CNRS Nantes University UFIP UFIP
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***  MLR  ***

elNémo ID: 20021322415366914

Job options:

ID        	=	 20021322415366914
JOBID     	=	 MLR
USERID    	=	 MLR
PRIVAT    	=	 0

NMODES    	=	 25
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER MLR

HEADER    HYDROLASE                               27-APR-04   1T3R              
TITLE     HIV PROTEASE WILD-TYPE IN COMPLEX WITH TMC114 INHIBITOR               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEASE RETROPEPSIN;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: HIV-1 PROTEASE;                                             
COMPND   5 EC: 3.4.23.16;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 OTHER_DETAILS: COMPLEXED WITH TMC114                                 
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;                 
SOURCE   3 ORGANISM_TAXID: 11676;                                               
SOURCE   4 GENE: GAG-POL;                                                       
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: P566                                      
KEYWDS    HIV-1 PROTEASE; DRUG RESISTANCE; THERMODYNAMICS; SUBSTRATE ENVELOPE,  
KEYWDS   2 HYDROLASE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.M.KING,M.PRABU-JEYABALAN,E.A.NALIVAIKA,P.B.WIGERNICK,M.P.DE         
AUTHOR   2 BETHUNE,C.A.SCHIFFER                                                 
REVDAT   3   13-JUL-11 1T3R    1       VERSN                                    
REVDAT   2   24-FEB-09 1T3R    1       VERSN                                    
REVDAT   1   03-MAY-05 1T3R    0                                                
JRNL        AUTH   D.L.SURLERAUX,A.TAHRI,W.G.VERSCHUEREN,G.M.PILLE,H.A.DE KOCK, 
JRNL        AUTH 2 T.H.JONCKERS,A.PEETERS,S.DE MEYER,H.AZIJN,R.PAUWELS,         
JRNL        AUTH 3 M.P.DE BETHUNE,N.M.KING,M.PRABU-JEYABALAN,C.A.SCHIFFER,      
JRNL        AUTH 4 P.B.WIGERINCK                                                
JRNL        TITL   DISCOVERY AND SELECTION OF TMC114, A NEXT GENERATION HIV-1   
JRNL        TITL 2 PROTEASE INHIBITOR                                           
JRNL        REF    J.MED.CHEM.                   V.  48  1813 2005              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   15771427                                                     
JRNL        DOI    10.1021/JM049560P                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.19                                        
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.26                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 52226                          
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) : 0.140                           
REMARK   3   FREE R VALUE                     : 0.179                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2775                            
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) : 1.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.23                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2913                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2040                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 146                          
REMARK   3   BIN FREE R VALUE                    : 0.2640                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1496                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 63                                      
REMARK   3   SOLVENT ATOMS            : 259                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.42                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.39000                                             
REMARK   3    B22 (A**2) : -0.06000                                             
REMARK   3    B33 (A**2) : 0.45000                                              
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): 0.040         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.042         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.028         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.622         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.976                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.965                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1664 ; 0.039 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1591 ; 0.007 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2284 ; 1.593 ; 2.018       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3708 ; 0.722 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   215 ; 6.960 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   270 ; 0.149 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1822 ; 0.021 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   301 ; 0.028 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   285 ; 0.244 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1925 ; 0.274 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1088 ; 0.095 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   172 ; 0.254 ; 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):    18 ; 0.310 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):   101 ; 0.312 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.338 ; 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):  1033 ; 3.219 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1690 ; 4.242 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   631 ; 5.811 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   593 ; 8.132 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  1664 ; 2.590 ; 1.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   267 ;16.645 ; 3.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  1628 ; 9.511 ; 3.000       
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   : 1.40                                          
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 1T3R COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-APR-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB022274.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 190                                
REMARK 200  PH                             : 6.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.900                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 55056                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.5                               
REMARK 200  DATA REDUNDANCY                : 5.500                              
REMARK 200  R MERGE                    (I) : 0.03800                            
REMARK 200  R SYM                      (I) : 0.03800                            
REMARK 200   FOR THE DATA SET  : 25.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.24                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 76.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.31700                            
REMARK 200  R SYM FOR SHELL            (I) : 0.31700                            
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: 1F7A                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 MG/ML PROTEIN; 5:1 LIGAND:PROTEIN;     
REMARK 280  30% AMSOR; SODIUM CITRATE AND SODIUM PHOSPHATE, PH 6.2, VAPOR       
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 300K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       25.37300            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       31.00300            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       28.90350            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       31.00300            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.37300            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       28.90350            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5530 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9340 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -56.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     LYS A   7    CG   CD   CE   NZ                                   
REMARK 470     LYS A  41    CG   CD   CE   NZ                                   
REMARK 470     LYS A  43    CG   CD   CE   NZ                                   
REMARK 470     LYS B  41    CG   CD   CE   NZ                                   
REMARK 470     LYS B  43    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    GLY A    16     O    HOH B   618     1655     1.94            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ARG A  14   CB    ARG A  14   CG     -0.173                       
REMARK 500    GLU A  34   CD    GLU A  34   OE1     0.144                       
REMARK 500    GLU A  35   CD    GLU A  35   OE2     0.069                       
REMARK 500    GLU A  65   CD    GLU A  65   OE2    -0.130                       
REMARK 500    CYS A  67   CB    CYS A  67   SG     -0.188                       
REMARK 500    CYS A  95   CB    CYS A  95   SG     -0.139                       
REMARK 500    THR B   4   CA    THR B   4   CB      0.248                       
REMARK 500    THR B   4   CB    THR B   4   OG1    -0.215                       
REMARK 500    ARG B   8   NE    ARG B   8   CZ      0.086                       
REMARK 500    ARG B  14   NE    ARG B  14   CZ     -0.098                       
REMARK 500    GLN B  18   CA    GLN B  18   CB      0.132                       
REMARK 500    LYS B  45   CD    LYS B  45   CE     -0.176                       
REMARK 500    LYS B  45   CE    LYS B  45   NZ     -0.196                       
REMARK 500    TYR B  59   CD1   TYR B  59   CE1    -0.100                       
REMARK 500    CYS B  67   CB    CYS B  67   SG     -0.185                       
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    ARG A  87   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
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 B 592        DISTANCE =  5.63 ANGSTROMS                       
REMARK 525    HOH B 594        DISTANCE =  5.03 ANGSTROMS                       
REMARK 525    HOH B 619        DISTANCE =  6.39 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 017 A 1200                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1F7A   RELATED DB: PDB                                   
REMARK 900 USED AS STARTING MODEL FOR MOLECULAR REPLACEMENT                     
REMARK 900 RELATED ID: 1T7I   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1T7J   RELATED DB: PDB                                   
DBREF  1T3R A    1    99  UNP    P03369   POL_HV1A2       57    155             
DBREF  1T3R B    1    99  UNP    P03369   POL_HV1A2       57    155             
SEQADV 1T3R LYS A    7  UNP  P03369    GLN    63 ENGINEERED                     
SEQADV 1T3R LYS B    7  UNP  P03369    GLN    63 ENGINEERED                     
SEQRES   1 A   99  PRO GLN ILE THR LEU TRP LYS ARG PRO LEU VAL THR ILE          
SEQRES   2 A   99  ARG ILE GLY GLY GLN LEU LYS GLU ALA LEU LEU ASP THR          
SEQRES   3 A   99  GLY ALA ASP ASP THR VAL LEU GLU GLU MET ASN LEU PRO          
SEQRES   4 A   99  GLY LYS TRP LYS PRO LYS MET ILE GLY GLY ILE GLY GLY          
SEQRES   5 A   99  PHE ILE LYS VAL ARG GLN TYR ASP GLN ILE PRO VAL GLU          
SEQRES   6 A   99  ILE CYS GLY HIS LYS ALA ILE GLY THR VAL LEU VAL GLY          
SEQRES   7 A   99  PRO THR PRO VAL ASN ILE ILE GLY ARG ASN LEU LEU THR          
SEQRES   8 A   99  GLN ILE GLY CYS THR LEU ASN PHE                              
SEQRES   1 B   99  PRO GLN ILE THR LEU TRP LYS ARG PRO LEU VAL THR ILE          
SEQRES   2 B   99  ARG ILE GLY GLY GLN LEU LYS GLU ALA LEU LEU ASP THR          
SEQRES   3 B   99  GLY ALA ASP ASP THR VAL LEU GLU GLU MET ASN LEU PRO          
SEQRES   4 B   99  GLY LYS TRP LYS PRO LYS MET ILE GLY GLY ILE GLY GLY          
SEQRES   5 B   99  PHE ILE LYS VAL ARG GLN TYR ASP GLN ILE PRO VAL GLU          
SEQRES   6 B   99  ILE CYS GLY HIS LYS ALA ILE GLY THR VAL LEU VAL GLY          
SEQRES   7 B   99  PRO THR PRO VAL ASN ILE ILE GLY ARG ASN LEU LEU THR          
SEQRES   8 B   99  GLN ILE GLY CYS THR LEU ASN PHE                              
HET    PO4  B 501       5                                                       
HET    PO4  A 502       5                                                       
HET    PO4  B 503       5                                                       
HET    PO4  A 504       5                                                       
HET    PO4  A 505       5                                                       
HET    017  A1200      38                                                       
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     017 (3R,3AS,6AR)-HEXAHYDROFURO[2,3-B]FURAN-3-YL(1S,2R)-3-            
HETNAM   2 017  [[(4-AMINOPHENYL)SULFONYL](ISOBUTYL)AMINO]-1-BENZYL-2-          
HETNAM   3 017  HYDROXYPROPYLCARBAMATE                                          
HETSYN     017 DARUNAVIR, TMC114, UIC-94017                                     
FORMUL   3  PO4    5(O4 P 3-)                                                   
FORMUL   8  017    C27 H37 N3 O7 S                                              
FORMUL   9  HOH   *259(H2 O)                                                    
HELIX    1   1 GLY A   86  THR A   91  1                                   6    
HELIX    2   2 GLY B   86  THR B   91  1                                   6    
SHEET    1   A 4 GLN A   2  ILE A   3  0                                        
SHEET    2   A 4 THR B  96  ASN B  98 -1  O  LEU B  97   N  ILE A   3           
SHEET    3   A 4 THR A  96  ASN A  98 -1  N  ASN A  98   O  THR B  96           
SHEET    4   A 4 GLN B   2  THR B   4 -1  O  ILE B   3   N  LEU A  97           
SHEET    1   B 8 LYS A  43  GLY A  49  0                                        
SHEET    2   B 8 GLY A  52  ILE A  66 -1  O  GLN A  58   N  LYS A  43           
SHEET    3   B 8 HIS A  69  VAL A  77 -1  O  HIS A  69   N  ILE A  66           
SHEET    4   B 8 VAL A  32  LEU A  33  1  N  LEU A  33   O  LEU A  76           
SHEET    5   B 8 ILE A  84  ILE A  85 -1  O  ILE A  84   N  VAL A  32           
SHEET    6   B 8 GLN A  18  LEU A  24  1  N  LEU A  23   O  ILE A  85           
SHEET    7   B 8 LEU A  10  ILE A  15 -1  N  ILE A  15   O  GLN A  18           
SHEET    8   B 8 GLY A  52  ILE A  66 -1  O  GLU A  65   N  ARG A  14           
SHEET    1   C 8 LYS B  43  GLY B  49  0                                        
SHEET    2   C 8 GLY B  52  ILE B  66 -1  O  GLN B  58   N  LYS B  43           
SHEET    3   C 8 HIS B  69  VAL B  77 -1  O  VAL B  75   N  TYR B  59           
SHEET    4   C 8 VAL B  32  LEU B  33  1  N  LEU B  33   O  LEU B  76           
SHEET    5   C 8 ILE B  84  ILE B  85 -1  O  ILE B  84   N  VAL B  32           
SHEET    6   C 8 GLN B  18  LEU B  24  1  N  LEU B  23   O  ILE B  85           
SHEET    7   C 8 LEU B  10  ILE B  15 -1  N  ILE B  13   O  LYS B  20           
SHEET    8   C 8 GLY B  52  ILE B  66 -1  O  GLU B  65   N  ARG B  14           
SITE     1 AC1 10 ARG A  14  GLY A  16  GLY A  17  HOH A1242                    
SITE     2 AC1 10 ARG B  14  GLY B  16  GLY B  17  HOH B 515                    
SITE     3 AC1 10 HOH B 525  HOH B 617                                          
SITE     1 AC2  3 LYS A   7  ARG A   8  HOH A1225                               
SITE     1 AC3  7 GLY A  68  HIS A  69  LYS A  70  HOH A1210                    
SITE     2 AC3  7 HOH A1249  PRO B   1  LYS B  55                               
SITE     1 AC4  5 MET A  36  ASN A  37  PRO B  39  GLY B  40                    
SITE     2 AC4  5 HOH B 621                                                     
SITE     1 AC5  6 LYS A  20  GLU A  21  ASN A  83  HOH A1219                    
SITE     2 AC5  6 HOH A1226  HOH B 616                                          
SITE     1 AC6 19 ASP A  25  GLY A  27  ALA A  28  ASP A  29                    
SITE     2 AC6 19 ASP A  30  GLY A  48  GLY A  49  ILE A  50                    
SITE     3 AC6 19 HOH A1203  HOH A1311  ASP B  25  GLY B  27                    
SITE     4 AC6 19 ALA B  28  ASP B  30  VAL B  32  GLY B  48                    
SITE     5 AC6 19 GLY B  49  VAL B  82  ILE B  84                               
CRYST1   50.746   57.807   62.006  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.019706  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.017299  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016127        0.00000                         
ATOM      1  N   PRO A   1      28.699  21.454  33.798  1.00 26.41           N  
ANISOU    1  N   PRO A   1     3228   3823   2983    326    -22   -139       N  
ATOM      2  CA  PRO A   1      27.719  22.265  34.525  1.00 24.79           C  
ANISOU    2  CA  PRO A   1     2833   3634   2950    238   -116    -18       C  
ATOM      3  C   PRO A   1      26.240  22.015  34.064  1.00 21.25           C  
ANISOU    3  C   PRO A   1     2737   3064   2273    403   -170     13       C  
ATOM      4  O   PRO A   1      26.033  21.403  33.071  1.00 22.75           O  
ANISOU    4  O   PRO A   1     3013   3254   2374    732   -293   -487       O  
ATOM      5  CB  PRO A   1      28.122  23.699  34.165  1.00 29.49           C  
ANISOU    5  CB  PRO A   1     3630   3780   3795    173      0    -64       C  
ATOM      6  CG  PRO A   1      28.733  23.595  32.866  1.00 29.10           C  
ANISOU    6  CG  PRO A   1     3506   4035   3514     18    -74     20       C  
ATOM      7  CD  PRO A   1      29.425  22.266  32.812  1.00 28.00           C  
ANISOU    7  CD  PRO A   1     3406   3822   3410    -76   -264     54       C  
ATOM      8  N   GLN A   2      25.279  22.419  34.914  1.00 21.01           N  
ANISOU    8  N   GLN A   2     2911   3208   1862    453   -246    -92       N  
ATOM      9  CA  GLN A   2      23.872  22.620  34.516  1.00 17.82           C  
ANISOU    9  CA  GLN A   2     2575   2782   1411    284    -61    121       C  
ATOM     10  C   GLN A   2      23.654  24.078  34.247  1.00 18.11           C  
ANISOU   10  C   GLN A   2     2783   2713   1384    344   -136   -147       C  
ATOM     11  O   GLN A   2      23.996  24.956  35.114  1.00 20.40           O  
ANISOU   11  O   GLN A   2     3304   2912   1535    262   -202      8       O  
ATOM     12  CB  GLN A   2      22.926  22.138  35.611  1.00 19.10           C  
ANISOU   12  CB  GLN A   2     2921   2892   1444    430    159    273       C  
ATOM     13  CG  GLN A   2      21.447  22.401  35.328  1.00 18.52           C  
ANISOU   13  CG  GLN A   2     2848   2709   1478    305    289    290       C  
ATOM     14  CD  GLN A   2      20.558  21.549  36.121  1.00 21.32           C  
ANISOU   14  CD  GLN A   2     3536   2808   1755    122    192    302       C  
ATOM     15  OE1 GLN A   2      20.145  20.502  35.662  1.00 22.49           O  
ANISOU   15  OE1 GLN A   2     3459   3395   1691   -395    479    368       O  
ATOM     16  NE2 GLN A   2      20.336  21.926  37.380  1.00 21.05           N  
ANISOU   16  NE2 GLN A   2     2979   3111   1907    347    513     40       N  
ATOM     17  N   ILE A   3      23.132  24.397  33.044  1.00 16.55           N  
ANISOU   17  N   ILE A   3     2472   2473   1341    339     18     60       N  
ATOM     18  CA  ILE A   3      22.953  25.808  32.633  1.00 16.67           C  
ANISOU   18  CA  ILE A   3     2552   2337   1442    458     -7   -249       C  
ATOM     19  C   ILE A   3      21.482  26.059  32.330  1.00 15.72           C  
ANISOU   19  C   ILE A   3     2477   2010   1485    376     -5     21       C  
ATOM     20  O   ILE A   3      20.868  25.364  31.520  1.00 15.91           O  
ANISOU   20  O   ILE A   3     2515   2236   1291    504    -13   -201       O  
ATOM     21  CB  ILE A   3      23.812  26.118  31.387  1.00 18.38           C  
ANISOU   21  CB  ILE A   3     2784   2439   1761    342    103     77       C  
ATOM     22  CG1 ILE A   3      25.342  25.949  31.689  1.00 18.48           C  
ANISOU   22  CG1 ILE A   3     2985   2333   1701    251    137    376       C  
ATOM     23  CG2 ILE A   3      23.547  27.527  30.875  1.00 19.52           C  
ANISOU   23  CG2 ILE A   3     2860   2478   2078    630    178     48       C  
ATOM     24  CD1 ILE A   3      26.162  26.103  30.549  1.00 21.55           C  
ANISOU   24  CD1 ILE A   3     3126   3115   1943    317    107    306       C  
ATOM     25  N   THR A   4      20.887  26.933  33.128  1.00 15.87           N  
ANISOU   25  N   THR A   4     2589   2347   1091    456   -119   -143       N  
ATOM     26  CA  THR A   4      19.503  27.351  32.833  1.00 15.75           C  
ANISOU   26  CA  THR A   4     2575   2027   1382    491     29   -180       C  
ATOM     27  C   THR A   4      19.446  28.398  31.741  1.00 15.51           C  
ANISOU   27  C   THR A   4     2468   2054   1369    336    -99   -229       C  
ATOM     28  O   THR A   4      20.430  28.870  31.310  1.00 16.38           O  
ANISOU   28  O   THR A   4     2558   2118   1547    285   -229    -99       O  
ATOM     29  CB  THR A   4      18.816  27.912  34.134  1.00 16.86           C  
ANISOU   29  CB  THR A   4     2566   2562   1276    509     19    -53       C  
ATOM     30  OG1 THR A   4      19.563  29.057  34.578  1.00 19.32           O  
ANISOU   30  OG1 THR A   4     3214   2740   1385    449    -40    -46       O  
ATOM     31  CG2 THR A   4      18.833  26.841  35.249  1.00 18.60           C  
ANISOU   31  CG2 THR A   4     2823   2523   1719    531    307   -138       C  
ATOM     32  N   LEU A   5      18.246  28.766  31.361  1.00 15.45           N  
ANISOU   32  N   LEU A   5     2625   2165   1078    453    118   -333       N  
ATOM     33  CA  LEU A   5      18.036  29.497  30.073  1.00 13.94           C  
ANISOU   33  CA  LEU A   5     2308   1907   1082    331     97   -220       C  
ATOM     34  C   LEU A   5      17.299  30.803  30.212  1.00 16.04           C  
ANISOU   34  C   LEU A   5     2760   1992   1339    574    107   -446       C  
ATOM     35  O   LEU A   5      16.815  31.385  29.209  1.00 15.73           O  
ANISOU   35  O   LEU A   5     2583   2163   1228    669     82   -220       O  
ATOM     36  CB  LEU A   5      17.384  28.590  29.088  1.00 13.41           C  
ANISOU   36  CB  LEU A   5     2125   1980    991    348     64    -94       C  
ATOM     37  CG  LEU A   5      18.226  27.325  28.692  1.00 13.46           C  
ANISOU   37  CG  LEU A   5     2129   1848   1135    335    126   -138       C  
ATOM     38  CD1 LEU A   5      17.455  26.412  27.870  1.00 14.28           C  
ANISOU   38  CD1 LEU A   5     2127   2146   1150    187    366   -102       C  
ATOM     39  CD2 LEU A   5      19.482  27.737  27.925  1.00 14.09           C  
ANISOU   39  CD2 LEU A   5     2222   2037   1095    246    -83   -179       C  
ATOM     40  N   TRP A   6      17.284  31.375  31.434  1.00 16.86           N  
ANISOU   40  N   TRP A   6     3074   2169   1159    722    174   -326       N  
ATOM     41  CA  TRP A   6      16.707  32.666  31.611  1.00 17.05           C  
ANISOU   41  CA  TRP A   6     2845   2216   1417    514    101   -445       C  
ATOM     42  C   TRP A   6      17.659  33.763  31.019  1.00 18.33           C  
ANISOU   42  C   TRP A   6     2805   2206   1951    433    112   -820       C  
ATOM     43  O   TRP A   6      17.204  34.845  30.676  1.00 20.73           O  
ANISOU   43  O   TRP A   6     2979   2194   2704    541    114   -236       O  
ATOM     44  CB  TRP A   6      16.356  32.919  33.157  1.00 20.30           C  
ANISOU   44  CB  TRP A   6     3282   2674   1756    530    482   -924       C  
ATOM     45  CG  TRP A   6      15.026  32.189  33.646  1.00 18.85           C  
ANISOU   45  CG  TRP A   6     3162   2816   1183    236    264   -555       C  
ATOM     46  CD1 TRP A   6      13.705  32.558  33.336  1.00 19.94           C  
ANISOU   46  CD1 TRP A   6     2761   3126   1688    528    471   -492       C  
ATOM     47  CD2 TRP A   6      14.941  30.990  34.423  1.00 20.40           C  
ANISOU   47  CD2 TRP A   6     3070   2639   2041    489     34   -613       C  
ATOM     48  NE1 TRP A   6      12.820  31.577  33.761  1.00 21.82           N  
ANISOU   48  NE1 TRP A   6     3094   3240   1955    369   -165   -339       N  
ATOM     49  CE2 TRP A   6      13.542  30.616  34.493  1.00 20.77           C  
ANISOU   49  CE2 TRP A   6     3332   2861   1696    267   -221   -230       C  
ATOM     50  CE3 TRP A   6      15.875  30.123  34.920  1.00 20.29           C  
ANISOU   50  CE3 TRP A   6     3064   2957   1689    692    256   -660       C  
ATOM     51  CZ2 TRP A   6      13.127  29.428  35.041  1.00 21.27           C  
ANISOU   51  CZ2 TRP A   6     2917   3585   1580    512    253   -145       C  
ATOM     52  CZ3 TRP A   6      15.452  28.956  35.526  1.00 23.27           C  
ANISOU   52  CZ3 TRP A   6     3170   3374   2296    417    261   -242       C  
ATOM     53  CH2 TRP A   6      14.085  28.634  35.609  1.00 21.71           C  
ANISOU   53  CH2 TRP A   6     3005   3133   2110    364    135    264       C  
ATOM     54  N   LYS A   7      18.943  33.460  30.863  1.00 18.01           N  
ANISOU   54  N   LYS A   7     2737   2297   1807    457     51   -527       N  
ATOM     55  CA  LYS A   7      19.868  34.291  30.152  1.00 18.47           C  
ANISOU   55  CA  LYS A   7     2899   2250   1865    354   -194   -724       C  
ATOM     56  C   LYS A   7      20.407  33.514  28.970  1.00 16.89           C  
ANISOU   56  C   LYS A   7     2823   2173   1421    142   -172   -516       C  
ATOM     57  O   LYS A   7      20.390  32.305  28.964  1.00 16.24           O  
ANISOU   57  O   LYS A   7     2656   1968   1545    314    -46   -329       O  
ATOM     58  CB  LYS A   7      21.039  34.694  31.043  1.00 22.07           C  
ANISOU   58  CB  LYS A   7     3564   3071   1750   -210    -21  -1190       C  
ATOM     59  N   ARG A   8      21.063  34.206  28.059  1.00 15.16           N  
ANISOU   59  N   ARG A   8     2350   1673   1735    309   -198   -369       N  
ATOM     60  CA  ARG A   8      21.751  33.512  26.958  1.00 14.08           C  
ANISOU   60  CA  ARG A   8     2189   1788   1372    217   -258   -291       C  
ATOM     61  C   ARG A   8      22.831  32.627  27.523  1.00 14.01           C  
ANISOU   61  C   ARG A   8     2373   1656   1292    157   -309   -472       C  
ATOM     62  O   ARG A   8      23.644  33.098  28.358  1.00 15.33           O  
ANISOU   62  O   ARG A   8     2562   1734   1527    118   -562   -560       O  
ATOM     63  CB  ARG A   8      22.393  34.533  25.995  1.00 15.05           C  
ANISOU   63  CB  ARG A   8     2299   1934   1482     27   -365   -398       C  
ATOM     64  CG  ARG A   8      21.388  35.299  25.145  1.00 16.10           C  
ANISOU   64  CG  ARG A   8     2276   1738   2101     22   -371   -147       C  
ATOM     65  CD  ARG A   8      21.981  36.283  24.289  1.00 18.66           C  
ANISOU   65  CD  ARG A   8     2387   2236   2466   -331   -391     53       C  
ATOM     66  NE  ARG A   8      20.974  36.967  23.478  1.00 26.58           N  
ANISOU   66  NE  ARG A   8     3371   2557   4169     56   -417    425       N  
ATOM     67  CZ  ARG A   8      21.155  38.127  22.865  1.00 28.39           C  
ANISOU   67  CZ  ARG A   8     4006   3149   3631   -544   -785    471       C  
ATOM     68  NH1 ARG A   8      22.298  38.861  23.072  1.00 32.61           N  
ANISOU   68  NH1 ARG A   8     4183   3313   4894   -969   -276    320       N  
ATOM     69  NH2 ARG A   8      20.234  38.582  22.075  1.00 27.89           N  
ANISOU   69  NH2 ARG A   8     3546   2574   4477   -274   -492   1381       N  
ATOM     70  N   PRO A   9      22.993  31.412  26.985  1.00 13.20           N  
ANISOU   70  N   PRO A   9     1991   1450   1572    105   -140   -365       N  
ATOM     71  CA  PRO A   9      24.058  30.507  27.473  1.00 12.81           C  
ANISOU   71  CA  PRO A   9     2230   1621   1016     43   -352   -232       C  
ATOM     72  C   PRO A   9      25.393  30.784  26.831  1.00 13.39           C  
ANISOU   72  C   PRO A   9     2008   1794   1283     -7   -242   -359       C  
ATOM     73  O   PRO A   9      25.886  30.054  25.979  1.00 13.14           O  
ANISOU   73  O   PRO A   9     2044   1590   1358     80   -393   -228       O  
ATOM     74  CB  PRO A   9      23.517  29.138  27.156  1.00 12.80           C  
ANISOU   74  CB  PRO A   9     2105   1505   1251    155   -110   -250       C  
ATOM     75  CG  PRO A   9      22.661  29.333  25.968  1.00 11.86           C  
ANISOU   75  CG  PRO A   9     1717   1600   1188   -155   -120   -315       C  
ATOM     76  CD  PRO A   9      21.995  30.679  26.191  1.00 12.06           C  
ANISOU   76  CD  PRO A   9     1750   1561   1270    -70    -48   -387       C  
ATOM     77  N   LEU A  10      25.975  31.915  27.261  1.00 15.80           N  
ANISOU   77  N   LEU A  10     2387   1989   1625   -202   -321   -598       N  
ATOM     78  CA  LEU A  10      27.264  32.344  26.801  1.00 14.99           C  
ANISOU   78  CA  LEU A  10     2194   1917   1581    -90   -250   -271       C  
ATOM     79  C   LEU A  10      28.381  31.764  27.624  1.00 17.09           C  
ANISOU   79  C   LEU A  10     2367   2704   1421   -279   -383   -378       C  
ATOM     80  O   LEU A  10      28.286  31.737  28.859  1.00 22.73           O  
ANISOU   80  O   LEU A  10     3001   4247   1387   -311   -330   -468       O  
ATOM     81  CB  LEU A  10      27.364  33.892  26.837  1.00 18.92           C  
ANISOU   81  CB  LEU A  10     2699   2186   2301   -538   -251   -730       C  
ATOM     82  CG  LEU A  10      26.444  34.574  25.905  1.00 20.44           C  
ANISOU   82  CG  LEU A  10     2503   1908   3353   -266     88   -169       C  
ATOM     83  CD1 LEU A  10      26.254  36.027  26.276  1.00 23.88           C  
ANISOU   83  CD1 LEU A  10     3524   1978   3572   -280    192   -301       C  
ATOM     84  CD2 LEU A  10      26.983  34.490  24.453  1.00 21.23           C  
ANISOU   84  CD2 LEU A  10     2827   2231   3008    152   -813   -231       C  
ATOM     85  N   VAL A  11      29.375  31.255  27.011  1.00 14.84           N  
ANISOU   85  N   VAL A  11     2085   2000   1552   -168   -746     51       N  
ATOM     86  CA  VAL A  11      30.473  30.664  27.715  1.00 16.59           C  
ANISOU   86  CA  VAL A  11     2390   2079   1833   -215   -869    353       C  
ATOM     87  C   VAL A  11      31.810  31.113  27.103  1.00 14.71           C  
ANISOU   87  C   VAL A  11     2325   1865   1397    -54   -849    -29       C  
ATOM     88  O   VAL A  11      31.877  31.590  25.971  1.00 15.58           O  
ANISOU   88  O   VAL A  11     2106   2043   1770   -331   -977    250       O  
ATOM     89  CB  VAL A  11      30.397  29.207  27.749  1.00 19.02           C  
ANISOU   89  CB  VAL A  11     2734   2264   2230   -209   -935    556       C  
ATOM     90  CG1 VAL A  11      29.094  28.704  28.409  1.00 23.88           C  
ANISOU   90  CG1 VAL A  11     3030   3081   2961   -579   -953    960       C  
ATOM     91  CG2 VAL A  11      30.583  28.631  26.486  1.00 19.95           C  
ANISOU   91  CG2 VAL A  11     2707   1692   3179   -291   -345     76       C  
ATOM     92  N   THR A  12      32.875  30.963  27.866  1.00 16.70           N  
ANISOU   92  N   THR A  12     2106   2100   2138   -320  -1140    385       N  
ATOM     93  CA  THR A  12      34.172  31.223  27.350  1.00 16.58           C  
ANISOU   93  CA  THR A  12     2279   2090   1931   -287  -1005    193       C  
ATOM     94  C   THR A  12      34.751  30.001  26.690  1.00 16.89           C  
ANISOU   94  C   THR A  12     2239   1953   2222      4  -1024    167       C  
ATOM     95  O   THR A  12      34.684  28.888  27.273  1.00 17.57           O  
ANISOU   95  O   THR A  12     2615   1762   2298    -67  -1057    519       O  
ATOM     96  CB  THR A  12      35.130  31.713  28.518  1.00 19.89           C  
ANISOU   96  CB  THR A  12     2514   2456   2587   -480  -1332     51       C  
ATOM     97  OG1 THR A  12      34.586  32.859  29.079  1.00 20.17           O  
ANISOU   97  OG1 THR A  12     2804   2324   2536   -492  -1298     42       O  
ATOM     98  CG2 THR A  12      36.444  32.085  28.007  1.00 20.97           C  
ANISOU   98  CG2 THR A  12     2508   2528   2930   -360  -1382     28       C  
ATOM     99  N   ILE A  13      35.321  30.172  25.494  1.00 15.74           N  
ANISOU   99  N   ILE A  13     2121   1652   2205   -476   -902    290       N  
ATOM    100  CA  ILE A  13      36.036  29.162  24.798  1.00 16.14           C  
ANISOU  100  CA  ILE A  13     1954   1921   2258   -305   -830    425       C  
ATOM    101  C   ILE A  13      37.486  29.576  24.558  1.00 18.01           C  
ANISOU  101  C   ILE A  13     1850   1844   3148   -674   -782    564       C  
ATOM    102  O   ILE A  13      37.809  30.785  24.600  1.00 18.55           O  
ANISOU  102  O   ILE A  13     2051   1799   3196   -487  -1307    655       O  
ATOM    103  CB  ILE A  13      35.326  28.822  23.452  1.00 15.76           C  
ANISOU  103  CB  ILE A  13     1951   1727   2307   -336   -877    347       C  
ATOM    104  CG1 ILE A  13      35.489  29.988  22.407  1.00 16.94           C  
ANISOU  104  CG1 ILE A  13     1828   1911   2695   -404  -1006    513       C  
ATOM    105  CG2 ILE A  13      33.854  28.522  23.730  1.00 15.87           C  
ANISOU  105  CG2 ILE A  13     1798   1818   2411   -231  -1098    361       C  
ATOM    106  CD1 ILE A  13      35.054  29.629  20.995  1.00 15.73           C  
ANISOU  106  CD1 ILE A  13     1730   1899   2347   -124   -756    454       C  
ATOM    107  N   ARG A  14      38.351  28.546  24.283  1.00 19.24           N  
ANISOU  107  N   ARG A  14     1923   1889   3499   -466   -972    416       N  
ATOM    108  CA  ARG A  14      39.740  28.714  23.796  1.00 19.48           C  
ANISOU  108  CA  ARG A  14     1845   2023   3531   -149   -998    564       C  
ATOM    109  C   ARG A  14      39.918  28.028  22.436  1.00 20.28           C  
ANISOU  109  C   ARG A  14     1550   2488   3665    111   -746    405       C  
ATOM    110  O   ARG A  14      39.637  26.872  22.330  1.00 21.28           O  
ANISOU  110  O   ARG A  14     2017   1749   4316   -146   -720   1058       O  
ATOM    111  CB  ARG A  14      40.748  27.997  24.860  1.00 25.11           C  
ANISOU  111  CB  ARG A  14     2133   3121   4284    148  -1143    376       C  
ATOM    112  CG  ARG A  14      41.974  28.524  25.047  1.00 26.05           C  
ANISOU  112  CG  ARG A  14     1978   4063   3854    268   -745    323       C  
ATOM    113  CD  ARG A  14      42.876  27.685  26.109  1.00 28.26           C  
ANISOU  113  CD  ARG A  14     2717   4106   3912    545  -1009     51       C  
ATOM    114  NE  ARG A  14      44.159  27.228  25.525  1.00 28.29           N  
ANISOU  114  NE  ARG A  14     2799   3645   4306    347   -687    672       N  
ATOM    115  CZ  ARG A  14      45.195  26.746  26.259  1.00 25.16           C  
ANISOU  115  CZ  ARG A  14     2982   3757   2820    500   -413    435       C  
ATOM    116  NH1 ARG A  14      45.134  26.730  27.627  1.00 31.96           N  
ANISOU  116  NH1 ARG A  14     4540   4469   3132    401    214    785       N  
ATOM    117  NH2 ARG A  14      46.281  26.301  25.639  1.00 25.69           N  
ANISOU  117  NH2 ARG A  14     2276   4004   3480    -37     -8    772       N  
ATOM    118  N   ILE A  15      40.496  28.785  21.374  1.00 17.55           N  
ANISOU  118  N   ILE A  15     1534   1745   3385   -283   -771    402       N  
ATOM    119  CA  ILE A  15      40.664  28.280  20.005  1.00 18.93           C  
ANISOU  119  CA  ILE A  15     1883   2053   3253   -116   -482    584       C  
ATOM    120  C   ILE A  15      41.849  29.017  19.370  1.00 22.09           C  
ANISOU  120  C   ILE A  15     2236   2087   4071   -105    106    528       C  
ATOM    121  O   ILE A  15      41.974  30.256  19.540  1.00 22.91           O  
ANISOU  121  O   ILE A  15     1533   2186   4986    104   -529    656       O  
ATOM    122  CB  ILE A  15      39.370  28.512  19.202  1.00 18.63           C  
ANISOU  122  CB  ILE A  15     1863   2082   3134     -2   -897    700       C  
ATOM    123  CG1 ILE A  15      39.539  27.963  17.824  1.00 20.53           C  
ANISOU  123  CG1 ILE A  15     1745   2882   3173    460    186    759       C  
ATOM    124  CG2 ILE A  15      38.906  30.049  19.262  1.00 22.07           C  
ANISOU  124  CG2 ILE A  15     1856   2382   4145    413   -431    930       C  
ATOM    125  CD1 ILE A  15      38.335  28.008  16.992  1.00 21.04           C  
ANISOU  125  CD1 ILE A  15     2041   3004   2947    614   -101   1296       C  
ATOM    126  N   GLY A  16      42.710  28.265  18.585  1.00 20.04           N  
ANISOU  126  N   GLY A  16     2183   2166   3263   -240   -109    176       N  
ATOM    127  CA  GLY A  16      43.870  28.844  17.943  1.00 21.12           C  
ANISOU  127  CA  GLY A  16     2402   2552   3067   -217    -98     18       C  
ATOM    128  C   GLY A  16      44.732  29.561  18.902  1.00 22.23           C  
ANISOU  128  C   GLY A  16     2924   2375   3147   -208   -153   -110       C  
ATOM    129  O   GLY A  16      45.498  30.522  18.511  1.00 23.46           O  
ANISOU  129  O   GLY A  16     2607   2706   3601   -441   -365    113       O  
ATOM    130  N   GLY A  17      44.609  29.232  20.109  1.00 20.72           N  
ANISOU  130  N   GLY A  17     2207   2616   3046    -76    134     17       N  
ATOM    131  CA  GLY A  17      45.383  29.828  21.189  1.00 25.17           C  
ANISOU  131  CA  GLY A  17     3543   2677   3341     -8   -401   -247       C  
ATOM    132  C   GLY A  17      44.727  30.930  21.930  1.00 23.89           C  
ANISOU  132  C   GLY A  17     2286   3756   3034    346   -429   -409       C  
ATOM    133  O   GLY A  17      45.299  31.459  22.831  1.00 26.29           O  
ANISOU  133  O   GLY A  17     3050   3550   3387    469   -955   -592       O  
ATOM    134  N   GLN A  18      43.639  31.479  21.343  1.00 21.91           N  
ANISOU  134  N   GLN A  18     2217   2477   3629     75   -593   -171       N  
ATOM    135  CA  GLN A  18      42.946  32.713  21.880  1.00 22.92           C  
ANISOU  135  CA  GLN A  18     2392   2618   3697   -262   -558   -156       C  
ATOM    136  C   GLN A  18      41.507  32.418  22.671  1.00 23.47           C  
ANISOU  136  C   GLN A  18     2534   2591   3792   -137   -746    358       C  
ATOM    137  O   GLN A  18      40.861  31.451  22.428  1.00 26.51           O  
ANISOU  137  O   GLN A  18     2861   2188   5021   -809   -776    583       O  
ATOM    138  CB  GLN A  18      42.656  33.686  20.670  1.00 23.78           C  
ANISOU  138  CB  GLN A  18     2811   2588   3636    -76   -943     44       C  
ATOM    139  CG  GLN A  18      43.872  34.050  19.911  1.00 31.20           C  
ANISOU  139  CG  GLN A  18     3794   3332   4727   -125   -198    150       C  
ATOM    140  CD  GLN A  18      44.718  34.960  20.660  1.00 30.20           C  
ANISOU  140  CD  GLN A  18     3851   3143   4481    438    191   -702       C  
ATOM    141  OE1 GLN A  18      44.237  36.091  21.096  1.00 27.16           O  
ANISOU  141  OE1 GLN A  18     3459   2773   4085      0   1015   -492       O  
ATOM    142  NE2 GLN A  18      45.999  34.565  20.884  1.00 29.54           N  
ANISOU  142  NE2 GLN A  18     3720   3330   4171    533    -81   -181       N  
ATOM    143  N  ALEU A  19      41.185  33.264  23.682  0.50 21.32           N  
ANISOU  143  N  ALEU A  19     2547   2245   3309   -370  -1047    405       N  
ATOM    144  N  BLEU A  19      41.153  33.288  23.569  0.50 19.10           N  
ANISOU  144  N  BLEU A  19     2285   1908   3064   -426  -1268    391       N  
ATOM    145  CA ALEU A  19      39.800  33.235  24.388  0.50 24.41           C  
ANISOU  145  CA ALEU A  19     2879   2841   3553    -77   -788    560       C  
ATOM    146  CA BLEU A  19      39.837  33.221  24.286  0.50 21.98           C  
ANISOU  146  CA BLEU A  19     2692   2479   3181    -99   -904    521       C  
ATOM    147  C  ALEU A  19      38.770  34.025  23.636  0.50 21.26           C  
ANISOU  147  C  ALEU A  19     2436   2303   3337   -537   -903    678       C  
ATOM    148  C  BLEU A  19      38.774  34.075  23.682  0.50 18.95           C  
ANISOU  148  C  BLEU A  19     2306   2130   2763   -619  -1363    721       C  
ATOM    149  O  ALEU A  19      39.058  35.123  23.132  0.50 26.30           O  
ANISOU  149  O  ALEU A  19     3088   2498   4408   -720   -859    937       O  
ATOM    150  O  BLEU A  19      38.981  35.286  23.492  0.50 23.09           O  
ANISOU  150  O  BLEU A  19     2472   2490   3811  -1003  -1956   1190       O  
ATOM    151  CB ALEU A  19      39.862  33.793  25.850  0.50 23.07           C  
ANISOU  151  CB ALEU A  19     2847   2265   3652   -248   -603    593       C  
ATOM    152  CB BLEU A  19      39.984  33.634  25.654  0.50 20.78           C  
ANISOU  152  CB BLEU A  19     2883   1683   3330   -237   -692    117       C  
ATOM    153  CG ALEU A  19      40.627  32.946  26.937  0.50 25.76           C  
ANISOU  153  CG ALEU A  19     2565   3564   3658    184   -981    299       C  
ATOM    154  CG BLEU A  19      41.050  32.880  26.462  0.50 18.52           C  
ANISOU  154  CG BLEU A  19     2249   2007   2778   -220   -443   -163       C  
ATOM    155  CD1ALEU A  19      42.060  32.745  26.506  0.50 26.02           C  
ANISOU  155  CD1ALEU A  19     3180   3271   3433     23   -227   -209       C  
ATOM    156  CD1BLEU A  19      41.201  33.481  27.694  0.50 18.51           C  
ANISOU  156  CD1BLEU A  19     2773   1784   2474   -184    779   -587       C  
ATOM    157  CD2ALEU A  19      40.547  33.647  28.307  0.50 24.53           C  
ANISOU  157  CD2ALEU A  19     2414   3269   3635    221   -140    672       C  
ATOM    158  CD2BLEU A  19      40.668  31.509  26.641  0.50 15.71           C  
ANISOU  158  CD2BLEU A  19     1613   1869   2484    -58  -1027    473       C  
ATOM    159  N   LYS A  20      37.513  33.520  23.671  1.00 20.23           N  
ANISOU  159  N   LYS A  20     2308   1955   3421   -729  -1122    789       N  
ATOM    160  CA  LYS A  20      36.328  34.205  23.109  1.00 17.88           C  
ANISOU  160  CA  LYS A  20     2219   1964   2607   -365   -938    741       C  
ATOM    161  C   LYS A  20      35.070  33.857  23.886  1.00 17.07           C  
ANISOU  161  C   LYS A  20     2129   1797   2556   -604  -1120    295       C  
ATOM    162  O   LYS A  20      35.007  32.812  24.512  1.00 19.34           O  
ANISOU  162  O   LYS A  20     2735   1836   2778   -439  -1127    670       O  
ATOM    163  CB  LYS A  20      36.137  33.795  21.686  1.00 20.70           C  
ANISOU  163  CB  LYS A  20     2550   2667   2648   -349   -652    768       C  
ATOM    164  CG  LYS A  20      37.224  34.141  20.858  1.00 22.91           C  
ANISOU  164  CG  LYS A  20     2741   2886   3077   -375   -467    781       C  
ATOM    165  CD  LYS A  20      37.058  33.621  19.526  1.00 20.63           C  
ANISOU  165  CD  LYS A  20     2421   2431   2985   -167    195    316       C  
ATOM    166  CE  LYS A  20      38.024  34.263  18.584  1.00 27.61           C  
ANISOU  166  CE  LYS A  20     3121   3971   3397    -61    120    707       C  
ATOM    167  NZ  LYS A  20      37.605  35.541  18.134  1.00 25.91           N  
ANISOU  167  NZ  LYS A  20     3438   3268   3135   -778   -293    690       N  
ATOM    168  N  AGLU A  21      34.054  34.645  23.757  0.50 16.90           N  
ANISOU  168  N  AGLU A  21     2188   1763   2467   -549  -1011    522       N  
ATOM    169  N  BGLU A  21      34.002  34.643  23.669  0.50 17.10           N  
ANISOU  169  N  BGLU A  21     2181   1862   2452   -447  -1063    390       N  
ATOM    170  CA AGLU A  21      32.820  34.252  24.177  0.50 15.90           C  
ANISOU  170  CA AGLU A  21     2119   1922   2000   -385   -886    251       C  
ATOM    171  CA BGLU A  21      32.684  34.357  24.231  0.50 16.10           C  
ANISOU  171  CA BGLU A  21     2280   1912   1925   -331   -890    262       C  
ATOM    172  C  AGLU A  21      32.056  33.618  23.043  0.50 13.94           C  
ANISOU  172  C  AGLU A  21     2102   1497   1695   -325   -790    421       C  
ATOM    173  C  BGLU A  21      31.778  33.810  23.163  0.50 12.52           C  
ANISOU  173  C  BGLU A  21     1480   1558   1718   -297   -654    195       C  
ATOM    174  O  AGLU A  21      32.174  34.070  21.815  0.50 11.55           O  
ANISOU  174  O  AGLU A  21     1370   1380   1639    -50   -324    -62       O  
ATOM    175  O  BGLU A  21      31.626  34.403  22.168  0.50 10.50           O  
ANISOU  175  O  BGLU A  21     1359   1343   1287    129   -248    213       O  
ATOM    176  CB AGLU A  21      32.025  35.452  24.767  0.50 17.73           C  
ANISOU  176  CB AGLU A  21     2362   2116   2257   -495   -805   -216       C  
ATOM    177  CB BGLU A  21      32.057  35.626  24.776  0.50 18.52           C  
ANISOU  177  CB BGLU A  21     2587   2063   2386   -429   -719   -123       C  
ATOM    178  CG AGLU A  21      32.740  36.131  26.034  0.50 19.06           C  
ANISOU  178  CG AGLU A  21     2367   2094   2780   -626  -1168   -248       C  
ATOM    179  CG BGLU A  21      30.733  35.411  25.410  0.50 19.19           C  
ANISOU  179  CG BGLU A  21     2865   2331   2092   -376   -629    -52       C  
ATOM    180  CD AGLU A  21      32.849  35.201  27.181  0.50 19.91           C  
ANISOU  180  CD AGLU A  21     2482   2308   2771   -294   -808   -307       C  
ATOM    181  CD BGLU A  21      30.248  36.632  26.247  0.50 24.59           C  
ANISOU  181  CD BGLU A  21     3313   2867   3162    -56   -264   -417       C  
ATOM    182  OE1AGLU A  21      33.949  34.909  27.552  0.50 18.25           O  
ANISOU  182  OE1AGLU A  21     2810   2298   1823   -306  -1317    370       O  
ATOM    183  OE1BGLU A  21      29.889  37.722  25.612  0.50 31.64           O  
ANISOU  183  OE1BGLU A  21     4446   3688   3887   -441   -283    601       O  
ATOM    184  OE2AGLU A  21      31.773  34.835  27.782  0.50 22.31           O  
ANISOU  184  OE2AGLU A  21     3113   3417   1945   -632   -813   -125       O  
ATOM    185  OE2BGLU A  21      30.107  36.482  27.566  0.50 27.19           O  
ANISOU  185  OE2BGLU A  21     3935   3297   3098   -196   -228   -485       O  
ATOM    186  N   ALA A  22      31.225  32.651  23.384  1.00 12.59           N  
ANISOU  186  N   ALA A  22     1849   1401   1531   -194   -380    243       N  
ATOM    187  CA  ALA A  22      30.334  31.986  22.363  1.00 11.08           C  
ANISOU  187  CA  ALA A  22     1562   1226   1420   -198   -365    126       C  
ATOM    188  C   ALA A  22      29.057  31.509  22.993  1.00 11.70           C  
ANISOU  188  C   ALA A  22     1691   1474   1279   -292   -302    329       C  
ATOM    189  O   ALA A  22      29.012  31.196  24.174  1.00 13.28           O  
ANISOU  189  O   ALA A  22     1884   1884   1276   -164   -470    294       O  
ATOM    190  CB  ALA A  22      31.084  30.851  21.700  1.00 11.90           C  
ANISOU  190  CB  ALA A  22     1541   1456   1525   -149   -364    196       C  
ATOM    191  N   LEU A  23      28.027  31.359  22.169  1.00 10.64           N  
ANISOU  191  N   LEU A  23     1410   1418   1213   -129   -357     60       N  
ATOM    192  CA  LEU A  23      26.747  30.934  22.555  1.00 10.58           C  
ANISOU  192  CA  LEU A  23     1559   1343   1117   -160   -295    -55       C  
ATOM    193  C   LEU A  23      26.536  29.464  22.322  1.00  9.27           C  
ANISOU  193  C   LEU A  23     1244   1202   1073    -43   -102   -104       C  
ATOM    194  O   LEU A  23      26.706  28.956  21.217  1.00 10.54           O  
ANISOU  194  O   LEU A  23     1614   1292   1098   -151    -92   -106       O  
ATOM    195  CB  LEU A  23      25.728  31.732  21.731  1.00 11.16           C  
ANISOU  195  CB  LEU A  23     1475   1507   1258     53   -244     -1       C  
ATOM    196  CG  LEU A  23      24.261  31.532  21.950  1.00 11.73           C  
ANISOU  196  CG  LEU A  23     1647   1330   1476   -105   -117    -57       C  
ATOM    197  CD1 LEU A  23      23.847  32.113  23.292  1.00 14.01           C  
ANISOU  197  CD1 LEU A  23     1903   2093   1327    127     29     76       C  
ATOM    198  CD2 LEU A  23      23.448  32.173  20.820  1.00 12.25           C  
ANISOU  198  CD2 LEU A  23     1655   1627   1369     32   -177    178       C  
ATOM    199  N   LEU A  24      26.167  28.747  23.370  1.00  9.83           N  
ANISOU  199  N   LEU A  24     1546   1246    940    -66   -201   -147       N  
ATOM    200  CA  LEU A  24      25.804  27.311  23.210  1.00  9.65           C  
ANISOU  200  CA  LEU A  24     1327   1398    941     75    -60    -57       C  
ATOM    201  C   LEU A  24      24.456  27.233  22.520  1.00  9.90           C  
ANISOU  201  C   LEU A  24     1124   1422   1215     76    -40   -156       C  
ATOM    202  O   LEU A  24      23.464  27.683  23.030  1.00 10.55           O  
ANISOU  202  O   LEU A  24     1416   1555   1037     13    -73   -245       O  
ATOM    203  CB  LEU A  24      25.761  26.606  24.556  1.00 10.38           C  
ANISOU  203  CB  LEU A  24     1581   1321   1040     49    -72     12       C  
ATOM    204  CG  LEU A  24      27.005  26.692  25.428  1.00 11.77           C  
ANISOU  204  CG  LEU A  24     1878   1448   1144    127   -398    110       C  
ATOM    205  CD1 LEU A  24      26.786  25.947  26.736  1.00 15.11           C  
ANISOU  205  CD1 LEU A  24     2469   1869   1399    127   -622    189       C  
ATOM    206  CD2 LEU A  24      28.214  26.124  24.701  1.00 14.24           C  
ANISOU  206  CD2 LEU A  24     1626   2034   1748    136   -577   -389       C  
ATOM    207  N   ASP A  25      24.465  26.647  21.304  1.00  9.16           N  
ANISOU  207  N   ASP A  25     1210   1133   1137     77   -173    -30       N  
ATOM    208  CA  ASP A  25      23.340  26.812  20.393  1.00  8.39           C  
ANISOU  208  CA  ASP A  25     1218   1203    766     39    -19    -18       C  
ATOM    209  C   ASP A  25      22.846  25.472  19.860  1.00  8.33           C  
ANISOU  209  C   ASP A  25     1065   1061   1037     45    -17    -12       C  
ATOM    210  O   ASP A  25      23.339  24.932  18.863  1.00  8.65           O  
ANISOU  210  O   ASP A  25     1219   1033   1034     82     96    -67       O  
ATOM    211  CB  ASP A  25      23.793  27.733  19.249  1.00  9.39           C  
ANISOU  211  CB  ASP A  25     1235   1253   1078     21     82     14       C  
ATOM    212  CG  ASP A  25      22.718  28.138  18.307  1.00 10.38           C  
ANISOU  212  CG  ASP A  25     1468   1240   1232    175    -38     63       C  
ATOM    213  OD1 ASP A  25      21.606  27.554  18.423  1.00 10.49           O  
ANISOU  213  OD1 ASP A  25     1268   1279   1437    101   -103   -106       O  
ATOM    214  OD2 ASP A  25      22.950  28.989  17.433  1.00 11.81           O  
ANISOU  214  OD2 ASP A  25     1433   1598   1454    125    -55    142       O  
ATOM    215  N   THR A  26      21.859  24.905  20.562  1.00  8.41           N  
ANISOU  215  N   THR A  26     1162   1085    949      0     96   -101       N  
ATOM    216  CA  THR A  26      21.386  23.566  20.190  1.00  8.04           C  
ANISOU  216  CA  THR A  26     1083   1070    899    -36     35    -40       C  
ATOM    217  C   THR A  26      20.648  23.556  18.880  1.00  8.17           C  
ANISOU  217  C   THR A  26     1111   1081    912      4    150     -6       C  
ATOM    218  O   THR A  26      20.489  22.492  18.288  1.00  8.68           O  
ANISOU  218  O   THR A  26     1293   1046    956     95     -5    -56       O  
ATOM    219  CB  THR A  26      20.495  22.967  21.267  1.00  8.00           C  
ANISOU  219  CB  THR A  26     1085    970    984     44      1    -56       C  
ATOM    220  OG1 THR A  26      19.409  23.844  21.563  1.00  8.69           O  
ANISOU  220  OG1 THR A  26     1158   1089   1053    115     63    -38       O  
ATOM    221  CG2 THR A  26      21.295  22.709  22.560  1.00  9.09           C  
ANISOU  221  CG2 THR A  26     1250   1139   1065    174     37     15       C  
ATOM    222  N   GLY A  27      20.199  24.723  18.372  1.00  7.84           N  
ANISOU  222  N   GLY A  27     1093    944    940     -5     96     -7       N  
ATOM    223  CA  GLY A  27      19.612  24.838  17.068  1.00  8.65           C  
ANISOU  223  CA  GLY A  27     1189   1097    999     55    -18    109       C  
ATOM    224  C   GLY A  27      20.580  24.986  15.932  1.00  8.31           C  
ANISOU  224  C   GLY A  27     1145   1055    957    128     23     51       C  
ATOM    225  O   GLY A  27      20.132  25.123  14.773  1.00  9.35           O  
ANISOU  225  O   GLY A  27     1198   1349   1006     88    -65    115       O  
ATOM    226  N   ALA A  28      21.856  24.973  16.210  1.00  8.21           N  
ANISOU  226  N   ALA A  28     1022   1168    928    135     64     10       N  
ATOM    227  CA  ALA A  28      22.892  25.033  15.169  1.00  8.59           C  
ANISOU  227  CA  ALA A  28     1209   1028   1027    142     19     67       C  
ATOM    228  C   ALA A  28      23.503  23.665  14.958  1.00  7.71           C  
ANISOU  228  C   ALA A  28      907   1054    968    -17    157      1       C  
ATOM    229  O   ALA A  28      23.988  23.034  15.918  1.00  8.48           O  
ANISOU  229  O   ALA A  28     1175   1100    945     85     -1     45       O  
ATOM    230  CB  ALA A  28      23.972  25.991  15.571  1.00  8.31           C  
ANISOU  230  CB  ALA A  28     1092   1150    915    151     12     87       C  
ATOM    231  N   ASP A  29      23.492  23.160  13.718  1.00  8.50           N  
ANISOU  231  N   ASP A  29     1231   1161    837    130     -1    -96       N  
ATOM    232  CA  ASP A  29      24.191  21.928  13.416  1.00  9.24           C  
ANISOU  232  CA  ASP A  29     1275   1238    995     95    212   -179       C  
ATOM    233  C   ASP A  29      25.682  22.139  13.572  1.00  9.82           C  
ANISOU  233  C   ASP A  29     1317   1267   1145    228    155   -186       C  
ATOM    234  O   ASP A  29      26.423  21.208  13.962  1.00 10.77           O  
ANISOU  234  O   ASP A  29     1393   1344   1354    284     20   -123       O  
ATOM    235  CB  ASP A  29      23.934  21.480  11.973  1.00 10.16           C  
ANISOU  235  CB  ASP A  29     1392   1320   1145     88    213   -234       C  
ATOM    236  CG  ASP A  29      22.488  21.270  11.630  1.00 11.43           C  
ANISOU  236  CG  ASP A  29     1568   1684   1089     68     -6   -116       C  
ATOM    237  OD1 ASP A  29      21.602  21.095  12.505  1.00 11.34           O  
ANISOU  237  OD1 ASP A  29     1464   1378   1466    113    -85    -25       O  
ATOM    238  OD2 ASP A  29      22.200  21.166  10.403  1.00 13.84           O  
ANISOU  238  OD2 ASP A  29     1748   2101   1407   -124   -113   -178       O  
ATOM    239  N   ASP A  30      26.121  23.313  13.168  1.00  9.92           N  
ANISOU  239  N   ASP A  30     1222   1348   1199    145    126    -71       N  
ATOM    240  CA  ASP A  30      27.545  23.670  12.985  1.00 10.48           C  
ANISOU  240  CA  ASP A  30     1304   1484   1191    210    186     62       C  
ATOM    241  C   ASP A  30      27.963  24.783  13.918  1.00 10.14           C  
ANISOU  241  C   ASP A  30     1274   1301   1276    102     68    169       C  
ATOM    242  O   ASP A  30      27.174  25.630  14.287  1.00 11.06           O  
ANISOU  242  O   ASP A  30     1136   1408   1655    139     35    -38       O  
ATOM    243  CB  ASP A  30      27.790  24.095  11.544  1.00 12.80           C  
ANISOU  243  CB  ASP A  30     1383   1933   1548     46    268    178       C  
ATOM    244  CG  ASP A  30      27.304  23.090  10.567  1.00 16.56           C  
ANISOU  244  CG  ASP A  30     1789   2807   1695    129    -48      3       C  
ATOM    245  OD1 ASP A  30      27.611  21.936  10.719  1.00 20.66           O  
ANISOU  245  OD1 ASP A  30     2666   2843   2339     23    391   -554       O  
ATOM    246  OD2 ASP A  30      26.521  23.392   9.651  1.00 29.18           O  
ANISOU  246  OD2 ASP A  30     3268   5742   2075   1169   -580   -868       O  
ATOM    247  N   THR A  31      29.260  24.806  14.222  1.00 10.81           N  
ANISOU  247  N   THR A  31     1187   1462   1455    279    -14   -185       N  
ATOM    248  CA  THR A  31      29.929  25.874  14.976  1.00  9.68           C  
ANISOU  248  CA  THR A  31     1241   1267   1167    192     88     62       C  
ATOM    249  C   THR A  31      30.409  26.961  14.006  1.00 10.39           C  
ANISOU  249  C   THR A  31     1227   1409   1309    142     66    235       C  
ATOM    250  O   THR A  31      31.077  26.652  13.017  1.00 11.54           O  
ANISOU  250  O   THR A  31     1388   1600   1395    219    354    176       O  
ATOM    251  CB  THR A  31      31.070  25.255  15.742  1.00  9.79           C  
ANISOU  251  CB  THR A  31     1036   1314   1369    113    165     96       C  
ATOM    252  OG1 THR A  31      30.521  24.363  16.716  1.00 10.39           O  
ANISOU  252  OG1 THR A  31     1155   1290   1501    133     30    292       O  
ATOM    253  CG2 THR A  31      31.896  26.279  16.453  1.00 11.59           C  
ANISOU  253  CG2 THR A  31     1106   1569   1728      0     10    329       C  
ATOM    254  N   VAL A  32      29.989  28.192  14.273  1.00 10.02           N  
ANISOU  254  N   VAL A  32     1147   1289   1369    101    126     84       N  
ATOM    255  CA  VAL A  32      30.273  29.340  13.384  1.00  9.86           C  
ANISOU  255  CA  VAL A  32     1187   1260   1297     93    128    208       C  
ATOM    256  C   VAL A  32      30.794  30.447  14.228  1.00 10.43           C  
ANISOU  256  C   VAL A  32     1443   1124   1394     31    -20    204       C  
ATOM    257  O   VAL A  32      30.123  30.918  15.153  1.00 10.70           O  
ANISOU  257  O   VAL A  32     1323   1322   1419    -19     61    144       O  
ATOM    258  CB  VAL A  32      29.035  29.788  12.591  1.00  9.96           C  
ANISOU  258  CB  VAL A  32     1226   1391   1165    142     78    182       C  
ATOM    259  CG1 VAL A  32      29.472  30.685  11.457  1.00 11.45           C  
ANISOU  259  CG1 VAL A  32     1505   1679   1165    218    -24    188       C  
ATOM    260  CG2 VAL A  32      28.280  28.616  12.052  1.00 11.48           C  
ANISOU  260  CG2 VAL A  32     1199   1669   1493    289     51     93       C  
ATOM    261  N   LEU A  33      32.020  30.890  13.917  1.00 10.63           N  
ANISOU  261  N   LEU A  33     1283   1262   1493    -48    102    183       N  
ATOM    262  CA  LEU A  33      32.664  31.982  14.629  1.00 10.43           C  
ANISOU  262  CA  LEU A  33     1263   1393   1305     76    118    298       C  
ATOM    263  C   LEU A  33      32.821  33.187  13.708  1.00 10.99           C  
ANISOU  263  C   LEU A  33     1199   1540   1434     67    -61    137       C  
ATOM    264  O   LEU A  33      32.975  33.045  12.513  1.00 11.39           O  
ANISOU  264  O   LEU A  33     1364   1582   1380    -11    -35    346       O  
ATOM    265  CB  LEU A  33      34.034  31.555  15.158  1.00 11.75           C  
ANISOU  265  CB  LEU A  33     1272   1483   1710     51    -56    462       C  
ATOM    266  CG  LEU A  33      34.038  30.342  16.075  1.00 13.47           C  
ANISOU  266  CG  LEU A  33     1540   1817   1759    310    -77    383       C  
ATOM    267  CD1 LEU A  33      35.442  30.092  16.586  1.00 15.13           C  
ANISOU  267  CD1 LEU A  33     1855   1648   2242    192   -274    549       C  
ATOM    268  CD2 LEU A  33      33.078  30.477  17.215  1.00 14.00           C  
ANISOU  268  CD2 LEU A  33     2129   1790   1397    -26   -204    390       C  
ATOM    269  N   GLU A  34      32.767  34.347  14.319  1.00 11.96           N  
ANISOU  269  N   GLU A  34     1540   1314   1689   -101    -64    221       N  
ATOM    270  CA  GLU A  34      33.059  35.623  13.638  1.00 13.57           C  
ANISOU  270  CA  GLU A  34     1652   1630   1872    -22   -190    530       C  
ATOM    271  C   GLU A  34      34.468  35.634  13.124  1.00 14.26           C  
ANISOU  271  C   GLU A  34     1664   1672   2080   -334   -156    550       C  
ATOM    272  O   GLU A  34      35.351  34.823  13.564  1.00 15.97           O  
ANISOU  272  O   GLU A  34     1684   1923   2461   -260   -268    790       O  
ATOM    273  CB  GLU A  34      32.847  36.786  14.626  1.00 16.99           C  
ANISOU  273  CB  GLU A  34     2329   1791   2335   -516   -138    490       C  
ATOM    274  CG  GLU A  34      31.411  36.889  15.194  1.00 19.71           C  
ANISOU  274  CG  GLU A  34     2713   2115   2660   -218     49    232       C  
ATOM    275  CD  GLU A  34      31.191  38.118  15.959  1.00 26.10           C  
ANISOU  275  CD  GLU A  34     4464   2405   3046   -250     21    205       C  
ATOM    276  OE1 GLU A  34      30.475  39.176  15.395  1.00 26.28           O  
ANISOU  276  OE1 GLU A  34     4027   2351   3605   -599   -140    243       O  
ATOM    277  OE2 GLU A  34      31.700  38.176  17.047  1.00 29.34           O  
ANISOU  277  OE2 GLU A  34     5408   2603   3137   -561   -732    305       O  
ATOM    278  N   GLU A  35      34.698  36.514  12.175  1.00 16.36           N  
ANISOU  278  N   GLU A  35     1669   2015   2531   -324   -132    996       N  
ATOM    279  CA  GLU A  35      35.990  36.650  11.528  1.00 17.77           C  
ANISOU  279  CA  GLU A  35     2129   2233   2388   -136    -72    817       C  
ATOM    280  C   GLU A  35      37.135  36.609  12.473  1.00 16.71           C  
ANISOU  280  C   GLU A  35     1935   2005   2409   -341   -130    562       C  
ATOM    281  O   GLU A  35      37.159  37.301  13.446  1.00 19.45           O  
ANISOU  281  O   GLU A  35     2119   2216   3054   -492   -289    377       O  
ATOM    282  CB  GLU A  35      36.047  37.946  10.703  1.00 19.52           C  
ANISOU  282  CB  GLU A  35     2215   2276   2923   -295    -46   1122       C  
ATOM    283  CG  GLU A  35      37.436  38.255  10.102  1.00 26.36           C  
ANISOU  283  CG  GLU A  35     2908   3309   3797   -477    496   1166       C  
ATOM    284  CD  GLU A  35      37.994  37.106   9.206  1.00 34.20           C  
ANISOU  284  CD  GLU A  35     4782   4590   3621   -323    156    159       C  
ATOM    285  OE1 GLU A  35      37.193  36.358   8.636  1.00 37.42           O  
ANISOU  285  OE1 GLU A  35     5521   4992   3703   -713    161    229       O  
ATOM    286  OE2 GLU A  35      39.302  36.994   9.056  1.00 43.68           O  
ANISOU  286  OE2 GLU A  35     5125   5852   5618   -201    356   -146       O  
ATOM    287  N   MET A  36      38.071  35.717  12.179  1.00 18.40           N  
ANISOU  287  N   MET A  36     1903   2161   2925   -467    -76    494       N  
ATOM    288  CA  MET A  36      39.325  35.509  12.967  1.00 19.59           C  
ANISOU  288  CA  MET A  36     2029   2473   2941   -508   -356    319       C  
ATOM    289  C   MET A  36      40.285  34.749  12.085  1.00 21.04           C  
ANISOU  289  C   MET A  36     2186   2924   2884   -403   -316    346       C  
ATOM    290  O   MET A  36      39.923  34.228  11.096  1.00 20.86           O  
ANISOU  290  O   MET A  36     1756   3499   2669    -93    -90    247       O  
ATOM    291  CB  MET A  36      39.040  34.723  14.206  1.00 18.89           C  
ANISOU  291  CB  MET A  36     2321   2023   2831   -415   -355    284       C  
ATOM    292  CG  MET A  36      38.683  33.296  13.972  1.00 17.19           C  
ANISOU  292  CG  MET A  36     1765   2170   2597   -169   -157    625       C  
ATOM    293  SD  MET A  36      38.555  32.305  15.425  1.00 20.88           S  
ANISOU  293  SD  MET A  36     2177   2364   3392   -174    319    551       S  
ATOM    294  CE  MET A  36      40.313  32.377  16.087  1.00 19.79           C  
ANISOU  294  CE  MET A  36     2257   2640   2620   -129    286    651       C  
ATOM    295  N   ASN A  37      41.582  34.807  12.419  1.00 21.74           N  
ANISOU  295  N   ASN A  37     2096   2869   3295   -339   -211    411       N  
ATOM    296  CA  ASN A  37      42.570  33.987  11.732  1.00 21.71           C  
ANISOU  296  CA  ASN A  37     2469   2807   2972   -340     84    586       C  
ATOM    297  C   ASN A  37      42.726  32.644  12.445  1.00 20.22           C  
ANISOU  297  C   ASN A  37     2136   2806   2741    196    -41    481       C  
ATOM    298  O   ASN A  37      42.709  32.595  13.651  1.00 20.97           O  
ANISOU  298  O   ASN A  37     2061   3246   2658    164    407    536       O  
ATOM    299  CB  ASN A  37      43.900  34.715  11.669  1.00 25.14           C  
ANISOU  299  CB  ASN A  37     2422   3566   3564   -505    187    693       C  
ATOM    300  CG  ASN A  37      43.805  36.057  10.895  1.00 27.66           C  
ANISOU  300  CG  ASN A  37     3322   3403   3784   -632    159    595       C  
ATOM    301  OD1 ASN A  37      44.126  37.178  11.454  1.00 35.11           O  
ANISOU  301  OD1 ASN A  37     4821   3589   4929   -729    355    269       O  
ATOM    302  ND2 ASN A  37      43.404  35.980   9.690  1.00 30.91           N  
ANISOU  302  ND2 ASN A  37     3348   4619   3777   -540    123    937       N  
ATOM    303  N   LEU A  38      42.770  31.587  11.682  1.00 19.08           N  
ANISOU  303  N   LEU A  38     1769   3060   2417    -13   -240    514       N  
ATOM    304  CA  LEU A  38      43.145  30.242  12.191  1.00 20.76           C  
ANISOU  304  CA  LEU A  38     2193   2897   2795    112   -204    158       C  
ATOM    305  C   LEU A  38      44.216  29.639  11.276  1.00 20.91           C  
ANISOU  305  C   LEU A  38     2416   3394   2133     14   -386   -124       C  
ATOM    306  O   LEU A  38      44.149  29.752  10.093  1.00 23.11           O  
ANISOU  306  O   LEU A  38     1682   4568   2530    174   -314      5       O  
ATOM    307  CB  LEU A  38      41.915  29.296  12.215  1.00 21.98           C  
ANISOU  307  CB  LEU A  38     2484   3196   2669     52     55    -59       C  
ATOM    308  CG  LEU A  38      40.893  29.505  13.284  1.00 21.42           C  
ANISOU  308  CG  LEU A  38     2430   3434   2273   -149    -86    -78       C  
ATOM    309  CD1 LEU A  38      39.650  28.635  13.067  1.00 20.59           C  
ANISOU  309  CD1 LEU A  38     2965   2729   2128   -130   -306    592       C  
ATOM    310  CD2 LEU A  38      41.500  29.256  14.649  1.00 21.38           C  
ANISOU  310  CD2 LEU A  38     3179   2729   2215   -208      8   -343       C  
ATOM    311  N   PRO A  39      45.081  28.825  11.834  1.00 25.42           N  
ANISOU  311  N   PRO A  39     2598   3843   3215    347   -437   -318       N  
ATOM    312  CA  PRO A  39      46.090  28.159  11.052  1.00 26.48           C  
ANISOU  312  CA  PRO A  39     2840   3798   3422    238   -352   -351       C  
ATOM    313  C   PRO A  39      45.562  27.031  10.171  1.00 25.01           C  
ANISOU  313  C   PRO A  39     2645   3447   3410    261   -191   -316       C  
ATOM    314  O   PRO A  39      44.673  26.312  10.562  1.00 27.21           O  
ANISOU  314  O   PRO A  39     2537   4103   3698    203   -219   -258       O  
ATOM    315  CB  PRO A  39      47.070  27.607  12.120  1.00 27.82           C  
ANISOU  315  CB  PRO A  39     2915   3806   3847    131   -857   -435       C  
ATOM    316  CG  PRO A  39      46.598  28.174  13.455  1.00 29.92           C  
ANISOU  316  CG  PRO A  39     3283   3816   4267    564   -351   -214       C  
ATOM    317  CD  PRO A  39      45.194  28.542  13.275  1.00 25.52           C  
ANISOU  317  CD  PRO A  39     3003   3292   3399    442   -649   -117       C  
ATOM    318  N   GLY A  40      46.273  26.771   9.080  1.00 26.67           N  
ANISOU  318  N   GLY A  40     2544   3786   3802    -11   -131   -434       N  
ATOM    319  CA  GLY A  40      46.069  25.598   8.306  1.00 27.90           C  
ANISOU  319  CA  GLY A  40     3076   3764   3757     99     -9   -439       C  
ATOM    320  C   GLY A  40      45.135  25.804   7.129  1.00 25.39           C  
ANISOU  320  C   GLY A  40     2459   3638   3550    220    160   -477       C  
ATOM    321  O   GLY A  40      44.690  26.967   6.791  1.00 26.01           O  
ANISOU  321  O   GLY A  40     2498   3598   3785   -206    198   -458       O  
ATOM    322  N   LYS A  41      44.866  24.735   6.474  1.00 25.54           N  
ANISOU  322  N   LYS A  41     2300   3559   3843    444    -29   -379       N  
ATOM    323  CA  LYS A  41      44.077  24.731   5.314  1.00 24.79           C  
ANISOU  323  CA  LYS A  41     2387   3698   3332    438    162   -450       C  
ATOM    324  C   LYS A  41      42.588  25.015   5.658  1.00 22.94           C  
ANISOU  324  C   LYS A  41     2003   3402   3311    519    307    -88       C  
ATOM    325  O   LYS A  41      42.093  24.657   6.796  1.00 24.65           O  
ANISOU  325  O   LYS A  41     2789   3511   3063    344   -235    136       O  
ATOM    326  CB  LYS A  41      44.194  23.364   4.616  1.00 27.25           C  
ANISOU  326  CB  LYS A  41     2722   3694   3936    792    -57   -493       C  
ATOM    327  N   TRP A  42      41.906  25.708   4.761  1.00 20.48           N  
ANISOU  327  N   TRP A  42     1868   3528   2383   -113    299    -34       N  
ATOM    328  CA  TRP A  42      40.471  25.831   4.864  1.00 17.40           C  
ANISOU  328  CA  TRP A  42     1587   2739   2285     16    285    131       C  
ATOM    329  C   TRP A  42      39.828  25.668   3.497  1.00 18.14           C  
ANISOU  329  C   TRP A  42     1829   2975   2086    145    374     31       C  
ATOM    330  O   TRP A  42      40.511  25.744   2.470  1.00 20.51           O  
ANISOU  330  O   TRP A  42     2218   3467   2106     13    632   -142       O  
ATOM    331  CB  TRP A  42      40.076  27.165   5.499  1.00 17.80           C  
ANISOU  331  CB  TRP A  42     2176   2722   1862   -284    158     -6       C  
ATOM    332  CG  TRP A  42      40.619  28.413   4.760  1.00 18.54           C  
ANISOU  332  CG  TRP A  42     1923   3094   2025    -59    134    177       C  
ATOM    333  CD1 TRP A  42      41.801  28.989   4.950  1.00 22.42           C  
ANISOU  333  CD1 TRP A  42     2500   3955   2061   -603    -78    196       C  
ATOM    334  CD2 TRP A  42      39.995  29.117   3.696  1.00 17.55           C  
ANISOU  334  CD2 TRP A  42     2215   2862   1592    -53    833    138       C  
ATOM    335  NE1 TRP A  42      41.933  30.073   4.151  1.00 22.53           N  
ANISOU  335  NE1 TRP A  42     2606   3371   2583   -732     73    176       N  
ATOM    336  CE2 TRP A  42      40.848  30.138   3.322  1.00 19.64           C  
ANISOU  336  CE2 TRP A  42     2109   3119   2234    -19    687    268       C  
ATOM    337  CE3 TRP A  42      38.789  29.015   3.073  1.00 17.18           C  
ANISOU  337  CE3 TRP A  42     2207   2386   1931    123    570   -204       C  
ATOM    338  CZ2 TRP A  42      40.491  31.095   2.357  1.00 22.13           C  
ANISOU  338  CZ2 TRP A  42     3246   2732   2429   -605    216    273       C  
ATOM    339  CZ3 TRP A  42      38.447  29.930   2.088  1.00 20.03           C  
ANISOU  339  CZ3 TRP A  42     2776   2749   2082   -189     34     69       C  
ATOM    340  CH2 TRP A  42      39.281  30.946   1.756  1.00 21.14           C  
ANISOU  340  CH2 TRP A  42     3227   3110   1695   -255    563    178       C  
ATOM    341  N   LYS A  43      38.530  25.368   3.481  1.00 16.57           N  
ANISOU  341  N   LYS A  43     1730   2568   1995    295    272    -24       N  
ATOM    342  CA  LYS A  43      37.784  25.272   2.263  1.00 18.91           C  
ANISOU  342  CA  LYS A  43     2093   2902   2189    508    112    -57       C  
ATOM    343  C   LYS A  43      36.677  26.281   2.281  1.00 16.98           C  
ANISOU  343  C   LYS A  43     1793   2467   2191    435    304   -103       C  
ATOM    344  O   LYS A  43      36.012  26.458   3.269  1.00 16.53           O  
ANISOU  344  O   LYS A  43     1833   2607   1840    405    454      0       O  
ATOM    345  CB  LYS A  43      37.225  23.898   2.129  1.00 24.19           C  
ANISOU  345  CB  LYS A  43     2905   3140   3146    512   -233   -447       C  
ATOM    346  N   PRO A  44      36.377  26.858   1.126  1.00 16.62           N  
ANISOU  346  N   PRO A  44     1626   2822   1865    453    273   -160       N  
ATOM    347  CA  PRO A  44      35.176  27.666   1.004  1.00 16.12           C  
ANISOU  347  CA  PRO A  44     1659   2405   2059    325     84    -74       C  
ATOM    348  C   PRO A  44      33.929  26.831   1.098  1.00 16.08           C  
ANISOU  348  C   PRO A  44     1886   2076   2144    261    258     34       C  
ATOM    349  O   PRO A  44      33.823  25.799   0.471  1.00 18.72           O  
ANISOU  349  O   PRO A  44     1852   2612   2647    258    317   -464       O  
ATOM    350  CB  PRO A  44      35.302  28.262  -0.399  1.00 17.89           C  
ANISOU  350  CB  PRO A  44     2178   2450   2168    171    496    213       C  
ATOM    351  CG  PRO A  44      36.699  28.037  -0.837  1.00 20.86           C  
ANISOU  351  CG  PRO A  44     2591   3625   1709    405    524    -44       C  
ATOM    352  CD  PRO A  44      37.216  26.876  -0.079  1.00 18.30           C  
ANISOU  352  CD  PRO A  44     1844   3203   1903    343    181   -297       C  
ATOM    353  N   LYS A  45      32.960  27.292   1.884  1.00 14.76           N  
ANISOU  353  N   LYS A  45     1726   2039   1841    206      5   -377       N  
ATOM    354  CA  LYS A  45      31.672  26.614   2.032  1.00 14.58           C  
ANISOU  354  CA  LYS A  45     1824   2015   1700    215    -17   -386       C  
ATOM    355  C   LYS A  45      30.576  27.697   2.122  1.00 13.40           C  
ANISOU  355  C   LYS A  45     1749   1819   1521    170    -56   -409       C  
ATOM    356  O   LYS A  45      30.877  28.890   2.350  1.00 14.14           O  
ANISOU  356  O   LYS A  45     1559   1859   1952    220     22   -230       O  
ATOM    357  CB  LYS A  45      31.665  25.726   3.266  1.00 18.03           C  
ANISOU  357  CB  LYS A  45     2280   1997   2574    391   -186    -28       C  
ATOM    358  CG  LYS A  45      32.634  24.460   3.145  1.00 24.24           C  
ANISOU  358  CG  LYS A  45     2673   2825   3712    498   -366     77       C  
ATOM    359  CD  LYS A  45      32.063  23.377   2.296  1.00 27.54           C  
ANISOU  359  CD  LYS A  45     3181   3004   4277    508   -122   -207       C  
ATOM    360  CE  LYS A  45      32.953  22.065   2.333  1.00 28.24           C  
ANISOU  360  CE  LYS A  45     3775   2674   4279    450     53   -263       C  
ATOM    361  NZ  LYS A  45      32.731  21.251   1.084  1.00 39.83           N  
ANISOU  361  NZ  LYS A  45     5741   4177   5215     53   -558   -916       N  
ATOM    362  N   MET A  46      29.358  27.260   1.998  1.00 13.14           N  
ANISOU  362  N   MET A  46     1737   1829   1427    161    -31   -288       N  
ATOM    363  CA  MET A  46      28.178  28.123   2.243  1.00 13.59           C  
ANISOU  363  CA  MET A  46     1745   1681   1738    190    114   -146       C  
ATOM    364  C   MET A  46      27.286  27.454   3.219  1.00 13.33           C  
ANISOU  364  C   MET A  46     1737   1519   1808    141    172    -55       C  
ATOM    365  O   MET A  46      27.165  26.243   3.223  1.00 15.98           O  
ANISOU  365  O   MET A  46     2045   1608   2418    184    519   -220       O  
ATOM    366  CB  MET A  46      27.428  28.373   0.937  1.00 13.92           C  
ANISOU  366  CB  MET A  46     1650   1826   1810    325   -105   -249       C  
ATOM    367  CG  MET A  46      28.192  29.272   0.003  1.00 15.83           C  
ANISOU  367  CG  MET A  46     2240   2473   1300    144    -67   -224       C  
ATOM    368  SD  MET A  46      27.339  29.508  -1.542  1.00 19.09           S  
ANISOU  368  SD  MET A  46     2837   2662   1754    210   -396   -349       S  
ATOM    369  CE  MET A  46      25.876  30.430  -0.989  1.00 20.19           C  
ANISOU  369  CE  MET A  46     2870   2803   1999    797   -306   -124       C  
ATOM    370  N  AILE A  47      26.614  28.259   4.045  0.50 11.47           N  
ANISOU  370  N  AILE A  47     1322   1568   1466    119     37    -16       N  
ATOM    371  N  BILE A  47      26.684  28.244   4.130  0.50 11.95           N  
ANISOU  371  N  BILE A  47     1526   1581   1433    172    138     27       N  
ATOM    372  CA AILE A  47      25.721  27.757   5.045  0.50 12.92           C  
ANISOU  372  CA AILE A  47     1587   1489   1832    117    146   -136       C  
ATOM    373  CA BILE A  47      25.632  27.730   5.008  0.50 12.13           C  
ANISOU  373  CA BILE A  47     1575   1368   1666    160    110   -196       C  
ATOM    374  C  AILE A  47      24.520  28.717   5.159  0.50 12.79           C  
ANISOU  374  C  AILE A  47     1565   1636   1658    168     49    -15       C  
ATOM    375  C  BILE A  47      24.480  28.684   5.063  0.50 12.05           C  
ANISOU  375  C  BILE A  47     1450   1594   1531    185   -100    -57       C  
ATOM    376  O  AILE A  47      24.661  29.907   4.948  0.50 12.70           O  
ANISOU  376  O  AILE A  47     1515   1479   1829    209    149     27       O  
ATOM    377  O  BILE A  47      24.657  29.887   4.910  0.50 12.53           O  
ANISOU  377  O  BILE A  47     1510   1464   1785    249    187     15       O  
ATOM    378  CB AILE A  47      26.460  27.598   6.438  0.50 13.91           C  
ANISOU  378  CB AILE A  47     1762   1698   1825    259    231    -90       C  
ATOM    379  CB BILE A  47      26.165  27.442   6.474  0.50 11.48           C  
ANISOU  379  CB BILE A  47     1425   1295   1641    338    249   -167       C  
ATOM    380  CG1AILE A  47      25.631  26.829   7.391  0.50 16.03           C  
ANISOU  380  CG1AILE A  47     1554   2103   2430   -161    193      2       C  
ATOM    381  CG1BILE A  47      26.745  28.728   7.117  0.50 11.13           C  
ANISOU  381  CG1BILE A  47     1438   1467   1321    270     52     99       C  
ATOM    382  CG2AILE A  47      26.807  28.962   7.058  0.50 16.42           C  
ANISOU  382  CG2AILE A  47     2124   2055   2059    181     71    -45       C  
ATOM    383  CG2BILE A  47      27.195  26.398   6.444  0.50 12.59           C  
ANISOU  383  CG2BILE A  47     1260   1439   2085    219    -22    104       C  
ATOM    384  CD1AILE A  47      26.404  26.234   8.490  0.50 18.22           C  
ANISOU  384  CD1AILE A  47     2278   2312   2331   -155    276    248       C  
ATOM    385  CD1BILE A  47      26.915  28.692   8.641  0.50 11.62           C  
ANISOU  385  CD1BILE A  47     1507   1619   1286    194      0     63       C  
ATOM    386  N   GLY A  48      23.357  28.156   5.461  1.00 12.00           N  
ANISOU  386  N   GLY A  48     1530   1500   1530    123     57    -17       N  
ATOM    387  CA  GLY A  48      22.140  28.930   5.627  1.00 12.49           C  
ANISOU  387  CA  GLY A  48     1436   1594   1714     56     51     48       C  
ATOM    388  C   GLY A  48      21.682  28.998   7.054  1.00 10.90           C  
ANISOU  388  C   GLY A  48     1510   1446   1186    103     58    141       C  
ATOM    389  O   GLY A  48      21.710  28.020   7.754  1.00 13.65           O  
ANISOU  389  O   GLY A  48     2212   1465   1509    255     80    106       O  
ATOM    390  N   GLY A  49      21.127  30.125   7.401  1.00 12.17           N  
ANISOU  390  N   GLY A  49     1494   1649   1481    304     28    249       N  
ATOM    391  CA  GLY A  49      20.531  30.386   8.694  1.00 11.10           C  
ANISOU  391  CA  GLY A  49     1370   1496   1348    281     43    287       C  
ATOM    392  C   GLY A  49      19.125  30.987   8.484  1.00 11.19           C  
ANISOU  392  C   GLY A  49     1573   1586   1090    255    -25    257       C  
ATOM    393  O   GLY A  49      18.503  30.806   7.401  1.00 12.43           O  
ANISOU  393  O   GLY A  49     1507   1835   1378    308    -79     -5       O  
ATOM    394  N   ILE A  50      18.607  31.602   9.501  1.00 10.19           N  
ANISOU  394  N   ILE A  50     1296   1372   1204    225    -76    202       N  
ATOM    395  CA  ILE A  50      17.245  32.068   9.435  1.00 10.92           C  
ANISOU  395  CA  ILE A  50     1388   1290   1471    189    103    103       C  
ATOM    396  C   ILE A  50      17.054  33.106   8.329  1.00 11.50           C  
ANISOU  396  C   ILE A  50     1373   1480   1517    240    -90    118       C  
ATOM    397  O   ILE A  50      15.949  33.258   7.803  1.00 12.89           O  
ANISOU  397  O   ILE A  50     1286   2034   1576    315   -147     72       O  
ATOM    398  CB  ILE A  50      16.762  32.604  10.811  1.00 12.62           C  
ANISOU  398  CB  ILE A  50     1500   1744   1548    337     -7    158       C  
ATOM    399  CG1 ILE A  50      15.244  32.402  10.939  1.00 13.79           C  
ANISOU  399  CG1 ILE A  50     1463   2360   1417    355     43    359       C  
ATOM    400  CG2 ILE A  50      17.244  34.025  11.037  1.00 14.24           C  
ANISOU  400  CG2 ILE A  50     2009   1742   1656    538   -159     37       C  
ATOM    401  CD1 ILE A  50      14.670  32.795  12.264  1.00 16.34           C  
ANISOU  401  CD1 ILE A  50     1808   2733   1667    608    -40    449       C  
ATOM    402  N   GLY A  51      18.093  33.877   8.024  1.00 12.09           N  
ANISOU  402  N   GLY A  51     1369   1495   1728    193   -117    311       N  
ATOM    403  CA  GLY A  51      17.999  35.016   7.146  1.00 12.75           C  
ANISOU  403  CA  GLY A  51     1534   1597   1711    182    -62    192       C  
ATOM    404  C   GLY A  51      18.533  34.794   5.785  1.00 13.69           C  
ANISOU  404  C   GLY A  51     1570   1745   1887    188   -112    259       C  
ATOM    405  O   GLY A  51      18.530  35.731   4.983  1.00 16.49           O  
ANISOU  405  O   GLY A  51     2647   1787   1831    414    392    435       O  
ATOM    406  N   GLY A  52      18.975  33.583   5.460  1.00 12.96           N  
ANISOU  406  N   GLY A  52     1657   1673   1591    241   -147    113       N  
ATOM    407  CA  GLY A  52      19.580  33.270   4.143  1.00 15.11           C  
ANISOU  407  CA  GLY A  52     1764   2319   1656    119   -157    -11       C  
ATOM    408  C   GLY A  52      20.961  32.649   4.313  1.00 11.45           C  
ANISOU  408  C   GLY A  52     1378   1630   1340     72   -157     96       C  
ATOM    409  O   GLY A  52      21.323  32.162   5.367  1.00 13.35           O  
ANISOU  409  O   GLY A  52     1790   1917   1362    484   -105    274       O  
ATOM    410  N   PHE A  53      21.719  32.715   3.235  1.00 11.37           N  
ANISOU  410  N   PHE A  53     1501   1693   1125     73   -253     48       N  
ATOM    411  CA  PHE A  53      22.973  32.032   3.102  1.00 10.60           C  
ANISOU  411  CA  PHE A  53     1484   1388   1152     16     25    -43       C  
ATOM    412  C   PHE A  53      24.141  32.987   3.193  1.00 10.82           C  
ANISOU  412  C   PHE A  53     1625   1361   1123    144    111      0       C  
ATOM    413  O   PHE A  53      24.081  34.093   2.717  1.00 12.42           O  
ANISOU  413  O   PHE A  53     1673   1554   1492     32   -279    185       O  
ATOM    414  CB  PHE A  53      23.017  31.226   1.805  1.00 13.29           C  
ANISOU  414  CB  PHE A  53     2004   1620   1426     38   -264   -405       C  
ATOM    415  CG  PHE A  53      22.251  29.989   1.874  1.00 14.51           C  
ANISOU  415  CG  PHE A  53     2196   1904   1413     80   -434   -286       C  
ATOM    416  CD1 PHE A  53      20.855  29.994   1.857  1.00 15.65           C  
ANISOU  416  CD1 PHE A  53     2140   2096   1708   -295   -405   -103       C  
ATOM    417  CD2 PHE A  53      22.898  28.798   2.053  1.00 15.67           C  
ANISOU  417  CD2 PHE A  53     2390   1834   1729    186   -457   -374       C  
ATOM    418  CE1 PHE A  53      20.145  28.860   2.083  1.00 18.18           C  
ANISOU  418  CE1 PHE A  53     2438   2455   2012   -157   -942   -101       C  
ATOM    419  CE2 PHE A  53      22.157  27.587   2.147  1.00 18.77           C  
ANISOU  419  CE2 PHE A  53     2767   1829   2534    135   -385   -288       C  
ATOM    420  CZ  PHE A  53      20.801  27.659   2.229  1.00 18.35           C  
ANISOU  420  CZ  PHE A  53     2828   1837   2306   -412   -834   -298       C  
ATOM    421  N   ILE A  54      25.249  32.475   3.756  1.00 10.69           N  
ANISOU  421  N   ILE A  54     1450   1336   1273     99    -98    -50       N  
ATOM    422  CA  ILE A  54      26.504  33.162   3.817  1.00 10.77           C  
ANISOU  422  CA  ILE A  54     1300   1547   1244     95    -44    -57       C  
ATOM    423  C   ILE A  54      27.643  32.272   3.359  1.00 10.93           C  
ANISOU  423  C   ILE A  54     1431   1456   1265    136    -52     84       C  
ATOM    424  O   ILE A  54      27.529  31.043   3.330  1.00 11.77           O  
ANISOU  424  O   ILE A  54     1458   1511   1502    104    170   -160       O  
ATOM    425  CB  ILE A  54      26.799  33.684   5.294  1.00 10.94           C  
ANISOU  425  CB  ILE A  54     1440   1225   1489     43    -41    -52       C  
ATOM    426  CG1 ILE A  54      26.981  32.499   6.274  1.00 10.79           C  
ANISOU  426  CG1 ILE A  54     1374   1572   1154    -62    199    -71       C  
ATOM    427  CG2 ILE A  54      25.727  34.626   5.767  1.00 12.19           C  
ANISOU  427  CG2 ILE A  54     1735   1436   1460    188    189     11       C  
ATOM    428  CD1 ILE A  54      27.571  32.927   7.581  1.00 11.45           C  
ANISOU  428  CD1 ILE A  54     1328   1659   1361    -20     62    -29       C  
ATOM    429  N   LYS A  55      28.744  32.912   2.999  1.00 10.89           N  
ANISOU  429  N   LYS A  55     1455   1484   1197    111    141    167       N  
ATOM    430  CA  LYS A  55      29.984  32.258   2.741  1.00 11.78           C  
ANISOU  430  CA  LYS A  55     1477   1615   1381    113     -4     44       C  
ATOM    431  C   LYS A  55      30.814  32.183   4.001  1.00 11.28           C  
ANISOU  431  C   LYS A  55     1531   1563   1192     95     83      9       C  
ATOM    432  O   LYS A  55      30.868  33.115   4.762  1.00 13.06           O  
ANISOU  432  O   LYS A  55     1812   1717   1433     96   -205    -29       O  
ATOM    433  CB  LYS A  55      30.781  32.994   1.660  1.00 12.60           C  
ANISOU  433  CB  LYS A  55     1578   1748   1459     85    -27    118       C  
ATOM    434  CG  LYS A  55      30.100  32.998   0.307  1.00 15.31           C  
ANISOU  434  CG  LYS A  55     1854   2453   1509    131    -34    154       C  
ATOM    435  CD  LYS A  55      30.691  34.017  -0.642  1.00 18.61           C  
ANISOU  435  CD  LYS A  55     2581   2797   1693    273    446    180       C  
ATOM    436  CE  LYS A  55      32.068  33.732  -0.973  1.00 21.97           C  
ANISOU  436  CE  LYS A  55     2747   3413   2186     32    803    633       C  
ATOM    437  NZ  LYS A  55      32.607  34.726  -1.947  1.00 28.59           N  
ANISOU  437  NZ  LYS A  55     3868   4362   2630   -201   1414    732       N  
ATOM    438  N   VAL A  56      31.389  31.022   4.250  1.00 11.48           N  
ANISOU  438  N   VAL A  56     1476   1614   1270    101     45    -68       N  
ATOM    439  CA  VAL A  56      32.262  30.783   5.368  1.00 11.33           C  
ANISOU  439  CA  VAL A  56     1299   1617   1388     88   -148    110       C  
ATOM    440  C   VAL A  56      33.556  30.087   4.887  1.00 13.60           C  
ANISOU  440  C   VAL A  56     1661   1804   1700     11    -18   -138       C  
ATOM    441  O   VAL A  56      33.617  29.495   3.807  1.00 14.57           O  
ANISOU  441  O   VAL A  56     1550   2213   1771    238     73    -60       O  
ATOM    442  CB  VAL A  56      31.565  29.890   6.474  1.00 12.18           C  
ANISOU  442  CB  VAL A  56     1421   1879   1325    114    109     90       C  
ATOM    443  CG1 VAL A  56      30.416  30.614   7.050  1.00 13.28           C  
ANISOU  443  CG1 VAL A  56     1457   1976   1613   -127    208    298       C  
ATOM    444  CG2 VAL A  56      31.165  28.535   5.935  1.00 13.59           C  
ANISOU  444  CG2 VAL A  56     1665   1940   1556    -30    229    341       C  
ATOM    445  N   ARG A  57      34.535  30.131   5.768  1.00 12.36           N  
ANISOU  445  N   ARG A  57     1395   1856   1445     33    107     41       N  
ATOM    446  CA  ARG A  57      35.747  29.317   5.648  1.00 12.54           C  
ANISOU  446  CA  ARG A  57     1269   2070   1426    139     19    139       C  
ATOM    447  C   ARG A  57      35.633  28.150   6.602  1.00 13.16           C  
ANISOU  447  C   ARG A  57     1198   1999   1802     70    200    123       C  
ATOM    448  O   ARG A  57      35.399  28.336   7.783  1.00 13.25           O  
ANISOU  448  O   ARG A  57     1460   1904   1669    124    369    207       O  
ATOM    449  CB  ARG A  57      37.002  30.155   6.009  1.00 14.02           C  
ANISOU  449  CB  ARG A  57     1337   2270   1719    171    315    248       C  
ATOM    450  CG  ARG A  57      37.164  31.460   5.161  1.00 16.21           C  
ANISOU  450  CG  ARG A  57     1889   2382   1885   -102    195    240       C  
ATOM    451  CD  ARG A  57      38.492  32.086   5.242  1.00 18.93           C  
ANISOU  451  CD  ARG A  57     1991   2607   2594   -237    191    -27       C  
ATOM    452  NE  ARG A  57      38.955  32.250   6.528  1.00 21.79           N  
ANISOU  452  NE  ARG A  57     2435   3179   2663   -381    496    424       N  
ATOM    453  CZ  ARG A  57      38.786  33.339   7.295  1.00 23.99           C  
ANISOU  453  CZ  ARG A  57     2648   3669   2797   -268    143    246       C  
ATOM    454  NH1 ARG A  57      37.908  34.290   6.961  1.00 30.84           N  
ANISOU  454  NH1 ARG A  57     3640   3690   4385     44     28    393       N  
ATOM    455  NH2 ARG A  57      39.412  33.414   8.455  1.00 25.76           N  
ANISOU  455  NH2 ARG A  57     2678   4236   2872  -1085      8     12       N  
ATOM    456  N   GLN A  58      35.774  26.931   6.062  1.00 13.70           N  
ANISOU  456  N   GLN A  58     1525   1998   1682    227    361    211       N  
ATOM    457  CA  GLN A  58      35.655  25.697   6.859  1.00 14.73           C  
ANISOU  457  CA  GLN A  58     1477   2142   1976    342    399    307       C  
ATOM    458  C   GLN A  58      36.992  25.206   7.228  1.00 16.12           C  
ANISOU  458  C   GLN A  58     1545   2255   2324    383    564    313       C  
ATOM    459  O   GLN A  58      37.813  24.852   6.333  1.00 16.24           O  
ANISOU  459  O   GLN A  58     1737   2409   2022    513    534    318       O  
ATOM    460  CB  GLN A  58      34.907  24.608   6.116  1.00 15.98           C  
ANISOU  460  CB  GLN A  58     1680   2101   2287    316    532    -43       C  
ATOM    461  CG  GLN A  58      34.880  23.308   6.844  1.00 19.05           C  
ANISOU  461  CG  GLN A  58     2153   2334   2747    347    998     27       C  
ATOM    462  CD  GLN A  58      34.080  22.227   6.132  1.00 22.51           C  
ANISOU  462  CD  GLN A  58     2754   2293   3505    223     25     -1       C  
ATOM    463  OE1 GLN A  58      33.035  22.504   5.567  1.00 28.13           O  
ANISOU  463  OE1 GLN A  58     3481   2479   4726    131   -512   -123       O  
ATOM    464  NE2 GLN A  58      34.435  20.988   6.397  1.00 28.81           N  
ANISOU  464  NE2 GLN A  58     4402   2282   4262    216    572     76       N  
ATOM    465  N   TYR A  59      37.280  25.189   8.537  1.00 14.95           N  
ANISOU  465  N   TYR A  59     1315   1914   2452    416    588    277       N  
ATOM    466  CA  TYR A  59      38.467  24.614   9.068  1.00 15.20           C  
ANISOU  466  CA  TYR A  59     1497   2301   1978    181    537    525       C  
ATOM    467  C   TYR A  59      38.098  23.298   9.756  1.00 16.18           C  
ANISOU  467  C   TYR A  59     1473   2222   2450    505    482    363       C  
ATOM    468  O   TYR A  59      37.283  23.275  10.684  1.00 17.45           O  
ANISOU  468  O   TYR A  59     1592   2237   2801    587    704    756       O  
ATOM    469  CB  TYR A  59      39.078  25.553  10.098  1.00 14.84           C  
ANISOU  469  CB  TYR A  59     1145   2578   1916    626    259    514       C  
ATOM    470  CG  TYR A  59      39.570  26.927   9.538  1.00 15.73           C  
ANISOU  470  CG  TYR A  59     1569   2338   2069    246    328    513       C  
ATOM    471  CD1 TYR A  59      38.699  27.947   9.350  1.00 16.06           C  
ANISOU  471  CD1 TYR A  59     1718   2262   2122    238    230    223       C  
ATOM    472  CD2 TYR A  59      40.914  27.137   9.196  1.00 16.55           C  
ANISOU  472  CD2 TYR A  59     1641   2626   2020    -14    141    248       C  
ATOM    473  CE1 TYR A  59      39.098  29.125   8.881  1.00 16.82           C  
ANISOU  473  CE1 TYR A  59     2000   2106   2282    264     59    341       C  
ATOM    474  CE2 TYR A  59      41.315  28.370   8.723  1.00 17.81           C  
ANISOU  474  CE2 TYR A  59     1846   2654   2265   -422    166     60       C  
ATOM    475  CZ  TYR A  59      40.414  29.343   8.573  1.00 18.86           C  
ANISOU  475  CZ  TYR A  59     2628   2418   2118   -370     45    554       C  
ATOM    476  OH  TYR A  59      40.808  30.628   8.062  1.00 23.73           O  
ANISOU  476  OH  TYR A  59     3455   2541   3019  -1056   -307    716       O  
ATOM    477  N   ASP A  60      38.837  22.240   9.444  1.00 19.24           N  
ANISOU  477  N   ASP A  60     1948   2379   2982    552    701    464       N  
ATOM    478  CA  ASP A  60      38.545  20.953   9.994  1.00 19.11           C  
ANISOU  478  CA  ASP A  60     2053   2252   2955    407    473    164       C  
ATOM    479  C   ASP A  60      39.469  20.595  11.129  1.00 18.20           C  
ANISOU  479  C   ASP A  60     1810   2557   2546    388    786    309       C  
ATOM    480  O   ASP A  60      40.642  21.038  11.191  1.00 20.89           O  
ANISOU  480  O   ASP A  60     1959   2468   3510    556    732    842       O  
ATOM    481  CB  ASP A  60      38.592  19.894   8.920  1.00 22.52           C  
ANISOU  481  CB  ASP A  60     2777   2668   3110    436    436     -7       C  
ATOM    482  CG  ASP A  60      37.455  20.030   7.920  1.00 27.11           C  
ANISOU  482  CG  ASP A  60     3115   3389   3796    704     91    184       C  
ATOM    483  OD1 ASP A  60      36.234  20.343   8.361  1.00 27.27           O  
ANISOU  483  OD1 ASP A  60     3533   3325   3502   1389    248   -183       O  
ATOM    484  OD2 ASP A  60      37.599  19.725   6.745  1.00 34.21           O  
ANISOU  484  OD2 ASP A  60     4194   4553   4249    479    605   -242       O  
ATOM    485  N   GLN A  61      38.999  19.716  12.002  1.00 18.26           N  
ANISOU  485  N   GLN A  61     2050   2175   2711    696    691    319       N  
ATOM    486  CA  GLN A  61      39.825  19.080  12.997  1.00 20.18           C  
ANISOU  486  CA  GLN A  61     1986   2824   2858    401    289    124       C  
ATOM    487  C   GLN A  61      40.547  20.079  13.806  1.00 15.81           C  
ANISOU  487  C   GLN A  61     1415   2256   2334    532    353    219       C  
ATOM    488  O   GLN A  61      41.768  19.969  14.076  1.00 21.66           O  
ANISOU  488  O   GLN A  61     1910   2683   3635    503    309    552       O  
ATOM    489  CB  GLN A  61      40.796  18.026  12.364  1.00 22.14           C  
ANISOU  489  CB  GLN A  61     2260   2881   3269    814    238    264       C  
ATOM    490  CG  GLN A  61      41.002  16.904  13.144  1.00 22.33           C  
ANISOU  490  CG  GLN A  61     3298   2129   3056    402   -101   -391       C  
ATOM    491  CD  GLN A  61      41.654  15.759  12.354  1.00 21.08           C  
ANISOU  491  CD  GLN A  61     3254   2547   2208    664    -62    -31       C  
ATOM    492  OE1 GLN A  61      41.188  15.416  11.287  1.00 28.33           O  
ANISOU  492  OE1 GLN A  61     4576   3457   2728    497   -432   -362       O  
ATOM    493  NE2 GLN A  61      42.691  15.140  12.937  1.00 21.08           N  
ANISOU  493  NE2 GLN A  61     2893   2309   2805     51     98    221       N  
ATOM    494  N   ILE A  62      39.801  21.134  14.225  1.00 16.87           N  
ANISOU  494  N   ILE A  62     1804   2208   2397    287    338    515       N  
ATOM    495  CA  ILE A  62      40.319  22.184  15.069  1.00 14.81           C  
ANISOU  495  CA  ILE A  62     1095   2098   2431    417    120    412       C  
ATOM    496  C   ILE A  62      40.049  21.974  16.602  1.00 16.43           C  
ANISOU  496  C   ILE A  62     1376   2450   2414    358     81    540       C  
ATOM    497  O   ILE A  62      38.912  21.892  17.018  1.00 15.43           O  
ANISOU  497  O   ILE A  62     1089   1988   2783    151    150    689       O  
ATOM    498  CB  ILE A  62      39.673  23.609  14.660  1.00 17.42           C  
ANISOU  498  CB  ILE A  62     1866   1865   2886    379    104    470       C  
ATOM    499  CG1 ILE A  62      39.955  23.977  13.265  1.00 18.86           C  
ANISOU  499  CG1 ILE A  62     1732   2413   3019    293    374    551       C  
ATOM    500  CG2 ILE A  62      40.094  24.628  15.597  1.00 16.46           C  
ANISOU  500  CG2 ILE A  62     1450   2118   2685    367     54    782       C  
ATOM    501  CD1 ILE A  62      41.451  24.195  12.951  1.00 21.10           C  
ANISOU  501  CD1 ILE A  62     1538   3163   3316    395    384   1066       C  
ATOM    502  N   PRO A  63      41.062  22.062  17.427  1.00 16.92           N  
ANISOU  502  N   PRO A  63     1296   2299   2831     10    -28    677       N  
ATOM    503  CA  PRO A  63      40.838  21.982  18.915  1.00 17.34           C  
ANISOU  503  CA  PRO A  63     1263   2326   2999    385   -220    474       C  
ATOM    504  C   PRO A  63      40.127  23.214  19.487  1.00 17.13           C  
ANISOU  504  C   PRO A  63     1594   2219   2695   -249   -125    313       C  
ATOM    505  O   PRO A  63      40.477  24.354  19.126  1.00 18.14           O  
ANISOU  505  O   PRO A  63     1474   2041   3375    -19   -275    701       O  
ATOM    506  CB  PRO A  63      42.315  21.773  19.488  1.00 18.47           C  
ANISOU  506  CB  PRO A  63     1931   2264   2822    226   -493    732       C  
ATOM    507  CG  PRO A  63      43.092  21.194  18.214  1.00 18.76           C  
ANISOU  507  CG  PRO A  63     1910   2433   2781   -132   -267    552       C  
ATOM    508  CD  PRO A  63      42.528  21.961  17.087  1.00 16.79           C  
ANISOU  508  CD  PRO A  63     1505   2482   2392    276    283    657       C  
ATOM    509  N   VAL A  64      39.067  22.981  20.261  1.00 16.71           N  
ANISOU  509  N   VAL A  64     1407   2183   2757    120   -235    584       N  
ATOM    510  CA  VAL A  64      38.362  24.033  20.905  1.00 14.86           C  
ANISOU  510  CA  VAL A  64     1567   1881   2198   -361   -292    338       C  
ATOM    511  C   VAL A  64      38.025  23.591  22.362  1.00 16.83           C  
ANISOU  511  C   VAL A  64     1473   2305   2615    -53   -517    597       C  
ATOM    512  O   VAL A  64      37.442  22.544  22.557  1.00 17.41           O  
ANISOU  512  O   VAL A  64     2099   2069   2444   -501   -150    534       O  
ATOM    513  CB  VAL A  64      36.982  24.368  20.192  1.00 15.91           C  
ANISOU  513  CB  VAL A  64     1446   2058   2540    -28   -363    573       C  
ATOM    514  CG1 VAL A  64      36.329  25.524  20.906  1.00 16.34           C  
ANISOU  514  CG1 VAL A  64     1778   2264   2165   -400   -293    498       C  
ATOM    515  CG2 VAL A  64      37.164  24.679  18.795  1.00 15.94           C  
ANISOU  515  CG2 VAL A  64     1586   1806   2662   -122   -316    839       C  
ATOM    516  N   GLU A  65      38.393  24.417  23.365  1.00 17.11           N  
ANISOU  516  N   GLU A  65     1895   1810   2793    -53   -632    526       N  
ATOM    517  CA  GLU A  65      38.066  24.113  24.779  1.00 17.76           C  
ANISOU  517  CA  GLU A  65     1878   2032   2837   -455   -810    182       C  
ATOM    518  C   GLU A  65      36.845  24.978  25.247  1.00 17.35           C  
ANISOU  518  C   GLU A  65     2115   1897   2577   -228   -755    444       C  
ATOM    519  O   GLU A  65      36.878  26.193  25.184  1.00 21.08           O  
ANISOU  519  O   GLU A  65     2415   1790   3803   -366   -820    512       O  
ATOM    520  CB  GLU A  65      39.279  24.358  25.725  1.00 21.09           C  
ANISOU  520  CB  GLU A  65     2395   2306   3310   -221  -1071    437       C  
ATOM    521  CG  GLU A  65      39.048  23.764  27.105  1.00 22.67           C  
ANISOU  521  CG  GLU A  65     2579   3113   2921   -119   -542   -120       C  
ATOM    522  CD  GLU A  65      40.335  23.784  28.021  1.00 32.00           C  
ANISOU  522  CD  GLU A  65     3327   4856   3974     93   -945    165       C  
ATOM    523  OE1 GLU A  65      40.209  23.524  29.224  1.00 40.34           O  
ANISOU  523  OE1 GLU A  65     5567   5494   4264    571  -1078    352       O  
ATOM    524  OE2 GLU A  65      41.337  23.892  27.528  1.00 32.44           O  
ANISOU  524  OE2 GLU A  65     2792   5292   4239   -542  -1478    861       O  
ATOM    525  N   ILE A  66      35.798  24.326  25.686  1.00 16.71           N  
ANISOU  525  N   ILE A  66     2169   1459   2719   -259   -684    199       N  
ATOM    526  CA  ILE A  66      34.543  24.984  25.984  1.00 17.69           C  
ANISOU  526  CA  ILE A  66     2245   1623   2852   -251   -479     49       C  
ATOM    527  C   ILE A  66      34.200  24.779  27.430  1.00 18.36           C  
ANISOU  527  C   ILE A  66     2320   1958   2696   -223   -486   -146       C  
ATOM    528  O   ILE A  66      33.973  23.670  27.865  1.00 18.90           O  
ANISOU  528  O   ILE A  66     2651   2193   2336   -333   -582    207       O  
ATOM    529  CB  ILE A  66      33.379  24.364  25.098  1.00 16.46           C  
ANISOU  529  CB  ILE A  66     2029   1492   2733   -313   -447     15       C  
ATOM    530  CG1 ILE A  66      33.742  24.403  23.554  1.00 17.32           C  
ANISOU  530  CG1 ILE A  66     2250   1695   2635   -178   -359    149       C  
ATOM    531  CG2 ILE A  66      32.046  24.983  25.423  1.00 18.85           C  
ANISOU  531  CG2 ILE A  66     2045   1949   3168   -266   -514    173       C  
ATOM    532  CD1 ILE A  66      32.997  23.507  22.749  1.00 18.67           C  
ANISOU  532  CD1 ILE A  66     2275   2567   2252   -149   -882    255       C  
ATOM    533  N   CYS A  67      34.258  25.849  28.232  1.00 21.23           N  
ANISOU  533  N   CYS A  67     3108   1930   3027   -252   -356   -193       N  
ATOM    534  CA  CYS A  67      34.069  25.709  29.704  1.00 24.95           C  
ANISOU  534  CA  CYS A  67     3519   2883   3078   -146   -438   -372       C  
ATOM    535  C   CYS A  67      34.967  24.641  30.264  1.00 25.34           C  
ANISOU  535  C   CYS A  67     3678   2952   2995   -172   -596   -537       C  
ATOM    536  O   CYS A  67      34.529  23.837  31.111  1.00 27.50           O  
ANISOU  536  O   CYS A  67     4187   3157   3103   -378   -251   -786       O  
ATOM    537  CB  CYS A  67      32.676  25.323  30.022  1.00 26.53           C  
ANISOU  537  CB  CYS A  67     3852   3115   3111      9     38   -124       C  
ATOM    538  SG  CYS A  67      31.562  26.480  29.783  1.00 34.91           S  
ANISOU  538  SG  CYS A  67     5120   4201   3940    655   -766    399       S  
ATOM    539  N   GLY A  68      36.157  24.533  29.747  1.00 21.55           N  
ANISOU  539  N   GLY A  68     3283   2482   2421   -346  -1004   -379       N  
ATOM    540  CA  GLY A  68      37.120  23.554  30.275  1.00 22.70           C  
ANISOU  540  CA  GLY A  68     3441   2494   2687     63   -907   -326       C  
ATOM    541  C   GLY A  68      37.041  22.134  29.657  1.00 22.05           C  
ANISOU  541  C   GLY A  68     3047   2430   2899    -64  -1122   -228       C  
ATOM    542  O   GLY A  68      37.810  21.293  30.016  1.00 25.26           O  
ANISOU  542  O   GLY A  68     3501   3012   3082    399  -1440   -299       O  
ATOM    543  N   HIS A  69      36.077  21.905  28.796  1.00 18.23           N  
ANISOU  543  N   HIS A  69     2554   2196   2176      8   -820   -178       N  
ATOM    544  CA  HIS A  69      35.898  20.596  28.135  1.00 16.56           C  
ANISOU  544  CA  HIS A  69     2185   1818   2288    -71   -656    372       C  
ATOM    545  C   HIS A  69      36.478  20.658  26.770  1.00 15.74           C  
ANISOU  545  C   HIS A  69     2003   1702   2273   -194   -582    107       C  
ATOM    546  O   HIS A  69      36.245  21.612  26.027  1.00 18.21           O  
ANISOU  546  O   HIS A  69     2667   1637   2614     29   -458    378       O  
ATOM    547  CB  HIS A  69      34.405  20.221  28.038  1.00 17.79           C  
ANISOU  547  CB  HIS A  69     2104   2055   2599   -145   -651    221       C  
ATOM    548  CG  HIS A  69      33.700  20.067  29.363  1.00 22.72           C  
ANISOU  548  CG  HIS A  69     2297   3275   3059    -62   -446    287       C  
ATOM    549  ND1 HIS A  69      32.361  20.163  29.440  1.00 41.64           N  
ANISOU  549  ND1 HIS A  69     3699   6956   5166   -579    703   -654       N  
ATOM    550  CD2 HIS A  69      34.082  19.598  30.541  1.00 35.67           C  
ANISOU  550  CD2 HIS A  69     4403   5767   3380     85    162    252       C  
ATOM    551  CE1 HIS A  69      31.999  20.112  30.734  1.00 39.78           C  
ANISOU  551  CE1 HIS A  69     4429   6574   4108    154   -841    -26       C  
ATOM    552  NE2 HIS A  69      33.015  19.821  31.412  1.00 28.19           N  
ANISOU  552  NE2 HIS A  69     3132   4991   2587    577   -567    159       N  
ATOM    553  N   LYS A  70      37.190  19.605  26.373  1.00 16.80           N  
ANISOU  553  N   LYS A  70     2267   2011   2102    199   -327    386       N  
ATOM    554  CA  LYS A  70      37.874  19.557  25.090  1.00 18.05           C  
ANISOU  554  CA  LYS A  70     2256   1958   2643    324   -180    463       C  
ATOM    555  C   LYS A  70      37.013  19.024  23.913  1.00 16.03           C  
ANISOU  555  C   LYS A  70     1861   1901   2327    375    -13    372       C  
ATOM    556  O   LYS A  70      36.346  17.976  24.020  1.00 17.43           O  
ANISOU  556  O   LYS A  70     2348   1885   2387   -104    -87    477       O  
ATOM    557  CB  LYS A  70      39.163  18.767  25.225  1.00 21.90           C  
ANISOU  557  CB  LYS A  70     2357   2861   3100    505   -589    625       C  
ATOM    558  CG  LYS A  70      40.224  19.486  26.169  1.00 27.91           C  
ANISOU  558  CG  LYS A  70     2890   3848   3866    -55   -658    477       C  
ATOM    559  CD  LYS A  70      41.442  18.586  26.499  1.00 35.63           C  
ANISOU  559  CD  LYS A  70     3645   4860   5031    488   -263    419       C  
ATOM    560  CE  LYS A  70      42.224  19.177  27.626  1.00 41.28           C  
ANISOU  560  CE  LYS A  70     4883   5468   5334   -144   -380    -80       C  
ATOM    561  NZ  LYS A  70      43.671  19.204  27.341  1.00 47.17           N  
ANISOU  561  NZ  LYS A  70     5059   6602   6260    229     15    100       N  
ATOM    562  N   ALA A  71      37.136  19.676  22.788  1.00 14.39           N  
ANISOU  562  N   ALA A  71     1526   1816   2125    -25    -13    412       N  
ATOM    563  CA  ALA A  71      36.590  19.188  21.546  1.00 13.87           C  
ANISOU  563  CA  ALA A  71     1437   1644   2187    225    213    244       C  
ATOM    564  C   ALA A  71      37.637  19.380  20.443  1.00 13.38           C  
ANISOU  564  C   ALA A  71     1448   1589   2046    227     91    446       C  
ATOM    565  O   ALA A  71      38.532  20.244  20.579  1.00 16.36           O  
ANISOU  565  O   ALA A  71     1453   1754   3005    211    122    551       O  
ATOM    566  CB  ALA A  71      35.306  19.952  21.209  1.00 13.51           C  
ANISOU  566  CB  ALA A  71     1541   1511   2078    313     16    237       C  
ATOM    567  N   ILE A  72      37.537  18.618  19.419  1.00 14.18           N  
ANISOU  567  N   ILE A  72     1640   1463   2285    379    373    368       N  
ATOM    568  CA  ILE A  72      38.308  18.847  18.169  1.00 14.64           C  
ANISOU  568  CA  ILE A  72     1696   1547   2318    491    426    406       C  
ATOM    569  C   ILE A  72      37.449  18.558  16.991  1.00 14.94           C  
ANISOU  569  C   ILE A  72     1446   1945   2284    394    283    386       C  
ATOM    570  O   ILE A  72      37.004  17.446  16.802  1.00 15.92           O  
ANISOU  570  O   ILE A  72     1839   1647   2561    251    561    394       O  
ATOM    571  CB  ILE A  72      39.591  17.876  18.107  1.00 15.63           C  
ANISOU  571  CB  ILE A  72     1748   1757   2433    326    273    421       C  
ATOM    572  CG1 ILE A  72      40.406  17.934  19.373  1.00 14.90           C  
ANISOU  572  CG1 ILE A  72     1573   1803   2282    346    305    384       C  
ATOM    573  CG2 ILE A  72      40.386  18.197  16.872  1.00 16.56           C  
ANISOU  573  CG2 ILE A  72     1733   2014   2542    336    490    367       C  
ATOM    574  CD1 ILE A  72      41.605  16.965  19.408  1.00 17.18           C  
ANISOU  574  CD1 ILE A  72     1787   1740   2998    416    299     46       C  
ATOM    575  N   GLY A  73      37.126  19.590  16.203  1.00 14.38           N  
ANISOU  575  N   GLY A  73     1685   1570   2206    414    470    460       N  
ATOM    576  CA  GLY A  73      36.213  19.418  15.104  1.00 15.04           C  
ANISOU  576  CA  GLY A  73     1585   1593   2533    307    409    257       C  
ATOM    577  C   GLY A  73      36.126  20.611  14.238  1.00 13.49           C  
ANISOU  577  C   GLY A  73     1647   1592   1884     19    403    348       C  
ATOM    578  O   GLY A  73      37.028  21.462  14.250  1.00 15.26           O  
ANISOU  578  O   GLY A  73     1287   1821   2688    349    216    476       O  
ATOM    579  N   THR A  74      35.109  20.634  13.415  1.00 14.48           N  
ANISOU  579  N   THR A  74     1509   1708   2281    283    290    389       N  
ATOM    580  CA  THR A  74      34.984  21.623  12.362  1.00 13.41           C  
ANISOU  580  CA  THR A  74     1360   1669   2065    214    459    383       C  
ATOM    581  C   THR A  74      34.521  22.943  12.904  1.00 13.32           C  
ANISOU  581  C   THR A  74     1793   1506   1763    440    372    368       C  
ATOM    582  O   THR A  74      33.567  23.029  13.711  1.00 13.10           O  
ANISOU  582  O   THR A  74     1376   1587   2011    167    530    240       O  
ATOM    583  CB  THR A  74      34.045  21.083  11.325  1.00 15.86           C  
ANISOU  583  CB  THR A  74     1977   1815   2234    448    364     25       C  
ATOM    584  OG1 THR A  74      34.596  19.868  10.758  1.00 20.19           O  
ANISOU  584  OG1 THR A  74     2522   2034   3113    771    353   -153       O  
ATOM    585  CG2 THR A  74      33.856  22.000  10.238  1.00 16.58           C  
ANISOU  585  CG2 THR A  74     1761   2080   2457    340    269     45       C  
ATOM    586  N   VAL A  75      35.204  24.013  12.511  1.00 12.43           N  
ANISOU  586  N   VAL A  75     1249   1481   1992    387    452    435       N  
ATOM    587  CA  VAL A  75      34.819  25.377  12.818  1.00 12.87           C  
ANISOU  587  CA  VAL A  75     1333   1670   1885    106    438    341       C  
ATOM    588  C   VAL A  75      34.663  26.137  11.521  1.00 11.91           C  
ANISOU  588  C   VAL A  75     1213   1529   1780    228    412    397       C  
ATOM    589  O   VAL A  75      35.532  26.126  10.656  1.00 13.58           O  
ANISOU  589  O   VAL A  75     1276   1907   1976    416    447    454       O  
ATOM    590  CB  VAL A  75      35.873  26.028  13.705  1.00 14.34           C  
ANISOU  590  CB  VAL A  75     1753   1671   2022     36    167    337       C  
ATOM    591  CG1 VAL A  75      35.643  27.460  13.925  1.00 13.91           C  
ANISOU  591  CG1 VAL A  75     1519   2002   1763     96     81    207       C  
ATOM    592  CG2 VAL A  75      36.030  25.271  15.027  1.00 15.38           C  
ANISOU  592  CG2 VAL A  75     1713   1999   2128    238    -56    326       C  
ATOM    593  N   LEU A  76      33.529  26.786  11.370  1.00 11.62           N  
ANISOU  593  N   LEU A  76     1119   1636   1660     89    216    260       N  
ATOM    594  CA  LEU A  76      33.255  27.664  10.242  1.00 11.68           C  
ANISOU  594  CA  LEU A  76     1164   1543   1729    115    282    199       C  
ATOM    595  C   LEU A  76      33.507  29.072  10.688  1.00 10.98           C  
ANISOU  595  C   LEU A  76     1058   1565   1547    171    209    164       C  
ATOM    596  O   LEU A  76      33.077  29.460  11.764  1.00 13.71           O  
ANISOU  596  O   LEU A  76     1636   1708   1864   -185    610     35       O  
ATOM    597  CB  LEU A  76      31.775  27.470   9.774  1.00 11.74           C  
ANISOU  597  CB  LEU A  76     1392   1577   1491    205    124    217       C  
ATOM    598  CG  LEU A  76      31.379  26.038   9.503  1.00 12.04           C  
ANISOU  598  CG  LEU A  76     1385   1635   1554    242    317    113       C  
ATOM    599  CD1 LEU A  76      29.930  25.962   9.028  1.00 13.14           C  
ANISOU  599  CD1 LEU A  76     1378   1775   1839    114    406     31       C  
ATOM    600  CD2 LEU A  76      32.302  25.353   8.471  1.00 13.45           C  
ANISOU  600  CD2 LEU A  76     1533   1586   1990    134    249   -126       C  
ATOM    601  N   VAL A  77      34.123  29.884   9.826  1.00 11.10           N  
ANISOU  601  N   VAL A  77     1228   1522   1468    105    148    351       N  
ATOM    602  CA  VAL A  77      34.415  31.270  10.144  1.00 11.76           C  
ANISOU  602  CA  VAL A  77     1241   1609   1615    -66     -4    428       C  
ATOM    603  C   VAL A  77      33.751  32.162   9.108  1.00 11.36           C  
ANISOU  603  C   VAL A  77     1332   1490   1493   -237     51    353       C  
ATOM    604  O   VAL A  77      33.965  31.989   7.912  1.00 12.22           O  
ANISOU  604  O   VAL A  77     1484   1640   1518   -114     72    271       O  
ATOM    605  CB  VAL A  77      35.952  31.530  10.155  1.00 13.68           C  
ANISOU  605  CB  VAL A  77     1389   2286   1520   -175    -49    298       C  
ATOM    606  CG1 VAL A  77      36.265  33.011  10.403  1.00 15.32           C  
ANISOU  606  CG1 VAL A  77     1285   2498   2036   -311   -229    233       C  
ATOM    607  CG2 VAL A  77      36.622  30.679  11.213  1.00 16.07           C  
ANISOU  607  CG2 VAL A  77     1344   2584   2177    254    105    371       C  
ATOM    608  N   GLY A  78      32.960  33.109   9.559  1.00 11.45           N  
ANISOU  608  N   GLY A  78     1592   1415   1341   -105    -92    325       N  
ATOM    609  CA  GLY A  78      32.274  34.021   8.626  1.00 13.32           C  
ANISOU  609  CA  GLY A  78     1880   1633   1548   -174   -159    294       C  
ATOM    610  C   GLY A  78      31.315  34.913   9.371  1.00 12.43           C  
ANISOU  610  C   GLY A  78     1929   1322   1471   -131    -15    229       C  
ATOM    611  O   GLY A  78      31.325  35.004  10.593  1.00 13.28           O  
ANISOU  611  O   GLY A  78     1903   1571   1571     55   -180    182       O  
ATOM    612  N   PRO A  79      30.449  35.606   8.611  1.00 13.00           N  
ANISOU  612  N   PRO A  79     1864   1434   1639      1   -231    243       N  
ATOM    613  CA  PRO A  79      29.646  36.704   9.175  1.00 13.49           C  
ANISOU  613  CA  PRO A  79     2109   1251   1763    171   -574     66       C  
ATOM    614  C   PRO A  79      28.442  36.186   9.885  1.00 13.71           C  
ANISOU  614  C   PRO A  79     1896   1766   1545    267   -432   -183       C  
ATOM    615  O   PRO A  79      27.342  36.499   9.535  1.00 18.42           O  
ANISOU  615  O   PRO A  79     2303   2755   1940    287   -426      3       O  
ATOM    616  CB  PRO A  79      29.257  37.538   7.952  1.00 14.97           C  
ANISOU  616  CB  PRO A  79     2437   1349   1899    -54   -526    261       C  
ATOM    617  CG  PRO A  79      29.242  36.562   6.826  1.00 14.79           C  
ANISOU  617  CG  PRO A  79     2256   1494   1868     47   -306    321       C  
ATOM    618  CD  PRO A  79      30.424  35.611   7.112  1.00 14.11           C  
ANISOU  618  CD  PRO A  79     2003   1685   1670    -98   -294    188       C  
ATOM    619  N   THR A  80      28.648  35.451  10.892  1.00 17.95           N  
ANISOU  619  N   THR A  80     2189   2404   2224   -213   -710    613       N  
ATOM    620  CA  THR A  80      27.599  35.138  11.841  1.00 16.10           C  
ANISOU  620  CA  THR A  80     1967   1995   2153   -342   -623    542       C  
ATOM    621  C   THR A  80      27.349  36.321  12.780  1.00 15.16           C  
ANISOU  621  C   THR A  80     2033   1396   2330   -183   -475    740       C  
ATOM    622  O   THR A  80      28.304  37.062  13.127  1.00 18.24           O  
ANISOU  622  O   THR A  80     2331   1893   2704   -548   -769    768       O  
ATOM    623  CB  THR A  80      27.957  33.895  12.659  1.00 14.80           C  
ANISOU  623  CB  THR A  80     1815   1859   1949   -164   -440    323       C  
ATOM    624  OG1 THR A  80      26.930  33.665  13.645  1.00 15.00           O  
ANISOU  624  OG1 THR A  80     1843   1877   1978   -327   -349    306       O  
ATOM    625  CG2 THR A  80      29.318  34.039  13.414  1.00 13.19           C  
ANISOU  625  CG2 THR A  80     1687   1791   1534    -67   -377    383       C  
ATOM    626  N   PRO A  81      26.105  36.536  13.276  1.00 16.32           N  
ANISOU  626  N   PRO A  81     2219   1652   2326    -15   -642    417       N  
ATOM    627  CA  PRO A  81      25.849  37.615  14.204  1.00 15.89           C  
ANISOU  627  CA  PRO A  81     2202   1453   2381   -123   -486    541       C  
ATOM    628  C   PRO A  81      26.561  37.488  15.582  1.00 14.60           C  
ANISOU  628  C   PRO A  81     1867   1305   2373   -243   -474    535       C  
ATOM    629  O   PRO A  81      26.748  38.497  16.309  1.00 17.40           O  
ANISOU  629  O   PRO A  81     2260   1385   2965   -253   -654    229       O  
ATOM    630  CB  PRO A  81      24.319  37.568  14.395  1.00 18.96           C  
ANISOU  630  CB  PRO A  81     2353   1974   2876    -68   -634    550       C  
ATOM    631  CG  PRO A  81      23.956  36.212  14.000  1.00 21.16           C  
ANISOU  631  CG  PRO A  81     2097   2410   3533   -172   -593   -408       C  
ATOM    632  CD  PRO A  81      24.843  35.838  12.878  1.00 18.23           C  
ANISOU  632  CD  PRO A  81     2007   2004   2913   -202   -663     28       C  
ATOM    633  N  AVAL A  82      26.899  36.280  15.945  0.50 14.33           N  
ANISOU  633  N  AVAL A  82     1703   1284   2456   -209   -254    582       N  
ATOM    634  N  BVAL A  82      26.749  36.295  16.038  0.50 13.89           N  
ANISOU  634  N  BVAL A  82     1880   1219   2176   -281   -198    724       N  
ATOM    635  CA AVAL A  82      27.455  35.976  17.262  0.50 15.62           C  
ANISOU  635  CA AVAL A  82     2095   1661   2177    117     71    451       C  
ATOM    636  CA BVAL A  82      27.548  36.039  17.293  0.50 13.59           C  
ANISOU  636  CA BVAL A  82     1945   1246   1970      0     36    427       C  
ATOM    637  C  AVAL A  82      28.215  34.637  17.101  0.50 12.57           C  
ANISOU  637  C  AVAL A  82     1745   1365   1663   -132   -129    384       C  
ATOM    638  C  BVAL A  82      28.200  34.677  17.118  0.50 11.42           C  
ANISOU  638  C  BVAL A  82     1667   1158   1514   -158   -127    264       C  
ATOM    639  O  AVAL A  82      27.873  33.829  16.251  0.50 13.64           O  
ANISOU  639  O  AVAL A  82     2053   1455   1673   -130   -232    584       O  
ATOM    640  O  BVAL A  82      27.713  33.831  16.341  0.50 11.84           O  
ANISOU  640  O  BVAL A  82     1612   1286   1601   -185   -220    327       O  
ATOM    641  CB AVAL A  82      26.289  35.865  18.366  0.50 18.94           C  
ANISOU  641  CB AVAL A  82     2262   2204   2730    208    158    317       C  
ATOM    642  CB BVAL A  82      26.636  36.055  18.584  0.50 13.45           C  
ANISOU  642  CB BVAL A  82     1933   1087   2087    149   -154    258       C  
ATOM    643  CG1AVAL A  82      26.777  35.361  19.587  0.50 20.58           C  
ANISOU  643  CG1AVAL A  82     2427   2758   2631    609    153    177       C  
ATOM    644  CG1BVAL A  82      25.606  34.866  18.524  0.50 13.39           C  
ANISOU  644  CG1BVAL A  82     1863    865   2357    -21    130     18       C  
ATOM    645  CG2AVAL A  82      25.646  37.225  18.579  0.50 21.35           C  
ANISOU  645  CG2AVAL A  82     2749   2567   2795    597    456    393       C  
ATOM    646  CG2BVAL A  82      27.500  36.040  19.918  0.50 17.64           C  
ANISOU  646  CG2BVAL A  82     2644   1830   2228    212    -90   -447       C  
ATOM    647  N   ASN A  83      29.262  34.454  17.843  1.00 12.23           N  
ANISOU  647  N   ASN A  83     1625   1405   1616   -199   -222    202       N  
ATOM    648  CA  ASN A  83      29.918  33.163  17.868  1.00 10.18           C  
ANISOU  648  CA  ASN A  83     1259   1146   1462     14    -90    233       C  
ATOM    649  C   ASN A  83      28.940  32.126  18.410  1.00  9.56           C  
ANISOU  649  C   ASN A  83     1305   1189   1138     11    -80    229       C  
ATOM    650  O   ASN A  83      28.401  32.316  19.499  1.00 10.88           O  
ANISOU  650  O   ASN A  83     1615   1343   1175   -176    -70     10       O  
ATOM    651  CB  ASN A  83      31.117  33.193  18.780  1.00 11.76           C  
ANISOU  651  CB  ASN A  83     1470   1442   1553   -156   -112    157       C  
ATOM    652  CG  ASN A  83      32.228  34.110  18.333  1.00 12.81           C  
ANISOU  652  CG  ASN A  83     1621   1357   1887    -19    -20     34       C  
ATOM    653  OD1 ASN A  83      32.509  34.281  17.161  1.00 14.86           O  
ANISOU  653  OD1 ASN A  83     1963   1765   1917   -585     84    164       O  
ATOM    654  ND2 ASN A  83      32.948  34.643  19.332  1.00 14.53           N  
ANISOU  654  ND2 ASN A  83     1718   1601   2200   -232   -440    201       N  
ATOM    655  N   ILE A  84      28.751  31.011  17.701  1.00  9.71           N  
ANISOU  655  N   ILE A  84     1313   1148   1229     35    -74    109       N  
ATOM    656  CA  ILE A  84      27.874  29.936  18.121  1.00  9.20           C  
ANISOU  656  CA  ILE A  84     1207   1142   1144     32    100     77       C  
ATOM    657  C   ILE A  84      28.601  28.631  18.142  1.00  9.26           C  
ANISOU  657  C   ILE A  84     1156   1055   1306     28    -69    -12       C  
ATOM    658  O   ILE A  84      29.316  28.267  17.216  1.00 10.16           O  
ANISOU  658  O   ILE A  84     1407   1239   1212    113     51    164       O  
ATOM    659  CB  ILE A  84      26.576  29.869  17.267  1.00  9.70           C  
ANISOU  659  CB  ILE A  84     1234   1202   1246    -26      7     43       C  
ATOM    660  CG1 ILE A  84      26.827  29.553  15.830  1.00 11.46           C  
ANISOU  660  CG1 ILE A  84     1488   1501   1362      0      4    -53       C  
ATOM    661  CG2 ILE A  84      25.763  31.145  17.415  1.00 10.32           C  
ANISOU  661  CG2 ILE A  84     1258   1325   1337     67    -89      3       C  
ATOM    662  CD1 ILE A  84      25.551  29.561  14.956  1.00 11.38           C  
ANISOU  662  CD1 ILE A  84     1527   1651   1143      5    -38    198       C  
ATOM    663  N   ILE A  85      28.365  27.876  19.221  1.00  9.14           N  
ANISOU  663  N   ILE A  85     1197   1056   1219     -8      0     75       N  
ATOM    664  CA  ILE A  85      28.828  26.486  19.351  1.00  9.36           C  
ANISOU  664  CA  ILE A  85     1212   1079   1263     84     30     93       C  
ATOM    665  C   ILE A  85      27.675  25.579  19.001  1.00  8.57           C  
ANISOU  665  C   ILE A  85     1078   1029   1149     82     -7     31       C  
ATOM    666  O   ILE A  85      26.640  25.590  19.683  1.00  9.80           O  
ANISOU  666  O   ILE A  85     1228   1281   1211     87    -24    -41       O  
ATOM    667  CB  ILE A  85      29.323  26.183  20.762  1.00 10.01           C  
ANISOU  667  CB  ILE A  85     1178   1266   1359    -27   -198     66       C  
ATOM    668  CG1 ILE A  85      30.370  27.194  21.246  1.00 11.67           C  
ANISOU  668  CG1 ILE A  85     1551   1401   1481   -115   -225    297       C  
ATOM    669  CG2 ILE A  85      29.861  24.734  20.790  1.00 11.12           C  
ANISOU  669  CG2 ILE A  85     1504   1467   1254     58   -359    120       C  
ATOM    670  CD1 ILE A  85      31.564  27.345  20.370  1.00 13.23           C  
ANISOU  670  CD1 ILE A  85     1549   1694   1783   -172   -303     67       C  
ATOM    671  N   GLY A  86      27.790  24.868  17.881  1.00  8.59           N  
ANISOU  671  N   GLY A  86     1194   1061   1005     17     72     69       N  
ATOM    672  CA  GLY A  86      26.758  23.991  17.406  1.00  8.51           C  
ANISOU  672  CA  GLY A  86     1171   1046   1014     21    -25     73       C  
ATOM    673  C   GLY A  86      26.921  22.578  17.831  1.00  8.53           C  
ANISOU  673  C   GLY A  86     1154   1105    979    214    -33     70       C  
ATOM    674  O   GLY A  86      27.866  22.214  18.537  1.00  8.90           O  
ANISOU  674  O   GLY A  86     1129   1152   1099     74    -32     19       O  
ATOM    675  N   ARG A  87      26.007  21.718  17.375  1.00  8.02           N  
ANISOU  675  N   ARG A  87     1132   1004    909     41    -60     65       N  
ATOM    676  CA  ARG A  87      25.947  20.365  17.846  1.00  8.66           C  
ANISOU  676  CA  ARG A  87     1113   1003   1173     34    -27     -1       C  
ATOM    677  C   ARG A  87      27.176  19.545  17.514  1.00  9.21           C  
ANISOU  677  C   ARG A  87     1241   1088   1168     74    -22    105       C  
ATOM    678  O   ARG A  87      27.501  18.630  18.264  1.00  9.73           O  
ANISOU  678  O   ARG A  87     1349   1121   1226     88    -64    104       O  
ATOM    679  CB  ARG A  87      24.700  19.647  17.320  1.00  8.89           C  
ANISOU  679  CB  ARG A  87     1181   1085   1112     48    141     37       C  
ATOM    680  CG  ARG A  87      23.394  20.197  17.875  1.00  8.86           C  
ANISOU  680  CG  ARG A  87     1255   1003   1106     67     -8     68       C  
ATOM    681  CD  ARG A  87      22.170  19.403  17.430  1.00  9.28           C  
ANISOU  681  CD  ARG A  87     1134   1182   1208     72    -23      6       C  
ATOM    682  NE  ARG A  87      21.968  19.409  15.990  1.00  9.49           N  
ANISOU  682  NE  ARG A  87     1184   1174   1247     36    -27     37       N  
ATOM    683  CZ  ARG A  87      22.388  18.449  15.166  1.00 10.06           C  
ANISOU  683  CZ  ARG A  87     1270   1240   1312    -13     -7    115       C  
ATOM    684  NH1 ARG A  87      22.890  17.326  15.617  1.00 10.43           N  
ANISOU  684  NH1 ARG A  87     1464   1294   1205     99     52   -148       N  
ATOM    685  NH2 ARG A  87      22.216  18.648  13.886  1.00 10.97           N  
ANISOU  685  NH2 ARG A  87     1516   1376   1275    184    -30     13       N  
ATOM    686  N   ASN A  88      27.887  19.896  16.470  1.00  9.32           N  
ANISOU  686  N   ASN A  88     1122   1155   1262    131     99      1       N  
ATOM    687  CA  ASN A  88      29.106  19.153  16.155  1.00 10.08           C  
ANISOU  687  CA  ASN A  88     1207   1216   1407     34     94     51       C  
ATOM    688  C   ASN A  88      30.087  19.154  17.303  1.00  9.96           C  
ANISOU  688  C   ASN A  88     1232   1152   1401    144     44    158       C  
ATOM    689  O   ASN A  88      30.781  18.162  17.501  1.00 12.07           O  
ANISOU  689  O   ASN A  88     1296   1289   1999    209   -210    -25       O  
ATOM    690  CB  ASN A  88      29.735  19.654  14.850  1.00 11.21           C  
ANISOU  690  CB  ASN A  88     1172   1403   1683    144    295     26       C  
ATOM    691  CG  ASN A  88      30.436  20.961  15.006  1.00 11.05           C  
ANISOU  691  CG  ASN A  88     1366   1400   1429     91    136     74       C  
ATOM    692  OD1 ASN A  88      29.816  21.949  15.423  1.00 10.95           O  
ANISOU  692  OD1 ASN A  88     1284   1328   1546    125    112    -15       O  
ATOM    693  ND2 ASN A  88      31.706  21.004  14.621  1.00 11.46           N  
ANISOU  693  ND2 ASN A  88     1242   1409   1702     48    269    273       N  
ATOM    694  N   LEU A  89      30.193  20.262  18.060  1.00  9.73           N  
ANISOU  694  N   LEU A  89     1082   1230   1385    163    -17      6       N  
ATOM    695  CA  LEU A  89      31.034  20.331  19.239  1.00 10.55           C  
ANISOU  695  CA  LEU A  89     1178   1226   1604     43      1    148       C  
ATOM    696  C   LEU A  89      30.293  20.075  20.534  1.00  9.81           C  
ANISOU  696  C   LEU A  89     1207   1007   1513    139    -29    134       C  
ATOM    697  O   LEU A  89      30.881  19.546  21.469  1.00 11.24           O  
ANISOU  697  O   LEU A  89     1341   1194   1733     81   -194    319       O  
ATOM    698  CB  LEU A  89      31.836  21.634  19.272  1.00 10.63           C  
ANISOU  698  CB  LEU A  89     1206   1188   1644    -32   -174    121       C  
ATOM    699  CG  LEU A  89      32.687  21.958  18.057  1.00 11.41           C  
ANISOU  699  CG  LEU A  89     1186   1384   1762     19    212    203       C  
ATOM    700  CD1 LEU A  89      33.503  23.222  18.294  1.00 13.05           C  
ANISOU  700  CD1 LEU A  89     1316   1493   2148     20   -116    402       C  
ATOM    701  CD2 LEU A  89      33.615  20.800  17.673  1.00 12.99           C  
ANISOU  701  CD2 LEU A  89     1267   1666   1999    199    -60    258       C  
ATOM    702  N   LEU A  90      29.012  20.439  20.626  1.00  9.75           N  
ANISOU  702  N   LEU A  90     1155   1248   1299    240    -54    196       N  
ATOM    703  CA  LEU A  90      28.258  20.161  21.849  1.00  9.36           C  
ANISOU  703  CA  LEU A  90     1235   1093   1225     95    -43      9       C  
ATOM    704  C   LEU A  90      28.221  18.668  22.129  1.00  9.28           C  
ANISOU  704  C   LEU A  90     1141   1335   1048    161     90    139       C  
ATOM    705  O   LEU A  90      28.290  18.263  23.285  1.00 10.52           O  
ANISOU  705  O   LEU A  90     1365   1341   1289     93    -58    205       O  
ATOM    706  CB  LEU A  90      26.836  20.707  21.745  1.00  9.47           C  
ANISOU  706  CB  LEU A  90     1183   1121   1293    106     51     -3       C  
ATOM    707  CG  LEU A  90      26.686  22.226  21.620  1.00 10.22           C  
ANISOU  707  CG  LEU A  90     1465   1170   1248    117     -1     38       C  
ATOM    708  CD1 LEU A  90      25.228  22.610  21.379  1.00 11.95           C  
ANISOU  708  CD1 LEU A  90     1525   1223   1791    279   -176    -54       C  
ATOM    709  CD2 LEU A  90      27.219  22.988  22.825  1.00 12.09           C  
ANISOU  709  CD2 LEU A  90     1550   1402   1641    102   -113    -32       C  
ATOM    710  N   THR A  91      28.118  17.837  21.093  1.00  9.64           N  
ANISOU  710  N   THR A  91     1252   1109   1301    102    -28     20       N  
ATOM    711  CA  THR A  91      28.120  16.392  21.315  1.00 10.34           C  
ANISOU  711  CA  THR A  91     1214   1275   1439     89    125    143       C  
ATOM    712  C   THR A  91      29.464  15.914  21.878  1.00  9.88           C  
ANISOU  712  C   THR A  91     1375   1050   1327    108     89     51       C  
ATOM    713  O   THR A  91      29.499  15.047  22.733  1.00 12.32           O  
ANISOU  713  O   THR A  91     1482   1383   1815    133    -15    398       O  
ATOM    714  CB  THR A  91      27.808  15.643  20.040  1.00 10.84           C  
ANISOU  714  CB  THR A  91     1270   1190   1656    -21     -9    126       C  
ATOM    715  OG1 THR A  91      28.726  16.002  19.005  1.00 12.52           O  
ANISOU  715  OG1 THR A  91     1486   1518   1751     -1    148   -274       O  
ATOM    716  CG2 THR A  91      26.405  15.853  19.571  1.00 12.40           C  
ANISOU  716  CG2 THR A  91     1418   1500   1792     40    -15    -38       C  
ATOM    717  N   GLN A  92      30.539  16.517  21.465  1.00 10.75           N  
ANISOU  717  N   GLN A  92     1265   1281   1536    171    -21    144       N  
ATOM    718  CA  GLN A  92      31.878  16.096  21.906  1.00 11.30           C  
ANISOU  718  CA  GLN A  92     1264   1254   1773    244   -154    128       C  
ATOM    719  C   GLN A  92      32.089  16.354  23.350  1.00 11.86           C  
ANISOU  719  C   GLN A  92     1180   1527   1796    148   -276     78       C  
ATOM    720  O   GLN A  92      32.775  15.580  24.018  1.00 14.53           O  
ANISOU  720  O   GLN A  92     1701   1905   1913    500   -254    316       O  
ATOM    721  CB  GLN A  92      32.983  16.797  21.104  1.00 12.37           C  
ANISOU  721  CB  GLN A  92     1188   1368   2141    252   -154    207       C  
ATOM    722  CG  GLN A  92      33.011  16.429  19.624  1.00 12.82           C  
ANISOU  722  CG  GLN A  92     1644   1205   2021    146     43     77       C  
ATOM    723  CD  GLN A  92      34.300  16.739  18.977  1.00 13.14           C  
ANISOU  723  CD  GLN A  92     1784   1280   1927    362     78    180       C  
ATOM    724  OE1 GLN A  92      35.323  16.922  19.678  1.00 14.38           O  
ANISOU  724  OE1 GLN A  92     1431   1921   2109    186     92    436       O  
ATOM    725  NE2 GLN A  92      34.329  16.732  17.674  1.00 14.02           N  
ANISOU  725  NE2 GLN A  92     1641   1810   1874    424    191    222       N  
ATOM    726  N   ILE A  93      31.497  17.425  23.911  1.00 11.35           N  
ANISOU  726  N   ILE A  93     1319   1482   1510     73   -271     60       N  
ATOM    727  CA  ILE A  93      31.625  17.763  25.302  1.00 12.60           C  
ANISOU  727  CA  ILE A  93     1496   1662   1627     -2   -239     12       C  
ATOM    728  C   ILE A  93      30.558  17.128  26.177  1.00 13.73           C  
ANISOU  728  C   ILE A  93     1735   1664   1815    290   -419     76       C  
ATOM    729  O   ILE A  93      30.514  17.394  27.407  1.00 15.32           O  
ANISOU  729  O   ILE A  93     2039   1958   1821    207   -174    264       O  
ATOM    730  CB  ILE A  93      31.745  19.306  25.539  1.00 14.20           C  
ANISOU  730  CB  ILE A  93     1767   2026   1599      0   -491    -61       C  
ATOM    731  CG1 ILE A  93      30.416  20.029  25.238  1.00 12.80           C  
ANISOU  731  CG1 ILE A  93     1779   1581   1501    -48   -277    -46       C  
ATOM    732  CG2 ILE A  93      32.910  19.873  24.748  1.00 14.93           C  
ANISOU  732  CG2 ILE A  93     1829   1768   2076    -61   -205   -180       C  
ATOM    733  CD1 ILE A  93      30.451  21.460  25.580  1.00 14.98           C  
ANISOU  733  CD1 ILE A  93     2061   1721   1909     30   -252    -79       C  
ATOM    734  N   GLY A  94      29.678  16.304  25.567  1.00 12.23           N  
ANISOU  734  N   GLY A  94     1557   1596   1491    205    -94    319       N  
ATOM    735  CA  GLY A  94      28.703  15.562  26.316  1.00 13.46           C  
ANISOU  735  CA  GLY A  94     1855   1569   1690    153   -123    499       C  
ATOM    736  C   GLY A  94      27.461  16.334  26.689  1.00 13.64           C  
ANISOU  736  C   GLY A  94     2119   1598   1465    311     13    345       C  
ATOM    737  O   GLY A  94      26.793  15.972  27.620  1.00 15.30           O  
ANISOU  737  O   GLY A  94     2000   2035   1775    288    168    571       O  
ATOM    738  N  ACYS A  95      27.101  17.327  25.899  0.50 13.18           N  
ANISOU  738  N  ACYS A  95     1735   1682   1589    281     60    349       N  
ATOM    739  N  BCYS A  95      27.155  17.364  25.954  0.50 12.75           N  
ANISOU  739  N  BCYS A  95     1639   1591   1611    235     40    335       N  
ATOM    740  CA ACYS A  95      25.865  18.124  26.160  0.50 13.40           C  
ANISOU  740  CA ACYS A  95     1927   1922   1240    345    172    161       C  
ATOM    741  CA BCYS A  95      26.063  18.261  26.299  0.50 12.64           C  
ANISOU  741  CA BCYS A  95     1716   1820   1265    422    -59    373       C  
ATOM    742  C  ACYS A  95      24.674  17.402  25.909  0.50 13.81           C  
ANISOU  742  C  ACYS A  95     1885   1882   1479    665   -121    231       C  
ATOM    743  C  BCYS A  95      24.701  17.680  25.814  0.50 13.90           C  
ANISOU  743  C  BCYS A  95     1780   1958   1542    389     47    286       C  
ATOM    744  O  ACYS A  95      24.485  16.789  24.794  0.50 15.63           O  
ANISOU  744  O  ACYS A  95     1987   2486   1463    236     11    245       O  
ATOM    745  O  BCYS A  95      24.589  17.165  24.708  0.50 15.65           O  
ANISOU  745  O  BCYS A  95     1892   2599   1454    576     64    306       O  
ATOM    746  CB ACYS A  95      25.836  19.309  25.300  0.50 13.29           C  
ANISOU  746  CB ACYS A  95     1899   1537   1610    277     12     90       C  
ATOM    747  CB BCYS A  95      26.313  19.608  25.637  0.50 12.05           C  
ANISOU  747  CB BCYS A  95     1645   1635   1299    107    -84    167       C  
ATOM    748  SG ACYS A  95      26.822  20.561  25.810  0.50 19.46           S  
ANISOU  748  SG ACYS A  95     2687   2376   2329    -36   -336    159       S  
ATOM    749  SG BCYS A  95      25.189  20.907  26.088  0.50 11.53           S  
ANISOU  749  SG BCYS A  95     1549   1463   1365    392    -10     94       S  
ATOM    750  N   THR A  96      23.713  17.650  26.759  1.00 13.94           N  
ANISOU  750  N   THR A  96     1860   2022   1412    483     91    332       N  
ATOM    751  CA  THR A  96      22.378  17.248  26.480  1.00 13.59           C  
ANISOU  751  CA  THR A  96     1925   1811   1428    442    261    377       C  
ATOM    752  C   THR A  96      21.397  18.301  26.950  1.00 12.68           C  
ANISOU  752  C   THR A  96     1891   1456   1467    243    121    321       C  
ATOM    753  O   THR A  96      21.734  19.172  27.712  1.00 13.65           O  
ANISOU  753  O   THR A  96     1798   1931   1455    336    -82    301       O  
ATOM    754  CB  THR A  96      21.987  15.914  27.176  1.00 16.90           C  
ANISOU  754  CB  THR A  96     2142   2095   2180    677    130    570       C  
ATOM    755  OG1 THR A  96      22.143  16.053  28.602  1.00 17.81           O  
ANISOU  755  OG1 THR A  96     2394   2420   1951    731    368    943       O  
ATOM    756  CG2 THR A  96      22.879  14.735  26.688  1.00 18.35           C  
ANISOU  756  CG2 THR A  96     2613   1981   2378    707    473    553       C  
ATOM    757  N   LEU A  97      20.177  18.221  26.421  1.00 12.57           N  
ANISOU  757  N   LEU A  97     1868   1760   1146    266    184    183       N  
ATOM    758  CA  LEU A  97      19.041  19.029  26.932  1.00 12.96           C  
ANISOU  758  CA  LEU A  97     1845   1731   1346    368     47    369       C  
ATOM    759  C   LEU A  97      18.255  18.178  27.906  1.00 13.77           C  
ANISOU  759  C   LEU A  97     2023   1759   1449    425    164    193       C  
ATOM    760  O   LEU A  97      18.061  17.025  27.669  1.00 15.41           O  
ANISOU  760  O   LEU A  97     2433   1890   1529     83    533    376       O  
ATOM    761  CB  LEU A  97      18.118  19.475  25.775  1.00 11.64           C  
ANISOU  761  CB  LEU A  97     1612   1529   1280    146    104    105       C  
ATOM    762  CG  LEU A  97      18.726  20.533  24.914  1.00 10.77           C  
ANISOU  762  CG  LEU A  97     1400   1418   1274    139     64    158       C  
ATOM    763  CD1 LEU A  97      18.001  20.608  23.601  1.00 13.97           C  
ANISOU  763  CD1 LEU A  97     1517   2138   1650     19    -67    425       C  
ATOM    764  CD2 LEU A  97      18.709  21.813  25.589  1.00 14.48           C  
ANISOU  764  CD2 LEU A  97     2073   1879   1547    138    219    259       C  
ATOM    765  N   ASN A  98      17.753  18.812  28.977  1.00 14.50           N  
ANISOU  765  N   ASN A  98     2424   1754   1331    576    343    607       N  
ATOM    766  CA  ASN A  98      17.076  18.128  30.058  1.00 15.60           C  
ANISOU  766  CA  ASN A  98     2273   2117   1537    518    459    512       C  
ATOM    767  C   ASN A  98      15.911  18.958  30.534  1.00 15.56           C  
ANISOU  767  C   ASN A  98     2199   2006   1705    216    297    370       C  
ATOM    768  O   ASN A  98      16.061  20.118  30.826  1.00 18.26           O  
ANISOU  768  O   ASN A  98     2562   2420   1953    656    546    521       O  
ATOM    769  CB  ASN A  98      18.055  17.798  31.230  1.00 16.66           C  
ANISOU  769  CB  ASN A  98     2660   2227   1440    767    459    601       C  
ATOM    770  CG  ASN A  98      19.140  16.852  30.800  1.00 19.48           C  
ANISOU  770  CG  ASN A  98     2633   2512   2257    710    540    873       C  
ATOM    771  OD1 ASN A  98      18.924  15.608  30.827  1.00 22.18           O  
ANISOU  771  OD1 ASN A  98     3392   2600   2433   1024    650    890       O  
ATOM    772  ND2 ASN A  98      20.186  17.375  30.236  1.00 19.32           N  
ANISOU  772  ND2 ASN A  98     2621   3228   1492    809    317    462       N  
ATOM    773  N   PHE A  99      14.824  18.328  30.719  1.00 18.27           N  
ANISOU  773  N   PHE A  99     2293   2165   2483    479    599    431       N  
ATOM    774  CA  PHE A  99      13.679  18.998  31.345  1.00 18.40           C  
ANISOU  774  CA  PHE A  99     2316   2335   2339    405    542    390       C  
ATOM    775  C   PHE A  99      12.735  17.947  32.006  1.00 22.44           C  
ANISOU  775  C   PHE A  99     2771   2766   2988    365    879    564       C  
ATOM    776  O   PHE A  99      13.146  16.777  32.048  1.00 23.51           O  
ANISOU  776  O   PHE A  99     3011   2778   3141    -21   1157    429       O  
ATOM    777  CB  PHE A  99      12.933  19.918  30.343  1.00 20.12           C  
ANISOU  777  CB  PHE A  99     2349   2488   2805    458    472    451       C  
ATOM    778  CG  PHE A  99      12.351  19.205  29.167  1.00 20.26           C  
ANISOU  778  CG  PHE A  99     2620   2607   2467    389    529    658       C  
ATOM    779  CD1 PHE A  99      13.075  19.057  28.024  1.00 25.24           C  
ANISOU  779  CD1 PHE A  99     3367   3704   2518     37    702    350       C  
ATOM    780  CD2 PHE A  99      11.026  18.889  29.137  1.00 28.26           C  
ANISOU  780  CD2 PHE A  99     3101   3626   4008   -401    126   -219       C  
ATOM    781  CE1 PHE A  99      12.509  18.483  26.918  1.00 24.03           C  
ANISOU  781  CE1 PHE A  99     3344   3712   2072    243    608    619       C  
ATOM    782  CE2 PHE A  99      10.500  18.330  28.110  1.00 27.07           C  
ANISOU  782  CE2 PHE A  99     3058   4144   3080   -145    266    407       C  
ATOM    783  CZ  PHE A  99      11.259  18.123  26.946  1.00 29.77           C  
ANISOU  783  CZ  PHE A  99     3638   4195   3476     -4    361    250       C  
ATOM    784  OXT PHE A  99      11.671  18.362  32.563  1.00 25.87           O  
ANISOU  784  OXT PHE A  99     2967   3709   3152    515   1177    413       O  
TER     785      PHE A  99                                                      
ATOM    786  N   PRO B   1      12.872  14.625  30.481  1.00 26.37           N  
ANISOU  786  N   PRO B   1     3042   3350   3625   -477    652    252       N  
ATOM    787  CA  PRO B   1      13.702  13.683  29.741  1.00 27.13           C  
ANISOU  787  CA  PRO B   1     3384   3299   3624   -425    522    226       C  
ATOM    788  C   PRO B   1      14.927  14.281  29.298  1.00 23.81           C  
ANISOU  788  C   PRO B   1     3223   2955   2869   -414    900    326       C  
ATOM    789  O   PRO B   1      15.187  15.454  29.666  1.00 25.05           O  
ANISOU  789  O   PRO B   1     3459   2701   3356    -51   1089    790       O  
ATOM    790  CB  PRO B   1      12.833  13.323  28.535  1.00 30.44           C  
ANISOU  790  CB  PRO B   1     3716   3921   3927   -391    335     67       C  
ATOM    791  CG  PRO B   1      11.907  14.442  28.388  1.00 32.22           C  
ANISOU  791  CG  PRO B   1     4015   4166   4058   -198    -76   -175       C  
ATOM    792  CD  PRO B   1      11.782  15.127  29.670  1.00 29.07           C  
ANISOU  792  CD  PRO B   1     3300   4055   3690    -54    503    177       C  
ATOM    793  N   GLN B   2      15.784  13.457  28.795  1.00 23.48           N  
ANISOU  793  N   GLN B   2     3376   2730   2815   -292    965    911       N  
ATOM    794  CA  GLN B   2      17.042  13.870  28.261  1.00 22.76           C  
ANISOU  794  CA  GLN B   2     3099   2655   2893     33    833    489       C  
ATOM    795  C   GLN B   2      17.085  13.741  26.716  1.00 22.86           C  
ANISOU  795  C   GLN B   2     3311   2366   3007   -222    721    386       C  
ATOM    796  O   GLN B   2      16.745  12.674  26.125  1.00 22.96           O  
ANISOU  796  O   GLN B   2     3552   2280   2891   -216   1041    562       O  
ATOM    797  CB  GLN B   2      18.163  13.040  28.867  1.00 24.33           C  
ANISOU  797  CB  GLN B   2     3380   2907   2954    152    831    655       C  
ATOM    798  CG  GLN B   2      19.454  13.476  28.448  1.00 23.12           C  
ANISOU  798  CG  GLN B   2     3076   2295   3414    429    678    649       C  
ATOM    799  CD  GLN B   2      20.528  12.781  29.156  1.00 26.04           C  
ANISOU  799  CD  GLN B   2     3692   2381   3820    860    323    545       C  
ATOM    800  OE1 GLN B   2      21.120  11.784  28.599  1.00 28.07           O  
ANISOU  800  OE1 GLN B   2     3730   2670   4265    726   1007    751       O  
ATOM    801  NE2 GLN B   2      20.950  13.335  30.364  1.00 26.69           N  
ANISOU  801  NE2 GLN B   2     3960   2922   3256    988    268   1028       N  
ATOM    802  N   ILE B   3      17.463  14.836  26.069  1.00 20.40           N  
ANISOU  802  N   ILE B   3     3230   2038   2480   -290   1141    119       N  
ATOM    803  CA  ILE B   3      17.585  14.885  24.634  1.00 20.06           C  
ANISOU  803  CA  ILE B   3     2973   2275   2373   -274    668   -250       C  
ATOM    804  C   ILE B   3      19.008  15.052  24.193  1.00 18.06           C  
ANISOU  804  C   ILE B   3     2924   1857   2080    257    778   -143       C  
ATOM    805  O   ILE B   3      19.716  15.949  24.638  1.00 16.86           O  
ANISOU  805  O   ILE B   3     2756   2014   1634    234    657    189       O  
ATOM    806  CB  ILE B   3      16.716  15.956  24.095  1.00 18.75           C  
ANISOU  806  CB  ILE B   3     2620   2561   1940   -243    823   -243       C  
ATOM    807  CG1 ILE B   3      15.336  15.680  24.509  1.00 24.56           C  
ANISOU  807  CG1 ILE B   3     2935   3525   2871    -45    617    -32       C  
ATOM    808  CG2 ILE B   3      16.817  16.033  22.581  1.00 21.61           C  
ANISOU  808  CG2 ILE B   3     3628   2687   1894   -814   1009     39       C  
ATOM    809  CD1 ILE B   3      14.593  16.522  24.230  1.00 22.20           C  
ANISOU  809  CD1 ILE B   3     2452   3010   2970    135    532    330       C  
ATOM    810  N   THR B   4      19.478  13.985  23.540  1.00 20.89           N  
ANISOU  810  N   THR B   4     3890   1647   2398     68   1561     46       N  
ATOM    811  CA  THR B   4      20.674  13.936  22.871  1.00 19.54           C  
ANISOU  811  CA  THR B   4     3027   1726   2670    524    834    443       C  
ATOM    812  C   THR B   4      20.847  14.999  21.796  1.00 14.64           C  
ANISOU  812  C   THR B   4     2465   1479   1618   -123    545    -37       C  
ATOM    813  O   THR B   4      19.897  15.354  21.179  1.00 16.96           O  
ANISOU  813  O   THR B   4     2319   2372   1751   -669    417   -292       O  
ATOM    814  CB  THR B   4      20.756  12.384  22.010  1.00 19.57           C  
ANISOU  814  CB  THR B   4     2777   2358   2298   -434    243   -381       C  
ATOM    815  OG1 THR B   4      21.890  12.259  21.599  1.00 22.11           O  
ANISOU  815  OG1 THR B   4     3293   2181   2926    545   -417   -689       O  
ATOM    816  CG2 THR B   4      19.934  12.449  20.615  1.00 25.26           C  
ANISOU  816  CG2 THR B   4     3049   1874   4674   -354  -1219   -573       C  
ATOM    817  N   LEU B   5      22.106  15.314  21.454  1.00 11.97           N  
ANISOU  817  N   LEU B   5     1924   1174   1450     49   -120    -69       N  
ATOM    818  CA  LEU B   5      22.356  16.291  20.383  1.00  9.93           C  
ANISOU  818  CA  LEU B   5     1468    972   1331     28     79     98       C  
ATOM    819  C   LEU B   5      23.064  15.662  19.173  1.00 10.10           C  
ANISOU  819  C   LEU B   5     1166   1139   1531    -14     -1    -62       C  
ATOM    820  O   LEU B   5      23.510  16.363  18.276  1.00 10.06           O  
ANISOU  820  O   LEU B   5     1406   1156   1260     25     -2    -80       O  
ATOM    821  CB  LEU B   5      23.104  17.470  20.914  1.00 10.43           C  
ANISOU  821  CB  LEU B   5     1513   1157   1291    245   -110    -99       C  
ATOM    822  CG  LEU B   5      22.317  18.306  21.955  1.00 10.63           C  
ANISOU  822  CG  LEU B   5     1514   1052   1472     47     -4    -60       C  
ATOM    823  CD1 LEU B   5      23.196  19.343  22.547  1.00 11.55           C  
ANISOU  823  CD1 LEU B   5     1749   1282   1357    287   -122    -18       C  
ATOM    824  CD2 LEU B   5      21.099  18.935  21.357  1.00 11.34           C  
ANISOU  824  CD2 LEU B   5     1591   1387   1331    214     88    -74       C  
ATOM    825  N   TRP B   6      23.052  14.325  19.078  1.00 10.96           N  
ANISOU  825  N   TRP B   6     1397   1184   1582    132     87      0       N  
ATOM    826  CA  TRP B   6      23.524  13.655  17.876  1.00 11.27           C  
ANISOU  826  CA  TRP B   6     1414   1160   1708    261     80   -141       C  
ATOM    827  C   TRP B   6      22.725  14.056  16.667  1.00 11.44           C  
ANISOU  827  C   TRP B   6     1413   1413   1519    297     -7   -313       C  
ATOM    828  O   TRP B   6      23.249  14.045  15.540  1.00 14.13           O  
ANISOU  828  O   TRP B   6     1458   2165   1745    440     98   -389       O  
ATOM    829  CB  TRP B   6      23.478  12.139  18.030  1.00 11.89           C  
ANISOU  829  CB  TRP B   6     1304   1211   2000    144    -73   -218       C  
ATOM    830  CG  TRP B   6      24.383  11.562  19.008  1.00 11.74           C  
ANISOU  830  CG  TRP B   6     1629   1183   1649    147     85    -35       C  
ATOM    831  CD1 TRP B   6      24.028  10.776  20.065  1.00 16.18           C  
ANISOU  831  CD1 TRP B   6     2374   1880   1893   -319    -42     73       C  
ATOM    832  CD2 TRP B   6      25.766  11.520  18.949  1.00 12.39           C  
ANISOU  832  CD2 TRP B   6     1734   1152   1820    148   -130    131       C  
ATOM    833  NE1 TRP B   6      25.113  10.313  20.685  1.00 18.51           N  
ANISOU  833  NE1 TRP B   6     2824   1790   2418   -437   -429    799       N  
ATOM    834  CE2 TRP B   6      26.198  10.655  20.006  1.00 15.16           C  
ANISOU  834  CE2 TRP B   6     1913   1835   2009     28   -431      0       C  
ATOM    835  CE3 TRP B   6      26.711  12.015  18.081  1.00 14.34           C  
ANISOU  835  CE3 TRP B   6     1605   1487   2355    213     17     45       C  
ATOM    836  CZ2 TRP B   6      27.520  10.356  20.222  1.00 17.51           C  
ANISOU  836  CZ2 TRP B   6     2416   1974   2261    339   -410     88       C  
ATOM    837  CZ3 TRP B   6      28.083  11.737  18.360  1.00 17.74           C  
ANISOU  837  CZ3 TRP B   6     1956   2190   2595    -23      4    150       C  
ATOM    838  CH2 TRP B   6      28.438  10.909  19.395  1.00 18.15           C  
ANISOU  838  CH2 TRP B   6     1928   2060   2908    434   -205    273       C  
ATOM    839  N   LYS B   7      21.454  14.304  16.845  1.00 11.00           N  
ANISOU  839  N   LYS B   7     1392   1242   1542    120     48   -121       N  
ATOM    840  CA  LYS B   7      20.574  14.755  15.767  1.00 10.96           C  
ANISOU  840  CA  LYS B   7     1382   1343   1437    143     18   -323       C  
ATOM    841  C   LYS B   7      19.888  16.049  16.244  1.00  9.99           C  
ANISOU  841  C   LYS B   7     1204   1286   1303     50     42   -244       C  
ATOM    842  O   LYS B   7      19.980  16.436  17.400  1.00 10.64           O  
ANISOU  842  O   LYS B   7     1483   1216   1343    144    -45   -228       O  
ATOM    843  CB  LYS B   7      19.508  13.669  15.406  1.00 13.34           C  
ANISOU  843  CB  LYS B   7     1758   1355   1952    335   -207   -290       C  
ATOM    844  CG  LYS B   7      18.559  13.314  16.346  1.00 18.18           C  
ANISOU  844  CG  LYS B   7     2540   1868   2498     47   -147   -130       C  
ATOM    845  CD  LYS B   7      17.454  12.215  15.713  1.00 24.02           C  
ANISOU  845  CD  LYS B   7     2950   2432   3743    107   -112   -274       C  
ATOM    846  CE  LYS B   7      16.544  11.634  16.772  1.00 26.45           C  
ANISOU  846  CE  LYS B   7     3233   2397   4419    272    191   -138       C  
ATOM    847  NZ  LYS B   7      15.347  10.832  16.155  1.00 36.56           N  
ANISOU  847  NZ  LYS B   7     4389   4117   5385    -92   -799   -592       N  
ATOM    848  N   ARG B   8      19.212  16.707  15.362  1.00 10.71           N  
ANISOU  848  N   ARG B   8     1339   1407   1324     77   -128   -232       N  
ATOM    849  CA  ARG B   8      18.504  17.931  15.739  1.00 10.03           C  
ANISOU  849  CA  ARG B   8     1209   1321   1279    141    -48   -279       C  
ATOM    850  C   ARG B   8      17.504  17.647  16.813  1.00 10.29           C  
ANISOU  850  C   ARG B   8     1217   1205   1486   -114     70   -197       C  
ATOM    851  O   ARG B   8      16.778  16.643  16.718  1.00 11.64           O  
ANISOU  851  O   ARG B   8     1356   1204   1861    -25     62   -330       O  
ATOM    852  CB  ARG B   8      17.799  18.508  14.549  1.00 11.87           C  
ANISOU  852  CB  ARG B   8     1534   1404   1570     70      3    -29       C  
ATOM    853  CG  ARG B   8      18.728  19.074  13.465  1.00 12.33           C  
ANISOU  853  CG  ARG B   8     1602   1692   1391    -47   -228    -38       C  
ATOM    854  CD  ARG B   8      17.984  19.805  12.366  1.00 16.65           C  
ANISOU  854  CD  ARG B   8     2130   2944   1252   -206    -10    250       C  
ATOM    855  NE  ARG B   8      18.893  20.425  11.448  1.00 20.33           N  
ANISOU  855  NE  ARG B   8     2397   3729   1598   -444   -259    593       N  
ATOM    856  CZ  ARG B   8      18.528  21.454  10.553  1.00 20.26           C  
ANISOU  856  CZ  ARG B   8     2607   2716   2374    -15     69     86       C  
ATOM    857  NH1 ARG B   8      17.356  22.175  10.798  1.00 29.12           N  
ANISOU  857  NH1 ARG B   8     2366   3661   5035    621      8   2402       N  
ATOM    858  NH2 ARG B   8      19.452  21.980   9.735  1.00 19.66           N  
ANISOU  858  NH2 ARG B   8     2581   2763   2126     66   -282     92       N  
ATOM    859  N   PRO B   9      17.392  18.489  17.828  1.00  9.33           N  
ANISOU  859  N   PRO B   9     1172   1112   1261     25     86    -43       N  
ATOM    860  CA  PRO B   9      16.482  18.214  18.959  1.00 10.43           C  
ANISOU  860  CA  PRO B   9     1158   1132   1672     95     53    127       C  
ATOM    861  C   PRO B   9      15.065  18.681  18.623  1.00  9.79           C  
ANISOU  861  C   PRO B   9     1198   1151   1369    -13    171    -15       C  
ATOM    862  O   PRO B   9      14.547  19.634  19.165  1.00 10.89           O  
ANISOU  862  O   PRO B   9     1304   1241   1590     82     27    -90       O  
ATOM    863  CB  PRO B   9      17.093  19.015  20.102  1.00 10.83           C  
ANISOU  863  CB  PRO B   9     1321   1352   1439    194     85     11       C  
ATOM    864  CG  PRO B   9      17.775  20.173  19.393  1.00 10.48           C  
ANISOU  864  CG  PRO B   9     1266   1346   1367     48     10   -145       C  
ATOM    865  CD  PRO B   9      18.340  19.575  18.137  1.00  9.92           C  
ANISOU  865  CD  PRO B   9     1161   1267   1340    -54    -27   -352       C  
ATOM    866  N   LEU B  10      14.429  17.958  17.701  1.00 11.79           N  
ANISOU  866  N   LEU B  10     1264   1487   1726     -8     90   -250       N  
ATOM    867  CA  LEU B  10      13.067  18.190  17.302  1.00 11.46           C  
ANISOU  867  CA  LEU B  10     1145   1432   1774    -82    -96   -195       C  
ATOM    868  C   LEU B  10      12.110  17.479  18.202  1.00 13.24           C  
ANISOU  868  C   LEU B  10     1487   1206   2336     31     13      4       C  
ATOM    869  O   LEU B  10      12.273  16.330  18.487  1.00 15.54           O  
ANISOU  869  O   LEU B  10     1564   1395   2942     16     36    104       O  
ATOM    870  CB  LEU B  10      12.893  17.698  15.904  1.00 15.18           C  
ANISOU  870  CB  LEU B  10     1619   1890   2256    -22   -348   -391       C  
ATOM    871  CG  LEU B  10      13.632  18.463  14.814  1.00 16.90           C  
ANISOU  871  CG  LEU B  10     2048   2834   1538    147   -140   -465       C  
ATOM    872  CD1 LEU B  10      13.660  17.698  13.525  1.00 23.06           C  
ANISOU  872  CD1 LEU B  10     3357   3121   2283    240    105   -664       C  
ATOM    873  CD2 LEU B  10      12.973  19.930  14.586  1.00 18.90           C  
ANISOU  873  CD2 LEU B  10     2581   2319   2278   -269   -185   -177       C  
ATOM    874  N   VAL B  11      11.109  18.190  18.637  1.00 12.06           N  
ANISOU  874  N   VAL B  11     1235   1382   1961     81     70    159       N  
ATOM    875  CA  VAL B  11      10.054  17.653  19.463  1.00 13.10           C  
ANISOU  875  CA  VAL B  11     1309   1635   2032     80    152    194       C  
ATOM    876  C   VAL B  11       8.702  18.109  18.995  1.00 13.85           C  
ANISOU  876  C   VAL B  11     1341   1697   2224   -208    -62    177       C  
ATOM    877  O   VAL B  11       8.596  19.022  18.162  1.00 14.46           O  
ANISOU  877  O   VAL B  11     1386   1767   2340   -158    -64    361       O  
ATOM    878  CB  VAL B  11      10.228  18.057  20.944  1.00 16.23           C  
ANISOU  878  CB  VAL B  11     1727   2420   2018     20    273    220       C  
ATOM    879  CG1 VAL B  11      11.540  17.546  21.485  1.00 18.98           C  
ANISOU  879  CG1 VAL B  11     1866   2580   2762     28   -176    490       C  
ATOM    880  CG2 VAL B  11      10.081  19.562  21.093  1.00 18.48           C  
ANISOU  880  CG2 VAL B  11     1562   2843   2614    174    223   -510       C  
ATOM    881  N   THR B  12       7.661  17.465  19.473  1.00 14.81           N  
ANISOU  881  N   THR B  12     1281   1906   2438   -166    -14    456       N  
ATOM    882  CA  THR B  12       6.309  17.838  19.125  1.00 16.16           C  
ANISOU  882  CA  THR B  12     1377   2226   2537   -304   -124    105       C  
ATOM    883  C   THR B  12       5.801  18.909  20.042  1.00 15.55           C  
ANISOU  883  C   THR B  12     1251   2318   2339   -105    -25    135       C  
ATOM    884  O   THR B  12       5.855  18.794  21.227  1.00 18.18           O  
ANISOU  884  O   THR B  12     1837   2432   2637     91    232    397       O  
ATOM    885  CB  THR B  12       5.378  16.583  19.163  1.00 17.76           C  
ANISOU  885  CB  THR B  12     1584   2170   2994   -375     73    271       C  
ATOM    886  OG1 THR B  12       5.901  15.589  18.269  1.00 20.95           O  
ANISOU  886  OG1 THR B  12     2074   2646   3240   -886   -136    -75       O  
ATOM    887  CG2 THR B  12       3.970  16.907  18.603  1.00 20.74           C  
ANISOU  887  CG2 THR B  12     1747   2554   3577   -578   -285    131       C  
ATOM    888  N   ILE B  13       5.216  19.915  19.435  1.00 17.31           N  
ANISOU  888  N   ILE B  13     1454   2202   2918   -142     -5    148       N  
ATOM    889  CA  ILE B  13       4.528  20.982  20.170  1.00 15.98           C  
ANISOU  889  CA  ILE B  13     1315   2047   2708    -76     97     82       C  
ATOM    890  C   ILE B  13       3.097  21.106  19.723  1.00 18.34           C  
ANISOU  890  C   ILE B  13     1846   2132   2989   -377    131    374       C  
ATOM    891  O   ILE B  13       2.746  20.644  18.660  1.00 20.02           O  
ANISOU  891  O   ILE B  13     1554   2445   3606     34   -332    267       O  
ATOM    892  CB  ILE B  13       5.271  22.334  19.947  1.00 16.98           C  
ANISOU  892  CB  ILE B  13     1497   2199   2754    289     95    318       C  
ATOM    893  CG1 ILE B  13       5.179  22.803  18.552  1.00 16.60           C  
ANISOU  893  CG1 ILE B  13     1433   2145   2726     23    -78    127       C  
ATOM    894  CG2 ILE B  13       6.716  22.166  20.292  1.00 16.95           C  
ANISOU  894  CG2 ILE B  13     1611   2254   2575    -30   -141    410       C  
ATOM    895  CD1 ILE B  13       5.575  24.223  18.362  1.00 19.27           C  
ANISOU  895  CD1 ILE B  13     2007   2599   2716     -7     31    548       C  
ATOM    896  N   ARG B  14       2.282  21.748  20.562  1.00 18.55           N  
ANISOU  896  N   ARG B  14     1364   2230   3454    -36    136    235       N  
ATOM    897  CA  ARG B  14       0.890  22.087  20.207  1.00 20.16           C  
ANISOU  897  CA  ARG B  14     1511   2131   4017   -137    209    185       C  
ATOM    898  C   ARG B  14       0.696  23.558  20.381  1.00 14.32           C  
ANISOU  898  C   ARG B  14     1203   1720   2516     24    351    518       C  
ATOM    899  O   ARG B  14       0.979  24.120  21.420  1.00 19.12           O  
ANISOU  899  O   ARG B  14     1755   2112   3395    245    284    523       O  
ATOM    900  CB  ARG B  14      -0.061  21.302  21.031  1.00 23.10           C  
ANISOU  900  CB  ARG B  14     1667   2476   4631   -212    411    412       C  
ATOM    901  CG  ARG B  14      -1.536  21.491  20.625  1.00 27.46           C  
ANISOU  901  CG  ARG B  14     1557   2831   6043   -504    382    626       C  
ATOM    902  CD  ARG B  14      -2.569  20.623  21.489  1.00 29.93           C  
ANISOU  902  CD  ARG B  14     2115   3881   5376   -761    302    697       C  
ATOM    903  NE  ARG B  14      -3.724  21.417  21.858  1.00 33.37           N  
ANISOU  903  NE  ARG B  14     2579   4718   5380  -1075    539   -761       N  
ATOM    904  CZ  ARG B  14      -4.769  21.431  21.213  1.00 41.32           C  
ANISOU  904  CZ  ARG B  14     4391   6070   5237    448   -515     69       C  
ATOM    905  NH1 ARG B  14      -4.834  20.749  20.077  1.00 50.56           N  
ANISOU  905  NH1 ARG B  14     6314   6785   6110   -148   -357   -633       N  
ATOM    906  NH2 ARG B  14      -5.891  22.096  21.696  1.00 40.22           N  
ANISOU  906  NH2 ARG B  14     4309   5572   5399    -29   -117    226       N  
ATOM    907  N   ILE B  15       0.175  24.179  19.340  1.00 19.64           N  
ANISOU  907  N   ILE B  15     1643   2211   3605      3    495    855       N  
ATOM    908  CA  ILE B  15      -0.056  25.637  19.395  1.00 19.19           C  
ANISOU  908  CA  ILE B  15     2019   2188   3082    254    578    484       C  
ATOM    909  C   ILE B  15      -1.175  25.998  18.496  1.00 20.95           C  
ANISOU  909  C   ILE B  15     1807   2777   3376   -330    438    123       C  
ATOM    910  O   ILE B  15      -1.312  25.453  17.417  1.00 27.04           O  
ANISOU  910  O   ILE B  15     3630   2669   3972    956    -76    -38       O  
ATOM    911  CB  ILE B  15       1.307  26.420  19.037  1.00 19.96           C  
ANISOU  911  CB  ILE B  15     2309   2315   2957   -268    355    472       C  
ATOM    912  CG1 ILE B  15       1.114  27.923  19.222  1.00 24.87           C  
ANISOU  912  CG1 ILE B  15     3504   2668   3278   -307    -20     -7       C  
ATOM    913  CG2 ILE B  15       1.821  26.012  17.700  1.00 19.04           C  
ANISOU  913  CG2 ILE B  15     2071   2372   2790   -388     32    327       C  
ATOM    914  CD1 ILE B  15       0.899  28.597  18.094  1.00 27.07           C  
ANISOU  914  CD1 ILE B  15     3549   2915   3821    697     -5    448       C  
ATOM    915  N   GLY B  16      -2.090  26.882  18.988  1.00 20.74           N  
ANISOU  915  N   GLY B  16     2208   2538   3130     65     35      5       N  
ATOM    916  CA  GLY B  16      -3.192  27.291  18.219  1.00 22.97           C  
ANISOU  916  CA  GLY B  16     2553   2912   3261    145   -298     32       C  
ATOM    917  C   GLY B  16      -4.059  26.119  17.739  1.00 23.82           C  
ANISOU  917  C   GLY B  16     2682   2779   3588    -25   -273    242       C  
ATOM    918  O   GLY B  16      -4.681  26.230  16.696  1.00 28.40           O  
ANISOU  918  O   GLY B  16     3043   3398   4349    -95   -586    447       O  
ATOM    919  N   GLY B  17      -4.102  24.987  18.551  1.00 21.83           N  
ANISOU  919  N   GLY B  17     2252   2668   3371    -73    127    397       N  
ATOM    920  CA  GLY B  17      -4.576  23.593  18.116  1.00 22.44           C  
ANISOU  920  CA  GLY B  17     1566   3576   3385   -977    261    -33       C  
ATOM    921  C   GLY B  17      -4.111  23.010  16.867  1.00 25.99           C  
ANISOU  921  C   GLY B  17     2720   3254   3902   -897    282    -45       C  
ATOM    922  O   GLY B  17      -4.809  22.110  16.302  1.00 29.71           O  
ANISOU  922  O   GLY B  17     2627   3786   4876  -1193    234   -442       O  
ATOM    923  N   GLN B  18      -2.832  23.264  16.528  1.00 24.80           N  
ANISOU  923  N   GLN B  18     1968   2889   4565   -583    -76      0       N  
ATOM    924  CA  GLN B  18      -2.092  22.379  15.603  1.00 24.41           C  
ANISOU  924  CA  GLN B  18     2784   2803   3686     55   -169     87       C  
ATOM    925  C   GLN B  18      -0.876  21.733  16.334  1.00 23.94           C  
ANISOU  925  C   GLN B  18     2429   2751   3915    323   -387    -29       C  
ATOM    926  O   GLN B  18      -0.324  22.311  17.244  1.00 24.70           O  
ANISOU  926  O   GLN B  18     1981   2501   4903    245   -281   -163       O  
ATOM    927  CB  GLN B  18      -1.464  23.176  14.280  1.00 21.11           C  
ANISOU  927  CB  GLN B  18     1756   3078   3183    568    -21   -268       C  
ATOM    928  CG  GLN B  18      -2.397  23.903  13.487  1.00 25.47           C  
ANISOU  928  CG  GLN B  18     2685   3236   3754    427   -388     -3       C  
ATOM    929  CD  GLN B  18      -1.772  24.583  12.336  1.00 26.79           C  
ANISOU  929  CD  GLN B  18     2639   3803   3736   -231   -416      9       C  
ATOM    930  OE1 GLN B  18      -1.997  24.157  11.119  1.00 34.37           O  
ANISOU  930  OE1 GLN B  18     4604   4914   3538    -18   -528   -162       O  
ATOM    931  NE2 GLN B  18      -0.862  25.547  12.618  1.00 30.78           N  
ANISOU  931  NE2 GLN B  18     2631   4117   4944   -207   -892     51       N  
ATOM    932  N   LEU B  19      -0.581  20.491  15.983  1.00 21.74           N  
ANISOU  932  N   LEU B  19     1672   2418   4170   -264   -575   -117       N  
ATOM    933  CA  LEU B  19       0.629  19.842  16.456  1.00 20.03           C  
ANISOU  933  CA  LEU B  19     1905   2374   3330   -239   -306    146       C  
ATOM    934  C   LEU B  19       1.677  20.061  15.416  1.00 21.22           C  
ANISOU  934  C   LEU B  19     2138   2716   3206   -302   -276    375       C  
ATOM    935  O   LEU B  19       1.401  20.021  14.256  1.00 25.14           O  
ANISOU  935  O   LEU B  19     2573   3166   3812   -445  -1050    270       O  
ATOM    936  CB  LEU B  19       0.407  18.324  16.705  1.00 20.87           C  
ANISOU  936  CB  LEU B  19     2597   2064   3266   -361   -296   -388       C  
ATOM    937  CG  LEU B  19      -0.395  17.872  17.837  1.00 21.62           C  
ANISOU  937  CG  LEU B  19     2778   2578   2858   -492   -434     55       C  
ATOM    938  CD1 LEU B  19      -0.235  16.385  17.951  1.00 27.22           C  
ANISOU  938  CD1 LEU B  19     3283   2874   4183   -408   -444   -258       C  
ATOM    939  CD2 LEU B  19      -0.051  18.486  19.085  1.00 25.61           C  
ANISOU  939  CD2 LEU B  19     3166   3116   3447   -659    -38   -572       C  
ATOM    940  N   LYS B  20       2.904  20.394  15.854  1.00 19.57           N  
ANISOU  940  N   LYS B  20     1871   2378   3184    -61   -449    322       N  
ATOM    941  CA  LYS B  20       3.968  20.718  14.943  1.00 19.04           C  
ANISOU  941  CA  LYS B  20     2227   2344   2660   -130   -342    304       C  
ATOM    942  C   LYS B  20       5.324  20.100  15.494  1.00 17.50           C  
ANISOU  942  C   LYS B  20     1899   2325   2425    -31   -777    179       C  
ATOM    943  O   LYS B  20       5.444  19.898  16.614  1.00 19.01           O  
ANISOU  943  O   LYS B  20     2111   2651   2459    199   -715     17       O  
ATOM    944  CB  LYS B  20       4.194  22.291  14.853  1.00 19.49           C  
ANISOU  944  CB  LYS B  20     2364   2301   2738    166   -635    145       C  
ATOM    945  CG  LYS B  20       2.958  23.031  14.535  1.00 19.62           C  
ANISOU  945  CG  LYS B  20     2376   2153   2923    101   -217    327       C  
ATOM    946  CD  LYS B  20       3.129  24.473  14.653  1.00 21.62           C  
ANISOU  946  CD  LYS B  20     2498   2298   3417    270    120    558       C  
ATOM    947  CE  LYS B  20       1.970  25.236  14.040  1.00 22.40           C  
ANISOU  947  CE  LYS B  20     1985   3092   3434   -139   -189    530       C  
ATOM    948  NZ  LYS B  20       2.058  25.347  12.538  1.00 23.87           N  
ANISOU  948  NZ  LYS B  20     2435   3246   3386   -239     47    878       N  
ATOM    949  N   GLU B  21       6.300  19.977  14.626  1.00 17.84           N  
ANISOU  949  N   GLU B  21     2147   2013   2618   -496   -783     64       N  
ATOM    950  CA  GLU B  21       7.724  19.613  15.052  1.00 16.17           C  
ANISOU  950  CA  GLU B  21     1897   2006   2237   -336   -685     30       C  
ATOM    951  C   GLU B  21       8.539  20.875  15.132  1.00 15.54           C  
ANISOU  951  C   GLU B  21     1964   1732   2208   -175   -533     72       C  
ATOM    952  O   GLU B  21       8.535  21.698  14.195  1.00 16.25           O  
ANISOU  952  O   GLU B  21     2282   1877   2012   -410   -713     62       O  
ATOM    953  CB  GLU B  21       8.378  18.644  14.034  1.00 18.44           C  
ANISOU  953  CB  GLU B  21     2340   2188   2478   -612   -439    -75       C  
ATOM    954  CG  GLU B  21       7.723  17.274  13.927  1.00 24.39           C  
ANISOU  954  CG  GLU B  21     2643   2842   3780   -878   -397   -205       C  
ATOM    955  CD  GLU B  21       7.663  16.559  15.253  1.00 25.99           C  
ANISOU  955  CD  GLU B  21     3170   2813   3892   -586   -113   -119       C  
ATOM    956  OE1 GLU B  21       6.500  16.318  15.777  1.00 28.19           O  
ANISOU  956  OE1 GLU B  21     3035   2798   4876   -704    -11   -542       O  
ATOM    957  OE2 GLU B  21       8.754  16.121  15.764  1.00 30.07           O  
ANISOU  957  OE2 GLU B  21     3490   2993   4940   -347   -488    441       O  
ATOM    958  N   ALA B  22       9.254  21.031  16.208  1.00 13.63           N  
ANISOU  958  N   ALA B  22     1672   1496   2009   -132   -406    180       N  
ATOM    959  CA  ALA B  22      10.031  22.247  16.434  1.00 12.58           C  
ANISOU  959  CA  ALA B  22     1587   1293   1899     66   -437      8       C  
ATOM    960  C   ALA B  22      11.360  21.897  17.139  1.00 10.83           C  
ANISOU  960  C   ALA B  22     1399   1415   1299     33   -121    141       C  
ATOM    961  O   ALA B  22      11.439  20.958  17.920  1.00 12.18           O  
ANISOU  961  O   ALA B  22     1337   1371   1920    -14    -87    413       O  
ATOM    962  CB  ALA B  22       9.247  23.191  17.292  1.00 12.98           C  
ANISOU  962  CB  ALA B  22     1587   1549   1795    -44   -306     42       C  
ATOM    963  N   LEU B  23      12.332  22.751  16.910  1.00 11.09           N  
ANISOU  963  N   LEU B  23     1484   1228   1502    -57   -189    198       N  
ATOM    964  CA  LEU B  23      13.662  22.627  17.505  1.00  9.96           C  
ANISOU  964  CA  LEU B  23     1292   1040   1451     90    -79    140       C  
ATOM    965  C   LEU B  23      13.684  23.189  18.884  1.00  9.75           C  
ANISOU  965  C   LEU B  23     1018   1142   1543     68    -67   -184       C  
ATOM    966  O   LEU B  23      13.306  24.369  19.080  1.00 12.57           O  
ANISOU  966  O   LEU B  23     1747   1299   1729    423   -255   -124       O  
ATOM    967  CB  LEU B  23      14.642  23.393  16.707  1.00 12.52           C  
ANISOU  967  CB  LEU B  23     1708   1285   1761    120    252    152       C  
ATOM    968  CG  LEU B  23      15.292  22.940  15.519  1.00 16.52           C  
ANISOU  968  CG  LEU B  23     2020   1696   2560     90    454     80       C  
ATOM    969  CD1 LEU B  23      16.162  24.055  14.930  1.00 15.74           C  
ANISOU  969  CD1 LEU B  23     2114   1809   2057    228    700    649       C  
ATOM    970  CD2 LEU B  23      16.129  21.714  15.762  1.00 16.06           C  
ANISOU  970  CD2 LEU B  23     1890   1563   2648    349    484    265       C  
ATOM    971  N   LEU B  24      14.219  22.458  19.838  1.00  9.78           N  
ANISOU  971  N   LEU B  24     1240    989   1485    133    -37     -7       N  
ATOM    972  CA  LEU B  24      14.536  23.029  21.136  1.00 10.42           C  
ANISOU  972  CA  LEU B  24     1146   1145   1667     23    -38    -12       C  
ATOM    973  C   LEU B  24      15.858  23.780  21.008  1.00  9.89           C  
ANISOU  973  C   LEU B  24     1222   1123   1413     -9     -5    -71       C  
ATOM    974  O   LEU B  24      16.891  23.139  20.880  1.00 10.79           O  
ANISOU  974  O   LEU B  24     1114   1302   1681    146    -26   -135       O  
ATOM    975  CB  LEU B  24      14.649  21.957  22.196  1.00 11.60           C  
ANISOU  975  CB  LEU B  24     1538   1203   1664     11     51    130       C  
ATOM    976  CG  LEU B  24      13.425  21.106  22.422  1.00 12.65           C  
ANISOU  976  CG  LEU B  24     1579   1395   1829     13    261     86       C  
ATOM    977  CD1 LEU B  24      13.834  19.936  23.434  1.00 16.75           C  
ANISOU  977  CD1 LEU B  24     2337   2105   1921   -608   -213    521       C  
ATOM    978  CD2 LEU B  24      12.223  21.901  22.935  1.00 17.13           C  
ANISOU  978  CD2 LEU B  24     1703   2158   2648   -310    446   -511       C  
ATOM    979  N   ASP B  25      15.794  25.119  20.987  1.00  9.19           N  
ANISOU  979  N   ASP B  25     1287   1049   1154     62    -30    -12       N  
ATOM    980  CA  ASP B  25      16.906  25.958  20.533  1.00  9.04           C  
ANISOU  980  CA  ASP B  25     1140   1074   1219    166     -4     64       C  
ATOM    981  C   ASP B  25      17.392  26.917  21.582  1.00  9.18           C  
ANISOU  981  C   ASP B  25     1279   1049   1159     82     64      0       C  
ATOM    982  O   ASP B  25      16.856  28.021  21.775  1.00  9.82           O  
ANISOU  982  O   ASP B  25     1307   1152   1270    178    141    -46       O  
ATOM    983  CB  ASP B  25      16.530  26.693  19.313  1.00  8.66           C  
ANISOU  983  CB  ASP B  25     1143   1006   1140     98    148    -84       C  
ATOM    984  CG  ASP B  25      17.674  27.300  18.619  1.00  9.06           C  
ANISOU  984  CG  ASP B  25     1282   1124   1034    211    -17     17       C  
ATOM    985  OD1 ASP B  25      18.811  27.268  19.209  1.00  9.95           O  
ANISOU  985  OD1 ASP B  25     1341   1312   1128     18     40    -19       O  
ATOM    986  OD2 ASP B  25      17.548  27.810  17.484  1.00 10.37           O  
ANISOU  986  OD2 ASP B  25     1339   1392   1207    107    133    154       O  
ATOM    987  N   THR B  26      18.468  26.541  22.265  1.00  9.25           N  
ANISOU  987  N   THR B  26     1334   1055   1124    205    -30    -15       N  
ATOM    988  CA  THR B  26      19.064  27.393  23.266  1.00  9.41           C  
ANISOU  988  CA  THR B  26     1337   1249    989    247     73   -142       C  
ATOM    989  C   THR B  26      19.709  28.658  22.685  1.00  9.20           C  
ANISOU  989  C   THR B  26     1335   1131   1027    126      6   -169       C  
ATOM    990  O   THR B  26      19.994  29.582  23.434  1.00 10.59           O  
ANISOU  990  O   THR B  26     1698   1161   1162    115      2    -87       O  
ATOM    991  CB  THR B  26      20.092  26.630  24.058  1.00  9.31           C  
ANISOU  991  CB  THR B  26     1474   1322    741    194    186   -219       C  
ATOM    992  OG1 THR B  26      21.171  26.194  23.211  1.00  9.58           O  
ANISOU  992  OG1 THR B  26     1437   1189   1011    108     30    -12       O  
ATOM    993  CG2 THR B  26      19.509  25.427  24.714  1.00  9.94           C  
ANISOU  993  CG2 THR B  26     1549   1275    952     85    121     66       C  
ATOM    994  N   GLY B  27      19.948  28.682  21.378  1.00  9.31           N  
ANISOU  994  N   GLY B  27     1322   1076   1136    124    145   -161       N  
ATOM    995  CA  GLY B  27      20.481  29.841  20.709  1.00 10.14           C  
ANISOU  995  CA  GLY B  27     1266   1360   1224    -70     36    -56       C  
ATOM    996  C   GLY B  27      19.470  30.904  20.315  1.00  9.76           C  
ANISOU  996  C   GLY B  27     1426   1056   1223     73     75     30       C  
ATOM    997  O   GLY B  27      19.845  31.926  19.780  1.00 11.36           O  
ANISOU  997  O   GLY B  27     1526   1356   1431    -68    187     86       O  
ATOM    998  N   ALA B  28      18.195  30.611  20.502  1.00  9.54           N  
ANISOU  998  N   ALA B  28     1376   1077   1172     45     29     31       N  
ATOM    999  CA  ALA B  28      17.115  31.482  20.082  1.00 10.67           C  
ANISOU  999  CA  ALA B  28     1555   1182   1314    220    150    114       C  
ATOM   1000  C   ALA B  28      16.526  32.175  21.333  1.00 10.65           C  
ANISOU 1000  C   ALA B  28     1465   1201   1380    112     16     42       C  
ATOM   1001  O   ALA B  28      16.056  31.518  22.252  1.00 10.66           O  
ANISOU 1001  O   ALA B  28     1712   1229   1108    104    117     -3       O  
ATOM   1002  CB  ALA B  28      16.023  30.684  19.434  1.00 10.57           C  
ANISOU 1002  CB  ALA B  28     1515   1245   1254    320     76     42       C  
ATOM   1003  N   ASP B  29      16.479  33.509  21.337  1.00 10.60           N  
ANISOU 1003  N   ASP B  29     1726   1082   1217    166     13     54       N  
ATOM   1004  CA  ASP B  29      15.920  34.212  22.459  1.00 11.21           C  
ANISOU 1004  CA  ASP B  29     1847   1179   1232    250    134    -46       C  
ATOM   1005  C   ASP B  29      14.441  33.954  22.545  1.00 12.25           C  
ANISOU 1005  C   ASP B  29     1714   1419   1521    456    186   -198       C  
ATOM   1006  O   ASP B  29      13.881  33.799  23.633  1.00 13.35           O  
ANISOU 1006  O   ASP B  29     1830   1806   1434    382    162   -176       O  
ATOM   1007  CB  ASP B  29      16.151  35.731  22.292  1.00 13.12           C  
ANISOU 1007  CB  ASP B  29     1817   1261   1904    216     -4   -245       C  
ATOM   1008  CG  ASP B  29      17.541  36.137  22.317  1.00 14.78           C  
ANISOU 1008  CG  ASP B  29     2054   1185   2377    179   -142      1       C  
ATOM   1009  OD1 ASP B  29      18.433  35.462  22.913  1.00 14.23           O  
ANISOU 1009  OD1 ASP B  29     2074   1549   1783    126   -201   -148       O  
ATOM   1010  OD2 ASP B  29      17.799  37.300  21.955  1.00 19.65           O  
ANISOU 1010  OD2 ASP B  29     2570   1616   3279   -236   -379    601       O  
ATOM   1011  N   ASP B  30      13.764  33.955  21.402  1.00 12.01           N  
ANISOU 1011  N   ASP B  30     1678   1467   1415    115     79     41       N  
ATOM   1012  CA  ASP B  30      12.337  33.876  21.321  1.00 12.45           C  
ANISOU 1012  CA  ASP B  30     1756   1625   1348    373     46     89       C  
ATOM   1013  C   ASP B  30      11.926  32.802  20.337  1.00 10.49           C  
ANISOU 1013  C   ASP B  30     1236   1540   1207    364     55    -53       C  
ATOM   1014  O   ASP B  30      12.525  32.664  19.311  1.00 16.23           O  
ANISOU 1014  O   ASP B  30     1724   2651   1791   -226    580   -481       O  
ATOM   1015  CB  ASP B  30      11.662  35.225  20.959  1.00 15.93           C  
ANISOU 1015  CB  ASP B  30     2232   1561   2257    293   -311   -104       C  
ATOM   1016  CG  ASP B  30      11.675  36.200  22.098  1.00 20.71           C  
ANISOU 1016  CG  ASP B  30     3575   2250   2042    576    -42   -122       C  
ATOM   1017  OD1 ASP B  30      11.163  35.857  23.248  1.00 23.88           O  
ANISOU 1017  OD1 ASP B  30     4046   2439   2587   1059    506   -153       O  
ATOM   1018  OD2 ASP B  30      12.190  37.229  21.983  1.00 28.67           O  
ANISOU 1018  OD2 ASP B  30     5457   2828   2608   -648    309     23       O  
ATOM   1019  N   THR B  31      10.812  32.211  20.597  1.00 11.55           N  
ANISOU 1019  N   THR B  31     1320   1462   1606    224    158     13       N  
ATOM   1020  CA  THR B  31      10.194  31.210  19.777  1.00 10.95           C  
ANISOU 1020  CA  THR B  31     1411   1216   1534    428    131    388       C  
ATOM   1021  C   THR B  31       9.725  31.796  18.437  1.00 10.47           C  
ANISOU 1021  C   THR B  31     1345   1238   1392    321    242    315       C  
ATOM   1022  O   THR B  31       9.052  32.857  18.417  1.00 11.63           O  
ANISOU 1022  O   THR B  31     1476   1275   1665    314    124    328       O  
ATOM   1023  CB  THR B  31       8.996  30.650  20.581  1.00 10.86           C  
ANISOU 1023  CB  THR B  31     1387   1449   1289    241    119    198       C  
ATOM   1024  OG1 THR B  31       9.532  29.958  21.708  1.00 11.64           O  
ANISOU 1024  OG1 THR B  31     1514   1650   1256    437    306    428       O  
ATOM   1025  CG2 THR B  31       8.152  29.702  19.791  1.00 11.82           C  
ANISOU 1025  CG2 THR B  31     1522   1715   1252    434    347    237       C  
ATOM   1026  N  AVAL B  32       9.986  31.087  17.371  0.50  9.67           N  
ANISOU 1026  N  AVAL B  32     1076   1301   1294    110     64    187       N  
ATOM   1027  N  BVAL B  32      10.038  31.124  17.363  0.50  9.96           N  
ANISOU 1027  N  BVAL B  32     1148   1333   1301    183     -5    122       N  
ATOM   1028  CA AVAL B  32       9.677  31.536  15.998  0.50 10.27           C  
ANISOU 1028  CA AVAL B  32     1039   1455   1406     52   -196    185       C  
ATOM   1029  CA BVAL B  32       9.595  31.576  16.039  0.50 10.37           C  
ANISOU 1029  CA BVAL B  32     1182   1368   1390     18   -248    147       C  
ATOM   1030  C  AVAL B  32       9.067  30.330  15.302  0.50 10.69           C  
ANISOU 1030  C  AVAL B  32     1471   1443   1147     54    -48    310       C  
ATOM   1031  C  BVAL B  32       9.131  30.396  15.213  0.50 11.58           C  
ANISOU 1031  C  BVAL B  32     1452   1500   1448    188    -54    219       C  
ATOM   1032  O  AVAL B  32       9.653  29.275  15.285  0.50 12.01           O  
ANISOU 1032  O  AVAL B  32     1527   1442   1594    314   -156    144       O  
ATOM   1033  O  BVAL B  32       9.883  29.415  14.984  0.50 10.76           O  
ANISOU 1033  O  BVAL B  32     1355   1288   1444    232    106    336       O  
ATOM   1034  CB AVAL B  32      10.951  32.007  15.202  0.50 12.58           C  
ANISOU 1034  CB AVAL B  32     1628   1899   1253    -82    -77    383       C  
ATOM   1035  CB BVAL B  32      10.613  32.441  15.331  0.50 10.87           C  
ANISOU 1035  CB BVAL B  32     1396   1405   1327    171   -103    254       C  
ATOM   1036  CG1AVAL B  32      10.531  32.779  13.929  0.50 14.76           C  
ANISOU 1036  CG1AVAL B  32     1829   2135   1642    -86   -551    178       C  
ATOM   1037  CG1BVAL B  32      11.912  31.703  15.139  0.50  9.64           C  
ANISOU 1037  CG1BVAL B  32     1262   1401   1000    195   -236     91       C  
ATOM   1038  CG2AVAL B  32      11.851  32.854  16.060  0.50 12.18           C  
ANISOU 1038  CG2AVAL B  32     1550   1716   1359    262     30     80       C  
ATOM   1039  CG2BVAL B  32      10.039  32.913  13.931  0.50 12.58           C  
ANISOU 1039  CG2BVAL B  32     1592   1535   1651   -360     -1    246       C  
ATOM   1040  N   LEU B  33       7.868  30.490  14.756  1.00 11.96           N  
ANISOU 1040  N   LEU B  33     1245   1438   1858    172   -206    200       N  
ATOM   1041  CA  LEU B  33       7.216  29.418  14.074  1.00 11.24           C  
ANISOU 1041  CA  LEU B  33     1406   1489   1376     72     15    218       C  
ATOM   1042  C   LEU B  33       7.002  29.790  12.642  1.00 11.12           C  
ANISOU 1042  C   LEU B  33     1235   1443   1545   -178   -117    122       C  
ATOM   1043  O   LEU B  33       6.810  30.994  12.262  1.00 12.51           O  
ANISOU 1043  O   LEU B  33     1655   1492   1604    -49    -44    281       O  
ATOM   1044  CB  LEU B  33       5.857  29.088  14.678  1.00 13.77           C  
ANISOU 1044  CB  LEU B  33     1693   1802   1735   -245   -162    -53       C  
ATOM   1045  CG  LEU B  33       5.931  28.738  16.215  1.00 16.72           C  
ANISOU 1045  CG  LEU B  33     2294   2264   1791   -131     99    312       C  
ATOM   1046  CD1 LEU B  33       4.606  28.398  16.743  1.00 18.93           C  
ANISOU 1046  CD1 LEU B  33     2631   2673   1885   -637    101    323       C  
ATOM   1047  CD2 LEU B  33       6.875  27.635  16.489  1.00 19.01           C  
ANISOU 1047  CD2 LEU B  33     2948   2185   2089     85   -221    346       C  
ATOM   1048  N   GLU B  34       6.947  28.752  11.801  1.00 12.53           N  
ANISOU 1048  N   GLU B  34     1722   1536   1501   -115    -18    146       N  
ATOM   1049  CA  GLU B  34       6.660  28.878  10.440  1.00 13.58           C  
ANISOU 1049  CA  GLU B  34     1749   1808   1600   -196     16    156       C  
ATOM   1050  C   GLU B  34       5.322  29.529  10.227  1.00 13.54           C  
ANISOU 1050  C   GLU B  34     1950   1997   1197    -95    -97     60       C  
ATOM   1051  O   GLU B  34       4.419  29.460  11.081  1.00 13.84           O  
ANISOU 1051  O   GLU B  34     1782   1865   1608   -141    -16    418       O  
ATOM   1052  CB  GLU B  34       6.665  27.499   9.785  1.00 14.53           C  
ANISOU 1052  CB  GLU B  34     2040   1883   1596     72    116    -70       C  
ATOM   1053  CG  GLU B  34       8.080  26.765   9.833  1.00 18.78           C  
ANISOU 1053  CG  GLU B  34     2193   2432   2510    112   -225   -197       C  
ATOM   1054  CD  GLU B  34       7.993  25.322   9.455  1.00 20.50           C  
ANISOU 1054  CD  GLU B  34     2415   2349   3026    146    205    -54       C  
ATOM   1055  OE1 GLU B  34       6.962  24.904   8.970  1.00 28.89           O  
ANISOU 1055  OE1 GLU B  34     3766   3280   3931    115   -858  -1109       O  
ATOM   1056  OE2 GLU B  34       9.022  24.587   9.611  1.00 28.63           O  
ANISOU 1056  OE2 GLU B  34     2705   3342   4828    529   -693   -805       O  
ATOM   1057  N   GLU B  35       5.186  30.158   9.070  1.00 14.04           N  
ANISOU 1057  N   GLU B  35     2031   2214   1087    230    101    110       N  
ATOM   1058  CA  GLU B  35       4.008  30.894   8.764  1.00 14.57           C  
ANISOU 1058  CA  GLU B  35     1929   2190   1414     77   -230    238       C  
ATOM   1059  C   GLU B  35       2.736  30.099   9.033  1.00 15.23           C  
ANISOU 1059  C   GLU B  35     2069   2042   1674     36   -428     99       C  
ATOM   1060  O   GLU B  35       2.618  28.985   8.623  1.00 17.36           O  
ANISOU 1060  O   GLU B  35     2225   2126   2243   -319   -528     18       O  
ATOM   1061  CB  GLU B  35       4.068  31.332   7.305  1.00 17.17           C  
ANISOU 1061  CB  GLU B  35     2435   2465   1621    322     96    128       C  
ATOM   1062  CG  GLU B  35       2.870  32.108   6.843  1.00 20.98           C  
ANISOU 1062  CG  GLU B  35     2953   2773   2245    370   -196    644       C  
ATOM   1063  CD  GLU B  35       2.585  33.345   7.670  1.00 22.72           C  
ANISOU 1063  CD  GLU B  35     3224   2484   2921    740   -365    645       C  
ATOM   1064  OE1 GLU B  35       1.408  33.515   8.064  1.00 28.18           O  
ANISOU 1064  OE1 GLU B  35     3828   3495   3383    860    574    768       O  
ATOM   1065  OE2 GLU B  35       3.546  34.159   7.932  1.00 24.58           O  
ANISOU 1065  OE2 GLU B  35     4444   2433   2461    301   -225    634       O  
ATOM   1066  N   MET B  36       1.805  30.723   9.840  1.00 14.73           N  
ANISOU 1066  N   MET B  36     1734   2131   1730   -182   -359    256       N  
ATOM   1067  CA  MET B  36       0.527  30.139  10.236  1.00 17.36           C  
ANISOU 1067  CA  MET B  36     1988   2200   2408   -478   -279    146       C  
ATOM   1068  C   MET B  36      -0.407  31.321  10.552  1.00 19.25           C  
ANISOU 1068  C   MET B  36     1910   2701   2701   -293   -265     89       C  
ATOM   1069  O   MET B  36       0.023  32.360  11.007  1.00 18.96           O  
ANISOU 1069  O   MET B  36     1660   2221   3320     68   -108    456       O  
ATOM   1070  CB  MET B  36       0.692  29.236  11.466  1.00 19.82           C  
ANISOU 1070  CB  MET B  36     2259   2658   2613   -566    -95    350       C  
ATOM   1071  CG  MET B  36       1.229  29.898  12.577  1.00 19.29           C  
ANISOU 1071  CG  MET B  36     2509   2393   2425   -143    231    397       C  
ATOM   1072  SD  MET B  36       1.356  28.807  14.099  1.00 22.97           S  
ANISOU 1072  SD  MET B  36     2923   3116   2687    214    131    664       S  
ATOM   1073  CE  MET B  36      -0.360  28.226  14.294  1.00 24.95           C  
ANISOU 1073  CE  MET B  36     2668   3729   3080    274    556    596       C  
ATOM   1074  N   ASN B  37      -1.709  31.132  10.332  1.00 20.26           N  
ANISOU 1074  N   ASN B  37     1792   3083   2820   -475    -82    171       N  
ATOM   1075  CA  ASN B  37      -2.638  32.231  10.517  1.00 21.01           C  
ANISOU 1075  CA  ASN B  37     2125   3453   2404   -119   -174    367       C  
ATOM   1076  C   ASN B  37      -3.266  32.173  11.886  1.00 21.41           C  
ANISOU 1076  C   ASN B  37     2074   3548   2509   -741    253    672       C  
ATOM   1077  O   ASN B  37      -4.454  31.833  12.014  1.00 24.76           O  
ANISOU 1077  O   ASN B  37     1863   4532   3012   -644     22    285       O  
ATOM   1078  CB  ASN B  37      -3.729  32.237   9.417  1.00 25.16           C  
ANISOU 1078  CB  ASN B  37     2584   4030   2944   -116   -461     74       C  
ATOM   1079  CG  ASN B  37      -4.495  33.615   9.318  1.00 28.86           C  
ANISOU 1079  CG  ASN B  37     2634   4647   3681    249   -448    199       C  
ATOM   1080  OD1 ASN B  37      -5.650  33.678   8.768  1.00 41.63           O  
ANISOU 1080  OD1 ASN B  37     3805   6512   5500    858  -1657    166       O  
ATOM   1081  ND2 ASN B  37      -3.954  34.630   9.900  1.00 30.12           N  
ANISOU 1081  ND2 ASN B  37     3041   4164   4236    -79    140    419       N  
ATOM   1082  N   LEU B  38      -2.522  32.587  12.908  1.00 21.91           N  
ANISOU 1082  N   LEU B  38     1943   3411   2969   -270    -67    663       N  
ATOM   1083  CA  LEU B  38      -3.034  32.656  14.287  1.00 19.95           C  
ANISOU 1083  CA  LEU B  38     2009   2797   2771   -395    -92    571       C  
ATOM   1084  C   LEU B  38      -4.029  33.750  14.449  1.00 21.78           C  
ANISOU 1084  C   LEU B  38     2374   2696   3203   -370     14    686       C  
ATOM   1085  O   LEU B  38      -3.793  34.868  14.014  1.00 21.95           O  
ANISOU 1085  O   LEU B  38     2841   2389   3110   -496   -219    816       O  
ATOM   1086  CB  LEU B  38      -1.936  32.923  15.259  1.00 22.74           C  
ANISOU 1086  CB  LEU B  38     2604   2808   3224   -625   -396    729       C  
ATOM   1087  CG  LEU B  38      -1.069  31.902  15.648  1.00 25.13           C  
ANISOU 1087  CG  LEU B  38     2741   2572   4232   -529   -718    492       C  
ATOM   1088  CD1 LEU B  38       0.047  32.416  16.502  1.00 21.59           C  
ANISOU 1088  CD1 LEU B  38     2760   2575   2864   -467   -487    878       C  
ATOM   1089  CD2 LEU B  38      -1.812  30.783  16.428  1.00 24.06           C  
ANISOU 1089  CD2 LEU B  38     2393   2669   4081   -233   -599    627       C  
ATOM   1090  N   PRO B  39      -4.979  33.534  15.305  1.00 21.55           N  
ANISOU 1090  N   PRO B  39     2268   2625   3292   -369    -52    309       N  
ATOM   1091  CA  PRO B  39      -5.876  34.619  15.681  1.00 22.44           C  
ANISOU 1091  CA  PRO B  39     2471   2940   3113    -47   -201    266       C  
ATOM   1092  C   PRO B  39      -5.241  35.554  16.642  1.00 21.52           C  
ANISOU 1092  C   PRO B  39     2190   2997   2987   -444    186    343       C  
ATOM   1093  O   PRO B  39      -4.319  35.148  17.343  1.00 23.61           O  
ANISOU 1093  O   PRO B  39     2429   3611   2929   -812     54    736       O  
ATOM   1094  CB  PRO B  39      -7.020  33.916  16.322  1.00 25.66           C  
ANISOU 1094  CB  PRO B  39     2585   3301   3861   -248    -19     91       C  
ATOM   1095  CG  PRO B  39      -6.481  32.552  16.730  1.00 24.43           C  
ANISOU 1095  CG  PRO B  39     2648   2971   3660   -441    416     84       C  
ATOM   1096  CD  PRO B  39      -5.407  32.216  15.866  1.00 24.15           C  
ANISOU 1096  CD  PRO B  39     2434   2995   3743   -591    332    369       C  
ATOM   1097  N   GLY B  40      -5.745  36.767  16.704  1.00 24.99           N  
ANISOU 1097  N   GLY B  40     3225   3284   2984   -408    218    221       N  
ATOM   1098  CA  GLY B  40      -5.375  37.721  17.748  1.00 25.65           C  
ANISOU 1098  CA  GLY B  40     3273   3280   3192   -731    500    147       C  
ATOM   1099  C   GLY B  40      -4.521  38.948  17.226  1.00 24.98           C  
ANISOU 1099  C   GLY B  40     2781   3194   3516   -491    429    160       C  
ATOM   1100  O   GLY B  40      -4.058  38.973  16.068  1.00 24.97           O  
ANISOU 1100  O   GLY B  40     2638   3253   3597    210    410    323       O  
ATOM   1101  N   LYS B  41      -4.249  39.859  18.112  1.00 22.61           N  
ANISOU 1101  N   LYS B  41     2563   2772   3253     50    793    138       N  
ATOM   1102  CA  LYS B  41      -3.396  41.006  17.797  1.00 22.18           C  
ANISOU 1102  CA  LYS B  41     2118   2784   3526    164    377     97       C  
ATOM   1103  C   LYS B  41      -1.942  40.606  17.690  1.00 19.98           C  
ANISOU 1103  C   LYS B  41     2115   2402   3075    457    642    355       C  
ATOM   1104  O   LYS B  41      -1.494  39.687  18.375  1.00 21.49           O  
ANISOU 1104  O   LYS B  41     2325   2479   3361    343    927    908       O  
ATOM   1105  CB  LYS B  41      -3.527  42.037  18.815  1.00 24.29           C  
ANISOU 1105  CB  LYS B  41     2044   3459   3725    623    599   -115       C  
ATOM   1106  N   TRP B  42      -1.191  41.380  16.943  1.00 17.83           N  
ANISOU 1106  N   TRP B  42     1632   2520   2620    492    396    484       N  
ATOM   1107  CA  TRP B  42       0.227  41.166  16.820  1.00 16.77           C  
ANISOU 1107  CA  TRP B  42     1782   2153   2434    519    385    416       C  
ATOM   1108  C   TRP B  42       0.923  42.476  16.515  1.00 19.20           C  
ANISOU 1108  C   TRP B  42     1959   2160   3176    666    374    596       C  
ATOM   1109  O   TRP B  42       0.256  43.504  16.205  1.00 19.32           O  
ANISOU 1109  O   TRP B  42     2220   2130   2990    730    323    668       O  
ATOM   1110  CB  TRP B  42       0.489  40.155  15.762  1.00 17.79           C  
ANISOU 1110  CB  TRP B  42     1968   2287   2503    123    252    481       C  
ATOM   1111  CG  TRP B  42      -0.066  40.502  14.375  1.00 20.38           C  
ANISOU 1111  CG  TRP B  42     2091   3156   2494    667    233    228       C  
ATOM   1112  CD1 TRP B  42      -1.329  40.198  13.883  1.00 25.45           C  
ANISOU 1112  CD1 TRP B  42     2674   3744   3251    -27     39    562       C  
ATOM   1113  CD2 TRP B  42       0.618  41.195  13.312  1.00 21.83           C  
ANISOU 1113  CD2 TRP B  42     2300   2580   3413    686    128    757       C  
ATOM   1114  NE1 TRP B  42      -1.460  40.670  12.600  1.00 27.98           N  
ANISOU 1114  NE1 TRP B  42     2867   3873   3891    507   -435   1131       N  
ATOM   1115  CE2 TRP B  42      -0.312  41.351  12.247  1.00 25.46           C  
ANISOU 1115  CE2 TRP B  42     2263   3599   3812    944    -98    783       C  
ATOM   1116  CE3 TRP B  42       1.862  41.799  13.189  1.00 20.31           C  
ANISOU 1116  CE3 TRP B  42     2780   2318   2616     89    479    584       C  
ATOM   1117  CZ2 TRP B  42       0.025  41.973  11.050  1.00 29.34           C  
ANISOU 1117  CZ2 TRP B  42     3756   3539   3853    242   -268    654       C  
ATOM   1118  CZ3 TRP B  42       2.172  42.434  12.012  1.00 24.40           C  
ANISOU 1118  CZ3 TRP B  42     3727   3039   2504    -16      6    558       C  
ATOM   1119  CH2 TRP B  42       1.280  42.439  10.927  1.00 26.01           C  
ANISOU 1119  CH2 TRP B  42     3990   3299   2593   -263   -181    749       C  
ATOM   1120  N   LYS B  43       2.250  42.460  16.608  1.00 17.48           N  
ANISOU 1120  N   LYS B  43     1697   2112   2830    577    645    679       N  
ATOM   1121  CA  LYS B  43       3.093  43.659  16.384  1.00 17.00           C  
ANISOU 1121  CA  LYS B  43     1564   2182   2712    536    551    372       C  
ATOM   1122  C   LYS B  43       4.218  43.209  15.433  1.00 15.16           C  
ANISOU 1122  C   LYS B  43     1641   1932   2185    600    295    449       C  
ATOM   1123  O   LYS B  43       4.762  42.138  15.617  1.00 15.41           O  
ANISOU 1123  O   LYS B  43     1781   1572   2499    631    376    412       O  
ATOM   1124  CB  LYS B  43       3.747  44.098  17.746  1.00 21.14           C  
ANISOU 1124  CB  LYS B  43     2264   2652   3116     13   1159   -364       C  
ATOM   1125  N   PRO B  44       4.634  44.042  14.449  1.00 14.87           N  
ANISOU 1125  N   PRO B  44     1682   1627   2339    386    382    483       N  
ATOM   1126  CA  PRO B  44       5.751  43.669  13.585  1.00 16.08           C  
ANISOU 1126  CA  PRO B  44     1850   1879   2378    228    227    406       C  
ATOM   1127  C   PRO B  44       7.053  43.707  14.292  1.00 14.07           C  
ANISOU 1127  C   PRO B  44     1662   1714   1970      4    312     75       C  
ATOM   1128  O   PRO B  44       7.311  44.549  15.161  1.00 15.46           O  
ANISOU 1128  O   PRO B  44     1761   1810   2301    300    247     53       O  
ATOM   1129  CB  PRO B  44       5.668  44.716  12.424  1.00 18.36           C  
ANISOU 1129  CB  PRO B  44     2055   2539   2379    201    315    596       C  
ATOM   1130  CG  PRO B  44       4.908  45.753  12.928  1.00 20.62           C  
ANISOU 1130  CG  PRO B  44     3406   1914   2513    140    265    528       C  
ATOM   1131  CD  PRO B  44       4.013  45.294  14.021  1.00 16.20           C  
ANISOU 1131  CD  PRO B  44     1729   1651   2772    311     55    491       C  
ATOM   1132  N   LYS B  45       7.976  42.792  13.856  1.00 12.76           N  
ANISOU 1132  N   LYS B  45     1664   1462   1718    271    307     83       N  
ATOM   1133  CA  LYS B  45       9.294  42.745  14.409  1.00 13.22           C  
ANISOU 1133  CA  LYS B  45     1638   1631   1754    306    163     46       C  
ATOM   1134  C   LYS B  45      10.238  42.236  13.336  1.00 11.33           C  
ANISOU 1134  C   LYS B  45     1463   1311   1529     64     43     75       C  
ATOM   1135  O   LYS B  45       9.804  41.550  12.424  1.00 12.84           O  
ANISOU 1135  O   LYS B  45     1512   1558   1809   -229    148   -180       O  
ATOM   1136  CB  LYS B  45       9.262  41.746  15.645  1.00 14.85           C  
ANISOU 1136  CB  LYS B  45     1987   1807   1846    260    442     -2       C  
ATOM   1137  CG  LYS B  45      10.453  41.652  16.442  1.00 16.26           C  
ANISOU 1137  CG  LYS B  45     2183   1898   2096     12    353    177       C  
ATOM   1138  CD  LYS B  45      10.251  40.656  17.625  1.00 18.57           C  
ANISOU 1138  CD  LYS B  45     2892   2046   2116     85    201    394       C  
ATOM   1139  CE  LYS B  45      11.388  40.350  18.247  1.00 24.01           C  
ANISOU 1139  CE  LYS B  45     2694   3450   2976     31    341     97       C  
ATOM   1140  NZ  LYS B  45      11.766  41.253  19.087  1.00 31.36           N  
ANISOU 1140  NZ  LYS B  45     3961   3817   4136   -645   -183   -226       N  
ATOM   1141  N  AMET B  46      11.526  42.568  13.486  0.50 10.65           N  
ANISOU 1141  N  AMET B  46     1552   1320   1174    -55     85   -138       N  
ATOM   1142  N  BMET B  46      11.506  42.525  13.476  0.50 10.79           N  
ANISOU 1142  N  BMET B  46     1559   1343   1196    -32    117   -120       N  
ATOM   1143  CA AMET B  46      12.615  41.969  12.670  0.50 10.47           C  
ANISOU 1143  CA AMET B  46     1472   1202   1302    -16     83   -247       C  
ATOM   1144  CA BMET B  46      12.502  41.909  12.624  0.50 10.99           C  
ANISOU 1144  CA BMET B  46     1512   1341   1321     96    122   -176       C  
ATOM   1145  C  AMET B  46      13.445  41.164  13.610  0.50 11.30           C  
ANISOU 1145  C  AMET B  46     1539   1514   1239    -77    -19   -197       C  
ATOM   1146  C  BMET B  46      13.537  41.236  13.513  0.50 11.55           C  
ANISOU 1146  C  BMET B  46     1605   1611   1172     37     19   -176       C  
ATOM   1147  O  AMET B  46      13.809  41.643  14.668  0.50 14.12           O  
ANISOU 1147  O  AMET B  46     1911   2037   1417    312   -194   -420       O  
ATOM   1148  O  BMET B  46      13.898  41.764  14.567  0.50 14.14           O  
ANISOU 1148  O  BMET B  46     1842   1974   1554    243   -320   -424       O  
ATOM   1149  CB AMET B  46      13.466  43.059  12.058  0.50 11.76           C  
ANISOU 1149  CB AMET B  46     1245   1571   1652   -220    159   -184       C  
ATOM   1150  CB BMET B  46      13.111  42.949  11.663  0.50 12.91           C  
ANISOU 1150  CB BMET B  46     1541   1544   1818    -98    374   -173       C  
ATOM   1151  CG AMET B  46      12.789  43.857  11.007  0.50 13.09           C  
ANISOU 1151  CG AMET B  46     1808   1271   1893    -72      6    -82       C  
ATOM   1152  CG BMET B  46      12.029  43.400  10.392  0.50 11.70           C  
ANISOU 1152  CG BMET B  46     1123   1023   2298    294    853    245       C  
ATOM   1153  SD AMET B  46      12.639  42.926   9.468  0.50 17.21           S  
ANISOU 1153  SD AMET B  46     2911   1698   1929   -647   -352     31       S  
ATOM   1154  SD BMET B  46      12.735  44.629   9.414  0.50 13.86           S  
ANISOU 1154  SD BMET B  46     2042   1471   1751   -322     63    -16       S  
ATOM   1155  CE AMET B  46      14.151  43.490   8.578  0.50 19.01           C  
ANISOU 1155  CE AMET B  46     2954   2253   2014   -142    167   -188       C  
ATOM   1156  CE BMET B  46      14.231  43.876   8.903  0.50 12.74           C  
ANISOU 1156  CE BMET B  46     1683   1763   1392   -424   -170    129       C  
ATOM   1157  N   ILE B  47      13.842  39.964  13.186  1.00 10.84           N  
ANISOU 1157  N   ILE B  47     1302   1474   1343     42     47   -247       N  
ATOM   1158  CA  ILE B  47      14.813  39.177  13.940  1.00 11.08           C  
ANISOU 1158  CA  ILE B  47     1332   1584   1293    -57     89   -142       C  
ATOM   1159  C   ILE B  47      15.931  38.753  13.009  1.00 10.70           C  
ANISOU 1159  C   ILE B  47     1336   1432   1296    -30     71    -66       C  
ATOM   1160  O   ILE B  47      15.724  38.518  11.826  1.00 11.02           O  
ANISOU 1160  O   ILE B  47     1459   1480   1247   -130    137   -107       O  
ATOM   1161  CB  ILE B  47      14.181  37.966  14.625  1.00 11.77           C  
ANISOU 1161  CB  ILE B  47     1255   1855   1360    176    123    146       C  
ATOM   1162  CG1 ILE B  47      13.549  37.010  13.637  1.00 11.90           C  
ANISOU 1162  CG1 ILE B  47     1347   1691   1483    100      5    270       C  
ATOM   1163  CG2 ILE B  47      13.173  38.421  15.662  1.00 13.94           C  
ANISOU 1163  CG2 ILE B  47     1676   2061   1557     24    267   -111       C  
ATOM   1164  CD1 ILE B  47      13.022  35.724  14.291  1.00 13.69           C  
ANISOU 1164  CD1 ILE B  47     1674   1731   1794    -87    -54    376       C  
ATOM   1165  N   GLY B  48      17.120  38.669  13.564  1.00 11.46           N  
ANISOU 1165  N   GLY B  48     1403   1586   1364     99    135    -59       N  
ATOM   1166  CA  GLY B  48      18.320  38.474  12.794  1.00 13.20           C  
ANISOU 1166  CA  GLY B  48     1515   1521   1978    142    177    -70       C  
ATOM   1167  C   GLY B  48      19.102  37.292  13.169  1.00 10.80           C  
ANISOU 1167  C   GLY B  48     1325   1319   1458      0     74     43       C  
ATOM   1168  O   GLY B  48      19.208  36.916  14.325  1.00 12.91           O  
ANISOU 1168  O   GLY B  48     1568   1853   1484    190     49   -126       O  
ATOM   1169  N   GLY B  49      19.683  36.657  12.171  1.00 10.19           N  
ANISOU 1169  N   GLY B  49     1305   1355   1212     38    121     32       N  
ATOM   1170  CA  GLY B  49      20.538  35.477  12.381  1.00 11.55           C  
ANISOU 1170  CA  GLY B  49     1590   1385   1410    234     26    197       C  
ATOM   1171  C   GLY B  49      21.561  35.370  11.272  1.00 10.81           C  
ANISOU 1171  C   GLY B  49     1576   1466   1062     93    127    149       C  
ATOM   1172  O   GLY B  49      21.815  36.339  10.553  1.00 10.84           O  
ANISOU 1172  O   GLY B  49     1339   1374   1403     29    118    172       O  
ATOM   1173  N   ILE B  50      22.071  34.177  11.061  1.00 11.10           N  
ANISOU 1173  N   ILE B  50     1450   1391   1374    311    121    345       N  
ATOM   1174  CA  ILE B  50      22.936  33.957   9.913  1.00 10.38           C  
ANISOU 1174  CA  ILE B  50     1104   1567   1270    206    145    143       C  
ATOM   1175  C   ILE B  50      22.138  34.215   8.636  1.00 10.65           C  
ANISOU 1175  C   ILE B  50     1366   1419   1258    168     14     64       C  
ATOM   1176  O   ILE B  50      21.036  33.724   8.470  1.00 11.98           O  
ANISOU 1176  O   ILE B  50     1394   1614   1542    152      5     49       O  
ATOM   1177  CB  ILE B  50      23.506  32.538   9.991  1.00 10.60           C  
ANISOU 1177  CB  ILE B  50     1324   1481   1223    180     86     44       C  
ATOM   1178  CG1 ILE B  50      24.579  32.499  11.107  1.00 12.14           C  
ANISOU 1178  CG1 ILE B  50     1549   1625   1439    258   -114    103       C  
ATOM   1179  CG2 ILE B  50      24.076  32.097   8.657  1.00 11.67           C  
ANISOU 1179  CG2 ILE B  50     1470   1672   1289    225    117     90       C  
ATOM   1180  CD1 ILE B  50      25.054  31.129  11.469  1.00 12.48           C  
ANISOU 1180  CD1 ILE B  50     1511   1683   1548    309   -244    223       C  
ATOM   1181  N   GLY B  51      22.724  35.054   7.768  1.00 11.06           N  
ANISOU 1181  N   GLY B  51     1193   1622   1385    216      1    151       N  
ATOM   1182  CA  GLY B  51      22.117  35.473   6.544  1.00 11.38           C  
ANISOU 1182  CA  GLY B  51     1455   1657   1211    331    122    383       C  
ATOM   1183  C   GLY B  51      21.413  36.789   6.607  1.00 12.55           C  
ANISOU 1183  C   GLY B  51     1614   1608   1545    130   -205    225       C  
ATOM   1184  O   GLY B  51      21.164  37.361   5.561  1.00 17.52           O  
ANISOU 1184  O   GLY B  51     2565   2381   1710    686   -457    456       O  
ATOM   1185  N   GLY B  52      21.137  37.318   7.779  1.00 11.23           N  
ANISOU 1185  N   GLY B  52     1330   1448   1487    104    145    277       N  
ATOM   1186  CA  GLY B  52      20.416  38.577   7.923  1.00 11.90           C  
ANISOU 1186  CA  GLY B  52     1319   1420   1783     19    184    369       C  
ATOM   1187  C   GLY B  52      19.111  38.420   8.657  1.00 10.49           C  
ANISOU 1187  C   GLY B  52     1343   1381   1258    -60     -2    136       C  
ATOM   1188  O   GLY B  52      18.942  37.539   9.473  1.00 11.27           O  
ANISOU 1188  O   GLY B  52     1383   1487   1410    148     92    232       O  
ATOM   1189  N   PHE B  53      18.185  39.321   8.346  1.00 12.20           N  
ANISOU 1189  N   PHE B  53     1423   1809   1403    229    104    451       N  
ATOM   1190  CA  PHE B  53      16.957  39.462   9.112  1.00 11.56           C  
ANISOU 1190  CA  PHE B  53     1218   1684   1488    120     26     -9       C  
ATOM   1191  C   PHE B  53      15.774  38.933   8.369  1.00 12.01           C  
ANISOU 1191  C   PHE B  53     1608   1863   1089    267      0    -72       C  
ATOM   1192  O   PHE B  53      15.726  38.936   7.123  1.00 14.24           O  
ANISOU 1192  O   PHE B  53     1686   2510   1214    407     55    -61       O  
ATOM   1193  CB  PHE B  53      16.725  40.951   9.501  1.00 12.89           C  
ANISOU 1193  CB  PHE B  53     1667   1721   1508    358    266    338       C  
ATOM   1194  CG  PHE B  53      17.579  41.421  10.634  1.00 12.18           C  
ANISOU 1194  CG  PHE B  53     1432   1268   1926    149     60    258       C  
ATOM   1195  CD1 PHE B  53      18.942  41.726  10.437  1.00 14.55           C  
ANISOU 1195  CD1 PHE B  53     1681   1390   2457    371     59    319       C  
ATOM   1196  CD2 PHE B  53      17.064  41.636  11.845  1.00 12.87           C  
ANISOU 1196  CD2 PHE B  53     1628   1350   1909   -134   -116    -82       C  
ATOM   1197  CE1 PHE B  53      19.705  42.160  11.508  1.00 14.95           C  
ANISOU 1197  CE1 PHE B  53     1518   1551   2609   -159    -33    159       C  
ATOM   1198  CE2 PHE B  53      17.868  42.077  12.876  1.00 14.30           C  
ANISOU 1198  CE2 PHE B  53     1956   1226   2248    -30   -272     36       C  
ATOM   1199  CZ  PHE B  53      19.203  42.267  12.664  1.00 16.23           C  
ANISOU 1199  CZ  PHE B  53     1918   2006   2241   -152   -580      3       C  
ATOM   1200  N   ILE B  54      14.734  38.522   9.114  1.00 11.86           N  
ANISOU 1200  N   ILE B  54     1240   1815   1451    152    -82    -94       N  
ATOM   1201  CA  ILE B  54      13.400  38.256   8.561  1.00 12.23           C  
ANISOU 1201  CA  ILE B  54     1475   1658   1513    288   -275   -370       C  
ATOM   1202  C   ILE B  54      12.393  39.047   9.341  1.00 10.99           C  
ANISOU 1202  C   ILE B  54     1390   1282   1502    100    -32   -221       C  
ATOM   1203  O   ILE B  54      12.606  39.407  10.497  1.00 11.96           O  
ANISOU 1203  O   ILE B  54     1371   1648   1525     14    -35   -327       O  
ATOM   1204  CB  ILE B  54      13.024  36.761   8.529  1.00 13.71           C  
ANISOU 1204  CB  ILE B  54     1714   1794   1698    334   -407   -513       C  
ATOM   1205  CG1 ILE B  54      12.995  36.149   9.924  1.00 14.03           C  
ANISOU 1205  CG1 ILE B  54     1871   1385   2074    389   -433   -398       C  
ATOM   1206  CG2 ILE B  54      13.908  36.034   7.589  1.00 15.57           C  
ANISOU 1206  CG2 ILE B  54     2228   2019   1666    649   -428   -456       C  
ATOM   1207  CD1 ILE B  54      12.236  34.848  10.004  1.00 15.87           C  
ANISOU 1207  CD1 ILE B  54     2111   1653   2264    315   -620   -256       C  
ATOM   1208  N   LYS B  55      11.280  39.342   8.666  1.00 11.17           N  
ANISOU 1208  N   LYS B  55     1381   1332   1529    144    -77    -94       N  
ATOM   1209  CA  LYS B  55      10.174  39.996   9.260  1.00 11.43           C  
ANISOU 1209  CA  LYS B  55     1470   1319   1553    139     -3    180       C  
ATOM   1210  C   LYS B  55       9.198  38.981   9.859  1.00 10.36           C  
ANISOU 1210  C   LYS B  55     1203   1289   1444     66   -189     30       C  
ATOM   1211  O   LYS B  55       8.862  38.018   9.201  1.00 12.33           O  
ANISOU 1211  O   LYS B  55     1534   1575   1575   -123   -129    -30       O  
ATOM   1212  CB  LYS B  55       9.432  40.791   8.181  1.00 13.42           C  
ANISOU 1212  CB  LYS B  55     1649   1536   1911    338    141    156       C  
ATOM   1213  CG  LYS B  55      10.264  41.756   7.342  1.00 20.94           C  
ANISOU 1213  CG  LYS B  55     2872   2013   3068      2    165    145       C  
ATOM   1214  CD  LYS B  55       9.439  42.429   6.150  1.00 24.72           C  
ANISOU 1214  CD  LYS B  55     4481   2386   2523     65     73    129       C  
ATOM   1215  CE  LYS B  55      10.298  43.532   5.433  1.00 27.31           C  
ANISOU 1215  CE  LYS B  55     4643   1903   3831   -365   -131      8       C  
ATOM   1216  NZ  LYS B  55      11.712  43.053   5.257  1.00 36.64           N  
ANISOU 1216  NZ  LYS B  55     4960   4001   4958     24    719   -235       N  
ATOM   1217  N   VAL B  56       8.757  39.233  11.072  1.00 11.07           N  
ANISOU 1217  N   VAL B  56     1357   1225   1623     -8   -139     81       N  
ATOM   1218  CA  VAL B  56       7.844  38.344  11.760  1.00 12.25           C  
ANISOU 1218  CA  VAL B  56     1484   1255   1914     72    111    388       C  
ATOM   1219  C   VAL B  56       6.728  39.131  12.437  1.00 13.12           C  
ANISOU 1219  C   VAL B  56     1525   1434   2026    -41     25    181       C  
ATOM   1220  O   VAL B  56       6.803  40.363  12.608  1.00 13.57           O  
ANISOU 1220  O   VAL B  56     1495   1633   2025    -26    195    146       O  
ATOM   1221  CB  VAL B  56       8.611  37.467  12.831  1.00 11.73           C  
ANISOU 1221  CB  VAL B  56     1420   1343   1693   -123    -60    249       C  
ATOM   1222  CG1 VAL B  56       9.655  36.610  12.170  1.00 13.60           C  
ANISOU 1222  CG1 VAL B  56     1340   1547   2277    145   -181    259       C  
ATOM   1223  CG2 VAL B  56       9.237  38.330  13.896  1.00 13.51           C  
ANISOU 1223  CG2 VAL B  56     1648   1524   1959     15   -166    398       C  
ATOM   1224  N   ARG B  57       5.696  38.403  12.787  1.00 12.50           N  
ANISOU 1224  N   ARG B  57     1481   1350   1918    180    117    302       N  
ATOM   1225  CA  ARG B  57       4.560  38.942  13.570  1.00 13.08           C  
ANISOU 1225  CA  ARG B  57     1257   1556   2156    194    146    351       C  
ATOM   1226  C   ARG B  57       4.664  38.433  14.984  1.00 12.16           C  
ANISOU 1226  C   ARG B  57     1170   1510   1940     90     82    289       C  
ATOM   1227  O   ARG B  57       4.804  37.195  15.199  1.00 13.63           O  
ANISOU 1227  O   ARG B  57     1602   1325   2251    322    142    376       O  
ATOM   1228  CB  ARG B  57       3.225  38.471  12.966  1.00 13.94           C  
ANISOU 1228  CB  ARG B  57     1563   1731   2000    280    -41    604       C  
ATOM   1229  CG  ARG B  57       3.043  38.872  11.615  1.00 16.79           C  
ANISOU 1229  CG  ARG B  57     1818   2370   2191    118   -153    119       C  
ATOM   1230  CD  ARG B  57       1.632  38.607  11.044  1.00 21.28           C  
ANISOU 1230  CD  ARG B  57     2074   2924   3087    345   -626    162       C  
ATOM   1231  NE  ARG B  57       1.161  37.191  11.178  1.00 22.37           N  
ANISOU 1231  NE  ARG B  57     2055   3053   3392     88   -465    191       N  
ATOM   1232  CZ  ARG B  57       1.465  36.189  10.335  1.00 21.77           C  
ANISOU 1232  CZ  ARG B  57     2646   2666   2959    -47   -366    668       C  
ATOM   1233  NH1 ARG B  57       2.387  36.360   9.365  1.00 27.38           N  
ANISOU 1233  NH1 ARG B  57     3324   2778   4298    223    578    346       N  
ATOM   1234  NH2 ARG B  57       0.865  35.026  10.476  1.00 26.50           N  
ANISOU 1234  NH2 ARG B  57     3222   2360   4485    158   -218   1227       N  
ATOM   1235  N   GLN B  58       4.697  39.355  15.955  1.00 13.39           N  
ANISOU 1235  N   GLN B  58     1610   1568   1906    403    199    250       N  
ATOM   1236  CA  GLN B  58       4.841  39.000  17.350  1.00 13.81           C  
ANISOU 1236  CA  GLN B  58     1578   1698   1968    561    430    173       C  
ATOM   1237  C   GLN B  58       3.486  38.871  18.028  1.00 13.68           C  
ANISOU 1237  C   GLN B  58     1603   1407   2188    389    396    361       C  
ATOM   1238  O   GLN B  58       2.746  39.890  18.138  1.00 15.93           O  
ANISOU 1238  O   GLN B  58     1938   1713   2400    746    525    522       O  
ATOM   1239  CB  GLN B  58       5.690  40.064  18.100  1.00 14.31           C  
ANISOU 1239  CB  GLN B  58     1849   1770   1816    572    208    252       C  
ATOM   1240  CG  GLN B  58       5.791  39.794  19.548  1.00 17.30           C  
ANISOU 1240  CG  GLN B  58     2249   2067   2256    663    407    274       C  
ATOM   1241  CD  GLN B  58       6.558  40.800  20.306  1.00 21.37           C  
ANISOU 1241  CD  GLN B  58     2895   2342   2883    153    338    180       C  
ATOM   1242  OE1 GLN B  58       7.463  41.445  19.772  1.00 23.86           O  
ANISOU 1242  OE1 GLN B  58     2941   2812   3312   -235    691   -200       O  
ATOM   1243  NE2 GLN B  58       6.225  40.944  21.634  1.00 29.58           N  
ANISOU 1243  NE2 GLN B  58     3956   3913   3370   -139    937   -274       N  
ATOM   1244  N   TYR B  59       3.128  37.677  18.463  1.00 14.84           N  
ANISOU 1244  N   TYR B  59     1577   1530   2530    458    527    581       N  
ATOM   1245  CA  TYR B  59       1.911  37.412  19.242  1.00 15.48           C  
ANISOU 1245  CA  TYR B  59     1634   2017   2231    622    517    535       C  
ATOM   1246  C   TYR B  59       2.275  37.193  20.712  1.00 18.41           C  
ANISOU 1246  C   TYR B  59     2246   2253   2494    693    431    586       C  
ATOM   1247  O   TYR B  59       3.236  36.515  21.014  1.00 22.25           O  
ANISOU 1247  O   TYR B  59     2291   3329   2833   1272    640   1244       O  
ATOM   1248  CB  TYR B  59       1.206  36.183  18.708  1.00 17.04           C  
ANISOU 1248  CB  TYR B  59     1826   1958   2690    611    714    578       C  
ATOM   1249  CG  TYR B  59       0.683  36.268  17.298  1.00 16.53           C  
ANISOU 1249  CG  TYR B  59     1367   1944   2967     14    460    564       C  
ATOM   1250  CD1 TYR B  59       1.502  36.057  16.219  1.00 18.28           C  
ANISOU 1250  CD1 TYR B  59     2119   2254   2572    188    442    826       C  
ATOM   1251  CD2 TYR B  59      -0.659  36.587  17.040  1.00 19.02           C  
ANISOU 1251  CD2 TYR B  59     1425   2428   3373    284    351    571       C  
ATOM   1252  CE1 TYR B  59       1.067  36.099  15.006  1.00 18.51           C  
ANISOU 1252  CE1 TYR B  59     1601   2575   2855   -235    325    546       C  
ATOM   1253  CE2 TYR B  59      -1.119  36.650  15.765  1.00 22.07           C  
ANISOU 1253  CE2 TYR B  59     1903   2540   3943    160   -422    359       C  
ATOM   1254  CZ  TYR B  59      -0.258  36.397  14.736  1.00 24.91           C  
ANISOU 1254  CZ  TYR B  59     2468   3065   3929     86    -73    493       C  
ATOM   1255  OH  TYR B  59      -0.661  36.458  13.375  1.00 29.61           O  
ANISOU 1255  OH  TYR B  59     2798   3849   4603   -472   -325    942       O  
ATOM   1256  N   ASP B  60       1.455  37.666  21.594  1.00 17.87           N  
ANISOU 1256  N   ASP B  60     2111   2011   2666    429    364    436       N  
ATOM   1257  CA  ASP B  60       1.731  37.530  22.961  1.00 19.83           C  
ANISOU 1257  CA  ASP B  60     2552   2332   2648    238    529    337       C  
ATOM   1258  C   ASP B  60       0.758  36.627  23.689  1.00 17.14           C  
ANISOU 1258  C   ASP B  60     2093   2121   2298    404    340    348       C  
ATOM   1259  O   ASP B  60      -0.392  36.374  23.190  1.00 18.65           O  
ANISOU 1259  O   ASP B  60     1929   2181   2974    458    378    443       O  
ATOM   1260  CB  ASP B  60       1.781  38.819  23.570  1.00 23.44           C  
ANISOU 1260  CB  ASP B  60     3853   2666   2384   -180    326    385       C  
ATOM   1261  CG  ASP B  60       2.976  39.730  22.992  1.00 26.11           C  
ANISOU 1261  CG  ASP B  60     3314   2965   3639    -41    566    141       C  
ATOM   1262  OD1 ASP B  60       4.110  39.185  22.656  1.00 27.61           O  
ANISOU 1262  OD1 ASP B  60     3634   3028   3829    -14    830    278       O  
ATOM   1263  OD2 ASP B  60       2.854  40.919  22.869  1.00 31.72           O  
ANISOU 1263  OD2 ASP B  60     4927   2884   4240    431   -270    183       O  
ATOM   1264  N   GLN B  61       1.269  35.955  24.712  1.00 17.98           N  
ANISOU 1264  N   GLN B  61     2279   2035   2516    332    518    416       N  
ATOM   1265  CA  GLN B  61       0.439  35.145  25.614  1.00 19.30           C  
ANISOU 1265  CA  GLN B  61     2504   2451   2375    430    784    418       C  
ATOM   1266  C   GLN B  61      -0.295  34.047  24.808  1.00 18.65           C  
ANISOU 1266  C   GLN B  61     2168   2230   2686    480    514    687       C  
ATOM   1267  O   GLN B  61      -1.468  33.750  25.031  1.00 20.35           O  
ANISOU 1267  O   GLN B  61     2144   2487   3099    475   1012    175       O  
ATOM   1268  CB  GLN B  61      -0.484  36.051  26.455  1.00 22.41           C  
ANISOU 1268  CB  GLN B  61     2911   2708   2895    443    745    366       C  
ATOM   1269  CG  GLN B  61       0.288  36.873  27.501  1.00 27.29           C  
ANISOU 1269  CG  GLN B  61     3209   3333   3826    353    689   -387       C  
ATOM   1270  CD  GLN B  61       0.981  35.947  28.615  1.00 34.82           C  
ANISOU 1270  CD  GLN B  61     4434   4535   4260    216    -93   -139       C  
ATOM   1271  OE1 GLN B  61       2.207  35.795  28.623  1.00 37.57           O  
ANISOU 1271  OE1 GLN B  61     4738   4963   4572    860    -82   -331       O  
ATOM   1272  NE2 GLN B  61       0.125  35.273  29.500  1.00 33.81           N  
ANISOU 1272  NE2 GLN B  61     5047   3624   4172    626     77   -150       N  
ATOM   1273  N   ILE B  62       0.471  33.333  23.970  1.00 15.71           N  
ANISOU 1273  N   ILE B  62     1823   1762   2385    364    372    441       N  
ATOM   1274  CA  ILE B  62      -0.064  32.232  23.229  1.00 14.75           C  
ANISOU 1274  CA  ILE B  62     1560   1903   2141    311    270    539       C  
ATOM   1275  C   ILE B  62       0.257  30.949  23.995  1.00 15.32           C  
ANISOU 1275  C   ILE B  62     1712   1786   2320    433    321    464       C  
ATOM   1276  O   ILE B  62       1.419  30.668  24.255  1.00 14.88           O  
ANISOU 1276  O   ILE B  62     1480   1916   2256    368    463    583       O  
ATOM   1277  CB  ILE B  62       0.561  32.163  21.805  1.00 15.35           C  
ANISOU 1277  CB  ILE B  62     1762   2013   2057    174    193    327       C  
ATOM   1278  CG1 ILE B  62       0.320  33.510  21.039  1.00 16.21           C  
ANISOU 1278  CG1 ILE B  62     2062   1954   2143    539    231    664       C  
ATOM   1279  CG2 ILE B  62       0.053  30.959  21.050  1.00 17.95           C  
ANISOU 1279  CG2 ILE B  62     2297   2108   2412    139      1    530       C  
ATOM   1280  CD1 ILE B  62      -1.134  33.857  20.839  1.00 21.41           C  
ANISOU 1280  CD1 ILE B  62     2100   2864   3170    774    284   1054       C  
ATOM   1281  N   PRO B  63      -0.757  30.078  24.249  1.00 15.79           N  
ANISOU 1281  N   PRO B  63     1725   2002   2271    221    245    539       N  
ATOM   1282  CA  PRO B  63      -0.478  28.785  24.834  1.00 15.81           C  
ANISOU 1282  CA  PRO B  63     1830   2048   2128    266    179    641       C  
ATOM   1283  C   PRO B  63       0.180  27.854  23.840  1.00 17.90           C  
ANISOU 1283  C   PRO B  63     2122   2034   2642    285    -77    423       C  
ATOM   1284  O   PRO B  63      -0.332  27.656  22.761  1.00 20.19           O  
ANISOU 1284  O   PRO B  63     3083   2191   2395    684    320    500       O  
ATOM   1285  CB  PRO B  63      -1.858  28.294  25.296  1.00 16.62           C  
ANISOU 1285  CB  PRO B  63     1997   2226   2090   -158     68    739       C  
ATOM   1286  CG  PRO B  63      -2.847  29.158  24.687  1.00 21.46           C  
ANISOU 1286  CG  PRO B  63     1928   2420   3804    172    508    836       C  
ATOM   1287  CD  PRO B  63      -2.213  30.354  24.122  1.00 16.28           C  
ANISOU 1287  CD  PRO B  63     1569   2093   2522     91    517    494       C  
ATOM   1288  N   VAL B  64       1.273  27.233  24.291  1.00 18.73           N  
ANISOU 1288  N   VAL B  64     2311   2251   2553    567    463    819       N  
ATOM   1289  CA  VAL B  64       2.082  26.260  23.472  1.00 20.00           C  
ANISOU 1289  CA  VAL B  64     2943   1840   2815    427    482    684       C  
ATOM   1290  C   VAL B  64       2.442  25.064  24.412  1.00 20.52           C  
ANISOU 1290  C   VAL B  64     2495   2361   2939    530    679    760       C  
ATOM   1291  O   VAL B  64       2.982  25.272  25.472  1.00 25.35           O  
ANISOU 1291  O   VAL B  64     3748   2796   3088   1033    719    964       O  
ATOM   1292  CB  VAL B  64       3.390  26.862  22.972  1.00 21.59           C  
ANISOU 1292  CB  VAL B  64     2717   2374   3109    539    738    670       C  
ATOM   1293  CG1 VAL B  64       4.155  25.811  22.022  1.00 21.11           C  
ANISOU 1293  CG1 VAL B  64     2568   2346   3105    111   1020    754       C  
ATOM   1294  CG2 VAL B  64       3.151  28.103  22.222  1.00 21.40           C  
ANISOU 1294  CG2 VAL B  64     2577   2584   2967    513    709    840       C  
ATOM   1295  N  AGLU B  65       2.089  23.875  24.045  0.50 19.18           N  
ANISOU 1295  N  AGLU B  65     2318   2293   2674    501    908    738       N  
ATOM   1296  N  BGLU B  65       2.003  23.810  23.945  0.50 18.67           N  
ANISOU 1296  N  BGLU B  65     2082   2207   2802    550    789    827       N  
ATOM   1297  CA AGLU B  65       2.536  22.729  24.809  0.50 19.38           C  
ANISOU 1297  CA AGLU B  65     2293   2306   2762    555    804    562       C  
ATOM   1298  CA BGLU B  65       2.279  22.520  24.628  0.50 18.85           C  
ANISOU 1298  CA BGLU B  65     2211   1999   2952    436    704    597       C  
ATOM   1299  C  AGLU B  65       3.643  22.060  24.072  0.50 18.94           C  
ANISOU 1299  C  AGLU B  65     2256   2195   2743    599    762    563       C  
ATOM   1300  C  BGLU B  65       3.483  21.853  23.982  0.50 19.15           C  
ANISOU 1300  C  BGLU B  65     2297   2015   2961    350    812    699       C  
ATOM   1301  O  AGLU B  65       3.696  22.094  22.897  0.50 19.26           O  
ANISOU 1301  O  AGLU B  65     2481   2054   2780    790    628    389       O  
ATOM   1302  O  BGLU B  65       3.447  21.543  22.794  0.50 18.55           O  
ANISOU 1302  O  BGLU B  65     1734   1800   3512    323    470    404       O  
ATOM   1303  CB AGLU B  65       1.381  21.757  25.077  0.50 19.40           C  
ANISOU 1303  CB AGLU B  65     2505   2023   2840    439    384    315       C  
ATOM   1304  CB BGLU B  65       1.002  21.559  24.537  0.50 19.51           C  
ANISOU 1304  CB BGLU B  65     2333   1933   3148    510    599    455       C  
ATOM   1305  CG AGLU B  65       1.582  20.823  26.243  0.50 20.44           C  
ANISOU 1305  CG AGLU B  65     2780   2563   2423    301    454    197       C  
ATOM   1306  CG BGLU B  65      -0.283  22.188  25.096  0.50 18.26           C  
ANISOU 1306  CG BGLU B  65     2302   2496   2137    302    567    457       C  
ATOM   1307  CD AGLU B  65       0.334  19.866  26.468  0.50 25.76           C  
ANISOU 1307  CD AGLU B  65     3298   3459   3027   -293    319    378       C  
ATOM   1308  CD BGLU B  65      -0.863  23.316  24.172  0.50 16.66           C  
ANISOU 1308  CD BGLU B  65     1755   2168   2405    454   -188   -181       C  
ATOM   1309  OE1AGLU B  65       0.139  18.890  25.646  0.50 32.72           O  
ANISOU 1309  OE1AGLU B  65     4465   4043   3923     98    244   -243       O  
ATOM   1310  OE1BGLU B  65      -1.206  23.027  22.991  0.50 16.36           O  
ANISOU 1310  OE1BGLU B  65     1691   2146   2379   -281    130    -71       O  
ATOM   1311  OE2AGLU B  65      -0.479  20.165  27.338  0.50 30.56           O  
ANISOU 1311  OE2AGLU B  65     3579   4162   3868    -26    555   -457       O  
ATOM   1312  OE2BGLU B  65      -0.977  24.486  24.629  0.50 17.64           O  
ANISOU 1312  OE2BGLU B  65     2313   2101   2288    778   -440   -412       O  
ATOM   1313  N   ILE B  66       4.571  21.627  24.800  1.00 18.41           N  
ANISOU 1313  N   ILE B  66     2349   2099   2545    718    961    600       N  
ATOM   1314  CA  ILE B  66       5.835  21.110  24.258  1.00 18.93           C  
ANISOU 1314  CA  ILE B  66     2336   2447   2406    640    877    476       C  
ATOM   1315  C   ILE B  66       6.100  19.787  24.970  1.00 19.74           C  
ANISOU 1315  C   ILE B  66     2426   2352   2722    759    402    493       C  
ATOM   1316  O   ILE B  66       6.411  19.753  26.180  1.00 20.51           O  
ANISOU 1316  O   ILE B  66     2563   2503   2728    961    895    624       O  
ATOM   1317  CB  ILE B  66       6.950  22.062  24.510  1.00 17.44           C  
ANISOU 1317  CB  ILE B  66     2295   2209   2122    726    723    460       C  
ATOM   1318  CG1 ILE B  66       6.659  23.423  23.842  1.00 19.85           C  
ANISOU 1318  CG1 ILE B  66     2427   2436   2678    638   1017    353       C  
ATOM   1319  CG2 ILE B  66       8.303  21.483  24.002  1.00 19.65           C  
ANISOU 1319  CG2 ILE B  66     2461   2752   2253    710   1104    506       C  
ATOM   1320  CD1 ILE B  66       7.307  24.492  24.460  1.00 23.26           C  
ANISOU 1320  CD1 ILE B  66     2881   2827   3127    380    247    774       C  
ATOM   1321  N   CYS B  67       6.008  18.742  24.250  1.00 21.88           N  
ANISOU 1321  N   CYS B  67     2637   2627   3049    806    517    385       N  
ATOM   1322  CA  CYS B  67       6.182  17.375  24.873  1.00 24.28           C  
ANISOU 1322  CA  CYS B  67     3267   2554   3403    799    405    313       C  
ATOM   1323  C   CYS B  67       5.366  17.172  26.108  1.00 25.79           C  
ANISOU 1323  C   CYS B  67     3571   3104   3125    759    249    521       C  
ATOM   1324  O   CYS B  67       5.855  16.673  27.101  1.00 27.22           O  
ANISOU 1324  O   CYS B  67     4135   2659   3546   1135    414    884       O  
ATOM   1325  CB  CYS B  67       7.633  17.111  25.199  1.00 24.09           C  
ANISOU 1325  CB  CYS B  67     3423   2549   3180   1320    563    306       C  
ATOM   1326  SG  CYS B  67       8.604  17.099  23.894  1.00 31.16           S  
ANISOU 1326  SG  CYS B  67     4058   3508   4272   1244   1242   1027       S  
ATOM   1327  N   GLY B  68       4.180  17.713  26.107  1.00 25.90           N  
ANISOU 1327  N   GLY B  68     3414   2873   3554    499    689    530       N  
ATOM   1328  CA  GLY B  68       3.290  17.572  27.238  1.00 27.05           C  
ANISOU 1328  CA  GLY B  68     3637   3121   3517   -175    659    604       C  
ATOM   1329  C   GLY B  68       3.498  18.534  28.363  1.00 26.45           C  
ANISOU 1329  C   GLY B  68     3095   3319   3635    157    831    495       C  
ATOM   1330  O   GLY B  68       2.704  18.531  29.315  1.00 33.24           O  
ANISOU 1330  O   GLY B  68     4132   4253   4242   -508   1551    923       O  
ATOM   1331  N   HIS B  69       4.375  19.493  28.190  1.00 21.02           N  
ANISOU 1331  N   HIS B  69     3154   2228   2605    604    738   1037       N  
ATOM   1332  CA  HIS B  69       4.559  20.500  29.180  1.00 21.59           C  
ANISOU 1332  CA  HIS B  69     3153   2228   2823    631    653    734       C  
ATOM   1333  C   HIS B  69       3.892  21.775  28.685  1.00 19.88           C  
ANISOU 1333  C   HIS B  69     3163   2137   2252    782   1145    819       C  
ATOM   1334  O   HIS B  69       4.115  22.197  27.529  1.00 22.83           O  
ANISOU 1334  O   HIS B  69     3681   2466   2524   1339   1604   1093       O  
ATOM   1335  CB  HIS B  69       6.070  20.777  29.452  1.00 21.94           C  
ANISOU 1335  CB  HIS B  69     3408   2112   2814    404    597    647       C  
ATOM   1336  CG  HIS B  69       6.802  19.631  30.091  1.00 22.26           C  
ANISOU 1336  CG  HIS B  69     2968   2657   2829    460    620    569       C  
ATOM   1337  ND1 HIS B  69       7.445  19.750  31.308  1.00 22.01           N  
ANISOU 1337  ND1 HIS B  69     3247   2421   2694    658    779    576       N  
ATOM   1338  CD2 HIS B  69       7.171  18.455  29.592  1.00 23.64           C  
ANISOU 1338  CD2 HIS B  69     3111   2729   3143    295    723    602       C  
ATOM   1339  CE1 HIS B  69       7.989  18.572  31.621  1.00 26.97           C  
ANISOU 1339  CE1 HIS B  69     4315   2599   3331    493     43    306       C  
ATOM   1340  NE2 HIS B  69       7.787  17.756  30.613  1.00 22.01           N  
ANISOU 1340  NE2 HIS B  69     2731   2421   3208    280    225    424       N  
ATOM   1341  N   LYS B  70       3.107  22.421  29.529  1.00 17.34           N  
ANISOU 1341  N   LYS B  70     2458   1999   2131    568    997    675       N  
ATOM   1342  CA  LYS B  70       2.416  23.604  29.142  1.00 17.00           C  
ANISOU 1342  CA  LYS B  70     2124   2080   2253    448    730    424       C  
ATOM   1343  C   LYS B  70       3.288  24.807  29.246  1.00 17.01           C  
ANISOU 1343  C   LYS B  70     2076   2343   2044    493    728    492       C  
ATOM   1344  O   LYS B  70       4.014  24.943  30.108  1.00 17.75           O  
ANISOU 1344  O   LYS B  70     2310   2265   2168    410    612    686       O  
ATOM   1345  CB  LYS B  70       1.237  23.779  30.027  1.00 16.10           C  
ANISOU 1345  CB  LYS B  70     2020   2156   1940    420    592    421       C  
ATOM   1346  CG  LYS B  70       0.160  22.712  29.840  1.00 16.98           C  
ANISOU 1346  CG  LYS B  70     2521   1859   2071    296    496    207       C  
ATOM   1347  CD  LYS B  70      -1.005  22.918  30.816  1.00 17.86           C  
ANISOU 1347  CD  LYS B  70     1976   2408   2399    152    715    215       C  
ATOM   1348  CE  LYS B  70      -2.078  21.899  30.621  1.00 20.28           C  
ANISOU 1348  CE  LYS B  70     2317   2725   2663    160    246     -2       C  
ATOM   1349  NZ  LYS B  70      -1.640  20.530  30.988  1.00 26.13           N  
ANISOU 1349  NZ  LYS B  70     2916   2746   4263     -6    389    409       N  
ATOM   1350  N   ALA B  71       3.130  25.731  28.289  1.00 18.17           N  
ANISOU 1350  N   ALA B  71     2192   2133   2578    408    525    841       N  
ATOM   1351  CA  ALA B  71       3.816  26.993  28.324  1.00 17.47           C  
ANISOU 1351  CA  ALA B  71     1820   2147   2670    477    427    558       C  
ATOM   1352  C   ALA B  71       2.837  28.074  27.783  1.00 14.22           C  
ANISOU 1352  C   ALA B  71     1688   1606   2107    386    489    300       C  
ATOM   1353  O   ALA B  71       1.858  27.725  27.133  1.00 16.13           O  
ANISOU 1353  O   ALA B  71     1899   1981   2246    281    564    616       O  
ATOM   1354  CB  ALA B  71       5.095  26.925  27.444  1.00 19.26           C  
ANISOU 1354  CB  ALA B  71     1924   2348   3045    636    645    850       C  
ATOM   1355  N   ILE B  72       3.179  29.298  27.996  1.00 15.20           N  
ANISOU 1355  N   ILE B  72     1637   1837   2301    337    457    543       N  
ATOM   1356  CA  ILE B  72       2.384  30.403  27.471  1.00 14.64           C  
ANISOU 1356  CA  ILE B  72     1661   1733   2167    410    516    341       C  
ATOM   1357  C   ILE B  72       3.219  31.617  27.364  1.00 13.60           C  
ANISOU 1357  C   ILE B  72     1697   1787   1684    313    354    385       C  
ATOM   1358  O   ILE B  72       3.908  32.002  28.282  1.00 15.90           O  
ANISOU 1358  O   ILE B  72     1809   2162   2069    440    256    417       O  
ATOM   1359  CB  ILE B  72       1.077  30.651  28.311  1.00 15.67           C  
ANISOU 1359  CB  ILE B  72     1727   2039   2187    392    454    459       C  
ATOM   1360  CG1 ILE B  72       0.319  31.794  27.716  1.00 16.78           C  
ANISOU 1360  CG1 ILE B  72     1666   2208   2499    474    614    326       C  
ATOM   1361  CG2 ILE B  72       1.381  30.863  29.746  1.00 18.77           C  
ANISOU 1361  CG2 ILE B  72     2168   2509   2454    372    325    431       C  
ATOM   1362  CD1 ILE B  72      -1.007  32.000  28.331  1.00 18.13           C  
ANISOU 1362  CD1 ILE B  72     1978   2266   2644    426    567    361       C  
ATOM   1363  N   GLY B  73       3.288  32.165  26.187  1.00 14.86           N  
ANISOU 1363  N   GLY B  73     1769   2042   1834    418    410    543       N  
ATOM   1364  CA  GLY B  73       4.132  33.324  25.987  1.00 15.71           C  
ANISOU 1364  CA  GLY B  73     1714   1946   2308    540    443    265       C  
ATOM   1365  C   GLY B  73       4.194  33.816  24.562  1.00 13.54           C  
ANISOU 1365  C   GLY B  73     1448   1914   1780    333    367    135       C  
ATOM   1366  O   GLY B  73       3.365  33.521  23.769  1.00 15.33           O  
ANISOU 1366  O   GLY B  73     1806   1987   2030    205    334    646       O  
ATOM   1367  N   THR B  74       5.247  34.518  24.277  1.00 15.55           N  
ANISOU 1367  N   THR B  74     1826   1878   2203    604    243    372       N  
ATOM   1368  CA  THR B  74       5.407  35.125  22.969  1.00 15.05           C  
ANISOU 1368  CA  THR B  74     1914   1773   2030    335    324    387       C  
ATOM   1369  C   THR B  74       5.758  34.136  21.922  1.00 13.14           C  
ANISOU 1369  C   THR B  74     1626   1565   1801    141    366    282       C  
ATOM   1370  O   THR B  74       6.640  33.290  22.110  1.00 14.41           O  
ANISOU 1370  O   THR B  74     1620   1909   1944    425    338    351       O  
ATOM   1371  CB  THR B  74       6.474  36.220  23.037  1.00 17.25           C  
ANISOU 1371  CB  THR B  74     2493   1966   2093    -37    337    241       C  
ATOM   1372  OG1 THR B  74       6.019  37.276  23.883  1.00 21.90           O  
ANISOU 1372  OG1 THR B  74     3665   2022   2632     54    471     97       O  
ATOM   1373  CG2 THR B  74       6.756  36.909  21.628  1.00 20.88           C  
ANISOU 1373  CG2 THR B  74     3095   2198   2637    -15    574    773       C  
ATOM   1374  N   VAL B  75       5.102  34.253  20.773  1.00 13.79           N  
ANISOU 1374  N   VAL B  75     1583   1751   1903    296    338    503       N  
ATOM   1375  CA  VAL B  75       5.382  33.457  19.636  1.00 13.36           C  
ANISOU 1375  CA  VAL B  75     1530   1596   1950    315      6    532       C  
ATOM   1376  C   VAL B  75       5.531  34.384  18.431  1.00 13.07           C  
ANISOU 1376  C   VAL B  75     1421   1562   1981    485     92    218       C  
ATOM   1377  O   VAL B  75       4.672  35.251  18.206  1.00 15.35           O  
ANISOU 1377  O   VAL B  75     1642   1777   2412    602    356    761       O  
ATOM   1378  CB  VAL B  75       4.250  32.408  19.366  1.00 17.14           C  
ANISOU 1378  CB  VAL B  75     2094   1751   2665    241     11    607       C  
ATOM   1379  CG1 VAL B  75       4.410  31.732  18.096  1.00 19.65           C  
ANISOU 1379  CG1 VAL B  75     2526   2072   2868     13    237    690       C  
ATOM   1380  CG2 VAL B  75       4.189  31.381  20.486  1.00 16.16           C  
ANISOU 1380  CG2 VAL B  75     2293   1626   2220    -48     69    423       C  
ATOM   1381  N   LEU B  76       6.645  34.278  17.764  1.00 11.62           N  
ANISOU 1381  N   LEU B  76     1221   1326   1865    374    -28    407       N  
ATOM   1382  CA  LEU B  76       6.872  35.022  16.525  1.00 11.76           C  
ANISOU 1382  CA  LEU B  76     1270   1314   1884    314    -55    269       C  
ATOM   1383  C   LEU B  76       6.490  34.153  15.367  1.00 13.28           C  
ANISOU 1383  C   LEU B  76     1745   1533   1765    304    -80    114       C  
ATOM   1384  O   LEU B  76       6.704  32.905  15.449  1.00 16.04           O  
ANISOU 1384  O   LEU B  76     2092   1521   2480    507   -540    -27       O  
ATOM   1385  CB  LEU B  76       8.343  35.439  16.439  1.00 11.19           C  
ANISOU 1385  CB  LEU B  76     1421   1239   1592    161    125    253       C  
ATOM   1386  CG  LEU B  76       8.894  36.181  17.689  1.00 11.60           C  
ANISOU 1386  CG  LEU B  76     1300   1588   1520    212    164    175       C  
ATOM   1387  CD1 LEU B  76      10.385  36.463  17.491  1.00 11.91           C  
ANISOU 1387  CD1 LEU B  76     1443   1532   1549     92     38    233       C  
ATOM   1388  CD2 LEU B  76       8.142  37.409  17.977  1.00 12.22           C  
ANISOU 1388  CD2 LEU B  76     1317   1879   1445    367      7     30       C  
ATOM   1389  N   VAL B  77       5.874  34.716  14.342  1.00 11.99           N  
ANISOU 1389  N   VAL B  77     1453   1319   1782    -13   -266    252       N  
ATOM   1390  CA  VAL B  77       5.465  33.952  13.192  1.00 11.32           C  
ANISOU 1390  CA  VAL B  77     1211   1438   1652    108   -110    165       C  
ATOM   1391  C   VAL B  77       5.982  34.613  11.937  1.00 12.45           C  
ANISOU 1391  C   VAL B  77     1400   1588   1738   -123   -165    194       C  
ATOM   1392  O   VAL B  77       5.785  35.814  11.728  1.00 12.71           O  
ANISOU 1392  O   VAL B  77     1517   1318   1992     75   -179    286       O  
ATOM   1393  CB  VAL B  77       3.874  33.835  13.112  1.00 13.96           C  
ANISOU 1393  CB  VAL B  77     1418   1631   2255    137   -185    329       C  
ATOM   1394  CG1 VAL B  77       3.486  33.081  11.873  1.00 14.29           C  
ANISOU 1394  CG1 VAL B  77     1432   2036   1961   -152   -194    376       C  
ATOM   1395  CG2 VAL B  77       3.351  33.147  14.348  1.00 13.90           C  
ANISOU 1395  CG2 VAL B  77     1462   1873   1946   -172   -167    118       C  
ATOM   1396  N   GLY B  78       6.629  33.837  11.086  1.00 11.83           N  
ANISOU 1396  N   GLY B  78     1449   1297   1748    -17     49    327       N  
ATOM   1397  CA  GLY B  78       7.126  34.368   9.834  1.00 12.40           C  
ANISOU 1397  CA  GLY B  78     1401   1653   1655      7   -121    232       C  
ATOM   1398  C   GLY B  78       7.859  33.346   9.076  1.00 12.37           C  
ANISOU 1398  C   GLY B  78     1458   1676   1566     32   -181    218       C  
ATOM   1399  O   GLY B  78       7.770  32.138   9.404  1.00 13.09           O  
ANISOU 1399  O   GLY B  78     1452   1649   1873     90    -85    247       O  
ATOM   1400  N   PRO B  79       8.585  33.749   8.054  1.00 12.67           N  
ANISOU 1400  N   PRO B  79     1657   1753   1404    196   -215    346       N  
ATOM   1401  CA  PRO B  79       9.089  32.809   7.052  1.00 12.58           C  
ANISOU 1401  CA  PRO B  79     1713   1617   1449    187   -251    150       C  
ATOM   1402  C   PRO B  79      10.408  32.208   7.529  1.00 12.83           C  
ANISOU 1402  C   PRO B  79     1846   1598   1431    266     40     18       C  
ATOM   1403  O   PRO B  79      11.400  32.231   6.795  1.00 14.93           O  
ANISOU 1403  O   PRO B  79     1903   2275   1494    433     54    374       O  
ATOM   1404  CB  PRO B  79       9.232  33.690   5.770  1.00 14.43           C  
ANISOU 1404  CB  PRO B  79     1775   2111   1596     72   -134    370       C  
ATOM   1405  CG  PRO B  79       9.540  35.090   6.346  1.00 13.68           C  
ANISOU 1405  CG  PRO B  79     1963   1698   1537     61   -110    230       C  
ATOM   1406  CD  PRO B  79       8.711  35.187   7.588  1.00 14.05           C  
ANISOU 1406  CD  PRO B  79     1775   1752   1810     46    -20    359       C  
ATOM   1407  N   THR B  80      10.398  31.573   8.699  1.00 13.07           N  
ANISOU 1407  N   THR B  80     1513   1830   1620    208    -13    442       N  
ATOM   1408  CA  THR B  80      11.514  30.801   9.145  1.00 12.42           C  
ANISOU 1408  CA  THR B  80     1455   1854   1410    109    -41    246       C  
ATOM   1409  C   THR B  80      11.468  29.475   8.428  1.00 13.63           C  
ANISOU 1409  C   THR B  80     1641   1838   1697    335   -159    429       C  
ATOM   1410  O   THR B  80      10.434  28.892   8.229  1.00 15.02           O  
ANISOU 1410  O   THR B  80     2119   1959   1629    182   -394    163       O  
ATOM   1411  CB  THR B  80      11.483  30.622  10.657  1.00 12.39           C  
ANISOU 1411  CB  THR B  80     1578   1791   1336     66    102    292       C  
ATOM   1412  OG1 THR B  80      12.580  29.738  11.040  1.00 13.35           O  
ANISOU 1412  OG1 THR B  80     1504   2002   1567    295   -131    371       O  
ATOM   1413  CG2 THR B  80      10.198  30.032  11.164  1.00 12.94           C  
ANISOU 1413  CG2 THR B  80     1535   1529   1850    123    -60    221       C  
ATOM   1414  N   PRO B  81      12.647  28.897   8.141  1.00 15.73           N  
ANISOU 1414  N   PRO B  81     2170   2475   1332    361   -296     49       N  
ATOM   1415  CA  PRO B  81      12.663  27.593   7.545  1.00 16.83           C  
ANISOU 1415  CA  PRO B  81     2549   2327   1516    624   -283     13       C  
ATOM   1416  C   PRO B  81      12.360  26.420   8.501  1.00 17.68           C  
ANISOU 1416  C   PRO B  81     2688   2395   1633    574   -513     41       C  
ATOM   1417  O   PRO B  81      12.108  25.302   8.037  1.00 19.76           O  
ANISOU 1417  O   PRO B  81     3076   2776   1654    547   -722   -132       O  
ATOM   1418  CB  PRO B  81      14.067  27.457   7.000  1.00 17.95           C  
ANISOU 1418  CB  PRO B  81     2578   2437   1803    342   -135    227       C  
ATOM   1419  CG  PRO B  81      14.882  28.338   7.692  1.00 20.48           C  
ANISOU 1419  CG  PRO B  81     2240   3284   2255    678   -334   -196       C  
ATOM   1420  CD  PRO B  81      13.949  29.488   8.173  1.00 16.07           C  
ANISOU 1420  CD  PRO B  81     1758   2754   1594    652    318    359       C  
ATOM   1421  N  AVAL B  82      12.402  26.670   9.785  0.50 15.90           N  
ANISOU 1421  N  AVAL B  82     2543   2141   1358    410   -664    -18       N  
ATOM   1422  N  BVAL B  82      12.388  26.681   9.783  0.50 15.81           N  
ANISOU 1422  N  BVAL B  82     2549   2110   1347    411   -699     26       N  
ATOM   1423  CA AVAL B  82      12.115  25.636  10.800  0.50 15.75           C  
ANISOU 1423  CA AVAL B  82     2267   2012   1703    438   -396     23       C  
ATOM   1424  CA BVAL B  82      12.203  25.650  10.810  0.50 15.48           C  
ANISOU 1424  CA BVAL B  82     2321   1891   1669    405   -477     49       C  
ATOM   1425  C  AVAL B  82      11.376  26.263  11.944  0.50 12.80           C  
ANISOU 1425  C  AVAL B  82     1815   1684   1362    134   -509    -65       C  
ATOM   1426  C  BVAL B  82      11.410  26.271  11.959  0.50 13.04           C  
ANISOU 1426  C  BVAL B  82     1891   1629   1433    172   -510    -14       C  
ATOM   1427  O  AVAL B  82      11.625  27.433  12.292  0.50 14.53           O  
ANISOU 1427  O  AVAL B  82     2410   1425   1686     42   -199     45       O  
ATOM   1428  O  BVAL B  82      11.630  27.439  12.303  0.50 14.55           O  
ANISOU 1428  O  BVAL B  82     2405   1419   1702     38   -214     46       O  
ATOM   1429  CB AVAL B  82      13.410  24.982  11.312  0.50 15.71           C  
ANISOU 1429  CB AVAL B  82     2388   1913   1666    446   -469     84       C  
ATOM   1430  CB BVAL B  82      13.597  25.119  11.328  0.50 15.79           C  
ANISOU 1430  CB BVAL B  82     2503   1671   1823    381   -536    297       C  
ATOM   1431  CG1AVAL B  82      14.046  24.150  10.247  0.50 19.47           C  
ANISOU 1431  CG1AVAL B  82     2506   2406   2485    392   -121    109       C  
ATOM   1432  CG1BVAL B  82      13.409  24.045  12.348  0.50 15.59           C  
ANISOU 1432  CG1BVAL B  82     2562   1878   1483    608   -122    295       C  
ATOM   1433  CG2AVAL B  82      14.360  26.018  11.802  0.50 15.45           C  
ANISOU 1433  CG2AVAL B  82     1689   2596   1584    -75   -166    685       C  
ATOM   1434  CG2BVAL B  82      14.444  24.615  10.180  0.50 17.10           C  
ANISOU 1434  CG2BVAL B  82     2035   1723   2737    -93   -408    231       C  
ATOM   1435  N   ASN B  83      10.552  25.493  12.623  1.00 13.45           N  
ANISOU 1435  N   ASN B  83     1975   1565   1568    -15   -590   -100       N  
ATOM   1436  CA  ASN B  83       9.913  25.948  13.859  1.00 13.03           C  
ANISOU 1436  CA  ASN B  83     1851   1439   1659    116   -438    -29       C  
ATOM   1437  C   ASN B  83      10.962  25.876  14.980  1.00 11.00           C  
ANISOU 1437  C   ASN B  83     1485   1257   1435    103   -311     72       C  
ATOM   1438  O   ASN B  83      11.658  24.863  15.113  1.00 12.32           O  
ANISOU 1438  O   ASN B  83     1941   1171   1567     91   -254     32       O  
ATOM   1439  CB  ASN B  83       8.729  25.043  14.268  1.00 14.23           C  
ANISOU 1439  CB  ASN B  83     1674   1673   2057    118   -501    149       C  
ATOM   1440  CG  ASN B  83       7.555  25.068  13.300  1.00 14.00           C  
ANISOU 1440  CG  ASN B  83     2031   1591   1695    179   -482    175       C  
ATOM   1441  OD1 ASN B  83       7.032  26.125  12.951  1.00 15.78           O  
ANISOU 1441  OD1 ASN B  83     1966   1724   2304     66   -643    209       O  
ATOM   1442  ND2 ASN B  83       7.094  23.906  12.930  1.00 17.67           N  
ANISOU 1442  ND2 ASN B  83     2127   1966   2621   -174   -869    -54       N  
ATOM   1443  N   ILE B  84      11.069  26.933  15.716  1.00 10.55           N  
ANISOU 1443  N   ILE B  84     1544   1204   1259    159   -275     88       N  
ATOM   1444  CA  ILE B  84      12.066  27.097  16.740  1.00 10.30           C  
ANISOU 1444  CA  ILE B  84     1441   1185   1286    132   -238     35       C  
ATOM   1445  C   ILE B  84      11.422  27.415  18.089  1.00 10.72           C  
ANISOU 1445  C   ILE B  84     1486   1138   1447    133    -28    -15       C  
ATOM   1446  O   ILE B  84      10.715  28.444  18.205  1.00 11.44           O  
ANISOU 1446  O   ILE B  84     1621   1368   1355    457     62    246       O  
ATOM   1447  CB  ILE B  84      13.018  28.257  16.333  1.00 10.72           C  
ANISOU 1447  CB  ILE B  84     1324   1383   1366    291   -147     92       C  
ATOM   1448  CG1 ILE B  84      13.836  27.841  15.107  1.00 12.61           C  
ANISOU 1448  CG1 ILE B  84     1434   1760   1597     37   -208    -20       C  
ATOM   1449  CG2 ILE B  84      13.962  28.701  17.485  1.00 12.47           C  
ANISOU 1449  CG2 ILE B  84     1527   1621   1590    182    -98   -192       C  
ATOM   1450  CD1 ILE B  84      14.544  28.997  14.424  1.00 13.63           C  
ANISOU 1450  CD1 ILE B  84     1462   1902   1814     70    180   -159       C  
ATOM   1451  N   ILE B  85      11.675  26.581  19.108  1.00 10.21           N  
ANISOU 1451  N   ILE B  85     1367   1098   1412    270     14      2       N  
ATOM   1452  CA  ILE B  85      11.297  26.930  20.476  1.00 10.72           C  
ANISOU 1452  CA  ILE B  85     1419   1255   1398    246    186     73       C  
ATOM   1453  C   ILE B  85      12.493  27.592  21.121  1.00  9.85           C  
ANISOU 1453  C   ILE B  85     1314   1379   1050    198    294     61       C  
ATOM   1454  O   ILE B  85      13.560  26.972  21.266  1.00 10.94           O  
ANISOU 1454  O   ILE B  85     1266   1395   1494    326    132    -60       O  
ATOM   1455  CB  ILE B  85      10.880  25.654  21.304  1.00 12.09           C  
ANISOU 1455  CB  ILE B  85     1633   1474   1484     95    137    168       C  
ATOM   1456  CG1 ILE B  85       9.754  24.932  20.582  1.00 15.23           C  
ANISOU 1456  CG1 ILE B  85     2090   1412   2284   -120    -47    322       C  
ATOM   1457  CG2 ILE B  85      10.524  26.063  22.665  1.00 12.69           C  
ANISOU 1457  CG2 ILE B  85     1481   1689   1649    120    474    429       C  
ATOM   1458  CD1 ILE B  85       8.467  25.766  20.430  1.00 18.65           C  
ANISOU 1458  CD1 ILE B  85     2246   1857   2980   -188   -631    190       C  
ATOM   1459  N   GLY B  86      12.333  28.857  21.483  1.00 10.06           N  
ANISOU 1459  N   GLY B  86     1415   1159   1248    315    104     26       N  
ATOM   1460  CA  GLY B  86      13.383  29.610  22.055  1.00  9.99           C  
ANISOU 1460  CA  GLY B  86     1661   1230    901    271    169     92       C  
ATOM   1461  C   GLY B  86      13.328  29.669  23.553  1.00  9.83           C  
ANISOU 1461  C   GLY B  86     1304   1351   1076    316    192     60       C  
ATOM   1462  O   GLY B  86      12.439  29.093  24.212  1.00 11.00           O  
ANISOU 1462  O   GLY B  86     1517   1370   1290    313    162    185       O  
ATOM   1463  N   ARG B  87      14.278  30.351  24.130  1.00 10.61           N  
ANISOU 1463  N   ARG B  87     1500   1486   1045    276    144    152       N  
ATOM   1464  CA  ARG B  87      14.458  30.370  25.564  1.00 10.61           C  
ANISOU 1464  CA  ARG B  87     1486   1670    872    412     78    -27       C  
ATOM   1465  C   ARG B  87      13.252  30.891  26.323  1.00 12.37           C  
ANISOU 1465  C   ARG B  87     1803   1745   1153    471     62    154       C  
ATOM   1466  O   ARG B  87      12.985  30.426  27.462  1.00 13.84           O  
ANISOU 1466  O   ARG B  87     1862   2188   1209    632    313    364       O  
ATOM   1467  CB  ARG B  87      15.676  31.153  25.942  1.00 10.62           C  
ANISOU 1467  CB  ARG B  87     1856   1374    801    382    133    -40       C  
ATOM   1468  CG  ARG B  87      16.983  30.575  25.492  1.00 11.63           C  
ANISOU 1468  CG  ARG B  87     1563   1597   1257    285     28    -99       C  
ATOM   1469  CD  ARG B  87      18.210  31.314  26.036  1.00 12.31           C  
ANISOU 1469  CD  ARG B  87     1754   1732   1189    493      3     67       C  
ATOM   1470  NE  ARG B  87      18.308  32.667  25.573  1.00 12.98           N  
ANISOU 1470  NE  ARG B  87     1897   1676   1358    249   -150   -309       N  
ATOM   1471  CZ  ARG B  87      17.923  33.750  26.266  1.00 14.06           C  
ANISOU 1471  CZ  ARG B  87     2167   1799   1374    377    -48    -54       C  
ATOM   1472  NH1 ARG B  87      17.482  33.674  27.521  1.00 14.54           N  
ANISOU 1472  NH1 ARG B  87     2423   1653   1449    477   -104   -390       N  
ATOM   1473  NH2 ARG B  87      17.988  34.931  25.701  1.00 15.22           N  
ANISOU 1473  NH2 ARG B  87     2707   1662   1411    152    -81   -344       N  
ATOM   1474  N   ASN B  88      12.454  31.772  25.714  1.00 11.17           N  
ANISOU 1474  N   ASN B  88     1733   1612    898    497    240     34       N  
ATOM   1475  CA  ASN B  88      11.272  32.266  26.405  1.00 12.83           C  
ANISOU 1475  CA  ASN B  88     1802   1709   1362    426    377   -222       C  
ATOM   1476  C   ASN B  88      10.330  31.186  26.827  1.00 13.19           C  
ANISOU 1476  C   ASN B  88     2034   1895   1082    587    358    294       C  
ATOM   1477  O   ASN B  88       9.654  31.352  27.847  1.00 15.57           O  
ANISOU 1477  O   ASN B  88     2168   2298   1448    667    793    250       O  
ATOM   1478  CB  ASN B  88      10.568  33.349  25.527  1.00 12.79           C  
ANISOU 1478  CB  ASN B  88     1684   1461   1712    476    432    -24       C  
ATOM   1479  CG  ASN B  88       9.803  32.782  24.387  1.00 13.49           C  
ANISOU 1479  CG  ASN B  88     1753   1619   1752    299    338    443       C  
ATOM   1480  OD1 ASN B  88      10.351  32.034  23.533  1.00 12.59           O  
ANISOU 1480  OD1 ASN B  88     1780   1641   1361    413    330    158       O  
ATOM   1481  ND2 ASN B  88       8.531  33.181  24.274  1.00 13.57           N  
ANISOU 1481  ND2 ASN B  88     1591   1843   1720    516    315    389       N  
ATOM   1482  N   LEU B  89      10.210  30.103  26.056  1.00 13.00           N  
ANISOU 1482  N   LEU B  89     1677   1803   1457    518    506    166       N  
ATOM   1483  CA  LEU B  89       9.413  28.958  26.411  1.00 13.92           C  
ANISOU 1483  CA  LEU B  89     1803   2000   1484    535    568    385       C  
ATOM   1484  C   LEU B  89      10.193  27.791  26.992  1.00 13.78           C  
ANISOU 1484  C   LEU B  89     1945   1956   1333    665    623    311       C  
ATOM   1485  O   LEU B  89       9.644  27.042  27.818  1.00 15.18           O  
ANISOU 1485  O   LEU B  89     1965   2276   1525    548    746    612       O  
ATOM   1486  CB  LEU B  89       8.590  28.506  25.270  1.00 13.59           C  
ANISOU 1486  CB  LEU B  89     1615   1784   1765    482    664    423       C  
ATOM   1487  CG  LEU B  89       7.658  29.568  24.600  1.00 13.46           C  
ANISOU 1487  CG  LEU B  89     1501   1825   1787    360    386    289       C  
ATOM   1488  CD1 LEU B  89       6.853  28.923  23.541  1.00 15.36           C  
ANISOU 1488  CD1 LEU B  89     1678   1960   2199    145    507    763       C  
ATOM   1489  CD2 LEU B  89       6.752  30.269  25.656  1.00 15.01           C  
ANISOU 1489  CD2 LEU B  89     1678   2036   1988    452    588    520       C  
ATOM   1490  N   LEU B  90      11.475  27.643  26.634  1.00 12.29           N  
ANISOU 1490  N   LEU B  90     1742   1651   1274    459    438    380       N  
ATOM   1491  CA  LEU B  90      12.274  26.603  27.228  1.00 12.48           C  
ANISOU 1491  CA  LEU B  90     1770   1769   1200    355    328    375       C  
ATOM   1492  C   LEU B  90      12.338  26.726  28.715  1.00 13.48           C  
ANISOU 1492  C   LEU B  90     1879   1987   1254    491    548    487       C  
ATOM   1493  O   LEU B  90      12.306  25.707  29.410  1.00 16.04           O  
ANISOU 1493  O   LEU B  90     2232   2357   1503    902    749    663       O  
ATOM   1494  CB  LEU B  90      13.692  26.573  26.629  1.00 11.51           C  
ANISOU 1494  CB  LEU B  90     1476   1638   1256    394    316    295       C  
ATOM   1495  CG  LEU B  90      13.788  26.238  25.125  1.00 11.34           C  
ANISOU 1495  CG  LEU B  90     1586   1428   1294    344    303    196       C  
ATOM   1496  CD1 LEU B  90      15.226  26.468  24.633  1.00 11.34           C  
ANISOU 1496  CD1 LEU B  90     1728   1777    801    364    218     12       C  
ATOM   1497  CD2 LEU B  90      13.358  24.827  24.881  1.00 12.38           C  
ANISOU 1497  CD2 LEU B  90     1530   1746   1425    306    294    124       C  
ATOM   1498  N   THR B  91      12.497  27.923  29.225  1.00 14.65           N  
ANISOU 1498  N   THR B  91     2234   2117   1214    715    276    423       N  
ATOM   1499  CA  THR B  91      12.514  28.086  30.712  1.00 16.50           C  
ANISOU 1499  CA  THR B  91     2097   3000   1169    869    320    220       C  
ATOM   1500  C   THR B  91      11.186  27.602  31.324  1.00 17.17           C  
ANISOU 1500  C   THR B  91     1983   3310   1231    955    416    170       C  
ATOM   1501  O   THR B  91      11.203  27.023  32.450  1.00 18.29           O  
ANISOU 1501  O   THR B  91     2387   3357   1202    944    474    416       O  
ATOM   1502  CB  THR B  91      12.764  29.538  31.103  1.00 18.89           C  
ANISOU 1502  CB  THR B  91     2453   3314   1408    818     52     -7       C  
ATOM   1503  OG1 THR B  91      11.819  30.395  30.494  1.00 19.93           O  
ANISOU 1503  OG1 THR B  91     2913   2927   1732   1323    135   -282       O  
ATOM   1504  CG2 THR B  91      14.145  30.047  30.670  1.00 18.42           C  
ANISOU 1504  CG2 THR B  91     2958   2824   1217    709     61   -112       C  
ATOM   1505  N   GLN B  92      10.071  27.832  30.653  1.00 16.73           N  
ANISOU 1505  N   GLN B  92     2180   2773   1403   1175    545    511       N  
ATOM   1506  CA  GLN B  92       8.791  27.545  31.232  1.00 18.14           C  
ANISOU 1506  CA  GLN B  92     2286   2876   1729    894    674    310       C  
ATOM   1507  C   GLN B  92       8.529  26.039  31.369  1.00 19.54           C  
ANISOU 1507  C   GLN B  92     2299   3023   2100    857    860    736       C  
ATOM   1508  O   GLN B  92       7.802  25.598  32.277  1.00 21.58           O  
ANISOU 1508  O   GLN B  92     2789   3456   1951   1024   1129   1072       O  
ATOM   1509  CB  GLN B  92       7.732  28.144  30.405  1.00 17.22           C  
ANISOU 1509  CB  GLN B  92     2097   2720   1722    740    709    735       C  
ATOM   1510  CG  GLN B  92       7.712  29.654  30.394  1.00 17.95           C  
ANISOU 1510  CG  GLN B  92     2104   2700   2014    590    709    652       C  
ATOM   1511  CD  GLN B  92       6.454  30.223  29.783  1.00 17.33           C  
ANISOU 1511  CD  GLN B  92     2444   2535   1606    342    191    509       C  
ATOM   1512  OE1 GLN B  92       5.679  29.511  29.362  1.00 23.32           O  
ANISOU 1512  OE1 GLN B  92     2379   2625   3855    347    -73   1046       O  
ATOM   1513  NE2 GLN B  92       6.483  31.502  29.461  1.00 24.09           N  
ANISOU 1513  NE2 GLN B  92     3164   2507   3479    619   -722    -76       N  
ATOM   1514  N   ILE B  93       9.182  25.254  30.533  1.00 19.08           N  
ANISOU 1514  N   ILE B  93     2357   2688   2201   1143   1103    788       N  
ATOM   1515  CA  ILE B  93       9.050  23.771  30.601  1.00 20.74           C  
ANISOU 1515  CA  ILE B  93     2331   2779   2770    675    841    740       C  
ATOM   1516  C   ILE B  93      10.219  23.103  31.326  1.00 20.47           C  
ANISOU 1516  C   ILE B  93     2569   3049   2159    732   1071    692       C  
ATOM   1517  O   ILE B  93      10.264  21.866  31.441  1.00 24.52           O  
ANISOU 1517  O   ILE B  93     3630   3150   2534   1295   1299   1095       O  
ATOM   1518  CB  ILE B  93       8.900  23.129  29.231  1.00 19.73           C  
ANISOU 1518  CB  ILE B  93     2458   2172   2863    607    990    763       C  
ATOM   1519  CG1 ILE B  93      10.196  23.290  28.417  1.00 19.59           C  
ANISOU 1519  CG1 ILE B  93     2528   2707   2207    561    983    649       C  
ATOM   1520  CG2 ILE B  93       7.757  23.755  28.458  1.00 20.63           C  
ANISOU 1520  CG2 ILE B  93     2574   2782   2479    584    884    579       C  
ATOM   1521  CD1 ILE B  93      10.176  22.541  27.111  1.00 21.14           C  
ANISOU 1521  CD1 ILE B  93     2588   2252   3191     84   1058    312       C  
ATOM   1522  N   GLY B  94      11.050  23.876  31.922  1.00 19.19           N  
ANISOU 1522  N   GLY B  94     2380   3020   1889   1028    984    809       N  
ATOM   1523  CA  GLY B  94      12.074  23.324  32.808  1.00 21.76           C  
ANISOU 1523  CA  GLY B  94     2784   3149   2335   1338    723    983       C  
ATOM   1524  C   GLY B  94      13.375  22.893  32.148  1.00 19.87           C  
ANISOU 1524  C   GLY B  94     2687   3063   1797   1249    867    866       C  
ATOM   1525  O   GLY B  94      14.147  22.175  32.749  1.00 21.90           O  
ANISOU 1525  O   GLY B  94     2818   3326   2177   1516   1095   1426       O  
ATOM   1526  N   CYS B  95      13.631  23.370  30.943  1.00 18.57           N  
ANISOU 1526  N   CYS B  95     2678   2794   1582   1278    623    687       N  
ATOM   1527  CA  CYS B  95      14.751  22.865  30.121  1.00 17.40           C  
ANISOU 1527  CA  CYS B  95     2586   2300   1725    914    679    421       C  
ATOM   1528  C   CYS B  95      16.098  23.520  30.542  1.00 16.89           C  
ANISOU 1528  C   CYS B  95     2527   2284   1606    763    732    515       C  
ATOM   1529  O   CYS B  95      16.240  24.742  30.594  1.00 20.06           O  
ANISOU 1529  O   CYS B  95     3119   2412   2091    998   1096    531       O  
ATOM   1530  CB  CYS B  95      14.445  23.138  28.633  1.00 17.32           C  
ANISOU 1530  CB  CYS B  95     2704   2173   1704    681    439    767       C  
ATOM   1531  SG  CYS B  95      15.519  22.343  27.529  1.00 18.62           S  
ANISOU 1531  SG  CYS B  95     2267   2733   2071    934    704    656       S  
ATOM   1532  N   THR B  96      17.141  22.650  30.687  1.00 16.03           N  
ANISOU 1532  N   THR B  96     2564   2249   1277    883    528    477       N  
ATOM   1533  CA  THR B  96      18.489  23.082  30.938  1.00 16.44           C  
ANISOU 1533  CA  THR B  96     2701   2136   1407    669    157    266       C  
ATOM   1534  C   THR B  96      19.433  22.409  29.949  1.00 13.17           C  
ANISOU 1534  C   THR B  96     2223   1846    933    505    133    199       C  
ATOM   1535  O   THR B  96      19.087  21.390  29.353  1.00 14.87           O  
ANISOU 1535  O   THR B  96     2240   2149   1259    489    214    172       O  
ATOM   1536  CB  THR B  96      18.970  22.705  32.364  1.00 18.50           C  
ANISOU 1536  CB  THR B  96     3047   2788   1192    682    400    271       C  
ATOM   1537  OG1 THR B  96      18.750  21.317  32.595  1.00 18.58           O  
ANISOU 1537  OG1 THR B  96     2795   2664   1600    692    367    568       O  
ATOM   1538  CG2 THR B  96      18.209  23.472  33.445  1.00 21.13           C  
ANISOU 1538  CG2 THR B  96     3503   2904   1619    687    459    -63       C  
ATOM   1539  N   LEU B  97      20.609  22.972  29.837  1.00 14.65           N  
ANISOU 1539  N   LEU B  97     2391   1775   1399    515    209    148       N  
ATOM   1540  CA  LEU B  97      21.738  22.344  29.161  1.00 13.67           C  
ANISOU 1540  CA  LEU B  97     2119   1810   1264    401    163     44       C  
ATOM   1541  C   LEU B  97      22.591  21.705  30.215  1.00 14.83           C  
ANISOU 1541  C   LEU B  97     2285   1831   1519    417    108     72       C  
ATOM   1542  O   LEU B  97      22.842  22.322  31.254  1.00 17.70           O  
ANISOU 1542  O   LEU B  97     2741   1926   2056    545   -328   -211       O  
ATOM   1543  CB  LEU B  97      22.591  23.388  28.477  1.00 16.03           C  
ANISOU 1543  CB  LEU B  97     2300   1929   1861    270     80    178       C  
ATOM   1544  CG  LEU B  97      22.060  23.965  27.249  1.00 16.05           C  
ANISOU 1544  CG  LEU B  97     1976   2223   1900    284    -99    -98       C  
ATOM   1545  CD1 LEU B  97      22.789  25.296  26.813  1.00 19.24           C  
ANISOU 1545  CD1 LEU B  97     2533   2486   2291    109     63    515       C  
ATOM   1546  CD2 LEU B  97      22.135  22.934  26.122  1.00 17.64           C  
ANISOU 1546  CD2 LEU B  97     2559   2702   1442    409     45    166       C  
ATOM   1547  N   ASN B  98      23.163  20.574  29.936  1.00 15.03           N  
ANISOU 1547  N   ASN B  98     2589   1870   1250    528    153    208       N  
ATOM   1548  CA  ASN B  98      23.929  19.848  30.932  1.00 16.84           C  
ANISOU 1548  CA  ASN B  98     2654   2145   1598    619    143    359       C  
ATOM   1549  C   ASN B  98      25.108  19.170  30.258  1.00 16.26           C  
ANISOU 1549  C   ASN B  98     2352   2055   1770    545    111    151       C  
ATOM   1550  O   ASN B  98      24.949  18.437  29.320  1.00 17.04           O  
ANISOU 1550  O   ASN B  98     2494   2205   1773    639     -5    223       O  
ATOM   1551  CB  ASN B  98      23.076  18.787  31.618  1.00 16.41           C  
ANISOU 1551  CB  ASN B  98     2131   2400   1703    612     57    223       C  
ATOM   1552  CG  ASN B  98      21.897  19.359  32.314  1.00 17.32           C  
ANISOU 1552  CG  ASN B  98     2763   2354   1463    672    244    260       C  
ATOM   1553  OD1 ASN B  98      20.861  19.696  31.696  1.00 21.19           O  
ANISOU 1553  OD1 ASN B  98     2948   3043   2057    974    164    467       O  
ATOM   1554  ND2 ASN B  98      21.968  19.398  33.597  1.00 21.01           N  
ANISOU 1554  ND2 ASN B  98     3211   3259   1510    316    363    506       N  
ATOM   1555  N   PHE B  99      26.308  19.340  30.868  1.00 19.05           N  
ANISOU 1555  N   PHE B  99     2538   2503   2195    610    -42    184       N  
ATOM   1556  CA  PHE B  99      27.477  18.594  30.495  1.00 19.26           C  
ANISOU 1556  CA  PHE B  99     2428   2636   2254    497     51    213       C  
ATOM   1557  C   PHE B  99      28.480  18.540  31.605  1.00 23.60           C  
ANISOU 1557  C   PHE B  99     2755   3459   2750    389    -84    119       C  
ATOM   1558  O   PHE B  99      29.553  17.923  31.408  1.00 26.36           O  
ANISOU 1558  O   PHE B  99     3025   3880   3110    792   -180    725       O  
ATOM   1559  CB  PHE B  99      28.125  19.197  29.195  1.00 18.95           C  
ANISOU 1559  CB  PHE B  99     2170   2672   2357    587   -100    132       C  
ATOM   1560  CG  PHE B  99      28.559  20.660  29.319  1.00 20.10           C  
ANISOU 1560  CG  PHE B  99     2544   2764   2326    458   -215    229       C  
ATOM   1561  CD1 PHE B  99      27.689  21.660  29.066  1.00 19.53           C  
ANISOU 1561  CD1 PHE B  99     2842   2443   2135    467   -389    200       C  
ATOM   1562  CD2 PHE B  99      29.904  20.980  29.389  1.00 22.05           C  
ANISOU 1562  CD2 PHE B  99     2672   2564   3139    206   -244    400       C  
ATOM   1563  CE1 PHE B  99      28.111  22.973  29.105  1.00 21.02           C  
ANISOU 1563  CE1 PHE B  99     2856   2490   2639    510   -248    507       C  
ATOM   1564  CE2 PHE B  99      30.313  22.255  29.420  1.00 22.95           C  
ANISOU 1564  CE2 PHE B  99     2734   2704   3280     29   -455    147       C  
ATOM   1565  CZ  PHE B  99      29.422  23.262  29.175  1.00 23.61           C  
ANISOU 1565  CZ  PHE B  99     3176   2409   3382    184    -69   -154       C  
ATOM   1566  OXT PHE B  99      28.224  19.068  32.704  1.00 24.03           O  
ANISOU 1566  OXT PHE B  99     3057   3529   2544    526   -310    201       O  
TER    1567      PHE B  99                                                      
HETATM 1568  P   PO4 A 502      21.885  38.055  28.472  1.00 48.18           P  
ANISOU 1568  P   PO4 A 502     7425   4338   6542   -728   -211   -475       P  
HETATM 1569  O1  PO4 A 502      20.858  37.017  28.170  1.00 29.71           O  
ANISOU 1569  O1  PO4 A 502     5708   2636   2942    169   -226   -847       O  
HETATM 1570  O2  PO4 A 502      22.214  37.997  29.948  1.00 51.15           O  
ANISOU 1570  O2  PO4 A 502     7216   5665   6553   -804   -686   -322       O  
HETATM 1571  O3  PO4 A 502      21.307  39.440  28.149  1.00 53.51           O  
ANISOU 1571  O3  PO4 A 502     7234   5416   7680    228   -110    241       O  
HETATM 1572  O4  PO4 A 502      23.219  37.809  27.658  1.00 51.63           O  
ANISOU 1572  O4  PO4 A 502     7180   5767   6669   -170   -184    195       O  
HETATM 1573  P   PO4 A 504      42.373  37.711  14.743  1.00 40.32           P  
ANISOU 1573  P   PO4 A 504     5222   3664   6432   -743   -338   1127       P  
HETATM 1574  O1  PO4 A 504      41.820  36.448  15.184  1.00 27.77           O  
ANISOU 1574  O1  PO4 A 504     3264   2652   4633   -286   -505    472       O  
HETATM 1575  O2  PO4 A 504      43.098  38.349  15.925  1.00 48.29           O  
ANISOU 1575  O2  PO4 A 504     5823   6185   6338    -52   -481    -28       O  
HETATM 1576  O3  PO4 A 504      41.277  38.652  14.226  1.00 44.12           O  
ANISOU 1576  O3  PO4 A 504     5603   4123   7036    370     26    345       O  
HETATM 1577  O4  PO4 A 504      43.377  37.445  13.606  1.00 50.93           O  
ANISOU 1577  O4  PO4 A 504     6722   6316   6311   -268     83    360       O  
HETATM 1578  P   PO4 A 505      34.643  38.029  22.219  1.00 49.35           P  
ANISOU 1578  P   PO4 A 505     4814   5880   8055    -96   -819    401       P  
HETATM 1579  O1  PO4 A 505      34.551  36.694  21.697  1.00 35.99           O  
ANISOU 1579  O1  PO4 A 505     2836   5070   5767    113   -781   1030       O  
HETATM 1580  O2  PO4 A 505      34.964  37.984  23.733  1.00 51.20           O  
ANISOU 1580  O2  PO4 A 505     6372   5473   7607   -361   -122   -185       O  
HETATM 1581  O3  PO4 A 505      33.267  38.781  21.998  1.00 49.54           O  
ANISOU 1581  O3  PO4 A 505     5555   5214   8054    303   -639     -7       O  
HETATM 1582  O4  PO4 A 505      35.779  38.755  21.456  1.00 55.19           O  
ANISOU 1582  O4  PO4 A 505     6207   7035   7727   -288    310    416       O  
HETATM 1583  N1  017 A1200      14.279  34.925  18.220  1.00 14.67           N  
ANISOU 1583  N1  017 A1200     1726   1789   2057    346    395     12       N  
HETATM 1584  C2  017 A1200      15.195  34.330  17.380  1.00 12.94           C  
ANISOU 1584  C2  017 A1200     1584   1675   1658    405    179      5       C  
HETATM 1585  C3  017 A1200      16.193  35.169  16.760  1.00 12.63           C  
ANISOU 1585  C3  017 A1200     1719   1582   1495    369   -308    -10       C  
HETATM 1586  C4  017 A1200      17.180  34.513  15.867  1.00 11.85           C  
ANISOU 1586  C4  017 A1200     1408   1448   1645    416    -79      9       C  
HETATM 1587  C5  017 A1200      17.012  33.220  15.616  1.00 10.81           C  
ANISOU 1587  C5  017 A1200     1451   1355   1300    269    -33     -5       C  
HETATM 1588  C6  017 A1200      15.919  32.472  16.187  1.00 13.71           C  
ANISOU 1588  C6  017 A1200     1658   1686   1863    473    126    250       C  
HETATM 1589  C7  017 A1200      14.979  33.107  17.003  1.00 14.04           C  
ANISOU 1589  C7  017 A1200     1909   1699   1726    543    239    297       C  
HETATM 1590  S8  017 A1200      18.136  32.331  14.660  1.00 10.16           S  
ANISOU 1590  S8  017 A1200     1418   1164   1278    192    106    157       S  
HETATM 1591  O9  017 A1200      18.756  33.247  13.785  1.00 11.32           O  
ANISOU 1591  O9  017 A1200     1718   1349   1233    111    239    206       O  
HETATM 1592  O10 017 A1200      17.453  31.221  14.098  1.00 11.42           O  
ANISOU 1592  O10 017 A1200     1475   1384   1478    321   -121    141       O  
HETATM 1593  N11 017 A1200      19.316  31.708  15.598  1.00 10.03           N  
ANISOU 1593  N11 017 A1200     1446   1137   1227    134     29     15       N  
HETATM 1594  C12 017 A1200      20.128  32.699  16.353  1.00 11.72           C  
ANISOU 1594  C12 017 A1200     1507   1407   1538    167    -46     61       C  
HETATM 1595  C13 017 A1200      21.628  32.355  16.432  1.00 11.02           C  
ANISOU 1595  C13 017 A1200     1317   1365   1505     56   -113    167       C  
HETATM 1596  C14 017 A1200      22.279  32.317  15.034  1.00 12.13           C  
ANISOU 1596  C14 017 A1200     1555   1426   1627    -39    102    230       C  
HETATM 1597  C15 017 A1200      22.282  33.401  17.329  1.00 12.08           C  
ANISOU 1597  C15 017 A1200     1486   1458   1645      2   -205     83       C  
HETATM 1598  C16 017 A1200      19.063  30.433  16.294  1.00  9.17           C  
ANISOU 1598  C16 017 A1200     1280   1120   1082     86     53    135       C  
HETATM 1599  C17 017 A1200      19.962  29.337  15.738  1.00  8.55           C  
ANISOU 1599  C17 017 A1200     1240   1147    861    126     11    147       C  
HETATM 1600  O18 017 A1200      19.895  28.206  16.604  1.00  9.54           O  
ANISOU 1600  O18 017 A1200     1295   1260   1068    195    -97     98       O  
HETATM 1601  C19 017 A1200      19.599  28.895  14.297  1.00  8.43           C  
ANISOU 1601  C19 017 A1200     1096   1073   1034    180    -16     70       C  
HETATM 1602  N20 017 A1200      20.709  28.031  13.805  1.00  8.78           N  
ANISOU 1602  N20 017 A1200     1143   1204    989     58      0    148       N  
HETATM 1603  C21 017 A1200      21.566  28.405  12.887  1.00  9.33           C  
ANISOU 1603  C21 017 A1200     1315   1111   1118     90     42    188       C  
HETATM 1604  O22 017 A1200      21.634  29.442  12.299  1.00  9.69           O  
ANISOU 1604  O22 017 A1200     1302   1143   1235    184    186    227       O  
HETATM 1605  O23 017 A1200      22.469  27.402  12.655  1.00  9.66           O  
ANISOU 1605  O23 017 A1200     1196   1329   1145    242    168    154       O  
HETATM 1606  C24 017 A1200      23.321  27.511  11.496  1.00 10.12           C  
ANISOU 1606  C24 017 A1200     1240   1372   1232    144    261    278       C  
HETATM 1607  C25 017 A1200      24.640  26.896  11.912  1.00 10.46           C  
ANISOU 1607  C25 017 A1200     1165   1457   1352     90    147    165       C  
HETATM 1608  O26 017 A1200      24.413  25.475  11.833  1.00 10.09           O  
ANISOU 1608  O26 017 A1200     1188   1459   1185    130    -49    122       O  
HETATM 1609  C27 017 A1200      23.493  25.227  10.779  1.00 10.21           C  
ANISOU 1609  C27 017 A1200     1408   1362   1110    288    163     49       C  
HETATM 1610  O28 017 A1200      22.483  24.363  11.236  1.00 10.86           O  
ANISOU 1610  O28 017 A1200     1465   1407   1254     45   -125     71       O  
HETATM 1611  C29 017 A1200      21.193  25.063  11.296  1.00 10.64           C  
ANISOU 1611  C29 017 A1200     1203   1440   1400    120    -93     88       C  
HETATM 1612  C30 017 A1200      21.363  26.256  10.383  1.00 10.81           C  
ANISOU 1612  C30 017 A1200     1355   1548   1202     -4   -129    210       C  
HETATM 1613  C31 017 A1200      22.839  26.537  10.396  1.00 10.71           C  
ANISOU 1613  C31 017 A1200     1364   1558   1144    157     27    206       C  
HETATM 1614  C32 017 A1200      18.307  28.149  14.166  1.00  9.08           C  
ANISOU 1614  C32 017 A1200     1009   1231   1208    103    -58    105       C  
HETATM 1615  C33 017 A1200      18.054  26.400  12.363  1.00 10.63           C  
ANISOU 1615  C33 017 A1200     1348   1355   1333    159   -153    -98       C  
HETATM 1616  C34 017 A1200      17.831  26.025  11.051  1.00 11.17           C  
ANISOU 1616  C34 017 A1200     1531   1274   1438    154   -274   -223       C  
HETATM 1617  C35 017 A1200      17.597  26.981  10.098  1.00 11.51           C  
ANISOU 1617  C35 017 A1200     1431   1533   1408    157    -58     11       C  
HETATM 1618  C36 017 A1200      17.550  28.293  10.460  1.00 11.00           C  
ANISOU 1618  C36 017 A1200     1533   1506   1138    130   -141     45       C  
HETATM 1619  C37 017 A1200      17.765  28.674  11.767  1.00 10.26           C  
ANISOU 1619  C37 017 A1200     1570   1360    968     29    -78     70       C  
HETATM 1620  C38 017 A1200      18.024  27.733  12.757  1.00  9.32           C  
ANISOU 1620  C38 017 A1200     1201   1244   1096     40    -21     23       C  
HETATM 1621  P   PO4 B 501      -5.626  26.300  22.085  1.00 23.36           P  
ANISOU 1621  P   PO4 B 501     2912   2992   2969   -349   -343    492       P  
HETATM 1622  O1  PO4 B 501      -4.465  25.632  22.864  1.00 24.90           O  
ANISOU 1622  O1  PO4 B 501     3245   3580   2633   -792  -1169    638       O  
HETATM 1623  O2  PO4 B 501      -4.920  27.015  21.053  1.00 26.37           O  
ANISOU 1623  O2  PO4 B 501     3311   2701   4008   -926   1056   -313       O  
HETATM 1624  O3  PO4 B 501      -6.680  25.278  21.514  1.00 31.16           O  
ANISOU 1624  O3  PO4 B 501     3220   4608   4010  -1522    423  -1016       O  
HETATM 1625  O4  PO4 B 501      -6.552  27.339  22.925  1.00 28.48           O  
ANISOU 1625  O4  PO4 B 501     2629   3651   4540    447    625    336       O  
HETATM 1626  P   PO4 B 503      12.482  12.194  33.278  1.00 38.88           P  
ANISOU 1626  P   PO4 B 503     6369   4805   3597   -929    774    992       P  
HETATM 1627  O1  PO4 B 503      12.623  10.721  33.366  1.00 39.20           O  
ANISOU 1627  O1  PO4 B 503     5784   4309   4799  -1573    383   1435       O  
HETATM 1628  O2  PO4 B 503      13.862  12.883  33.347  1.00 49.22           O  
ANISOU 1628  O2  PO4 B 503     5744   6389   6568   -583     94    124       O  
HETATM 1629  O3  PO4 B 503      11.756  12.585  32.008  1.00 43.18           O  
ANISOU 1629  O3  PO4 B 503     5696   6200   4508    113    220    684       O  
HETATM 1630  O4  PO4 B 503      11.649  12.645  34.454  1.00 51.01           O  
ANISOU 1630  O4  PO4 B 503     7301   7162   4918     59   1055   -122       O  
HETATM 1631  O   HOH A1201      20.056  21.395  15.795  1.00  9.72           O  
ANISOU 1631  O   HOH A1201     1375   1126   1189     88    -87   -142       O  
HETATM 1632  O   HOH A1202      19.502  22.761  13.407  1.00 11.00           O  
ANISOU 1632  O   HOH A1202     1590   1367   1221     61    -42    218       O  
HETATM 1633  O   HOH A1203      20.376  31.870  11.841  1.00 11.01           O  
ANISOU 1633  O   HOH A1203     1577   1310   1293    166     87    226       O  
HETATM 1634  O   HOH A1204      24.470  14.948  23.041  1.00 18.99           O  
ANISOU 1634  O   HOH A1204     2570   2506   2139    941    -33    277       O  
HETATM 1635  O   HOH A1205      32.126  16.598  15.801  1.00 20.67           O  
ANISOU 1635  O   HOH A1205     2331   2679   2841    845    337     46       O  
HETATM 1636  O   HOH A1206      31.152  23.564  12.349  1.00 14.98           O  
ANISOU 1636  O   HOH A1206     1647   2270   1773    693    514    273       O  
HETATM 1637  O   HOH A1207      19.773  31.510  33.212  1.00 23.07           O  
ANISOU 1637  O   HOH A1207     4176   2651   1938    803   -645   -498       O  
HETATM 1638  O   HOH A1208      38.527  15.568  15.489  1.00 16.16           O  
ANISOU 1638  O   HOH A1208     2405   1867   1866    392    391    357       O  
HETATM 1639  O   HOH A1209      30.242  38.855  12.622  1.00 19.27           O  
ANISOU 1639  O   HOH A1209     2149   1880   3291     76   -131    659       O  
HETATM 1640  O   HOH A1210      37.509  18.927  30.928  1.00 66.30           O  
ANISOU 1640  O   HOH A1210     8978   8382   7828    -19   -219   -412       O  
HETATM 1641  O   HOH A1211      22.554  36.018   1.390  1.00 22.79           O  
ANISOU 1641  O   HOH A1211     2783   3019   2854    198   -398  -1102       O  
HETATM 1642  O   HOH A1212      15.214  33.413   5.158  1.00 23.27           O  
ANISOU 1642  O   HOH A1212     2278   4460   2101   -258    -84    -41       O  
HETATM 1643  O   HOH A1213      32.655  38.325  11.281  1.00 18.19           O  
ANISOU 1643  O   HOH A1213     2230   1700   2979     66   -393    643       O  
HETATM 1644  O   HOH A1214      36.725  18.360  11.936  1.00 23.65           O  
ANISOU 1644  O   HOH A1214     2453   2693   3839    880    958    164       O  
HETATM 1645  O   HOH A1215      30.244  36.892  19.101  1.00 19.55           O  
ANISOU 1645  O   HOH A1215     3088   1953   2386    220   -860   -189       O  
HETATM 1646  O   HOH A1216      22.211  30.573  30.150  1.00 20.39           O  
ANISOU 1646  O   HOH A1216     2890   2568   2288    509    181    193       O  
HETATM 1647  O   HOH A1217      26.106  18.484  13.537  1.00 24.44           O  
ANISOU 1647  O   HOH A1217     3413   1901   3972     -8   -663   -464       O  
HETATM 1648  O   HOH A1218      40.990  22.357   7.513  1.00 26.41           O  
ANISOU 1648  O   HOH A1218     2412   3857   3763    478    846    246       O  
HETATM 1649  O   HOH A1219      35.011  36.725  19.441  1.00 27.60           O  
ANISOU 1649  O   HOH A1219     3016   2766   4702   -976   -109    749       O  
HETATM 1650  O   HOH A1220      28.937  24.711   0.721  1.00 26.97           O  
ANISOU 1650  O   HOH A1220     3138   2632   4478    219   -146  -1635       O  
HETATM 1651  O   HOH A1221      32.743  37.872   8.649  1.00 27.12           O  
ANISOU 1651  O   HOH A1221     3094   4525   2684   -604    -72    230       O  
HETATM 1652  O   HOH A1222      30.254  21.326  11.163  1.00 27.66           O  
ANISOU 1652  O   HOH A1222     2607   4229   3673    729   -536   -928       O  
HETATM 1653  O   HOH A1223      24.667  15.436  29.507  1.00 21.39           O  
ANISOU 1653  O   HOH A1223     2577   2492   3055    821    233    746       O  
HETATM 1654  O   HOH A1224      35.448  34.771  16.380  1.00 21.81           O  
ANISOU 1654  O   HOH A1224     2696   2786   2803   -658   -771    845       O  
HETATM 1655  O   HOH A1225      24.419  35.603  29.375  1.00 26.71           O  
ANISOU 1655  O   HOH A1225     3973   2778   3397   -332   -209  -1372       O  
HETATM 1656  O   HOH A1226      31.153  37.034  21.547  1.00 24.76           O  
ANISOU 1656  O   HOH A1226     3566   2877   2965    164   -890    265       O  
HETATM 1657  O   HOH A1227      23.183  25.239   5.038  1.00 25.08           O  
ANISOU 1657  O   HOH A1227     2607   2497   4423    119    386    193       O  
HETATM 1658  O   HOH A1228      40.557  20.352  22.611  1.00 25.67           O  
ANISOU 1658  O   HOH A1228     2459   3479   3813   -359   -341   1070       O  
HETATM 1659  O   HOH A1229      34.909  34.098   6.281  1.00 27.77           O  
ANISOU 1659  O   HOH A1229     3899   3374   3277   -680   1030    679       O  
HETATM 1660  O   HOH A1230      26.947  37.818   4.115  1.00 34.01           O  
ANISOU 1660  O   HOH A1230     4955   3701   4266    918    474   1212       O  
HETATM 1661  O   HOH A1231      19.571  33.367  35.118  1.00 30.22           O  
ANISOU 1661  O   HOH A1231     5115   3454   2912   -298     26   -871       O  
HETATM 1662  O   HOH A1232      14.317  35.443  30.347  1.00 41.94           O  
ANISOU 1662  O   HOH A1232     4360   6363   5210    637    775   -169       O  
HETATM 1663  O   HOH A1233      24.076  21.260   8.457  1.00 32.39           O  
ANISOU 1663  O   HOH A1233     4193   5959   2155   -574    562    -17       O  
HETATM 1664  O   HOH A1234      32.796  30.455   0.789  1.00 28.13           O  
ANISOU 1664  O   HOH A1234     3757   3722   3207    577   1230    604       O  
HETATM 1665  O   HOH A1235      16.879  37.933   4.787  1.00 28.00           O  
ANISOU 1665  O   HOH A1235     4775   3244   2618   1317    871    530       O  
HETATM 1666  O   HOH A1236      24.953  40.472  16.765  1.00 34.00           O  
ANISOU 1666  O   HOH A1236     5190   3691   4035   1705   -689  -1214       O  
HETATM 1667  O   HOH A1237      34.545  31.412   1.720  1.00 30.01           O  
ANISOU 1667  O   HOH A1237     4551   3782   3070    474   1018   1060       O  
HETATM 1668  O   HOH A1238      35.938  33.777  31.163  1.00 29.47           O  
ANISOU 1668  O   HOH A1238     4540   3366   3289    611  -1556   -212       O  
HETATM 1669  O   HOH A1239      14.337  33.445  28.692  1.00 30.90           O  
ANISOU 1669  O   HOH A1239     4148   4326   3266    780   -194    287       O  
HETATM 1670  O   HOH A1240      22.650  28.564  34.792  1.00 26.66           O  
ANISOU 1670  O   HOH A1240     3904   3793   2430   -204   -494   -843       O  
HETATM 1671  O   HOH A1241      25.499  12.874  24.637  1.00 29.83           O  
ANISOU 1671  O   HOH A1241     3296   3301   4735   1147   -813   -506       O  
HETATM 1672  O   HOH A1242      41.746  25.134  22.803  1.00 24.60           O  
ANISOU 1672  O   HOH A1242     2203   2906   4235    137    -11   1156       O  
HETATM 1673  O   HOH A1243      42.773  18.912  22.293  1.00 35.51           O  
ANISOU 1673  O   HOH A1243     3873   4602   5017    550   -554   1170       O  
HETATM 1674  O   HOH A1244      28.371  14.951  16.383  1.00 27.22           O  
ANISOU 1674  O   HOH A1244     3819   4042   2482   -623   -114   -284       O  
HETATM 1675  O   HOH A1245      46.003  28.741  16.572  1.00 29.53           O  
ANISOU 1675  O   HOH A1245     3841   4245   3133   -623     29    -25       O  
HETATM 1676  O   HOH A1246      37.435  40.536  13.076  1.00 41.26           O  
ANISOU 1676  O   HOH A1246     4436   5395   5844    761   -350    692       O  
HETATM 1677  O   HOH A1247      25.053  23.610   7.494  1.00 31.32           O  
ANISOU 1677  O   HOH A1247     3884   4875   3141   -850   -530   -233       O  
HETATM 1678  O   HOH A1248      33.742  16.688  28.022  1.00 26.46           O  
ANISOU 1678  O   HOH A1248     3868   2978   3206    170   -462    539       O  
HETATM 1679  O   HOH A1249      35.443  16.383  25.881  1.00 31.26           O  
ANISOU 1679  O   HOH A1249     4264   4481   3130   -565    721   1030       O  
HETATM 1680  O   HOH A1250      15.513  16.399  33.653  1.00 28.44           O  
ANISOU 1680  O   HOH A1250     4050   4163   2590    -82    499    831       O  
HETATM 1681  O   HOH A1251      25.338  27.070  35.519  1.00 35.80           O  
ANISOU 1681  O   HOH A1251     5802   4431   3369   -860   -398   -773       O  
HETATM 1682  O   HOH A1252      36.111  28.461  29.662  1.00 28.85           O  
ANISOU 1682  O   HOH A1252     4595   2921   3443     -8  -1378    585       O  
HETATM 1683  O  AHOH A1253      31.177  12.878  24.119  0.50 24.08           O  
ANISOU 1683  O  AHOH A1253     4439   2318   2389   -395    -42    -82       O  
HETATM 1684  O  BHOH A1253      18.188  40.860   6.058  0.50 35.73           O  
ANISOU 1684  O  BHOH A1253     4555   5185   3833    105     57   1635       O  
HETATM 1685  O   HOH A1254      10.764  20.315  33.810  1.00 30.38           O  
ANISOU 1685  O   HOH A1254     5087   3512   2942    647   1096    863       O  
HETATM 1686  O   HOH A1255      27.995  14.575  29.793  1.00 30.38           O  
ANISOU 1686  O   HOH A1255     3766   4299   3475    501   -259   1274       O  
HETATM 1687  O   HOH A1256      37.545  26.813  28.286  1.00 30.35           O  
ANISOU 1687  O   HOH A1256     3518   3012   5002   -493   -397   -375       O  
HETATM 1688  O   HOH A1257      43.767  18.571  15.523  1.00 26.15           O  
ANISOU 1688  O   HOH A1257     2598   2867   4469    272    157    732       O  
HETATM 1689  O   HOH A1258      25.719  12.974  27.397  1.00 32.15           O  
ANISOU 1689  O   HOH A1258     5055   3078   4080    551   -353   -102       O  
HETATM 1690  O   HOH A1259      32.635  35.021   4.224  1.00 30.91           O  
ANISOU 1690  O   HOH A1259     4455   3489   3800  -1433    926   -445       O  
HETATM 1691  O   HOH A1260      44.792  24.695  12.710  1.00 30.61           O  
ANISOU 1691  O   HOH A1260     2414   3839   5377    -73   -579   -471       O  
HETATM 1692  O   HOH A1261      32.684  28.589  30.555  1.00 41.52           O  
ANISOU 1692  O   HOH A1261     6500   5633   3643   1384  -1889     56       O  
HETATM 1693  O   HOH A1262      24.455  31.227  31.391  1.00 32.24           O  
ANISOU 1693  O   HOH A1262     4609   4550   3090   -532   -233   -472       O  
HETATM 1694  O   HOH A1263      18.720  18.456  36.423  1.00 28.00           O  
ANISOU 1694  O   HOH A1263     3599   3822   3215   -361    231    404       O  
HETATM 1695  O   HOH A1264      27.912  12.399  23.952  1.00 38.97           O  
ANISOU 1695  O   HOH A1264     6223   1620   6962   1327   1449   -839       O  
HETATM 1696  O   HOH A1265      29.009  37.657  23.043  1.00 39.75           O  
ANISOU 1696  O   HOH A1265     4725   5789   4589     11   -541    313       O  
HETATM 1697  O   HOH A1266      41.992  22.457  23.047  1.00 30.43           O  
ANISOU 1697  O   HOH A1266     3585   3606   4368    291   -701    220       O  
HETATM 1698  O   HOH A1267      46.896  32.717  19.184  1.00 29.90           O  
ANISOU 1698  O   HOH A1267     3133   4208   4017   -763    262   -803       O  
HETATM 1699  O   HOH A1268      44.655  29.609   7.419  1.00 30.54           O  
ANISOU 1699  O   HOH A1268     4032   5151   2418  -1248    386   -212       O  
HETATM 1700  O   HOH A1269      28.110  32.805  -3.098  1.00 29.00           O  
ANISOU 1700  O   HOH A1269     3636   4827   2554   -830    123   -357       O  
HETATM 1701  O   HOH A1270      20.387  24.569   4.514  1.00 41.39           O  
ANISOU 1701  O   HOH A1270     5563   4342   5818   -293    -13    344       O  
HETATM 1702  O   HOH A1271      17.306  14.511  32.564  1.00 27.93           O  
ANISOU 1702  O   HOH A1271     3812   3323   3475    449    683    851       O  
HETATM 1703  O   HOH A1272      26.089  16.318  15.993  1.00 31.89           O  
ANISOU 1703  O   HOH A1272     3091   4141   4886    -68   -167    809       O  
HETATM 1704  O   HOH A1273      25.310  36.597   2.688  1.00 28.48           O  
ANISOU 1704  O   HOH A1273     4392   3081   3347   -553   -181     22       O  
HETATM 1705  O   HOH A1274      32.223  30.978  30.868  1.00 35.13           O  
ANISOU 1705  O   HOH A1274     5173   4798   3377   -176  -1281    -46       O  
HETATM 1706  O   HOH A1275      25.031  16.305  13.856  1.00 33.56           O  
ANISOU 1706  O   HOH A1275     4413   4571   3764   1187   1078   -534       O  
HETATM 1707  O   HOH A1276      30.501  21.624   8.159  1.00 34.20           O  
ANISOU 1707  O   HOH A1276     4910   4627   3456    246   -139   -699       O  
HETATM 1708  O   HOH A1277      24.712  17.765  11.324  1.00 34.86           O  
ANISOU 1708  O   HOH A1277     5012   5053   3178    866   -133   -996       O  
HETATM 1709  O   HOH A1278      42.106  37.123  19.766  1.00 33.83           O  
ANISOU 1709  O   HOH A1278     4176   3767   4910   -262   -986    767       O  
HETATM 1710  O   HOH A1279      19.937  26.074   6.365  1.00 38.55           O  
ANISOU 1710  O   HOH A1279     5898   3256   5493  -1400     32   -288       O  
HETATM 1711  O   HOH A1280      22.643  31.133  33.338  1.00 35.62           O  
ANISOU 1711  O   HOH A1280     4976   4258   4299   -267   -226   -418       O  
HETATM 1712  O   HOH A1281      25.340  23.312   5.051  1.00 42.71           O  
ANISOU 1712  O   HOH A1281     6433   5477   4317   -537   -102   -541       O  
HETATM 1713  O   HOH A1282      38.841  22.407   5.563  1.00 35.94           O  
ANISOU 1713  O   HOH A1282     5656   3304   4692    575   1814    198       O  
HETATM 1714  O   HOH A1283      44.781  18.255  11.861  1.00 40.96           O  
ANISOU 1714  O   HOH A1283     3882   5394   6287  -1323   -331   -297       O  
HETATM 1715  O   HOH A1284      18.218  36.012  34.680  1.00 38.51           O  
ANISOU 1715  O   HOH A1284     5701   5100   3830     48     58   -783       O  
HETATM 1716  O   HOH A1285      43.783  28.111  29.364  1.00 44.82           O  
ANISOU 1716  O   HOH A1285     5344   4814   6869    621   1439   -214       O  
HETATM 1717  O   HOH A1286      38.353  37.628  16.353  1.00 36.63           O  
ANISOU 1717  O   HOH A1286     5419   4003   4494    403    205    427       O  
HETATM 1718  O   HOH A1287      28.388  39.092  19.490  1.00 37.49           O  
ANISOU 1718  O   HOH A1287     5082   3711   5452    -51    593   -454       O  
HETATM 1719  O   HOH A1288      32.279  20.461  34.588  1.00 39.70           O  
ANISOU 1719  O   HOH A1288     4630   5344   5109    603   -792   -231       O  
HETATM 1720  O   HOH A1289      27.637  16.777  14.422  1.00 36.29           O  
ANISOU 1720  O   HOH A1289     5179   3745   4863   -639   -787  -1028       O  
HETATM 1721  O   HOH A1290      34.831  36.424   7.793  1.00 32.74           O  
ANISOU 1721  O   HOH A1290     4505   3325   4607   -690   -220    211       O  
HETATM 1722  O   HOH A1291      18.420  28.713   5.642  1.00 32.44           O  
ANISOU 1722  O   HOH A1291     3231   4835   4258    953   -622  -1846       O  
HETATM 1723  O   HOH A1292      44.539  21.832  12.952  1.00 40.72           O  
ANISOU 1723  O   HOH A1292     4806   4662   6000   1432    583   -342       O  
HETATM 1724  O   HOH A1293      28.710  40.292  17.167  1.00 32.26           O  
ANISOU 1724  O   HOH A1293     3265   4536   4454  -1210   -364   -120       O  
HETATM 1725  O   HOH A1294      31.089  18.696  11.526  1.00 32.98           O  
ANISOU 1725  O   HOH A1294     4166   4527   3836    -74    339   -399       O  
HETATM 1726  O   HOH A1295      22.138  25.318   7.205  1.00 36.48           O  
ANISOU 1726  O   HOH A1295     6915   3234   3708    155    598   -935       O  
HETATM 1727  O   HOH A1296      43.165  35.376  24.302  1.00 34.46           O  
ANISOU 1727  O   HOH A1296     3710   4141   5242  -1698   -710   -297       O  
HETATM 1728  O   HOH A1297       9.950  16.601  33.231  1.00 42.27           O  
ANISOU 1728  O   HOH A1297     4559   6389   5109     29   1494    287       O  
HETATM 1729  O   HOH A1298      47.676  26.803  15.174  1.00 32.51           O  
ANISOU 1729  O   HOH A1298     3158   5693   3501   -660    422     44       O  
HETATM 1730  O   HOH A1299      24.497  38.712  24.884  1.00 35.29           O  
ANISOU 1730  O   HOH A1299     3929   4092   5388   -193   -312   -231       O  
HETATM 1731  O   HOH A1300      26.077  23.475  37.496  1.00 39.84           O  
ANISOU 1731  O   HOH A1300     4840   7383   2914    172   -836  -1032       O  
HETATM 1732  O   HOH A1301      45.583  39.291  21.124  1.00 42.18           O  
ANISOU 1732  O   HOH A1301     4339   5985   5702   -446    183   -202       O  
HETATM 1733  O   HOH A1302      36.208  35.773  26.365  1.00 39.14           O  
ANISOU 1733  O   HOH A1302     4346   4878   5646   -328  -1089   -314       O  
HETATM 1734  O   HOH A1303      41.931  23.159   1.641  1.00 40.61           O  
ANISOU 1734  O   HOH A1303     4660   4994   5776     92    845    439       O  
HETATM 1735  O   HOH A1304      40.929  38.006  10.984  1.00 42.83           O  
ANISOU 1735  O   HOH A1304     3860   6268   6144   -947    272   1001       O  
HETATM 1736  O   HOH A1305      21.309  15.342  33.578  1.00 45.22           O  
ANISOU 1736  O   HOH A1305     5988   5651   5541    361  -1157    843       O  
HETATM 1737  O   HOH A1306      46.579  37.296  24.570  1.00 42.72           O  
ANISOU 1737  O   HOH A1306     5358   4744   6127   -779    129    776       O  
HETATM 1738  O   HOH A1307      36.639  33.881   2.663  1.00 43.37           O  
ANISOU 1738  O   HOH A1307     6399   4186   5893     43   -186    966       O  
HETATM 1739  O   HOH A1308      24.975  36.848   8.418  1.00 15.39           O  
ANISOU 1739  O   HOH A1308     2102   2177   1568    221    -38   -356       O  
HETATM 1740  O   HOH A1309      45.923  21.928   7.589  1.00 42.77           O  
ANISOU 1740  O   HOH A1309     5852   5104   5293   -202   -570   -899       O  
HETATM 1741  O   HOH A1310      34.878  23.303  -0.051  1.00 32.26           O  
ANISOU 1741  O   HOH A1310     4519   3025   4713    524    724    234       O  
HETATM 1742  O   HOH A1311      13.769  37.610  19.371  1.00 31.62           O  
ANISOU 1742  O   HOH A1311     4348   3054   4611   1299   -825   -942       O  
HETATM 1743  O   HOH A1312      22.704  16.012  12.662  1.00 37.90           O  
ANISOU 1743  O   HOH A1312     7779   3030   3590    290   1264  -1233       O  
HETATM 1744  O   HOH A1313      44.642  32.978  24.326  1.00 34.43           O  
ANISOU 1744  O   HOH A1313     2991   5138   4951    841    647     48       O  
HETATM 1745  O   HOH A1314      43.119  24.270   9.372  1.00 28.78           O  
ANISOU 1745  O   HOH A1314     3499   3775   3658    -64   -509   -462       O  
HETATM 1746  O   HOH A1315      22.451  36.019  20.668  1.00 22.40           O  
ANISOU 1746  O   HOH A1315     2973   2949   2588   -618    754   -250       O  
HETATM 1747  O   HOH A1316      28.600  35.812   2.964  1.00 17.57           O  
ANISOU 1747  O   HOH A1316     2534   1887   2252   -123    138    444       O  
HETATM 1748  O   HOH A1317      33.107  18.564  13.765  1.00 17.56           O  
ANISOU 1748  O   HOH A1317     1421   2326   2925    370    669     21       O  
HETATM 1749  O   HOH A1318      26.425  19.750   9.549  1.00 39.08           O  
ANISOU 1749  O   HOH A1318     4618   5214   5014     56    834  -2297       O  
HETATM 1750  O   HOH A1319      33.522  18.357   4.079  1.00 44.77           O  
ANISOU 1750  O   HOH A1319     6330   4799   5881    991    168      1       O  
HETATM 1751  O   HOH A1320      22.063  41.553  21.585  1.00 47.19           O  
ANISOU 1751  O   HOH A1320     6058   4796   7072   -137    402    299       O  
HETATM 1752  O   HOH A1321      19.608  40.813  19.710  1.00 39.21           O  
ANISOU 1752  O   HOH A1321     5887   4626   4385   -641      2   -359       O  
HETATM 1753  O   HOH A1322      30.733  20.588  36.755  1.00 47.94           O  
ANISOU 1753  O   HOH A1322     5188   6224   6802    184    206     47       O  
HETATM 1754  O   HOH A1323      32.724  23.497  33.263  1.00 40.20           O  
ANISOU 1754  O   HOH A1323     5334   4929   5008   -208   -189   -143       O  
HETATM 1755  O   HOH A1324      20.727  21.038  40.272  1.00 36.61           O  
ANISOU 1755  O   HOH A1324     4855   4269   4785    755    725   -450       O  
HETATM 1756  O   HOH A1325      32.029  25.530  35.172  1.00 39.36           O  
ANISOU 1756  O   HOH A1325     4394   4484   6076   -332   -674   -747       O  
HETATM 1757  O   HOH A1326      40.751  22.044   4.169  1.00 43.23           O  
ANISOU 1757  O   HOH A1326     6176   5901   4347   -410   -577    137       O  
HETATM 1758  O   HOH A1327      35.055  30.170  31.704  1.00 38.05           O  
ANISOU 1758  O   HOH A1327     5614   5239   3603   1297  -1587    499       O  
HETATM 1759  O   HOH A1328      26.870  35.574  30.263  1.00 43.47           O  
ANISOU 1759  O   HOH A1328     5210   5791   5515     64   -389   -456       O  
HETATM 1760  O   HOH A1329      31.101  33.574  30.326  1.00 48.08           O  
ANISOU 1760  O   HOH A1329     7009   5814   5442    286   -127   -286       O  
HETATM 1761  O   HOH A1330      39.572  37.150  21.646  1.00 42.30           O  
ANISOU 1761  O   HOH A1330     6553   3087   6431   -318    118    469       O  
HETATM 1762  O   HOH A1331      46.762  22.551  10.702  1.00 40.74           O  
ANISOU 1762  O   HOH A1331     4384   5898   5194     13    884    845       O  
HETATM 1763  O   HOH A1332      35.775  17.843   5.329  1.00 44.19           O  
ANISOU 1763  O   HOH A1332     6412   5111   5266    132     34     53       O  
HETATM 1764  O   HOH A1333      22.630  37.426  18.479  1.00 44.32           O  
ANISOU 1764  O   HOH A1333     6025   4330   6482    120    216    456       O  
HETATM 1765  O   HOH B 504      20.059  32.352  23.522  1.00 13.80           O  
ANISOU 1765  O   HOH B 504     2205   1382   1654     97    215   -199       O  
HETATM 1766  O   HOH B 505      20.507  34.197  21.507  1.00 15.58           O  
ANISOU 1766  O   HOH B 505     2051   2003   1863     64     12    272       O  
HETATM 1767  O   HOH B 506      16.430  20.696  33.775  1.00 23.03           O  
ANISOU 1767  O   HOH B 506     2894   3631   2226   1097    912   1031       O  
HETATM 1768  O   HOH B 507       4.274  26.896  12.385  1.00 19.03           O  
ANISOU 1768  O   HOH B 507     2115   2300   2813   -105   -241    506       O  
HETATM 1769  O   HOH B 508       7.331  35.119  26.449  1.00 27.78           O  
ANISOU 1769  O   HOH B 508     1916   3439   5200    564    599   2096       O  
HETATM 1770  O   HOH B 509      18.250  34.775  19.403  1.00 19.66           O  
ANISOU 1770  O   HOH B 509     3078   2854   1537   -987   -147    459       O  
HETATM 1771  O   HOH B 510      11.226  38.582   5.803  1.00 16.85           O  
ANISOU 1771  O   HOH B 510     2428   2169   1805    427   -501   -352       O  
HETATM 1772  O   HOH B 511       7.083  21.848  32.909  1.00 21.68           O  
ANISOU 1772  O   HOH B 511     3430   3033   1772    680    652    353       O  
HETATM 1773  O   HOH B 512      18.309  15.699  19.458  1.00 22.14           O  
ANISOU 1773  O   HOH B 512     2786   3613   2012   1029    152    557       O  
HETATM 1774  O   HOH B 513      13.268  21.368  35.290  1.00 16.39           O  
ANISOU 1774  O   HOH B 513     2248   2271   1707      5    221    335       O  
HETATM 1775  O   HOH B 514      12.879  24.151  35.808  1.00 18.35           O  
ANISOU 1775  O   HOH B 514     2318   2532   2119    269   -233   -159       O  
HETATM 1776  O   HOH B 515      -2.282  25.216  21.978  1.00 21.48           O  
ANISOU 1776  O   HOH B 515     2665   2895   2598    502    469    248       O  
HETATM 1777  O   HOH B 516      14.238  34.890  26.221  1.00 24.98           O  
ANISOU 1777  O   HOH B 516     3612   3458   2418    103    -86   -857       O  
HETATM 1778  O   HOH B 517       5.459  23.896  32.088  1.00 21.41           O  
ANISOU 1778  O   HOH B 517     3376   3312   1445   1316    425    -74       O  
HETATM 1779  O   HOH B 518       7.728  29.685   7.373  1.00 16.96           O  
ANISOU 1779  O   HOH B 518     2202   2301   1937     90     56    491       O  
HETATM 1780  O   HOH B 519       9.015  29.148  34.883  1.00 43.32           O  
ANISOU 1780  O   HOH B 519     5159   6251   5049     22   -653    190       O  
HETATM 1781  O   HOH B 520      13.623  26.044  33.466  1.00 24.43           O  
ANISOU 1781  O   HOH B 520     2829   4366   2084    938    500    862       O  
HETATM 1782  O   HOH B 521      25.112   9.620  24.647  1.00 24.58           O  
ANISOU 1782  O   HOH B 521     3315   2355   3668    250    -82   -848       O  
HETATM 1783  O   HOH B 522      -0.061  25.407  27.096  1.00 22.33           O  
ANISOU 1783  O   HOH B 522     3494   2715   2275     11     71    305       O  
HETATM 1784  O   HOH B 523      10.236  22.555  12.067  1.00 21.91           O  
ANISOU 1784  O   HOH B 523     2677   2242   3403    -20   -329   -577       O  
HETATM 1785  O   HOH B 524       3.775  36.921  25.815  1.00 24.11           O  
ANISOU 1785  O   HOH B 524     3201   2669   3290    595    -69    130       O  
HETATM 1786  O   HOH B 525      -2.442  28.288  21.282  1.00 24.81           O  
ANISOU 1786  O   HOH B 525     2446   2824   4154   -142   1464   -501       O  
HETATM 1787  O   HOH B 526       8.878  34.461  21.070  1.00 26.92           O  
ANISOU 1787  O   HOH B 526     3729   3369   3130    236    759   -237       O  
HETATM 1788  O   HOH B 527       2.194  26.368   9.454  1.00 28.97           O  
ANISOU 1788  O   HOH B 527     4441   3240   3325    -18   -254    512       O  
HETATM 1789  O   HOH B 528      20.476  37.082   2.968  1.00 26.68           O  
ANISOU 1789  O   HOH B 528     3695   3941   2500    324    408    750       O  
HETATM 1790  O   HOH B 529      16.194  13.952  19.322  1.00 26.95           O  
ANISOU 1790  O   HOH B 529     3007   3901   3331    625   -472    -85       O  
HETATM 1791  O   HOH B 530      -7.964  25.545  18.326  1.00 23.85           O  
ANISOU 1791  O   HOH B 530     1852   2040   5167    187    181    722       O  
HETATM 1792  O   HOH B 531      20.049  15.903  12.263  1.00 23.87           O  
ANISOU 1792  O   HOH B 531     4650   2462   1956     93   -561   -664       O  
HETATM 1793  O   HOH B 532      12.163  20.807  10.967  1.00 26.82           O  
ANISOU 1793  O   HOH B 532     2793   3698   3698    358  -1144   -432       O  
HETATM 1794  O   HOH B 533       9.143  39.275   4.185  1.00 20.88           O  
ANISOU 1794  O   HOH B 533     2601   2708   2624    330   -607   -448       O  
HETATM 1795  O   HOH B 534      20.093   8.373  28.681  1.00 32.60           O  
ANISOU 1795  O   HOH B 534     3790   3875   4721    520   1145    750       O  
HETATM 1796  O   HOH B 535       6.030  20.723  11.805  1.00 30.51           O  
ANISOU 1796  O   HOH B 535     3332   4437   3822   -207  -1155   1504       O  
HETATM 1797  O   HOH B 536      15.739  14.859  14.844  1.00 22.41           O  
ANISOU 1797  O   HOH B 536     3274   2593   2645   -383   -540   -872       O  
HETATM 1798  O   HOH B 537       9.565  36.985  25.150  1.00 39.25           O  
ANISOU 1798  O   HOH B 537     5575   4020   5317    947    386   -560       O  
HETATM 1799  O   HOH B 538       9.010  23.208  34.209  1.00 35.10           O  
ANISOU 1799  O   HOH B 538     3560   5872   3902    -51   1652   -357       O  
HETATM 1800  O   HOH B 539      -2.501  43.372  15.143  1.00 27.05           O  
ANISOU 1800  O   HOH B 539     2521   3119   4635    768   -770    658       O  
HETATM 1801  O   HOH B 540      -0.804  39.254  20.807  1.00 30.39           O  
ANISOU 1801  O   HOH B 540     3340   4511   3693   2147     86   -457       O  
HETATM 1802  O   HOH B 541       2.375  18.404  22.966  1.00 34.98           O  
ANISOU 1802  O   HOH B 541     3201   2788   7300    640     71    611       O  
HETATM 1803  O   HOH B 542      14.905  20.464  11.029  1.00 32.13           O  
ANISOU 1803  O   HOH B 542     2431   4163   5613    560    -39    981       O  
HETATM 1804  O   HOH B 543       6.448  27.696   5.934  1.00 19.77           O  
ANISOU 1804  O   HOH B 543     3544   2230   1735    -11    -33    221       O  
HETATM 1805  O   HOH B 544       8.935  33.449  29.391  1.00 25.53           O  
ANISOU 1805  O   HOH B 544     3264   2747   3688    248   1075   -453       O  
HETATM 1806  O   HOH B 545       6.544  38.062   7.813  1.00 25.33           O  
ANISOU 1806  O   HOH B 545     3052   3176   3393    273  -1185   -305       O  
HETATM 1807  O   HOH B 546      16.565  12.122  21.874  1.00 29.60           O  
ANISOU 1807  O   HOH B 546     2969   2812   5462   -175   -181    604       O  
HETATM 1808  O   HOH B 547       4.396  13.392  17.438  1.00 37.27           O  
ANISOU 1808  O   HOH B 547     4239   3734   6186  -1381   -948    405       O  
HETATM 1809  O   HOH B 548       0.308  21.158  12.000  1.00 39.57           O  
ANISOU 1809  O   HOH B 548     5833   3704   5495    606   -618    568       O  
HETATM 1810  O   HOH B 549      -0.393  45.321  18.257  1.00 32.29           O  
ANISOU 1810  O   HOH B 549     4718   3652   3898   1594    196   -323       O  
HETATM 1811  O   HOH B 550      17.386  39.870  16.168  1.00 26.60           O  
ANISOU 1811  O   HOH B 550     3264   4994   1849    710   -779  -1094       O  
HETATM 1812  O   HOH B 551      -2.683  35.785  11.621  1.00 37.04           O  
ANISOU 1812  O   HOH B 551     4445   5690   3939  -1327   -441   1761       O  
HETATM 1813  O   HOH B 552      12.086  32.851  29.741  1.00 27.50           O  
ANISOU 1813  O   HOH B 552     4155   3559   2734    849    313    478       O  
HETATM 1814  O   HOH B 553      25.957  14.039  15.127  1.00 31.32           O  
ANISOU 1814  O   HOH B 553     3931   3865   4103    328     69    411       O  
HETATM 1815  O   HOH B 554      10.396  24.580   5.830  1.00 32.31           O  
ANISOU 1815  O   HOH B 554     5231   4091   2954   -252  -1555    539       O  
HETATM 1816  O   HOH B 555      -2.925  37.102  19.155  1.00 33.59           O  
ANISOU 1816  O   HOH B 555     4263   3511   4988   -185   1265   1023       O  
HETATM 1817  O   HOH B 556       4.351  24.868   8.774  1.00 28.02           O  
ANISOU 1817  O   HOH B 556     3617   3137   3892     75   -251    319       O  
HETATM 1818  O   HOH B 557       3.954  16.798  14.667  1.00 33.46           O  
ANISOU 1818  O   HOH B 557     3716   3692   5303  -1114   -225   -235       O  
HETATM 1819  O   HOH B 558      30.464  16.088  29.801  1.00 28.82           O  
ANISOU 1819  O   HOH B 558     4479   3861   2609    283   -166    714       O  
HETATM 1820  O   HOH B 559      20.575  10.240  27.056  1.00 33.54           O  
ANISOU 1820  O   HOH B 559     5838   3285   3618    982    377    506       O  
HETATM 1821  O   HOH B 560       9.556  41.810  21.114  1.00 38.40           O  
ANISOU 1821  O   HOH B 560     5335   5825   3429    141    558   -413       O  
HETATM 1822  O   HOH B 561      15.411  18.004  10.490  1.00 29.83           O  
ANISOU 1822  O   HOH B 561     3495   4219   3619   -530     19    -62       O  
HETATM 1823  O   HOH B 562       5.893  47.878  10.061  1.00 35.92           O  
ANISOU 1823  O   HOH B 562     4482   5504   3660   -247     12   -910       O  
HETATM 1824  O   HOH B 563      -2.201  28.661   8.649  1.00 29.85           O  
ANISOU 1824  O   HOH B 563     2088   5250   4004   -527   -306  -1032       O  
HETATM 1825  O   HOH B 564      -0.992  17.924  23.164  1.00 46.28           O  
ANISOU 1825  O   HOH B 564     4652   6199   6730    906  -1493    745       O  
HETATM 1826  O   HOH B 565       7.688  25.319   6.067  1.00 31.58           O  
ANISOU 1826  O   HOH B 565     3873   3629   4495     98   -553    844       O  
HETATM 1827  O   HOH B 566      13.615  43.441  17.686  1.00 42.24           O  
ANISOU 1827  O   HOH B 566     5342   6448   4259    229  -1367    918       O  
HETATM 1828  O   HOH B 567      21.217  36.675  16.069  1.00 29.55           O  
ANISOU 1828  O   HOH B 567     3379   4224   3624    241   -514    628       O  
HETATM 1829  O   HOH B 568      15.299  37.397  25.335  1.00 39.49           O  
ANISOU 1829  O   HOH B 568     5895   4269   4841    847    801   -306       O  
HETATM 1830  O   HOH B 569       9.672  39.413  21.198  1.00 34.96           O  
ANISOU 1830  O   HOH B 569     3726   4371   5186   -176    121   -637       O  
HETATM 1831  O   HOH B 570      13.360  13.966  14.676  1.00 40.67           O  
ANISOU 1831  O   HOH B 570     5473   3842   6135   -487    -96   -106       O  
HETATM 1832  O   HOH B 571      -2.420  19.334  14.090  1.00 32.17           O  
ANISOU 1832  O   HOH B 571     2791   3447   5985   -673  -1320   -617       O  
HETATM 1833  O   HOH B 572      18.414  10.500  25.086  1.00 28.06           O  
ANISOU 1833  O   HOH B 572     3579   2524   4556    361     -1    195       O  
HETATM 1834  O   HOH B 573       8.336  15.094  29.931  1.00 36.46           O  
ANISOU 1834  O   HOH B 573     4152   3893   5806   1305    727   -424       O  
HETATM 1835  O   HOH B 574      15.859  43.115  16.268  1.00 36.67           O  
ANISOU 1835  O   HOH B 574     3175   5961   4797   -488   -463    319       O  
HETATM 1836  O   HOH B 575      -3.998  33.357  26.145  1.00 40.72           O  
ANISOU 1836  O   HOH B 575     4712   5064   5694    558   1119   -242       O  
HETATM 1837  O   HOH B 576      -4.768  19.887  15.201  1.00 30.33           O  
ANISOU 1837  O   HOH B 576     3418   4355   3748  -1190     55     17       O  
HETATM 1838  O   HOH B 577       4.627  23.440  11.393  1.00 30.89           O  
ANISOU 1838  O   HOH B 577     3224   4353   4157    -53  -1529   -177       O  
HETATM 1839  O   HOH B 578      -0.745  18.321  12.691  1.00 43.86           O  
ANISOU 1839  O   HOH B 578     5823   6338   4504   -962     69   -417       O  
HETATM 1840  O   HOH B 579      13.539  38.539  23.395  1.00 38.02           O  
ANISOU 1840  O   HOH B 579     5086   4717   4641    113    565   -575       O  
HETATM 1841  O   HOH B 580       2.196  41.646  20.232  1.00 28.67           O  
ANISOU 1841  O   HOH B 580     4634   3081   3176    589    400     41       O  
HETATM 1842  O   HOH B 581      19.277  36.583  17.288  1.00 31.14           O  
ANISOU 1842  O   HOH B 581     4561   3572   3696   -442   -499    662       O  
HETATM 1843  O   HOH B 582       5.480  41.755  10.332  1.00 36.06           O  
ANISOU 1843  O   HOH B 582     4819   4098   4782    729     61   1129       O  
HETATM 1844  O  AHOH B 583      -6.758  25.612  15.632  0.50 35.22           O  
ANISOU 1844  O  AHOH B 583     4940   4199   4242     18   -796   -158       O  
HETATM 1845  O  BHOH B 583      43.882  26.857  16.886  0.50 27.44           O  
ANISOU 1845  O  BHOH B 583     3203   3375   3848   -591   -426    159       O  
HETATM 1846  O   HOH B 584      23.632  11.006  28.594  1.00 35.39           O  
ANISOU 1846  O   HOH B 584     5406   3736   4303    819    206   -760       O  
HETATM 1847  O   HOH B 585       3.731  27.861   6.408  1.00 31.19           O  
ANISOU 1847  O   HOH B 585     3431   4043   4373   -396    557  -1371       O  
HETATM 1848  O   HOH B 586      10.145  27.141  35.000  1.00 32.58           O  
ANISOU 1848  O   HOH B 586     3978   5681   2716    910    929   -157       O  
HETATM 1849  O   HOH B 587      16.466  38.778  20.376  1.00 39.28           O  
ANISOU 1849  O   HOH B 587     5254   5308   4361    470   -842   1218       O  
HETATM 1850  O   HOH B 588      24.244  18.394  35.194  1.00 36.68           O  
ANISOU 1850  O   HOH B 588     5152   5584   3198    409   -939    839       O  
HETATM 1851  O   HOH B 589       1.876  34.177  31.837  1.00 39.05           O  
ANISOU 1851  O   HOH B 589     5691   4368   4779     41    929   -252       O  
HETATM 1852  O   HOH B 590      14.237  15.403  20.359  1.00 31.39           O  
ANISOU 1852  O   HOH B 590     3039   3737   5148    -10   -711    804       O  
HETATM 1853  O   HOH B 591      -3.904  37.568  13.766  1.00 37.01           O  
ANISOU 1853  O   HOH B 591     6016   4724   3320   -310   -459    878       O  
HETATM 1854  O   HOH B 592      11.467  12.816  24.176  1.00 53.16           O  
ANISOU 1854  O   HOH B 592     6875   6280   7043   -252    247    360       O  
HETATM 1855  O   HOH B 593      30.886  18.101  33.805  1.00 41.22           O  
ANISOU 1855  O   HOH B 593     4524   6591   4545    497   -979    578       O  
HETATM 1856  O   HOH B 594       8.305  18.925  10.000  1.00 40.55           O  
ANISOU 1856  O   HOH B 594     4855   6205   4347   -470   -606   -770       O  
HETATM 1857  O   HOH B 595       0.608  42.091  23.682  1.00 41.95           O  
ANISOU 1857  O   HOH B 595     6257   4317   5364    437    169    368       O  
HETATM 1858  O   HOH B 596      -2.835  37.043  21.662  1.00 38.49           O  
ANISOU 1858  O   HOH B 596     4161   5365   5097    466    108   -423       O  
HETATM 1859  O   HOH B 597      31.877  14.104  28.088  1.00 42.77           O  
ANISOU 1859  O   HOH B 597     5466   4601   6184   1003   -900   -522       O  
HETATM 1860  O   HOH B 598      11.726  22.221   8.513  1.00 37.15           O  
ANISOU 1860  O   HOH B 598     5349   5190   3574   -264   -521   -222       O  
HETATM 1861  O   HOH B 599       4.009  38.970   8.409  1.00 36.03           O  
ANISOU 1861  O   HOH B 599     4655   5122   3913    152    385   -237       O  
HETATM 1862  O   HOH B 600      22.873  13.384  12.622  1.00 40.97           O  
ANISOU 1862  O   HOH B 600     7104   5648   2814    267   -711  -1293       O  
HETATM 1863  O   HOH B 601       8.981  14.232  17.795  1.00 44.16           O  
ANISOU 1863  O   HOH B 601     6358   4024   6395    721   -239    188       O  
HETATM 1864  O   HOH B 602      10.472  15.549  13.972  1.00 34.62           O  
ANISOU 1864  O   HOH B 602     4601   4959   3593   -586     83   -961       O  
HETATM 1865  O   HOH B 603       1.667  22.963  11.160  1.00 33.58           O  
ANISOU 1865  O   HOH B 603     4330   4668   3760    933   -390   -212       O  
HETATM 1866  O   HOH B 604       8.483  32.492  32.082  1.00 35.98           O  
ANISOU 1866  O   HOH B 604     5920   3923   3828    388   1780   -142       O  
HETATM 1867  O   HOH B 605      17.528  15.097  11.965  1.00 27.88           O  
ANISOU 1867  O   HOH B 605     4305   3876   2410   -431   -914   -667       O  
HETATM 1868  O   HOH B 606      13.150  44.978  20.881  1.00 40.24           O  
ANISOU 1868  O   HOH B 606     5280   4683   5324  -1207    -21    432       O  
HETATM 1869  O   HOH B 607       8.214  38.896  24.913  1.00 44.14           O  
ANISOU 1869  O   HOH B 607     5501   4960   6309    -21   -653   -411       O  
HETATM 1870  O   HOH B 608      16.031  27.056  32.040  1.00 19.14           O  
ANISOU 1870  O   HOH B 608     2437   3120   1716    691    430     18       O  
HETATM 1871  O   HOH B 609      10.056  30.638  32.854  1.00 28.43           O  
ANISOU 1871  O   HOH B 609     3406   4263   3130    440   1140   -332       O  
HETATM 1872  O   HOH B 610      18.547  11.703  22.884  1.00 31.79           O  
ANISOU 1872  O   HOH B 610     5336   2397   4342     48    133   -196       O  
HETATM 1873  O   HOH B 611       5.592  21.384   9.577  1.00 47.06           O  
ANISOU 1873  O   HOH B 611     5970   6075   5836   -223   -577   -450       O  
HETATM 1874  O   HOH B 612      -5.144  43.897  19.917  1.00 44.74           O  
ANISOU 1874  O   HOH B 612     5254   5646   6099     46    -10    212       O  
HETATM 1875  O   HOH B 613      19.313   8.939  32.071  1.00 41.91           O  
ANISOU 1875  O   HOH B 613     4338   5731   5853   1452   1344   -168       O  
HETATM 1876  O   HOH B 614      22.632  11.763  24.215  1.00 26.98           O  
ANISOU 1876  O   HOH B 614     5643   2113   2492   -930  -1142    670       O  
HETATM 1877  O   HOH B 615      11.544  12.328   9.955  1.00 41.90           O  
ANISOU 1877  O   HOH B 615     6118   3938   5862   -108     66   -107       O  
HETATM 1878  O   HOH B 616      12.874   8.983  11.202  1.00 38.70           O  
ANISOU 1878  O   HOH B 616     5156   4108   5439   -178    170   -396       O  
HETATM 1879  O   HOH B 617      -5.262  23.446  24.464  1.00 39.61           O  
ANISOU 1879  O   HOH B 617     4794   5790   4463   -407    411   -806       O  
HETATM 1880  O   HOH B 618      -3.348  30.127  18.634  1.00 25.99           O  
ANISOU 1880  O   HOH B 618     2940   3436   3497   -304     50    185       O  
HETATM 1881  O   HOH B 619      13.304  14.435  11.295  1.00 37.67           O  
ANISOU 1881  O   HOH B 619     4783   4676   4851    501   -278  -1021       O  
HETATM 1882  O   HOH B 620       9.200  22.233   8.943  1.00 39.37           O  
ANISOU 1882  O   HOH B 620     5001   3369   6587    112    -93   -651       O  
HETATM 1883  O   HOH B 621      -9.978  36.285  17.171  1.00 39.62           O  
ANISOU 1883  O   HOH B 621     5501   3915   5638   -572    611   -111       O  
HETATM 1884  O   HOH B 622       3.425  39.605  26.787  1.00 42.29           O  
ANISOU 1884  O   HOH B 622     6190   3995   5881    265   -402  -1043       O  
HETATM 1885  O   HOH B 623       6.931  43.326  23.857  1.00 46.08           O  
ANISOU 1885  O   HOH B 623     6081   4712   6714      9   -226   -328       O  
HETATM 1886  O   HOH B 624      19.394  23.793   7.557  1.00 36.05           O  
ANISOU 1886  O   HOH B 624     5358   4321   4015      7  -1187   1434       O  
HETATM 1887  O   HOH B 625      16.818  22.966   7.539  1.00 43.73           O  
ANISOU 1887  O   HOH B 625     5706   5875   5034    129   -232    564       O  
HETATM 1888  O   HOH B 626       1.926  16.063  21.899  1.00 49.70           O  
ANISOU 1888  O   HOH B 626     6715   6529   5638   -328    256   -269       O  
HETATM 1889  O   HOH B 627      13.147  40.781   5.590  1.00 37.44           O  
ANISOU 1889  O   HOH B 627     4743   5073   4409  -1260    344   1079       O  
HETATM 1890  O   HOH B 628      17.482  36.806  27.827  1.00 40.89           O  
ANISOU 1890  O   HOH B 628     8112   3503   3921   1512   -323  -1429       O  
HETATM 1891  O   HOH B 629       7.528  15.609  22.388  1.00 27.69           O  
ANISOU 1891  O   HOH B 629     3750   2732   4036   -102   1098    502       O  
CONECT 1568 1569 1570 1571 1572                                                 
CONECT 1569 1568                                                                
CONECT 1570 1568                                                                
CONECT 1571 1568                                                                
CONECT 1572 1568                                                                
CONECT 1573 1574 1575 1576 1577                                                 
CONECT 1574 1573                                                                
CONECT 1575 1573                                                                
CONECT 1576 1573                                                                
CONECT 1577 1573                                                                
CONECT 1578 1579 1580 1581 1582                                                 
CONECT 1579 1578                                                                
CONECT 1580 1578                                                                
CONECT 1581 1578                                                                
CONECT 1582 1578                                                                
CONECT 1583 1584                                                                
CONECT 1584 1583 1585 1589                                                      
CONECT 1585 1584 1586                                                           
CONECT 1586 1585 1587                                                           
CONECT 1587 1586 1588 1590                                                      
CONECT 1588 1587 1589                                                           
CONECT 1589 1584 1588                                                           
CONECT 1590 1587 1591 1592 1593                                                 
CONECT 1591 1590                                                                
CONECT 1592 1590                                                                
CONECT 1593 1590 1594 1598                                                      
CONECT 1594 1593 1595                                                           
CONECT 1595 1594 1596 1597                                                      
CONECT 1596 1595                                                                
CONECT 1597 1595                                                                
CONECT 1598 1593 1599                                                           
CONECT 1599 1598 1600 1601                                                      
CONECT 1600 1599                                                                
CONECT 1601 1599 1602 1614                                                      
CONECT 1602 1601 1603                                                           
CONECT 1603 1602 1604 1605                                                      
CONECT 1604 1603                                                                
CONECT 1605 1603 1606                                                           
CONECT 1606 1605 1607 1613                                                      
CONECT 1607 1606 1608                                                           
CONECT 1608 1607 1609                                                           
CONECT 1609 1608 1610 1613                                                      
CONECT 1610 1609 1611                                                           
CONECT 1611 1610 1612                                                           
CONECT 1612 1611 1613                                                           
CONECT 1613 1606 1609 1612                                                      
CONECT 1614 1601 1620                                                           
CONECT 1615 1616 1620                                                           
CONECT 1616 1615 1617                                                           
CONECT 1617 1616 1618                                                           
CONECT 1618 1617 1619                                                           
CONECT 1619 1618 1620                                                           
CONECT 1620 1614 1615 1619                                                      
CONECT 1621 1622 1623 1624 1625                                                 
CONECT 1622 1621                                                                
CONECT 1623 1621                                                                
CONECT 1624 1621                                                                
CONECT 1625 1621                                                                
CONECT 1626 1627 1628 1629 1630                                                 
CONECT 1627 1626                                                                
CONECT 1628 1626                                                                
CONECT 1629 1626                                                                
CONECT 1630 1626                                                                
MASTER      362    0    6    2   20    0   15    6 1818    2   63   16          
END                                                                             



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