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***  TRANSCRIPTION/DNA 28-SEP-94 1YTB  ***

elNémo ID: 22100322100925783

Job options:

ID        	=	 22100322100925783
JOBID     	=	 TRANSCRIPTION/DNA 28-SEP-94 1YTB
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    TRANSCRIPTION/DNA                       28-SEP-94   1YTB              
TITLE     CRYSTAL STRUCTURE OF A YEAST TBP/TATA-BOX COMPLEX                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA (29MER);                                               
COMPND   3 CHAIN: C, D;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: PROTEIN (TATA BINDING PROTEIN (TBP));                      
COMPND   7 CHAIN: A, B;                                                         
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 SYNTHETIC: YES;                                                      
SOURCE   3 MOL_ID: 2;                                                           
SOURCE   4 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   5 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   6 ORGANISM_TAXID: 4932;                                                
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PROTEIN-DNA COMPLEX, TRANSCRIPTION/DNA COMPLEX                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.KIM,J.H.GEIGER,S.HAHN,P.B.SIGLER                                    
REVDAT   2   24-FEB-09 1YTB    1       VERSN                                    
REVDAT   1   26-JAN-95 1YTB    0                                                
JRNL        AUTH   Y.KIM,J.H.GEIGER,S.HAHN,P.B.SIGLER                           
JRNL        TITL   CRYSTAL STRUCTURE OF A YEAST TBP/TATA-BOX COMPLEX.           
JRNL        REF    NATURE                        V. 365   512 1993              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   8413604                                                      
JRNL        DOI    10.1038/365512A0                                             
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 86.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 51009                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.201                           
REMARK   3   FREE R VALUE                     : 0.261                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2832                                    
REMARK   3   NUCLEIC ACID ATOMS       : 1194                                    
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 513                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.30                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.015                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.56                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 31.20                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.38                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1YTB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 7.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : XENTRONICS                         
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 59705                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.50, VAPOR DIFFUSION, HANGING        
REMARK 280  DROP, TEMPERATURE 295.00K                                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y,X,Z+3/4                                              
REMARK 290       4555   Y,-X,Z+1/4                                              
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       33.25000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       49.87500            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       16.62500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK:                                                              
REMARK 300 MTRIX                                                                
REMARK 300  THE TRANSFORMATIONS PRESENTED ON MTRIX RECORDS BELOW                
REMARK 300  DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG THE               
REMARK 300  VARIOUS DOMAINS IN THIS ENTRY.  APPLYING THE APPROPRIATE            
REMARK 300  MTRIX TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL              
REMARK 300  YIELD APPROXIMATE COORDINATES FOR THE RESIDUES LISTED               
REMARK 300  SECOND.                                                             
REMARK 300                                                                      
REMARK 300            APPLIED TO          TRANSFORMED TO                        
REMARK 300  MTRIX   CHAIN  RESIDUES       CHAIN  RESIDUES     RMSD              
REMARK 300    M1   A   61  -  A  240     B   61  -  B  240    0.445             
REMARK 300    M1   C    1  -  C   29     D    1  -  D   29    1.571             
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 APPLY THE FOLLOWING TO CHAINS: C, A                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, 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 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     DA C   3   N9     DA C   3   C4      0.044                       
REMARK 500     DA C   5   N3     DA C   5   C4      0.040                       
REMARK 500     DT C   6   O4'    DT C   6   C1'     0.069                       
REMARK 500     DA C   9   N3     DA C   9   C4      0.040                       
REMARK 500     DA C   9   C5     DA C   9   N7      0.038                       
REMARK 500     DG C  16   C5     DG C  16   N7      0.046                       
REMARK 500     DC C  18   P      DC C  18   O5'     0.063                       
REMARK 500     DC C  18   C5     DC C  18   C6      0.057                       
REMARK 500     DT C  20   N1     DT C  20   C2      0.056                       
REMARK 500     DT C  21   P      DT C  21   O5'    -0.060                       
REMARK 500     DT C  23   C6     DT C  23   N1     -0.054                       
REMARK 500     DA C  24   O4'    DA C  24   C1'     0.067                       
REMARK 500     DT C  25   N1     DT C  25   C2      0.059                       
REMARK 500     DA C  26   O4'    DA C  26   C1'     0.066                       
REMARK 500     DC C  29   O4'    DC C  29   C4'    -0.065                       
REMARK 500     DT D   6   N1     DT D   6   C2      0.062                       
REMARK 500     DA D  10   N9     DA D  10   C4      0.037                       
REMARK 500     DC D  11   C5     DC D  11   C6      0.048                       
REMARK 500     DG D  16   O4'    DG D  16   C1'     0.069                       
REMARK 500     DT D  20   N1     DT D  20   C2      0.085                       
REMARK 500     DT D  20   C4     DT D  20   C5      0.055                       
REMARK 500     DT D  21   N1     DT D  21   C2      0.053                       
REMARK 500     DT D  21   C4     DT D  21   C5      0.054                       
REMARK 500     DT D  22   N1     DT D  22   C2      0.055                       
REMARK 500     DA D  24   C4     DA D  24   C5     -0.043                       
REMARK 500     DT D  25   N1     DT D  25   C2      0.059                       
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     DA C   3   C4' -  C3' -  C2' ANGL. DEV. =   5.4 DEGREES          
REMARK 500     DC C  18   O4' -  C1' -  N1  ANGL. DEV. =   1.9 DEGREES          
REMARK 500     DA C  28   C3' -  C2' -  C1' ANGL. DEV. =  -4.9 DEGREES          
REMARK 500     DC C  29   C1' -  O4' -  C4' ANGL. DEV. =  -6.1 DEGREES          
REMARK 500     DA D   3   C4' -  C3' -  C2' ANGL. DEV. =   5.4 DEGREES          
REMARK 500     DG D  13   C3' -  C2' -  C1' ANGL. DEV. =  -4.9 DEGREES          
REMARK 500     DC D  18   C3' -  C2' -  C1' ANGL. DEV. =  -5.8 DEGREES          
REMARK 500     DA D  24   C4' -  C3' -  C2' ANGL. DEV. =   5.4 DEGREES          
REMARK 500     DA D  24   O4' -  C1' -  C2' ANGL. DEV. =   3.6 DEGREES          
REMARK 500     DT D  27   C4  -  C5  -  C6  ANGL. DEV. =   3.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TYR A  94      106.14   -162.66                                   
REMARK 500    PHE B  99      136.28   -170.08                                   
REMARK 500    ALA B 100       45.54    -86.19                                   
REMARK 500    LYS B 167      -21.95     75.32                                   
REMARK 500    PHE B 237       32.06    -92.07                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500     DT C   6         0.06    SIDE_CHAIN                              
REMARK 500     DA C   7         0.06    SIDE_CHAIN                              
REMARK 500     DA C   8         0.05    SIDE_CHAIN                              
REMARK 500     DT C  22         0.06    SIDE_CHAIN                              
REMARK 500     DT C  27         0.06    SIDE_CHAIN                              
REMARK 500     DA D   3         0.08    SIDE_CHAIN                              
REMARK 500     DG D  13         0.09    SIDE_CHAIN                              
REMARK 500     DG D  16         0.05    SIDE_CHAIN                              
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 C 373        DISTANCE =  5.82 ANGSTROMS                       
REMARK 525    HOH B 608        DISTANCE =  5.30 ANGSTROMS                       
REMARK 525    HOH C 458        DISTANCE =  7.91 ANGSTROMS                       
REMARK 525    HOH C 482        DISTANCE =  6.27 ANGSTROMS                       
DBREF  1YTB A   61   240  UNP    P13393   TBP_YEAST       60    239             
DBREF  1YTB B   61   240  UNP    P13393   TBP_YEAST       60    239             
DBREF  1YTB C    1    29  PDB    1YTB     1YTB             1     29             
DBREF  1YTB D    1    29  PDB    1YTB     1YTB             1     29             
SEQRES   1 C   29   DG  DT  DA  DT  DA  DT  DA  DA  DA  DA  DC  DG  DG          
SEQRES   2 C   29   DG  DT  DG  DG  DC  DG  DT  DT  DT  DT  DA  DT  DA          
SEQRES   3 C   29   DT  DA  DC                                                  
SEQRES   1 D   29   DG  DT  DA  DT  DA  DT  DA  DA  DA  DA  DC  DG  DG          
SEQRES   2 D   29   DG  DT  DG  DG  DC  DG  DT  DT  DT  DT  DA  DT  DA          
SEQRES   3 D   29   DT  DA  DC                                                  
SEQRES   1 A  180  SER GLY ILE VAL PRO THR LEU GLN ASN ILE VAL ALA THR          
SEQRES   2 A  180  VAL THR LEU GLY CYS ARG LEU ASP LEU LYS THR VAL ALA          
SEQRES   3 A  180  LEU HIS ALA ARG ASN ALA GLU TYR ASN PRO LYS ARG PHE          
SEQRES   4 A  180  ALA ALA VAL ILE MET ARG ILE ARG GLU PRO LYS THR THR          
SEQRES   5 A  180  ALA LEU ILE PHE ALA SER GLY LYS MET VAL VAL THR GLY          
SEQRES   6 A  180  ALA LYS SER GLU ASP ASP SER LYS LEU ALA SER ARG LYS          
SEQRES   7 A  180  TYR ALA ARG ILE ILE GLN LYS ILE GLY PHE ALA ALA LYS          
SEQRES   8 A  180  PHE THR ASP PHE LYS ILE GLN ASN ILE VAL GLY SER CYS          
SEQRES   9 A  180  ASP VAL LYS PHE PRO ILE ARG LEU GLU GLY LEU ALA PHE          
SEQRES  10 A  180  SER HIS GLY THR PHE SER SER TYR GLU PRO GLU LEU PHE          
SEQRES  11 A  180  PRO GLY LEU ILE TYR ARG MET VAL LYS PRO LYS ILE VAL          
SEQRES  12 A  180  LEU LEU ILE PHE VAL SER GLY LYS ILE VAL LEU THR GLY          
SEQRES  13 A  180  ALA LYS GLN ARG GLU GLU ILE TYR GLN ALA PHE GLU ALA          
SEQRES  14 A  180  ILE TYR PRO VAL LEU SER GLU PHE ARG LYS MET                  
SEQRES   1 B  180  SER GLY ILE VAL PRO THR LEU GLN ASN ILE VAL ALA THR          
SEQRES   2 B  180  VAL THR LEU GLY CYS ARG LEU ASP LEU LYS THR VAL ALA          
SEQRES   3 B  180  LEU HIS ALA ARG ASN ALA GLU TYR ASN PRO LYS ARG PHE          
SEQRES   4 B  180  ALA ALA VAL ILE MET ARG ILE ARG GLU PRO LYS THR THR          
SEQRES   5 B  180  ALA LEU ILE PHE ALA SER GLY LYS MET VAL VAL THR GLY          
SEQRES   6 B  180  ALA LYS SER GLU ASP ASP SER LYS LEU ALA SER ARG LYS          
SEQRES   7 B  180  TYR ALA ARG ILE ILE GLN LYS ILE GLY PHE ALA ALA LYS          
SEQRES   8 B  180  PHE THR ASP PHE LYS ILE GLN ASN ILE VAL GLY SER CYS          
SEQRES   9 B  180  ASP VAL LYS PHE PRO ILE ARG LEU GLU GLY LEU ALA PHE          
SEQRES  10 B  180  SER HIS GLY THR PHE SER SER TYR GLU PRO GLU LEU PHE          
SEQRES  11 B  180  PRO GLY LEU ILE TYR ARG MET VAL LYS PRO LYS ILE VAL          
SEQRES  12 B  180  LEU LEU ILE PHE VAL SER GLY LYS ILE VAL LEU THR GLY          
SEQRES  13 B  180  ALA LYS GLN ARG GLU GLU ILE TYR GLN ALA PHE GLU ALA          
SEQRES  14 B  180  ILE TYR PRO VAL LEU SER GLU PHE ARG LYS MET                  
FORMUL   5  HOH   *513(H2 O)                                                    
HELIX    1  A1 ASP A   81  ALA A   89  1                                   9    
HELIX    2  A2 SER A  128  GLY A  147  1                                  20    
HELIX    3  A3 ARG A  171  HIS A  179  1                                   9    
HELIX    4  A4 ARG A  220  PHE A  237  1                                  18    
HELIX    5  B1 ASP B   81  ALA B   89  1                                   9    
HELIX    6  B2 SER B  128  GLY B  147  1                                  20    
HELIX    7  B3 ARG B  171  HIS B  179  1                                   9    
HELIX    8  B4 ARG B  220  PHE B  237  1                                  18    
SHEET    1 SH110 ASN A  91  TYR A  94  0                                        
SHEET    2 SH110 VAL A 102  ILE A 106 -1  N  ARG A 105   O  ASN A  91           
SHEET    3 SH110 THR A 111  PHE A 116 -1  N  ALA A 113   O  MET A 104           
SHEET    4 SH110 LYS A 120  GLY A 125 -1  N  THR A 124   O  THR A 112           
SHEET    5 SH110 PRO A  65  LEU A  76 -1  N  ALA A  72   O  VAL A 123           
SHEET    6 SH110 THR A 153  VAL A 166 -1  O  VAL A 161   N  ASN A  69           
SHEET    7 SH110 LYS A 211  ALA A 217 -1  O  LEU A 214   N  GLY A 162           
SHEET    8 SH110 ILE A 202  PHE A 207 -1  O  LEU A 205   N  THR A 215           
SHEET    9 SH110 LEU A 193  MET A 197 -1  O  TYR A 195   N  LEU A 204           
SHEET   10 SH110 PHE A 182  TYR A 185 -1  O  SER A 184   N  ILE A 194           
SHEET    1 SH210 ASN B  91  TYR B  94  0                                        
SHEET    2 SH210 VAL B 102  ILE B 106 -1  N  ARG B 105   O  ASN B  91           
SHEET    3 SH210 THR B 111  PHE B 116 -1  N  ALA B 113   O  MET B 104           
SHEET    4 SH210 LYS B 120  GLY B 125 -1  N  THR B 124   O  THR B 112           
SHEET    5 SH210 PRO B  65  LEU B  76 -1  N  ALA B  72   O  VAL B 123           
SHEET    6 SH210 THR B 153  VAL B 166 -1  O  VAL B 161   N  ASN B  69           
SHEET    7 SH210 LYS B 211  ALA B 217 -1  O  LEU B 214   N  GLY B 162           
SHEET    8 SH210 ILE B 202  PHE B 207 -1  O  LEU B 205   N  THR B 215           
SHEET    9 SH210 LEU B 193  MET B 197 -1  O  TYR B 195   N  LEU B 204           
SHEET   10 SH210 PHE B 182  TYR B 185 -1  O  SER B 184   N  ILE B 194           
CISPEP   1 GLU A  108    PRO A  109          0        -0.61                     
CISPEP   2 LYS A  199    PRO A  200          0        -1.33                     
CISPEP   3 GLU B  108    PRO B  109          0        -0.03                     
CISPEP   4 LYS B  199    PRO B  200          0        -0.41                     
CRYST1  100.770  100.770   66.500  90.00  90.00  90.00 P 43          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      0.009924  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009924  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015038        0.00000                         
MTRIX1   1 -0.063190 -0.997700  0.023700       49.65000    1                    
MTRIX2   1 -0.993900  0.060770 -0.091690       55.11000    1                    
MTRIX3   1  0.090040 -0.029350 -0.995500       66.59000    1                    
ATOM   1197  N   SER A  61      44.411  49.565  60.147  1.00 66.54           N  
ATOM   1198  CA  SER A  61      43.596  48.411  59.649  1.00 64.83           C  
ATOM   1199  C   SER A  61      44.211  47.102  60.179  1.00 64.23           C  
ATOM   1200  O   SER A  61      44.527  46.998  61.369  1.00 64.08           O  
ATOM   1201  CB  SER A  61      43.512  48.429  58.104  1.00 64.27           C  
ATOM   1202  OG  SER A  61      42.344  47.773  57.633  1.00 61.59           O  
ATOM   1203  N   GLY A  62      44.425  46.136  59.289  1.00 62.42           N  
ATOM   1204  CA  GLY A  62      44.973  44.856  59.695  1.00 60.03           C  
ATOM   1205  C   GLY A  62      43.896  43.784  59.684  1.00 57.67           C  
ATOM   1206  O   GLY A  62      44.185  42.580  59.668  1.00 58.56           O  
ATOM   1207  N   ILE A  63      42.645  44.235  59.672  1.00 52.62           N  
ATOM   1208  CA  ILE A  63      41.499  43.343  59.680  1.00 48.19           C  
ATOM   1209  C   ILE A  63      41.208  42.866  58.274  1.00 44.74           C  
ATOM   1210  O   ILE A  63      41.335  43.625  57.322  1.00 43.06           O  
ATOM   1211  CB  ILE A  63      40.231  44.026  60.230  1.00 50.40           C  
ATOM   1212  CG1 ILE A  63      40.536  44.771  61.535  1.00 51.36           C  
ATOM   1213  CG2 ILE A  63      39.155  42.984  60.465  1.00 50.57           C  
ATOM   1214  CD1 ILE A  63      40.646  46.278  61.369  1.00 53.14           C  
ATOM   1215  N   VAL A  64      40.880  41.583  58.168  1.00 41.50           N  
ATOM   1216  CA  VAL A  64      40.549  40.932  56.908  1.00 38.47           C  
ATOM   1217  C   VAL A  64      39.266  40.182  57.256  1.00 35.95           C  
ATOM   1218  O   VAL A  64      39.219  39.522  58.295  1.00 38.72           O  
ATOM   1219  CB  VAL A  64      41.619  39.904  56.497  1.00 37.28           C  
ATOM   1220  CG1 VAL A  64      41.384  39.456  55.081  1.00 40.01           C  
ATOM   1221  CG2 VAL A  64      43.001  40.494  56.627  1.00 37.00           C  
ATOM   1222  N   PRO A  65      38.212  40.279  56.418  1.00 32.09           N  
ATOM   1223  CA  PRO A  65      36.947  39.587  56.714  1.00 31.12           C  
ATOM   1224  C   PRO A  65      37.008  38.050  56.767  1.00 30.93           C  
ATOM   1225  O   PRO A  65      37.755  37.433  56.017  1.00 32.74           O  
ATOM   1226  CB  PRO A  65      36.021  40.067  55.581  1.00 29.67           C  
ATOM   1227  CG  PRO A  65      36.591  41.366  55.180  1.00 28.37           C  
ATOM   1228  CD  PRO A  65      38.073  41.091  55.199  1.00 30.24           C  
ATOM   1229  N   THR A  66      36.208  37.444  57.639  1.00 28.03           N  
ATOM   1230  CA  THR A  66      36.153  35.996  57.756  1.00 29.28           C  
ATOM   1231  C   THR A  66      34.956  35.480  56.954  1.00 28.63           C  
ATOM   1232  O   THR A  66      33.856  36.017  57.073  1.00 28.97           O  
ATOM   1233  CB  THR A  66      35.946  35.588  59.210  1.00 31.88           C  
ATOM   1234  OG1 THR A  66      36.850  36.320  60.039  1.00 39.07           O  
ATOM   1235  CG2 THR A  66      36.177  34.086  59.400  1.00 30.74           C  
ATOM   1236  N   LEU A  67      35.146  34.436  56.151  1.00 27.00           N  
ATOM   1237  CA  LEU A  67      34.027  33.899  55.389  1.00 27.43           C  
ATOM   1238  C   LEU A  67      33.155  33.083  56.359  1.00 27.85           C  
ATOM   1239  O   LEU A  67      33.669  32.399  57.244  1.00 26.35           O  
ATOM   1240  CB  LEU A  67      34.504  33.103  54.166  1.00 25.72           C  
ATOM   1241  CG  LEU A  67      35.372  33.851  53.128  1.00 25.30           C  
ATOM   1242  CD1 LEU A  67      35.516  33.027  51.845  1.00 24.27           C  
ATOM   1243  CD2 LEU A  67      34.791  35.231  52.776  1.00 23.97           C  
ATOM   1244  N   GLN A  68      31.835  33.239  56.236  1.00 28.49           N  
ATOM   1245  CA  GLN A  68      30.879  32.589  57.135  1.00 25.33           C  
ATOM   1246  C   GLN A  68      29.926  31.596  56.510  1.00 22.97           C  
ATOM   1247  O   GLN A  68      29.443  30.718  57.215  1.00 23.15           O  
ATOM   1248  CB  GLN A  68      30.039  33.645  57.868  1.00 24.05           C  
ATOM   1249  CG  GLN A  68      30.840  34.640  58.667  1.00 27.75           C  
ATOM   1250  CD  GLN A  68      31.618  34.016  59.836  1.00 30.63           C  
ATOM   1251  OE1 GLN A  68      31.319  32.917  60.307  1.00 32.61           O  
ATOM   1252  NE2 GLN A  68      32.585  34.773  60.354  1.00 29.56           N  
ATOM   1253  N   ASN A  69      29.600  31.777  55.231  1.00 23.12           N  
ATOM   1254  CA  ASN A  69      28.688  30.876  54.547  1.00 21.94           C  
ATOM   1255  C   ASN A  69      28.874  30.968  53.044  1.00 25.22           C  
ATOM   1256  O   ASN A  69      29.008  32.065  52.502  1.00 26.48           O  
ATOM   1257  CB  ASN A  69      27.229  31.209  54.923  1.00 23.53           C  
ATOM   1258  CG  ASN A  69      26.189  30.278  54.246  1.00 24.19           C  
ATOM   1259  OD1 ASN A  69      26.364  29.064  54.175  1.00 25.04           O  
ATOM   1260  ND2 ASN A  69      25.079  30.866  53.781  1.00 25.11           N  
ATOM   1261  N   ILE A  70      28.890  29.813  52.379  1.00 26.08           N  
ATOM   1262  CA  ILE A  70      29.035  29.722  50.922  1.00 23.66           C  
ATOM   1263  C   ILE A  70      27.864  28.896  50.381  1.00 22.92           C  
ATOM   1264  O   ILE A  70      27.609  27.802  50.882  1.00 21.81           O  
ATOM   1265  CB  ILE A  70      30.366  29.046  50.530  1.00 23.44           C  
ATOM   1266  CG1 ILE A  70      31.531  29.780  51.205  1.00 28.28           C  
ATOM   1267  CG2 ILE A  70      30.507  28.988  49.033  1.00 23.68           C  
ATOM   1268  CD1 ILE A  70      32.563  30.327  50.281  1.00 30.77           C  
ATOM   1269  N   VAL A  71      27.157  29.436  49.386  1.00 21.72           N  
ATOM   1270  CA  VAL A  71      25.990  28.788  48.770  1.00 22.94           C  
ATOM   1271  C   VAL A  71      26.334  28.392  47.347  1.00 24.96           C  
ATOM   1272  O   VAL A  71      26.774  29.253  46.582  1.00 24.94           O  
ATOM   1273  CB  VAL A  71      24.780  29.777  48.712  1.00 23.79           C  
ATOM   1274  CG1 VAL A  71      23.546  29.140  48.029  1.00 21.65           C  
ATOM   1275  CG2 VAL A  71      24.467  30.282  50.125  1.00 20.75           C  
ATOM   1276  N   ALA A  72      26.105  27.133  46.963  1.00 23.67           N  
ATOM   1277  CA  ALA A  72      26.447  26.707  45.605  1.00 24.23           C  
ATOM   1278  C   ALA A  72      25.383  25.872  44.921  1.00 24.57           C  
ATOM   1279  O   ALA A  72      24.492  25.327  45.582  1.00 23.64           O  
ATOM   1280  CB  ALA A  72      27.767  25.938  45.604  1.00 23.73           C  
ATOM   1281  N   THR A  73      25.437  25.812  43.595  1.00 22.63           N  
ATOM   1282  CA  THR A  73      24.484  25.004  42.846  1.00 25.27           C  
ATOM   1283  C   THR A  73      25.210  23.912  42.041  1.00 24.74           C  
ATOM   1284  O   THR A  73      26.360  24.080  41.640  1.00 24.13           O  
ATOM   1285  CB  THR A  73      23.629  25.873  41.898  1.00 25.29           C  
ATOM   1286  OG1 THR A  73      24.468  26.774  41.155  1.00 24.03           O  
ATOM   1287  CG2 THR A  73      22.624  26.648  42.715  1.00 26.10           C  
ATOM   1288  N   VAL A  74      24.551  22.772  41.876  1.00 25.75           N  
ATOM   1289  CA  VAL A  74      25.125  21.634  41.162  1.00 24.68           C  
ATOM   1290  C   VAL A  74      24.025  20.941  40.349  1.00 26.29           C  
ATOM   1291  O   VAL A  74      22.897  20.751  40.825  1.00 28.09           O  
ATOM   1292  CB  VAL A  74      25.696  20.584  42.136  1.00 22.93           C  
ATOM   1293  CG1 VAL A  74      26.262  19.412  41.370  1.00 29.03           C  
ATOM   1294  CG2 VAL A  74      26.769  21.176  42.972  1.00 24.82           C  
ATOM   1295  N   THR A  75      24.345  20.556  39.121  1.00 26.97           N  
ATOM   1296  CA  THR A  75      23.375  19.869  38.286  1.00 27.59           C  
ATOM   1297  C   THR A  75      23.759  18.401  38.315  1.00 29.38           C  
ATOM   1298  O   THR A  75      24.897  18.066  38.011  1.00 30.65           O  
ATOM   1299  CB  THR A  75      23.395  20.407  36.829  1.00 27.76           C  
ATOM   1300  OG1 THR A  75      23.048  21.812  36.818  1.00 30.38           O  
ATOM   1301  CG2 THR A  75      22.401  19.641  35.956  1.00 25.60           C  
ATOM   1302  N   LEU A  76      22.843  17.546  38.773  1.00 31.34           N  
ATOM   1303  CA  LEU A  76      23.093  16.098  38.839  1.00 30.79           C  
ATOM   1304  C   LEU A  76      22.826  15.444  37.477  1.00 33.04           C  
ATOM   1305  O   LEU A  76      23.302  14.341  37.197  1.00 35.77           O  
ATOM   1306  CB  LEU A  76      22.269  15.419  39.944  1.00 28.89           C  
ATOM   1307  CG  LEU A  76      22.627  15.841  41.384  1.00 29.34           C  
ATOM   1308  CD1 LEU A  76      21.742  15.142  42.404  1.00 27.58           C  
ATOM   1309  CD2 LEU A  76      24.069  15.575  41.672  1.00 28.17           C  
ATOM   1310  N   GLY A  77      22.026  16.102  36.647  1.00 32.76           N  
ATOM   1311  CA  GLY A  77      21.753  15.601  35.310  1.00 33.02           C  
ATOM   1312  C   GLY A  77      20.706  14.537  35.087  1.00 34.58           C  
ATOM   1313  O   GLY A  77      20.489  14.124  33.931  1.00 35.73           O  
ATOM   1314  N   CYS A  78      20.053  14.091  36.152  1.00 33.42           N  
ATOM   1315  CA  CYS A  78      19.028  13.075  36.006  1.00 34.88           C  
ATOM   1316  C   CYS A  78      17.907  13.339  36.993  1.00 35.56           C  
ATOM   1317  O   CYS A  78      18.104  14.001  38.005  1.00 36.64           O  
ATOM   1318  CB  CYS A  78      19.592  11.684  36.272  1.00 34.61           C  
ATOM   1319  SG  CYS A  78      19.963  11.388  37.998  1.00 36.00           S  
ATOM   1320  N   ARG A  79      16.730  12.817  36.688  1.00 34.99           N  
ATOM   1321  CA  ARG A  79      15.566  12.975  37.541  1.00 36.07           C  
ATOM   1322  C   ARG A  79      15.712  12.086  38.758  1.00 35.59           C  
ATOM   1323  O   ARG A  79      16.282  10.990  38.687  1.00 35.73           O  
ATOM   1324  CB  ARG A  79      14.316  12.575  36.776  1.00 37.28           C  
ATOM   1325  CG  ARG A  79      13.701  13.690  35.995  1.00 42.13           C  
ATOM   1326  CD  ARG A  79      12.447  14.047  36.684  1.00 44.96           C  
ATOM   1327  NE  ARG A  79      12.186  15.460  36.543  1.00 48.06           N  
ATOM   1328  CZ  ARG A  79      11.318  16.129  37.288  1.00 47.82           C  
ATOM   1329  NH1 ARG A  79      10.616  15.509  38.238  1.00 44.45           N  
ATOM   1330  NH2 ARG A  79      11.150  17.423  37.069  1.00 49.54           N  
ATOM   1331  N   LEU A  80      15.166  12.544  39.872  1.00 34.61           N  
ATOM   1332  CA  LEU A  80      15.254  11.788  41.116  1.00 36.00           C  
ATOM   1333  C   LEU A  80      13.902  11.481  41.743  1.00 37.76           C  
ATOM   1334  O   LEU A  80      12.952  12.276  41.620  1.00 38.97           O  
ATOM   1335  CB  LEU A  80      16.065  12.557  42.158  1.00 34.29           C  
ATOM   1336  CG  LEU A  80      17.424  13.091  41.727  1.00 34.03           C  
ATOM   1337  CD1 LEU A  80      18.068  13.789  42.881  1.00 33.58           C  
ATOM   1338  CD2 LEU A  80      18.311  11.950  41.245  1.00 37.93           C  
ATOM   1339  N   ASP A  81      13.831  10.315  42.402  1.00 36.93           N  
ATOM   1340  CA  ASP A  81      12.626   9.932  43.133  1.00 37.28           C  
ATOM   1341  C   ASP A  81      12.940  10.316  44.564  1.00 35.11           C  
ATOM   1342  O   ASP A  81      13.715   9.630  45.258  1.00 31.23           O  
ATOM   1343  CB  ASP A  81      12.287   8.451  43.066  1.00 39.61           C  
ATOM   1344  CG  ASP A  81      10.916   8.162  43.656  1.00 43.06           C  
ATOM   1345  OD1 ASP A  81      10.809   7.977  44.894  1.00 42.06           O  
ATOM   1346  OD2 ASP A  81       9.933   8.195  42.886  1.00 46.37           O  
ATOM   1347  N   LEU A  82      12.334  11.420  44.996  1.00 33.63           N  
ATOM   1348  CA  LEU A  82      12.585  11.968  46.317  1.00 34.26           C  
ATOM   1349  C   LEU A  82      12.268  11.098  47.514  1.00 33.76           C  
ATOM   1350  O   LEU A  82      12.958  11.186  48.537  1.00 31.82           O  
ATOM   1351  CB  LEU A  82      11.980  13.365  46.442  1.00 32.76           C  
ATOM   1352  CG  LEU A  82      12.540  14.412  45.469  1.00 31.51           C  
ATOM   1353  CD1 LEU A  82      11.995  15.779  45.876  1.00 32.61           C  
ATOM   1354  CD2 LEU A  82      14.064  14.427  45.443  1.00 28.73           C  
ATOM   1355  N   LYS A  83      11.241  10.260  47.412  1.00 36.64           N  
ATOM   1356  CA  LYS A  83      10.908   9.385  48.532  1.00 40.06           C  
ATOM   1357  C   LYS A  83      12.051   8.370  48.683  1.00 39.96           C  
ATOM   1358  O   LYS A  83      12.485   8.034  49.804  1.00 40.00           O  
ATOM   1359  CB  LYS A  83       9.588   8.658  48.286  1.00 43.82           C  
ATOM   1360  CG  LYS A  83       8.371   9.557  48.221  1.00 47.84           C  
ATOM   1361  CD  LYS A  83       7.900  10.010  49.601  1.00 52.60           C  
ATOM   1362  CE  LYS A  83       6.683  10.943  49.467  1.00 55.19           C  
ATOM   1363  NZ  LYS A  83       6.165  11.474  50.768  1.00 55.25           N  
ATOM   1364  N   THR A  84      12.546   7.902  47.539  1.00 38.93           N  
ATOM   1365  CA  THR A  84      13.632   6.938  47.479  1.00 38.38           C  
ATOM   1366  C   THR A  84      14.900   7.530  48.054  1.00 38.61           C  
ATOM   1367  O   THR A  84      15.619   6.881  48.840  1.00 38.10           O  
ATOM   1368  CB  THR A  84      13.893   6.560  46.048  1.00 39.93           C  
ATOM   1369  OG1 THR A  84      12.683   6.040  45.496  1.00 41.57           O  
ATOM   1370  CG2 THR A  84      14.999   5.534  45.958  1.00 41.28           C  
ATOM   1371  N   VAL A  85      15.187   8.757  47.632  1.00 35.28           N  
ATOM   1372  CA  VAL A  85      16.365   9.474  48.086  1.00 33.20           C  
ATOM   1373  C   VAL A  85      16.320   9.649  49.615  1.00 32.57           C  
ATOM   1374  O   VAL A  85      17.243   9.230  50.337  1.00 30.61           O  
ATOM   1375  CB  VAL A  85      16.454  10.847  47.389  1.00 33.08           C  
ATOM   1376  CG1 VAL A  85      17.568  11.683  48.007  1.00 32.25           C  
ATOM   1377  CG2 VAL A  85      16.697  10.654  45.890  1.00 30.94           C  
ATOM   1378  N   ALA A  86      15.202  10.187  50.101  1.00 33.04           N  
ATOM   1379  CA  ALA A  86      15.004  10.446  51.521  1.00 35.14           C  
ATOM   1380  C   ALA A  86      15.066   9.180  52.346  1.00 38.16           C  
ATOM   1381  O   ALA A  86      15.593   9.182  53.462  1.00 40.02           O  
ATOM   1382  CB  ALA A  86      13.683  11.141  51.747  1.00 37.98           C  
ATOM   1383  N   LEU A  87      14.525   8.102  51.788  1.00 39.45           N  
ATOM   1384  CA  LEU A  87      14.488   6.814  52.429  1.00 37.86           C  
ATOM   1385  C   LEU A  87      15.877   6.204  52.535  1.00 37.73           C  
ATOM   1386  O   LEU A  87      16.251   5.680  53.574  1.00 39.92           O  
ATOM   1387  CB  LEU A  87      13.560   5.895  51.643  1.00 40.73           C  
ATOM   1388  CG  LEU A  87      13.388   4.444  52.100  1.00 47.20           C  
ATOM   1389  CD1 LEU A  87      12.787   4.362  53.504  1.00 49.27           C  
ATOM   1390  CD2 LEU A  87      12.482   3.735  51.113  1.00 50.83           C  
ATOM   1391  N   HIS A  88      16.668   6.292  51.478  1.00 37.58           N  
ATOM   1392  CA  HIS A  88      17.981   5.683  51.505  1.00 37.55           C  
ATOM   1393  C   HIS A  88      19.119   6.465  52.090  1.00 38.24           C  
ATOM   1394  O   HIS A  88      20.114   5.885  52.546  1.00 41.80           O  
ATOM   1395  CB  HIS A  88      18.330   5.092  50.144  1.00 39.44           C  
ATOM   1396  CG  HIS A  88      17.447   3.948  49.768  1.00 41.33           C  
ATOM   1397  ND1 HIS A  88      17.593   2.685  50.308  1.00 42.59           N  
ATOM   1398  CD2 HIS A  88      16.331   3.900  49.003  1.00 42.55           C  
ATOM   1399  CE1 HIS A  88      16.609   1.912  49.897  1.00 43.05           C  
ATOM   1400  NE2 HIS A  88      15.826   2.623  49.105  1.00 42.17           N  
ATOM   1401  N   ALA A  89      18.989   7.779  52.128  1.00 37.72           N  
ATOM   1402  CA  ALA A  89      20.051   8.609  52.703  1.00 35.65           C  
ATOM   1403  C   ALA A  89      20.112   8.443  54.229  1.00 33.26           C  
ATOM   1404  O   ALA A  89      19.085   8.275  54.883  1.00 32.81           O  
ATOM   1405  CB  ALA A  89      19.832  10.066  52.339  1.00 36.67           C  
ATOM   1406  N   ARG A  90      21.317   8.519  54.793  1.00 31.85           N  
ATOM   1407  CA  ARG A  90      21.519   8.383  56.239  1.00 31.43           C  
ATOM   1408  C   ARG A  90      21.002   9.590  57.028  1.00 33.60           C  
ATOM   1409  O   ARG A  90      20.525   9.445  58.152  1.00 33.45           O  
ATOM   1410  CB  ARG A  90      23.018   8.167  56.551  1.00 29.13           C  
ATOM   1411  CG  ARG A  90      23.666   6.991  55.824  1.00 26.29           C  
ATOM   1412  CD  ARG A  90      25.143   6.866  56.148  1.00 28.41           C  
ATOM   1413  NE  ARG A  90      25.803   5.931  55.229  1.00 30.65           N  
ATOM   1414  CZ  ARG A  90      27.099   5.615  55.238  1.00 29.67           C  
ATOM   1415  NH1 ARG A  90      27.928   6.133  56.130  1.00 29.76           N  
ATOM   1416  NH2 ARG A  90      27.579   4.812  54.305  1.00 32.11           N  
ATOM   1417  N   ASN A  91      21.068  10.771  56.424  1.00 32.97           N  
ATOM   1418  CA  ASN A  91      20.675  12.003  57.103  1.00 33.03           C  
ATOM   1419  C   ASN A  91      19.778  12.856  56.185  1.00 34.07           C  
ATOM   1420  O   ASN A  91      20.186  13.859  55.629  1.00 32.40           O  
ATOM   1421  CB  ASN A  91      21.974  12.742  57.485  1.00 33.62           C  
ATOM   1422  CG  ASN A  91      21.795  13.733  58.615  1.00 36.79           C  
ATOM   1423  OD1 ASN A  91      20.701  14.265  58.847  1.00 37.16           O  
ATOM   1424  ND2 ASN A  91      22.899  14.021  59.314  1.00 34.03           N  
ATOM   1425  N   ALA A  92      18.546  12.424  56.011  1.00 35.35           N  
ATOM   1426  CA  ALA A  92      17.621  13.130  55.153  1.00 36.97           C  
ATOM   1427  C   ALA A  92      16.286  13.446  55.825  1.00 40.52           C  
ATOM   1428  O   ALA A  92      15.887  12.787  56.788  1.00 41.35           O  
ATOM   1429  CB  ALA A  92      17.394  12.337  53.877  1.00 35.67           C  
ATOM   1430  N   GLU A  93      15.630  14.491  55.314  1.00 43.27           N  
ATOM   1431  CA  GLU A  93      14.320  14.982  55.757  1.00 43.81           C  
ATOM   1432  C   GLU A  93      13.580  15.177  54.454  1.00 42.94           C  
ATOM   1433  O   GLU A  93      14.180  15.626  53.478  1.00 40.08           O  
ATOM   1434  CB  GLU A  93      14.411  16.390  56.363  1.00 46.02           C  
ATOM   1435  CG  GLU A  93      14.893  16.517  57.772  1.00 52.23           C  
ATOM   1436  CD  GLU A  93      14.654  17.922  58.302  1.00 56.42           C  
ATOM   1437  OE1 GLU A  93      13.474  18.305  58.427  1.00 59.57           O  
ATOM   1438  OE2 GLU A  93      15.629  18.654  58.576  1.00 57.81           O  
ATOM   1439  N   TYR A  94      12.278  14.909  54.458  1.00 43.65           N  
ATOM   1440  CA  TYR A  94      11.452  15.118  53.273  1.00 44.26           C  
ATOM   1441  C   TYR A  94       9.966  15.158  53.597  1.00 44.97           C  
ATOM   1442  O   TYR A  94       9.360  14.155  53.944  1.00 45.69           O  
ATOM   1443  CB  TYR A  94      11.757  14.066  52.184  1.00 42.26           C  
ATOM   1444  CG  TYR A  94      10.923  14.201  50.909  1.00 36.92           C  
ATOM   1445  CD1 TYR A  94      10.859  15.409  50.203  1.00 35.52           C  
ATOM   1446  CD2 TYR A  94      10.166  13.133  50.447  1.00 34.00           C  
ATOM   1447  CE1 TYR A  94      10.048  15.550  49.048  1.00 37.89           C  
ATOM   1448  CE2 TYR A  94       9.348  13.251  49.316  1.00 36.84           C  
ATOM   1449  CZ  TYR A  94       9.287  14.453  48.611  1.00 38.09           C  
ATOM   1450  OH  TYR A  94       8.491  14.514  47.487  1.00 37.21           O  
ATOM   1451  N   ASN A  95       9.396  16.351  53.555  1.00 48.43           N  
ATOM   1452  CA  ASN A  95       7.971  16.513  53.808  1.00 51.12           C  
ATOM   1453  C   ASN A  95       7.465  17.343  52.635  1.00 48.07           C  
ATOM   1454  O   ASN A  95       7.562  18.574  52.667  1.00 46.78           O  
ATOM   1455  CB  ASN A  95       7.705  17.263  55.133  1.00 56.68           C  
ATOM   1456  CG  ASN A  95       8.629  16.801  56.282  1.00 62.72           C  
ATOM   1457  OD1 ASN A  95       8.387  15.776  56.938  1.00 66.79           O  
ATOM   1458  ND2 ASN A  95       9.693  17.570  56.525  1.00 59.64           N  
ATOM   1459  N   PRO A  96       6.964  16.676  51.568  1.00 47.38           N  
ATOM   1460  CA  PRO A  96       6.413  17.240  50.322  1.00 47.01           C  
ATOM   1461  C   PRO A  96       5.471  18.424  50.572  1.00 48.20           C  
ATOM   1462  O   PRO A  96       5.420  19.370  49.784  1.00 47.91           O  
ATOM   1463  CB  PRO A  96       5.622  16.085  49.730  1.00 46.97           C  
ATOM   1464  CG  PRO A  96       6.294  14.865  50.221  1.00 44.90           C  
ATOM   1465  CD  PRO A  96       6.916  15.193  51.560  1.00 46.47           C  
ATOM   1466  N   LYS A  97       4.666  18.307  51.625  1.00 49.87           N  
ATOM   1467  CA  LYS A  97       3.704  19.329  52.031  1.00 51.52           C  
ATOM   1468  C   LYS A  97       4.301  20.662  52.491  1.00 52.19           C  
ATOM   1469  O   LYS A  97       3.641  21.699  52.427  1.00 53.29           O  
ATOM   1470  CB  LYS A  97       2.786  18.757  53.106  1.00 54.42           C  
ATOM   1471  CG  LYS A  97       1.777  17.770  52.536  1.00 59.45           C  
ATOM   1472  CD  LYS A  97       1.108  16.903  53.599  1.00 63.46           C  
ATOM   1473  CE  LYS A  97       0.017  16.036  52.984  1.00 67.16           C  
ATOM   1474  NZ  LYS A  97       0.408  15.584  51.603  1.00 73.61           N  
ATOM   1475  N   ARG A  98       5.544  20.636  52.963  1.00 52.76           N  
ATOM   1476  CA  ARG A  98       6.227  21.839  53.438  1.00 52.08           C  
ATOM   1477  C   ARG A  98       7.158  22.459  52.379  1.00 49.67           C  
ATOM   1478  O   ARG A  98       7.102  23.673  52.122  1.00 51.67           O  
ATOM   1479  CB  ARG A  98       7.023  21.522  54.701  1.00 54.70           C  
ATOM   1480  CG  ARG A  98       7.458  22.754  55.458  1.00 60.56           C  
ATOM   1481  CD  ARG A  98       8.661  22.457  56.341  1.00 64.95           C  
ATOM   1482  NE  ARG A  98       9.244  23.690  56.866  1.00 67.01           N  
ATOM   1483  CZ  ARG A  98      10.214  23.747  57.776  1.00 67.94           C  
ATOM   1484  NH1 ARG A  98      10.741  22.633  58.275  1.00 68.56           N  
ATOM   1485  NH2 ARG A  98      10.626  24.926  58.224  1.00 68.27           N  
ATOM   1486  N   PHE A  99       8.017  21.637  51.778  1.00 44.38           N  
ATOM   1487  CA  PHE A  99       8.956  22.101  50.762  1.00 39.10           C  
ATOM   1488  C   PHE A  99       9.223  20.952  49.812  1.00 37.12           C  
ATOM   1489  O   PHE A  99       9.417  19.825  50.248  1.00 37.94           O  
ATOM   1490  CB  PHE A  99      10.277  22.536  51.407  1.00 38.55           C  
ATOM   1491  CG  PHE A  99      11.166  23.346  50.487  1.00 38.58           C  
ATOM   1492  CD1 PHE A  99      10.730  24.557  49.962  1.00 39.68           C  
ATOM   1493  CD2 PHE A  99      12.424  22.899  50.147  1.00 40.16           C  
ATOM   1494  CE1 PHE A  99      11.530  25.303  49.119  1.00 39.00           C  
ATOM   1495  CE2 PHE A  99      13.227  23.644  49.300  1.00 42.19           C  
ATOM   1496  CZ  PHE A  99      12.776  24.851  48.783  1.00 41.68           C  
ATOM   1497  N   ALA A 100       9.350  21.273  48.533  1.00 33.69           N  
ATOM   1498  CA  ALA A 100       9.567  20.270  47.500  1.00 33.48           C  
ATOM   1499  C   ALA A 100      11.013  19.878  47.248  1.00 31.95           C  
ATOM   1500  O   ALA A 100      11.494  19.961  46.114  1.00 33.16           O  
ATOM   1501  CB  ALA A 100       8.918  20.717  46.216  1.00 33.56           C  
ATOM   1502  N   ALA A 101      11.682  19.383  48.281  1.00 32.12           N  
ATOM   1503  CA  ALA A 101      13.086  18.976  48.166  1.00 31.79           C  
ATOM   1504  C   ALA A 101      13.450  18.137  49.367  1.00 30.92           C  
ATOM   1505  O   ALA A 101      12.813  18.240  50.427  1.00 31.63           O  
ATOM   1506  CB  ALA A 101      14.034  20.217  48.107  1.00 26.27           C  
ATOM   1507  N   VAL A 102      14.427  17.257  49.178  1.00 28.12           N  
ATOM   1508  CA  VAL A 102      14.918  16.445  50.275  1.00 27.63           C  
ATOM   1509  C   VAL A 102      15.996  17.337  50.881  1.00 27.85           C  
ATOM   1510  O   VAL A 102      16.749  18.010  50.164  1.00 29.49           O  
ATOM   1511  CB  VAL A 102      15.547  15.097  49.798  1.00 26.17           C  
ATOM   1512  CG1 VAL A 102      16.223  14.385  50.952  1.00 26.74           C  
ATOM   1513  CG2 VAL A 102      14.485  14.193  49.215  1.00 25.66           C  
ATOM   1514  N   ILE A 103      15.988  17.433  52.198  1.00 26.35           N  
ATOM   1515  CA  ILE A 103      16.966  18.220  52.896  1.00 25.95           C  
ATOM   1516  C   ILE A 103      17.907  17.173  53.436  1.00 26.89           C  
ATOM   1517  O   ILE A 103      17.563  16.455  54.365  1.00 28.37           O  
ATOM   1518  CB  ILE A 103      16.315  19.044  54.018  1.00 25.40           C  
ATOM   1519  CG1 ILE A 103      15.265  19.968  53.401  1.00 26.03           C  
ATOM   1520  CG2 ILE A 103      17.375  19.830  54.792  1.00 25.61           C  
ATOM   1521  CD1 ILE A 103      14.383  20.663  54.384  1.00 29.31           C  
ATOM   1522  N   MET A 104      19.051  17.031  52.771  1.00 28.31           N  
ATOM   1523  CA  MET A 104      20.079  16.064  53.136  1.00 27.60           C  
ATOM   1524  C   MET A 104      21.277  16.769  53.805  1.00 28.50           C  
ATOM   1525  O   MET A 104      21.562  17.934  53.515  1.00 25.22           O  
ATOM   1526  CB  MET A 104      20.531  15.322  51.881  1.00 25.28           C  
ATOM   1527  CG  MET A 104      21.361  14.088  52.142  1.00 31.74           C  
ATOM   1528  SD  MET A 104      21.934  13.289  50.620  1.00 36.71           S  
ATOM   1529  CE  MET A 104      20.358  12.737  49.934  1.00 31.94           C  
ATOM   1530  N   ARG A 105      21.964  16.071  54.711  1.00 28.45           N  
ATOM   1531  CA  ARG A 105      23.111  16.630  55.419  1.00 29.60           C  
ATOM   1532  C   ARG A 105      24.246  15.639  55.550  1.00 30.42           C  
ATOM   1533  O   ARG A 105      24.027  14.419  55.543  1.00 29.76           O  
ATOM   1534  CB  ARG A 105      22.707  17.074  56.822  1.00 30.21           C  
ATOM   1535  CG  ARG A 105      21.657  18.171  56.835  1.00 31.77           C  
ATOM   1536  CD  ARG A 105      21.433  18.686  58.247  1.00 34.24           C  
ATOM   1537  NE  ARG A 105      20.652  19.923  58.243  1.00 33.66           N  
ATOM   1538  CZ  ARG A 105      19.335  19.973  58.093  1.00 35.06           C  
ATOM   1539  NH1 ARG A 105      18.629  18.852  57.950  1.00 35.21           N  
ATOM   1540  NH2 ARG A 105      18.729  21.151  58.039  1.00 34.34           N  
ATOM   1541  N   ILE A 106      25.468  16.165  55.616  1.00 31.26           N  
ATOM   1542  CA  ILE A 106      26.671  15.330  55.799  1.00 30.95           C  
ATOM   1543  C   ILE A 106      27.482  15.967  56.925  1.00 31.73           C  
ATOM   1544  O   ILE A 106      27.380  17.166  57.162  1.00 30.38           O  
ATOM   1545  CB  ILE A 106      27.567  15.181  54.516  1.00 30.37           C  
ATOM   1546  CG1 ILE A 106      28.086  16.553  54.062  1.00 28.24           C  
ATOM   1547  CG2 ILE A 106      26.833  14.393  53.407  1.00 28.15           C  
ATOM   1548  CD1 ILE A 106      29.081  16.497  52.950  1.00 25.46           C  
ATOM   1549  N   ARG A 107      28.280  15.172  57.620  1.00 32.11           N  
ATOM   1550  CA  ARG A 107      29.034  15.705  58.729  1.00 33.21           C  
ATOM   1551  C   ARG A 107      30.333  16.393  58.371  1.00 35.98           C  
ATOM   1552  O   ARG A 107      30.772  17.316  59.097  1.00 34.82           O  
ATOM   1553  CB  ARG A 107      29.298  14.603  59.760  1.00 34.25           C  
ATOM   1554  CG  ARG A 107      28.031  14.066  60.373  1.00 34.95           C  
ATOM   1555  CD  ARG A 107      28.346  12.850  61.176  1.00 36.23           C  
ATOM   1556  NE  ARG A 107      27.132  12.186  61.629  1.00 38.91           N  
ATOM   1557  CZ  ARG A 107      27.063  10.900  61.967  1.00 38.60           C  
ATOM   1558  NH1 ARG A 107      28.150  10.131  61.900  1.00 34.39           N  
ATOM   1559  NH2 ARG A 107      25.908  10.390  62.379  1.00 36.32           N  
ATOM   1560  N   GLU A 108      30.959  15.962  57.279  1.00 34.81           N  
ATOM   1561  CA  GLU A 108      32.216  16.566  56.893  1.00 38.23           C  
ATOM   1562  C   GLU A 108      32.382  16.725  55.381  1.00 36.66           C  
ATOM   1563  O   GLU A 108      32.401  15.744  54.651  1.00 36.89           O  
ATOM   1564  CB  GLU A 108      33.370  15.753  57.469  1.00 44.10           C  
ATOM   1565  CG  GLU A 108      34.382  16.591  58.230  1.00 56.74           C  
ATOM   1566  CD  GLU A 108      34.280  16.428  59.736  1.00 61.36           C  
ATOM   1567  OE1 GLU A 108      34.826  15.425  60.263  1.00 66.61           O  
ATOM   1568  OE2 GLU A 108      33.678  17.314  60.388  1.00 63.07           O  
ATOM   1569  N   PRO A 109      32.432  17.992  54.888  1.00 33.98           N  
ATOM   1570  CA  PRO A 109      32.330  19.243  55.660  1.00 30.72           C  
ATOM   1571  C   PRO A 109      30.877  19.422  56.083  1.00 30.43           C  
ATOM   1572  O   PRO A 109      29.966  19.020  55.351  1.00 31.50           O  
ATOM   1573  CB  PRO A 109      32.733  20.305  54.639  1.00 30.27           C  
ATOM   1574  CG  PRO A 109      33.644  19.582  53.707  1.00 31.01           C  
ATOM   1575  CD  PRO A 109      32.904  18.284  53.515  1.00 31.74           C  
ATOM   1576  N   LYS A 110      30.654  19.984  57.266  1.00 29.65           N  
ATOM   1577  CA  LYS A 110      29.294  20.203  57.768  1.00 29.25           C  
ATOM   1578  C   LYS A 110      28.520  21.133  56.828  1.00 29.19           C  
ATOM   1579  O   LYS A 110      28.818  22.323  56.727  1.00 29.93           O  
ATOM   1580  CB  LYS A 110      29.332  20.764  59.191  1.00 28.38           C  
ATOM   1581  CG  LYS A 110      27.981  20.702  59.867  1.00 31.71           C  
ATOM   1582  CD  LYS A 110      27.860  21.716  60.964  1.00 33.32           C  
ATOM   1583  CE  LYS A 110      26.415  22.062  61.175  1.00 35.01           C  
ATOM   1584  NZ  LYS A 110      26.134  22.067  62.620  1.00 41.36           N  
ATOM   1585  N   THR A 111      27.547  20.575  56.121  1.00 28.52           N  
ATOM   1586  CA  THR A 111      26.759  21.325  55.165  1.00 26.69           C  
ATOM   1587  C   THR A 111      25.353  20.751  55.127  1.00 27.28           C  
ATOM   1588  O   THR A 111      25.074  19.726  55.746  1.00 27.33           O  
ATOM   1589  CB  THR A 111      27.315  21.118  53.738  1.00 27.22           C  
ATOM   1590  OG1 THR A 111      27.686  19.745  53.600  1.00 26.87           O  
ATOM   1591  CG2 THR A 111      28.531  22.022  53.429  1.00 26.38           C  
ATOM   1592  N   THR A 112      24.501  21.402  54.326  1.00 27.58           N  
ATOM   1593  CA  THR A 112      23.107  21.020  54.112  1.00 26.12           C  
ATOM   1594  C   THR A 112      22.866  21.167  52.601  1.00 25.71           C  
ATOM   1595  O   THR A 112      23.334  22.136  51.984  1.00 24.20           O  
ATOM   1596  CB  THR A 112      22.107  21.956  54.905  1.00 27.31           C  
ATOM   1597  OG1 THR A 112      22.320  21.817  56.320  1.00 27.25           O  
ATOM   1598  CG2 THR A 112      20.639  21.610  54.591  1.00 23.80           C  
ATOM   1599  N   ALA A 113      22.157  20.199  52.015  1.00 25.41           N  
ATOM   1600  CA  ALA A 113      21.833  20.203  50.593  1.00 24.13           C  
ATOM   1601  C   ALA A 113      20.328  20.162  50.409  1.00 24.93           C  
ATOM   1602  O   ALA A 113      19.616  19.512  51.190  1.00 25.60           O  
ATOM   1603  CB  ALA A 113      22.457  18.993  49.872  1.00 20.77           C  
ATOM   1604  N   LEU A 114      19.844  20.888  49.403  1.00 25.60           N  
ATOM   1605  CA  LEU A 114      18.420  20.910  49.065  1.00 27.35           C  
ATOM   1606  C   LEU A 114      18.411  20.193  47.725  1.00 27.52           C  
ATOM   1607  O   LEU A 114      18.998  20.688  46.751  1.00 25.62           O  
ATOM   1608  CB  LEU A 114      17.894  22.347  48.924  1.00 27.68           C  
ATOM   1609  CG  LEU A 114      18.031  23.268  50.148  1.00 31.09           C  
ATOM   1610  CD1 LEU A 114      17.509  24.661  49.793  1.00 30.40           C  
ATOM   1611  CD2 LEU A 114      17.272  22.699  51.356  1.00 29.56           C  
ATOM   1612  N   ILE A 115      17.864  18.976  47.725  1.00 28.03           N  
ATOM   1613  CA  ILE A 115      17.814  18.124  46.527  1.00 29.21           C  
ATOM   1614  C   ILE A 115      16.428  18.038  45.875  1.00 28.38           C  
ATOM   1615  O   ILE A 115      15.458  17.580  46.490  1.00 28.75           O  
ATOM   1616  CB  ILE A 115      18.399  16.703  46.835  1.00 29.63           C  
ATOM   1617  CG1 ILE A 115      19.827  16.867  47.383  1.00 27.77           C  
ATOM   1618  CG2 ILE A 115      18.434  15.854  45.564  1.00 27.46           C  
ATOM   1619  CD1 ILE A 115      20.450  15.617  47.936  1.00 29.95           C  
ATOM   1620  N   PHE A 116      16.369  18.454  44.614  1.00 26.64           N  
ATOM   1621  CA  PHE A 116      15.138  18.487  43.849  1.00 26.27           C  
ATOM   1622  C   PHE A 116      14.907  17.329  42.873  1.00 24.87           C  
ATOM   1623  O   PHE A 116      15.848  16.710  42.395  1.00 25.49           O  
ATOM   1624  CB  PHE A 116      15.064  19.830  43.105  1.00 26.77           C  
ATOM   1625  CG  PHE A 116      15.050  21.019  44.030  1.00 25.53           C  
ATOM   1626  CD1 PHE A 116      16.219  21.512  44.580  1.00 25.88           C  
ATOM   1627  CD2 PHE A 116      13.851  21.586  44.419  1.00 26.03           C  
ATOM   1628  CE1 PHE A 116      16.196  22.550  45.511  1.00 27.15           C  
ATOM   1629  CE2 PHE A 116      13.819  22.621  45.349  1.00 29.15           C  
ATOM   1630  CZ  PHE A 116      14.996  23.106  45.895  1.00 27.63           C  
ATOM   1631  N   ALA A 117      13.648  17.104  42.507  1.00 27.66           N  
ATOM   1632  CA  ALA A 117      13.291  16.023  41.579  1.00 27.51           C  
ATOM   1633  C   ALA A 117      13.927  16.178  40.192  1.00 29.27           C  
ATOM   1634  O   ALA A 117      14.215  15.190  39.517  1.00 32.28           O  
ATOM   1635  CB  ALA A 117      11.782  15.912  41.460  1.00 25.63           C  
ATOM   1636  N   SER A 118      14.179  17.419  39.788  1.00 30.01           N  
ATOM   1637  CA  SER A 118      14.763  17.731  38.488  1.00 27.43           C  
ATOM   1638  C   SER A 118      16.206  17.285  38.456  1.00 29.12           C  
ATOM   1639  O   SER A 118      16.827  17.242  37.392  1.00 31.16           O  
ATOM   1640  CB  SER A 118      14.736  19.241  38.275  1.00 29.36           C  
ATOM   1641  OG  SER A 118      15.482  19.920  39.301  1.00 27.10           O  
ATOM   1642  N   GLY A 119      16.765  17.031  39.636  1.00 27.40           N  
ATOM   1643  CA  GLY A 119      18.153  16.629  39.722  1.00 25.53           C  
ATOM   1644  C   GLY A 119      19.051  17.813  40.063  1.00 26.78           C  
ATOM   1645  O   GLY A 119      20.277  17.690  40.074  1.00 27.47           O  
ATOM   1646  N   LYS A 120      18.465  18.993  40.230  1.00 26.14           N  
ATOM   1647  CA  LYS A 120      19.251  20.169  40.576  1.00 24.17           C  
ATOM   1648  C   LYS A 120      19.429  20.124  42.098  1.00 25.07           C  
ATOM   1649  O   LYS A 120      18.578  19.600  42.839  1.00 24.79           O  
ATOM   1650  CB  LYS A 120      18.543  21.451  40.156  1.00 23.59           C  
ATOM   1651  CG  LYS A 120      18.415  21.666  38.642  1.00 24.52           C  
ATOM   1652  CD  LYS A 120      19.757  21.915  38.019  1.00 26.66           C  
ATOM   1653  CE  LYS A 120      19.654  22.256  36.544  1.00 29.32           C  
ATOM   1654  NZ  LYS A 120      19.108  23.610  36.242  1.00 29.76           N  
ATOM   1655  N   MET A 121      20.527  20.685  42.571  1.00 23.57           N  
ATOM   1656  CA  MET A 121      20.812  20.651  43.977  1.00 23.77           C  
ATOM   1657  C   MET A 121      21.435  21.962  44.429  1.00 24.44           C  
ATOM   1658  O   MET A 121      22.230  22.568  43.698  1.00 23.15           O  
ATOM   1659  CB  MET A 121      21.751  19.465  44.220  1.00 27.97           C  
ATOM   1660  CG  MET A 121      22.460  19.370  45.555  1.00 31.67           C  
ATOM   1661  SD  MET A 121      23.386  17.792  45.726  1.00 35.02           S  
ATOM   1662  CE  MET A 121      24.975  18.178  44.994  1.00 28.46           C  
ATOM   1663  N   VAL A 122      21.028  22.428  45.611  1.00 25.01           N  
ATOM   1664  CA  VAL A 122      21.597  23.639  46.211  1.00 23.14           C  
ATOM   1665  C   VAL A 122      22.381  23.159  47.434  1.00 21.36           C  
ATOM   1666  O   VAL A 122      21.856  22.383  48.220  1.00 21.38           O  
ATOM   1667  CB  VAL A 122      20.520  24.624  46.701  1.00 23.57           C  
ATOM   1668  CG1 VAL A 122      21.154  25.753  47.502  1.00 19.89           C  
ATOM   1669  CG2 VAL A 122      19.759  25.174  45.519  1.00 21.93           C  
ATOM   1670  N   VAL A 123      23.640  23.562  47.569  1.00 21.05           N  
ATOM   1671  CA  VAL A 123      24.462  23.167  48.718  1.00 21.95           C  
ATOM   1672  C   VAL A 123      24.842  24.433  49.525  1.00 24.52           C  
ATOM   1673  O   VAL A 123      25.417  25.394  48.978  1.00 26.84           O  
ATOM   1674  CB  VAL A 123      25.745  22.393  48.283  1.00 22.32           C  
ATOM   1675  CG1 VAL A 123      26.512  21.931  49.511  1.00 19.43           C  
ATOM   1676  CG2 VAL A 123      25.385  21.205  47.390  1.00 19.72           C  
ATOM   1677  N   THR A 124      24.546  24.439  50.822  1.00 23.85           N  
ATOM   1678  CA  THR A 124      24.831  25.616  51.629  1.00 22.64           C  
ATOM   1679  C   THR A 124      25.441  25.298  52.998  1.00 24.09           C  
ATOM   1680  O   THR A 124      25.493  24.136  53.404  1.00 25.44           O  
ATOM   1681  CB  THR A 124      23.542  26.472  51.764  1.00 24.58           C  
ATOM   1682  OG1 THR A 124      23.848  27.703  52.428  1.00 25.17           O  
ATOM   1683  CG2 THR A 124      22.408  25.720  52.493  1.00 19.58           C  
ATOM   1684  N   GLY A 125      26.003  26.303  53.663  1.00 23.57           N  
ATOM   1685  CA  GLY A 125      26.576  26.078  54.982  1.00 22.85           C  
ATOM   1686  C   GLY A 125      28.083  25.963  55.082  1.00 24.54           C  
ATOM   1687  O   GLY A 125      28.638  25.982  56.178  1.00 27.23           O  
ATOM   1688  N   ALA A 126      28.754  25.853  53.949  1.00 23.61           N  
ATOM   1689  CA  ALA A 126      30.198  25.730  53.937  1.00 25.30           C  
ATOM   1690  C   ALA A 126      30.879  27.055  54.311  1.00 27.13           C  
ATOM   1691  O   ALA A 126      30.328  28.129  54.053  1.00 27.10           O  
ATOM   1692  CB  ALA A 126      30.648  25.272  52.565  1.00 22.30           C  
ATOM   1693  N   LYS A 127      32.084  26.979  54.883  1.00 28.15           N  
ATOM   1694  CA  LYS A 127      32.840  28.175  55.280  1.00 28.62           C  
ATOM   1695  C   LYS A 127      33.975  28.482  54.323  1.00 28.15           C  
ATOM   1696  O   LYS A 127      34.658  29.487  54.496  1.00 28.64           O  
ATOM   1697  CB  LYS A 127      33.409  28.047  56.696  1.00 30.44           C  
ATOM   1698  CG  LYS A 127      32.365  27.810  57.778  1.00 34.97           C  
ATOM   1699  CD  LYS A 127      32.209  29.003  58.697  1.00 39.59           C  
ATOM   1700  CE  LYS A 127      30.944  28.862  59.541  1.00 42.86           C  
ATOM   1701  NZ  LYS A 127      30.586  30.175  60.147  1.00 44.96           N  
ATOM   1702  N   SER A 128      34.210  27.598  53.352  1.00 26.98           N  
ATOM   1703  CA  SER A 128      35.256  27.824  52.357  1.00 28.31           C  
ATOM   1704  C   SER A 128      34.812  27.256  51.024  1.00 26.03           C  
ATOM   1705  O   SER A 128      33.954  26.387  50.989  1.00 23.36           O  
ATOM   1706  CB  SER A 128      36.595  27.206  52.790  1.00 29.33           C  
ATOM   1707  OG  SER A 128      36.635  25.804  52.576  1.00 31.90           O  
ATOM   1708  N   GLU A 129      35.383  27.782  49.942  1.00 27.80           N  
ATOM   1709  CA  GLU A 129      35.068  27.368  48.572  1.00 28.51           C  
ATOM   1710  C   GLU A 129      35.449  25.899  48.325  1.00 31.08           C  
ATOM   1711  O   GLU A 129      34.797  25.179  47.558  1.00 31.13           O  
ATOM   1712  CB  GLU A 129      35.792  28.276  47.565  1.00 26.66           C  
ATOM   1713  CG  GLU A 129      35.534  29.767  47.724  1.00 25.81           C  
ATOM   1714  CD  GLU A 129      36.615  30.523  48.519  1.00 26.66           C  
ATOM   1715  OE1 GLU A 129      37.145  29.993  49.516  1.00 27.35           O  
ATOM   1716  OE2 GLU A 129      36.912  31.684  48.159  1.00 28.85           O  
ATOM   1717  N   ASP A 130      36.514  25.483  48.995  1.00 33.87           N  
ATOM   1718  CA  ASP A 130      37.073  24.125  48.955  1.00 37.72           C  
ATOM   1719  C   ASP A 130      36.057  23.204  49.579  1.00 34.11           C  
ATOM   1720  O   ASP A 130      35.708  22.168  49.023  1.00 30.92           O  
ATOM   1721  CB  ASP A 130      38.377  24.146  49.791  1.00 50.32           C  
ATOM   1722  CG  ASP A 130      38.876  22.754  50.271  1.00 61.79           C  
ATOM   1723  OD1 ASP A 130      38.115  21.922  50.862  1.00 64.28           O  
ATOM   1724  OD2 ASP A 130      40.112  22.557  50.147  1.00 70.34           O  
ATOM   1725  N   ASP A 131      35.586  23.597  50.755  1.00 32.49           N  
ATOM   1726  CA  ASP A 131      34.617  22.800  51.480  1.00 32.21           C  
ATOM   1727  C   ASP A 131      33.335  22.667  50.716  1.00 30.33           C  
ATOM   1728  O   ASP A 131      32.705  21.604  50.768  1.00 30.96           O  
ATOM   1729  CB  ASP A 131      34.346  23.379  52.865  1.00 36.00           C  
ATOM   1730  CG  ASP A 131      35.396  22.968  53.885  1.00 42.08           C  
ATOM   1731  OD1 ASP A 131      36.277  22.118  53.576  1.00 45.36           O  
ATOM   1732  OD2 ASP A 131      35.340  23.504  55.010  1.00 42.84           O  
ATOM   1733  N   SER A 132      32.961  23.722  49.988  1.00 27.16           N  
ATOM   1734  CA  SER A 132      31.738  23.717  49.187  1.00 25.41           C  
ATOM   1735  C   SER A 132      31.803  22.675  48.069  1.00 24.09           C  
ATOM   1736  O   SER A 132      30.892  21.857  47.931  1.00 25.99           O  
ATOM   1737  CB  SER A 132      31.440  25.113  48.607  1.00 23.59           C  
ATOM   1738  OG  SER A 132      30.153  25.155  48.005  1.00 20.86           O  
ATOM   1739  N   LYS A 133      32.883  22.680  47.287  1.00 24.29           N  
ATOM   1740  CA  LYS A 133      33.042  21.731  46.181  1.00 24.78           C  
ATOM   1741  C   LYS A 133      33.167  20.304  46.714  1.00 24.27           C  
ATOM   1742  O   LYS A 133      32.594  19.358  46.147  1.00 24.16           O  
ATOM   1743  CB  LYS A 133      34.256  22.098  45.303  1.00 26.74           C  
ATOM   1744  CG  LYS A 133      34.467  21.154  44.089  1.00 29.12           C  
ATOM   1745  CD  LYS A 133      35.452  21.699  43.090  1.00 33.39           C  
ATOM   1746  CE  LYS A 133      36.920  21.628  43.580  1.00 36.58           C  
ATOM   1747  NZ  LYS A 133      37.534  20.291  43.379  1.00 38.81           N  
ATOM   1748  N   LEU A 134      33.890  20.160  47.824  1.00 25.93           N  
ATOM   1749  CA  LEU A 134      34.103  18.861  48.471  1.00 28.70           C  
ATOM   1750  C   LEU A 134      32.772  18.246  48.900  1.00 26.88           C  
ATOM   1751  O   LEU A 134      32.454  17.108  48.549  1.00 24.66           O  
ATOM   1752  CB  LEU A 134      34.997  19.026  49.710  1.00 30.39           C  
ATOM   1753  CG  LEU A 134      36.163  18.068  49.968  1.00 30.63           C  
ATOM   1754  CD1 LEU A 134      36.353  17.944  51.466  1.00 27.33           C  
ATOM   1755  CD2 LEU A 134      35.908  16.688  49.372  1.00 33.07           C  
ATOM   1756  N   ALA A 135      32.005  19.002  49.675  1.00 26.78           N  
ATOM   1757  CA  ALA A 135      30.717  18.540  50.159  1.00 26.71           C  
ATOM   1758  C   ALA A 135      29.766  18.267  48.994  1.00 26.15           C  
ATOM   1759  O   ALA A 135      28.980  17.336  49.061  1.00 26.48           O  
ATOM   1760  CB  ALA A 135      30.122  19.542  51.127  1.00 28.05           C  
ATOM   1761  N   SER A 136      29.827  19.082  47.938  1.00 26.04           N  
ATOM   1762  CA  SER A 136      28.994  18.889  46.750  1.00 24.16           C  
ATOM   1763  C   SER A 136      29.305  17.557  46.065  1.00 24.20           C  
ATOM   1764  O   SER A 136      28.403  16.812  45.666  1.00 24.19           O  
ATOM   1765  CB  SER A 136      29.203  20.033  45.744  1.00 25.87           C  
ATOM   1766  OG  SER A 136      28.755  21.273  46.258  1.00 26.96           O  
ATOM   1767  N   ARG A 137      30.585  17.264  45.882  1.00 26.15           N  
ATOM   1768  CA  ARG A 137      30.964  15.997  45.253  1.00 28.83           C  
ATOM   1769  C   ARG A 137      30.412  14.868  46.140  1.00 29.30           C  
ATOM   1770  O   ARG A 137      29.807  13.924  45.639  1.00 33.00           O  
ATOM   1771  CB  ARG A 137      32.490  15.856  45.118  1.00 30.83           C  
ATOM   1772  CG  ARG A 137      33.160  16.865  44.216  1.00 32.45           C  
ATOM   1773  CD  ARG A 137      34.675  16.733  44.299  1.00 40.54           C  
ATOM   1774  NE  ARG A 137      35.359  17.709  43.438  1.00 47.50           N  
ATOM   1775  CZ  ARG A 137      35.459  17.588  42.112  1.00 51.41           C  
ATOM   1776  NH1 ARG A 137      34.927  16.524  41.512  1.00 54.44           N  
ATOM   1777  NH2 ARG A 137      36.047  18.540  41.379  1.00 46.47           N  
ATOM   1778  N   LYS A 138      30.532  15.015  47.459  1.00 26.43           N  
ATOM   1779  CA  LYS A 138      30.053  13.999  48.389  1.00 26.36           C  
ATOM   1780  C   LYS A 138      28.569  13.732  48.282  1.00 26.67           C  
ATOM   1781  O   LYS A 138      28.157  12.571  48.294  1.00 25.51           O  
ATOM   1782  CB  LYS A 138      30.455  14.322  49.838  1.00 28.26           C  
ATOM   1783  CG  LYS A 138      31.953  14.151  50.064  1.00 33.69           C  
ATOM   1784  CD  LYS A 138      32.384  14.455  51.470  1.00 36.72           C  
ATOM   1785  CE  LYS A 138      33.866  14.205  51.626  1.00 37.27           C  
ATOM   1786  NZ  LYS A 138      34.342  14.600  52.978  1.00 44.57           N  
ATOM   1787  N   TYR A 139      27.771  14.786  48.118  1.00 25.15           N  
ATOM   1788  CA  TYR A 139      26.336  14.620  48.006  1.00 25.19           C  
ATOM   1789  C   TYR A 139      26.031  13.892  46.724  1.00 26.54           C  
ATOM   1790  O   TYR A 139      25.170  13.000  46.710  1.00 28.56           O  
ATOM   1791  CB  TYR A 139      25.590  15.957  48.035  1.00 24.28           C  
ATOM   1792  CG  TYR A 139      25.477  16.559  49.412  1.00 22.02           C  
ATOM   1793  CD1 TYR A 139      24.667  15.980  50.389  1.00 21.80           C  
ATOM   1794  CD2 TYR A 139      26.172  17.735  49.746  1.00 24.03           C  
ATOM   1795  CE1 TYR A 139      24.553  16.553  51.673  1.00 23.48           C  
ATOM   1796  CE2 TYR A 139      26.056  18.316  51.026  1.00 22.84           C  
ATOM   1797  CZ  TYR A 139      25.241  17.720  51.981  1.00 22.59           C  
ATOM   1798  OH  TYR A 139      25.098  18.278  53.228  1.00 23.42           O  
ATOM   1799  N   ALA A 140      26.761  14.226  45.660  1.00 25.29           N  
ATOM   1800  CA  ALA A 140      26.562  13.589  44.355  1.00 26.64           C  
ATOM   1801  C   ALA A 140      26.849  12.065  44.435  1.00 26.96           C  
ATOM   1802  O   ALA A 140      26.085  11.246  43.891  1.00 24.46           O  
ATOM   1803  CB  ALA A 140      27.440  14.287  43.263  1.00 24.72           C  
ATOM   1804  N   ARG A 141      27.910  11.696  45.164  1.00 28.72           N  
ATOM   1805  CA  ARG A 141      28.282  10.295  45.334  1.00 31.40           C  
ATOM   1806  C   ARG A 141      27.159   9.533  46.042  1.00 33.40           C  
ATOM   1807  O   ARG A 141      26.838   8.401  45.653  1.00 34.88           O  
ATOM   1808  CB  ARG A 141      29.607  10.131  46.085  1.00 31.99           C  
ATOM   1809  CG  ARG A 141      30.130   8.696  46.046  1.00 37.31           C  
ATOM   1810  CD  ARG A 141      30.153   8.153  44.605  1.00 44.01           C  
ATOM   1811  NE  ARG A 141      30.542   6.731  44.490  1.00 52.44           N  
ATOM   1812  CZ  ARG A 141      30.442   5.990  43.376  1.00 52.87           C  
ATOM   1813  NH1 ARG A 141      29.964   6.502  42.246  1.00 53.51           N  
ATOM   1814  NH2 ARG A 141      30.881   4.735  43.375  1.00 50.76           N  
ATOM   1815  N   ILE A 142      26.539  10.157  47.051  1.00 32.45           N  
ATOM   1816  CA  ILE A 142      25.428   9.564  47.811  1.00 29.69           C  
ATOM   1817  C   ILE A 142      24.287   9.265  46.852  1.00 29.58           C  
ATOM   1818  O   ILE A 142      23.732   8.171  46.853  1.00 31.68           O  
ATOM   1819  CB  ILE A 142      24.923  10.513  48.953  1.00 29.41           C  
ATOM   1820  CG1 ILE A 142      26.029  10.676  50.002  1.00 30.94           C  
ATOM   1821  CG2 ILE A 142      23.640   9.959  49.616  1.00 27.40           C  
ATOM   1822  CD1 ILE A 142      25.749  11.727  51.059  1.00 29.27           C  
ATOM   1823  N   ILE A 143      23.949  10.220  45.995  1.00 29.73           N  
ATOM   1824  CA  ILE A 143      22.867  10.013  45.042  1.00 27.42           C  
ATOM   1825  C   ILE A 143      23.211   8.803  44.142  1.00 29.12           C  
ATOM   1826  O   ILE A 143      22.370   7.920  43.919  1.00 30.58           O  
ATOM   1827  CB  ILE A 143      22.599  11.300  44.212  1.00 25.88           C  
ATOM   1828  CG1 ILE A 143      22.152  12.431  45.146  1.00 25.70           C  
ATOM   1829  CG2 ILE A 143      21.571  11.045  43.121  1.00 21.61           C  
ATOM   1830  CD1 ILE A 143      21.045  12.044  46.137  1.00 24.43           C  
ATOM   1831  N   GLN A 144      24.464   8.724  43.688  1.00 30.43           N  
ATOM   1832  CA  GLN A 144      24.929   7.621  42.835  1.00 30.92           C  
ATOM   1833  C   GLN A 144      24.790   6.279  43.577  1.00 32.29           C  
ATOM   1834  O   GLN A 144      24.243   5.294  43.050  1.00 32.37           O  
ATOM   1835  CB  GLN A 144      26.394   7.846  42.416  1.00 27.42           C  
ATOM   1836  CG  GLN A 144      26.569   9.030  41.478  1.00 28.50           C  
ATOM   1837  CD  GLN A 144      28.018   9.323  41.131  1.00 29.69           C  
ATOM   1838  OE1 GLN A 144      28.916   8.946  41.860  1.00 29.75           O  
ATOM   1839  NE2 GLN A 144      28.246  10.021  40.024  1.00 30.09           N  
ATOM   1840  N   LYS A 145      25.243   6.274  44.827  1.00 33.57           N  
ATOM   1841  CA  LYS A 145      25.215   5.095  45.664  1.00 35.12           C  
ATOM   1842  C   LYS A 145      23.804   4.597  45.875  1.00 33.12           C  
ATOM   1843  O   LYS A 145      23.573   3.402  45.969  1.00 34.65           O  
ATOM   1844  CB  LYS A 145      25.923   5.349  46.990  1.00 40.11           C  
ATOM   1845  CG  LYS A 145      26.194   4.043  47.726  1.00 58.87           C  
ATOM   1846  CD  LYS A 145      26.726   4.198  49.159  1.00 67.26           C  
ATOM   1847  CE  LYS A 145      26.058   3.181  50.152  1.00 67.45           C  
ATOM   1848  NZ  LYS A 145      26.753   3.141  51.497  1.00 70.44           N  
ATOM   1849  N   ILE A 146      22.845   5.513  45.861  1.00 34.31           N  
ATOM   1850  CA  ILE A 146      21.443   5.158  46.026  1.00 33.31           C  
ATOM   1851  C   ILE A 146      20.931   4.559  44.705  1.00 34.34           C  
ATOM   1852  O   ILE A 146      19.862   3.926  44.660  1.00 35.20           O  
ATOM   1853  CB  ILE A 146      20.614   6.379  46.519  1.00 32.76           C  
ATOM   1854  CG1 ILE A 146      21.047   6.748  47.945  1.00 33.72           C  
ATOM   1855  CG2 ILE A 146      19.125   6.071  46.521  1.00 30.98           C  
ATOM   1856  CD1 ILE A 146      20.409   8.017  48.505  1.00 34.32           C  
ATOM   1857  N   GLY A 147      21.671   4.792  43.621  1.00 34.98           N  
ATOM   1858  CA  GLY A 147      21.293   4.196  42.356  1.00 35.03           C  
ATOM   1859  C   GLY A 147      20.902   5.013  41.147  1.00 37.22           C  
ATOM   1860  O   GLY A 147      20.525   4.425  40.117  1.00 40.59           O  
ATOM   1861  N   PHE A 148      20.988   6.334  41.218  1.00 33.50           N  
ATOM   1862  CA  PHE A 148      20.609   7.136  40.065  1.00 30.28           C  
ATOM   1863  C   PHE A 148      21.806   7.434  39.159  1.00 29.93           C  
ATOM   1864  O   PHE A 148      22.963   7.421  39.610  1.00 30.58           O  
ATOM   1865  CB  PHE A 148      19.966   8.422  40.551  1.00 29.62           C  
ATOM   1866  CG  PHE A 148      18.746   8.185  41.391  1.00 29.74           C  
ATOM   1867  CD1 PHE A 148      17.498   8.010  40.796  1.00 30.69           C  
ATOM   1868  CD2 PHE A 148      18.833   8.119  42.781  1.00 28.96           C  
ATOM   1869  CE1 PHE A 148      16.357   7.775  41.577  1.00 29.03           C  
ATOM   1870  CE2 PHE A 148      17.698   7.885  43.562  1.00 29.42           C  
ATOM   1871  CZ  PHE A 148      16.455   7.715  42.955  1.00 29.15           C  
ATOM   1872  N   ALA A 149      21.538   7.734  37.892  1.00 28.48           N  
ATOM   1873  CA  ALA A 149      22.614   8.028  36.942  1.00 29.99           C  
ATOM   1874  C   ALA A 149      23.044   9.520  37.031  1.00 31.84           C  
ATOM   1875  O   ALA A 149      23.059  10.282  36.039  1.00 33.00           O  
ATOM   1876  CB  ALA A 149      22.178   7.643  35.498  1.00 26.71           C  
ATOM   1877  N   ALA A 150      23.423   9.917  38.237  1.00 33.06           N  
ATOM   1878  CA  ALA A 150      23.825  11.280  38.509  1.00 32.08           C  
ATOM   1879  C   ALA A 150      25.258  11.547  38.088  1.00 32.40           C  
ATOM   1880  O   ALA A 150      26.094  10.648  38.068  1.00 32.97           O  
ATOM   1881  CB  ALA A 150      23.634  11.597  40.007  1.00 31.60           C  
ATOM   1882  N   LYS A 151      25.535  12.811  37.803  1.00 33.75           N  
ATOM   1883  CA  LYS A 151      26.849  13.270  37.384  1.00 32.81           C  
ATOM   1884  C   LYS A 151      27.139  14.582  38.122  1.00 30.46           C  
ATOM   1885  O   LYS A 151      26.246  15.389  38.321  1.00 31.94           O  
ATOM   1886  CB  LYS A 151      26.837  13.527  35.872  1.00 33.39           C  
ATOM   1887  CG  LYS A 151      28.205  13.800  35.278  1.00 37.26           C  
ATOM   1888  CD  LYS A 151      28.130  14.160  33.813  1.00 39.11           C  
ATOM   1889  CE  LYS A 151      29.523  14.477  33.282  1.00 40.34           C  
ATOM   1890  NZ  LYS A 151      29.542  14.863  31.834  1.00 41.19           N  
ATOM   1891  N   PHE A 152      28.369  14.771  38.570  1.00 28.89           N  
ATOM   1892  CA  PHE A 152      28.733  16.010  39.244  1.00 29.07           C  
ATOM   1893  C   PHE A 152      29.075  17.060  38.170  1.00 29.06           C  
ATOM   1894  O   PHE A 152      30.164  17.034  37.569  1.00 30.47           O  
ATOM   1895  CB  PHE A 152      29.928  15.769  40.182  1.00 29.61           C  
ATOM   1896  CG  PHE A 152      30.507  17.029  40.813  1.00 31.72           C  
ATOM   1897  CD1 PHE A 152      29.785  17.749  41.765  1.00 32.67           C  
ATOM   1898  CD2 PHE A 152      31.775  17.488  40.454  1.00 30.58           C  
ATOM   1899  CE1 PHE A 152      30.326  18.907  42.333  1.00 30.43           C  
ATOM   1900  CE2 PHE A 152      32.309  18.639  41.026  1.00 31.73           C  
ATOM   1901  CZ  PHE A 152      31.582  19.349  41.964  1.00 30.90           C  
ATOM   1902  N   THR A 153      28.125  17.937  37.873  1.00 28.89           N  
ATOM   1903  CA  THR A 153      28.377  18.981  36.903  1.00 30.33           C  
ATOM   1904  C   THR A 153      27.911  20.364  37.327  1.00 29.13           C  
ATOM   1905  O   THR A 153      27.186  20.548  38.296  1.00 27.74           O  
ATOM   1906  CB  THR A 153      27.752  18.696  35.489  1.00 33.81           C  
ATOM   1907  OG1 THR A 153      26.416  18.187  35.604  1.00 37.66           O  
ATOM   1908  CG2 THR A 153      28.603  17.713  34.704  1.00 38.25           C  
ATOM   1909  N   ASP A 154      28.398  21.336  36.577  1.00 29.05           N  
ATOM   1910  CA  ASP A 154      28.049  22.722  36.765  1.00 29.34           C  
ATOM   1911  C   ASP A 154      28.177  23.322  38.154  1.00 29.35           C  
ATOM   1912  O   ASP A 154      27.403  24.204  38.525  1.00 31.59           O  
ATOM   1913  CB  ASP A 154      26.672  22.959  36.183  1.00 25.74           C  
ATOM   1914  CG  ASP A 154      26.614  22.626  34.720  1.00 31.56           C  
ATOM   1915  OD1 ASP A 154      27.656  22.706  34.043  1.00 30.17           O  
ATOM   1916  OD2 ASP A 154      25.528  22.254  34.236  1.00 35.17           O  
ATOM   1917  N   PHE A 155      29.164  22.862  38.909  1.00 27.05           N  
ATOM   1918  CA  PHE A 155      29.399  23.424  40.223  1.00 27.01           C  
ATOM   1919  C   PHE A 155      29.686  24.922  40.105  1.00 27.14           C  
ATOM   1920  O   PHE A 155      30.653  25.326  39.441  1.00 29.34           O  
ATOM   1921  CB  PHE A 155      30.575  22.753  40.914  1.00 25.63           C  
ATOM   1922  CG  PHE A 155      30.908  23.371  42.239  1.00 25.74           C  
ATOM   1923  CD1 PHE A 155      30.098  23.126  43.349  1.00 24.06           C  
ATOM   1924  CD2 PHE A 155      31.985  24.245  42.375  1.00 26.78           C  
ATOM   1925  CE1 PHE A 155      30.345  23.740  44.558  1.00 22.83           C  
ATOM   1926  CE2 PHE A 155      32.241  24.870  43.609  1.00 27.44           C  
ATOM   1927  CZ  PHE A 155      31.419  24.618  44.698  1.00 25.13           C  
ATOM   1928  N   LYS A 156      28.892  25.738  40.800  1.00 26.86           N  
ATOM   1929  CA  LYS A 156      29.054  27.190  40.763  1.00 26.95           C  
ATOM   1930  C   LYS A 156      28.634  27.810  42.074  1.00 23.39           C  
ATOM   1931  O   LYS A 156      27.566  27.520  42.575  1.00 23.16           O  
ATOM   1932  CB  LYS A 156      28.209  27.773  39.635  1.00 30.35           C  
ATOM   1933  CG  LYS A 156      28.160  29.297  39.543  1.00 37.94           C  
ATOM   1934  CD  LYS A 156      27.229  29.682  38.404  1.00 44.09           C  
ATOM   1935  CE  LYS A 156      26.891  31.157  38.395  1.00 50.73           C  
ATOM   1936  NZ  LYS A 156      25.980  31.450  37.243  1.00 52.48           N  
ATOM   1937  N   ILE A 157      29.502  28.641  42.633  1.00 23.63           N  
ATOM   1938  CA  ILE A 157      29.243  29.355  43.881  1.00 23.21           C  
ATOM   1939  C   ILE A 157      28.380  30.558  43.499  1.00 22.68           C  
ATOM   1940  O   ILE A 157      28.748  31.320  42.617  1.00 23.35           O  
ATOM   1941  CB  ILE A 157      30.567  29.824  44.546  1.00 23.10           C  
ATOM   1942  CG1 ILE A 157      31.248  28.619  45.234  1.00 23.64           C  
ATOM   1943  CG2 ILE A 157      30.300  30.983  45.513  1.00 22.43           C  
ATOM   1944  CD1 ILE A 157      32.755  28.800  45.591  1.00 23.71           C  
ATOM   1945  N   GLN A 158      27.233  30.708  44.161  1.00 23.27           N  
ATOM   1946  CA  GLN A 158      26.273  31.785  43.882  1.00 21.69           C  
ATOM   1947  C   GLN A 158      26.278  32.938  44.871  1.00 22.02           C  
ATOM   1948  O   GLN A 158      25.861  34.048  44.524  1.00 21.50           O  
ATOM   1949  CB  GLN A 158      24.851  31.220  43.861  1.00 23.50           C  
ATOM   1950  CG  GLN A 158      24.629  30.061  42.896  1.00 22.72           C  
ATOM   1951  CD  GLN A 158      24.552  30.488  41.441  1.00 23.75           C  
ATOM   1952  OE1 GLN A 158      24.390  29.652  40.570  1.00 27.99           O  
ATOM   1953  NE2 GLN A 158      24.619  31.784  41.176  1.00 23.83           N  
ATOM   1954  N   ASN A 159      26.687  32.647  46.106  1.00 21.40           N  
ATOM   1955  CA  ASN A 159      26.713  33.631  47.173  1.00 22.71           C  
ATOM   1956  C   ASN A 159      27.771  33.287  48.236  1.00 21.99           C  
ATOM   1957  O   ASN A 159      27.973  32.102  48.583  1.00 21.90           O  
ATOM   1958  CB  ASN A 159      25.324  33.698  47.821  1.00 18.21           C  
ATOM   1959  CG  ASN A 159      25.190  34.810  48.851  1.00 23.11           C  
ATOM   1960  OD1 ASN A 159      25.730  35.908  48.688  1.00 22.80           O  
ATOM   1961  ND2 ASN A 159      24.430  34.540  49.907  1.00 26.13           N  
ATOM   1962  N   ILE A 160      28.500  34.325  48.655  1.00 21.45           N  
ATOM   1963  CA  ILE A 160      29.516  34.251  49.704  1.00 20.67           C  
ATOM   1964  C   ILE A 160      29.196  35.369  50.728  1.00 21.31           C  
ATOM   1965  O   ILE A 160      28.959  36.529  50.372  1.00 20.29           O  
ATOM   1966  CB  ILE A 160      30.959  34.443  49.165  1.00 23.19           C  
ATOM   1967  CG1 ILE A 160      31.318  33.335  48.172  1.00 24.76           C  
ATOM   1968  CG2 ILE A 160      31.989  34.439  50.312  1.00 20.08           C  
ATOM   1969  CD1 ILE A 160      32.714  33.508  47.561  1.00 23.38           C  
ATOM   1970  N   VAL A 161      29.187  34.983  51.996  1.00 20.71           N  
ATOM   1971  CA  VAL A 161      28.919  35.866  53.111  1.00 20.52           C  
ATOM   1972  C   VAL A 161      30.201  35.991  53.963  1.00 22.60           C  
ATOM   1973  O   VAL A 161      30.877  34.991  54.235  1.00 24.14           O  
ATOM   1974  CB  VAL A 161      27.765  35.297  54.010  1.00 21.02           C  
ATOM   1975  CG1 VAL A 161      27.380  36.279  55.094  1.00 22.24           C  
ATOM   1976  CG2 VAL A 161      26.564  34.948  53.175  1.00 20.26           C  
ATOM   1977  N   GLY A 162      30.535  37.210  54.385  1.00 22.22           N  
ATOM   1978  CA  GLY A 162      31.711  37.400  55.209  1.00 21.68           C  
ATOM   1979  C   GLY A 162      31.401  38.353  56.346  1.00 24.23           C  
ATOM   1980  O   GLY A 162      30.390  39.039  56.315  1.00 23.26           O  
ATOM   1981  N   SER A 163      32.231  38.361  57.378  1.00 25.27           N  
ATOM   1982  CA  SER A 163      32.021  39.290  58.483  1.00 27.65           C  
ATOM   1983  C   SER A 163      33.324  39.623  59.201  1.00 27.75           C  
ATOM   1984  O   SER A 163      34.319  38.901  59.083  1.00 27.51           O  
ATOM   1985  CB  SER A 163      30.994  38.758  59.486  1.00 26.27           C  
ATOM   1986  OG  SER A 163      31.509  37.678  60.229  1.00 28.91           O  
ATOM   1987  N   CYS A 164      33.326  40.773  59.872  1.00 28.53           N  
ATOM   1988  CA  CYS A 164      34.467  41.210  60.657  1.00 31.36           C  
ATOM   1989  C   CYS A 164      34.084  42.249  61.718  1.00 33.09           C  
ATOM   1990  O   CYS A 164      32.904  42.658  61.823  1.00 31.95           O  
ATOM   1991  CB  CYS A 164      35.624  41.687  59.766  1.00 34.89           C  
ATOM   1992  SG  CYS A 164      35.220  42.967  58.614  1.00 35.54           S  
ATOM   1993  N   ASP A 165      35.091  42.685  62.477  1.00 33.83           N  
ATOM   1994  CA  ASP A 165      34.901  43.627  63.564  1.00 33.30           C  
ATOM   1995  C   ASP A 165      35.945  44.722  63.454  1.00 35.01           C  
ATOM   1996  O   ASP A 165      37.133  44.422  63.497  1.00 34.29           O  
ATOM   1997  CB  ASP A 165      35.123  42.860  64.852  1.00 33.14           C  
ATOM   1998  CG  ASP A 165      34.651  43.595  66.055  1.00 35.75           C  
ATOM   1999  OD1 ASP A 165      34.374  44.806  65.977  1.00 38.06           O  
ATOM   2000  OD2 ASP A 165      34.552  42.941  67.104  1.00 42.43           O  
ATOM   2001  N   VAL A 166      35.523  45.985  63.337  1.00 35.84           N  
ATOM   2002  CA  VAL A 166      36.502  47.078  63.229  1.00 36.21           C  
ATOM   2003  C   VAL A 166      37.004  47.578  64.562  1.00 37.76           C  
ATOM   2004  O   VAL A 166      37.910  48.394  64.608  1.00 39.31           O  
ATOM   2005  CB  VAL A 166      36.021  48.284  62.408  1.00 36.36           C  
ATOM   2006  CG1 VAL A 166      35.793  47.869  60.962  1.00 36.71           C  
ATOM   2007  CG2 VAL A 166      34.791  48.931  63.035  1.00 34.02           C  
ATOM   2008  N   LYS A 167      36.373  47.105  65.628  1.00 37.86           N  
ATOM   2009  CA  LYS A 167      36.744  47.425  67.004  1.00 39.54           C  
ATOM   2010  C   LYS A 167      36.422  48.825  67.548  1.00 38.71           C  
ATOM   2011  O   LYS A 167      36.965  49.228  68.574  1.00 39.78           O  
ATOM   2012  CB  LYS A 167      38.209  47.043  67.268  1.00 42.07           C  
ATOM   2013  CG  LYS A 167      38.522  45.557  67.038  1.00 46.13           C  
ATOM   2014  CD  LYS A 167      37.861  44.663  68.083  1.00 52.78           C  
ATOM   2015  CE  LYS A 167      38.253  43.176  67.943  1.00 57.67           C  
ATOM   2016  NZ  LYS A 167      39.733  42.872  68.070  1.00 63.26           N  
ATOM   2017  N   PHE A 168      35.519  49.540  66.879  1.00 35.80           N  
ATOM   2018  CA  PHE A 168      35.079  50.863  67.339  1.00 35.97           C  
ATOM   2019  C   PHE A 168      33.624  51.043  66.964  1.00 35.86           C  
ATOM   2020  O   PHE A 168      33.163  50.384  66.021  1.00 34.51           O  
ATOM   2021  CB  PHE A 168      35.950  52.046  66.815  1.00 32.51           C  
ATOM   2022  CG  PHE A 168      36.159  52.082  65.293  1.00 32.92           C  
ATOM   2023  CD1 PHE A 168      35.228  52.674  64.446  1.00 30.64           C  
ATOM   2024  CD2 PHE A 168      37.329  51.599  64.735  1.00 31.56           C  
ATOM   2025  CE1 PHE A 168      35.499  52.775  63.080  1.00 27.82           C  
ATOM   2026  CE2 PHE A 168      37.582  51.708  63.374  1.00 28.83           C  
ATOM   2027  CZ  PHE A 168      36.674  52.294  62.552  1.00 27.11           C  
ATOM   2028  N   PRO A 169      32.868  51.878  67.725  1.00 35.52           N  
ATOM   2029  CA  PRO A 169      31.448  52.129  67.452  1.00 34.46           C  
ATOM   2030  C   PRO A 169      31.315  53.060  66.260  1.00 34.26           C  
ATOM   2031  O   PRO A 169      32.183  53.927  66.038  1.00 34.01           O  
ATOM   2032  CB  PRO A 169      30.970  52.840  68.724  1.00 36.13           C  
ATOM   2033  CG  PRO A 169      31.965  52.440  69.763  1.00 34.33           C  
ATOM   2034  CD  PRO A 169      33.251  52.512  68.998  1.00 35.00           C  
ATOM   2035  N   ILE A 170      30.195  52.941  65.548  1.00 32.45           N  
ATOM   2036  CA  ILE A 170      29.940  53.741  64.352  1.00 32.00           C  
ATOM   2037  C   ILE A 170      28.678  54.605  64.463  1.00 31.75           C  
ATOM   2038  O   ILE A 170      27.661  54.181  65.022  1.00 29.18           O  
ATOM   2039  CB  ILE A 170      29.826  52.827  63.085  1.00 32.82           C  
ATOM   2040  CG1 ILE A 170      31.062  51.925  62.964  1.00 33.04           C  
ATOM   2041  CG2 ILE A 170      29.686  53.673  61.808  1.00 29.27           C  
ATOM   2042  CD1 ILE A 170      30.949  50.879  61.849  1.00 35.50           C  
ATOM   2043  N   ARG A 171      28.743  55.807  63.890  1.00 30.90           N  
ATOM   2044  CA  ARG A 171      27.621  56.748  63.867  1.00 30.31           C  
ATOM   2045  C   ARG A 171      26.790  56.481  62.597  1.00 29.88           C  
ATOM   2046  O   ARG A 171      26.983  57.111  61.546  1.00 29.49           O  
ATOM   2047  CB  ARG A 171      28.156  58.188  63.910  1.00 32.88           C  
ATOM   2048  CG  ARG A 171      28.680  58.649  65.296  1.00 34.05           C  
ATOM   2049  CD  ARG A 171      29.956  59.512  65.228  1.00 37.67           C  
ATOM   2050  NE  ARG A 171      29.877  60.554  64.196  1.00 41.41           N  
ATOM   2051  CZ  ARG A 171      30.888  60.900  63.395  1.00 39.97           C  
ATOM   2052  NH1 ARG A 171      32.077  60.307  63.499  1.00 34.75           N  
ATOM   2053  NH2 ARG A 171      30.694  61.825  62.461  1.00 39.81           N  
ATOM   2054  N   LEU A 172      25.821  55.578  62.718  1.00 27.95           N  
ATOM   2055  CA  LEU A 172      25.011  55.176  61.571  1.00 26.97           C  
ATOM   2056  C   LEU A 172      24.195  56.264  60.923  1.00 29.20           C  
ATOM   2057  O   LEU A 172      24.054  56.280  59.702  1.00 29.83           O  
ATOM   2058  CB  LEU A 172      24.115  53.979  61.923  1.00 25.93           C  
ATOM   2059  CG  LEU A 172      24.815  52.710  62.426  1.00 24.49           C  
ATOM   2060  CD1 LEU A 172      23.815  51.605  62.646  1.00 20.99           C  
ATOM   2061  CD2 LEU A 172      25.862  52.270  61.423  1.00 24.20           C  
ATOM   2062  N   GLU A 173      23.659  57.174  61.730  1.00 32.47           N  
ATOM   2063  CA  GLU A 173      22.838  58.264  61.219  1.00 32.84           C  
ATOM   2064  C   GLU A 173      23.670  59.248  60.385  1.00 30.34           C  
ATOM   2065  O   GLU A 173      23.204  59.741  59.364  1.00 30.26           O  
ATOM   2066  CB  GLU A 173      22.105  58.962  62.379  1.00 37.90           C  
ATOM   2067  CG  GLU A 173      21.078  60.021  61.967  1.00 46.36           C  
ATOM   2068  CD  GLU A 173      20.185  59.569  60.815  1.00 53.32           C  
ATOM   2069  OE1 GLU A 173      19.459  58.551  60.963  1.00 58.65           O  
ATOM   2070  OE2 GLU A 173      20.228  60.238  59.754  1.00 56.98           O  
ATOM   2071  N   GLY A 174      24.909  59.498  60.811  1.00 28.47           N  
ATOM   2072  CA  GLY A 174      25.799  60.391  60.093  1.00 27.70           C  
ATOM   2073  C   GLY A 174      26.181  59.781  58.766  1.00 29.66           C  
ATOM   2074  O   GLY A 174      26.116  60.453  57.724  1.00 31.30           O  
ATOM   2075  N   LEU A 175      26.528  58.490  58.802  1.00 28.83           N  
ATOM   2076  CA  LEU A 175      26.897  57.716  57.618  1.00 28.59           C  
ATOM   2077  C   LEU A 175      25.736  57.679  56.633  1.00 28.41           C  
ATOM   2078  O   LEU A 175      25.914  57.977  55.457  1.00 30.73           O  
ATOM   2079  CB  LEU A 175      27.308  56.296  58.035  1.00 33.08           C  
ATOM   2080  CG  LEU A 175      27.692  55.108  57.114  1.00 37.12           C  
ATOM   2081  CD1 LEU A 175      28.152  55.523  55.741  1.00 35.81           C  
ATOM   2082  CD2 LEU A 175      28.798  54.303  57.811  1.00 34.13           C  
ATOM   2083  N   ALA A 176      24.529  57.419  57.120  1.00 28.69           N  
ATOM   2084  CA  ALA A 176      23.343  57.363  56.273  1.00 31.29           C  
ATOM   2085  C   ALA A 176      23.075  58.709  55.589  1.00 34.32           C  
ATOM   2086  O   ALA A 176      22.597  58.752  54.429  1.00 36.79           O  
ATOM   2087  CB  ALA A 176      22.123  56.934  57.096  1.00 30.42           C  
ATOM   2088  N   PHE A 177      23.348  59.803  56.299  1.00 34.57           N  
ATOM   2089  CA  PHE A 177      23.131  61.150  55.770  1.00 33.40           C  
ATOM   2090  C   PHE A 177      24.191  61.460  54.702  1.00 32.73           C  
ATOM   2091  O   PHE A 177      23.884  61.981  53.616  1.00 30.36           O  
ATOM   2092  CB  PHE A 177      23.167  62.155  56.926  1.00 34.75           C  
ATOM   2093  CG  PHE A 177      23.053  63.610  56.503  1.00 39.78           C  
ATOM   2094  CD1 PHE A 177      21.854  64.130  56.015  1.00 41.00           C  
ATOM   2095  CD2 PHE A 177      24.148  64.475  56.633  1.00 39.84           C  
ATOM   2096  CE1 PHE A 177      21.747  65.490  55.668  1.00 41.10           C  
ATOM   2097  CE2 PHE A 177      24.036  65.829  56.286  1.00 39.93           C  
ATOM   2098  CZ  PHE A 177      22.843  66.333  55.806  1.00 39.86           C  
ATOM   2099  N   SER A 178      25.433  61.097  55.005  1.00 30.42           N  
ATOM   2100  CA  SER A 178      26.559  61.317  54.109  1.00 31.99           C  
ATOM   2101  C   SER A 178      26.546  60.430  52.860  1.00 31.97           C  
ATOM   2102  O   SER A 178      26.863  60.871  51.749  1.00 30.28           O  
ATOM   2103  CB  SER A 178      27.850  61.107  54.872  1.00 30.97           C  
ATOM   2104  OG  SER A 178      28.955  61.132  53.991  1.00 38.79           O  
ATOM   2105  N   HIS A 179      26.223  59.164  53.047  1.00 30.85           N  
ATOM   2106  CA  HIS A 179      26.189  58.229  51.941  1.00 28.88           C  
ATOM   2107  C   HIS A 179      24.764  57.808  51.642  1.00 29.43           C  
ATOM   2108  O   HIS A 179      24.483  56.655  51.329  1.00 27.86           O  
ATOM   2109  CB  HIS A 179      27.061  57.026  52.257  1.00 27.23           C  
ATOM   2110  CG  HIS A 179      28.520  57.345  52.287  1.00 28.48           C  
ATOM   2111  ND1 HIS A 179      29.457  56.621  51.603  1.00 27.48           N  
ATOM   2112  CD2 HIS A 179      29.196  58.338  52.927  1.00 29.56           C  
ATOM   2113  CE1 HIS A 179      30.646  57.125  51.785  1.00 27.33           C  
ATOM   2114  NE2 HIS A 179      30.533  58.177  52.595  1.00 31.42           N  
ATOM   2115  N   GLY A 180      23.896  58.808  51.642  1.00 28.55           N  
ATOM   2116  CA  GLY A 180      22.480  58.604  51.414  1.00 29.88           C  
ATOM   2117  C   GLY A 180      22.022  57.789  50.226  1.00 31.07           C  
ATOM   2118  O   GLY A 180      21.089  57.003  50.362  1.00 35.02           O  
ATOM   2119  N   THR A 181      22.638  57.950  49.062  1.00 30.48           N  
ATOM   2120  CA  THR A 181      22.175  57.191  47.910  1.00 31.08           C  
ATOM   2121  C   THR A 181      22.479  55.707  47.939  1.00 29.42           C  
ATOM   2122  O   THR A 181      21.837  54.941  47.211  1.00 31.10           O  
ATOM   2123  CB  THR A 181      22.657  57.784  46.593  1.00 29.97           C  
ATOM   2124  OG1 THR A 181      24.012  58.236  46.731  1.00 33.70           O  
ATOM   2125  CG2 THR A 181      21.756  58.923  46.203  1.00 35.29           C  
ATOM   2126  N   PHE A 182      23.464  55.306  48.747  1.00 28.16           N  
ATOM   2127  CA  PHE A 182      23.832  53.888  48.868  1.00 27.05           C  
ATOM   2128  C   PHE A 182      23.282  53.274  50.155  1.00 29.56           C  
ATOM   2129  O   PHE A 182      23.155  52.062  50.263  1.00 30.08           O  
ATOM   2130  CB  PHE A 182      25.353  53.714  48.868  1.00 27.00           C  
ATOM   2131  CG  PHE A 182      26.046  54.453  47.751  1.00 29.93           C  
ATOM   2132  CD1 PHE A 182      25.666  54.270  46.428  1.00 28.03           C  
ATOM   2133  CD2 PHE A 182      27.019  55.393  48.030  1.00 30.92           C  
ATOM   2134  CE1 PHE A 182      26.240  55.020  45.410  1.00 29.11           C  
ATOM   2135  CE2 PHE A 182      27.593  56.150  47.012  1.00 33.21           C  
ATOM   2136  CZ  PHE A 182      27.200  55.964  45.701  1.00 31.38           C  
ATOM   2137  N   SER A 183      22.928  54.127  51.107  1.00 27.62           N  
ATOM   2138  CA  SER A 183      22.461  53.709  52.409  1.00 27.20           C  
ATOM   2139  C   SER A 183      20.971  53.637  52.629  1.00 29.48           C  
ATOM   2140  O   SER A 183      20.199  54.386  52.042  1.00 33.97           O  
ATOM   2141  CB  SER A 183      23.048  54.642  53.466  1.00 27.25           C  
ATOM   2142  OG  SER A 183      24.461  54.563  53.457  1.00 26.27           O  
ATOM   2143  N   SER A 184      20.597  52.790  53.572  1.00 28.31           N  
ATOM   2144  CA  SER A 184      19.225  52.606  53.969  1.00 27.67           C  
ATOM   2145  C   SER A 184      19.345  52.298  55.456  1.00 26.84           C  
ATOM   2146  O   SER A 184      20.044  51.369  55.850  1.00 25.73           O  
ATOM   2147  CB  SER A 184      18.597  51.455  53.190  1.00 27.96           C  
ATOM   2148  OG  SER A 184      17.324  51.133  53.711  1.00 33.57           O  
ATOM   2149  N   TYR A 185      18.713  53.125  56.275  1.00 24.98           N  
ATOM   2150  CA  TYR A 185      18.777  52.970  57.709  1.00 28.09           C  
ATOM   2151  C   TYR A 185      17.464  53.343  58.353  1.00 30.85           C  
ATOM   2152  O   TYR A 185      17.065  54.505  58.350  1.00 30.80           O  
ATOM   2153  CB  TYR A 185      19.892  53.862  58.263  1.00 29.33           C  
ATOM   2154  CG  TYR A 185      20.102  53.802  59.768  1.00 30.80           C  
ATOM   2155  CD1 TYR A 185      20.213  52.569  60.429  1.00 30.31           C  
ATOM   2156  CD2 TYR A 185      20.196  54.976  60.531  1.00 28.49           C  
ATOM   2157  CE1 TYR A 185      20.411  52.493  61.811  1.00 30.70           C  
ATOM   2158  CE2 TYR A 185      20.384  54.918  61.918  1.00 27.10           C  
ATOM   2159  CZ  TYR A 185      20.491  53.671  62.552  1.00 31.77           C  
ATOM   2160  OH  TYR A 185      20.651  53.574  63.912  1.00 30.84           O  
ATOM   2161  N   GLU A 186      16.807  52.342  58.921  1.00 31.94           N  
ATOM   2162  CA  GLU A 186      15.534  52.497  59.622  1.00 33.16           C  
ATOM   2163  C   GLU A 186      15.696  51.617  60.873  1.00 33.16           C  
ATOM   2164  O   GLU A 186      15.176  50.498  60.907  1.00 29.46           O  
ATOM   2165  CB  GLU A 186      14.396  51.978  58.747  1.00 36.78           C  
ATOM   2166  CG  GLU A 186      14.194  52.802  57.494  1.00 46.44           C  
ATOM   2167  CD  GLU A 186      13.433  52.044  56.429  1.00 51.90           C  
ATOM   2168  OE1 GLU A 186      12.246  51.678  56.664  1.00 54.80           O  
ATOM   2169  OE2 GLU A 186      14.046  51.801  55.362  1.00 54.67           O  
ATOM   2170  N   PRO A 187      16.362  52.157  61.932  1.00 34.16           N  
ATOM   2171  CA  PRO A 187      16.658  51.510  63.219  1.00 33.77           C  
ATOM   2172  C   PRO A 187      15.471  50.904  63.966  1.00 36.04           C  
ATOM   2173  O   PRO A 187      15.636  50.034  64.823  1.00 38.72           O  
ATOM   2174  CB  PRO A 187      17.348  52.610  64.006  1.00 29.08           C  
ATOM   2175  CG  PRO A 187      16.677  53.802  63.545  1.00 28.86           C  
ATOM   2176  CD  PRO A 187      16.605  53.613  62.052  1.00 33.93           C  
ATOM   2177  N   GLU A 188      14.271  51.369  63.662  1.00 37.25           N  
ATOM   2178  CA  GLU A 188      13.093  50.822  64.288  1.00 38.50           C  
ATOM   2179  C   GLU A 188      12.680  49.556  63.534  1.00 37.73           C  
ATOM   2180  O   GLU A 188      12.024  48.681  64.093  1.00 39.65           O  
ATOM   2181  CB  GLU A 188      11.970  51.849  64.239  1.00 46.51           C  
ATOM   2182  CG  GLU A 188      11.363  52.181  65.596  1.00 55.46           C  
ATOM   2183  CD  GLU A 188      12.387  52.703  66.590  1.00 60.67           C  
ATOM   2184  OE1 GLU A 188      13.268  53.516  66.194  1.00 64.84           O  
ATOM   2185  OE2 GLU A 188      12.301  52.279  67.767  1.00 64.64           O  
ATOM   2186  N   LEU A 189      13.062  49.458  62.264  1.00 34.40           N  
ATOM   2187  CA  LEU A 189      12.707  48.302  61.452  1.00 31.93           C  
ATOM   2188  C   LEU A 189      13.776  47.220  61.570  1.00 30.04           C  
ATOM   2189  O   LEU A 189      13.469  46.044  61.737  1.00 30.14           O  
ATOM   2190  CB  LEU A 189      12.520  48.728  59.998  1.00 30.46           C  
ATOM   2191  CG  LEU A 189      12.153  47.598  59.052  1.00 32.59           C  
ATOM   2192  CD1 LEU A 189      10.757  47.080  59.350  1.00 36.79           C  
ATOM   2193  CD2 LEU A 189      12.239  48.084  57.625  1.00 35.28           C  
ATOM   2194  N   PHE A 190      15.030  47.639  61.513  1.00 28.50           N  
ATOM   2195  CA  PHE A 190      16.172  46.747  61.609  1.00 26.06           C  
ATOM   2196  C   PHE A 190      17.303  47.688  62.100  1.00 24.81           C  
ATOM   2197  O   PHE A 190      17.484  48.779  61.565  1.00 25.42           O  
ATOM   2198  CB  PHE A 190      16.436  46.097  60.233  1.00 23.47           C  
ATOM   2199  CG  PHE A 190      17.612  45.141  60.219  1.00 23.53           C  
ATOM   2200  CD1 PHE A 190      17.570  43.938  60.920  1.00 23.09           C  
ATOM   2201  CD2 PHE A 190      18.802  45.503  59.598  1.00 22.48           C  
ATOM   2202  CE1 PHE A 190      18.693  43.126  61.016  1.00 20.96           C  
ATOM   2203  CE2 PHE A 190      19.926  44.701  59.689  1.00 22.32           C  
ATOM   2204  CZ  PHE A 190      19.881  43.502  60.407  1.00 21.20           C  
ATOM   2205  N   PRO A 191      18.039  47.287  63.154  1.00 25.15           N  
ATOM   2206  CA  PRO A 191      19.121  48.096  63.720  1.00 24.98           C  
ATOM   2207  C   PRO A 191      20.370  48.399  62.888  1.00 26.47           C  
ATOM   2208  O   PRO A 191      21.141  49.297  63.260  1.00 27.19           O  
ATOM   2209  CB  PRO A 191      19.488  47.334  64.994  1.00 21.35           C  
ATOM   2210  CG  PRO A 191      19.267  45.950  64.606  1.00 24.76           C  
ATOM   2211  CD  PRO A 191      17.939  46.008  63.878  1.00 25.76           C  
ATOM   2212  N   GLY A 192      20.608  47.635  61.821  1.00 24.13           N  
ATOM   2213  CA  GLY A 192      21.796  47.858  61.011  1.00 22.59           C  
ATOM   2214  C   GLY A 192      21.555  48.697  59.780  1.00 23.17           C  
ATOM   2215  O   GLY A 192      20.432  48.794  59.301  1.00 22.42           O  
ATOM   2216  N   LEU A 193      22.609  49.348  59.309  1.00 23.30           N  
ATOM   2217  CA  LEU A 193      22.545  50.172  58.107  1.00 24.46           C  
ATOM   2218  C   LEU A 193      22.828  49.261  56.893  1.00 23.05           C  
ATOM   2219  O   LEU A 193      23.767  48.476  56.916  1.00 24.20           O  
ATOM   2220  CB  LEU A 193      23.595  51.296  58.193  1.00 22.94           C  
ATOM   2221  CG  LEU A 193      23.617  52.357  57.083  1.00 26.57           C  
ATOM   2222  CD1 LEU A 193      24.012  53.674  57.704  1.00 26.35           C  
ATOM   2223  CD2 LEU A 193      24.579  51.987  55.947  1.00 23.85           C  
ATOM   2224  N   ILE A 194      22.001  49.345  55.855  1.00 21.75           N  
ATOM   2225  CA  ILE A 194      22.189  48.540  54.655  1.00 20.63           C  
ATOM   2226  C   ILE A 194      22.859  49.408  53.606  1.00 20.17           C  
ATOM   2227  O   ILE A 194      22.288  50.386  53.131  1.00 19.64           O  
ATOM   2228  CB  ILE A 194      20.862  47.961  54.169  1.00 20.07           C  
ATOM   2229  CG1 ILE A 194      20.323  47.051  55.267  1.00 23.14           C  
ATOM   2230  CG2 ILE A 194      21.043  47.145  52.900  1.00 17.79           C  
ATOM   2231  CD1 ILE A 194      18.852  47.011  55.281  1.00 25.65           C  
ATOM   2232  N   TYR A 195      24.108  49.070  53.313  1.00 22.30           N  
ATOM   2233  CA  TYR A 195      24.915  49.809  52.364  1.00 21.66           C  
ATOM   2234  C   TYR A 195      25.081  49.024  51.071  1.00 21.00           C  
ATOM   2235  O   TYR A 195      25.633  47.925  51.064  1.00 20.09           O  
ATOM   2236  CB  TYR A 195      26.267  50.109  52.999  1.00 22.06           C  
ATOM   2237  CG  TYR A 195      27.057  51.176  52.283  1.00 27.07           C  
ATOM   2238  CD1 TYR A 195      27.671  50.906  51.058  1.00 26.95           C  
ATOM   2239  CD2 TYR A 195      27.242  52.454  52.849  1.00 28.51           C  
ATOM   2240  CE1 TYR A 195      28.453  51.877  50.417  1.00 29.58           C  
ATOM   2241  CE2 TYR A 195      28.028  53.433  52.215  1.00 26.33           C  
ATOM   2242  CZ  TYR A 195      28.630  53.128  51.007  1.00 30.56           C  
ATOM   2243  OH  TYR A 195      29.450  54.022  50.393  1.00 30.98           O  
ATOM   2244  N   ARG A 196      24.578  49.592  49.979  1.00 21.44           N  
ATOM   2245  CA  ARG A 196      24.642  48.961  48.662  1.00 23.50           C  
ATOM   2246  C   ARG A 196      25.770  49.555  47.810  1.00 24.27           C  
ATOM   2247  O   ARG A 196      25.621  50.605  47.179  1.00 22.17           O  
ATOM   2248  CB  ARG A 196      23.276  49.035  47.962  1.00 24.37           C  
ATOM   2249  CG  ARG A 196      22.188  48.330  48.763  1.00 24.56           C  
ATOM   2250  CD  ARG A 196      20.909  48.128  47.994  1.00 31.89           C  
ATOM   2251  NE  ARG A 196      19.811  47.729  48.893  1.00 38.80           N  
ATOM   2252  CZ  ARG A 196      19.308  46.493  49.001  1.00 41.80           C  
ATOM   2253  NH1 ARG A 196      19.790  45.502  48.247  1.00 44.99           N  
ATOM   2254  NH2 ARG A 196      18.341  46.231  49.879  1.00 41.12           N  
ATOM   2255  N   MET A 197      26.920  48.885  47.850  1.00 25.13           N  
ATOM   2256  CA  MET A 197      28.113  49.303  47.120  1.00 27.15           C  
ATOM   2257  C   MET A 197      27.977  49.084  45.617  1.00 28.95           C  
ATOM   2258  O   MET A 197      27.431  48.073  45.174  1.00 30.63           O  
ATOM   2259  CB  MET A 197      29.363  48.569  47.649  1.00 25.14           C  
ATOM   2260  CG  MET A 197      30.687  49.230  47.269  1.00 21.24           C  
ATOM   2261  SD  MET A 197      32.072  48.636  48.216  1.00 26.50           S  
ATOM   2262  CE  MET A 197      31.971  49.631  49.637  1.00 20.21           C  
ATOM   2263  N   VAL A 198      28.461  50.053  44.838  1.00 30.67           N  
ATOM   2264  CA  VAL A 198      28.430  49.981  43.380  1.00 29.97           C  
ATOM   2265  C   VAL A 198      29.543  49.069  42.824  1.00 28.52           C  
ATOM   2266  O   VAL A 198      29.258  48.107  42.100  1.00 30.50           O  
ATOM   2267  CB  VAL A 198      28.486  51.401  42.743  1.00 29.50           C  
ATOM   2268  CG1 VAL A 198      28.486  51.323  41.224  1.00 29.18           C  
ATOM   2269  CG2 VAL A 198      27.294  52.205  43.210  1.00 28.69           C  
ATOM   2270  N   LYS A 199      30.800  49.364  43.140  1.00 30.39           N  
ATOM   2271  CA  LYS A 199      31.923  48.540  42.662  1.00 34.36           C  
ATOM   2272  C   LYS A 199      32.887  48.203  43.807  1.00 32.86           C  
ATOM   2273  O   LYS A 199      33.525  49.099  44.395  1.00 33.10           O  
ATOM   2274  CB  LYS A 199      32.661  49.236  41.507  1.00 39.33           C  
ATOM   2275  CG  LYS A 199      33.161  48.299  40.384  1.00 48.03           C  
ATOM   2276  CD  LYS A 199      34.329  47.388  40.808  1.00 55.67           C  
ATOM   2277  CE  LYS A 199      34.147  45.951  40.248  1.00 60.46           C  
ATOM   2278  NZ  LYS A 199      35.131  44.905  40.751  1.00 62.41           N  
ATOM   2279  N   PRO A 200      32.933  46.912  44.220  1.00 29.82           N  
ATOM   2280  CA  PRO A 200      32.128  45.807  43.695  1.00 28.92           C  
ATOM   2281  C   PRO A 200      30.672  45.884  44.163  1.00 27.11           C  
ATOM   2282  O   PRO A 200      30.357  46.607  45.105  1.00 28.40           O  
ATOM   2283  CB  PRO A 200      32.837  44.572  44.259  1.00 27.37           C  
ATOM   2284  CG  PRO A 200      33.364  45.042  45.539  1.00 28.72           C  
ATOM   2285  CD  PRO A 200      33.900  46.406  45.223  1.00 29.11           C  
ATOM   2286  N   LYS A 201      29.777  45.196  43.465  1.00 28.47           N  
ATOM   2287  CA  LYS A 201      28.361  45.183  43.836  1.00 29.22           C  
ATOM   2288  C   LYS A 201      28.164  44.202  44.995  1.00 28.80           C  
ATOM   2289  O   LYS A 201      27.946  43.000  44.808  1.00 29.46           O  
ATOM   2290  CB  LYS A 201      27.493  44.816  42.647  1.00 28.20           C  
ATOM   2291  CG  LYS A 201      26.032  45.040  42.871  1.00 30.51           C  
ATOM   2292  CD  LYS A 201      25.320  44.975  41.550  1.00 34.19           C  
ATOM   2293  CE  LYS A 201      23.849  45.296  41.669  1.00 34.90           C  
ATOM   2294  NZ  LYS A 201      23.171  44.213  42.391  1.00 36.66           N  
ATOM   2295  N   ILE A 202      28.301  44.746  46.196  1.00 28.76           N  
ATOM   2296  CA  ILE A 202      28.211  44.004  47.444  1.00 26.55           C  
ATOM   2297  C   ILE A 202      27.295  44.780  48.383  1.00 25.05           C  
ATOM   2298  O   ILE A 202      27.210  46.022  48.315  1.00 22.69           O  
ATOM   2299  CB  ILE A 202      29.664  43.876  48.085  1.00 25.99           C  
ATOM   2300  CG1 ILE A 202      30.518  42.951  47.225  1.00 25.33           C  
ATOM   2301  CG2 ILE A 202      29.637  43.338  49.520  1.00 26.05           C  
ATOM   2302  CD1 ILE A 202      29.896  41.623  46.980  1.00 21.16           C  
ATOM   2303  N   VAL A 203      26.566  44.033  49.211  1.00 23.68           N  
ATOM   2304  CA  VAL A 203      25.683  44.622  50.215  1.00 22.54           C  
ATOM   2305  C   VAL A 203      26.332  44.436  51.586  1.00 22.36           C  
ATOM   2306  O   VAL A 203      26.740  43.325  51.936  1.00 19.50           O  
ATOM   2307  CB  VAL A 203      24.270  43.982  50.234  1.00 21.47           C  
ATOM   2308  CG1 VAL A 203      23.422  44.597  51.352  1.00 19.49           C  
ATOM   2309  CG2 VAL A 203      23.585  44.212  48.893  1.00 21.59           C  
ATOM   2310  N   LEU A 204      26.453  45.530  52.337  1.00 20.65           N  
ATOM   2311  CA  LEU A 204      27.032  45.476  53.675  1.00 21.23           C  
ATOM   2312  C   LEU A 204      26.009  45.876  54.735  1.00 21.69           C  
ATOM   2313  O   LEU A 204      25.196  46.776  54.514  1.00 20.23           O  
ATOM   2314  CB  LEU A 204      28.259  46.396  53.801  1.00 21.79           C  
ATOM   2315  CG  LEU A 204      29.420  46.272  52.793  1.00 24.58           C  
ATOM   2316  CD1 LEU A 204      29.170  47.169  51.564  1.00 24.65           C  
ATOM   2317  CD2 LEU A 204      30.706  46.694  53.489  1.00 26.49           C  
ATOM   2318  N   LEU A 205      26.004  45.153  55.853  1.00 21.07           N  
ATOM   2319  CA  LEU A 205      25.120  45.463  56.978  1.00 21.14           C  
ATOM   2320  C   LEU A 205      26.086  46.047  58.015  1.00 20.04           C  
ATOM   2321  O   LEU A 205      27.013  45.377  58.465  1.00 20.74           O  
ATOM   2322  CB  LEU A 205      24.430  44.202  57.522  1.00 21.19           C  
ATOM   2323  CG  LEU A 205      23.748  43.263  56.515  1.00 24.50           C  
ATOM   2324  CD1 LEU A 205      22.844  42.299  57.273  1.00 23.21           C  
ATOM   2325  CD2 LEU A 205      22.912  44.042  55.506  1.00 26.19           C  
ATOM   2326  N   ILE A 206      25.887  47.304  58.368  1.00 20.21           N  
ATOM   2327  CA  ILE A 206      26.770  47.981  59.307  1.00 22.75           C  
ATOM   2328  C   ILE A 206      26.070  48.256  60.646  1.00 21.46           C  
ATOM   2329  O   ILE A 206      24.975  48.834  60.688  1.00 21.32           O  
ATOM   2330  CB  ILE A 206      27.310  49.272  58.650  1.00 23.85           C  
ATOM   2331  CG1 ILE A 206      28.083  48.879  57.375  1.00 24.31           C  
ATOM   2332  CG2 ILE A 206      28.230  50.035  59.604  1.00 22.90           C  
ATOM   2333  CD1 ILE A 206      28.264  50.033  56.378  1.00 24.51           C  
ATOM   2334  N   PHE A 207      26.710  47.833  61.730  1.00 21.51           N  
ATOM   2335  CA  PHE A 207      26.126  47.985  63.044  1.00 23.10           C  
ATOM   2336  C   PHE A 207      26.876  48.958  63.963  1.00 23.73           C  
ATOM   2337  O   PHE A 207      28.102  49.090  63.869  1.00 24.06           O  
ATOM   2338  CB  PHE A 207      25.993  46.603  63.710  1.00 20.08           C  
ATOM   2339  CG  PHE A 207      25.182  45.625  62.895  1.00 21.62           C  
ATOM   2340  CD1 PHE A 207      25.776  44.851  61.914  1.00 23.16           C  
ATOM   2341  CD2 PHE A 207      23.801  45.510  63.082  1.00 21.89           C  
ATOM   2342  CE1 PHE A 207      25.023  43.977  61.131  1.00 25.36           C  
ATOM   2343  CE2 PHE A 207      23.044  44.641  62.307  1.00 23.16           C  
ATOM   2344  CZ  PHE A 207      23.655  43.871  61.327  1.00 24.79           C  
ATOM   2345  N   VAL A 208      26.134  49.582  64.886  1.00 25.74           N  
ATOM   2346  CA  VAL A 208      26.674  50.555  65.844  1.00 27.51           C  
ATOM   2347  C   VAL A 208      27.896  50.018  66.574  1.00 28.36           C  
ATOM   2348  O   VAL A 208      28.833  50.763  66.840  1.00 31.63           O  
ATOM   2349  CB  VAL A 208      25.603  50.993  66.905  1.00 25.79           C  
ATOM   2350  CG1 VAL A 208      26.231  51.877  67.984  1.00 30.78           C  
ATOM   2351  CG2 VAL A 208      24.533  51.803  66.234  1.00 29.28           C  
ATOM   2352  N   SER A 209      27.887  48.722  66.863  1.00 28.47           N  
ATOM   2353  CA  SER A 209      28.974  48.049  67.567  1.00 29.33           C  
ATOM   2354  C   SER A 209      30.289  47.981  66.799  1.00 30.05           C  
ATOM   2355  O   SER A 209      31.335  47.723  67.384  1.00 28.56           O  
ATOM   2356  CB  SER A 209      28.561  46.607  67.844  1.00 29.36           C  
ATOM   2357  OG  SER A 209      28.280  45.931  66.618  1.00 30.72           O  
ATOM   2358  N   GLY A 210      30.215  48.125  65.482  1.00 29.00           N  
ATOM   2359  CA  GLY A 210      31.408  48.016  64.672  1.00 28.58           C  
ATOM   2360  C   GLY A 210      31.498  46.659  63.984  1.00 26.76           C  
ATOM   2361  O   GLY A 210      32.484  46.365  63.300  1.00 25.36           O  
ATOM   2362  N   LYS A 211      30.507  45.794  64.201  1.00 27.96           N  
ATOM   2363  CA  LYS A 211      30.505  44.485  63.526  1.00 27.52           C  
ATOM   2364  C   LYS A 211      29.991  44.758  62.102  1.00 28.30           C  
ATOM   2365  O   LYS A 211      29.081  45.583  61.925  1.00 28.72           O  
ATOM   2366  CB  LYS A 211      29.577  43.495  64.217  1.00 24.53           C  
ATOM   2367  CG  LYS A 211      29.947  43.186  65.664  1.00 24.93           C  
ATOM   2368  CD  LYS A 211      31.139  42.252  65.756  1.00 30.40           C  
ATOM   2369  CE  LYS A 211      31.039  41.344  66.994  1.00 32.37           C  
ATOM   2370  NZ  LYS A 211      31.046  42.076  68.274  1.00 31.42           N  
ATOM   2371  N   ILE A 212      30.598  44.114  61.102  1.00 27.16           N  
ATOM   2372  CA  ILE A 212      30.232  44.311  59.693  1.00 25.51           C  
ATOM   2373  C   ILE A 212      29.907  42.987  59.006  1.00 23.87           C  
ATOM   2374  O   ILE A 212      30.621  42.000  59.201  1.00 22.15           O  
ATOM   2375  CB  ILE A 212      31.421  44.952  58.889  1.00 28.20           C  
ATOM   2376  CG1 ILE A 212      31.938  46.221  59.595  1.00 25.95           C  
ATOM   2377  CG2 ILE A 212      31.004  45.305  57.453  1.00 29.83           C  
ATOM   2378  CD1 ILE A 212      30.887  47.326  59.715  1.00 24.70           C  
ATOM   2379  N   VAL A 213      28.852  42.983  58.186  1.00 23.87           N  
ATOM   2380  CA  VAL A 213      28.451  41.807  57.398  1.00 22.34           C  
ATOM   2381  C   VAL A 213      28.510  42.213  55.910  1.00 21.38           C  
ATOM   2382  O   VAL A 213      28.010  43.279  55.538  1.00 21.39           O  
ATOM   2383  CB  VAL A 213      27.009  41.286  57.730  1.00 20.47           C  
ATOM   2384  CG1 VAL A 213      26.617  40.177  56.799  1.00 22.79           C  
ATOM   2385  CG2 VAL A 213      26.967  40.741  59.109  1.00 20.72           C  
ATOM   2386  N   LEU A 214      29.144  41.380  55.081  1.00 20.09           N  
ATOM   2387  CA  LEU A 214      29.288  41.615  53.641  1.00 21.04           C  
ATOM   2388  C   LEU A 214      28.704  40.397  52.950  1.00 20.91           C  
ATOM   2389  O   LEU A 214      29.037  39.267  53.309  1.00 19.87           O  
ATOM   2390  CB  LEU A 214      30.768  41.752  53.245  1.00 20.29           C  
ATOM   2391  CG  LEU A 214      31.607  42.788  54.022  1.00 24.68           C  
ATOM   2392  CD1 LEU A 214      32.387  42.112  55.181  1.00 20.57           C  
ATOM   2393  CD2 LEU A 214      32.586  43.465  53.067  1.00 22.26           C  
ATOM   2394  N   THR A 215      27.872  40.631  51.938  1.00 21.85           N  
ATOM   2395  CA  THR A 215      27.185  39.551  51.216  1.00 22.13           C  
ATOM   2396  C   THR A 215      26.873  39.927  49.758  1.00 23.91           C  
ATOM   2397  O   THR A 215      26.935  41.109  49.382  1.00 24.90           O  
ATOM   2398  CB  THR A 215      25.855  39.145  51.940  1.00 21.53           C  
ATOM   2399  OG1 THR A 215      25.341  37.929  51.376  1.00 24.01           O  
ATOM   2400  CG2 THR A 215      24.794  40.229  51.811  1.00 18.89           C  
ATOM   2401  N   GLY A 216      26.513  38.914  48.964  1.00 24.24           N  
ATOM   2402  CA  GLY A 216      26.198  39.101  47.558  1.00 20.56           C  
ATOM   2403  C   GLY A 216      27.388  38.842  46.642  1.00 23.42           C  
ATOM   2404  O   GLY A 216      27.310  39.094  45.436  1.00 23.64           O  
ATOM   2405  N   ALA A 217      28.497  38.356  47.200  1.00 22.70           N  
ATOM   2406  CA  ALA A 217      29.713  38.086  46.413  1.00 24.77           C  
ATOM   2407  C   ALA A 217      29.706  36.737  45.689  1.00 25.26           C  
ATOM   2408  O   ALA A 217      29.170  35.753  46.190  1.00 25.26           O  
ATOM   2409  CB  ALA A 217      30.960  38.167  47.301  1.00 20.96           C  
ATOM   2410  N   LYS A 218      30.310  36.716  44.500  1.00 28.19           N  
ATOM   2411  CA  LYS A 218      30.464  35.515  43.677  1.00 28.58           C  
ATOM   2412  C   LYS A 218      31.910  35.016  43.816  1.00 31.12           C  
ATOM   2413  O   LYS A 218      32.190  33.841  43.604  1.00 29.38           O  
ATOM   2414  CB  LYS A 218      30.182  35.838  42.214  1.00 26.92           C  
ATOM   2415  CG  LYS A 218      28.708  35.986  41.881  1.00 29.57           C  
ATOM   2416  CD  LYS A 218      28.027  34.638  41.752  1.00 34.32           C  
ATOM   2417  CE  LYS A 218      26.704  34.745  41.004  1.00 34.65           C  
ATOM   2418  NZ  LYS A 218      25.543  34.742  41.929  1.00 39.86           N  
ATOM   2419  N   GLN A 219      32.800  35.921  44.223  1.00 31.83           N  
ATOM   2420  CA  GLN A 219      34.217  35.623  44.410  1.00 32.38           C  
ATOM   2421  C   GLN A 219      34.727  36.273  45.700  1.00 31.14           C  
ATOM   2422  O   GLN A 219      34.329  37.384  46.052  1.00 27.23           O  
ATOM   2423  CB  GLN A 219      35.037  36.132  43.212  1.00 35.47           C  
ATOM   2424  CG  GLN A 219      35.405  35.047  42.208  1.00 48.75           C  
ATOM   2425  CD  GLN A 219      34.333  34.799  41.147  1.00 58.46           C  
ATOM   2426  OE1 GLN A 219      34.137  33.662  40.701  1.00 62.61           O  
ATOM   2427  NE2 GLN A 219      33.672  35.868  40.698  1.00 65.61           N  
ATOM   2428  N   ARG A 220      35.608  35.570  46.400  1.00 30.63           N  
ATOM   2429  CA  ARG A 220      36.206  36.026  47.654  1.00 30.10           C  
ATOM   2430  C   ARG A 220      36.817  37.435  47.609  1.00 31.08           C  
ATOM   2431  O   ARG A 220      36.700  38.201  48.581  1.00 29.27           O  
ATOM   2432  CB  ARG A 220      37.258  34.993  48.105  1.00 34.26           C  
ATOM   2433  CG  ARG A 220      38.131  35.428  49.272  1.00 36.32           C  
ATOM   2434  CD  ARG A 220      39.167  34.379  49.659  1.00 35.49           C  
ATOM   2435  NE  ARG A 220      38.598  33.099  50.114  1.00 32.66           N  
ATOM   2436  CZ  ARG A 220      39.019  32.440  51.193  1.00 31.55           C  
ATOM   2437  NH1 ARG A 220      39.994  32.956  51.939  1.00 33.23           N  
ATOM   2438  NH2 ARG A 220      38.560  31.217  51.464  1.00 27.95           N  
ATOM   2439  N   GLU A 221      37.455  37.786  46.490  1.00 30.89           N  
ATOM   2440  CA  GLU A 221      38.096  39.107  46.345  1.00 32.93           C  
ATOM   2441  C   GLU A 221      37.124  40.259  46.478  1.00 28.40           C  
ATOM   2442  O   GLU A 221      37.508  41.332  46.942  1.00 26.70           O  
ATOM   2443  CB  GLU A 221      38.874  39.255  45.023  1.00 37.04           C  
ATOM   2444  CG  GLU A 221      40.189  38.462  44.943  1.00 44.84           C  
ATOM   2445  CD  GLU A 221      40.942  38.685  43.625  1.00 49.50           C  
ATOM   2446  OE1 GLU A 221      40.407  38.304  42.542  1.00 50.41           O  
ATOM   2447  OE2 GLU A 221      42.069  39.246  43.687  1.00 49.43           O  
ATOM   2448  N   GLU A 222      35.873  40.029  46.081  1.00 26.56           N  
ATOM   2449  CA  GLU A 222      34.832  41.051  46.160  1.00 28.36           C  
ATOM   2450  C   GLU A 222      34.528  41.369  47.626  1.00 29.16           C  
ATOM   2451  O   GLU A 222      34.301  42.533  47.979  1.00 32.26           O  
ATOM   2452  CB  GLU A 222      33.569  40.625  45.423  1.00 28.13           C  
ATOM   2453  CG  GLU A 222      33.788  40.245  43.968  1.00 31.31           C  
ATOM   2454  CD  GLU A 222      32.572  39.567  43.319  1.00 37.16           C  
ATOM   2455  OE1 GLU A 222      31.736  38.986  44.032  1.00 38.71           O  
ATOM   2456  OE2 GLU A 222      32.462  39.595  42.070  1.00 45.62           O  
ATOM   2457  N   ILE A 223      34.535  40.356  48.488  1.00 29.01           N  
ATOM   2458  CA  ILE A 223      34.321  40.565  49.928  1.00 28.84           C  
ATOM   2459  C   ILE A 223      35.487  41.428  50.428  1.00 28.67           C  
ATOM   2460  O   ILE A 223      35.303  42.443  51.116  1.00 28.50           O  
ATOM   2461  CB  ILE A 223      34.354  39.206  50.717  1.00 29.82           C  
ATOM   2462  CG1 ILE A 223      33.173  38.311  50.301  1.00 34.27           C  
ATOM   2463  CG2 ILE A 223      34.398  39.437  52.250  1.00 27.45           C  
ATOM   2464  CD1 ILE A 223      31.769  38.761  50.812  1.00 37.40           C  
ATOM   2465  N   TYR A 224      36.697  41.030  50.056  1.00 28.86           N  
ATOM   2466  CA  TYR A 224      37.896  41.745  50.481  1.00 28.13           C  
ATOM   2467  C   TYR A 224      37.942  43.173  49.919  1.00 26.86           C  
ATOM   2468  O   TYR A 224      38.306  44.123  50.628  1.00 26.77           O  
ATOM   2469  CB  TYR A 224      39.145  40.967  50.054  1.00 27.65           C  
ATOM   2470  CG  TYR A 224      39.402  39.637  50.776  1.00 29.62           C  
ATOM   2471  CD1 TYR A 224      38.657  39.244  51.901  1.00 28.73           C  
ATOM   2472  CD2 TYR A 224      40.400  38.760  50.316  1.00 31.40           C  
ATOM   2473  CE1 TYR A 224      38.898  38.023  52.541  1.00 28.86           C  
ATOM   2474  CE2 TYR A 224      40.647  37.532  50.949  1.00 30.63           C  
ATOM   2475  CZ  TYR A 224      39.899  37.171  52.059  1.00 30.95           C  
ATOM   2476  OH  TYR A 224      40.181  35.979  52.682  1.00 32.41           O  
ATOM   2477  N   GLN A 225      37.508  43.328  48.670  1.00 26.89           N  
ATOM   2478  CA  GLN A 225      37.500  44.621  47.983  1.00 30.33           C  
ATOM   2479  C   GLN A 225      36.583  45.624  48.665  1.00 29.82           C  
ATOM   2480  O   GLN A 225      36.966  46.789  48.915  1.00 26.78           O  
ATOM   2481  CB  GLN A 225      37.033  44.433  46.545  1.00 36.75           C  
ATOM   2482  CG  GLN A 225      38.123  44.602  45.504  1.00 50.00           C  
ATOM   2483  CD  GLN A 225      38.088  43.520  44.416  1.00 56.40           C  
ATOM   2484  OE1 GLN A 225      37.024  43.207  43.847  1.00 54.48           O  
ATOM   2485  NE2 GLN A 225      39.280  42.975  44.091  1.00 61.40           N  
ATOM   2486  N   ALA A 226      35.365  45.168  48.952  1.00 26.53           N  
ATOM   2487  CA  ALA A 226      34.342  45.984  49.582  1.00 25.13           C  
ATOM   2488  C   ALA A 226      34.768  46.482  50.960  1.00 24.81           C  
ATOM   2489  O   ALA A 226      34.605  47.665  51.274  1.00 27.35           O  
ATOM   2490  CB  ALA A 226      33.029  45.220  49.659  1.00 20.29           C  
ATOM   2491  N   PHE A 227      35.331  45.600  51.782  1.00 26.06           N  
ATOM   2492  CA  PHE A 227      35.775  46.006  53.109  1.00 27.80           C  
ATOM   2493  C   PHE A 227      36.866  47.081  53.008  1.00 29.18           C  
ATOM   2494  O   PHE A 227      36.802  48.101  53.705  1.00 28.97           O  
ATOM   2495  CB  PHE A 227      36.258  44.822  53.940  1.00 26.00           C  
ATOM   2496  CG  PHE A 227      36.618  45.202  55.362  1.00 28.56           C  
ATOM   2497  CD1 PHE A 227      35.677  45.752  56.218  1.00 28.36           C  
ATOM   2498  CD2 PHE A 227      37.912  45.068  55.831  1.00 31.37           C  
ATOM   2499  CE1 PHE A 227      36.027  46.165  57.511  1.00 29.31           C  
ATOM   2500  CE2 PHE A 227      38.255  45.486  57.134  1.00 28.73           C  
ATOM   2501  CZ  PHE A 227      37.309  46.032  57.962  1.00 28.15           C  
ATOM   2502  N   GLU A 228      37.832  46.874  52.113  1.00 32.70           N  
ATOM   2503  CA  GLU A 228      38.916  47.827  51.909  1.00 34.84           C  
ATOM   2504  C   GLU A 228      38.302  49.148  51.544  1.00 32.39           C  
ATOM   2505  O   GLU A 228      38.729  50.191  52.028  1.00 33.15           O  
ATOM   2506  CB  GLU A 228      39.850  47.393  50.777  1.00 38.98           C  
ATOM   2507  CG  GLU A 228      40.821  46.277  51.117  1.00 55.31           C  
ATOM   2508  CD  GLU A 228      41.655  45.855  49.898  1.00 65.92           C  
ATOM   2509  OE1 GLU A 228      42.308  46.741  49.286  1.00 72.52           O  
ATOM   2510  OE2 GLU A 228      41.642  44.647  49.542  1.00 68.62           O  
ATOM   2511  N   ALA A 229      37.279  49.117  50.701  1.00 30.95           N  
ATOM   2512  CA  ALA A 229      36.622  50.346  50.273  1.00 28.59           C  
ATOM   2513  C   ALA A 229      35.793  51.016  51.355  1.00 29.20           C  
ATOM   2514  O   ALA A 229      35.743  52.251  51.425  1.00 28.50           O  
ATOM   2515  CB  ALA A 229      35.778  50.086  49.052  1.00 28.81           C  
ATOM   2516  N   ILE A 230      35.164  50.216  52.219  1.00 28.93           N  
ATOM   2517  CA  ILE A 230      34.331  50.764  53.293  1.00 28.10           C  
ATOM   2518  C   ILE A 230      35.110  51.241  54.533  1.00 29.56           C  
ATOM   2519  O   ILE A 230      34.721  52.272  55.135  1.00 27.61           O  
ATOM   2520  CB  ILE A 230      33.183  49.787  53.714  1.00 25.92           C  
ATOM   2521  CG1 ILE A 230      32.026  50.549  54.390  1.00 23.90           C  
ATOM   2522  CG2 ILE A 230      33.723  48.715  54.624  1.00 26.06           C  
ATOM   2523  CD1 ILE A 230      31.142  51.399  53.445  1.00 19.62           C  
ATOM   2524  N   TYR A 231      36.247  50.604  54.852  1.00 28.65           N  
ATOM   2525  CA  TYR A 231      37.021  50.974  56.052  1.00 29.87           C  
ATOM   2526  C   TYR A 231      37.264  52.462  56.313  1.00 30.76           C  
ATOM   2527  O   TYR A 231      37.080  52.925  57.452  1.00 31.21           O  
ATOM   2528  CB  TYR A 231      38.325  50.199  56.168  1.00 28.80           C  
ATOM   2529  CG  TYR A 231      38.914  50.263  57.574  1.00 34.65           C  
ATOM   2530  CD1 TYR A 231      38.528  49.347  58.564  1.00 35.81           C  
ATOM   2531  CD2 TYR A 231      39.863  51.241  57.924  1.00 38.05           C  
ATOM   2532  CE1 TYR A 231      39.073  49.396  59.862  1.00 36.16           C  
ATOM   2533  CE2 TYR A 231      40.414  51.297  59.217  1.00 38.57           C  
ATOM   2534  CZ  TYR A 231      40.018  50.368  60.175  1.00 39.36           C  
ATOM   2535  OH  TYR A 231      40.630  50.385  61.406  1.00 41.66           O  
ATOM   2536  N   PRO A 232      37.672  53.246  55.295  1.00 30.56           N  
ATOM   2537  CA  PRO A 232      37.911  54.686  55.496  1.00 31.86           C  
ATOM   2538  C   PRO A 232      36.640  55.416  55.932  1.00 32.62           C  
ATOM   2539  O   PRO A 232      36.685  56.374  56.726  1.00 30.40           O  
ATOM   2540  CB  PRO A 232      38.333  55.143  54.110  1.00 33.92           C  
ATOM   2541  CG  PRO A 232      39.046  53.961  53.563  1.00 33.74           C  
ATOM   2542  CD  PRO A 232      38.095  52.850  53.939  1.00 32.52           C  
ATOM   2543  N   VAL A 233      35.516  54.956  55.386  1.00 31.59           N  
ATOM   2544  CA  VAL A 233      34.208  55.524  55.678  1.00 31.63           C  
ATOM   2545  C   VAL A 233      33.772  55.206  57.102  1.00 32.44           C  
ATOM   2546  O   VAL A 233      33.208  56.057  57.789  1.00 34.28           O  
ATOM   2547  CB  VAL A 233      33.154  54.999  54.711  1.00 30.74           C  
ATOM   2548  CG1 VAL A 233      31.846  55.740  54.906  1.00 29.68           C  
ATOM   2549  CG2 VAL A 233      33.639  55.138  53.299  1.00 31.24           C  
ATOM   2550  N   LEU A 234      34.016  53.972  57.533  1.00 31.39           N  
ATOM   2551  CA  LEU A 234      33.659  53.567  58.879  1.00 29.99           C  
ATOM   2552  C   LEU A 234      34.507  54.387  59.842  1.00 33.41           C  
ATOM   2553  O   LEU A 234      34.000  54.813  60.888  1.00 32.54           O  
ATOM   2554  CB  LEU A 234      33.921  52.081  59.099  1.00 31.06           C  
ATOM   2555  CG  LEU A 234      33.209  51.104  58.162  1.00 29.91           C  
ATOM   2556  CD1 LEU A 234      33.619  49.709  58.525  1.00 29.17           C  
ATOM   2557  CD2 LEU A 234      31.691  51.255  58.231  1.00 30.84           C  
ATOM   2558  N   SER A 235      35.777  54.639  59.489  1.00 31.25           N  
ATOM   2559  CA  SER A 235      36.677  55.431  60.341  1.00 34.53           C  
ATOM   2560  C   SER A 235      36.241  56.861  60.511  1.00 31.40           C  
ATOM   2561  O   SER A 235      36.310  57.406  61.598  1.00 31.93           O  
ATOM   2562  CB  SER A 235      38.099  55.405  59.826  1.00 33.71           C  
ATOM   2563  OG  SER A 235      38.852  54.540  60.643  1.00 45.91           O  
ATOM   2564  N   GLU A 236      35.753  57.435  59.421  1.00 34.00           N  
ATOM   2565  CA  GLU A 236      35.259  58.811  59.379  1.00 35.45           C  
ATOM   2566  C   GLU A 236      34.038  58.972  60.313  1.00 35.87           C  
ATOM   2567  O   GLU A 236      33.809  60.051  60.885  1.00 36.18           O  
ATOM   2568  CB  GLU A 236      34.847  59.145  57.940  1.00 35.87           C  
ATOM   2569  CG  GLU A 236      34.420  60.573  57.708  1.00 38.55           C  
ATOM   2570  CD  GLU A 236      33.657  60.763  56.410  1.00 42.61           C  
ATOM   2571  OE1 GLU A 236      33.578  59.807  55.611  1.00 47.69           O  
ATOM   2572  OE2 GLU A 236      33.134  61.885  56.184  1.00 40.95           O  
ATOM   2573  N   PHE A 237      33.281  57.891  60.491  1.00 35.04           N  
ATOM   2574  CA  PHE A 237      32.101  57.922  61.331  1.00 32.20           C  
ATOM   2575  C   PHE A 237      32.155  57.193  62.654  1.00 31.19           C  
ATOM   2576  O   PHE A 237      31.127  56.815  63.211  1.00 28.11           O  
ATOM   2577  CB  PHE A 237      30.913  57.495  60.508  1.00 32.69           C  
ATOM   2578  CG  PHE A 237      30.574  58.471  59.443  1.00 34.19           C  
ATOM   2579  CD1 PHE A 237      29.873  59.621  59.746  1.00 32.76           C  
ATOM   2580  CD2 PHE A 237      31.015  58.276  58.139  1.00 34.84           C  
ATOM   2581  CE1 PHE A 237      29.615  60.562  58.773  1.00 32.67           C  
ATOM   2582  CE2 PHE A 237      30.765  59.219  57.154  1.00 32.85           C  
ATOM   2583  CZ  PHE A 237      30.066  60.362  57.469  1.00 34.36           C  
ATOM   2584  N   ARG A 238      33.363  57.046  63.178  1.00 34.33           N  
ATOM   2585  CA  ARG A 238      33.588  56.404  64.477  1.00 42.36           C  
ATOM   2586  C   ARG A 238      33.059  57.251  65.677  1.00 46.12           C  
ATOM   2587  O   ARG A 238      32.741  58.447  65.541  1.00 47.39           O  
ATOM   2588  CB  ARG A 238      35.077  56.093  64.666  1.00 41.39           C  
ATOM   2589  CG  ARG A 238      35.983  57.311  64.772  1.00 46.64           C  
ATOM   2590  CD  ARG A 238      37.270  56.976  65.493  1.00 49.74           C  
ATOM   2591  NE  ARG A 238      38.175  56.131  64.722  1.00 57.77           N  
ATOM   2592  CZ  ARG A 238      38.948  56.556  63.718  1.00 64.88           C  
ATOM   2593  NH1 ARG A 238      38.948  57.839  63.322  1.00 65.94           N  
ATOM   2594  NH2 ARG A 238      39.828  55.705  63.177  1.00 68.43           N  
ATOM   2595  N   LYS A 239      32.915  56.607  66.834  1.00 48.16           N  
ATOM   2596  CA  LYS A 239      32.454  57.288  68.038  1.00 51.45           C  
ATOM   2597  C   LYS A 239      33.586  57.476  69.065  1.00 55.78           C  
ATOM   2598  O   LYS A 239      33.542  58.407  69.872  1.00 57.19           O  
ATOM   2599  CB  LYS A 239      31.273  56.546  68.646  1.00 51.92           C  
ATOM   2600  CG  LYS A 239      30.144  56.296  67.658  1.00 50.62           C  
ATOM   2601  CD  LYS A 239      28.784  56.675  68.232  1.00 53.47           C  
ATOM   2602  CE  LYS A 239      27.973  55.479  68.720  1.00 53.02           C  
ATOM   2603  NZ  LYS A 239      26.611  55.946  69.149  1.00 49.70           N  
ATOM   2604  N   MET A 240      34.547  56.551  69.083  1.00 60.08           N  
ATOM   2605  CA  MET A 240      35.726  56.617  69.965  1.00 66.80           C  
ATOM   2606  C   MET A 240      36.751  55.648  69.382  1.00 70.25           C  
ATOM   2607  O   MET A 240      37.581  56.106  68.566  1.00 72.29           O  
ATOM   2608  CB  MET A 240      35.459  56.202  71.432  1.00 69.52           C  
ATOM   2609  CG  MET A 240      34.033  56.283  71.980  1.00 74.32           C  
ATOM   2610  SD  MET A 240      33.078  54.717  71.949  1.00 78.32           S  
ATOM   2611  CE  MET A 240      34.152  53.622  72.904  1.00 75.84           C  
ATOM   2612  OXT MET A 240      36.686  54.431  69.702  1.00 74.35           O  
TER    2613      MET A 240                                                      
HETATM 4031  O   HOH C 314       9.829  23.913  45.043  1.00 29.71           O  
HETATM 4032  O   HOH C 321       8.041  27.162  39.153  1.00 49.94           O  
HETATM 4033  O   HOH C 326      18.582  37.825  45.931  1.00 28.95           O  
HETATM 4034  O   HOH C 332      20.798  25.462  37.704  1.00 45.98           O  
HETATM 4035  O   HOH C 337      15.718  21.504  58.210  1.00 36.48           O  
HETATM 4036  O   HOH C 341      22.659  23.301  59.881  1.00 50.57           O  
HETATM 4037  O   HOH C 356      24.941  37.165  67.620  1.00 46.02           O  
HETATM 4038  O   HOH C 357      18.021  38.794  48.538  1.00 47.39           O  
HETATM 4039  O   HOH C 366      28.592  39.492  67.937  1.00 35.52           O  
HETATM 4040  O   HOH C 367      24.088  39.699  67.770  1.00 52.36           O  
HETATM 4041  O   HOH C 368       8.335  45.107  56.539  1.00 52.69           O  
HETATM 4042  O   HOH C 369      16.692  36.435  52.631  1.00 38.75           O  
HETATM 4043  O   HOH C 370      17.723  34.241  60.472  1.00 32.10           O  
HETATM 4044  O   HOH C 371      15.537  33.546  52.117  1.00 32.03           O  
HETATM 4045  O   HOH C 372       4.977  30.223  56.448  1.00 77.88           O  
HETATM 4046  O   HOH C 373      14.361  32.136  68.253  1.00 63.24           O  
HETATM 4047  O   HOH C 374      15.604  33.439  46.009  1.00 37.17           O  
HETATM 4048  O   HOH C 375      14.298  31.422  42.670  1.00 34.78           O  
HETATM 4049  O   HOH C 376      13.055  30.524  40.504  1.00 40.23           O  
HETATM 4050  O   HOH C 377      20.399  28.570  59.701  1.00 31.03           O  
HETATM 4051  O   HOH C 378       8.254  34.416  40.957  1.00 76.21           O  
HETATM 4052  O   HOH C 379      10.902  34.966  59.242  1.00 35.70           O  
HETATM 4053  O   HOH C 380      14.633  36.696  57.453  1.00 32.74           O  
HETATM 4054  O   HOH C 381      17.227  35.549  57.881  1.00 27.89           O  
HETATM 4055  O   HOH C 382      17.162  33.557  56.018  1.00 32.06           O  
HETATM 4056  O   HOH C 383       9.259  33.384  52.717  1.00 39.75           O  
HETATM 4057  O   HOH C 384      11.653  30.189  55.495  1.00 41.86           O  
HETATM 4058  O   HOH C 385      17.458  31.117  57.249  1.00 34.22           O  
HETATM 4059  O   HOH C 386      12.942  33.944  46.840  1.00 45.58           O  
HETATM 4060  O   HOH C 387      16.629  32.739  41.811  1.00 50.31           O  
HETATM 4061  O   HOH C 388      13.675  34.443  59.153  1.00 50.34           O  
HETATM 4062  O   HOH C 389       7.645  25.981  48.609  1.00 45.17           O  
HETATM 4063  O   HOH C 393      17.684  35.506  44.974  1.00 23.14           O  
HETATM 4064  O   HOH C 394       5.203  27.640  38.873  1.00 49.12           O  
HETATM 4065  O   HOH C 395      14.934  28.157  39.939  1.00 50.91           O  
HETATM 4066  O   HOH C 396      20.056  33.137  38.337  1.00 44.78           O  
HETATM 4067  O   HOH C 398      14.455  44.994  64.143  1.00 33.26           O  
HETATM 4068  O   HOH C 399      -1.142  31.927  47.002  1.00 80.78           O  
HETATM 4069  O   HOH C 400      -0.227  37.594  39.997  1.00 49.35           O  
HETATM 4070  O   HOH C 401      12.274  35.664  51.450  1.00 53.45           O  
HETATM 4071  O   HOH C 403      18.093  36.705  41.175  1.00 69.03           O  
HETATM 4072  O   HOH C 404      22.884  31.104  61.471  1.00 50.03           O  
HETATM 4073  O   HOH C 406      24.852  33.881  65.204  1.00 53.03           O  
HETATM 4074  O   HOH C 407       1.230  26.891  38.998  1.00 58.39           O  
HETATM 4075  O   HOH C 408       0.164  28.917  36.857  1.00 47.22           O  
HETATM 4076  O   HOH C 409       4.212  28.507  49.481  1.00 57.91           O  
HETATM 4077  O   HOH C 410       4.684  25.572  48.454  1.00 67.08           O  
HETATM 4078  O   HOH C 411      19.016  35.576  64.714  1.00 62.55           O  
HETATM 4079  O   HOH C 417       3.535  35.108  56.787  1.00 57.10           O  
HETATM 4080  O   HOH C 424      16.404  35.669  65.711  1.00 49.86           O  
HETATM 4081  O   HOH C 425      16.713  28.316  57.388  1.00 41.18           O  
HETATM 4082  O   HOH C 426       8.161  35.900  49.343  1.00 45.93           O  
HETATM 4083  O   HOH C 427      16.683  39.428  51.496  1.00 43.37           O  
HETATM 4084  O   HOH C 428       3.210  36.742  53.253  1.00 57.98           O  
HETATM 4085  O   HOH C 429       5.738  17.688  39.935  1.00 70.40           O  
HETATM 4086  O   HOH C 430       3.657  19.704  39.751  1.00 47.15           O  
HETATM 4087  O   HOH C 432      17.431  25.807  36.732  1.00 52.23           O  
HETATM 4088  O   HOH C 433      -0.102  24.898  41.316  1.00 49.72           O  
HETATM 4089  O   HOH C 435     -10.548  32.033  32.551  1.00 41.27           O  
HETATM 4090  O   HOH C 436      -2.403  33.672  29.377  1.00 48.13           O  
HETATM 4091  O   HOH C 437      -3.321  36.647  36.305  1.00 42.85           O  
HETATM 4092  O   HOH C 438      -2.355  31.540  41.722  1.00 32.81           O  
HETATM 4093  O   HOH C 439      19.940  41.886  44.657  1.00 37.15           O  
HETATM 4094  O   HOH C 441      20.424  37.404  66.946  1.00 46.72           O  
HETATM 4095  O   HOH C 442      25.699  36.483  64.995  1.00 64.05           O  
HETATM 4096  O   HOH C 443      27.194  33.337  66.715  1.00 46.32           O  
HETATM 4097  O   HOH C 444       9.399  33.076  57.757  1.00 51.27           O  
HETATM 4098  O   HOH C 445      16.301  35.377  62.631  1.00 54.65           O  
HETATM 4099  O   HOH C 458      15.496  34.826  73.602  1.00 67.69           O  
HETATM 4100  O   HOH C 462      12.684  21.736  36.210  1.00 48.91           O  
HETATM 4101  O   HOH C 472       7.532  40.804  39.512  1.00 56.42           O  
HETATM 4102  O   HOH C 476      26.143  44.767  69.916  1.00 42.83           O  
HETATM 4103  O   HOH C 477      11.910  45.811  70.156  1.00 44.37           O  
HETATM 4104  O   HOH C 478      22.393  33.683  62.162  1.00 36.23           O  
HETATM 4105  O   HOH C 479      22.752  38.212  40.987  1.00 49.72           O  
HETATM 4106  O   HOH C 482      12.593  30.593  66.717  1.00 49.28           O  
HETATM 4107  O   HOH C 485       9.087  29.571  40.251  1.00 58.97           O  
HETATM 4108  O   HOH C 486      19.474  38.932  42.170  1.00 42.03           O  
HETATM 4109  O   HOH C 490      -5.078  37.581  38.040  1.00 53.93           O  
HETATM 4110  O   HOH C 491      12.338  39.123  57.561  1.00 41.15           O  
HETATM 4111  O   HOH C 492      -7.945  36.439  39.893  1.00 68.65           O  
HETATM 4112  O   HOH C 494       1.417  36.496  42.969  1.00 50.20           O  
HETATM 4113  O   HOH C 501      16.833  23.137  60.593  1.00 52.80           O  
HETATM 4114  O   HOH C 502      10.756  28.074  37.903  1.00 64.62           O  
HETATM 4115  O   HOH C 522      13.718  39.712  54.519  1.00 63.55           O  
HETATM 4116  O   HOH C 529      12.812  32.548  56.321  1.00 44.02           O  
HETATM 4117  O   HOH C 530      14.252  34.020  49.781  1.00 34.51           O  
HETATM 4118  O   HOH C 531      24.883  29.662  64.204  1.00 55.00           O  
HETATM 4119  O   HOH C 532      14.148  34.332  65.080  1.00 47.82           O  
HETATM 4120  O   HOH C 533       8.118  41.149  56.137  1.00 48.95           O  
HETATM 4121  O   HOH C 534      10.988  37.014  48.214  1.00 50.84           O  
HETATM 4122  O   HOH C 535      13.545  26.923  37.831  1.00 56.62           O  
HETATM 4123  O   HOH C 536       6.892  31.715  39.974  1.00 45.23           O  
HETATM 4124  O   HOH C 538      16.465  22.651  35.930  1.00 61.24           O  
HETATM 4125  O   HOH C 539      14.296  34.026  54.628  1.00 49.04           O  
HETATM 4126  O   HOH C 541      28.822  29.074  62.293  1.00 40.75           O  
HETATM 4127  O   HOH C 544      -2.316  33.852  43.849  1.00 44.96           O  
HETATM 4128  O   HOH C 551     -12.251  33.429  30.180  1.00 36.35           O  
HETATM 4129  O   HOH C 558      10.220  32.846  42.656  1.00 38.52           O  
HETATM 4130  O   HOH C 721      12.217  34.661  43.865  1.00 67.70           O  
HETATM 4131  O   HOH C 773      17.413  32.138  39.082  1.00 60.11           O  
HETATM 4132  O   HOH D 537      21.835  41.716   8.999  1.00 64.20           O  
HETATM 4133  O   HOH D 550      25.581  55.348  22.708  1.00 70.73           O  
HETATM 4134  O   HOH D 571      28.174  61.998  24.266  1.00 26.58           O  
HETATM 4135  O   HOH D 574      26.352  42.697  22.022  1.00 31.23           O  
HETATM 4136  O   HOH D 580      22.906  40.144  29.612  1.00 50.09           O  
HETATM 4137  O   HOH D 581      16.574  38.819  19.203  1.00 63.59           O  
HETATM 4138  O   HOH D 584      13.623  31.116  27.036  1.00 49.89           O  
HETATM 4139  O   HOH D 586      11.805  34.968  21.282  1.00 26.75           O  
HETATM 4140  O   HOH D 592      23.887  32.673  30.706  1.00 28.38           O  
HETATM 4141  O   HOH D 601      26.773  29.028   8.482  1.00 31.88           O  
HETATM 4142  O   HOH D 614       0.987  36.599   9.974  1.00 43.83           O  
HETATM 4143  O   HOH D 616      12.703  25.891   0.465  1.00 39.36           O  
HETATM 4144  O   HOH D 617      10.860  35.376  18.935  1.00 41.54           O  
HETATM 4145  O   HOH D 626      10.237  22.830   0.447  1.00 41.66           O  
HETATM 4146  O   HOH D 627      10.449  27.114  -0.019  1.00 37.60           O  
HETATM 4147  O   HOH D 628       5.592  44.604   9.191  1.00 54.04           O  
HETATM 4148  O   HOH D 629      13.837  35.678  14.459  1.00 36.47           O  
HETATM 4149  O   HOH D 630      24.070  36.512   8.237  1.00 66.89           O  
HETATM 4150  O   HOH D 631      16.264  37.170  15.090  1.00 26.21           O  
HETATM 4151  O   HOH D 632      20.397  46.888  10.007  1.00 58.53           O  
HETATM 4152  O   HOH D 633      21.619  35.749  10.250  1.00 49.11           O  
HETATM 4153  O   HOH D 634      16.349  37.388  21.350  1.00 29.82           O  
HETATM 4154  O   HOH D 635      18.981  39.047  25.265  1.00 48.74           O  
HETATM 4155  O   HOH D 636      17.827  39.424  28.181  1.00 81.24           O  
HETATM 4156  O   HOH D 637      21.469  31.894   8.485  1.00 37.71           O  
HETATM 4157  O   HOH D 638      15.862  40.366  24.059  1.00 50.84           O  
HETATM 4158  O   HOH D 639      15.265  40.502   7.994  1.00 35.48           O  
HETATM 4159  O   HOH D 640      13.028  37.041   9.038  1.00 57.85           O  
HETATM 4160  O   HOH D 641      14.384  34.924   9.677  1.00 31.93           O  
HETATM 4161  O   HOH D 642      16.471  35.297  11.554  1.00 36.09           O  
HETATM 4162  O   HOH D 643      16.307  38.255  12.077  1.00 55.63           O  
HETATM 4163  O   HOH D 644      20.110  40.323  11.794  1.00 42.93           O  
HETATM 4164  O   HOH D 645      19.028  34.391   9.983  1.00 42.82           O  
HETATM 4165  O   HOH D 646      16.201  40.174  21.464  1.00 34.40           O  
HETATM 4166  O   HOH D 647      16.983  37.033  25.337  1.00 39.75           O  
HETATM 4167  O   HOH D 648      15.883  37.899   7.610  1.00 49.63           O  
HETATM 4168  O   HOH D 649      24.416  44.503  18.296  1.00 29.51           O  
HETATM 4169  O   HOH D 653      14.150  35.958  22.405  1.00 31.68           O  
HETATM 4170  O   HOH D 654      26.018  47.048  27.979  1.00 58.34           O  
HETATM 4171  O   HOH D 655      20.971  38.544  27.725  1.00 53.72           O  
HETATM 4172  O   HOH D 660      12.736  55.750  33.350  1.00 73.66           O  
HETATM 4173  O   HOH D 661      14.940  40.875  15.091  1.00 46.97           O  
HETATM 4174  O   HOH D 663      11.290  34.998  25.462  1.00 57.33           O  
HETATM 4175  O   HOH D 664      18.313  28.710   6.403  1.00 39.74           O  
HETATM 4176  O   HOH D 666      16.098  29.989   5.640  1.00 41.67           O  
HETATM 4177  O   HOH D 667      23.277  50.754  28.332  1.00 42.99           O  
HETATM 4178  O   HOH D 668      21.218  51.953  30.705  1.00 51.37           O  
HETATM 4179  O   HOH D 669      21.356  48.356  17.814  1.00 44.78           O  
HETATM 4180  O   HOH D 671      14.689  34.712   2.236  1.00 62.71           O  
HETATM 4181  O   HOH D 680      25.104  28.253   6.540  1.00 37.13           O  
HETATM 4182  O   HOH D 683       5.361  43.982   5.736  1.00 45.55           O  
HETATM 4183  O   HOH D 688      19.844  40.802   4.969  1.00 63.92           O  
HETATM 4184  O   HOH D 699      17.952  41.953  12.299  1.00 65.10           O  
HETATM 4185  O   HOH D 700       2.332  38.268  11.738  1.00 51.12           O  
HETATM 4186  O   HOH D 705       7.520  34.876  21.877  1.00 51.58           O  
HETATM 4187  O   HOH D 707       9.658  42.182   1.884  1.00 38.23           O  
HETATM 4188  O   HOH D 708      11.746  38.300  17.664  1.00 34.18           O  
HETATM 4189  O   HOH D 710      17.960  53.946  20.469  1.00 60.17           O  
HETATM 4190  O   HOH D 711      18.923  54.754  25.988  1.00 31.70           O  
HETATM 4191  O   HOH D 713      17.855  53.399  38.225  1.00 67.66           O  
HETATM 4192  O   HOH D 714      28.403  40.167  30.485  1.00 43.19           O  
HETATM 4193  O   HOH D 715      19.633  44.419  27.166  1.00 67.32           O  
HETATM 4194  O   HOH D 719      21.414  38.624   9.977  1.00 70.92           O  
HETATM 4195  O   HOH D 726      30.019  54.129  21.528  1.00 53.19           O  
HETATM 4196  O   HOH D 728      26.299  58.446  22.318  1.00 73.94           O  
HETATM 4197  O   HOH D 729      15.885  34.758  29.367  1.00 36.36           O  
HETATM 4198  O   HOH D 730      24.572  41.019   8.901  1.00 44.00           O  
HETATM 4199  O   HOH D 731      28.284  45.966  20.097  1.00 48.44           O  
HETATM 4200  O   HOH D 736      21.315  26.100   4.527  1.00 70.15           O  
HETATM 4201  O   HOH D 739      16.242  54.935  24.210  1.00 37.06           O  
HETATM 4202  O   HOH D 747      23.430  59.612  21.970  1.00 41.74           O  
HETATM 4203  O   HOH D 753      15.308  45.783   6.304  1.00 58.56           O  
HETATM 4204  O   HOH D 754      20.970  29.301   7.351  1.00 26.61           O  
HETATM 4205  O   HOH D 755      25.139  47.323  19.576  1.00 42.51           O  
HETATM 4206  O   HOH D 756      13.891  43.984  18.652  1.00 43.36           O  
HETATM 4207  O   HOH D 757      10.287  46.261   7.173  1.00 72.32           O  
HETATM 4208  O   HOH D 760       1.219  29.608  -0.339  1.00 63.54           O  
HETATM 4209  O   HOH D 761       7.684  37.596  16.399  1.00 60.42           O  
HETATM 4210  O   HOH D 762      15.363  39.138  16.888  1.00 49.33           O  
HETATM 4211  O   HOH D 764      15.846  50.974  20.217  1.00 47.91           O  
HETATM 4212  O   HOH D 766      24.870  51.992  26.657  1.00 36.37           O  
HETATM 4213  O   HOH D 769      13.794  43.164  15.970  1.00 83.85           O  
HETATM 4214  O   HOH D 771      24.806  43.867  29.947  1.00 57.39           O  
HETATM 4215  O   HOH D 772      17.427  42.849  24.610  1.00 40.06           O  
HETATM 4216  O   HOH D 783      17.592  36.147  28.113  1.00 42.59           O  
HETATM 4217  O   HOH D 795      15.240  32.549   5.241  1.00 57.70           O  
HETATM 4218  O   HOH D 796      19.400  38.736   2.686  1.00 53.54           O  
HETATM 4219  O   HOH D 797       4.072  41.247  12.469  1.00 51.71           O  
HETATM 4220  O   HOH D 798      30.412  48.064  28.141  1.00 57.53           O  
HETATM 4221  O   HOH D 799      26.844  49.425  26.552  1.00 58.85           O  
HETATM 4222  O   HOH D 800      16.249  44.963  26.402  1.00 48.15           O  
HETATM 4223  O   HOH D 801      10.158  53.403  29.846  1.00 57.81           O  
HETATM 4224  O   HOH D 802      13.703  55.395  30.286  1.00 55.03           O  
HETATM 4225  O   HOH D 805      27.902  54.277  28.342  1.00 66.30           O  
HETATM 4226  O   HOH D 806      12.426  52.987  27.955  1.00 58.41           O  
HETATM 4227  O   HOH D 807       6.410  39.864  -0.383  1.00 59.36           O  
HETATM 4228  O   HOH D 811      10.696  39.191   9.201  1.00 55.91           O  
HETATM 4229  O   HOH A 301      37.269  40.684  62.595  1.00 28.83           O  
HETATM 4230  O   HOH A 302      38.652  35.201  54.829  1.00 47.61           O  
HETATM 4231  O   HOH A 303      35.653  30.690  58.197  1.00 40.76           O  
HETATM 4232  O   HOH A 304      28.175  25.359  49.748  1.00 22.35           O  
HETATM 4233  O   HOH A 305      24.986  25.519  38.755  1.00 29.70           O  
HETATM 4234  O   HOH A 306      20.912  23.781  40.932  1.00 26.42           O  
HETATM 4235  O   HOH A 308      19.582  17.803  36.835  1.00 36.64           O  
HETATM 4236  O   HOH A 309      11.214  18.758  43.618  1.00 34.60           O  
HETATM 4237  O   HOH A 310      10.001  12.411  43.245  1.00 35.58           O  
HETATM 4238  O   HOH A 311      23.163  10.213  60.757  1.00 41.49           O  
HETATM 4239  O   HOH A 312      10.781  18.378  52.325  1.00 32.88           O  
HETATM 4240  O   HOH A 313       8.429  23.655  47.286  1.00 32.74           O  
HETATM 4241  O   HOH A 315      24.917  19.366  58.534  1.00 50.86           O  
HETATM 4242  O   HOH A 316      29.951  17.834  61.514  1.00 36.81           O  
HETATM 4243  O   HOH A 317      24.615  22.885  58.058  1.00 28.28           O  
HETATM 4244  O   HOH A 318      33.264  20.830  58.538  1.00 35.37           O  
HETATM 4245  O   HOH A 319      31.071  13.334  55.366  1.00 28.65           O  
HETATM 4246  O   HOH A 320      32.301  14.363  62.309  1.00 48.24           O  
HETATM 4247  O   HOH A 322      36.131  32.854  46.015  1.00 25.65           O  
HETATM 4248  O   HOH A 323      33.097  13.419  38.870  1.00 61.00           O  
HETATM 4249  O   HOH A 324      23.095  34.987  40.787  1.00 37.95           O  
HETATM 4250  O   HOH A 325      32.499  28.960  41.328  1.00 29.95           O  
HETATM 4251  O   HOH A 327      37.634  38.856  60.611  1.00 45.50           O  
HETATM 4252  O   HOH A 328      37.790  32.877  56.122  1.00 22.47           O  
HETATM 4253  O   HOH A 329      37.378  30.069  54.116  1.00 47.65           O  
HETATM 4254  O   HOH A 330      32.942  24.559  55.639  1.00 32.21           O  
HETATM 4255  O   HOH A 331      22.674  23.874  38.674  1.00 25.23           O  
HETATM 4256  O   HOH A 333      23.962  29.432  36.705  1.00 57.30           O  
HETATM 4257  O   HOH A 334      12.150  19.254  40.704  1.00 36.82           O  
HETATM 4258  O   HOH A 335      17.503  10.253  57.442  1.00 44.36           O  
HETATM 4259  O   HOH A 336      22.983  11.833  54.465  1.00 28.38           O  
HETATM 4260  O   HOH A 338       5.897  18.648  46.882  1.00 58.92           O  
HETATM 4261  O   HOH A 339       8.693  17.367  43.403  1.00 32.61           O  
HETATM 4262  O   HOH A 340      27.519  17.931  62.346  1.00 41.49           O  
HETATM 4263  O   HOH A 342      26.812  23.958  57.739  1.00 40.60           O  
HETATM 4264  O   HOH A 343      36.389  16.198  54.807  1.00 44.63           O  
HETATM 4265  O   HOH A 344      30.363  11.659  53.317  1.00 29.15           O  
HETATM 4266  O   HOH A 345       8.466  14.600  43.364  1.00 69.01           O  
HETATM 4267  O   HOH A 346      31.157  12.621  42.607  1.00 65.77           O  
HETATM 4268  O   HOH A 347      30.220  12.197  38.689  1.00 33.52           O  
HETATM 4269  O   HOH A 349      34.131  31.698  44.394  1.00 27.46           O  
HETATM 4270  O   HOH A 350      32.364  45.316  68.197  1.00 40.30           O  
HETATM 4271  O   HOH A 351      23.873  51.484  45.216  1.00 28.88           O  
HETATM 4272  O   HOH A 352      25.010  46.873  45.550  1.00 33.31           O  
HETATM 4273  O   HOH A 353      19.324  55.245  49.050  1.00 47.67           O  
HETATM 4274  O   HOH A 354      16.292  49.364  56.821  1.00 34.81           O  
HETATM 4275  O   HOH A 355      38.634  48.122  46.986  1.00 41.78           O  
HETATM 4276  O   HOH A 358      32.008  39.124  62.963  1.00 46.40           O  
HETATM 4277  O   HOH A 359      23.126  48.324  65.249  1.00 22.89           O  
HETATM 4278  O   HOH A 360      23.892  48.674  43.817  1.00 52.51           O  
HETATM 4279  O   HOH A 361      20.775  50.537  50.631  1.00 32.40           O  
HETATM 4280  O   HOH A 362      17.768  49.689  58.878  1.00 24.01           O  
HETATM 4281  O   HOH A 363      25.228  47.473  67.839  1.00 31.39           O  
HETATM 4282  O   HOH A 364      27.029  47.908  40.663  1.00 37.56           O  
HETATM 4283  O   HOH A 365      33.908  54.870  49.626  1.00 72.12           O  
HETATM 4284  O   HOH A 390      23.003  43.200  44.957  1.00 47.77           O  
HETATM 4285  O   HOH A 391      11.325  19.849  37.885  1.00 41.67           O  
HETATM 4286  O   HOH A 392      19.026  19.163  34.426  1.00 55.27           O  
HETATM 4287  O   HOH A 397      40.491  42.927  53.088  1.00 53.25           O  
HETATM 4288  O   HOH A 402       5.948  22.677  47.323  1.00 46.33           O  
HETATM 4289  O   HOH A 405      14.951  47.606  65.694  1.00 49.15           O  
HETATM 4290  O   HOH A 413      41.270  35.468  58.200  1.00 68.48           O  
HETATM 4291  O   HOH A 414      24.999  40.902  44.488  1.00 38.36           O  
HETATM 4292  O   HOH A 415      35.048  38.538  63.641  1.00 43.26           O  
HETATM 4293  O   HOH A 416      37.086  18.954  45.629  1.00 27.24           O  
HETATM 4294  O   HOH A 418      13.359  17.623  34.888  1.00 44.81           O  
HETATM 4295  O   HOH A 419       9.970   4.790  47.991  1.00 40.78           O  
HETATM 4296  O   HOH A 420      29.357  41.398  71.555  1.00 72.87           O  
HETATM 4297  O   HOH A 421      25.074  60.907  48.972  1.00 47.16           O  
HETATM 4298  O   HOH A 422      24.934  55.426  65.872  1.00 46.56           O  
HETATM 4299  O   HOH A 423       9.241  42.719  64.655  1.00 53.32           O  
HETATM 4300  O   HOH A 431      12.559  21.140  59.527  1.00 80.97           O  
HETATM 4301  O   HOH A 434      29.322  52.784  46.183  1.00 34.48           O  
HETATM 4302  O   HOH A 440      31.131  34.116  64.902  1.00 55.77           O  
HETATM 4303  O   HOH A 446      40.127  29.491  53.610  1.00 50.71           O  
HETATM 4304  O   HOH A 447      18.889   7.856  37.154  1.00 47.54           O  
HETATM 4305  O   HOH A 448      29.599  10.829  50.444  1.00 45.06           O  
HETATM 4306  O   HOH A 449      25.428  17.720  60.562  1.00 59.52           O  
HETATM 4307  O   HOH A 450       8.330   6.245  45.353  1.00 49.42           O  
HETATM 4308  O   HOH A 451      27.353   7.351  62.710  1.00 33.11           O  
HETATM 4309  O   HOH A 452      30.542  10.101  60.646  1.00 37.39           O  
HETATM 4310  O   HOH A 453      31.192   4.151  40.733  1.00 37.63           O  
HETATM 4311  O   HOH A 454      30.596  21.326  34.355  1.00 34.21           O  
HETATM 4312  O   HOH A 455      23.895  62.512  62.079  1.00 43.19           O  
HETATM 4313  O   HOH A 456      19.760  57.399  53.720  1.00 43.79           O  
HETATM 4314  O   HOH A 457      20.308  52.346  48.576  1.00 29.26           O  
HETATM 4315  O   HOH A 459      21.396  51.753  46.141  1.00 41.96           O  
HETATM 4316  O   HOH A 461      23.506  16.094  60.982  1.00 47.61           O  
HETATM 4317  O   HOH A 463      37.320  27.935  44.391  1.00 31.52           O  
HETATM 4318  O   HOH A 464      24.114   4.937  40.227  1.00 30.58           O  
HETATM 4319  O   HOH A 465      34.537  16.780  38.468  1.00 64.30           O  
HETATM 4320  O   HOH A 466      22.909   6.277  51.468  1.00 35.33           O  
HETATM 4321  O   HOH A 467      31.323  20.732  38.386  1.00 39.07           O  
HETATM 4322  O   HOH A 469      18.181  55.726  55.108  1.00 73.58           O  
HETATM 4323  O   HOH A 470      11.077  51.921  59.219  1.00 46.51           O  
HETATM 4324  O   HOH A 471      20.288  51.125  65.038  1.00 27.03           O  
HETATM 4325  O   HOH A 473      38.250  35.416  44.595  1.00 26.78           O  
HETATM 4326  O   HOH A 474      22.852  41.410  41.945  1.00 57.43           O  
HETATM 4327  O   HOH A 475      31.375  53.548  48.352  1.00 49.46           O  
HETATM 4328  O   HOH A 480      19.334  50.175  45.049  1.00 58.56           O  
HETATM 4329  O   HOH A 481      18.511  48.947  51.113  1.00 51.71           O  
HETATM 4330  O   HOH A 483      39.830  20.032  48.696  1.00 54.04           O  
HETATM 4331  O   HOH A 487      15.569  54.313  54.514  1.00 50.60           O  
HETATM 4332  O   HOH A 488      30.988   9.204  63.623  1.00 70.01           O  
HETATM 4333  O   HOH A 489      24.344   4.150  53.566  1.00 56.52           O  
HETATM 4334  O   HOH A 495      41.580  31.576  54.726  1.00 46.84           O  
HETATM 4335  O   HOH A 496      20.868   3.823  37.229  1.00 44.33           O  
HETATM 4336  O   HOH A 497      21.171  12.016  32.338  1.00 76.84           O  
HETATM 4337  O   HOH A 498      35.072  12.167  55.025  1.00 68.76           O  
HETATM 4338  O   HOH A 499      24.453  13.567  62.487  1.00 57.20           O  
HETATM 4339  O   HOH A 500      37.586  14.407  52.152  1.00 54.58           O  
HETATM 4340  O   HOH A 503      32.480  62.549  60.558  1.00 32.76           O  
HETATM 4341  O   HOH A 504      23.902  57.556  64.668  1.00 45.56           O  
HETATM 4342  O   HOH A 505      11.071  45.148  63.257  1.00 50.34           O  
HETATM 4343  O   HOH A 506      31.204  43.185  41.549  1.00 37.66           O  
HETATM 4344  O   HOH A 507      16.678   8.050  55.939  1.00 47.09           O  
HETATM 4345  O   HOH A 508      30.998  31.766  62.943  1.00 51.73           O  
HETATM 4346  O   HOH A 509      28.877  42.774  69.258  1.00 39.75           O  
HETATM 4347  O   HOH A 510      16.188  16.556  34.526  1.00 47.37           O  
HETATM 4348  O   HOH A 511      23.599  32.965  38.607  1.00 66.37           O  
HETATM 4349  O   HOH A 512      40.635  27.449  51.975  1.00 40.43           O  
HETATM 4350  O   HOH A 513      35.759  25.417  44.619  1.00 53.17           O  
HETATM 4351  O   HOH A 514      31.105  23.833  57.708  1.00 43.75           O  
HETATM 4352  O   HOH A 515      25.454   3.457  38.291  1.00 45.98           O  
HETATM 4353  O   HOH A 516      22.932   2.525  39.735  1.00 40.44           O  
HETATM 4354  O   HOH A 518      26.688   9.467  35.638  1.00 42.08           O  
HETATM 4355  O   HOH A 519      25.940  37.272  43.412  1.00 49.07           O  
HETATM 4356  O   HOH A 521      22.450  45.933  45.469  1.00 51.97           O  
HETATM 4357  O   HOH A 523      29.407  40.956  43.168  1.00 51.60           O  
HETATM 4358  O   HOH A 524      32.200  61.537  51.429  1.00 52.82           O  
HETATM 4359  O   HOH A 525      31.331  62.598  54.071  1.00 57.47           O  
HETATM 4360  O   HOH A 526      35.901  58.332  53.690  1.00 50.50           O  
HETATM 4361  O   HOH A 527      38.880  58.237  56.984  1.00 51.99           O  
HETATM 4362  O   HOH A 528      23.981  54.943  68.680  1.00 58.56           O  
HETATM 4363  O   HOH A 540       9.464   5.982  52.017  1.00 63.97           O  
HETATM 4364  O   HOH A 542      35.717  40.340  67.374  1.00 79.17           O  
HETATM 4365  O   HOH A 543      38.819  42.540  64.402  1.00 81.83           O  
HETATM 4366  O   HOH A 545      41.210  50.362  53.473  1.00 48.11           O  
HETATM 4367  O   HOH A 546      30.451  46.271  39.857  1.00 54.50           O  
HETATM 4368  O   HOH A 547      26.823  63.330  57.779  1.00 60.00           O  
HETATM 4369  O   HOH A 548      41.318  40.133  60.711  1.00 76.41           O  
HETATM 4370  O   HOH A 552      18.634   5.353  35.986  1.00 60.09           O  
HETATM 4371  O   HOH A 554      38.540  27.620  49.915  1.00 46.78           O  
HETATM 4372  O   HOH A 555      37.913  21.324  46.972  1.00 47.33           O  
HETATM 4373  O   HOH A 556      29.283   3.016  50.246  1.00 31.49           O  
HETATM 4374  O   HOH A 557      12.565  53.977  61.607  1.00 40.64           O  
HETATM 4375  O   HOH A 559      10.688  19.595  55.168  1.00 47.04           O  
HETATM 4376  O   HOH A 560       9.155  10.831  45.407  1.00 80.08           O  
HETATM 4377  O   HOH A 659      32.712  12.547  60.194  1.00 47.57           O  
HETATM 4378  O   HOH A 672      26.915  19.681  64.386  1.00 61.86           O  
HETATM 4379  O   HOH A 674      29.560  13.628  64.271  1.00 60.94           O  
HETATM 4380  O   HOH A 678      27.346  53.107  70.887  1.00 47.65           O  
HETATM 4381  O   HOH A 681      28.762  34.984  37.988  1.00 50.92           O  
HETATM 4382  O   HOH A 690      24.783  49.276  41.198  1.00 42.23           O  
HETATM 4383  O   HOH A 692      27.114  21.338  31.089  1.00 31.66           O  
HETATM 4384  O   HOH A 694      28.194  30.608  35.280  1.00 59.82           O  
HETATM 4385  O   HOH A 701      28.611  50.261  70.677  1.00 53.59           O  
HETATM 4386  O   HOH A 720      31.308  32.153  41.595  1.00 29.28           O  
HETATM 4387  O   HOH A 740      33.212  12.391  57.239  1.00 36.81           O  
HETATM 4388  O   HOH A 741      32.588  18.773  36.824  1.00 58.84           O  
HETATM 4389  O   HOH A 765      31.508  51.854  44.713  1.00 44.51           O  
HETATM 4390  O   HOH A 777      18.042  58.074  56.417  1.00 74.00           O  
HETATM 4391  O   HOH B 307      25.365  27.118  36.784  1.00 44.07           O  
HETATM 4392  O   HOH B 348      25.148  15.460  32.531  1.00 57.22           O  
HETATM 4393  O   HOH B 412      48.713  32.036  22.699  1.00 69.60           O  
HETATM 4394  O   HOH B 460      33.912  46.439  12.521  1.00 54.16           O  
HETATM 4395  O   HOH B 468      32.180  22.482  36.408  1.00 50.43           O  
HETATM 4396  O   HOH B 484      -2.430  20.536  32.438  1.00 52.63           O  
HETATM 4397  O   HOH B 493      28.752  26.349  36.024  1.00 33.47           O  
HETATM 4398  O   HOH B 517      29.739  19.953  31.952  1.00 52.83           O  
HETATM 4399  O   HOH B 520      30.017  28.548  35.141  1.00 55.91           O  
HETATM 4400  O   HOH B 549      24.982  20.573  11.780  1.00 32.16           O  
HETATM 4401  O   HOH B 553      36.005  21.390  30.593  1.00 66.79           O  
HETATM 4402  O   HOH B 561       8.018  14.393   6.768  1.00 48.78           O  
HETATM 4403  O   HOH B 562      13.754  13.684  14.879  1.00 36.14           O  
HETATM 4404  O   HOH B 563      18.072  16.078  11.283  1.00 46.16           O  
HETATM 4405  O   HOH B 564      23.540  24.122  18.723  1.00 21.80           O  
HETATM 4406  O   HOH B 565      23.556  28.408  29.610  1.00 22.52           O  
HETATM 4407  O   HOH B 566      25.531  31.760  26.891  1.00 26.82           O  
HETATM 4408  O   HOH B 567      22.063  29.077  31.697  1.00 46.56           O  
HETATM 4409  O   HOH B 568      31.942  32.863  31.056  1.00 32.61           O  
HETATM 4410  O   HOH B 569      31.612  40.928  24.066  1.00 27.91           O  
HETATM 4411  O   HOH B 570      37.676  41.768  23.899  1.00 30.58           O  
HETATM 4412  O   HOH B 572      31.705  40.807  15.198  1.00 28.85           O  
HETATM 4413  O   HOH B 573      26.751  43.656  19.644  1.00 34.37           O  
HETATM 4414  O   HOH B 575      30.249  25.955   9.908  1.00 42.01           O  
HETATM 4415  O   HOH B 576      30.895  20.882   6.986  1.00 31.77           O  
HETATM 4416  O   HOH B 577      26.995  27.053  10.291  1.00 25.84           O  
HETATM 4417  O   HOH B 578      27.915  18.430  10.653  1.00 28.02           O  
HETATM 4418  O   HOH B 579      35.148  20.279  13.365  1.00 33.15           O  
HETATM 4419  O   HOH B 582      16.302  17.009  23.103  1.00 43.40           O  
HETATM 4420  O   HOH B 583      35.881  21.788  28.062  1.00 42.32           O  
HETATM 4421  O   HOH B 585      19.647  21.484  27.657  1.00 45.15           O  
HETATM 4422  O   HOH B 587      10.238  14.227   8.920  1.00 40.74           O  
HETATM 4423  O   HOH B 588      15.652  14.573  13.232  1.00 31.02           O  
HETATM 4424  O   HOH B 589      18.248  15.032  14.814  1.00 40.89           O  
HETATM 4425  O   HOH B 590      24.271  18.722  13.493  1.00 37.28           O  
HETATM 4426  O   HOH B 591      25.435  30.643  29.565  1.00 28.32           O  
HETATM 4427  O   HOH B 593      19.663  30.497  30.624  1.00 46.58           O  
HETATM 4428  O   HOH B 594      30.522  40.292  26.620  1.00 32.98           O  
HETATM 4429  O   HOH B 595      39.721  34.112  10.119  1.00 53.69           O  
HETATM 4430  O   HOH B 596      37.598  28.064  13.830  1.00 31.25           O  
HETATM 4431  O   HOH B 597      28.692  35.528   9.434  1.00 39.93           O  
HETATM 4432  O   HOH B 598      32.254  46.085  20.904  1.00 46.31           O  
HETATM 4433  O   HOH B 599      33.012  43.347  23.939  1.00 32.79           O  
HETATM 4434  O   HOH B 600      31.067  23.429   6.218  1.00 33.47           O  
HETATM 4435  O   HOH B 602      25.372  25.049  10.741  1.00 26.47           O  
HETATM 4436  O   HOH B 603      31.934  15.337  14.552  1.00 39.91           O  
HETATM 4437  O   HOH B 604      37.463  20.904  15.300  1.00 22.29           O  
HETATM 4438  O   HOH B 605      38.586  29.334  34.546  1.00 63.73           O  
HETATM 4439  O   HOH B 606      35.837  20.549  25.459  1.00 33.17           O  
HETATM 4440  O   HOH B 607      34.430  18.692  29.465  1.00 53.95           O  
HETATM 4441  O   HOH B 608       5.921  27.034  28.845  1.00 62.45           O  
HETATM 4442  O   HOH B 609      16.809  19.128  25.355  1.00 38.72           O  
HETATM 4443  O   HOH B 610       3.884  19.006   0.428  1.00 45.31           O  
HETATM 4444  O   HOH B 611      -1.588  30.370  22.284  1.00 34.02           O  
HETATM 4445  O   HOH B 612       2.447  29.038  21.680  1.00 27.00           O  
HETATM 4446  O   HOH B 613      -4.915  34.941  17.636  1.00 46.02           O  
HETATM 4447  O   HOH B 615       0.374  15.493  21.985  1.00 59.25           O  
HETATM 4448  O   HOH B 618      10.110  19.971   5.157  1.00 54.66           O  
HETATM 4449  O   HOH B 619       1.259  28.593   2.302  1.00 31.53           O  
HETATM 4450  O   HOH B 620       3.499  31.913  21.689  1.00 51.52           O  
HETATM 4451  O   HOH B 621      -0.885  33.151  16.210  1.00 32.21           O  
HETATM 4452  O   HOH B 622       0.154  34.745   7.826  1.00 28.77           O  
HETATM 4453  O   HOH B 623       2.254  26.847  -0.271  1.00 48.21           O  
HETATM 4454  O   HOH B 624       1.404  27.790  27.187  1.00 49.70           O  
HETATM 4455  O   HOH B 625      -4.141  22.705  33.189  1.00 53.83           O  
HETATM 4456  O   HOH B 650       5.708  30.491  22.033  1.00 39.20           O  
HETATM 4457  O   HOH B 651      30.592  41.705  29.850  1.00 37.26           O  
HETATM 4458  O   HOH B 652      31.344  33.255  33.783  1.00 50.67           O  
HETATM 4459  O   HOH B 656      17.467  32.406  30.355  1.00 62.23           O  
HETATM 4460  O   HOH B 657       5.689  12.777  16.004  1.00 50.01           O  
HETATM 4461  O   HOH B 658       5.571  37.264   2.283  1.00 31.30           O  
HETATM 4462  O   HOH B 662      28.118  46.943  17.726  1.00 48.44           O  
HETATM 4463  O   HOH B 665       3.116  36.662   0.857  1.00 53.59           O  
HETATM 4464  O   HOH B 670      31.073  40.713  12.580  1.00 43.11           O  
HETATM 4465  O   HOH B 673      35.945  28.068  33.426  1.00 35.85           O  
HETATM 4466  O   HOH B 675      43.055  27.590  16.400  1.00 33.87           O  
HETATM 4467  O   HOH B 676      38.035  20.218   7.597  1.00 33.40           O  
HETATM 4468  O   HOH B 677      34.431  41.576  29.530  1.00 36.38           O  
HETATM 4469  O   HOH B 679      27.586  35.718   6.900  1.00 56.28           O  
HETATM 4470  O   HOH B 682      24.327  20.457   9.024  1.00 41.56           O  
HETATM 4471  O   HOH B 684      23.135  25.813  34.787  1.00 53.70           O  
HETATM 4472  O   HOH B 685      27.483  15.967  30.602  1.00 36.89           O  
HETATM 4473  O   HOH B 686      29.415  12.773  20.750  1.00 39.05           O  
HETATM 4474  O   HOH B 687      32.160  12.564  22.531  1.00 37.44           O  
HETATM 4475  O   HOH B 689      47.697  24.527  23.535  1.00 47.04           O  
HETATM 4476  O   HOH B 691      41.797  32.638  31.166  1.00 37.53           O  
HETATM 4477  O   HOH B 693      24.550  12.874  33.105  1.00 38.74           O  
HETATM 4478  O   HOH B 695      22.796  14.761  25.290  1.00 58.23           O  
HETATM 4479  O   HOH B 696       5.962  12.288  -2.158  1.00 88.89           O  
HETATM 4480  O   HOH B 697     -10.301  29.641  19.136  1.00 28.27           O  
HETATM 4481  O   HOH B 698      -2.475  33.733  18.476  1.00 39.83           O  
HETATM 4482  O   HOH B 702      -4.210  23.426  19.811  1.00 30.74           O  
HETATM 4483  O   HOH B 703       5.626  23.410  26.699  1.00 44.78           O  
HETATM 4484  O   HOH B 704       7.249  28.354  22.010  1.00 36.77           O  
HETATM 4485  O   HOH B 706      16.363  22.850  27.543  1.00 40.41           O  
HETATM 4486  O   HOH B 709      35.984  18.632  11.368  1.00 41.10           O  
HETATM 4487  O   HOH B 712       7.309  31.512  26.444  1.00 56.78           O  
HETATM 4488  O   HOH B 716       8.823  10.259   9.298  1.00 41.90           O  
HETATM 4489  O   HOH B 717       5.364  40.895   3.062  1.00 45.25           O  
HETATM 4490  O   HOH B 718      18.633  16.407   8.623  1.00 51.69           O  
HETATM 4491  O   HOH B 722      47.779  27.932  20.782  1.00 47.52           O  
HETATM 4492  O   HOH B 723      46.209  29.007  18.945  1.00 47.16           O  
HETATM 4493  O   HOH B 724      33.064  32.407  10.676  1.00 37.12           O  
HETATM 4494  O   HOH B 725      39.045  19.455   4.637  1.00 52.64           O  
HETATM 4495  O   HOH B 727      41.798  33.726  12.119  1.00 45.73           O  
HETATM 4496  O   HOH B 732      33.558  43.530  21.154  1.00 47.94           O  
HETATM 4497  O   HOH B 733      24.913  45.538  15.817  1.00 49.83           O  
HETATM 4498  O   HOH B 734      -2.771  36.393  17.791  1.00 63.49           O  
HETATM 4499  O   HOH B 735      36.262  16.283  13.092  1.00 56.99           O  
HETATM 4500  O   HOH B 737      32.536  27.524   7.223  1.00 46.76           O  
HETATM 4501  O   HOH B 738      45.567  21.278  17.807  1.00 34.85           O  
HETATM 4502  O   HOH B 742      -6.487  34.634  10.958  1.00 69.61           O  
HETATM 4503  O   HOH B 743      32.531  10.625  24.706  1.00 67.12           O  
HETATM 4504  O   HOH B 744      43.446  27.967  18.997  1.00 52.88           O  
HETATM 4505  O   HOH B 745     -11.580  19.895   0.695  1.00 46.54           O  
HETATM 4506  O   HOH B 746      -7.100  28.505   2.148  1.00 45.85           O  
HETATM 4507  O   HOH B 748      33.347  18.851   6.615  1.00 53.29           O  
HETATM 4508  O   HOH B 749       5.693  12.064  21.206  1.00 77.28           O  
HETATM 4509  O   HOH B 750      -9.685  21.324  13.993  1.00 54.09           O  
HETATM 4510  O   HOH B 751      -8.759  14.039   5.736  1.00 70.93           O  
HETATM 4511  O   HOH B 752      12.079  12.015  22.661  1.00 46.04           O  
HETATM 4512  O   HOH B 758      18.362  15.758  20.092  1.00 27.45           O  
HETATM 4513  O   HOH B 759      -0.883  27.417  29.602  1.00 53.98           O  
HETATM 4514  O   HOH B 763      27.356  37.200  32.658  1.00 66.97           O  
HETATM 4515  O   HOH B 767      39.080  21.201  32.028  1.00 56.48           O  
HETATM 4516  O   HOH B 768      22.634  36.369  33.068  1.00 46.38           O  
HETATM 4517  O   HOH B 770      33.670  25.638  36.557  1.00 64.50           O  
HETATM 4518  O   HOH B 774      44.595  38.053  25.719  1.00 46.64           O  
HETATM 4519  O   HOH B 775      34.737  18.341  26.649  1.00 42.53           O  
HETATM 4520  O   HOH B 776      42.043  39.806  15.361  1.00 49.44           O  
HETATM 4521  O   HOH B 778      39.881  40.901  14.134  1.00 53.60           O  
HETATM 4522  O   HOH B 779      32.659  46.334  24.871  1.00 52.71           O  
HETATM 4523  O   HOH B 780      32.589  30.851   6.447  1.00 48.51           O  
HETATM 4524  O   HOH B 781      45.049  26.240  14.517  1.00 36.33           O  
HETATM 4525  O   HOH B 782      47.689  25.204  12.965  1.00 46.65           O  
HETATM 4526  O   HOH B 784      40.608  35.497  31.441  1.00 51.00           O  
HETATM 4527  O   HOH B 785      39.509  42.409  22.003  1.00 72.07           O  
HETATM 4528  O   HOH B 786      38.966  35.827  33.768  1.00 48.10           O  
HETATM 4529  O   HOH B 787     -14.128  17.966   1.178  1.00 45.01           O  
HETATM 4530  O   HOH B 788      23.770  35.879  30.744  1.00 33.48           O  
HETATM 4531  O   HOH B 789      36.071  17.604  21.993  1.00 49.39           O  
HETATM 4532  O   HOH B 790      37.802  21.688  17.958  1.00 33.29           O  
HETATM 4533  O   HOH B 791      29.955  15.687  12.337  1.00 64.97           O  
HETATM 4534  O   HOH B 792      22.360  22.911   9.934  1.00 56.42           O  
HETATM 4535  O   HOH B 793      27.735  13.762  26.194  1.00 50.55           O  
HETATM 4536  O   HOH B 794      42.940  22.179  26.147  1.00 57.26           O  
HETATM 4537  O   HOH B 803      40.504  17.069   3.886  1.00 64.14           O  
HETATM 4538  O   HOH B 804       1.169  35.329  15.760  1.00 48.82           O  
HETATM 4539  O   HOH B 808      35.663  18.562   8.326  1.00 55.06           O  
HETATM 4540  O   HOH B 809      -1.182  31.906   1.083  1.00 62.85           O  
HETATM 4541  O   HOH B 810      38.381  19.073  19.663  1.00 33.79           O  
HETATM 4542  O   HOH B 812      35.779  14.557  18.727  1.00 71.03           O  
HETATM 4543  O   HOH B 813      28.962  15.404  24.013  1.00 45.68           O  
MASTER      352    4    0    8   20    0    0    9 4539    4    0   34          
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.