CNRS Nantes University UFIP UFIP
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***  soso  ***

elNémo ID: 19112910460344001

Job options:

ID        	=	 19112910460344001
JOBID     	=	 soso
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 soso

HEADER    HYDROLASE                               26-JUN-00   1GFY              
TITLE     RESIDUE 259 IS A KEY DETERMINANT OF SUBSTRATE SPECIFICITY OF PROTEIN- 
TITLE    2 TYROSINE PHOSPHATASE 1B AND ALPHA                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (PROTEIN-TYROSINE PHOSPHATASE 1B);                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: CATALYTIC DOMAIN;                                          
COMPND   5 SYNONYM: PTP1B;                                                      
COMPND   6 EC: 3.1.3.48;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    HYDROLASE                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.F.IVERSEN                                                           
REVDAT   4   07-MAR-18 1GFY    1       REMARK                                   
REVDAT   3   24-FEB-09 1GFY    1       VERSN                                    
REVDAT   2   01-APR-03 1GFY    1       JRNL                                     
REVDAT   1   04-JUL-00 1GFY    0                                                
JRNL        AUTH   G.H.PETERS,L.F.IVERSEN,S.BRANNER,H.S.ANDERSEN,S.B.MORTENSEN, 
JRNL        AUTH 2 O.H.OLSEN,K.B.MOLLER,N.P.MOLLER                              
JRNL        TITL   RESIDUE 259 IS A KEY DETERMINANT OF SUBSTRATE SPECIFICITY OF 
JRNL        TITL 2 PROTEIN-TYROSINE PHOSPHATASES 1B AND ALPHA.                  
JRNL        REF    J.BIOL.CHEM.                  V. 275 18201 2000              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   10748206                                                     
JRNL        DOI    10.1074/JBC.M910273199                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.13 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) : 2.13                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 26558                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.191                           
REMARK   3   FREE R VALUE                     : 0.250                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
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            : 2417                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 18                                      
REMARK   3   SOLVENT ATOMS            : 209                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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) : NULL                            
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) : 0.019                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.970                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
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 1GFY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JUN-00.                  
REMARK 100 THE DEPOSITION ID IS D_1000001478.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : MAX II                             
REMARK 200  BEAMLINE                       : I711                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26558                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.130                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 5.300                              
REMARK 200  R MERGE                    (I) : 0.07300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 14.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.13                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.17                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.38700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 3.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.33                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.35                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.5                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       34.57600            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       69.15200            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       69.15200            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       34.57600            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     GLU A     2                                                      
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    GLN A  21   CG    GLN A  21   CD      0.167                       
REMARK 500    HIS A  25   CG    HIS A  25   CD2     0.085                       
REMARK 500    GLU A 186   CG    GLU A 186   CD      0.109                       
REMARK 500    SER A 201   CB    SER A 201   OG      0.078                       
REMARK 500    SER A 205   CB    SER A 205   OG      0.187                       
REMARK 500    SER A 242   CB    SER A 242   OG      0.093                       
REMARK 500    SER A 285   CB    SER A 285   OG      0.112                       
REMARK 500    HIS A 296   CG    HIS A 296   CD2     0.057                       
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    ALA A  18   CB  -  CA  -  C   ANGL. DEV. =  -9.4 DEGREES          
REMARK 500    HIS A  25   CA  -  CB  -  CG  ANGL. DEV. = -11.4 DEGREES          
REMARK 500    ARG A  33   NE  -  CZ  -  NH1 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ARG A  45   NE  -  CZ  -  NH1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ARG A  45   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    VAL A  49   CA  -  CB  -  CG1 ANGL. DEV. =  11.3 DEGREES          
REMARK 500    PHE A  52   CB  -  CG  -  CD1 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    ARG A  56   NE  -  CZ  -  NH1 ANGL. DEV. =  10.1 DEGREES          
REMARK 500    ARG A  56   NE  -  CZ  -  NH2 ANGL. DEV. = -10.2 DEGREES          
REMARK 500    TYR A  66   CB  -  CG  -  CD2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    TYR A  66   CB  -  CG  -  CD1 ANGL. DEV. =   4.5 DEGREES          
REMARK 500    ARG A  79   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG A  79   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    TYR A  81   CB  -  CG  -  CD1 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    SER A 118   CA  -  CB  -  OG  ANGL. DEV. = -16.3 DEGREES          
REMARK 500    CYS A 121   CA  -  CB  -  SG  ANGL. DEV. =   9.0 DEGREES          
REMARK 500    LYS A 131   CD  -  CE  -  NZ  ANGL. DEV. =  15.7 DEGREES          
REMARK 500    THR A 151   CB  -  CA  -  C   ANGL. DEV. = -17.8 DEGREES          
REMARK 500    LEU A 160   CB  -  CG  -  CD2 ANGL. DEV. =  10.3 DEGREES          
REMARK 500    ASN A 162   CB  -  CA  -  C   ANGL. DEV. =  13.4 DEGREES          
REMARK 500    ARG A 169   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ARG A 199   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    SER A 205   CB  -  CA  -  C   ANGL. DEV. =  13.7 DEGREES          
REMARK 500    LEU A 234   CB  -  CG  -  CD1 ANGL. DEV. =  14.5 DEGREES          
REMARK 500    LYS A 237   CA  -  CB  -  CG  ANGL. DEV. =  13.8 DEGREES          
REMARK 500    ARG A 238   NE  -  CZ  -  NH1 ANGL. DEV. =   7.9 DEGREES          
REMARK 500    ARG A 238   NE  -  CZ  -  NH2 ANGL. DEV. = -10.7 DEGREES          
REMARK 500    SER A 243   CB  -  CA  -  C   ANGL. DEV. = -12.3 DEGREES          
REMARK 500    ASP A 252   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    MET A 253   CG  -  SD  -  CE  ANGL. DEV. =  -9.9 DEGREES          
REMARK 500    ARG A 254   NE  -  CZ  -  NH2 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG A 257   CD  -  NE  -  CZ  ANGL. DEV. =  12.0 DEGREES          
REMARK 500    ARG A 268   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG A 268   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.4 DEGREES          
REMARK 500    LEU A 272   CB  -  CG  -  CD1 ANGL. DEV. =  10.4 DEGREES          
REMARK 500    ASP A 289   CB  -  CA  -  C   ANGL. DEV. =  12.5 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    ASP A  63      -74.32    -47.76                                   
REMARK 500    LYS A 103       33.40     70.85                                   
REMARK 500    CYS A 121      146.21   -170.14                                   
REMARK 500    LYS A 131       73.74   -117.83                                   
REMARK 500    SER A 146      178.04    179.14                                   
REMARK 500    PHE A 182       16.61     58.82                                   
REMARK 500    CYS A 215     -136.71   -123.79                                   
REMARK 500    ILE A 219      -50.76   -132.82                                   
REMARK 500    ILE A 261      117.37     77.07                                   
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    ARG A  33         0.11    SIDE CHAIN                              
REMARK 500    ARG A 105         0.15    SIDE CHAIN                              
REMARK 500    ARG A 112         0.14    SIDE CHAIN                              
REMARK 500    TYR A 153         0.08    SIDE CHAIN                              
REMARK 500    ARG A 254         0.15    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COL A 301                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1ECV   RELATED DB: PDB                                   
REMARK 900 PTP1B COMPLEXED WITH 5-IODO-2-(OXALYL-AMINO)-BENZOIC ACID            
REMARK 900 RELATED ID: 1C83   RELATED DB: PDB                                   
REMARK 900 PTP1B COMPLEXED WITH 6-(OXALYL-AMINO)-1H-INDOLE-5-CARBOXYLIC ACID    
REMARK 900 RELATED ID: 1C84   RELATED DB: PDB                                   
REMARK 900 PTP1B COMPLEXED WITH 3-(OXALYL-AMINO)-NAPHTHALENE-2-CARBOXLIC ACID   
REMARK 900 RELATED ID: 1C85   RELATED DB: PDB                                   
REMARK 900 PTP1B COMPLEXED WITH 2-(OXALYL-AMINO)-BENZOIC ACID                   
REMARK 900 RELATED ID: 1C86   RELATED DB: PDB                                   
REMARK 900 PTP1B (R47V, D48N) COMPLEXED WITH 2-(OXALYL-AMINO)-4,7-DIHYDRO-5H-   
REMARK 900 THIENO[2,3-C]PYRAN-3-CARBOXYLIC ACID                                 
REMARK 900 RELATED ID: 1C87   RELATED DB: PDB                                   
REMARK 900 PTP1B COMPLEXED WITH 2-(OXALYL-AMINO)-4,7-DIHYDRO-5H-THIENO[2,3-C]   
REMARK 900 PYRAN-3-CARBOXYLIC ACID                                              
REMARK 900 RELATED ID: 1C88   RELATED DB: PDB                                   
REMARK 900 PTP1B COMPLEXED WITH 2-(OXALYL-AMINO)-4,5,6,7-TETRAHYDRO-THIENO[2,3- 
REMARK 900 C]PYRIDINE-3-CARBOXYLIC ACID                                         
DBREF  1GFY A    1   298  UNP    P18031   PTN1_HUMAN       1    298             
SEQADV 1GFY VAL A   47  UNP  P18031    ARG    47 ENGINEERED                     
SEQADV 1GFY ASN A   48  UNP  P18031    ASP    48 ENGINEERED                     
SEQADV 1GFY THR A  151  UNP  P18031    SER   151 CONFLICT                       
SEQADV 1GFY ASP A  252  UNP  P18031    GLU   252 CONFLICT                       
SEQADV 1GFY CYS A  258  UNP  P18031    MET   258 ENGINEERED                     
SEQADV 1GFY GLN A  259  UNP  P18031    GLY   259 ENGINEERED                     
SEQRES   1 A  298  MET GLU MET GLU LYS GLU PHE GLU GLN ILE ASP LYS SER          
SEQRES   2 A  298  GLY SER TRP ALA ALA ILE TYR GLN ASP ILE ARG HIS GLU          
SEQRES   3 A  298  ALA SER ASP PHE PRO CYS ARG VAL ALA LYS LEU PRO LYS          
SEQRES   4 A  298  ASN LYS ASN ARG ASN ARG TYR VAL ASN VAL SER PRO PHE          
SEQRES   5 A  298  ASP HIS SER ARG ILE LYS LEU HIS GLN GLU ASP ASN ASP          
SEQRES   6 A  298  TYR ILE ASN ALA SER LEU ILE LYS MET GLU GLU ALA GLN          
SEQRES   7 A  298  ARG SER TYR ILE LEU THR GLN GLY PRO LEU PRO ASN THR          
SEQRES   8 A  298  CYS GLY HIS PHE TRP GLU MET VAL TRP GLU GLN LYS SER          
SEQRES   9 A  298  ARG GLY VAL VAL MET LEU ASN ARG VAL MET GLU LYS GLY          
SEQRES  10 A  298  SER LEU LYS CYS ALA GLN TYR TRP PRO GLN LYS GLU GLU          
SEQRES  11 A  298  LYS GLU MET ILE PHE GLU ASP THR ASN LEU LYS LEU THR          
SEQRES  12 A  298  LEU ILE SER GLU ASP ILE LYS THR TYR TYR THR VAL ARG          
SEQRES  13 A  298  GLN LEU GLU LEU GLU ASN LEU THR THR GLN GLU THR ARG          
SEQRES  14 A  298  GLU ILE LEU HIS PHE HIS TYR THR THR TRP PRO ASP PHE          
SEQRES  15 A  298  GLY VAL PRO GLU SER PRO ALA SER PHE LEU ASN PHE LEU          
SEQRES  16 A  298  PHE LYS VAL ARG GLU SER GLY SER LEU SER PRO GLU HIS          
SEQRES  17 A  298  GLY PRO VAL VAL VAL HIS CYS SER ALA GLY ILE GLY ARG          
SEQRES  18 A  298  SER GLY THR PHE CYS LEU ALA ASP THR CYS LEU LEU LEU          
SEQRES  19 A  298  MET ASP LYS ARG LYS ASP PRO SER SER VAL ASP ILE LYS          
SEQRES  20 A  298  LYS VAL LEU LEU ASP MET ARG LYS PHE ARG CYS GLN LEU          
SEQRES  21 A  298  ILE GLN THR ALA ASP GLN LEU ARG PHE SER TYR LEU ALA          
SEQRES  22 A  298  VAL ILE GLU GLY ALA LYS PHE ILE MET GLY ASP SER SER          
SEQRES  23 A  298  VAL GLN ASP GLN TRP LYS GLU LEU SER HIS GLU ASP              
HET    COL  A 301      18                                                       
HETNAM     COL 2-(OXALYL-AMINO)-4,7-DIHYDRO-5H-THIENO[2,3-C]THIOPYRAN-          
HETNAM   2 COL  3-CARBOXYLIC ACID                                               
FORMUL   2  COL    C10 H9 N O5 S2                                               
FORMUL   3  HOH   *209(H2 O)                                                    
HELIX    1   1 MET A    3  SER A   13  1                                  11    
HELIX    2   2 SER A   15  ALA A   27  1                                  13    
HELIX    3   3 LEU A   37  ASN A   44  5                                   8    
HELIX    4   4 PHE A   52  HIS A   54  5                                   3    
HELIX    5   5 THR A   91  LYS A  103  1                                  13    
HELIX    6   6 SER A  187  SER A  201  1                                  15    
HELIX    7   7 ILE A  219  LYS A  239  1                                  21    
HELIX    8   8 ASP A  240  VAL A  244  5                                   5    
HELIX    9   9 ASP A  245  LYS A  255  1                                  11    
HELIX   10  10 THR A  263  MET A  282  1                                  20    
HELIX   11  11 SER A  285  HIS A  296  1                                  12    
SHEET    1   A 9 ARG A  56  LYS A  58  0                                        
SHEET    2   A 9 TYR A  66  MET A  74 -1  N  ILE A  67   O  ILE A  57           
SHEET    3   A 9 ARG A  79  THR A  84 -1  O  ARG A  79   N  MET A  74           
SHEET    4   A 9 VAL A 211  HIS A 214  1  O  VAL A 211   N  ILE A  82           
SHEET    5   A 9 GLY A 106  MET A 109  1  O  GLY A 106   N  VAL A 212           
SHEET    6   A 9 THR A 168  TYR A 176  1  O  LEU A 172   N  VAL A 107           
SHEET    7   A 9 TYR A 153  ASN A 162 -1  O  THR A 154   N  HIS A 175           
SHEET    8   A 9 LEU A 140  ILE A 149 -1  O  LYS A 141   N  GLU A 161           
SHEET    9   A 9 MET A 133  PHE A 135 -1  N  MET A 133   O  LEU A 142           
SHEET    1   B 2 MET A 114  GLU A 115  0                                        
SHEET    2   B 2 SER A 118  LEU A 119 -1  N  SER A 118   O  GLU A 115           
SITE     1 AC1 15 TYR A  46  ASN A  48  LYS A 120  ASP A 181                    
SITE     2 AC1 15 PHE A 182  CYS A 215  SER A 216  ALA A 217                    
SITE     3 AC1 15 ILE A 219  GLY A 220  ARG A 221  GLN A 262                    
SITE     4 AC1 15 SER A 285  HOH A 322  HOH A 329                               
CRYST1   88.195   88.195  103.728  90.00  90.00 120.00 P 31 2 1      6          
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      0.011338  0.006546  0.000000        0.00000                         
SCALE2      0.000000  0.013092  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009640        0.00000                         
ATOM      1  N   MET A   3      19.241  66.717  36.291  1.00 41.44           N  
ATOM      2  CA  MET A   3      18.708  66.107  35.083  1.00 40.17           C  
ATOM      3  C   MET A   3      18.075  67.183  34.230  1.00 38.77           C  
ATOM      4  O   MET A   3      18.005  67.080  33.031  1.00 37.65           O  
ATOM      5  CB  MET A   3      17.702  65.017  35.504  1.00 40.69           C  
ATOM      6  CG  MET A   3      16.647  65.541  36.503  1.00 39.62           C  
ATOM      7  SD  MET A   3      15.551  64.243  36.999  1.00 40.39           S  
ATOM      8  CE  MET A   3      16.583  63.327  38.187  1.00 41.32           C  
ATOM      9  N   GLU A   4      17.619  68.196  34.944  1.00 38.89           N  
ATOM     10  CA  GLU A   4      16.825  69.295  34.392  1.00 42.16           C  
ATOM     11  C   GLU A   4      17.692  70.399  33.699  1.00 42.33           C  
ATOM     12  O   GLU A   4      17.387  70.895  32.635  1.00 41.61           O  
ATOM     13  CB  GLU A   4      15.968  69.804  35.565  1.00 43.99           C  
ATOM     14  CG  GLU A   4      14.875  70.797  35.109  1.00 48.01           C  
ATOM     15  CD  GLU A   4      13.714  71.024  36.135  1.00 51.00           C  
ATOM     16  OE1 GLU A   4      13.839  70.692  37.349  1.00 50.92           O  
ATOM     17  OE2 GLU A   4      12.673  71.511  35.663  1.00 52.27           O  
ATOM     18  N   LYS A   5      18.877  70.634  34.298  1.00 43.47           N  
ATOM     19  CA  LYS A   5      19.873  71.396  33.558  1.00 45.37           C  
ATOM     20  C   LYS A   5      20.435  70.562  32.397  1.00 44.11           C  
ATOM     21  O   LYS A   5      20.459  71.002  31.255  1.00 44.22           O  
ATOM     22  CB  LYS A   5      20.982  71.988  34.476  1.00 49.49           C  
ATOM     23  CG  LYS A   5      20.619  73.461  34.952  1.00 54.83           C  
ATOM     24  CD  LYS A   5      21.649  74.168  35.923  1.00 57.46           C  
ATOM     25  CE  LYS A   5      21.195  74.227  37.427  1.00 59.46           C  
ATOM     26  NZ  LYS A   5      21.726  73.204  38.384  1.00 59.99           N  
ATOM     27  N   GLU A   6      20.811  69.320  32.736  1.00 42.53           N  
ATOM     28  CA  GLU A   6      21.159  68.329  31.698  1.00 41.35           C  
ATOM     29  C   GLU A   6      20.107  68.251  30.508  1.00 40.56           C  
ATOM     30  O   GLU A   6      20.419  68.251  29.324  1.00 40.28           O  
ATOM     31  CB  GLU A   6      21.421  66.976  32.408  1.00 41.61           C  
ATOM     32  CG  GLU A   6      21.582  65.890  31.363  1.00 43.53           C  
ATOM     33  CD  GLU A   6      22.246  64.581  31.782  1.00 45.56           C  
ATOM     34  OE1 GLU A   6      22.115  64.095  32.917  1.00 47.27           O  
ATOM     35  OE2 GLU A   6      22.946  64.020  30.944  1.00 46.59           O  
ATOM     36  N   PHE A   7      18.824  68.248  30.874  1.00 38.67           N  
ATOM     37  CA  PHE A   7      17.792  68.112  29.873  1.00 38.09           C  
ATOM     38  C   PHE A   7      17.844  69.289  28.899  1.00 38.88           C  
ATOM     39  O   PHE A   7      17.900  69.125  27.697  1.00 37.28           O  
ATOM     40  CB  PHE A   7      16.401  67.997  30.522  1.00 35.56           C  
ATOM     41  CG  PHE A   7      15.294  67.771  29.524  1.00 33.75           C  
ATOM     42  CD1 PHE A   7      14.978  66.479  29.141  1.00 32.53           C  
ATOM     43  CD2 PHE A   7      14.589  68.832  28.959  1.00 33.36           C  
ATOM     44  CE1 PHE A   7      13.951  66.234  28.241  1.00 32.40           C  
ATOM     45  CE2 PHE A   7      13.585  68.588  28.023  1.00 31.43           C  
ATOM     46  CZ  PHE A   7      13.259  67.286  27.678  1.00 31.65           C  
ATOM     47  N   GLU A   8      17.899  70.480  29.479  1.00 41.65           N  
ATOM     48  CA  GLU A   8      17.925  71.645  28.586  1.00 44.13           C  
ATOM     49  C   GLU A   8      19.273  71.875  27.836  1.00 42.16           C  
ATOM     50  O   GLU A   8      19.336  72.272  26.687  1.00 42.65           O  
ATOM     51  CB  GLU A   8      17.457  72.823  29.383  1.00 48.96           C  
ATOM     52  CG  GLU A   8      15.909  72.836  29.448  1.00 56.68           C  
ATOM     53  CD  GLU A   8      15.442  73.978  30.413  1.00 63.26           C  
ATOM     54  OE1 GLU A   8      16.007  75.098  30.321  1.00 65.73           O  
ATOM     55  OE2 GLU A   8      14.538  73.726  31.244  1.00 65.75           O  
ATOM     56  N   GLN A   9      20.379  71.524  28.415  1.00 40.62           N  
ATOM     57  CA  GLN A   9      21.586  71.395  27.592  1.00 40.61           C  
ATOM     58  C   GLN A   9      21.512  70.387  26.372  1.00 40.26           C  
ATOM     59  O   GLN A   9      22.086  70.645  25.315  1.00 39.96           O  
ATOM     60  CB  GLN A   9      22.538  70.879  28.576  1.00 42.19           C  
ATOM     61  CG  GLN A   9      23.977  71.150  28.257  1.00 48.45           C  
ATOM     62  CD  GLN A   9      24.693  70.643  29.524  1.00 53.64           C  
ATOM     63  OE1 GLN A   9      25.216  69.534  29.612  1.00 57.21           O  
ATOM     64  NE2 GLN A   9      24.561  71.489  30.549  1.00 54.06           N  
ATOM     65  N   ILE A  10      20.765  69.261  26.546  1.00 38.90           N  
ATOM     66  CA  ILE A  10      20.605  68.282  25.466  1.00 36.87           C  
ATOM     67  C   ILE A  10      19.671  68.799  24.340  1.00 37.89           C  
ATOM     68  O   ILE A  10      19.967  68.734  23.151  1.00 37.89           O  
ATOM     69  CB  ILE A  10      20.167  66.878  25.913  1.00 34.51           C  
ATOM     70  CG1 ILE A  10      21.161  66.416  26.964  1.00 33.27           C  
ATOM     71  CG2 ILE A  10      20.215  65.894  24.707  1.00 30.42           C  
ATOM     72  CD1 ILE A  10      20.550  65.441  27.902  1.00 34.99           C  
ATOM     73  N   ASP A  11      18.516  69.274  24.825  1.00 38.40           N  
ATOM     74  CA  ASP A  11      17.448  69.766  23.970  1.00 40.02           C  
ATOM     75  C   ASP A  11      17.957  71.022  23.260  1.00 42.42           C  
ATOM     76  O   ASP A  11      17.769  71.260  22.080  1.00 42.74           O  
ATOM     77  CB  ASP A  11      16.242  70.123  24.887  1.00 39.90           C  
ATOM     78  CG  ASP A  11      14.874  69.521  24.571  1.00 37.86           C  
ATOM     79  OD1 ASP A  11      14.825  68.397  24.188  1.00 37.61           O  
ATOM     80  OD2 ASP A  11      13.850  70.143  24.791  1.00 37.16           O  
ATOM     81  N   LYS A  12      18.694  71.822  24.060  1.00 44.51           N  
ATOM     82  CA  LYS A  12      19.065  73.126  23.524  1.00 47.42           C  
ATOM     83  C   LYS A  12      19.959  72.845  22.345  1.00 47.16           C  
ATOM     84  O   LYS A  12      19.807  73.462  21.322  1.00 48.84           O  
ATOM     85  CB  LYS A  12      19.792  74.136  24.476  1.00 50.43           C  
ATOM     86  CG  LYS A  12      21.333  73.912  24.557  1.00 54.79           C  
ATOM     87  CD  LYS A  12      22.112  74.557  25.724  1.00 57.54           C  
ATOM     88  CE  LYS A  12      23.586  74.037  25.836  1.00 58.37           C  
ATOM     89  NZ  LYS A  12      23.858  72.730  25.177  1.00 59.45           N  
ATOM     90  N   SER A  13      20.875  71.880  22.507  1.00 45.73           N  
ATOM     91  CA  SER A  13      21.737  71.622  21.372  1.00 45.08           C  
ATOM     92  C   SER A  13      21.344  70.404  20.582  1.00 44.18           C  
ATOM     93  O   SER A  13      22.188  69.746  20.011  1.00 46.78           O  
ATOM     94  CB  SER A  13      23.157  71.382  21.802  1.00 45.92           C  
ATOM     95  OG  SER A  13      23.162  70.474  22.967  1.00 47.01           O  
ATOM     96  N   GLY A  14      20.069  70.109  20.537  1.00 41.62           N  
ATOM     97  CA  GLY A  14      19.629  68.997  19.685  1.00 39.40           C  
ATOM     98  C   GLY A  14      20.475  67.710  19.668  1.00 37.99           C  
ATOM     99  O   GLY A  14      20.826  67.292  18.597  1.00 39.07           O  
ATOM    100  N   SER A  15      20.800  67.093  20.828  1.00 36.70           N  
ATOM    101  CA  SER A  15      21.801  65.993  20.997  1.00 35.05           C  
ATOM    102  C   SER A  15      21.236  64.712  21.630  1.00 32.48           C  
ATOM    103  O   SER A  15      21.992  63.806  21.916  1.00 32.16           O  
ATOM    104  CB  SER A  15      22.898  66.547  21.927  1.00 36.05           C  
ATOM    105  OG  SER A  15      22.667  67.977  22.300  1.00 41.18           O  
ATOM    106  N   TRP A  16      19.886  64.619  21.743  1.00 30.19           N  
ATOM    107  CA  TRP A  16      19.247  63.359  22.154  1.00 27.16           C  
ATOM    108  C   TRP A  16      19.709  62.101  21.382  1.00 26.50           C  
ATOM    109  O   TRP A  16      19.938  61.107  22.029  1.00 27.89           O  
ATOM    110  CB  TRP A  16      17.704  63.508  22.126  1.00 25.22           C  
ATOM    111  CG  TRP A  16      17.259  64.413  23.257  1.00 23.15           C  
ATOM    112  CD1 TRP A  16      16.779  65.723  23.144  1.00 22.07           C  
ATOM    113  CD2 TRP A  16      17.321  64.091  24.697  1.00 22.72           C  
ATOM    114  NE1 TRP A  16      16.572  66.222  24.415  1.00 24.77           N  
ATOM    115  CE2 TRP A  16      16.904  65.261  25.389  1.00 22.52           C  
ATOM    116  CE3 TRP A  16      17.679  62.938  25.416  1.00 21.57           C  
ATOM    117  CZ2 TRP A  16      16.883  65.267  26.744  1.00 22.94           C  
ATOM    118  CZ3 TRP A  16      17.634  62.925  26.817  1.00 21.58           C  
ATOM    119  CH2 TRP A  16      17.239  64.113  27.468  1.00 23.33           C  
ATOM    120  N   ALA A  17      19.868  62.113  20.047  1.00 25.32           N  
ATOM    121  CA  ALA A  17      20.272  60.819  19.359  1.00 25.51           C  
ATOM    122  C   ALA A  17      21.726  60.344  19.592  1.00 24.40           C  
ATOM    123  O   ALA A  17      22.125  59.231  19.728  1.00 23.86           O  
ATOM    124  CB  ALA A  17      20.029  61.063  17.892  1.00 26.36           C  
ATOM    125  N   ALA A  18      22.572  61.327  19.767  1.00 25.77           N  
ATOM    126  CA  ALA A  18      23.962  61.064  20.114  1.00 25.62           C  
ATOM    127  C   ALA A  18      24.118  60.611  21.516  1.00 25.71           C  
ATOM    128  O   ALA A  18      24.848  59.693  21.757  1.00 28.45           O  
ATOM    129  CB  ALA A  18      24.688  62.408  20.168  1.00 25.47           C  
ATOM    130  N   ILE A  19      23.475  61.284  22.451  1.00 25.10           N  
ATOM    131  CA  ILE A  19      23.413  60.714  23.808  1.00 26.72           C  
ATOM    132  C   ILE A  19      22.855  59.247  23.816  1.00 25.65           C  
ATOM    133  O   ILE A  19      23.400  58.346  24.429  1.00 26.21           O  
ATOM    134  CB  ILE A  19      22.427  61.597  24.637  1.00 29.31           C  
ATOM    135  CG1 ILE A  19      22.865  63.062  24.589  1.00 32.71           C  
ATOM    136  CG2 ILE A  19      22.145  61.131  26.117  1.00 30.74           C  
ATOM    137  CD1 ILE A  19      23.943  63.395  25.608  1.00 35.88           C  
ATOM    138  N   TYR A  20      21.685  59.062  23.149  1.00 25.40           N  
ATOM    139  CA  TYR A  20      21.106  57.774  23.060  1.00 25.27           C  
ATOM    140  C   TYR A  20      22.108  56.794  22.430  1.00 26.78           C  
ATOM    141  O   TYR A  20      22.493  55.838  23.097  1.00 26.47           O  
ATOM    142  CB  TYR A  20      19.746  57.866  22.388  1.00 24.30           C  
ATOM    143  CG  TYR A  20      19.142  56.484  22.236  1.00 23.54           C  
ATOM    144  CD1 TYR A  20      18.621  55.795  23.322  1.00 24.64           C  
ATOM    145  CD2 TYR A  20      19.109  55.856  20.994  1.00 23.23           C  
ATOM    146  CE1 TYR A  20      18.115  54.486  23.198  1.00 23.72           C  
ATOM    147  CE2 TYR A  20      18.576  54.579  20.839  1.00 24.00           C  
ATOM    148  CZ  TYR A  20      18.105  53.840  21.982  1.00 24.18           C  
ATOM    149  OH  TYR A  20      17.653  52.523  22.070  1.00 19.62           O  
ATOM    150  N   GLN A  21      22.583  57.060  21.198  1.00 29.02           N  
ATOM    151  CA  GLN A  21      23.777  56.422  20.589  1.00 31.80           C  
ATOM    152  C   GLN A  21      24.953  56.100  21.610  1.00 30.46           C  
ATOM    153  O   GLN A  21      25.496  54.995  21.685  1.00 30.02           O  
ATOM    154  CB  GLN A  21      24.309  57.412  19.499  1.00 39.52           C  
ATOM    155  CG  GLN A  21      23.536  57.694  18.149  1.00 48.06           C  
ATOM    156  CD  GLN A  21      23.629  59.082  17.219  1.00 54.00           C  
ATOM    157  OE1 GLN A  21      24.571  59.905  17.144  1.00 55.77           O  
ATOM    158  NE2 GLN A  21      22.607  59.177  16.356  1.00 56.02           N  
ATOM    159  N   ASP A  22      25.349  57.078  22.413  1.00 30.00           N  
ATOM    160  CA  ASP A  22      26.423  56.879  23.402  1.00 32.26           C  
ATOM    161  C   ASP A  22      26.092  55.845  24.467  1.00 30.85           C  
ATOM    162  O   ASP A  22      26.878  54.948  24.716  1.00 30.19           O  
ATOM    163  CB  ASP A  22      26.646  58.161  24.192  1.00 35.46           C  
ATOM    164  CG  ASP A  22      27.435  59.163  23.432  1.00 40.21           C  
ATOM    165  OD1 ASP A  22      28.255  58.729  22.630  1.00 42.90           O  
ATOM    166  OD2 ASP A  22      27.260  60.366  23.668  1.00 43.54           O  
ATOM    167  N   ILE A  23      24.853  55.984  25.027  1.00 30.05           N  
ATOM    168  CA  ILE A  23      24.344  54.968  25.971  1.00 30.03           C  
ATOM    169  C   ILE A  23      24.475  53.511  25.345  1.00 29.66           C  
ATOM    170  O   ILE A  23      24.872  52.511  25.946  1.00 27.20           O  
ATOM    171  CB  ILE A  23      22.856  55.273  26.302  1.00 28.92           C  
ATOM    172  CG1 ILE A  23      22.811  56.383  27.329  1.00 30.78           C  
ATOM    173  CG2 ILE A  23      22.124  54.047  26.871  1.00 29.05           C  
ATOM    174  CD1 ILE A  23      21.442  57.044  27.372  1.00 31.42           C  
ATOM    175  N   ARG A  24      24.021  53.507  24.053  1.00 30.63           N  
ATOM    176  CA  ARG A  24      24.030  52.292  23.273  1.00 31.29           C  
ATOM    177  C   ARG A  24      25.425  51.702  23.151  1.00 30.29           C  
ATOM    178  O   ARG A  24      25.568  50.510  23.210  1.00 27.51           O  
ATOM    179  CB  ARG A  24      23.339  52.585  21.960  1.00 34.61           C  
ATOM    180  CG  ARG A  24      22.786  51.333  21.303  1.00 41.26           C  
ATOM    181  CD  ARG A  24      21.772  51.721  20.221  1.00 45.30           C  
ATOM    182  NE  ARG A  24      21.207  50.488  19.693  1.00 50.07           N  
ATOM    183  CZ  ARG A  24      21.877  49.600  18.932  1.00 52.38           C  
ATOM    184  NH1 ARG A  24      23.026  49.915  18.362  1.00 52.90           N  
ATOM    185  NH2 ARG A  24      21.360  48.400  18.756  1.00 52.25           N  
ATOM    186  N   HIS A  25      26.432  52.565  23.048  1.00 30.69           N  
ATOM    187  CA  HIS A  25      27.805  52.049  22.954  1.00 32.87           C  
ATOM    188  C   HIS A  25      28.458  51.600  24.220  1.00 32.55           C  
ATOM    189  O   HIS A  25      29.251  50.656  24.164  1.00 32.51           O  
ATOM    190  CB  HIS A  25      28.641  53.085  22.246  1.00 38.37           C  
ATOM    191  CG  HIS A  25      28.182  52.935  20.795  1.00 47.38           C  
ATOM    192  ND1 HIS A  25      28.321  51.731  20.095  1.00 50.55           N  
ATOM    193  CD2 HIS A  25      27.528  53.903  19.955  1.00 49.56           C  
ATOM    194  CE1 HIS A  25      27.770  51.962  18.874  1.00 52.60           C  
ATOM    195  NE2 HIS A  25      27.281  53.255  18.772  1.00 53.00           N  
ATOM    196  N   GLU A  26      28.053  52.268  25.344  1.00 31.30           N  
ATOM    197  CA  GLU A  26      28.411  51.899  26.726  1.00 30.65           C  
ATOM    198  C   GLU A  26      27.730  50.665  27.311  1.00 29.49           C  
ATOM    199  O   GLU A  26      28.315  50.010  28.142  1.00 29.39           O  
ATOM    200  CB  GLU A  26      28.049  53.065  27.567  1.00 33.91           C  
ATOM    201  CG  GLU A  26      28.963  54.216  27.158  1.00 40.31           C  
ATOM    202  CD  GLU A  26      28.537  55.542  27.801  1.00 43.78           C  
ATOM    203  OE1 GLU A  26      28.340  55.560  29.057  1.00 46.00           O  
ATOM    204  OE2 GLU A  26      28.435  56.525  27.027  1.00 43.48           O  
ATOM    205  N   ALA A  27      26.488  50.382  26.833  1.00 28.77           N  
ATOM    206  CA  ALA A  27      25.689  49.263  27.418  1.00 28.94           C  
ATOM    207  C   ALA A  27      26.467  47.864  27.379  1.00 29.21           C  
ATOM    208  O   ALA A  27      27.198  47.530  26.437  1.00 29.08           O  
ATOM    209  CB  ALA A  27      24.254  49.300  26.810  1.00 25.68           C  
ATOM    210  N   SER A  28      26.211  47.058  28.423  1.00 28.51           N  
ATOM    211  CA  SER A  28      26.718  45.698  28.543  1.00 27.55           C  
ATOM    212  C   SER A  28      26.283  44.809  27.464  1.00 28.28           C  
ATOM    213  O   SER A  28      25.265  44.955  26.836  1.00 28.71           O  
ATOM    214  CB  SER A  28      26.086  45.011  29.783  1.00 27.29           C  
ATOM    215  OG  SER A  28      26.069  45.845  30.982  1.00 25.75           O  
ATOM    216  N   ASP A  29      27.077  43.777  27.390  1.00 29.95           N  
ATOM    217  CA  ASP A  29      26.695  42.628  26.623  1.00 30.36           C  
ATOM    218  C   ASP A  29      27.238  41.333  27.297  1.00 27.93           C  
ATOM    219  O   ASP A  29      28.401  41.173  27.572  1.00 29.78           O  
ATOM    220  CB  ASP A  29      27.284  42.957  25.281  1.00 34.47           C  
ATOM    221  CG  ASP A  29      26.813  41.932  24.267  1.00 38.83           C  
ATOM    222  OD1 ASP A  29      25.671  41.437  24.383  1.00 40.22           O  
ATOM    223  OD2 ASP A  29      27.626  41.643  23.389  1.00 42.42           O  
ATOM    224  N   PHE A  30      26.335  40.489  27.647  1.00 23.75           N  
ATOM    225  CA  PHE A  30      26.572  39.213  28.276  1.00 22.49           C  
ATOM    226  C   PHE A  30      25.958  38.151  27.294  1.00 22.69           C  
ATOM    227  O   PHE A  30      25.132  38.511  26.440  1.00 21.06           O  
ATOM    228  CB  PHE A  30      25.898  39.220  29.644  1.00 18.96           C  
ATOM    229  CG  PHE A  30      26.534  40.273  30.514  1.00 18.56           C  
ATOM    230  CD1 PHE A  30      27.785  40.046  31.098  1.00 17.54           C  
ATOM    231  CD2 PHE A  30      25.899  41.455  30.802  1.00 17.97           C  
ATOM    232  CE1 PHE A  30      28.388  40.945  31.954  1.00 16.20           C  
ATOM    233  CE2 PHE A  30      26.475  42.315  31.730  1.00 18.71           C  
ATOM    234  CZ  PHE A  30      27.704  42.069  32.310  1.00 17.51           C  
ATOM    235  N   PRO A  31      26.441  36.872  27.422  1.00 22.68           N  
ATOM    236  CA  PRO A  31      25.884  35.809  26.591  1.00 21.55           C  
ATOM    237  C   PRO A  31      24.369  35.581  26.845  1.00 21.15           C  
ATOM    238  O   PRO A  31      23.870  35.871  27.912  1.00 19.73           O  
ATOM    239  CB  PRO A  31      26.787  34.614  26.892  1.00 20.67           C  
ATOM    240  CG  PRO A  31      27.480  34.972  28.213  1.00 21.97           C  
ATOM    241  CD  PRO A  31      27.593  36.469  28.255  1.00 20.09           C  
ATOM    242  N   CYS A  32      23.692  35.127  25.801  1.00 20.41           N  
ATOM    243  CA  CYS A  32      22.302  34.678  25.810  1.00 21.60           C  
ATOM    244  C   CYS A  32      22.253  33.281  25.180  1.00 22.13           C  
ATOM    245  O   CYS A  32      21.589  33.094  24.163  1.00 20.89           O  
ATOM    246  CB  CYS A  32      21.453  35.604  24.928  1.00 20.77           C  
ATOM    247  SG  CYS A  32      21.653  37.366  25.375  1.00 25.94           S  
ATOM    248  N   ARG A  33      23.094  32.354  25.715  1.00 21.76           N  
ATOM    249  CA  ARG A  33      23.290  31.073  25.045  1.00 22.10           C  
ATOM    250  C   ARG A  33      22.022  30.209  25.188  1.00 21.48           C  
ATOM    251  O   ARG A  33      21.679  29.466  24.270  1.00 20.64           O  
ATOM    252  CB  ARG A  33      24.496  30.268  25.582  1.00 24.07           C  
ATOM    253  CG  ARG A  33      25.790  31.090  25.501  1.00 34.01           C  
ATOM    254  CD  ARG A  33      27.130  30.358  25.943  1.00 42.48           C  
ATOM    255  NE  ARG A  33      28.157  31.299  26.554  1.00 48.78           N  
ATOM    256  CZ  ARG A  33      28.850  31.105  27.722  1.00 50.12           C  
ATOM    257  NH1 ARG A  33      29.088  29.938  28.312  1.00 51.53           N  
ATOM    258  NH2 ARG A  33      29.300  32.149  28.328  1.00 50.86           N  
ATOM    259  N   VAL A  34      21.331  30.216  26.353  1.00 20.78           N  
ATOM    260  CA  VAL A  34      20.135  29.339  26.427  1.00 20.32           C  
ATOM    261  C   VAL A  34      19.005  29.820  25.428  1.00 19.96           C  
ATOM    262  O   VAL A  34      18.425  29.047  24.680  1.00 20.32           O  
ATOM    263  CB  VAL A  34      19.703  28.830  27.834  1.00 19.28           C  
ATOM    264  CG1 VAL A  34      20.701  29.060  28.949  1.00 16.50           C  
ATOM    265  CG2 VAL A  34      18.274  29.122  28.196  1.00 20.79           C  
ATOM    266  N   ALA A  35      18.808  31.123  25.326  1.00 19.58           N  
ATOM    267  CA  ALA A  35      17.877  31.766  24.415  1.00 20.16           C  
ATOM    268  C   ALA A  35      18.093  31.234  23.054  1.00 20.87           C  
ATOM    269  O   ALA A  35      17.167  31.012  22.296  1.00 20.43           O  
ATOM    270  CB  ALA A  35      18.108  33.321  24.298  1.00 18.01           C  
ATOM    271  N   LYS A  36      19.378  31.112  22.720  1.00 21.87           N  
ATOM    272  CA  LYS A  36      19.738  30.752  21.354  1.00 21.81           C  
ATOM    273  C   LYS A  36      19.859  29.290  21.177  1.00 22.80           C  
ATOM    274  O   LYS A  36      20.177  28.899  20.089  1.00 24.87           O  
ATOM    275  CB  LYS A  36      21.030  31.375  20.922  1.00 23.65           C  
ATOM    276  CG  LYS A  36      20.974  32.897  20.834  1.00 27.00           C  
ATOM    277  CD  LYS A  36      19.739  33.284  20.010  1.00 32.03           C  
ATOM    278  CE  LYS A  36      19.856  34.639  19.356  1.00 35.80           C  
ATOM    279  NZ  LYS A  36      18.478  34.976  18.997  1.00 39.52           N  
ATOM    280  N   LEU A  37      19.561  28.447  22.159  1.00 22.83           N  
ATOM    281  CA  LEU A  37      19.488  27.038  21.812  1.00 23.69           C  
ATOM    282  C   LEU A  37      18.338  26.746  20.752  1.00 25.41           C  
ATOM    283  O   LEU A  37      17.238  27.321  20.786  1.00 24.86           O  
ATOM    284  CB  LEU A  37      19.204  26.145  23.051  1.00 23.13           C  
ATOM    285  CG  LEU A  37      20.216  26.316  24.152  1.00 23.02           C  
ATOM    286  CD1 LEU A  37      19.838  25.472  25.387  1.00 23.58           C  
ATOM    287  CD2 LEU A  37      21.579  25.936  23.641  1.00 22.03           C  
ATOM    288  N   PRO A  38      18.596  25.782  19.821  1.00 25.96           N  
ATOM    289  CA  PRO A  38      17.635  25.472  18.797  1.00 26.50           C  
ATOM    290  C   PRO A  38      16.253  25.115  19.308  1.00 26.47           C  
ATOM    291  O   PRO A  38      15.256  25.612  18.826  1.00 26.35           O  
ATOM    292  CB  PRO A  38      18.301  24.272  18.097  1.00 27.77           C  
ATOM    293  CG  PRO A  38      19.756  24.630  18.144  1.00 27.19           C  
ATOM    294  CD  PRO A  38      19.900  25.165  19.563  1.00 27.37           C  
ATOM    295  N   LYS A  39      16.273  24.325  20.382  1.00 25.12           N  
ATOM    296  CA  LYS A  39      14.963  24.056  20.980  1.00 26.53           C  
ATOM    297  C   LYS A  39      14.108  25.326  21.472  1.00 27.58           C  
ATOM    298  O   LYS A  39      12.894  25.178  21.641  1.00 29.61           O  
ATOM    299  CB  LYS A  39      15.048  23.017  22.124  1.00 25.51           C  
ATOM    300  CG  LYS A  39      15.797  23.567  23.329  1.00 26.60           C  
ATOM    301  CD  LYS A  39      15.634  22.677  24.531  1.00 29.87           C  
ATOM    302  CE  LYS A  39      16.737  22.909  25.612  1.00 32.63           C  
ATOM    303  NZ  LYS A  39      16.389  22.250  26.870  1.00 33.29           N  
ATOM    304  N   ASN A  40      14.758  26.527  21.697  1.00 26.69           N  
ATOM    305  CA  ASN A  40      14.080  27.721  22.268  1.00 24.21           C  
ATOM    306  C   ASN A  40      13.657  28.705  21.140  1.00 24.61           C  
ATOM    307  O   ASN A  40      13.173  29.825  21.317  1.00 21.92           O  
ATOM    308  CB  ASN A  40      14.995  28.328  23.357  1.00 22.62           C  
ATOM    309  CG  ASN A  40      14.981  27.346  24.525  1.00 22.98           C  
ATOM    310  OD1 ASN A  40      13.991  26.635  24.750  1.00 20.30           O  
ATOM    311  ND2 ASN A  40      16.167  27.320  25.143  1.00 20.14           N  
ATOM    312  N   LYS A  41      13.884  28.194  19.906  1.00 25.08           N  
ATOM    313  CA  LYS A  41      13.689  29.092  18.784  1.00 26.23           C  
ATOM    314  C   LYS A  41      12.232  29.659  18.811  1.00 23.91           C  
ATOM    315  O   LYS A  41      11.987  30.846  18.728  1.00 22.32           O  
ATOM    316  CB  LYS A  41      14.084  28.277  17.536  1.00 31.01           C  
ATOM    317  CG  LYS A  41      13.997  29.048  16.186  1.00 39.31           C  
ATOM    318  CD  LYS A  41      14.558  28.305  14.878  1.00 46.96           C  
ATOM    319  CE  LYS A  41      14.240  28.953  13.442  1.00 51.17           C  
ATOM    320  NZ  LYS A  41      15.192  29.961  12.837  1.00 54.80           N  
ATOM    321  N   ASN A  42      11.308  28.731  19.050  1.00 21.85           N  
ATOM    322  CA  ASN A  42       9.902  29.164  19.101  1.00 19.84           C  
ATOM    323  C   ASN A  42       9.405  29.741  20.429  1.00 18.29           C  
ATOM    324  O   ASN A  42       8.216  29.842  20.662  1.00 15.25           O  
ATOM    325  CB  ASN A  42       9.002  27.973  18.726  1.00 21.00           C  
ATOM    326  CG  ASN A  42       8.939  26.907  19.804  1.00 24.32           C  
ATOM    327  OD1 ASN A  42       9.399  26.999  20.942  1.00 24.97           O  
ATOM    328  ND2 ASN A  42       8.402  25.826  19.306  1.00 25.93           N  
ATOM    329  N   ARG A  43      10.383  29.980  21.302  1.00 18.26           N  
ATOM    330  CA  ARG A  43      10.061  30.646  22.559  1.00 17.75           C  
ATOM    331  C   ARG A  43      10.420  32.121  22.484  1.00 16.70           C  
ATOM    332  O   ARG A  43      10.044  32.873  23.324  1.00 16.29           O  
ATOM    333  CB  ARG A  43      10.688  29.882  23.726  1.00 17.84           C  
ATOM    334  CG  ARG A  43      10.094  28.453  24.024  1.00 19.42           C  
ATOM    335  CD  ARG A  43      10.755  27.817  25.297  1.00 17.25           C  
ATOM    336  NE  ARG A  43      10.055  26.547  25.455  1.00 18.69           N  
ATOM    337  CZ  ARG A  43       9.738  26.038  26.615  1.00 19.23           C  
ATOM    338  NH1 ARG A  43      10.043  26.645  27.727  1.00 20.35           N  
ATOM    339  NH2 ARG A  43       9.072  24.920  26.635  1.00 19.58           N  
ATOM    340  N   ASN A  44      11.036  32.561  21.318  1.00 15.50           N  
ATOM    341  CA  ASN A  44      11.400  34.003  21.246  1.00 14.99           C  
ATOM    342  C   ASN A  44      10.618  34.645  20.176  1.00 14.33           C  
ATOM    343  O   ASN A  44      10.482  34.108  19.092  1.00 13.22           O  
ATOM    344  CB  ASN A  44      12.886  34.220  20.939  1.00 16.20           C  
ATOM    345  CG  ASN A  44      13.672  33.552  22.031  1.00 20.25           C  
ATOM    346  OD1 ASN A  44      13.774  33.998  23.151  1.00 21.65           O  
ATOM    347  ND2 ASN A  44      14.404  32.560  21.603  1.00 19.29           N  
ATOM    348  N   ARG A  45      10.106  35.802  20.477  1.00 14.70           N  
ATOM    349  CA  ARG A  45       9.290  36.567  19.559  1.00 15.22           C  
ATOM    350  C   ARG A  45      10.185  37.251  18.500  1.00 17.12           C  
ATOM    351  O   ARG A  45       9.868  37.304  17.294  1.00 17.00           O  
ATOM    352  CB  ARG A  45       8.512  37.626  20.388  1.00 14.57           C  
ATOM    353  CG  ARG A  45       7.535  38.381  19.485  1.00 13.56           C  
ATOM    354  CD  ARG A  45       6.548  39.126  20.331  1.00 14.40           C  
ATOM    355  NE  ARG A  45       5.451  38.367  20.925  1.00 13.56           N  
ATOM    356  CZ  ARG A  45       4.373  38.024  20.170  1.00 13.37           C  
ATOM    357  NH1 ARG A  45       4.209  38.291  18.873  1.00 12.72           N  
ATOM    358  NH2 ARG A  45       3.484  37.337  20.777  1.00 10.92           N  
ATOM    359  N   TYR A  46      11.358  37.750  18.978  1.00 16.06           N  
ATOM    360  CA  TYR A  46      12.234  38.455  18.080  1.00 15.76           C  
ATOM    361  C   TYR A  46      13.621  37.814  18.189  1.00 17.70           C  
ATOM    362  O   TYR A  46      14.286  37.682  19.213  1.00 17.60           O  
ATOM    363  CB  TYR A  46      12.318  39.885  18.561  1.00 14.99           C  
ATOM    364  CG  TYR A  46      11.010  40.578  18.460  1.00 17.49           C  
ATOM    365  CD1 TYR A  46      10.402  40.714  17.210  1.00 17.33           C  
ATOM    366  CD2 TYR A  46      10.352  41.109  19.581  1.00 16.91           C  
ATOM    367  CE1 TYR A  46       9.159  41.351  17.051  1.00 17.36           C  
ATOM    368  CE2 TYR A  46       9.110  41.779  19.434  1.00 16.71           C  
ATOM    369  CZ  TYR A  46       8.512  41.929  18.172  1.00 19.02           C  
ATOM    370  OH  TYR A  46       7.330  42.627  18.064  1.00 17.62           O  
ATOM    371  N   VAL A  47      14.133  37.504  17.009  1.00 19.03           N  
ATOM    372  CA  VAL A  47      15.442  36.849  16.911  1.00 18.77           C  
ATOM    373  C   VAL A  47      16.548  37.658  17.598  1.00 19.00           C  
ATOM    374  O   VAL A  47      17.457  37.139  18.208  1.00 19.45           O  
ATOM    375  CB  VAL A  47      15.676  36.541  15.386  1.00 19.07           C  
ATOM    376  CG1 VAL A  47      16.205  37.719  14.522  1.00 15.19           C  
ATOM    377  CG2 VAL A  47      16.608  35.343  15.241  1.00 21.29           C  
ATOM    378  N   ASN A  48      16.440  38.971  17.535  1.00 18.22           N  
ATOM    379  CA  ASN A  48      17.459  39.748  18.142  1.00 17.19           C  
ATOM    380  C   ASN A  48      17.115  40.295  19.523  1.00 17.05           C  
ATOM    381  O   ASN A  48      17.728  41.232  19.960  1.00 17.46           O  
ATOM    382  CB  ASN A  48      17.673  40.927  17.256  1.00 19.52           C  
ATOM    383  CG  ASN A  48      16.442  41.795  17.198  1.00 22.60           C  
ATOM    384  OD1 ASN A  48      15.329  41.304  17.079  1.00 23.04           O  
ATOM    385  ND2 ASN A  48      16.661  43.110  17.278  1.00 22.83           N  
ATOM    386  N   VAL A  49      16.127  39.762  20.196  1.00 18.16           N  
ATOM    387  CA  VAL A  49      15.859  40.161  21.597  1.00 16.85           C  
ATOM    388  C   VAL A  49      15.668  38.900  22.510  1.00 17.15           C  
ATOM    389  O   VAL A  49      14.743  38.079  22.473  1.00 15.78           O  
ATOM    390  CB  VAL A  49      14.850  41.307  21.863  1.00 17.58           C  
ATOM    391  CG1 VAL A  49      14.213  42.133  20.710  1.00 13.70           C  
ATOM    392  CG2 VAL A  49      13.962  41.047  23.129  1.00 17.40           C  
ATOM    393  N   SER A  50      16.789  38.811  23.298  1.00 16.63           N  
ATOM    394  CA  SER A  50      17.008  37.680  24.173  1.00 15.25           C  
ATOM    395  C   SER A  50      17.411  38.169  25.565  1.00 14.97           C  
ATOM    396  O   SER A  50      17.981  39.213  25.745  1.00 13.94           O  
ATOM    397  CB  SER A  50      18.105  36.752  23.525  1.00 16.23           C  
ATOM    398  OG  SER A  50      17.976  36.337  22.095  1.00 18.98           O  
ATOM    399  N   PRO A  51      17.085  37.382  26.555  1.00 14.90           N  
ATOM    400  CA  PRO A  51      17.593  37.545  27.892  1.00 15.53           C  
ATOM    401  C   PRO A  51      19.089  37.087  28.028  1.00 16.31           C  
ATOM    402  O   PRO A  51      19.424  36.028  27.538  1.00 17.34           O  
ATOM    403  CB  PRO A  51      16.686  36.465  28.675  1.00 14.06           C  
ATOM    404  CG  PRO A  51      16.283  35.396  27.666  1.00 14.20           C  
ATOM    405  CD  PRO A  51      16.271  36.169  26.373  1.00 14.36           C  
ATOM    406  N   PHE A  52      19.958  37.888  28.682  1.00 15.64           N  
ATOM    407  CA  PHE A  52      21.259  37.292  29.089  1.00 14.83           C  
ATOM    408  C   PHE A  52      21.079  36.123  29.991  1.00 15.53           C  
ATOM    409  O   PHE A  52      20.129  36.057  30.777  1.00 16.85           O  
ATOM    410  CB  PHE A  52      22.078  38.300  29.880  1.00 14.05           C  
ATOM    411  CG  PHE A  52      22.105  39.693  29.329  1.00 12.00           C  
ATOM    412  CD1 PHE A  52      22.480  39.824  28.040  1.00 10.98           C  
ATOM    413  CD2 PHE A  52      21.880  40.810  30.102  1.00  9.87           C  
ATOM    414  CE1 PHE A  52      22.744  41.095  27.565  1.00 12.80           C  
ATOM    415  CE2 PHE A  52      22.040  42.050  29.628  1.00 10.90           C  
ATOM    416  CZ  PHE A  52      22.547  42.190  28.360  1.00 12.69           C  
ATOM    417  N   ASP A  53      21.994  35.214  29.911  1.00 15.51           N  
ATOM    418  CA  ASP A  53      21.829  34.025  30.733  1.00 16.45           C  
ATOM    419  C   ASP A  53      21.904  34.403  32.248  1.00 15.96           C  
ATOM    420  O   ASP A  53      21.286  33.799  33.129  1.00 16.88           O  
ATOM    421  CB  ASP A  53      22.891  32.930  30.414  1.00 17.53           C  
ATOM    422  CG  ASP A  53      22.947  32.485  28.993  1.00 18.56           C  
ATOM    423  OD1 ASP A  53      21.982  31.959  28.500  1.00 19.67           O  
ATOM    424  OD2 ASP A  53      23.997  32.570  28.371  1.00 18.09           O  
ATOM    425  N   HIS A  54      22.711  35.415  32.601  1.00 15.46           N  
ATOM    426  CA  HIS A  54      22.981  35.533  34.030  1.00 15.17           C  
ATOM    427  C   HIS A  54      21.719  36.052  34.734  1.00 16.46           C  
ATOM    428  O   HIS A  54      21.598  35.859  35.911  1.00 17.80           O  
ATOM    429  CB  HIS A  54      24.241  36.412  34.320  1.00 13.81           C  
ATOM    430  CG  HIS A  54      23.902  37.880  34.150  1.00 12.22           C  
ATOM    431  ND1 HIS A  54      23.319  38.626  35.104  1.00 13.92           N  
ATOM    432  CD2 HIS A  54      24.134  38.723  33.080  1.00 12.93           C  
ATOM    433  CE1 HIS A  54      23.188  39.862  34.706  1.00 10.97           C  
ATOM    434  NE2 HIS A  54      23.665  39.937  33.483  1.00 13.89           N  
ATOM    435  N   SER A  55      20.759  36.715  34.056  1.00 16.84           N  
ATOM    436  CA  SER A  55      19.597  37.269  34.759  1.00 16.01           C  
ATOM    437  C   SER A  55      18.277  36.769  34.235  1.00 15.69           C  
ATOM    438  O   SER A  55      17.247  37.355  34.509  1.00 15.80           O  
ATOM    439  CB  SER A  55      19.659  38.776  34.494  1.00 14.63           C  
ATOM    440  OG  SER A  55      19.745  39.208  33.084  1.00 16.69           O  
ATOM    441  N   ARG A  56      18.320  35.724  33.408  1.00 15.99           N  
ATOM    442  CA  ARG A  56      17.067  35.180  32.848  1.00 17.03           C  
ATOM    443  C   ARG A  56      16.252  34.484  33.984  1.00 17.82           C  
ATOM    444  O   ARG A  56      16.800  33.974  34.953  1.00 16.05           O  
ATOM    445  CB  ARG A  56      17.349  34.257  31.612  1.00 16.09           C  
ATOM    446  CG  ARG A  56      17.887  32.903  32.085  1.00 16.48           C  
ATOM    447  CD  ARG A  56      18.287  31.986  30.923  1.00 16.93           C  
ATOM    448  NE  ARG A  56      18.515  30.641  31.481  1.00 16.43           N  
ATOM    449  CZ  ARG A  56      17.683  29.624  31.593  1.00 18.31           C  
ATOM    450  NH1 ARG A  56      16.390  29.544  31.339  1.00 16.37           N  
ATOM    451  NH2 ARG A  56      18.281  28.625  32.115  1.00 17.41           N  
ATOM    452  N   ILE A  57      14.887  34.522  33.834  1.00 19.09           N  
ATOM    453  CA  ILE A  57      14.041  33.768  34.766  1.00 17.65           C  
ATOM    454  C   ILE A  57      13.985  32.308  34.341  1.00 18.10           C  
ATOM    455  O   ILE A  57      13.587  32.042  33.223  1.00 16.91           O  
ATOM    456  CB  ILE A  57      12.609  34.363  34.815  1.00 18.25           C  
ATOM    457  CG1 ILE A  57      12.707  35.851  35.213  1.00 16.47           C  
ATOM    458  CG2 ILE A  57      11.652  33.590  35.754  1.00 15.03           C  
ATOM    459  CD1 ILE A  57      12.980  36.094  36.682  1.00 19.68           C  
ATOM    460  N   LYS A  58      14.339  31.411  35.283  1.00 17.67           N  
ATOM    461  CA  LYS A  58      14.128  30.025  34.906  1.00 19.93           C  
ATOM    462  C   LYS A  58      12.716  29.545  35.361  1.00 20.25           C  
ATOM    463  O   LYS A  58      12.354  29.696  36.495  1.00 20.58           O  
ATOM    464  CB  LYS A  58      15.205  29.198  35.594  1.00 21.36           C  
ATOM    465  CG  LYS A  58      16.588  29.747  35.310  1.00 24.55           C  
ATOM    466  CD  LYS A  58      17.551  28.708  35.781  1.00 31.08           C  
ATOM    467  CE  LYS A  58      18.999  29.191  35.787  1.00 37.81           C  
ATOM    468  NZ  LYS A  58      19.835  28.560  34.729  1.00 44.61           N  
ATOM    469  N   LEU A  59      11.978  28.871  34.473  1.00 20.70           N  
ATOM    470  CA  LEU A  59      10.733  28.187  34.851  1.00 21.29           C  
ATOM    471  C   LEU A  59      11.084  27.053  35.816  1.00 22.86           C  
ATOM    472  O   LEU A  59      12.057  26.365  35.577  1.00 22.54           O  
ATOM    473  CB  LEU A  59      10.082  27.610  33.566  1.00 20.96           C  
ATOM    474  CG  LEU A  59       9.225  28.494  32.626  1.00 21.97           C  
ATOM    475  CD1 LEU A  59       8.946  29.936  33.038  1.00 18.13           C  
ATOM    476  CD2 LEU A  59       9.329  28.209  31.150  1.00 20.00           C  
ATOM    477  N   HIS A  60      10.338  26.820  36.888  1.00 23.85           N  
ATOM    478  CA  HIS A  60      10.599  25.681  37.741  1.00 26.10           C  
ATOM    479  C   HIS A  60       9.938  24.390  37.137  1.00 29.87           C  
ATOM    480  O   HIS A  60       8.944  23.834  37.597  1.00 30.49           O  
ATOM    481  CB  HIS A  60      10.029  25.870  39.137  1.00 24.67           C  
ATOM    482  CG  HIS A  60      10.469  27.103  39.898  1.00 23.02           C  
ATOM    483  ND1 HIS A  60       9.901  27.403  41.095  1.00 22.90           N  
ATOM    484  CD2 HIS A  60      11.447  28.047  39.613  1.00 21.73           C  
ATOM    485  CE1 HIS A  60      10.549  28.507  41.506  1.00 22.09           C  
ATOM    486  NE2 HIS A  60      11.471  28.902  40.657  1.00 21.17           N  
ATOM    487  N   GLN A  61      10.624  23.901  36.094  1.00 34.06           N  
ATOM    488  CA  GLN A  61      10.166  22.715  35.406  1.00 37.46           C  
ATOM    489  C   GLN A  61      11.354  22.104  34.725  1.00 38.51           C  
ATOM    490  O   GLN A  61      12.275  22.762  34.268  1.00 38.23           O  
ATOM    491  CB  GLN A  61       9.048  23.008  34.437  1.00 39.10           C  
ATOM    492  CG  GLN A  61       9.539  23.956  33.349  1.00 43.72           C  
ATOM    493  CD  GLN A  61       8.761  23.707  32.047  1.00 49.77           C  
ATOM    494  OE1 GLN A  61       9.181  22.865  31.232  1.00 53.00           O  
ATOM    495  NE2 GLN A  61       7.618  24.435  31.886  1.00 49.05           N  
ATOM    496  N   GLU A  62      11.272  20.781  34.750  1.00 40.96           N  
ATOM    497  CA  GLU A  62      12.442  20.011  34.351  1.00 43.19           C  
ATOM    498  C   GLU A  62      12.596  19.969  32.828  1.00 41.90           C  
ATOM    499  O   GLU A  62      13.700  20.080  32.356  1.00 41.98           O  
ATOM    500  CB  GLU A  62      12.362  18.608  34.981  1.00 47.27           C  
ATOM    501  CG  GLU A  62      12.024  18.720  36.482  1.00 55.82           C  
ATOM    502  CD  GLU A  62      11.986  17.351  37.183  1.00 62.85           C  
ATOM    503  OE1 GLU A  62      12.668  16.452  36.664  1.00 66.38           O  
ATOM    504  OE2 GLU A  62      11.258  17.199  38.204  1.00 66.12           O  
ATOM    505  N   ASP A  63      11.456  19.822  32.104  1.00 41.14           N  
ATOM    506  CA  ASP A  63      11.478  19.710  30.639  1.00 39.60           C  
ATOM    507  C   ASP A  63      12.337  20.760  29.950  1.00 35.04           C  
ATOM    508  O   ASP A  63      13.437  20.494  29.590  1.00 35.82           O  
ATOM    509  CB  ASP A  63      10.024  19.744  30.158  1.00 45.16           C  
ATOM    510  CG  ASP A  63       9.943  19.353  28.664  1.00 50.62           C  
ATOM    511  OD1 ASP A  63      10.001  18.141  28.394  1.00 52.13           O  
ATOM    512  OD2 ASP A  63       9.774  20.267  27.820  1.00 53.85           O  
ATOM    513  N   ASN A  64      11.820  21.965  29.918  1.00 30.93           N  
ATOM    514  CA  ASN A  64      12.547  23.084  29.399  1.00 25.73           C  
ATOM    515  C   ASN A  64      12.182  24.285  30.284  1.00 24.83           C  
ATOM    516  O   ASN A  64      11.033  24.746  30.318  1.00 24.34           O  
ATOM    517  CB  ASN A  64      12.090  23.213  27.928  1.00 24.25           C  
ATOM    518  CG  ASN A  64      12.921  24.274  27.296  1.00 22.43           C  
ATOM    519  OD1 ASN A  64      13.478  25.033  28.031  1.00 24.77           O  
ATOM    520  ND2 ASN A  64      12.996  24.496  26.047  1.00 18.28           N  
ATOM    521  N   ASP A  65      13.204  24.751  30.998  1.00 23.33           N  
ATOM    522  CA  ASP A  65      13.108  25.852  31.945  1.00 22.60           C  
ATOM    523  C   ASP A  65      13.158  27.283  31.284  1.00 21.60           C  
ATOM    524  O   ASP A  65      13.187  28.273  32.006  1.00 21.66           O  
ATOM    525  CB  ASP A  65      14.189  25.736  33.028  1.00 22.56           C  
ATOM    526  CG  ASP A  65      15.629  26.246  32.672  1.00 25.91           C  
ATOM    527  OD1 ASP A  65      15.893  26.807  31.613  1.00 26.04           O  
ATOM    528  OD2 ASP A  65      16.525  26.112  33.508  1.00 29.75           O  
ATOM    529  N   TYR A  66      13.178  27.384  29.939  1.00 20.41           N  
ATOM    530  CA  TYR A  66      13.462  28.706  29.297  1.00 17.71           C  
ATOM    531  C   TYR A  66      12.150  29.538  29.105  1.00 16.87           C  
ATOM    532  O   TYR A  66      11.145  29.047  28.614  1.00 16.31           O  
ATOM    533  CB  TYR A  66      14.274  28.491  28.032  1.00 13.90           C  
ATOM    534  CG  TYR A  66      14.482  29.790  27.348  1.00 15.03           C  
ATOM    535  CD1 TYR A  66      15.414  30.781  27.732  1.00 11.95           C  
ATOM    536  CD2 TYR A  66      13.695  30.046  26.252  1.00 14.49           C  
ATOM    537  CE1 TYR A  66      15.481  32.021  27.135  1.00 11.45           C  
ATOM    538  CE2 TYR A  66      13.895  31.232  25.564  1.00 12.73           C  
ATOM    539  CZ  TYR A  66      14.683  32.319  26.054  1.00 11.12           C  
ATOM    540  OH  TYR A  66      14.841  33.624  25.555  1.00 10.88           O  
ATOM    541  N   ILE A  67      12.238  30.773  29.542  1.00 16.50           N  
ATOM    542  CA  ILE A  67      11.325  31.789  29.052  1.00 14.40           C  
ATOM    543  C   ILE A  67      12.120  33.026  28.689  1.00 14.23           C  
ATOM    544  O   ILE A  67      13.056  33.417  29.388  1.00 13.96           O  
ATOM    545  CB  ILE A  67      10.258  32.093  30.192  1.00 15.66           C  
ATOM    546  CG1 ILE A  67       9.143  33.077  29.678  1.00 13.43           C  
ATOM    547  CG2 ILE A  67      10.899  32.446  31.589  1.00 12.21           C  
ATOM    548  CD1 ILE A  67       7.834  33.193  30.499  1.00 15.36           C  
ATOM    549  N   ASN A  68      11.640  33.752  27.661  1.00 12.59           N  
ATOM    550  CA  ASN A  68      12.236  35.017  27.391  1.00 13.55           C  
ATOM    551  C   ASN A  68      11.857  36.054  28.455  1.00 13.99           C  
ATOM    552  O   ASN A  68      10.975  36.901  28.255  1.00 14.30           O  
ATOM    553  CB  ASN A  68      11.858  35.560  25.980  1.00 13.30           C  
ATOM    554  CG  ASN A  68      12.722  36.711  25.490  1.00 13.89           C  
ATOM    555  OD1 ASN A  68      12.927  37.706  26.214  1.00 14.22           O  
ATOM    556  ND2 ASN A  68      12.986  36.663  24.183  1.00 14.55           N  
ATOM    557  N   ALA A  69      12.624  36.074  29.568  1.00 13.53           N  
ATOM    558  CA  ALA A  69      12.275  37.030  30.613  1.00 13.02           C  
ATOM    559  C   ALA A  69      13.540  37.247  31.431  1.00 13.09           C  
ATOM    560  O   ALA A  69      14.295  36.311  31.615  1.00 11.98           O  
ATOM    561  CB  ALA A  69      11.195  36.358  31.537  1.00 13.28           C  
ATOM    562  N   SER A  70      13.745  38.481  31.925  1.00 12.26           N  
ATOM    563  CA  SER A  70      14.881  38.730  32.829  1.00 13.52           C  
ATOM    564  C   SER A  70      14.479  39.418  34.113  1.00 13.62           C  
ATOM    565  O   SER A  70      13.566  40.203  34.076  1.00 13.85           O  
ATOM    566  CB  SER A  70      15.725  39.829  32.132  1.00 10.63           C  
ATOM    567  OG  SER A  70      15.832  39.550  30.714  1.00 13.85           O  
ATOM    568  N   LEU A  71      15.246  39.212  35.159  1.00 14.86           N  
ATOM    569  CA  LEU A  71      15.085  39.911  36.420  1.00 17.06           C  
ATOM    570  C   LEU A  71      16.060  41.098  36.424  1.00 17.09           C  
ATOM    571  O   LEU A  71      17.248  40.941  36.296  1.00 16.58           O  
ATOM    572  CB  LEU A  71      15.398  38.862  37.511  1.00 18.82           C  
ATOM    573  CG  LEU A  71      14.873  39.137  38.954  1.00 21.26           C  
ATOM    574  CD1 LEU A  71      16.040  39.419  39.801  1.00 20.33           C  
ATOM    575  CD2 LEU A  71      13.793  40.221  39.180  1.00 19.89           C  
ATOM    576  N   ILE A  72      15.466  42.274  36.487  1.00 17.24           N  
ATOM    577  CA  ILE A  72      16.137  43.547  36.627  1.00 18.02           C  
ATOM    578  C   ILE A  72      16.139  43.822  38.180  1.00 19.69           C  
ATOM    579  O   ILE A  72      15.131  44.174  38.782  1.00 19.91           O  
ATOM    580  CB  ILE A  72      15.436  44.687  35.806  1.00 17.38           C  
ATOM    581  CG1 ILE A  72      15.432  44.672  34.258  1.00 15.91           C  
ATOM    582  CG2 ILE A  72      16.101  46.061  36.116  1.00 17.63           C  
ATOM    583  CD1 ILE A  72      15.322  43.363  33.589  1.00 14.55           C  
ATOM    584  N   LYS A  73      17.309  43.588  38.768  1.00 20.19           N  
ATOM    585  CA  LYS A  73      17.447  43.785  40.179  1.00 22.60           C  
ATOM    586  C   LYS A  73      18.152  45.128  40.468  1.00 21.17           C  
ATOM    587  O   LYS A  73      19.316  45.243  40.228  1.00 20.17           O  
ATOM    588  CB  LYS A  73      18.109  42.506  40.619  1.00 25.71           C  
ATOM    589  CG  LYS A  73      18.293  42.551  42.133  1.00 35.11           C  
ATOM    590  CD  LYS A  73      17.825  41.280  42.888  1.00 43.21           C  
ATOM    591  CE  LYS A  73      17.851  41.513  44.442  1.00 48.72           C  
ATOM    592  NZ  LYS A  73      17.163  40.448  45.188  1.00 53.06           N  
ATOM    593  N   MET A  74      17.353  46.140  40.854  1.00 20.96           N  
ATOM    594  CA  MET A  74      17.941  47.453  41.055  1.00 19.46           C  
ATOM    595  C   MET A  74      18.352  47.589  42.544  1.00 22.01           C  
ATOM    596  O   MET A  74      17.566  47.958  43.399  1.00 20.82           O  
ATOM    597  CB  MET A  74      16.895  48.502  40.652  1.00 17.74           C  
ATOM    598  CG  MET A  74      16.520  48.477  39.170  1.00 16.89           C  
ATOM    599  SD  MET A  74      18.042  48.479  38.165  1.00 18.86           S  
ATOM    600  CE  MET A  74      18.379  50.254  38.226  1.00 12.07           C  
ATOM    601  N   GLU A  75      19.602  47.300  42.876  1.00 25.71           N  
ATOM    602  CA  GLU A  75      19.991  47.087  44.292  1.00 27.90           C  
ATOM    603  C   GLU A  75      19.889  48.377  45.226  1.00 27.55           C  
ATOM    604  O   GLU A  75      19.278  48.496  46.309  1.00 25.68           O  
ATOM    605  CB  GLU A  75      21.385  46.546  44.180  1.00 30.19           C  
ATOM    606  CG  GLU A  75      21.885  46.264  45.574  1.00 37.61           C  
ATOM    607  CD  GLU A  75      23.305  45.744  45.515  1.00 43.38           C  
ATOM    608  OE1 GLU A  75      24.183  46.418  44.996  1.00 46.10           O  
ATOM    609  OE2 GLU A  75      23.534  44.657  46.002  1.00 47.75           O  
ATOM    610  N   GLU A  76      20.494  49.406  44.693  1.00 28.07           N  
ATOM    611  CA  GLU A  76      20.387  50.650  45.429  1.00 29.37           C  
ATOM    612  C   GLU A  76      18.925  51.111  45.738  1.00 29.38           C  
ATOM    613  O   GLU A  76      18.549  51.406  46.887  1.00 29.32           O  
ATOM    614  CB  GLU A  76      21.173  51.651  44.648  1.00 31.42           C  
ATOM    615  CG  GLU A  76      21.148  53.030  45.297  1.00 36.90           C  
ATOM    616  CD  GLU A  76      21.822  54.022  44.380  1.00 42.56           C  
ATOM    617  OE1 GLU A  76      21.943  53.828  43.162  1.00 44.55           O  
ATOM    618  OE2 GLU A  76      22.224  55.020  44.931  1.00 46.15           O  
ATOM    619  N   ALA A  77      18.107  51.103  44.654  1.00 28.34           N  
ATOM    620  CA  ALA A  77      16.681  51.431  44.752  1.00 27.30           C  
ATOM    621  C   ALA A  77      15.938  50.382  45.561  1.00 27.68           C  
ATOM    622  O   ALA A  77      14.886  50.698  46.081  1.00 28.52           O  
ATOM    623  CB  ALA A  77      16.009  51.480  43.378  1.00 27.64           C  
ATOM    624  N   GLN A  78      16.490  49.174  45.654  1.00 27.32           N  
ATOM    625  CA  GLN A  78      15.799  48.085  46.343  1.00 29.25           C  
ATOM    626  C   GLN A  78      14.378  47.680  45.734  1.00 28.70           C  
ATOM    627  O   GLN A  78      13.425  47.420  46.455  1.00 29.17           O  
ATOM    628  CB  GLN A  78      15.620  48.521  47.771  1.00 32.56           C  
ATOM    629  CG  GLN A  78      16.893  49.014  48.475  1.00 39.13           C  
ATOM    630  CD  GLN A  78      17.253  47.804  49.226  1.00 45.55           C  
ATOM    631  OE1 GLN A  78      16.718  47.586  50.306  1.00 48.28           O  
ATOM    632  NE2 GLN A  78      18.005  46.950  48.517  1.00 48.41           N  
ATOM    633  N   ARG A  79      14.267  47.733  44.388  1.00 26.70           N  
ATOM    634  CA  ARG A  79      13.078  47.302  43.660  1.00 22.74           C  
ATOM    635  C   ARG A  79      13.570  46.400  42.585  1.00 21.49           C  
ATOM    636  O   ARG A  79      14.543  46.778  41.958  1.00 23.14           O  
ATOM    637  CB  ARG A  79      12.358  48.505  43.042  1.00 21.82           C  
ATOM    638  CG  ARG A  79      10.980  48.034  42.504  1.00 19.65           C  
ATOM    639  CD  ARG A  79       9.869  49.078  42.265  1.00 19.79           C  
ATOM    640  NE  ARG A  79       9.277  49.513  43.502  1.00 20.05           N  
ATOM    641  CZ  ARG A  79       8.696  50.675  43.742  1.00 20.50           C  
ATOM    642  NH1 ARG A  79       8.494  51.587  42.833  1.00 21.27           N  
ATOM    643  NH2 ARG A  79       8.359  50.914  44.958  1.00 21.86           N  
ATOM    644  N   SER A  80      12.938  45.274  42.333  1.00 20.40           N  
ATOM    645  CA  SER A  80      13.214  44.447  41.191  1.00 18.43           C  
ATOM    646  C   SER A  80      11.997  44.391  40.285  1.00 17.53           C  
ATOM    647  O   SER A  80      10.896  44.363  40.723  1.00 15.85           O  
ATOM    648  CB  SER A  80      13.228  43.036  41.787  1.00 20.59           C  
ATOM    649  OG  SER A  80      14.517  42.773  42.489  1.00 27.09           O  
ATOM    650  N   TYR A  81      12.238  44.210  38.984  1.00 16.07           N  
ATOM    651  CA  TYR A  81      11.112  43.945  38.046  1.00 14.02           C  
ATOM    652  C   TYR A  81      11.523  42.784  37.196  1.00 13.14           C  
ATOM    653  O   TYR A  81      12.722  42.611  36.958  1.00 12.92           O  
ATOM    654  CB  TYR A  81      10.926  45.066  37.040  1.00 13.21           C  
ATOM    655  CG  TYR A  81      11.082  46.441  37.602  1.00 12.53           C  
ATOM    656  CD1 TYR A  81      12.363  46.915  37.708  1.00 13.99           C  
ATOM    657  CD2 TYR A  81      10.007  47.205  37.996  1.00 11.28           C  
ATOM    658  CE1 TYR A  81      12.574  48.147  38.268  1.00 15.13           C  
ATOM    659  CE2 TYR A  81      10.191  48.480  38.479  1.00 12.53           C  
ATOM    660  CZ  TYR A  81      11.467  48.976  38.643  1.00 14.93           C  
ATOM    661  OH  TYR A  81      11.520  50.285  39.184  1.00 13.21           O  
ATOM    662  N   ILE A  82      10.515  42.028  36.734  1.00 13.03           N  
ATOM    663  CA  ILE A  82      10.699  41.029  35.635  1.00 13.20           C  
ATOM    664  C   ILE A  82      10.317  41.671  34.306  1.00 13.36           C  
ATOM    665  O   ILE A  82       9.185  42.140  34.207  1.00 14.60           O  
ATOM    666  CB  ILE A  82       9.964  39.661  35.892  1.00 13.67           C  
ATOM    667  CG1 ILE A  82      10.603  38.999  37.148  1.00 14.25           C  
ATOM    668  CG2 ILE A  82       9.990  38.709  34.644  1.00 12.08           C  
ATOM    669  CD1 ILE A  82       9.882  37.732  37.683  1.00 13.11           C  
ATOM    670  N   LEU A  83      11.240  41.724  33.314  1.00 12.28           N  
ATOM    671  CA  LEU A  83      10.857  42.264  32.019  1.00 11.69           C  
ATOM    672  C   LEU A  83      10.789  41.109  31.025  1.00 14.02           C  
ATOM    673  O   LEU A  83      11.695  40.286  30.965  1.00 16.03           O  
ATOM    674  CB  LEU A  83      11.749  43.387  31.454  1.00  9.21           C  
ATOM    675  CG  LEU A  83      11.496  44.811  31.971  1.00 12.38           C  
ATOM    676  CD1 LEU A  83      11.563  44.845  33.479  1.00 12.73           C  
ATOM    677  CD2 LEU A  83      12.576  45.775  31.411  1.00 13.19           C  
ATOM    678  N   THR A  84       9.678  41.051  30.270  1.00 13.90           N  
ATOM    679  CA  THR A  84       9.402  39.884  29.412  1.00 11.81           C  
ATOM    680  C   THR A  84       8.759  40.342  28.102  1.00 11.80           C  
ATOM    681  O   THR A  84       8.343  41.499  27.950  1.00 11.65           O  
ATOM    682  CB  THR A  84       8.580  38.813  30.149  1.00 10.49           C  
ATOM    683  OG1 THR A  84       8.831  37.527  29.489  1.00 11.91           O  
ATOM    684  CG2 THR A  84       7.161  39.265  30.560  1.00 10.15           C  
ATOM    685  N   GLN A  85       8.881  39.482  27.098  1.00 12.15           N  
ATOM    686  CA  GLN A  85       8.264  39.796  25.813  1.00 12.37           C  
ATOM    687  C   GLN A  85       6.740  39.518  25.906  1.00 13.70           C  
ATOM    688  O   GLN A  85       6.176  38.870  26.795  1.00 14.08           O  
ATOM    689  CB  GLN A  85       8.889  38.941  24.686  1.00 10.58           C  
ATOM    690  CG  GLN A  85       8.551  37.487  24.948  1.00 12.10           C  
ATOM    691  CD  GLN A  85       9.112  36.545  23.985  1.00 15.39           C  
ATOM    692  OE1 GLN A  85       8.710  35.422  23.877  1.00 17.83           O  
ATOM    693  NE2 GLN A  85      10.145  36.913  23.302  1.00 13.63           N  
ATOM    694  N   GLY A  86       6.046  40.106  24.911  1.00 13.29           N  
ATOM    695  CA  GLY A  86       4.653  39.742  24.942  1.00 12.54           C  
ATOM    696  C   GLY A  86       4.470  38.274  24.652  1.00 13.12           C  
ATOM    697  O   GLY A  86       4.981  37.797  23.638  1.00 13.43           O  
ATOM    698  N   PRO A  87       3.693  37.585  25.527  1.00 13.86           N  
ATOM    699  CA  PRO A  87       3.672  36.134  25.369  1.00 14.07           C  
ATOM    700  C   PRO A  87       3.357  35.660  23.955  1.00 15.17           C  
ATOM    701  O   PRO A  87       2.586  36.331  23.256  1.00 15.33           O  
ATOM    702  CB  PRO A  87       2.613  35.594  26.383  1.00 12.31           C  
ATOM    703  CG  PRO A  87       2.738  36.632  27.480  1.00 13.23           C  
ATOM    704  CD  PRO A  87       3.079  38.008  26.806  1.00 11.57           C  
ATOM    705  N   LEU A  88       3.931  34.541  23.537  1.00 16.09           N  
ATOM    706  CA  LEU A  88       3.566  33.933  22.210  1.00 18.15           C  
ATOM    707  C   LEU A  88       2.381  32.930  22.387  1.00 18.18           C  
ATOM    708  O   LEU A  88       1.998  32.572  23.505  1.00 15.72           O  
ATOM    709  CB  LEU A  88       4.718  33.009  21.632  1.00 17.37           C  
ATOM    710  CG  LEU A  88       5.906  33.636  20.885  1.00 18.29           C  
ATOM    711  CD1 LEU A  88       5.723  34.907  20.167  1.00 17.93           C  
ATOM    712  CD2 LEU A  88       7.281  33.381  21.444  1.00 16.00           C  
ATOM    713  N   PRO A  89       1.813  32.442  21.238  1.00 18.26           N  
ATOM    714  CA  PRO A  89       0.694  31.573  21.417  1.00 18.28           C  
ATOM    715  C   PRO A  89       1.067  30.244  22.164  1.00 20.06           C  
ATOM    716  O   PRO A  89       0.185  29.634  22.708  1.00 19.97           O  
ATOM    717  CB  PRO A  89       0.194  31.362  19.994  1.00 18.80           C  
ATOM    718  CG  PRO A  89       0.735  32.511  19.171  1.00 17.44           C  
ATOM    719  CD  PRO A  89       2.049  32.861  19.834  1.00 17.37           C  
ATOM    720  N   ASN A  90       2.364  29.802  22.166  1.00 18.92           N  
ATOM    721  CA  ASN A  90       2.781  28.559  22.856  1.00 17.17           C  
ATOM    722  C   ASN A  90       3.482  28.834  24.210  1.00 16.96           C  
ATOM    723  O   ASN A  90       4.041  27.924  24.796  1.00 16.96           O  
ATOM    724  CB  ASN A  90       3.766  27.850  21.946  1.00 17.80           C  
ATOM    725  CG  ASN A  90       4.960  28.761  21.518  1.00 20.65           C  
ATOM    726  OD1 ASN A  90       4.767  29.900  21.107  1.00 23.34           O  
ATOM    727  ND2 ASN A  90       6.228  28.274  21.627  1.00 20.78           N  
ATOM    728  N   THR A  91       3.541  30.115  24.605  1.00 15.75           N  
ATOM    729  CA  THR A  91       4.326  30.394  25.789  1.00 13.54           C  
ATOM    730  C   THR A  91       3.476  31.196  26.774  1.00 13.48           C  
ATOM    731  O   THR A  91       3.949  31.758  27.735  1.00 12.85           O  
ATOM    732  CB  THR A  91       5.645  31.120  25.546  1.00 13.92           C  
ATOM    733  OG1 THR A  91       5.069  32.422  25.216  1.00 14.66           O  
ATOM    734  CG2 THR A  91       6.553  30.646  24.374  1.00 13.18           C  
ATOM    735  N   CYS A  92       2.144  31.218  26.626  1.00 14.55           N  
ATOM    736  CA  CYS A  92       1.200  31.856  27.622  1.00 14.58           C  
ATOM    737  C   CYS A  92       1.113  31.040  28.927  1.00 14.55           C  
ATOM    738  O   CYS A  92       1.015  31.559  30.038  1.00 14.49           O  
ATOM    739  CB  CYS A  92      -0.252  31.947  27.088  1.00 13.64           C  
ATOM    740  SG  CYS A  92      -0.379  32.959  25.594  1.00 18.83           S  
ATOM    741  N   GLY A  93       1.192  29.729  28.780  1.00 15.83           N  
ATOM    742  CA  GLY A  93       1.260  28.900  29.984  1.00 15.19           C  
ATOM    743  C   GLY A  93       2.584  29.017  30.787  1.00 16.92           C  
ATOM    744  O   GLY A  93       2.606  29.168  31.999  1.00 18.18           O  
ATOM    745  N   HIS A  94       3.762  29.063  30.109  1.00 17.25           N  
ATOM    746  CA  HIS A  94       5.055  29.525  30.711  1.00 15.62           C  
ATOM    747  C   HIS A  94       4.964  30.913  31.357  1.00 16.87           C  
ATOM    748  O   HIS A  94       5.360  31.142  32.490  1.00 18.53           O  
ATOM    749  CB  HIS A  94       6.114  29.716  29.622  1.00 13.70           C  
ATOM    750  CG  HIS A  94       6.220  28.509  28.780  1.00 12.61           C  
ATOM    751  ND1 HIS A  94       6.645  28.606  27.547  1.00 13.14           N  
ATOM    752  CD2 HIS A  94       5.971  27.168  29.015  1.00 14.54           C  
ATOM    753  CE1 HIS A  94       6.670  27.443  26.949  1.00 12.55           C  
ATOM    754  NE2 HIS A  94       6.259  26.526  27.859  1.00 16.22           N  
ATOM    755  N   PHE A  95       4.391  31.908  30.659  1.00 17.15           N  
ATOM    756  CA  PHE A  95       4.231  33.255  31.269  1.00 14.23           C  
ATOM    757  C   PHE A  95       3.547  33.204  32.627  1.00 15.03           C  
ATOM    758  O   PHE A  95       3.978  33.794  33.616  1.00 14.93           O  
ATOM    759  CB  PHE A  95       3.402  34.128  30.285  1.00 12.09           C  
ATOM    760  CG  PHE A  95       3.073  35.498  30.845  1.00 11.62           C  
ATOM    761  CD1 PHE A  95       3.952  36.568  30.646  1.00 11.13           C  
ATOM    762  CD2 PHE A  95       1.905  35.721  31.534  1.00  8.92           C  
ATOM    763  CE1 PHE A  95       3.684  37.846  31.174  1.00 12.55           C  
ATOM    764  CE2 PHE A  95       1.656  36.981  32.081  1.00 10.37           C  
ATOM    765  CZ  PHE A  95       2.540  38.051  31.947  1.00 10.80           C  
ATOM    766  N   TRP A  96       2.389  32.467  32.620  1.00 15.30           N  
ATOM    767  CA  TRP A  96       1.639  32.309  33.896  1.00 15.99           C  
ATOM    768  C   TRP A  96       2.350  31.417  34.940  1.00 16.87           C  
ATOM    769  O   TRP A  96       2.308  31.676  36.130  1.00 17.03           O  
ATOM    770  CB  TRP A  96       0.154  31.886  33.631  1.00 15.98           C  
ATOM    771  CG  TRP A  96      -0.536  33.079  33.005  1.00 14.71           C  
ATOM    772  CD1 TRP A  96      -1.020  33.135  31.704  1.00 15.44           C  
ATOM    773  CD2 TRP A  96      -0.807  34.354  33.636  1.00 14.21           C  
ATOM    774  NE1 TRP A  96      -1.592  34.371  31.507  1.00 16.45           N  
ATOM    775  CE2 TRP A  96      -1.475  35.130  32.687  1.00 14.54           C  
ATOM    776  CE3 TRP A  96      -0.581  34.834  34.889  1.00 13.30           C  
ATOM    777  CZ2 TRP A  96      -1.875  36.391  33.004  1.00 14.89           C  
ATOM    778  CZ3 TRP A  96      -0.992  36.098  35.236  1.00 13.30           C  
ATOM    779  CH2 TRP A  96      -1.638  36.888  34.280  1.00 15.00           C  
ATOM    780  N   GLU A  97       3.089  30.388  34.459  1.00 17.93           N  
ATOM    781  CA  GLU A  97       3.963  29.616  35.338  1.00 15.34           C  
ATOM    782  C   GLU A  97       4.964  30.526  36.017  1.00 14.72           C  
ATOM    783  O   GLU A  97       5.078  30.497  37.199  1.00 15.33           O  
ATOM    784  CB  GLU A  97       4.589  28.507  34.501  1.00 14.16           C  
ATOM    785  CG  GLU A  97       5.480  27.677  35.475  1.00 18.39           C  
ATOM    786  CD  GLU A  97       6.476  26.693  34.817  1.00 19.80           C  
ATOM    787  OE1 GLU A  97       6.435  26.551  33.621  1.00 18.40           O  
ATOM    788  OE2 GLU A  97       7.265  26.041  35.486  1.00 20.96           O  
ATOM    789  N   MET A  98       5.564  31.414  35.263  1.00 14.78           N  
ATOM    790  CA  MET A  98       6.505  32.433  35.756  1.00 14.65           C  
ATOM    791  C   MET A  98       5.860  33.369  36.785  1.00 15.22           C  
ATOM    792  O   MET A  98       6.349  33.631  37.873  1.00 16.02           O  
ATOM    793  CB  MET A  98       7.082  33.202  34.545  1.00 13.00           C  
ATOM    794  CG  MET A  98       8.011  34.296  35.086  1.00 14.97           C  
ATOM    795  SD  MET A  98       8.736  35.414  33.865  1.00 17.69           S  
ATOM    796  CE  MET A  98       7.251  36.224  33.140  1.00 10.76           C  
ATOM    797  N   VAL A  99       4.690  33.941  36.451  1.00 15.83           N  
ATOM    798  CA  VAL A  99       4.014  34.813  37.443  1.00 14.83           C  
ATOM    799  C   VAL A  99       3.777  34.074  38.836  1.00 16.89           C  
ATOM    800  O   VAL A  99       4.026  34.613  39.912  1.00 17.20           O  
ATOM    801  CB  VAL A  99       2.691  35.294  36.811  1.00 14.60           C  
ATOM    802  CG1 VAL A  99       1.859  35.957  37.904  1.00 16.02           C  
ATOM    803  CG2 VAL A  99       2.816  36.268  35.618  1.00 10.37           C  
ATOM    804  N   TRP A 100       3.319  32.794  38.726  1.00 16.81           N  
ATOM    805  CA  TRP A 100       3.070  31.991  39.936  1.00 16.94           C  
ATOM    806  C   TRP A 100       4.335  31.683  40.779  1.00 16.62           C  
ATOM    807  O   TRP A 100       4.411  31.862  41.981  1.00 17.80           O  
ATOM    808  CB  TRP A 100       2.459  30.660  39.466  1.00 17.67           C  
ATOM    809  CG  TRP A 100       2.087  29.897  40.694  1.00 18.67           C  
ATOM    810  CD1 TRP A 100       2.916  28.994  41.347  1.00 20.46           C  
ATOM    811  CD2 TRP A 100       0.865  29.963  41.445  1.00 20.62           C  
ATOM    812  NE1 TRP A 100       2.275  28.521  42.444  1.00 21.12           N  
ATOM    813  CE2 TRP A 100       1.019  29.090  42.549  1.00 22.26           C  
ATOM    814  CE3 TRP A 100      -0.288  30.648  41.316  1.00 20.24           C  
ATOM    815  CZ2 TRP A 100       0.011  28.927  43.454  1.00 22.37           C  
ATOM    816  CZ3 TRP A 100      -1.300  30.466  42.230  1.00 21.76           C  
ATOM    817  CH2 TRP A 100      -1.165  29.618  43.312  1.00 20.40           C  
ATOM    818  N   GLU A 101       5.344  31.146  40.104  1.00 17.13           N  
ATOM    819  CA  GLU A 101       6.608  30.765  40.749  1.00 17.55           C  
ATOM    820  C   GLU A 101       7.307  31.955  41.328  1.00 18.69           C  
ATOM    821  O   GLU A 101       7.681  31.840  42.479  1.00 21.08           O  
ATOM    822  CB  GLU A 101       7.480  30.037  39.708  1.00 18.42           C  
ATOM    823  CG  GLU A 101       6.890  28.622  39.434  1.00 17.77           C  
ATOM    824  CD  GLU A 101       7.444  27.931  38.205  1.00 19.09           C  
ATOM    825  OE1 GLU A 101       8.292  28.501  37.575  1.00 17.96           O  
ATOM    826  OE2 GLU A 101       7.002  26.800  37.921  1.00 19.87           O  
ATOM    827  N   GLN A 102       7.378  33.089  40.581  1.00 18.06           N  
ATOM    828  CA  GLN A 102       7.941  34.387  41.042  1.00 18.51           C  
ATOM    829  C   GLN A 102       7.126  35.192  42.086  1.00 18.99           C  
ATOM    830  O   GLN A 102       7.672  36.152  42.669  1.00 20.21           O  
ATOM    831  CB  GLN A 102       8.307  35.286  39.827  1.00 18.55           C  
ATOM    832  CG  GLN A 102       9.280  34.578  38.884  1.00 18.86           C  
ATOM    833  CD  GLN A 102      10.546  34.048  39.644  1.00 21.08           C  
ATOM    834  OE1 GLN A 102      11.210  34.771  40.395  1.00 22.70           O  
ATOM    835  NE2 GLN A 102      10.868  32.809  39.409  1.00 18.66           N  
ATOM    836  N   LYS A 103       5.807  34.814  42.257  1.00 17.99           N  
ATOM    837  CA  LYS A 103       4.923  35.371  43.316  1.00 17.89           C  
ATOM    838  C   LYS A 103       4.529  36.796  43.082  1.00 17.77           C  
ATOM    839  O   LYS A 103       4.409  37.626  43.996  1.00 17.35           O  
ATOM    840  CB  LYS A 103       5.530  35.220  44.720  1.00 20.43           C  
ATOM    841  CG  LYS A 103       5.482  33.743  45.210  1.00 23.62           C  
ATOM    842  CD  LYS A 103       6.304  33.487  46.463  1.00 29.61           C  
ATOM    843  CE  LYS A 103       7.157  32.223  46.300  1.00 35.48           C  
ATOM    844  NZ  LYS A 103       8.002  32.420  45.074  1.00 42.09           N  
ATOM    845  N   SER A 104       4.408  37.046  41.783  1.00 17.94           N  
ATOM    846  CA  SER A 104       4.109  38.446  41.407  1.00 16.61           C  
ATOM    847  C   SER A 104       2.642  38.729  41.636  1.00 16.65           C  
ATOM    848  O   SER A 104       1.794  37.879  41.507  1.00 18.23           O  
ATOM    849  CB  SER A 104       4.478  38.627  39.910  1.00 16.19           C  
ATOM    850  OG  SER A 104       5.867  38.248  39.528  1.00 16.57           O  
ATOM    851  N   ARG A 105       2.347  39.945  42.004  1.00 17.41           N  
ATOM    852  CA  ARG A 105       1.028  40.421  42.299  1.00 18.48           C  
ATOM    853  C   ARG A 105       0.450  41.198  41.127  1.00 17.07           C  
ATOM    854  O   ARG A 105      -0.764  41.245  40.928  1.00 17.33           O  
ATOM    855  CB  ARG A 105       1.243  41.376  43.496  1.00 22.45           C  
ATOM    856  CG  ARG A 105      -0.022  41.601  44.321  1.00 27.88           C  
ATOM    857  CD  ARG A 105      -0.918  42.680  43.810  1.00 32.70           C  
ATOM    858  NE  ARG A 105      -1.974  42.993  44.802  1.00 35.93           N  
ATOM    859  CZ  ARG A 105      -3.156  42.338  44.851  1.00 36.71           C  
ATOM    860  NH1 ARG A 105      -3.278  41.108  44.435  1.00 36.46           N  
ATOM    861  NH2 ARG A 105      -4.230  43.001  45.275  1.00 36.79           N  
ATOM    862  N   GLY A 106       1.365  41.835  40.390  1.00 15.20           N  
ATOM    863  CA  GLY A 106       1.043  42.690  39.277  1.00 14.07           C  
ATOM    864  C   GLY A 106       1.705  42.298  37.990  1.00 14.51           C  
ATOM    865  O   GLY A 106       2.806  41.818  37.954  1.00 13.80           O  
ATOM    866  N   VAL A 107       0.980  42.559  36.884  1.00 16.30           N  
ATOM    867  CA  VAL A 107       1.453  42.490  35.447  1.00 15.47           C  
ATOM    868  C   VAL A 107       1.101  43.855  34.796  1.00 14.81           C  
ATOM    869  O   VAL A 107      -0.044  44.280  34.760  1.00 14.67           O  
ATOM    870  CB  VAL A 107       0.770  41.355  34.650  1.00 14.34           C  
ATOM    871  CG1 VAL A 107       1.038  41.407  33.139  1.00 12.87           C  
ATOM    872  CG2 VAL A 107       1.043  39.954  35.244  1.00 14.25           C  
ATOM    873  N   VAL A 108       2.151  44.535  34.341  1.00 13.34           N  
ATOM    874  CA  VAL A 108       2.018  45.759  33.621  1.00 13.01           C  
ATOM    875  C   VAL A 108       2.253  45.438  32.140  1.00 14.22           C  
ATOM    876  O   VAL A 108       3.330  45.023  31.720  1.00 15.47           O  
ATOM    877  CB  VAL A 108       3.055  46.740  34.162  1.00 11.54           C  
ATOM    878  CG1 VAL A 108       2.964  48.111  33.499  1.00  9.95           C  
ATOM    879  CG2 VAL A 108       2.857  46.999  35.666  1.00 11.51           C  
ATOM    880  N   MET A 109       1.210  45.724  31.346  1.00 14.43           N  
ATOM    881  CA  MET A 109       1.216  45.542  29.881  1.00 14.30           C  
ATOM    882  C   MET A 109       1.190  46.820  29.161  1.00 13.44           C  
ATOM    883  O   MET A 109       0.273  47.576  29.345  1.00 13.73           O  
ATOM    884  CB  MET A 109      -0.043  44.743  29.553  1.00 14.30           C  
ATOM    885  CG  MET A 109      -0.324  44.679  28.020  1.00 14.29           C  
ATOM    886  SD  MET A 109      -1.370  43.263  27.618  1.00 14.25           S  
ATOM    887  CE  MET A 109      -1.392  43.296  25.759  1.00 12.92           C  
ATOM    888  N   LEU A 110       2.222  47.095  28.392  1.00 12.10           N  
ATOM    889  CA  LEU A 110       2.275  48.460  27.840  1.00 10.00           C  
ATOM    890  C   LEU A 110       1.899  48.594  26.384  1.00 11.67           C  
ATOM    891  O   LEU A 110       2.157  49.650  25.844  1.00 11.78           O  
ATOM    892  CB  LEU A 110       3.706  49.009  28.015  1.00 10.33           C  
ATOM    893  CG  LEU A 110       4.068  49.098  29.521  1.00 11.53           C  
ATOM    894  CD1 LEU A 110       5.549  49.489  29.657  1.00  9.74           C  
ATOM    895  CD2 LEU A 110       3.074  50.062  30.326  1.00 10.69           C  
ATOM    896  N   ASN A 111       1.417  47.472  25.760  1.00 11.93           N  
ATOM    897  CA  ASN A 111       1.177  47.420  24.332  1.00 14.88           C  
ATOM    898  C   ASN A 111      -0.248  46.883  24.121  1.00 16.23           C  
ATOM    899  O   ASN A 111      -0.762  46.325  25.067  1.00 14.25           O  
ATOM    900  CB  ASN A 111       2.100  46.384  23.624  1.00 15.33           C  
ATOM    901  CG  ASN A 111       1.887  44.965  24.120  1.00 15.63           C  
ATOM    902  OD1 ASN A 111       1.373  44.112  23.429  1.00 18.72           O  
ATOM    903  ND2 ASN A 111       2.387  44.658  25.313  1.00 10.97           N  
ATOM    904  N   ARG A 112      -0.723  46.945  22.864  1.00 17.12           N  
ATOM    905  CA  ARG A 112      -1.914  46.223  22.461  1.00 19.15           C  
ATOM    906  C   ARG A 112      -1.580  44.894  21.831  1.00 17.59           C  
ATOM    907  O   ARG A 112      -0.486  44.721  21.351  1.00 17.89           O  
ATOM    908  CB  ARG A 112      -2.675  47.175  21.519  1.00 21.11           C  
ATOM    909  CG  ARG A 112      -3.000  48.465  22.273  1.00 26.61           C  
ATOM    910  CD  ARG A 112      -4.116  49.277  21.627  1.00 34.46           C  
ATOM    911  NE  ARG A 112      -4.102  49.097  20.181  1.00 42.15           N  
ATOM    912  CZ  ARG A 112      -3.663  50.039  19.336  1.00 47.94           C  
ATOM    913  NH1 ARG A 112      -3.717  51.279  19.695  1.00 50.21           N  
ATOM    914  NH2 ARG A 112      -3.139  49.660  18.160  1.00 51.55           N  
ATOM    915  N   VAL A 113      -2.510  43.953  21.784  1.00 18.50           N  
ATOM    916  CA  VAL A 113      -2.375  42.705  20.995  1.00 19.02           C  
ATOM    917  C   VAL A 113      -2.163  43.009  19.509  1.00 19.97           C  
ATOM    918  O   VAL A 113      -1.230  42.540  18.881  1.00 18.43           O  
ATOM    919  CB  VAL A 113      -3.578  41.754  21.282  1.00 19.40           C  
ATOM    920  CG1 VAL A 113      -3.764  40.468  20.389  1.00 19.21           C  
ATOM    921  CG2 VAL A 113      -3.527  41.265  22.743  1.00 19.58           C  
ATOM    922  N   MET A 114      -3.009  43.866  18.948  1.00 21.44           N  
ATOM    923  CA  MET A 114      -2.696  44.397  17.621  1.00 24.28           C  
ATOM    924  C   MET A 114      -2.218  45.863  17.563  1.00 24.97           C  
ATOM    925  O   MET A 114      -2.868  46.781  18.024  1.00 24.79           O  
ATOM    926  CB  MET A 114      -3.875  44.248  16.650  1.00 26.65           C  
ATOM    927  CG  MET A 114      -3.343  44.546  15.184  1.00 32.79           C  
ATOM    928  SD  MET A 114      -4.251  43.661  13.917  1.00 36.97           S  
ATOM    929  CE  MET A 114      -4.848  45.171  13.166  1.00 36.58           C  
ATOM    930  N   GLU A 115      -1.090  46.019  16.860  1.00 25.87           N  
ATOM    931  CA  GLU A 115      -0.458  47.337  16.696  1.00 26.26           C  
ATOM    932  C   GLU A 115       0.199  47.323  15.345  1.00 26.55           C  
ATOM    933  O   GLU A 115       0.763  46.303  14.937  1.00 27.06           O  
ATOM    934  CB  GLU A 115       0.735  47.584  17.658  1.00 24.81           C  
ATOM    935  CG  GLU A 115       0.337  47.539  19.142  1.00 26.48           C  
ATOM    936  CD  GLU A 115       1.478  47.755  20.155  1.00 24.38           C  
ATOM    937  OE1 GLU A 115       2.595  47.315  19.936  1.00 21.80           O  
ATOM    938  OE2 GLU A 115       1.234  48.346  21.200  1.00 20.70           O  
ATOM    939  N   LYS A 116       0.075  48.462  14.660  1.00 27.85           N  
ATOM    940  CA  LYS A 116       0.602  48.729  13.308  1.00 27.89           C  
ATOM    941  C   LYS A 116       0.344  47.519  12.380  1.00 26.53           C  
ATOM    942  O   LYS A 116       1.201  46.967  11.681  1.00 25.50           O  
ATOM    943  CB  LYS A 116       2.094  48.963  13.493  1.00 29.61           C  
ATOM    944  CG  LYS A 116       2.338  50.311  14.144  1.00 31.34           C  
ATOM    945  CD  LYS A 116       3.831  50.460  14.408  1.00 35.76           C  
ATOM    946  CE  LYS A 116       4.229  51.903  14.760  1.00 39.47           C  
ATOM    947  NZ  LYS A 116       3.065  52.516  15.431  1.00 42.18           N  
ATOM    948  N   GLY A 117      -0.913  47.076  12.544  1.00 25.25           N  
ATOM    949  CA  GLY A 117      -1.358  46.014  11.623  1.00 25.58           C  
ATOM    950  C   GLY A 117      -0.954  44.576  11.891  1.00 25.32           C  
ATOM    951  O   GLY A 117      -1.367  43.770  11.052  1.00 25.78           O  
ATOM    952  N   SER A 118      -0.211  44.333  13.026  1.00 23.39           N  
ATOM    953  CA  SER A 118       0.442  43.050  13.417  1.00 24.38           C  
ATOM    954  C   SER A 118       0.121  42.626  14.795  1.00 22.38           C  
ATOM    955  O   SER A 118      -0.175  43.462  15.630  1.00 23.50           O  
ATOM    956  CB  SER A 118       1.964  43.171  13.503  1.00 25.64           C  
ATOM    957  OG  SER A 118       2.103  43.927  12.236  1.00 34.57           O  
ATOM    958  N   LEU A 119       0.169  41.321  14.990  1.00 21.31           N  
ATOM    959  CA  LEU A 119      -0.144  40.702  16.293  1.00 20.49           C  
ATOM    960  C   LEU A 119       1.133  40.698  17.155  1.00 20.06           C  
ATOM    961  O   LEU A 119       1.993  39.875  17.064  1.00 19.83           O  
ATOM    962  CB  LEU A 119      -0.830  39.343  16.097  1.00 18.90           C  
ATOM    963  CG  LEU A 119      -2.139  39.484  15.263  1.00 18.65           C  
ATOM    964  CD1 LEU A 119      -2.598  38.169  14.804  1.00 17.51           C  
ATOM    965  CD2 LEU A 119      -3.219  40.075  16.159  1.00 17.83           C  
ATOM    966  N   LYS A 120       1.171  41.771  17.957  1.00 19.15           N  
ATOM    967  CA  LYS A 120       2.364  42.084  18.717  1.00 18.50           C  
ATOM    968  C   LYS A 120       2.503  41.191  20.017  1.00 15.93           C  
ATOM    969  O   LYS A 120       3.474  41.266  20.751  1.00 14.76           O  
ATOM    970  CB  LYS A 120       2.345  43.659  18.924  1.00 18.09           C  
ATOM    971  CG  LYS A 120       2.864  44.528  17.660  1.00 20.24           C  
ATOM    972  CD  LYS A 120       4.315  44.218  17.261  1.00 19.52           C  
ATOM    973  CE  LYS A 120       5.283  45.057  16.419  1.00 21.45           C  
ATOM    974  NZ  LYS A 120       6.421  44.169  15.984  1.00 27.90           N  
ATOM    975  N   CYS A 121       1.474  40.416  20.316  1.00 15.15           N  
ATOM    976  CA  CYS A 121       1.436  39.679  21.592  1.00 17.19           C  
ATOM    977  C   CYS A 121       0.226  38.676  21.515  1.00 19.13           C  
ATOM    978  O   CYS A 121      -0.798  39.073  20.947  1.00 21.85           O  
ATOM    979  CB  CYS A 121       1.278  40.693  22.805  1.00 18.14           C  
ATOM    980  SG  CYS A 121       0.990  40.161  24.514  1.00 13.92           S  
ATOM    981  N   ALA A 122       0.309  37.460  22.136  1.00 18.26           N  
ATOM    982  CA  ALA A 122      -0.861  36.594  22.342  1.00 15.76           C  
ATOM    983  C   ALA A 122      -1.963  37.246  23.234  1.00 16.81           C  
ATOM    984  O   ALA A 122      -1.728  38.068  24.114  1.00 15.96           O  
ATOM    985  CB  ALA A 122      -0.390  35.231  22.931  1.00 13.04           C  
ATOM    986  N   GLN A 123      -3.223  36.839  23.020  1.00 17.09           N  
ATOM    987  CA  GLN A 123      -4.283  37.186  23.966  1.00 18.13           C  
ATOM    988  C   GLN A 123      -4.116  36.221  25.131  1.00 17.76           C  
ATOM    989  O   GLN A 123      -4.690  35.139  25.176  1.00 18.87           O  
ATOM    990  CB  GLN A 123      -5.664  36.964  23.249  1.00 20.77           C  
ATOM    991  CG  GLN A 123      -6.895  37.441  24.106  1.00 20.46           C  
ATOM    992  CD  GLN A 123      -6.777  38.910  24.549  1.00 20.70           C  
ATOM    993  OE1 GLN A 123      -6.840  39.142  25.740  1.00 21.95           O  
ATOM    994  NE2 GLN A 123      -6.660  39.884  23.671  1.00 18.13           N  
ATOM    995  N   TYR A 124      -3.247  36.612  26.065  1.00 16.85           N  
ATOM    996  CA  TYR A 124      -2.951  35.644  27.151  1.00 15.83           C  
ATOM    997  C   TYR A 124      -3.863  35.690  28.432  1.00 14.93           C  
ATOM    998  O   TYR A 124      -3.594  34.949  29.387  1.00 16.10           O  
ATOM    999  CB  TYR A 124      -1.423  35.810  27.589  1.00 15.02           C  
ATOM   1000  CG  TYR A 124      -1.057  37.148  28.184  1.00 14.36           C  
ATOM   1001  CD1 TYR A 124      -0.693  38.243  27.398  1.00 15.59           C  
ATOM   1002  CD2 TYR A 124      -1.107  37.304  29.544  1.00 15.61           C  
ATOM   1003  CE1 TYR A 124      -0.371  39.469  27.972  1.00 15.51           C  
ATOM   1004  CE2 TYR A 124      -0.778  38.501  30.159  1.00 14.91           C  
ATOM   1005  CZ  TYR A 124      -0.418  39.583  29.376  1.00 16.55           C  
ATOM   1006  OH  TYR A 124      -0.146  40.747  30.018  1.00 14.68           O  
ATOM   1007  N   TRP A 125      -4.845  36.615  28.472  1.00 14.19           N  
ATOM   1008  CA  TRP A 125      -5.699  36.714  29.655  1.00 14.71           C  
ATOM   1009  C   TRP A 125      -7.148  36.660  29.092  1.00 15.75           C  
ATOM   1010  O   TRP A 125      -7.327  36.994  27.939  1.00 14.68           O  
ATOM   1011  CB  TRP A 125      -5.258  37.927  30.536  1.00 14.01           C  
ATOM   1012  CG  TRP A 125      -5.713  39.149  29.866  1.00 16.36           C  
ATOM   1013  CD1 TRP A 125      -6.950  39.757  30.085  1.00 17.63           C  
ATOM   1014  CD2 TRP A 125      -5.087  39.878  28.787  1.00 17.57           C  
ATOM   1015  NE1 TRP A 125      -7.117  40.795  29.188  1.00 17.30           N  
ATOM   1016  CE2 TRP A 125      -5.992  40.922  28.396  1.00 17.82           C  
ATOM   1017  CE3 TRP A 125      -3.889  39.734  28.139  1.00 16.97           C  
ATOM   1018  CZ2 TRP A 125      -5.693  41.805  27.380  1.00 17.93           C  
ATOM   1019  CZ3 TRP A 125      -3.584  40.620  27.097  1.00 18.62           C  
ATOM   1020  CH2 TRP A 125      -4.478  41.672  26.720  1.00 18.79           C  
ATOM   1021  N   PRO A 126      -8.180  36.152  29.923  1.00 18.51           N  
ATOM   1022  CA  PRO A 126      -9.619  36.143  29.502  1.00 17.95           C  
ATOM   1023  C   PRO A 126     -10.185  37.574  29.409  1.00 19.02           C  
ATOM   1024  O   PRO A 126     -10.062  38.421  30.270  1.00 20.67           O  
ATOM   1025  CB  PRO A 126     -10.306  35.173  30.474  1.00 14.22           C  
ATOM   1026  CG  PRO A 126      -9.430  35.306  31.709  1.00 16.74           C  
ATOM   1027  CD  PRO A 126      -8.017  35.513  31.263  1.00 16.48           C  
ATOM   1028  N   GLN A 127     -10.814  37.830  28.303  1.00 21.03           N  
ATOM   1029  CA  GLN A 127     -11.584  39.034  28.164  1.00 23.39           C  
ATOM   1030  C   GLN A 127     -13.024  38.839  28.727  1.00 23.07           C  
ATOM   1031  O   GLN A 127     -13.789  39.752  28.788  1.00 22.46           O  
ATOM   1032  CB  GLN A 127     -11.626  39.262  26.642  1.00 26.64           C  
ATOM   1033  CG  GLN A 127     -10.186  39.397  26.087  1.00 30.57           C  
ATOM   1034  CD  GLN A 127     -10.263  39.522  24.590  1.00 31.67           C  
ATOM   1035  OE1 GLN A 127     -10.475  38.582  23.837  1.00 31.45           O  
ATOM   1036  NE2 GLN A 127     -10.131  40.723  24.203  1.00 32.32           N  
ATOM   1037  N   LYS A 128     -13.456  37.644  29.149  1.00 23.30           N  
ATOM   1038  CA  LYS A 128     -14.691  37.670  29.949  1.00 22.09           C  
ATOM   1039  C   LYS A 128     -14.863  36.635  30.967  1.00 20.02           C  
ATOM   1040  O   LYS A 128     -14.342  35.555  30.853  1.00 20.13           O  
ATOM   1041  CB  LYS A 128     -15.886  37.668  29.128  1.00 26.13           C  
ATOM   1042  CG  LYS A 128     -15.877  36.917  27.865  1.00 30.02           C  
ATOM   1043  CD  LYS A 128     -16.775  37.826  27.031  1.00 36.81           C  
ATOM   1044  CE  LYS A 128     -18.248  37.793  27.548  1.00 43.23           C  
ATOM   1045  NZ  LYS A 128     -19.196  37.964  26.440  1.00 47.04           N  
ATOM   1046  N   GLU A 129     -15.565  37.049  32.005  1.00 19.32           N  
ATOM   1047  CA  GLU A 129     -15.662  36.357  33.243  1.00 18.75           C  
ATOM   1048  C   GLU A 129     -16.093  34.900  33.039  1.00 20.50           C  
ATOM   1049  O   GLU A 129     -15.434  34.045  33.585  1.00 20.76           O  
ATOM   1050  CB  GLU A 129     -16.673  37.093  34.134  1.00 19.21           C  
ATOM   1051  CG  GLU A 129     -16.262  38.416  34.794  1.00 17.81           C  
ATOM   1052  CD  GLU A 129     -16.635  39.583  33.895  1.00 21.94           C  
ATOM   1053  OE1 GLU A 129     -16.770  39.362  32.682  1.00 22.45           O  
ATOM   1054  OE2 GLU A 129     -16.753  40.724  34.347  1.00 21.03           O  
ATOM   1055  N   GLU A 130     -17.142  34.589  32.230  1.00 22.46           N  
ATOM   1056  CA  GLU A 130     -17.684  33.198  31.909  1.00 23.67           C  
ATOM   1057  C   GLU A 130     -16.725  32.177  31.119  1.00 24.35           C  
ATOM   1058  O   GLU A 130     -16.941  30.961  31.029  1.00 24.86           O  
ATOM   1059  CB  GLU A 130     -18.882  33.213  30.917  1.00 22.38           C  
ATOM   1060  CG  GLU A 130     -19.786  34.337  31.013  1.00 24.17           C  
ATOM   1061  CD  GLU A 130     -19.436  35.584  30.311  1.00 24.22           C  
ATOM   1062  OE1 GLU A 130     -18.733  36.377  30.871  1.00 25.14           O  
ATOM   1063  OE2 GLU A 130     -19.954  35.875  29.267  1.00 27.15           O  
ATOM   1064  N   LYS A 131     -15.677  32.766  30.504  1.00 25.32           N  
ATOM   1065  CA  LYS A 131     -14.679  32.061  29.693  1.00 25.82           C  
ATOM   1066  C   LYS A 131     -13.217  32.189  30.323  1.00 25.15           C  
ATOM   1067  O   LYS A 131     -12.336  32.900  29.815  1.00 22.36           O  
ATOM   1068  CB  LYS A 131     -14.820  32.735  28.321  1.00 28.53           C  
ATOM   1069  CG  LYS A 131     -15.783  32.027  27.377  1.00 32.98           C  
ATOM   1070  CD  LYS A 131     -15.172  30.634  26.865  1.00 41.04           C  
ATOM   1071  CE  LYS A 131     -13.640  30.068  27.107  1.00 44.86           C  
ATOM   1072  NZ  LYS A 131     -13.111  29.327  28.323  1.00 45.80           N  
ATOM   1073  N   GLU A 132     -13.032  31.430  31.434  1.00 25.49           N  
ATOM   1074  CA  GLU A 132     -11.668  31.182  32.020  1.00 25.87           C  
ATOM   1075  C   GLU A 132     -10.697  30.627  30.950  1.00 24.11           C  
ATOM   1076  O   GLU A 132     -11.137  30.066  29.965  1.00 24.22           O  
ATOM   1077  CB  GLU A 132     -11.543  30.051  33.105  1.00 27.47           C  
ATOM   1078  CG  GLU A 132     -12.754  29.748  33.934  1.00 31.90           C  
ATOM   1079  CD  GLU A 132     -13.769  28.990  33.038  1.00 31.56           C  
ATOM   1080  OE1 GLU A 132     -13.474  27.885  32.625  1.00 33.58           O  
ATOM   1081  OE2 GLU A 132     -14.815  29.524  32.683  1.00 30.25           O  
ATOM   1082  N   MET A 133      -9.409  30.785  31.231  1.00 22.67           N  
ATOM   1083  CA  MET A 133      -8.416  30.074  30.431  1.00 21.71           C  
ATOM   1084  C   MET A 133      -7.826  28.911  31.184  1.00 22.23           C  
ATOM   1085  O   MET A 133      -7.335  29.119  32.289  1.00 22.26           O  
ATOM   1086  CB  MET A 133      -7.311  31.103  30.048  1.00 21.75           C  
ATOM   1087  CG  MET A 133      -7.844  31.963  28.926  1.00 22.37           C  
ATOM   1088  SD  MET A 133      -6.784  33.278  28.459  1.00 23.06           S  
ATOM   1089  CE  MET A 133      -5.617  32.292  27.505  1.00 20.29           C  
ATOM   1090  N   ILE A 134      -7.763  27.702  30.622  1.00 23.61           N  
ATOM   1091  CA  ILE A 134      -6.891  26.691  31.296  1.00 25.47           C  
ATOM   1092  C   ILE A 134      -5.644  26.458  30.497  1.00 25.84           C  
ATOM   1093  O   ILE A 134      -5.677  26.190  29.339  1.00 27.31           O  
ATOM   1094  CB  ILE A 134      -7.532  25.316  31.598  1.00 26.87           C  
ATOM   1095  CG1 ILE A 134      -8.509  25.400  32.798  1.00 27.40           C  
ATOM   1096  CG2 ILE A 134      -6.449  24.360  32.073  1.00 25.68           C  
ATOM   1097  CD1 ILE A 134      -9.949  25.708  32.353  1.00 31.37           C  
ATOM   1098  N   PHE A 135      -4.515  26.522  31.163  1.00 26.37           N  
ATOM   1099  CA  PHE A 135      -3.260  26.364  30.442  1.00 26.19           C  
ATOM   1100  C   PHE A 135      -2.751  24.959  30.784  1.00 27.07           C  
ATOM   1101  O   PHE A 135      -2.266  24.639  31.856  1.00 25.87           O  
ATOM   1102  CB  PHE A 135      -2.317  27.508  30.843  1.00 23.64           C  
ATOM   1103  CG  PHE A 135      -2.777  28.890  30.578  1.00 21.62           C  
ATOM   1104  CD1 PHE A 135      -2.720  29.363  29.287  1.00 21.00           C  
ATOM   1105  CD2 PHE A 135      -3.263  29.669  31.608  1.00 20.55           C  
ATOM   1106  CE1 PHE A 135      -3.183  30.635  29.004  1.00 20.85           C  
ATOM   1107  CE2 PHE A 135      -3.754  30.923  31.331  1.00 20.94           C  
ATOM   1108  CZ  PHE A 135      -3.724  31.410  30.033  1.00 20.56           C  
ATOM   1109  N   GLU A 136      -2.995  24.083  29.876  1.00 30.03           N  
ATOM   1110  CA  GLU A 136      -2.807  22.684  30.260  1.00 33.71           C  
ATOM   1111  C   GLU A 136      -1.305  22.305  30.367  1.00 32.09           C  
ATOM   1112  O   GLU A 136      -0.920  21.555  31.254  1.00 31.93           O  
ATOM   1113  CB  GLU A 136      -3.551  21.716  29.289  1.00 39.19           C  
ATOM   1114  CG  GLU A 136      -5.124  21.545  29.411  1.00 46.50           C  
ATOM   1115  CD  GLU A 136      -5.604  20.392  28.450  1.00 53.51           C  
ATOM   1116  OE1 GLU A 136      -4.912  20.107  27.438  1.00 57.26           O  
ATOM   1117  OE2 GLU A 136      -6.636  19.763  28.743  1.00 56.16           O  
ATOM   1118  N   ASP A 137      -0.452  22.832  29.506  1.00 30.23           N  
ATOM   1119  CA  ASP A 137       0.945  22.501  29.690  1.00 28.94           C  
ATOM   1120  C   ASP A 137       1.485  22.837  31.113  1.00 28.25           C  
ATOM   1121  O   ASP A 137       2.305  22.105  31.636  1.00 29.74           O  
ATOM   1122  CB  ASP A 137       1.727  23.153  28.555  1.00 29.45           C  
ATOM   1123  CG  ASP A 137       1.848  24.660  28.726  1.00 31.99           C  
ATOM   1124  OD1 ASP A 137       0.944  25.255  29.287  1.00 31.59           O  
ATOM   1125  OD2 ASP A 137       2.894  25.189  28.393  1.00 33.27           O  
ATOM   1126  N   THR A 138       0.984  23.884  31.777  1.00 26.14           N  
ATOM   1127  CA  THR A 138       1.595  24.151  33.098  1.00 23.93           C  
ATOM   1128  C   THR A 138       0.560  24.028  34.184  1.00 24.23           C  
ATOM   1129  O   THR A 138       0.806  24.374  35.321  1.00 23.60           O  
ATOM   1130  CB  THR A 138       2.167  25.616  33.067  1.00 22.06           C  
ATOM   1131  OG1 THR A 138       1.155  26.597  32.747  1.00 20.86           O  
ATOM   1132  CG2 THR A 138       3.422  25.805  32.146  1.00 22.29           C  
ATOM   1133  N   ASN A 139      -0.613  23.498  33.839  1.00 25.20           N  
ATOM   1134  CA  ASN A 139      -1.601  23.174  34.890  1.00 25.91           C  
ATOM   1135  C   ASN A 139      -2.115  24.356  35.711  1.00 24.94           C  
ATOM   1136  O   ASN A 139      -2.080  24.365  36.941  1.00 24.01           O  
ATOM   1137  CB  ASN A 139      -1.028  22.114  35.859  1.00 30.45           C  
ATOM   1138  CG  ASN A 139      -2.155  21.222  36.449  1.00 36.19           C  
ATOM   1139  OD1 ASN A 139      -3.025  20.753  35.716  1.00 39.30           O  
ATOM   1140  ND2 ASN A 139      -2.156  21.003  37.767  1.00 36.59           N  
ATOM   1141  N   LEU A 140      -2.600  25.354  34.992  1.00 25.24           N  
ATOM   1142  CA  LEU A 140      -2.897  26.657  35.684  1.00 25.08           C  
ATOM   1143  C   LEU A 140      -4.189  27.181  35.122  1.00 24.04           C  
ATOM   1144  O   LEU A 140      -4.436  26.978  33.947  1.00 24.05           O  
ATOM   1145  CB  LEU A 140      -1.868  27.750  35.369  1.00 24.93           C  
ATOM   1146  CG  LEU A 140      -0.766  28.145  36.390  1.00 24.67           C  
ATOM   1147  CD1 LEU A 140      -0.777  27.585  37.779  1.00 22.42           C  
ATOM   1148  CD2 LEU A 140       0.583  28.163  35.740  1.00 21.90           C  
ATOM   1149  N   LYS A 141      -4.996  27.812  35.961  1.00 23.03           N  
ATOM   1150  CA  LYS A 141      -6.281  28.371  35.460  1.00 22.50           C  
ATOM   1151  C   LYS A 141      -6.329  29.851  35.809  1.00 19.75           C  
ATOM   1152  O   LYS A 141      -5.748  30.299  36.782  1.00 20.12           O  
ATOM   1153  CB  LYS A 141      -7.424  27.614  36.107  1.00 23.74           C  
ATOM   1154  CG  LYS A 141      -8.753  28.031  35.570  1.00 27.70           C  
ATOM   1155  CD  LYS A 141      -9.803  27.129  36.211  1.00 30.67           C  
ATOM   1156  CE  LYS A 141     -10.677  27.712  37.263  1.00 32.97           C  
ATOM   1157  NZ  LYS A 141     -11.510  26.677  37.944  1.00 36.95           N  
ATOM   1158  N   LEU A 142      -6.856  30.534  34.850  1.00 18.47           N  
ATOM   1159  CA  LEU A 142      -6.956  31.967  35.037  1.00 19.43           C  
ATOM   1160  C   LEU A 142      -8.383  32.473  34.668  1.00 19.66           C  
ATOM   1161  O   LEU A 142      -8.884  32.262  33.529  1.00 20.98           O  
ATOM   1162  CB  LEU A 142      -5.858  32.613  34.170  1.00 18.19           C  
ATOM   1163  CG  LEU A 142      -5.743  34.146  34.235  1.00 18.15           C  
ATOM   1164  CD1 LEU A 142      -5.162  34.702  35.549  1.00 18.84           C  
ATOM   1165  CD2 LEU A 142      -4.857  34.548  33.054  1.00 16.69           C  
ATOM   1166  N   THR A 143      -8.894  33.267  35.601  1.00 18.28           N  
ATOM   1167  CA  THR A 143     -10.202  33.884  35.317  1.00 19.61           C  
ATOM   1168  C   THR A 143     -10.184  35.346  35.482  1.00 18.96           C  
ATOM   1169  O   THR A 143      -9.592  35.803  36.431  1.00 19.75           O  
ATOM   1170  CB  THR A 143     -11.131  33.326  36.411  1.00 18.70           C  
ATOM   1171  OG1 THR A 143     -11.046  31.883  36.297  1.00 15.40           O  
ATOM   1172  CG2 THR A 143     -12.603  33.531  36.141  1.00 19.99           C  
ATOM   1173  N   LEU A 144     -10.880  36.075  34.615  1.00 19.08           N  
ATOM   1174  CA  LEU A 144     -11.211  37.508  34.784  1.00 18.75           C  
ATOM   1175  C   LEU A 144     -12.246  37.741  35.905  1.00 20.20           C  
ATOM   1176  O   LEU A 144     -13.384  37.261  35.869  1.00 19.98           O  
ATOM   1177  CB  LEU A 144     -11.819  38.029  33.479  1.00 18.97           C  
ATOM   1178  CG  LEU A 144     -12.168  39.492  33.545  1.00 16.93           C  
ATOM   1179  CD1 LEU A 144     -10.861  40.256  33.720  1.00 17.35           C  
ATOM   1180  CD2 LEU A 144     -12.912  39.900  32.276  1.00 14.40           C  
ATOM   1181  N   ILE A 145     -11.748  38.428  36.948  1.00 20.96           N  
ATOM   1182  CA  ILE A 145     -12.624  38.703  38.097  1.00 20.24           C  
ATOM   1183  C   ILE A 145     -13.364  39.998  37.875  1.00 21.16           C  
ATOM   1184  O   ILE A 145     -14.509  40.096  38.216  1.00 20.37           O  
ATOM   1185  CB  ILE A 145     -11.915  38.686  39.428  1.00 19.92           C  
ATOM   1186  CG1 ILE A 145     -11.317  37.270  39.641  1.00 18.61           C  
ATOM   1187  CG2 ILE A 145     -12.845  39.143  40.578  1.00 17.56           C  
ATOM   1188  CD1 ILE A 145     -12.278  36.076  39.470  1.00 16.79           C  
ATOM   1189  N   SER A 146     -12.671  40.951  37.277  1.00 21.10           N  
ATOM   1190  CA  SER A 146     -13.413  42.082  36.839  1.00 21.69           C  
ATOM   1191  C   SER A 146     -12.437  43.003  36.232  1.00 21.93           C  
ATOM   1192  O   SER A 146     -11.260  42.744  36.258  1.00 21.67           O  
ATOM   1193  CB  SER A 146     -13.931  42.841  38.023  1.00 23.69           C  
ATOM   1194  OG  SER A 146     -12.848  43.429  38.840  1.00 27.48           O  
ATOM   1195  N   GLU A 147     -12.921  44.092  35.729  1.00 23.34           N  
ATOM   1196  CA  GLU A 147     -12.088  45.107  35.118  1.00 25.24           C  
ATOM   1197  C   GLU A 147     -12.646  46.535  35.118  1.00 24.76           C  
ATOM   1198  O   GLU A 147     -13.835  46.749  35.100  1.00 27.11           O  
ATOM   1199  CB  GLU A 147     -11.813  44.665  33.728  1.00 27.26           C  
ATOM   1200  CG  GLU A 147     -13.016  44.539  32.907  1.00 29.98           C  
ATOM   1201  CD  GLU A 147     -12.545  44.477  31.468  1.00 37.59           C  
ATOM   1202  OE1 GLU A 147     -11.376  44.224  31.132  1.00 39.37           O  
ATOM   1203  OE2 GLU A 147     -13.408  44.703  30.661  1.00 42.31           O  
ATOM   1204  N   ASP A 148     -11.744  47.509  35.158  1.00 24.11           N  
ATOM   1205  CA  ASP A 148     -12.064  48.913  35.233  1.00 23.81           C  
ATOM   1206  C   ASP A 148     -11.429  49.594  34.055  1.00 23.70           C  
ATOM   1207  O   ASP A 148     -10.226  49.765  34.010  1.00 23.96           O  
ATOM   1208  CB  ASP A 148     -11.526  49.250  36.604  1.00 25.68           C  
ATOM   1209  CG  ASP A 148     -11.473  50.717  36.959  1.00 29.82           C  
ATOM   1210  OD1 ASP A 148     -12.394  51.451  36.503  1.00 26.36           O  
ATOM   1211  OD2 ASP A 148     -10.474  51.077  37.693  1.00 32.27           O  
ATOM   1212  N   ILE A 149     -12.244  49.896  33.056  1.00 23.08           N  
ATOM   1213  CA  ILE A 149     -11.773  50.444  31.772  1.00 25.07           C  
ATOM   1214  C   ILE A 149     -11.790  51.991  31.753  1.00 27.35           C  
ATOM   1215  O   ILE A 149     -12.843  52.598  31.924  1.00 30.32           O  
ATOM   1216  CB  ILE A 149     -12.770  50.005  30.729  1.00 24.91           C  
ATOM   1217  CG1 ILE A 149     -12.907  48.497  30.801  1.00 24.15           C  
ATOM   1218  CG2 ILE A 149     -12.543  50.612  29.310  1.00 26.58           C  
ATOM   1219  CD1 ILE A 149     -13.566  47.937  29.570  1.00 27.07           C  
ATOM   1220  N   LYS A 150     -10.635  52.639  31.602  1.00 26.82           N  
ATOM   1221  CA  LYS A 150     -10.564  54.074  31.604  1.00 25.00           C  
ATOM   1222  C   LYS A 150     -10.329  54.361  30.142  1.00 24.43           C  
ATOM   1223  O   LYS A 150     -10.489  53.483  29.315  1.00 23.73           O  
ATOM   1224  CB  LYS A 150      -9.482  54.377  32.624  1.00 25.80           C  
ATOM   1225  CG  LYS A 150      -9.831  53.826  34.042  1.00 27.30           C  
ATOM   1226  CD  LYS A 150     -10.497  54.992  34.677  1.00 31.43           C  
ATOM   1227  CE  LYS A 150     -10.826  54.855  36.130  1.00 36.64           C  
ATOM   1228  NZ  LYS A 150     -11.398  56.189  36.465  1.00 40.37           N  
ATOM   1229  N   THR A 151     -10.025  55.587  29.797  1.00 24.13           N  
ATOM   1230  CA  THR A 151     -10.000  55.888  28.350  1.00 25.23           C  
ATOM   1231  C   THR A 151      -8.685  55.543  27.757  1.00 25.23           C  
ATOM   1232  O   THR A 151      -8.657  55.425  26.544  1.00 30.20           O  
ATOM   1233  CB  THR A 151      -9.704  57.416  28.375  1.00 25.91           C  
ATOM   1234  OG1 THR A 151      -8.731  57.821  29.363  1.00 28.13           O  
ATOM   1235  CG2 THR A 151     -10.983  58.108  28.793  1.00 30.45           C  
ATOM   1236  N   TYR A 152      -7.616  55.547  28.566  1.00 21.84           N  
ATOM   1237  CA  TYR A 152      -6.327  55.197  27.919  1.00 20.81           C  
ATOM   1238  C   TYR A 152      -5.675  53.878  28.566  1.00 21.05           C  
ATOM   1239  O   TYR A 152      -4.533  53.526  28.238  1.00 21.83           O  
ATOM   1240  CB  TYR A 152      -5.451  56.446  27.965  1.00 18.19           C  
ATOM   1241  CG  TYR A 152      -4.804  56.796  29.289  1.00 19.20           C  
ATOM   1242  CD1 TYR A 152      -3.631  56.232  29.718  1.00 19.33           C  
ATOM   1243  CD2 TYR A 152      -5.351  57.817  30.078  1.00 18.65           C  
ATOM   1244  CE1 TYR A 152      -3.027  56.688  30.857  1.00 21.71           C  
ATOM   1245  CE2 TYR A 152      -4.864  58.136  31.332  1.00 20.19           C  
ATOM   1246  CZ  TYR A 152      -3.649  57.612  31.702  1.00 21.37           C  
ATOM   1247  OH  TYR A 152      -3.031  58.039  32.845  1.00 19.61           O  
ATOM   1248  N   TYR A 153      -6.340  53.354  29.647  1.00 19.35           N  
ATOM   1249  CA  TYR A 153      -5.836  52.140  30.303  1.00 18.74           C  
ATOM   1250  C   TYR A 153      -7.017  51.415  30.880  1.00 18.79           C  
ATOM   1251  O   TYR A 153      -8.034  51.986  31.209  1.00 20.65           O  
ATOM   1252  CB  TYR A 153      -4.723  52.383  31.357  1.00 17.61           C  
ATOM   1253  CG  TYR A 153      -5.106  53.066  32.657  1.00 19.80           C  
ATOM   1254  CD1 TYR A 153      -5.206  54.440  32.702  1.00 20.52           C  
ATOM   1255  CD2 TYR A 153      -5.395  52.343  33.822  1.00 19.47           C  
ATOM   1256  CE1 TYR A 153      -5.711  55.119  33.800  1.00 19.87           C  
ATOM   1257  CE2 TYR A 153      -5.910  53.015  34.921  1.00 19.19           C  
ATOM   1258  CZ  TYR A 153      -6.105  54.389  34.934  1.00 21.59           C  
ATOM   1259  OH  TYR A 153      -6.722  54.863  36.098  1.00 24.75           O  
ATOM   1260  N   THR A 154      -6.787  50.164  31.194  1.00 18.00           N  
ATOM   1261  CA  THR A 154      -7.806  49.319  31.867  1.00 18.65           C  
ATOM   1262  C   THR A 154      -7.060  48.630  33.027  1.00 18.29           C  
ATOM   1263  O   THR A 154      -5.916  48.209  32.808  1.00 17.24           O  
ATOM   1264  CB  THR A 154      -8.322  48.136  30.919  1.00 18.24           C  
ATOM   1265  OG1 THR A 154      -8.990  48.892  29.859  1.00 18.17           O  
ATOM   1266  CG2 THR A 154      -9.329  47.146  31.541  1.00 16.76           C  
ATOM   1267  N   VAL A 155      -7.693  48.486  34.220  1.00 16.27           N  
ATOM   1268  CA  VAL A 155      -7.192  47.637  35.284  1.00 17.56           C  
ATOM   1269  C   VAL A 155      -8.108  46.411  35.375  1.00 19.27           C  
ATOM   1270  O   VAL A 155      -9.316  46.557  35.504  1.00 18.69           O  
ATOM   1271  CB  VAL A 155      -7.143  48.314  36.683  1.00 17.97           C  
ATOM   1272  CG1 VAL A 155      -6.632  47.319  37.784  1.00 15.21           C  
ATOM   1273  CG2 VAL A 155      -6.259  49.550  36.543  1.00 17.01           C  
ATOM   1274  N   ARG A 156      -7.480  45.201  35.361  1.00 18.89           N  
ATOM   1275  CA  ARG A 156      -8.205  43.943  35.540  1.00 18.01           C  
ATOM   1276  C   ARG A 156      -7.708  43.320  36.803  1.00 18.66           C  
ATOM   1277  O   ARG A 156      -6.562  43.404  37.197  1.00 16.46           O  
ATOM   1278  CB  ARG A 156      -8.092  42.949  34.365  1.00 17.79           C  
ATOM   1279  CG  ARG A 156      -8.255  43.679  33.035  1.00 19.61           C  
ATOM   1280  CD  ARG A 156      -8.514  42.801  31.770  1.00 22.91           C  
ATOM   1281  NE  ARG A 156      -8.780  43.640  30.513  1.00 25.43           N  
ATOM   1282  CZ  ARG A 156      -7.895  44.329  29.784  1.00 23.86           C  
ATOM   1283  NH1 ARG A 156      -6.630  44.280  30.134  1.00 25.52           N  
ATOM   1284  NH2 ARG A 156      -8.237  45.058  28.767  1.00 26.95           N  
ATOM   1285  N   GLN A 157      -8.660  42.675  37.404  1.00 20.00           N  
ATOM   1286  CA  GLN A 157      -8.344  41.713  38.441  1.00 21.50           C  
ATOM   1287  C   GLN A 157      -8.611  40.294  37.929  1.00 20.70           C  
ATOM   1288  O   GLN A 157      -9.668  39.943  37.425  1.00 21.33           O  
ATOM   1289  CB  GLN A 157      -9.318  42.049  39.530  1.00 25.80           C  
ATOM   1290  CG  GLN A 157      -9.109  41.209  40.761  1.00 33.83           C  
ATOM   1291  CD  GLN A 157     -10.269  41.502  41.713  1.00 39.60           C  
ATOM   1292  OE1 GLN A 157     -11.181  42.316  41.468  1.00 41.84           O  
ATOM   1293  NE2 GLN A 157     -10.224  40.661  42.753  1.00 40.10           N  
ATOM   1294  N   LEU A 158      -7.587  39.485  38.081  1.00 20.48           N  
ATOM   1295  CA  LEU A 158      -7.509  38.117  37.612  1.00 20.01           C  
ATOM   1296  C   LEU A 158      -7.408  37.177  38.848  1.00 19.56           C  
ATOM   1297  O   LEU A 158      -6.875  37.544  39.885  1.00 20.85           O  
ATOM   1298  CB  LEU A 158      -6.251  38.075  36.694  1.00 20.49           C  
ATOM   1299  CG  LEU A 158      -6.358  38.394  35.186  1.00 20.48           C  
ATOM   1300  CD1 LEU A 158      -7.498  39.252  34.813  1.00 20.34           C  
ATOM   1301  CD2 LEU A 158      -5.055  39.027  34.709  1.00 19.31           C  
ATOM   1302  N   GLU A 159      -7.947  35.985  38.700  1.00 18.41           N  
ATOM   1303  CA  GLU A 159      -7.700  34.951  39.661  1.00 20.45           C  
ATOM   1304  C   GLU A 159      -6.806  33.925  38.981  1.00 20.22           C  
ATOM   1305  O   GLU A 159      -7.132  33.460  37.936  1.00 20.09           O  
ATOM   1306  CB  GLU A 159      -9.033  34.376  40.148  1.00 21.80           C  
ATOM   1307  CG  GLU A 159      -8.667  33.283  41.145  1.00 27.75           C  
ATOM   1308  CD  GLU A 159      -9.847  32.768  41.994  1.00 30.89           C  
ATOM   1309  OE1 GLU A 159     -10.525  33.587  42.591  1.00 33.11           O  
ATOM   1310  OE2 GLU A 159     -10.035  31.575  42.142  1.00 30.25           O  
ATOM   1311  N   LEU A 160      -5.628  33.670  39.523  1.00 21.55           N  
ATOM   1312  CA  LEU A 160      -4.750  32.602  38.998  1.00 22.85           C  
ATOM   1313  C   LEU A 160      -4.882  31.371  39.984  1.00 23.90           C  
ATOM   1314  O   LEU A 160      -4.529  31.513  41.154  1.00 19.41           O  
ATOM   1315  CB  LEU A 160      -3.261  33.117  39.058  1.00 24.00           C  
ATOM   1316  CG  LEU A 160      -2.276  32.781  37.878  1.00 27.01           C  
ATOM   1317  CD1 LEU A 160      -0.779  33.015  38.238  1.00 25.78           C  
ATOM   1318  CD2 LEU A 160      -2.527  31.561  36.932  1.00 26.37           C  
ATOM   1319  N   GLU A 161      -5.353  30.216  39.458  1.00 25.46           N  
ATOM   1320  CA  GLU A 161      -5.350  28.943  40.186  1.00 27.28           C  
ATOM   1321  C   GLU A 161      -4.211  27.947  39.690  1.00 28.97           C  
ATOM   1322  O   GLU A 161      -4.046  27.482  38.545  1.00 27.35           O  
ATOM   1323  CB  GLU A 161      -6.721  28.255  40.140  1.00 26.79           C  
ATOM   1324  CG  GLU A 161      -6.771  27.118  41.143  1.00 28.31           C  
ATOM   1325  CD  GLU A 161      -8.114  26.478  41.258  1.00 31.61           C  
ATOM   1326  OE1 GLU A 161      -9.046  27.007  40.725  1.00 33.54           O  
ATOM   1327  OE2 GLU A 161      -8.262  25.415  41.875  1.00 34.01           O  
ATOM   1328  N   ASN A 162      -3.400  27.602  40.691  1.00 30.07           N  
ATOM   1329  CA  ASN A 162      -2.530  26.485  40.462  1.00 32.34           C  
ATOM   1330  C   ASN A 162      -3.388  25.198  40.589  1.00 33.51           C  
ATOM   1331  O   ASN A 162      -3.811  24.787  41.658  1.00 33.57           O  
ATOM   1332  CB  ASN A 162      -1.252  26.750  41.284  1.00 33.98           C  
ATOM   1333  CG  ASN A 162      -0.497  25.465  41.668  1.00 36.09           C  
ATOM   1334  OD1 ASN A 162      -1.016  24.370  41.537  1.00 37.80           O  
ATOM   1335  ND2 ASN A 162       0.717  25.577  42.126  1.00 36.85           N  
ATOM   1336  N   LEU A 163      -3.644  24.573  39.428  1.00 34.05           N  
ATOM   1337  CA  LEU A 163      -4.582  23.435  39.430  1.00 34.68           C  
ATOM   1338  C   LEU A 163      -4.045  22.171  40.224  1.00 36.98           C  
ATOM   1339  O   LEU A 163      -4.751  21.204  40.475  1.00 37.29           O  
ATOM   1340  CB  LEU A 163      -4.849  23.098  37.967  1.00 31.90           C  
ATOM   1341  CG  LEU A 163      -6.129  23.601  37.327  1.00 32.47           C  
ATOM   1342  CD1 LEU A 163      -6.727  24.848  37.992  1.00 32.57           C  
ATOM   1343  CD2 LEU A 163      -5.965  23.719  35.794  1.00 28.98           C  
ATOM   1344  N   THR A 164      -2.758  22.210  40.576  1.00 37.62           N  
ATOM   1345  CA  THR A 164      -2.120  21.067  41.194  1.00 38.95           C  
ATOM   1346  C   THR A 164      -2.269  21.094  42.711  1.00 41.73           C  
ATOM   1347  O   THR A 164      -2.296  20.067  43.377  1.00 43.94           O  
ATOM   1348  CB  THR A 164      -0.595  21.068  40.868  1.00 37.54           C  
ATOM   1349  OG1 THR A 164      -0.207  20.926  39.455  1.00 35.68           O  
ATOM   1350  CG2 THR A 164       0.220  20.274  41.924  1.00 36.12           C  
ATOM   1351  N   THR A 165      -2.351  22.305  43.242  1.00 42.47           N  
ATOM   1352  CA  THR A 165      -2.643  22.446  44.674  1.00 41.11           C  
ATOM   1353  C   THR A 165      -4.082  23.000  44.876  1.00 41.56           C  
ATOM   1354  O   THR A 165      -4.702  22.918  45.914  1.00 42.55           O  
ATOM   1355  CB  THR A 165      -1.618  23.498  45.092  1.00 39.61           C  
ATOM   1356  OG1 THR A 165      -1.867  24.774  44.475  1.00 40.86           O  
ATOM   1357  CG2 THR A 165      -0.192  23.032  44.768  1.00 37.19           C  
ATOM   1358  N   GLN A 166      -4.618  23.612  43.862  1.00 41.36           N  
ATOM   1359  CA  GLN A 166      -5.790  24.454  44.105  1.00 41.79           C  
ATOM   1360  C   GLN A 166      -5.504  25.748  44.908  1.00 39.60           C  
ATOM   1361  O   GLN A 166      -6.425  26.452  45.291  1.00 38.84           O  
ATOM   1362  CB  GLN A 166      -6.950  23.675  44.750  1.00 45.24           C  
ATOM   1363  CG  GLN A 166      -7.120  22.277  44.119  1.00 50.80           C  
ATOM   1364  CD  GLN A 166      -8.613  22.007  43.785  1.00 54.34           C  
ATOM   1365  OE1 GLN A 166      -9.174  20.957  44.013  1.00 55.42           O  
ATOM   1366  NE2 GLN A 166      -9.277  22.997  43.224  1.00 57.30           N  
ATOM   1367  N   GLU A 167      -4.216  26.068  45.152  1.00 37.93           N  
ATOM   1368  CA  GLU A 167      -3.962  27.428  45.593  1.00 36.88           C  
ATOM   1369  C   GLU A 167      -4.347  28.482  44.510  1.00 34.09           C  
ATOM   1370  O   GLU A 167      -4.269  28.237  43.330  1.00 33.10           O  
ATOM   1371  CB  GLU A 167      -2.531  27.555  46.085  1.00 40.79           C  
ATOM   1372  CG  GLU A 167      -2.271  28.927  46.779  1.00 49.13           C  
ATOM   1373  CD  GLU A 167      -0.812  29.168  47.287  1.00 54.44           C  
ATOM   1374  OE1 GLU A 167      -0.183  28.194  47.747  1.00 56.45           O  
ATOM   1375  OE2 GLU A 167      -0.316  30.319  47.196  1.00 56.84           O  
ATOM   1376  N   THR A 168      -4.774  29.654  44.958  1.00 31.59           N  
ATOM   1377  CA  THR A 168      -5.403  30.723  44.161  1.00 29.86           C  
ATOM   1378  C   THR A 168      -4.662  31.983  44.487  1.00 28.95           C  
ATOM   1379  O   THR A 168      -4.262  32.094  45.626  1.00 29.15           O  
ATOM   1380  CB  THR A 168      -6.883  30.883  44.629  1.00 29.23           C  
ATOM   1381  OG1 THR A 168      -7.627  30.276  43.536  1.00 32.80           O  
ATOM   1382  CG2 THR A 168      -7.295  32.240  45.230  1.00 30.85           C  
ATOM   1383  N   ARG A 169      -4.503  32.923  43.539  1.00 27.32           N  
ATOM   1384  CA  ARG A 169      -3.930  34.236  43.873  1.00 24.13           C  
ATOM   1385  C   ARG A 169      -4.555  35.248  43.026  1.00 22.41           C  
ATOM   1386  O   ARG A 169      -4.901  34.956  41.884  1.00 20.53           O  
ATOM   1387  CB  ARG A 169      -2.493  34.257  43.458  1.00 25.84           C  
ATOM   1388  CG  ARG A 169      -1.723  33.261  44.302  1.00 29.03           C  
ATOM   1389  CD  ARG A 169      -0.248  33.513  44.107  1.00 32.66           C  
ATOM   1390  NE  ARG A 169       0.455  32.486  44.838  1.00 34.77           N  
ATOM   1391  CZ  ARG A 169       1.636  32.136  44.378  1.00 37.61           C  
ATOM   1392  NH1 ARG A 169       2.198  32.861  43.421  1.00 35.90           N  
ATOM   1393  NH2 ARG A 169       2.178  31.032  44.909  1.00 38.17           N  
ATOM   1394  N   GLU A 170      -4.646  36.428  43.560  1.00 22.26           N  
ATOM   1395  CA  GLU A 170      -5.122  37.497  42.731  1.00 23.16           C  
ATOM   1396  C   GLU A 170      -3.949  38.217  42.097  1.00 21.44           C  
ATOM   1397  O   GLU A 170      -2.962  38.578  42.712  1.00 20.71           O  
ATOM   1398  CB  GLU A 170      -5.947  38.519  43.512  1.00 25.19           C  
ATOM   1399  CG  GLU A 170      -6.460  39.723  42.685  1.00 30.67           C  
ATOM   1400  CD  GLU A 170      -6.806  40.849  43.675  1.00 36.99           C  
ATOM   1401  OE1 GLU A 170      -5.989  41.273  44.487  1.00 40.67           O  
ATOM   1402  OE2 GLU A 170      -7.891  41.362  43.651  1.00 40.20           O  
ATOM   1403  N   ILE A 171      -4.197  38.496  40.811  1.00 20.04           N  
ATOM   1404  CA  ILE A 171      -3.195  39.213  39.991  1.00 19.46           C  
ATOM   1405  C   ILE A 171      -3.882  40.424  39.457  1.00 16.74           C  
ATOM   1406  O   ILE A 171      -4.917  40.313  38.885  1.00 16.14           O  
ATOM   1407  CB  ILE A 171      -2.619  38.309  38.799  1.00 20.14           C  
ATOM   1408  CG1 ILE A 171      -2.109  36.894  39.193  1.00 19.81           C  
ATOM   1409  CG2 ILE A 171      -1.589  39.043  37.952  1.00 18.82           C  
ATOM   1410  CD1 ILE A 171      -1.002  36.838  40.275  1.00 20.61           C  
ATOM   1411  N   LEU A 172      -3.310  41.579  39.584  1.00 15.27           N  
ATOM   1412  CA  LEU A 172      -3.819  42.752  38.949  1.00 13.88           C  
ATOM   1413  C   LEU A 172      -3.025  42.973  37.634  1.00 15.51           C  
ATOM   1414  O   LEU A 172      -1.811  42.870  37.608  1.00 14.77           O  
ATOM   1415  CB  LEU A 172      -3.481  43.915  39.933  1.00 14.58           C  
ATOM   1416  CG  LEU A 172      -4.460  44.229  41.110  1.00 18.81           C  
ATOM   1417  CD1 LEU A 172      -5.473  43.172  41.504  1.00 18.10           C  
ATOM   1418  CD2 LEU A 172      -3.751  44.767  42.351  1.00 16.24           C  
ATOM   1419  N   HIS A 173      -3.774  43.320  36.570  1.00 14.35           N  
ATOM   1420  CA  HIS A 173      -3.281  43.555  35.231  1.00 15.21           C  
ATOM   1421  C   HIS A 173      -3.505  45.052  34.935  1.00 16.72           C  
ATOM   1422  O   HIS A 173      -4.639  45.503  34.969  1.00 18.37           O  
ATOM   1423  CB  HIS A 173      -4.096  42.605  34.362  1.00 13.63           C  
ATOM   1424  CG  HIS A 173      -3.649  42.561  32.926  1.00 13.93           C  
ATOM   1425  ND1 HIS A 173      -4.365  43.044  31.902  1.00 15.75           N  
ATOM   1426  CD2 HIS A 173      -2.492  41.991  32.415  1.00 13.82           C  
ATOM   1427  CE1 HIS A 173      -3.652  42.769  30.803  1.00 15.67           C  
ATOM   1428  NE2 HIS A 173      -2.531  42.136  31.078  1.00 14.10           N  
ATOM   1429  N   PHE A 174      -2.412  45.823  34.715  1.00 16.63           N  
ATOM   1430  CA  PHE A 174      -2.483  47.255  34.388  1.00 16.63           C  
ATOM   1431  C   PHE A 174      -2.104  47.363  32.913  1.00 17.52           C  
ATOM   1432  O   PHE A 174      -0.963  47.109  32.561  1.00 18.52           O  
ATOM   1433  CB  PHE A 174      -1.453  48.026  35.198  1.00 14.35           C  
ATOM   1434  CG  PHE A 174      -1.772  47.832  36.652  1.00 15.38           C  
ATOM   1435  CD1 PHE A 174      -2.632  48.693  37.320  1.00 13.95           C  
ATOM   1436  CD2 PHE A 174      -1.182  46.797  37.360  1.00 14.64           C  
ATOM   1437  CE1 PHE A 174      -2.961  48.469  38.670  1.00 14.89           C  
ATOM   1438  CE2 PHE A 174      -1.524  46.580  38.672  1.00 14.31           C  
ATOM   1439  CZ  PHE A 174      -2.443  47.394  39.315  1.00 12.17           C  
ATOM   1440  N   HIS A 175      -3.108  47.679  32.078  1.00 16.20           N  
ATOM   1441  CA  HIS A 175      -2.971  47.616  30.613  1.00 15.42           C  
ATOM   1442  C   HIS A 175      -2.965  49.009  29.961  1.00 15.19           C  
ATOM   1443  O   HIS A 175      -3.985  49.640  29.894  1.00 17.28           O  
ATOM   1444  CB  HIS A 175      -4.091  46.703  30.059  1.00 15.18           C  
ATOM   1445  CG  HIS A 175      -3.993  46.424  28.579  1.00 13.52           C  
ATOM   1446  ND1 HIS A 175      -3.023  46.842  27.720  1.00 15.31           N  
ATOM   1447  CD2 HIS A 175      -4.854  45.681  27.821  1.00 14.02           C  
ATOM   1448  CE1 HIS A 175      -3.284  46.384  26.502  1.00 11.28           C  
ATOM   1449  NE2 HIS A 175      -4.367  45.671  26.551  1.00 14.96           N  
ATOM   1450  N   TYR A 176      -1.801  49.507  29.515  1.00 14.84           N  
ATOM   1451  CA  TYR A 176      -1.768  50.818  28.943  1.00 14.85           C  
ATOM   1452  C   TYR A 176      -2.093  50.600  27.474  1.00 15.94           C  
ATOM   1453  O   TYR A 176      -1.394  49.864  26.825  1.00 14.59           O  
ATOM   1454  CB  TYR A 176      -0.319  51.285  29.220  1.00 16.78           C  
ATOM   1455  CG  TYR A 176      -0.131  52.768  29.134  1.00 18.21           C  
ATOM   1456  CD1 TYR A 176      -0.375  53.391  27.916  1.00 20.14           C  
ATOM   1457  CD2 TYR A 176       0.306  53.550  30.208  1.00 16.38           C  
ATOM   1458  CE1 TYR A 176      -0.228  54.795  27.787  1.00 19.78           C  
ATOM   1459  CE2 TYR A 176       0.393  54.946  30.100  1.00 16.48           C  
ATOM   1460  CZ  TYR A 176       0.096  55.598  28.905  1.00 17.44           C  
ATOM   1461  OH  TYR A 176       0.160  56.973  28.897  1.00 19.20           O  
ATOM   1462  N   THR A 177      -3.204  51.173  27.006  1.00 17.01           N  
ATOM   1463  CA  THR A 177      -3.634  50.884  25.626  1.00 19.61           C  
ATOM   1464  C   THR A 177      -3.276  52.017  24.582  1.00 21.46           C  
ATOM   1465  O   THR A 177      -3.601  51.929  23.410  1.00 23.43           O  
ATOM   1466  CB  THR A 177      -5.153  50.539  25.686  1.00 19.04           C  
ATOM   1467  OG1 THR A 177      -5.675  51.783  26.241  1.00 22.99           O  
ATOM   1468  CG2 THR A 177      -5.331  49.289  26.528  1.00 16.89           C  
ATOM   1469  N   THR A 178      -2.585  53.088  24.991  1.00 21.16           N  
ATOM   1470  CA  THR A 178      -2.478  54.193  23.983  1.00 22.32           C  
ATOM   1471  C   THR A 178      -0.983  54.652  23.966  1.00 22.10           C  
ATOM   1472  O   THR A 178      -0.644  55.826  23.751  1.00 24.87           O  
ATOM   1473  CB  THR A 178      -3.353  55.317  24.646  1.00 21.62           C  
ATOM   1474  OG1 THR A 178      -2.968  55.321  26.018  1.00 22.99           O  
ATOM   1475  CG2 THR A 178      -4.901  55.143  24.358  1.00 20.24           C  
ATOM   1476  N   TRP A 179      -0.057  53.722  24.232  1.00 18.57           N  
ATOM   1477  CA  TRP A 179       1.362  54.034  24.175  1.00 17.07           C  
ATOM   1478  C   TRP A 179       1.852  53.312  22.920  1.00 17.18           C  
ATOM   1479  O   TRP A 179       1.955  52.100  22.866  1.00 17.65           O  
ATOM   1480  CB  TRP A 179       2.036  53.523  25.412  1.00 14.27           C  
ATOM   1481  CG  TRP A 179       3.504  53.876  25.507  1.00 12.93           C  
ATOM   1482  CD1 TRP A 179       4.420  54.258  24.530  1.00 12.07           C  
ATOM   1483  CD2 TRP A 179       4.240  53.776  26.719  1.00 15.86           C  
ATOM   1484  NE1 TRP A 179       5.667  54.411  25.039  1.00 14.13           N  
ATOM   1485  CE2 TRP A 179       5.592  54.130  26.422  1.00 16.66           C  
ATOM   1486  CE3 TRP A 179       3.855  53.417  27.998  1.00 14.60           C  
ATOM   1487  CZ2 TRP A 179       6.522  54.103  27.438  1.00 14.31           C  
ATOM   1488  CZ3 TRP A 179       4.824  53.408  28.988  1.00 13.47           C  
ATOM   1489  CH2 TRP A 179       6.137  53.737  28.730  1.00 11.19           C  
ATOM   1490  N   PRO A 180       2.215  54.068  21.844  1.00 17.75           N  
ATOM   1491  CA  PRO A 180       2.549  53.399  20.572  1.00 16.45           C  
ATOM   1492  C   PRO A 180       3.895  52.636  20.541  1.00 15.88           C  
ATOM   1493  O   PRO A 180       4.869  53.143  21.075  1.00 14.16           O  
ATOM   1494  CB  PRO A 180       2.600  54.568  19.587  1.00 17.59           C  
ATOM   1495  CG  PRO A 180       1.937  55.699  20.321  1.00 18.30           C  
ATOM   1496  CD  PRO A 180       2.285  55.535  21.782  1.00 16.69           C  
ATOM   1497  N   ASP A 181       3.940  51.479  19.862  1.00 14.70           N  
ATOM   1498  CA  ASP A 181       5.213  50.795  19.755  1.00 17.30           C  
ATOM   1499  C   ASP A 181       6.317  51.728  19.226  1.00 18.62           C  
ATOM   1500  O   ASP A 181       5.980  52.454  18.295  1.00 20.04           O  
ATOM   1501  CB  ASP A 181       5.026  49.564  18.830  1.00 17.54           C  
ATOM   1502  CG  ASP A 181       6.179  48.537  19.036  1.00 19.48           C  
ATOM   1503  OD1 ASP A 181       7.136  48.812  19.782  1.00 18.75           O  
ATOM   1504  OD2 ASP A 181       6.087  47.448  18.490  1.00 17.24           O  
ATOM   1505  N   PHE A 182       7.556  51.763  19.762  1.00 18.49           N  
ATOM   1506  CA  PHE A 182       8.558  52.772  19.342  1.00 17.45           C  
ATOM   1507  C   PHE A 182       8.151  54.222  19.537  1.00 18.05           C  
ATOM   1508  O   PHE A 182       8.743  55.139  18.946  1.00 17.47           O  
ATOM   1509  CB  PHE A 182       8.994  52.579  17.889  1.00 17.49           C  
ATOM   1510  CG  PHE A 182       9.641  51.229  17.872  1.00 18.92           C  
ATOM   1511  CD1 PHE A 182      10.943  51.093  18.358  1.00 17.52           C  
ATOM   1512  CD2 PHE A 182       8.955  50.124  17.369  1.00 17.58           C  
ATOM   1513  CE1 PHE A 182      11.588  49.872  18.296  1.00 15.78           C  
ATOM   1514  CE2 PHE A 182       9.624  48.915  17.329  1.00 18.42           C  
ATOM   1515  CZ  PHE A 182      10.931  48.803  17.771  1.00 15.88           C  
ATOM   1516  N   GLY A 183       7.088  54.358  20.393  1.00 16.76           N  
ATOM   1517  CA  GLY A 183       6.472  55.659  20.671  1.00 17.16           C  
ATOM   1518  C   GLY A 183       6.620  56.100  22.124  1.00 17.75           C  
ATOM   1519  O   GLY A 183       7.314  55.453  22.915  1.00 18.51           O  
ATOM   1520  N   VAL A 184       5.933  57.214  22.477  1.00 18.39           N  
ATOM   1521  CA  VAL A 184       5.945  57.748  23.869  1.00 17.12           C  
ATOM   1522  C   VAL A 184       4.530  57.874  24.280  1.00 18.45           C  
ATOM   1523  O   VAL A 184       3.603  57.809  23.467  1.00 17.86           O  
ATOM   1524  CB  VAL A 184       6.708  59.040  24.057  1.00 16.90           C  
ATOM   1525  CG1 VAL A 184       8.163  58.941  23.674  1.00 14.26           C  
ATOM   1526  CG2 VAL A 184       6.111  60.147  23.234  1.00 16.42           C  
ATOM   1527  N   PRO A 185       4.331  57.967  25.636  1.00 19.61           N  
ATOM   1528  CA  PRO A 185       3.001  58.222  26.153  1.00 19.32           C  
ATOM   1529  C   PRO A 185       2.509  59.616  25.599  1.00 20.77           C  
ATOM   1530  O   PRO A 185       3.315  60.461  25.213  1.00 19.11           O  
ATOM   1531  CB  PRO A 185       3.215  58.177  27.725  1.00 18.07           C  
ATOM   1532  CG  PRO A 185       4.412  57.296  27.889  1.00 16.06           C  
ATOM   1533  CD  PRO A 185       5.285  57.727  26.708  1.00 18.79           C  
ATOM   1534  N   GLU A 186       1.172  59.838  25.647  1.00 22.20           N  
ATOM   1535  CA  GLU A 186       0.642  61.132  25.273  1.00 24.65           C  
ATOM   1536  C   GLU A 186       1.262  62.293  26.105  1.00 24.98           C  
ATOM   1537  O   GLU A 186       1.514  63.367  25.588  1.00 26.75           O  
ATOM   1538  CB  GLU A 186      -0.874  61.088  25.135  1.00 28.24           C  
ATOM   1539  CG  GLU A 186      -1.458  59.671  24.832  1.00 36.26           C  
ATOM   1540  CD  GLU A 186      -1.760  58.779  26.155  1.00 41.23           C  
ATOM   1541  OE1 GLU A 186      -0.795  58.271  26.799  1.00 39.68           O  
ATOM   1542  OE2 GLU A 186      -2.974  58.649  26.500  1.00 40.31           O  
ATOM   1543  N   SER A 187       1.516  62.056  27.403  1.00 23.38           N  
ATOM   1544  CA  SER A 187       2.146  63.141  28.150  1.00 21.23           C  
ATOM   1545  C   SER A 187       2.737  62.562  29.374  1.00 19.17           C  
ATOM   1546  O   SER A 187       2.379  61.463  29.762  1.00 17.96           O  
ATOM   1547  CB  SER A 187       1.046  64.157  28.616  1.00 20.15           C  
ATOM   1548  OG  SER A 187      -0.093  63.478  29.215  1.00 20.26           O  
ATOM   1549  N   PRO A 188       3.659  63.287  29.981  1.00 20.13           N  
ATOM   1550  CA  PRO A 188       4.120  62.973  31.327  1.00 21.39           C  
ATOM   1551  C   PRO A 188       2.992  62.785  32.310  1.00 21.39           C  
ATOM   1552  O   PRO A 188       3.054  61.773  33.009  1.00 24.15           O  
ATOM   1553  CB  PRO A 188       5.140  64.066  31.741  1.00 21.09           C  
ATOM   1554  CG  PRO A 188       5.548  64.613  30.367  1.00 22.68           C  
ATOM   1555  CD  PRO A 188       4.319  64.458  29.436  1.00 20.70           C  
ATOM   1556  N   ALA A 189       1.924  63.597  32.294  1.00 20.45           N  
ATOM   1557  CA  ALA A 189       0.749  63.490  33.222  1.00 20.00           C  
ATOM   1558  C   ALA A 189       0.106  62.130  33.203  1.00 20.13           C  
ATOM   1559  O   ALA A 189      -0.225  61.496  34.186  1.00 20.29           O  
ATOM   1560  CB  ALA A 189      -0.374  64.503  32.822  1.00 19.08           C  
ATOM   1561  N   SER A 190      -0.141  61.694  32.000  1.00 20.34           N  
ATOM   1562  CA  SER A 190      -0.932  60.465  31.834  1.00 20.88           C  
ATOM   1563  C   SER A 190      -0.121  59.204  32.094  1.00 19.68           C  
ATOM   1564  O   SER A 190      -0.589  58.260  32.724  1.00 19.50           O  
ATOM   1565  CB  SER A 190      -1.565  60.383  30.389  1.00 21.68           C  
ATOM   1566  OG  SER A 190      -0.869  60.947  29.242  1.00 25.09           O  
ATOM   1567  N   PHE A 191       1.174  59.300  31.663  1.00 18.89           N  
ATOM   1568  CA  PHE A 191       2.108  58.256  32.088  1.00 16.53           C  
ATOM   1569  C   PHE A 191       2.273  58.196  33.608  1.00 16.18           C  
ATOM   1570  O   PHE A 191       2.208  57.138  34.200  1.00 15.95           O  
ATOM   1571  CB  PHE A 191       3.446  58.551  31.444  1.00 16.63           C  
ATOM   1572  CG  PHE A 191       4.500  57.616  32.007  1.00 17.08           C  
ATOM   1573  CD1 PHE A 191       4.577  56.292  31.555  1.00 14.80           C  
ATOM   1574  CD2 PHE A 191       5.352  58.075  33.028  1.00 15.95           C  
ATOM   1575  CE1 PHE A 191       5.521  55.446  32.114  1.00 14.95           C  
ATOM   1576  CE2 PHE A 191       6.253  57.194  33.645  1.00 15.32           C  
ATOM   1577  CZ  PHE A 191       6.340  55.887  33.171  1.00 14.56           C  
ATOM   1578  N   LEU A 192       2.478  59.355  34.235  1.00 16.30           N  
ATOM   1579  CA  LEU A 192       2.615  59.418  35.715  1.00 16.25           C  
ATOM   1580  C   LEU A 192       1.375  58.963  36.473  1.00 15.93           C  
ATOM   1581  O   LEU A 192       1.453  58.206  37.423  1.00 15.33           O  
ATOM   1582  CB  LEU A 192       3.061  60.810  36.193  1.00 14.47           C  
ATOM   1583  CG  LEU A 192       4.473  61.107  35.772  1.00 14.65           C  
ATOM   1584  CD1 LEU A 192       4.755  62.591  35.844  1.00 13.49           C  
ATOM   1585  CD2 LEU A 192       5.478  60.312  36.632  1.00 14.14           C  
ATOM   1586  N   ASN A 193       0.227  59.370  35.942  1.00 18.71           N  
ATOM   1587  CA  ASN A 193      -1.057  58.898  36.441  1.00 19.18           C  
ATOM   1588  C   ASN A 193      -1.154  57.350  36.383  1.00 19.45           C  
ATOM   1589  O   ASN A 193      -1.472  56.669  37.373  1.00 19.03           O  
ATOM   1590  CB  ASN A 193      -2.197  59.671  35.701  1.00 19.32           C  
ATOM   1591  CG  ASN A 193      -3.623  59.104  36.130  1.00 21.18           C  
ATOM   1592  OD1 ASN A 193      -3.953  59.294  37.295  1.00 24.50           O  
ATOM   1593  ND2 ASN A 193      -4.437  58.461  35.304  1.00 15.33           N  
ATOM   1594  N   PHE A 194      -0.797  56.836  35.182  1.00 18.52           N  
ATOM   1595  CA  PHE A 194      -0.644  55.354  35.090  1.00 17.74           C  
ATOM   1596  C   PHE A 194       0.408  54.718  36.127  1.00 18.08           C  
ATOM   1597  O   PHE A 194       0.058  53.796  36.861  1.00 17.16           O  
ATOM   1598  CB  PHE A 194      -0.338  54.961  33.628  1.00 18.26           C  
ATOM   1599  CG  PHE A 194      -0.305  53.449  33.482  1.00 17.53           C  
ATOM   1600  CD1 PHE A 194      -1.484  52.741  33.259  1.00 18.15           C  
ATOM   1601  CD2 PHE A 194       0.908  52.751  33.550  1.00 17.35           C  
ATOM   1602  CE1 PHE A 194      -1.482  51.346  33.091  1.00 18.04           C  
ATOM   1603  CE2 PHE A 194       0.917  51.342  33.361  1.00 16.91           C  
ATOM   1604  CZ  PHE A 194      -0.268  50.647  33.114  1.00 16.10           C  
ATOM   1605  N   LEU A 195       1.670  55.237  36.215  1.00 16.80           N  
ATOM   1606  CA  LEU A 195       2.669  54.692  37.106  1.00 17.07           C  
ATOM   1607  C   LEU A 195       2.181  54.646  38.605  1.00 18.11           C  
ATOM   1608  O   LEU A 195       2.383  53.733  39.394  1.00 15.97           O  
ATOM   1609  CB  LEU A 195       3.910  55.627  36.992  1.00 15.84           C  
ATOM   1610  CG  LEU A 195       5.015  55.279  38.022  1.00 15.44           C  
ATOM   1611  CD1 LEU A 195       5.299  53.786  37.990  1.00 16.81           C  
ATOM   1612  CD2 LEU A 195       6.301  56.042  37.764  1.00 11.95           C  
ATOM   1613  N   PHE A 196       1.526  55.749  38.969  1.00 19.62           N  
ATOM   1614  CA  PHE A 196       1.022  55.914  40.344  1.00 18.96           C  
ATOM   1615  C   PHE A 196      -0.254  55.010  40.535  1.00 18.68           C  
ATOM   1616  O   PHE A 196      -0.398  54.400  41.579  1.00 19.68           O  
ATOM   1617  CB  PHE A 196       0.861  57.416  40.610  1.00 20.56           C  
ATOM   1618  CG  PHE A 196       2.166  58.067  40.952  1.00 24.38           C  
ATOM   1619  CD1 PHE A 196       3.154  58.365  40.005  1.00 25.22           C  
ATOM   1620  CD2 PHE A 196       2.452  58.367  42.250  1.00 27.31           C  
ATOM   1621  CE1 PHE A 196       4.413  58.858  40.334  1.00 26.24           C  
ATOM   1622  CE2 PHE A 196       3.731  58.836  42.592  1.00 30.27           C  
ATOM   1623  CZ  PHE A 196       4.740  59.064  41.658  1.00 27.79           C  
ATOM   1624  N   LYS A 197      -1.133  54.805  39.524  1.00 19.21           N  
ATOM   1625  CA  LYS A 197      -2.108  53.701  39.708  1.00 19.92           C  
ATOM   1626  C   LYS A 197      -1.450  52.369  40.059  1.00 18.67           C  
ATOM   1627  O   LYS A 197      -1.864  51.705  40.989  1.00 17.77           O  
ATOM   1628  CB  LYS A 197      -3.029  53.500  38.486  1.00 22.84           C  
ATOM   1629  CG  LYS A 197      -4.398  54.177  38.665  1.00 31.03           C  
ATOM   1630  CD  LYS A 197      -5.572  53.161  38.666  1.00 37.07           C  
ATOM   1631  CE  LYS A 197      -6.965  53.560  39.321  1.00 40.57           C  
ATOM   1632  NZ  LYS A 197      -8.039  52.526  39.303  1.00 44.43           N  
ATOM   1633  N   VAL A 198      -0.395  51.969  39.307  1.00 18.79           N  
ATOM   1634  CA  VAL A 198       0.317  50.711  39.607  1.00 17.11           C  
ATOM   1635  C   VAL A 198       0.874  50.740  41.044  1.00 18.55           C  
ATOM   1636  O   VAL A 198       0.653  49.846  41.867  1.00 18.54           O  
ATOM   1637  CB  VAL A 198       1.451  50.465  38.619  1.00 16.20           C  
ATOM   1638  CG1 VAL A 198       2.159  49.161  38.991  1.00 14.96           C  
ATOM   1639  CG2 VAL A 198       0.877  50.358  37.204  1.00 16.51           C  
ATOM   1640  N   ARG A 199       1.586  51.854  41.349  1.00 19.80           N  
ATOM   1641  CA  ARG A 199       2.170  51.997  42.697  1.00 20.62           C  
ATOM   1642  C   ARG A 199       1.126  51.878  43.848  1.00 22.78           C  
ATOM   1643  O   ARG A 199       1.290  51.058  44.750  1.00 24.51           O  
ATOM   1644  CB  ARG A 199       2.910  53.305  42.788  1.00 18.77           C  
ATOM   1645  CG  ARG A 199       4.337  53.198  42.291  1.00 20.18           C  
ATOM   1646  CD  ARG A 199       4.892  54.615  42.278  1.00 22.10           C  
ATOM   1647  NE  ARG A 199       6.312  54.522  41.984  1.00 23.87           N  
ATOM   1648  CZ  ARG A 199       7.226  55.271  42.548  1.00 25.72           C  
ATOM   1649  NH1 ARG A 199       6.918  56.101  43.527  1.00 26.76           N  
ATOM   1650  NH2 ARG A 199       8.442  55.165  42.100  1.00 25.48           N  
ATOM   1651  N   GLU A 200       0.074  52.690  43.793  1.00 23.32           N  
ATOM   1652  CA  GLU A 200      -0.941  52.686  44.827  1.00 24.60           C  
ATOM   1653  C   GLU A 200      -1.524  51.278  45.060  1.00 23.64           C  
ATOM   1654  O   GLU A 200      -1.988  50.939  46.135  1.00 24.69           O  
ATOM   1655  CB  GLU A 200      -2.012  53.678  44.374  1.00 28.13           C  
ATOM   1656  CG  GLU A 200      -1.435  55.116  44.190  1.00 34.68           C  
ATOM   1657  CD  GLU A 200      -2.017  56.202  45.102  1.00 40.18           C  
ATOM   1658  OE1 GLU A 200      -2.964  55.859  45.806  1.00 44.64           O  
ATOM   1659  OE2 GLU A 200      -1.534  57.352  45.136  1.00 40.35           O  
ATOM   1660  N   SER A 201      -1.490  50.420  44.028  1.00 22.41           N  
ATOM   1661  CA  SER A 201      -2.213  49.153  44.152  1.00 20.94           C  
ATOM   1662  C   SER A 201      -1.486  48.120  45.079  1.00 22.81           C  
ATOM   1663  O   SER A 201      -1.948  47.010  45.420  1.00 22.93           O  
ATOM   1664  CB  SER A 201      -2.286  48.586  42.725  1.00 18.13           C  
ATOM   1665  OG  SER A 201      -1.052  47.856  42.297  1.00 14.89           O  
ATOM   1666  N   GLY A 202      -0.252  48.550  45.359  1.00 22.68           N  
ATOM   1667  CA  GLY A 202       0.593  47.703  46.116  1.00 24.37           C  
ATOM   1668  C   GLY A 202       1.407  46.689  45.300  1.00 26.70           C  
ATOM   1669  O   GLY A 202       2.185  45.923  45.840  1.00 28.74           O  
ATOM   1670  N   SER A 203       1.246  46.639  43.975  1.00 26.23           N  
ATOM   1671  CA  SER A 203       1.911  45.486  43.341  1.00 26.02           C  
ATOM   1672  C   SER A 203       3.398  45.597  43.277  1.00 27.85           C  
ATOM   1673  O   SER A 203       4.007  44.623  42.947  1.00 28.04           O  
ATOM   1674  CB  SER A 203       1.531  45.393  41.859  1.00 24.34           C  
ATOM   1675  OG  SER A 203       0.071  45.507  41.683  1.00 22.29           O  
ATOM   1676  N   LEU A 204       3.905  46.838  43.564  1.00 27.74           N  
ATOM   1677  CA  LEU A 204       5.343  47.064  43.527  1.00 28.07           C  
ATOM   1678  C   LEU A 204       5.989  46.813  44.926  1.00 30.53           C  
ATOM   1679  O   LEU A 204       7.063  47.285  45.268  1.00 34.73           O  
ATOM   1680  CB  LEU A 204       5.605  48.492  43.023  1.00 25.55           C  
ATOM   1681  CG  LEU A 204       5.173  48.699  41.593  1.00 23.50           C  
ATOM   1682  CD1 LEU A 204       5.269  50.144  41.149  1.00 24.51           C  
ATOM   1683  CD2 LEU A 204       6.151  48.022  40.708  1.00 26.27           C  
ATOM   1684  N   SER A 205       5.194  46.267  45.826  1.00 29.75           N  
ATOM   1685  CA  SER A 205       5.608  46.455  47.172  1.00 31.35           C  
ATOM   1686  C   SER A 205       6.513  45.234  47.482  1.00 31.80           C  
ATOM   1687  O   SER A 205       6.282  44.189  46.921  1.00 32.67           O  
ATOM   1688  CB  SER A 205       4.416  46.884  48.050  1.00 33.87           C  
ATOM   1689  OG  SER A 205       4.250  48.479  47.996  1.00 39.84           O  
ATOM   1690  N   PRO A 206       7.545  45.324  48.368  1.00 31.54           N  
ATOM   1691  CA  PRO A 206       8.543  44.269  48.480  1.00 30.69           C  
ATOM   1692  C   PRO A 206       8.015  43.022  49.239  1.00 29.28           C  
ATOM   1693  O   PRO A 206       8.598  41.971  49.320  1.00 29.54           O  
ATOM   1694  CB  PRO A 206       9.635  44.974  49.246  1.00 31.14           C  
ATOM   1695  CG  PRO A 206       8.853  45.846  50.211  1.00 31.99           C  
ATOM   1696  CD  PRO A 206       7.662  46.315  49.413  1.00 32.81           C  
ATOM   1697  N   GLU A 207       6.816  43.089  49.758  1.00 29.68           N  
ATOM   1698  CA  GLU A 207       6.230  41.851  50.187  1.00 29.93           C  
ATOM   1699  C   GLU A 207       5.868  40.923  49.058  1.00 27.80           C  
ATOM   1700  O   GLU A 207       5.741  39.742  49.314  1.00 29.47           O  
ATOM   1701  CB  GLU A 207       5.065  42.123  51.129  1.00 35.23           C  
ATOM   1702  CG  GLU A 207       3.791  42.841  50.613  1.00 43.96           C  
ATOM   1703  CD  GLU A 207       3.710  44.418  50.627  1.00 48.96           C  
ATOM   1704  OE1 GLU A 207       4.783  45.054  50.615  1.00 51.18           O  
ATOM   1705  OE2 GLU A 207       2.579  44.953  50.564  1.00 50.34           O  
ATOM   1706  N   HIS A 208       5.716  41.423  47.828  1.00 24.70           N  
ATOM   1707  CA  HIS A 208       5.303  40.652  46.619  1.00 22.96           C  
ATOM   1708  C   HIS A 208       6.508  40.227  45.817  1.00 20.96           C  
ATOM   1709  O   HIS A 208       7.552  40.774  46.034  1.00 20.02           O  
ATOM   1710  CB  HIS A 208       4.377  41.468  45.669  1.00 23.81           C  
ATOM   1711  CG  HIS A 208       3.106  41.688  46.429  1.00 25.02           C  
ATOM   1712  ND1 HIS A 208       2.625  42.904  46.709  1.00 26.69           N  
ATOM   1713  CD2 HIS A 208       2.251  40.756  47.033  1.00 23.58           C  
ATOM   1714  CE1 HIS A 208       1.516  42.754  47.457  1.00 23.67           C  
ATOM   1715  NE2 HIS A 208       1.275  41.463  47.658  1.00 23.34           N  
ATOM   1716  N   GLY A 209       6.347  39.218  44.940  1.00 18.87           N  
ATOM   1717  CA  GLY A 209       7.379  38.919  43.980  1.00 17.00           C  
ATOM   1718  C   GLY A 209       7.601  40.148  43.115  1.00 16.57           C  
ATOM   1719  O   GLY A 209       6.837  41.062  43.249  1.00 16.49           O  
ATOM   1720  N   PRO A 210       8.618  40.167  42.195  1.00 16.47           N  
ATOM   1721  CA  PRO A 210       8.774  41.367  41.350  1.00 15.40           C  
ATOM   1722  C   PRO A 210       7.567  41.586  40.415  1.00 15.85           C  
ATOM   1723  O   PRO A 210       7.087  40.600  39.803  1.00 16.01           O  
ATOM   1724  CB  PRO A 210      10.073  41.055  40.595  1.00 14.52           C  
ATOM   1725  CG  PRO A 210      10.384  39.581  40.743  1.00 14.79           C  
ATOM   1726  CD  PRO A 210       9.597  39.111  41.946  1.00 15.42           C  
ATOM   1727  N   VAL A 211       7.204  42.854  40.220  1.00 14.73           N  
ATOM   1728  CA  VAL A 211       6.232  43.046  39.179  1.00 14.94           C  
ATOM   1729  C   VAL A 211       6.790  42.482  37.828  1.00 15.10           C  
ATOM   1730  O   VAL A 211       7.951  42.648  37.444  1.00 15.28           O  
ATOM   1731  CB  VAL A 211       5.840  44.524  39.204  1.00 14.73           C  
ATOM   1732  CG1 VAL A 211       6.994  45.402  38.664  1.00 15.37           C  
ATOM   1733  CG2 VAL A 211       4.599  44.837  38.353  1.00 12.94           C  
ATOM   1734  N   VAL A 212       5.911  41.747  37.062  1.00 16.14           N  
ATOM   1735  CA  VAL A 212       6.139  41.459  35.626  1.00 15.23           C  
ATOM   1736  C   VAL A 212       5.766  42.699  34.680  1.00 17.09           C  
ATOM   1737  O   VAL A 212       4.600  43.077  34.584  1.00 18.99           O  
ATOM   1738  CB  VAL A 212       5.399  40.180  35.211  1.00 14.38           C  
ATOM   1739  CG1 VAL A 212       5.500  39.992  33.696  1.00 12.38           C  
ATOM   1740  CG2 VAL A 212       5.891  38.908  35.941  1.00  9.47           C  
ATOM   1741  N   VAL A 213       6.747  43.371  33.977  1.00 15.78           N  
ATOM   1742  CA  VAL A 213       6.409  44.417  32.988  1.00 13.77           C  
ATOM   1743  C   VAL A 213       6.654  43.813  31.574  1.00 15.36           C  
ATOM   1744  O   VAL A 213       7.707  43.222  31.337  1.00 15.63           O  
ATOM   1745  CB  VAL A 213       7.343  45.647  33.203  1.00 12.31           C  
ATOM   1746  CG1 VAL A 213       6.833  46.756  32.330  1.00  9.59           C  
ATOM   1747  CG2 VAL A 213       7.403  46.107  34.672  1.00  9.69           C  
ATOM   1748  N   HIS A 214       5.688  43.935  30.639  1.00 12.67           N  
ATOM   1749  CA  HIS A 214       5.957  43.563  29.275  1.00 11.40           C  
ATOM   1750  C   HIS A 214       5.427  44.678  28.276  1.00 13.19           C  
ATOM   1751  O   HIS A 214       4.497  45.467  28.539  1.00 12.64           O  
ATOM   1752  CB  HIS A 214       5.486  42.148  28.970  1.00 10.51           C  
ATOM   1753  CG  HIS A 214       4.042  42.048  28.669  1.00 11.08           C  
ATOM   1754  ND1 HIS A 214       3.530  42.236  27.424  1.00 10.67           N  
ATOM   1755  CD2 HIS A 214       3.011  41.768  29.549  1.00 10.64           C  
ATOM   1756  CE1 HIS A 214       2.208  42.091  27.547  1.00 10.17           C  
ATOM   1757  NE2 HIS A 214       1.887  41.801  28.821  1.00 12.06           N  
ATOM   1758  N   CYS A 215       6.070  44.694  27.089  1.00 12.27           N  
ATOM   1759  CA  CYS A 215       5.447  45.308  25.952  1.00 12.08           C  
ATOM   1760  C   CYS A 215       5.431  44.220  24.943  1.00 13.53           C  
ATOM   1761  O   CYS A 215       5.160  43.079  25.260  1.00 12.99           O  
ATOM   1762  CB  CYS A 215       6.163  46.563  25.448  1.00 13.92           C  
ATOM   1763  SG  CYS A 215       7.996  46.386  25.661  1.00 15.35           S  
ATOM   1764  N   SER A 216       5.768  44.555  23.717  1.00 12.97           N  
ATOM   1765  CA  SER A 216       5.827  43.425  22.788  1.00 13.07           C  
ATOM   1766  C   SER A 216       7.197  42.647  22.872  1.00 12.59           C  
ATOM   1767  O   SER A 216       7.229  41.438  22.932  1.00 12.54           O  
ATOM   1768  CB  SER A 216       5.598  44.035  21.320  1.00 10.87           C  
ATOM   1769  OG  SER A 216       5.689  42.993  20.319  1.00 12.83           O  
ATOM   1770  N   ALA A 217       8.366  43.405  23.005  1.00 13.22           N  
ATOM   1771  CA  ALA A 217       9.727  42.795  23.066  1.00 12.04           C  
ATOM   1772  C   ALA A 217      10.242  42.716  24.509  1.00 13.17           C  
ATOM   1773  O   ALA A 217      11.193  42.015  24.840  1.00 14.16           O  
ATOM   1774  CB  ALA A 217      10.648  43.750  22.348  1.00 11.34           C  
ATOM   1775  N   GLY A 218       9.597  43.525  25.391  1.00 12.56           N  
ATOM   1776  CA  GLY A 218      10.068  43.593  26.792  1.00 12.84           C  
ATOM   1777  C   GLY A 218      11.263  44.581  26.924  1.00 13.29           C  
ATOM   1778  O   GLY A 218      12.083  44.404  27.796  1.00 13.11           O  
ATOM   1779  N   ILE A 219      11.407  45.553  26.005  1.00 14.32           N  
ATOM   1780  CA  ILE A 219      12.581  46.426  26.043  1.00 15.04           C  
ATOM   1781  C   ILE A 219      12.293  47.907  25.910  1.00 13.97           C  
ATOM   1782  O   ILE A 219      12.768  48.680  26.720  1.00 13.50           O  
ATOM   1783  CB  ILE A 219      13.737  45.890  25.091  1.00 14.81           C  
ATOM   1784  CG1 ILE A 219      13.240  45.679  23.698  1.00 14.25           C  
ATOM   1785  CG2 ILE A 219      14.399  44.559  25.566  1.00 13.90           C  
ATOM   1786  CD1 ILE A 219      14.484  45.386  22.840  1.00 16.99           C  
ATOM   1787  N   GLY A 220      11.539  48.331  24.922  1.00 13.77           N  
ATOM   1788  CA  GLY A 220      11.426  49.772  24.719  1.00 14.22           C  
ATOM   1789  C   GLY A 220      10.462  50.546  25.607  1.00 15.67           C  
ATOM   1790  O   GLY A 220      10.866  51.310  26.490  1.00 16.19           O  
ATOM   1791  N   ARG A 221       9.146  50.310  25.406  1.00 15.77           N  
ATOM   1792  CA  ARG A 221       8.134  50.743  26.394  1.00 15.10           C  
ATOM   1793  C   ARG A 221       8.389  50.187  27.857  1.00 15.09           C  
ATOM   1794  O   ARG A 221       8.401  50.961  28.809  1.00 14.06           O  
ATOM   1795  CB  ARG A 221       6.725  50.398  25.855  1.00 12.71           C  
ATOM   1796  CG  ARG A 221       6.412  51.114  24.555  1.00 11.36           C  
ATOM   1797  CD  ARG A 221       5.040  50.730  24.077  1.00 12.08           C  
ATOM   1798  NE  ARG A 221       5.221  49.454  23.415  1.00 12.16           N  
ATOM   1799  CZ  ARG A 221       4.243  48.980  22.599  1.00 13.78           C  
ATOM   1800  NH1 ARG A 221       3.090  49.596  22.507  1.00 12.84           N  
ATOM   1801  NH2 ARG A 221       4.468  47.916  21.860  1.00 13.94           N  
ATOM   1802  N   SER A 222       8.637  48.846  28.048  1.00 14.17           N  
ATOM   1803  CA  SER A 222       8.982  48.425  29.400  1.00 15.44           C  
ATOM   1804  C   SER A 222      10.208  49.078  30.090  1.00 15.81           C  
ATOM   1805  O   SER A 222      10.126  49.323  31.275  1.00 15.18           O  
ATOM   1806  CB  SER A 222       9.263  46.950  29.362  1.00 14.11           C  
ATOM   1807  OG  SER A 222       8.356  46.167  28.567  1.00 15.24           O  
ATOM   1808  N   GLY A 223      11.307  49.316  29.312  1.00 15.27           N  
ATOM   1809  CA  GLY A 223      12.509  49.957  29.794  1.00 13.45           C  
ATOM   1810  C   GLY A 223      12.163  51.349  30.277  1.00 15.03           C  
ATOM   1811  O   GLY A 223      12.627  51.810  31.302  1.00 15.46           O  
ATOM   1812  N   THR A 224      11.268  51.996  29.497  1.00 15.05           N  
ATOM   1813  CA  THR A 224      10.883  53.400  29.792  1.00 15.80           C  
ATOM   1814  C   THR A 224      10.102  53.505  31.111  1.00 15.71           C  
ATOM   1815  O   THR A 224      10.419  54.302  31.981  1.00 15.03           O  
ATOM   1816  CB  THR A 224      10.038  53.994  28.630  1.00 15.69           C  
ATOM   1817  OG1 THR A 224      10.841  53.897  27.376  1.00 15.57           O  
ATOM   1818  CG2 THR A 224       9.586  55.456  28.851  1.00 13.78           C  
ATOM   1819  N   PHE A 225       9.103  52.586  31.223  1.00 15.05           N  
ATOM   1820  CA  PHE A 225       8.330  52.401  32.496  1.00 13.76           C  
ATOM   1821  C   PHE A 225       9.211  52.247  33.756  1.00 12.89           C  
ATOM   1822  O   PHE A 225       9.147  53.031  34.699  1.00 13.06           O  
ATOM   1823  CB  PHE A 225       7.269  51.273  32.274  1.00 12.60           C  
ATOM   1824  CG  PHE A 225       6.399  51.081  33.478  1.00 13.81           C  
ATOM   1825  CD1 PHE A 225       5.229  51.827  33.649  1.00 13.69           C  
ATOM   1826  CD2 PHE A 225       6.767  50.156  34.464  1.00 15.05           C  
ATOM   1827  CE1 PHE A 225       4.387  51.599  34.743  1.00 11.59           C  
ATOM   1828  CE2 PHE A 225       5.953  49.981  35.598  1.00 13.98           C  
ATOM   1829  CZ  PHE A 225       4.757  50.689  35.718  1.00 11.09           C  
ATOM   1830  N   CYS A 226      10.072  51.202  33.646  1.00 13.33           N  
ATOM   1831  CA  CYS A 226      11.003  50.926  34.754  1.00 14.93           C  
ATOM   1832  C   CYS A 226      12.033  52.007  35.014  1.00 14.39           C  
ATOM   1833  O   CYS A 226      12.355  52.315  36.132  1.00 14.11           O  
ATOM   1834  CB  CYS A 226      11.762  49.582  34.548  1.00 17.26           C  
ATOM   1835  SG  CYS A 226      10.445  48.295  34.316  1.00 22.84           S  
ATOM   1836  N   LEU A 227      12.624  52.574  33.971  1.00 15.02           N  
ATOM   1837  CA  LEU A 227      13.570  53.689  34.247  1.00 15.48           C  
ATOM   1838  C   LEU A 227      12.987  54.852  35.071  1.00 15.44           C  
ATOM   1839  O   LEU A 227      13.563  55.264  36.074  1.00 14.33           O  
ATOM   1840  CB  LEU A 227      14.149  54.183  32.919  1.00 14.35           C  
ATOM   1841  CG  LEU A 227      15.159  55.314  33.093  1.00 17.23           C  
ATOM   1842  CD1 LEU A 227      16.333  54.899  34.008  1.00 16.68           C  
ATOM   1843  CD2 LEU A 227      15.563  55.940  31.700  1.00 18.19           C  
ATOM   1844  N   ALA A 228      11.815  55.350  34.601  1.00 15.80           N  
ATOM   1845  CA  ALA A 228      11.014  56.336  35.415  1.00 17.01           C  
ATOM   1846  C   ALA A 228      10.701  55.848  36.900  1.00 17.08           C  
ATOM   1847  O   ALA A 228      10.933  56.541  37.895  1.00 15.13           O  
ATOM   1848  CB  ALA A 228       9.732  56.825  34.685  1.00 14.08           C  
ATOM   1849  N   ASP A 229      10.187  54.607  37.017  1.00 16.91           N  
ATOM   1850  CA  ASP A 229       9.827  54.177  38.353  1.00 17.52           C  
ATOM   1851  C   ASP A 229      11.022  54.296  39.334  1.00 17.80           C  
ATOM   1852  O   ASP A 229      11.016  54.931  40.388  1.00 17.65           O  
ATOM   1853  CB  ASP A 229       9.116  52.811  38.239  1.00 16.25           C  
ATOM   1854  CG  ASP A 229       8.668  52.431  39.635  1.00 18.30           C  
ATOM   1855  OD1 ASP A 229       7.923  53.160  40.309  1.00 17.37           O  
ATOM   1856  OD2 ASP A 229       9.140  51.445  40.127  1.00 19.14           O  
ATOM   1857  N   THR A 230      12.085  53.689  38.857  1.00 18.36           N  
ATOM   1858  CA  THR A 230      13.316  53.567  39.684  1.00 19.18           C  
ATOM   1859  C   THR A 230      13.980  54.870  39.943  1.00 18.35           C  
ATOM   1860  O   THR A 230      14.446  55.036  41.061  1.00 18.80           O  
ATOM   1861  CB  THR A 230      14.366  52.676  38.878  1.00 20.46           C  
ATOM   1862  OG1 THR A 230      13.885  51.336  38.589  1.00 21.79           O  
ATOM   1863  CG2 THR A 230      15.625  52.349  39.681  1.00 18.70           C  
ATOM   1864  N   CYS A 231      13.996  55.788  38.930  1.00 17.09           N  
ATOM   1865  CA  CYS A 231      14.550  57.156  39.191  1.00 15.59           C  
ATOM   1866  C   CYS A 231      13.733  57.819  40.292  1.00 16.39           C  
ATOM   1867  O   CYS A 231      14.278  58.353  41.235  1.00 16.95           O  
ATOM   1868  CB  CYS A 231      14.618  58.017  37.933  1.00 13.27           C  
ATOM   1869  SG  CYS A 231      15.913  57.398  36.863  1.00 15.79           S  
ATOM   1870  N   LEU A 232      12.423  57.685  40.182  1.00 15.08           N  
ATOM   1871  CA  LEU A 232      11.598  58.289  41.193  1.00 16.45           C  
ATOM   1872  C   LEU A 232      11.778  57.579  42.611  1.00 18.91           C  
ATOM   1873  O   LEU A 232      11.747  58.208  43.667  1.00 20.55           O  
ATOM   1874  CB  LEU A 232      10.131  58.230  40.691  1.00 14.57           C  
ATOM   1875  CG  LEU A 232       9.823  59.195  39.519  1.00 15.49           C  
ATOM   1876  CD1 LEU A 232       8.379  58.974  39.003  1.00 12.57           C  
ATOM   1877  CD2 LEU A 232      10.092  60.648  39.937  1.00 14.65           C  
ATOM   1878  N   LEU A 233      12.007  56.267  42.644  1.00 18.84           N  
ATOM   1879  CA  LEU A 233      12.239  55.623  43.921  1.00 17.27           C  
ATOM   1880  C   LEU A 233      13.552  56.092  44.607  1.00 18.19           C  
ATOM   1881  O   LEU A 233      13.686  56.359  45.788  1.00 18.62           O  
ATOM   1882  CB  LEU A 233      12.330  54.124  43.589  1.00 17.20           C  
ATOM   1883  CG  LEU A 233      11.670  53.139  44.585  1.00 18.98           C  
ATOM   1884  CD1 LEU A 233      12.361  51.781  44.575  1.00 15.54           C  
ATOM   1885  CD2 LEU A 233      11.465  53.627  46.003  1.00 19.40           C  
ATOM   1886  N   LEU A 234      14.591  56.137  43.786  1.00 18.27           N  
ATOM   1887  CA  LEU A 234      15.897  56.588  44.221  1.00 18.69           C  
ATOM   1888  C   LEU A 234      15.839  57.953  44.896  1.00 18.96           C  
ATOM   1889  O   LEU A 234      16.209  58.069  46.040  1.00 18.69           O  
ATOM   1890  CB  LEU A 234      16.755  56.698  42.974  1.00 17.93           C  
ATOM   1891  CG  LEU A 234      17.934  55.771  42.870  1.00 20.75           C  
ATOM   1892  CD1 LEU A 234      18.243  54.618  43.825  1.00 19.09           C  
ATOM   1893  CD2 LEU A 234      17.857  55.230  41.464  1.00 22.95           C  
ATOM   1894  N   MET A 235      15.324  58.912  44.125  1.00 19.10           N  
ATOM   1895  CA  MET A 235      15.036  60.240  44.574  1.00 21.57           C  
ATOM   1896  C   MET A 235      14.263  60.312  45.939  1.00 23.42           C  
ATOM   1897  O   MET A 235      14.618  61.100  46.813  1.00 22.74           O  
ATOM   1898  CB  MET A 235      14.183  60.803  43.447  1.00 23.55           C  
ATOM   1899  CG  MET A 235      14.002  62.301  43.590  1.00 27.50           C  
ATOM   1900  SD  MET A 235      13.056  62.975  42.238  1.00 32.69           S  
ATOM   1901  CE  MET A 235      14.108  62.519  40.862  1.00 26.68           C  
ATOM   1902  N   ASP A 236      13.244  59.424  46.043  1.00 23.53           N  
ATOM   1903  CA  ASP A 236      12.390  59.307  47.229  1.00 23.62           C  
ATOM   1904  C   ASP A 236      13.180  58.855  48.418  1.00 26.52           C  
ATOM   1905  O   ASP A 236      13.135  59.398  49.486  1.00 25.78           O  
ATOM   1906  CB  ASP A 236      11.304  58.300  46.852  1.00 20.71           C  
ATOM   1907  CG  ASP A 236      10.028  58.557  47.616  1.00 20.39           C  
ATOM   1908  OD1 ASP A 236       9.923  59.593  48.192  1.00 19.89           O  
ATOM   1909  OD2 ASP A 236       9.114  57.752  47.535  1.00 17.83           O  
ATOM   1910  N   LYS A 237      14.080  57.859  48.168  1.00 30.64           N  
ATOM   1911  CA  LYS A 237      14.762  57.323  49.350  1.00 33.70           C  
ATOM   1912  C   LYS A 237      15.710  58.288  49.956  1.00 33.04           C  
ATOM   1913  O   LYS A 237      15.868  58.365  51.161  1.00 34.32           O  
ATOM   1914  CB  LYS A 237      15.407  55.918  49.306  1.00 39.34           C  
ATOM   1915  CG  LYS A 237      16.317  55.361  48.228  1.00 44.32           C  
ATOM   1916  CD  LYS A 237      16.787  53.964  48.794  1.00 49.60           C  
ATOM   1917  CE  LYS A 237      15.689  52.871  49.194  1.00 52.13           C  
ATOM   1918  NZ  LYS A 237      15.214  52.663  50.595  1.00 53.44           N  
ATOM   1919  N   ARG A 238      16.351  59.046  49.089  1.00 32.43           N  
ATOM   1920  CA  ARG A 238      17.112  60.184  49.673  1.00 32.60           C  
ATOM   1921  C   ARG A 238      16.428  61.536  49.793  1.00 32.37           C  
ATOM   1922  O   ARG A 238      17.000  62.463  50.291  1.00 33.50           O  
ATOM   1923  CB  ARG A 238      18.326  60.366  48.809  1.00 35.88           C  
ATOM   1924  CG  ARG A 238      18.017  60.386  47.319  1.00 38.02           C  
ATOM   1925  CD  ARG A 238      19.222  59.898  46.513  1.00 43.57           C  
ATOM   1926  NE  ARG A 238      19.727  58.557  46.711  1.00 47.67           N  
ATOM   1927  CZ  ARG A 238      20.402  57.911  45.697  1.00 50.83           C  
ATOM   1928  NH1 ARG A 238      20.799  58.417  44.483  1.00 48.49           N  
ATOM   1929  NH2 ARG A 238      20.617  56.666  46.036  1.00 52.38           N  
ATOM   1930  N   LYS A 239      15.264  61.724  49.251  1.00 31.68           N  
ATOM   1931  CA  LYS A 239      14.741  63.055  48.998  1.00 30.76           C  
ATOM   1932  C   LYS A 239      15.765  64.011  48.392  1.00 31.22           C  
ATOM   1933  O   LYS A 239      15.828  65.139  48.772  1.00 33.06           O  
ATOM   1934  CB  LYS A 239      14.056  63.624  50.239  1.00 29.81           C  
ATOM   1935  CG  LYS A 239      12.866  62.790  50.771  1.00 27.29           C  
ATOM   1936  CD  LYS A 239      11.680  62.650  49.827  1.00 27.98           C  
ATOM   1937  CE  LYS A 239      10.352  62.723  50.527  1.00 28.16           C  
ATOM   1938  NZ  LYS A 239       9.355  61.756  50.102  1.00 32.63           N  
ATOM   1939  N   ASP A 240      16.542  63.530  47.386  1.00 30.03           N  
ATOM   1940  CA  ASP A 240      17.627  64.330  46.798  1.00 28.78           C  
ATOM   1941  C   ASP A 240      17.665  64.174  45.259  1.00 29.98           C  
ATOM   1942  O   ASP A 240      18.378  63.364  44.659  1.00 28.94           O  
ATOM   1943  CB  ASP A 240      18.945  63.938  47.482  1.00 28.34           C  
ATOM   1944  CG  ASP A 240      20.215  64.605  46.933  1.00 30.37           C  
ATOM   1945  OD1 ASP A 240      20.174  65.496  46.078  1.00 33.58           O  
ATOM   1946  OD2 ASP A 240      21.286  64.154  47.313  1.00 31.49           O  
ATOM   1947  N   PRO A 241      16.848  64.982  44.561  1.00 29.74           N  
ATOM   1948  CA  PRO A 241      16.770  64.866  43.097  1.00 29.82           C  
ATOM   1949  C   PRO A 241      18.070  64.946  42.257  1.00 30.59           C  
ATOM   1950  O   PRO A 241      18.263  64.347  41.196  1.00 29.43           O  
ATOM   1951  CB  PRO A 241      15.701  65.926  42.699  1.00 29.47           C  
ATOM   1952  CG  PRO A 241      14.982  66.331  43.975  1.00 28.58           C  
ATOM   1953  CD  PRO A 241      15.944  65.958  45.131  1.00 30.85           C  
ATOM   1954  N   SER A 242      18.972  65.671  42.895  1.00 31.68           N  
ATOM   1955  CA  SER A 242      20.138  66.076  42.195  1.00 33.74           C  
ATOM   1956  C   SER A 242      21.178  65.020  42.286  1.00 32.52           C  
ATOM   1957  O   SER A 242      22.140  64.990  41.525  1.00 34.90           O  
ATOM   1958  CB  SER A 242      20.612  67.389  42.861  1.00 39.09           C  
ATOM   1959  OG  SER A 242      19.659  68.558  42.955  1.00 46.44           O  
ATOM   1960  N   SER A 243      20.949  64.110  43.205  1.00 29.96           N  
ATOM   1961  CA  SER A 243      21.874  62.996  43.142  1.00 27.94           C  
ATOM   1962  C   SER A 243      21.421  61.831  42.238  1.00 28.03           C  
ATOM   1963  O   SER A 243      21.993  60.778  42.446  1.00 30.35           O  
ATOM   1964  CB  SER A 243      21.684  62.283  44.518  1.00 27.43           C  
ATOM   1965  OG  SER A 243      20.320  61.739  44.653  1.00 26.78           O  
ATOM   1966  N   VAL A 244      20.360  61.921  41.387  1.00 26.96           N  
ATOM   1967  CA  VAL A 244      19.985  60.766  40.517  1.00 25.80           C  
ATOM   1968  C   VAL A 244      20.526  60.997  39.087  1.00 25.75           C  
ATOM   1969  O   VAL A 244      20.269  62.042  38.469  1.00 26.23           O  
ATOM   1970  CB  VAL A 244      18.530  60.186  40.591  1.00 25.75           C  
ATOM   1971  CG1 VAL A 244      17.677  60.452  41.815  1.00 21.70           C  
ATOM   1972  CG2 VAL A 244      17.743  60.278  39.314  1.00 26.29           C  
ATOM   1973  N   ASP A 245      21.301  60.016  38.613  1.00 24.75           N  
ATOM   1974  CA  ASP A 245      21.897  60.087  37.309  1.00 24.74           C  
ATOM   1975  C   ASP A 245      21.088  59.147  36.419  1.00 23.09           C  
ATOM   1976  O   ASP A 245      21.268  57.952  36.384  1.00 21.87           O  
ATOM   1977  CB  ASP A 245      23.359  59.708  37.418  1.00 26.44           C  
ATOM   1978  CG  ASP A 245      24.071  60.023  36.088  1.00 29.05           C  
ATOM   1979  OD1 ASP A 245      23.462  60.012  34.982  1.00 28.16           O  
ATOM   1980  OD2 ASP A 245      25.291  60.259  36.153  1.00 33.32           O  
ATOM   1981  N   ILE A 246      20.146  59.762  35.648  1.00 22.58           N  
ATOM   1982  CA  ILE A 246      19.209  58.933  34.782  1.00 21.14           C  
ATOM   1983  C   ILE A 246      19.981  58.063  33.789  1.00 19.84           C  
ATOM   1984  O   ILE A 246      19.646  56.903  33.679  1.00 19.33           O  
ATOM   1985  CB  ILE A 246      18.124  59.796  34.000  1.00 20.72           C  
ATOM   1986  CG1 ILE A 246      17.227  60.540  35.038  1.00 20.71           C  
ATOM   1987  CG2 ILE A 246      17.254  58.975  33.029  1.00 18.02           C  
ATOM   1988  CD1 ILE A 246      16.282  61.557  34.404  1.00 21.70           C  
ATOM   1989  N   LYS A 247      20.991  58.640  33.045  1.00 19.95           N  
ATOM   1990  CA  LYS A 247      21.666  57.796  32.064  1.00 22.46           C  
ATOM   1991  C   LYS A 247      22.398  56.643  32.794  1.00 21.57           C  
ATOM   1992  O   LYS A 247      22.431  55.511  32.355  1.00 20.63           O  
ATOM   1993  CB  LYS A 247      22.662  58.543  31.173  1.00 26.04           C  
ATOM   1994  CG  LYS A 247      22.144  59.828  30.517  1.00 33.73           C  
ATOM   1995  CD  LYS A 247      23.300  60.752  29.927  1.00 38.01           C  
ATOM   1996  CE  LYS A 247      24.213  61.417  31.020  1.00 43.07           C  
ATOM   1997  NZ  LYS A 247      23.583  61.822  32.352  1.00 48.11           N  
ATOM   1998  N   LYS A 248      22.927  56.980  33.982  1.00 21.82           N  
ATOM   1999  CA  LYS A 248      23.595  55.966  34.784  1.00 24.00           C  
ATOM   2000  C   LYS A 248      22.712  54.847  35.370  1.00 22.50           C  
ATOM   2001  O   LYS A 248      23.124  53.686  35.361  1.00 20.35           O  
ATOM   2002  CB  LYS A 248      24.341  56.641  35.906  1.00 27.28           C  
ATOM   2003  CG  LYS A 248      25.482  55.758  36.348  1.00 33.42           C  
ATOM   2004  CD  LYS A 248      26.628  56.577  36.951  1.00 39.27           C  
ATOM   2005  CE  LYS A 248      27.290  57.572  35.954  1.00 40.86           C  
ATOM   2006  NZ  LYS A 248      27.420  58.781  36.780  1.00 44.82           N  
ATOM   2007  N   VAL A 249      21.457  55.244  35.766  1.00 21.35           N  
ATOM   2008  CA  VAL A 249      20.425  54.225  36.049  1.00 19.83           C  
ATOM   2009  C   VAL A 249      20.004  53.419  34.872  1.00 18.71           C  
ATOM   2010  O   VAL A 249      19.871  52.218  35.030  1.00 17.64           O  
ATOM   2011  CB  VAL A 249      19.274  54.522  37.073  1.00 20.85           C  
ATOM   2012  CG1 VAL A 249      19.429  55.800  37.865  1.00 20.70           C  
ATOM   2013  CG2 VAL A 249      17.873  54.097  36.754  1.00 17.15           C  
ATOM   2014  N   LEU A 250      19.821  54.039  33.702  1.00 16.98           N  
ATOM   2015  CA  LEU A 250      19.550  53.167  32.541  1.00 15.63           C  
ATOM   2016  C   LEU A 250      20.720  52.169  32.222  1.00 15.76           C  
ATOM   2017  O   LEU A 250      20.520  51.004  31.883  1.00 13.83           O  
ATOM   2018  CB  LEU A 250      19.288  54.100  31.322  1.00 13.50           C  
ATOM   2019  CG  LEU A 250      18.857  53.368  30.016  1.00 14.55           C  
ATOM   2020  CD1 LEU A 250      17.588  52.411  30.204  1.00 12.26           C  
ATOM   2021  CD2 LEU A 250      18.634  54.428  28.910  1.00 12.02           C  
ATOM   2022  N   LEU A 251      21.953  52.666  32.383  1.00 16.78           N  
ATOM   2023  CA  LEU A 251      23.063  51.710  32.150  1.00 16.45           C  
ATOM   2024  C   LEU A 251      23.075  50.508  33.147  1.00 16.65           C  
ATOM   2025  O   LEU A 251      23.235  49.350  32.807  1.00 15.39           O  
ATOM   2026  CB  LEU A 251      24.320  52.569  32.193  1.00 16.96           C  
ATOM   2027  CG  LEU A 251      25.023  52.882  30.844  1.00 20.50           C  
ATOM   2028  CD1 LEU A 251      24.415  52.342  29.576  1.00 18.79           C  
ATOM   2029  CD2 LEU A 251      25.625  54.277  30.637  1.00 19.42           C  
ATOM   2030  N   ASP A 252      22.789  50.824  34.446  1.00 18.59           N  
ATOM   2031  CA  ASP A 252      22.673  49.745  35.423  1.00 19.97           C  
ATOM   2032  C   ASP A 252      21.595  48.786  35.052  1.00 19.45           C  
ATOM   2033  O   ASP A 252      21.744  47.611  35.148  1.00 19.13           O  
ATOM   2034  CB  ASP A 252      22.526  50.169  36.943  1.00 22.18           C  
ATOM   2035  CG  ASP A 252      23.664  49.345  37.766  1.00 30.30           C  
ATOM   2036  OD1 ASP A 252      24.823  49.820  37.806  1.00 35.64           O  
ATOM   2037  OD2 ASP A 252      23.486  48.224  38.278  1.00 30.08           O  
ATOM   2038  N   MET A 253      20.459  49.264  34.600  1.00 19.76           N  
ATOM   2039  CA  MET A 253      19.413  48.319  34.183  1.00 20.35           C  
ATOM   2040  C   MET A 253      19.778  47.481  32.955  1.00 18.23           C  
ATOM   2041  O   MET A 253      19.356  46.325  32.842  1.00 16.06           O  
ATOM   2042  CB  MET A 253      18.124  49.053  33.739  1.00 24.04           C  
ATOM   2043  CG  MET A 253      17.388  49.762  34.860  1.00 29.29           C  
ATOM   2044  SD  MET A 253      15.863  50.526  34.192  1.00 32.68           S  
ATOM   2045  CE  MET A 253      15.072  50.377  35.805  1.00 29.90           C  
ATOM   2046  N   ARG A 254      20.536  48.161  32.078  1.00 16.76           N  
ATOM   2047  CA  ARG A 254      21.028  47.394  30.904  1.00 18.29           C  
ATOM   2048  C   ARG A 254      22.083  46.241  31.181  1.00 16.70           C  
ATOM   2049  O   ARG A 254      22.261  45.331  30.359  1.00 16.63           O  
ATOM   2050  CB  ARG A 254      21.506  48.258  29.728  1.00 17.76           C  
ATOM   2051  CG  ARG A 254      20.574  49.394  29.334  1.00 18.57           C  
ATOM   2052  CD  ARG A 254      20.437  49.426  27.884  1.00 22.15           C  
ATOM   2053  NE  ARG A 254      19.998  50.699  27.344  1.00 22.81           N  
ATOM   2054  CZ  ARG A 254      19.900  50.825  26.000  1.00 26.31           C  
ATOM   2055  NH1 ARG A 254      20.667  50.097  25.217  1.00 26.65           N  
ATOM   2056  NH2 ARG A 254      19.041  51.623  25.411  1.00 25.93           N  
ATOM   2057  N   LYS A 255      22.628  46.210  32.385  1.00 15.35           N  
ATOM   2058  CA  LYS A 255      23.296  44.960  32.844  1.00 13.70           C  
ATOM   2059  C   LYS A 255      22.397  43.769  32.903  1.00 13.45           C  
ATOM   2060  O   LYS A 255      22.891  42.676  32.843  1.00 15.24           O  
ATOM   2061  CB  LYS A 255      23.848  45.122  34.264  1.00 12.20           C  
ATOM   2062  CG  LYS A 255      24.874  46.218  34.249  1.00 14.20           C  
ATOM   2063  CD  LYS A 255      25.295  46.670  35.661  1.00 17.76           C  
ATOM   2064  CE  LYS A 255      26.420  47.737  35.511  1.00 19.49           C  
ATOM   2065  NZ  LYS A 255      26.979  47.967  36.833  1.00 21.29           N  
ATOM   2066  N   PHE A 256      21.080  43.939  33.074  1.00 12.60           N  
ATOM   2067  CA  PHE A 256      20.186  42.774  33.288  1.00 12.54           C  
ATOM   2068  C   PHE A 256      19.291  42.451  32.096  1.00 12.20           C  
ATOM   2069  O   PHE A 256      18.798  41.366  31.963  1.00 12.20           O  
ATOM   2070  CB  PHE A 256      19.238  43.073  34.446  1.00 13.28           C  
ATOM   2071  CG  PHE A 256      19.980  43.425  35.676  1.00 12.49           C  
ATOM   2072  CD1 PHE A 256      20.438  42.387  36.495  1.00 14.42           C  
ATOM   2073  CD2 PHE A 256      20.224  44.738  35.975  1.00 11.19           C  
ATOM   2074  CE1 PHE A 256      21.125  42.633  37.684  1.00 15.50           C  
ATOM   2075  CE2 PHE A 256      20.965  44.999  37.108  1.00 13.93           C  
ATOM   2076  CZ  PHE A 256      21.400  43.963  37.964  1.00 13.80           C  
ATOM   2077  N   ARG A 257      19.055  43.401  31.237  1.00 13.72           N  
ATOM   2078  CA  ARG A 257      18.449  43.005  29.941  1.00 12.95           C  
ATOM   2079  C   ARG A 257      18.943  44.016  28.841  1.00 14.10           C  
ATOM   2080  O   ARG A 257      19.062  45.213  29.083  1.00 10.93           O  
ATOM   2081  CB  ARG A 257      16.916  43.026  30.120  1.00 13.07           C  
ATOM   2082  CG  ARG A 257      16.086  42.487  28.890  1.00 11.53           C  
ATOM   2083  CD  ARG A 257      14.538  42.439  29.180  1.00 12.75           C  
ATOM   2084  NE  ARG A 257      13.717  41.807  28.063  1.00 13.26           N  
ATOM   2085  CZ  ARG A 257      13.487  40.569  27.637  1.00 14.09           C  
ATOM   2086  NH1 ARG A 257      14.169  39.598  28.155  1.00 10.99           N  
ATOM   2087  NH2 ARG A 257      12.612  40.310  26.663  1.00 14.00           N  
ATOM   2088  N   CYS A 258      19.242  43.497  27.639  1.00 17.93           N  
ATOM   2089  CA  CYS A 258      19.742  44.292  26.524  1.00 20.53           C  
ATOM   2090  C   CYS A 258      18.713  45.318  26.021  1.00 21.12           C  
ATOM   2091  O   CYS A 258      17.556  45.081  25.716  1.00 20.80           O  
ATOM   2092  CB  CYS A 258      20.069  43.398  25.310  1.00 23.74           C  
ATOM   2093  SG  CYS A 258      18.450  42.622  24.749  1.00 35.56           S  
ATOM   2094  N   GLN A 259      19.246  46.505  25.871  1.00 22.22           N  
ATOM   2095  CA  GLN A 259      18.645  47.458  24.962  1.00 23.37           C  
ATOM   2096  C   GLN A 259      17.291  48.025  25.341  1.00 21.01           C  
ATOM   2097  O   GLN A 259      16.562  48.560  24.539  1.00 19.49           O  
ATOM   2098  CB  GLN A 259      18.853  47.061  23.490  1.00 29.25           C  
ATOM   2099  CG  GLN A 259      19.999  47.902  22.793  1.00 35.56           C  
ATOM   2100  CD  GLN A 259      19.466  48.936  21.760  1.00 39.75           C  
ATOM   2101  OE1 GLN A 259      19.245  48.596  20.606  1.00 43.17           O  
ATOM   2102  NE2 GLN A 259      19.275  50.191  22.109  1.00 39.33           N  
ATOM   2103  N   LEU A 260      17.170  48.043  26.687  1.00 19.28           N  
ATOM   2104  CA  LEU A 260      16.240  48.855  27.482  1.00 16.01           C  
ATOM   2105  C   LEU A 260      16.152  50.337  26.998  1.00 15.01           C  
ATOM   2106  O   LEU A 260      17.127  51.097  27.066  1.00 13.97           O  
ATOM   2107  CB  LEU A 260      16.530  48.696  29.006  1.00 13.92           C  
ATOM   2108  CG  LEU A 260      16.393  47.253  29.484  1.00 14.46           C  
ATOM   2109  CD1 LEU A 260      16.471  47.259  31.024  1.00 15.51           C  
ATOM   2110  CD2 LEU A 260      15.092  46.480  28.983  1.00 10.64           C  
ATOM   2111  N   ILE A 261      14.902  50.656  26.543  1.00 13.78           N  
ATOM   2112  CA  ILE A 261      14.547  51.932  25.906  1.00 14.75           C  
ATOM   2113  C   ILE A 261      15.070  51.893  24.457  1.00 16.45           C  
ATOM   2114  O   ILE A 261      16.281  51.764  24.241  1.00 15.16           O  
ATOM   2115  CB  ILE A 261      15.004  53.223  26.693  1.00 14.86           C  
ATOM   2116  CG1 ILE A 261      14.585  53.185  28.163  1.00 13.25           C  
ATOM   2117  CG2 ILE A 261      14.602  54.491  25.947  1.00 16.03           C  
ATOM   2118  CD1 ILE A 261      14.257  54.480  28.822  1.00 12.37           C  
ATOM   2119  N   GLN A 262      14.076  51.972  23.526  1.00 17.23           N  
ATOM   2120  CA  GLN A 262      14.332  51.705  22.122  1.00 17.59           C  
ATOM   2121  C   GLN A 262      14.660  52.920  21.262  1.00 17.67           C  
ATOM   2122  O   GLN A 262      15.351  52.743  20.313  1.00 18.42           O  
ATOM   2123  CB  GLN A 262      13.264  50.810  21.554  1.00 16.63           C  
ATOM   2124  CG  GLN A 262      13.568  49.398  22.006  1.00 18.59           C  
ATOM   2125  CD  GLN A 262      14.720  48.873  21.132  1.00 20.48           C  
ATOM   2126  OE1 GLN A 262      14.564  48.762  19.930  1.00 24.45           O  
ATOM   2127  NE2 GLN A 262      15.888  48.594  21.695  1.00 18.63           N  
ATOM   2128  N   THR A 263      14.223  54.128  21.605  1.00 17.90           N  
ATOM   2129  CA  THR A 263      14.623  55.294  20.814  1.00 15.72           C  
ATOM   2130  C   THR A 263      15.056  56.492  21.676  1.00 16.65           C  
ATOM   2131  O   THR A 263      14.845  56.593  22.903  1.00 17.62           O  
ATOM   2132  CB  THR A 263      13.363  55.815  20.066  1.00 15.38           C  
ATOM   2133  OG1 THR A 263      12.496  56.427  21.079  1.00 15.11           O  
ATOM   2134  CG2 THR A 263      12.408  54.755  19.540  1.00 13.34           C  
ATOM   2135  N   ALA A 264      15.651  57.486  21.035  1.00 17.08           N  
ATOM   2136  CA  ALA A 264      16.080  58.690  21.754  1.00 19.17           C  
ATOM   2137  C   ALA A 264      14.874  59.547  22.300  1.00 18.70           C  
ATOM   2138  O   ALA A 264      14.971  60.146  23.372  1.00 19.96           O  
ATOM   2139  CB  ALA A 264      16.933  59.493  20.782  1.00 17.56           C  
ATOM   2140  N   ASP A 265      13.717  59.548  21.640  1.00 18.68           N  
ATOM   2141  CA  ASP A 265      12.565  60.251  22.249  1.00 19.05           C  
ATOM   2142  C   ASP A 265      11.991  59.486  23.478  1.00 18.13           C  
ATOM   2143  O   ASP A 265      11.546  60.040  24.449  1.00 18.45           O  
ATOM   2144  CB  ASP A 265      11.445  60.363  21.199  1.00 21.58           C  
ATOM   2145  CG  ASP A 265      10.555  61.559  21.527  1.00 24.97           C  
ATOM   2146  OD1 ASP A 265      11.061  62.618  21.873  1.00 27.63           O  
ATOM   2147  OD2 ASP A 265       9.349  61.406  21.427  1.00 27.31           O  
ATOM   2148  N   GLN A 266      12.055  58.155  23.498  1.00 17.14           N  
ATOM   2149  CA  GLN A 266      11.751  57.491  24.776  1.00 16.31           C  
ATOM   2150  C   GLN A 266      12.684  57.886  25.934  1.00 17.12           C  
ATOM   2151  O   GLN A 266      12.278  58.044  27.070  1.00 18.68           O  
ATOM   2152  CB  GLN A 266      11.780  55.968  24.570  1.00 13.61           C  
ATOM   2153  CG  GLN A 266      10.487  55.406  23.862  1.00 14.52           C  
ATOM   2154  CD  GLN A 266      10.664  53.919  23.499  1.00 15.52           C  
ATOM   2155  OE1 GLN A 266      11.761  53.410  23.677  1.00 18.32           O  
ATOM   2156  NE2 GLN A 266       9.619  53.279  22.994  1.00 15.39           N  
ATOM   2157  N   LEU A 267      13.998  58.068  25.668  1.00 18.95           N  
ATOM   2158  CA  LEU A 267      15.002  58.550  26.650  1.00 17.70           C  
ATOM   2159  C   LEU A 267      14.623  59.915  27.142  1.00 19.96           C  
ATOM   2160  O   LEU A 267      14.549  60.213  28.327  1.00 19.84           O  
ATOM   2161  CB  LEU A 267      16.330  58.785  26.022  1.00 17.88           C  
ATOM   2162  CG  LEU A 267      17.378  59.050  27.071  1.00 18.83           C  
ATOM   2163  CD1 LEU A 267      17.416  57.946  28.180  1.00 18.35           C  
ATOM   2164  CD2 LEU A 267      18.739  59.284  26.401  1.00 17.21           C  
ATOM   2165  N   ARG A 268      14.330  60.748  26.137  1.00 20.48           N  
ATOM   2166  CA  ARG A 268      13.862  62.114  26.396  1.00 19.61           C  
ATOM   2167  C   ARG A 268      12.517  62.230  27.183  1.00 19.86           C  
ATOM   2168  O   ARG A 268      12.430  62.969  28.168  1.00 19.82           O  
ATOM   2169  CB  ARG A 268      13.805  62.827  25.069  1.00 19.90           C  
ATOM   2170  CG  ARG A 268      13.485  64.286  25.359  1.00 21.96           C  
ATOM   2171  CD  ARG A 268      13.123  64.955  24.043  1.00 25.10           C  
ATOM   2172  NE  ARG A 268      12.980  66.390  24.260  1.00 24.79           N  
ATOM   2173  CZ  ARG A 268      11.816  66.952  24.414  1.00 23.92           C  
ATOM   2174  NH1 ARG A 268      10.679  66.298  24.392  1.00 22.48           N  
ATOM   2175  NH2 ARG A 268      11.893  68.217  24.596  1.00 23.19           N  
ATOM   2176  N   PHE A 269      11.535  61.411  26.795  1.00 17.93           N  
ATOM   2177  CA  PHE A 269      10.387  61.328  27.620  1.00 16.85           C  
ATOM   2178  C   PHE A 269      10.686  60.864  29.060  1.00 17.29           C  
ATOM   2179  O   PHE A 269      10.075  61.331  30.007  1.00 17.84           O  
ATOM   2180  CB  PHE A 269       9.381  60.365  26.957  1.00 18.43           C  
ATOM   2181  CG  PHE A 269       8.074  60.241  27.757  1.00 19.23           C  
ATOM   2182  CD1 PHE A 269       7.051  61.152  27.550  1.00 18.43           C  
ATOM   2183  CD2 PHE A 269       7.903  59.257  28.734  1.00 21.03           C  
ATOM   2184  CE1 PHE A 269       5.898  61.106  28.326  1.00 19.07           C  
ATOM   2185  CE2 PHE A 269       6.766  59.249  29.540  1.00 20.40           C  
ATOM   2186  CZ  PHE A 269       5.763  60.181  29.347  1.00 18.95           C  
ATOM   2187  N   SER A 270      11.611  59.928  29.241  1.00 18.01           N  
ATOM   2188  CA  SER A 270      11.918  59.521  30.618  1.00 18.66           C  
ATOM   2189  C   SER A 270      12.424  60.650  31.513  1.00 20.66           C  
ATOM   2190  O   SER A 270      12.041  60.754  32.679  1.00 21.02           O  
ATOM   2191  CB  SER A 270      13.056  58.484  30.622  1.00 16.97           C  
ATOM   2192  OG  SER A 270      12.765  57.383  29.737  1.00 20.89           O  
ATOM   2193  N   TYR A 271      13.324  61.492  30.939  1.00 20.79           N  
ATOM   2194  CA  TYR A 271      13.701  62.754  31.654  1.00 21.25           C  
ATOM   2195  C   TYR A 271      12.406  63.598  31.981  1.00 22.16           C  
ATOM   2196  O   TYR A 271      12.268  64.004  33.136  1.00 25.53           O  
ATOM   2197  CB  TYR A 271      14.583  63.659  30.825  1.00 19.36           C  
ATOM   2198  CG  TYR A 271      16.014  63.296  30.889  1.00 19.72           C  
ATOM   2199  CD1 TYR A 271      16.460  62.189  30.184  1.00 18.90           C  
ATOM   2200  CD2 TYR A 271      16.900  64.112  31.611  1.00 20.65           C  
ATOM   2201  CE1 TYR A 271      17.788  61.826  30.236  1.00 20.97           C  
ATOM   2202  CE2 TYR A 271      18.252  63.842  31.597  1.00 21.90           C  
ATOM   2203  CZ  TYR A 271      18.688  62.664  30.915  1.00 22.75           C  
ATOM   2204  OH  TYR A 271      20.014  62.287  30.906  1.00 23.67           O  
ATOM   2205  N   LEU A 272      11.484  63.780  30.975  1.00 20.51           N  
ATOM   2206  CA  LEU A 272      10.263  64.559  31.237  1.00 18.85           C  
ATOM   2207  C   LEU A 272       9.485  64.002  32.460  1.00 19.09           C  
ATOM   2208  O   LEU A 272       9.153  64.622  33.470  1.00 18.88           O  
ATOM   2209  CB  LEU A 272       9.511  64.461  29.929  1.00 17.27           C  
ATOM   2210  CG  LEU A 272       9.594  65.766  29.075  1.00 19.61           C  
ATOM   2211  CD1 LEU A 272      10.769  66.692  29.176  1.00 16.74           C  
ATOM   2212  CD2 LEU A 272       9.376  65.470  27.619  1.00 19.10           C  
ATOM   2213  N   ALA A 273       9.288  62.657  32.334  1.00 18.73           N  
ATOM   2214  CA  ALA A 273       8.522  61.911  33.361  1.00 18.83           C  
ATOM   2215  C   ALA A 273       9.130  62.032  34.759  1.00 18.98           C  
ATOM   2216  O   ALA A 273       8.379  62.225  35.699  1.00 18.96           O  
ATOM   2217  CB  ALA A 273       8.387  60.428  32.949  1.00 16.46           C  
ATOM   2218  N   VAL A 274      10.477  61.884  34.891  1.00 17.37           N  
ATOM   2219  CA  VAL A 274      11.126  61.901  36.194  1.00 16.73           C  
ATOM   2220  C   VAL A 274      11.171  63.291  36.804  1.00 17.90           C  
ATOM   2221  O   VAL A 274      11.008  63.439  38.007  1.00 18.72           O  
ATOM   2222  CB  VAL A 274      12.521  61.384  36.053  1.00 14.56           C  
ATOM   2223  CG1 VAL A 274      13.329  61.568  37.338  1.00 12.35           C  
ATOM   2224  CG2 VAL A 274      12.501  59.905  35.695  1.00 14.54           C  
ATOM   2225  N   ILE A 275      11.354  64.296  35.917  1.00 18.54           N  
ATOM   2226  CA  ILE A 275      11.461  65.720  36.311  1.00 18.48           C  
ATOM   2227  C   ILE A 275      10.103  66.140  36.824  1.00 18.83           C  
ATOM   2228  O   ILE A 275      10.085  66.710  37.914  1.00 20.00           O  
ATOM   2229  CB  ILE A 275      11.994  66.702  35.192  1.00 18.66           C  
ATOM   2230  CG1 ILE A 275      13.519  66.495  34.959  1.00 19.56           C  
ATOM   2231  CG2 ILE A 275      11.669  68.217  35.450  1.00 16.74           C  
ATOM   2232  CD1 ILE A 275      14.055  66.957  33.571  1.00 17.02           C  
ATOM   2233  N   GLU A 276       9.001  65.752  36.084  1.00 16.37           N  
ATOM   2234  CA  GLU A 276       7.639  66.055  36.578  1.00 16.08           C  
ATOM   2235  C   GLU A 276       7.255  65.337  37.890  1.00 16.37           C  
ATOM   2236  O   GLU A 276       6.740  65.905  38.873  1.00 16.39           O  
ATOM   2237  CB  GLU A 276       6.683  65.758  35.448  1.00 16.36           C  
ATOM   2238  CG  GLU A 276       5.206  65.945  35.766  1.00 18.33           C  
ATOM   2239  CD  GLU A 276       4.831  67.398  36.212  1.00 21.68           C  
ATOM   2240  OE1 GLU A 276       5.575  68.333  35.917  1.00 21.78           O  
ATOM   2241  OE2 GLU A 276       3.792  67.590  36.875  1.00 21.06           O  
ATOM   2242  N   GLY A 277       7.624  64.019  37.901  1.00 16.06           N  
ATOM   2243  CA  GLY A 277       7.331  63.113  39.048  1.00 15.95           C  
ATOM   2244  C   GLY A 277       8.004  63.587  40.398  1.00 17.98           C  
ATOM   2245  O   GLY A 277       7.448  63.447  41.485  1.00 18.38           O  
ATOM   2246  N   ALA A 278       9.209  64.168  40.235  1.00 18.44           N  
ATOM   2247  CA  ALA A 278       9.943  64.764  41.331  1.00 19.40           C  
ATOM   2248  C   ALA A 278       9.089  65.818  42.096  1.00 20.48           C  
ATOM   2249  O   ALA A 278       9.241  65.958  43.300  1.00 21.05           O  
ATOM   2250  CB  ALA A 278      11.255  65.396  40.852  1.00 19.05           C  
ATOM   2251  N   LYS A 279       8.166  66.479  41.377  1.00 20.90           N  
ATOM   2252  CA  LYS A 279       7.411  67.495  42.154  1.00 21.71           C  
ATOM   2253  C   LYS A 279       6.616  66.809  43.331  1.00 22.07           C  
ATOM   2254  O   LYS A 279       6.586  67.123  44.504  1.00 21.33           O  
ATOM   2255  CB  LYS A 279       6.506  68.244  41.200  1.00 21.34           C  
ATOM   2256  CG  LYS A 279       7.224  69.013  40.089  1.00 23.02           C  
ATOM   2257  CD  LYS A 279       6.095  69.536  39.175  1.00 24.63           C  
ATOM   2258  CE  LYS A 279       6.485  70.672  38.225  1.00 27.22           C  
ATOM   2259  NZ  LYS A 279       5.532  70.759  37.143  1.00 30.34           N  
ATOM   2260  N   PHE A 280       6.019  65.699  42.887  1.00 22.49           N  
ATOM   2261  CA  PHE A 280       5.326  64.848  43.864  1.00 22.28           C  
ATOM   2262  C   PHE A 280       6.258  64.203  44.940  1.00 22.21           C  
ATOM   2263  O   PHE A 280       6.010  64.299  46.122  1.00 20.52           O  
ATOM   2264  CB  PHE A 280       4.562  63.830  43.056  1.00 22.98           C  
ATOM   2265  CG  PHE A 280       3.693  63.029  43.958  1.00 25.24           C  
ATOM   2266  CD1 PHE A 280       2.458  63.514  44.361  1.00 26.35           C  
ATOM   2267  CD2 PHE A 280       4.090  61.783  44.413  1.00 27.14           C  
ATOM   2268  CE1 PHE A 280       1.610  62.778  45.194  1.00 24.16           C  
ATOM   2269  CE2 PHE A 280       3.234  61.054  45.247  1.00 26.53           C  
ATOM   2270  CZ  PHE A 280       1.992  61.539  45.609  1.00 23.55           C  
ATOM   2271  N   ILE A 281       7.380  63.557  44.471  1.00 22.00           N  
ATOM   2272  CA  ILE A 281       8.345  62.948  45.411  1.00 20.97           C  
ATOM   2273  C   ILE A 281       8.834  64.092  46.419  1.00 21.87           C  
ATOM   2274  O   ILE A 281       9.010  63.903  47.604  1.00 22.50           O  
ATOM   2275  CB  ILE A 281       9.463  62.196  44.588  1.00 20.49           C  
ATOM   2276  CG1 ILE A 281       9.023  61.019  43.695  1.00 20.20           C  
ATOM   2277  CG2 ILE A 281      10.633  61.691  45.387  1.00 19.71           C  
ATOM   2278  CD1 ILE A 281       8.050  59.966  44.239  1.00 20.20           C  
ATOM   2279  N   MET A 282       9.037  65.318  45.919  1.00 20.55           N  
ATOM   2280  CA  MET A 282       9.599  66.241  46.831  1.00 19.98           C  
ATOM   2281  C   MET A 282       8.532  66.936  47.712  1.00 21.50           C  
ATOM   2282  O   MET A 282       8.803  67.920  48.399  1.00 23.55           O  
ATOM   2283  CB  MET A 282      10.460  67.140  45.966  1.00 21.86           C  
ATOM   2284  CG  MET A 282      11.721  66.348  45.478  1.00 23.73           C  
ATOM   2285  SD  MET A 282      12.661  65.526  46.815  1.00 27.29           S  
ATOM   2286  CE  MET A 282      13.566  66.955  47.457  1.00 25.18           C  
ATOM   2287  N   GLY A 283       7.312  66.392  47.777  1.00 21.61           N  
ATOM   2288  CA  GLY A 283       6.350  66.895  48.813  1.00 21.44           C  
ATOM   2289  C   GLY A 283       5.128  67.674  48.313  1.00 20.91           C  
ATOM   2290  O   GLY A 283       4.312  68.093  49.135  1.00 21.44           O  
ATOM   2291  N   ASP A 284       4.980  67.817  46.985  1.00 21.37           N  
ATOM   2292  CA  ASP A 284       3.748  68.394  46.419  1.00 21.53           C  
ATOM   2293  C   ASP A 284       2.765  67.359  45.875  1.00 22.16           C  
ATOM   2294  O   ASP A 284       2.550  67.060  44.696  1.00 22.66           O  
ATOM   2295  CB  ASP A 284       4.043  69.490  45.442  1.00 22.31           C  
ATOM   2296  CG  ASP A 284       2.769  70.172  44.975  1.00 25.72           C  
ATOM   2297  OD1 ASP A 284       1.639  69.832  45.380  1.00 27.46           O  
ATOM   2298  OD2 ASP A 284       2.859  71.040  44.138  1.00 28.74           O  
ATOM   2299  N   SER A 285       2.056  66.835  46.865  1.00 23.01           N  
ATOM   2300  CA  SER A 285       1.064  65.846  46.458  1.00 23.47           C  
ATOM   2301  C   SER A 285       0.006  66.337  45.513  1.00 24.74           C  
ATOM   2302  O   SER A 285      -0.538  65.506  44.824  1.00 26.04           O  
ATOM   2303  CB  SER A 285       0.543  65.044  47.646  1.00 23.75           C  
ATOM   2304  OG  SER A 285       1.761  64.455  48.361  1.00 18.78           O  
ATOM   2305  N   SER A 286      -0.255  67.665  45.411  1.00 24.54           N  
ATOM   2306  CA  SER A 286      -1.282  68.174  44.512  1.00 25.78           C  
ATOM   2307  C   SER A 286      -1.036  67.895  43.023  1.00 26.95           C  
ATOM   2308  O   SER A 286      -1.981  67.738  42.230  1.00 26.25           O  
ATOM   2309  CB  SER A 286      -1.451  69.687  44.619  1.00 24.95           C  
ATOM   2310  OG  SER A 286      -0.445  70.531  43.974  1.00 29.64           O  
ATOM   2311  N   VAL A 287       0.274  67.768  42.704  1.00 26.59           N  
ATOM   2312  CA  VAL A 287       0.584  67.426  41.291  1.00 27.03           C  
ATOM   2313  C   VAL A 287      -0.056  66.126  40.880  1.00 26.32           C  
ATOM   2314  O   VAL A 287      -0.570  66.061  39.788  1.00 27.11           O  
ATOM   2315  CB  VAL A 287       2.061  67.522  40.862  1.00 26.94           C  
ATOM   2316  CG1 VAL A 287       2.640  68.844  41.377  1.00 26.12           C  
ATOM   2317  CG2 VAL A 287       2.860  66.327  41.371  1.00 27.35           C  
ATOM   2318  N   GLN A 288      -0.127  65.146  41.794  1.00 25.14           N  
ATOM   2319  CA  GLN A 288      -0.749  63.883  41.470  1.00 25.66           C  
ATOM   2320  C   GLN A 288      -2.199  64.005  40.974  1.00 28.45           C  
ATOM   2321  O   GLN A 288      -2.606  63.334  40.033  1.00 29.91           O  
ATOM   2322  CB  GLN A 288      -0.581  62.906  42.622  1.00 23.99           C  
ATOM   2323  CG  GLN A 288      -1.487  61.736  42.429  1.00 28.11           C  
ATOM   2324  CD  GLN A 288      -1.321  60.533  43.348  1.00 32.29           C  
ATOM   2325  OE1 GLN A 288      -0.962  60.639  44.495  1.00 34.24           O  
ATOM   2326  NE2 GLN A 288      -1.656  59.366  42.785  1.00 34.59           N  
ATOM   2327  N   ASP A 289      -3.006  64.836  41.619  1.00 31.32           N  
ATOM   2328  CA  ASP A 289      -4.412  64.917  41.184  1.00 33.11           C  
ATOM   2329  C   ASP A 289      -4.542  65.830  39.955  1.00 30.52           C  
ATOM   2330  O   ASP A 289      -5.394  65.630  39.122  1.00 30.14           O  
ATOM   2331  CB  ASP A 289      -5.356  65.019  42.418  1.00 41.00           C  
ATOM   2332  CG  ASP A 289      -5.929  63.550  42.769  1.00 49.38           C  
ATOM   2333  OD1 ASP A 289      -6.694  62.972  41.960  1.00 52.46           O  
ATOM   2334  OD2 ASP A 289      -5.572  62.970  43.813  1.00 54.20           O  
ATOM   2335  N   GLN A 290      -3.563  66.727  39.761  1.00 28.67           N  
ATOM   2336  CA  GLN A 290      -3.366  67.389  38.474  1.00 28.04           C  
ATOM   2337  C   GLN A 290      -3.076  66.444  37.298  1.00 26.18           C  
ATOM   2338  O   GLN A 290      -3.658  66.586  36.243  1.00 25.13           O  
ATOM   2339  CB  GLN A 290      -2.261  68.408  38.513  1.00 31.10           C  
ATOM   2340  CG  GLN A 290      -2.600  69.421  39.579  1.00 37.10           C  
ATOM   2341  CD  GLN A 290      -1.395  70.239  39.941  1.00 42.87           C  
ATOM   2342  OE1 GLN A 290      -0.607  70.609  39.090  1.00 46.76           O  
ATOM   2343  NE2 GLN A 290      -1.254  70.497  41.220  1.00 44.56           N  
ATOM   2344  N   TRP A 291      -2.209  65.463  37.508  1.00 23.20           N  
ATOM   2345  CA  TRP A 291      -1.970  64.498  36.433  1.00 21.95           C  
ATOM   2346  C   TRP A 291      -3.242  63.754  36.128  1.00 23.23           C  
ATOM   2347  O   TRP A 291      -3.607  63.450  35.002  1.00 23.51           O  
ATOM   2348  CB  TRP A 291      -0.923  63.441  36.803  1.00 18.39           C  
ATOM   2349  CG  TRP A 291       0.384  64.051  37.232  1.00 15.12           C  
ATOM   2350  CD1 TRP A 291       0.974  65.247  36.808  1.00 15.53           C  
ATOM   2351  CD2 TRP A 291       1.307  63.453  38.155  1.00 14.74           C  
ATOM   2352  NE1 TRP A 291       2.176  65.385  37.405  1.00 16.20           N  
ATOM   2353  CE2 TRP A 291       2.416  64.322  38.242  1.00 14.01           C  
ATOM   2354  CE3 TRP A 291       1.271  62.309  38.894  1.00 13.38           C  
ATOM   2355  CZ2 TRP A 291       3.465  64.003  39.050  1.00 14.55           C  
ATOM   2356  CZ3 TRP A 291       2.348  61.981  39.729  1.00 11.99           C  
ATOM   2357  CH2 TRP A 291       3.461  62.821  39.815  1.00 13.01           C  
ATOM   2358  N   LYS A 292      -3.899  63.483  37.217  1.00 24.42           N  
ATOM   2359  CA  LYS A 292      -5.124  62.808  37.027  1.00 28.18           C  
ATOM   2360  C   LYS A 292      -6.205  63.574  36.103  1.00 29.50           C  
ATOM   2361  O   LYS A 292      -6.778  63.031  35.144  1.00 28.20           O  
ATOM   2362  CB  LYS A 292      -5.660  62.582  38.427  1.00 31.20           C  
ATOM   2363  CG  LYS A 292      -6.680  61.491  38.209  1.00 36.30           C  
ATOM   2364  CD  LYS A 292      -7.488  61.329  39.443  1.00 40.76           C  
ATOM   2365  CE  LYS A 292      -8.464  60.246  39.107  1.00 44.50           C  
ATOM   2366  NZ  LYS A 292      -9.214  60.215  40.348  1.00 50.59           N  
ATOM   2367  N   GLU A 293      -6.408  64.870  36.421  1.00 30.52           N  
ATOM   2368  CA  GLU A 293      -7.178  65.765  35.539  1.00 31.16           C  
ATOM   2369  C   GLU A 293      -6.645  65.818  34.094  1.00 29.22           C  
ATOM   2370  O   GLU A 293      -7.288  65.422  33.141  1.00 29.96           O  
ATOM   2371  CB  GLU A 293      -7.325  67.112  36.222  1.00 35.80           C  
ATOM   2372  CG  GLU A 293      -8.150  66.958  37.510  1.00 45.00           C  
ATOM   2373  CD  GLU A 293      -9.632  67.473  37.502  1.00 51.44           C  
ATOM   2374  OE1 GLU A 293      -9.806  68.680  37.662  1.00 57.46           O  
ATOM   2375  OE2 GLU A 293     -10.599  66.704  37.407  1.00 52.44           O  
ATOM   2376  N   LEU A 294      -5.417  66.237  33.916  1.00 27.51           N  
ATOM   2377  CA  LEU A 294      -4.846  66.241  32.588  1.00 26.50           C  
ATOM   2378  C   LEU A 294      -4.998  64.968  31.765  1.00 26.78           C  
ATOM   2379  O   LEU A 294      -4.961  64.999  30.560  1.00 26.55           O  
ATOM   2380  CB  LEU A 294      -3.341  66.417  32.755  1.00 26.19           C  
ATOM   2381  CG  LEU A 294      -2.879  67.841  32.729  1.00 26.70           C  
ATOM   2382  CD1 LEU A 294      -3.939  68.782  33.161  1.00 28.85           C  
ATOM   2383  CD2 LEU A 294      -1.696  67.990  33.629  1.00 26.69           C  
ATOM   2384  N   SER A 295      -5.077  63.851  32.449  1.00 27.37           N  
ATOM   2385  CA  SER A 295      -4.920  62.604  31.739  1.00 28.83           C  
ATOM   2386  C   SER A 295      -6.202  62.207  31.106  1.00 31.25           C  
ATOM   2387  O   SER A 295      -6.244  61.343  30.246  1.00 32.67           O  
ATOM   2388  CB  SER A 295      -4.538  61.468  32.707  1.00 25.99           C  
ATOM   2389  OG  SER A 295      -5.714  60.936  33.399  1.00 28.81           O  
ATOM   2390  N   HIS A 296      -7.267  62.861  31.575  1.00 33.82           N  
ATOM   2391  CA  HIS A 296      -8.618  62.556  31.062  1.00 38.26           C  
ATOM   2392  C   HIS A 296      -8.979  61.083  31.198  1.00 39.04           C  
ATOM   2393  O   HIS A 296      -9.336  60.435  30.228  1.00 39.04           O  
ATOM   2394  CB  HIS A 296      -8.883  63.008  29.584  1.00 41.98           C  
ATOM   2395  CG  HIS A 296      -8.554  64.461  29.494  1.00 46.50           C  
ATOM   2396  ND1 HIS A 296      -7.472  64.914  28.830  1.00 49.85           N  
ATOM   2397  CD2 HIS A 296      -9.125  65.532  30.214  1.00 48.41           C  
ATOM   2398  CE1 HIS A 296      -7.363  66.232  29.151  1.00 49.95           C  
ATOM   2399  NE2 HIS A 296      -8.352  66.628  29.984  1.00 49.11           N  
ATOM   2400  N   GLU A 297      -8.837  60.588  32.462  1.00 40.65           N  
ATOM   2401  CA  GLU A 297      -8.850  59.146  32.551  1.00 40.99           C  
ATOM   2402  C   GLU A 297     -10.269  58.466  32.258  1.00 42.73           C  
ATOM   2403  O   GLU A 297     -10.401  57.294  31.957  1.00 43.27           O  
ATOM   2404  CB  GLU A 297      -8.202  58.487  33.726  1.00 40.49           C  
ATOM   2405  CG  GLU A 297      -8.844  58.875  35.006  1.00 40.13           C  
ATOM   2406  CD  GLU A 297      -8.245  58.109  36.145  1.00 41.83           C  
ATOM   2407  OE1 GLU A 297      -7.079  57.670  36.154  1.00 40.38           O  
ATOM   2408  OE2 GLU A 297      -9.026  57.929  37.068  1.00 44.94           O  
ATOM   2409  N   ASP A 298     -11.354  59.219  32.469  1.00 45.28           N  
ATOM   2410  CA  ASP A 298     -12.716  58.676  32.489  1.00 47.99           C  
ATOM   2411  C   ASP A 298     -13.352  58.628  31.076  1.00 49.51           C  
ATOM   2412  O   ASP A 298     -13.196  59.592  30.314  1.00 50.89           O  
ATOM   2413  CB  ASP A 298     -13.531  59.511  33.494  1.00 49.49           C  
ATOM   2414  CG  ASP A 298     -13.193  59.163  34.950  1.00 53.62           C  
ATOM   2415  OD1 ASP A 298     -13.029  57.970  35.246  1.00 56.28           O  
ATOM   2416  OD2 ASP A 298     -13.081  60.056  35.797  1.00 54.94           O  
ATOM   2417  OXT ASP A 298     -13.966  57.602  30.726  1.00 51.84           O  
TER    2418      ASP A 298                                                      
HETATM 2419  S1  COL A 301      14.194  45.059  17.006  1.00 23.15           S  
HETATM 2420  C2  COL A 301      13.958  45.570  18.702  1.00 17.76           C  
HETATM 2421  C3  COL A 301      12.499  45.548  18.970  1.00 19.49           C  
HETATM 2422  C4  COL A 301      11.449  45.264  18.167  1.00 18.45           C  
HETATM 2423  C5  COL A 301      11.406  44.649  16.812  1.00 18.90           C  
HETATM 2424  C6  COL A 301      12.761  43.942  16.720  1.00 19.60           C  
HETATM 2425  S13 COL A 301      11.996  46.235  20.479  1.00 17.68           S  
HETATM 2426  C14 COL A 301      10.401  46.044  20.020  1.00 17.64           C  
HETATM 2427  C15 COL A 301      10.166  45.556  18.818  1.00 18.49           C  
HETATM 2428  C16 COL A 301       8.729  45.429  18.284  1.00 18.49           C  
HETATM 2429  O17 COL A 301       7.738  45.423  18.957  1.00 17.21           O  
HETATM 2430  O18 COL A 301       8.667  45.355  17.013  1.00 17.03           O  
HETATM 2431  N19 COL A 301       9.308  46.505  20.851  1.00 18.93           N  
HETATM 2432  C20 COL A 301       9.498  47.204  21.976  1.00 18.64           C  
HETATM 2433  C21 COL A 301       8.159  47.645  22.546  1.00 17.05           C  
HETATM 2434  O22 COL A 301       7.158  46.717  22.400  1.00 16.38           O  
HETATM 2435  O23 COL A 301       7.942  48.586  23.234  1.00 18.07           O  
HETATM 2436  O24 COL A 301      10.569  47.268  22.601  1.00 17.29           O  
HETATM 2437  O   HOH A 302       6.794  34.163  26.222  1.00 18.64           O  
HETATM 2438  O   HOH A 303      19.607  33.004  27.337  1.00 15.47           O  
HETATM 2439  O   HOH A 304       8.848  30.073  27.279  1.00 20.61           O  
HETATM 2440  O   HOH A 305       4.191  41.963  41.861  1.00 17.26           O  
HETATM 2441  O   HOH A 306      22.153  57.757  40.020  1.00 26.93           O  
HETATM 2442  O   HOH A 307      16.023  25.678  27.452  1.00 20.13           O  
HETATM 2443  O   HOH A 308      14.664  31.716  30.878  1.00 15.28           O  
HETATM 2444  O   HOH A 309       9.722  31.196  37.367  1.00 16.53           O  
HETATM 2445  O   HOH A 310      11.904  32.772  24.958  1.00 85.28           O  
HETATM 2446  O   HOH A 311      13.500  59.346  18.626  1.00 24.08           O  
HETATM 2447  O   HOH A 312       6.625  36.579  28.240  1.00 16.39           O  
HETATM 2448  O   HOH A 313       4.510  58.341  20.078  1.00 27.75           O  
HETATM 2449  O   HOH A 314       8.147  45.272  41.512  1.00 19.68           O  
HETATM 2450  O   HOH A 315      11.073  44.157  44.544  1.00 28.95           O  
HETATM 2451  O   HOH A 316      21.395  46.848  40.614  1.00 24.86           O  
HETATM 2452  O   HOH A 317      -1.365  26.512  27.258  1.00 39.50           O  
HETATM 2453  O   HOH A 318      25.060  48.399  30.800  1.00 16.91           O  
HETATM 2454  O   HOH A 319      -4.952  44.662  23.281  1.00 28.31           O  
HETATM 2455  O   HOH A 320       7.750  69.494  45.152  1.00 30.72           O  
HETATM 2456  O   HOH A 321      -9.226  42.875  25.888  1.00 46.62           O  
HETATM 2457  O   HOH A 322       9.478  50.560  21.812  1.00 17.65           O  
HETATM 2458  O   HOH A 323       8.764  67.422  32.595  1.00 24.79           O  
HETATM 2459  O   HOH A 324      -0.424  50.907  24.562  1.00 16.96           O  
HETATM 2460  O   HOH A 325       1.351  36.321  19.659  1.00 27.21           O  
HETATM 2461  O   HOH A 326       9.610  63.870  24.442  1.00 30.16           O  
HETATM 2462  O   HOH A 327       6.896  61.289  51.493  1.00 20.88           O  
HETATM 2463  O   HOH A 328      20.898  30.063  32.922  1.00 42.90           O  
HETATM 2464  O   HOH A 329       1.183  62.045  49.114  1.00 23.03           O  
HETATM 2465  O   HOH A 330     -13.861  27.073  37.160  1.00 38.00           O  
HETATM 2466  O   HOH A 331     -19.472  40.030  38.524  1.00 21.04           O  
HETATM 2467  O   HOH A 332      12.167  38.176  21.785  1.00 17.44           O  
HETATM 2468  O   HOH A 333      16.788  54.898  17.865  1.00 50.40           O  
HETATM 2469  O   HOH A 334     -10.132  47.120  27.978  1.00 31.38           O  
HETATM 2470  O   HOH A 335      15.792  67.721  50.602  1.00 34.60           O  
HETATM 2471  O   HOH A 336       2.003  34.945  41.838  1.00 23.30           O  
HETATM 2472  O   HOH A 337      -7.957  51.995  28.017  1.00 45.02           O  
HETATM 2473  O   HOH A 338      25.404  34.797  23.464  1.00 37.72           O  
HETATM 2474  O   HOH A 339      -3.728  36.760  46.376  1.00 31.51           O  
HETATM 2475  O   HOH A 340      14.768  53.000  53.013  1.00 49.52           O  
HETATM 2476  O   HOH A 341      15.282  32.571  37.924  1.00 28.74           O  
HETATM 2477  O   HOH A 342       9.919  33.831  44.385  1.00 60.99           O  
HETATM 2478  O   HOH A 343      16.981  44.794  44.551  1.00 46.30           O  
HETATM 2479  O   HOH A 344       2.461  37.016  16.616  1.00 25.23           O  
HETATM 2480  O   HOH A 345      14.458  20.719  26.499  1.00 34.34           O  
HETATM 2481  O   HOH A 346      20.372  57.596  18.168  1.00 32.55           O  
HETATM 2482  O   HOH A 347       5.222  72.485  35.347  1.00 63.43           O  
HETATM 2483  O   HOH A 348      -8.764  30.919  37.568  1.00 25.11           O  
HETATM 2484  O   HOH A 349      17.791  38.985  47.110  1.00100.00           O  
HETATM 2485  O   HOH A 350       7.016  73.455  40.966  1.00 55.50           O  
HETATM 2486  O   HOH A 351     -18.616  36.431  24.583  1.00 71.43           O  
HETATM 2487  O   HOH A 352      -9.730  27.529  28.356  1.00 52.31           O  
HETATM 2488  O   HOH A 353       1.980  66.372  31.181  1.00 26.42           O  
HETATM 2489  O   HOH A 354      21.649  23.419  32.153  1.00100.00           O  
HETATM 2490  O   HOH A 355       5.778  42.056  13.946  1.00 37.25           O  
HETATM 2491  O   HOH A 356      13.613  67.496  20.827  1.00 48.95           O  
HETATM 2492  O   HOH A 357       0.581  29.246  25.373  1.00 23.65           O  
HETATM 2493  O   HOH A 358      -5.526  52.689  21.185  1.00 41.60           O  
HETATM 2494  O   HOH A 359      -1.718  50.419  15.870  1.00 30.20           O  
HETATM 2495  O   HOH A 360      19.381  40.658  23.263  1.00 30.56           O  
HETATM 2496  O   HOH A 361      18.164  37.954  31.385  1.00 17.93           O  
HETATM 2497  O   HOH A 362      18.961  39.160  37.901  1.00 21.51           O  
HETATM 2498  O   HOH A 363      22.790  45.662  27.750  1.00 20.95           O  
HETATM 2499  O   HOH A 364     -12.718  34.409  33.025  1.00 19.10           O  
HETATM 2500  O   HOH A 365      11.987  67.499  51.288  1.00 56.09           O  
HETATM 2501  O   HOH A 366     -21.903  36.497  24.583  1.00 49.96           O  
HETATM 2502  O   HOH A 367      26.176  48.469  41.629  1.00 36.22           O  
HETATM 2503  O   HOH A 368      28.860  48.667  39.569  1.00 35.57           O  
HETATM 2504  O   HOH A 369       9.115  56.658  45.110  1.00 25.06           O  
HETATM 2505  O   HOH A 370       4.325  63.862  48.402  1.00 29.26           O  
HETATM 2506  O   HOH A 371       8.261  59.406  19.674  1.00 23.08           O  
HETATM 2507  O   HOH A 372      15.568  35.817  20.751  1.00 19.10           O  
HETATM 2508  O   HOH A 373       1.815  50.863  17.848  1.00 28.82           O  
HETATM 2509  O   HOH A 374      20.887  53.282  40.750  1.00 36.17           O  
HETATM 2510  O   HOH A 375      16.499  30.007  19.969  1.00 24.01           O  
HETATM 2511  O   HOH A 376      22.204  39.183  37.561  1.00 31.04           O  
HETATM 2512  O   HOH A 377      23.468  28.914  22.611  1.00 38.45           O  
HETATM 2513  O   HOH A 378      15.985  22.854  31.404  1.00 36.48           O  
HETATM 2514  O   HOH A 379      17.861  51.149  19.524  1.00 28.24           O  
HETATM 2515  O   HOH A 380      -4.449  51.396  42.087  1.00 26.61           O  
HETATM 2516  O   HOH A 381     -19.457  44.504  35.594  1.00 27.51           O  
HETATM 2517  O   HOH A 382       4.426  62.864  25.523  1.00 32.98           O  
HETATM 2518  O   HOH A 383       3.014  25.807  37.415  1.00 31.88           O  
HETATM 2519  O   HOH A 384       3.211  49.164  45.081  1.00 17.21           O  
HETATM 2520  O   HOH A 385      19.204  32.705  36.138  1.00 30.03           O  
HETATM 2521  O   HOH A 386       1.200  57.600  45.644  1.00 30.69           O  
HETATM 2522  O   HOH A 387      13.205  33.836  17.101  1.00 40.35           O  
HETATM 2523  O   HOH A 388     -11.942  60.801  27.926  1.00 48.42           O  
HETATM 2524  O   HOH A 389      -7.741  56.743  39.106  1.00 45.52           O  
HETATM 2525  O   HOH A 390       9.283  39.210  48.750  1.00 64.14           O  
HETATM 2526  O   HOH A 391       8.028  69.323  35.243  1.00 31.71           O  
HETATM 2527  O   HOH A 392      -7.187  69.190  30.649  1.00 51.19           O  
HETATM 2528  O   HOH A 393      14.930  34.990  39.824  1.00 43.92           O  
HETATM 2529  O   HOH A 394       2.553  37.242  46.519  1.00 45.26           O  
HETATM 2530  O   HOH A 395     -12.519  42.146  28.468  1.00 35.55           O  
HETATM 2531  O   HOH A 396      21.002  67.822  15.987  1.00 38.05           O  
HETATM 2532  O   HOH A 397      30.556  48.112  28.095  1.00 44.49           O  
HETATM 2533  O   HOH A 398       5.362  25.872  39.863  1.00 56.18           O  
HETATM 2534  O   HOH A 399     -16.915  40.800  37.050  1.00 21.65           O  
HETATM 2535  O   HOH A 400       7.631  43.737  44.333  1.00 27.75           O  
HETATM 2536  O   HOH A 401      14.164  57.290  53.177  1.00 28.66           O  
HETATM 2537  O   HOH A 402      14.678  66.142  53.117  1.00 33.44           O  
HETATM 2538  O   HOH A 403      19.163  40.549  27.535  1.00 14.89           O  
HETATM 2539  O   HOH A 404      15.747  55.791  55.473  1.00 27.38           O  
HETATM 2540  O   HOH A 405      -2.298  60.630  39.171  1.00 20.77           O  
HETATM 2541  O   HOH A 406     -12.338  34.530  27.730  1.00 36.24           O  
HETATM 2542  O   HOH A 407      -3.075  31.687  22.852  1.00 28.57           O  
HETATM 2543  O   HOH A 408       5.589  71.337  43.130  1.00 38.54           O  
HETATM 2544  O   HOH A 409      -0.958  50.740  21.244  1.00 36.75           O  
HETATM 2545  O   HOH A 410      12.063  22.185  24.491  1.00 50.67           O  
HETATM 2546  O   HOH A 411      -1.442  57.100  20.304  1.00 39.44           O  
HETATM 2547  O   HOH A 412     -10.000  29.822  40.217  1.00 24.00           O  
HETATM 2548  O   HOH A 413       2.861  27.759  27.443  1.00 20.38           O  
HETATM 2549  O   HOH A 414       5.675  27.408  43.184  1.00 37.95           O  
HETATM 2550  O   HOH A 415       6.236  37.056  48.462  1.00 33.89           O  
HETATM 2551  O   HOH A 416      28.526  44.826  34.919  1.00 23.80           O  
HETATM 2552  O   HOH A 417       1.558  58.811  21.730  1.00 45.96           O  
HETATM 2553  O   HOH A 418      24.957  46.193  39.602  1.00 30.18           O  
HETATM 2554  O   HOH A 419       4.869  30.614  44.396  1.00 28.40           O  
HETATM 2555  O   HOH A 420      -0.305  37.692  44.902  1.00 42.65           O  
HETATM 2556  O   HOH A 421      -7.239  39.117  20.911  1.00 40.18           O  
HETATM 2557  O   HOH A 422      30.055  57.092  24.514  1.00 35.06           O  
HETATM 2558  O   HOH A 423      13.631  64.231  20.347  1.00 47.14           O  
HETATM 2559  O   HOH A 424     -14.215  55.158  29.077  1.00 39.47           O  
HETATM 2560  O   HOH A 425      -4.568  60.464  28.505  1.00 31.08           O  
HETATM 2561  O   HOH A 426      22.865  26.959  20.027  1.00 29.65           O  
HETATM 2562  O   HOH A 427      19.020  37.709  20.302  1.00 24.12           O  
HETATM 2563  O   HOH A 428      11.271  69.283  38.864  1.00 41.99           O  
HETATM 2564  O   HOH A 429       7.453  71.189  47.745  1.00 40.65           O  
HETATM 2565  O   HOH A 430      25.854  50.127  19.676  1.00 46.21           O  
HETATM 2566  O   HOH A 431       9.569  25.145  22.851  1.00 33.43           O  
HETATM 2567  O   HOH A 432      20.471  62.946  35.245  1.00 32.01           O  
HETATM 2568  O   HOH A 433      16.308  33.332  19.006  1.00 38.05           O  
HETATM 2569  O   HOH A 434      -0.855  67.365  29.876  1.00 31.03           O  
HETATM 2570  O   HOH A 435      19.420  25.246  33.395  1.00 40.36           O  
HETATM 2571  O   HOH A 436      -2.485  64.324  28.517  1.00 42.15           O  
HETATM 2572  O   HOH A 437      23.200  34.462  37.751  1.00 62.98           O  
HETATM 2573  O   HOH A 438     -11.541  46.034  38.111  1.00 35.70           O  
HETATM 2574  O   HOH A 439      30.133  33.569  26.324  1.00 36.97           O  
HETATM 2575  O   HOH A 440      20.097  43.606  17.601  1.00 44.97           O  
HETATM 2576  O   HOH A 441      23.788  28.944  31.692  1.00 50.85           O  
HETATM 2577  O   HOH A 442      17.335  30.848  16.967  1.00 47.10           O  
HETATM 2578  O   HOH A 443      11.914  25.556  19.057  1.00 38.40           O  
HETATM 2579  O   HOH A 444       6.589  33.946  49.863  1.00 63.39           O  
HETATM 2580  O   HOH A 445      -8.061  42.556  21.801  1.00 43.63           O  
HETATM 2581  O   HOH A 446     -10.723  36.434  25.595  1.00 55.46           O  
HETATM 2582  O   HOH A 447      -7.013  44.285  44.942  1.00 42.06           O  
HETATM 2583  O   HOH A 448      10.423  57.130  20.076  1.00 28.36           O  
HETATM 2584  O   HOH A 449      17.894  25.368  29.937  1.00 30.93           O  
HETATM 2585  O   HOH A 450      13.305  30.886  39.597  1.00 28.17           O  
HETATM 2586  O   HOH A 451      23.595  44.644  42.203  1.00 41.61           O  
HETATM 2587  O   HOH A 452      21.931  49.482  41.972  1.00 35.10           O  
HETATM 2588  O   HOH A 453      19.107  51.002  42.046  1.00 27.76           O  
HETATM 2589  O   HOH A 454      -9.393  46.896  40.306  1.00 42.41           O  
HETATM 2590  O   HOH A 455      -8.219  34.400  25.572  1.00 54.53           O  
HETATM 2591  O   HOH A 456      25.768  52.235  36.066  1.00 35.57           O  
HETATM 2592  O   HOH A 457      14.272  67.492  39.189  1.00 37.29           O  
HETATM 2593  O   HOH A 458      -0.176  26.010  46.305  1.00 34.10           O  
HETATM 2594  O   HOH A 459      -8.114  65.633  40.285  1.00 40.33           O  
HETATM 2595  O   HOH A 460      -1.558  61.362  47.970  1.00 44.42           O  
HETATM 2596  O   HOH A 461       5.276  54.255  16.453  1.00 42.80           O  
HETATM 2597  O   HOH A 462      20.636  38.408  17.307  1.00 54.83           O  
HETATM 2598  O   HOH A 463      24.101  65.003  46.116  1.00 58.24           O  
HETATM 2599  O   HOH A 464      -0.027  58.256  48.712  1.00 56.82           O  
HETATM 2600  O   HOH A 465       5.773  73.772  46.303  1.00 45.47           O  
HETATM 2601  O   HOH A 466      19.679  69.343  38.140  1.00 47.50           O  
HETATM 2602  O   HOH A 467       4.814  23.824  26.454  1.00 39.97           O  
HETATM 2603  O   HOH A 468      28.662  45.921  31.946  1.00 35.92           O  
HETATM 2604  O   HOH A 469      -2.933  29.495  25.298  1.00 44.06           O  
HETATM 2605  O   HOH A 470      20.209  28.904  17.027  1.00 58.57           O  
HETATM 2606  O   HOH A 471      17.005  68.849  40.509  1.00 62.76           O  
HETATM 2607  O   HOH A 472       8.424  22.731  28.598  1.00 37.07           O  
HETATM 2608  O   HOH A 473       1.088  72.019  41.949  1.00 41.74           O  
HETATM 2609  O   HOH A 474       7.848  64.256  50.519  1.00 69.37           O  
HETATM 2610  O   HOH A 475       2.853  26.267  44.514  1.00 41.06           O  
HETATM 2611  O   HOH A 476      20.400  49.939  49.263  1.00 42.30           O  
HETATM 2612  O   HOH A 477      19.741  65.043  38.881  1.00 32.76           O  
HETATM 2613  O   HOH A 478      18.125  35.355  38.368  1.00 69.60           O  
HETATM 2614  O   HOH A 479      21.850  47.634  25.507  1.00 32.84           O  
HETATM 2615  O   HOH A 480      -7.644  46.231  26.381  1.00 41.61           O  
HETATM 2616  O   HOH A 481      10.533  55.833  16.367  1.00 57.45           O  
HETATM 2617  O   HOH A 482      14.265  43.694  45.769  1.00 36.84           O  
HETATM 2618  O   HOH A 483      19.828  53.047  17.768  1.00 55.87           O  
HETATM 2619  O   HOH A 484      24.796  69.641  32.954  1.00 52.27           O  
HETATM 2620  O   HOH A 485       3.387  56.767  17.466  1.00 44.03           O  
HETATM 2621  O   HOH A 486      15.529  62.202  18.174  1.00 43.69           O  
HETATM 2622  O   HOH A 487       8.164  29.676  43.585  1.00 38.53           O  
HETATM 2623  O   HOH A 488      21.556  67.780  35.694  1.00 43.69           O  
HETATM 2624  O   HOH A 489     -10.064  23.415  40.579  1.00 61.35           O  
HETATM 2625  O   HOH A 490     -15.830  44.162  35.083  1.00 27.83           O  
HETATM 2626  O   HOH A 491     -17.429  43.682  37.966  1.00 33.50           O  
HETATM 2627  O   HOH A 492      -5.450  28.486  27.036  1.00 36.88           O  
HETATM 2628  O   HOH A 493      26.168  30.991  28.714  1.00 36.12           O  
HETATM 2629  O   HOH A 494      21.496  24.746  29.272  1.00100.00           O  
HETATM 2630  O   HOH A 495       4.734  22.918  35.205  1.00 40.60           O  
HETATM 2631  O   HOH A 496       2.073  67.721  27.953  1.00 50.00           O  
HETATM 2632  O   HOH A 497     -16.649  46.582  33.009  1.00 45.00           O  
HETATM 2633  O   HOH A 498      30.093  43.910  28.772  1.00 42.56           O  
HETATM 2634  O   HOH A 499      11.749  41.983  48.443  1.00 45.61           O  
HETATM 2635  O   HOH A 500     -13.983  35.711  24.625  1.00 65.11           O  
HETATM 2636  O   HOH A 501      16.208  25.470  36.294  1.00 41.98           O  
HETATM 2637  O   HOH A 502      11.366  69.445  42.760  1.00 53.99           O  
HETATM 2638  O   HOH A 503      -3.669  63.945  48.296  1.00 42.35           O  
HETATM 2639  O   HOH A 504     -15.354  49.542  33.351  1.00 34.97           O  
HETATM 2640  O   HOH A 505      25.014  37.390  38.082  1.00 31.83           O  
HETATM 2641  O   HOH A 506      26.479  57.974  28.723  1.00 58.16           O  
HETATM 2642  O   HOH A 507       2.026  69.882  37.261  1.00 40.34           O  
HETATM 2643  O   HOH A 508      10.041  48.216  46.962  1.00 36.04           O  
HETATM 2644  O   HOH A 509       9.053  69.707  25.110  1.00 61.73           O  
HETATM 2645  O   HOH A 510     -14.228  55.854  33.877  1.00 44.48           O  
CONECT 2419 2420 2424                                                           
CONECT 2420 2419 2421                                                           
CONECT 2421 2420 2422 2425                                                      
CONECT 2422 2421 2423 2427                                                      
CONECT 2423 2422 2424                                                           
CONECT 2424 2419 2423                                                           
CONECT 2425 2421 2426                                                           
CONECT 2426 2425 2427 2431                                                      
CONECT 2427 2422 2426 2428                                                      
CONECT 2428 2427 2429 2430                                                      
CONECT 2429 2428                                                                
CONECT 2430 2428                                                                
CONECT 2431 2426 2432                                                           
CONECT 2432 2431 2433 2436                                                      
CONECT 2433 2432 2434 2435                                                      
CONECT 2434 2433                                                                
CONECT 2435 2433                                                                
CONECT 2436 2432                                                                
MASTER      365    0    1   11   11    0    4    6 2644    1   18   23          
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.