU 1047  O   LYS A 128      841   2475   2596    -76    446    -51       O  
ATOM   1048  CB  LYS A 128       8.460  22.653 -11.238  1.00 15.34           C  
ANISOU 1048  CB  LYS A 128     1199   2582   2046    250    -38   -192       C  
ATOM   1049  CG  LYS A 128       6.989  22.978 -11.356  1.00 14.92           C  
ANISOU 1049  CG  LYS A 128      764   2702   2203    227    123    -67       C  
ATOM   1050  CD  LYS A 128       6.314  23.232 -10.024  1.00 16.41           C  
ANISOU 1050  CD  LYS A 128     1649   2607   1978    672    158     90       C  
ATOM   1051  CE  LYS A 128       4.796  23.360 -10.215  1.00 21.24           C  
ANISOU 1051  CE  LYS A 128     1994   3576   2498    853    252     25       C  
ATOM   1052  NZ  LYS A 128       4.072  23.572  -8.954  1.00 23.95           N  
ANISOU 1052  NZ  LYS A 128     2300   3914   2885   1564    793    462       N  
ATOM   1053  N   VAL A 129      11.186  21.246 -12.114  1.00 15.64           N  
ANISOU 1053  N   VAL A 129      814   2464   2661    124    746    -60       N  
ATOM   1054  CA  VAL A 129      12.629  21.087 -12.131  1.00 16.87           C  
ANISOU 1054  CA  VAL A 129     1240   2544   2625     31    684    153       C  
ATOM   1055  C   VAL A 129      13.159  21.141 -13.582  1.00 18.30           C  
ANISOU 1055  C   VAL A 129     1737   2380   2833     72    461    -13       C  
ATOM   1056  O   VAL A 129      14.198  21.790 -13.867  1.00 17.49           O  
ANISOU 1056  O   VAL A 129      788   3027   2828     51    809   -111       O  
ATOM   1057  CB  VAL A 129      13.043  19.776 -11.448  1.00 18.01           C  
ANISOU 1057  CB  VAL A 129     1161   2879   2800     82    611     12       C  
ATOM   1058  CG1 VAL A 129      14.470  19.402 -11.806  1.00 20.72           C  
ANISOU 1058  CG1 VAL A 129      967   3347   3557    447    532    127       C  
ATOM   1059  CG2 VAL A 129      12.865  19.892  -9.922  1.00 19.17           C  
ANISOU 1059  CG2 VAL A 129     1495   2795   2991    606    329    111       C  
ATOM   1060  N   GLY A 130      12.441  20.513 -14.505  1.00 17.23           N  
ANISOU 1060  N   GLY A 130     1202   2589   2753    144    867   -237       N  
ATOM   1061  CA  GLY A 130      12.857  20.517 -15.926  1.00 17.95           C  
ANISOU 1061  CA  GLY A 130     1303   2708   2806     26   1036   -322       C  
ATOM   1062  C   GLY A 130      12.860  21.925 -16.508  1.00 18.94           C  
ANISOU 1062  C   GLY A 130     1930   2698   2568     46    902     36       C  
ATOM   1063  O   GLY A 130      13.650  22.241 -17.396  1.00 20.54           O  
ANISOU 1063  O   GLY A 130     1915   2994   2895   -188    849   -208       O  
ATOM   1064  N   ALA A 131      11.984  22.777 -15.981  1.00 17.61           N  
ANISOU 1064  N   ALA A 131     1419   2811   2461    -37    599   -131       N  
ATOM   1065  CA  ALA A 131      11.864  24.159 -16.433  1.00 16.55           C  
ANISOU 1065  CA  ALA A 131     1219   2823   2245    117    533    -80       C  
ATOM   1066  C   ALA A 131      12.836  25.112 -15.686  1.00 16.29           C  
ANISOU 1066  C   ALA A 131     1638   2643   1909    177    930    -22       C  
ATOM   1067  O   ALA A 131      12.847  26.313 -15.937  1.00 17.20           O  
ANISOU 1067  O   ALA A 131     1237   2829   2468    -44    596    -20       O  
ATOM   1068  CB  ALA A 131      10.403  24.640 -16.267  1.00 18.05           C  
ANISOU 1068  CB  ALA A 131     1554   3004   2298    171    528    -14       C  
ATOM   1069  N   LYS A 132      13.617  24.559 -14.756  1.00 14.26           N  
ANISOU 1069  N   LYS A 132      628   2574   2215    -39    849   -220       N  
ATOM   1070  CA  LYS A 132      14.590  25.328 -13.999  1.00 16.72           C  
ANISOU 1070  CA  LYS A 132     1275   2530   2548     66    315    -61       C  
ATOM   1071  C   LYS A 132      13.927  26.391 -13.136  1.00 14.64           C  
ANISOU 1071  C   LYS A 132      939   2342   2281   -127    520   -104       C  
ATOM   1072  O   LYS A 132      14.458  27.448 -12.923  1.00 14.01           O  
ANISOU 1072  O   LYS A 132      454   2415   2450    -54    665   -226       O  
ATOM   1073  CB  LYS A 132      15.591  25.967 -14.941  1.00 19.35           C  
ANISOU 1073  CB  LYS A 132     1577   3112   2660    -63    702   -232       C  
ATOM   1074  CG  LYS A 132      16.388  24.935 -15.779  1.00 23.66           C  
ANISOU 1074  CG  LYS A 132     2293   3561   3134     -9    797   -171       C  
ATOM   1075  N  AILE A 133      12.756  26.087 -12.621  0.50 13.99           N  
ANISOU 1075  N  AILE A 133      641   2551   2123    -56    245   -126       N  
ATOM   1076  N  BILE A 133      12.738  26.064 -12.632  0.50 13.80           N  
ANISOU 1076  N  BILE A 133      624   2526   2091    -50    288   -126       N  
ATOM   1077  CA AILE A 133      12.094  27.017 -11.741  0.50 13.14           C  
ANISOU 1077  CA AILE A 133      485   2450   2057   -133    -11   -114       C  
ATOM   1078  CA BILE A 133      12.032  26.918 -11.673  0.50 12.85           C  
ANISOU 1078  CA BILE A 133      482   2473   1926   -126    209    -78       C  
ATOM   1079  C  AILE A 133      12.794  27.016 -10.370  0.50 15.08           C  
ANISOU 1079  C  AILE A 133     1091   2470   2165    -96    288    -34       C  
ATOM   1080  C  BILE A 133      12.824  26.996 -10.356  0.50 14.90           C  
ANISOU 1080  C  BILE A 133     1094   2469   2098    -71    324    -21       C  
ATOM   1081  O  AILE A 133      13.196  25.964  -9.865  0.50 14.67           O  
ANISOU 1081  O  AILE A 133      593   2587   2394    181    268   -204       O  
ATOM   1082  O  BILE A 133      13.259  25.967  -9.827  0.50 14.72           O  
ANISOU 1082  O  BILE A 133      604   2820   2165    116    216      4       O  
ATOM   1083  CB AILE A 133      10.596  26.692 -11.626  0.50 11.52           C  
ANISOU 1083  CB AILE A 133      338   2216   1820   -278   -262    -33       C  
ATOM   1084  CB BILE A 133      10.604  26.347 -11.385  0.50 11.97           C  
ANISOU 1084  CB BILE A 133      256   2234   2058     13    -78     72       C  
ATOM   1085  CG1AILE A 133       9.885  27.008 -12.960  0.50 13.82           C  
ANISOU 1085  CG1AILE A 133     1427   1705   2116    358     -5    102       C  
ATOM   1086  CG1BILE A 133       9.751  26.287 -12.673  0.50 10.70           C  
ANISOU 1086  CG1BILE A 133      367   1891   1804   -206     84    -79       C  
ATOM   1087  CG2AILE A 133       9.960  27.485 -10.487  0.50 13.50           C  
ANISOU 1087  CG2AILE A 133      546   2610   1973    -77   -287   -127       C  
ATOM   1088  CG2BILE A 133       9.889  27.175 -10.322  0.50 14.69           C  
ANISOU 1088  CG2BILE A 133     1391   2460   1728   -214    560   -103       C  
ATOM   1089  CD1AILE A 133       8.392  26.584 -13.018  0.50 17.48           C  
ANISOU 1089  CD1AILE A 133     1175   3003   2461   -353   -992   -129       C  
ATOM   1090  CD1BILE A 133       9.682  27.605 -13.444  0.50 11.63           C  
ANISOU 1090  CD1BILE A 133      273   2316   1830    183     88    124       C  
ATOM   1091  N   GLN A 134      13.002  28.211  -9.820  1.00 11.82           N  
ANISOU 1091  N   GLN A 134      324   2329   1838     78    328     23       N  
ATOM   1092  CA  GLN A 134      13.616  28.375  -8.481  1.00 12.02           C  
ANISOU 1092  CA  GLN A 134      353   2404   1810    100    389     78       C  
ATOM   1093  C   GLN A 134      13.330  29.758  -7.956  1.00 13.21           C  
ANISOU 1093  C   GLN A 134      635   2377   2006    -49    129     92       C  
ATOM   1094  O   GLN A 134      13.892  30.737  -8.411  1.00 14.06           O  
ANISOU 1094  O   GLN A 134      353   2734   2255    130    421   -182       O  
ATOM   1095  CB  GLN A 134      15.139  28.100  -8.461  1.00 15.62           C  
ANISOU 1095  CB  GLN A 134      344   3267   2321    399    255   -196       C  
ATOM   1096  CG  GLN A 134      15.848  28.338  -9.688  1.00 21.10           C  
ANISOU 1096  CG  GLN A 134     1355   3822   2839     98    -87   -236       C  
ATOM   1097  CD  GLN A 134      17.345  27.991  -9.555  1.00 22.03           C  
ANISOU 1097  CD  GLN A 134     1694   3969   2706     91   -403     65       C  
ATOM   1098  OE1 GLN A 134      17.827  27.591  -8.471  1.00 24.32           O  
ANISOU 1098  OE1 GLN A 134     1489   4448   3302    326     -2    419       O  
ATOM   1099  NE2 GLN A 134      18.088  28.165 -10.644  1.00 20.46           N  
ANISOU 1099  NE2 GLN A 134     1404   3422   2947     86   1107     24       N  
ATOM   1100  N  AILE A 135      12.397  29.838  -7.012  0.50 11.56           N  
ANISOU 1100  N  AILE A 135      275   2198   1919      4    191     13       N  
ATOM   1101  N  BILE A 135      12.367  29.845  -7.043  0.50 11.62           N  
ANISOU 1101  N  BILE A 135      278   2201   1936     28    204     41       N  
ATOM   1102  CA AILE A 135      11.963  31.111  -6.507  0.50 10.78           C  
ANISOU 1102  CA AILE A 135      253   2198   1645    -19    -21    -47       C  
ATOM   1103  CA BILE A 135      11.945  31.127  -6.521  0.50 10.89           C  
ANISOU 1103  CA BILE A 135      253   2239   1642     -9     29    -36       C  
ATOM   1104  C  AILE A 135      11.306  30.979  -5.137  0.50 10.67           C  
ANISOU 1104  C  AILE A 135      258   2127   1666     87     41      3       C  
ATOM   1105  C  BILE A 135      11.295  30.987  -5.146  0.50 10.73           C  
ANISOU 1105  C  BILE A 135      260   2150   1664     94     64      0       C  
ATOM   1106  O  AILE A 135      10.631  29.985  -4.849  0.50 11.54           O  
ANISOU 1106  O  AILE A 135      381   2106   1897     38    145    -28       O  
ATOM   1107  O  BILE A 135      10.621  29.992  -4.861  0.50 11.61           O  
ANISOU 1107  O  BILE A 135      387   2144   1879     31    142    -28       O  
ATOM   1108  CB AILE A 135      10.964  31.778  -7.496  0.50 11.24           C  
ANISOU 1108  CB AILE A 135      293   2418   1559   -230   -138    -31       C  
ATOM   1109  CB BILE A 135      10.945  31.834  -7.510  0.50 11.17           C  
ANISOU 1109  CB BILE A 135      268   2429   1544   -165    -58    -48       C  
ATOM   1110  CG1AILE A 135      10.822  33.273  -7.196  0.50 12.51           C  
ANISOU 1110  CG1AILE A 135      255   2739   1757     60    -21     73       C  
ATOM   1111  CG1BILE A 135      10.585  33.241  -7.006  0.50 14.44           C  
ANISOU 1111  CG1BILE A 135      705   2630   2149    180    -93     29       C  
ATOM   1112  CG2AILE A 135       9.599  31.056  -7.464  0.50 11.89           C  
ANISOU 1112  CG2AILE A 135      264   2201   2050    -26   -136    -98       C  
ATOM   1113  CG2BILE A 135       9.670  30.957  -7.737  0.50 11.02           C  
ANISOU 1113  CG2BILE A 135      255   2683   1247     61    -16     95       C  
ATOM   1114  CD1AILE A 135      12.032  34.102  -7.616  0.50 12.91           C  
ANISOU 1114  CD1AILE A 135      837   2170   1895   -527   -249    181       C  
ATOM   1115  CD1BILE A 135       9.806  34.111  -8.043  0.50 13.70           C  
ANISOU 1115  CD1BILE A 135      727   2665   1811     78    385   -113       C  
ATOM   1116  N   ARG A 136      11.514  31.986  -4.300  1.00 11.30           N  
ANISOU 1116  N   ARG A 136      297   2397   1599     33    242     13       N  
ATOM   1117  CA  ARG A 136      10.714  32.182  -3.100  1.00 10.68           C  
ANISOU 1117  CA  ARG A 136      259   2143   1653   -100    -32     46       C  
ATOM   1118  C   ARG A 136       9.668  33.219  -3.440  1.00 10.68           C  
ANISOU 1118  C   ARG A 136      266   2052   1739     98    106    -77       C  
ATOM   1119  O   ARG A 136       9.929  34.412  -3.437  1.00 11.14           O  
ANISOU 1119  O   ARG A 136      262   2327   1641     29    110    -47       O  
ATOM   1120  CB  ARG A 136      11.596  32.716  -1.952  1.00 12.09           C  
ANISOU 1120  CB  ARG A 136      279   2450   1864    195    105   -150       C  
ATOM   1121  CG  ARG A 136      12.831  31.866  -1.638  1.00 11.22           C  
ANISOU 1121  CG  ARG A 136      259   2267   1736     65     66   -246       C  
ATOM   1122  CD  ARG A 136      13.517  32.398  -0.415  1.00 13.98           C  
ANISOU 1122  CD  ARG A 136      523   2248   2539      1     32   -112       C  
ATOM   1123  NE  ARG A 136      14.789  31.743  -0.185  1.00 14.93           N  
ANISOU 1123  NE  ARG A 136      337   3102   2232    430    128    164       N  
ATOM   1124  CZ  ARG A 136      15.332  31.588   1.007  1.00 17.44           C  
ANISOU 1124  CZ  ARG A 136      839   3039   2747    192    479    432       C  
ATOM   1125  NH1 ARG A 136      14.698  32.019   2.091  1.00 16.31           N  
ANISOU 1125  NH1 ARG A 136      453   3245   2496     75   -658    253       N  
ATOM   1126  NH2 ARG A 136      16.522  31.023   1.113  1.00 16.79           N  
ANISOU 1126  NH2 ARG A 136      303   3711   2366    262   -251     40       N  
ATOM   1127  N   GLN A 137       8.450  32.762  -3.777  1.00 10.37           N  
ANISOU 1127  N   GLN A 137      283   2036   1621   -198    108    -60       N  
ATOM   1128  CA  GLN A 137       7.530  33.650  -4.475  1.00 10.09           C  
ANISOU 1128  CA  GLN A 137      277   1974   1579   -144    119     63       C  
ATOM   1129  C   GLN A 137       6.932  34.732  -3.580  1.00  9.78           C  
ANISOU 1129  C   GLN A 137      333   2066   1313   -376    -22   -102       C  
ATOM   1130  O   GLN A 137       6.647  35.823  -4.053  1.00 10.17           O  
ANISOU 1130  O   GLN A 137      264   2038   1560    -50    106    160       O  
ATOM   1131  CB  GLN A 137       6.405  32.861  -5.186  1.00 11.20           C  
ANISOU 1131  CB  GLN A 137      270   2126   1860   -178     12   -183       C  
ATOM   1132  CG  GLN A 137       5.314  32.250  -4.294  1.00 11.64           C  
ANISOU 1132  CG  GLN A 137      383   2324   1714   -495    -99   -129       C  
ATOM   1133  CD  GLN A 137       5.617  30.834  -3.844  1.00 12.63           C  
ANISOU 1133  CD  GLN A 137      648   2226   1925    168   -169    315       C  
ATOM   1134  OE1 GLN A 137       6.770  30.477  -3.557  1.00 13.26           O  
ANISOU 1134  OE1 GLN A 137      361   2439   2235     58   -294    137       O  
ATOM   1135  NE2 GLN A 137       4.572  30.022  -3.727  1.00 14.05           N  
ANISOU 1135  NE2 GLN A 137      417   2463   2459   -300   -200    313       N  
ATOM   1136  N   PHE A 138       6.834  34.485  -2.287  1.00  9.49           N  
ANISOU 1136  N   PHE A 138      266   1803   1534     31   -128     -5       N  
ATOM   1137  CA  PHE A 138       6.221  35.499  -1.420  1.00 10.08           C  
ANISOU 1137  CA  PHE A 138      280   2069   1480   -180   -108     -4       C  
ATOM   1138  C   PHE A 138       7.162  36.676  -1.094  1.00 10.15           C  
ANISOU 1138  C   PHE A 138      261   2120   1475   -118     35     36       C  
ATOM   1139  O   PHE A 138       6.795  37.827  -1.266  1.00 10.81           O  
ANISOU 1139  O   PHE A 138      298   2264   1542   -122    219      0       O  
ATOM   1140  CB  PHE A 138       5.595  34.859  -0.181  1.00 10.81           C  
ANISOU 1140  CB  PHE A 138      344   2119   1643   -408     52    -28       C  
ATOM   1141  CG  PHE A 138       4.371  34.050  -0.504  1.00  9.92           C  
ANISOU 1141  CG  PHE A 138      278   2075   1413     77    161     32       C  
ATOM   1142  CD1 PHE A 138       3.249  34.681  -0.971  1.00 10.39           C  
ANISOU 1142  CD1 PHE A 138      273   1819   1856    177     12    -10       C  
ATOM   1143  CD2 PHE A 138       4.382  32.701  -0.453  1.00 10.48           C  
ANISOU 1143  CD2 PHE A 138      262   2093   1624     42   -103    102       C  
ATOM   1144  CE1 PHE A 138       2.061  33.934  -1.310  1.00 12.76           C  
ANISOU 1144  CE1 PHE A 138      319   2565   1961   -348   -180    197       C  
ATOM   1145  CE2 PHE A 138       3.242  31.942  -0.796  1.00 10.69           C  
ANISOU 1145  CE2 PHE A 138      321   1856   1883   -214   -250    -19       C  
ATOM   1146  CZ  PHE A 138       2.075  32.592  -1.226  1.00 11.78           C  
ANISOU 1146  CZ  PHE A 138      282   2546   1645    -18   -199    -13       C  
ATOM   1147  N   PRO A 139       8.436  36.388  -0.735  1.00 10.59           N  
ANISOU 1147  N   PRO A 139      255   2003   1765    -35    -51    -19       N  
ATOM   1148  CA  PRO A 139       9.379  37.484  -0.740  1.00 10.90           C  
ANISOU 1148  CA  PRO A 139      570   1911   1661    184    -52    -48       C  
ATOM   1149  C   PRO A 139       9.369  38.275  -2.063  1.00 10.82           C  
ANISOU 1149  C   PRO A 139      263   2070   1775     48   -112     56       C  
ATOM   1150  O   PRO A 139       9.396  39.501  -2.056  1.00 10.64           O  
ANISOU 1150  O   PRO A 139      265   2184   1593    -14    127      3       O  
ATOM   1151  CB  PRO A 139      10.718  36.775  -0.500  1.00 11.19           C  
ANISOU 1151  CB  PRO A 139      360   2221   1670    165   -180     78       C  
ATOM   1152  CG  PRO A 139      10.343  35.610   0.353  1.00 11.68           C  
ANISOU 1152  CG  PRO A 139      459   2303   1674   -147   -529     23       C  
ATOM   1153  CD  PRO A 139       9.026  35.145  -0.216  1.00 10.26           C  
ANISOU 1153  CD  PRO A 139      295   2161   1440   -269    -69      1       C  
ATOM   1154  N   TYR A 140       9.325  37.569  -3.178  1.00 10.18           N  
ANISOU 1154  N   TYR A 140      253   1983   1629    -27    -15     59       N  
ATOM   1155  CA  TYR A 140       9.385  38.212  -4.451  1.00 10.40           C  
ANISOU 1155  CA  TYR A 140      256   1908   1786     25    -67    119       C  
ATOM   1156  C   TYR A 140       8.163  39.135  -4.691  1.00 10.02           C  
ANISOU 1156  C   TYR A 140      293   2007   1506   -132    193     -4       C  
ATOM   1157  O   TYR A 140       8.289  40.274  -5.112  1.00 10.42           O  
ANISOU 1157  O   TYR A 140      254   2118   1586     -6     33     42       O  
ATOM   1158  CB  TYR A 140       9.529  37.184  -5.582  1.00 10.90           C  
ANISOU 1158  CB  TYR A 140      289   2201   1651    266      9     13       C  
ATOM   1159  CG  TYR A 140       9.962  37.800  -6.885  1.00 10.30           C  
ANISOU 1159  CG  TYR A 140      276   2228   1407    -99    145    -10       C  
ATOM   1160  CD1 TYR A 140       9.036  38.325  -7.748  1.00 10.75           C  
ANISOU 1160  CD1 TYR A 140      262   2239   1581   -105    -75    120       C  
ATOM   1161  CD2 TYR A 140      11.329  37.915  -7.230  1.00 11.55           C  
ANISOU 1161  CD2 TYR A 140      299   2358   1731    -26    259    -32       C  
ATOM   1162  CE1 TYR A 140       9.398  38.909  -8.896  1.00 12.24           C  
ANISOU 1162  CE1 TYR A 140      334   2508   1808    -46   -354     76       C  
ATOM   1163  CE2 TYR A 140      11.692  38.505  -8.392  1.00 12.95           C  
ANISOU 1163  CE2 TYR A 140      522   2536   1859   -247   -120      4       C  
ATOM   1164  CZ  TYR A 140      10.735  39.010  -9.230  1.00 12.06           C  
ANISOU 1164  CZ  TYR A 140      355   2785   1442   -225    309     34       C  
ATOM   1165  OH  TYR A 140      11.032  39.624 -10.419  1.00 12.67           O  
ANISOU 1165  OH  TYR A 140      260   2681   1870   -102     67     35       O  
ATOM   1166  N   ILE A 141       6.953  38.610  -4.419  1.00 10.06           N  
ANISOU 1166  N   ILE A 141      304   2004   1512   -174    189    160       N  
ATOM   1167  CA  ILE A 141       5.711  39.404  -4.570  1.00 10.20           C  
ANISOU 1167  CA  ILE A 141      364   2069   1442    305   -268    -12       C  
ATOM   1168  C   ILE A 141       5.779  40.657  -3.708  1.00 10.46           C  
ANISOU 1168  C   ILE A 141      398   2138   1438   -240    362     45       C  
ATOM   1169  O   ILE A 141       5.475  41.763  -4.160  1.00 10.54           O  
ANISOU 1169  O   ILE A 141      265   2184   1555    -87     98     68       O  
ATOM   1170  CB  ILE A 141       4.456  38.576  -4.188  1.00 11.14           C  
ANISOU 1170  CB  ILE A 141      322   2134   1775   -332    -79   -159       C  
ATOM   1171  CG1 ILE A 141       4.172  37.513  -5.241  1.00 12.15           C  
ANISOU 1171  CG1 ILE A 141      322   2558   1736    391    -66    -31       C  
ATOM   1172  CG2 ILE A 141       3.228  39.488  -4.023  1.00 11.93           C  
ANISOU 1172  CG2 ILE A 141      318   2171   2042    343    -68     64       C  
ATOM   1173  CD1 ILE A 141       3.335  36.364  -4.720  1.00 15.64           C  
ANISOU 1173  CD1 ILE A 141     1064   2484   2392   -287   -324   -328       C  
ATOM   1174  N   LEU A 142       6.193  40.490  -2.458  1.00 10.56           N  
ANISOU 1174  N   LEU A 142      254   2051   1705    -35     10     84       N  
ATOM   1175  CA  LEU A 142       6.274  41.612  -1.565  1.00 10.81           C  
ANISOU 1175  CA  LEU A 142      253   2056   1795     -8     16    250       C  
ATOM   1176  C   LEU A 142       7.272  42.682  -2.107  1.00 11.08           C  
ANISOU 1176  C   LEU A 142      390   2199   1619   -135     90   -224       C  
ATOM   1177  O   LEU A 142       6.996  43.871  -2.057  1.00 11.17           O  
ANISOU 1177  O   LEU A 142      288   2045   1908   -239    -45   -215       O  
ATOM   1178  CB  LEU A 142       6.704  41.139  -0.178  1.00 10.86           C  
ANISOU 1178  CB  LEU A 142      260   1831   2033    100     19   -285       C  
ATOM   1179  CG  LEU A 142       5.602  40.374   0.591  1.00 10.92           C  
ANISOU 1179  CG  LEU A 142      287   2237   1625    -25    214    -24       C  
ATOM   1180  CD1 LEU A 142       6.215  39.870   1.887  1.00 13.51           C  
ANISOU 1180  CD1 LEU A 142      286   3209   1638    160    202    384       C  
ATOM   1181  CD2 LEU A 142       4.337  41.265   0.867  1.00 11.89           C  
ANISOU 1181  CD2 LEU A 142      351   2014   2151     24    430    152       C  
ATOM   1182  N   GLN A 143       8.425  42.249  -2.637  1.00 11.08           N  
ANISOU 1182  N   GLN A 143      420   2075   1714   -218     58     65       N  
ATOM   1183  CA  GLN A 143       9.343  43.202  -3.207  1.00 10.94           C  
ANISOU 1183  CA  GLN A 143      293   2111   1752    182    174    -69       C  
ATOM   1184  C   GLN A 143       8.794  43.895  -4.461  1.00 10.63           C  
ANISOU 1184  C   GLN A 143      288   2030   1721     34    217   -223       C  
ATOM   1185  O   GLN A 143       9.002  45.082  -4.658  1.00 11.74           O  
ANISOU 1185  O   GLN A 143      263   2184   2011    -81    -99   -223       O  
ATOM   1186  CB  GLN A 143      10.686  42.541  -3.510  1.00 11.69           C  
ANISOU 1186  CB  GLN A 143      266   2356   1816    -40    136     54       C  
ATOM   1187  CG  GLN A 143      11.782  43.523  -3.995  1.00 12.38           C  
ANISOU 1187  CG  GLN A 143      289   2504   1911   -197    190   -181       C  
ATOM   1188  CD  GLN A 143      12.248  44.459  -2.910  1.00 14.27           C  
ANISOU 1188  CD  GLN A 143      326   2946   2148   -309    258     64       C  
ATOM   1189  OE1 GLN A 143      12.047  44.215  -1.737  1.00 16.34           O  
ANISOU 1189  OE1 GLN A 143      578   3440   2189   -543    168   -197       O  
ATOM   1190  NE2 GLN A 143      13.010  45.465  -3.305  1.00 21.88           N  
ANISOU 1190  NE2 GLN A 143     1976   3276   3059   -858   -345   -129       N  
ATOM   1191  N   VAL A 144       8.080  43.147  -5.304  1.00 10.90           N  
ANISOU 1191  N   VAL A 144      332   1974   1835   -148    256    -55       N  
ATOM   1192  CA  VAL A 144       7.429  43.751  -6.467  1.00 10.66           C  
ANISOU 1192  CA  VAL A 144      379   2011   1658    281    223    122       C  
ATOM   1193  C   VAL A 144       6.422  44.848  -6.006  1.00 10.97           C  
ANISOU 1193  C   VAL A 144      276   2291   1600   -193    -92    118       C  
ATOM   1194  O   VAL A 144       6.381  45.940  -6.554  1.00 10.94           O  
ANISOU 1194  O   VAL A 144      254   2066   1837    -36     35     50       O  
ATOM   1195  CB  VAL A 144       6.706  42.675  -7.309  1.00 11.50           C  
ANISOU 1195  CB  VAL A 144      259   2444   1665     33    -88     -2       C  
ATOM   1196  CG1 VAL A 144       5.710  43.305  -8.313  1.00 12.63           C  
ANISOU 1196  CG1 VAL A 144      338   2389   2072    -28   -392     -4       C  
ATOM   1197  CG2 VAL A 144       7.706  41.797  -8.041  1.00 12.45           C  
ANISOU 1197  CG2 VAL A 144      326   2221   2180     51    366   -180       C  
ATOM   1198  N   LEU A 145       5.648  44.542  -4.963  1.00 10.67           N  
ANISOU 1198  N   LEU A 145      259   2084   1707   -105    -34    110       N  
ATOM   1199  CA  LEU A 145       4.669  45.511  -4.454  1.00 10.29           C  
ANISOU 1199  CA  LEU A 145      335   1770   1803   -107    265    -77       C  
ATOM   1200  C   LEU A 145       5.361  46.746  -3.847  1.00 11.23           C  
ANISOU 1200  C   LEU A 145      307   2122   1835   -166    207    210       C  
ATOM   1201  O   LEU A 145       4.902  47.884  -4.045  1.00 11.47           O  
ANISOU 1201  O   LEU A 145      263   1914   2180   -125    -31   -102       O  
ATOM   1202  CB  LEU A 145       3.747  44.842  -3.428  1.00 11.38           C  
ANISOU 1202  CB  LEU A 145      258   2139   1923    -45    -78   -115       C  
ATOM   1203  CG  LEU A 145       2.759  43.816  -4.008  1.00 11.23           C  
ANISOU 1203  CG  LEU A 145      275   2038   1952   -138   -131   -126       C  
ATOM   1204  CD1 LEU A 145       2.097  43.057  -2.881  1.00 13.06           C  
ANISOU 1204  CD1 LEU A 145      315   2703   1944     95    322    458       C  
ATOM   1205  CD2 LEU A 145       1.714  44.490  -4.904  1.00 14.22           C  
ANISOU 1205  CD2 LEU A 145      394   2512   2497   -240   -526    173       C  
ATOM   1206  N   LEU A 146       6.460  46.529  -3.108  1.00 11.95           N  
ANISOU 1206  N   LEU A 146      366   2162   2011   -194    -63   -100       N  
ATOM   1207  CA  LEU A 146       7.231  47.661  -2.559  1.00 11.30           C  
ANISOU 1207  CA  LEU A 146      267   2118   1909    117   -103     51       C  
ATOM   1208  C   LEU A 146       7.750  48.529  -3.691  1.00 11.77           C  
ANISOU 1208  C   LEU A 146      385   2088   2000    -96   -464   -105       C  
ATOM   1209  O   LEU A 146       7.667  49.748  -3.642  1.00 13.08           O  
ANISOU 1209  O   LEU A 146      292   2298   2378   -239   -143    -72       O  
ATOM   1210  CB  LEU A 146       8.410  47.177  -1.713  1.00 11.70           C  
ANISOU 1210  CB  LEU A 146      272   2099   2075    -61   -173    -40       C  
ATOM   1211  CG  LEU A 146       8.065  46.651  -0.320  1.00 15.48           C  
ANISOU 1211  CG  LEU A 146     1006   2609   2266     98   -233    -27       C  
ATOM   1212  CD1 LEU A 146       9.259  45.916   0.234  1.00 16.98           C  
ANISOU 1212  CD1 LEU A 146     1259   2873   2317     79   -275    -36       C  
ATOM   1213  CD2 LEU A 146       7.635  47.772   0.625  1.00 15.87           C  
ANISOU 1213  CD2 LEU A 146      279   2910   2840    141   -222   -107       C  
ATOM   1214  N   THR A 147       8.306  47.876  -4.705  1.00 11.93           N  
ANISOU 1214  N   THR A 147      357   2267   1907   -305   -280   -184       N  
ATOM   1215  CA  THR A 147       8.890  48.574  -5.845  1.00 12.04           C  
ANISOU 1215  CA  THR A 147      449   2249   1874   -131    -16     60       C  
ATOM   1216  C   THR A 147       7.822  49.326  -6.653  1.00 12.67           C  
ANISOU 1216  C   THR A 147      332   2313   2167   -402    -39     97       C  
ATOM   1217  O   THR A 147       8.041  50.450  -7.088  1.00 12.97           O  
ANISOU 1217  O   THR A 147      293   2392   2244   -245    139    108       O  
ATOM   1218  CB  THR A 147       9.684  47.603  -6.732  1.00 12.45           C  
ANISOU 1218  CB  THR A 147      404   2539   1786    -65   -278   -143       C  
ATOM   1219  OG1 THR A 147      10.689  46.977  -5.940  1.00 14.82           O  
ANISOU 1219  OG1 THR A 147      255   2993   2382     74      5    199       O  
ATOM   1220  CG2 THR A 147      10.355  48.323  -7.935  1.00 14.89           C  
ANISOU 1220  CG2 THR A 147      613   2797   2245   -206    439    183       C  
ATOM   1221  N   ALA A 148       6.620  48.740  -6.769  1.00 11.67           N  
ANISOU 1221  N   ALA A 148      281   2072   2080   -131    183     43       N  
ATOM   1222  CA  ALA A 148       5.492  49.451  -7.383  1.00 12.26           C  
ANISOU 1222  CA  ALA A 148      519   2074   2065    266    183    254       C  
ATOM   1223  C   ALA A 148       5.184  50.746  -6.613  1.00 12.34           C  
ANISOU 1223  C   ALA A 148      259   2130   2300   -106      7    121       C  
ATOM   1224  O   ALA A 148       5.110  51.824  -7.195  1.00 13.32           O  
ANISOU 1224  O   ALA A 148      273   2314   2472   -186   -101    200       O  
ATOM   1225  CB  ALA A 148       4.257  48.534  -7.446  1.00 13.38           C  
ANISOU 1225  CB  ALA A 148      399   2164   2518   -510    116    113       C  
ATOM   1226  N   ASP A 149       5.060  50.647  -5.294  1.00 13.38           N  
ANISOU 1226  N   ASP A 149      326   2420   2335   -256    197     12       N  
ATOM   1227  CA  ASP A 149       4.785  51.839  -4.487  1.00 13.84           C  
ANISOU 1227  CA  ASP A 149      762   2036   2460    -78    144    -16       C  
ATOM   1228  C   ASP A 149       5.901  52.884  -4.639  1.00 13.88           C  
ANISOU 1228  C   ASP A 149      502   2218   2550      9    269   -128       C  
ATOM   1229  O   ASP A 149       5.637  54.078  -4.725  1.00 15.25           O  
ANISOU 1229  O   ASP A 149      451   2459   2884   -108    125    -94       O  
ATOM   1230  CB  ASP A 149       4.618  51.474  -3.012  1.00 13.93           C  
ANISOU 1230  CB  ASP A 149      499   2226   2568   -138     49   -148       C  
ATOM   1231  CG  ASP A 149       3.265  50.906  -2.700  1.00 19.25           C  
ANISOU 1231  CG  ASP A 149     1417   3011   2886    -25   -641    184       C  
ATOM   1232  OD1 ASP A 149       2.358  51.007  -3.563  1.00 19.34           O  
ANISOU 1232  OD1 ASP A 149      265   3632   3450   -152    117    311       O  
ATOM   1233  OD2 ASP A 149       3.085  50.373  -1.581  1.00 19.56           O  
ANISOU 1233  OD2 ASP A 149      800   3375   3255   -208    281     41       O  
ATOM   1234  N   ASN A 150       7.143  52.420  -4.680  1.00 13.92           N  
ANISOU 1234  N   ASN A 150      349   2189   2750   -111    296    -20       N  
ATOM   1235  CA  ASN A 150       8.292  53.321  -4.803  1.00 14.78           C  
ANISOU 1235  CA  ASN A 150      611   2339   2664   -503     38    -89       C  
ATOM   1236  C   ASN A 150       8.277  54.074  -6.128  1.00 14.79           C  
ANISOU 1236  C   ASN A 150      444   2389   2787   -599    249    -33       C  
ATOM   1237  O   ASN A 150       8.866  55.152  -6.251  1.00 17.37           O  
ANISOU 1237  O   ASN A 150      973   2550   3074   -761    261    -32       O  
ATOM   1238  CB  ASN A 150       9.606  52.541  -4.632  1.00 15.62           C  
ANISOU 1238  CB  ASN A 150      511   2705   2718   -345   -151    -70       C  
ATOM   1239  CG  ASN A 150       9.834  52.102  -3.205  1.00 18.59           C  
ANISOU 1239  CG  ASN A 150      968   2646   3449   -548    163   -127       C  
ATOM   1240  OD1 ASN A 150       9.237  52.645  -2.283  1.00 24.36           O  
ANISOU 1240  OD1 ASN A 150     2009   3828   3418   -517   -570   -456       O  
ATOM   1241  ND2 ASN A 150      10.689  51.107  -3.017  1.00 20.29           N  
ANISOU 1241  ND2 ASN A 150      989   2754   3962   -953  -1189     35       N  
ATOM   1242  N   ASN A 151       7.628  53.479  -7.125  1.00 15.29           N  
ANISOU 1242  N   ASN A 151      678   2382   2746   -418    -33    143       N  
ATOM   1243  CA  ASN A 151       7.512  54.053  -8.433  1.00 15.66           C  
ANISOU 1243  CA  ASN A 151      851   2248   2851   -196    166    162       C  
ATOM   1244  C   ASN A 151       6.097  54.593  -8.708  1.00 17.06           C  
ANISOU 1244  C   ASN A 151     1091   2555   2833   -326   -148    284       C  
ATOM   1245  O   ASN A 151       5.726  54.845  -9.861  1.00 18.15           O  
ANISOU 1245  O   ASN A 151     1104   2616   3177   -339    -13    459       O  
ATOM   1246  CB  ASN A 151       7.897  53.014  -9.483  1.00 17.14           C  
ANISOU 1246  CB  ASN A 151     1313   2449   2748    -97     58    304       C  
ATOM   1247  CG  ASN A 151       9.374  52.813  -9.567  1.00 19.11           C  
ANISOU 1247  CG  ASN A 151     1695   2296   3270   -301    266    216       C  
ATOM   1248  OD1 ASN A 151      10.061  53.568 -10.244  1.00 22.12           O  
ANISOU 1248  OD1 ASN A 151     1190   2981   4234    -85   1392   1223       O  
ATOM   1249  ND2 ASN A 151       9.892  51.846  -8.834  1.00 18.16           N  
ANISOU 1249  ND2 ASN A 151     1643   2372   2882   -597    712     69       N  
ATOM   1250  N   ASN A 152       5.319  54.761  -7.642  1.00 16.12           N  
ANISOU 1250  N   ASN A 152      739   2557   2826    -47   -330    122       N  
ATOM   1251  CA  ASN A 152       4.033  55.437  -7.716  1.00 17.75           C  
ANISOU 1251  CA  ASN A 152     1146   2527   3071     16   -276    263       C  
ATOM   1252  C   ASN A 152       3.052  54.792  -8.690  1.00 18.18           C  
ANISOU 1252  C   ASN A 152      664   2887   3354    364    120     59       C  
ATOM   1253  O   ASN A 152       2.268  55.487  -9.351  1.00 20.32           O  
ANISOU 1253  O   ASN A 152      806   2758   4154   -158   -354    546       O  
ATOM   1254  CB  ASN A 152       4.250  56.913  -8.033  1.00 19.15           C  
ANISOU 1254  CB  ASN A 152      554   3233   3488     84   -153    -81       C  
ATOM   1255  CG  ASN A 152       5.086  57.612  -6.958  1.00 20.92           C  
ANISOU 1255  CG  ASN A 152     1133   3223   3590   -156   -628    289       C  
ATOM   1256  OD1 ASN A 152       4.747  57.563  -5.780  1.00 27.78           O  
ANISOU 1256  OD1 ASN A 152     2894   3668   3993   -327    496   -282       O  
ATOM   1257  ND2 ASN A 152       6.217  58.216  -7.360  1.00 25.69           N  
ANISOU 1257  ND2 ASN A 152     2316   2997   4444   -868    270   -439       N  
ATOM   1258  N   ILE A 153       3.028  53.458  -8.715  1.00 15.24           N  
ANISOU 1258  N   ILE A 153      292   2654   2841     98     66    384       N  
ATOM   1259  CA  ILE A 153       1.947  52.735  -9.384  1.00 14.65           C  
ANISOU 1259  CA  ILE A 153      408   2697   2461      5   -189    287       C  
ATOM   1260  C   ILE A 153       1.387  51.661  -8.468  1.00 13.36           C  
ANISOU 1260  C   ILE A 153      290   2478   2307    120   -239    226       C  
ATOM   1261  O   ILE A 153       2.018  51.295  -7.456  1.00 15.41           O  
ANISOU 1261  O   ILE A 153      514   2846   2494   -100     62    292       O  
ATOM   1262  CB  ILE A 153       2.377  52.104 -10.735  1.00 15.59           C  
ANISOU 1262  CB  ILE A 153      280   2781   2859     68   -251    136       C  
ATOM   1263  CG1 ILE A 153       3.398  50.983 -10.515  1.00 15.58           C  
ANISOU 1263  CG1 ILE A 153      257   3170   2493    -39    -88    190       C  
ATOM   1264  CG2 ILE A 153       2.935  53.178 -11.675  1.00 19.85           C  
ANISOU 1264  CG2 ILE A 153     1516   3081   2944   -831    -21    566       C  
ATOM   1265  CD1 ILE A 153       3.567  50.077 -11.703  1.00 16.54           C  
ANISOU 1265  CD1 ILE A 153      754   3063   2465   -199     14    292       C  
ATOM   1266  N   GLN A 154       0.180  51.199  -8.785  1.00 15.51           N  
ANISOU 1266  N   GLN A 154      337   2792   2763   -220   -407     45       N  
ATOM   1267  CA  GLN A 154      -0.410  50.110  -8.051  1.00 14.66           C  
ANISOU 1267  CA  GLN A 154      357   2724   2488     28    175     17       C  
ATOM   1268  C   GLN A 154      -0.763  48.984  -9.009  1.00 12.93           C  
ANISOU 1268  C   GLN A 154      285   2440   2188   -214    167   -217       C  
ATOM   1269  O   GLN A 154      -0.999  49.224 -10.184  1.00 15.78           O  
ANISOU 1269  O   GLN A 154      993   2561   2441     -8    -80    -25       O  
ATOM   1270  CB  GLN A 154      -1.651  50.598  -7.316  1.00 19.66           C  
ANISOU 1270  CB  GLN A 154     1127   2977   3363   -556    337   -247       C  
ATOM   1271  CG  GLN A 154      -1.327  51.650  -6.264  1.00 24.29           C  
ANISOU 1271  CG  GLN A 154     1774   3771   3682   -388    675   -600       C  
ATOM   1272  CD  GLN A 154      -2.537  52.326  -5.729  1.00 27.11           C  
ANISOU 1272  CD  GLN A 154     2588   3380   4332   -284    506   -480       C  
ATOM   1273  OE1 GLN A 154      -3.317  52.915  -6.479  1.00 29.86           O  
ANISOU 1273  OE1 GLN A 154     2680   4050   4612    -45   1045     -8       O  
ATOM   1274  NE2 GLN A 154      -2.702  52.281  -4.414  1.00 32.92           N  
ANISOU 1274  NE2 GLN A 154     3072   4739   4697   -296    628   -325       N  
ATOM   1275  N   LEU A 155      -0.715  47.762  -8.509  1.00 13.66           N  
ANISOU 1275  N   LEU A 155      294   2583   2312   -122    266     40       N  
ATOM   1276  CA  LEU A 155      -0.880  46.575  -9.331  1.00 12.41           C  
ANISOU 1276  CA  LEU A 155      364   2435   1914    108    423     77       C  
ATOM   1277  C   LEU A 155      -2.193  45.871  -9.057  1.00 13.45           C  
ANISOU 1277  C   LEU A 155      556   2526   2025   -147    422     98       C  
ATOM   1278  O   LEU A 155      -2.663  45.815  -7.921  1.00 12.96           O  
ANISOU 1278  O   LEU A 155      270   2675   1979    -60    160     79       O  
ATOM   1279  CB  LEU A 155       0.256  45.585  -9.060  1.00 12.25           C  
ANISOU 1279  CB  LEU A 155      290   2455   1908   -174    193     22       C  
ATOM   1280  CG  LEU A 155       1.672  46.119  -9.252  1.00 14.09           C  
ANISOU 1280  CG  LEU A 155      292   2377   2682   -197    208    173       C  
ATOM   1281  CD1 LEU A 155       2.631  44.997  -9.048  1.00 18.57           C  
ANISOU 1281  CD1 LEU A 155      453   3365   3238     89    -10    610       C  
ATOM   1282  CD2 LEU A 155       1.791  46.709 -10.618  1.00 15.73           C  
ANISOU 1282  CD2 LEU A 155      325   3095   2554    -15    401    340       C  
ATOM   1283  N   SER A 156      -2.736  45.275 -10.099  1.00 12.97           N  
ANISOU 1283  N   SER A 156      356   2497   2071     87    247     43       N  
ATOM   1284  CA  SER A 156      -3.918  44.443  -9.981  1.00 12.40           C  
ANISOU 1284  CA  SER A 156      377   2319   2015   -133     46   -141       C  
ATOM   1285  C   SER A 156      -3.517  42.994  -9.789  1.00 12.44           C  
ANISOU 1285  C   SER A 156      323   2196   2207    127    331     98       C  
ATOM   1286  O   SER A 156      -2.353  42.612 -10.000  1.00 12.34           O  
ANISOU 1286  O   SER A 156      289   2383   2015    226    142    -42       O  
ATOM   1287  CB  SER A 156      -4.766  44.558 -11.239  1.00 13.99           C  
ANISOU 1287  CB  SER A 156      377   2486   2453   -102    272     33       C  
ATOM   1288  OG  SER A 156      -4.107  43.911 -12.325  1.00 14.57           O  
ANISOU 1288  OG  SER A 156      302   2752   2482    347    -56    -80       O  
ATOM   1289  N  ALYS A 157      -4.482  42.167  -9.435  0.50 13.01           N  
ANISOU 1289  N  ALYS A 157      380   2378   2184    -26    206    -12       N  
ATOM   1290  N  BLYS A 157      -4.488  42.169  -9.447  0.50 12.92           N  
ANISOU 1290  N  BLYS A 157      382   2347   2179    -17    208    -23       N  
ATOM   1291  CA ALYS A 157      -4.263  40.739  -9.343  0.50 13.04           C  
ANISOU 1291  CA ALYS A 157      262   2562   2128   -134     44     75       C  
ATOM   1292  CA BLYS A 157      -4.276  40.744  -9.343  0.50 13.01           C  
ANISOU 1292  CA BLYS A 157      263   2550   2129   -150     15     69       C  
ATOM   1293  C  ALYS A 157      -3.843  40.164 -10.689  0.50 13.02           C  
ANISOU 1293  C  ALYS A 157      679   2159   2108    -78   -233    200       C  
ATOM   1294  C  BLYS A 157      -3.852  40.161 -10.686  0.50 13.03           C  
ANISOU 1294  C  BLYS A 157      686   2147   2114    -62   -245    198       C  
ATOM   1295  O  ALYS A 157      -3.052  39.225 -10.746  0.50 13.14           O  
ANISOU 1295  O  ALYS A 157      298   2457   2237   -187    233     80       O  
ATOM   1296  O  BLYS A 157      -3.063  39.220 -10.737  0.50 13.11           O  
ANISOU 1296  O  BLYS A 157      297   2449   2232   -186    231     79       O  
ATOM   1297  CB ALYS A 157      -5.537  40.045  -8.845  0.50 16.71           C  
ANISOU 1297  CB ALYS A 157     1002   2865   2481   -164    505    200       C  
ATOM   1298  CB BLYS A 157      -5.559  40.058  -8.839  0.50 17.25           C  
ANISOU 1298  CB BLYS A 157     1240   2755   2557   -189    402    221       C  
ATOM   1299  CG ALYS A 157      -5.456  38.536  -8.831  0.50 21.02           C  
ANISOU 1299  CG ALYS A 157     1771   3235   2978   -372    372    161       C  
ATOM   1300  CG BLYS A 157      -5.990  40.499  -7.437  0.50 21.82           C  
ANISOU 1300  CG BLYS A 157     2320   3162   2807   -316    231     42       C  
ATOM   1301  CD ALYS A 157      -6.651  37.934  -8.103  0.50 24.91           C  
ANISOU 1301  CD ALYS A 157     2620   3601   3243   -580    692    336       C  
ATOM   1302  CD BLYS A 157      -7.211  41.443  -7.462  0.50 29.03           C  
ANISOU 1302  CD BLYS A 157     3724   3784   3519     -8   -193    198       C  
ATOM   1303  CE ALYS A 157      -7.946  38.618  -8.507  0.50 26.12           C  
ANISOU 1303  CE ALYS A 157     2740   3944   3240   -153    241    253       C  
ATOM   1304  CE BLYS A 157      -6.815  42.896  -7.723  0.50 18.82           C  
ANISOU 1304  CE BLYS A 157     1518   2826   2806    598    -61    -59       C  
ATOM   1305  NZ ALYS A 157      -8.691  37.846  -9.540  0.50 28.75           N  
ANISOU 1305  NZ ALYS A 157     1937   4856   4129   -512    107   -155       N  
ATOM   1306  NZ BLYS A 157      -7.112  43.331  -9.126  0.50 21.59           N  
ANISOU 1306  NZ BLYS A 157     1432   3671   3097    276    718    291       N  
ATOM   1307  N   ASP A 158      -4.406  40.692 -11.773  1.00 12.31           N  
ANISOU 1307  N   ASP A 158      268   2340   2069   -128   -109    -42       N  
ATOM   1308  CA  ASP A 158      -4.047  40.233 -13.115  1.00 12.20           C  
ANISOU 1308  CA  ASP A 158      279   2173   2183    -74   -215     68       C  
ATOM   1309  C   ASP A 158      -2.592  40.584 -13.459  1.00 12.22           C  
ANISOU 1309  C   ASP A 158      370   2135   2137    -89    -84     47       C  
ATOM   1310  O   ASP A 158      -1.916  39.808 -14.132  1.00 12.81           O  
ANISOU 1310  O   ASP A 158      334   2404   2126   -154   -369     89       O  
ATOM   1311  CB  ASP A 158      -5.028  40.826 -14.181  1.00 12.96           C  
ANISOU 1311  CB  ASP A 158      322   2424   2175      1   -363   -106       C  
ATOM   1312  CG  ASP A 158      -6.441  40.209 -14.114  1.00 17.01           C  
ANISOU 1312  CG  ASP A 158      342   3058   3061     44   -449    203       C  
ATOM   1313  OD1 ASP A 158      -6.553  38.992 -13.834  1.00 19.41           O  
ANISOU 1313  OD1 ASP A 158      396   3088   3889   -514   -480    306       O  
ATOM   1314  OD2 ASP A 158      -7.430  40.947 -14.387  1.00 27.65           O  
ANISOU 1314  OD2 ASP A 158     2016   3063   5426    302   -230    284       O  
ATOM   1315  N   ASP A 159      -2.140  41.742 -13.017  1.00 11.77           N  
ANISOU 1315  N   ASP A 159      272   2141   2058     -5    187     99       N  
ATOM   1316  CA  ASP A 159      -0.730  42.130 -13.204  1.00 11.29           C  
ANISOU 1316  CA  ASP A 159      290   2429   1568   -263     54    214       C  
ATOM   1317  C   ASP A 159       0.178  41.127 -12.504  1.00 11.60           C  
ANISOU 1317  C   ASP A 159      720   2202   1485   -192    -50    -68       C  
ATOM   1318  O   ASP A 159       1.145  40.639 -13.092  1.00 12.06           O  
ANISOU 1318  O   ASP A 159      277   2577   1725      7    189   -114       O  
ATOM   1319  CB  ASP A 159      -0.468  43.504 -12.613  1.00 12.84           C  
ANISOU 1319  CB  ASP A 159      584   2221   2073   -145    143    148       C  
ATOM   1320  CG  ASP A 159      -1.112  44.630 -13.399  1.00 14.65           C  
ANISOU 1320  CG  ASP A 159      776   2491   2297   -497    307    -11       C  
ATOM   1321  OD1 ASP A 159      -1.266  44.499 -14.639  1.00 16.58           O  
ANISOU 1321  OD1 ASP A 159     1013   3070   2213    -32    200     66       O  
ATOM   1322  OD2 ASP A 159      -1.383  45.702 -12.774  1.00 14.65           O  
ANISOU 1322  OD2 ASP A 159      547   2687   2329   -178     79     -7       O  
ATOM   1323  N  AILE A 160      -0.144  40.802 -11.261  0.50 10.43           N  
ANISOU 1323  N  AILE A 160      258   2136   1569    -91     19    106       N  
ATOM   1324  N  BILE A 160      -0.122  40.824 -11.245  0.50 10.66           N  
ANISOU 1324  N  BILE A 160      258   2190   1600    -94     23    104       N  
ATOM   1325  CA AILE A 160       0.678  39.872 -10.504  0.50 10.75           C  
ANISOU 1325  CA AILE A 160      276   2238   1570    -23   -173     67       C  
ATOM   1326  CA BILE A 160       0.674  39.841 -10.516  0.50 11.00           C  
ANISOU 1326  CA BILE A 160      267   2285   1626    -21   -138    116       C  
ATOM   1327  C  AILE A 160       0.608  38.461 -11.110  0.50 11.24           C  
ANISOU 1327  C  AILE A 160      636   1996   1636    103    -94    -99       C  
ATOM   1328  C  BILE A 160       0.633  38.508 -11.241  0.50 11.71           C  
ANISOU 1328  C  BILE A 160      744   1879   1826     -1   -188     58       C  
ATOM   1329  O  AILE A 160       1.597  37.721 -11.113  0.50 10.24           O  
ANISOU 1329  O  AILE A 160      254   2038   1598     -2     36    112       O  
ATOM   1330  O  BILE A 160       1.642  37.869 -11.442  0.50  9.67           O  
ANISOU 1330  O  BILE A 160      273   2105   1296    -17    144     62       O  
ATOM   1331  CB AILE A 160       0.276  39.848  -9.028  0.50 10.63           C  
ANISOU 1331  CB AILE A 160      262   2175   1602    -35   -106     27       C  
ATOM   1332  CB BILE A 160       0.182  39.656  -9.084  0.50 11.53           C  
ANISOU 1332  CB BILE A 160      304   2347   1727     67   -153    214       C  
ATOM   1333  CG1AILE A 160       0.468  41.236  -8.403  0.50 12.40           C  
ANISOU 1333  CG1AILE A 160      422   2382   1907   -107    -53    -22       C  
ATOM   1334  CG1BILE A 160       0.441  40.923  -8.262  0.50 14.51           C  
ANISOU 1334  CG1BILE A 160      530   2469   2512    146     -3    108       C  
ATOM   1335  CG2AILE A 160       1.086  38.816  -8.268  0.50 12.31           C  
ANISOU 1335  CG2AILE A 160      883   2006   1785     16   -131   -139       C  
ATOM   1336  CG2BILE A 160       0.848  38.429  -8.437  0.50 11.88           C  
ANISOU 1336  CG2BILE A 160      262   2566   1687    139    -27    -29       C  
ATOM   1337  CD1AILE A 160      -0.164  41.373  -7.010  0.50 10.97           C  
ANISOU 1337  CD1AILE A 160      390   2246   1529   -198   -108   -343       C  
ATOM   1338  CD1BILE A 160       1.896  41.257  -8.076  0.50 19.75           C  
ANISOU 1338  CD1BILE A 160     1794   2676   3031    -63   -139   -196       C  
ATOM   1339  N   ALA A 161      -0.541  38.110 -11.677  1.00 11.31           N  
ANISOU 1339  N   ALA A 161      279   2250   1767   -176   -114   -113       N  
ATOM   1340  CA  ALA A 161      -0.692  36.839 -12.343  1.00 10.69           C  
ANISOU 1340  CA  ALA A 161      281   2195   1582   -188   -136    232       C  
ATOM   1341  C   ALA A 161       0.203  36.730 -13.571  1.00 10.99           C  
ANISOU 1341  C   ALA A 161      414   2105   1655   -268   -414      0       C  
ATOM   1342  O   ALA A 161       0.943  35.771 -13.708  1.00 12.02           O  
ANISOU 1342  O   ALA A 161      421   2296   1848     69    -67     76       O  
ATOM   1343  CB  ALA A 161      -2.182  36.610 -12.741  1.00 12.31           C  
ANISOU 1343  CB  ALA A 161      406   2209   2062   -320   -462    230       C  
ATOM   1344  N   TYR A 162       0.084  37.683 -14.490  1.00 11.00           N  
ANISOU 1344  N   TYR A 162      378   2074   1728    -63   -110    103       N  
ATOM   1345  CA  TYR A 162       0.736  37.562 -15.797  1.00 10.94           C  
ANISOU 1345  CA  TYR A 162      322   2271   1563   -364    -66      3       C  
ATOM   1346  C   TYR A 162       2.214  37.840 -15.694  1.00 10.21           C  
ANISOU 1346  C   TYR A 162      266   2120   1492    -74   -110    -93       C  
ATOM   1347  O   TYR A 162       3.024  37.141 -16.295  1.00 11.73           O  
ANISOU 1347  O   TYR A 162      531   2328   1595    -30    -65    -43       O  
ATOM   1348  CB  TYR A 162       0.115  38.544 -16.790  1.00 12.10           C  
ANISOU 1348  CB  TYR A 162      482   2504   1609    -62   -210     93       C  
ATOM   1349  CG  TYR A 162       0.701  38.451 -18.182  1.00 12.61           C  
ANISOU 1349  CG  TYR A 162      524   2635   1630     15   -609    102       C  
ATOM   1350  CD1 TYR A 162       0.279  37.473 -19.067  1.00 14.42           C  
ANISOU 1350  CD1 TYR A 162     1006   2559   1913   -121   -363    -44       C  
ATOM   1351  CD2 TYR A 162       1.735  39.300 -18.579  1.00 14.66           C  
ANISOU 1351  CD2 TYR A 162      996   2530   2044   -216    243   -289       C  
ATOM   1352  CE1 TYR A 162       0.847  37.354 -20.322  1.00 15.71           C  
ANISOU 1352  CE1 TYR A 162     1854   2520   1593     47   -205     10       C  
ATOM   1353  CE2 TYR A 162       2.312  39.195 -19.840  1.00 15.04           C  
ANISOU 1353  CE2 TYR A 162     1223   2700   1789      8      1    108       C  
ATOM   1354  CZ  TYR A 162       1.863  38.221 -20.708  1.00 17.45           C  
ANISOU 1354  CZ  TYR A 162     2028   2700   1902     13   -186    114       C  
ATOM   1355  OH  TYR A 162       2.422  38.120 -21.970  1.00 20.70           O  
ANISOU 1355  OH  TYR A 162     2639   3514   1712    133    111    114       O  
ATOM   1356  N   TYR A 163       2.551  38.894 -14.973  1.00 10.45           N  
ANISOU 1356  N   TYR A 163      261   2193   1516   -112     43      5       N  
ATOM   1357  CA  TYR A 163       3.939  39.372 -14.975  1.00 10.71           C  
ANISOU 1357  CA  TYR A 163      278   2385   1404   -184     92    124       C  
ATOM   1358  C   TYR A 163       4.823  38.669 -13.950  1.00 12.54           C  
ANISOU 1358  C   TYR A 163      863   2480   1420      2    107    111       C  
ATOM   1359  O   TYR A 163       6.059  38.689 -14.081  1.00 12.62           O  
ANISOU 1359  O   TYR A 163      264   2692   1838    -70    110    226       O  
ATOM   1360  CB  TYR A 163       3.995  40.881 -14.771  1.00 11.12           C  
ANISOU 1360  CB  TYR A 163      323   2301   1600   -376     25    110       C  
ATOM   1361  CG  TYR A 163       3.404  41.698 -15.903  1.00 11.58           C  
ANISOU 1361  CG  TYR A 163      372   2210   1818   -306    286    273       C  
ATOM   1362  CD1 TYR A 163       4.150  42.005 -17.026  1.00 13.75           C  
ANISOU 1362  CD1 TYR A 163      638   2592   1993   -340   -133    259       C  
ATOM   1363  CD2 TYR A 163       2.099  42.176 -15.835  1.00 12.11           C  
ANISOU 1363  CD2 TYR A 163      262   2526   1810    -63    101    217       C  
ATOM   1364  CE1 TYR A 163       3.627  42.766 -18.057  1.00 13.43           C  
ANISOU 1364  CE1 TYR A 163      463   2717   1923   -259    154    274       C  
ATOM   1365  CE2 TYR A 163       1.562  42.926 -16.864  1.00 14.30           C  
ANISOU 1365  CE2 TYR A 163      715   2699   2018   -109    290    179       C  
ATOM   1366  CZ  TYR A 163       2.339  43.238 -17.959  1.00 13.33           C  
ANISOU 1366  CZ  TYR A 163      495   2597   1970     -5     31    352       C  
ATOM   1367  OH  TYR A 163       1.784  43.995 -18.968  1.00 16.57           O  
ANISOU 1367  OH  TYR A 163     1264   2916   2112     11   -140    470       O  
ATOM   1368  N   VAL A 164       4.225  38.052 -12.936  1.00 10.54           N  
ANISOU 1368  N   VAL A 164      254   2398   1353      0     35    -17       N  
ATOM   1369  CA  VAL A 164       4.978  37.433 -11.838  1.00 10.88           C  
ANISOU 1369  CA  VAL A 164      261   2418   1453    -17     97    146       C  
ATOM   1370  C   VAL A 164       4.677  35.942 -11.686  1.00 10.22           C  
ANISOU 1370  C   VAL A 164      265   2192   1423      1    118   -240       C  
ATOM   1371  O   VAL A 164       5.506  35.106 -12.055  1.00 10.85           O  
ANISOU 1371  O   VAL A 164      263   2265   1591    -51    113    -81       O  
ATOM   1372  CB  VAL A 164       4.740  38.171 -10.511  1.00 10.82           C  
ANISOU 1372  CB  VAL A 164      269   2517   1325   -190      7    162       C  
ATOM   1373  CG1 VAL A 164       5.485  37.502  -9.355  1.00 11.59           C  
ANISOU 1373  CG1 VAL A 164      266   2484   1652    -76    121     29       C  
ATOM   1374  CG2 VAL A 164       5.101  39.635 -10.649  1.00 12.55           C  
ANISOU 1374  CG2 VAL A 164      277   2488   2001   -170    140    -25       C  
ATOM   1375  N   LEU A 165       3.440  35.580 -11.274  1.00  9.90           N  
ANISOU 1375  N   LEU A 165      262   2133   1364    -88    -77     44       N  
ATOM   1376  CA  LEU A 165       3.211  34.212 -10.816  1.00 10.29           C  
ANISOU 1376  CA  LEU A 165      256   2358   1295     18     55   -193       C  
ATOM   1377  C   LEU A 165       2.985  33.195 -11.939  1.00 10.76           C  
ANISOU 1377  C   LEU A 165      332   2290   1464     28    309    136       C  
ATOM   1378  O   LEU A 165       3.026  31.987 -11.692  1.00 10.97           O  
ANISOU 1378  O   LEU A 165      489   2198   1481    -66    -40    -15       O  
ATOM   1379  CB  LEU A 165       2.087  34.144  -9.799  1.00 10.21           C  
ANISOU 1379  CB  LEU A 165      322   2103   1452    192    248     46       C  
ATOM   1380  CG  LEU A 165       2.467  34.625  -8.397  1.00 10.79           C  
ANISOU 1380  CG  LEU A 165      261   2392   1447     -3     96   -233       C  
ATOM   1381  CD1 LEU A 165       1.221  34.645  -7.521  1.00 11.93           C  
ANISOU 1381  CD1 LEU A 165      327   2743   1460     58    286   -279       C  
ATOM   1382  CD2 LEU A 165       3.558  33.745  -7.743  1.00 13.11           C  
ANISOU 1382  CD2 LEU A 165      379   2734   1867    376   -347    -91       C  
ATOM   1383  N   ASN A 166       2.785  33.682 -13.171  1.00  9.98           N  
ANISOU 1383  N   ASN A 166      258   2197   1335    -97     11     71       N  
ATOM   1384  CA  ASN A 166       2.717  32.824 -14.346  1.00 10.33           C  
ANISOU 1384  CA  ASN A 166      273   2219   1431    -79   -140    -12       C  
ATOM   1385  C   ASN A 166       3.825  33.126 -15.369  1.00 11.03           C  
ANISOU 1385  C   ASN A 166      751   2052   1388   -119      1   -147       C  
ATOM   1386  O   ASN A 166       3.783  32.634 -16.469  1.00 11.38           O  
ANISOU 1386  O   ASN A 166      286   2481   1554   -270    -10   -128       O  
ATOM   1387  CB  ASN A 166       1.369  32.991 -15.045  1.00 11.02           C  
ANISOU 1387  CB  ASN A 166      398   2297   1491   -266   -360    -72       C  
ATOM   1388  CG  ASN A 166       0.835  31.672 -15.658  1.00 10.66           C  
ANISOU 1388  CG  ASN A 166      265   2365   1420      0    118     79       C  
ATOM   1389  OD1 ASN A 166       0.492  30.737 -14.937  1.00 11.26           O  
ANISOU 1389  OD1 ASN A 166      333   2491   1452    -49     16    109       O  
ATOM   1390  ND2 ASN A 166       0.760  31.619 -16.990  1.00 11.71           N  
ANISOU 1390  ND2 ASN A 166      509   2543   1394    -55   -216     31       N  
ATOM   1391  N   SER A 167       4.793  33.963 -14.991  1.00 10.53           N  
ANISOU 1391  N   SER A 167      260   2272   1466    -50     88   -136       N  
ATOM   1392  CA  SER A 167       5.920  34.298 -15.873  1.00 11.05           C  
ANISOU 1392  CA  SER A 167      281   2379   1538      1    188   -114       C  
ATOM   1393  C   SER A 167       7.057  33.292 -15.684  1.00 12.20           C  
ANISOU 1393  C   SER A 167      689   2305   1641   -161    579   -184       C  
ATOM   1394  O   SER A 167       7.615  33.181 -14.600  1.00 11.67           O  
ANISOU 1394  O   SER A 167      268   2662   1503     45    132    -91       O  
ATOM   1395  CB  SER A 167       6.438  35.712 -15.579  1.00 11.55           C  
ANISOU 1395  CB  SER A 167      278   2245   1865   -102    177     71       C  
ATOM   1396  OG  SER A 167       7.787  35.913 -16.097  1.00 12.93           O  
ANISOU 1396  OG  SER A 167      297   2690   1925   -149    246    -63       O  
ATOM   1397  N   LEU A 168       7.372  32.549 -16.735  1.00 12.19           N  
ANISOU 1397  N   LEU A 168      497   2448   1684    -23    263    -98       N  
ATOM   1398  CA  LEU A 168       8.442  31.572 -16.657  1.00 12.68           C  
ANISOU 1398  CA  LEU A 168      743   2315   1757     36    307    -74       C  
ATOM   1399  C   LEU A 168       9.751  32.204 -16.177  1.00 12.61           C  
ANISOU 1399  C   LEU A 168      847   2274   1667     -2    495    144       C  
ATOM   1400  O   LEU A 168      10.430  31.654 -15.304  1.00 12.17           O  
ANISOU 1400  O   LEU A 168      276   2528   1818    -63    183      4       O  
ATOM   1401  CB  LEU A 168       8.643  30.893 -18.003  1.00 12.98           C  
ANISOU 1401  CB  LEU A 168      383   2623   1927      0    346    -60       C  
ATOM   1402  CG  LEU A 168       9.802  29.900 -18.051  1.00 15.10           C  
ANISOU 1402  CG  LEU A 168      534   2898   2305    -71    494   -341       C  
ATOM   1403  CD1 LEU A 168       9.544  28.696 -17.128  1.00 17.38           C  
ANISOU 1403  CD1 LEU A 168      959   2607   3037    178    378   -162       C  
ATOM   1404  CD2 LEU A 168      10.085  29.442 -19.513  1.00 19.41           C  
ANISOU 1404  CD2 LEU A 168     2086   3179   2109    316    237   -701       C  
ATOM   1405  N   GLN A 169      10.116  33.347 -16.746  1.00 11.65           N  
ANISOU 1405  N   GLN A 169      263   2463   1699   -100     88     -9       N  
ATOM   1406  CA  GLN A 169      11.419  33.934 -16.431  1.00 12.68           C  
ANISOU 1406  CA  GLN A 169      313   2687   1817    -78    305   -148       C  
ATOM   1407  C   GLN A 169      11.497  34.396 -14.995  1.00 11.87           C  
ANISOU 1407  C   GLN A 169      362   2537   1610   -227    367   -296       C  
ATOM   1408  O   GLN A 169      12.527  34.229 -14.330  1.00 12.52           O  
ANISOU 1408  O   GLN A 169      259   2680   1818   -125      6    -77       O  
ATOM   1409  CB  GLN A 169      11.766  35.078 -17.383  1.00 13.39           C  
ANISOU 1409  CB  GLN A 169      563   2593   1930    -90   -154   -136       C  
ATOM   1410  CG  GLN A 169      12.091  34.608 -18.789  1.00 15.30           C  
ANISOU 1410  CG  GLN A 169      597   3112   2103   -184     67    -28       C  
ATOM   1411  CD  GLN A 169      12.423  35.747 -19.733  1.00 18.54           C  
ANISOU 1411  CD  GLN A 169     1542   3054   2448    419    268     76       C  
ATOM   1412  OE1 GLN A 169      12.423  36.897 -19.346  1.00 23.64           O  
ANISOU 1412  OE1 GLN A 169     3331   3295   2356    132    529     84       O  
ATOM   1413  NE2 GLN A 169      12.727  35.410 -20.988  1.00 25.65           N  
ANISOU 1413  NE2 GLN A 169     2996   4204   2545    -44   1164   -147       N  
ATOM   1414  N   VAL A 170      10.393  34.942 -14.476  1.00 11.68           N  
ANISOU 1414  N   VAL A 170      353   2556   1527   -243    329   -230       N  
ATOM   1415  CA  VAL A 170      10.368  35.323 -13.085  1.00 11.54           C  
ANISOU 1415  CA  VAL A 170      275   2356   1751    -24    183    -54       C  
ATOM   1416  C   VAL A 170      10.488  34.087 -12.203  1.00 11.47           C  
ANISOU 1416  C   VAL A 170      326   2390   1642     97    295   -241       C  
ATOM   1417  O   VAL A 170      11.238  34.080 -11.233  1.00 11.39           O  
ANISOU 1417  O   VAL A 170      274   2513   1540   -201     64      1       O  
ATOM   1418  CB  VAL A 170       9.063  36.114 -12.734  1.00 11.17           C  
ANISOU 1418  CB  VAL A 170      267   2312   1665    -20    140   -240       C  
ATOM   1419  CG1 VAL A 170       8.893  36.222 -11.211  1.00 12.25           C  
ANISOU 1419  CG1 VAL A 170      260   2685   1710     55     79   -360       C  
ATOM   1420  CG2 VAL A 170       9.094  37.484 -13.387  1.00 13.19           C  
ANISOU 1420  CG2 VAL A 170      616   2373   2022   -143   -188      4       C  
ATOM   1421  N   LEU A 171       9.731  33.035 -12.532  1.00 11.15           N  
ANISOU 1421  N   LEU A 171      253   2168   1815     -4     27    -64       N  
ATOM   1422  CA  LEU A 171       9.721  31.816 -11.738  1.00 10.90           C  
ANISOU 1422  CA  LEU A 171      279   2107   1752    139    145   -114       C  
ATOM   1423  C   LEU A 171      11.084  31.082 -11.781  1.00 11.21           C  
ANISOU 1423  C   LEU A 171      260   2382   1617     14     -2    -68       C  
ATOM   1424  O   LEU A 171      11.410  30.321 -10.875  1.00 12.42           O  
ANISOU 1424  O   LEU A 171      258   2661   1797     53     79    -86       O  
ATOM   1425  CB  LEU A 171       8.583  30.886 -12.203  1.00 11.36           C  
ANISOU 1425  CB  LEU A 171      634   2139   1540   -276    176    -12       C  
ATOM   1426  CG  LEU A 171       7.138  31.371 -11.997  1.00 11.03           C  
ANISOU 1426  CG  LEU A 171      314   2239   1635     95    280     38       C  
ATOM   1427  CD1 LEU A 171       6.237  30.434 -12.755  1.00 14.75           C  
ANISOU 1427  CD1 LEU A 171      743   2541   2318     25    363   -366       C  
ATOM   1428  CD2 LEU A 171       6.805  31.428 -10.515  1.00 13.53           C  
ANISOU 1428  CD2 LEU A 171      361   2929   1850    193    390     30       C  
ATOM   1429  N   GLN A 172      11.838  31.313 -12.851  1.00 12.64           N  
ANISOU 1429  N   GLN A 172      368   2616   1815      1    121     -6       N  
ATOM   1430  CA  GLN A 172      13.214  30.801 -12.975  1.00 12.08           C  
ANISOU 1430  CA  GLN A 172      382   2293   1913    100    183   -161       C  
ATOM   1431  C   GLN A 172      14.213  31.621 -12.198  1.00 13.00           C  
ANISOU 1431  C   GLN A 172      327   2467   2143    200    214     42       C  
ATOM   1432  O   GLN A 172      15.406  31.271 -12.135  1.00 14.11           O  
ANISOU 1432  O   GLN A 172      278   2790   2292    147    175   -110       O  
ATOM   1433  CB  GLN A 172      13.620  30.771 -14.437  1.00 13.74           C  
ANISOU 1433  CB  GLN A 172      732   2485   2003    168    439    -12       C  
ATOM   1434  CG  GLN A 172      12.885  29.720 -15.261  1.00 12.88           C  
ANISOU 1434  CG  GLN A 172      330   2511   2051    143    342   -124       C  
ATOM   1435  CD  GLN A 172      13.225  29.805 -16.714  1.00 13.64           C  
ANISOU 1435  CD  GLN A 172      853   2406   1923    116    445   -210       C  
ATOM   1436  OE1 GLN A 172      13.373  30.897 -17.254  1.00 15.87           O  
ANISOU 1436  OE1 GLN A 172     1219   2589   2221    -91    529    -65       O  
ATOM   1437  NE2 GLN A 172      13.348  28.639 -17.376  1.00 15.48           N  
ANISOU 1437  NE2 GLN A 172      555   3137   2190     26    419   -167       N  
ATOM   1438  N   GLY A 173      13.782  32.716 -11.612  1.00 12.63           N  
ANISOU 1438  N   GLY A 173      332   2490   1976   -143   -118   -208       N  
ATOM   1439  CA  GLY A 173      14.697  33.532 -10.816  1.00 12.45           C  
ANISOU 1439  CA  GLY A 173      301   2524   1903    297    113    -65       C  
ATOM   1440  C   GLY A 173      15.641  34.390 -11.661  1.00 14.30           C  
ANISOU 1440  C   GLY A 173      619   2628   2187    -63    423    -66       C  
ATOM   1441  O   GLY A 173      16.709  34.761 -11.204  1.00 16.35           O  
ANISOU 1441  O   GLY A 173      258   3272   2682   -101     25      0       O  
ATOM   1442  N   LYS A 174      15.225  34.747 -12.869  1.00 12.86           N  
ANISOU 1442  N   LYS A 174      297   2497   2090    -67    278    -67       N  
ATOM   1443  CA  LYS A 174      16.073  35.505 -13.787  1.00 13.85           C  
ANISOU 1443  CA  LYS A 174      492   2554   2214   -146    669     37       C  
ATOM   1444  C   LYS A 174      15.853  37.016 -13.729  1.00 14.41           C  
ANISOU 1444  C   LYS A 174      429   2681   2363   -252    572   -106       C  
ATOM   1445  O   LYS A 174      16.636  37.782 -14.290  1.00 15.98           O  
ANISOU 1445  O   LYS A 174      400   2723   2948   -244    417    -26       O  
ATOM   1446  CB  LYS A 174      15.837  35.021 -15.207  1.00 15.64           C  
ANISOU 1446  CB  LYS A 174      618   2910   2414    -70    711     97       C  
ATOM   1447  CG  LYS A 174      16.376  33.608 -15.471  1.00 18.80           C  
ANISOU 1447  CG  LYS A 174     1179   3153   2808    243    651   -257       C  
ATOM   1448  CD  LYS A 174      16.062  33.177 -16.872  1.00 20.15           C  
ANISOU 1448  CD  LYS A 174      979   3494   3182   -467    886   -151       C  
ATOM   1449  CE  LYS A 174      16.479  31.747 -17.131  1.00 22.67           C  
ANISOU 1449  CE  LYS A 174     1487   3712   3414    -39    261   -456       C  
ATOM   1450  NZ  LYS A 174      16.008  31.268 -18.472  1.00 31.41           N  
ANISOU 1450  NZ  LYS A 174     3197   4588   4147   -559   -323   -608       N  
ATOM   1451  N   ILE A 175      14.759  37.445 -13.089  1.00 13.13           N  
ANISOU 1451  N   ILE A 175      408   2300   2279   -336    469   -123       N  
ATOM   1452  CA  ILE A 175      14.260  38.803 -13.275  1.00 13.35           C  
ANISOU 1452  CA  ILE A 175      425   2528   2119   -497    328     70       C  
ATOM   1453  C   ILE A 175      14.194  39.570 -11.955  1.00 13.41           C  
ANISOU 1453  C   ILE A 175      709   2170   2216   -328    177   -163       C  
ATOM   1454  O   ILE A 175      13.627  39.077 -10.985  1.00 14.35           O  
ANISOU 1454  O   ILE A 175      442   2770   2238   -145    596     41       O  
ATOM   1455  CB  ILE A 175      12.816  38.762 -13.860  1.00 13.12           C  
ANISOU 1455  CB  ILE A 175      297   2610   2077   -189    237   -111       C  
ATOM   1456  CG1 ILE A 175      12.752  37.893 -15.133  1.00 14.43           C  
ANISOU 1456  CG1 ILE A 175      832   2500   2148   -201    226    110       C  
ATOM   1457  CG2 ILE A 175      12.309  40.175 -14.127  1.00 14.84           C  
ANISOU 1457  CG2 ILE A 175      331   2628   2678    -44    358    164       C  
ATOM   1458  CD1 ILE A 175      13.683  38.376 -16.274  1.00 15.12           C  
ANISOU 1458  CD1 ILE A 175      356   3046   2341   -151    396     74       C  
ATOM   1459  N  ALYS A 176      14.687  40.816 -11.972  0.50 12.76           N  
ANISOU 1459  N  ALYS A 176      308   2536   2004    -63    307    -29       N  
ATOM   1460  N  BLYS A 176      14.726  40.777 -11.879  0.50 13.92           N  
ANISOU 1460  N  BLYS A 176      305   2718   2263    -16    324    -48       N  
ATOM   1461  CA ALYS A 176      14.570  41.718 -10.813  0.50 11.90           C  
ANISOU 1461  CA ALYS A 176      476   2028   2016   -454    279    -24       C  
ATOM   1462  CA BLYS A 176      14.479  41.533 -10.650  0.50 16.49           C  
ANISOU 1462  CA BLYS A 176     1176   2642   2448    -85     73   -153       C  
ATOM   1463  C  ALYS A 176      13.190  42.407 -10.766  0.50 14.05           C  
ANISOU 1463  C  ALYS A 176      621   2527   2189    -18    -54    -80       C  
ATOM   1464  C  BLYS A 176      13.189  42.295 -10.715  0.50 15.57           C  
ANISOU 1464  C  BLYS A 176      741   2763   2410    103    -66   -142       C  
ATOM   1465  O  ALYS A 176      12.634  42.775 -11.798  0.50 14.48           O  
ANISOU 1465  O  ALYS A 176      617   2477   2406   -232    240     61       O  
ATOM   1466  O  BLYS A 176      12.672  42.588 -11.788  0.50 14.96           O  
ANISOU 1466  O  BLYS A 176      675   2572   2438   -123    303     30       O  
ATOM   1467  CB ALYS A 176      15.668  42.766 -10.846  0.50 13.24           C  
ANISOU 1467  CB ALYS A 176      823   2338   1868   -118    950     44       C  
ATOM   1468  CB BLYS A 176      15.595  42.458 -10.286  0.50 19.95           C  
ANISOU 1468  CB BLYS A 176     1859   3069   2652    128    460    -37       C  
ATOM   1469  CG ALYS A 176      17.081  42.155 -10.794  0.50 11.98           C  
ANISOU 1469  CG ALYS A 176      475   1882   2194    -23    656    -75       C  
ATOM   1470  CG BLYS A 176      16.144  43.152 -11.370  0.50 23.24           C  
ANISOU 1470  CG BLYS A 176     2962   2827   3040   -512    -60    -66       C  
ATOM   1471  CD ALYS A 176      18.113  43.160 -10.360  0.50 19.74           C  
ANISOU 1471  CD ALYS A 176     2192   2552   2754   -193   -100   -201       C  
ATOM   1472  CD BLYS A 176      17.493  42.687 -11.578  0.50 23.30           C  
ANISOU 1472  CD BLYS A 176     2239   3364   3249    508   -222    -46       C  
ATOM   1473  CE ALYS A 176      19.493  42.509 -10.223  0.50 27.25           C  
ANISOU 1473  CE ALYS A 176     2940   3486   3927     23    136    -91       C  
ATOM   1474  CE BLYS A 176      18.400  43.818 -11.656  0.50 23.80           C  
ANISOU 1474  CE BLYS A 176     2480   3244   3319   -588    261   -176       C  
ATOM   1475  NZ ALYS A 176      19.610  41.658  -8.990  0.50 26.03           N  
ANISOU 1475  NZ ALYS A 176     1547   4652   3689   -585   -335    -37       N  
ATOM   1476  NZ BLYS A 176      18.007  44.728 -12.745  0.50 29.95           N  
ANISOU 1476  NZ BLYS A 176     3211   4381   3788    373   -354    -56       N  
ATOM   1477  N   PRO A 177      12.632  42.566  -9.559  1.00 12.72           N  
ANISOU 1477  N   PRO A 177      285   2431   2117    -73    140   -147       N  
ATOM   1478  CA  PRO A 177      11.359  43.272  -9.431  1.00 13.45           C  
ANISOU 1478  CA  PRO A 177      264   2584   2260    156    -36   -182       C  
ATOM   1479  C   PRO A 177      11.287  44.593 -10.176  1.00 13.56           C  
ANISOU 1479  C   PRO A 177      679   2415   2057   -273     44     82       C  
ATOM   1480  O   PRO A 177      10.301  44.871 -10.812  1.00 12.88           O  
ANISOU 1480  O   PRO A 177      276   2606   2011   -210     76     96       O  
ATOM   1481  CB  PRO A 177      11.225  43.443  -7.932  1.00 13.91           C  
ANISOU 1481  CB  PRO A 177      599   2555   2130   -145    263      0       C  
ATOM   1482  CG  PRO A 177      11.849  42.219  -7.395  1.00 13.08           C  
ANISOU 1482  CG  PRO A 177      295   2807   1864    -94    259   -292       C  
ATOM   1483  CD  PRO A 177      13.076  42.030  -8.268  1.00 14.03           C  
ANISOU 1483  CD  PRO A 177      267   2604   2460   -177     67   -233       C  
ATOM   1484  N   ILE A 178      12.355  45.371 -10.203  1.00 13.66           N  
ANISOU 1484  N   ILE A 178      411   2547   2232   -309    486    -50       N  
ATOM   1485  CA  ILE A 178      12.295  46.632 -10.935  1.00 14.01           C  
ANISOU 1485  CA  ILE A 178      300   2526   2498   -247    232   -210       C  
ATOM   1486  C   ILE A 178      12.087  46.413 -12.441  1.00 14.67           C  
ANISOU 1486  C   ILE A 178      913   2176   2484   -278    295    -54       C  
ATOM   1487  O   ILE A 178      11.450  47.230 -13.111  1.00 15.08           O  
ANISOU 1487  O   ILE A 178      417   2725   2588   -384    516   -156       O  
ATOM   1488  CB  ILE A 178      13.572  47.522 -10.718  1.00 14.92           C  
ANISOU 1488  CB  ILE A 178      422   2852   2393   -598    253     29       C  
ATOM   1489  CG1 ILE A 178      13.345  48.885 -11.390  1.00 18.33           C  
ANISOU 1489  CG1 ILE A 178     1034   2891   3037   -755    615   -127       C  
ATOM   1490  CG2 ILE A 178      14.874  46.825 -11.241  1.00 18.35           C  
ANISOU 1490  CG2 ILE A 178      674   3386   2910   -373    536   -412       C  
ATOM   1491  CD1 ILE A 178      12.223  49.726 -10.749  1.00 19.22           C  
ANISOU 1491  CD1 ILE A 178     1583   2980   2738   -603    230   -209       C  
ATOM   1492  N   GLU A 179      12.637  45.326 -12.982  1.00 15.01           N  
ANISOU 1492  N   GLU A 179      448   2782   2470   -310    602    -95       N  
ATOM   1493  CA  GLU A 179      12.366  44.982 -14.387  1.00 14.93           C  
ANISOU 1493  CA  GLU A 179      577   2462   2632   -389    643    -42       C  
ATOM   1494  C   GLU A 179      10.886  44.732 -14.653  1.00 14.24           C  
ANISOU 1494  C   GLU A 179      773   2577   2059   -420    517    153       C  
ATOM   1495  O   GLU A 179      10.382  45.067 -15.721  1.00 15.40           O  
ANISOU 1495  O   GLU A 179      847   2870   2133   -294    442    109       O  
ATOM   1496  CB  GLU A 179      13.139  43.759 -14.797  1.00 14.02           C  
ANISOU 1496  CB  GLU A 179      486   2677   2164   -326    381    115       C  
ATOM   1497  CG  GLU A 179      14.600  43.948 -14.858  1.00 18.31           C  
ANISOU 1497  CG  GLU A 179     1140   3129   2685    151    210    448       C  
ATOM   1498  CD  GLU A 179      15.312  42.659 -15.221  1.00 18.76           C  
ANISOU 1498  CD  GLU A 179      730   3577   2820    380    790     61       C  
ATOM   1499  OE1 GLU A 179      15.292  42.283 -16.431  1.00 24.42           O  
ANISOU 1499  OE1 GLU A 179     1754   3809   3715     85    550     81       O  
ATOM   1500  OE2 GLU A 179      15.819  41.987 -14.305  1.00 19.06           O  
ANISOU 1500  OE2 GLU A 179      652   3910   2678   -312    947     38       O  
ATOM   1501  N   VAL A 180      10.206  44.076 -13.708  1.00 13.68           N  
ANISOU 1501  N   VAL A 180      405   2693   2099   -203    399     30       N  
ATOM   1502  CA  VAL A 180       8.791  43.799 -13.835  1.00 13.46           C  
ANISOU 1502  CA  VAL A 180      520   2503   2092   -374   -153    137       C  
ATOM   1503  C   VAL A 180       8.027  45.116 -13.836  1.00 13.28           C  
ANISOU 1503  C   VAL A 180      515   2586   1942   -629    126    -76       C  
ATOM   1504  O   VAL A 180       7.181  45.358 -14.693  1.00 14.37           O  
ANISOU 1504  O   VAL A 180      782   2692   1984   -232     11     69       O  
ATOM   1505  CB  VAL A 180       8.304  42.900 -12.681  1.00 12.93           C  
ANISOU 1505  CB  VAL A 180      312   2545   2054   -325   -169    109       C  
ATOM   1506  CG1 VAL A 180       6.783  42.746 -12.737  1.00 15.30           C  
ANISOU 1506  CG1 VAL A 180      391   3251   2169   -608   -176     50       C  
ATOM   1507  CG2 VAL A 180       8.975  41.533 -12.758  1.00 16.33           C  
ANISOU 1507  CG2 VAL A 180     1119   2614   2472   -299   -175    124       C  
ATOM   1508  N   ILE A 181       8.351  45.981 -12.881  1.00 14.50           N  
ANISOU 1508  N   ILE A 181      501   2658   2349   -315    258    -31       N  
ATOM   1509  CA  ILE A 181       7.676  47.248 -12.755  1.00 13.56           C  
ANISOU 1509  CA  ILE A 181      591   2483   2074   -217    281    -87       C  
ATOM   1510  C   ILE A 181       7.890  48.120 -13.995  1.00 13.72           C  
ANISOU 1510  C   ILE A 181      500   2452   2260    -51    193     60       C  
ATOM   1511  O   ILE A 181       6.955  48.708 -14.524  1.00 14.25           O  
ANISOU 1511  O   ILE A 181      298   2731   2386   -103    179    369       O  
ATOM   1512  CB  ILE A 181       8.143  47.972 -11.490  1.00 14.21           C  
ANISOU 1512  CB  ILE A 181      342   2792   2265   -295    337    -46       C  
ATOM   1513  CG1 ILE A 181       7.644  47.203 -10.219  1.00 14.52           C  
ANISOU 1513  CG1 ILE A 181      316   2822   2378   -218   -276   -324       C  
ATOM   1514  CG2 ILE A 181       7.696  49.444 -11.502  1.00 17.19           C  
ANISOU 1514  CG2 ILE A 181     1075   2877   2577    173    -30   -437       C  
ATOM   1515  CD1 ILE A 181       6.184  46.780 -10.256  1.00 16.97           C  
ANISOU 1515  CD1 ILE A 181     1126   3005   2315   -544   -330    -32       C  
ATOM   1516  N   GLU A 182       9.109  48.184 -14.482  1.00 14.47           N  
ANISOU 1516  N   GLU A 182      475   2597   2426   -345    446     22       N  
ATOM   1517  CA  GLU A 182       9.386  48.984 -15.674  1.00 15.26           C  
ANISOU 1517  CA  GLU A 182      653   2615   2527   -205    759    185       C  
ATOM   1518  C   GLU A 182       8.608  48.468 -16.900  1.00 14.80           C  
ANISOU 1518  C   GLU A 182      868   2414   2340     -1    553    289       C  
ATOM   1519  O   GLU A 182       8.063  49.253 -17.686  1.00 16.57           O  
ANISOU 1519  O   GLU A 182      925   2682   2689   -164    269    536       O  
ATOM   1520  CB  GLU A 182      10.897  49.030 -15.955  1.00 17.48           C  
ANISOU 1520  CB  GLU A 182     1062   2755   2825   -196    854    282       C  
ATOM   1521  CG  GLU A 182      11.659  49.904 -14.943  1.00 21.55           C  
ANISOU 1521  CG  GLU A 182     1813   3110   3265   -428    520     -7       C  
ATOM   1522  CD  GLU A 182      13.194  49.791 -15.037  1.00 29.91           C  
ANISOU 1522  CD  GLU A 182     3059   4377   3927   -419    489   -643       C  
ATOM   1523  OE1 GLU A 182      13.707  48.836 -15.655  1.00 37.75           O  
ANISOU 1523  OE1 GLU A 182     3392   5434   5516    -47    429   -754       O  
ATOM   1524  OE2 GLU A 182      13.882  50.659 -14.456  1.00 28.96           O  
ANISOU 1524  OE2 GLU A 182     2521   4356   4123  -1823   -128    -24       O  
ATOM   1525  N   LYS A 183       8.486  47.149 -17.014  1.00 15.39           N  
ANISOU 1525  N   LYS A 183      641   2735   2471     -1    628    170       N  
ATOM   1526  CA  LYS A 183       7.740  46.549 -18.115  1.00 15.66           C  
ANISOU 1526  CA  LYS A 183     1045   2701   2204   -177    660    125       C  
ATOM   1527  C   LYS A 183       6.232  46.857 -18.009  1.00 15.02           C  
ANISOU 1527  C   LYS A 183      927   2662   2118   -430    414    289       C  
ATOM   1528  O   LYS A 183       5.569  47.166 -19.016  1.00 16.52           O  
ANISOU 1528  O   LYS A 183      863   3207   2206   -122    309    308       O  
ATOM   1529  CB  LYS A 183       7.986  45.035 -18.140  1.00 16.55           C  
ANISOU 1529  CB  LYS A 183     1088   2785   2416    -64    453    189       C  
ATOM   1530  CG  LYS A 183       7.164  44.271 -19.150  1.00 17.23           C  
ANISOU 1530  CG  LYS A 183     1478   2670   2398   -157    599    -80       C  
ATOM   1531  CD  LYS A 183       7.385  44.748 -20.569  1.00 19.86           C  
ANISOU 1531  CD  LYS A 183     2089   2876   2580   -370     22    178       C  
ATOM   1532  CE  LYS A 183       6.639  43.886 -21.552  1.00 22.53           C  
ANISOU 1532  CE  LYS A 183     2408   3402   2749     81   -106    310       C  
ATOM   1533  NZ  LYS A 183       6.540  44.511 -22.896  1.00 27.93           N  
ANISOU 1533  NZ  LYS A 183     3956   4019   2636   -189    435    436       N  
ATOM   1534  N   ILE A 184       5.689  46.791 -16.797  1.00 13.67           N  
ANISOU 1534  N   ILE A 184      500   2607   2086    -41    132    209       N  
ATOM   1535  CA  ILE A 184       4.275  47.111 -16.594  1.00 13.62           C  
ANISOU 1535  CA  ILE A 184      443   2526   2206   -191    -56    186       C  
ATOM   1536  C   ILE A 184       4.019  48.567 -16.966  1.00 15.71           C  
ANISOU 1536  C   ILE A 184     1209   2594   2163   -164     46    302       C  
ATOM   1537  O   ILE A 184       3.071  48.872 -17.655  1.00 16.60           O  
ANISOU 1537  O   ILE A 184      842   2787   2675   -336     64    536       O  
ATOM   1538  CB  ILE A 184       3.816  46.812 -15.141  1.00 13.87           C  
ANISOU 1538  CB  ILE A 184      566   2579   2124   -186    -17    -55       C  
ATOM   1539  CG1 ILE A 184       3.824  45.290 -14.908  1.00 14.35           C  
ANISOU 1539  CG1 ILE A 184      703   2595   2151   -253   -173    -87       C  
ATOM   1540  CG2 ILE A 184       2.403  47.405 -14.869  1.00 15.21           C  
ANISOU 1540  CG2 ILE A 184      278   2973   2525    -71    224    159       C  
ATOM   1541  CD1 ILE A 184       3.525  44.853 -13.479  1.00 14.49           C  
ANISOU 1541  CD1 ILE A 184      947   2708   1849   -537     54     46       C  
ATOM   1542  N   ILE A 185       4.920  49.454 -16.573  1.00 16.61           N  
ANISOU 1542  N   ILE A 185     1038   2459   2814   -130    324    417       N  
ATOM   1543  CA  ILE A 185       4.760  50.862 -16.883  1.00 17.00           C  
ANISOU 1543  CA  ILE A 185     1229   2544   2683   -142    410    159       C  
ATOM   1544  C   ILE A 185       4.812  51.095 -18.415  1.00 16.90           C  
ANISOU 1544  C   ILE A 185     1149   2724   2548     57     81    378       C  
ATOM   1545  O   ILE A 185       4.006  51.848 -18.959  1.00 19.53           O  
ANISOU 1545  O   ILE A 185     1414   2925   3080   -437     65    611       O  
ATOM   1546  CB  ILE A 185       5.833  51.712 -16.179  1.00 18.56           C  
ANISOU 1546  CB  ILE A 185     1475   2586   2989    -70    177     69       C  
ATOM   1547  CG1 ILE A 185       5.550  51.763 -14.659  1.00 18.94           C  
ANISOU 1547  CG1 ILE A 185     1886   2350   2960   -413     98    190       C  
ATOM   1548  CG2 ILE A 185       5.880  53.129 -16.785  1.00 19.74           C  
ANISOU 1548  CG2 ILE A 185     1674   2736   3087   -517     50    276       C  
ATOM   1549  CD1 ILE A 185       6.682  52.402 -13.828  1.00 20.16           C  
ANISOU 1549  CD1 ILE A 185     1597   2660   3402    -76   -351   -172       C  
ATOM   1550  N  AGLU A 186       5.724  50.419 -19.103  0.60 17.79           N  
ANISOU 1550  N  AGLU A 186     1421   2770   2568   -156    203    452       N  
ATOM   1551  N  BGLU A 186       5.752  50.422 -19.084  0.40 18.44           N  
ANISOU 1551  N  BGLU A 186     1594   2771   2638   -150    185    374       N  
ATOM   1552  CA AGLU A 186       5.806  50.551 -20.562  0.60 18.78           C  
ANISOU 1552  CA AGLU A 186     1695   2848   2590   -192    268    408       C  
ATOM   1553  CA BGLU A 186       5.859  50.479 -20.550  0.40 19.58           C  
ANISOU 1553  CA BGLU A 186     1886   2892   2660   -208    184    316       C  
ATOM   1554  C  AGLU A 186       4.549  50.006 -21.231  0.60 18.99           C  
ANISOU 1554  C  AGLU A 186     1950   2766   2497   -187     81    549       C  
ATOM   1555  C  BGLU A 186       4.555  50.015 -21.194  0.40 19.18           C  
ANISOU 1555  C  BGLU A 186     1957   2789   2538   -217     66    457       C  
ATOM   1556  O  AGLU A 186       3.982  50.644 -22.125  0.60 19.26           O  
ANISOU 1556  O  AGLU A 186     1563   3169   2584   -279    110    905       O  
ATOM   1557  O  BGLU A 186       3.976  50.712 -22.031  0.40 19.83           O  
ANISOU 1557  O  BGLU A 186     1796   3113   2625   -241    160    767       O  
ATOM   1558  CB AGLU A 186       7.034  49.833 -21.111  0.60 19.17           C  
ANISOU 1558  CB AGLU A 186     1823   2779   2679    113    271    227       C  
ATOM   1559  CB BGLU A 186       7.012  49.584 -21.049  0.40 20.58           C  
ANISOU 1559  CB BGLU A 186     2105   2934   2781   -132    254    194       C  
ATOM   1560  CG AGLU A 186       7.183  49.963 -22.625  0.60 22.06           C  
ANISOU 1560  CG AGLU A 186     2340   3207   2833     24    109    228       C  
ATOM   1561  CG BGLU A 186       8.291  49.625 -20.195  0.40 26.80           C  
ANISOU 1561  CG BGLU A 186     2951   3870   3359   -210     19     19       C  
ATOM   1562  CD AGLU A 186       8.254  49.055 -23.194  0.60 25.16           C  
ANISOU 1562  CD AGLU A 186     2191   3498   3870   -104     73     91       C  
ATOM   1563  CD BGLU A 186       9.298  48.521 -20.581  0.40 31.97           C  
ANISOU 1563  CD BGLU A 186     3888   4324   3932   -211    204   -118       C  
ATOM   1564  OE1AGLU A 186       9.451  49.412 -23.105  0.60 33.08           O  
ANISOU 1564  OE1AGLU A 186     2883   4889   4794   -122    125    309       O  
ATOM   1565  OE1BGLU A 186       9.003  47.744 -21.513  0.40 35.31           O  
ANISOU 1565  OE1BGLU A 186     4604   4696   4113   -314    726   -382       O  
ATOM   1566  OE2AGLU A 186       7.899  47.994 -23.753  0.60 31.08           O  
ANISOU 1566  OE2AGLU A 186     2864   4594   4348   -337    393    -99       O  
ATOM   1567  OE2BGLU A 186      10.375  48.435 -19.946  0.40 32.74           O  
ANISOU 1567  OE2BGLU A 186     3408   5243   3788     65   1107     -6       O  
ATOM   1568  N   ASP A 187       4.092  48.840 -20.783  1.00 17.80           N  
ANISOU 1568  N   ASP A 187     1429   2858   2473   -530   -130    483       N  
ATOM   1569  CA  ASP A 187       2.907  48.242 -21.352  1.00 17.68           C  
ANISOU 1569  CA  ASP A 187     1439   2814   2461   -233    127    374       C  
ATOM   1570  C   ASP A 187       1.689  49.156 -21.176  1.00 18.96           C  
ANISOU 1570  C   ASP A 187     1862   2798   2544     34    -96    551       C  
ATOM   1571  O   ASP A 187       0.920  49.369 -22.119  1.00 20.55           O  
ANISOU 1571  O   ASP A 187     1946   3287   2574   -284   -143    646       O  
ATOM   1572  CB  ASP A 187       2.651  46.875 -20.719  1.00 17.29           C  
ANISOU 1572  CB  ASP A 187     1479   2703   2384   -222   -151    338       C  
ATOM   1573  CG  ASP A 187       3.438  45.755 -21.396  1.00 18.64           C  
ANISOU 1573  CG  ASP A 187     1503   3171   2408   -122    214    523       C  
ATOM   1574  OD1 ASP A 187       4.197  46.045 -22.364  1.00 22.75           O  
ANISOU 1574  OD1 ASP A 187     2947   3271   2423   -268    909    421       O  
ATOM   1575  OD2 ASP A 187       3.314  44.584 -20.950  1.00 19.98           O  
ANISOU 1575  OD2 ASP A 187     1817   3199   2573   -206    380    645       O  
ATOM   1576  N   ARG A 188       1.521  49.707 -19.982  1.00 19.24           N  
ANISOU 1576  N   ARG A 188     2039   2667   2603     59    111    407       N  
ATOM   1577  CA  ARG A 188       0.388  50.600 -19.723  1.00 20.54           C  
ANISOU 1577  CA  ARG A 188     1981   2881   2939    -35     63    443       C  
ATOM   1578  C   ARG A 188       0.464  51.827 -20.618  1.00 21.11           C  
ANISOU 1578  C   ARG A 188     2248   2912   2858     93    101    689       C  
ATOM   1579  O   ARG A 188      -0.559  52.343 -21.062  1.00 22.99           O  
ANISOU 1579  O   ARG A 188     2094   3464   3176    363    170    972       O  
ATOM   1580  CB  ARG A 188       0.351  51.031 -18.263  1.00 18.60           C  
ANISOU 1580  CB  ARG A 188     1487   2745   2833    -97    242    347       C  
ATOM   1581  CG  ARG A 188      -0.013  49.916 -17.300  1.00 18.98           C  
ANISOU 1581  CG  ARG A 188     1492   2781   2935   -137    237    372       C  
ATOM   1582  CD  ARG A 188      -0.090  50.410 -15.889  1.00 15.99           C  
ANISOU 1582  CD  ARG A 188      773   2545   2757   -143     59    432       C  
ATOM   1583  NE  ARG A 188      -0.441  49.338 -14.966  1.00 15.36           N  
ANISOU 1583  NE  ARG A 188      469   2656   2709    -50   -304    168       N  
ATOM   1584  CZ  ARG A 188      -0.560  49.485 -13.653  1.00 15.74           C  
ANISOU 1584  CZ  ARG A 188     1084   2459   2435    317     77    169       C  
ATOM   1585  NH1 ARG A 188      -0.363  50.667 -13.093  1.00 17.39           N  
ANISOU 1585  NH1 ARG A 188     1151   2552   2902    -29    -72    338       N  
ATOM   1586  NH2 ARG A 188      -0.860  48.439 -12.898  1.00 15.28           N  
ANISOU 1586  NH2 ARG A 188      766   2594   2444    -72   -146    231       N  
ATOM   1587  N   SER A 189       1.678  52.300 -20.873  1.00 21.26           N  
ANISOU 1587  N   SER A 189     1933   3088   3057    124    203    860       N  
ATOM   1588  CA  SER A 189       1.863  53.500 -21.705  1.00 23.33           C  
ANISOU 1588  CA  SER A 189     2812   2923   3129    -93    161    595       C  
ATOM   1589  C   SER A 189       1.481  53.230 -23.156  1.00 23.96           C  
ANISOU 1589  C   SER A 189     2838   3061   3203     56     83    741       C  
ATOM   1590  O   SER A 189       1.225  54.161 -23.928  1.00 26.64           O  
ANISOU 1590  O   SER A 189     3383   3414   3323   -134    325   1045       O  
ATOM   1591  CB  SER A 189       3.308  54.008 -21.619  1.00 25.16           C  
ANISOU 1591  CB  SER A 189     3291   3103   3164   -208    351    652       C  
ATOM   1592  OG  SER A 189       4.174  53.244 -22.434  1.00 26.75           O  
ANISOU 1592  OG  SER A 189     3567   3000   3596   -117    474    749       O  
ATOM   1593  N   ASN A 190       1.421  51.954 -23.512  1.00 22.77           N  
ANISOU 1593  N   ASN A 190     2850   3022   2777     -4   -158    786       N  
ATOM   1594  CA  ASN A 190       1.024  51.533 -24.837  1.00 24.06           C  
ANISOU 1594  CA  ASN A 190     2986   3066   3087   -233   -187    710       C  
ATOM   1595  C   ASN A 190      -0.379  50.956 -24.824  1.00 25.04           C  
ANISOU 1595  C   ASN A 190     3019   3325   3170   -222   -366    704       C  
ATOM   1596  O   ASN A 190      -0.789  50.283 -25.768  1.00 28.60           O  
ANISOU 1596  O   ASN A 190     3554   3869   3443   -285   -550    645       O  
ATOM   1597  CB  ASN A 190       2.007  50.494 -25.369  1.00 23.17           C  
ANISOU 1597  CB  ASN A 190     3088   3161   2554   -293     73    708       C  
ATOM   1598  CG  ASN A 190       3.341  51.106 -25.760  1.00 25.38           C  
ANISOU 1598  CG  ASN A 190     2576   3753   3311   -193   -210    852       C  
ATOM   1599  OD1 ASN A 190       3.382  52.127 -26.433  1.00 31.48           O  
ANISOU 1599  OD1 ASN A 190     3594   4089   4277   -248     97   1672       O  
ATOM   1600  ND2 ASN A 190       4.434  50.482 -25.340  1.00 25.20           N  
ANISOU 1600  ND2 ASN A 190     2569   4381   2624   -322    154    803       N  
ATOM   1601  N   ASP A 191      -1.100  51.209 -23.733  1.00 25.32           N  
ANISOU 1601  N   ASP A 191     2779   3411   3428    -95   -357    605       N  
ATOM   1602  CA  ASP A 191      -2.489  50.729 -23.567  1.00 25.77           C  
ANISOU 1602  CA  ASP A 191     2742   3496   3551   -138   -630    670       C  
ATOM   1603  C   ASP A 191      -2.590  49.207 -23.694  1.00 26.12           C  
ANISOU 1603  C   ASP A 191     2737   3428   3756   -393   -799    603       C  
ATOM   1604  O   ASP A 191      -3.587  48.670 -24.208  1.00 29.01           O  
ANISOU 1604  O   ASP A 191     3015   3865   4142   -443  -1133    917       O  
ATOM   1605  CB  ASP A 191      -3.415  51.417 -24.566  1.00 29.24           C  
ANISOU 1605  CB  ASP A 191     3507   3789   3814    -99   -436    749       C  
ATOM   1606  CG  ASP A 191      -3.455  52.923 -24.374  1.00 37.88           C  
ANISOU 1606  CG  ASP A 191     5056   4588   4748    102   -309    435       C  
ATOM   1607  OD1 ASP A 191      -3.606  53.378 -23.216  1.00 42.95           O  
ANISOU 1607  OD1 ASP A 191     5429   5684   5203    310   -301    210       O  
ATOM   1608  OD2 ASP A 191      -3.321  53.653 -25.377  1.00 50.69           O  
ANISOU 1608  OD2 ASP A 191     7035   6190   6035   -328   -194    926       O  
ATOM   1609  N   ILE A 192      -1.575  48.523 -23.183  1.00 24.31           N  
ANISOU 1609  N   ILE A 192     2543   3120   3574   -316   -493    578       N  
ATOM   1610  CA  ILE A 192      -1.547  47.074 -23.146  1.00 24.68           C  
ANISOU 1610  CA  ILE A 192     2690   3463   3225   -247   -328    457       C  
ATOM   1611  C   ILE A 192      -1.882  46.598 -21.740  1.00 24.63           C  
ANISOU 1611  C   ILE A 192     2615   3386   3356   -314   -417    533       C  
ATOM   1612  O   ILE A 192      -1.245  47.017 -20.762  1.00 23.89           O  
ANISOU 1612  O   ILE A 192     2292   3567   3218   -291   -486    870       O  
ATOM   1613  CB  ILE A 192      -0.151  46.541 -23.540  1.00 25.00           C  
ANISOU 1613  CB  ILE A 192     2925   3355   3217   -220    -99    277       C  
ATOM   1614  CG1 ILE A 192       0.131  46.837 -25.015  1.00 28.11           C  
ANISOU 1614  CG1 ILE A 192     3229   3907   3544   -230   -169    453       C  
ATOM   1615  CG2 ILE A 192      -0.040  45.043 -23.271  1.00 24.66           C  
ANISOU 1615  CG2 ILE A 192     2091   3571   3705   -402   -360    443       C  
ATOM   1616  CD1 ILE A 192       1.600  46.635 -25.416  1.00 28.81           C  
ANISOU 1616  CD1 ILE A 192     3285   4178   3483   -434    334    200       C  
ATOM   1617  N   THR A 193      -2.915  45.766 -21.638  1.00 22.19           N  
ANISOU 1617  N   THR A 193     2046   3263   3120     93   -622    864       N  
ATOM   1618  CA  THR A 193      -3.271  45.136 -20.383  1.00 22.91           C  
ANISOU 1618  CA  THR A 193     2239   3259   3205   -145   -454    456       C  
ATOM   1619  C   THR A 193      -3.220  43.620 -20.588  1.00 21.71           C  
ANISOU 1619  C   THR A 193     2224   3226   2798   -185   -522    560       C  
ATOM   1620  O   THR A 193      -3.411  43.131 -21.705  1.00 22.33           O  
ANISOU 1620  O   THR A 193     2132   3132   3219    111   -826    480       O  
ATOM   1621  CB  THR A 193      -4.671  45.576 -19.932  1.00 28.61           C  
ANISOU 1621  CB  THR A 193     3558   3755   3555     20     23    473       C  
ATOM   1622  OG1 THR A 193      -4.920  45.130 -18.595  1.00 36.76           O  
ANISOU 1622  OG1 THR A 193     4815   4480   4671    214    331    290       O  
ATOM   1623  CG2 THR A 193      -5.707  45.022 -20.845  1.00 29.97           C  
ANISOU 1623  CG2 THR A 193     2878   4284   4226     57   -432    353       C  
ATOM   1624  N   LYS A 194      -2.915  42.880 -19.533  1.00 18.81           N  
ANISOU 1624  N   LYS A 194     1350   2859   2937   -146   -737    443       N  
ATOM   1625  CA  LYS A 194      -2.691  41.449 -19.670  1.00 18.47           C  
ANISOU 1625  CA  LYS A 194     1712   2969   2335     11   -492    322       C  
ATOM   1626  C   LYS A 194      -3.456  40.646 -18.623  1.00 17.21           C  
ANISOU 1626  C   LYS A 194     1427   2607   2505   -107   -416    165       C  
ATOM   1627  O   LYS A 194      -3.649  41.094 -17.496  1.00 21.95           O  
ANISOU 1627  O   LYS A 194     2789   2835   2716   -487   -161    197       O  
ATOM   1628  CB  LYS A 194      -1.182  41.136 -19.555  1.00 18.85           C  
ANISOU 1628  CB  LYS A 194     1523   2851   2787    113   -706    459       C  
ATOM   1629  CG  LYS A 194      -0.347  41.668 -20.706  1.00 22.10           C  
ANISOU 1629  CG  LYS A 194     1905   3316   3173   -110   -468    829       C  
ATOM   1630  CD  LYS A 194      -0.526  40.828 -21.967  1.00 27.30           C  
ANISOU 1630  CD  LYS A 194     3226   3085   4062    -93    158    544       C  
ATOM   1631  CE  LYS A 194       0.471  41.225 -23.055  1.00 33.78           C  
ANISOU 1631  CE  LYS A 194     4722   4324   3788    117    -89    151       C  
ATOM   1632  NZ  LYS A 194       0.002  40.817 -24.404  1.00 42.62           N  
ANISOU 1632  NZ  LYS A 194     6027   5512   4653     92    -89      8       N  
ATOM   1633  N  ALYS A 195      -3.867  39.445 -19.012  0.50 17.15           N  
ANISOU 1633  N  ALYS A 195     1482   2647   2385   -382   -446    310       N  
ATOM   1634  N  BLYS A 195      -3.839  39.435 -18.987  0.50 16.68           N  
ANISOU 1634  N  BLYS A 195     1383   2605   2350   -382   -456    346       N  
ATOM   1635  CA ALYS A 195      -4.469  38.488 -18.094  0.50 15.92           C  
ANISOU 1635  CA ALYS A 195     1047   2681   2319   -286    -99    136       C  
ATOM   1636  CA BLYS A 195      -4.394  38.497 -18.030  0.50 15.34           C  
ANISOU 1636  CA BLYS A 195      882   2670   2273   -233     -2    166       C  
ATOM   1637  C  ALYS A 195      -3.951  37.095 -18.404  0.50 14.93           C  
ANISOU 1637  C  ALYS A 195      988   2522   2160   -481   -291    137       C  
ATOM   1638  C  BLYS A 195      -4.044  37.080 -18.425  0.50 14.07           C  
ANISOU 1638  C  BLYS A 195      677   2519   2151   -421   -232    206       C  
ATOM   1639  O  ALYS A 195      -3.382  36.858 -19.473  0.50 17.61           O  
ANISOU 1639  O  ALYS A 195     1598   3011   2081   -178   -180    272       O  
ATOM   1640  O  BLYS A 195      -3.710  36.805 -19.581  0.50 17.96           O  
ANISOU 1640  O  BLYS A 195     1643   3027   2152   -149     -5    461       O  
ATOM   1641  CB ALYS A 195      -5.993  38.513 -18.218  0.50 17.70           C  
ANISOU 1641  CB ALYS A 195     1254   2978   2490   -116    205    230       C  
ATOM   1642  CB BLYS A 195      -5.907  38.654 -17.941  0.50 17.00           C  
ANISOU 1642  CB BLYS A 195     1067   2781   2611    -51    361    310       C  
ATOM   1643  CG ALYS A 195      -6.621  39.812 -17.755  0.50 23.67           C  
ANISOU 1643  CG ALYS A 195     2994   2993   3005      8   -204   -100       C  
ATOM   1644  CG BLYS A 195      -6.635  38.316 -19.224  0.50 19.97           C  
ANISOU 1644  CG BLYS A 195     1832   2879   2874   -180     37     33       C  
ATOM   1645  CD ALYS A 195      -8.129  39.720 -17.713  0.50 26.47           C  
ANISOU 1645  CD ALYS A 195     3229   3586   3240    -25     24    182       C  
ATOM   1646  CD BLYS A 195      -8.142  38.497 -19.073  0.50 25.96           C  
ANISOU 1646  CD BLYS A 195     2587   3475   3801    319    244     71       C  
ATOM   1647  CE ALYS A 195      -8.751  41.051 -17.318  0.50 31.41           C  
ANISOU 1647  CE ALYS A 195     3963   4061   3908    278   -103     41       C  
ATOM   1648  CE BLYS A 195      -8.850  38.391 -20.415  0.50 31.23           C  
ANISOU 1648  CE BLYS A 195     3486   4144   4233     49     43     99       C  
ATOM   1649  NZ ALYS A 195     -10.240  41.013 -17.367  0.50 36.30           N  
ANISOU 1649  NZ ALYS A 195     4349   4652   4792     39   -232    252       N  
ATOM   1650  NZ BLYS A 195     -10.329  38.292 -20.256  0.50 36.05           N  
ANISOU 1650  NZ BLYS A 195     3813   5123   4760   -102    228     65       N  
ATOM   1651  N   VAL A 196      -4.116  36.178 -17.460  1.00 14.67           N  
ANISOU 1651  N   VAL A 196      983   2622   1969   -111   -481    180       N  
ATOM   1652  CA  VAL A 196      -3.732  34.787 -17.677  1.00 12.97           C  
ANISOU 1652  CA  VAL A 196      257   2733   1935    105     18    184       C  
ATOM   1653  C   VAL A 196      -4.980  33.948 -17.963  1.00 14.08           C  
ANISOU 1653  C   VAL A 196      450   2840   2057   -432    106     18       C  
ATOM   1654  O   VAL A 196      -5.832  33.809 -17.117  1.00 14.76           O  
ANISOU 1654  O   VAL A 196      453   2787   2366   -200   -451   -231       O  
ATOM   1655  CB  VAL A 196      -3.028  34.222 -16.428  1.00 12.22           C  
ANISOU 1655  CB  VAL A 196      319   2616   1708   -203   -277    135       C  
ATOM   1656  CG1 VAL A 196      -2.747  32.744 -16.606  1.00 12.39           C  
ANISOU 1656  CG1 VAL A 196      303   2629   1776     15   -273    149       C  
ATOM   1657  CG2 VAL A 196      -1.734  35.022 -16.134  1.00 13.65           C  
ANISOU 1657  CG2 VAL A 196      267   2922   1996   -165    -70   -145       C  
ATOM   1658  N   ARG A 197      -5.013  33.348 -19.153  1.00 16.05           N  
ANISOU 1658  N   ARG A 197     1123   2668   2305   -321   -495    153       N  
ATOM   1659  CA  ARG A 197      -6.085  32.461 -19.556  1.00 14.20           C  
ANISOU 1659  CA  ARG A 197      881   2616   1896   -224   -821    -36       C  
ATOM   1660  C   ARG A 197      -5.451  31.326 -20.382  1.00 15.95           C  
ANISOU 1660  C   ARG A 197     1742   2683   1635   -203   -358     56       C  
ATOM   1661  O   ARG A 197      -4.319  31.454 -20.863  1.00 16.89           O  
ANISOU 1661  O   ARG A 197     1917   2859   1639   -596    -42     -8       O  
ATOM   1662  CB  ARG A 197      -7.134  33.217 -20.398  1.00 15.75           C  
ANISOU 1662  CB  ARG A 197      500   3108   2376   -488   -518    221       C  
ATOM   1663  CG  ARG A 197      -7.883  34.350 -19.642  1.00 21.73           C  
ANISOU 1663  CG  ARG A 197     2667   3119   2467    160   -792     58       C  
ATOM   1664  CD  ARG A 197      -8.780  33.802 -18.532  1.00 22.68           C  
ANISOU 1664  CD  ARG A 197     1947   3500   3169    280   -845   -491       C  
ATOM   1665  NE  ARG A 197      -9.584  34.850 -17.892  1.00 24.41           N  
ANISOU 1665  NE  ARG A 197     1610   3872   3790    -76   -598   -666       N  
ATOM   1666  CZ  ARG A 197      -9.197  35.568 -16.838  1.00 22.00           C  
ANISOU 1666  CZ  ARG A 197     1480   3309   3568    -89   -125   -443       C  
ATOM   1667  NH1 ARG A 197      -7.981  35.400 -16.318  1.00 19.72           N  
ANISOU 1667  NH1 ARG A 197      611   4083   2796    -33   -332    255       N  
ATOM   1668  NH2 ARG A 197     -10.004  36.495 -16.330  1.00 27.84           N  
ANISOU 1668  NH2 ARG A 197     2224   4232   4119      8    288   -275       N  
ATOM   1669  N   HIS A 198      -6.179  30.234 -20.528  1.00 14.15           N  
ANISOU 1669  N   HIS A 198     1004   2601   1770   -215   -431   -109       N  
ATOM   1670  CA  HIS A 198      -5.696  29.047 -21.217  1.00 13.90           C  
ANISOU 1670  CA  HIS A 198      862   2769   1647    -28   -260     51       C  
ATOM   1671  C   HIS A 198      -6.781  28.566 -22.173  1.00 13.65           C  
ANISOU 1671  C   HIS A 198      798   2782   1606   -204   -167    -23       C  
ATOM   1672  O   HIS A 198      -7.964  28.698 -21.876  1.00 15.45           O  
ANISOU 1672  O   HIS A 198      718   3326   1824   -333   -408    -39       O  
ATOM   1673  CB  HIS A 198      -5.371  27.943 -20.199  1.00 13.34           C  
ANISOU 1673  CB  HIS A 198      478   2837   1751    -18   -309   -138       C  
ATOM   1674  CG  HIS A 198      -4.247  28.292 -19.276  1.00 12.97           C  
ANISOU 1674  CG  HIS A 198      331   2938   1659   -144   -217    292       C  
ATOM   1675  ND1 HIS A 198      -4.444  28.967 -18.094  1.00 13.48           N  
ANISOU 1675  ND1 HIS A 198      596   3004   1522    -83   -269    -58       N  
ATOM   1676  CD2 HIS A 198      -2.909  28.114 -19.392  1.00 13.90           C  
ANISOU 1676  CD2 HIS A 198      799   2798   1684    -64    324    -90       C  
ATOM   1677  CE1 HIS A 198      -3.279  29.154 -17.503  1.00 13.19           C  
ANISOU 1677  CE1 HIS A 198      893   2673   1446    118     65   -249       C  
ATOM   1678  NE2 HIS A 198      -2.332  28.657 -18.277  1.00 12.98           N  
ANISOU 1678  NE2 HIS A 198      670   2684   1576   -513   -628    -46       N  
ATOM   1679  N   PRO A 199      -6.380  28.053 -23.349  1.00 14.96           N  
ANISOU 1679  N   PRO A 199      915   3024   1744   -411   -175   -171       N  
ATOM   1680  CA  PRO A 199      -7.345  27.761 -24.400  1.00 15.96           C  
ANISOU 1680  CA  PRO A 199     1211   3161   1688   -304   -345   -191       C  
ATOM   1681  C   PRO A 199      -8.344  26.716 -23.957  1.00 14.61           C  
ANISOU 1681  C   PRO A 199      993   2871   1685   -255   -479   -177       C  
ATOM   1682  O   PRO A 199      -7.956  25.627 -23.557  1.00 15.97           O  
ANISOU 1682  O   PRO A 199      765   3008   2292    -92     40   -324       O  
ATOM   1683  CB  PRO A 199      -6.492  27.222 -25.551  1.00 19.09           C  
ANISOU 1683  CB  PRO A 199     1834   3445   1973   -412    -55   -443       C  
ATOM   1684  CG  PRO A 199      -5.094  27.427 -25.177  1.00 20.90           C  
ANISOU 1684  CG  PRO A 199     2124   3754   2062   -452    -15   -479       C  
ATOM   1685  CD  PRO A 199      -4.993  27.772 -23.753  1.00 13.94           C  
ANISOU 1685  CD  PRO A 199      783   2945   1565   -490    -42   -172       C  
ATOM   1686  N   GLY A 200      -9.626  27.031 -24.047  1.00 15.44           N  
ANISOU 1686  N   GLY A 200     1028   3047   1788   -205   -608    -99       N  
ATOM   1687  CA  GLY A 200     -10.651  26.075 -23.704  1.00 14.36           C  
ANISOU 1687  CA  GLY A 200      650   2823   1981   -115   -228   -123       C  
ATOM   1688  C   GLY A 200     -10.772  25.740 -22.221  1.00 15.32           C  
ANISOU 1688  C   GLY A 200     1076   2885   1857   -191   -123   -285       C  
ATOM   1689  O   GLY A 200     -11.464  24.805 -21.867  1.00 17.74           O  
ANISOU 1689  O   GLY A 200      995   3531   2214   -773   -280    -53       O  
ATOM   1690  N   LYS A 201     -10.116  26.520 -21.352  1.00 13.66           N  
ANISOU 1690  N   LYS A 201      637   2942   1611    -30   -230   -113       N  
ATOM   1691  CA  LYS A 201     -10.143  26.245 -19.910  1.00 13.14           C  
ANISOU 1691  CA  LYS A 201      853   2375   1763    -19   -365    -19       C  
ATOM   1692  C   LYS A 201     -10.903  27.313 -19.145  1.00 12.02           C  
ANISOU 1692  C   LYS A 201      383   2627   1554   -102   -409    120       C  
ATOM   1693  O   LYS A 201     -10.918  28.491 -19.527  1.00 13.58           O  
ANISOU 1693  O   LYS A 201      770   2570   1818     55   -219     23       O  
ATOM   1694  CB  LYS A 201      -8.721  26.175 -19.342  1.00 13.36           C  
ANISOU 1694  CB  LYS A 201      775   2554   1745   -156   -450      0       C  
ATOM   1695  CG  LYS A 201      -7.759  25.255 -20.062  1.00 15.51           C  
ANISOU 1695  CG  LYS A 201      964   2631   2298     29   -361    104       C  
ATOM   1696  CD  LYS A 201      -8.249  23.870 -20.157  1.00 20.60           C  
ANISOU 1696  CD  LYS A 201     1387   2998   3441    101   -394    180       C  
ATOM   1697  CE  LYS A 201      -8.206  23.178 -18.831  1.00 22.51           C  
ANISOU 1697  CE  LYS A 201     2876   3349   2326   -735     17    -83       C  
ATOM   1698  NZ  LYS A 201      -8.244  21.665 -18.966  1.00 22.69           N  
ANISOU 1698  NZ  LYS A 201     2612   3212   2797   -402    660    -25       N  
ATOM   1699  N   GLU A 202     -11.523  26.907 -18.046  1.00 13.74           N  
ANISOU 1699  N   GLU A 202      947   2441   1829   -126   -340    119       N  
ATOM   1700  CA  GLU A 202     -12.247  27.830 -17.214  1.00 14.44           C  
ANISOU 1700  CA  GLU A 202     1046   2687   1751    -59   -107     -5       C  
ATOM   1701  C   GLU A 202     -11.275  28.667 -16.387  1.00 12.69           C  
ANISOU 1701  C   GLU A 202      597   2358   1864     57    -30    -44       C  
ATOM   1702  O   GLU A 202     -10.104  28.303 -16.215  1.00 12.80           O  
ANISOU 1702  O   GLU A 202      287   2810   1765    182   -176     61       O  
ATOM   1703  CB  GLU A 202     -13.206  27.071 -16.289  1.00 15.55           C  
ANISOU 1703  CB  GLU A 202      546   3288   2075   -246    -24    289       C  
ATOM   1704  CG  GLU A 202     -14.317  26.261 -17.012  1.00 18.24           C  
ANISOU 1704  CG  GLU A 202      722   3739   2470   -339    173    103       C  
ATOM   1705  CD  GLU A 202     -15.139  27.103 -17.945  1.00 26.56           C  
ANISOU 1705  CD  GLU A 202     2216   3822   4053   -302   -173   -404       C  
ATOM   1706  OE1 GLU A 202     -15.528  28.213 -17.547  1.00 30.09           O  
ANISOU 1706  OE1 GLU A 202     1914   5086   4432    200   -488   -350       O  
ATOM   1707  OE2 GLU A 202     -15.385  26.662 -19.088  1.00 35.09           O  
ANISOU 1707  OE2 GLU A 202     3719   5747   3864   -212  -1062   -323       O  
ATOM   1708  N   THR A 203     -11.748  29.771 -15.850  1.00 12.88           N  
ANISOU 1708  N   THR A 203      364   2493   2035    102   -439    -94       N  
ATOM   1709  CA  THR A 203     -10.879  30.705 -15.174  1.00 12.53           C  
ANISOU 1709  CA  THR A 203      271   2547   1940   -117    125    318       C  
ATOM   1710  C   THR A 203     -10.246  30.109 -13.903  1.00 12.24           C  
ANISOU 1710  C   THR A 203      718   2216   1715   -184   -121    158       C  
ATOM   1711  O   THR A 203      -9.098  30.435 -13.565  1.00 12.24           O  
ANISOU 1711  O   THR A 203      267   2324   2060    119   -121   -125       O  
ATOM   1712  CB  THR A 203     -11.616  32.021 -14.898  1.00 16.52           C  
ANISOU 1712  CB  THR A 203     1214   2657   2405    164   -510     42       C  
ATOM   1713  OG1 THR A 203     -11.995  32.597 -16.153  1.00 19.83           O  
ANISOU 1713  OG1 THR A 203     1391   3326   2814    392   -494    496       O  
ATOM   1714  CG2 THR A 203     -10.761  32.980 -14.157  1.00 18.89           C  
ANISOU 1714  CG2 THR A 203      864   3163   3150      3    254    -54       C  
ATOM   1715  N   SER A 204     -10.912  29.162 -13.266  1.00 11.22           N  
ANISOU 1715  N   SER A 204      266   2391   1603     93   -103    204       N  
ATOM   1716  CA  SER A 204     -10.309  28.525 -12.089  1.00 10.20           C  
ANISOU 1716  CA  SER A 204      300   2091   1481     14     99    -86       C  
ATOM   1717  C   SER A 204      -8.977  27.831 -12.436  1.00 10.77           C  
ANISOU 1717  C   SER A 204      261   2310   1520    -80     83    -11       C  
ATOM   1718  O   SER A 204      -8.029  27.860 -11.643  1.00 11.01           O  
ANISOU 1718  O   SER A 204      295   2429   1458   -130   -199    -71       O  
ATOM   1719  CB  SER A 204     -11.278  27.543 -11.454  1.00 12.49           C  
ANISOU 1719  CB  SER A 204      615   2563   1567     84     47    280       C  
ATOM   1720  OG  SER A 204     -11.599  26.480 -12.335  1.00 11.74           O  
ANISOU 1720  OG  SER A 204      271   2478   1711    -90   -138   -169       O  
ATOM   1721  N   TYR A 205      -8.909  27.211 -13.598  1.00 10.71           N  
ANISOU 1721  N   TYR A 205      259   2392   1417    -35    -79   -225       N  
ATOM   1722  CA  TYR A 205      -7.694  26.537 -14.039  1.00 10.44           C  
ANISOU 1722  CA  TYR A 205      385   2042   1540    -36    406    154       C  
ATOM   1723  C   TYR A 205      -6.571  27.535 -14.114  1.00 10.52           C  
ANISOU 1723  C   TYR A 205      508   2145   1344    201    -85    126       C  
ATOM   1724  O   TYR A 205      -5.459  27.263 -13.642  1.00 10.82           O  
ANISOU 1724  O   TYR A 205      301   2369   1438    212   -177     -3       O  
ATOM   1725  CB  TYR A 205      -7.930  25.905 -15.399  1.00 10.80           C  
ANISOU 1725  CB  TYR A 205      276   2334   1491    170     11     77       C  
ATOM   1726  CG  TYR A 205      -6.751  25.126 -15.909  1.00 10.64           C  
ANISOU 1726  CG  TYR A 205      295   2224   1522    168   -189    -15       C  
ATOM   1727  CD1 TYR A 205      -6.495  23.843 -15.448  1.00 10.52           C  
ANISOU 1727  CD1 TYR A 205      264   2268   1462    -33   -112    -36       C  
ATOM   1728  CD2 TYR A 205      -5.883  25.672 -16.841  1.00 10.99           C  
ANISOU 1728  CD2 TYR A 205      318   2261   1594   -318    151    -62       C  
ATOM   1729  CE1 TYR A 205      -5.419  23.120 -15.901  1.00 11.92           C  
ANISOU 1729  CE1 TYR A 205      266   2296   1967    159     19    -24       C  
ATOM   1730  CE2 TYR A 205      -4.768  24.950 -17.298  1.00 12.45           C  
ANISOU 1730  CE2 TYR A 205      282   2746   1699    108    194    113       C  
ATOM   1731  CZ  TYR A 205      -4.554  23.666 -16.814  1.00 12.92           C  
ANISOU 1731  CZ  TYR A 205      502   2624   1780     74    147   -290       C  
ATOM   1732  OH  TYR A 205      -3.471  22.922 -17.232  1.00 15.68           O  
ANISOU 1732  OH  TYR A 205     1087   2885   1983    545    170     26       O  
ATOM   1733  N   SER A 206      -6.860  28.702 -14.651  1.00  9.69           N  
ANISOU 1733  N   SER A 206      286   1967   1429   -167   -154    151       N  
ATOM   1734  CA  SER A 206      -5.868  29.706 -14.901  1.00 10.18           C  
ANISOU 1734  CA  SER A 206      255   2224   1386    -64      3      2       C  
ATOM   1735  C   SER A 206      -5.470  30.501 -13.669  1.00 11.11           C  
ANISOU 1735  C   SER A 206      295   2443   1482    -47   -227     89       C  
ATOM   1736  O   SER A 206      -4.300  30.923 -13.544  1.00 11.33           O  
ANISOU 1736  O   SER A 206      273   2436   1595    -80   -148    -91       O  
ATOM   1737  CB  SER A 206      -6.380  30.681 -15.954  1.00 10.61           C  
ANISOU 1737  CB  SER A 206      318   1997   1713   -263    162    194       C  
ATOM   1738  OG  SER A 206      -6.715  30.018 -17.137  1.00 11.85           O  
ANISOU 1738  OG  SER A 206      325   2662   1516    -28   -300     55       O  
ATOM   1739  N   MET A 207      -6.422  30.735 -12.769  1.00 10.86           N  
ANISOU 1739  N   MET A 207      277   2434   1414   -102   -147    -41       N  
ATOM   1740  CA  MET A 207      -6.261  31.760 -11.759  1.00 10.98           C  
ANISOU 1740  CA  MET A 207      516   2122   1533     12   -213     76       C  
ATOM   1741  C   MET A 207      -6.442  31.312 -10.302  1.00 10.03           C  
ANISOU 1741  C   MET A 207      426   1787   1596    225    -76    -19       C  
ATOM   1742  O   MET A 207      -5.970  32.002  -9.400  1.00 10.35           O  
ANISOU 1742  O   MET A 207      352   2020   1558    -42   -202    -99       O  
ATOM   1743  CB  MET A 207      -7.187  32.939 -12.044  1.00 11.75           C  
ANISOU 1743  CB  MET A 207      452   2079   1934   -115   -168   -157       C  
ATOM   1744  CG  MET A 207      -6.684  33.871 -13.141  1.00 12.83           C  
ANISOU 1744  CG  MET A 207      670   2439   1763   -169   -523     71       C  
ATOM   1745  SD  MET A 207      -5.184  34.735 -12.695  1.00 13.78           S  
ANISOU 1745  SD  MET A 207      461   2537   2236    -75   -141     74       S  
ATOM   1746  CE  MET A 207      -5.805  35.789 -11.374  1.00 15.87           C  
ANISOU 1746  CE  MET A 207      319   3304   2403    -84   -369    -90       C  
ATOM   1747  N   GLN A 208      -7.027  30.155 -10.046  1.00  9.40           N  
ANISOU 1747  N   GLN A 208      284   1993   1294    165   -136    -99       N  
ATOM   1748  CA  GLN A 208      -7.395  29.886  -8.674  1.00 10.24           C  
ANISOU 1748  CA  GLN A 208      435   1990   1463    -99   -460    -27       C  
ATOM   1749  C   GLN A 208      -6.131  29.789  -7.796  1.00  9.49           C  
ANISOU 1749  C   GLN A 208      307   1961   1337   -199    209   -246       C  
ATOM   1750  O   GLN A 208      -6.106  30.270  -6.685  1.00 10.25           O  
ANISOU 1750  O   GLN A 208      261   2119   1513    -52    -86   -171       O  
ATOM   1751  CB  GLN A 208      -8.255  28.629  -8.528  1.00  9.86           C  
ANISOU 1751  CB  GLN A 208      310   1828   1607    135   -249     -7       C  
ATOM   1752  CG  GLN A 208      -8.667  28.402  -7.076  1.00  9.54           C  
ANISOU 1752  CG  GLN A 208      254   1973   1394     30     27    -48       C  
ATOM   1753  CD  GLN A 208      -9.754  27.389  -6.889  1.00  9.39           C  
ANISOU 1753  CD  GLN A 208      282   1909   1374      0   -179    -88       C  
ATOM   1754  OE1 GLN A 208     -10.324  26.886  -7.860  1.00 10.69           O  
ANISOU 1754  OE1 GLN A 208      253   2407   1400     14    -15   -150       O  
ATOM   1755  NE2 GLN A 208     -10.058  27.085  -5.633  1.00  9.73           N  
ANISOU 1755  NE2 GLN A 208      279   2054   1363    218      3     86       N  
ATOM   1756  N   HIS A 209      -5.084  29.162  -8.323  1.00  9.76           N  
ANISOU 1756  N   HIS A 209      255   2233   1219     21    -45    -65       N  
ATOM   1757  CA  HIS A 209      -3.838  28.996  -7.548  1.00  9.73           C  
ANISOU 1757  CA  HIS A 209      403   1922   1372   -116   -409    216       C  
ATOM   1758  C   HIS A 209      -3.073  30.324  -7.382  1.00  9.22           C  
ANISOU 1758  C   HIS A 209      280   2096   1124    -69    148    -30       C  
ATOM   1759  O   HIS A 209      -2.297  30.480  -6.442  1.00 10.52           O  
ANISOU 1759  O   HIS A 209      323   2217   1457   -104   -281     66       O  
ATOM   1760  CB  HIS A 209      -2.903  27.942  -8.188  1.00 10.29           C  
ANISOU 1760  CB  HIS A 209      271   2027   1611    174     50     96       C  
ATOM   1761  CG  HIS A 209      -2.569  28.228  -9.605  1.00  9.65           C  
ANISOU 1761  CG  HIS A 209      307   2065   1292    261    137     56       C  
ATOM   1762  ND1 HIS A 209      -3.466  28.025 -10.626  1.00 10.74           N  
ANISOU 1762  ND1 HIS A 209      452   2280   1349     -9   -466    -35       N  
ATOM   1763  CD2 HIS A 209      -1.440  28.722 -10.179  1.00 11.18           C  
ANISOU 1763  CD2 HIS A 209      328   2342   1576     78    304   -111       C  
ATOM   1764  CE1 HIS A 209      -2.923  28.413 -11.760  1.00 12.01           C  
ANISOU 1764  CE1 HIS A 209      475   2737   1350    162   -319    103       C  
ATOM   1765  NE2 HIS A 209      -1.676  28.804 -11.517  1.00 10.82           N  
ANISOU 1765  NE2 HIS A 209      254   2321   1534     34     17    -43       N  
ATOM   1766  N   ILE A 210      -3.312  31.258  -8.278  1.00  9.53           N  
ANISOU 1766  N   ILE A 210      275   2001   1343   -174     57    158       N  
ATOM   1767  CA  ILE A 210      -2.740  32.559  -8.191  1.00  9.98           C  
ANISOU 1767  CA  ILE A 210      334   1852   1603    183   -280     41       C  
ATOM   1768  C   ILE A 210      -3.460  33.404  -7.162  1.00 10.34           C  
ANISOU 1768  C   ILE A 210      429   2008   1491   -141   -448    -35       C  
ATOM   1769  O   ILE A 210      -2.847  33.983  -6.272  1.00 10.19           O  
ANISOU 1769  O   ILE A 210      289   2098   1484   -148   -118    -84       O  
ATOM   1770  CB  ILE A 210      -2.679  33.226  -9.575  1.00  9.99           C  
ANISOU 1770  CB  ILE A 210      310   1924   1561   -194   -231    183       C  
ATOM   1771  CG1 ILE A 210      -1.763  32.403 -10.487  1.00 12.38           C  
ANISOU 1771  CG1 ILE A 210      995   1977   1731    383      6    135       C  
ATOM   1772  CG2 ILE A 210      -2.260  34.656  -9.467  1.00 12.02           C  
ANISOU 1772  CG2 ILE A 210      597   2156   1812    104     38    229       C  
ATOM   1773  CD1 ILE A 210      -1.663  32.874 -11.929  1.00 12.15           C  
ANISOU 1773  CD1 ILE A 210      322   2425   1870     88    -25    151       C  
ATOM   1774  N  AARG A 211      -4.787  33.446  -7.263  0.50 10.27           N  
ANISOU 1774  N  AARG A 211      318   2131   1452   -133   -255    -49       N  
ATOM   1775  N  BARG A 211      -4.792  33.439  -7.243  0.50 10.20           N  
ANISOU 1775  N  BARG A 211      318   2109   1446   -141   -251    -48       N  
ATOM   1776  CA AARG A 211      -5.589  34.101  -6.255  0.50  9.68           C  
ANISOU 1776  CA AARG A 211      450   1823   1404   -307   -252     35       C  
ATOM   1777  CA BARG A 211      -5.558  34.133  -6.230  0.50  9.25           C  
ANISOU 1777  CA BARG A 211      403   1737   1372   -349   -257     24       C  
ATOM   1778  C  AARG A 211      -5.285  33.542  -4.862  0.50  9.75           C  
ANISOU 1778  C  AARG A 211      258   1937   1509     76    -53   -152       C  
ATOM   1779  C  BARG A 211      -5.292  33.545  -4.844  0.50  9.63           C  
ANISOU 1779  C  BARG A 211      259   1924   1475     79    -59   -152       C  
ATOM   1780  O  AARG A 211      -5.169  34.285  -3.903  0.50 10.02           O  
ANISOU 1780  O  AARG A 211      253   2004   1548     19    -21   -140       O  
ATOM   1781  O  BARG A 211      -5.212  34.269  -3.868  0.50  9.96           O  
ANISOU 1781  O  BARG A 211      253   2000   1528      0      0   -148       O  
ATOM   1782  CB AARG A 211      -7.089  33.929  -6.573  0.50 10.88           C  
ANISOU 1782  CB AARG A 211      309   2204   1620     20   -277     42       C  
ATOM   1783  CB BARG A 211      -7.073  34.096  -6.530  0.50 10.84           C  
ANISOU 1783  CB BARG A 211      326   2327   1465     -9   -298      4       C  
ATOM   1784  CG AARG A 211      -7.998  34.355  -5.436  0.50 12.96           C  
ANISOU 1784  CG AARG A 211      420   2461   2040    181   -508    143       C  
ATOM   1785  CG BARG A 211      -7.869  34.878  -5.493  0.50 11.92           C  
ANISOU 1785  CG BARG A 211      376   1918   2235    210   -427     77       C  
ATOM   1786  CD AARG A 211      -7.750  35.810  -5.028  0.50 15.12           C  
ANISOU 1786  CD AARG A 211      720   2588   2435    385   -119    263       C  
ATOM   1787  CD BARG A 211      -9.365  34.791  -5.687  0.50 12.88           C  
ANISOU 1787  CD BARG A 211      574   2069   2248    353   -270    194       C  
ATOM   1788  NE AARG A 211      -8.542  36.199  -3.860  0.50 15.01           N  
ANISOU 1788  NE AARG A 211      266   2796   2640     16   -174    171       N  
ATOM   1789  NE BARG A 211     -10.072  35.308  -4.516  0.50 22.55           N  
ANISOU 1789  NE BARG A 211     1908   3225   3432    125    494    171       N  
ATOM   1790  CZ AARG A 211      -9.686  36.869  -3.920  0.50 20.79           C  
ANISOU 1790  CZ AARG A 211     1626   3377   2897    363     43    122       C  
ATOM   1791  CZ BARG A 211     -10.180  36.603  -4.213  0.50 26.32           C  
ANISOU 1791  CZ BARG A 211     2250   3799   3949    427    225     -9       C  
ATOM   1792  NH1AARG A 211     -10.191  37.207  -5.093  0.50 20.71           N  
ANISOU 1792  NH1AARG A 211      560   3688   3619   1025     57    356       N  
ATOM   1793  NH1BARG A 211      -9.651  37.526  -5.010  0.50 32.47           N  
ANISOU 1793  NH1BARG A 211     3229   4408   4699    278     82    124       N  
ATOM   1794  NH2AARG A 211     -10.327  37.190  -2.806  0.50 26.20           N  
ANISOU 1794  NH2AARG A 211     2588   3942   3422    253   -266   -241       N  
ATOM   1795  NH2BARG A 211     -10.828  36.976  -3.117  0.50 35.47           N  
ANISOU 1795  NH2BARG A 211     4293   4854   4329    231    300   -321       N  
ATOM   1796  N   GLU A 212      -5.209  32.230  -4.752  1.00  9.21           N  
ANISOU 1796  N   GLU A 212      267   1936   1296    -52   -109   -115       N  
ATOM   1797  CA  GLU A 212      -5.050  31.613  -3.443  1.00  9.62           C  
ANISOU 1797  CA  GLU A 212      291   1991   1370    172      3   -165       C  
ATOM   1798  C   GLU A 212      -3.671  31.847  -2.802  1.00  9.88           C  
ANISOU 1798  C   GLU A 212      340   2230   1182    278    216     44       C  
ATOM   1799  O   GLU A 212      -3.576  32.048  -1.633  1.00 10.01           O  
ANISOU 1799  O   GLU A 212      261   2155   1385     35    -93    -34       O  
ATOM   1800  CB  GLU A 212      -5.423  30.151  -3.476  1.00  9.59           C  
ANISOU 1800  CB  GLU A 212      337   2042   1262    159     56    131       C  
ATOM   1801  CG  GLU A 212      -6.956  30.015  -3.646  1.00 10.83           C  
ANISOU 1801  CG  GLU A 212      261   2209   1643    -24   -105    -79       C  
ATOM   1802  CD  GLU A 212      -7.504  28.610  -3.622  1.00 10.72           C  
ANISOU 1802  CD  GLU A 212      287   2157   1629    -22    214     -8       C  
ATOM   1803  OE1 GLU A 212      -6.762  27.634  -3.738  1.00 10.82           O  
ANISOU 1803  OE1 GLU A 212      273   2139   1700    140      6    112       O  
ATOM   1804  OE2 GLU A 212      -8.761  28.493  -3.503  1.00 11.66           O  
ANISOU 1804  OE2 GLU A 212      265   2497   1665   -131     84   -133       O  
ATOM   1805  N   GLN A 213      -2.641  31.942  -3.619  1.00 10.39           N  
ANISOU 1805  N   GLN A 213      436   2212   1299     -1   -432   -216       N  
ATOM   1806  CA  GLN A 213      -1.363  32.397  -3.111  1.00  8.95           C  
ANISOU 1806  CA  GLN A 213      305   2015   1081   -118   -187    -51       C  
ATOM   1807  C   GLN A 213      -1.525  33.792  -2.497  1.00  9.34           C  
ANISOU 1807  C   GLN A 213      366   1984   1199   -169    286    135       C  
ATOM   1808  O   GLN A 213      -1.079  34.053  -1.357  1.00 10.07           O  
ANISOU 1808  O   GLN A 213      257   2173   1395    -45     60    -42       O  
ATOM   1809  CB  GLN A 213      -0.300  32.372  -4.227  1.00  9.76           C  
ANISOU 1809  CB  GLN A 213      285   2116   1306    147   -154   -100       C  
ATOM   1810  CG  GLN A 213       0.202  30.968  -4.529  1.00 10.23           C  
ANISOU 1810  CG  GLN A 213      309   2361   1217     51   -229    -20       C  
ATOM   1811  CD  GLN A 213       1.175  30.934  -5.674  1.00 10.31           C  
ANISOU 1811  CD  GLN A 213      291   2180   1445    -37   -210     -2       C  
ATOM   1812  OE1 GLN A 213       2.405  31.042  -5.465  1.00 11.43           O  
ANISOU 1812  OE1 GLN A 213      272   2328   1742     94   -153   -133       O  
ATOM   1813  NE2 GLN A 213       0.680  30.757  -6.872  1.00 10.77           N  
ANISOU 1813  NE2 GLN A 213      312   2305   1473    189      0     80       N  
ATOM   1814  N   LEU A 214      -2.168  34.712  -3.225  1.00  9.22           N  
ANISOU 1814  N   LEU A 214      275   1927   1299   -193    -17    156       N  
ATOM   1815  CA  LEU A 214      -2.385  36.015  -2.686  1.00  9.56           C  
ANISOU 1815  CA  LEU A 214      287   1942   1402   -157   -159    123       C  
ATOM   1816  C   LEU A 214      -3.231  35.955  -1.391  1.00 10.04           C  
ANISOU 1816  C   LEU A 214      280   2217   1317   -229    -13   -132       C  
ATOM   1817  O   LEU A 214      -3.001  36.701  -0.472  1.00 10.16           O  
ANISOU 1817  O   LEU A 214      286   2108   1465     90   -192   -146       O  
ATOM   1818  CB  LEU A 214      -3.011  36.958  -3.729  1.00 10.68           C  
ANISOU 1818  CB  LEU A 214      416   2020   1620      4    157     11       C  
ATOM   1819  CG  LEU A 214      -2.105  37.257  -4.911  1.00 12.24           C  
ANISOU 1819  CG  LEU A 214      763   2329   1556   -333    225     56       C  
ATOM   1820  CD1 LEU A 214      -2.848  37.981  -5.993  1.00 13.96           C  
ANISOU 1820  CD1 LEU A 214     1040   2614   1650   -307    -89    475       C  
ATOM   1821  CD2 LEU A 214      -0.940  38.065  -4.466  1.00 14.88           C  
ANISOU 1821  CD2 LEU A 214      542   3002   2107   -688   -278    244       C  
ATOM   1822  N   ASN A 215      -4.254  35.079  -1.362  1.00  9.56           N  
ANISOU 1822  N   ASN A 215      288   2013   1331     22   -194    -99       N  
ATOM   1823  CA  ASN A 215      -5.034  34.896  -0.138  1.00 10.12           C  
ANISOU 1823  CA  ASN A 215      289   2260   1297     -1   -192    -93       C  
ATOM   1824  C   ASN A 215      -4.174  34.601   1.082  1.00  9.63           C  
ANISOU 1824  C   ASN A 215      389   1725   1543     74    -63   -116       C  
ATOM   1825  O   ASN A 215      -4.487  35.040   2.183  1.00 10.01           O  
ANISOU 1825  O   ASN A 215      281   2186   1336   -188     92   -106       O  
ATOM   1826  CB  ASN A 215      -6.053  33.737  -0.307  1.00 10.82           C  
ANISOU 1826  CB  ASN A 215      303   2143   1665    -55   -252   -227       C  
ATOM   1827  CG  ASN A 215      -7.273  34.101  -1.127  1.00 11.58           C  
ANISOU 1827  CG  ASN A 215      291   2447   1662   -268    133   -404       C  
ATOM   1828  OD1 ASN A 215      -7.515  35.264  -1.447  1.00 13.47           O  
ANISOU 1828  OD1 ASN A 215      287   2424   2407    105   -252    -41       O  
ATOM   1829  ND2 ASN A 215      -8.044  33.077  -1.467  1.00 12.32           N  
ANISOU 1829  ND2 ASN A 215      281   2399   1998   -164   -148   -214       N  
ATOM   1830  N   TYR A 216      -3.147  33.777   0.919  1.00 10.01           N  
ANISOU 1830  N   TYR A 216      266   2195   1340     20     81   -178       N  
ATOM   1831  CA  TYR A 216      -2.324  33.424   2.069  1.00 10.12           C  
ANISOU 1831  CA  TYR A 216      347   2100   1399    120    122   -110       C  
ATOM   1832  C   TYR A 216      -1.503  34.623   2.542  1.00  9.57           C  
ANISOU 1832  C   TYR A 216      254   2165   1216    -20    -29    -21       C  
ATOM   1833  O   TYR A 216      -1.307  34.796   3.715  1.00 10.60           O  
ANISOU 1833  O   TYR A 216      254   2332   1442    -10     41    -71       O  
ATOM   1834  CB  TYR A 216      -1.456  32.155   1.785  1.00 12.43           C  
ANISOU 1834  CB  TYR A 216      768   2663   1290    212   -120    -71       C  
ATOM   1835  CG  TYR A 216      -2.343  30.959   1.518  1.00 11.53           C  
ANISOU 1835  CG  TYR A 216      328   2279   1770     55     81   -102       C  
ATOM   1836  CD1 TYR A 216      -3.365  30.637   2.389  1.00 11.15           C  
ANISOU 1836  CD1 TYR A 216      374   2337   1524    165   -157   -378       C  
ATOM   1837  CD2 TYR A 216      -2.225  30.227   0.352  1.00 12.28           C  
ANISOU 1837  CD2 TYR A 216      532   2507   1627    380     50   -200       C  
ATOM   1838  CE1 TYR A 216      -4.243  29.616   2.119  1.00 12.91           C  
ANISOU 1838  CE1 TYR A 216      742   2385   1778    118   -185   -205       C  
ATOM   1839  CE2 TYR A 216      -3.114  29.203   0.069  1.00 13.06           C  
ANISOU 1839  CE2 TYR A 216     1080   2304   1576    290   -162   -256       C  
ATOM   1840  CZ  TYR A 216      -4.127  28.909   0.971  1.00 12.46           C  
ANISOU 1840  CZ  TYR A 216      731   2386   1614    155   -323   -272       C  
ATOM   1841  OH  TYR A 216      -5.080  27.920   0.677  1.00 13.74           O  
ANISOU 1841  OH  TYR A 216      791   2355   2074    358   -121   -317       O  
ATOM   1842  N  ALEU A 217      -1.086  35.463   1.617  0.50 10.25           N  
ANISOU 1842  N  ALEU A 217      282   2282   1331    148   -140     -4       N  
ATOM   1843  N  BLEU A 217      -1.055  35.468   1.615  0.50 10.22           N  
ANISOU 1843  N  BLEU A 217      276   2309   1296    164   -102      7       N  
ATOM   1844  CA ALEU A 217      -0.410  36.685   1.980  0.50 11.51           C  
ANISOU 1844  CA ALEU A 217      569   2318   1486   -199      7     59       C  
ATOM   1845  CA BLEU A 217      -0.437  36.740   2.014  0.50 11.70           C  
ANISOU 1845  CA BLEU A 217      517   2423   1502   -147     82     60       C  
ATOM   1846  C  ALEU A 217      -1.382  37.691   2.657  0.50 10.30           C  
ANISOU 1846  C  ALEU A 217      478   2217   1216   -417   -318   -189       C  
ATOM   1847  C  BLEU A 217      -1.424  37.602   2.767  0.50 10.08           C  
ANISOU 1847  C  BLEU A 217      388   2212   1228   -326   -241   -212       C  
ATOM   1848  O  ALEU A 217      -0.970  38.494   3.504  0.50 11.82           O  
ANISOU 1848  O  ALEU A 217      496   2290   1704   -404   -258    164       O  
ATOM   1849  O  BLEU A 217      -1.069  38.264   3.749  0.50 11.06           O  
ANISOU 1849  O  BLEU A 217      346   2418   1435   -219    -81    215       O  
ATOM   1850  CB ALEU A 217       0.250  37.297   0.739  0.50 11.54           C  
ANISOU 1850  CB ALEU A 217      281   2566   1536   -241     43    155       C  
ATOM   1851  CB BLEU A 217       0.084  37.518   0.804  0.50 12.87           C  
ANISOU 1851  CB BLEU A 217      304   2801   1784   -254    154    105       C  
ATOM   1852  CG ALEU A 217       1.453  38.202   0.911  0.50  9.60           C  
ANISOU 1852  CG ALEU A 217      277   1717   1651    -34    175    148       C  
ATOM   1853  CG BLEU A 217       1.492  37.245   0.329  0.50 10.63           C  
ANISOU 1853  CG BLEU A 217      341   2183   1512    140    320     88       C  
ATOM   1854  CD1ALEU A 217       2.589  37.480   1.634  0.50 13.75           C  
ANISOU 1854  CD1ALEU A 217      428   2198   2596   -313   -587    328       C  
ATOM   1855  CD1BLEU A 217       1.761  38.016  -0.957  0.50 12.79           C  
ANISOU 1855  CD1BLEU A 217      292   2664   1904    221   -171     50       C  
ATOM   1856  CD2ALEU A 217       1.914  38.726  -0.450  0.50 11.63           C  
ANISOU 1856  CD2ALEU A 217      413   2093   1910    502    300    392       C  
ATOM   1857  CD2BLEU A 217       2.524  37.622   1.409  0.50 13.81           C  
ANISOU 1857  CD2BLEU A 217      448   2694   2103    234   -488    577       C  
ATOM   1858  N   GLU A 218      -2.666  37.618   2.300  1.00 10.64           N  
ANISOU 1858  N   GLU A 218      354   2253   1433   -238   -208   -163       N  
ATOM   1859  CA  GLU A 218      -3.668  38.429   2.942  1.00 10.79           C  
ANISOU 1859  CA  GLU A 218      463   2041   1595   -422    -59   -179       C  
ATOM   1860  C   GLU A 218      -4.001  37.906   4.349  1.00 10.67           C  
ANISOU 1860  C   GLU A 218      326   2109   1619   -292   -169   -134       C  
ATOM   1861  O   GLU A 218      -4.154  38.693   5.294  1.00 11.91           O  
ANISOU 1861  O   GLU A 218      373   2396   1755   -282    110   -241       O  
ATOM   1862  CB  GLU A 218      -4.934  38.471   2.088  1.00 11.19           C  
ANISOU 1862  CB  GLU A 218      296   2324   1630    -89    234    -81       C  
ATOM   1863  CG  GLU A 218      -5.999  39.445   2.599  1.00 13.63           C  
ANISOU 1863  CG  GLU A 218      434   2466   2276   -176    349   -174       C  
ATOM   1864  CD  GLU A 218      -7.219  39.481   1.707  1.00 19.27           C  
ANISOU 1864  CD  GLU A 218     1235   3192   2893     11   -137    227       C  
ATOM   1865  OE1 GLU A 218      -7.915  38.438   1.619  1.00 19.90           O  
ANISOU 1865  OE1 GLU A 218      704   3219   3636    334   -246    394       O  
ATOM   1866  OE2 GLU A 218      -7.470  40.552   1.096  1.00 21.30           O  
ANISOU 1866  OE2 GLU A 218     1114   3295   3684   -112    115    481       O  
ATOM   1867  N   LEU A 219      -4.072  36.583   4.494  1.00 10.37           N  
ANISOU 1867  N   LEU A 219      274   2191   1473   -170    -75   -150       N  
ATOM   1868  CA  LEU A 219      -4.263  35.981   5.804  1.00 10.27           C  
ANISOU 1868  CA  LEU A 219      305   2280   1316     -4    136    -34       C  
ATOM   1869  C   LEU A 219      -3.102  36.243   6.761  1.00 11.03           C  
ANISOU 1869  C   LEU A 219      704   2359   1124   -300    108     36       C  
ATOM   1870  O   LEU A 219      -3.287  36.251   7.961  1.00 12.48           O  
ANISOU 1870  O   LEU A 219      430   2854   1454   -190     16    -65       O  
ATOM   1871  CB  LEU A 219      -4.512  34.475   5.666  1.00 10.42           C  
ANISOU 1871  CB  LEU A 219      254   2263   1442     30     39    143       C  
ATOM   1872  CG  LEU A 219      -5.901  34.083   5.144  1.00 12.05           C  
ANISOU 1872  CG  LEU A 219      309   2286   1984   -175   -277    150       C  
ATOM   1873  CD1 LEU A 219      -5.903  32.669   4.676  1.00 13.14           C  
ANISOU 1873  CD1 LEU A 219      254   2806   1930    -64     -8    150       C  
ATOM   1874  CD2 LEU A 219      -6.935  34.302   6.231  1.00 14.55           C  
ANISOU 1874  CD2 LEU A 219      589   2762   2177   -155    802   -235       C  
ATOM   1875  N   ALA A 220      -1.914  36.444   6.205  1.00 11.16           N  
ANISOU 1875  N   ALA A 220      589   2383   1267   -226    138    -21       N  
ATOM   1876  CA  ALA A 220      -0.720  36.825   6.976  1.00 12.17           C  
ANISOU 1876  CA  ALA A 220      762   2479   1383   -182   -191     42       C  
ATOM   1877  C   ALA A 220      -0.756  38.319   7.360  1.00 11.25           C  
ANISOU 1877  C   ALA A 220      259   2537   1478   -110    -24   -213       C  
ATOM   1878  O   ALA A 220       0.124  38.807   8.069  1.00 13.86           O  
ANISOU 1878  O   ALA A 220      449   2902   1913   -515   -161   -322       O  
ATOM   1879  CB  ALA A 220       0.527  36.516   6.164  1.00 12.45           C  
ANISOU 1879  CB  ALA A 220      355   2783   1591   -172    -84    204       C  
ATOM   1880  N  AASN A 221      -1.807  39.020   6.920  0.50 12.03           N  
ANISOU 1880  N  AASN A 221      377   2450   1742    -66   -193   -120       N  
ATOM   1881  N  BASN A 221      -1.769  39.024   6.851  0.50 12.50           N  
ANISOU 1881  N  BASN A 221      453   2425   1869   -198   -288    -21       N  
ATOM   1882  CA AASN A 221      -1.965  40.455   7.172  0.50 13.09           C  
ANISOU 1882  CA AASN A 221      480   2633   1859   -246     66   -110       C  
ATOM   1883  CA BASN A 221      -1.981  40.434   7.140  0.50 13.09           C  
ANISOU 1883  CA BASN A 221      478   2630   1863   -320     36   -107       C  
ATOM   1884  C  AASN A 221      -0.884  41.318   6.520  0.50 12.68           C  
ANISOU 1884  C  AASN A 221      477   2416   1924   -409     83   -288       C  
ATOM   1885  C  BASN A 221      -0.995  41.366   6.423  0.50 13.62           C  
ANISOU 1885  C  BASN A 221      843   2445   1883   -304     -5   -166       C  
ATOM   1886  O  AASN A 221      -0.593  42.410   6.993  0.50 16.06           O  
ANISOU 1886  O  AASN A 221     1361   2650   2091   -408    679   -610       O  
ATOM   1887  O  BASN A 221      -0.900  42.548   6.743  0.50 12.60           O  
ANISOU 1887  O  BASN A 221      397   2512   1878   -559    -44   -192       O  
ATOM   1888  CB AASN A 221      -2.001  40.734   8.675  0.50 16.24           C  
ANISOU 1888  CB AASN A 221     1435   2615   2120   -324    100   -281       C  
ATOM   1889  CB BASN A 221      -1.927  40.687   8.635  0.50 16.95           C  
ANISOU 1889  CB BASN A 221     1548   2723   2170   -417    153   -255       C  
ATOM   1890  CG AASN A 221      -3.349  40.460   9.276  0.50 13.99           C  
ANISOU 1890  CG AASN A 221      699   2549   2065    159   -614    198       C  
ATOM   1891  CG BASN A 221      -2.723  41.877   9.031  0.50 15.33           C  
ANISOU 1891  CG BASN A 221     1276   2676   1872   -604    406      7       C  
ATOM   1892  OD1AASN A 221      -4.360  40.444   8.573  0.50 14.83           O  
ANISOU 1892  OD1AASN A 221      417   3148   2068   -254    368    298       O  
ATOM   1893  OD1BASN A 221      -3.686  42.240   8.352  0.50 21.42           O  
ANISOU 1893  OD1BASN A 221     2501   3010   2627    422    581   -431       O  
ATOM   1894  ND2AASN A 221      -3.383  40.248  10.586  0.50 15.84           N  
ANISOU 1894  ND2AASN A 221     1173   2785   2061    -77    353    -50       N  
ATOM   1895  ND2BASN A 221      -2.322  42.531  10.121  0.50 19.66           N  
ANISOU 1895  ND2BASN A 221     2320   2750   2399   -100    480    -50       N  
ATOM   1896  N   LEU A 222      -0.324  40.847   5.414  1.00 12.32           N  
ANISOU 1896  N   LEU A 222      733   2342   1606   -416    -46   -162       N  
ATOM   1897  CA  LEU A 222       0.726  41.605   4.735  1.00 12.72           C  
ANISOU 1897  CA  LEU A 222      821   2230   1780   -432    185   -184       C  
ATOM   1898  C   LEU A 222       0.191  42.409   3.556  1.00 12.27           C  
ANISOU 1898  C   LEU A 222      395   2260   2004   -497    182      0       C  
ATOM   1899  O   LEU A 222       0.784  43.438   3.179  1.00 13.15           O  
ANISOU 1899  O   LEU A 222      670   2223   2102   -483    337    -37       O  
ATOM   1900  CB  LEU A 222       1.854  40.690   4.305  1.00 12.63           C  
ANISOU 1900  CB  LEU A 222      370   2735   1692   -410    265     -1       C  
ATOM   1901  CG  LEU A 222       2.454  39.890   5.451  1.00 13.87           C  
ANISOU 1901  CG  LEU A 222      866   2801   1601   -432    181    -60       C  
ATOM   1902  CD1 LEU A 222       3.579  39.033   4.951  1.00 20.76           C  
ANISOU 1902  CD1 LEU A 222     1352   4000   2536    634    628    602       C  
ATOM   1903  CD2 LEU A 222       2.904  40.815   6.609  1.00 17.51           C  
ANISOU 1903  CD2 LEU A 222     1340   2937   2376   -447   -508    213       C  
ATOM   1904  N   ILE A 223      -0.961  41.990   3.024  1.00 12.33           N  
ANISOU 1904  N   ILE A 223      390   2330   1962   -166    173    -39       N  
ATOM   1905  CA  ILE A 223      -1.600  42.695   1.920  1.00 12.94           C  
ANISOU 1905  CA  ILE A 223      451   2408   2055   -300    534    -30       C  
ATOM   1906  C   ILE A 223      -3.091  42.734   2.100  1.00 13.37           C  
ANISOU 1906  C   ILE A 223      580   2509   1989    -88    745     95       C  
ATOM   1907  O   ILE A 223      -3.636  42.032   2.936  1.00 13.70           O  
ANISOU 1907  O   ILE A 223      496   2489   2220   -161    467    -18       O  
ATOM   1908  CB  ILE A 223      -1.280  42.046   0.577  1.00 14.42           C  
ANISOU 1908  CB  ILE A 223      991   2902   1583   -482    542   -245       C  
ATOM   1909  CG1 ILE A 223      -1.919  40.635   0.481  1.00 12.04           C  
ANISOU 1909  CG1 ILE A 223      273   2308   1992     45    185    124       C  
ATOM   1910  CG2 ILE A 223       0.265  42.007   0.346  1.00 17.86           C  
ANISOU 1910  CG2 ILE A 223      536   3504   2745   -634    719   -509       C  
ATOM   1911  CD1 ILE A 223      -1.941  39.991  -0.901  1.00 12.83           C  
ANISOU 1911  CD1 ILE A 223      379   2583   1911   -109    448      5       C  
ATOM   1912  N  AARG A 224      -3.743  43.577   1.305  0.50 13.67           N  
ANISOU 1912  N  AARG A 224      340   2419   2433   -269    312    227       N  
ATOM   1913  N  BARG A 224      -3.744  43.579   1.311  0.50 13.72           N  
ANISOU 1913  N  BARG A 224      341   2429   2441   -265    319    222       N  
ATOM   1914  CA AARG A 224      -5.191  43.593   1.200  0.50 15.95           C  
ANISOU 1914  CA AARG A 224      975   2525   2557     20    300    132       C  
ATOM   1915  CA BARG A 224      -5.188  43.565   1.191  0.50 16.38           C  
ANISOU 1915  CA BARG A 224     1083   2589   2552     51    318    123       C  
ATOM   1916  C  AARG A 224      -5.553  43.543  -0.283  0.50 15.82           C  
ANISOU 1916  C  AARG A 224      915   2366   2730    222    178    266       C  
ATOM   1917  C  BARG A 224      -5.549  43.535  -0.284  0.50 15.94           C  
ANISOU 1917  C  BARG A 224      932   2381   2741    226    174    259       C  
ATOM   1918  O  AARG A 224      -5.021  44.325  -1.088  0.50 16.99           O  
ANISOU 1918  O  AARG A 224      667   2909   2879   -267    124    478       O  
ATOM   1919  O  BARG A 224      -5.016  44.321  -1.083  0.50 17.12           O  
ANISOU 1919  O  BARG A 224      704   2915   2884   -267    132    474       O  
ATOM   1920  CB AARG A 224      -5.753  44.862   1.841  0.50 17.94           C  
ANISOU 1920  CB AARG A 224     1132   2924   2759    162     60    111       C  
ATOM   1921  CB BARG A 224      -5.790  44.792   1.863  0.50 19.05           C  
ANISOU 1921  CB BARG A 224     1334   3048   2857    175     85     77       C  
ATOM   1922  CG AARG A 224      -7.271  44.901   1.914  0.50 18.49           C  
ANISOU 1922  CG AARG A 224      882   2832   3310   -337   -107    383       C  
ATOM   1923  CG BARG A 224      -6.287  44.533   3.278  0.50 22.81           C  
ANISOU 1923  CG BARG A 224     2211   3469   2986    228    333     32       C  
ATOM   1924  CD AARG A 224      -7.780  44.876   3.367  0.50 27.71           C  
ANISOU 1924  CD AARG A 224     2731   3934   3862    161      0   -193       C  
ATOM   1925  CD BARG A 224      -7.685  43.905   3.278  0.50 31.18           C  
ANISOU 1925  CD BARG A 224     3368   4318   4161   -128   -101     32       C  
ATOM   1926  NE AARG A 224      -8.306  43.564   3.766  0.50 33.16           N  
ANISOU 1926  NE AARG A 224     4042   3898   4658    133     79    263       N  
ATOM   1927  NE BARG A 224      -7.700  42.549   3.831  0.50 35.59           N  
ANISOU 1927  NE BARG A 224     3851   4832   4837    247    -60    -51       N  
ATOM   1928  CZ AARG A 224      -9.045  42.780   2.983  0.50 30.50           C  
ANISOU 1928  CZ AARG A 224     3204   4012   4372    224    -66    -44       C  
ATOM   1929  CZ BARG A 224      -7.873  42.270   5.121  0.50 32.92           C  
ANISOU 1929  CZ BARG A 224     3345   4657   4502     68    126    162       C  
ATOM   1930  NH1AARG A 224      -9.352  43.164   1.761  0.50 36.98           N  
ANISOU 1930  NH1AARG A 224     4416   4841   4792     86    116     -1       N  
ATOM   1931  NH1BARG A 224      -8.028  43.255   6.002  0.50 39.82           N  
ANISOU 1931  NH1BARG A 224     4384   5345   5400   -230   -106     39       N  
ATOM   1932  NH2AARG A 224      -9.479  41.610   3.431  0.50 28.19           N  
ANISOU 1932  NH2AARG A 224     1708   4586   4415    313    127    -33       N  
ATOM   1933  NH2BARG A 224      -7.886  41.009   5.533  0.50 27.29           N  
ANISOU 1933  NH2BARG A 224     1826   4143   4398    739    252   -617       N  
ATOM   1934  N   ILE A 225      -6.374  42.560  -0.653  1.00 13.47           N  
ANISOU 1934  N   ILE A 225      341   2399   2376    322    390    799       N  
ATOM   1935  CA  ILE A 225      -6.816  42.382  -2.001  1.00 14.22           C  
ANISOU 1935  CA  ILE A 225      289   2817   2295    292    122    447       C  
ATOM   1936  C   ILE A 225      -8.210  42.991  -2.103  1.00 15.19           C  
ANISOU 1936  C   ILE A 225      336   2908   2527    260    409    590       C  
ATOM   1937  O   ILE A 225      -9.123  42.551  -1.422  1.00 21.62           O  
ANISOU 1937  O   ILE A 225      575   3969   3668    871    553   1458       O  
ATOM   1938  CB  ILE A 225      -6.963  40.855  -2.346  1.00 16.32           C  
ANISOU 1938  CB  ILE A 225      472   3025   2702    778     41    311       C  
ATOM   1939  CG1 ILE A 225      -5.667  40.077  -2.071  1.00 15.85           C  
ANISOU 1939  CG1 ILE A 225      403   2788   2830    299    566    202       C  
ATOM   1940  CG2 ILE A 225      -7.383  40.673  -3.806  1.00 19.21           C  
ANISOU 1940  CG2 ILE A 225     1259   3132   2908    128   -184    270       C  
ATOM   1941  CD1 ILE A 225      -5.870  38.561  -2.069  1.00 18.50           C  
ANISOU 1941  CD1 ILE A 225      574   3187   3269    906    485    438       C  
ATOM   1942  N   ASP A 226      -8.361  44.008  -2.915  1.00 13.77           N  
ANISOU 1942  N   ASP A 226      268   2665   2296    184    -12    334       N  
ATOM   1943  CA  ASP A 226      -9.708  44.511  -3.218  1.00 14.04           C  
ANISOU 1943  CA  ASP A 226      352   2685   2296    289   -317    360       C  
ATOM   1944  C   ASP A 226     -10.090  44.155  -4.655  1.00 17.03           C  
ANISOU 1944  C   ASP A 226      989   2906   2573    300   -187    193       C  
ATOM   1945  O   ASP A 226      -9.451  43.325  -5.287  1.00 17.03           O  
ANISOU 1945  O   ASP A 226      387   3225   2856    420   -337    -44       O  
ATOM   1946  CB  ASP A 226      -9.830  46.007  -2.897  1.00 14.23           C  
ANISOU 1946  CB  ASP A 226      292   2924   2189    318      2    409       C  
ATOM   1947  CG  ASP A 226      -9.016  46.900  -3.811  1.00 14.63           C  
ANISOU 1947  CG  ASP A 226      332   2892   2334    121   -390     16       C  
ATOM   1948  OD1 ASP A 226      -9.122  46.778  -5.044  1.00 16.68           O  
ANISOU 1948  OD1 ASP A 226      289   3514   2532    305   -119    139       O  
ATOM   1949  OD2 ASP A 226      -8.307  47.800  -3.274  1.00 19.49           O  
ANISOU 1949  OD2 ASP A 226     1272   3363   2771     60    514   -124       O  
ATOM   1950  N   GLY A 227     -11.226  44.658  -5.110  1.00 15.36           N  
ANISOU 1950  N   GLY A 227      302   3188   2347    378     46    215       N  
ATOM   1951  CA  GLY A 227     -11.738  44.308  -6.442  1.00 16.11           C  
ANISOU 1951  CA  GLY A 227      301   3185   2635    -71    335   -126       C  
ATOM   1952  C   GLY A 227     -10.788  44.718  -7.569  1.00 17.76           C  
ANISOU 1952  C   GLY A 227      511   3394   2841    291    360   -320       C  
ATOM   1953  O   GLY A 227     -10.832  44.152  -8.667  1.00 20.18           O  
ANISOU 1953  O   GLY A 227      265   4275   3126     69    171   -242       O  
ATOM   1954  N   ASN A 228     -10.025  45.778  -7.317  1.00 17.87           N  
ANISOU 1954  N   ASN A 228      861   3477   2451   -278    -35    129       N  
ATOM   1955  CA  ASN A 228      -9.232  46.432  -8.346  1.00 16.84           C  
ANISOU 1955  CA  ASN A 228      318   3384   2694     16    397    141       C  
ATOM   1956  C   ASN A 228      -7.728  46.134  -8.181  1.00 16.53           C  
ANISOU 1956  C   ASN A 228      407   3413   2460    -74    580    -51       C  
ATOM   1957  O   ASN A 228      -7.005  46.016  -9.174  1.00 18.44           O  
ANISOU 1957  O   ASN A 228      355   3904   2747    310    445    119       O  
ATOM   1958  CB  ASN A 228      -9.412  47.967  -8.276  1.00 17.70           C  
ANISOU 1958  CB  ASN A 228      410   3277   3038    146    657    322       C  
ATOM   1959  CG  ASN A 228     -10.814  48.433  -8.664  1.00 21.50           C  
ANISOU 1959  CG  ASN A 228     1411   3542   3213    730    498    169       C  
ATOM   1960  OD1 ASN A 228     -11.226  49.534  -8.308  1.00 25.96           O  
ANISOU 1960  OD1 ASN A 228     1914   4211   3738    337    628    911       O  
ATOM   1961  ND2 ASN A 228     -11.505  47.636  -9.414  1.00 21.82           N  
ANISOU 1961  ND2 ASN A 228     1785   3572   2931      9   -100    606       N  
ATOM   1962  N   LEU A 229      -7.255  46.061  -6.932  1.00 14.84           N  
ANISOU 1962  N   LEU A 229      319   3277   2043    -16    342     14       N  
ATOM   1963  CA  LEU A 229      -5.811  46.222  -6.643  1.00 13.30           C  
ANISOU 1963  CA  LEU A 229      328   2704   2021      0    361    204       C  
ATOM   1964  C   LEU A 229      -5.360  45.294  -5.562  1.00 13.69           C  
ANISOU 1964  C   LEU A 229      414   2585   2202   -108    547     94       C  
ATOM   1965  O   LEU A 229      -6.150  44.893  -4.698  1.00 15.07           O  
ANISOU 1965  O   LEU A 229      305   3084   2336     73    329    301       O  
ATOM   1966  CB  LEU A 229      -5.557  47.648  -6.199  1.00 14.51           C  
ANISOU 1966  CB  LEU A 229      277   2960   2275    226    117    150       C  
ATOM   1967  CG  LEU A 229      -5.738  48.722  -7.248  1.00 17.10           C  
ANISOU 1967  CG  LEU A 229      336   3058   3103    388    303     89       C  
ATOM   1968  CD1 LEU A 229      -5.428  50.083  -6.629  1.00 19.38           C  
ANISOU 1968  CD1 LEU A 229      729   2761   3870    674    371    -51       C  
ATOM   1969  CD2 LEU A 229      -4.873  48.452  -8.495  1.00 21.00           C  
ANISOU 1969  CD2 LEU A 229      755   3881   3341    299    393    589       C  
ATOM   1970  N   VAL A 230      -4.052  44.979  -5.577  1.00 12.34           N  
ANISOU 1970  N   VAL A 230      280   2432   1976     22    215    238       N  
ATOM   1971  CA  VAL A 230      -3.415  44.327  -4.460  1.00 13.91           C  
ANISOU 1971  CA  VAL A 230      490   2618   2176   -135    659     69       C  
ATOM   1972  C   VAL A 230      -2.504  45.347  -3.798  1.00 13.20           C  
ANISOU 1972  C   VAL A 230      473   2517   2023      0      7    181       C  
ATOM   1973  O   VAL A 230      -1.601  45.878  -4.449  1.00 15.86           O  
ANISOU 1973  O   VAL A 230      317   3110   2597   -269    297     47       O  
ATOM   1974  CB  VAL A 230      -2.567  43.140  -4.950  1.00 14.61           C  
ANISOU 1974  CB  VAL A 230      442   2763   2344    501    103    145       C  
ATOM   1975  CG1 VAL A 230      -1.766  42.532  -3.784  1.00 17.82           C  
ANISOU 1975  CG1 VAL A 230     1174   3211   2383    455    185    323       C  
ATOM   1976  CG2 VAL A 230      -3.450  42.087  -5.638  1.00 17.26           C  
ANISOU 1976  CG2 VAL A 230      911   2834   2810   -360    528   -143       C  
ATOM   1977  N   LYS A 231      -2.737  45.636  -2.520  1.00 13.52           N  
ANISOU 1977  N   LYS A 231      276   2494   2365   -192    109    154       N  
ATOM   1978  CA  LYS A 231      -1.981  46.682  -1.803  1.00 15.48           C  
ANISOU 1978  CA  LYS A 231     1186   2489   2204   -302    -15    164       C  
ATOM   1979  C   LYS A 231      -1.340  46.157  -0.527  1.00 15.08           C  
ANISOU 1979  C   LYS A 231      830   2538   2361   -241    167     52       C  
ATOM   1980  O   LYS A 231      -1.903  45.318   0.149  1.00 16.35           O  
ANISOU 1980  O   LYS A 231      844   2742   2626    -70    -78    277       O  
ATOM   1981  CB  LYS A 231      -2.904  47.845  -1.454  1.00 17.50           C  
ANISOU 1981  CB  LYS A 231     1558   2304   2786   -281   -107   -128       C  
ATOM   1982  CG  LYS A 231      -3.480  48.558  -2.673  1.00 21.24           C  
ANISOU 1982  CG  LYS A 231     1325   3265   3481     28   -464   -138       C  
ATOM   1983  CD  LYS A 231      -4.549  49.562  -2.280  1.00 27.43           C  
ANISOU 1983  CD  LYS A 231     2276   3733   4411    132   -533   -151       C  
ATOM   1984  CE  LYS A 231      -3.950  50.744  -1.540  1.00 32.16           C  
ANISOU 1984  CE  LYS A 231     3273   4176   4769    325   -547   -199       C  
ATOM   1985  NZ  LYS A 231      -4.971  51.779  -1.233  1.00 35.48           N  
ANISOU 1985  NZ  LYS A 231     3460   4700   5320   1462    148    259       N  
ATOM   1986  N   LEU A 232      -0.129  46.639  -0.221  1.00 13.61           N  
ANISOU 1986  N   LEU A 232      345   2488   2336      7    250    175       N  
ATOM   1987  CA  LEU A 232       0.507  46.330   1.032  1.00 13.11           C  
ANISOU 1987  CA  LEU A 232      384   2358   2237   -113    415     12       C  
ATOM   1988  C   LEU A 232      -0.227  46.934   2.212  1.00 14.07           C  
ANISOU 1988  C   LEU A 232      343   2480   2523     58    128     36       C  
ATOM   1989  O   LEU A 232      -0.750  48.029   2.128  1.00 15.97           O  
ANISOU 1989  O   LEU A 232      459   2583   3025   -105    720    -85       O  
ATOM   1990  CB  LEU A 232       1.972  46.815   1.037  1.00 12.49           C  
ANISOU 1990  CB  LEU A 232      286   2273   2183    -51    234     32       C  
ATOM   1991  CG  LEU A 232       2.901  46.100   0.055  1.00 13.09           C  
ANISOU 1991  CG  LEU A 232      276   2555   2142    -33    210   -144       C  
ATOM   1992  CD1 LEU A 232       4.202  46.908  -0.170  1.00 16.66           C  
ANISOU 1992  CD1 LEU A 232      523   3097   2708   -718    525   -236       C  
ATOM   1993  CD2 LEU A 232       3.268  44.683   0.524  1.00 13.55           C  
ANISOU 1993  CD2 LEU A 232      309   2382   2457   -169    172    143       C  
ATOM   1994  N   ASN A 233      -0.193  46.220   3.321  1.00 13.66           N  
ANISOU 1994  N   ASN A 233      720   2440   2028     -3    358     -8       N  
ATOM   1995  CA  ASN A 233      -0.649  46.731   4.601  1.00 15.01           C  
ANISOU 1995  CA  ASN A 233      974   2571   2156   -143    153   -154       C  
ATOM   1996  C   ASN A 233       0.521  47.260   5.442  1.00 13.69           C  
ANISOU 1996  C   ASN A 233      917   2512   1771    -60    431    -88       C  
ATOM   1997  O   ASN A 233       1.198  46.498   6.146  1.00 14.83           O  
ANISOU 1997  O   ASN A 233      947   2481   2207   -220    342   -189       O  
ATOM   1998  CB  ASN A 233      -1.366  45.631   5.370  1.00 14.94           C  
ANISOU 1998  CB  ASN A 233      819   2815   2040    -70    528   -196       C  
ATOM   1999  CG  ASN A 233      -1.755  46.064   6.755  1.00 17.26           C  
ANISOU 1999  CG  ASN A 233     1272   2753   2532   -187    483   -192       C  
ATOM   2000  OD1 ASN A 233      -1.861  47.263   7.034  1.00 19.17           O  
ANISOU 2000  OD1 ASN A 233     1508   2940   2836   -221    889   -543       O  
ATOM   2001  ND2 ASN A 233      -1.903  45.111   7.648  1.00 17.87           N  
ANISOU 2001  ND2 ASN A 233     1496   2844   2448   -339    712    -59       N  
ATOM   2002  N   TYR A 234       0.767  48.558   5.372  1.00 16.23           N  
ANISOU 2002  N   TYR A 234     1313   2446   2406   -230    319   -127       N  
ATOM   2003  CA  TYR A 234       1.985  49.112   5.977  1.00 17.18           C  
ANISOU 2003  CA  TYR A 234     1642   2472   2411   -481    439   -287       C  
ATOM   2004  C   TYR A 234       1.933  49.136   7.516  1.00 16.27           C  
ANISOU 2004  C   TYR A 234     1001   2750   2429   -281    991   -289       C  
ATOM   2005  O   TYR A 234       2.928  49.418   8.158  1.00 19.42           O  
ANISOU 2005  O   TYR A 234     1736   2896   2746   -481    325   -690       O  
ATOM   2006  CB  TYR A 234       2.291  50.503   5.410  1.00 17.78           C  
ANISOU 2006  CB  TYR A 234     1420   2709   2625   -487    659   -225       C  
ATOM   2007  CG  TYR A 234       2.934  50.453   4.031  1.00 15.29           C  
ANISOU 2007  CG  TYR A 234      664   2474   2669   -398    506   -110       C  
ATOM   2008  CD1 TYR A 234       4.287  50.222   3.896  1.00 16.65           C  
ANISOU 2008  CD1 TYR A 234      991   2516   2818   -282    419   -335       C  
ATOM   2009  CD2 TYR A 234       2.171  50.588   2.872  1.00 19.82           C  
ANISOU 2009  CD2 TYR A 234     1973   2717   2840    -38    588     18       C  
ATOM   2010  CE1 TYR A 234       4.887  50.161   2.656  1.00 16.51           C  
ANISOU 2010  CE1 TYR A 234     1294   2399   2579   -180    427   -132       C  
ATOM   2011  CE2 TYR A 234       2.754  50.513   1.619  1.00 18.01           C  
ANISOU 2011  CE2 TYR A 234     1421   2391   3031   -584    532    -47       C  
ATOM   2012  CZ  TYR A 234       4.137  50.323   1.525  1.00 17.04           C  
ANISOU 2012  CZ  TYR A 234     1364   2462   2648   -600    358     -5       C  
ATOM   2013  OH  TYR A 234       4.775  50.252   0.297  1.00 16.83           O  
ANISOU 2013  OH  TYR A 234     1088   2597   2707   -300    561    -74       O  
ATOM   2014  N   ARG A 235       0.782  48.823   8.098  1.00 17.73           N  
ANISOU 2014  N   ARG A 235     1228   2696   2812    -81    620   -319       N  
ATOM   2015  CA  ARG A 235       0.736  48.548   9.518  1.00 18.04           C  
ANISOU 2015  CA  ARG A 235     1656   2769   2429   -412    504   -294       C  
ATOM   2016  C   ARG A 235       1.662  47.375   9.870  1.00 17.15           C  
ANISOU 2016  C   ARG A 235     1258   3062   2196   -684    503   -187       C  
ATOM   2017  O   ARG A 235       2.120  47.259  10.998  1.00 20.37           O  
ANISOU 2017  O   ARG A 235     2130   3593   2015   -718    576   -555       O  
ATOM   2018  CB  ARG A 235      -0.703  48.252   9.963  1.00 19.90           C  
ANISOU 2018  CB  ARG A 235     1837   3157   2566     88    564   -264       C  
ATOM   2019  CG  ARG A 235      -1.634  49.429   9.796  1.00 24.28           C  
ANISOU 2019  CG  ARG A 235     1738   3978   3508   -132    734     -2       C  
ATOM   2020  N   GLU A 236       1.943  46.523   8.878  1.00 14.98           N  
ANISOU 2020  N   GLU A 236     1003   2630   2058   -539    219   -455       N  
ATOM   2021  CA  GLU A 236       2.827  45.368   9.047  1.00 14.67           C  
ANISOU 2021  CA  GLU A 236     1170   2396   2008   -488    370   -223       C  
ATOM   2022  C   GLU A 236       4.146  45.594   8.292  1.00 14.46           C  
ANISOU 2022  C   GLU A 236      970   2486   2036   -584    277   -224       C  
ATOM   2023  O   GLU A 236       4.784  44.640   7.823  1.00 15.63           O  
ANISOU 2023  O   GLU A 236     1433   2455   2047   -538    252   -256       O  
ATOM   2024  CB  GLU A 236       2.156  44.101   8.536  1.00 16.83           C  
ANISOU 2024  CB  GLU A 236     1225   2609   2559   -191    427   -424       C  
ATOM   2025  CG  GLU A 236       1.004  43.626   9.409  1.00 18.45           C  
ANISOU 2025  CG  GLU A 236     1040   3252   2716   -709    233   -254       C  
ATOM   2026  CD  GLU A 236       1.461  42.787  10.586  1.00 29.80           C  
ANISOU 2026  CD  GLU A 236     3229   4462   3632   -152    790    116       C  
ATOM   2027  OE1 GLU A 236       2.672  42.478  10.679  1.00 28.62           O  
ANISOU 2027  OE1 GLU A 236     2817   3968   4087   -784    787    756       O  
ATOM   2028  OE2 GLU A 236       0.594  42.429  11.424  1.00 34.45           O  
ANISOU 2028  OE2 GLU A 236     3043   5829   4216  -1244   1114    734       O  
ATOM   2029  N   ALA A 237       4.558  46.858   8.200  1.00 15.25           N  
ANISOU 2029  N   ALA A 237     1264   2424   2106   -492    315   -306       N  
ATOM   2030  CA  ALA A 237       5.794  47.216   7.506  1.00 16.21           C  
ANISOU 2030  CA  ALA A 237     1154   2886   2119   -746    274    -55       C  
ATOM   2031  C   ALA A 237       6.989  46.400   7.982  1.00 15.79           C  
ANISOU 2031  C   ALA A 237     1556   2675   1767   -592     -1   -101       C  
ATOM   2032  O   ALA A 237       7.832  46.029   7.182  1.00 16.23           O  
ANISOU 2032  O   ALA A 237     1038   3172   1957   -810    123   -299       O  
ATOM   2033  CB  ALA A 237       6.079  48.708   7.661  1.00 19.37           C  
ANISOU 2033  CB  ALA A 237     1881   2520   2956   -823    406     43       C  
ATOM   2034  N   GLU A 238       7.070  46.118   9.275  1.00 16.36           N  
ANISOU 2034  N   GLU A 238     1327   2808   2080   -574    -17   -221       N  
ATOM   2035  CA  GLU A 238       8.247  45.401   9.795  1.00 14.89           C  
ANISOU 2035  CA  GLU A 238      786   2885   1986   -762    108    -25       C  
ATOM   2036  C   GLU A 238       8.333  43.992   9.204  1.00 15.66           C  
ANISOU 2036  C   GLU A 238      793   3221   1934   -468    120     39       C  
ATOM   2037  O   GLU A 238       9.377  43.581   8.702  1.00 17.69           O  
ANISOU 2037  O   GLU A 238     1093   3443   2185   -731    -18   -106       O  
ATOM   2038  CB  GLU A 238       8.227  45.338  11.309  1.00 19.78           C  
ANISOU 2038  CB  GLU A 238     1681   3310   2523   -715    -44   -193       C  
ATOM   2039  CG  GLU A 238       8.482  46.661  11.972  1.00 23.09           C  
ANISOU 2039  CG  GLU A 238     2383   3449   2941   -572    148   -202       C  
ATOM   2040  CD  GLU A 238       8.893  46.511  13.421  1.00 32.87           C  
ANISOU 2040  CD  GLU A 238     3869   4857   3762   -633    114   -244       C  
ATOM   2041  OE1 GLU A 238       8.049  46.094  14.227  1.00 30.29           O  
ANISOU 2041  OE1 GLU A 238     2138   5954   3415   -594    524   -527       O  
ATOM   2042  OE2 GLU A 238      10.065  46.816  13.751  1.00 33.53           O  
ANISOU 2042  OE2 GLU A 238     3116   5511   4113   -678   -211   -113       O  
ATOM   2043  N   ASN A 239       7.211  43.288   9.203  1.00 15.39           N  
ANISOU 2043  N   ASN A 239      598   3183   2065   -514    114   -193       N  
ATOM   2044  CA  ASN A 239       7.163  41.951   8.620  1.00 13.94           C  
ANISOU 2044  CA  ASN A 239      344   2967   1986   -435   -118   -137       C  
ATOM   2045  C   ASN A 239       7.302  41.972   7.104  1.00 15.47           C  
ANISOU 2045  C   ASN A 239     1070   2887   1919    -31   -100   -225       C  
ATOM   2046  O   ASN A 239       7.953  41.119   6.533  1.00 16.34           O  
ANISOU 2046  O   ASN A 239      474   3449   2282   -159    -74   -216       O  
ATOM   2047  CB  ASN A 239       5.883  41.244   9.017  1.00 14.83           C  
ANISOU 2047  CB  ASN A 239      682   2870   2083   -558    146   -250       C  
ATOM   2048  CG  ASN A 239       5.962  40.650  10.404  1.00 20.56           C  
ANISOU 2048  CG  ASN A 239     1895   3135   2780   -125    250   -157       C  
ATOM   2049  OD1 ASN A 239       6.954  40.027  10.765  1.00 27.21           O  
ANISOU 2049  OD1 ASN A 239     2925   4511   2900   -772   -283    861       O  
ATOM   2050  ND2 ASN A 239       4.905  40.821  11.179  1.00 25.97           N  
ANISOU 2050  ND2 ASN A 239     1930   5386   2551   -291    633   -311       N  
ATOM   2051  N   ILE A 240       6.648  42.922   6.452  1.00 13.45           N  
ANISOU 2051  N   ILE A 240      446   2733   1932   -196     20    -68       N  
ATOM   2052  CA  ILE A 240       6.780  43.062   5.001  1.00 14.15           C  
ANISOU 2052  CA  ILE A 240      815   2816   1746   -320    -56   -234       C  
ATOM   2053  C   ILE A 240       8.250  43.191   4.609  1.00 15.42           C  
ANISOU 2053  C   ILE A 240     1026   3133   1701    141   -213   -256       C  
ATOM   2054  O   ILE A 240       8.736  42.498   3.708  1.00 15.76           O  
ANISOU 2054  O   ILE A 240      727   3325   1934    -43   -132   -183       O  
ATOM   2055  CB  ILE A 240       6.014  44.284   4.478  1.00 12.57           C  
ANISOU 2055  CB  ILE A 240      620   2467   1688   -173     27   -323       C  
ATOM   2056  CG1 ILE A 240       4.494  44.041   4.579  1.00 14.04           C  
ANISOU 2056  CG1 ILE A 240      472   2708   2153   -388     64   -372       C  
ATOM   2057  CG2 ILE A 240       6.413  44.589   3.045  1.00 14.75           C  
ANISOU 2057  CG2 ILE A 240      618   2883   2100   -203      9   -148       C  
ATOM   2058  CD1 ILE A 240       3.675  45.314   4.419  1.00 13.97           C  
ANISOU 2058  CD1 ILE A 240      308   2778   2219   -358    126   -227       C  
ATOM   2059  N   ASN A 241       8.968  44.051   5.294  1.00 15.31           N  
ANISOU 2059  N   ASN A 241      535   3710   1570   -542    255   -129       N  
ATOM   2060  CA  ASN A 241      10.354  44.282   4.919  1.00 15.52           C  
ANISOU 2060  CA  ASN A 241      603   3351   1939   -364     85    -76       C  
ATOM   2061  C   ASN A 241      11.258  43.063   5.200  1.00 17.46           C  
ANISOU 2061  C   ASN A 241      824   3841   1969   -244    116    188       C  
ATOM   2062  O   ASN A 241      12.134  42.722   4.381  1.00 17.50           O  
ANISOU 2062  O   ASN A 241      696   3839   2114   -157    451    139       O  
ATOM   2063  CB  ASN A 241      10.888  45.542   5.585  1.00 19.22           C  
ANISOU 2063  CB  ASN A 241     1152   3976   2174   -735    390   -256       C  
ATOM   2064  CG  ASN A 241      10.595  46.799   4.771  1.00 19.17           C  
ANISOU 2064  CG  ASN A 241      842   3228   3214   -118    446   -312       C  
ATOM   2065  OD1 ASN A 241      11.017  46.921   3.625  1.00 24.30           O  
ANISOU 2065  OD1 ASN A 241     2365   3599   3265   -882    699     70       O  
ATOM   2066  ND2 ASN A 241       9.857  47.724   5.356  1.00 32.11           N  
ANISOU 2066  ND2 ASN A 241     2641   5214   4344    223    848   -522       N  
ATOM   2067  N   TYR A 242      11.060  42.414   6.324  1.00 16.77           N  
ANISOU 2067  N   TYR A 242     1028   3272   2071   -491    110    115       N  
ATOM   2068  CA  TYR A 242      11.837  41.250   6.645  1.00 17.43           C  
ANISOU 2068  CA  TYR A 242     1004   3459   2158   -445    283    165       C  
ATOM   2069  C   TYR A 242      11.689  40.174   5.561  1.00 15.04           C  
ANISOU 2069  C   TYR A 242      312   3748   1652   -452      3    111       C  
ATOM   2070  O   TYR A 242      12.693  39.669   5.038  1.00 18.69           O  
ANISOU 2070  O   TYR A 242      819   4231   2048   -133    180    -42       O  
ATOM   2071  CB  TYR A 242      11.449  40.696   8.015  1.00 18.02           C  
ANISOU 2071  CB  TYR A 242      911   3579   2354   -246    303    298       C  
ATOM   2072  CG  TYR A 242      12.126  39.390   8.341  1.00 15.92           C  
ANISOU 2072  CG  TYR A 242      522   3740   1786   -397     16    -18       C  
ATOM   2073  CD1 TYR A 242      13.497  39.342   8.683  1.00 19.91           C  
ANISOU 2073  CD1 TYR A 242     1153   4030   2380   -209     51    167       C  
ATOM   2074  CD2 TYR A 242      11.428  38.191   8.236  1.00 20.91           C  
ANISOU 2074  CD2 TYR A 242     1355   3808   2780   -220    147    -54       C  
ATOM   2075  CE1 TYR A 242      14.105  38.138   8.989  1.00 16.35           C  
ANISOU 2075  CE1 TYR A 242      267   3697   2247   -189    -78    -44       C  
ATOM   2076  CE2 TYR A 242      12.022  36.983   8.546  1.00 18.34           C  
ANISOU 2076  CE2 TYR A 242      360   3985   2622   -279    451     -1       C  
ATOM   2077  CZ  TYR A 242      13.373  36.953   8.885  1.00 19.66           C  
ANISOU 2077  CZ  TYR A 242     1321   2973   3174   -195    305    218       C  
ATOM   2078  OH  TYR A 242      13.969  35.755   9.170  1.00 20.81           O  
ANISOU 2078  OH  TYR A 242     1485   3940   2479   -303    415    136       O  
ATOM   2079  N   ILE A 243      10.450  39.862   5.188  1.00 14.51           N  
ANISOU 2079  N   ILE A 243      266   3271   1974   -167    -78     16       N  
ATOM   2080  CA  ILE A 243      10.231  38.816   4.259  1.00 13.15           C  
ANISOU 2080  CA  ILE A 243      255   2829   1910     33    -58    176       C  
ATOM   2081  C   ILE A 243      10.653  39.233   2.853  1.00 12.49           C  
ANISOU 2081  C   ILE A 243      527   2539   1678   -294   -584     40       C  
ATOM   2082  O   ILE A 243      11.226  38.436   2.115  1.00 12.84           O  
ANISOU 2082  O   ILE A 243      277   2843   1756    -35   -188     39       O  
ATOM   2083  CB  ILE A 243       8.738  38.355   4.287  1.00 13.30           C  
ANISOU 2083  CB  ILE A 243      471   2595   1987     17      1    558       C  
ATOM   2084  CG1 ILE A 243       8.392  37.825   5.683  1.00 16.99           C  
ANISOU 2084  CG1 ILE A 243     1072   3047   2337    127     -4    110       C  
ATOM   2085  CG2 ILE A 243       8.476  37.299   3.236  1.00 14.96           C  
ANISOU 2085  CG2 ILE A 243      514   2740   2429   -284    352     67       C  
ATOM   2086  CD1 ILE A 243       6.901  37.535   5.891  1.00 18.82           C  
ANISOU 2086  CD1 ILE A 243      694   3543   2910   -534    277    351       C  
ATOM   2087  N   ALA A 244      10.340  40.472   2.471  1.00 12.96           N  
ANISOU 2087  N   ALA A 244      257   2650   2015    -40    -82     23       N  
ATOM   2088  CA  ALA A 244      10.678  40.962   1.121  1.00 11.97           C  
ANISOU 2088  CA  ALA A 244      277   2555   1714   -130    153     19       C  
ATOM   2089  C   ALA A 244      12.172  40.851   0.837  1.00 11.88           C  
ANISOU 2089  C   ALA A 244      271   2700   1540     11   -154     27       C  
ATOM   2090  O   ALA A 244      12.565  40.643  -0.287  1.00 12.30           O  
ANISOU 2090  O   ALA A 244      260   2669   1745   -112    -49     17       O  
ATOM   2091  CB  ALA A 244      10.247  42.386   0.951  1.00 12.10           C  
ANISOU 2091  CB  ALA A 244      260   2699   1636    -57    -85    -64       C  
ATOM   2092  N  AGLN A 245      12.983  40.983   1.883  0.50 12.68           N  
ANISOU 2092  N  AGLN A 245      266   2764   1785    -17    138    102       N  
ATOM   2093  N  BGLN A 245      12.988  40.996   1.879  0.50 12.70           N  
ANISOU 2093  N  BGLN A 245      265   2764   1792    -16    137     94       N  
ATOM   2094  CA AGLN A 245      14.449  41.026   1.720  0.50 12.18           C  
ANISOU 2094  CA AGLN A 245      268   2457   1902   -110   -125    -39       C  
ATOM   2095  CA BGLN A 245      14.456  41.036   1.702  0.50 12.24           C  
ANISOU 2095  CA BGLN A 245      266   2479   1904   -115   -107    -46       C  
ATOM   2096  C  AGLN A 245      15.035  39.700   1.253  0.50 13.73           C  
ANISOU 2096  C  AGLN A 245      824   2521   1871   -308     59     33       C  
ATOM   2097  C  BGLN A 245      15.039  39.699   1.253  0.50 13.82           C  
ANISOU 2097  C  BGLN A 245      845   2530   1875   -310     57     28       C  
ATOM   2098  O  AGLN A 245      16.173  39.652   0.824  0.50 14.18           O  
ANISOU 2098  O  AGLN A 245      264   2888   2235   -119    109   -106       O  
ATOM   2099  O  BGLN A 245      16.181  39.641   0.840  0.50 14.31           O  
ANISOU 2099  O  BGLN A 245      267   2906   2264   -137    123   -124       O  
ATOM   2100  CB AGLN A 245      15.120  41.487   3.022  0.50 14.26           C  
ANISOU 2100  CB AGLN A 245      262   2815   2341   -149    -15   -183       C  
ATOM   2101  CB BGLN A 245      15.146  41.522   2.987  0.50 14.27           C  
ANISOU 2101  CB BGLN A 245      265   2841   2314   -158    -58   -199       C  
ATOM   2102  CG AGLN A 245      15.133  43.000   3.161  0.50 15.43           C  
ANISOU 2102  CG AGLN A 245      529   2828   2503    -22      7    -36       C  
ATOM   2103  CG BGLN A 245      15.021  43.030   3.195  0.50 15.88           C  
ANISOU 2103  CG BGLN A 245      512   3005   2515    -37    191   -157       C  
ATOM   2104  CD AGLN A 245      15.339  43.474   4.582  0.50 16.24           C  
ANISOU 2104  CD AGLN A 245      883   2622   2663    118      4   -179       C  
ATOM   2105  CD BGLN A 245      15.733  43.527   4.441  0.50 16.35           C  
ANISOU 2105  CD BGLN A 245      450   3196   2566   -630    427   -233       C  
ATOM   2106  OE1AGLN A 245      15.578  42.678   5.492  0.50 18.27           O  
ANISOU 2106  OE1AGLN A 245     1415   2821   2706    283   -849   -121       O  
ATOM   2107  OE1BGLN A 245      16.976  43.622   4.479  0.50 21.84           O  
ANISOU 2107  OE1BGLN A 245      384   4282   3630   -475    541   -350       O  
ATOM   2108  NE2AGLN A 245      15.236  44.782   4.784  0.50 16.89           N  
ANISOU 2108  NE2AGLN A 245      698   2256   3463     99   -239    -15       N  
ATOM   2109  NE2BGLN A 245      14.954  43.890   5.457  0.50 21.47           N  
ANISOU 2109  NE2BGLN A 245     2343   2871   2941   -236    381   -487       N  
ATOM   2110  N   PHE A 246      14.242  38.638   1.289  1.00 12.28           N  
ANISOU 2110  N   PHE A 246      268   2476   1919   -176    -48    -11       N  
ATOM   2111  CA  PHE A 246      14.660  37.346   0.764  1.00 11.73           C  
ANISOU 2111  CA  PHE A 246      328   2336   1790   -296   -238    107       C  
ATOM   2112  C   PHE A 246      14.345  37.153  -0.728  1.00 11.87           C  
ANISOU 2112  C   PHE A 246      347   2139   2022   -399    116     63       C  
ATOM   2113  O   PHE A 246      14.552  36.069  -1.265  1.00 12.67           O  
ANISOU 2113  O   PHE A 246      278   2545   1991   -143   -174    115       O  
ATOM   2114  CB  PHE A 246      14.033  36.205   1.580  1.00 11.88           C  
ANISOU 2114  CB  PHE A 246      272   2554   1685   -189    -72     38       C  
ATOM   2115  CG  PHE A 246      14.485  36.163   2.996  1.00 12.29           C  
ANISOU 2115  CG  PHE A 246      272   2384   2012   -139    126     56       C  
ATOM   2116  CD1 PHE A 246      13.904  36.978   3.949  1.00 13.08           C  
ANISOU 2116  CD1 PHE A 246      335   2893   1742   -318   -261     43       C  
ATOM   2117  CD2 PHE A 246      15.540  35.334   3.377  1.00 13.89           C  
ANISOU 2117  CD2 PHE A 246      703   2426   2145   -379    262     13       C  
ATOM   2118  CE1 PHE A 246      14.315  36.944   5.254  1.00 14.75           C  
ANISOU 2118  CE1 PHE A 246      391   3264   1946   -453   -376    219       C  
ATOM   2119  CE2 PHE A 246      15.978  35.304   4.681  1.00 14.87           C  
ANISOU 2119  CE2 PHE A 246      477   3042   2129   -616   -456    236       C  
ATOM   2120  CZ  PHE A 246      15.395  36.131   5.622  1.00 15.37           C  
ANISOU 2120  CZ  PHE A 246      514   3562   1761   -415   -577    136       C  
ATOM   2121  N   TRP A 247      13.866  38.200  -1.398  1.00 11.79           N  
ANISOU 2121  N   TRP A 247      290   2340   1848   -244    120    -46       N  
ATOM   2122  CA  TRP A 247      13.411  38.053  -2.775  1.00 11.64           C  
ANISOU 2122  CA  TRP A 247      273   2376   1773   -165    114   -108       C  
ATOM   2123  C   TRP A 247      14.454  37.515  -3.724  1.00 13.06           C  
ANISOU 2123  C   TRP A 247      591   2410   1958   -477     85     73       C  
ATOM   2124  O   TRP A 247      14.120  36.825  -4.703  1.00 13.25           O  
ANISOU 2124  O   TRP A 247      253   2741   2039    -35      4    -27       O  
ATOM   2125  CB  TRP A 247      12.864  39.370  -3.319  1.00 12.40           C  
ANISOU 2125  CB  TRP A 247      306   2407   1998   -293    142     56       C  
ATOM   2126  CG  TRP A 247      13.911  40.454  -3.566  1.00 12.54           C  
ANISOU 2126  CG  TRP A 247      283   2755   1726     23    208     11       C  
ATOM   2127  CD1 TRP A 247      14.229  41.491  -2.732  1.00 14.18           C  
ANISOU 2127  CD1 TRP A 247      436   2760   2189    -79    589     51       C  
ATOM   2128  CD2 TRP A 247      14.726  40.642  -4.753  1.00 12.44           C  
ANISOU 2128  CD2 TRP A 247      382   2464   1877    -80    -67     44       C  
ATOM   2129  NE1 TRP A 247      15.194  42.280  -3.305  1.00 15.59           N  
ANISOU 2129  NE1 TRP A 247      499   2797   2624    -50    284    -19       N  
ATOM   2130  CE2 TRP A 247      15.492  41.790  -4.549  1.00 13.92           C  
ANISOU 2130  CE2 TRP A 247      426   2588   2272    263    259    108       C  
ATOM   2131  CE3 TRP A 247      14.871  39.947  -5.946  1.00 13.38           C  
ANISOU 2131  CE3 TRP A 247      272   2857   1953     15    182     84       C  
ATOM   2132  CZ2 TRP A 247      16.407  42.245  -5.487  1.00 15.75           C  
ANISOU 2132  CZ2 TRP A 247      295   3300   2389   -186    257    -15       C  
ATOM   2133  CZ3 TRP A 247      15.804  40.387  -6.862  1.00 14.38           C  
ANISOU 2133  CZ3 TRP A 247      392   3014   2057     92    350    -79       C  
ATOM   2134  CH2 TRP A 247      16.534  41.534  -6.637  1.00 17.60           C  
ANISOU 2134  CH2 TRP A 247     1260   3056   2370   -145    404    122       C  
ATOM   2135  N   GLY A 248      15.719  37.860  -3.473  1.00 12.85           N  
ANISOU 2135  N   GLY A 248      264   2583   2033   -159      0    -24       N  
ATOM   2136  CA  GLY A 248      16.815  37.470  -4.370  1.00 14.25           C  
ANISOU 2136  CA  GLY A 248      359   2664   2388    284    400     53       C  
ATOM   2137  C   GLY A 248      17.518  36.185  -3.994  1.00 15.12           C  
ANISOU 2137  C   GLY A 248      715   2860   2170     10    -56     -9       C  
ATOM   2138  O   GLY A 248      18.463  35.778  -4.673  1.00 17.15           O  
ANISOU 2138  O   GLY A 248      550   3155   2811    201    369   -242       O  
ATOM   2139  N   ASN A 249      17.044  35.524  -2.942  1.00 13.50           N  
ANISOU 2139  N   ASN A 249      255   2663   2212     35     60    173       N  
ATOM   2140  CA  ASN A 249      17.654  34.289  -2.466  1.00 13.89           C  
ANISOU 2140  CA  ASN A 249      275   2621   2378    -14   -219    201       C  
ATOM   2141  C   ASN A 249      17.216  33.080  -3.276  1.00 13.93           C  
ANISOU 2141  C   ASN A 249      296   2706   2287   -307    -74   -189       C  
ATOM   2142  O   ASN A 249      16.032  32.926  -3.587  1.00 14.57           O  
ANISOU 2142  O   ASN A 249      281   2774   2480   -207   -140   -152       O  
ATOM   2143  CB  ASN A 249      17.303  34.048  -1.005  1.00 14.82           C  
ANISOU 2143  CB  ASN A 249      408   2808   2412    132   -407   -110       C  
ATOM   2144  CG  ASN A 249      18.086  34.934  -0.053  1.00 16.23           C  
ANISOU 2144  CG  ASN A 249      697   3022   2447    -24   -400    446       C  
ATOM   2145  OD1 ASN A 249      18.269  36.125  -0.306  1.00 22.10           O  
ANISOU 2145  OD1 ASN A 249     2232   3116   3050   -424  -1129    303       O  
ATOM   2146  ND2 ASN A 249      18.515  34.359   1.088  1.00 18.62           N  
ANISOU 2146  ND2 ASN A 249      279   3606   3191    126   -223    595       N  
ATOM   2147  N   LYS A 250      18.122  32.160  -3.514  1.00 15.35           N  
ANISOU 2147  N   LYS A 250      589   2538   2704    295    305     80       N  
ATOM   2148  CA  LYS A 250      17.750  30.851  -3.968  1.00 15.17           C  
ANISOU 2148  CA  LYS A 250      373   2832   2559    280    446    -67       C  
ATOM   2149  C   LYS A 250      16.810  30.243  -2.934  1.00 15.09           C  
ANISOU 2149  C   LYS A 250      445   2878   2407    337    546   -144       C  
ATOM   2150  O   LYS A 250      16.917  30.547  -1.755  1.00 15.33           O  
ANISOU 2150  O   LYS A 250      328   3125   2371    -24    399     10       O  
ATOM   2151  CB  LYS A 250      19.012  29.982  -4.141  1.00 18.62           C  
ANISOU 2151  CB  LYS A 250      645   3050   3378    138   1095    -42       C  
ATOM   2152  CG  LYS A 250      19.695  30.135  -5.469  1.00 26.32           C  
ANISOU 2152  CG  LYS A 250     1827   3958   4214    617    675     19       C  
ATOM   2153  CD  LYS A 250      20.706  29.009  -5.707  1.00 29.56           C  
ANISOU 2153  CD  LYS A 250     2349   4004   4877    956    456    -94       C  
ATOM   2154  CE  LYS A 250      20.787  28.637  -7.181  1.00 33.40           C  
ANISOU 2154  CE  LYS A 250     2821   4982   4887    785     56    113       C  
ATOM   2155  NZ  LYS A 250      21.832  29.426  -7.899  1.00 46.07           N  
ANISOU 2155  NZ  LYS A 250     5065   6198   6239   -588    202    267       N  
ATOM   2156  N   PRO A 251      15.930  29.339  -3.380  1.00 15.02           N  
ANISOU 2156  N   PRO A 251      792   2696   2219    108     45    -35       N  
ATOM   2157  CA  PRO A 251      15.150  28.552  -2.444  1.00 14.42           C  
ANISOU 2157  CA  PRO A 251      331   2802   2346    398    198    110       C  
ATOM   2158  C   PRO A 251      16.013  27.908  -1.362  1.00 14.32           C  
ANISOU 2158  C   PRO A 251      580   2674   2184     35    -76    242       C  
ATOM   2159  O   PRO A 251      17.103  27.398  -1.646  1.00 16.77           O  
ANISOU 2159  O   PRO A 251      313   3169   2888    265    190     72       O  
ATOM   2160  CB  PRO A 251      14.530  27.489  -3.326  1.00 16.28           C  
ANISOU 2160  CB  PRO A 251     1139   2694   2350      3     41     69       C  
ATOM   2161  CG  PRO A 251      14.368  28.151  -4.644  1.00 17.59           C  
ANISOU 2161  CG  PRO A 251     1788   2597   2299    237     62    -18       C  
ATOM   2162  CD  PRO A 251      15.585  29.029  -4.780  1.00 16.95           C  
ANISOU 2162  CD  PRO A 251     1355   2408   2676    180    161   -155       C  
ATOM   2163  N   GLU A 252      15.542  27.953  -0.131  1.00 13.80           N  
ANISOU 2163  N   GLU A 252      273   2590   2381    170   -114    142       N  
ATOM   2164  CA  GLU A 252      16.243  27.341   0.984  1.00 16.04           C  
ANISOU 2164  CA  GLU A 252      714   2882   2496   -182    -96    338       C  
ATOM   2165  C   GLU A 252      16.356  25.823   0.806  1.00 17.31           C  
ANISOU 2165  C   GLU A 252     1223   2806   2546   -180   -196    377       C  
ATOM   2166  O   GLU A 252      17.346  25.217   1.169  1.00 18.74           O  
ANISOU 2166  O   GLU A 252      819   2961   3340    416   -787    574       O  
ATOM   2167  CB  GLU A 252      15.506  27.664   2.273  1.00 16.54           C  
ANISOU 2167  CB  GLU A 252      420   3203   2660   -127     77    481       C  
ATOM   2168  CG  GLU A 252      16.221  27.261   3.529  1.00 17.65           C  
ANISOU 2168  CG  GLU A 252      394   3641   2670     49   -333     22       C  
ATOM   2169  CD  GLU A 252      17.570  27.937   3.665  1.00 28.71           C  
ANISOU 2169  CD  GLU A 252     2547   4198   4162   -206   -377    193       C  
ATOM   2170  OE1 GLU A 252      17.670  29.149   3.365  1.00 29.25           O  
ANISOU 2170  OE1 GLU A 252     2435   4803   3875   -260   -799   -187       O  
ATOM   2171  OE2 GLU A 252      18.526  27.258   4.055  1.00 39.18           O  
ANISOU 2171  OE2 GLU A 252     3125   6176   5582    -62   -794    195       O  
ATOM   2172  N   PHE A 253      15.305  25.217   0.296  1.00 14.55           N  
ANISOU 2172  N   PHE A 253      285   2593   2650    183   -192    170       N  
ATOM   2173  CA  PHE A 253      15.280  23.787   0.022  1.00 13.68           C  
ANISOU 2173  CA  PHE A 253      254   2722   2223     28    -24    220       C  
ATOM   2174  C   PHE A 253      15.670  23.528  -1.438  1.00 14.82           C  
ANISOU 2174  C   PHE A 253      818   2397   2415    330    -74    218       C  
ATOM   2175  O   PHE A 253      15.076  24.066  -2.358  1.00 14.05           O  
ANISOU 2175  O   PHE A 253      268   2709   2360    189     72    325       O  
ATOM   2176  CB  PHE A 253      13.880  23.212   0.324  1.00 13.92           C  
ANISOU 2176  CB  PHE A 253      254   2715   2320    -21    -36    164       C  
ATOM   2177  CG  PHE A 253      13.756  21.750   0.062  1.00 16.54           C  
ANISOU 2177  CG  PHE A 253      388   3232   2662    209    189    451       C  
ATOM   2178  CD1 PHE A 253      14.147  20.820   1.021  1.00 17.56           C  
ANISOU 2178  CD1 PHE A 253      270   3329   3069    175    172    495       C  
ATOM   2179  CD2 PHE A 253      13.264  21.286  -1.149  1.00 16.60           C  
ANISOU 2179  CD2 PHE A 253      465   2901   2939     90    541    473       C  
ATOM   2180  CE1 PHE A 253      14.028  19.462   0.780  1.00 18.74           C  
ANISOU 2180  CE1 PHE A 253      323   3435   3359    293    395    327       C  
ATOM   2181  CE2 PHE A 253      13.153  19.932  -1.395  1.00 19.26           C  
ANISOU 2181  CE2 PHE A 253      501   3186   3627    107    901   -149       C  
ATOM   2182  CZ  PHE A 253      13.550  19.019  -0.425  1.00 18.51           C  
ANISOU 2182  CZ  PHE A 253      604   2844   3584    374    975   -126       C  
ATOM   2183  N   ASN A 254      16.737  22.765  -1.628  1.00 15.93           N  
ANISOU 2183  N   ASN A 254      390   2858   2802    503   -276    215       N  
ATOM   2184  CA  ASN A 254      17.300  22.567  -2.951  1.00 15.79           C  
ANISOU 2184  CA  ASN A 254      366   2863   2768    398   -337    163       C  
ATOM   2185  C   ASN A 254      16.777  21.301  -3.633  1.00 15.77           C  
ANISOU 2185  C   ASN A 254      380   2703   2908    286    -73    359       C  
ATOM   2186  O   ASN A 254      17.242  20.175  -3.339  1.00 20.58           O  
ANISOU 2186  O   ASN A 254     1097   2964   3756    296    132    332       O  
ATOM   2187  CB  ASN A 254      18.836  22.508  -2.848  1.00 17.17           C  
ANISOU 2187  CB  ASN A 254      323   3014   3184    273   -342    124       C  
ATOM   2188  CG  ASN A 254      19.490  22.368  -4.171  1.00 24.20           C  
ANISOU 2188  CG  ASN A 254     2321   3901   2972    179    144   -115       C  
ATOM   2189  OD1 ASN A 254      18.844  22.366  -5.204  1.00 21.66           O  
ANISOU 2189  OD1 ASN A 254      330   4606   3291    421    270   -587       O  
ATOM   2190  ND2 ASN A 254      20.816  22.229  -4.157  1.00 26.50           N  
ANISOU 2190  ND2 ASN A 254      264   5499   4302    235     59   -140       N  
ATOM   2191  N   ALA A 255      15.816  21.480  -4.550  1.00 15.61           N  
ANISOU 2191  N   ALA A 255      476   2540   2913    448    -82    -85       N  
ATOM   2192  CA  ALA A 255      15.189  20.348  -5.236  1.00 16.13           C  
ANISOU 2192  CA  ALA A 255      380   2532   3215    537    -11     33       C  
ATOM   2193  C   ALA A 255      16.133  19.712  -6.255  1.00 17.50           C  
ANISOU 2193  C   ALA A 255     1184   2468   2997    190    244     70       C  
ATOM   2194  O   ALA A 255      15.900  18.603  -6.740  1.00 22.40           O  
ANISOU 2194  O   ALA A 255     1772   3141   3595    196    418   -135       O  
ATOM   2195  CB  ALA A 255      13.910  20.817  -5.925  1.00 16.55           C  
ANISOU 2195  CB  ALA A 255      352   2960   2975    518      5   -102       C  
ATOM   2196  N   TYR A 256      17.189  20.422  -6.579  1.00 17.43           N  
ANISOU 2196  N   TYR A 256      624   2968   3029    159    517     34       N  
ATOM   2197  CA  TYR A 256      18.053  20.051  -7.699  1.00 19.31           C  
ANISOU 2197  CA  TYR A 256     1278   3073   2984    482    249     82       C  
ATOM   2198  C   TYR A 256      19.173  19.079  -7.287  1.00 22.34           C  
ANISOU 2198  C   TYR A 256     2019   3312   3155    286    120    234       C  
ATOM   2199  O   TYR A 256      19.964  18.660  -8.114  1.00 21.32           O  
ANISOU 2199  O   TYR A 256      706   3661   3734   1053    660    -16       O  
ATOM   2200  CB  TYR A 256      18.606  21.314  -8.360  1.00 17.71           C  
ANISOU 2200  CB  TYR A 256      982   2941   2803    540    639    -26       C  
ATOM   2201  CG  TYR A 256      17.540  22.073  -9.108  1.00 15.78           C  
ANISOU 2201  CG  TYR A 256      785   2588   2621    411    254    125       C  
ATOM   2202  CD1 TYR A 256      16.705  22.986  -8.446  1.00 17.24           C  
ANISOU 2202  CD1 TYR A 256      859   3134   2554    286    372   -363       C  
ATOM   2203  CD2 TYR A 256      17.270  21.793 -10.425  1.00 16.84           C  
ANISOU 2203  CD2 TYR A 256      780   3017   2601    343    130   -309       C  
ATOM   2204  CE1 TYR A 256      15.683  23.646  -9.105  1.00 15.85           C  
ANISOU 2204  CE1 TYR A 256      956   2464   2601    371    259   -262       C  
ATOM   2205  CE2 TYR A 256      16.231  22.439 -11.102  1.00 17.34           C  
ANISOU 2205  CE2 TYR A 256      600   3330   2657    496    522   -468       C  
ATOM   2206  CZ  TYR A 256      15.437  23.376 -10.422  1.00 16.38           C  
ANISOU 2206  CZ  TYR A 256      692   3147   2383    607    403   -212       C  
ATOM   2207  OH  TYR A 256      14.404  23.996 -11.080  1.00 17.33           O  
ANISOU 2207  OH  TYR A 256      733   3192   2659    279     64    -53       O  
ATOM   2208  N  ALYS A 257      19.197  18.685  -6.022  0.50 22.47           N  
ANISOU 2208  N  ALYS A 257     1782   3318   3435    483     51     39       N  
ATOM   2209  N  BLYS A 257      19.199  18.702  -6.009  0.50 22.36           N  
ANISOU 2209  N  BLYS A 257     1701   3334   3460    464     48     48       N  
ATOM   2210  CA ALYS A 257      20.184  17.706  -5.562  0.50 19.24           C  
ANISOU 2210  CA ALYS A 257      804   3041   3464    715    241    -47       C  
ATOM   2211  CA BLYS A 257      20.165  17.699  -5.515  0.50 19.69           C  
ANISOU 2211  CA BLYS A 257      837   3085   3558    665    170     -5       C  
ATOM   2212  C  ALYS A 257      19.584  16.300  -5.486  0.50 21.64           C  
ANISOU 2212  C  ALYS A 257     1512   3055   3654    524     59    -30       C  
ATOM   2213  C  BLYS A 257      19.654  16.279  -5.730  0.50 21.21           C  
ANISOU 2213  C  BLYS A 257     1301   3068   3689    536    120    -28       C  
ATOM   2214  O  ALYS A 257      20.213  15.380  -4.981  0.50 25.94           O  
ANISOU 2214  O  ALYS A 257     2207   3532   4116    148    337    228       O  
ATOM   2215  O  BLYS A 257      20.425  15.313  -5.679  0.50 25.79           O  
ANISOU 2215  O  BLYS A 257     2051   3463   4283    515    130     -3       O  
ATOM   2216  CB ALYS A 257      20.734  18.108  -4.202  0.50 22.11           C  
ANISOU 2216  CB ALYS A 257     1807   3057   3535    613    -34     80       C  
ATOM   2217  CB BLYS A 257      20.418  17.899  -4.031  0.50 21.94           C  
ANISOU 2217  CB BLYS A 257     1492   3153   3688    467    -32    188       C  
ATOM   2218  CG ALYS A 257      19.768  17.893  -3.061  0.50 21.93           C  
ANISOU 2218  CG ALYS A 257     2383   3011   2938    445    281   -111       C  
ATOM   2219  CG BLYS A 257      21.157  19.164  -3.681  0.50 25.75           C  
ANISOU 2219  CG BLYS A 257     2353   3484   3945    453   -340    139       C  
ATOM   2220  CD ALYS A 257      20.383  18.294  -1.740  0.50 29.32           C  
ANISOU 2220  CD ALYS A 257     3349   3973   3817     87   -180    -46       C  
ATOM   2221  CD BLYS A 257      20.994  19.471  -2.221  0.50 30.91           C  
ANISOU 2221  CD BLYS A 257     3455   4117   4170    318    -37     17       C  
ATOM   2222  CE ALYS A 257      19.419  18.059  -0.584  0.50 30.14           C  
ANISOU 2222  CE ALYS A 257     3518   4117   3814    134    -25   -139       C  
ATOM   2223  CE BLYS A 257      20.490  18.246  -1.462  0.50 36.11           C  
ANISOU 2223  CE BLYS A 257     4250   4721   4747     61      5     90       C  
ATOM   2224  NZ ALYS A 257      19.958  18.563   0.722  0.50 33.95           N  
ANISOU 2224  NZ ALYS A 257     4096   4669   4134    365   -377   -110       N  
ATOM   2225  NZ BLYS A 257      19.958  18.602  -0.118  0.50 40.69           N  
ANISOU 2225  NZ BLYS A 257     4849   5497   5112    236    211    -42       N  
ATOM   2226  N   TYR A 258      18.347  16.154  -5.951  1.00 22.99           N  
ANISOU 2226  N   TYR A 258     1448   3422   3863    347    241     -9       N  
ATOM   2227  CA  TYR A 258      17.701  14.868  -5.980  1.00 20.88           C  
ANISOU 2227  CA  TYR A 258     1444   2970   3520    654    441   -129       C  
ATOM   2228  C   TYR A 258      17.634  14.315  -7.396  1.00 22.84           C  
ANISOU 2228  C   TYR A 258     1696   3221   3759    199    462    131       C  
ATOM   2229  O   TYR A 258      17.419  15.052  -8.353  1.00 25.70           O  
ANISOU 2229  O   TYR A 258     2067   3824   3871    890   -114   -104       O  
ATOM   2230  CB  TYR A 258      16.284  14.982  -5.386  1.00 17.70           C  
ANISOU 2230  CB  TYR A 258      413   3024   3287    429    124    -35       C  
ATOM   2231  CG  TYR A 258      16.275  15.414  -3.937  1.00 19.45           C  
ANISOU 2231  CG  TYR A 258      974   2840   3572    430    305     61       C  
ATOM   2232  CD1 TYR A 258      16.282  16.761  -3.592  1.00 18.97           C  
ANISOU 2232  CD1 TYR A 258      878   2892   3437    449     -5    -66       C  
ATOM   2233  CD2 TYR A 258      16.275  14.474  -2.908  1.00 18.42           C  
ANISOU 2233  CD2 TYR A 258      537   2690   3770    831   -120   -260       C  
ATOM   2234  CE1 TYR A 258      16.308  17.154  -2.274  1.00 19.37           C  
ANISOU 2234  CE1 TYR A 258     1068   2724   3565    553    482     29       C  
ATOM   2235  CE2 TYR A 258      16.278  14.857  -1.598  1.00 19.90           C  
ANISOU 2235  CE2 TYR A 258     1071   2926   3561    656    288    138       C  
ATOM   2236  CZ  TYR A 258      16.313  16.203  -1.276  1.00 20.69           C  
ANISOU 2236  CZ  TYR A 258     1344   2782   3733    148    202    -25       C  
ATOM   2237  OH  TYR A 258      16.306  16.600   0.063  1.00 21.23           O  
ANISOU 2237  OH  TYR A 258     1275   3300   3491    538    259    144       O  
ATOM   2238  N   ASP A 259      17.863  13.010  -7.520  1.00 23.86           N  
ANISOU 2238  N   ASP A 259     1374   3609   4081    557    621   -268       N  
ATOM   2239  CA  ASP A 259      17.709  12.312  -8.789  1.00 26.26           C  
ANISOU 2239  CA  ASP A 259     2009   3873   4096    496    455   -313       C  
ATOM   2240  C   ASP A 259      16.321  11.678  -8.847  1.00 26.56           C  
ANISOU 2240  C   ASP A 259     2312   3762   4015    147    402   -337       C  
ATOM   2241  O   ASP A 259      16.046  10.723  -8.141  1.00 25.01           O  
ANISOU 2241  O   ASP A 259     1566   3715   4221    158   1151   -623       O  
ATOM   2242  CB  ASP A 259      18.798  11.230  -8.917  1.00 27.14           C  
ANISOU 2242  CB  ASP A 259     1573   4244   4492    396    -20   -286       C  
ATOM   2243  CG  ASP A 259      18.690  10.429 -10.202  1.00 31.28           C  
ANISOU 2243  CG  ASP A 259     2445   4642   4795    905    422   -502       C  
ATOM   2244  OD1 ASP A 259      17.790  10.714 -11.031  1.00 38.53           O  
ANISOU 2244  OD1 ASP A 259     3343   5883   5412    649    376   -822       O  
ATOM   2245  OD2 ASP A 259      19.509   9.507 -10.385  1.00 39.34           O  
ANISOU 2245  OD2 ASP A 259     3627   5474   5846    634    403   -433       O  
ATOM   2246  N   PHE A 260      15.441  12.240  -9.670  1.00 25.21           N  
ANISOU 2246  N   PHE A 260     2190   3621   3765    209    589   -439       N  
ATOM   2247  CA  PHE A 260      14.030  11.837  -9.646  1.00 23.81           C  
ANISOU 2247  CA  PHE A 260     1864   3572   3612    250    431   -334       C  
ATOM   2248  C   PHE A 260      13.760  10.596 -10.477  1.00 27.36           C  
ANISOU 2248  C   PHE A 260     2527   3867   4000     92    233   -330       C  
ATOM   2249  O   PHE A 260      12.600  10.206 -10.671  1.00 27.86           O  
ANISOU 2249  O   PHE A 260     2672   3778   4134     69      3   -358       O  
ATOM   2250  CB  PHE A 260      13.131  12.990 -10.089  1.00 25.55           C  
ANISOU 2250  CB  PHE A 260     2235   3926   3544    140    -15   -252       C  
ATOM   2251  CG  PHE A 260      13.120  14.131  -9.132  1.00 23.82           C  
ANISOU 2251  CG  PHE A 260     1850   3739   3459    550    153    -85       C  
ATOM   2252  CD1 PHE A 260      12.594  13.975  -7.857  1.00 24.92           C  
ANISOU 2252  CD1 PHE A 260     1098   4605   3764    -74     96   -480       C  
ATOM   2253  CD2 PHE A 260      13.679  15.335  -9.470  1.00 23.21           C  
ANISOU 2253  CD2 PHE A 260     1509   3539   3769    853    331   -240       C  
ATOM   2254  CE1 PHE A 260      12.618  15.010  -6.961  1.00 21.67           C  
ANISOU 2254  CE1 PHE A 260     1500   3731   3003    648    440   -273       C  
ATOM   2255  CE2 PHE A 260      13.711  16.370  -8.569  1.00 27.31           C  
ANISOU 2255  CE2 PHE A 260     3144   3546   3685    640    277   -185       C  
ATOM   2256  CZ  PHE A 260      13.180  16.206  -7.314  1.00 20.76           C  
ANISOU 2256  CZ  PHE A 260      869   3639   3379   1444      0     -4       C  
ATOM   2257  N   THR A 261      14.829   9.959 -10.954  1.00 30.00           N  
ANISOU 2257  N   THR A 261     3539   3737   4120    223    133   -451       N  
ATOM   2258  CA  THR A 261      14.730   8.609 -11.498  1.00 31.38           C  
ANISOU 2258  CA  THR A 261     3687   4016   4217    258    145   -378       C  
ATOM   2259  C   THR A 261      15.245   7.586 -10.490  1.00 30.94           C  
ANISOU 2259  C   THR A 261     3728   3794   4234    346     88   -362       C  
ATOM   2260  O   THR A 261      15.207   6.384 -10.743  1.00 34.80           O  
ANISOU 2260  O   THR A 261     4254   4308   4659    287     79   -348       O  
ATOM   2261  CB  THR A 261      15.510   8.461 -12.831  1.00 31.86           C  
ANISOU 2261  CB  THR A 261     3878   4100   4125    330     59   -386       C  
ATOM   2262  OG1 THR A 261      16.922   8.579 -12.589  1.00 36.13           O  
ANISOU 2262  OG1 THR A 261     3741   5307   4679    557    527   -669       O  
ATOM   2263  CG2 THR A 261      15.069   9.521 -13.838  1.00 37.84           C  
ANISOU 2263  CG2 THR A 261     5314   4656   4407    104    136   -151       C  
ATOM   2264  N   SER A 262      15.729   8.070  -9.346  1.00 29.67           N  
ANISOU 2264  N   SER A 262     3312   3738   4223    540     51   -324       N  
ATOM   2265  CA  SER A 262      16.161   7.186  -8.256  1.00 29.09           C  
ANISOU 2265  CA  SER A 262     3141   3609   4301    361    151   -316       C  
ATOM   2266  C   SER A 262      15.041   6.949  -7.259  1.00 27.80           C  
ANISOU 2266  C   SER A 262     2470   3437   4654    405    -23   -124       C  
ATOM   2267  O   SER A 262      14.501   7.888  -6.680  1.00 26.39           O  
ANISOU 2267  O   SER A 262     1805   3301   4920    570    217   -336       O  
ATOM   2268  CB  SER A 262      17.364   7.777  -7.526  1.00 29.52           C  
ANISOU 2268  CB  SER A 262     2896   3943   4374    453    104   -330       C  
ATOM   2269  OG  SER A 262      17.504   7.199  -6.237  1.00 27.08           O  
ANISOU 2269  OG  SER A 262     1920   3838   4531   1108    616   -474       O  
ATOM   2270  N   GLU A 263      14.732   5.687  -7.021  1.00 28.07           N  
ANISOU 2270  N   GLU A 263     2610   3296   4756    729   -242     69       N  
ATOM   2271  CA  GLU A 263      13.645   5.329  -6.129  1.00 27.87           C  
ANISOU 2271  CA  GLU A 263     3130   3008   4450    345   -123    231       C  
ATOM   2272  C   GLU A 263      13.882   5.850  -4.711  1.00 29.79           C  
ANISOU 2272  C   GLU A 263     3291   3237   4791    398   -120    114       C  
ATOM   2273  O   GLU A 263      12.953   6.327  -4.056  1.00 29.50           O  
ANISOU 2273  O   GLU A 263     2267   3503   5437    548    -91    870       O  
ATOM   2274  CB  GLU A 263      13.451   3.808  -6.114  1.00 31.82           C  
ANISOU 2274  CB  GLU A 263     3956   3560   4571    267   -142    147       C  
ATOM   2275  CG  GLU A 263      13.011   3.243  -7.454  1.00 34.06           C  
ANISOU 2275  CG  GLU A 263     4034   3881   5024   -185   -372      9       C  
ATOM   2276  CD  GLU A 263      11.753   3.913  -7.978  1.00 37.98           C  
ANISOU 2276  CD  GLU A 263     4297   5100   5034    324     41   -186       C  
ATOM   2277  OE1 GLU A 263      10.837   4.184  -7.168  1.00 38.45           O  
ANISOU 2277  OE1 GLU A 263     3064   6704   4840  -1390      0   -543       O  
ATOM   2278  OE2 GLU A 263      11.684   4.182  -9.194  1.00 40.37           O  
ANISOU 2278  OE2 GLU A 263     4761   5643   4933    754    234   -489       O  
ATOM   2279  N   ASP A 264      15.132   5.779  -4.252  1.00 29.02           N  
ANISOU 2279  N   ASP A 264     3179   3097   4747    674   -188     55       N  
ATOM   2280  CA  ASP A 264      15.504   6.271  -2.916  1.00 28.45           C  
ANISOU 2280  CA  ASP A 264     2995   3302   4510    631    -76     70       C  
ATOM   2281  C   ASP A 264      15.358   7.795  -2.812  1.00 26.82           C  
ANISOU 2281  C   ASP A 264     2764   3183   4243    508    216     19       C  
ATOM   2282  O   ASP A 264      14.887   8.314  -1.793  1.00 26.28           O  
ANISOU 2282  O   ASP A 264     2343   3041   4598    824    260    163       O  
ATOM   2283  CB  ASP A 264      16.955   5.888  -2.593  1.00 29.35           C  
ANISOU 2283  CB  ASP A 264     2892   3592   4666    663    -50     57       C  
ATOM   2284  CG  ASP A 264      17.115   4.413  -2.248  1.00 37.56           C  
ANISOU 2284  CG  ASP A 264     4309   4195   5767    487   -119    118       C  
ATOM   2285  OD1 ASP A 264      16.096   3.744  -1.963  1.00 41.98           O  
ANISOU 2285  OD1 ASP A 264     5347   3954   6648    853   -384    658       O  
ATOM   2286  OD2 ASP A 264      18.270   3.928  -2.251  1.00 46.79           O  
ANISOU 2286  OD2 ASP A 264     5412   5368   6995    861    149     26       O  
ATOM   2287  N   ASP A 265      15.803   8.506  -3.851  1.00 25.49           N  
ANISOU 2287  N   ASP A 265     2239   3093   4352    673    328     47       N  
ATOM   2288  CA  ASP A 265      15.736   9.977  -3.863  1.00 22.77           C  
ANISOU 2288  CA  ASP A 265     1571   3166   3912    262    573    -22       C  
ATOM   2289  C   ASP A 265      14.300  10.457  -3.936  1.00 24.31           C  
ANISOU 2289  C   ASP A 265     1886   3240   4109    589    715   -140       C  
ATOM   2290  O   ASP A 265      13.954  11.468  -3.325  1.00 29.28           O  
ANISOU 2290  O   ASP A 265     3203   3157   4765    494   1484    -80       O  
ATOM   2291  CB  ASP A 265      16.532  10.553  -5.041  1.00 22.29           C  
ANISOU 2291  CB  ASP A 265     1431   3306   3730    373    747   -199       C  
ATOM   2292  CG  ASP A 265      18.028  10.614  -4.767  1.00 26.43           C  
ANISOU 2292  CG  ASP A 265     2095   3742   4205    557    101    188       C  
ATOM   2293  OD1 ASP A 265      18.490   9.982  -3.802  1.00 29.96           O  
ANISOU 2293  OD1 ASP A 265     2000   4500   4880    380    922    450       O  
ATOM   2294  OD2 ASP A 265      18.735  11.319  -5.512  1.00 29.54           O  
ANISOU 2294  OD2 ASP A 265     2421   4169   4634    350    414     36       O  
ATOM   2295  N   LYS A 266      13.468   9.771  -4.719  1.00 24.32           N  
ANISOU 2295  N   LYS A 266     1841   3155   4244   1084    488    146       N  
ATOM   2296  CA  LYS A 266      12.053  10.138  -4.791  1.00 24.74           C  
ANISOU 2296  CA  LYS A 266     1980   3082   4337   1295    456    190       C  
ATOM   2297  C   LYS A 266      11.518  10.206  -3.365  1.00 27.05           C  
ANISOU 2297  C   LYS A 266     2585   3379   4313    831    373    537       C  
ATOM   2298  O   LYS A 266      10.833  11.158  -2.990  1.00 30.46           O  
ANISOU 2298  O   LYS A 266     2672   3754   5147   1851   1010    452       O  
ATOM   2299  CB  LYS A 266      11.250   9.113  -5.604  1.00 25.58           C  
ANISOU 2299  CB  LYS A 266     1990   3410   4317   1171    246    272       C  
ATOM   2300  CG  LYS A 266      11.454   9.178  -7.149  1.00 26.76           C  
ANISOU 2300  CG  LYS A 266     1878   3802   4487    880     87    436       C  
ATOM   2301  CD  LYS A 266      10.699   8.019  -7.864  1.00 31.39           C  
ANISOU 2301  CD  LYS A 266     3596   4038   4292    736   -135    497       C  
ATOM   2302  CE  LYS A 266      11.048   7.918  -9.344  1.00 30.60           C  
ANISOU 2302  CE  LYS A 266     2924   3863   4839    253   -223    182       C  
ATOM   2303  NZ  LYS A 266      10.402   6.736 -10.009  1.00 33.95           N  
ANISOU 2303  NZ  LYS A 266     3752   4421   4724    580    -18    120       N  
ATOM   2304  N   LYS A 267      11.834   9.200  -2.566  1.00 24.41           N  
ANISOU 2304  N   LYS A 267     2043   2987   4244    646    357    424       N  
ATOM   2305  CA  LYS A 267      11.293   9.110  -1.229  1.00 25.19           C  
ANISOU 2305  CA  LYS A 267     2789   2951   3829    615    208    211       C  
ATOM   2306  C   LYS A 267      11.891  10.158  -0.303  1.00 23.44           C  
ANISOU 2306  C   LYS A 267     1741   3290   3874    350    485    391       C  
ATOM   2307  O   LYS A 267      11.163  10.777   0.487  1.00 26.45           O  
ANISOU 2307  O   LYS A 267     2549   3552   3947   1108    777    167       O  
ATOM   2308  CB  LYS A 267      11.500   7.707  -0.654  1.00 27.37           C  
ANISOU 2308  CB  LYS A 267     3108   3325   3965    201    121    308       C  
ATOM   2309  CG  LYS A 267      10.700   6.626  -1.360  1.00 30.04           C  
ANISOU 2309  CG  LYS A 267     3842   3369   4202    232    295     80       C  
ATOM   2310  CD  LYS A 267      10.862   5.284  -0.670  1.00 36.02           C  
ANISOU 2310  CD  LYS A 267     4897   4337   4452    269    446    298       C  
ATOM   2311  N   SER A 268      13.204  10.377  -0.405  1.00 21.65           N  
ANISOU 2311  N   SER A 268     1606   2827   3790    781    197    294       N  
ATOM   2312  CA  SER A 268      13.881  11.358   0.436  1.00 19.15           C  
ANISOU 2312  CA  SER A 268     1205   2829   3241    853    423    160       C  
ATOM   2313  C   SER A 268      13.388  12.781   0.139  1.00 19.31           C  
ANISOU 2313  C   SER A 268     1362   2850   3123    621    187    230       C  
ATOM   2314  O   SER A 268      13.274  13.608   1.032  1.00 20.58           O  
ANISOU 2314  O   SER A 268     1443   2968   3408    901   -198    334       O  
ATOM   2315  CB  SER A 268      15.381  11.286   0.213  1.00 21.20           C  
ANISOU 2315  CB  SER A 268     1319   2899   3836   1183    -42    290       C  
ATOM   2316  OG  SER A 268      15.929  10.071   0.726  1.00 33.39           O  
ANISOU 2316  OG  SER A 268     3306   4206   5172   1284     50    552       O  
ATOM   2317  N   PHE A 269      13.135  13.053  -1.127  1.00 19.10           N  
ANISOU 2317  N   PHE A 269     1411   2861   2984    856    292    238       N  
ATOM   2318  CA  PHE A 269      12.679  14.374  -1.548  1.00 16.11           C  
ANISOU 2318  CA  PHE A 269      934   2542   2645    412    312     79       C  
ATOM   2319  C   PHE A 269      11.465  14.804  -0.749  1.00 16.71           C  
ANISOU 2319  C   PHE A 269     1063   2744   2540    275     12   -109       C  
ATOM   2320  O   PHE A 269      11.447  15.882  -0.177  1.00 15.52           O  
ANISOU 2320  O   PHE A 269      445   2687   2764    243     72     24       O  
ATOM   2321  CB  PHE A 269      12.359  14.364  -3.029  1.00 16.90           C  
ANISOU 2321  CB  PHE A 269      782   2782   2856    641    498     43       C  
ATOM   2322  CG  PHE A 269      11.798  15.645  -3.536  1.00 16.43           C  
ANISOU 2322  CG  PHE A 269      846   2600   2795    339    114    132       C  
ATOM   2323  CD1 PHE A 269      12.590  16.733  -3.733  1.00 15.77           C  
ANISOU 2323  CD1 PHE A 269      427   2576   2989    559    316    -49       C  
ATOM   2324  CD2 PHE A 269      10.443  15.751  -3.819  1.00 15.71           C  
ANISOU 2324  CD2 PHE A 269      256   3164   2546     55    -82   -271       C  
ATOM   2325  CE1 PHE A 269      12.072  17.908  -4.234  1.00 17.98           C  
ANISOU 2325  CE1 PHE A 269     1286   2634   2909    -84     26     27       C  
ATOM   2326  CE2 PHE A 269       9.916  16.934  -4.291  1.00 16.40           C  
ANISOU 2326  CE2 PHE A 269      687   3288   2255    300    341     78       C  
ATOM   2327  CZ  PHE A 269      10.742  18.007  -4.498  1.00 17.54           C  
ANISOU 2327  CZ  PHE A 269      712   3267   2682    417    441    132       C  
ATOM   2328  N   PHE A 270      10.441  13.958  -0.719  1.00 15.81           N  
ANISOU 2328  N   PHE A 270      906   2359   2740    696    -28    -25       N  
ATOM   2329  CA  PHE A 270       9.205  14.332  -0.067  1.00 15.28           C  
ANISOU 2329  CA  PHE A 270      871   2411   2521    389    -64     54       C  
ATOM   2330  C   PHE A 270       9.343  14.384   1.445  1.00 16.41           C  
ANISOU 2330  C   PHE A 270     1239   2456   2538    607    -66     32       C  
ATOM   2331  O   PHE A 270       8.757  15.243   2.086  1.00 17.22           O  
ANISOU 2331  O   PHE A 270      758   2977   2807    604    110     96       O  
ATOM   2332  CB  PHE A 270       8.077  13.405  -0.483  1.00 15.64           C  
ANISOU 2332  CB  PHE A 270      950   2366   2625    129    310    143       C  
ATOM   2333  CG  PHE A 270       7.673  13.572  -1.912  1.00 15.53           C  
ANISOU 2333  CG  PHE A 270      788   2498   2613    240     92     38       C  
ATOM   2334  CD1 PHE A 270       7.029  14.721  -2.331  1.00 15.97           C  
ANISOU 2334  CD1 PHE A 270     1214   2317   2535    155    126    -43       C  
ATOM   2335  CD2 PHE A 270       7.975  12.606  -2.850  1.00 19.88           C  
ANISOU 2335  CD2 PHE A 270     2186   2715   2650    513   -248     52       C  
ATOM   2336  CE1 PHE A 270       6.691  14.896  -3.645  1.00 17.20           C  
ANISOU 2336  CE1 PHE A 270      610   2833   3091    201    149   -196       C  
ATOM   2337  CE2 PHE A 270       7.621  12.772  -4.161  1.00 18.30           C  
ANISOU 2337  CE2 PHE A 270     1940   2275   2738    465    -96   -164       C  
ATOM   2338  CZ  PHE A 270       6.961  13.919  -4.555  1.00 17.60           C  
ANISOU 2338  CZ  PHE A 270     1292   2821   2574    262   -302    -78       C  
ATOM   2339  N   LYS A 271      10.171  13.508   2.008  1.00 16.56           N  
ANISOU 2339  N   LYS A 271      919   2673   2697    238   -123    349       N  
ATOM   2340  CA  LYS A 271      10.399  13.510   3.447  1.00 18.13           C  
ANISOU 2340  CA  LYS A 271     1426   2622   2841    549    -46    269       C  
ATOM   2341  C   LYS A 271      11.174  14.745   3.880  1.00 16.71           C  
ANISOU 2341  C   LYS A 271     1185   2493   2671    778    135    282       C  
ATOM   2342  O   LYS A 271      10.810  15.410   4.862  1.00 17.30           O  
ANISOU 2342  O   LYS A 271      807   3165   2602    698   -180    279       O  
ATOM   2343  CB  LYS A 271      11.154  12.251   3.879  1.00 20.72           C  
ANISOU 2343  CB  LYS A 271     2080   2759   3033    273    -67    221       C  
ATOM   2344  CG  LYS A 271      11.225  12.083   5.377  1.00 29.61           C  
ANISOU 2344  CG  LYS A 271     3641   3620   3988    611   -224     68       C  
ATOM   2345  CD  LYS A 271      12.175  10.974   5.783  0.01 24.10           C  
ANISOU 2345  CD  LYS A 271     2994   3047   3116    122    -41     24       C  
ATOM   2346  CE  LYS A 271      12.193  10.790   7.294  0.01 23.12           C  
ANISOU 2346  CE  LYS A 271     2886   2892   3007     60    -26      4       C  
ATOM   2347  NZ  LYS A 271      13.052   9.648   7.710  0.01 22.47           N  
ANISOU 2347  NZ  LYS A 271     2819   2820   2896     12    -12     18       N  
ATOM   2348  N   ASP A 272      12.246  15.058   3.147  1.00 17.55           N  
ANISOU 2348  N   ASP A 272     1330   2774   2564    339     46    487       N  
ATOM   2349  CA  ASP A 272      13.066  16.206   3.456  1.00 16.85           C  
ANISOU 2349  CA  ASP A 272      997   2759   2646    562    160    217       C  
ATOM   2350  C   ASP A 272      12.277  17.498   3.251  1.00 16.18           C  
ANISOU 2350  C   ASP A 272      956   2578   2614    457   -156    223       C  
ATOM   2351  O   ASP A 272      12.432  18.454   4.019  1.00 15.41           O  
ANISOU 2351  O   ASP A 272      359   2955   2540    501   -148    129       O  
ATOM   2352  CB  ASP A 272      14.308  16.235   2.565  1.00 17.08           C  
ANISOU 2352  CB  ASP A 272     1133   2703   2654    420     36    231       C  
ATOM   2353  CG  ASP A 272      15.237  15.053   2.798  1.00 22.82           C  
ANISOU 2353  CG  ASP A 272     1731   3731   3207    389    485    390       C  
ATOM   2354  OD1 ASP A 272      15.152  14.399   3.858  1.00 26.33           O  
ANISOU 2354  OD1 ASP A 272     2096   4048   3859    591   -137    612       O  
ATOM   2355  OD2 ASP A 272      16.086  14.807   1.923  1.00 22.57           O  
ANISOU 2355  OD2 ASP A 272     1190   4043   3341    928    188    880       O  
ATOM   2356  N   TRP A 273      11.455  17.549   2.202  1.00 14.48           N  
ANISOU 2356  N   TRP A 273      432   2728   2339    614    -35     45       N  
ATOM   2357  CA  TRP A 273      10.614  18.735   1.997  1.00 13.77           C  
ANISOU 2357  CA  TRP A 273      554   2563   2113    403    -86     74       C  
ATOM   2358  C   TRP A 273       9.713  18.968   3.220  1.00 13.41           C  
ANISOU 2358  C   TRP A 273      441   2519   2135    231   -537    170       C  
ATOM   2359  O   TRP A 273       9.595  20.082   3.716  1.00 13.24           O  
ANISOU 2359  O   TRP A 273      292   2708   2029    260   -127    176       O  
ATOM   2360  CB  TRP A 273       9.751  18.631   0.735  1.00 13.61           C  
ANISOU 2360  CB  TRP A 273      733   2405   2030    245    -95    127       C  
ATOM   2361  CG  TRP A 273       8.638  19.660   0.784  1.00 13.04           C  
ANISOU 2361  CG  TRP A 273      269   2519   2167    181     46    -60       C  
ATOM   2362  CD1 TRP A 273       7.339  19.455   1.182  1.00 12.49           C  
ANISOU 2362  CD1 TRP A 273      259   2599   1886    -96     55    242       C  
ATOM   2363  CD2 TRP A 273       8.770  21.060   0.571  1.00 11.73           C  
ANISOU 2363  CD2 TRP A 273      271   2297   1888    190    -13    -15       C  
ATOM   2364  NE1 TRP A 273       6.652  20.646   1.191  1.00 12.47           N  
ANISOU 2364  NE1 TRP A 273      364   2341   2032    338   -201    101       N  
ATOM   2365  CE2 TRP A 273       7.509  21.650   0.828  1.00 12.16           C  
ANISOU 2365  CE2 TRP A 273      407   2273   1939    375    -31     35       C  
ATOM   2366  CE3 TRP A 273       9.831  21.883   0.162  1.00 13.03           C  
ANISOU 2366  CE3 TRP A 273      295   2590   2064    302    106    211       C  
ATOM   2367  CZ2 TRP A 273       7.294  22.993   0.692  1.00 13.78           C  
ANISOU 2367  CZ2 TRP A 273      530   2647   2057    211    -97    135       C  
ATOM   2368  CZ3 TRP A 273       9.623  23.206   0.042  1.00 12.63           C  
ANISOU 2368  CZ3 TRP A 273      341   2341   2114     98   -301    417       C  
ATOM   2369  CH2 TRP A 273       8.367  23.772   0.324  1.00 12.33           C  
ANISOU 2369  CH2 TRP A 273      505   2104   2073    264   -614     67       C  
ATOM   2370  N   GLN A 274       9.089  17.913   3.702  1.00 13.98           N  
ANISOU 2370  N   GLN A 274      626   2401   2284    463    -52    197       N  
ATOM   2371  CA  GLN A 274       8.134  18.074   4.795  1.00 13.82           C  
ANISOU 2371  CA  GLN A 274      612   2606   2029    197    145     10       C  
ATOM   2372  C   GLN A 274       8.839  18.565   6.077  1.00 13.91           C  
ANISOU 2372  C   GLN A 274      307   2745   2233    367     18    112       C  
ATOM   2373  O   GLN A 274       8.294  19.382   6.823  1.00 15.03           O  
ANISOU 2373  O   GLN A 274      952   2649   2109    312   -162     84       O  
ATOM   2374  CB  GLN A 274       7.373  16.780   5.064  1.00 15.49           C  
ANISOU 2374  CB  GLN A 274      591   2768   2526    251   -106    274       C  
ATOM   2375  CG  GLN A 274       6.141  16.951   5.966  1.00 15.43           C  
ANISOU 2375  CG  GLN A 274     1090   2816   1957     66   -107    467       C  
ATOM   2376  CD  GLN A 274       4.996  17.674   5.271  1.00 15.63           C  
ANISOU 2376  CD  GLN A 274     1318   2780   1839     -8    318    645       C  
ATOM   2377  OE1 GLN A 274       5.058  17.940   4.075  1.00 15.21           O  
ANISOU 2377  OE1 GLN A 274      320   3069   2389    233    211    368       O  
ATOM   2378  NE2 GLN A 274       3.918  17.961   6.021  1.00 14.94           N  
ANISOU 2378  NE2 GLN A 274      731   2967   1975     77     69    381       N  
ATOM   2379  N  AGLN A 275      10.067  18.101   6.293  0.50 14.66           N  
ANISOU 2379  N  AGLN A 275      438   2914   2218    441    -52    -76       N  
ATOM   2380  N  BGLN A 275      10.055  18.090   6.306  0.50 15.14           N  
ANISOU 2380  N  BGLN A 275      503   2965   2282    468    -39    -85       N  
ATOM   2381  CA AGLN A 275      10.854  18.526   7.448  0.50 15.08           C  
ANISOU 2381  CA AGLN A 275      656   2845   2226    173   -156     49       C  
ATOM   2382  CA BGLN A 275      10.830  18.541   7.447  0.50 16.46           C  
ANISOU 2382  CA BGLN A 275      920   2961   2371    242   -149     22       C  
ATOM   2383  C  AGLN A 275      11.258  20.003   7.347  0.50 17.06           C  
ANISOU 2383  C  AGLN A 275     1179   3038   2263    289    -29     67       C  
ATOM   2384  C  BGLN A 275      11.179  20.021   7.327  0.50 17.50           C  
ANISOU 2384  C  BGLN A 275     1239   3105   2303    330    -24     39       C  
ATOM   2385  O  AGLN A 275      11.264  20.724   8.344  0.50 16.31           O  
ANISOU 2385  O  AGLN A 275      678   3185   2334    227     20      8       O  
ATOM   2386  O  BGLN A 275      11.031  20.780   8.284  0.50 18.18           O  
ANISOU 2386  O  BGLN A 275     1403   3205   2297    386   -289     46       O  
ATOM   2387  CB AGLN A 275      12.108  17.654   7.584  0.50 16.73           C  
ANISOU 2387  CB AGLN A 275     1037   2886   2430    219   -132    154       C  
ATOM   2388  CB BGLN A 275      12.104  17.708   7.592  0.50 18.79           C  
ANISOU 2388  CB BGLN A 275     1340   3155   2641    298    -76     64       C  
ATOM   2389  CG AGLN A 275      13.100  18.146   8.637  0.50 15.94           C  
ANISOU 2389  CG AGLN A 275      958   2770   2327    -26   -336    345       C  
ATOM   2390  CG BGLN A 275      11.888  16.393   8.322  0.50 23.29           C  
ANISOU 2390  CG BGLN A 275     2203   3418   3225    508   -248    144       C  
ATOM   2391  CD AGLN A 275      12.535  18.117  10.051  0.50 19.22           C  
ANISOU 2391  CD AGLN A 275     1538   2945   2819    331   -232    111       C  
ATOM   2392  CD BGLN A 275      11.424  16.584   9.760  0.50 27.83           C  
ANISOU 2392  CD BGLN A 275     3038   3860   3674    321    118    185       C  
ATOM   2393  OE1AGLN A 275      11.737  17.241  10.399  0.50 17.92           O  
ANISOU 2393  OE1AGLN A 275      987   3158   2663    428   -598    708       O  
ATOM   2394  OE1BGLN A 275      11.625  17.644  10.357  0.50 35.17           O  
ANISOU 2394  OE1BGLN A 275     4091   4422   4849    239   -207    258       O  
ATOM   2395  NE2AGLN A 275      12.977  19.059  10.886  0.50 22.22           N  
ANISOU 2395  NE2AGLN A 275     2480   2914   3048    451   -734    371       N  
ATOM   2396  NE2BGLN A 275      10.815  15.553  10.323  0.50 36.56           N  
ANISOU 2396  NE2BGLN A 275     3981   4547   5362   -110    -44    139       N  
ATOM   2397  N   TYR A 276      11.652  20.429   6.152  1.00 14.34           N  
ANISOU 2397  N   TYR A 276      268   2976   2205     70   -160     65       N  
ATOM   2398  CA  TYR A 276      11.951  21.834   5.913  1.00 14.10           C  
ANISOU 2398  CA  TYR A 276      288   2771   2297    -13   -134     73       C  
ATOM   2399  C   TYR A 276      10.712  22.717   6.129  1.00 14.34           C  
ANISOU 2399  C   TYR A 276      516   2833   2098    226   -133     33       C  
ATOM   2400  O   TYR A 276      10.762  23.737   6.820  1.00 15.53           O  
ANISOU 2400  O   TYR A 276      373   3301   2226    248   -446    -24       O  
ATOM   2401  CB  TYR A 276      12.495  22.034   4.489  1.00 13.91           C  
ANISOU 2401  CB  TYR A 276      254   2859   2169     61    -18     75       C  
ATOM   2402  CG  TYR A 276      12.333  23.431   4.006  1.00 13.72           C  
ANISOU 2402  CG  TYR A 276      253   2859   2099    -13     -6    121       C  
ATOM   2403  CD1 TYR A 276      13.133  24.449   4.482  1.00 16.26           C  
ANISOU 2403  CD1 TYR A 276      741   2704   2732    385   -221    287       C  
ATOM   2404  CD2 TYR A 276      11.344  23.751   3.100  1.00 14.03           C  
ANISOU 2404  CD2 TYR A 276      285   2760   2286   -171   -208     84       C  
ATOM   2405  CE1 TYR A 276      12.930  25.752   4.076  1.00 15.28           C  
ANISOU 2405  CE1 TYR A 276      259   2630   2916    -24   -122    -78       C  
ATOM   2406  CE2 TYR A 276      11.131  25.029   2.702  1.00 14.84           C  
ANISOU 2406  CE2 TYR A 276      558   2627   2452     95    112    179       C  
ATOM   2407  CZ  TYR A 276      11.895  26.034   3.192  1.00 14.00           C  
ANISOU 2407  CZ  TYR A 276      421   2626   2270   -172   -282    113       C  
ATOM   2408  OH  TYR A 276      11.670  27.324   2.791  1.00 15.25           O  
ANISOU 2408  OH  TYR A 276      256   2947   2589    -57     63    192       O  
ATOM   2409  N   TYR A 277       9.610  22.325   5.524  1.00 13.58           N  
ANISOU 2409  N   TYR A 277      506   2733   1918     82   -186   -103       N  
ATOM   2410  CA  TYR A 277       8.429  23.203   5.409  1.00 12.40           C  
ANISOU 2410  CA  TYR A 277      334   2527   1850    232     69    134       C  
ATOM   2411  C   TYR A 277       7.621  23.274   6.684  1.00 14.18           C  
ANISOU 2411  C   TYR A 277      489   2659   2240    273   -207    206       C  
ATOM   2412  O   TYR A 277       7.084  24.318   7.012  1.00 15.70           O  
ANISOU 2412  O   TYR A 277      394   3212   2357    474    -63    150       O  
ATOM   2413  CB  TYR A 277       7.547  22.725   4.271  1.00 11.67           C  
ANISOU 2413  CB  TYR A 277      278   2341   1814    227    -19     88       C  
ATOM   2414  CG  TYR A 277       6.306  23.593   4.045  1.00 11.81           C  
ANISOU 2414  CG  TYR A 277      295   2471   1721    255   -156   -153       C  
ATOM   2415  CD1 TYR A 277       6.425  24.880   3.558  1.00 12.52           C  
ANISOU 2415  CD1 TYR A 277      293   2309   2152    144   -236     14       C  
ATOM   2416  CD2 TYR A 277       5.032  23.095   4.259  1.00 11.01           C  
ANISOU 2416  CD2 TYR A 277      300   2068   1812   -187   -112    271       C  
ATOM   2417  CE1 TYR A 277       5.337  25.660   3.333  1.00 10.94           C  
ANISOU 2417  CE1 TYR A 277      515   1796   1846   -208   -230    198       C  
ATOM   2418  CE2 TYR A 277       3.940  23.860   4.005  1.00 11.61           C  
ANISOU 2418  CE2 TYR A 277      352   2391   1668    429   -123     53       C  
ATOM   2419  CZ  TYR A 277       4.096  25.144   3.550  1.00 10.80           C  
ANISOU 2419  CZ  TYR A 277      308   2161   1633   -283   -147     69       C  
ATOM   2420  OH  TYR A 277       2.976  25.920   3.296  1.00 12.06           O  
ANISOU 2420  OH  TYR A 277      280   2196   2103    210    -75    123       O  
ATOM   2421  N  ASER A 278       7.549  22.159   7.409  0.70 13.43           N  
ANISOU 2421  N  ASER A 278      312   2809   1981    339    171    127       N  
ATOM   2422  N  BSER A 278       7.572  22.176   7.428  0.30 13.36           N  
ANISOU 2422  N  BSER A 278      300   2707   2066    322    105     95       N  
ATOM   2423  CA ASER A 278       6.617  22.041   8.525  0.70 13.93           C  
ANISOU 2423  CA ASER A 278      495   2921   1875    261    -55    212       C  
ATOM   2424  CA BSER A 278       6.623  22.053   8.528  0.30 15.16           C  
ANISOU 2424  CA BSER A 278      882   2849   2028    152    -85     84       C  
ATOM   2425  C  ASER A 278       7.239  22.365   9.889  0.70 14.80           C  
ANISOU 2425  C  ASER A 278      697   2754   2172    -88     11    -59       C  
ATOM   2426  C  BSER A 278       7.242  22.324   9.902  0.30 16.06           C  
ANISOU 2426  C  BSER A 278      948   2905   2245      9    -61    -49       C  
ATOM   2427  O  ASER A 278       6.522  22.717  10.828  0.70 15.08           O  
ANISOU 2427  O  ASER A 278      598   3136   1996    355   -231   -156       O  
ATOM   2428  O  BSER A 278       6.524  22.594  10.866  0.30 16.07           O  
ANISOU 2428  O  BSER A 278      767   3125   2213    344   -163    -91       O  
ATOM   2429  CB ASER A 278       6.040  20.642   8.567  0.70 14.98           C  
ANISOU 2429  CB ASER A 278      583   2988   2120    -17      3     93       C  
ATOM   2430  CB BSER A 278       6.007  20.667   8.517  0.30 16.05           C  
ANISOU 2430  CB BSER A 278     1085   2838   2173     92     44     30       C  
ATOM   2431  OG ASER A 278       6.960  19.719   9.118  0.70 16.78           O  
ANISOU 2431  OG ASER A 278     1398   2805   2169     69    139    482       O  
ATOM   2432  OG BSER A 278       5.528  20.346   7.226  0.30 16.53           O  
ANISOU 2432  OG BSER A 278     1222   3110   1949    171   -487     64       O  
ATOM   2433  N   ASN A 279       8.571  22.253   9.984  1.00 17.22           N  
ANISOU 2433  N   ASN A 279      507   3712   2321   -123     21   -211       N  
ATOM   2434  CA  ASN A 279       9.269  22.173  11.286  1.00 22.08           C  
ANISOU 2434  CA  ASN A 279     1795   3632   2960   -178   -230   -118       C  
ATOM   2435  C   ASN A 279      10.338  23.236  11.411  1.00 24.68           C  
ANISOU 2435  C   ASN A 279     2160   4167   3049   -448   -177    -79       C  
ATOM   2436  O   ASN A 279      10.716  23.843  10.442  1.00 24.88           O  
ANISOU 2436  O   ASN A 279     1464   4739   3248   -164   -356   -152       O  
ATOM   2437  CB  ASN A 279       9.945  20.790  11.459  1.00 25.59           C  
ANISOU 2437  CB  ASN A 279     3138   3600   2983    126   -319    -66       C  
ATOM   2438  CG  ASN A 279       8.945  19.674  11.742  1.00 22.83           C  
ANISOU 2438  CG  ASN A 279     2128   3473   3072    489   -619    111       C  
ATOM   2439  OD1 ASN A 279       7.836  19.928  12.171  1.00 19.51           O  
ANISOU 2439  OD1 ASN A 279     1264   3371   2776    509    339    209       O  
ATOM   2440  ND2 ASN A 279       9.343  18.427  11.468  1.00 29.86           N  
ANISOU 2440  ND2 ASN A 279     3281   3897   4166    420    149     33       N  
ATOM   2441  N   VAL A 280      10.833  23.438  12.629  1.00 28.83           N  
ANISOU 2441  N   VAL A 280     2781   4670   3503    -78   -540    -55       N  
ATOM   2442  CA  VAL A 280      11.821  24.493  12.883  1.00 30.26           C  
ANISOU 2442  CA  VAL A 280     2834   4624   4036    -92   -308    -63       C  
ATOM   2443  C   VAL A 280      13.245  23.994  12.639  1.00 33.52           C  
ANISOU 2443  C   VAL A 280     3629   4733   4373    156   -489   -237       C  
ATOM   2444  O   VAL A 280      13.609  22.901  13.071  1.00 38.24           O  
ANISOU 2444  O   VAL A 280     4009   5250   5270    251   -362     83       O  
ATOM   2445  CB  VAL A 280      11.712  25.011  14.317  1.00 30.31           C  
ANISOU 2445  CB  VAL A 280     2631   4778   4106   -432   -470   -369       C  
ATOM   2446  CG1 VAL A 280      12.704  26.134  14.555  1.00 35.49           C  
ANISOU 2446  CG1 VAL A 280     3491   4871   5120   -374    -84    -59       C  
ATOM   2447  CG2 VAL A 280      10.276  25.474  14.607  1.00 36.63           C  
ANISOU 2447  CG2 VAL A 280     3848   5413   4656    750    113    262       C  
TER    2448      VAL A 280                                                      
ATOM   2449  O5'  DG L 101      -8.914  -4.083  -8.580  1.00 42.62           O  
ANISOU 2449  O5'  DG L 101     5306   5157   5731    441   -350   -168       O  
ATOM   2450  C5'  DG L 101      -7.739  -4.746  -8.134  1.00 37.85           C  
ANISOU 2450  C5'  DG L 101     4858   4326   5197    399   -482   -550       C  
ATOM   2451  C4'  DG L 101      -7.016  -3.947  -7.066  1.00 27.74           C  
ANISOU 2451  C4'  DG L 101     3037   3230   4272    795     16   -455       C  
ATOM   2452  O4'  DG L 101      -5.817  -3.359  -7.617  1.00 27.48           O  
ANISOU 2452  O4'  DG L 101     3194   3160   4086   1058    174   -176       O  
ATOM   2453  C3'  DG L 101      -7.780  -2.771  -6.460  1.00 22.23           C  
ANISOU 2453  C3'  DG L 101     1052   3154   4238    157    164   -352       C  
ATOM   2454  O3'  DG L 101      -7.511  -2.767  -5.083  1.00 28.09           O  
ANISOU 2454  O3'  DG L 101     2624   3355   4694   -179   1036   -599       O  
ATOM   2455  C2'  DG L 101      -7.194  -1.560  -7.181  1.00 25.20           C  
ANISOU 2455  C2'  DG L 101     2404   3200   3971    628   -285   -219       C  
ATOM   2456  C1'  DG L 101      -5.753  -1.991  -7.286  1.00 23.90           C  
ANISOU 2456  C1'  DG L 101     1825   3475   3780    584   -439   -216       C  
ATOM   2457  N9   DG L 101      -4.945  -1.324  -8.289  1.00 22.48           N  
ANISOU 2457  N9   DG L 101     1973   2846   3722    616   -390   -266       N  
ATOM   2458  C8   DG L 101      -5.076  -1.364  -9.653  1.00 25.08           C  
ANISOU 2458  C8   DG L 101     2165   3632   3729    842    -90     85       C  
ATOM   2459  N7   DG L 101      -4.128  -0.706 -10.290  1.00 25.43           N  
ANISOU 2459  N7   DG L 101     2316   3458   3888    390   -330     -1       N  
ATOM   2460  C5   DG L 101      -3.310  -0.223  -9.279  1.00 21.99           C  
ANISOU 2460  C5   DG L 101     1501   2810   4044    568    237   -248       C  
ATOM   2461  C6   DG L 101      -2.141   0.564  -9.336  1.00 21.19           C  
ANISOU 2461  C6   DG L 101     2095   2307   3647    667    236      3       C  
ATOM   2462  O6   DG L 101      -1.552   1.009 -10.335  1.00 23.42           O  
ANISOU 2462  O6   DG L 101     2151   2870   3875   1045     20    -31       O  
ATOM   2463  N1   DG L 101      -1.645   0.826  -8.066  1.00 20.46           N  
ANISOU 2463  N1   DG L 101     2173   1911   3690    820    253     69       N  
ATOM   2464  C2   DG L 101      -2.204   0.396  -6.890  1.00 17.89           C  
ANISOU 2464  C2   DG L 101     1235   2027   3536   1077    -44    332       C  
ATOM   2465  N2   DG L 101      -1.565   0.747  -5.760  1.00 19.39           N  
ANISOU 2465  N2   DG L 101     1536   2431   3398    708   -122     -5       N  
ATOM   2466  N3   DG L 101      -3.287  -0.354  -6.822  1.00 21.57           N  
ANISOU 2466  N3   DG L 101     1881   2569   3744    694    195   -369       N  
ATOM   2467  C4   DG L 101      -3.802  -0.601  -8.042  1.00 18.89           C  
ANISOU 2467  C4   DG L 101      945   2787   3445    448    435   -287       C  
ATOM   2468  P    DG L 102      -8.030  -1.600  -4.120  1.00 29.73           P  
ANISOU 2468  P    DG L 102     2803   3335   5155    314   1782   -366       P  
ATOM   2469  OP1  DG L 102      -8.251  -2.193  -2.782  1.00 33.95           O  
ANISOU 2469  OP1  DG L 102     4060   3678   5159   -250    766   -509       O  
ATOM   2470  OP2  DG L 102      -9.087  -0.822  -4.806  1.00 32.04           O  
ANISOU 2470  OP2  DG L 102     2480   3514   6176   -104    392   -384       O  
ATOM   2471  O5'  DG L 102      -6.758  -0.649  -4.056  1.00 22.59           O  
ANISOU 2471  O5'  DG L 102     1865   2453   4265   -145    623   -412       O  
ATOM   2472  C5'  DG L 102      -5.623  -1.078  -3.401  1.00 23.62           C  
ANISOU 2472  C5'  DG L 102     2041   3175   3757   -153    717    -27       C  
ATOM   2473  C4'  DG L 102      -4.940   0.060  -2.672  1.00 22.22           C  
ANISOU 2473  C4'  DG L 102     2466   2713   3262     54    832   -289       C  
ATOM   2474  O4'  DG L 102      -4.172   0.885  -3.598  1.00 22.43           O  
ANISOU 2474  O4'  DG L 102     2003   2906   3611    309    904     16       O  
ATOM   2475  C3'  DG L 102      -5.858   1.029  -1.943  1.00 21.51           C  
ANISOU 2475  C3'  DG L 102     2452   2359   3360    -84    774    -25       C  
ATOM   2476  O3'  DG L 102      -5.160   1.407  -0.757  1.00 22.47           O  
ANISOU 2476  O3'  DG L 102     2788   2302   3445    112    769   -196       O  
ATOM   2477  C2'  DG L 102      -6.061   2.157  -2.966  1.00 18.49           C  
ANISOU 2477  C2'  DG L 102      998   2530   3495    153    440   -172       C  
ATOM   2478  C1'  DG L 102      -4.732   2.190  -3.711  1.00 17.99           C  
ANISOU 2478  C1'  DG L 102     1510   2038   3283    453    320   -101       C  
ATOM   2479  N9   DG L 102      -4.774   2.457  -5.139  1.00 16.52           N  
ANISOU 2479  N9   DG L 102      923   2274   3077    109    401   -167       N  
ATOM   2480  C8   DG L 102      -5.648   1.937  -6.054  1.00 17.91           C  
ANISOU 2480  C8   DG L 102     1366   2342   3096    356    -11     77       C  
ATOM   2481  N7   DG L 102      -5.390   2.288  -7.278  1.00 17.68           N  
ANISOU 2481  N7   DG L 102     1012   2237   3465    437   -223    -44       N  
ATOM   2482  C5   DG L 102      -4.242   3.062  -7.174  1.00 17.95           C  
ANISOU 2482  C5   DG L 102     1823   1825   3172    318     95   -152       C  
ATOM   2483  C6   DG L 102      -3.484   3.707  -8.173  1.00 15.19           C  
ANISOU 2483  C6   DG L 102      627   1882   3259    461   -247     32       C  
ATOM   2484  O6   DG L 102      -3.667   3.714  -9.410  1.00 19.73           O  
ANISOU 2484  O6   DG L 102     1931   2426   3138    334    -81   -108       O  
ATOM   2485  N1   DG L 102      -2.419   4.399  -7.628  1.00 14.80           N  
ANISOU 2485  N1   DG L 102      780   2157   2685    289     72    197       N  
ATOM   2486  C2   DG L 102      -2.114   4.457  -6.302  1.00 17.21           C  
ANISOU 2486  C2   DG L 102     1621   2005   2911    528    -38     54       C  
ATOM   2487  N2   DG L 102      -1.019   5.167  -5.976  1.00 16.60           N  
ANISOU 2487  N2   DG L 102      822   2404   3080    129    427    -22       N  
ATOM   2488  N3   DG L 102      -2.797   3.836  -5.363  1.00 17.90           N  
ANISOU 2488  N3   DG L 102     1665   2178   2956    304    121    -90       N  
ATOM   2489  C4   DG L 102      -3.857   3.173  -5.868  1.00 17.19           C  
ANISOU 2489  C4   DG L 102     1261   2149   3120    426    647   -233       C  
ATOM   2490  P    DT L 103      -5.606   2.579   0.224  1.00 22.66           P  
ANISOU 2490  P    DT L 103     2474   2680   3453     23    806    132       P  
ATOM   2491  OP1  DT L 103      -5.055   2.232   1.549  1.00 26.57           O  
ANISOU 2491  OP1  DT L 103     3403   2699   3991   -341    666    275       O  
ATOM   2492  OP2  DT L 103      -7.051   2.891   0.059  1.00 24.55           O  
ANISOU 2492  OP2  DT L 103     2225   2500   4602    -56    830   -429       O  
ATOM   2493  O5'  DT L 103      -4.830   3.823  -0.323  1.00 19.31           O  
ANISOU 2493  O5'  DT L 103     1739   2365   3229    161    595    -30       O  
ATOM   2494  C5'  DT L 103      -3.421   3.771  -0.384  1.00 17.64           C  
ANISOU 2494  C5'  DT L 103     1219   2534   2949    386    141    165       C  
ATOM   2495  C4'  DT L 103      -2.886   5.054  -0.960  1.00 16.67           C  
ANISOU 2495  C4'  DT L 103     1716   1962   2654    254    -85    -50       C  
ATOM   2496  O4'  DT L 103      -3.324   5.182  -2.316  1.00 17.72           O  
ANISOU 2496  O4'  DT L 103     1651   2528   2552    504     76   -275       O  
ATOM   2497  C3'  DT L 103      -3.347   6.326  -0.243  1.00 16.81           C  
ANISOU 2497  C3'  DT L 103     1631   2362   2392      7    -67     43       C  
ATOM   2498  O3'  DT L 103      -2.169   6.974   0.200  1.00 15.92           O  
ANISOU 2498  O3'  DT L 103     1156   2428   2462    145     -1    103       O  
ATOM   2499  C2'  DT L 103      -4.141   7.109  -1.309  1.00 15.99           C  
ANISOU 2499  C2'  DT L 103     1112   2427   2534    196     17   -296       C  
ATOM   2500  C1'  DT L 103      -3.600   6.546  -2.606  1.00 17.32           C  
ANISOU 2500  C1'  DT L 103     1617   2161   2802     76   -189     54       C  
ATOM   2501  N1   DT L 103      -4.465   6.455  -3.793  1.00 12.86           N  
ANISOU 2501  N1   DT L 103      631   1938   2316     -9     88    -89       N  
ATOM   2502  C2   DT L 103      -3.974   6.895  -5.005  1.00 15.09           C  
ANISOU 2502  C2   DT L 103     1557   1709   2466    506   -318      6       C  
ATOM   2503  O2   DT L 103      -2.931   7.522  -5.115  1.00 14.86           O  
ANISOU 2503  O2   DT L 103      964   2220   2461    151     16    129       O  
ATOM   2504  N3   DT L 103      -4.777   6.642  -6.075  1.00 14.57           N  
ANISOU 2504  N3   DT L 103     1177   1943   2413    151    -36   -122       N  
ATOM   2505  C4   DT L 103      -5.981   5.956  -6.078  1.00 14.67           C  
ANISOU 2505  C4   DT L 103     1304   1736   2534    445    -94     86       C  
ATOM   2506  O4   DT L 103      -6.599   5.772  -7.114  1.00 15.26           O  
ANISOU 2506  O4   DT L 103      962   2243   2593    126   -257    -73       O  
ATOM   2507  C5   DT L 103      -6.454   5.517  -4.773  1.00 13.60           C  
ANISOU 2507  C5   DT L 103      685   2005   2475    338   -302    -52       C  
ATOM   2508  C7   DT L 103      -7.779   4.824  -4.629  1.00 16.28           C  
ANISOU 2508  C7   DT L 103      607   2341   3235   -319     91   -225       C  
ATOM   2509  C6   DT L 103      -5.661   5.758  -3.711  1.00 14.30           C  
ANISOU 2509  C6   DT L 103      923   1943   2567   -118    -27    -82       C  
ATOM   2510  P    DA L 104      -2.188   8.340   1.035  1.00 17.03           P  
ANISOU 2510  P    DA L 104     1625   2542   2300     68   -268    111       P  
ATOM   2511  OP1  DA L 104      -0.900   8.361   1.746  1.00 19.48           O  
ANISOU 2511  OP1  DA L 104     1776   2749   2875   -162   -957    316       O  
ATOM   2512  OP2  DA L 104      -3.433   8.473   1.772  1.00 17.54           O  
ANISOU 2512  OP2  DA L 104     1976   2340   2346    -57    441     21       O  
ATOM   2513  O5'  DA L 104      -2.196   9.446  -0.112  1.00 15.07           O  
ANISOU 2513  O5'  DA L 104     1154   2445   2124    275    157     98       O  
ATOM   2514  C5'  DA L 104      -1.122   9.520  -1.013  1.00 15.06           C  
ANISOU 2514  C5'  DA L 104     1489   2284   1947     42    -59    -63       C  
ATOM   2515  C4'  DA L 104      -1.401  10.633  -2.006  1.00 12.41           C  
ANISOU 2515  C4'  DA L 104      706   1918   2090   -128     -7    -40       C  
ATOM   2516  O4'  DA L 104      -2.397  10.202  -2.960  1.00 13.24           O  
ANISOU 2516  O4'  DA L 104      950   2190   1888    180   -182   -270       O  
ATOM   2517  C3'  DA L 104      -1.947  11.915  -1.376  1.00 11.77           C  
ANISOU 2517  C3'  DA L 104      938   1927   1606     32   -173   -228       C  
ATOM   2518  O3'  DA L 104      -1.326  13.053  -1.965  1.00 12.62           O  
ANISOU 2518  O3'  DA L 104      723   2188   1885     26     -8     14       O  
ATOM   2519  C2'  DA L 104      -3.434  11.830  -1.694  1.00 11.27           C  
ANISOU 2519  C2'  DA L 104      266   2288   1726     45   -136    -99       C  
ATOM   2520  C1'  DA L 104      -3.377  11.203  -3.063  1.00 12.61           C  
ANISOU 2520  C1'  DA L 104      985   1851   1952    158    -39    157       C  
ATOM   2521  N9   DA L 104      -4.590  10.552  -3.515  1.00 11.12           N  
ANISOU 2521  N9   DA L 104      309   2045   1868    147    251   -172       N  
ATOM   2522  C8   DA L 104      -5.602   9.993  -2.782  1.00 12.91           C  
ANISOU 2522  C8   DA L 104      753   2220   1932    228    -49     23       C  
ATOM   2523  N7   DA L 104      -6.531   9.443  -3.517  1.00 12.62           N  
ANISOU 2523  N7   DA L 104      476   2282   2035    415   -173   -180       N  
ATOM   2524  C5   DA L 104      -6.119   9.666  -4.814  1.00 11.82           C  
ANISOU 2524  C5   DA L 104      685   1831   1973    402    100   -220       C  
ATOM   2525  C6   DA L 104      -6.649   9.310  -6.068  1.00 13.17           C  
ANISOU 2525  C6   DA L 104      943   2279   1780    365    124   -249       C  
ATOM   2526  N6   DA L 104      -7.787   8.635  -6.221  1.00 14.74           N  
ANISOU 2526  N6   DA L 104     1029   1951   2621    123   -168    -17       N  
ATOM   2527  N1   DA L 104      -5.947   9.657  -7.159  1.00 12.32           N  
ANISOU 2527  N1   DA L 104      688   1991   2001     54   -101    -99       N  
ATOM   2528  C2   DA L 104      -4.796  10.321  -7.013  1.00 12.26           C  
ANISOU 2528  C2   DA L 104      923   1947   1786    260     23    -65       C  
ATOM   2529  N3   DA L 104      -4.191  10.697  -5.892  1.00 12.49           N  
ANISOU 2529  N3   DA L 104      852   2101   1792    406     87     -5       N  
ATOM   2530  C4   DA L 104      -4.903  10.315  -4.822  1.00 11.88           C  
ANISOU 2530  C4   DA L 104      532   2229   1754    294   -140   -101       C  
ATOM   2531  P    DC L 105      -1.073  14.361  -1.060  1.00 11.87           P  
ANISOU 2531  P    DC L 105      326   2336   1845     80    103    -48       P  
ATOM   2532  OP1  DC L 105      -0.257  13.947   0.100  1.00 12.74           O  
ANISOU 2532  OP1  DC L 105      529   2362   1949     73   -380    -19       O  
ATOM   2533  OP2  DC L 105      -2.367  15.016  -0.826  1.00 11.44           O  
ANISOU 2533  OP2  DC L 105      320   2233   1791    -57    192    -14       O  
ATOM   2534  O5'  DC L 105      -0.122  15.216  -2.026  1.00 12.75           O  
ANISOU 2534  O5'  DC L 105      524   2436   1883    104    138    -87       O  
ATOM   2535  C5'  DC L 105      -0.586  16.359  -2.697  1.00 12.78           C  
ANISOU 2535  C5'  DC L 105      775   2187   1894    313   -195     62       C  
ATOM   2536  C4'  DC L 105      -0.527  16.176  -4.186  1.00 12.59           C  
ANISOU 2536  C4'  DC L 105      633   2270   1879   -297    296    122       C  
ATOM   2537  O4'  DC L 105      -1.392  15.068  -4.574  1.00 12.62           O  
ANISOU 2537  O4'  DC L 105      377   2125   2290    303   -370    122       O  
ATOM   2538  C3'  DC L 105      -1.001  17.362  -4.994  1.00 10.31           C  
ANISOU 2538  C3'  DC L 105      260   1996   1659     80     81    177       C  
ATOM   2539  O3'  DC L 105      -0.364  17.356  -6.273  1.00 11.59           O  
ANISOU 2539  O3'  DC L 105      327   2377   1699    120    129      7       O  
ATOM   2540  C2'  DC L 105      -2.504  17.066  -5.050  1.00 11.28           C  
ANISOU 2540  C2'  DC L 105      259   2114   1911     48     94     94       C  
ATOM   2541  C1'  DC L 105      -2.454  15.575  -5.366  1.00 11.59           C  
ANISOU 2541  C1'  DC L 105      253   2267   1881     25     19     68       C  
ATOM   2542  N1   DC L 105      -3.702  14.864  -5.076  1.00  9.89           N  
ANISOU 2542  N1   DC L 105      255   1986   1516    -15    -54    -92       N  
ATOM   2543  C2   DC L 105      -4.421  14.241  -6.105  1.00 11.45           C  
ANISOU 2543  C2   DC L 105     1013   1818   1518    114    353    -66       C  
ATOM   2544  O2   DC L 105      -3.954  14.246  -7.262  1.00 11.65           O  
ANISOU 2544  O2   DC L 105      579   2165   1683    -67     57   -154       O  
ATOM   2545  N3   DC L 105      -5.600  13.617  -5.799  1.00 10.54           N  
ANISOU 2545  N3   DC L 105      596   1897   1512    -93     -9     63       N  
ATOM   2546  C4   DC L 105      -6.058  13.628  -4.558  1.00 10.20           C  
ANISOU 2546  C4   DC L 105      264   1922   1690    101     79    -53       C  
ATOM   2547  N4   DC L 105      -7.222  13.000  -4.307  1.00 11.53           N  
ANISOU 2547  N4   DC L 105      265   2095   2019     47    140     16       N  
ATOM   2548  C5   DC L 105      -5.377  14.267  -3.503  1.00 11.09           C  
ANISOU 2548  C5   DC L 105      455   2019   1740    320    325     15       C  
ATOM   2549  C6   DC L 105      -4.201  14.861  -3.801  1.00 10.48           C  
ANISOU 2549  C6   DC L 105      570   2119   1292    320     46   -321       C  
ATOM   2550  P    DC L 106      -0.588  18.527  -7.346  1.00 12.18           P  
ANISOU 2550  P    DC L 106      420   2402   1804    171    -39     46       P  
ATOM   2551  OP1  DC L 106       0.666  18.574  -8.149  1.00 12.79           O  
ANISOU 2551  OP1  DC L 106      425   2469   1966    173    528     96       O  
ATOM   2552  OP2  DC L 106      -1.114  19.726  -6.645  1.00 12.11           O  
ANISOU 2552  OP2  DC L 106      388   2450   1762    136   -241    144       O  
ATOM   2553  O5'  DC L 106      -1.862  18.010  -8.203  1.00 11.87           O  
ANISOU 2553  O5'  DC L 106      516   2329   1664    321    -71    -19       O  
ATOM   2554  C5'  DC L 106      -1.681  17.047  -9.249  1.00 12.00           C  
ANISOU 2554  C5'  DC L 106      278   2321   1960    204    -27      9       C  
ATOM   2555  C4'  DC L 106      -2.849  17.110 -10.204  1.00 11.17           C  
ANISOU 2555  C4'  DC L 106      258   2259   1724    -70     61    -62       C  
ATOM   2556  O4'  DC L 106      -4.019  16.572  -9.575  1.00 11.59           O  
ANISOU 2556  O4'  DC L 106      604   1983   1816     25    271   -123       O  
ATOM   2557  C3'  DC L 106      -3.229  18.504 -10.687  1.00 12.17           C  
ANISOU 2557  C3'  DC L 106      559   2086   1978   -124    227    137       C  
ATOM   2558  O3'  DC L 106      -3.459  18.432 -12.084  1.00 12.40           O  
ANISOU 2558  O3'  DC L 106      869   2377   1463    168    104   -175       O  
ATOM   2559  C2'  DC L 106      -4.484  18.861  -9.880  1.00 10.00           C  
ANISOU 2559  C2'  DC L 106      262   1801   1734    103     69    118       C  
ATOM   2560  C1'  DC L 106      -5.109  17.507  -9.681  1.00 10.62           C  
ANISOU 2560  C1'  DC L 106      476   2232   1327    561   -227   -130       C  
ATOM   2561  N1   DC L 106      -5.895  17.301  -8.478  1.00 10.28           N  
ANISOU 2561  N1   DC L 106      467   2029   1409     86     94    -41       N  
ATOM   2562  C2   DC L 106      -7.187  16.737  -8.559  1.00 11.63           C  
ANISOU 2562  C2   DC L 106     1044   1913   1461    -17     -9    -72       C  
ATOM   2563  O2   DC L 106      -7.723  16.584  -9.662  1.00 11.32           O  
ANISOU 2563  O2   DC L 106      411   2219   1670    175   -157   -119       O  
ATOM   2564  N3   DC L 106      -7.823  16.417  -7.417  1.00 10.27           N  
ANISOU 2564  N3   DC L 106      363   2045   1493    114   -143    -19       N  
ATOM   2565  C4   DC L 106      -7.268  16.650  -6.234  1.00  9.12           C  
ANISOU 2565  C4   DC L 106      260   1860   1344     22    -85     76       C  
ATOM   2566  N4   DC L 106      -7.956  16.320  -5.126  1.00 10.59           N  
ANISOU 2566  N4   DC L 106      389   2035   1596    214   -145    -46       N  
ATOM   2567  C5   DC L 106      -5.967  17.226  -6.142  1.00  9.31           C  
ANISOU 2567  C5   DC L 106      314   1971   1249   -105   -229    -72       C  
ATOM   2568  C6   DC L 106      -5.331  17.499  -7.273  1.00 10.24           C  
ANISOU 2568  C6   DC L 106      413   2127   1348     23   -164    -42       C  
ATOM   2569  P    DC L 107      -3.762  19.728 -12.954  1.00 13.70           P  
ANISOU 2569  P    DC L 107     1122   2462   1621     21    112    -33       P  
ATOM   2570  OP1  DC L 107      -3.309  19.390 -14.314  1.00 16.27           O  
ANISOU 2570  OP1  DC L 107     1909   2557   1715    -49    -39     -9       O  
ATOM   2571  OP2  DC L 107      -3.189  20.917 -12.297  1.00 13.71           O  
ANISOU 2571  OP2  DC L 107     1160   2235   1814    209     70    110       O  
ATOM   2572  O5'  DC L 107      -5.354  19.891 -12.891  1.00 12.80           O  
ANISOU 2572  O5'  DC L 107      439   2731   1691    206    -28    -44       O  
ATOM   2573  C5'  DC L 107      -6.193  18.918 -13.504  1.00 13.22           C  
ANISOU 2573  C5'  DC L 107      996   2413   1610     42   -241     49       C  
ATOM   2574  C4'  DC L 107      -7.657  19.208 -13.204  1.00 13.08           C  
ANISOU 2574  C4'  DC L 107     1085   2269   1613   -153   -291    -73       C  
ATOM   2575  O4'  DC L 107      -7.929  18.974 -11.789  1.00 12.60           O  
ANISOU 2575  O4'  DC L 107      929   2052   1806    -27     42     23       O  
ATOM   2576  C3'  DC L 107      -8.104  20.655 -13.446  1.00 12.36           C  
ANISOU 2576  C3'  DC L 107      456   2270   1970    -46   -589     77       C  
ATOM   2577  O3'  DC L 107      -9.382  20.641 -14.047  1.00 13.29           O  
ANISOU 2577  O3'  DC L 107      528   2605   1916   -173   -475     61       O  
ATOM   2578  C2'  DC L 107      -8.242  21.233 -12.049  1.00 12.53           C  
ANISOU 2578  C2'  DC L 107      699   2157   1905    171   -312   -180       C  
ATOM   2579  C1'  DC L 107      -8.753  20.030 -11.317  1.00 13.21           C  
ANISOU 2579  C1'  DC L 107      918   2176   1925    238   -315   -192       C  
ATOM   2580  N1   DC L 107      -8.671  20.017  -9.845  1.00 12.37           N  
ANISOU 2580  N1   DC L 107     1121   2016   1560     41   -227   -141       N  
ATOM   2581  C2   DC L 107      -9.678  19.375  -9.134  1.00 11.75           C  
ANISOU 2581  C2   DC L 107      634   1909   1919    337   -594     81       C  
ATOM   2582  O2   DC L 107     -10.642  18.914  -9.760  1.00 12.83           O  
ANISOU 2582  O2   DC L 107      437   2572   1865   -142   -380    -79       O  
ATOM   2583  N3   DC L 107      -9.604  19.312  -7.789  1.00 11.34           N  
ANISOU 2583  N3   DC L 107      432   2234   1641     28   -459   -168       N  
ATOM   2584  C4   DC L 107      -8.517  19.792  -7.173  1.00  9.43           C  
ANISOU 2584  C4   DC L 107      292   2015   1274    250     38   -165       C  
ATOM   2585  N4   DC L 107      -8.446  19.709  -5.852  1.00 10.34           N  
ANISOU 2585  N4   DC L 107      254   1903   1769     48      4    -74       N  
ATOM   2586  C5   DC L 107      -7.477  20.440  -7.888  1.00 10.26           C  
ANISOU 2586  C5   DC L 107      305   1952   1639    196    181   -162       C  
ATOM   2587  C6   DC L 107      -7.592  20.535  -9.204  1.00 10.73           C  
ANISOU 2587  C6   DC L 107      389   1942   1745    220     37    -26       C  
ATOM   2588  P    DG L 108      -9.745  21.442 -15.381  1.00 13.20           P  
ANISOU 2588  P    DG L 108      626   2712   1678    -17   -258   -107       P  
ATOM   2589  OP1  DG L 108      -8.805  21.053 -16.432  1.00 14.64           O  
ANISOU 2589  OP1  DG L 108      893   2680   1986    -61   -232   -305       O  
ATOM   2590  OP2  DG L 108      -9.892  22.874 -15.087  1.00 13.76           O  
ANISOU 2590  OP2  DG L 108      707   2751   1770   -156   -293    -44       O  
ATOM   2591  O5'  DG L 108     -11.209  20.890 -15.666  1.00 14.16           O  
ANISOU 2591  O5'  DG L 108      613   2849   1916   -214   -426    -59       O  
ATOM   2592  C5'  DG L 108     -11.386  19.491 -15.897  1.00 13.90           C  
ANISOU 2592  C5'  DG L 108      440   2881   1957   -361     95   -278       C  
ATOM   2593  C4'  DG L 108     -12.774  19.049 -15.501  1.00 14.51           C  
ANISOU 2593  C4'  DG L 108      742   2657   2112   -485   -128   -286       C  
ATOM   2594  O4'  DG L 108     -12.919  19.117 -14.059  1.00 15.73           O  
ANISOU 2594  O4'  DG L 108     1391   2758   1827   -415   -195   -239       O  
ATOM   2595  C3'  DG L 108     -13.910  19.888 -16.052  1.00 16.90           C  
ANISOU 2595  C3'  DG L 108     1733   2887   1799   -271   -420   -110       C  
ATOM   2596  O3'  DG L 108     -15.047  19.032 -16.347  1.00 25.37           O  
ANISOU 2596  O3'  DG L 108     2487   4080   3071   -806    311   -582       O  
ATOM   2597  C2'  DG L 108     -14.186  20.912 -14.928  1.00 18.08           C  
ANISOU 2597  C2'  DG L 108     1404   3400   2064   -436     -7    153       C  
ATOM   2598  C1'  DG L 108     -13.903  20.098 -13.679  1.00 15.24           C  
ANISOU 2598  C1'  DG L 108      957   3017   1813    -83   -522   -398       C  
ATOM   2599  N9   DG L 108     -13.320  20.786 -12.532  1.00 13.11           N  
ANISOU 2599  N9   DG L 108      422   2852   1705   -250   -365     36       N  
ATOM   2600  C8   DG L 108     -12.232  21.636 -12.529  1.00 13.64           C  
ANISOU 2600  C8   DG L 108      259   2963   1960   -116     44    -98       C  
ATOM   2601  N7   DG L 108     -11.888  22.025 -11.338  1.00 13.14           N  
ANISOU 2601  N7   DG L 108      952   2305   1733    -55     24     94       N  
ATOM   2602  C5   DG L 108     -12.781  21.354 -10.497  1.00 10.68           C  
ANISOU 2602  C5   DG L 108      319   2254   1485    -34   -284      2       C  
ATOM   2603  C6   DG L 108     -12.852  21.321  -9.098  1.00 11.14           C  
ANISOU 2603  C6   DG L 108      293   2117   1820   -123    242   -361       C  
ATOM   2604  O6   DG L 108     -12.172  21.907  -8.269  1.00 11.28           O  
ANISOU 2604  O6   DG L 108      257   2361   1667     86    -30   -213       O  
ATOM   2605  N1   DG L 108     -13.917  20.505  -8.637  1.00 10.46           N  
ANISOU 2605  N1   DG L 108      261   2270   1441     96    -71   -138       N  
ATOM   2606  C2   DG L 108     -14.747  19.762  -9.442  1.00 12.09           C  
ANISOU 2606  C2   DG L 108      368   2431   1795     90    -83   -150       C  
ATOM   2607  N2   DG L 108     -15.716  19.026  -8.805  1.00 13.44           N  
ANISOU 2607  N2   DG L 108      272   2711   2121   -149   -131   -118       N  
ATOM   2608  N3   DG L 108     -14.666  19.765 -10.767  1.00 12.08           N  
ANISOU 2608  N3   DG L 108      344   2347   1897   -119    -64   -169       N  
ATOM   2609  C4   DG L 108     -13.657  20.566 -11.216  1.00 11.99           C  
ANISOU 2609  C4   DG L 108      303   2617   1634   -204   -198   -161       C  
ATOM   2610  P    DT L 109     -16.349  19.627 -16.930  1.00 36.30           P  
ANISOU 2610  P    DT L 109     3754   5629   4409    280   1155   -194       P  
ATOM   2611  OP1  DT L 109     -17.068  18.468 -17.466  1.00 29.28           O  
ANISOU 2611  OP1  DT L 109     2028   5284   3813  -1333   -914   -699       O  
ATOM   2612  OP2  DT L 109     -16.032  20.787 -17.797  1.00 31.86           O  
ANISOU 2612  OP2  DT L 109     3044   5134   3925   -155   -293    346       O  
ATOM   2613  O5'  DT L 109     -17.172  20.167 -15.678  1.00 30.29           O  
ANISOU 2613  O5'  DT L 109     3435   4458   3615    209    470   -105       O  
ATOM   2614  C5'  DT L 109     -17.742  19.254 -14.757  1.00 23.75           C  
ANISOU 2614  C5'  DT L 109     2190   3360   3473   -857   -529   -439       C  
ATOM   2615  C4'  DT L 109     -18.199  20.004 -13.540  1.00 22.62           C  
ANISOU 2615  C4'  DT L 109     2508   2972   3113   -682     71   -177       C  
ATOM   2616  O4'  DT L 109     -17.084  20.704 -12.941  1.00 18.95           O  
ANISOU 2616  O4'  DT L 109     1561   3004   2636   -615   -504     12       O  
ATOM   2617  C3'  DT L 109     -19.224  21.090 -13.802  1.00 21.55           C  
ANISOU 2617  C3'  DT L 109     2306   2749   3130   -850   -249   -310       C  
ATOM   2618  O3'  DT L 109     -20.553  20.525 -13.558  1.00 23.29           O  
ANISOU 2618  O3'  DT L 109     1672   3424   3750  -1023   -642   -174       O  
ATOM   2619  C2'  DT L 109     -18.814  22.261 -12.865  1.00 22.20           C  
ANISOU 2619  C2'  DT L 109     1504   3455   3475    378   -125   -267       C  
ATOM   2620  C1'  DT L 109     -17.642  21.699 -12.079  1.00 18.59           C  
ANISOU 2620  C1'  DT L 109     1618   2778   2667   -253   -225    -82       C  
ATOM   2621  N1   DT L 109     -16.590  22.661 -11.734  1.00 14.79           N  
ANISOU 2621  N1   DT L 109      708   2776   2136   -288    -99   -128       N  
ATOM   2622  C2   DT L 109     -16.320  22.908 -10.419  1.00 13.92           C  
ANISOU 2622  C2   DT L 109      923   2439   1925   -476   -634   -168       C  
ATOM   2623  O2   DT L 109     -16.927  22.425  -9.483  1.00 13.94           O  
ANISOU 2623  O2   DT L 109      306   2821   2168   -262   -225     30       O  
ATOM   2624  N3   DT L 109     -15.261  23.770 -10.209  1.00 11.49           N  
ANISOU 2624  N3   DT L 109      274   2413   1678     34   -174   -129       N  
ATOM   2625  C4   DT L 109     -14.512  24.392 -11.169  1.00 13.17           C  
ANISOU 2625  C4   DT L 109      987   2334   1682     16   -408   -244       C  
ATOM   2626  O4   DT L 109     -13.595  25.147 -10.854  1.00 12.45           O  
ANISOU 2626  O4   DT L 109      272   2625   1832   -107   -149    -66       O  
ATOM   2627  C5   DT L 109     -14.838  24.079 -12.528  1.00 15.21           C  
ANISOU 2627  C5   DT L 109     1296   2403   2077   -428   -296     21       C  
ATOM   2628  C7   DT L 109     -14.074  24.694 -13.659  1.00 16.31           C  
ANISOU 2628  C7   DT L 109      815   3483   1896   -663   -345    -45       C  
ATOM   2629  C6   DT L 109     -15.843  23.220 -12.742  1.00 15.90           C  
ANISOU 2629  C6   DT L 109     1348   2871   1822   -258   -546   -108       C  
ATOM   2630  P    DG L 110     -21.867  21.322 -13.895  1.00 34.67           P  
ANISOU 2630  P    DG L 110     3227   5140   4804    363    574    120       P  
ATOM   2631  OP1  DG L 110     -22.883  20.314 -14.105  1.00 38.59           O  
ANISOU 2631  OP1  DG L 110     3654   5429   5579    447     92   -264       O  
ATOM   2632  OP2  DG L 110     -21.584  22.337 -14.953  1.00 41.15           O  
ANISOU 2632  OP2  DG L 110     3668   5664   6300    204    599    987       O  
ATOM   2633  O5'  DG L 110     -22.105  22.107 -12.502  1.00 30.56           O  
ANISOU 2633  O5'  DG L 110     3067   3968   4574     66     62    -67       O  
ATOM   2634  C5'  DG L 110     -22.430  21.335 -11.345  1.00 27.54           C  
ANISOU 2634  C5'  DG L 110     2852   3686   3925   -428   -243   -329       C  
ATOM   2635  C4'  DG L 110     -22.556  22.210 -10.119  1.00 23.86           C  
ANISOU 2635  C4'  DG L 110     2127   3355   3581   -216   -559   -245       C  
ATOM   2636  O4'  DG L 110     -21.295  22.884  -9.923  1.00 24.90           O  
ANISOU 2636  O4'  DG L 110     2255   3292   3912   -165   -690    -61       O  
ATOM   2637  C3'  DG L 110     -23.604  23.331 -10.192  1.00 23.69           C  
ANISOU 2637  C3'  DG L 110     1555   3669   3777   -239   -852      1       C  
ATOM   2638  O3'  DG L 110     -24.148  23.603  -8.911  1.00 24.55           O  
ANISOU 2638  O3'  DG L 110     1336   3890   4102   -454   -730   -485       O  
ATOM   2639  C2'  DG L 110     -22.781  24.498 -10.702  1.00 26.24           C  
ANISOU 2639  C2'  DG L 110     2918   3525   3526    128   -854    241       C  
ATOM   2640  C1'  DG L 110     -21.524  24.275  -9.885  1.00 21.68           C  
ANISOU 2640  C1'  DG L 110     1999   3307   2932    277   -602    207       C  
ATOM   2641  N9   DG L 110     -20.334  24.947 -10.375  1.00 19.13           N  
ANISOU 2641  N9   DG L 110     1240   3256   2772   -278   -314   -383       N  
ATOM   2642  C8   DG L 110     -20.013  25.301 -11.659  1.00 20.57           C  
ANISOU 2642  C8   DG L 110      952   3900   2961   -352   -508   -239       C  
ATOM   2643  N7   DG L 110     -18.833  25.878 -11.765  1.00 21.34           N  
ANISOU 2643  N7   DG L 110     1133   3555   3419    -71   -202   -241       N  
ATOM   2644  C5   DG L 110     -18.366  25.943 -10.443  1.00 15.59           C  
ANISOU 2644  C5   DG L 110      756   3190   1975     84   -928   -333       C  
ATOM   2645  C6   DG L 110     -17.175  26.478  -9.901  1.00 16.26           C  
ANISOU 2645  C6   DG L 110     1345   2830   2002    289   -473    199       C  
ATOM   2646  O6   DG L 110     -16.258  27.046 -10.496  1.00 16.55           O  
ANISOU 2646  O6   DG L 110     1556   2606   2124    184   -255   -151       O  
ATOM   2647  N1   DG L 110     -17.139  26.341  -8.515  1.00 14.20           N  
ANISOU 2647  N1   DG L 110      379   2656   2357    199   -180   -123       N  
ATOM   2648  C2   DG L 110     -18.088  25.715  -7.760  1.00 13.30           C  
ANISOU 2648  C2   DG L 110      283   2375   2394    -33   -248   -199       C  
ATOM   2649  N2   DG L 110     -17.879  25.649  -6.435  1.00 15.29           N  
ANISOU 2649  N2   DG L 110      311   2934   2564    258   -315   -459       N  
ATOM   2650  N3   DG L 110     -19.206  25.214  -8.265  1.00 17.34           N  
ANISOU 2650  N3   DG L 110      672   2871   3045    -35   -627   -195       N  
ATOM   2651  C4   DG L 110     -19.272  25.372  -9.592  1.00 17.57           C  
ANISOU 2651  C4   DG L 110      952   3142   2581   -136   -322   -320       C  
ATOM   2652  P    DG L 111     -25.745  23.712  -8.695  1.00 26.06           P  
ANISOU 2652  P    DG L 111     1064   4023   4813   -498   -495   -220       P  
ATOM   2653  OP1  DG L 111     -26.363  22.405  -9.028  1.00 39.22           O  
ANISOU 2653  OP1  DG L 111     4736   4667   5499   -470   -240   -573       O  
ATOM   2654  OP2  DG L 111     -26.217  24.960  -9.360  1.00 30.60           O  
ANISOU 2654  OP2  DG L 111     2499   4647   4480   -639   -549    242       O  
ATOM   2655  O5'  DG L 111     -25.846  23.934  -7.137  1.00 28.73           O  
ANISOU 2655  O5'  DG L 111     1559   4459   4897   -301   -289    149       O  
ATOM   2656  C5'  DG L 111     -25.218  23.018  -6.286  1.00 26.33           C  
ANISOU 2656  C5'  DG L 111     1886   3546   4569     81   -470   -245       C  
ATOM   2657  C4'  DG L 111     -24.634  23.726  -5.100  1.00 27.76           C  
ANISOU 2657  C4'  DG L 111     2411   3541   4595   -426   -396   -232       C  
ATOM   2658  O4'  DG L 111     -23.433  24.459  -5.493  1.00 27.06           O  
ANISOU 2658  O4'  DG L 111     1920   3195   5167    -51   -445    144       O  
ATOM   2659  C3'  DG L 111     -25.561  24.748  -4.474  1.00 27.07           C  
ANISOU 2659  C3'  DG L 111     1908   3674   4701   -556   -544   -218       C  
ATOM   2660  O3'  DG L 111     -25.372  24.694  -3.098  1.00 31.01           O  
ANISOU 2660  O3'  DG L 111     2710   4383   4689   -367   -471   -228       O  
ATOM   2661  C2'  DG L 111     -25.117  26.065  -5.099  1.00 25.00           C  
ANISOU 2661  C2'  DG L 111     1448   3461   4589    -17   -491    -80       C  
ATOM   2662  C1'  DG L 111     -23.623  25.855  -5.266  1.00 23.90           C  
ANISOU 2662  C1'  DG L 111     1840   3249   3989    132   -549   -300       C  
ATOM   2663  N9   DG L 111     -23.020  26.543  -6.389  1.00 25.00           N  
ANISOU 2663  N9   DG L 111     2277   3057   4163    -22   -517   -320       N  
ATOM   2664  C8   DG L 111     -23.457  26.591  -7.692  1.00 22.86           C  
ANISOU 2664  C8   DG L 111     1320   3458   3908    -54   -674   -253       C  
ATOM   2665  N7   DG L 111     -22.669  27.258  -8.488  1.00 22.75           N  
ANISOU 2665  N7   DG L 111     1437   3322   3884    351  -1498    -17       N  
ATOM   2666  C5   DG L 111     -21.601  27.629  -7.659  1.00 18.92           C  
ANISOU 2666  C5   DG L 111     1270   2887   3029    614   -961    -42       C  
ATOM   2667  C6   DG L 111     -20.447  28.384  -7.941  1.00 21.05           C  
ANISOU 2667  C6   DG L 111     2208   2577   3211    537   -879     76       C  
ATOM   2668  O6   DG L 111     -20.072  28.848  -9.015  1.00 22.94           O  
ANISOU 2668  O6   DG L 111     2530   3010   3175    347  -1132   -189       O  
ATOM   2669  N1   DG L 111     -19.667  28.567  -6.801  1.00 18.65           N  
ANISOU 2669  N1   DG L 111     1307   2478   3300    787   -737   -143       N  
ATOM   2670  C2   DG L 111     -19.964  28.081  -5.567  1.00 20.69           C  
ANISOU 2670  C2   DG L 111     1863   2623   3374    807   -151      2       C  
ATOM   2671  N2   DG L 111     -19.096  28.356  -4.605  1.00 20.04           N  
ANISOU 2671  N2   DG L 111      714   2970   3929    321  -1287   -441       N  
ATOM   2672  N3   DG L 111     -21.038  27.374  -5.278  1.00 21.07           N  
ANISOU 2672  N3   DG L 111     1525   2614   3867    292   -459   -389       N  
ATOM   2673  C4   DG L 111     -21.816  27.196  -6.372  1.00 21.48           C  
ANISOU 2673  C4   DG L 111     1732   2737   3690    221   -528   -214       C  
ATOM   2674  P    DA L 112     -26.179  25.607  -2.094  1.00 34.72           P  
ANISOU 2674  P    DA L 112     2328   5051   5811   -263    241    123       P  
ATOM   2675  OP1  DA L 112     -26.272  24.850  -0.823  1.00 35.44           O  
ANISOU 2675  OP1  DA L 112     3130   4724   5611   -681   -338    263       O  
ATOM   2676  OP2  DA L 112     -27.401  26.142  -2.745  1.00 41.72           O  
ANISOU 2676  OP2  DA L 112     3234   6113   6502    477   -428     93       O  
ATOM   2677  O5'  DA L 112     -25.191  26.815  -1.884  1.00 29.27           O  
ANISOU 2677  O5'  DA L 112     1479   4055   5584    343     18     64       O  
ATOM   2678  C5'  DA L 112     -23.973  26.559  -1.222  1.00 26.64           C  
ANISOU 2678  C5'  DA L 112     2247   3333   4541    799    -14     62       C  
ATOM   2679  C4'  DA L 112     -23.203  27.841  -1.042  1.00 26.96           C  
ANISOU 2679  C4'  DA L 112     2269   3245   4727     93    319   -182       C  
ATOM   2680  O4'  DA L 112     -22.802  28.332  -2.344  1.00 28.94           O  
ANISOU 2680  O4'  DA L 112     2800   2941   5253    875    175   -173       O  
ATOM   2681  C3'  DA L 112     -23.981  28.971  -0.371  1.00 31.11           C  
ANISOU 2681  C3'  DA L 112     3631   3889   4300    160    328   -326       C  
ATOM   2682  O3'  DA L 112     -23.261  29.452   0.752  1.00 37.08           O  
ANISOU 2682  O3'  DA L 112     4537   4089   5461     24    474  -1125       O  
ATOM   2683  C2'  DA L 112     -24.142  30.023  -1.467  1.00 31.51           C  
ANISOU 2683  C2'  DA L 112     3485   3577   4908    409    691   -211       C  
ATOM   2684  C1'  DA L 112     -22.993  29.721  -2.412  1.00 27.05           C  
ANISOU 2684  C1'  DA L 112     2208   3147   4922    191    -26    -27       C  
ATOM   2685  N9   DA L 112     -23.225  30.003  -3.811  1.00 24.93           N  
ANISOU 2685  N9   DA L 112     2316   2689   4466    157    -78   -270       N  
ATOM   2686  C8   DA L 112     -24.316  29.646  -4.551  1.00 28.32           C  
ANISOU 2686  C8   DA L 112     2973   2528   5257   -238   -298    183       C  
ATOM   2687  N7   DA L 112     -24.225  29.964  -5.820  1.00 24.29           N  
ANISOU 2687  N7   DA L 112     1582   2242   5405    346    -77    227       N  
ATOM   2688  C5   DA L 112     -22.964  30.558  -5.918  1.00 21.46           C  
ANISOU 2688  C5   DA L 112     1358   2176   4616    436   -798   -185       C  
ATOM   2689  C6   DA L 112     -22.270  31.130  -7.001  1.00 22.98           C  
ANISOU 2689  C6   DA L 112     1452   3087   4192    555   -879   -345       C  
ATOM   2690  N6   DA L 112     -22.772  31.171  -8.246  1.00 25.59           N  
ANISOU 2690  N6   DA L 112     2059   2891   4771    -95  -1257   -332       N  
ATOM   2691  N1   DA L 112     -21.034  31.636  -6.763  1.00 22.89           N  
ANISOU 2691  N1   DA L 112     1586   2472   4639    507   -295   -267       N  
ATOM   2692  C2   DA L 112     -20.557  31.582  -5.511  1.00 19.42           C  
ANISOU 2692  C2   DA L 112      992   2705   3681    848    -36    -43       C  
ATOM   2693  N3   DA L 112     -21.124  31.080  -4.419  1.00 20.18           N  
ANISOU 2693  N3   DA L 112     1198   2620   3848    279    231   -131       N  
ATOM   2694  C4   DA L 112     -22.337  30.578  -4.694  1.00 23.54           C  
ANISOU 2694  C4   DA L 112     2174   2398   4371    417   -138   -208       C  
TER    2695       DA L 112                                                      
ATOM   2696  O5'  DT M 201     -16.033  36.659 -12.055  1.00 30.24           O  
ANISOU 2696  O5'  DT M 201     2113   4597   4777    739    573    557       O  
ATOM   2697  C5'  DT M 201     -16.126  37.792 -11.180  1.00 29.09           C  
ANISOU 2697  C5'  DT M 201     2419   4809   3822    106   -383    534       C  
ATOM   2698  C4'  DT M 201     -15.963  37.383  -9.728  1.00 24.09           C  
ANISOU 2698  C4'  DT M 201     1827   3793   3531    176   -365    560       C  
ATOM   2699  O4'  DT M 201     -17.104  36.606  -9.277  1.00 21.85           O  
ANISOU 2699  O4'  DT M 201     1561   3525   3215     74     67    444       O  
ATOM   2700  C3'  DT M 201     -14.769  36.506  -9.460  1.00 21.93           C  
ANISOU 2700  C3'  DT M 201     1219   3877   3235    695    -21    216       C  
ATOM   2701  O3'  DT M 201     -14.219  36.849  -8.206  1.00 24.99           O  
ANISOU 2701  O3'  DT M 201     2035   4454   3006     -4   -352    180       O  
ATOM   2702  C2'  DT M 201     -15.353  35.093  -9.511  1.00 23.37           C  
ANISOU 2702  C2'  DT M 201     1564   3765   3551    709    -12    254       C  
ATOM   2703  C1'  DT M 201     -16.698  35.301  -8.879  1.00 20.97           C  
ANISOU 2703  C1'  DT M 201     1658   3179   3130    405   -179    450       C  
ATOM   2704  N1   DT M 201     -17.769  34.362  -9.291  1.00 20.80           N  
ANISOU 2704  N1   DT M 201     2072   2984   2847    519   -392   -138       N  
ATOM   2705  C2   DT M 201     -18.520  33.727  -8.325  1.00 19.68           C  
ANISOU 2705  C2   DT M 201     1525   2895   3057    611   -454    218       C  
ATOM   2706  O2   DT M 201     -18.322  33.840  -7.139  1.00 18.48           O  
ANISOU 2706  O2   DT M 201     1263   3122   2634    142   -413    -88       O  
ATOM   2707  N3   DT M 201     -19.531  32.935  -8.806  1.00 19.91           N  
ANISOU 2707  N3   DT M 201     1779   2614   3170    787   -268   -576       N  
ATOM   2708  C4   DT M 201     -19.874  32.724 -10.124  1.00 22.91           C  
ANISOU 2708  C4   DT M 201     2410   2676   3616    546   -509   -478       C  
ATOM   2709  O4   DT M 201     -20.826  32.004 -10.443  1.00 26.77           O  
ANISOU 2709  O4   DT M 201     2851   3422   3899    116  -1281   -142       O  
ATOM   2710  C5   DT M 201     -19.062  33.435 -11.088  1.00 23.96           C  
ANISOU 2710  C5   DT M 201     2626   3052   3424    515   -304   -309       C  
ATOM   2711  C7   DT M 201     -19.347  33.320 -12.557  1.00 33.32           C  
ANISOU 2711  C7   DT M 201     4423   4691   3544    131   -541   -241       C  
ATOM   2712  C6   DT M 201     -18.064  34.215 -10.629  1.00 23.09           C  
ANISOU 2712  C6   DT M 201     2595   3199   2977    581   -186   -145       C  
ATOM   2713  P    DC M 202     -12.787  36.341  -7.725  1.00 23.26           P  
ANISOU 2713  P    DC M 202     1368   4554   2912    348   -252   -187       P  
ATOM   2714  OP1  DC M 202     -12.086  37.492  -7.150  1.00 29.15           O  
ANISOU 2714  OP1  DC M 202     3395   3841   3838   -192   -292    301       O  
ATOM   2715  OP2  DC M 202     -12.108  35.538  -8.767  1.00 27.15           O  
ANISOU 2715  OP2  DC M 202     1629   5310   3374    220   -304   -655       O  
ATOM   2716  O5'  DC M 202     -13.150  35.342  -6.555  1.00 22.71           O  
ANISOU 2716  O5'  DC M 202     2115   4174   2337    968    -18    422       O  
ATOM   2717  C5'  DC M 202     -13.910  35.781  -5.487  1.00 19.49           C  
ANISOU 2717  C5'  DC M 202     1523   3486   2394   1113    216    -17       C  
ATOM   2718  C4'  DC M 202     -14.318  34.596  -4.677  1.00 16.18           C  
ANISOU 2718  C4'  DC M 202     1378   2480   2290    692   -273     -9       C  
ATOM   2719  O4'  DC M 202     -15.251  33.800  -5.423  1.00 22.01           O  
ANISOU 2719  O4'  DC M 202     1697   3547   3119    566   -399   -728       O  
ATOM   2720  C3'  DC M 202     -13.167  33.672  -4.307  1.00 15.24           C  
ANISOU 2720  C3'  DC M 202      602   2621   2565    587    -33    331       C  
ATOM   2721  O3'  DC M 202     -13.145  33.606  -2.894  1.00 15.02           O  
ANISOU 2721  O3'  DC M 202      668   2689   2348    339   -234     45       O  
ATOM   2722  C2'  DC M 202     -13.497  32.347  -5.005  1.00 15.20           C  
ANISOU 2722  C2'  DC M 202      733   2790   2250    572   -397   -181       C  
ATOM   2723  C1'  DC M 202     -15.008  32.429  -5.181  1.00 18.87           C  
ANISOU 2723  C1'  DC M 202     1501   2734   2932    265   -404   -281       C  
ATOM   2724  N1   DC M 202     -15.623  31.722  -6.335  1.00 17.02           N  
ANISOU 2724  N1   DC M 202      560   2897   3009    787   -504   -207       N  
ATOM   2725  C2   DC M 202     -16.724  30.882  -6.125  1.00 17.96           C  
ANISOU 2725  C2   DC M 202     1657   3108   2059    455   -435    223       C  
ATOM   2726  O2   DC M 202     -17.111  30.663  -4.985  1.00 18.96           O  
ANISOU 2726  O2   DC M 202     1300   3297   2607    433   -502    -51       O  
ATOM   2727  N3   DC M 202     -17.330  30.319  -7.201  1.00 18.93           N  
ANISOU 2727  N3   DC M 202     1799   2920   2473    733   -715   -196       N  
ATOM   2728  C4   DC M 202     -16.889  30.575  -8.429  1.00 17.00           C  
ANISOU 2728  C4   DC M 202     1543   2559   2354    663   -463   -188       C  
ATOM   2729  N4   DC M 202     -17.547  30.004  -9.463  1.00 20.77           N  
ANISOU 2729  N4   DC M 202     1909   3097   2884    668   -751   -440       N  
ATOM   2730  C5   DC M 202     -15.782  31.441  -8.666  1.00 17.15           C  
ANISOU 2730  C5   DC M 202     1215   2846   2453    541   -295   -250       C  
ATOM   2731  C6   DC M 202     -15.197  32.003  -7.594  1.00 17.49           C  
ANISOU 2731  C6   DC M 202      914   3173   2557    961   -678   -174       C  
ATOM   2732  P    DC M 203     -11.969  32.924  -2.099  1.00 13.89           P  
ANISOU 2732  P    DC M 203      387   2659   2232    221   -120    -89       P  
ATOM   2733  OP1  DC M 203     -12.107  33.431  -0.714  1.00 16.44           O  
ANISOU 2733  OP1  DC M 203     1191   2667   2388    302   -581   -213       O  
ATOM   2734  OP2  DC M 203     -10.713  33.048  -2.836  1.00 13.78           O  
ANISOU 2734  OP2  DC M 203      258   2491   2483    -81    -75      3       O  
ATOM   2735  O5'  DC M 203     -12.340  31.370  -2.120  1.00 13.20           O  
ANISOU 2735  O5'  DC M 203      331   2637   2045    198    334     34       O  
ATOM   2736  C5'  DC M 203     -13.501  30.906  -1.446  1.00 13.36           C  
ANISOU 2736  C5'  DC M 203      426   2905   1742    424    394     -8       C  
ATOM   2737  C4'  DC M 203     -13.795  29.478  -1.821  1.00 14.72           C  
ANISOU 2737  C4'  DC M 203      755   2993   1844     44    528   -238       C  
ATOM   2738  O4'  DC M 203     -14.254  29.411  -3.184  1.00 13.24           O  
ANISOU 2738  O4'  DC M 203      345   3023   1661    229    308   -138       O  
ATOM   2739  C3'  DC M 203     -12.571  28.570  -1.778  1.00 13.79           C  
ANISOU 2739  C3'  DC M 203      476   2868   1895   -122     82    225       C  
ATOM   2740  O3'  DC M 203     -12.846  27.312  -1.193  1.00 19.25           O  
ANISOU 2740  O3'  DC M 203      592   3597   3123   -737   -809    486       O  
ATOM   2741  C2'  DC M 203     -12.224  28.389  -3.254  1.00 15.91           C  
ANISOU 2741  C2'  DC M 203      898   2876   2269   -157   -567    256       C  
ATOM   2742  C1'  DC M 203     -13.629  28.303  -3.789  1.00 15.35           C  
ANISOU 2742  C1'  DC M 203     1029   2542   2259   -184   -135   -449       C  
ATOM   2743  N1   DC M 203     -13.764  28.392  -5.223  1.00 12.82           N  
ANISOU 2743  N1   DC M 203      422   2716   1729    542     54   -415       N  
ATOM   2744  C2   DC M 203     -14.788  27.678  -5.878  1.00 14.20           C  
ANISOU 2744  C2   DC M 203     1196   1967   2231    434    -31   -519       C  
ATOM   2745  O2   DC M 203     -15.636  27.020  -5.211  1.00 13.66           O  
ANISOU 2745  O2   DC M 203      419   2587   2184    161   -558   -207       O  
ATOM   2746  N3   DC M 203     -14.857  27.766  -7.220  1.00 12.97           N  
ANISOU 2746  N3   DC M 203      442   2538   1945    531    -36   -367       N  
ATOM   2747  C4   DC M 203     -13.976  28.490  -7.902  1.00 12.94           C  
ANISOU 2747  C4   DC M 203      449   2553   1914    264    233   -244       C  
ATOM   2748  N4   DC M 203     -14.099  28.549  -9.219  1.00 14.69           N  
ANISOU 2748  N4   DC M 203      462   2886   2232    346    185   -403       N  
ATOM   2749  C5   DC M 203     -12.931  29.186  -7.249  1.00 14.52           C  
ANISOU 2749  C5   DC M 203      474   2815   2225    475   -104   -463       C  
ATOM   2750  C6   DC M 203     -12.839  29.081  -5.935  1.00 14.61           C  
ANISOU 2750  C6   DC M 203      416   3041   2092    566    266   -142       C  
ATOM   2751  P    DA M 204     -12.552  26.957   0.340  1.00 12.15           P  
ANISOU 2751  P    DA M 204      323   2408   1883    212   -174    -44       P  
ATOM   2752  OP1  DA M 204     -13.365  27.789   1.153  1.00 19.89           O  
ANISOU 2752  OP1  DA M 204      263   2969   4322    -56    204  -1580       O  
ATOM   2753  OP2  DA M 204     -11.074  26.926   0.485  1.00 11.46           O  
ANISOU 2753  OP2  DA M 204      282   2330   1740     67    194   -133       O  
ATOM   2754  O5'  DA M 204     -13.108  25.513   0.275  1.00 12.34           O  
ANISOU 2754  O5'  DA M 204      303   2194   2190    -65    311   -224       O  
ATOM   2755  C5'  DA M 204     -14.545  25.328   0.381  1.00 11.91           C  
ANISOU 2755  C5'  DA M 204      338   2187   2001     42    383     42       C  
ATOM   2756  C4'  DA M 204     -14.953  24.115  -0.415  1.00 12.00           C  
ANISOU 2756  C4'  DA M 204      269   2073   2218    162     80    356       C  
ATOM   2757  O4'  DA M 204     -14.896  24.382  -1.837  1.00 11.51           O  
ANISOU 2757  O4'  DA M 204      268   2250   1855    162     56     17       O  
ATOM   2758  C3'  DA M 204     -14.073  22.871  -0.197  1.00 10.78           C  
ANISOU 2758  C3'  DA M 204      277   2216   1603    -28   -179    137       C  
ATOM   2759  O3'  DA M 204     -14.909  21.728  -0.229  1.00 11.67           O  
ANISOU 2759  O3'  DA M 204      268   2130   2037   -133    116   -281       O  
ATOM   2760  C2'  DA M 204     -13.170  22.905  -1.415  1.00 10.61           C  
ANISOU 2760  C2'  DA M 204      275   2042   1715     12    178    -18       C  
ATOM   2761  C1'  DA M 204     -14.137  23.364  -2.487  1.00 10.15           C  
ANISOU 2761  C1'  DA M 204      254   1969   1631      5    -39      7       C  
ATOM   2762  N9   DA M 204     -13.538  23.914  -3.674  1.00 10.13           N  
ANISOU 2762  N9   DA M 204      324   1956   1568   -298    168    -71       N  
ATOM   2763  C8   DA M 204     -12.370  24.645  -3.772  1.00 10.30           C  
ANISOU 2763  C8   DA M 204      278   1950   1683    -71   -175    -21       C  
ATOM   2764  N7   DA M 204     -12.106  25.044  -4.987  1.00 10.79           N  
ANISOU 2764  N7   DA M 204      273   2170   1655    -12   -164   -221       N  
ATOM   2765  C5   DA M 204     -13.150  24.560  -5.763  1.00 10.24           C  
ANISOU 2765  C5   DA M 204      547   1921   1423    190    329   -104       C  
ATOM   2766  C6   DA M 204     -13.441  24.634  -7.118  1.00 10.19           C  
ANISOU 2766  C6   DA M 204      370   2280   1220     22   -337   -132       C  
ATOM   2767  N6   DA M 204     -12.729  25.269  -8.045  1.00 10.77           N  
ANISOU 2767  N6   DA M 204      318   2353   1419    348    107     77       N  
ATOM   2768  N1   DA M 204     -14.602  24.036  -7.533  1.00 11.01           N  
ANISOU 2768  N1   DA M 204      288   2291   1605     -7   -213   -259       N  
ATOM   2769  C2   DA M 204     -15.364  23.377  -6.622  1.00 11.32           C  
ANISOU 2769  C2   DA M 204      322   2218   1760    358     40   -198       C  
ATOM   2770  N3   DA M 204     -15.202  23.255  -5.331  1.00 11.09           N  
ANISOU 2770  N3   DA M 204      255   2222   1736    -70      0   -231       N  
ATOM   2771  C4   DA M 204     -14.035  23.866  -4.949  1.00  9.85           C  
ANISOU 2771  C4   DA M 204      284   2193   1265    243     20     -3       C  
ATOM   2772  P    DC M 205     -14.540  20.383   0.532  1.00 11.92           P  
ANISOU 2772  P    DC M 205      269   2370   1890    -47    158   -116       P  
ATOM   2773  OP1  DC M 205     -14.701  20.569   1.970  1.00 12.59           O  
ANISOU 2773  OP1  DC M 205      326   2370   2085   -309    254   -200       O  
ATOM   2774  OP2  DC M 205     -13.225  19.874   0.083  1.00 12.16           O  
ANISOU 2774  OP2  DC M 205      271   2358   1991    -93    161   -166       O  
ATOM   2775  O5'  DC M 205     -15.687  19.431  -0.070  1.00 12.33           O  
ANISOU 2775  O5'  DC M 205      365   2294   2024   -202   -327    -93       O  
ATOM   2776  C5'  DC M 205     -17.061  19.865  -0.212  1.00 12.15           C  
ANISOU 2776  C5'  DC M 205      331   2261   2024    382     97      6       C  
ATOM   2777  C4'  DC M 205     -17.622  19.101  -1.373  1.00 13.42           C  
ANISOU 2777  C4'  DC M 205      264   2597   2236   -160    -19   -159       C  
ATOM   2778  O4'  DC M 205     -17.027  19.609  -2.619  1.00 13.11           O  
ANISOU 2778  O4'  DC M 205      275   2534   2170   -160    154   -114       O  
ATOM   2779  C3'  DC M 205     -17.293  17.610  -1.328  1.00 11.04           C  
ANISOU 2779  C3'  DC M 205      327   2088   1778   -254   -233    -63       C  
ATOM   2780  O3'  DC M 205     -18.498  16.890  -1.662  1.00 13.44           O  
ANISOU 2780  O3'  DC M 205      348   2628   2131   -321   -267   -310       O  
ATOM   2781  C2'  DC M 205     -16.241  17.388  -2.387  1.00 12.58           C  
ANISOU 2781  C2'  DC M 205      496   2255   2027   -305    247    -64       C  
ATOM   2782  C1'  DC M 205     -16.435  18.538  -3.344  1.00 12.76           C  
ANISOU 2782  C1'  DC M 205      275   2497   2076   -123    182   -320       C  
ATOM   2783  N1   DC M 205     -15.170  19.132  -3.915  1.00 10.68           N  
ANISOU 2783  N1   DC M 205      255   2243   1556     43    -47    -35       N  
ATOM   2784  C2   DC M 205     -15.145  19.461  -5.260  1.00 11.74           C  
ANISOU 2784  C2   DC M 205      433   2332   1695    386    435    235       C  
ATOM   2785  O2   DC M 205     -16.102  19.154  -5.999  1.00 13.95           O  
ANISOU 2785  O2   DC M 205      510   3002   1786    138   -383     11       O  
ATOM   2786  N3   DC M 205     -14.039  20.072  -5.788  1.00 10.60           N  
ANISOU 2786  N3   DC M 205      263   2506   1256    149     21     23       N  
ATOM   2787  C4   DC M 205     -13.057  20.408  -4.969  1.00  9.45           C  
ANISOU 2787  C4   DC M 205      290   2075   1225    235    -64    144       C  
ATOM   2788  N4   DC M 205     -11.994  21.039  -5.506  1.00 10.55           N  
ANISOU 2788  N4   DC M 205      318   2033   1655    -35    300    -20       N  
ATOM   2789  C5   DC M 205     -13.062  20.088  -3.608  1.00 11.00           C  
ANISOU 2789  C5   DC M 205      424   1817   1936    198    493    -17       C  
ATOM   2790  C6   DC M 205     -14.137  19.490  -3.096  1.00 10.73           C  
ANISOU 2790  C6   DC M 205      321   2450   1303     62     36    -34       C  
ATOM   2791  P    DG M 206     -18.665  15.323  -1.351  1.00 14.41           P  
ANISOU 2791  P    DG M 206      369   2710   2396   -380     14   -228       P  
ATOM   2792  OP1  DG M 206     -20.151  15.050  -1.398  1.00 16.59           O  
ANISOU 2792  OP1  DG M 206      506   3060   2738   -551     40   -212       O  
ATOM   2793  OP2  DG M 206     -17.897  14.945  -0.154  1.00 13.77           O  
ANISOU 2793  OP2  DG M 206      312   2583   2333   -293   -192   -190       O  
ATOM   2794  O5'  DG M 206     -17.927  14.636  -2.602  1.00 15.13           O  
ANISOU 2794  O5'  DG M 206      563   2826   2357   -437    -18   -390       O  
ATOM   2795  C5'  DG M 206     -18.452  14.786  -3.889  1.00 13.66           C  
ANISOU 2795  C5'  DG M 206      548   2210   2430   -427     25   -453       C  
ATOM   2796  C4'  DG M 206     -17.482  14.285  -4.897  1.00 13.61           C  
ANISOU 2796  C4'  DG M 206      631   2401   2137   -319     25   -269       C  
ATOM   2797  O4'  DG M 206     -16.364  15.215  -4.913  1.00 13.26           O  
ANISOU 2797  O4'  DG M 206      378   2403   2258    -74   -212   -191       O  
ATOM   2798  C3'  DG M 206     -16.852  12.910  -4.627  1.00 14.03           C  
ANISOU 2798  C3'  DG M 206      653   2348   2328   -374     -6    -27       C  
ATOM   2799  O3'  DG M 206     -16.654  12.247  -5.854  1.00 15.53           O  
ANISOU 2799  O3'  DG M 206      735   2584   2582   -179   -118   -525       O  
ATOM   2800  C2'  DG M 206     -15.505  13.264  -4.029  1.00 13.24           C  
ANISOU 2800  C2'  DG M 206      270   2464   2294   -166    -71   -280       C  
ATOM   2801  C1'  DG M 206     -15.159  14.484  -4.883  1.00 12.92           C  
ANISOU 2801  C1'  DG M 206      414   2472   2022   -307   -397   -375       C  
ATOM   2802  N9   DG M 206     -14.069  15.323  -4.418  1.00 11.75           N  
ANISOU 2802  N9   DG M 206      265   2439   1761   -125     68   -123       N  
ATOM   2803  C8   DG M 206     -13.579  15.443  -3.160  1.00 12.00           C  
ANISOU 2803  C8   DG M 206      505   2137   1917    -34    -76    -86       C  
ATOM   2804  N7   DG M 206     -12.550  16.268  -3.090  1.00 11.38           N  
ANISOU 2804  N7   DG M 206      263   2085   1976     70   -120   -229       N  
ATOM   2805  C5   DG M 206     -12.373  16.706  -4.390  1.00 11.08           C  
ANISOU 2805  C5   DG M 206      311   2339   1558    297   -142      7       C  
ATOM   2806  C6   DG M 206     -11.418  17.581  -4.957  1.00 11.20           C  
ANISOU 2806  C6   DG M 206      340   2252   1661    187    276   -333       C  
ATOM   2807  O6   DG M 206     -10.505  18.170  -4.346  1.00 11.30           O  
ANISOU 2807  O6   DG M 206      281   2186   1823     23   -210    -52       O  
ATOM   2808  N1   DG M 206     -11.587  17.729  -6.318  1.00 10.60           N  
ANISOU 2808  N1   DG M 206      261   2058   1705    121    -24    -95       N  
ATOM   2809  C2   DG M 206     -12.577  17.130  -7.067  1.00 10.78           C  
ANISOU 2809  C2   DG M 206      257   1997   1839     26    -79   -256       C  
ATOM   2810  N2   DG M 206     -12.587  17.425  -8.366  1.00 12.00           N  
ANISOU 2810  N2   DG M 206      325   2261   1971    100   -344    -91       N  
ATOM   2811  N3   DG M 206     -13.472  16.301  -6.545  1.00 11.58           N  
ANISOU 2811  N3   DG M 206      405   2172   1822    119    122   -168       N  
ATOM   2812  C4   DG M 206     -13.302  16.125  -5.221  1.00 11.53           C  
ANISOU 2812  C4   DG M 206      279   2245   1857    172    116   -184       C  
ATOM   2813  P    DG M 207     -17.114  10.735  -6.060  1.00 17.94           P  
ANISOU 2813  P    DG M 207     1064   3002   2747   -316   -112   -445       P  
ATOM   2814  OP1  DG M 207     -18.556  10.612  -5.813  1.00 20.66           O  
ANISOU 2814  OP1  DG M 207      955   3828   3067   -426    258   -361       O  
ATOM   2815  OP2  DG M 207     -16.108   9.889  -5.343  1.00 21.13           O  
ANISOU 2815  OP2  DG M 207     1498   3179   3351   -315    174     27       O  
ATOM   2816  O5'  DG M 207     -16.821  10.577  -7.627  1.00 18.19           O  
ANISOU 2816  O5'  DG M 207     1403   2708   2798   -737   -431   -467       O  
ATOM   2817  C5'  DG M 207     -17.469  11.402  -8.561  1.00 17.56           C  
ANISOU 2817  C5'  DG M 207     1263   3162   2246   -535   -275   -536       C  
ATOM   2818  C4'  DG M 207     -16.528  11.875  -9.650  1.00 17.71           C  
ANISOU 2818  C4'  DG M 207      967   3202   2559   -572   -419   -331       C  
ATOM   2819  O4'  DG M 207     -15.515  12.734  -9.067  1.00 15.26           O  
ANISOU 2819  O4'  DG M 207      300   3042   2453    -82   -303   -302       O  
ATOM   2820  C3'  DG M 207     -15.737  10.796 -10.397  1.00 17.40           C  
ANISOU 2820  C3'  DG M 207     1042   2892   2677   -768   -794   -364       C  
ATOM   2821  O3'  DG M 207     -15.549  11.226 -11.729  1.00 19.37           O  
ANISOU 2821  O3'  DG M 207     1168   3839   2350   -675   -464   -492       O  
ATOM   2822  C2'  DG M 207     -14.429  10.733  -9.621  1.00 16.49           C  
ANISOU 2822  C2'  DG M 207     1255   2471   2539   -370   -266   -320       C  
ATOM   2823  C1'  DG M 207     -14.211  12.197  -9.314  1.00 13.39           C  
ANISOU 2823  C1'  DG M 207      478   2768   1839     -1   -135     17       C  
ATOM   2824  N9   DG M 207     -13.386  12.478  -8.163  1.00 12.25           N  
ANISOU 2824  N9   DG M 207      473   2300   1878   -255    -12    -92       N  
ATOM   2825  C8   DG M 207     -13.495  12.010  -6.899  1.00 12.97           C  
ANISOU 2825  C8   DG M 207      372   2627   1925   -106    -27   -255       C  
ATOM   2826  N7   DG M 207     -12.595  12.486  -6.077  1.00 12.84           N  
ANISOU 2826  N7   DG M 207      517   2442   1920     19   -258   -128       N  
ATOM   2827  C5   DG M 207     -11.836  13.344  -6.873  1.00 11.92           C  
ANISOU 2827  C5   DG M 207      257   2054   2217     54     68    -88       C  
ATOM   2828  C6   DG M 207     -10.709  14.168  -6.573  1.00 11.77           C  
ANISOU 2828  C6   DG M 207      384   2378   1708    229     85   -152       C  
ATOM   2829  O6   DG M 207     -10.151  14.347  -5.472  1.00 11.06           O  
ANISOU 2829  O6   DG M 207      260   2184   1757    116     24    -28       O  
ATOM   2830  N1   DG M 207     -10.264  14.839  -7.701  1.00 10.71           N  
ANISOU 2830  N1   DG M 207      378   2104   1587   -187   -198   -249       N  
ATOM   2831  C2   DG M 207     -10.827  14.750  -8.949  1.00 10.83           C  
ANISOU 2831  C2   DG M 207      271   2002   1841    154   -109   -267       C  
ATOM   2832  N2   DG M 207     -10.230  15.485  -9.923  1.00 11.82           N  
ANISOU 2832  N2   DG M 207      436   2377   1675    -67   -254    -17       N  
ATOM   2833  N3   DG M 207     -11.904  14.014  -9.234  1.00 12.61           N  
ANISOU 2833  N3   DG M 207      725   2142   1923   -252   -177    -52       N  
ATOM   2834  C4   DG M 207     -12.343  13.347  -8.162  1.00 11.00           C  
ANISOU 2834  C4   DG M 207      280   2091   1806   -102   -169   -203       C  
ATOM   2835  P    DG M 208     -14.563  10.500 -12.757  1.00 21.72           P  
ANISOU 2835  P    DG M 208     1874   3756   2622   -950   -158   -619       P  
ATOM   2836  OP1  DG M 208     -15.165  10.666 -14.097  1.00 25.29           O  
ANISOU 2836  OP1  DG M 208     2584   4513   2512   -633   -489   -277       O  
ATOM   2837  OP2  DG M 208     -14.224   9.154 -12.246  1.00 25.64           O  
ANISOU 2837  OP2  DG M 208     3770   3320   2649   -690    134   -491       O  
ATOM   2838  O5'  DG M 208     -13.219  11.358 -12.667  1.00 18.69           O  
ANISOU 2838  O5'  DG M 208     1466   3174   2459   -288   -137   -258       O  
ATOM   2839  C5'  DG M 208     -13.182  12.725 -13.151  1.00 16.89           C  
ANISOU 2839  C5'  DG M 208     1281   2972   2164   -288     30   -433       C  
ATOM   2840  C4'  DG M 208     -11.770  13.118 -13.555  1.00 15.88           C  
ANISOU 2840  C4'  DG M 208      740   3094   2199    -36   -149    223       C  
ATOM   2841  O4'  DG M 208     -10.921  13.276 -12.388  1.00 15.66           O  
ANISOU 2841  O4'  DG M 208     1394   2680   1873      2   -427    -32       O  
ATOM   2842  C3'  DG M 208     -11.060  12.128 -14.438  1.00 15.61           C  
ANISOU 2842  C3'  DG M 208      809   2981   2140   -114   -346    -87       C  
ATOM   2843  O3'  DG M 208     -10.284  12.883 -15.370  1.00 18.43           O  
ANISOU 2843  O3'  DG M 208     1156   3662   2184    -87   -205     32       O  
ATOM   2844  C2'  DG M 208     -10.229  11.306 -13.434  1.00 17.11           C  
ANISOU 2844  C2'  DG M 208     1530   2888   2082     63   -305   -410       C  
ATOM   2845  C1'  DG M 208      -9.822  12.346 -12.402  1.00 14.20           C  
ANISOU 2845  C1'  DG M 208      614   2811   1969     37     21     47       C  
ATOM   2846  N9   DG M 208      -9.705  11.918 -11.023  1.00 13.61           N  
ANISOU 2846  N9   DG M 208      480   2721   1968    186     82   -336       N  
ATOM   2847  C8   DG M 208     -10.596  11.167 -10.311  1.00 13.16           C  
ANISOU 2847  C8   DG M 208      734   2326   1939     75    330   -144       C  
ATOM   2848  N7   DG M 208     -10.274  11.046  -9.040  1.00 12.35           N  
ANISOU 2848  N7   DG M 208      670   2137   1883     81      1   -133       N  
ATOM   2849  C5   DG M 208      -9.117  11.787  -8.918  1.00 10.48           C  
ANISOU 2849  C5   DG M 208      267   1839   1873     66    -58     67       C  
ATOM   2850  C6   DG M 208      -8.312  12.047  -7.768  1.00 10.48           C  
ANISOU 2850  C6   DG M 208      386   1861   1735    308   -278    249       C  
ATOM   2851  O6   DG M 208      -8.501  11.681  -6.601  1.00 12.09           O  
ANISOU 2851  O6   DG M 208      672   2142   1778     12    -91     97       O  
ATOM   2852  N1   DG M 208      -7.194  12.832  -8.074  1.00 11.68           N  
ANISOU 2852  N1   DG M 208      607   2165   1664    -17    272    -48       N  
ATOM   2853  C2   DG M 208      -6.932  13.348  -9.306  1.00 11.68           C  
ANISOU 2853  C2   DG M 208      612   1978   1848    139    -88    -51       C  
ATOM   2854  N2   DG M 208      -5.812  14.092  -9.419  1.00 12.41           N  
ANISOU 2854  N2   DG M 208      398   2271   2046     22    105    -89       N  
ATOM   2855  N3   DG M 208      -7.688  13.116 -10.377  1.00 11.66           N  
ANISOU 2855  N3   DG M 208      268   2569   1591    -21   -141   -193       N  
ATOM   2856  C4   DG M 208      -8.775  12.343 -10.110  1.00 12.12           C  
ANISOU 2856  C4   DG M 208      452   2308   1845    214   -513     15       C  
ATOM   2857  P    DT M 209      -9.452  12.217 -16.562  1.00 21.91           P  
ANISOU 2857  P    DT M 209     1480   4824   2021    245    -55   -238       P  
ATOM   2858  OP1  DT M 209      -9.285  13.261 -17.599  1.00 24.96           O  
ANISOU 2858  OP1  DT M 209     2009   5156   2316    144     67     82       O  
ATOM   2859  OP2  DT M 209     -10.027  10.903 -16.895  1.00 24.14           O  
ANISOU 2859  OP2  DT M 209     2347   4178   2645    118      4  -1148       O  
ATOM   2860  O5'  DT M 209      -8.039  11.941 -15.902  1.00 19.26           O  
ANISOU 2860  O5'  DT M 209     1242   3753   2320    124   -264   -530       O  
ATOM   2861  C5'  DT M 209      -7.230  13.041 -15.517  1.00 17.47           C  
ANISOU 2861  C5'  DT M 209     1784   3142   1711     99    -59    350       C  
ATOM   2862  C4'  DT M 209      -6.092  12.597 -14.654  1.00 17.74           C  
ANISOU 2862  C4'  DT M 209     1740   3009   1988    194   -517    -64       C  
ATOM   2863  O4'  DT M 209      -6.574  11.988 -13.439  1.00 16.87           O  
ANISOU 2863  O4'  DT M 209     1816   2786   1804   -102    -59     -4       O  
ATOM   2864  C3'  DT M 209      -5.192  11.568 -15.297  1.00 17.77           C  
ANISOU 2864  C3'  DT M 209     1189   3230   2332    445    -17   -120       C  
ATOM   2865  O3'  DT M 209      -4.000  12.250 -15.727  1.00 19.77           O  
ANISOU 2865  O3'  DT M 209     1532   3538   2442    178     62    106       O  
ATOM   2866  C2'  DT M 209      -4.944  10.508 -14.194  1.00 17.81           C  
ANISOU 2866  C2'  DT M 209     1091   3352   2322    309     68   -192       C  
ATOM   2867  C1'  DT M 209      -5.539  11.125 -12.955  1.00 16.61           C  
ANISOU 2867  C1'  DT M 209     1079   3174   2054    234   -540    149       C  
ATOM   2868  N1   DT M 209      -6.213  10.237 -12.005  1.00 16.00           N  
ANISOU 2868  N1   DT M 209     1193   2786   2100    306     65    -38       N  
ATOM   2869  C2   DT M 209      -5.837  10.281 -10.694  1.00 13.82           C  
ANISOU 2869  C2   DT M 209     1104   2196   1950    441    145   -254       C  
ATOM   2870  O2   DT M 209      -4.899  10.950 -10.283  1.00 15.33           O  
ANISOU 2870  O2   DT M 209      935   2729   2160    518   -379    -79       O  
ATOM   2871  N3   DT M 209      -6.617   9.523  -9.853  1.00 13.13           N  
ANISOU 2871  N3   DT M 209      415   2506   2068    282   -191   -206       N  
ATOM   2872  C4   DT M 209      -7.706   8.762 -10.169  1.00 15.29           C  
ANISOU 2872  C4   DT M 209     1257   2310   2242    373    -37     22       C  
ATOM   2873  O4   DT M 209      -8.314   8.118  -9.314  1.00 16.06           O  
ANISOU 2873  O4   DT M 209     1146   2654   2301    346   -219   -270       O  
ATOM   2874  C5   DT M 209      -8.039   8.717 -11.574  1.00 14.07           C  
ANISOU 2874  C5   DT M 209      491   2652   2202    212   -220     41       C  
ATOM   2875  C7   DT M 209      -9.169   7.827 -12.048  1.00 19.42           C  
ANISOU 2875  C7   DT M 209     1204   2750   3424    -58   -650   -194       C  
ATOM   2876  C6   DT M 209      -7.312   9.478 -12.413  1.00 14.60           C  
ANISOU 2876  C6   DT M 209      804   2694   2048     47   -199   -412       C  
ATOM   2877  P    DA M 210      -2.893  11.542 -16.611  1.00 21.07           P  
ANISOU 2877  P    DA M 210     1533   4153   2320    481    263    -57       P  
ATOM   2878  OP1  DA M 210      -2.262  12.616 -17.392  1.00 25.34           O  
ANISOU 2878  OP1  DA M 210     2554   4314   2758    183    370    464       O  
ATOM   2879  OP2  DA M 210      -3.446  10.342 -17.262  1.00 24.42           O  
ANISOU 2879  OP2  DA M 210     2860   4027   2392    808    253   -710       O  
ATOM   2880  O5'  DA M 210      -1.861  11.014 -15.532  1.00 19.03           O  
ANISOU 2880  O5'  DA M 210     1694   3333   2201    205      7     71       O  
ATOM   2881  C5'  DA M 210      -1.167  11.917 -14.726  1.00 18.38           C  
ANISOU 2881  C5'  DA M 210     2085   2889   2010    353    117    213       C  
ATOM   2882  C4'  DA M 210      -0.431  11.185 -13.614  1.00 14.67           C  
ANISOU 2882  C4'  DA M 210      365   2995   2212    310    313     35       C  
ATOM   2883  O4'  DA M 210      -1.393  10.549 -12.734  1.00 17.28           O  
ANISOU 2883  O4'  DA M 210     1563   2859   2141    396    322    -19       O  
ATOM   2884  C3'  DA M 210       0.528  10.068 -14.068  1.00 17.31           C  
ANISOU 2884  C3'  DA M 210     1407   2867   2303    361     91   -178       C  
ATOM   2885  O3'  DA M 210       1.656  10.073 -13.232  1.00 17.53           O  
ANISOU 2885  O3'  DA M 210     1182   3111   2366    754    -57   -245       O  
ATOM   2886  C2'  DA M 210      -0.316   8.827 -13.842  1.00 17.90           C  
ANISOU 2886  C2'  DA M 210     2186   2342   2272    274    169   -274       C  
ATOM   2887  C1'  DA M 210      -0.983   9.211 -12.530  1.00 18.16           C  
ANISOU 2887  C1'  DA M 210     2224   2528   2148    346    169   -220       C  
ATOM   2888  N9   DA M 210      -2.143   8.427 -12.157  1.00 16.47           N  
ANISOU 2888  N9   DA M 210     1626   2717   1912    344   -282   -201       N  
ATOM   2889  C8   DA M 210      -3.047   7.820 -12.980  1.00 17.11           C  
ANISOU 2889  C8   DA M 210     1824   2616   2059    326    -76     19       C  
ATOM   2890  N7   DA M 210      -4.004   7.211 -12.339  1.00 17.61           N  
ANISOU 2890  N7   DA M 210     1806   2578   2306     50   -398   -172       N  
ATOM   2891  C5   DA M 210      -3.739   7.462 -11.008  1.00 15.75           C  
ANISOU 2891  C5   DA M 210     1054   2453   2478    372   -215   -159       C  
ATOM   2892  C6   DA M 210      -4.379   7.076  -9.826  1.00 15.63           C  
ANISOU 2892  C6   DA M 210     1572   1900   2463    485    -84   -247       C  
ATOM   2893  N6   DA M 210      -5.496   6.349  -9.806  1.00 15.52           N  
ANISOU 2893  N6   DA M 210      764   2165   2966    209   -346   -356       N  
ATOM   2894  N1   DA M 210      -3.847   7.489  -8.665  1.00 14.36           N  
ANISOU 2894  N1   DA M 210     1079   2020   2357    204   -163   -105       N  
ATOM   2895  C2   DA M 210      -2.735   8.221  -8.683  1.00 13.55           C  
ANISOU 2895  C2   DA M 210      987   2088   2071     95    107   -153       C  
ATOM   2896  N3   DA M 210      -2.032   8.646  -9.729  1.00 13.37           N  
ANISOU 2896  N3   DA M 210      467   2426   2186    391    -36   -101       N  
ATOM   2897  C4   DA M 210      -2.591   8.209 -10.877  1.00 14.40           C  
ANISOU 2897  C4   DA M 210     1094   2288   2088    279    -39    -72       C  
ATOM   2898  P    DC M 211       3.056   9.417 -13.624  1.00 18.45           P  
ANISOU 2898  P    DC M 211     1467   3010   2530    459    263   -177       P  
ATOM   2899  OP1  DC M 211       3.786  10.377 -14.455  1.00 20.52           O  
ANISOU 2899  OP1  DC M 211     1695   3223   2880    215    669     59       O  
ATOM   2900  OP2  DC M 211       2.832   8.029 -14.113  1.00 20.32           O  
ANISOU 2900  OP2  DC M 211     2145   2961   2613    221    596   -205       O  
ATOM   2901  O5'  DC M 211       3.742   9.292 -12.202  1.00 17.08           O  
ANISOU 2901  O5'  DC M 211     1449   2359   2682    370    158   -310       O  
ATOM   2902  C5'  DC M 211       3.747  10.379 -11.326  1.00 17.27           C  
ANISOU 2902  C5'  DC M 211     1184   2977   2400    383    -88     62       C  
ATOM   2903  C4'  DC M 211       3.452   9.934  -9.916  1.00 16.00           C  
ANISOU 2903  C4'  DC M 211      951   2750   2375     46    205   -160       C  
ATOM   2904  O4'  DC M 211       2.174   9.279  -9.858  1.00 16.31           O  
ANISOU 2904  O4'  DC M 211      841   2572   2784    157    130     76       O  
ATOM   2905  C3'  DC M 211       4.431   8.942  -9.330  1.00 18.59           C  
ANISOU 2905  C3'  DC M 211     1449   2750   2861    261    436    -81       C  
ATOM   2906  O3'  DC M 211       4.653   9.332  -8.001  1.00 19.15           O  
ANISOU 2906  O3'  DC M 211     1353   3363   2559    364   -140    -29       O  
ATOM   2907  C2'  DC M 211       3.707   7.608  -9.447  1.00 17.29           C  
ANISOU 2907  C2'  DC M 211      988   2938   2641    562   -145     19       C  
ATOM   2908  C1'  DC M 211       2.278   8.028  -9.216  1.00 15.00           C  
ANISOU 2908  C1'  DC M 211      510   2712   2474    341    -76   -137       C  
ATOM   2909  N1   DC M 211       1.270   7.100  -9.770  1.00 16.69           N  
ANISOU 2909  N1   DC M 211     1698   2399   2244     88     24    -57       N  
ATOM   2910  C2   DC M 211       0.280   6.592  -8.924  1.00 15.30           C  
ANISOU 2910  C2   DC M 211      957   2625   2229    576   -390    107       C  
ATOM   2911  O2   DC M 211       0.279   6.931  -7.738  1.00 15.52           O  
ANISOU 2911  O2   DC M 211      750   2557   2588   -227    -60      3       O  
ATOM   2912  N3   DC M 211      -0.651   5.749  -9.438  1.00 15.41           N  
ANISOU 2912  N3   DC M 211      887   2563   2403    277   -192   -349       N  
ATOM   2913  C4   DC M 211      -0.622   5.428 -10.743  1.00 14.19           C  
ANISOU 2913  C4   DC M 211      652   1930   2806    259    121   -128       C  
ATOM   2914  N4   DC M 211      -1.591   4.600 -11.203  1.00 17.47           N  
ANISOU 2914  N4   DC M 211     1386   2279   2971    247   -299   -418       N  
ATOM   2915  C5   DC M 211       0.376   5.953 -11.620  1.00 16.44           C  
ANISOU 2915  C5   DC M 211     1276   2465   2506    209   -206    -70       C  
ATOM   2916  C6   DC M 211       1.284   6.779 -11.096  1.00 16.28           C  
ANISOU 2916  C6   DC M 211     1043   2622   2517    374    515     91       C  
ATOM   2917  P    DC M 212       5.697   8.640  -7.049  1.00 20.95           P  
ANISOU 2917  P    DC M 212     1208   3324   3425     76   -144    404       P  
ATOM   2918  OP1  DC M 212       6.169   9.682  -6.066  1.00 22.33           O  
ANISOU 2918  OP1  DC M 212     1570   3305   3609   -422   -350    369       O  
ATOM   2919  OP2  DC M 212       6.683   7.857  -7.817  1.00 22.70           O  
ANISOU 2919  OP2  DC M 212     1731   3004   3887   1091     95    690       O  
ATOM   2920  O5'  DC M 212       4.815   7.544  -6.297  1.00 20.02           O  
ANISOU 2920  O5'  DC M 212      972   3363   3272     68    318    168       O  
ATOM   2921  C5'  DC M 212       3.896   7.911  -5.281  1.00 21.17           C  
ANISOU 2921  C5'  DC M 212     1704   3261   3078    -31    379     30       C  
ATOM   2922  C4'  DC M 212       3.329   6.658  -4.631  1.00 22.89           C  
ANISOU 2922  C4'  DC M 212     2670   3002   3023   -309     79    125       C  
ATOM   2923  O4'  DC M 212       2.535   5.963  -5.602  1.00 19.98           O  
ANISOU 2923  O4'  DC M 212     1344   2882   3365     67   -490    345       O  
ATOM   2924  C3'  DC M 212       4.362   5.639  -4.170  1.00 26.36           C  
ANISOU 2924  C3'  DC M 212     2558   3568   3889    177    400     26       C  
ATOM   2925  O3'  DC M 212       4.296   5.450  -2.743  1.00 28.81           O  
ANISOU 2925  O3'  DC M 212     3029   3982   3935   -190   -248    538       O  
ATOM   2926  C2'  DC M 212       4.019   4.359  -4.943  1.00 21.05           C  
ANISOU 2926  C2'  DC M 212     1226   3663   3107    547   -301     24       C  
ATOM   2927  C1'  DC M 212       2.592   4.572  -5.385  1.00 23.96           C  
ANISOU 2927  C1'  DC M 212     2373   3326   3402    556   -421    213       C  
ATOM   2928  N1   DC M 212       2.180   3.939  -6.675  1.00 19.38           N  
ANISOU 2928  N1   DC M 212     1717   2366   3280    266      2    490       N  
ATOM   2929  C2   DC M 212       1.154   2.976  -6.743  1.00 19.74           C  
ANISOU 2929  C2   DC M 212     1796   2217   3486   1039    244   -166       C  
ATOM   2930  O2   DC M 212       0.626   2.561  -5.710  1.00 22.26           O  
ANISOU 2930  O2   DC M 212     2341   2405   3711    508    471    165       O  
ATOM   2931  N3   DC M 212       0.781   2.502  -7.956  1.00 19.73           N  
ANISOU 2931  N3   DC M 212     1920   2048   3528    369     70    274       N  
ATOM   2932  C4   DC M 212       1.375   2.941  -9.070  1.00 21.90           C  
ANISOU 2932  C4   DC M 212     2614   1727   3979   1126    346    246       C  
ATOM   2933  N4   DC M 212       0.965   2.434 -10.252  1.00 23.37           N  
ANISOU 2933  N4   DC M 212     1820   3075   3983    943    255     10       N  
ATOM   2934  C5   DC M 212       2.427   3.900  -9.023  1.00 21.22           C  
ANISOU 2934  C5   DC M 212     2828   2297   2937    606    205    119       C  
ATOM   2935  C6   DC M 212       2.785   4.375  -7.824  1.00 20.26           C  
ANISOU 2935  C6   DC M 212     1785   2500   3411    207   -105    625       C  
TER    2936       DC M 212                                                      
HETATM 2937  C1  PG6 A1281      18.639  32.247 -12.182  1.00 27.99           C  
ANISOU 2937  C1  PG6 A1281     1810   4291   4533    215     68  -1090       C  
HETATM 2938  O1  PG6 A1281      19.223  32.461 -10.886  1.00 33.73           O  
ANISOU 2938  O1  PG6 A1281     3214   4719   4881    511    115   -345       O  
HETATM 2939  C2  PG6 A1281      19.652  31.246 -10.288  1.00 37.86           C  
ANISOU 2939  C2  PG6 A1281     4499   4766   5119    -58     60    194       C  
HETATM 2940  C3  PG6 A1281      19.131  31.129  -8.854  1.00 37.14           C  
ANISOU 2940  C3  PG6 A1281     4644   4631   4835     -2     14     -3       C  
HETATM 2941  O2  PG6 A1281      18.283  32.228  -8.523  1.00 34.24           O  
ANISOU 2941  O2  PG6 A1281     3663   4556   4789   -295   -294    388       O  
HETATM 2942  C4  PG6 A1281      17.054  31.803  -7.944  1.00 28.45           C  
ANISOU 2942  C4  PG6 A1281     2870   4215   3724   -286   -191      7       C  
HETATM 2943  C5  PG6 A1281      16.436  32.934  -7.127  1.00 25.19           C  
ANISOU 2943  C5  PG6 A1281     2085   3831   3655   -807   -695    242       C  
HETATM 2944  O3  PG6 A1281      16.277  34.085  -7.944  1.00 30.46           O  
ANISOU 2944  O3  PG6 A1281     2557   4937   4076   -667   -183   -111       O  
HETATM 2945  C6  PG6 A1281      15.646  35.146  -7.255  1.00 28.00           C  
ANISOU 2945  C6  PG6 A1281     2775   4166   3698   -532   -375   -804       C  
HETATM 2946  C7  PG6 A1281      15.437  36.333  -8.194  1.00 22.74           C  
ANISOU 2946  C7  PG6 A1281     1872   3856   2911   -317   -543   -936       C  
HETATM 2947  O4  PG6 A1281      16.702  36.894  -8.594  1.00 26.83           O  
ANISOU 2947  O4  PG6 A1281     2118   4210   3863    342   -930   -877       O  
HETATM 2948  C8  PG6 A1281      16.505  37.891  -9.592  1.00 31.81           C  
ANISOU 2948  C8  PG6 A1281     4611   3922   3553    629   -491   -318       C  
HETATM 2949  C9  PG6 A1281      17.838  38.426 -10.116  1.00 35.88           C  
ANISOU 2949  C9  PG6 A1281     4803   4211   4618    410   -218    131       C  
HETATM 2950  O5  PG6 A1281      18.801  37.375 -10.200  1.00 42.20           O  
ANISOU 2950  O5  PG6 A1281     5505   5303   5226    115    377    -70       O  
HETATM 2951  C10 PG6 A1281      19.536  37.404 -11.419  1.00 43.51           C  
ANISOU 2951  C10 PG6 A1281     5298   5620   5613   -128    166     80       C  
HETATM 2952  C11 PG6 A1281      20.534  36.253 -11.431  1.00 46.67           C  
ANISOU 2952  C11 PG6 A1281     5715   6057   5957     78    139    171       C  
HETATM 2953  O6  PG6 A1281      21.264  36.245 -10.204  1.00 53.98           O  
ANISOU 2953  O6  PG6 A1281     6937   6891   6680     86    113    177       O  
HETATM 2954  C12 PG6 A1281      21.635  34.922  -9.810  1.00 54.63           C  
ANISOU 2954  C12 PG6 A1281     6742   6847   7165     86     90    111       C  
HETATM 2955 NA    NA A1282      18.490  34.917  -9.354  1.00 15.19          NA  
ANISOU 2955 NA    NA A1282      298   3056   2416   -106     17     -2      NA  
HETATM 2956  O   HOH A2001      14.216  37.313 -22.735  1.00 34.74           O  
ANISOU 2956  O   HOH A2001     3364   5273   4562    261   1190    723       O  
HETATM 2957  O   HOH A2002      17.177  44.404 -20.405  1.00 49.51           O  
ANISOU 2957  O   HOH A2002     6218   6226   6368    -24    580    168       O  
HETATM 2958  O   HOH A2003      11.323  44.129 -20.611  1.00 43.35           O  
ANISOU 2958  O   HOH A2003     6131   5267   5071   -288      8     26       O  
HETATM 2959  O   HOH A2004       5.929  28.161 -23.614  1.00 31.84           O  
ANISOU 2959  O   HOH A2004     3577   5495   3024   1122   -173   -483       O  
HETATM 2960  O   HOH A2005       4.970  32.444 -24.945  1.00 32.32           O  
ANISOU 2960  O   HOH A2005     2721   5275   4281   -225    960    546       O  
HETATM 2961  O   HOH A2006       7.895  34.908 -27.078  1.00 48.72           O  
ANISOU 2961  O   HOH A2006     4900   7047   6562    600    111    -30       O  
HETATM 2962  O   HOH A2007       8.511  35.097 -18.645  1.00 14.82           O  
ANISOU 2962  O   HOH A2007      887   2860   1881     69    291    114       O  
HETATM 2963  O   HOH A2008      13.385  31.414 -20.026  1.00 29.37           O  
ANISOU 2963  O   HOH A2008     3944   3695   3520    216    969    -83       O  
HETATM 2964  O   HOH A2009     -16.114  24.641   4.132  1.00 27.79           O  
ANISOU 2964  O   HOH A2009     1181   4097   5278   -160   1245   -903       O  
HETATM 2965  O   HOH A2010     -13.928   4.854  -0.103  1.00 42.73           O  
ANISOU 2965  O   HOH A2010     5203   5053   5979   -820   -411    -95       O  
HETATM 2966  O   HOH A2011      -0.920  34.162 -19.868  1.00 17.35           O  
ANISOU 2966  O   HOH A2011      926   3642   2023     65    -57     -5       O  
HETATM 2967  O   HOH A2012       6.829  27.849 -20.776  1.00 27.18           O  
ANISOU 2967  O   HOH A2012     1163   5286   3875    704     81  -1628       O  
HETATM 2968  O   HOH A2013       4.484  30.641 -23.134  1.00 23.88           O  
ANISOU 2968  O   HOH A2013     2270   4327   2475   -494    562   -762       O  
HETATM 2969  O   HOH A2014      -0.128  22.889 -14.837  1.00 34.81           O  
ANISOU 2969  O   HOH A2014     1731   3730   7765   -493    791     75       O  
HETATM 2970  O   HOH A2015       1.823  23.559 -12.275  1.00 25.11           O  
ANISOU 2970  O   HOH A2015     2830   3688   3022     11   -171   -333       O  
HETATM 2971  O   HOH A2016      -1.093  19.417  25.777  1.00 33.58           O  
ANISOU 2971  O   HOH A2016     5360   4707   2690   1232    820    615       O  
HETATM 2972  O   HOH A2017       2.108  30.464  -9.426  1.00 13.64           O  
ANISOU 2972  O   HOH A2017      770   2467   1945    -37    380   -126       O  
HETATM 2973  O   HOH A2018       0.183  22.205  -6.899  1.00 13.28           O  
ANISOU 2973  O   HOH A2018      484   2247   2315   -101    149    -88       O  
HETATM 2974  O   HOH A2019      -0.500  21.410 -11.541  1.00 23.76           O  
ANISOU 2974  O   HOH A2019     1351   3786   3889    150   -364    683       O  
HETATM 2975  O   HOH A2020       8.692  31.305  14.316  1.00 41.37           O  
ANISOU 2975  O   HOH A2020     4584   5520   5611   -870    -29    -88       O  
HETATM 2976  O   HOH A2021      -4.104  23.284  -7.976  1.00 12.58           O  
ANISOU 2976  O   HOH A2021      511   2491   1777     32     88   -127       O  
HETATM 2977  O   HOH A2022       1.181  23.633  -3.169  1.00 11.99           O  
ANISOU 2977  O   HOH A2022      298   2336   1920    129   -245     23       O  
HETATM 2978  O   HOH A2023       9.857  11.677 -16.366  1.00 35.09           O  
ANISOU 2978  O   HOH A2023     3629   4804   4896    498   1539   -964       O  
HETATM 2979  O   HOH A2024      -7.531  20.446  -3.000  1.00 13.86           O  
ANISOU 2979  O   HOH A2024      590   2513   2160    -19    -90     -6       O  
HETATM 2980  O   HOH A2025      -5.962  25.446  -7.924  1.00 10.74           O  
ANISOU 2980  O   HOH A2025      273   2143   1663    101   -143     19       O  
HETATM 2981  O   HOH A2026      13.641  12.835 -14.630  1.00 41.47           O  
ANISOU 2981  O   HOH A2026     3689   5407   6658    747    938   -311       O  
HETATM 2982  O   HOH A2027     -10.026  21.709  -3.303  1.00 11.46           O  
ANISOU 2982  O   HOH A2027      291   2322   1740   -238    122      8       O  
HETATM 2983  O   HOH A2028     -15.667   8.475   6.685  1.00 43.40           O  
ANISOU 2983  O   HOH A2028     5242   5453   5794   -265    775    293       O  
HETATM 2984  O   HOH A2029     -14.277  22.767   3.567  1.00 15.85           O  
ANISOU 2984  O   HOH A2029      770   2833   2417   -200    234   -162       O  
HETATM 2985  O   HOH A2030      -7.225  25.617   2.267  1.00 21.11           O  
ANISOU 2985  O   HOH A2030      791   5120   2108   -586    113  -1006       O  
HETATM 2986  O   HOH A2031     -10.484  32.918   5.587  1.00 25.04           O  
ANISOU 2986  O   HOH A2031     2465   3564   3484   -679     52     44       O  
HETATM 2987  O   HOH A2032     -12.040  36.748   4.228  1.00 49.58           O  
ANISOU 2987  O   HOH A2032     6772   6426   5637   -628   -656   -161       O  
HETATM 2988  O   HOH A2033     -13.468  33.936   4.075  1.00 31.31           O  
ANISOU 2988  O   HOH A2033     1431   5968   4498   -592    193   -683       O  
HETATM 2989  O   HOH A2034     -21.353  11.479  10.895  1.00 41.46           O  
ANISOU 2989  O   HOH A2034     3731   6593   5428  -1243   1331    362       O  
HETATM 2990  O   HOH A2035     -13.760  32.911   1.648  1.00 21.17           O  
ANISOU 2990  O   HOH A2035     1345   3447   3249   -175    488   -656       O  
HETATM 2991  O   HOH A2036     -15.485  32.125   7.853  1.00 32.26           O  
ANISOU 2991  O   HOH A2036     1612   4739   5907   -384   1219  -2433       O  
HETATM 2992  O   HOH A2037     -17.532  26.168   2.317  1.00 26.87           O  
ANISOU 2992  O   HOH A2037     1585   4101   4522     40    345   -754       O  
HETATM 2993  O   HOH A2038     -16.710  32.572  -0.173  1.00 32.80           O  
ANISOU 2993  O   HOH A2038     3116   5574   3770    694   -174    937       O  
HETATM 2994  O   HOH A2039     -19.501   8.961   7.560  1.00 43.22           O  
ANISOU 2994  O   HOH A2039     6099   5219   5102   -601   -460    117       O  
HETATM 2995  O   HOH A2040     -20.370   8.718   1.438  1.00 49.35           O  
ANISOU 2995  O   HOH A2040     5498   6229   7021  -1395   -162    846       O  
HETATM 2996  O   HOH A2041     -16.783   5.425   2.894  1.00 45.78           O  
ANISOU 2996  O   HOH A2041     5220   5233   6939  -1058   -445    113       O  
HETATM 2997  O   HOH A2042     -13.762  26.269   4.058  1.00 17.73           O  
ANISOU 2997  O   HOH A2042      355   2685   3694    181   -220   -655       O  
HETATM 2998  O   HOH A2043     -13.127   7.057  -1.008  1.00 23.68           O  
ANISOU 2998  O   HOH A2043     2297   3385   3314   -123    -82     -8       O  
HETATM 2999  O   HOH A2044     -13.378   6.804  -3.701  1.00 25.97           O  
ANISOU 2999  O   HOH A2044     2834   3474   3557    143   -357    141       O  
HETATM 3000  O   HOH A2045     -11.551   5.648  -4.828  1.00 36.64           O  
ANISOU 3000  O   HOH A2045     3047   4122   6749  -1079    -15   -204       O  
HETATM 3001  O   HOH A2046      -9.823  34.011   8.957  1.00 38.96           O  
ANISOU 3001  O   HOH A2046     2063   4907   7832    478   -272    937       O  
HETATM 3002  O   HOH A2047     -10.032  30.647  14.884  1.00 22.40           O  
ANISOU 3002  O   HOH A2047     1328   3688   3494   -180     82   -473       O  
HETATM 3003  O   HOH A2048     -13.396  31.869   9.033  1.00 27.75           O  
ANISOU 3003  O   HOH A2048     1730   3953   4859    571    180   -254       O  
HETATM 3004  O   HOH A2049      -0.309  12.355   4.408  1.00 18.77           O  
ANISOU 3004  O   HOH A2049     2061   2768   2301    324      6     72       O  
HETATM 3005  O   HOH A2050     -12.950  24.185  15.605  1.00 34.22           O  
ANISOU 3005  O   HOH A2050     4140   4864   3994   -110    806    158       O  
HETATM 3006  O   HOH A2051     -13.386  27.647  17.025  1.00 41.39           O  
ANISOU 3006  O   HOH A2051     4489   7032   4204   -443   -591   -601       O  
HETATM 3007  O   HOH A2052     -19.127  28.681  12.749  1.00 37.11           O  
ANISOU 3007  O   HOH A2052     2127   5256   6717   1217    781    133       O  
HETATM 3008  O   HOH A2053     -16.601  27.740  16.152  1.00 36.65           O  
ANISOU 3008  O   HOH A2053     2658   5894   5374    346   -333    -14       O  
HETATM 3009  O   HOH A2054       2.489  12.902   5.501  1.00 33.73           O  
ANISOU 3009  O   HOH A2054     3484   6390   2941    494    -53    -31       O  
HETATM 3010  O   HOH A2055      -5.641  24.432  20.999  1.00 20.55           O  
ANISOU 3010  O   HOH A2055     1109   3692   3007    -97   -504   -763       O  
HETATM 3011  O   HOH A2056      -5.322  20.275  21.557  1.00 30.07           O  
ANISOU 3011  O   HOH A2056     2979   5546   2898    395    645    202       O  
HETATM 3012  O   HOH A2057     -10.924  22.915  17.704  1.00 27.25           O  
ANISOU 3012  O   HOH A2057     1418   5348   3586   -568    493   -455       O  
HETATM 3013  O   HOH A2058       8.477  27.558  16.568  1.00 46.55           O  
ANISOU 3013  O   HOH A2058     5451   6096   6139   -193    436   -100       O  
HETATM 3014  O   HOH A2059       5.104  15.915  19.506  1.00 41.46           O  
ANISOU 3014  O   HOH A2059     5254   5536   4964    -58   -950    947       O  
HETATM 3015  O   HOH A2060       1.687  22.509  23.596  1.00 34.45           O  
ANISOU 3015  O   HOH A2060     4230   4663   4196    550   -195    179       O  
HETATM 3016  O   HOH A2061       5.397  23.355  21.323  1.00 40.93           O  
ANISOU 3016  O   HOH A2061     5294   5764   4492    398   1447   -956       O  
HETATM 3017  O   HOH A2062       8.910  25.423  20.788  1.00 40.76           O  
ANISOU 3017  O   HOH A2062     3452   6906   5127    804   -234    308       O  
HETATM 3018  O   HOH A2063      -1.300  21.049  23.762  1.00 26.88           O  
ANISOU 3018  O   HOH A2063     3650   3666   2896    138    240    199       O  
HETATM 3019  O   HOH A2064       0.632  16.057  20.608  1.00 34.48           O  
ANISOU 3019  O   HOH A2064     3410   5436   4251    967   -193   -182       O  
HETATM 3020  O   HOH A2065       0.722  23.314  26.444  1.00 36.68           O  
ANISOU 3020  O   HOH A2065     2972   4980   5984   -690   1302  -1459       O  
HETATM 3021  O   HOH A2066      -3.956  10.947  22.326  1.00 38.07           O  
ANISOU 3021  O   HOH A2066     6596   4696   3172    331    309   1208       O  
HETATM 3022  O   HOH A2067      -3.867  17.674  23.135  1.00 38.85           O  
ANISOU 3022  O   HOH A2067     5290   4623   4848   -719   -137   -181       O  
HETATM 3023  O   HOH A2068      -1.450  13.667  22.012  1.00 25.02           O  
ANISOU 3023  O   HOH A2068     3531   3928   2045    183   -488    349       O  
HETATM 3024  O   HOH A2069      11.432  30.345  12.752  1.00 39.70           O  
ANISOU 3024  O   HOH A2069     3847   5286   5948   -803   -243    -48       O  
HETATM 3025  O   HOH A2070       9.092  35.111   9.148  1.00 44.64           O  
ANISOU 3025  O   HOH A2070     3856   7069   6034   -508   1154   -382       O  
HETATM 3026  O   HOH A2071       0.206   2.084  10.671  1.00 43.58           O  
ANISOU 3026  O   HOH A2071     6019   4623   5915    -39    327    621       O  
HETATM 3027  O   HOH A2072       7.546  12.530 -15.499  1.00 26.10           O  
ANISOU 3027  O   HOH A2072     2737   3490   3688     92    790   -449       O  
HETATM 3028  O   HOH A2073       8.595  16.505 -17.542  1.00 37.01           O  
ANISOU 3028  O   HOH A2073     4589   5567   3904    133    329     18       O  
HETATM 3029  O   HOH A2074       2.516  13.005  -3.969  1.00 31.65           O  
ANISOU 3029  O   HOH A2074     3722   4493   3806   1701   -187   -424       O  
HETATM 3030  O   HOH A2075      13.958  14.950 -13.207  1.00 35.57           O  
ANISOU 3030  O   HOH A2075     3056   5205   5252   -290    106    519       O  
HETATM 3031  O   HOH A2076      15.650  18.024 -14.978  1.00 41.80           O  
ANISOU 3031  O   HOH A2076     5586   4573   5723    252   1380   -190       O  
HETATM 3032  O   HOH A2077      12.961  16.759 -17.379  1.00 43.90           O  
ANISOU 3032  O   HOH A2077     4834   6314   5531    369    543   -749       O  
HETATM 3033  O   HOH A2078     -11.621   7.440  15.983  1.00 36.06           O  
ANISOU 3033  O   HOH A2078     4237   4738   4723  -1230    222    667       O  
HETATM 3034  O   HOH A2079     -10.910  10.334  16.610  1.00 34.01           O  
ANISOU 3034  O   HOH A2079     4199   4837   3885   -188   1007    514       O  
HETATM 3035  O   HOH A2080      18.411  28.928 -14.982  1.00 33.71           O  
ANISOU 3035  O   HOH A2080     3163   4758   4884   -229   1562   -169       O  
HETATM 3036  O   HOH A2081     -13.052   7.807   7.133  1.00 37.15           O  
ANISOU 3036  O   HOH A2081     4482   5313   4320  -1883    794   -765       O  
HETATM 3037  O   HOH A2082     -14.985   9.419   9.411  1.00 37.63           O  
ANISOU 3037  O   HOH A2082     5142   5062   4090  -1228    559    120       O  
HETATM 3038  O   HOH A2083     -17.633  11.085  14.086  1.00 34.49           O  
ANISOU 3038  O   HOH A2083     3129   6050   3925  -1285     43    756       O  
HETATM 3039  O   HOH A2084     -12.753   7.243  10.225  1.00 35.52           O  
ANISOU 3039  O   HOH A2084     3458   4276   5759   -418   -577    505       O  
HETATM 3040  O   HOH A2085     -14.532  17.050  16.140  1.00 29.08           O  
ANISOU 3040  O   HOH A2085     2898   5130   3021   -362    115   -431       O  
HETATM 3041  O   HOH A2086     -12.144  19.000  16.904  1.00 43.36           O  
ANISOU 3041  O   HOH A2086     4536   7718   4218    692   1644    212       O  
HETATM 3042  O   HOH A2087      -9.669  12.350  19.610  1.00 48.68           O  
ANISOU 3042  O   HOH A2087     6051   6849   5596    -77    824    149       O  
HETATM 3043  O   HOH A2088       3.962  55.666 -13.968  1.00 34.28           O  
ANISOU 3043  O   HOH A2088     4629   3929   4465     -3     50     91       O  
HETATM 3044  O   HOH A2089     -21.253  17.598  14.109  1.00 45.76           O  
ANISOU 3044  O   HOH A2089     3702   6462   7223   -631   1245    352       O  
HETATM 3045  O   HOH A2090      -0.639  54.901 -12.195  1.00 32.13           O  
ANISOU 3045  O   HOH A2090     3999   4030   4177    568    755    307       O  
HETATM 3046  O   HOH A2091     -18.822  23.753  11.166  1.00 41.23           O  
ANISOU 3046  O   HOH A2091     5981   4372   5310    706   -370   -124       O  
HETATM 3047  O   HOH A2092     -21.995  21.058   9.424  1.00 43.08           O  
ANISOU 3047  O   HOH A2092     3797   5238   7332    671    926   -692       O  
HETATM 3048  O   HOH A2093     -18.565  21.963   5.382  1.00 26.31           O  
ANISOU 3048  O   HOH A2093     1000   5191   3805    632   1164    376       O  
HETATM 3049  O   HOH A2094     -23.862  16.980  10.136  1.00 37.20           O  
ANISOU 3049  O   HOH A2094     3377   5780   4976   -314    748   -490       O  
HETATM 3050  O   HOH A2095     -21.532  10.128   8.488  1.00 41.49           O  
ANISOU 3050  O   HOH A2095     4644   6052   5065  -1257   1105    253       O  
HETATM 3051  O   HOH A2096     -20.750  10.500   5.083  1.00 41.64           O  
ANISOU 3051  O   HOH A2096     4074   5183   6564   -446    -56    311       O  
HETATM 3052  O   HOH A2097     -22.536  11.612   1.246  1.00 45.30           O  
ANISOU 3052  O   HOH A2097     4911   5942   6356  -1087     86   -115       O  
HETATM 3053  O   HOH A2098     -18.605  18.367   3.058  1.00 26.22           O  
ANISOU 3053  O   HOH A2098     1662   4370   3930  -1037      8    -68       O  
HETATM 3054  O   HOH A2099     -17.917   9.695   5.511  1.00 34.71           O  
ANISOU 3054  O   HOH A2099     4012   5277   3900  -1287    708    431       O  
HETATM 3055  O   HOH A2100      17.239  45.434  -8.061  1.00 29.90           O  
ANISOU 3055  O   HOH A2100     1433   5158   4768   -493   -322   -693       O  
HETATM 3056  O   HOH A2101     -17.606   7.895   1.495  1.00 29.82           O  
ANISOU 3056  O   HOH A2101     2281   3599   5447   -656   -543    728       O  
HETATM 3057  O   HOH A2102      -7.829   4.797   4.205  1.00 42.30           O  
ANISOU 3057  O   HOH A2102     5719   5612   4740    278   -141   -268       O  
HETATM 3058  O   HOH A2103       8.078  53.488 -19.970  1.00 37.04           O  
ANISOU 3058  O   HOH A2103     3308   5169   5595   -746    392    706       O  
HETATM 3059  O   HOH A2104       9.748  53.419 -15.953  1.00 45.83           O  
ANISOU 3059  O   HOH A2104     4349   5771   7291   -425   -240     74       O  
HETATM 3060  O   HOH A2105      -9.999   7.834  -4.542  1.00 16.04           O  
ANISOU 3060  O   HOH A2105     1047   2502   2544    186     64   -259       O  
HETATM 3061  O   HOH A2106     -15.529   8.488  -0.626  1.00 17.69           O  
ANISOU 3061  O   HOH A2106      885   2973   2860   -833   -151   -260       O  
HETATM 3062  O   HOH A2107       4.979  46.040 -26.384  1.00 36.02           O  
ANISOU 3062  O   HOH A2107     4478   5715   3492    -90    111     71       O  
HETATM 3063  O   HOH A2108       2.374  53.750 -15.309  1.00 25.80           O  
ANISOU 3063  O   HOH A2108     1908   3849   4045     71    538    395       O  
HETATM 3064  O   HOH A2109       4.265  56.106 -18.614  1.00 36.56           O  
ANISOU 3064  O   HOH A2109     5492   3780   4617   -582    318   1092       O  
HETATM 3065  O   HOH A2110      -1.608  53.992 -16.460  1.00 36.48           O  
ANISOU 3065  O   HOH A2110     1748   5527   6583    326   -230    322       O  
HETATM 3066  O   HOH A2111       6.633  49.474 -28.339  1.00 41.18           O  
ANISOU 3066  O   HOH A2111     5205   5807   4635    294   1899   -136       O  
HETATM 3067  O   HOH A2112      -3.290  52.191 -17.468  1.00 45.08           O  
ANISOU 3067  O   HOH A2112     4240   6250   6639    156   -142     19       O  
HETATM 3068  O   HOH A2113      -7.330   7.407   1.153  1.00 22.87           O  
ANISOU 3068  O   HOH A2113     2077   2855   3754   -183    573   -262       O  
HETATM 3069  O   HOH A2114     -10.642   8.177  -0.302  1.00 19.27           O  
ANISOU 3069  O   HOH A2114     1708   3032   2580    162    292   -127       O  
HETATM 3070  O   HOH A2115     -13.567  29.408 -23.842  1.00 38.66           O  
ANISOU 3070  O   HOH A2115     5089   5668   3929    607     16   -603       O  
HETATM 3071  O   HOH A2116      -5.730  35.414 -22.799  1.00 46.21           O  
ANISOU 3071  O   HOH A2116     5324   6137   6094     -9   -599    -83       O  
HETATM 3072  O   HOH A2117     -13.982  26.849 -24.352  1.00 42.60           O  
ANISOU 3072  O   HOH A2117     3040   6094   7050   1270   -239    689       O  
HETATM 3073  O   HOH A2118      -5.870   6.889   3.355  1.00 37.22           O  
ANISOU 3073  O   HOH A2118     4836   5053   4251   -724  -1379   -614       O  
HETATM 3074  O   HOH A2119      -2.388  11.041   5.884  1.00 19.95           O  
ANISOU 3074  O   HOH A2119     2196   2760   2623    431   -341    124       O  
HETATM 3075  O   HOH A2120      -6.289  12.129  -0.089  1.00 12.13           O  
ANISOU 3075  O   HOH A2120      608   2208   1793     40    110    -64       O  
HETATM 3076  O   HOH A2121      -5.320  20.455  -5.088  1.00 13.41           O  
ANISOU 3076  O   HOH A2121      712   2338   2045   -148    -15   -168       O  
HETATM 3077  O   HOH A2122       4.274  12.646  -0.016  1.00 27.91           O  
ANISOU 3077  O   HOH A2122     2386   2987   5229    305    313      0       O  
HETATM 3078  O   HOH A2123      -7.546  50.949  -9.481  1.00 35.11           O  
ANISOU 3078  O   HOH A2123     3042   5103   5195    638   1014    445       O  
HETATM 3079  O   HOH A2124     -15.955  51.211  -9.946  1.00 45.21           O  
ANISOU 3079  O   HOH A2124     6482   7117   3578   -489    396   -863       O  
HETATM 3080  O   HOH A2125      -4.754  47.754   4.448  1.00 42.84           O  
ANISOU 3080  O   HOH A2125     3329   6155   6791    425    687   -835       O  
HETATM 3081  O   HOH A2126      -6.219  48.578   0.843  1.00 32.98           O  
ANISOU 3081  O   HOH A2126     2426   4682   5423    229    372      8       O  
HETATM 3082  O   HOH A2127      10.039  12.863  15.575  1.00 42.31           O  
ANISOU 3082  O   HOH A2127     4002   5931   6143    306   -291    446       O  
HETATM 3083  O   HOH A2128       6.755  13.496   6.690  1.00 27.07           O  
ANISOU 3083  O   HOH A2128     3117   3369   3797   -345    409    140       O  
HETATM 3084  O   HOH A2129       1.921  10.755   6.580  1.00 41.97           O  
ANISOU 3084  O   HOH A2129     6626   5246   4075    240   -721   -344       O  
HETATM 3085  O   HOH A2130      21.049  26.022  -2.875  1.00 37.65           O  
ANISOU 3085  O   HOH A2130     1236   6251   6815    571   -438   -996       O  
HETATM 3086  O   HOH A2131      16.714  20.263   3.495  1.00 39.13           O  
ANISOU 3086  O   HOH A2131     2767   7343   4758   -429   -103     -5       O  
HETATM 3087  O   HOH A2132      24.724  23.805  -1.657  1.00 51.06           O  
ANISOU 3087  O   HOH A2132     6006   6664   6728   -218   -317    348       O  
HETATM 3088  O   HOH A2133      11.916  10.917 -14.863  1.00 35.85           O  
ANISOU 3088  O   HOH A2133     3306   4775   5537    848   1148   -848       O  
HETATM 3089  O   HOH A2134       6.017  17.501  17.457  1.00 34.37           O  
ANISOU 3089  O   HOH A2134     4957   4376   3726    341  -1831    318       O  
HETATM 3090  O   HOH A2135       7.186  25.191  17.200  1.00 26.85           O  
ANISOU 3090  O   HOH A2135     2160   4954   3085     67   -777   -460       O  
HETATM 3091  O   HOH A2136       6.666  27.343  13.285  1.00 30.44           O  
ANISOU 3091  O   HOH A2136     1635   4043   5887   -559    -16    306       O  
HETATM 3092  O   HOH A2137       7.073   9.162  -1.314  1.00 38.70           O  
ANISOU 3092  O   HOH A2137     3603   4384   6715    353   1572   -413       O  
HETATM 3093  O   HOH A2138       2.329  28.699  13.602  1.00 14.20           O  
ANISOU 3093  O   HOH A2138      873   2924   1597    -73   -235     36       O  
HETATM 3094  O   HOH A2139       1.364  20.733  19.714  1.00 38.17           O  
ANISOU 3094  O   HOH A2139     4000   5367   5135   -339    -88   -645       O  
HETATM 3095  O   HOH A2140       8.139  22.203  17.710  1.00 33.05           O  
ANISOU 3095  O   HOH A2140     3211   5758   3586    722   -834   -284       O  
HETATM 3096  O   HOH A2141       3.804  18.219  20.293  1.00 51.46           O  
ANISOU 3096  O   HOH A2141     7379   6344   5828    -49   -140   -120       O  
HETATM 3097  O   HOH A2142       2.592  23.044  21.313  1.00 24.89           O  
ANISOU 3097  O   HOH A2142     1762   4363   3332   -292   -644    750       O  
HETATM 3098  O   HOH A2143      14.013  28.832   6.019  1.00 39.28           O  
ANISOU 3098  O   HOH A2143     2492   5936   6495   -729    453   -330       O  
HETATM 3099  O   HOH A2144       4.954  34.748  15.782  1.00 31.28           O  
ANISOU 3099  O   HOH A2144     4144   3823   3915    121  -1191    291       O  
HETATM 3100  O   HOH A2145       6.165  25.763  19.540  1.00 28.02           O  
ANISOU 3100  O   HOH A2145     2599   4521   3523   -246  -1156    -42       O  
HETATM 3101  O   HOH A2146      -7.394  30.678  14.230  1.00 24.86           O  
ANISOU 3101  O   HOH A2146     1741   4272   3432   -598    531    500       O  
HETATM 3102  O   HOH A2147      -3.759  25.040  22.839  1.00 16.76           O  
ANISOU 3102  O   HOH A2147     1443   2770   2155   -156    -79   -182       O  
HETATM 3103  O   HOH A2148       5.943  24.721  23.654  1.00 27.43           O  
ANISOU 3103  O   HOH A2148     2512   4308   3602    857    511   -255       O  
HETATM 3104  O   HOH A2149      -1.748  31.727  23.793  1.00 20.26           O  
ANISOU 3104  O   HOH A2149     1444   3260   2992   -122      0   -102       O  
HETATM 3105  O   HOH A2150       0.516  29.132  25.337  1.00 12.30           O  
ANISOU 3105  O   HOH A2150      356   2691   1625   -247     55   -176       O  
HETATM 3106  O   HOH A2151      -0.525  25.157  24.756  1.00 34.48           O  
ANISOU 3106  O   HOH A2151     3672   5743   3683  -1846     70   -716       O  
HETATM 3107  O   HOH A2152       1.046  30.698  15.022  1.00 14.52           O  
ANISOU 3107  O   HOH A2152      742   2713   2062     71    -22    111       O  
HETATM 3108  O   HOH A2153      -0.506  34.757  21.395  1.00 29.59           O  
ANISOU 3108  O   HOH A2153     5324   3299   2617   -285   -540   -486       O  
HETATM 3109  O   HOH A2154      -3.012  35.112  19.043  1.00 42.36           O  
ANISOU 3109  O   HOH A2154     4140   6015   5939    -80   -661   -561       O  
HETATM 3110  O   HOH A2155      -8.084  31.659  19.986  1.00 39.85           O  
ANISOU 3110  O   HOH A2155     4435   6565   4140     58   -156   -380       O  
HETATM 3111  O   HOH A2156      -6.685  31.981  16.364  1.00 30.91           O  
ANISOU 3111  O   HOH A2156     1020   7463   3260    167    253   -626       O  
HETATM 3112  O   HOH A2157      -5.273  34.837  15.379  1.00 19.29           O  
ANISOU 3112  O   HOH A2157     1247   3655   2427    507    671    -85       O  
HETATM 3113  O   HOH A2158      -1.634  38.232  14.963  1.00 39.67           O  
ANISOU 3113  O   HOH A2158     6287   4424   4361    361  -1756   -791       O  
HETATM 3114  O   HOH A2159       1.656  38.038  14.383  1.00 38.34           O  
ANISOU 3114  O   HOH A2159     4032   4538   5996   -951   1096    948       O  
HETATM 3115  O   HOH A2160      -5.619  35.706   9.431  1.00 20.54           O  
ANISOU 3115  O   HOH A2160     1353   4013   2436   -666    680   -309       O  
HETATM 3116  O   HOH A2161       4.096  30.908  12.849  1.00 25.60           O  
ANISOU 3116  O   HOH A2161     2062   4884   2778    810   -243    232       O  
HETATM 3117  O   HOH A2162       5.462  33.618  11.632  1.00 30.97           O  
ANISOU 3117  O   HOH A2162     2325   4855   4584  -1557    169    303       O  
HETATM 3118  O   HOH A2163       6.153  35.326  13.509  1.00 49.99           O  
ANISOU 3118  O   HOH A2163     6196   6585   6213   -355    546   -263       O  
HETATM 3119  O   HOH A2164       2.665  37.659  12.157  1.00 36.42           O  
ANISOU 3119  O   HOH A2164     4115   4726   4997   -816    452    226       O  
HETATM 3120  O   HOH A2165       7.459  25.719   9.518  1.00 31.24           O  
ANISOU 3120  O   HOH A2165     3839   4852   3175   1101   -292   -104       O  
HETATM 3121  O   HOH A2166       7.704  32.877  10.488  1.00 32.03           O  
ANISOU 3121  O   HOH A2166      704   5855   5611  -1420   -366  -1232       O  
HETATM 3122  O   HOH A2167       9.752  28.964  10.912  1.00 43.22           O  
ANISOU 3122  O   HOH A2167     3623   7030   5767     90    477   -524       O  
HETATM 3123  O   HOH A2168      12.136  33.253   2.833  1.00 18.21           O  
ANISOU 3123  O   HOH A2168      658   3836   2422   -477     85    -77       O  
HETATM 3124  O   HOH A2169      10.901  30.591   0.933  1.00 12.93           O  
ANISOU 3124  O   HOH A2169      264   2620   2028    128     84     55       O  
HETATM 3125  O   HOH A2170       7.762  32.307  -0.511  1.00 11.66           O  
ANISOU 3125  O   HOH A2170      268   2361   1802   -176     -6    -16       O  
HETATM 3126  O   HOH A2171      12.857  28.839   0.233  1.00 15.72           O  
ANISOU 3126  O   HOH A2171      313   3081   2577    193   -333    -56       O  
HETATM 3127  O   HOH A2172       3.081  23.872  -5.320  1.00 12.22           O  
ANISOU 3127  O   HOH A2172      257   2639   1746    -13    -75     -1       O  
HETATM 3128  O   HOH A2173       3.184  15.491  -3.186  1.00 19.64           O  
ANISOU 3128  O   HOH A2173     1643   2912   2906    292    217    119       O  
HETATM 3129  O   HOH A2174       7.414  21.142  -7.210  1.00 14.43           O  
ANISOU 3129  O   HOH A2174      649   2512   2320    -21    146    -53       O  
HETATM 3130  O   HOH A2175       1.751  10.447  -6.848  1.00 19.81           O  
ANISOU 3130  O   HOH A2175     2040   2892   2594   -302   -117    176       O  
HETATM 3131  O   HOH A2176      -1.416  10.938  -6.246  1.00 21.44           O  
ANISOU 3131  O   HOH A2176     1012   4471   2661   -231    542   -478       O  
HETATM 3132  O   HOH A2177       4.091  11.899  -6.182  1.00 16.48           O  
ANISOU 3132  O   HOH A2177     1018   2404   2837    116   -291    194       O  
HETATM 3133  O   HOH A2178      -0.645  15.085 -12.934  1.00 27.34           O  
ANISOU 3133  O   HOH A2178     2226   3651   4509    422     17    269       O  
HETATM 3134  O   HOH A2179       6.804  15.166 -15.732  1.00 23.50           O  
ANISOU 3134  O   HOH A2179     2667   3483   2777    753    696    -96       O  
HETATM 3135  O   HOH A2180      10.509  18.011 -17.792  1.00 38.67           O  
ANISOU 3135  O   HOH A2180     5180   4419   5092   -156    141   -462       O  
HETATM 3136  O   HOH A2181      13.157  17.235 -14.715  1.00 29.59           O  
ANISOU 3136  O   HOH A2181     2930   3264   5050     82   1203   -627       O  
HETATM 3137  O   HOH A2182       9.243  21.304 -17.887  1.00 33.90           O  
ANISOU 3137  O   HOH A2182     5084   4860   2935  -1065    674   -596       O  
HETATM 3138  O   HOH A2183       3.034  24.281 -16.744  1.00 19.61           O  
ANISOU 3138  O   HOH A2183     1814   3085   2551    439     95   -535       O  
HETATM 3139  O   HOH A2184       4.394  21.781 -13.092  1.00 42.84           O  
ANISOU 3139  O   HOH A2184     4000   6664   5611   -496   1311   -940       O  
HETATM 3140  O   HOH A2185       6.429  22.117 -18.944  1.00 33.89           O  
ANISOU 3140  O   HOH A2185     3292   4817   4765    723    389   -719       O  
HETATM 3141  O   HOH A2186      16.631  20.711 -14.812  1.00 38.85           O  
ANISOU 3141  O   HOH A2186     2663   6456   5641   -140    430     94       O  
HETATM 3142  O   HOH A2187      12.545  25.416 -19.760  1.00 43.84           O  
ANISOU 3142  O   HOH A2187     7294   6012   3351   -249    430    493       O  
HETATM 3143  O   HOH A2188      16.644  29.016 -12.986  1.00 17.65           O  
ANISOU 3143  O   HOH A2188      474   3206   3026    -23    773   -521       O  
HETATM 3144  O   HOH A2189      17.064  25.920  -6.215  1.00 23.92           O  
ANISOU 3144  O   HOH A2189     1907   3737   3442    424    -10   -353       O  
HETATM 3145  O   HOH A2190      20.963  28.059 -10.901  1.00 40.66           O  
ANISOU 3145  O   HOH A2190     2504   5798   7146    -46    116    -63       O  
HETATM 3146  O   HOH A2191      13.619  44.391   0.343  1.00 26.21           O  
ANISOU 3146  O   HOH A2191     1858   4970   3130    425   -368   -580       O  
HETATM 3147  O   HOH A2192      14.475  47.135  -1.395  1.00 32.25           O  
ANISOU 3147  O   HOH A2192     4226   3996   4029   -987   -437   -153       O  
HETATM 3148  O   HOH A2193       2.166  48.323  -4.504  1.00 17.73           O  
ANISOU 3148  O   HOH A2193      267   2911   3557    107    176   -155       O  
HETATM 3149  O   HOH A2194      13.448  46.320  -6.181  1.00 24.05           O  
ANISOU 3149  O   HOH A2194      938   4958   3242   -240     77   -189       O  
HETATM 3150  O   HOH A2195       1.055  48.579  -1.918  1.00 23.00           O  
ANISOU 3150  O   HOH A2195     1628   3855   3254   -389   -398    934       O  
HETATM 3151  O   HOH A2196       1.490  53.556  -5.003  1.00 39.23           O  
ANISOU 3151  O   HOH A2196     3162   5816   5924    185   -299    507       O  
HETATM 3152  O   HOH A2197       6.068  56.369  -3.181  1.00 40.17           O  
ANISOU 3152  O   HOH A2197     5180   3473   6607    229   1052   -192       O  
HETATM 3153  O   HOH A2198      -0.366  51.196  -2.328  1.00 40.60           O  
ANISOU 3153  O   HOH A2198     3583   5129   6713    925    994    660       O  
HETATM 3154  O   HOH A2199       8.764  56.945  -4.178  1.00 26.70           O  
ANISOU 3154  O   HOH A2199     3459   3063   3622   -390   -398   -181       O  
HETATM 3155  O   HOH A2200      11.918  49.792  -4.838  1.00 38.98           O  
ANISOU 3155  O   HOH A2200     2757   6920   5133   -511  -1684  -1183       O  
HETATM 3156  O   HOH A2201      11.939  48.557  -1.658  1.00 38.50           O  
ANISOU 3156  O   HOH A2201     2663   5898   6065   -943    222    361       O  
HETATM 3157  O   HOH A2202      13.011  53.777 -10.335  1.00 21.03           O  
ANISOU 3157  O   HOH A2202      498   4041   3450    382    270    248       O  
HETATM 3158  O   HOH A2203       6.267  55.787 -12.277  1.00 35.84           O  
ANISOU 3158  O   HOH A2203     5473   4097   4045   -643    730   1039       O  
HETATM 3159  O   HOH A2204      10.394  52.837 -13.385  1.00 42.68           O  
ANISOU 3159  O   HOH A2204     3802   6111   6303   -324    526   -234       O  
HETATM 3160  O   HOH A2205       7.859  59.436  -5.179  1.00 28.46           O  
ANISOU 3160  O   HOH A2205     2285   4304   4223     57   -704    -49       O  
HETATM 3161  O   HOH A2206       7.515  58.009 -10.181  1.00 40.77           O  
ANISOU 3161  O   HOH A2206     4854   5449   5187   -710   1098      6       O  
HETATM 3162  O   HOH A2207       1.795  57.828  -5.487  1.00 41.14           O  
ANISOU 3162  O   HOH A2207     6114   4062   5452   -309   -411    250       O  
HETATM 3163  O   HOH A2208       1.432  56.617 -11.567  1.00 46.00           O  
ANISOU 3163  O   HOH A2208     5881   5234   6363   -116   -228    639       O  
HETATM 3164  O   HOH A2209      -0.352  56.200  -8.138  1.00 45.07           O  
ANISOU 3164  O   HOH A2209     3969   6391   6762    738    635   -284       O  
HETATM 3165  O   HOH A2210      -3.712  50.222 -11.659  1.00 45.04           O  
ANISOU 3165  O   HOH A2210     4068   7625   5418     16   1645    -78       O  
HETATM 3166  O   HOH A2211      -3.537  53.165  -9.174  1.00 35.45           O  
ANISOU 3166  O   HOH A2211     2554   4897   6017    696    536   -211       O  
HETATM 3167  O   HOH A2212      -6.061  53.037  -4.330  1.00 45.43           O  
ANISOU 3167  O   HOH A2212     5399   4445   7414   2357   1065  -1693       O  
HETATM 3168  O   HOH A2213      -1.164  52.625 -10.919  1.00 20.29           O  
ANISOU 3168  O   HOH A2213      704   3305   3700     75   -412   -164       O  
HETATM 3169  O   HOH A2214      -4.897  44.650 -14.818  1.00 25.90           O  
ANISOU 3169  O   HOH A2214     2077   3850   3913    291   -596    416       O  
HETATM 3170  O   HOH A2215      -9.035  35.339  -9.459  1.00 37.01           O  
ANISOU 3170  O   HOH A2215     3170   6293   4600   1227    178    937       O  
HETATM 3171  O   HOH A2216      -9.349  36.012 -12.021  1.00 29.20           O  
ANISOU 3171  O   HOH A2216     2548   4638   3906   -527    -43    144       O  
HETATM 3172  O   HOH A2217      -7.186  42.196 -11.719  1.00 25.00           O  
ANISOU 3172  O   HOH A2217      938   4227   4331   -157   -343   -197       O  
HETATM 3173  O   HOH A2218      -9.672  40.430 -14.397  1.00 40.86           O  
ANISOU 3173  O   HOH A2218     2562   5962   7001    708    -90    705       O  
HETATM 3174  O   HOH A2219      -7.247  43.421 -15.430  1.00 37.53           O  
ANISOU 3174  O   HOH A2219     2920   5336   6004   -123    124    848       O  
HETATM 3175  O   HOH A2220      -5.070  37.015 -14.906  1.00 19.06           O  
ANISOU 3175  O   HOH A2220     2407   2565   2268    -41     86     25       O  
HETATM 3176  O   HOH A2221      -8.589  37.220 -14.062  1.00 29.82           O  
ANISOU 3176  O   HOH A2221     2197   4835   4297   -508   -237    419       O  
HETATM 3177  O   HOH A2222      -1.168  46.802 -16.077  1.00 17.21           O  
ANISOU 3177  O   HOH A2222     1216   2784   2536   -286   -161    139       O  
HETATM 3178  O   HOH A2223      -3.826  46.844 -13.894  1.00 34.08           O  
ANISOU 3178  O   HOH A2223     2297   5176   5473    803    141    736       O  
HETATM 3179  O   HOH A2224      -2.832  43.479 -16.405  1.00 25.23           O  
ANISOU 3179  O   HOH A2224     2987   3632   2966   -807   -807    224       O  
HETATM 3180  O   HOH A2225       1.871  35.857 -23.353  1.00 31.71           O  
ANISOU 3180  O   HOH A2225     5223   4231   2592  -1484    -87   -427       O  
HETATM 3181  O   HOH A2226       4.099  40.228 -22.980  1.00 35.84           O  
ANISOU 3181  O   HOH A2226     5186   4502   3929   -249    844    773       O  
HETATM 3182  O   HOH A2227      -2.001  29.592 -14.526  1.00 11.54           O  
ANISOU 3182  O   HOH A2227      287   2398   1700    127   -192     44       O  
HETATM 3183  O   HOH A2228       0.885  29.888 -12.497  1.00 11.43           O  
ANISOU 3183  O   HOH A2228      261   2421   1658    130     35     75       O  
HETATM 3184  O   HOH A2229      15.402  36.918 -19.229  1.00 41.52           O  
ANISOU 3184  O   HOH A2229     5554   6607   3614    126    798   -422       O  
HETATM 3185  O   HOH A2230      12.999  36.222 -11.025  1.00 13.22           O  
ANISOU 3185  O   HOH A2230      294   2784   1945    -84    253     19       O  
HETATM 3186  O   HOH A2231      14.173  28.677 -20.344  1.00 30.50           O  
ANISOU 3186  O   HOH A2231     3177   5924   2488   -270   1414   -432       O  
HETATM 3187  O   HOH A2232      17.349  46.448 -13.777  1.00 40.37           O  
ANISOU 3187  O   HOH A2232     4341   4905   6090   -788     -3     55       O  
HETATM 3188  O   HOH A2233      14.421  45.031  -8.267  1.00 18.14           O  
ANISOU 3188  O   HOH A2233      376   3578   2936   -633      5   -454       O  
HETATM 3189  O   HOH A2234      14.479  43.474 -18.510  1.00 25.59           O  
ANISOU 3189  O   HOH A2234     1356   5076   3291   -474   1137    -34       O  
HETATM 3190  O   HOH A2235      11.824  45.547 -18.042  1.00 22.62           O  
ANISOU 3190  O   HOH A2235     1341   4452   2801   -757    635    339       O  
HETATM 3191  O   HOH A2236      17.805  40.243 -14.097  1.00 31.26           O  
ANISOU 3191  O   HOH A2236     2081   4429   5367   -176    190   -358       O  
HETATM 3192  O   HOH A2237       9.219  51.726 -17.968  1.00 29.26           O  
ANISOU 3192  O   HOH A2237     2131   3434   5553   -448    433    617       O  
HETATM 3193  O   HOH A2238      12.665  52.881 -13.306  1.00 35.37           O  
ANISOU 3193  O   HOH A2238     3037   4982   5419  -1556   -718   -458       O  
HETATM 3194  O   HOH A2239      13.801  47.366 -17.612  1.00 40.08           O  
ANISOU 3194  O   HOH A2239     4286   5148   5791   -743   1587    -34       O  
HETATM 3195  O   HOH A2240      14.308  53.401 -16.265  1.00 56.11           O  
ANISOU 3195  O   HOH A2240     6743   7725   6849   -327    492    -12       O  
HETATM 3196  O   HOH A2241       2.617  54.003 -17.941  1.00 22.82           O  
ANISOU 3196  O   HOH A2241     2092   3024   3554    -18     81    526       O  
HETATM 3197  O   HOH A2242      11.947  50.801 -19.123  1.00 49.54           O  
ANISOU 3197  O   HOH A2242     6596   6599   5628   -679    907    139       O  
HETATM 3198  O   HOH A2243       3.532  42.667 -22.755  1.00 37.67           O  
ANISOU 3198  O   HOH A2243     5096   4723   4494   -917    269   -501       O  
HETATM 3199  O   HOH A2244       5.123  47.710 -24.251  1.00 27.15           O  
ANISOU 3199  O   HOH A2244     3329   3804   3183   -510    840    598       O  
HETATM 3200  O   HOH A2245      -3.075  51.700 -19.896  1.00 40.48           O  
ANISOU 3200  O   HOH A2245     3737   5625   6018   -184   -367    859       O  
HETATM 3201  O   HOH A2246      -0.098  53.384 -14.276  1.00 22.29           O  
ANISOU 3201  O   HOH A2246     2027   2974   3465     18    140    446       O  
HETATM 3202  O   HOH A2247       0.140  54.739 -18.602  1.00 29.42           O  
ANISOU 3202  O   HOH A2247     2863   3823   4490   -113     -9    474       O  
HETATM 3203  O   HOH A2248      -3.794  50.526 -15.698  1.00 43.11           O  
ANISOU 3203  O   HOH A2248     2924   6533   6921    616    371    548       O  
HETATM 3204  O   HOH A2249       7.471  51.183 -26.369  1.00 43.47           O  
ANISOU 3204  O   HOH A2249     4790   6282   5443  -1171    396   1773       O  
HETATM 3205  O   HOH A2250       5.255  52.352 -28.574  1.00 30.16           O  
ANISOU 3205  O   HOH A2250     2961   4764   3733   -203    534   1384       O  
HETATM 3206  O   HOH A2251       4.196  54.942 -25.940  1.00 53.86           O  
ANISOU 3206  O   HOH A2251     7312   6118   7032   -325    -86   -450       O  
HETATM 3207  O   HOH A2252      -2.854  48.936 -19.653  1.00 34.98           O  
ANISOU 3207  O   HOH A2252     3294   4313   5684   -288   -833    392       O  
HETATM 3208  O   HOH A2253      -0.209  46.007 -18.477  1.00 24.32           O  
ANISOU 3208  O   HOH A2253     1658   4741   2841    789     10    917       O  
HETATM 3209  O   HOH A2254      -3.596  47.739 -16.683  1.00 38.06           O  
ANISOU 3209  O   HOH A2254     2527   5295   6636   1088   -742    939       O  
HETATM 3210  O   HOH A2255      -4.138  45.028 -24.320  1.00 38.41           O  
ANISOU 3210  O   HOH A2255     4517   5554   4520   -810  -1609    226       O  
HETATM 3211  O   HOH A2256      -3.790  38.874 -21.983  1.00 34.46           O  
ANISOU 3211  O   HOH A2256     5114   4883   3094  -2061   -510    231       O  
HETATM 3212  O   HOH A2257      -3.655  34.471 -21.506  1.00 27.01           O  
ANISOU 3212  O   HOH A2257     2210   4699   3353   -619   -420    962       O  
HETATM 3213  O   HOH A2258      -9.771  30.711 -22.123  1.00 30.49           O  
ANISOU 3213  O   HOH A2258     2779   4881   3923   1076   -857   -318       O  
HETATM 3214  O   HOH A2259     -11.956  22.517 -23.307  1.00 33.82           O  
ANISOU 3214  O   HOH A2259     3821   4621   4405   -871   1146   -835       O  
HETATM 3215  O   HOH A2260     -13.729  24.573 -20.328  1.00 24.14           O  
ANISOU 3215  O   HOH A2260     1352   4875   2945   -450    -72     63       O  
HETATM 3216  O   HOH A2261     -10.686  29.683 -24.728  1.00 39.05           O  
ANISOU 3216  O   HOH A2261     4517   4504   5816    100  -1940    463       O  
HETATM 3217  O   HOH A2262      -5.362  20.944 -19.654  1.00 29.93           O  
ANISOU 3217  O   HOH A2262     2974   4864   3531   -496    539   -178       O  
HETATM 3218  O   HOH A2263     -14.615  30.441 -16.240  1.00 28.76           O  
ANISOU 3218  O   HOH A2263     2060   4024   4843    273   -543    530       O  
HETATM 3219  O   HOH A2264     -14.272  27.315 -21.723  1.00 45.49           O  
ANISOU 3219  O   HOH A2264     4191   7018   6073   -260   -431    309       O  
HETATM 3220  O   HOH A2265     -11.253  24.309 -17.088  1.00 16.90           O  
ANISOU 3220  O   HOH A2265     1378   2816   2225   -221   -157    301       O  
HETATM 3221  O   HOH A2266     -13.475  34.719 -15.864  1.00 35.03           O  
ANISOU 3221  O   HOH A2266     3377   4771   5160   1592   -688    220       O  
HETATM 3222  O   HOH A2267     -11.850  31.466 -18.942  1.00 38.02           O  
ANISOU 3222  O   HOH A2267     5137   4718   4590    947     16    759       O  
HETATM 3223  O   HOH A2268      -5.861  26.535 -10.484  1.00 11.57           O  
ANISOU 3223  O   HOH A2268      365   2414   1617    114     54    -37       O  
HETATM 3224  O   HOH A2269     -13.895  29.274 -13.324  1.00 21.12           O  
ANISOU 3224  O   HOH A2269      342   4616   3064    624    -25   -117       O  
HETATM 3225  O   HOH A2270      -2.403  23.438 -19.453  1.00 29.18           O  
ANISOU 3225  O   HOH A2270     3457   5072   2559   1886   1462   1038       O  
HETATM 3226  O   HOH A2271      -8.788  30.313 -18.897  1.00 14.82           O  
ANISOU 3226  O   HOH A2271      640   2713   2276    -24   -392    102       O  
HETATM 3227  O   HOH A2272     -10.170  31.540 -10.017  1.00 32.22           O  
ANISOU 3227  O   HOH A2272     3679   4374   4189   1251    185   -431       O  
HETATM 3228  O   HOH A2273     -10.275  39.726  -1.556  1.00 35.58           O  
ANISOU 3228  O   HOH A2273     1199   5041   7277    575    826   -110       O  
HETATM 3229  O   HOH A2274      -4.935  26.722  -5.642  1.00 10.89           O  
ANISOU 3229  O   HOH A2274      290   2157   1691     92   -210     94       O  
HETATM 3230  O   HOH A2275      -7.398  30.444  -0.198  1.00 14.60           O  
ANISOU 3230  O   HOH A2275      505   2888   2152     60     77   -109       O  
HETATM 3231  O   HOH A2276      -4.803  26.966  -1.822  1.00 11.72           O  
ANISOU 3231  O   HOH A2276      253   2404   1795     12     -5    -80       O  
HETATM 3232  O   HOH A2277      -8.011  36.527   3.493  1.00 33.02           O  
ANISOU 3232  O   HOH A2277     2542   3898   6104  -1246  -1588   1443       O  
HETATM 3233  O   HOH A2278      -9.167  37.069  -0.168  1.00 24.89           O  
ANISOU 3233  O   HOH A2278     1305   4070   4080   -133    849   -369       O  
HETATM 3234  O   HOH A2279      -2.722  45.252  10.486  1.00 28.03           O  
ANISOU 3234  O   HOH A2279     2579   5202   2869   -656    578    -89       O  
HETATM 3235  O   HOH A2280      -6.754  39.415   9.623  1.00 38.73           O  
ANISOU 3235  O   HOH A2280     3495   5729   5491   -267    534    208       O  
HETATM 3236  O   HOH A2281      -5.615  39.859  12.724  1.00 46.95           O  
ANISOU 3236  O   HOH A2281     4856   6290   6690   2113    642   -745       O  
HETATM 3237  O   HOH A2282      -5.282  43.765   9.621  1.00 40.90           O  
ANISOU 3237  O   HOH A2282     4858   4423   6258    310    192    168       O  
HETATM 3238  O   HOH A2283     -10.205  41.123   0.559  1.00 32.76           O  
ANISOU 3238  O   HOH A2283     2364   4999   5084  -1091    364   2078       O  
HETATM 3239  O   HOH A2284     -10.856  39.044   2.985  1.00 40.24           O  
ANISOU 3239  O   HOH A2284     5365   5302   4620   -731   -918   -188       O  
HETATM 3240  O   HOH A2285      -5.177  41.797   5.320  1.00 33.24           O  
ANISOU 3240  O   HOH A2285     3643   5430   3557    567    363    324       O  
HETATM 3241  O   HOH A2286     -10.670  45.191   1.304  1.00 20.99           O  
ANISOU 3241  O   HOH A2286     1102   3865   3007   -313     63   -451       O  
HETATM 3242  O   HOH A2287      -5.967  40.081   6.540  1.00 31.47           O  
ANISOU 3242  O   HOH A2287     2699   5235   4022    489     51   -769       O  
HETATM 3243  O   HOH A2288      -7.237  37.915   6.754  1.00 45.48           O  
ANISOU 3243  O   HOH A2288     4350   4889   8039   1346   1179   -570       O  
HETATM 3244  O   HOH A2289      -5.377  45.216   5.913  1.00 39.88           O  
ANISOU 3244  O   HOH A2289     3668   6375   5109     65     15   -957       O  
HETATM 3245  O   HOH A2290      -6.525  46.868  -1.336  1.00 23.47           O  
ANISOU 3245  O   HOH A2290      959   3567   4391   -298  -1231     -8       O  
HETATM 3246  O   HOH A2291      -8.513  50.287  -4.422  1.00 25.79           O  
ANISOU 3246  O   HOH A2291     1892   4099   3806     26    925    542       O  
HETATM 3247  O   HOH A2292      -7.838  46.334 -11.870  1.00 42.70           O  
ANISOU 3247  O   HOH A2292     2785   7996   5442   1201   -144    653       O  
HETATM 3248  O   HOH A2293     -12.872  51.821  -8.821  1.00 33.23           O  
ANISOU 3248  O   HOH A2293     1472   5101   6051   1028    783    553       O  
HETATM 3249  O   HOH A2294      -9.015  51.061  -7.035  1.00 30.24           O  
ANISOU 3249  O   HOH A2294     1952   4973   4562    663    179    446       O  
HETATM 3250  O   HOH A2295      -0.043  47.591  -5.790  1.00 18.06           O  
ANISOU 3250  O   HOH A2295      415   3898   2549   -467    344    314       O  
HETATM 3251  O   HOH A2296      -0.816  50.306   0.397  1.00 26.61           O  
ANISOU 3251  O   HOH A2296     1759   3455   4897   -717  -1070     33       O  
HETATM 3252  O   HOH A2297      -3.455  48.437   2.272  1.00 48.41           O  
ANISOU 3252  O   HOH A2297     3048   8757   6588   -329   1057    -86       O  
HETATM 3253  O   HOH A2298      -3.364  49.536   5.740  1.00 31.74           O  
ANISOU 3253  O   HOH A2298     2258   4351   5448   -885   1279    -75       O  
HETATM 3254  O   HOH A2299      -1.220  50.494   4.490  1.00 26.28           O  
ANISOU 3254  O   HOH A2299     2121   3444   4418    157    558    440       O  
HETATM 3255  O   HOH A2300       3.341  51.177  10.707  1.00 41.23           O  
ANISOU 3255  O   HOH A2300     4288   4881   6495  -1232    428    -59       O  
HETATM 3256  O   HOH A2301       7.254  51.424   0.097  1.00 33.22           O  
ANISOU 3256  O   HOH A2301     2330   4394   5898   -450    455    861       O  
HETATM 3257  O   HOH A2302      -0.649  40.517  11.903  1.00 31.20           O  
ANISOU 3257  O   HOH A2302     4082   4186   3587   -168    132   -384       O  
HETATM 3258  O   HOH A2303       4.985  43.903  11.007  1.00 24.58           O  
ANISOU 3258  O   HOH A2303     1890   4827   2622   -232    369    -32       O  
HETATM 3259  O   HOH A2304       5.095  47.000  11.332  1.00 28.18           O  
ANISOU 3259  O   HOH A2304     2649   5628   2427    161    146   -549       O  
HETATM 3260  O   HOH A2305      10.798  40.245  12.135  1.00 45.78           O  
ANISOU 3260  O   HOH A2305     6362   6466   4565   -840  -1101    193       O  
HETATM 3261  O   HOH A2306      10.950  37.639  12.145  1.00 43.19           O  
ANISOU 3261  O   HOH A2306     4619   7483   4307     93    109   -465       O  
HETATM 3262  O   HOH A2307      11.431  49.059   1.774  1.00 32.75           O  
ANISOU 3262  O   HOH A2307     2255   5266   4921   -658   -800   1178       O  
HETATM 3263  O   HOH A2308      13.047  46.025   2.634  1.00 28.06           O  
ANISOU 3263  O   HOH A2308     2616   4749   3294   -260   -128   -573       O  
HETATM 3264  O   HOH A2309      18.207  43.106   6.709  1.00 29.75           O  
ANISOU 3264  O   HOH A2309     2850   4218   4237    -42    378    332       O  
HETATM 3265  O   HOH A2310      14.436  43.364   8.006  1.00 36.96           O  
ANISOU 3265  O   HOH A2310     4353   4563   5127    750    -97   -230       O  
HETATM 3266  O   HOH A2311      16.007  44.071  -0.801  1.00 30.42           O  
ANISOU 3266  O   HOH A2311     1996   4625   4935   -233     85    -62       O  
HETATM 3267  O   HOH A2312      13.617  34.025  -4.481  1.00 13.01           O  
ANISOU 3267  O   HOH A2312      262   2595   2085   -110     88    -54       O  
HETATM 3268  O   HOH A2313      19.761  31.575   0.554  1.00 34.86           O  
ANISOU 3268  O   HOH A2313     2595   4827   5820    554   -692    192       O  
HETATM 3269  O   HOH A2314      18.226  26.062  -3.741  1.00 23.04           O  
ANISOU 3269  O   HOH A2314     1461   3733   3561    260    521   -203       O  
HETATM 3270  O   HOH A2315      19.272  28.543  -0.416  1.00 37.08           O  
ANISOU 3270  O   HOH A2315      636   7224   6227  -1165   -563    551       O  
HETATM 3271  O   HOH A2316      16.773  31.679   4.296  1.00 34.97           O  
ANISOU 3271  O   HOH A2316     4531   5105   3648   -817   1888    224       O  
HETATM 3272  O   HOH A2317      19.990  25.785   1.497  1.00 51.88           O  
ANISOU 3272  O   HOH A2317     4096   7700   7915    761     52   -468       O  
HETATM 3273  O   HOH A2318      15.052  24.209  -5.200  1.00 18.49           O  
ANISOU 3273  O   HOH A2318     1303   3228   2493   1056    -92     57       O  
HETATM 3274  O   HOH A2319      19.814  24.456  -6.902  1.00 34.47           O  
ANISOU 3274  O   HOH A2319     1752   4759   6585    299    384   -634       O  
HETATM 3275  O   HOH A2320      22.040  24.211  -1.780  1.00 52.49           O  
ANISOU 3275  O   HOH A2320     6997   6374   6572   -266   -238     16       O  
HETATM 3276  O   HOH A2321      17.998  21.508   0.627  1.00 21.94           O  
ANISOU 3276  O   HOH A2321      843   3554   3938    838  -1058    437       O  
HETATM 3277  O   HOH A2322      20.804  21.708   0.468  1.00 51.90           O  
ANISOU 3277  O   HOH A2322     4919   8110   6690   -348  -1762    256       O  
HETATM 3278  O   HOH A2323      22.983  15.281  -4.266  1.00 45.77           O  
ANISOU 3278  O   HOH A2323     4383   5713   7291    940   -661    215       O  
HETATM 3279  O   HOH A2324      17.567  18.714   1.342  1.00 37.48           O  
ANISOU 3279  O   HOH A2324     2842   4939   6458    169   -539    -95       O  
HETATM 3280  O   HOH A2325      16.753  17.281  -9.132  1.00 44.18           O  
ANISOU 3280  O   HOH A2325     5202   3942   7642    339   -604    107       O  
HETATM 3281  O   HOH A2326      16.241  14.196 -11.825  1.00 38.33           O  
ANISOU 3281  O   HOH A2326     3288   5675   5599   -969   1092   -173       O  
HETATM 3282  O   HOH A2327      10.812   9.515 -12.656  1.00 33.20           O  
ANISOU 3282  O   HOH A2327     3707   3465   5439    821    325   -389       O  
HETATM 3283  O   HOH A2328      13.569   4.526 -11.323  1.00 47.07           O  
ANISOU 3283  O   HOH A2328     5031   5852   6999   -740   -749     31       O  
HETATM 3284  O   HOH A2329      10.357   5.285  -5.169  1.00 33.14           O  
ANISOU 3284  O   HOH A2329     2884   3673   6031    504    475     37       O  
HETATM 3285  O   HOH A2330      16.718   3.701  -8.218  1.00 42.33           O  
ANISOU 3285  O   HOH A2330     6303   3733   6044    709   -355   -107       O  
HETATM 3286  O   HOH A2331      16.931   3.927  -5.248  1.00 40.31           O  
ANISOU 3286  O   HOH A2331     5120   4127   6066   1632  -1048    -24       O  
HETATM 3287  O   HOH A2332      15.069   7.282   0.807  1.00 41.13           O  
ANISOU 3287  O   HOH A2332     4511   5139   5976    993   -928    128       O  
HETATM 3288  O   HOH A2333      13.683   2.855  -2.520  1.00 45.41           O  
ANISOU 3288  O   HOH A2333     4459   6217   6576    109   -260    142       O  
HETATM 3289  O   HOH A2334      18.038   9.305  -1.098  1.00 38.16           O  
ANISOU 3289  O   HOH A2334     3269   5531   5698    923    275     66       O  
HETATM 3290  O   HOH A2335       8.511   9.958   0.957  1.00 28.72           O  
ANISOU 3290  O   HOH A2335     2556   3533   4821    688    626    540       O  
HETATM 3291  O   HOH A2336       6.117  16.239   1.642  1.00 22.45           O  
ANISOU 3291  O   HOH A2336     1780   3324   3423    319   -650    101       O  
HETATM 3292  O   HOH A2337       9.379  14.495   7.086  1.00 21.91           O  
ANISOU 3292  O   HOH A2337     1259   3875   3191    531    146    420       O  
HETATM 3293  O   HOH A2338      14.984  15.603   6.478  1.00 46.11           O  
ANISOU 3293  O   HOH A2338     5347   7142   5029   1613    165    412       O  
HETATM 3294  O   HOH A2339      14.866  19.023   5.058  1.00 34.80           O  
ANISOU 3294  O   HOH A2339     3095   4715   5411    217   -137   -565       O  
HETATM 3295  O   HOH A2340       4.235  20.097   2.541  1.00 13.31           O  
ANISOU 3295  O   HOH A2340      289   2575   2191     12    -75    102       O  
HETATM 3296  O   HOH A2341      12.581  15.331  13.251  1.00 52.07           O  
ANISOU 3296  O   HOH A2341     5729   7275   6777   -571    125    133       O  
HETATM 3297  O   HOH A2342      13.305  22.458   9.290  1.00 36.70           O  
ANISOU 3297  O   HOH A2342     4322   5507   4114   -231    532   -173       O  
HETATM 3298  O   HOH A2343      12.759  29.549   4.121  1.00 28.27           O  
ANISOU 3298  O   HOH A2343     1714   4726   4301   -166   -375   -483       O  
HETATM 3299  O   HOH A2344      12.782  25.067   8.049  1.00 32.92           O  
ANISOU 3299  O   HOH A2344     2739   5886   3883   -841   -469   -684       O  
HETATM 3300  O   HOH A2345       8.763  19.648  15.324  1.00 38.88           O  
ANISOU 3300  O   HOH A2345     4924   5999   3849   -404   -493    -94       O  
HETATM 3301  O   HOH A2346       8.227  25.517  12.030  1.00 33.70           O  
ANISOU 3301  O   HOH A2346     3925   4062   4816    868  -1772   -156       O  
HETATM 3302  O   HOH A2347       9.802  21.776  14.973  1.00 32.58           O  
ANISOU 3302  O   HOH A2347     2962   6137   3279    800   -258    -94       O  
HETATM 3303  O   HOH L2001     -12.994  18.193 -19.363  1.00 41.08           O  
ANISOU 3303  O   HOH L2001     4889   5757   4961   1334    250   -164       O  
HETATM 3304  O   HOH L2002       1.395   8.939  -3.154  1.00 30.61           O  
ANISOU 3304  O   HOH L2002     2467   4718   4445   1283    290   -559       O  
HETATM 3305  O   HOH L2003       0.792   3.953  -1.017  1.00 42.76           O  
ANISOU 3305  O   HOH L2003     3837   6196   6212    523   -526    232       O  
HETATM 3306  O   HOH L2004     -10.186   4.069  -1.787  1.00 45.93           O  
ANISOU 3306  O   HOH L2004     5125   6642   5683   -417    294    989       O  
HETATM 3307  O   HOH L2005       2.427  10.817  -2.095  1.00 30.49           O  
ANISOU 3307  O   HOH L2005     2255   5126   4201    255   1005   -554       O  
HETATM 3308  O   HOH L2006       2.315  15.258   4.011  1.00 33.89           O  
ANISOU 3308  O   HOH L2006     2714   5838   4322   -920   -374    754       O  
HETATM 3309  O   HOH L2007      -2.044   6.224   5.232  1.00 42.23           O  
ANISOU 3309  O   HOH L2007     5372   5651   5021    553    -83   1485       O  
HETATM 3310  O   HOH L2008     -11.823  20.895 -19.455  1.00 42.58           O  
ANISOU 3310  O   HOH L2008     5748   6099   4329    489    293     90       O  
HETATM 3311  O   HOH L2009      -4.671  18.990 -18.452  1.00 40.90           O  
ANISOU 3311  O   HOH L2009     4452   6144   4944   -205   -814    361       O  
HETATM 3312  O   HOH L2010     -17.504  23.878 -15.569  1.00 26.73           O  
ANISOU 3312  O   HOH L2010     2245   4728   3181    250   -554    -88       O  
HETATM 3313  O   HOH L2011     -25.014  24.627 -13.662  1.00 43.10           O  
ANISOU 3313  O   HOH L2011     4251   6477   5647    602   -714     99       O  
HETATM 3314  O   HOH L2012     -22.461  20.751  -5.115  1.00 41.13           O  
ANISOU 3314  O   HOH L2012     3439   5386   6801    359  -1029    483       O  
HETATM 3315  O   HOH L2013     -20.415  21.398  -1.635  1.00 32.12           O  
ANISOU 3315  O   HOH L2013     2306   4130   5767    208     48   -144       O  
HETATM 3316  O   HOH L2014      -1.697   0.866 -12.800  1.00 42.76           O  
ANISOU 3316  O   HOH L2014     5255   5977   5012   -582   -160   -122       O  
HETATM 3317  O   HOH L2015      -4.001  -1.201 -13.076  1.00 39.42           O  
ANISOU 3317  O   HOH L2015     5727   4860   4389   1239    652    -53       O  
HETATM 3318  O   HOH L2016      -1.292   0.449  -2.030  1.00 31.55           O  
ANISOU 3318  O   HOH L2016     4212   3547   4225    484     50    391       O  
HETATM 3319  O   HOH L2017      -5.181   2.726 -11.357  1.00 28.91           O  
ANISOU 3319  O   HOH L2017     2775   3615   4593   -578  -2043   -256       O  
HETATM 3320  O   HOH L2018      -7.017   1.701  -9.242  1.00 37.37           O  
ANISOU 3320  O   HOH L2018     3135   4838   6224   -269  -1361   -256       O  
HETATM 3321  O   HOH L2019      -9.113   1.609  -4.749  1.00 33.99           O  
ANISOU 3321  O   HOH L2019     2386   4003   6525   -118   -195    359       O  
HETATM 3322  O   HOH L2020      -1.164   2.941  -3.176  1.00 22.47           O  
ANISOU 3322  O   HOH L2020     1862   2869   3805    462   -407   -332       O  
HETATM 3323  O   HOH L2021      -0.175   6.014  -3.214  1.00 23.14           O  
ANISOU 3323  O   HOH L2021     1910   3498   3382     73    489    -11       O  
HETATM 3324  O   HOH L2022      -8.657   3.392   2.171  1.00 36.55           O  
ANISOU 3324  O   HOH L2022     3480   6229   4177     97   1079    810       O  
HETATM 3325  O   HOH L2023      -8.766   4.485  -8.016  1.00 37.05           O  
ANISOU 3325  O   HOH L2023     4010   5149   4918   -926   -990   -650       O  
HETATM 3326  O   HOH L2024      -7.656   5.529  -0.842  1.00 21.74           O  
ANISOU 3326  O   HOH L2024     1771   3376   3113   -214    328    142       O  
HETATM 3327  O   HOH L2025      -0.369   8.617  -5.276  1.00 26.92           O  
ANISOU 3327  O   HOH L2025     2738   3788   3700   -952   -349   -317       O  
HETATM 3328  O   HOH L2026      -8.573   7.845  -2.240  1.00 18.02           O  
ANISOU 3328  O   HOH L2026     1130   2784   2933   -200     25     61       O  
HETATM 3329  O   HOH L2027      -2.976   8.845   4.443  1.00 28.59           O  
ANISOU 3329  O   HOH L2027     4917   3360   2583   -420    288    207       O  
HETATM 3330  O   HOH L2028      -5.775   9.514   0.603  1.00 16.85           O  
ANISOU 3330  O   HOH L2028     1264   2342   2794   -179    260   -100       O  
HETATM 3331  O   HOH L2029       0.596  10.481   2.503  1.00 22.46           O  
ANISOU 3331  O   HOH L2029     2028   2843   3660    165   -713   -365       O  
HETATM 3332  O   HOH L2030       0.072  12.766  -5.009  1.00 22.03           O  
ANISOU 3332  O   HOH L2030     1425   3050   3894    340    206   -817       O  
HETATM 3333  O   HOH L2031      -0.027  14.518   2.687  1.00 13.70           O  
ANISOU 3333  O   HOH L2031      311   2665   2229    154    -31     48       O  
HETATM 3334  O   HOH L2032       1.498  11.940   0.209  1.00 18.75           O  
ANISOU 3334  O   HOH L2032      998   2905   3217    582   -264   -717       O  
HETATM 3335  O   HOH L2033      -4.770  15.224 -12.627  1.00 20.26           O  
ANISOU 3335  O   HOH L2033     1419   3205   3075    -42    199   -301       O  
HETATM 3336  O   HOH L2034       1.593  20.863  -9.409  1.00 23.16           O  
ANISOU 3336  O   HOH L2034     1846   3356   3596    -64    888    215       O  
HETATM 3337  O   HOH L2035      -7.495  15.386 -12.096  1.00 14.81           O  
ANISOU 3337  O   HOH L2035      876   2729   2020    -72   -167   -241       O  
HETATM 3338  O   HOH L2036      -3.693  20.624  -7.141  1.00 14.32           O  
ANISOU 3338  O   HOH L2036      518   2636   2286     92   -183    -37       O  
HETATM 3339  O   HOH L2037      -4.839  22.465 -10.658  1.00 13.66           O  
ANISOU 3339  O   HOH L2037      865   2480   1844    -98    117     10       O  
HETATM 3340  O   HOH L2038      -2.948  20.522 -16.490  1.00 34.19           O  
ANISOU 3340  O   HOH L2038     6347   3863   2780   1719   1942    565       O  
HETATM 3341  O   HOH L2039      -3.980  16.600 -15.036  1.00 32.90           O  
ANISOU 3341  O   HOH L2039     5174   3491   3836    494   1232    -23       O  
HETATM 3342  O   HOH L2040     -11.412  17.598 -12.159  1.00 18.36           O  
ANISOU 3342  O   HOH L2040      342   3594   3039   -201   -155    204       O  
HETATM 3343  O   HOH L2041     -16.012  17.554 -11.944  1.00 32.89           O  
ANISOU 3343  O   HOH L2041     4515   4862   3118  -2392   -532   -443       O  
HETATM 3344  O   HOH L2042      -9.761  24.318 -12.672  1.00 11.64           O  
ANISOU 3344  O   HOH L2042      324   2284   1814   -116   -187    -69       O  
HETATM 3345  O   HOH L2043      -7.566  18.800 -17.016  1.00 34.92           O  
ANISOU 3345  O   HOH L2043     5064   5039   3163   2380     18   -779       O  
HETATM 3346  O   HOH L2044     -19.271  21.581  -8.339  1.00 21.41           O  
ANISOU 3346  O   HOH L2044      374   4185   3574   -690   -184    992       O  
HETATM 3347  O   HOH L2045     -13.236  22.897 -18.346  1.00 31.01           O  
ANISOU 3347  O   HOH L2045     3274   4398   4108   -723  -1403    264       O  
HETATM 3348  O   HOH L2046     -25.391  20.251 -13.268  1.00 43.84           O  
ANISOU 3348  O   HOH L2046     3293   6174   7189   -748   -187   -419       O  
HETATM 3349  O   HOH L2047     -22.174  25.041 -14.199  1.00 41.23           O  
ANISOU 3349  O   HOH L2047     5339   6135   4191   -599  -1131   -228       O  
HETATM 3350  O   HOH L2048     -19.452  23.707  -4.683  1.00 32.18           O  
ANISOU 3350  O   HOH L2048     2272   5647   4308    400    392    563       O  
HETATM 3351  O   HOH L2049     -17.579  26.227 -14.357  1.00 31.29           O  
ANISOU 3351  O   HOH L2049     4207   4629   3051   -350   -793   -158       O  
HETATM 3352  O   HOH L2050     -16.014  27.907 -12.937  1.00 23.20           O  
ANISOU 3352  O   HOH L2050     2238   3651   2926    140   -278     73       O  
HETATM 3353  O   HOH L2051     -27.430  27.032  -7.928  1.00 41.49           O  
ANISOU 3353  O   HOH L2051     4508   5705   5551    528  -1542    -35       O  
HETATM 3354  O   HOH L2052     -21.149  23.186  -6.626  1.00 36.67           O  
ANISOU 3354  O   HOH L2052     3254   5758   4918   1215   -653   -335       O  
HETATM 3355  O   HOH L2053     -22.243  23.008  -2.366  1.00 40.05           O  
ANISOU 3355  O   HOH L2053     4634   4712   5869     69   -463    701       O  
HETATM 3356  O   HOH L2054     -19.671  28.231  -1.668  1.00 40.88           O  
ANISOU 3356  O   HOH L2054     5272   4541   5718    197    652    114       O  
HETATM 3357  O   HOH L2055     -20.856  25.640  -2.991  1.00 25.34           O  
ANISOU 3357  O   HOH L2055      731   3583   5312    -57   -311   -200       O  
HETATM 3358  O   HOH L2056     -19.309  31.852  -2.431  1.00 36.07           O  
ANISOU 3358  O   HOH L2056     2556   6526   4623   -528    379   -688       O  
HETATM 3359  O   HOH L2057     -26.474  29.587  -7.129  1.00 36.79           O  
ANISOU 3359  O   HOH L2057     2958   4407   6612      5  -1541    -79       O  
HETATM 3360  O   HOH M2001     -14.189  15.654 -15.053  1.00 39.98           O  
ANISOU 3360  O   HOH M2001     5338   4544   5307    139   -965   1320       O  
HETATM 3361  O   HOH M2002     -18.350  23.234  -1.228  1.00 23.47           O  
ANISOU 3361  O   HOH M2002     1066   4388   3460    -56    112   -320       O  
HETATM 3362  O   HOH M2003     -10.408  31.711  -7.163  1.00 21.76           O  
ANISOU 3362  O   HOH M2003     1032   4318   2918    434    215   -353       O  
HETATM 3363  O   HOH M2004     -19.418   8.611  -2.636  1.00 35.23           O  
ANISOU 3363  O   HOH M2004     2931   4845   5610   -134  -1050   -783       O  
HETATM 3364  O   HOH M2005     -16.004   5.662  -3.821  1.00 42.73           O  
ANISOU 3364  O   HOH M2005     5089   5112   6034   -410   -773   -150       O  
HETATM 3365  O   HOH M2006     -20.890  17.946   1.778  1.00 31.86           O  
ANISOU 3365  O   HOH M2006     2385   5188   4530    -54   -462    136       O  
HETATM 3366  O   HOH M2007      -6.671  16.617 -16.511  1.00 35.20           O  
ANISOU 3366  O   HOH M2007     4299   4480   4595    433   -582   -678       O  
HETATM 3367  O   HOH M2008     -12.376  16.235 -17.553  1.00 43.78           O  
ANISOU 3367  O   HOH M2008     5183   6350   5099    188   -354   -954       O  
HETATM 3368  O   HOH M2009     -10.298  18.018 -19.247  1.00 40.51           O  
ANISOU 3368  O   HOH M2009     5513   5704   4173     35    976  -1608       O  
HETATM 3369  O   HOH M2010     -18.545  22.778   1.581  1.00 34.53           O  
ANISOU 3369  O   HOH M2010     3683   5006   4431   1522    411   -296       O  
HETATM 3370  O   HOH M2011       8.102   9.195 -12.625  1.00 34.91           O  
ANISOU 3370  O   HOH M2011     3799   4346   5119   1895   -376   -339       O  
HETATM 3371  O   HOH M2012       8.137   6.352  -4.370  1.00 34.38           O  
ANISOU 3371  O   HOH M2012     1807   6153   5100   -601    544    518       O  
HETATM 3372  O   HOH M2013     -17.059  29.840  -2.221  1.00 26.62           O  
ANISOU 3372  O   HOH M2013      360   7080   2672   -234    -28   -788       O  
HETATM 3373  O   HOH M2014     -11.827  34.667 -11.231  1.00 32.94           O  
ANISOU 3373  O   HOH M2014     2988   5955   3571   -580    673   -142       O  
HETATM 3374  O   HOH M2015     -12.783  30.753 -10.764  1.00 27.63           O  
ANISOU 3374  O   HOH M2015     3645   3335   3517    185   1448     60       O  
HETATM 3375  O   HOH M2016     -14.520  35.013  -0.642  1.00 35.22           O  
ANISOU 3375  O   HOH M2016     4342   4737   4301   1989    341   -996       O  
HETATM 3376  O   HOH M2017     -11.031  35.265   0.870  1.00 25.84           O  
ANISOU 3376  O   HOH M2017     2001   3802   4014   -409   -203  -1051       O  
HETATM 3377  O   HOH M2018     -16.717  26.313  -2.833  1.00 20.00           O  
ANISOU 3377  O   HOH M2018      902   3698   2997    706     27    227       O  
HETATM 3378  O   HOH M2019     -10.144  30.843  -4.531  1.00 15.91           O  
ANISOU 3378  O   HOH M2019      412   3246   2384    598   -396   -564       O  
HETATM 3379  O   HOH M2020      -9.151  28.357  -0.711  1.00 13.15           O  
ANISOU 3379  O   HOH M2020      463   2495   2037   -160      7    -25       O  
HETATM 3380  O   HOH M2021     -17.331  22.285  -3.720  1.00 16.13           O  
ANISOU 3380  O   HOH M2021      296   2867   2966   -301    143     40       O  
HETATM 3381  O   HOH M2022     -11.747  17.732  -0.807  1.00 12.05           O  
ANISOU 3381  O   HOH M2022      293   2389   1893   -173    -70    -24       O  
HETATM 3382  O   HOH M2023     -20.320  19.594  -4.013  1.00 31.47           O  
ANISOU 3382  O   HOH M2023     1640   5114   5201   -179     57   -519       O  
HETATM 3383  O   HOH M2024     -18.588  20.325  -5.974  1.00 26.40           O  
ANISOU 3383  O   HOH M2024      746   4797   4487     65   -400    467       O  
HETATM 3384  O   HOH M2025     -17.225  20.783   3.176  1.00 21.55           O  
ANISOU 3384  O   HOH M2025     1090   3967   3129   -729    567   -765       O  
HETATM 3385  O   HOH M2026     -18.040  16.621  -7.620  1.00 39.53           O  
ANISOU 3385  O   HOH M2026     3374   5027   6619    340    407   1899       O  
HETATM 3386  O   HOH M2027     -21.605  15.659   0.688  1.00 26.67           O  
ANISOU 3386  O   HOH M2027     1859   4643   3630   -307    653   -683       O  
HETATM 3387  O   HOH M2028     -21.453  17.299  -3.030  1.00 29.72           O  
ANISOU 3387  O   HOH M2028     1736   4852   4703     52    -67    255       O  
HETATM 3388  O   HOH M2029     -21.480  12.963  -2.532  1.00 26.90           O  
ANISOU 3388  O   HOH M2029     1671   3700   4847  -1131   -695   -159       O  
HETATM 3389  O   HOH M2030     -15.638  15.503  -8.236  1.00 17.23           O  
ANISOU 3389  O   HOH M2030      551   3662   2334   -415   -303   -419       O  
HETATM 3390  O   HOH M2031     -20.224  10.700  -3.790  1.00 32.51           O  
ANISOU 3390  O   HOH M2031     2553   5323   4472  -1209    -54   -339       O  
HETATM 3391  O   HOH M2032     -13.432   9.100  -5.235  1.00 23.22           O  
ANISOU 3391  O   HOH M2032     2449   2993   3380   -207    182    -80       O  
HETATM 3392  O   HOH M2033     -20.609  12.660  -6.666  1.00 38.97           O  
ANISOU 3392  O   HOH M2033     1919   6630   6255    650   -740     83       O  
HETATM 3393  O   HOH M2034     -13.438  15.791 -11.041  1.00 19.98           O  
ANISOU 3393  O   HOH M2034     1702   3329   2559   -594   -588    -97       O  
HETATM 3394  O   HOH M2035     -16.821   8.823  -2.960  1.00 32.30           O  
ANISOU 3394  O   HOH M2035     3331   5220   3720   -293   -203    975       O  
HETATM 3395  O   HOH M2036     -12.013   7.991 -14.339  1.00 40.03           O  
ANISOU 3395  O   HOH M2036     4064   4894   6249    724  -1175   -402       O  
HETATM 3396  O   HOH M2037     -14.353  11.209 -16.623  1.00 44.88           O  
ANISOU 3396  O   HOH M2037     5014   7098   4940   -218   -588   -122       O  
HETATM 3397  O   HOH M2038      -9.641  16.214 -13.835  1.00 20.38           O  
ANISOU 3397  O   HOH M2038     2265   2973   2504    -86   -239   -198       O  
HETATM 3398  O   HOH M2039     -11.706   9.118  -7.493  1.00 18.13           O  
ANISOU 3398  O   HOH M2039     1186   2988   2712   -140   -292     -3       O  
HETATM 3399  O   HOH M2040      -8.284   8.753 -15.674  1.00 44.85           O  
ANISOU 3399  O   HOH M2040     7793   5343   3905   -854    195   -979       O  
HETATM 3400  O   HOH M2041     -10.490   6.833  -8.867  1.00 30.92           O  
ANISOU 3400  O   HOH M2041     3200   4459   4086   -280   -742   -156       O  
HETATM 3401  O   HOH M2042      -9.903  16.023 -16.517  1.00 35.24           O  
ANISOU 3401  O   HOH M2042     6689   3762   2938   1115     71    142       O  
HETATM 3402  O   HOH M2043      -2.871  12.540  -9.206  1.00 17.53           O  
ANISOU 3402  O   HOH M2043     1367   2678   2614    340    -43   -329       O  
HETATM 3403  O   HOH M2044      -3.377  13.212 -19.726  1.00 42.77           O  
ANISOU 3403  O   HOH M2044     5734   6848   3665   -406   -165   1033       O  
HETATM 3404  O   HOH M2045      -3.065   7.854 -16.341  1.00 33.34           O  
ANISOU 3404  O   HOH M2045     4855   4620   3189   -300   -335   -437       O  
HETATM 3405  O   HOH M2046      -2.632  13.769 -11.735  1.00 20.30           O  
ANISOU 3405  O   HOH M2046     1696   3150   2865    257     18   -298       O  
HETATM 3406  O   HOH M2047      -5.942   5.965 -13.828  1.00 32.53           O  
ANISOU 3406  O   HOH M2047     3904   3968   4488   -389   -776   -886       O  
HETATM 3407  O   HOH M2048      -7.126   4.791 -11.686  1.00 30.92           O  
ANISOU 3407  O   HOH M2048     3240   3638   4870    403  -1384  -1105       O  
HETATM 3408  O   HOH M2049      -1.634   3.941 -14.030  1.00 33.40           O  
ANISOU 3408  O   HOH M2049     4949   4364   3376    214   -565   -987       O  
HETATM 3409  O   HOH M2050       3.990   5.668 -13.171  1.00 34.09           O  
ANISOU 3409  O   HOH M2050     4280   4386   4286   1292   -424   -349       O  
HETATM 3410  O   HOH M2051       2.379  12.437 -15.810  1.00 33.82           O  
ANISOU 3410  O   HOH M2051     3845   4885   4120   -609   -748   -102       O  
HETATM 3411  O   HOH M2052       1.738   6.789 -16.136  1.00 33.63           O  
ANISOU 3411  O   HOH M2052     3925   5136   3714    462   -185  -1350       O  
HETATM 3412  O   HOH M2053       6.293  11.215 -13.523  1.00 22.90           O  
ANISOU 3412  O   HOH M2053     1855   3443   3401    691    341   -130       O  
HETATM 3413  O   HOH M2054       2.073   1.623  -3.321  1.00 31.31           O  
ANISOU 3413  O   HOH M2054     3127   4591   4177   -640   -584    360       O  
HETATM 3414  O   HOH M2055       7.776   9.105  -4.063  1.00 27.84           O  
ANISOU 3414  O   HOH M2055     2560   4016   4001    358     70   -160       O  
HETATM 3415  O   HOH M2056       7.574   7.396 -10.279  1.00 29.43           O  
ANISOU 3415  O   HOH M2056     2111   3907   5163    540    238   -480       O  
HETATM 3416  O   HOH M2057       2.359   3.206 -12.745  1.00 31.31           O  
ANISOU 3416  O   HOH M2057     3014   4395   4484    378   1302    286       O  
CONECT 1441 2955                                                                
CONECT 2937 2938                                                                
CONECT 2938 2937 2939                                                           
CONECT 2939 2938 2940                                                           
CONECT 2940 2939 2941                                                           
CONECT 2941 2940 2942                                                           
CONECT 2942 2941 2943                                                           
CONECT 2943 2942 2944                                                           
CONECT 2944 2943 2945                                                           
CONECT 2945 2944 2946                                                           
CONECT 2946 2945 2947                                                           
CONECT 2947 2946 2948                                                           
CONECT 2948 2947 2949                                                           
CONECT 2949 2948 2950                                                           
CONECT 2950 2949 2951                                                           
CONECT 2951 2950 2952                                                           
CONECT 2952 2951 2953                                                           
CONECT 2953 2952 2954                                                           
CONECT 2954 2953                                                                
CONECT 2955 1441                                                                
MASTER      340    0    2   13    5    0    3    6 3255    3   20   24          
END

Display Options: Goto PDB code: 3D presentation of molecule is powered by 3Dmol, which supports all modern browsers and mobile devices via WebGL.
Hold mouse button: left to rotate,middle to shift,right to zoom

Related entries of code: 2vla

Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code	Check Database	Protein Sequence Similarity
No similar entries are found!
Complexes with the same small molecule ligand
PDB Code	Check Database	Ligand Name
No complexes with the same small molecule ligand are found!

Entry Information

PDB ID	2vla
Complex Type	Protein-Nucleic Acid
PDBbind Subset	general set
Protein Name	RESTRICTION ENDONUCLEASE R.BPUJI recognition domain
Ligand Name	cognate DNA
EC.Number	E.C.3.1.21.4
Resolution	1.3(Å)
Affinity (Kd/Ki/IC50)	Kd=7.3nM
Release Year	2008
Protein/NA Sequence	Check fasta file
Primary Reference	(2008) J.Mol.Biol. Vol. 378: pp. 1084-1093

Links to External Databases

RCSB PDB	The mother database
PDBsum	Enhanced annotations on PDB entries
Pubchem	Comprehensive collection of chemical and biological data
UniProtKB AC	UniProt accession number (AC): A3FMN7
Entrez Gene ID	No matched NCBI Entrez Gene ID found!
ASD	Information of known allosteric effects of PDB entries

This site has been visited

times since Nov 2007.

Technical Support（技术支持）: yingsaisi@foxmail.com