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***  HYDROLASE (SULFHYDRYL PROTEINASE) 31-MAR-86 9PAP  ***

elNémo ID: 201009021054930

Job options:

ID        	=	 201009021054930
JOBID     	=	 HYDROLASE (SULFHYDRYL PROTEINASE) 31-MAR-86 9PAP
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    HYDROLASE (SULFHYDRYL PROTEINASE)       31-MAR-86   9PAP              
TITLE     STRUCTURE OF PAPAIN REFINED AT 1.65 ANGSTROMS RESOLUTION              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PAPAIN;                                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.4.22.2;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CARICA PAPAYA;                                  
SOURCE   3 ORGANISM_COMMON: PAPAYA;                                             
SOURCE   4 ORGANISM_TAXID: 3649                                                 
KEYWDS    HYDROLASE (SULFHYDRYL PROTEINASE)                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    I.G.KAMPHUIS,J.DRENTH                                                 
REVDAT   7   29-NOV-17 9PAP    1       HELIX                                    
REVDAT   6   24-FEB-09 9PAP    1       VERSN                                    
REVDAT   5   01-APR-03 9PAP    1       JRNL                                     
REVDAT   4   15-JAN-95 9PAP    1       SPRSDE                                   
REVDAT   3   31-OCT-93 9PAP    1       HET                                      
REVDAT   2   15-OCT-92 9PAP    1       SHEET                                    
REVDAT   1   24-OCT-86 9PAP    0                                                
SPRSDE     24-OCT-86 9PAP      3PAD 8PAP                                        
JRNL        AUTH   I.G.KAMPHUIS,K.H.KALK,M.B.SWARTE,J.DRENTH                    
JRNL        TITL   STRUCTURE OF PAPAIN REFINED AT 1.65 A RESOLUTION             
JRNL        REF    J.MOL.BIOL.                   V. 179   233 1984              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   6502713                                                      
JRNL        DOI    10.1016/0022-2836(84)90467-4                                 
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   I.G.KAMPHUIS,J.DRENTH,E.N.BAKER                              
REMARK   1  TITL   THIOL PROTEASES. COMPARATIVE STUDIES BASED ON THE            
REMARK   1  TITL 2 HIGH-RESOLUTION STRUCTURES OF PAPAIN AND ACTINIDIN, AND ON   
REMARK   1  TITL 3 AMINO ACID SEQUENCE INFORMATION FOR CATHEPSINS B AND H, AND  
REMARK   1  TITL 4 STEM BROMELAIN                                               
REMARK   1  REF    J.MOL.BIOL.                   V. 182   317 1985              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   J.DRENTH,K.H.KALK,H.M.SWEN                                   
REMARK   1  TITL   BINDING OF CHLOROMETHYL KETONE SUBSTRATE ANALOGUES TO        
REMARK   1  TITL 2 CRYSTALLINE PAPAIN                                           
REMARK   1  REF    BIOCHEMISTRY                  V.  15  3731 1976              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   J.DRENTH,J.N.JANSONIUS,R.KOEKOEK,B.G.WOLTHERS                
REMARK   1  TITL   THE STRUCTURE OF PAPAIN                                      
REMARK   1  REF    ADV.PROTEIN CHEM.             V.  25    79 1971              
REMARK   1  REFN                   ISSN 0065-3233                               
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   J.DRENTH,J.N.JANSONIUS,R.KOEKOEK,L.A.A.SLUYTERMAN,           
REMARK   1  AUTH 2 B.G.WOLTHERS                                                 
REMARK   1  TITL   THE STRUCTURE OF THE PAPAIN MOLECULE                         
REMARK   1  REF    PHILOS.TRANS.R.SOC.LONDON,    V. 257   231 1970              
REMARK   1  REF  2 SER.B                                                        
REMARK   1  REFN                   ISSN 0080-4622                               
REMARK   1 REFERENCE 5                                                          
REMARK   1  AUTH   J.DRENTH,J.N.JANSONIUS,R.KOEKOEK,H.M.SWEN,B.G.WOLTHERS       
REMARK   1  TITL   STRUCTURE OF PAPAIN                                          
REMARK   1  REF    NATURE                        V. 218   929 1968              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PROLSQ                                               
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : NULL                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.161                           
REMARK   3   R VALUE            (WORKING SET) : NULL                            
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1655                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 58                                      
REMARK   3   SOLVENT ATOMS            : 195                                     
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  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.022 ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : 0.047 ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; 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  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 9PAP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000180069.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.04                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       22.60000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       25.44000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.32000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       25.44000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       22.60000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.32000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 139    CD   CE   NZ                                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   ND2  ASN A    46     O    HOH A   384              1.97            
REMARK 500   O    MOH A   225     O    HOH A   282              2.04            
REMARK 500   O    HOH A   284     O    HOH A   339              2.07            
REMARK 500   O    HOH A   314     O    HOH A   322              2.07            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    TRP A  26   NE1   TRP A  26   CE2    -0.093                       
REMARK 500    GLU A  52   CD    GLU A  52   OE2    -0.076                       
REMARK 500    TRP A  69   NE1   TRP A  69   CE2    -0.095                       
REMARK 500    TYR A  86   CD1   TYR A  86   CE1     0.096                       
REMARK 500    TYR A  88   CD1   TYR A  88   CE1     0.090                       
REMARK 500    CYS A  95   CA    CYS A  95   CB     -0.101                       
REMARK 500    GLU A  99   CG    GLU A  99   CD      0.102                       
REMARK 500    TYR A 166   CD1   TYR A 166   CE1     0.090                       
REMARK 500    TYR A 170   CD1   TYR A 170   CE1     0.091                       
REMARK 500    GLU A 183   CD    GLU A 183   OE2    -0.066                       
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    GLU A   3   OE1 -  CD  -  OE2 ANGL. DEV. =  11.0 DEGREES          
REMARK 500    ARG A   8   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.1 DEGREES          
REMARK 500    ARG A   8   NE  -  CZ  -  NH2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    GLN A   9   CA  -  CB  -  CG  ANGL. DEV. = -15.2 DEGREES          
REMARK 500    GLN A   9   CB  -  CG  -  CD  ANGL. DEV. =  17.8 DEGREES          
REMARK 500    GLY A  23   O   -  C   -  N   ANGL. DEV. =  10.6 DEGREES          
REMARK 500    VAL A  32   CA  -  CB  -  CG2 ANGL. DEV. =  12.1 DEGREES          
REMARK 500    GLU A  35   OE1 -  CD  -  OE2 ANGL. DEV. =   8.5 DEGREES          
REMARK 500    ARG A  41   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    LEU A  45   CB  -  CG  -  CD2 ANGL. DEV. = -11.1 DEGREES          
REMARK 500    TYR A  48   CB  -  CG  -  CD1 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    GLU A  52   OE1 -  CD  -  OE2 ANGL. DEV. =   8.8 DEGREES          
REMARK 500    ARG A  58   CB  -  CG  -  CD  ANGL. DEV. =  15.7 DEGREES          
REMARK 500    ARG A  59   CB  -  CG  -  CD  ANGL. DEV. =  17.4 DEGREES          
REMARK 500    ARG A  59   CG  -  CD  -  NE  ANGL. DEV. =  13.3 DEGREES          
REMARK 500    TYR A  61   CB  -  CG  -  CD1 ANGL. DEV. =  -5.3 DEGREES          
REMARK 500    TYR A  67   CB  -  CG  -  CD2 ANGL. DEV. =  -7.2 DEGREES          
REMARK 500    TYR A  82   CB  -  CG  -  CD1 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    ARG A  83   NH1 -  CZ  -  NH2 ANGL. DEV. =   7.2 DEGREES          
REMARK 500    ARG A  83   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    ASN A  84   CA  -  CB  -  CG  ANGL. DEV. = -16.7 DEGREES          
REMARK 500    TYR A  88   CB  -  CG  -  CD1 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    GLU A  89   OE1 -  CD  -  OE2 ANGL. DEV. =   8.2 DEGREES          
REMARK 500    ARG A  93   CA  -  CB  -  CG  ANGL. DEV. =  14.2 DEGREES          
REMARK 500    TYR A  94   CA  -  CB  -  CG  ANGL. DEV. = -12.7 DEGREES          
REMARK 500    CYS A  95   CA  -  CB  -  SG  ANGL. DEV. =   6.9 DEGREES          
REMARK 500    ARG A  98   CD  -  NE  -  CZ  ANGL. DEV. =   9.4 DEGREES          
REMARK 500    GLU A  99   CG  -  CD  -  OE1 ANGL. DEV. = -16.2 DEGREES          
REMARK 500    ASP A 108   CA  -  CB  -  CG  ANGL. DEV. = -14.3 DEGREES          
REMARK 500    ASP A 108   CB  -  CG  -  OD1 ANGL. DEV. =  12.2 DEGREES          
REMARK 500    ASP A 108   CB  -  CG  -  OD2 ANGL. DEV. =  -6.4 DEGREES          
REMARK 500    VAL A 110   CA  -  CB  -  CG1 ANGL. DEV. =   9.8 DEGREES          
REMARK 500    ARG A 111   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    GLN A 142   CA  -  CB  -  CG  ANGL. DEV. = -13.8 DEGREES          
REMARK 500    ARG A 145   CD  -  NE  -  CZ  ANGL. DEV. =  13.7 DEGREES          
REMARK 500    ARG A 145   NH1 -  CZ  -  NH2 ANGL. DEV. =   8.7 DEGREES          
REMARK 500    ARG A 145   NE  -  CZ  -  NH1 ANGL. DEV. =  -7.6 DEGREES          
REMARK 500    PHE A 149   CB  -  CG  -  CD1 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ASN A 155   CA  -  CB  -  CG  ANGL. DEV. =  15.7 DEGREES          
REMARK 500    TYR A 166   CB  -  CG  -  CD2 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    TYR A 166   CB  -  CG  -  CD1 ANGL. DEV. =  -8.5 DEGREES          
REMARK 500    ASN A 169   CB  -  CG  -  OD1 ANGL. DEV. =  14.7 DEGREES          
REMARK 500    TYR A 170   CB  -  CG  -  CD1 ANGL. DEV. =  -6.8 DEGREES          
REMARK 500    GLU A 183   OE1 -  CD  -  OE2 ANGL. DEV. =  14.3 DEGREES          
REMARK 500    TYR A 186   CB  -  CG  -  CD1 ANGL. DEV. =  -4.7 DEGREES          
REMARK 500    TYR A 186   CG  -  CD1 -  CE1 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    ARG A 188   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    VAL A 199   CA  -  CB  -  CG2 ANGL. DEV. =  10.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PRO A  15      156.49    -47.68                                   
REMARK 500    SER A  21       52.05    -94.68                                   
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 111         0.11    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    ARG A  58        -13.52                                           
REMARK 500    ARG A  59         10.44                                           
REMARK 500    CYS A 200        -10.43                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: ACT                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MOH A 214                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MOH A 215                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MOH A 216                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MOH A 217                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MOH A 218                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MOH A 219                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MOH A 220                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MOH A 221                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MOH A 222                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MOH A 223                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MOH A 224                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MOH A 225                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MOH A 227                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MOH A 228                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MOH A 229                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MOH A 230                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MOH A 231                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MOH A 232                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MOH A 233                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MOH A 234                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MOH A 235                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MOH A 236                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MOH A 237                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MOH A 238                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MOH A 239                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MOH A 240                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MOH A 241                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MOH A 242                 
DBREF  9PAP A    1   212  UNP    P00784   PAPA_CARPA     134    345             
SEQADV 9PAP GLN A   47  UNP  P00784    GLU   180 CONFLICT                       
SEQADV 9PAP GLN A  118  UNP  P00784    GLU   251 CONFLICT                       
SEQADV 9PAP GLN A  135  UNP  P00784    GLU   268 CONFLICT                       
SEQRES   1 A  212  ILE PRO GLU TYR VAL ASP TRP ARG GLN LYS GLY ALA VAL          
SEQRES   2 A  212  THR PRO VAL LYS ASN GLN GLY SER CYS GLY SER OCS TRP          
SEQRES   3 A  212  ALA PHE SER ALA VAL VAL THR ILE GLU GLY ILE ILE LYS          
SEQRES   4 A  212  ILE ARG THR GLY ASN LEU ASN GLN TYR SER GLU GLN GLU          
SEQRES   5 A  212  LEU LEU ASP CYS ASP ARG ARG SER TYR GLY CYS ASN GLY          
SEQRES   6 A  212  GLY TYR PRO TRP SER ALA LEU GLN LEU VAL ALA GLN TYR          
SEQRES   7 A  212  GLY ILE HIS TYR ARG ASN THR TYR PRO TYR GLU GLY VAL          
SEQRES   8 A  212  GLN ARG TYR CYS ARG SER ARG GLU LYS GLY PRO TYR ALA          
SEQRES   9 A  212  ALA LYS THR ASP GLY VAL ARG GLN VAL GLN PRO TYR ASN          
SEQRES  10 A  212  GLN GLY ALA LEU LEU TYR SER ILE ALA ASN GLN PRO VAL          
SEQRES  11 A  212  SER VAL VAL LEU GLN ALA ALA GLY LYS ASP PHE GLN LEU          
SEQRES  12 A  212  TYR ARG GLY GLY ILE PHE VAL GLY PRO CYS GLY ASN LYS          
SEQRES  13 A  212  VAL ASP HIS ALA VAL ALA ALA VAL GLY TYR GLY PRO ASN          
SEQRES  14 A  212  TYR ILE LEU ILE LYS ASN SER TRP GLY THR GLY TRP GLY          
SEQRES  15 A  212  GLU ASN GLY TYR ILE ARG ILE LYS ARG GLY THR GLY ASN          
SEQRES  16 A  212  SER TYR GLY VAL CYS GLY LEU TYR THR SER SER PHE TYR          
SEQRES  17 A  212  PRO VAL LYS ASN                                              
MODRES 9PAP OCS A   25  CYS  CYSTEINESULFONIC ACID                              
HET    OCS  A  25       9                                                       
HET    MOH  A 214       2                                                       
HET    MOH  A 215       2                                                       
HET    MOH  A 216       2                                                       
HET    MOH  A 217       2                                                       
HET    MOH  A 218       2                                                       
HET    MOH  A 219       2                                                       
HET    MOH  A 220       2                                                       
HET    MOH  A 221       2                                                       
HET    MOH  A 222       2                                                       
HET    MOH  A 223       2                                                       
HET    MOH  A 224       2                                                       
HET    MOH  A 225       2                                                       
HET    MOH  A 226       2                                                       
HET    MOH  A 227       2                                                       
HET    MOH  A 228       2                                                       
HET    MOH  A 229       2                                                       
HET    MOH  A 230       2                                                       
HET    MOH  A 231       2                                                       
HET    MOH  A 232       2                                                       
HET    MOH  A 233       2                                                       
HET    MOH  A 234       2                                                       
HET    MOH  A 235       2                                                       
HET    MOH  A 236       2                                                       
HET    MOH  A 237       2                                                       
HET    MOH  A 238       2                                                       
HET    MOH  A 239       2                                                       
HET    MOH  A 240       2                                                       
HET    MOH  A 241       2                                                       
HET    MOH  A 242       2                                                       
HETNAM     OCS CYSTEINESULFONIC ACID                                            
HETNAM     MOH METHANOL                                                         
FORMUL   1  OCS    C3 H7 N O5 S                                                 
FORMUL   2  MOH    29(C H4 O)                                                   
FORMUL  31  HOH   *195(H2 O)                                                    
HELIX    1  L1 SER A   24  GLY A   43  1DISRUPTION IN THE CENTER          20    
HELIX    2  L2 GLU A   50  ASP A   57  1                                   8    
HELIX    3  L3 TYR A   67  TYR A   78  1                                  12    
HELIX    4  R1 ASN A  117  GLN A  128  1                                  12    
HELIX    5  R2 GLY A  138  LEU A  143  1                                   6    
SHEET    1  S1 4 VAL A   5  TRP A   7  0                                        
SHEET    2  S1 4 VAL A 164  GLY A 167 -1  O  TYR A 166   N  VAL A   5           
SHEET    3  S1 4 TYR A 170  ASN A 175 -1  O  LEU A 172   N  VAL A 164           
SHEET    4  S1 4 GLY A 185  ARG A 191 -1  O  ILE A 187   N  ILE A 173           
SHEET    1  S2 4 ASP A 108  VAL A 113  0                                        
SHEET    2  S2 4 SER A 206  VAL A 210 -1  O  TYR A 208   N  ARG A 111           
SHEET    3  S2 4 VAL A 130  LEU A 134 -1  O  SER A 131   N  PHE A 207           
SHEET    4  S2 4 ASP A 158  ALA A 163 -1  O  VAL A 161   N  VAL A 132           
SSBOND   1 CYS A   22    CYS A   63                          1555   1555  2.08  
SSBOND   2 CYS A   56    CYS A   95                          1555   1555  2.07  
SSBOND   3 CYS A  153    CYS A  200                          1555   1555  2.05  
LINK         C   SER A  24                 N   OCS A  25     1555   1555  1.31  
LINK         C   OCS A  25                 N   TRP A  26     1555   1555  1.28  
CISPEP   1 GLY A  151    PRO A  152          0         2.09                     
SITE     1 ACT  2 HIS A 159  ASN A 175                                          
SITE     1 AC1  4 TYR A  78  LYS A 106  HOH A 341  HOH A 432                    
SITE     1 AC2  3 LEU A 143  ARG A 145  GLY A 146                               
SITE     1 AC3  2 ILE A  40  ARG A  41                                          
SITE     1 AC4  2 ALA A 126  ASN A 127                                          
SITE     1 AC5  3 SER A  97  GLY A 101  TYR A 103                               
SITE     1 AC6  5 CYS A 153  GLY A 154  CYS A 200  HOH A 299                    
SITE     2 AC6  5 HOH A 413                                                     
SITE     1 AC7  3 SER A 124  ASN A 127  GLN A 128                               
SITE     1 AC8  3 OCS A  25  GLY A  65  GLY A  66                               
SITE     1 AC9  1 HOH A 383                                                     
SITE     1 BC1  2 ARG A 145  GLY A 194                                          
SITE     1 BC2  3 ARG A 111  GLN A 112  HOH A 336                               
SITE     1 BC3  2 PRO A  68  HOH A 282                                          
SITE     1 BC4  1 HOH A 363                                                     
SITE     1 BC5  4 ASP A 140  GLY A 151  PRO A 152  HOH A 390                    
SITE     1 BC6  2 PRO A  15  HOH A 379                                          
SITE     1 BC7  3 GLY A  20  SER A  21  HOH A 414                               
SITE     1 BC8  1 TYR A  78                                                     
SITE     1 BC9  2 ASN A  18  GLY A  20                                          
SITE     1 CC1  3 ARG A 188  MOH A 235  HOH A 404                               
SITE     1 CC2  1 ASN A  64                                                     
SITE     1 CC3  4 GLY A 147  GLU A 183  ARG A 188  MOH A 233                    
SITE     1 CC4  1 TYR A 208                                                     
SITE     1 CC5  6 THR A  42  ASN A  44  ASN A  46  TYR A  82                    
SITE     2 CC5  6 HOH A 287  HOH A 328                                          
SITE     1 CC6  2 TYR A  82  HOH A 416                                          
SITE     1 CC7  5 ILE A  37  ARG A  41  ASN A 127  GLN A 128                    
SITE     2 CC7  5 HOH A 388                                                     
SITE     1 CC8  2 TYR A 116  SER A 196                                          
SITE     1 CC9  2 GLN A 142  HOH A 381                                          
SITE     1 DC1  3 ARG A  59  TYR A  61  TYR A  67                               
CRYST1   45.200  104.640   50.880  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.022124  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009557  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019654        0.00000                         
ATOM      1  N   ILE A   1      35.777  56.566  -4.248  1.00 27.36           N  
ATOM      2  CA  ILE A   1      36.362  57.401  -3.154  1.00 18.63           C  
ATOM      3  C   ILE A   1      37.586  56.660  -2.600  1.00 26.92           C  
ATOM      4  O   ILE A   1      37.724  55.421  -2.562  1.00 24.50           O  
ATOM      5  CB  ILE A   1      35.313  57.630  -2.080  1.00 13.60           C  
ATOM      6  CG1 ILE A   1      34.791  56.335  -1.379  1.00 16.35           C  
ATOM      7  CG2 ILE A   1      34.186  58.464  -2.701  1.00 15.83           C  
ATOM      8  CD1 ILE A   1      33.606  56.698  -0.492  1.00 10.98           C  
ATOM      9  N   PRO A   2      38.564  57.482  -2.182  1.00 21.14           N  
ATOM     10  CA  PRO A   2      39.810  57.032  -1.652  1.00 20.36           C  
ATOM     11  C   PRO A   2      39.558  56.197  -0.370  1.00 13.98           C  
ATOM     12  O   PRO A   2      38.561  56.333   0.372  1.00 13.68           O  
ATOM     13  CB  PRO A   2      40.585  58.275  -1.299  1.00 24.67           C  
ATOM     14  CG  PRO A   2      39.791  59.433  -1.786  1.00 18.03           C  
ATOM     15  CD  PRO A   2      38.369  58.931  -2.057  1.00 12.40           C  
ATOM     16  N   GLU A   3      40.632  55.472  -0.127  1.00 10.22           N  
ATOM     17  CA  GLU A   3      40.770  54.630   1.055  1.00 19.67           C  
ATOM     18  C   GLU A   3      40.948  55.426   2.354  1.00 21.18           C  
ATOM     19  O   GLU A   3      40.433  55.020   3.416  1.00 14.60           O  
ATOM     20  CB  GLU A   3      42.049  53.745   0.855  1.00 19.54           C  
ATOM     21  CG  GLU A   3      42.074  52.634   1.908  1.00  8.43           C  
ATOM     22  CD  GLU A   3      43.333  51.695   1.794  1.00 32.67           C  
ATOM     23  OE1 GLU A   3      44.160  52.240   1.035  1.00 29.56           O  
ATOM     24  OE2 GLU A   3      43.312  50.671   2.406  1.00 20.68           O  
ATOM     25  N   TYR A   4      41.694  56.563   2.189  1.00 13.38           N  
ATOM     26  CA  TYR A   4      41.967  57.533   3.235  1.00 14.45           C  
ATOM     27  C   TYR A   4      41.457  58.933   2.818  1.00 12.89           C  
ATOM     28  O   TYR A   4      41.815  59.430   1.718  1.00 12.74           O  
ATOM     29  CB  TYR A   4      43.545  57.646   3.534  1.00 15.37           C  
ATOM     30  CG  TYR A   4      44.051  56.438   4.319  1.00 22.91           C  
ATOM     31  CD1 TYR A   4      44.002  56.462   5.715  1.00 27.55           C  
ATOM     32  CD2 TYR A   4      44.546  55.317   3.658  1.00 33.04           C  
ATOM     33  CE1 TYR A   4      44.489  55.270   6.432  1.00 24.63           C  
ATOM     34  CE2 TYR A   4      45.029  54.151   4.333  1.00 14.58           C  
ATOM     35  CZ  TYR A   4      44.966  54.220   5.713  1.00 13.60           C  
ATOM     36  OH  TYR A   4      45.400  53.150   6.486  1.00 23.99           O  
ATOM     37  N   VAL A   5      40.772  59.646   3.732  1.00 11.75           N  
ATOM     38  CA  VAL A   5      40.482  61.062   3.472  1.00 12.05           C  
ATOM     39  C   VAL A   5      40.860  61.854   4.717  1.00 12.69           C  
ATOM     40  O   VAL A   5      40.524  61.390   5.797  1.00  9.66           O  
ATOM     41  CB  VAL A   5      39.044  61.273   3.037  1.00 11.57           C  
ATOM     42  CG1 VAL A   5      38.612  62.748   3.258  1.00 19.37           C  
ATOM     43  CG2 VAL A   5      38.752  60.861   1.566  1.00 11.69           C  
ATOM     44  N   ASP A   6      41.652  62.918   4.639  1.00 10.79           N  
ATOM     45  CA  ASP A   6      41.971  63.791   5.743  1.00  6.65           C  
ATOM     46  C   ASP A   6      41.908  65.238   5.259  1.00 11.42           C  
ATOM     47  O   ASP A   6      42.946  65.659   4.758  1.00  9.96           O  
ATOM     48  CB  ASP A   6      43.435  63.557   6.178  1.00  9.97           C  
ATOM     49  CG  ASP A   6      43.702  64.245   7.492  1.00 19.09           C  
ATOM     50  OD1 ASP A   6      43.108  65.266   7.788  1.00 14.00           O  
ATOM     51  OD2 ASP A   6      44.504  63.793   8.260  1.00 17.84           O  
ATOM     52  N   TRP A   7      40.851  65.989   5.537  1.00 10.30           N  
ATOM     53  CA  TRP A   7      40.741  67.366   5.117  1.00  9.60           C  
ATOM     54  C   TRP A   7      41.756  68.305   5.787  1.00  8.45           C  
ATOM     55  O   TRP A   7      41.979  69.404   5.259  1.00  8.84           O  
ATOM     56  CB  TRP A   7      39.280  67.841   5.351  1.00  7.06           C  
ATOM     57  CG  TRP A   7      38.344  67.166   4.307  1.00 12.95           C  
ATOM     58  CD1 TRP A   7      37.374  66.241   4.482  1.00  9.46           C  
ATOM     59  CD2 TRP A   7      38.385  67.452   2.924  1.00 11.25           C  
ATOM     60  NE1 TRP A   7      36.776  65.923   3.172  1.00  9.66           N  
ATOM     61  CE2 TRP A   7      37.398  66.657   2.293  1.00 14.00           C  
ATOM     62  CE3 TRP A   7      39.160  68.307   2.181  1.00 12.31           C  
ATOM     63  CZ2 TRP A   7      37.161  66.686   0.913  1.00 12.31           C  
ATOM     64  CZ3 TRP A   7      38.921  68.333   0.788  1.00  9.87           C  
ATOM     65  CH2 TRP A   7      37.961  67.543   0.208  1.00  4.94           C  
ATOM     66  N   ARG A   8      42.359  67.801   6.897  1.00 10.06           N  
ATOM     67  CA  ARG A   8      43.359  68.640   7.572  1.00 11.68           C  
ATOM     68  C   ARG A   8      44.622  68.695   6.671  1.00  7.18           C  
ATOM     69  O   ARG A   8      45.136  69.778   6.351  1.00 15.79           O  
ATOM     70  CB  ARG A   8      43.807  68.181   8.960  1.00 13.89           C  
ATOM     71  CG  ARG A   8      42.599  67.960   9.918  1.00 12.88           C  
ATOM     72  CD  ARG A   8      43.390  67.360  11.159  1.00 18.02           C  
ATOM     73  NE  ARG A   8      43.852  66.038  10.722  1.00 29.61           N  
ATOM     74  CZ  ARG A   8      44.275  65.035  11.486  1.00 33.59           C  
ATOM     75  NH1 ARG A   8      44.315  65.293  12.789  1.00 16.15           N  
ATOM     76  NH2 ARG A   8      44.789  63.895  11.060  1.00 18.67           N  
ATOM     77  N   GLN A   9      44.902  67.537   6.082  1.00 12.47           N  
ATOM     78  CA  GLN A   9      46.060  67.372   5.227  1.00 17.22           C  
ATOM     79  C   GLN A   9      45.830  68.172   3.971  1.00 16.10           C  
ATOM     80  O   GLN A   9      46.840  68.593   3.413  1.00 19.22           O  
ATOM     81  CB  GLN A   9      46.312  65.899   4.769  1.00 16.64           C  
ATOM     82  CG  GLN A   9      46.840  65.373   6.033  1.00 63.11           C  
ATOM     83  CD  GLN A   9      47.263  63.975   6.380  1.00 65.48           C  
ATOM     84  OE1 GLN A   9      47.186  63.036   5.502  1.00 60.52           O  
ATOM     85  NE2 GLN A   9      47.688  63.824   7.591  1.00 43.03           N  
ATOM     86  N   LYS A  10      44.603  68.293   3.518  1.00 11.48           N  
ATOM     87  CA  LYS A  10      44.282  69.013   2.307  1.00  8.64           C  
ATOM     88  C   LYS A  10      44.147  70.473   2.563  1.00 13.28           C  
ATOM     89  O   LYS A  10      44.026  71.178   1.542  1.00 14.81           O  
ATOM     90  CB  LYS A  10      43.069  68.378   1.638  1.00 19.10           C  
ATOM     91  CG  LYS A  10      43.467  67.164   0.817  1.00 25.71           C  
ATOM     92  CD  LYS A  10      42.362  66.152   0.574  1.00 49.16           C  
ATOM     93  CE  LYS A  10      41.989  65.204   1.691  1.00 61.87           C  
ATOM     94  NZ  LYS A  10      42.605  63.844   1.697  1.00 19.23           N  
ATOM     95  N   GLY A  11      44.378  70.969   3.775  1.00  7.26           N  
ATOM     96  CA  GLY A  11      44.337  72.395   4.060  1.00  7.35           C  
ATOM     97  C   GLY A  11      42.926  72.952   4.211  1.00 10.62           C  
ATOM     98  O   GLY A  11      42.807  74.230   4.077  1.00 13.31           O  
ATOM     99  N   ALA A  12      41.923  72.132   4.537  1.00  7.81           N  
ATOM    100  CA  ALA A  12      40.514  72.597   4.603  1.00  5.19           C  
ATOM    101  C   ALA A  12      40.000  72.716   6.057  1.00  7.80           C  
ATOM    102  O   ALA A  12      38.785  72.851   6.238  1.00  9.18           O  
ATOM    103  CB  ALA A  12      39.526  71.694   3.812  1.00  6.99           C  
ATOM    104  N   VAL A  13      40.853  72.584   7.017  1.00  5.51           N  
ATOM    105  CA  VAL A  13      40.502  72.565   8.462  1.00  9.31           C  
ATOM    106  C   VAL A  13      41.383  73.450   9.314  1.00  2.03           C  
ATOM    107  O   VAL A  13      42.584  73.546   9.140  1.00  8.32           O  
ATOM    108  CB  VAL A  13      40.563  71.104   8.984  1.00  4.10           C  
ATOM    109  CG1 VAL A  13      40.040  71.015  10.490  1.00  9.07           C  
ATOM    110  CG2 VAL A  13      39.965  70.048   8.155  1.00 12.20           C  
ATOM    111  N   THR A  14      40.717  74.341  10.067  1.00  5.83           N  
ATOM    112  CA  THR A  14      41.366  75.304  10.969  1.00  2.66           C  
ATOM    113  C   THR A  14      41.658  74.678  12.324  1.00 10.98           C  
ATOM    114  O   THR A  14      41.133  73.577  12.603  1.00  9.32           O  
ATOM    115  CB  THR A  14      40.488  76.569  10.984  1.00  5.28           C  
ATOM    116  OG1 THR A  14      39.358  76.203  11.799  1.00  9.44           O  
ATOM    117  CG2 THR A  14      40.058  77.069   9.648  1.00  8.98           C  
ATOM    118  N   PRO A  15      42.479  75.348  13.114  1.00  9.61           N  
ATOM    119  CA  PRO A  15      42.899  74.904  14.480  1.00  7.60           C  
ATOM    120  C   PRO A  15      41.686  74.475  15.276  1.00  9.92           C  
ATOM    121  O   PRO A  15      40.527  74.942  15.169  1.00  9.23           O  
ATOM    122  CB  PRO A  15      43.581  76.132  15.045  1.00 14.51           C  
ATOM    123  CG  PRO A  15      44.286  76.643  13.805  1.00  9.95           C  
ATOM    124  CD  PRO A  15      43.111  76.662  12.807  1.00  8.75           C  
ATOM    125  N   VAL A  16      41.948  73.640  16.258  1.00  8.44           N  
ATOM    126  CA  VAL A  16      40.888  73.066  17.133  1.00 15.90           C  
ATOM    127  C   VAL A  16      40.448  74.178  18.055  1.00 10.96           C  
ATOM    128  O   VAL A  16      41.375  74.893  18.547  1.00 10.81           O  
ATOM    129  CB  VAL A  16      41.543  71.860  17.851  1.00 11.85           C  
ATOM    130  CG1 VAL A  16      40.968  71.645  19.201  1.00 12.21           C  
ATOM    131  CG2 VAL A  16      41.473  70.587  16.949  1.00  8.46           C  
ATOM    132  N   LYS A  17      39.159  74.292  18.413  1.00  8.36           N  
ATOM    133  CA  LYS A  17      38.681  75.313  19.351  1.00  5.82           C  
ATOM    134  C   LYS A  17      38.155  74.617  20.615  1.00  7.46           C  
ATOM    135  O   LYS A  17      37.893  73.446  20.578  1.00  7.85           O  
ATOM    136  CB  LYS A  17      37.580  76.217  18.843  1.00 11.80           C  
ATOM    137  CG  LYS A  17      37.675  76.644  17.392  1.00 14.31           C  
ATOM    138  CD  LYS A  17      38.964  77.225  17.046  1.00 14.06           C  
ATOM    139  CE  LYS A  17      39.066  78.044  15.794  1.00  6.30           C  
ATOM    140  NZ  LYS A  17      39.049  77.376  14.473  1.00 10.43           N  
ATOM    141  N   ASN A  18      37.913  75.431  21.634  1.00 14.72           N  
ATOM    142  CA  ASN A  18      37.294  74.991  22.912  1.00 10.27           C  
ATOM    143  C   ASN A  18      36.007  75.755  23.158  1.00  8.74           C  
ATOM    144  O   ASN A  18      36.029  77.063  23.142  1.00 17.04           O  
ATOM    145  CB  ASN A  18      38.351  75.286  24.014  1.00 10.44           C  
ATOM    146  CG  ASN A  18      37.869  74.603  25.285  1.00 14.25           C  
ATOM    147  OD1 ASN A  18      36.719  74.205  25.399  1.00 12.36           O  
ATOM    148  ND2 ASN A  18      38.784  74.460  26.278  1.00 21.59           N  
ATOM    149  N   GLN A  19      34.838  75.110  23.256  1.00  6.16           N  
ATOM    150  CA  GLN A  19      33.575  75.807  23.358  1.00  6.64           C  
ATOM    151  C   GLN A  19      33.431  76.299  24.846  1.00  8.64           C  
ATOM    152  O   GLN A  19      32.554  77.127  25.084  1.00 11.00           O  
ATOM    153  CB  GLN A  19      32.386  74.933  23.104  1.00 10.30           C  
ATOM    154  CG  GLN A  19      32.307  73.728  23.957  1.00 11.36           C  
ATOM    155  CD  GLN A  19      31.241  72.724  23.468  1.00 11.12           C  
ATOM    156  OE1 GLN A  19      31.470  72.028  22.433  1.00 14.03           O  
ATOM    157  NE2 GLN A  19      30.151  72.573  24.058  1.00 12.41           N  
ATOM    158  N   GLY A  20      34.256  75.685  25.675  1.00 16.41           N  
ATOM    159  CA  GLY A  20      34.238  76.074  27.125  1.00 11.26           C  
ATOM    160  C   GLY A  20      32.959  75.594  27.743  1.00 16.53           C  
ATOM    161  O   GLY A  20      32.464  74.515  27.301  1.00 20.66           O  
ATOM    162  N   SER A  21      32.407  76.299  28.727  1.00 22.43           N  
ATOM    163  CA  SER A  21      31.173  75.829  29.408  1.00 29.16           C  
ATOM    164  C   SER A  21      29.860  76.385  28.868  1.00 32.58           C  
ATOM    165  O   SER A  21      29.019  76.954  29.605  1.00 53.86           O  
ATOM    166  CB  SER A  21      31.309  76.220  30.872  1.00 22.05           C  
ATOM    167  OG  SER A  21      32.185  77.340  30.934  1.00 63.06           O  
ATOM    168  N   CYS A  22      29.664  76.272  27.581  1.00 11.60           N  
ATOM    169  CA  CYS A  22      28.518  76.841  26.880  1.00  4.52           C  
ATOM    170  C   CYS A  22      28.232  75.702  25.897  1.00  8.91           C  
ATOM    171  O   CYS A  22      29.250  75.170  25.465  1.00 13.72           O  
ATOM    172  CB  CYS A  22      28.922  78.106  26.237  1.00 18.10           C  
ATOM    173  SG  CYS A  22      27.709  78.666  24.932  1.00 14.04           S  
ATOM    174  N   GLY A  23      27.021  75.307  25.781  1.00  4.59           N  
ATOM    175  CA  GLY A  23      26.687  74.108  24.942  1.00 13.11           C  
ATOM    176  C   GLY A  23      26.385  74.697  23.511  1.00  7.82           C  
ATOM    177  O   GLY A  23      25.254  74.653  23.072  1.00 11.27           O  
ATOM    178  N   SER A  24      27.525  75.141  23.025  1.00 10.35           N  
ATOM    179  CA  SER A  24      27.622  75.774  21.726  1.00  7.80           C  
ATOM    180  C   SER A  24      28.194  74.863  20.638  1.00  5.05           C  
ATOM    181  O   SER A  24      28.305  75.318  19.496  1.00 11.85           O  
ATOM    182  CB  SER A  24      28.460  77.037  21.765  1.00 11.68           C  
ATOM    183  OG  SER A  24      29.782  76.847  22.238  1.00  9.19           O  
HETATM  184  N   OCS A  25      28.275  73.587  20.928  1.00  5.83           N  
HETATM  185  CA  OCS A  25      28.795  72.582  19.999  1.00  1.95           C  
HETATM  186  CB  OCS A  25      28.752  71.158  20.610  1.00 11.35           C  
HETATM  187  SG  OCS A  25      27.218  70.786  21.442  1.00 16.15           S  
HETATM  188  C   OCS A  25      28.113  72.682  18.650  1.00  4.66           C  
HETATM  189  O   OCS A  25      28.882  72.580  17.639  1.00 11.59           O  
HETATM  190  OD1 OCS A  25      27.433  71.478  22.772  1.00 14.24           O  
HETATM  191  OD2 OCS A  25      26.057  71.420  20.892  1.00 20.03           O  
HETATM  192  OD3 OCS A  25      27.128  69.383  21.436  1.00 25.97           O  
ATOM    193  N   TRP A  26      26.847  72.854  18.585  1.00  8.53           N  
ATOM    194  CA  TRP A  26      26.082  72.965  17.359  1.00  1.76           C  
ATOM    195  C   TRP A  26      26.652  74.015  16.413  1.00  8.69           C  
ATOM    196  O   TRP A  26      26.702  73.726  15.227  1.00  8.08           O  
ATOM    197  CB  TRP A  26      24.597  73.074  17.632  1.00  5.23           C  
ATOM    198  CG  TRP A  26      24.336  74.326  18.554  1.00  7.76           C  
ATOM    199  CD1 TRP A  26      24.427  74.429  19.898  1.00  5.95           C  
ATOM    200  CD2 TRP A  26      23.965  75.606  18.094  1.00  7.66           C  
ATOM    201  NE1 TRP A  26      24.097  75.798  20.258  1.00  6.71           N  
ATOM    202  CE2 TRP A  26      23.825  76.482  19.213  1.00  8.83           C  
ATOM    203  CE3 TRP A  26      23.734  76.075  16.791  1.00 11.30           C  
ATOM    204  CZ2 TRP A  26      23.476  77.784  19.107  1.00  7.53           C  
ATOM    205  CZ3 TRP A  26      23.371  77.420  16.710  1.00  4.69           C  
ATOM    206  CH2 TRP A  26      23.249  78.241  17.839  1.00  7.17           C  
ATOM    207  N   ALA A  27      27.162  75.137  16.911  1.00  7.97           N  
ATOM    208  CA  ALA A  27      27.613  76.305  16.212  1.00  8.05           C  
ATOM    209  C   ALA A  27      29.041  76.031  15.775  1.00  4.93           C  
ATOM    210  O   ALA A  27      29.391  76.243  14.588  1.00  5.29           O  
ATOM    211  CB  ALA A  27      27.688  77.527  17.158  1.00  7.27           C  
ATOM    212  N   PHE A  28      29.768  75.375  16.651  1.00  4.68           N  
ATOM    213  CA  PHE A  28      31.168  74.950  16.362  1.00  3.57           C  
ATOM    214  C   PHE A  28      31.173  73.956  15.210  1.00 11.91           C  
ATOM    215  O   PHE A  28      31.983  74.059  14.240  1.00 10.72           O  
ATOM    216  CB  PHE A  28      31.847  74.369  17.596  1.00  6.33           C  
ATOM    217  CG  PHE A  28      32.429  75.493  18.394  1.00 19.43           C  
ATOM    218  CD1 PHE A  28      31.670  76.129  19.370  1.00 12.15           C  
ATOM    219  CD2 PHE A  28      33.705  75.905  18.165  1.00 12.26           C  
ATOM    220  CE1 PHE A  28      32.299  77.212  20.105  1.00  6.44           C  
ATOM    221  CE2 PHE A  28      34.251  76.983  18.936  1.00 17.25           C  
ATOM    222  CZ  PHE A  28      33.587  77.620  19.886  1.00  3.71           C  
ATOM    223  N   SER A  29      30.272  73.029  15.311  1.00  5.86           N  
ATOM    224  CA  SER A  29      30.128  71.956  14.253  1.00  6.33           C  
ATOM    225  C   SER A  29      29.800  72.573  12.901  1.00 13.77           C  
ATOM    226  O   SER A  29      30.375  72.207  11.848  1.00  2.97           O  
ATOM    227  CB  SER A  29      28.966  71.095  14.820  1.00  9.55           C  
ATOM    228  OG  SER A  29      28.621  70.062  13.873  1.00 18.48           O  
ATOM    229  N   ALA A  30      28.793  73.422  12.811  1.00  7.28           N  
ATOM    230  CA  ALA A  30      28.328  74.063  11.608  1.00  8.85           C  
ATOM    231  C   ALA A  30      29.501  74.846  11.011  1.00 12.88           C  
ATOM    232  O   ALA A  30      29.804  74.785   9.752  1.00  5.47           O  
ATOM    233  CB  ALA A  30      27.172  74.993  11.982  1.00  5.93           C  
ATOM    234  N   VAL A  31      30.245  75.531  11.877  1.00  6.16           N  
ATOM    235  CA  VAL A  31      31.357  76.400  11.370  1.00 11.35           C  
ATOM    236  C   VAL A  31      32.460  75.552  10.734  1.00  5.27           C  
ATOM    237  O   VAL A  31      32.948  75.993   9.621  1.00  7.95           O  
ATOM    238  CB  VAL A  31      31.857  77.420  12.367  1.00  1.00           C  
ATOM    239  CG1 VAL A  31      33.249  78.010  12.165  1.00  1.46           C  
ATOM    240  CG2 VAL A  31      30.847  78.564  12.533  1.00  8.21           C  
ATOM    241  N   VAL A  32      32.770  74.364  11.267  1.00  4.62           N  
ATOM    242  CA  VAL A  32      33.802  73.574  10.556  1.00  5.93           C  
ATOM    243  C   VAL A  32      33.378  73.309   9.107  1.00  6.33           C  
ATOM    244  O   VAL A  32      34.276  73.299   8.242  1.00  9.34           O  
ATOM    245  CB  VAL A  32      34.409  72.424  11.343  1.00 12.11           C  
ATOM    246  CG1 VAL A  32      34.060  72.524  12.801  1.00 14.37           C  
ATOM    247  CG2 VAL A  32      34.707  71.058  10.726  1.00  9.34           C  
ATOM    248  N   THR A  33      32.123  72.956   8.829  1.00  5.23           N  
ATOM    249  CA  THR A  33      31.565  72.609   7.546  1.00  6.27           C  
ATOM    250  C   THR A  33      31.582  73.834   6.590  1.00 12.78           C  
ATOM    251  O   THR A  33      31.886  73.651   5.387  1.00  7.27           O  
ATOM    252  CB  THR A  33      30.194  71.994   7.638  1.00  5.60           C  
ATOM    253  OG1 THR A  33      29.289  73.032   7.930  1.00  9.10           O  
ATOM    254  CG2 THR A  33      30.125  70.875   8.645  1.00  2.81           C  
ATOM    255  N   ILE A  34      31.371  75.005   7.190  1.00  6.41           N  
ATOM    256  CA  ILE A  34      31.492  76.257   6.371  1.00  5.04           C  
ATOM    257  C   ILE A  34      32.936  76.574   6.002  1.00  7.56           C  
ATOM    258  O   ILE A  34      33.295  76.953   4.836  1.00  6.50           O  
ATOM    259  CB  ILE A  34      30.746  77.405   7.142  1.00  6.41           C  
ATOM    260  CG1 ILE A  34      29.222  77.057   7.195  1.00  8.73           C  
ATOM    261  CG2 ILE A  34      31.184  78.712   6.464  1.00  4.03           C  
ATOM    262  CD1 ILE A  34      28.393  77.730   8.263  1.00 35.20           C  
ATOM    263  N   GLU A  35      33.862  76.567   6.992  1.00  7.07           N  
ATOM    264  CA  GLU A  35      35.315  76.745   6.657  1.00  7.76           C  
ATOM    265  C   GLU A  35      35.811  75.783   5.583  1.00  8.02           C  
ATOM    266  O   GLU A  35      36.553  76.086   4.666  1.00 11.15           O  
ATOM    267  CB  GLU A  35      36.174  76.459   7.947  1.00  4.76           C  
ATOM    268  CG  GLU A  35      35.823  77.513   9.003  1.00  1.00           C  
ATOM    269  CD  GLU A  35      36.431  77.408  10.413  1.00  5.44           C  
ATOM    270  OE1 GLU A  35      36.827  76.246  10.651  1.00  8.99           O  
ATOM    271  OE2 GLU A  35      36.446  78.437  11.094  1.00  9.28           O  
ATOM    272  N   GLY A  36      35.370  74.492   5.690  1.00  3.94           N  
ATOM    273  CA  GLY A  36      35.654  73.447   4.737  1.00  2.24           C  
ATOM    274  C   GLY A  36      35.137  73.703   3.339  1.00  5.12           C  
ATOM    275  O   GLY A  36      35.931  73.543   2.417  1.00  7.17           O  
ATOM    276  N   ILE A  37      33.871  74.008   3.158  1.00  6.07           N  
ATOM    277  CA  ILE A  37      33.284  74.186   1.799  1.00  8.11           C  
ATOM    278  C   ILE A  37      33.773  75.482   1.158  1.00  8.12           C  
ATOM    279  O   ILE A  37      34.005  75.560  -0.094  1.00  6.17           O  
ATOM    280  CB  ILE A  37      31.743  74.004   1.815  1.00  9.62           C  
ATOM    281  CG1 ILE A  37      31.173  73.732   0.350  1.00  7.34           C  
ATOM    282  CG2 ILE A  37      31.097  75.262   2.429  1.00  4.09           C  
ATOM    283  CD1 ILE A  37      31.812  72.436  -0.267  1.00 11.03           C  
ATOM    284  N   ILE A  38      34.049  76.526   1.902  1.00  3.13           N  
ATOM    285  CA  ILE A  38      34.582  77.785   1.286  1.00 15.71           C  
ATOM    286  C   ILE A  38      35.994  77.453   0.788  1.00 13.95           C  
ATOM    287  O   ILE A  38      36.441  77.899  -0.315  1.00 12.69           O  
ATOM    288  CB  ILE A  38      34.535  78.946   2.287  1.00  9.76           C  
ATOM    289  CG1 ILE A  38      33.077  79.235   2.739  1.00 13.78           C  
ATOM    290  CG2 ILE A  38      35.149  80.170   1.647  1.00  6.27           C  
ATOM    291  CD1 ILE A  38      32.133  79.497   1.522  1.00 11.45           C  
ATOM    292  N   LYS A  39      36.748  76.704   1.645  1.00 10.74           N  
ATOM    293  CA  LYS A  39      38.127  76.362   1.161  1.00  4.26           C  
ATOM    294  C   LYS A  39      38.005  75.565  -0.132  1.00  8.78           C  
ATOM    295  O   LYS A  39      38.693  75.851  -1.111  1.00  8.56           O  
ATOM    296  CB  LYS A  39      38.945  75.732   2.251  1.00  5.99           C  
ATOM    297  CG  LYS A  39      40.187  75.045   1.752  1.00  8.69           C  
ATOM    298  CD  LYS A  39      41.185  76.046   1.136  1.00 16.76           C  
ATOM    299  CE  LYS A  39      42.337  75.300   0.414  1.00 13.60           C  
ATOM    300  NZ  LYS A  39      43.492  76.249   0.303  1.00  6.55           N  
ATOM    301  N   ILE A  40      37.172  74.508  -0.144  1.00  6.89           N  
ATOM    302  CA  ILE A  40      37.016  73.596  -1.310  1.00  5.98           C  
ATOM    303  C   ILE A  40      36.644  74.373  -2.563  1.00  9.72           C  
ATOM    304  O   ILE A  40      37.154  74.129  -3.698  1.00 11.81           O  
ATOM    305  CB  ILE A  40      36.020  72.432  -0.995  1.00  8.34           C  
ATOM    306  CG1 ILE A  40      36.589  71.418   0.008  1.00 14.22           C  
ATOM    307  CG2 ILE A  40      35.692  71.761  -2.338  1.00 12.14           C  
ATOM    308  CD1 ILE A  40      35.631  70.453   0.701  1.00 11.01           C  
ATOM    309  N   ARG A  41      35.612  75.261  -2.419  1.00 11.03           N  
ATOM    310  CA  ARG A  41      35.152  76.028  -3.561  1.00 10.04           C  
ATOM    311  C   ARG A  41      35.919  77.256  -3.955  1.00 19.82           C  
ATOM    312  O   ARG A  41      35.798  77.545  -5.189  1.00 20.45           O  
ATOM    313  CB  ARG A  41      33.658  76.408  -3.279  1.00  7.34           C  
ATOM    314  CG  ARG A  41      32.849  75.102  -3.240  1.00 18.70           C  
ATOM    315  CD  ARG A  41      32.310  74.974  -4.709  1.00 24.31           C  
ATOM    316  NE  ARG A  41      31.411  73.842  -4.531  1.00 27.05           N  
ATOM    317  CZ  ARG A  41      31.696  72.572  -4.765  1.00 36.08           C  
ATOM    318  NH1 ARG A  41      32.809  72.304  -5.479  1.00 40.63           N  
ATOM    319  NH2 ARG A  41      30.784  71.673  -4.413  1.00 39.07           N  
ATOM    320  N   THR A  42      36.623  77.991  -3.096  1.00 19.02           N  
ATOM    321  CA  THR A  42      37.287  79.252  -3.427  1.00  9.81           C  
ATOM    322  C   THR A  42      38.834  79.116  -3.447  1.00  6.85           C  
ATOM    323  O   THR A  42      39.506  80.015  -3.894  1.00 15.12           O  
ATOM    324  CB  THR A  42      36.877  80.407  -2.467  1.00  7.88           C  
ATOM    325  OG1 THR A  42      37.418  80.203  -1.163  1.00  9.39           O  
ATOM    326  CG2 THR A  42      35.324  80.398  -2.460  1.00 12.47           C  
ATOM    327  N   GLY A  43      39.271  78.094  -2.653  1.00  7.69           N  
ATOM    328  CA  GLY A  43      40.672  77.944  -2.347  1.00 10.46           C  
ATOM    329  C   GLY A  43      41.070  78.682  -1.086  1.00  8.03           C  
ATOM    330  O   GLY A  43      42.288  78.659  -0.803  1.00  9.88           O  
ATOM    331  N   ASN A  44      40.188  79.493  -0.491  1.00  9.87           N  
ATOM    332  CA  ASN A  44      40.676  80.378   0.631  1.00  8.72           C  
ATOM    333  C   ASN A  44      40.333  79.649   1.985  1.00 12.46           C  
ATOM    334  O   ASN A  44      39.122  79.360   2.101  1.00  8.55           O  
ATOM    335  CB  ASN A  44      40.005  81.741   0.657  1.00 15.69           C  
ATOM    336  CG  ASN A  44      40.441  82.641  -0.506  1.00 16.88           C  
ATOM    337  OD1 ASN A  44      39.629  83.254  -1.136  1.00 19.07           O  
ATOM    338  ND2 ASN A  44      41.739  82.715  -0.789  1.00 11.27           N  
ATOM    339  N   LEU A  45      41.302  79.585   2.899  1.00  9.16           N  
ATOM    340  CA  LEU A  45      40.982  79.008   4.216  1.00 12.54           C  
ATOM    341  C   LEU A  45      40.770  80.135   5.225  1.00 13.58           C  
ATOM    342  O   LEU A  45      41.766  80.870   5.449  1.00 13.24           O  
ATOM    343  CB  LEU A  45      42.077  78.105   4.778  1.00 12.36           C  
ATOM    344  CG  LEU A  45      41.733  77.356   6.096  1.00 10.54           C  
ATOM    345  CD1 LEU A  45      40.640  76.363   5.951  1.00 11.95           C  
ATOM    346  CD2 LEU A  45      43.094  76.679   6.381  1.00 19.16           C  
ATOM    347  N   ASN A  46      39.523  80.245   5.717  1.00  6.89           N  
ATOM    348  CA  ASN A  46      39.227  81.364   6.673  1.00  5.12           C  
ATOM    349  C   ASN A  46      38.656  80.772   7.951  1.00 10.00           C  
ATOM    350  O   ASN A  46      38.149  79.650   7.841  1.00 11.19           O  
ATOM    351  CB  ASN A  46      38.207  82.333   6.089  1.00  9.02           C  
ATOM    352  CG  ASN A  46      38.552  82.865   4.715  1.00 11.52           C  
ATOM    353  OD1 ASN A  46      37.972  82.675   3.672  1.00 19.77           O  
ATOM    354  ND2 ASN A  46      39.668  83.633   4.796  1.00  9.43           N  
ATOM    355  N   GLN A  47      38.606  81.500   9.084  1.00  9.49           N  
ATOM    356  CA  GLN A  47      37.786  81.042  10.207  1.00  5.96           C  
ATOM    357  C   GLN A  47      36.547  81.953  10.229  1.00  8.08           C  
ATOM    358  O   GLN A  47      36.641  83.190  10.007  1.00  9.44           O  
ATOM    359  CB  GLN A  47      38.473  81.149  11.536  1.00  3.43           C  
ATOM    360  CG  GLN A  47      39.652  80.288  11.578  1.00  8.24           C  
ATOM    361  CD  GLN A  47      40.536  80.461  12.825  1.00 22.27           C  
ATOM    362  OE1 GLN A  47      41.071  79.487  13.397  1.00 11.46           O  
ATOM    363  NE2 GLN A  47      40.690  81.645  13.239  1.00 17.57           N  
ATOM    364  N   TYR A  48      35.403  81.274  10.538  1.00 12.37           N  
ATOM    365  CA  TYR A  48      34.106  81.952  10.672  1.00  9.65           C  
ATOM    366  C   TYR A  48      33.538  81.865  12.099  1.00  4.19           C  
ATOM    367  O   TYR A  48      34.031  81.091  12.952  1.00  8.14           O  
ATOM    368  CB  TYR A  48      33.162  81.290   9.669  1.00  8.88           C  
ATOM    369  CG  TYR A  48      33.647  81.651   8.248  1.00  6.27           C  
ATOM    370  CD1 TYR A  48      34.127  80.577   7.484  1.00  4.48           C  
ATOM    371  CD2 TYR A  48      33.593  82.974   7.780  1.00  9.11           C  
ATOM    372  CE1 TYR A  48      34.589  80.855   6.151  1.00 14.57           C  
ATOM    373  CE2 TYR A  48      34.058  83.228   6.457  1.00 12.94           C  
ATOM    374  CZ  TYR A  48      34.539  82.138   5.713  1.00 14.49           C  
ATOM    375  OH  TYR A  48      35.005  82.341   4.410  1.00 12.04           O  
ATOM    376  N   SER A  49      32.485  82.708  12.281  1.00 10.10           N  
ATOM    377  CA  SER A  49      32.032  82.996  13.672  1.00  5.90           C  
ATOM    378  C   SER A  49      31.006  82.038  14.200  1.00  2.72           C  
ATOM    379  O   SER A  49      29.776  82.095  13.901  1.00 10.39           O  
ATOM    380  CB  SER A  49      31.596  84.444  13.727  1.00  7.98           C  
ATOM    381  OG  SER A  49      31.133  84.797  15.017  1.00  9.53           O  
ATOM    382  N   GLU A  50      31.484  81.352  15.310  1.00  8.71           N  
ATOM    383  CA  GLU A  50      30.536  80.526  16.112  1.00 13.43           C  
ATOM    384  C   GLU A  50      29.590  81.427  16.965  1.00  4.39           C  
ATOM    385  O   GLU A  50      28.410  81.074  17.124  1.00  6.99           O  
ATOM    386  CB  GLU A  50      31.260  79.554  17.084  1.00  7.58           C  
ATOM    387  CG  GLU A  50      32.202  78.553  16.344  1.00 12.28           C  
ATOM    388  CD  GLU A  50      33.697  78.976  16.093  1.00 17.90           C  
ATOM    389  OE1 GLU A  50      33.934  80.131  16.451  1.00 10.79           O  
ATOM    390  OE2 GLU A  50      34.428  78.162  15.589  1.00 12.25           O  
ATOM    391  N   GLN A  51      30.144  82.540  17.433  1.00  9.06           N  
ATOM    392  CA  GLN A  51      29.494  83.422  18.372  1.00  9.66           C  
ATOM    393  C   GLN A  51      28.291  83.954  17.620  1.00 11.40           C  
ATOM    394  O   GLN A  51      27.168  84.011  18.174  1.00  8.32           O  
ATOM    395  CB  GLN A  51      30.341  84.552  18.859  1.00  9.17           C  
ATOM    396  CG  GLN A  51      29.563  85.402  19.861  1.00  7.39           C  
ATOM    397  CD  GLN A  51      29.375  84.804  21.281  1.00  8.02           C  
ATOM    398  OE1 GLN A  51      30.264  84.051  21.678  1.00  8.84           O  
ATOM    399  NE2 GLN A  51      28.323  85.125  21.936  1.00  7.83           N  
ATOM    400  N   GLU A  52      28.519  84.204  16.305  1.00 12.18           N  
ATOM    401  CA  GLU A  52      27.425  84.766  15.490  1.00 12.42           C  
ATOM    402  C   GLU A  52      26.205  83.908  15.368  1.00  8.25           C  
ATOM    403  O   GLU A  52      25.032  84.321  15.521  1.00 10.28           O  
ATOM    404  CB  GLU A  52      27.988  85.136  14.090  1.00  9.58           C  
ATOM    405  CG  GLU A  52      26.858  85.767  13.177  1.00 20.45           C  
ATOM    406  CD  GLU A  52      27.546  86.532  11.974  1.00  9.93           C  
ATOM    407  OE1 GLU A  52      28.626  86.061  11.669  1.00 16.85           O  
ATOM    408  OE2 GLU A  52      26.933  87.441  11.548  1.00 18.84           O  
ATOM    409  N   LEU A  53      26.426  82.580  15.282  1.00  5.00           N  
ATOM    410  CA  LEU A  53      25.317  81.635  15.254  1.00  8.30           C  
ATOM    411  C   LEU A  53      24.651  81.518  16.610  1.00  4.84           C  
ATOM    412  O   LEU A  53      23.391  81.390  16.642  1.00 14.43           O  
ATOM    413  CB  LEU A  53      25.780  80.309  14.722  1.00  9.16           C  
ATOM    414  CG  LEU A  53      26.378  80.362  13.355  1.00 10.60           C  
ATOM    415  CD1 LEU A  53      27.108  79.036  13.175  1.00 13.97           C  
ATOM    416  CD2 LEU A  53      25.319  80.462  12.287  1.00 17.09           C  
ATOM    417  N   LEU A  54      25.467  81.455  17.642  1.00 10.03           N  
ATOM    418  CA  LEU A  54      25.037  81.465  19.044  1.00 20.10           C  
ATOM    419  C   LEU A  54      24.060  82.625  19.367  1.00  8.94           C  
ATOM    420  O   LEU A  54      22.973  82.403  19.897  1.00 17.22           O  
ATOM    421  CB  LEU A  54      26.191  81.644  20.059  1.00 17.14           C  
ATOM    422  CG  LEU A  54      26.402  80.718  21.213  1.00 25.57           C  
ATOM    423  CD1 LEU A  54      27.391  81.282  22.193  1.00 16.15           C  
ATOM    424  CD2 LEU A  54      25.103  80.361  21.827  1.00 16.52           C  
ATOM    425  N   ASP A  55      24.395  83.780  18.921  1.00  9.42           N  
ATOM    426  CA  ASP A  55      23.619  84.992  19.184  1.00 13.87           C  
ATOM    427  C   ASP A  55      22.341  84.980  18.346  1.00 25.96           C  
ATOM    428  O   ASP A  55      21.296  85.483  18.777  1.00 19.47           O  
ATOM    429  CB  ASP A  55      24.420  86.275  18.834  1.00 13.21           C  
ATOM    430  CG  ASP A  55      25.528  86.472  19.819  1.00 16.19           C  
ATOM    431  OD1 ASP A  55      25.635  85.816  20.894  1.00 15.03           O  
ATOM    432  OD2 ASP A  55      26.349  87.318  19.526  1.00  9.93           O  
ATOM    433  N   CYS A  56      22.498  84.545  17.087  1.00 11.58           N  
ATOM    434  CA  CYS A  56      21.526  84.793  16.056  1.00 13.79           C  
ATOM    435  C   CYS A  56      20.653  83.628  15.674  1.00 11.81           C  
ATOM    436  O   CYS A  56      19.594  83.968  15.035  1.00 15.99           O  
ATOM    437  CB  CYS A  56      22.134  85.366  14.782  1.00 17.62           C  
ATOM    438  SG  CYS A  56      23.298  86.769  15.079  1.00 14.96           S  
ATOM    439  N   ASP A  57      20.960  82.389  16.061  1.00  7.88           N  
ATOM    440  CA  ASP A  57      20.037  81.341  15.639  1.00 18.73           C  
ATOM    441  C   ASP A  57      18.976  81.262  16.715  1.00 18.83           C  
ATOM    442  O   ASP A  57      19.268  80.638  17.763  1.00 22.95           O  
ATOM    443  CB  ASP A  57      20.800  80.034  15.416  1.00 16.81           C  
ATOM    444  CG  ASP A  57      19.785  78.941  14.982  1.00 23.37           C  
ATOM    445  OD1 ASP A  57      18.614  79.225  14.793  1.00 12.27           O  
ATOM    446  OD2 ASP A  57      20.220  77.821  14.852  1.00 18.74           O  
ATOM    447  N   ARG A  58      17.807  81.775  16.436  1.00 19.09           N  
ATOM    448  CA  ARG A  58      16.771  81.739  17.515  1.00 34.18           C  
ATOM    449  C   ARG A  58      15.907  80.527  17.398  1.00 26.45           C  
ATOM    450  O   ARG A  58      15.200  80.234  18.385  1.00 27.68           O  
ATOM    451  CB  ARG A  58      16.144  83.113  17.798  1.00 21.18           C  
ATOM    452  CG  ARG A  58      17.145  84.114  18.402  1.00 42.88           C  
ATOM    453  CD  ARG A  58      17.798  84.045  19.749  1.00 28.89           C  
ATOM    454  NE  ARG A  58      18.756  85.134  20.048  1.00 66.36           N  
ATOM    455  CZ  ARG A  58      18.792  85.974  21.125  1.00 69.54           C  
ATOM    456  NH1 ARG A  58      17.834  85.883  22.072  1.00 47.60           N  
ATOM    457  NH2 ARG A  58      19.796  86.832  21.308  1.00 31.97           N  
ATOM    458  N   ARG A  59      16.190  79.548  16.547  1.00 14.68           N  
ATOM    459  CA  ARG A  59      15.577  78.213  16.538  1.00 21.68           C  
ATOM    460  C   ARG A  59      16.270  77.325  17.550  1.00 14.69           C  
ATOM    461  O   ARG A  59      15.835  76.221  17.800  1.00 22.29           O  
ATOM    462  CB  ARG A  59      15.781  77.473  15.184  1.00 19.54           C  
ATOM    463  CG  ARG A  59      14.647  77.231  14.270  1.00 27.67           C  
ATOM    464  CD  ARG A  59      14.622  77.257  12.813  1.00 46.78           C  
ATOM    465  NE  ARG A  59      15.744  77.583  11.972  1.00 34.09           N  
ATOM    466  CZ  ARG A  59      15.903  78.758  11.312  1.00 69.47           C  
ATOM    467  NH1 ARG A  59      14.880  79.646  11.273  1.00 69.54           N  
ATOM    468  NH2 ARG A  59      17.037  79.018  10.672  1.00 40.74           N  
ATOM    469  N   SER A  60      17.552  77.662  17.791  1.00 15.63           N  
ATOM    470  CA  SER A  60      18.486  76.929  18.674  1.00 14.97           C  
ATOM    471  C   SER A  60      18.366  77.561  20.073  1.00 13.53           C  
ATOM    472  O   SER A  60      17.711  78.642  20.247  1.00 11.70           O  
ATOM    473  CB  SER A  60      19.872  76.928  18.119  1.00  8.06           C  
ATOM    474  OG  SER A  60      20.097  76.129  16.968  1.00 11.39           O  
ATOM    475  N   TYR A  61      19.171  77.022  21.036  1.00 22.81           N  
ATOM    476  CA  TYR A  61      18.968  77.440  22.429  1.00 18.56           C  
ATOM    477  C   TYR A  61      20.157  78.025  23.101  1.00  8.80           C  
ATOM    478  O   TYR A  61      20.278  77.708  24.292  1.00 13.44           O  
ATOM    479  CB  TYR A  61      18.561  76.212  23.280  1.00 10.66           C  
ATOM    480  CG  TYR A  61      17.458  75.470  22.535  1.00 16.21           C  
ATOM    481  CD1 TYR A  61      16.235  76.139  22.440  1.00 17.07           C  
ATOM    482  CD2 TYR A  61      17.641  74.238  21.979  1.00 24.05           C  
ATOM    483  CE1 TYR A  61      15.142  75.491  21.739  1.00 25.69           C  
ATOM    484  CE2 TYR A  61      16.573  73.599  21.282  1.00 48.82           C  
ATOM    485  CZ  TYR A  61      15.347  74.274  21.199  1.00 54.47           C  
ATOM    486  OH  TYR A  61      14.280  73.688  20.537  1.00 42.44           O  
ATOM    487  N   GLY A  62      20.989  78.749  22.400  1.00 14.26           N  
ATOM    488  CA  GLY A  62      22.236  79.329  22.845  1.00 20.74           C  
ATOM    489  C   GLY A  62      23.171  78.321  23.494  1.00 14.10           C  
ATOM    490  O   GLY A  62      23.587  77.305  22.923  1.00 17.07           O  
ATOM    491  N   CYS A  63      23.528  78.681  24.732  1.00 14.58           N  
ATOM    492  CA  CYS A  63      24.441  77.845  25.545  1.00  6.78           C  
ATOM    493  C   CYS A  63      23.835  76.593  26.061  1.00  8.47           C  
ATOM    494  O   CYS A  63      24.540  75.725  26.636  1.00 19.17           O  
ATOM    495  CB  CYS A  63      24.976  78.654  26.745  1.00 12.89           C  
ATOM    496  SG  CYS A  63      26.326  79.714  26.085  1.00 16.60           S  
ATOM    497  N   ASN A  64      22.613  76.319  25.694  1.00 11.23           N  
ATOM    498  CA  ASN A  64      21.815  75.169  26.092  1.00 13.24           C  
ATOM    499  C   ASN A  64      21.609  74.235  24.925  1.00 15.77           C  
ATOM    500  O   ASN A  64      20.723  73.386  25.093  1.00 27.06           O  
ATOM    501  CB  ASN A  64      20.485  75.735  26.597  1.00 11.18           C  
ATOM    502  CG  ASN A  64      20.715  76.496  27.900  1.00 26.82           C  
ATOM    503  OD1 ASN A  64      20.604  77.713  28.000  1.00 33.73           O  
ATOM    504  ND2 ASN A  64      21.078  75.688  28.958  1.00 29.26           N  
ATOM    505  N   GLY A  65      22.472  74.293  23.903  1.00 22.56           N  
ATOM    506  CA  GLY A  65      22.265  73.332  22.795  1.00 14.95           C  
ATOM    507  C   GLY A  65      21.503  74.032  21.660  1.00  9.63           C  
ATOM    508  O   GLY A  65      21.015  75.167  21.756  1.00 17.24           O  
ATOM    509  N   GLY A  66      21.415  73.232  20.578  1.00  9.80           N  
ATOM    510  CA  GLY A  66      20.853  73.859  19.332  1.00  5.85           C  
ATOM    511  C   GLY A  66      21.092  72.898  18.197  1.00  5.70           C  
ATOM    512  O   GLY A  66      21.379  71.696  18.507  1.00 12.83           O  
ATOM    513  N   TYR A  67      20.816  73.376  16.996  1.00 11.75           N  
ATOM    514  CA  TYR A  67      20.762  72.420  15.820  1.00  8.13           C  
ATOM    515  C   TYR A  67      21.720  72.829  14.763  1.00 11.97           C  
ATOM    516  O   TYR A  67      21.602  73.964  14.217  1.00 12.85           O  
ATOM    517  CB  TYR A  67      19.339  72.423  15.266  1.00 10.46           C  
ATOM    518  CG  TYR A  67      18.203  72.295  16.281  1.00 11.19           C  
ATOM    519  CD1 TYR A  67      17.530  73.395  16.807  1.00 19.15           C  
ATOM    520  CD2 TYR A  67      17.913  70.998  16.628  1.00 11.65           C  
ATOM    521  CE1 TYR A  67      16.473  73.129  17.770  1.00 26.77           C  
ATOM    522  CE2 TYR A  67      16.879  70.712  17.572  1.00 23.71           C  
ATOM    523  CZ  TYR A  67      16.211  71.840  18.093  1.00 36.11           C  
ATOM    524  OH  TYR A  67      15.230  71.478  18.987  1.00 47.25           O  
ATOM    525  N   PRO A  68      22.629  71.902  14.376  1.00 13.90           N  
ATOM    526  CA  PRO A  68      23.648  72.259  13.336  1.00  9.09           C  
ATOM    527  C   PRO A  68      23.011  72.639  11.990  1.00  6.22           C  
ATOM    528  O   PRO A  68      23.329  73.649  11.340  1.00  9.48           O  
ATOM    529  CB  PRO A  68      24.501  71.045  13.263  1.00 15.71           C  
ATOM    530  CG  PRO A  68      24.414  70.414  14.627  1.00  8.46           C  
ATOM    531  CD  PRO A  68      22.931  70.582  15.031  1.00  8.06           C  
ATOM    532  N   TRP A  69      21.853  71.920  11.761  1.00 14.67           N  
ATOM    533  CA  TRP A  69      21.014  72.140  10.522  1.00  8.87           C  
ATOM    534  C   TRP A  69      20.295  73.484  10.525  1.00  5.41           C  
ATOM    535  O   TRP A  69      20.305  74.188   9.478  1.00 10.69           O  
ATOM    536  CB  TRP A  69      20.069  70.957  10.485  1.00 16.57           C  
ATOM    537  CG  TRP A  69      19.018  70.777  11.651  1.00 15.68           C  
ATOM    538  CD1 TRP A  69      18.984  69.919  12.668  1.00 17.12           C  
ATOM    539  CD2 TRP A  69      17.851  71.592  11.794  1.00 24.05           C  
ATOM    540  NE1 TRP A  69      17.779  70.181  13.472  1.00 18.96           N  
ATOM    541  CE2 TRP A  69      17.146  71.155  12.944  1.00 26.64           C  
ATOM    542  CE3 TRP A  69      17.358  72.649  11.048  1.00 51.95           C  
ATOM    543  CZ2 TRP A  69      15.942  71.730  13.401  1.00 40.91           C  
ATOM    544  CZ3 TRP A  69      16.153  73.244  11.478  1.00 23.45           C  
ATOM    545  CH2 TRP A  69      15.482  72.785  12.623  1.00 28.97           C  
ATOM    546  N   SER A  70      19.957  73.998  11.721  1.00  8.23           N  
ATOM    547  CA  SER A  70      19.358  75.342  11.800  1.00  4.05           C  
ATOM    548  C   SER A  70      20.416  76.389  11.570  1.00  6.11           C  
ATOM    549  O   SER A  70      20.264  77.415  10.875  1.00  8.85           O  
ATOM    550  CB  SER A  70      18.793  75.363  13.207  1.00 10.84           C  
ATOM    551  OG  SER A  70      18.384  76.647  13.409  1.00 23.05           O  
ATOM    552  N   ALA A  71      21.626  76.161  12.167  1.00 12.83           N  
ATOM    553  CA  ALA A  71      22.763  77.077  11.972  1.00  9.61           C  
ATOM    554  C   ALA A  71      23.212  77.170  10.497  1.00 18.92           C  
ATOM    555  O   ALA A  71      23.435  78.248   9.915  1.00 10.61           O  
ATOM    556  CB  ALA A  71      23.968  76.658  12.776  1.00  6.72           C  
ATOM    557  N   LEU A  72      23.158  76.034   9.832  1.00  7.92           N  
ATOM    558  CA  LEU A  72      23.572  75.907   8.404  1.00  7.69           C  
ATOM    559  C   LEU A  72      22.546  76.639   7.570  1.00 11.81           C  
ATOM    560  O   LEU A  72      22.876  77.332   6.604  1.00  9.28           O  
ATOM    561  CB  LEU A  72      23.751  74.423   8.029  1.00  6.10           C  
ATOM    562  CG  LEU A  72      25.005  73.645   8.441  1.00  6.25           C  
ATOM    563  CD1 LEU A  72      25.012  72.245   7.924  1.00  8.86           C  
ATOM    564  CD2 LEU A  72      26.207  74.412   8.007  1.00  9.64           C  
ATOM    565  N   GLN A  73      21.292  76.508   7.999  1.00  8.34           N  
ATOM    566  CA  GLN A  73      20.164  77.180   7.256  1.00 11.69           C  
ATOM    567  C   GLN A  73      20.305  78.685   7.327  1.00  7.25           C  
ATOM    568  O   GLN A  73      20.221  79.396   6.336  1.00  8.81           O  
ATOM    569  CB  GLN A  73      18.865  76.645   7.778  1.00  8.19           C  
ATOM    570  CG  GLN A  73      17.702  77.433   7.305  1.00 16.92           C  
ATOM    571  CD  GLN A  73      16.386  76.795   7.852  1.00 21.40           C  
ATOM    572  OE1 GLN A  73      15.456  77.668   7.986  1.00 35.24           O  
ATOM    573  NE2 GLN A  73      16.384  75.550   8.089  1.00 31.63           N  
ATOM    574  N   LEU A  74      20.740  79.191   8.505  1.00  7.54           N  
ATOM    575  CA  LEU A  74      20.977  80.608   8.757  1.00 12.78           C  
ATOM    576  C   LEU A  74      22.090  81.135   7.868  1.00 12.06           C  
ATOM    577  O   LEU A  74      21.889  82.286   7.414  1.00 13.61           O  
ATOM    578  CB  LEU A  74      21.408  80.871  10.199  1.00 12.29           C  
ATOM    579  CG  LEU A  74      20.708  81.775  11.159  1.00 41.81           C  
ATOM    580  CD1 LEU A  74      21.727  82.733  11.719  1.00 28.03           C  
ATOM    581  CD2 LEU A  74      19.506  82.497  10.594  1.00 19.04           C  
ATOM    582  N   VAL A  75      23.167  80.360   7.704  1.00  7.96           N  
ATOM    583  CA  VAL A  75      24.305  80.882   6.868  1.00  6.67           C  
ATOM    584  C   VAL A  75      23.936  80.939   5.363  1.00 13.19           C  
ATOM    585  O   VAL A  75      24.421  81.845   4.672  1.00 12.54           O  
ATOM    586  CB  VAL A  75      25.598  80.096   7.104  1.00 11.49           C  
ATOM    587  CG1 VAL A  75      26.751  80.460   6.200  1.00  6.22           C  
ATOM    588  CG2 VAL A  75      26.012  80.161   8.590  1.00 11.33           C  
ATOM    589  N   ALA A  76      23.025  80.029   4.975  1.00 15.10           N  
ATOM    590  CA  ALA A  76      22.390  80.046   3.616  1.00  8.51           C  
ATOM    591  C   ALA A  76      21.369  81.162   3.415  1.00  9.71           C  
ATOM    592  O   ALA A  76      21.217  81.729   2.303  1.00 11.71           O  
ATOM    593  CB  ALA A  76      21.704  78.720   3.339  1.00  7.70           C  
ATOM    594  N   GLN A  77      20.729  81.628   4.469  1.00 14.77           N  
ATOM    595  CA  GLN A  77      19.738  82.690   4.424  1.00 13.81           C  
ATOM    596  C   GLN A  77      20.437  84.029   4.492  1.00 13.99           C  
ATOM    597  O   GLN A  77      20.148  84.947   3.670  1.00 13.78           O  
ATOM    598  CB  GLN A  77      18.709  82.577   5.522  1.00 10.58           C  
ATOM    599  CG  GLN A  77      17.673  81.610   5.257  1.00 15.31           C  
ATOM    600  CD  GLN A  77      16.780  81.402   6.504  1.00 34.33           C  
ATOM    601  OE1 GLN A  77      17.327  81.478   7.642  1.00 31.09           O  
ATOM    602  NE2 GLN A  77      15.563  81.177   6.333  1.00 20.69           N  
ATOM    603  N   TYR A  78      21.276  84.172   5.486  1.00  7.72           N  
ATOM    604  CA  TYR A  78      21.915  85.471   5.720  1.00  6.79           C  
ATOM    605  C   TYR A  78      23.407  85.584   5.346  1.00 25.73           C  
ATOM    606  O   TYR A  78      23.870  86.595   4.758  1.00 44.74           O  
ATOM    607  CB  TYR A  78      21.741  85.822   7.225  1.00 15.79           C  
ATOM    608  CG  TYR A  78      20.261  86.026   7.509  1.00 19.09           C  
ATOM    609  CD1 TYR A  78      19.631  87.185   7.017  1.00 35.71           C  
ATOM    610  CD2 TYR A  78      19.583  85.092   8.235  1.00 51.55           C  
ATOM    611  CE1 TYR A  78      18.214  87.379   7.288  1.00 24.49           C  
ATOM    612  CE2 TYR A  78      18.186  85.267   8.513  1.00 31.02           C  
ATOM    613  CZ  TYR A  78      17.566  86.431   8.012  1.00 56.99           C  
ATOM    614  OH  TYR A  78      16.223  86.524   8.323  1.00 39.29           O  
ATOM    615  N   GLY A  79      24.189  84.670   5.893  1.00 13.25           N  
ATOM    616  CA  GLY A  79      25.597  84.526   5.739  1.00  9.77           C  
ATOM    617  C   GLY A  79      26.234  84.535   7.113  1.00  8.20           C  
ATOM    618  O   GLY A  79      25.503  84.405   8.113  1.00 11.30           O  
ATOM    619  N   ILE A  80      27.559  84.658   7.073  1.00 12.89           N  
ATOM    620  CA  ILE A  80      28.350  84.608   8.323  1.00 17.66           C  
ATOM    621  C   ILE A  80      29.508  85.569   8.239  1.00  9.55           C  
ATOM    622  O   ILE A  80      30.016  85.755   7.140  1.00  9.23           O  
ATOM    623  CB  ILE A  80      28.799  83.131   8.596  1.00 14.00           C  
ATOM    624  CG1 ILE A  80      29.278  83.013  10.098  1.00  7.04           C  
ATOM    625  CG2 ILE A  80      29.679  82.660   7.461  1.00  9.04           C  
ATOM    626  CD1 ILE A  80      29.156  81.512  10.500  1.00  8.39           C  
ATOM    627  N   HIS A  81      29.953  86.157   9.322  1.00  7.61           N  
ATOM    628  CA  HIS A  81      31.165  87.004   9.381  1.00  7.76           C  
ATOM    629  C   HIS A  81      32.392  86.144   9.688  1.00  9.14           C  
ATOM    630  O   HIS A  81      32.265  85.027  10.258  1.00 10.69           O  
ATOM    631  CB  HIS A  81      30.881  88.009  10.553  1.00 13.52           C  
ATOM    632  CG  HIS A  81      30.072  89.209  10.102  1.00 21.56           C  
ATOM    633  ND1 HIS A  81      28.781  89.432  10.478  1.00 16.03           N  
ATOM    634  CD2 HIS A  81      30.376  90.265   9.297  1.00 16.52           C  
ATOM    635  CE1 HIS A  81      28.324  90.551   9.945  1.00 15.42           C  
ATOM    636  NE2 HIS A  81      29.272  91.049   9.238  1.00 16.71           N  
ATOM    637  N   TYR A  82      33.629  86.674   9.475  1.00 10.80           N  
ATOM    638  CA  TYR A  82      34.875  86.107   9.956  1.00  9.59           C  
ATOM    639  C   TYR A  82      34.881  86.087  11.491  1.00 10.26           C  
ATOM    640  O   TYR A  82      34.244  86.927  12.214  1.00 10.87           O  
ATOM    641  CB  TYR A  82      36.156  86.916   9.584  1.00 12.35           C  
ATOM    642  CG  TYR A  82      36.395  86.931   8.069  1.00 12.72           C  
ATOM    643  CD1 TYR A  82      36.461  85.675   7.433  1.00 19.76           C  
ATOM    644  CD2 TYR A  82      36.546  88.074   7.339  1.00 25.36           C  
ATOM    645  CE1 TYR A  82      36.687  85.640   5.996  1.00 12.26           C  
ATOM    646  CE2 TYR A  82      36.763  88.056   5.927  1.00 12.59           C  
ATOM    647  CZ  TYR A  82      36.827  86.819   5.327  1.00 17.83           C  
ATOM    648  OH  TYR A  82      37.041  86.718   3.959  1.00 25.84           O  
ATOM    649  N   ARG A  83      35.587  85.052  11.980  1.00  8.85           N  
ATOM    650  CA  ARG A  83      35.694  84.801  13.408  1.00  8.21           C  
ATOM    651  C   ARG A  83      36.285  86.043  14.136  1.00 12.33           C  
ATOM    652  O   ARG A  83      35.941  86.358  15.265  1.00 17.85           O  
ATOM    653  CB  ARG A  83      36.553  83.588  13.745  1.00 10.68           C  
ATOM    654  CG  ARG A  83      36.340  83.159  15.208  1.00  9.15           C  
ATOM    655  CD  ARG A  83      36.976  81.746  15.307  1.00 17.02           C  
ATOM    656  NE  ARG A  83      36.408  80.987  16.439  1.00 16.97           N  
ATOM    657  CZ  ARG A  83      37.078  80.839  17.645  1.00 16.01           C  
ATOM    658  NH1 ARG A  83      38.384  81.224  17.715  1.00 14.99           N  
ATOM    659  NH2 ARG A  83      36.398  80.181  18.573  1.00 16.24           N  
ATOM    660  N   ASN A  84      37.262  86.630  13.507  1.00 12.91           N  
ATOM    661  CA  ASN A  84      37.982  87.831  13.804  1.00 17.09           C  
ATOM    662  C   ASN A  84      37.143  89.065  14.024  1.00 15.67           C  
ATOM    663  O   ASN A  84      37.390  89.903  14.954  1.00 20.09           O  
ATOM    664  CB  ASN A  84      38.583  88.175  12.324  1.00 43.55           C  
ATOM    665  CG  ASN A  84      40.019  88.396  12.763  1.00 63.15           C  
ATOM    666  OD1 ASN A  84      40.591  87.463  13.311  1.00 61.76           O  
ATOM    667  ND2 ASN A  84      40.494  89.669  12.487  1.00 73.25           N  
ATOM    668  N   THR A  85      36.085  89.133  13.187  1.00 11.64           N  
ATOM    669  CA  THR A  85      35.207  90.333  13.285  1.00  9.16           C  
ATOM    670  C   THR A  85      34.138  90.122  14.346  1.00 21.06           C  
ATOM    671  O   THR A  85      33.490  91.103  14.804  1.00 21.27           O  
ATOM    672  CB  THR A  85      34.630  90.580  11.852  1.00 15.80           C  
ATOM    673  OG1 THR A  85      33.695  89.544  11.741  1.00 42.02           O  
ATOM    674  CG2 THR A  85      35.668  90.544  10.796  1.00 23.28           C  
ATOM    675  N   TYR A  86      33.940  88.812  14.652  1.00 14.56           N  
ATOM    676  CA  TYR A  86      32.845  88.457  15.622  1.00  8.27           C  
ATOM    677  C   TYR A  86      33.295  87.277  16.505  1.00  9.67           C  
ATOM    678  O   TYR A  86      32.770  86.162  16.366  1.00 12.25           O  
ATOM    679  CB  TYR A  86      31.605  88.185  14.771  1.00 16.82           C  
ATOM    680  CG  TYR A  86      30.244  88.255  15.479  1.00 23.19           C  
ATOM    681  CD1 TYR A  86      29.128  88.594  14.702  1.00  9.81           C  
ATOM    682  CD2 TYR A  86      30.101  87.990  16.838  1.00 14.53           C  
ATOM    683  CE1 TYR A  86      27.809  88.656  15.382  1.00  4.99           C  
ATOM    684  CE2 TYR A  86      28.839  88.058  17.454  1.00 11.22           C  
ATOM    685  CZ  TYR A  86      27.733  88.395  16.699  1.00 12.91           C  
ATOM    686  OH  TYR A  86      26.506  88.461  17.277  1.00  9.50           O  
ATOM    687  N   PRO A  87      34.213  87.516  17.421  1.00 17.46           N  
ATOM    688  CA  PRO A  87      34.917  86.545  18.249  1.00 11.97           C  
ATOM    689  C   PRO A  87      34.067  85.906  19.338  1.00 30.02           C  
ATOM    690  O   PRO A  87      33.009  86.464  19.749  1.00 13.98           O  
ATOM    691  CB  PRO A  87      36.048  87.364  18.862  1.00 11.81           C  
ATOM    692  CG  PRO A  87      35.495  88.739  18.959  1.00 15.37           C  
ATOM    693  CD  PRO A  87      34.550  88.892  17.791  1.00  7.76           C  
ATOM    694  N   TYR A  88      34.533  84.697  19.750  1.00 13.28           N  
ATOM    695  CA  TYR A  88      33.734  83.838  20.652  1.00 11.79           C  
ATOM    696  C   TYR A  88      33.788  84.390  22.063  1.00 12.08           C  
ATOM    697  O   TYR A  88      34.921  84.636  22.557  1.00 13.02           O  
ATOM    698  CB  TYR A  88      34.384  82.452  20.591  1.00  9.29           C  
ATOM    699  CG  TYR A  88      33.565  81.441  21.433  1.00 12.29           C  
ATOM    700  CD1 TYR A  88      32.198  81.302  21.105  1.00  8.37           C  
ATOM    701  CD2 TYR A  88      34.135  80.717  22.467  1.00  8.71           C  
ATOM    702  CE1 TYR A  88      31.399  80.347  21.904  1.00 15.03           C  
ATOM    703  CE2 TYR A  88      33.385  79.805  23.238  1.00  7.34           C  
ATOM    704  CZ  TYR A  88      32.014  79.666  22.898  1.00 14.28           C  
ATOM    705  OH  TYR A  88      31.297  78.771  23.657  1.00 11.83           O  
ATOM    706  N   GLU A  89      32.669  84.426  22.739  1.00  7.44           N  
ATOM    707  CA  GLU A  89      32.579  84.779  24.152  1.00 14.16           C  
ATOM    708  C   GLU A  89      32.089  83.694  25.080  1.00 15.98           C  
ATOM    709  O   GLU A  89      32.166  83.833  26.349  1.00 20.80           O  
ATOM    710  CB  GLU A  89      31.642  86.043  24.280  1.00 11.35           C  
ATOM    711  CG  GLU A  89      31.749  87.109  23.198  1.00 10.09           C  
ATOM    712  CD  GLU A  89      30.894  88.402  23.523  1.00 21.86           C  
ATOM    713  OE1 GLU A  89      30.891  89.080  22.514  1.00 18.96           O  
ATOM    714  OE2 GLU A  89      30.386  88.573  24.598  1.00 44.17           O  
ATOM    715  N   GLY A  90      31.432  82.653  24.648  1.00 10.79           N  
ATOM    716  CA  GLY A  90      30.975  81.530  25.417  1.00 14.79           C  
ATOM    717  C   GLY A  90      29.745  81.930  26.224  1.00 18.28           C  
ATOM    718  O   GLY A  90      29.457  81.240  27.216  1.00 17.03           O  
ATOM    719  N   VAL A  91      29.021  82.959  25.793  1.00 12.45           N  
ATOM    720  CA  VAL A  91      27.776  83.443  26.413  1.00 11.53           C  
ATOM    721  C   VAL A  91      26.878  83.953  25.247  1.00 17.62           C  
ATOM    722  O   VAL A  91      27.452  84.680  24.412  1.00 16.07           O  
ATOM    723  CB  VAL A  91      28.121  84.686  27.283  1.00 17.85           C  
ATOM    724  CG1 VAL A  91      26.931  85.531  27.561  1.00 27.86           C  
ATOM    725  CG2 VAL A  91      28.935  84.363  28.534  1.00 20.93           C  
ATOM    726  N   GLN A  92      25.555  83.683  25.304  1.00 11.69           N  
ATOM    727  CA  GLN A  92      24.651  84.250  24.311  1.00 11.20           C  
ATOM    728  C   GLN A  92      24.379  85.734  24.623  1.00 12.33           C  
ATOM    729  O   GLN A  92      24.068  86.219  25.704  1.00 21.97           O  
ATOM    730  CB  GLN A  92      23.360  83.548  24.197  1.00 12.95           C  
ATOM    731  CG  GLN A  92      22.367  84.141  23.235  1.00 22.42           C  
ATOM    732  CD  GLN A  92      21.108  83.280  22.985  1.00 24.02           C  
ATOM    733  OE1 GLN A  92      20.745  82.951  21.756  1.00 20.33           O  
ATOM    734  NE2 GLN A  92      20.461  82.906  24.007  1.00 21.70           N  
ATOM    735  N   ARG A  93      24.474  86.467  23.485  1.00 19.26           N  
ATOM    736  CA  ARG A  93      24.305  87.944  23.500  1.00 22.89           C  
ATOM    737  C   ARG A  93      23.244  88.257  22.430  1.00 13.34           C  
ATOM    738  O   ARG A  93      22.642  87.382  21.800  1.00 18.63           O  
ATOM    739  CB  ARG A  93      25.620  88.649  23.160  1.00 31.74           C  
ATOM    740  CG  ARG A  93      26.799  88.860  24.054  1.00 21.06           C  
ATOM    741  CD  ARG A  93      26.761  88.341  25.438  1.00 22.18           C  
ATOM    742  NE  ARG A  93      27.943  88.736  26.233  1.00 48.26           N  
ATOM    743  CZ  ARG A  93      27.817  89.070  27.535  1.00 53.04           C  
ATOM    744  NH1 ARG A  93      26.602  89.060  28.116  1.00 50.06           N  
ATOM    745  NH2 ARG A  93      28.868  89.440  28.241  1.00 41.12           N  
ATOM    746  N   TYR A  94      23.104  89.539  22.197  1.00 14.76           N  
ATOM    747  CA  TYR A  94      22.268  90.199  21.196  1.00 24.02           C  
ATOM    748  C   TYR A  94      22.797  89.744  19.866  1.00 15.41           C  
ATOM    749  O   TYR A  94      24.035  89.618  19.772  1.00 13.51           O  
ATOM    750  CB  TYR A  94      22.456  91.786  21.611  1.00 34.75           C  
ATOM    751  CG  TYR A  94      21.509  92.462  20.593  1.00 63.36           C  
ATOM    752  CD1 TYR A  94      20.117  92.431  20.831  1.00 61.22           C  
ATOM    753  CD2 TYR A  94      22.043  93.055  19.483  1.00 41.51           C  
ATOM    754  CE1 TYR A  94      19.237  93.061  19.853  1.00 37.84           C  
ATOM    755  CE2 TYR A  94      21.165  93.673  18.525  1.00 74.37           C  
ATOM    756  CZ  TYR A  94      19.773  93.644  18.763  1.00 66.69           C  
ATOM    757  OH  TYR A  94      18.995  94.257  17.796  1.00 48.95           O  
ATOM    758  N   CYS A  95      22.069  89.512  18.783  1.00 11.10           N  
ATOM    759  CA  CYS A  95      22.669  89.244  17.460  1.00 12.60           C  
ATOM    760  C   CYS A  95      23.168  90.618  16.888  1.00 15.39           C  
ATOM    761  O   CYS A  95      22.401  91.568  16.687  1.00 21.32           O  
ATOM    762  CB  CYS A  95      21.695  88.658  16.600  1.00  5.48           C  
ATOM    763  SG  CYS A  95      22.041  88.397  14.814  1.00 15.20           S  
ATOM    764  N   ARG A  96      24.478  90.638  16.600  1.00  9.43           N  
ATOM    765  CA  ARG A  96      25.146  91.889  16.243  1.00 17.41           C  
ATOM    766  C   ARG A  96      25.549  91.846  14.777  1.00 13.94           C  
ATOM    767  O   ARG A  96      26.419  92.650  14.492  1.00 17.19           O  
ATOM    768  CB  ARG A  96      26.349  92.116  17.189  1.00 11.88           C  
ATOM    769  CG  ARG A  96      25.886  92.398  18.664  1.00 10.91           C  
ATOM    770  CD  ARG A  96      27.076  92.209  19.614  1.00 13.75           C  
ATOM    771  NE  ARG A  96      27.096  90.753  20.000  1.00 12.07           N  
ATOM    772  CZ  ARG A  96      28.047  90.177  20.744  1.00 17.77           C  
ATOM    773  NH1 ARG A  96      29.047  90.963  21.253  1.00 12.18           N  
ATOM    774  NH2 ARG A  96      27.990  88.877  20.907  1.00 14.72           N  
ATOM    775  N   SER A  97      25.046  90.885  14.024  1.00  9.57           N  
ATOM    776  CA  SER A  97      25.473  90.755  12.600  1.00 10.21           C  
ATOM    777  C   SER A  97      25.581  92.131  11.901  1.00 10.02           C  
ATOM    778  O   SER A  97      26.471  92.545  11.181  1.00 24.70           O  
ATOM    779  CB  SER A  97      24.491  89.936  11.778  1.00  9.72           C  
ATOM    780  OG  SER A  97      24.527  88.633  12.359  1.00 17.03           O  
ATOM    781  N   ARG A  98      24.446  92.759  11.997  1.00 19.26           N  
ATOM    782  CA  ARG A  98      23.972  94.024  11.454  1.00 25.95           C  
ATOM    783  C   ARG A  98      24.983  95.108  11.676  1.00 18.28           C  
ATOM    784  O   ARG A  98      25.395  95.821  10.746  1.00 21.11           O  
ATOM    785  CB  ARG A  98      22.635  94.282  12.247  1.00 66.31           C  
ATOM    786  CG  ARG A  98      22.124  92.977  12.990  1.00 60.42           C  
ATOM    787  CD  ARG A  98      22.427  93.036  14.494  1.00 36.22           C  
ATOM    788  NE  ARG A  98      22.157  94.349  15.042  1.00 67.65           N  
ATOM    789  CZ  ARG A  98      22.930  95.266  15.658  1.00 62.01           C  
ATOM    790  NH1 ARG A  98      24.153  94.898  16.030  1.00 60.81           N  
ATOM    791  NH2 ARG A  98      22.411  96.462  15.898  1.00 62.59           N  
ATOM    792  N   GLU A  99      25.510  95.162  12.877  1.00 13.15           N  
ATOM    793  CA  GLU A  99      26.563  96.080  13.260  1.00 23.74           C  
ATOM    794  C   GLU A  99      27.972  95.745  12.810  1.00 23.25           C  
ATOM    795  O   GLU A  99      28.875  96.531  13.192  1.00 37.28           O  
ATOM    796  CB  GLU A  99      26.719  96.119  14.809  1.00 23.87           C  
ATOM    797  CG  GLU A  99      25.503  96.470  15.665  1.00 26.20           C  
ATOM    798  CD  GLU A  99      25.899  96.476  17.233  1.00 39.78           C  
ATOM    799  OE1 GLU A  99      24.832  96.708  17.765  1.00 44.85           O  
ATOM    800  OE2 GLU A  99      26.981  96.295  17.742  1.00 38.05           O  
ATOM    801  N   LYS A 100      28.249  94.678  12.089  1.00 18.66           N  
ATOM    802  CA  LYS A 100      29.624  94.253  11.821  1.00 25.28           C  
ATOM    803  C   LYS A 100      29.922  94.442  10.327  1.00 25.81           C  
ATOM    804  O   LYS A 100      30.955  93.922   9.800  1.00 35.98           O  
ATOM    805  CB  LYS A 100      29.853  92.765  12.121  1.00 37.62           C  
ATOM    806  CG  LYS A 100      29.758  92.204  13.485  1.00 28.59           C  
ATOM    807  CD  LYS A 100      30.611  92.901  14.512  1.00 20.16           C  
ATOM    808  CE  LYS A 100      30.266  92.290  15.932  1.00 11.27           C  
ATOM    809  NZ  LYS A 100      31.603  92.477  16.595  1.00 22.41           N  
ATOM    810  N   GLY A 101      28.891  94.957   9.650  1.00 17.99           N  
ATOM    811  CA  GLY A 101      29.125  95.070   8.167  1.00 14.87           C  
ATOM    812  C   GLY A 101      28.595  93.795   7.517  1.00 12.10           C  
ATOM    813  O   GLY A 101      27.907  92.891   8.018  1.00 23.07           O  
ATOM    814  N   PRO A 102      28.843  93.838   6.192  1.00 27.66           N  
ATOM    815  CA  PRO A 102      28.458  92.792   5.251  1.00 57.26           C  
ATOM    816  C   PRO A 102      29.041  91.487   5.839  1.00 13.64           C  
ATOM    817  O   PRO A 102      30.195  91.423   6.295  1.00 16.53           O  
ATOM    818  CB  PRO A 102      29.060  93.232   3.943  1.00 28.52           C  
ATOM    819  CG  PRO A 102      29.657  94.600   4.192  1.00 29.58           C  
ATOM    820  CD  PRO A 102      30.069  94.470   5.674  1.00 38.44           C  
ATOM    821  N   TYR A 103      28.350  90.462   5.445  1.00 18.36           N  
ATOM    822  CA  TYR A 103      28.769  89.071   5.760  1.00 19.56           C  
ATOM    823  C   TYR A 103      29.984  88.793   4.918  1.00 13.58           C  
ATOM    824  O   TYR A 103      30.084  89.351   3.779  1.00 19.16           O  
ATOM    825  CB  TYR A 103      27.540  88.258   5.331  1.00 13.35           C  
ATOM    826  CG  TYR A 103      26.397  88.428   6.329  1.00 39.09           C  
ATOM    827  CD1 TYR A 103      25.181  89.012   5.920  1.00 25.31           C  
ATOM    828  CD2 TYR A 103      26.571  88.002   7.627  1.00 13.80           C  
ATOM    829  CE1 TYR A 103      24.126  89.146   6.907  1.00 33.05           C  
ATOM    830  CE2 TYR A 103      25.526  88.135   8.590  1.00 21.54           C  
ATOM    831  CZ  TYR A 103      24.324  88.721   8.169  1.00 57.79           C  
ATOM    832  OH  TYR A 103      23.306  88.858   9.090  1.00 61.59           O  
ATOM    833  N   ALA A 104      30.774  87.819   5.397  1.00 10.34           N  
ATOM    834  CA  ALA A 104      31.976  87.407   4.704  1.00  8.38           C  
ATOM    835  C   ALA A 104      31.747  86.181   3.819  1.00 13.09           C  
ATOM    836  O   ALA A 104      32.454  86.061   2.778  1.00 24.64           O  
ATOM    837  CB  ALA A 104      33.119  87.123   5.656  1.00 12.51           C  
ATOM    838  N   ALA A 105      30.735  85.367   4.057  1.00 11.33           N  
ATOM    839  CA  ALA A 105      30.442  84.193   3.226  1.00 14.57           C  
ATOM    840  C   ALA A 105      28.962  83.909   3.302  1.00 15.02           C  
ATOM    841  O   ALA A 105      28.249  84.299   4.249  1.00 14.20           O  
ATOM    842  CB  ALA A 105      31.305  82.982   3.652  1.00 12.14           C  
ATOM    843  N   LYS A 106      28.449  83.192   2.310  1.00 12.24           N  
ATOM    844  CA  LYS A 106      27.015  82.792   2.311  1.00 13.04           C  
ATOM    845  C   LYS A 106      26.958  81.516   1.482  1.00 11.19           C  
ATOM    846  O   LYS A 106      27.789  81.438   0.545  1.00 23.89           O  
ATOM    847  CB  LYS A 106      26.121  83.920   1.787  1.00  9.35           C  
ATOM    848  CG  LYS A 106      24.634  83.642   1.757  1.00 11.11           C  
ATOM    849  CD  LYS A 106      23.854  84.854   1.269  1.00 20.76           C  
ATOM    850  CE  LYS A 106      22.351  84.546   1.301  1.00 29.75           C  
ATOM    851  NZ  LYS A 106      21.538  85.784   1.349  1.00 17.81           N  
ATOM    852  N   THR A 107      26.101  80.584   1.819  1.00  9.73           N  
ATOM    853  CA  THR A 107      26.053  79.315   1.034  1.00  8.26           C  
ATOM    854  C   THR A 107      24.759  79.271   0.232  1.00 18.04           C  
ATOM    855  O   THR A 107      23.896  80.116   0.497  1.00 10.56           O  
ATOM    856  CB  THR A 107      26.200  78.147   2.007  1.00 14.94           C  
ATOM    857  OG1 THR A 107      25.263  78.315   3.029  1.00 13.00           O  
ATOM    858  CG2 THR A 107      27.560  78.111   2.684  1.00  7.02           C  
ATOM    859  N   ASP A 108      24.607  78.201  -0.567  1.00 18.84           N  
ATOM    860  CA  ASP A 108      23.441  78.011  -1.426  1.00 11.13           C  
ATOM    861  C   ASP A 108      22.448  76.994  -0.978  1.00 10.50           C  
ATOM    862  O   ASP A 108      21.413  76.800  -1.699  1.00 13.16           O  
ATOM    863  CB  ASP A 108      23.918  77.754  -2.946  1.00  7.59           C  
ATOM    864  CG  ASP A 108      24.793  78.993  -3.137  1.00 11.44           C  
ATOM    865  OD1 ASP A 108      24.554  80.151  -2.946  1.00 32.57           O  
ATOM    866  OD2 ASP A 108      25.933  78.698  -3.522  1.00 15.92           O  
ATOM    867  N   GLY A 109      22.636  76.503   0.299  1.00  9.13           N  
ATOM    868  CA  GLY A 109      21.540  75.623   0.815  1.00 14.26           C  
ATOM    869  C   GLY A 109      22.124  74.643   1.854  1.00  7.66           C  
ATOM    870  O   GLY A 109      23.278  74.867   2.281  1.00  7.69           O  
ATOM    871  N   VAL A 110      21.416  73.638   2.193  1.00 13.83           N  
ATOM    872  CA  VAL A 110      21.840  72.643   3.240  1.00  9.77           C  
ATOM    873  C   VAL A 110      21.301  71.334   2.763  1.00  8.92           C  
ATOM    874  O   VAL A 110      20.240  71.362   2.172  1.00 13.08           O  
ATOM    875  CB  VAL A 110      21.551  73.072   4.650  1.00 11.26           C  
ATOM    876  CG1 VAL A 110      20.552  74.149   4.931  1.00 17.42           C  
ATOM    877  CG2 VAL A 110      21.422  71.963   5.756  1.00  8.63           C  
ATOM    878  N   ARG A 111      21.985  70.232   2.966  1.00  7.12           N  
ATOM    879  CA  ARG A 111      21.477  68.921   2.645  1.00 10.52           C  
ATOM    880  C   ARG A 111      21.737  68.026   3.864  1.00 17.19           C  
ATOM    881  O   ARG A 111      22.675  68.312   4.628  1.00 13.56           O  
ATOM    882  CB  ARG A 111      22.120  68.304   1.389  1.00 14.59           C  
ATOM    883  CG  ARG A 111      21.964  69.164   0.175  1.00 15.26           C  
ATOM    884  CD  ARG A 111      21.201  68.730  -1.069  1.00 64.85           C  
ATOM    885  NE  ARG A 111      20.929  70.048  -1.707  1.00 49.06           N  
ATOM    886  CZ  ARG A 111      19.762  70.705  -1.609  1.00 42.34           C  
ATOM    887  NH1 ARG A 111      18.616  70.022  -1.430  1.00 44.45           N  
ATOM    888  NH2 ARG A 111      19.790  71.995  -1.875  1.00 49.72           N  
ATOM    889  N   GLN A 112      20.926  67.004   3.951  1.00 11.19           N  
ATOM    890  CA  GLN A 112      21.040  66.001   5.020  1.00 18.68           C  
ATOM    891  C   GLN A 112      21.558  64.724   4.371  1.00 12.96           C  
ATOM    892  O   GLN A 112      21.207  64.481   3.187  1.00 17.66           O  
ATOM    893  CB  GLN A 112      19.626  65.765   5.561  1.00 11.13           C  
ATOM    894  CG  GLN A 112      19.700  64.941   6.766  1.00 33.45           C  
ATOM    895  CD  GLN A 112      18.495  64.509   7.582  1.00 22.32           C  
ATOM    896  OE1 GLN A 112      17.363  64.917   7.175  1.00 27.95           O  
ATOM    897  NE2 GLN A 112      18.671  63.779   8.609  1.00 20.49           N  
ATOM    898  N   VAL A 113      22.453  64.033   5.023  1.00 10.52           N  
ATOM    899  CA  VAL A 113      22.876  62.715   4.455  1.00 15.55           C  
ATOM    900  C   VAL A 113      21.827  61.689   4.901  1.00  9.18           C  
ATOM    901  O   VAL A 113      21.276  61.742   5.985  1.00 10.02           O  
ATOM    902  CB  VAL A 113      24.322  62.370   4.625  1.00 22.54           C  
ATOM    903  CG1 VAL A 113      25.169  63.516   5.222  1.00 12.13           C  
ATOM    904  CG2 VAL A 113      24.670  60.932   4.930  1.00  8.33           C  
ATOM    905  N   GLN A 114      21.645  60.696   3.971  1.00 14.14           N  
ATOM    906  CA  GLN A 114      20.721  59.581   4.357  1.00 17.94           C  
ATOM    907  C   GLN A 114      21.101  59.027   5.725  1.00 10.72           C  
ATOM    908  O   GLN A 114      22.238  58.488   5.797  1.00 13.75           O  
ATOM    909  CB  GLN A 114      20.998  58.524   3.301  1.00 15.66           C  
ATOM    910  CG  GLN A 114      19.726  57.786   3.067  1.00 31.26           C  
ATOM    911  CD  GLN A 114      19.974  56.420   2.403  1.00 63.73           C  
ATOM    912  OE1 GLN A 114      21.102  56.286   1.805  1.00 59.73           O  
ATOM    913  NE2 GLN A 114      19.062  55.550   2.497  1.00 59.89           N  
ATOM    914  N   PRO A 115      20.241  58.926   6.724  1.00 13.69           N  
ATOM    915  CA  PRO A 115      20.667  58.494   8.047  1.00 15.09           C  
ATOM    916  C   PRO A 115      20.841  56.977   8.024  1.00 15.16           C  
ATOM    917  O   PRO A 115      20.320  56.296   7.121  1.00 18.05           O  
ATOM    918  CB  PRO A 115      19.656  58.868   9.058  1.00 11.92           C  
ATOM    919  CG  PRO A 115      18.431  59.226   8.228  1.00 18.74           C  
ATOM    920  CD  PRO A 115      18.922  59.517   6.808  1.00 13.36           C  
ATOM    921  N   TYR A 116      21.560  56.584   9.070  1.00 16.87           N  
ATOM    922  CA  TYR A 116      21.822  55.145   9.324  1.00 19.06           C  
ATOM    923  C   TYR A 116      22.503  54.425   8.177  1.00 13.93           C  
ATOM    924  O   TYR A 116      22.157  53.308   7.826  1.00 20.90           O  
ATOM    925  CB  TYR A 116      20.419  54.574   9.667  1.00 13.97           C  
ATOM    926  CG  TYR A 116      19.759  55.341  10.800  1.00 25.61           C  
ATOM    927  CD1 TYR A 116      20.447  55.427  12.012  1.00 25.37           C  
ATOM    928  CD2 TYR A 116      18.538  55.937  10.643  1.00 14.78           C  
ATOM    929  CE1 TYR A 116      19.839  56.162  13.126  1.00 28.65           C  
ATOM    930  CE2 TYR A 116      17.936  56.653  11.720  1.00 17.67           C  
ATOM    931  CZ  TYR A 116      18.632  56.729  12.935  1.00 35.42           C  
ATOM    932  OH  TYR A 116      18.022  57.429  13.951  1.00 36.01           O  
ATOM    933  N   ASN A 117      23.420  55.108   7.508  1.00 10.18           N  
ATOM    934  CA  ASN A 117      24.065  54.530   6.316  1.00 12.45           C  
ATOM    935  C   ASN A 117      25.515  54.964   6.353  1.00 11.09           C  
ATOM    936  O   ASN A 117      25.727  56.159   6.122  1.00 13.74           O  
ATOM    937  CB  ASN A 117      23.265  55.106   5.153  1.00  9.22           C  
ATOM    938  CG  ASN A 117      23.683  54.558   3.828  1.00 13.61           C  
ATOM    939  OD1 ASN A 117      24.840  54.369   3.403  1.00 15.63           O  
ATOM    940  ND2 ASN A 117      22.638  54.236   3.002  1.00 33.36           N  
ATOM    941  N   GLN A 118      26.425  54.041   6.648  1.00 11.93           N  
ATOM    942  CA  GLN A 118      27.848  54.363   6.752  1.00 12.54           C  
ATOM    943  C   GLN A 118      28.304  54.817   5.366  1.00 13.23           C  
ATOM    944  O   GLN A 118      29.032  55.799   5.294  1.00 10.82           O  
ATOM    945  CB  GLN A 118      28.652  53.188   7.211  1.00 10.81           C  
ATOM    946  CG  GLN A 118      30.104  53.555   7.572  1.00 16.68           C  
ATOM    947  CD  GLN A 118      30.799  52.313   8.196  1.00 14.46           C  
ATOM    948  OE1 GLN A 118      31.648  51.684   7.605  1.00  8.56           O  
ATOM    949  NE2 GLN A 118      30.434  51.972   9.398  1.00 11.36           N  
ATOM    950  N   GLY A 119      27.919  54.113   4.357  1.00 12.22           N  
ATOM    951  CA  GLY A 119      28.325  54.371   2.983  1.00  8.78           C  
ATOM    952  C   GLY A 119      28.018  55.804   2.574  1.00  7.41           C  
ATOM    953  O   GLY A 119      28.891  56.487   1.995  1.00 14.96           O  
ATOM    954  N   ALA A 120      26.788  56.227   2.780  1.00 10.33           N  
ATOM    955  CA  ALA A 120      26.361  57.586   2.421  1.00  8.32           C  
ATOM    956  C   ALA A 120      27.108  58.668   3.177  1.00  9.68           C  
ATOM    957  O   ALA A 120      27.429  59.715   2.598  1.00 13.62           O  
ATOM    958  CB  ALA A 120      24.901  57.763   2.790  1.00 14.78           C  
ATOM    959  N   LEU A 121      27.379  58.389   4.463  1.00 13.80           N  
ATOM    960  CA  LEU A 121      28.229  59.269   5.267  1.00 10.39           C  
ATOM    961  C   LEU A 121      29.624  59.380   4.691  1.00 11.78           C  
ATOM    962  O   LEU A 121      30.229  60.478   4.614  1.00  7.52           O  
ATOM    963  CB  LEU A 121      28.251  58.815   6.778  1.00  7.58           C  
ATOM    964  CG  LEU A 121      29.202  59.707   7.624  1.00 14.45           C  
ATOM    965  CD1 LEU A 121      28.838  61.138   7.377  1.00 11.05           C  
ATOM    966  CD2 LEU A 121      29.182  59.386   9.080  1.00 11.72           C  
ATOM    967  N   LEU A 122      30.343  58.302   4.328  1.00  7.85           N  
ATOM    968  CA  LEU A 122      31.706  58.243   3.831  1.00 15.47           C  
ATOM    969  C   LEU A 122      31.798  58.938   2.440  1.00  8.02           C  
ATOM    970  O   LEU A 122      32.743  59.717   2.260  1.00  9.84           O  
ATOM    971  CB  LEU A 122      32.251  56.806   3.666  1.00  9.42           C  
ATOM    972  CG  LEU A 122      32.392  55.942   4.908  1.00 10.57           C  
ATOM    973  CD1 LEU A 122      32.731  54.524   4.526  1.00  8.70           C  
ATOM    974  CD2 LEU A 122      33.444  56.527   5.812  1.00 14.96           C  
ATOM    975  N   TYR A 123      30.709  58.801   1.673  1.00  8.76           N  
ATOM    976  CA  TYR A 123      30.773  59.482   0.332  1.00 10.47           C  
ATOM    977  C   TYR A 123      30.705  60.983   0.518  1.00  5.21           C  
ATOM    978  O   TYR A 123      31.397  61.753  -0.194  1.00 10.08           O  
ATOM    979  CB  TYR A 123      29.700  58.907  -0.487  1.00 12.00           C  
ATOM    980  CG  TYR A 123      29.634  59.524  -1.890  1.00 15.49           C  
ATOM    981  CD1 TYR A 123      30.319  58.917  -2.943  1.00 23.28           C  
ATOM    982  CD2 TYR A 123      28.897  60.655  -2.075  1.00 26.09           C  
ATOM    983  CE1 TYR A 123      30.217  59.535  -4.257  1.00 39.69           C  
ATOM    984  CE2 TYR A 123      28.790  61.269  -3.351  1.00 53.63           C  
ATOM    985  CZ  TYR A 123      29.482  60.650  -4.397  1.00 32.13           C  
ATOM    986  OH  TYR A 123      29.366  61.258  -5.632  1.00 70.89           O  
ATOM    987  N   SER A 124      29.898  61.372   1.514  1.00 10.36           N  
ATOM    988  CA  SER A 124      29.852  62.831   1.881  1.00  5.91           C  
ATOM    989  C   SER A 124      31.221  63.317   2.322  1.00  9.51           C  
ATOM    990  O   SER A 124      31.578  64.424   1.923  1.00 12.06           O  
ATOM    991  CB  SER A 124      28.720  63.171   2.852  1.00 11.98           C  
ATOM    992  OG  SER A 124      27.520  62.782   2.187  1.00 18.03           O  
ATOM    993  N   ILE A 125      31.838  62.734   3.335  1.00  6.06           N  
ATOM    994  CA  ILE A 125      33.171  63.143   3.833  1.00  2.05           C  
ATOM    995  C   ILE A 125      34.190  63.240   2.728  1.00  5.71           C  
ATOM    996  O   ILE A 125      35.068  64.138   2.780  1.00 12.30           O  
ATOM    997  CB  ILE A 125      33.601  62.204   4.999  1.00  7.73           C  
ATOM    998  CG1 ILE A 125      32.529  62.109   6.116  1.00  8.59           C  
ATOM    999  CG2 ILE A 125      34.969  62.826   5.397  1.00 10.16           C  
ATOM   1000  CD1 ILE A 125      32.846  61.075   7.246  1.00  4.09           C  
ATOM   1001  N   ALA A 126      34.135  62.335   1.755  1.00  8.21           N  
ATOM   1002  CA  ALA A 126      35.027  62.337   0.605  1.00 11.05           C  
ATOM   1003  C   ALA A 126      34.879  63.617  -0.189  1.00 12.90           C  
ATOM   1004  O   ALA A 126      35.846  64.079  -0.794  1.00 10.38           O  
ATOM   1005  CB  ALA A 126      34.703  61.190  -0.340  1.00  5.52           C  
ATOM   1006  N   ASN A 127      33.769  64.319  -0.063  1.00  8.83           N  
ATOM   1007  CA  ASN A 127      33.432  65.505  -0.800  1.00 10.65           C  
ATOM   1008  C   ASN A 127      33.665  66.731   0.062  1.00 11.96           C  
ATOM   1009  O   ASN A 127      34.145  67.729  -0.486  1.00  9.70           O  
ATOM   1010  CB  ASN A 127      31.954  65.455  -1.273  1.00 14.51           C  
ATOM   1011  CG  ASN A 127      31.607  64.548  -2.429  1.00 35.35           C  
ATOM   1012  OD1 ASN A 127      30.823  63.634  -2.476  1.00 26.76           O  
ATOM   1013  ND2 ASN A 127      32.275  64.802  -3.605  1.00 25.67           N  
ATOM   1014  N   GLN A 128      33.451  66.639   1.398  1.00  6.94           N  
ATOM   1015  CA  GLN A 128      33.672  67.803   2.222  1.00  5.03           C  
ATOM   1016  C   GLN A 128      33.432  67.452   3.730  1.00  5.39           C  
ATOM   1017  O   GLN A 128      32.784  66.438   3.900  1.00  9.42           O  
ATOM   1018  CB  GLN A 128      32.678  68.885   1.788  1.00 10.23           C  
ATOM   1019  CG  GLN A 128      31.323  68.440   2.032  1.00 12.45           C  
ATOM   1020  CD  GLN A 128      30.226  69.313   1.426  1.00 11.44           C  
ATOM   1021  OE1 GLN A 128      29.711  68.835   0.356  1.00 15.02           O  
ATOM   1022  NE2 GLN A 128      29.896  70.417   1.996  1.00 10.87           N  
ATOM   1023  N   PRO A 129      33.844  68.350   4.599  1.00 14.40           N  
ATOM   1024  CA  PRO A 129      33.551  68.101   6.036  1.00 11.42           C  
ATOM   1025  C   PRO A 129      32.052  68.134   6.208  1.00 11.26           C  
ATOM   1026  O   PRO A 129      31.308  68.944   5.608  1.00  8.94           O  
ATOM   1027  CB  PRO A 129      34.313  69.225   6.742  1.00 11.42           C  
ATOM   1028  CG  PRO A 129      35.513  69.591   5.838  1.00  7.33           C  
ATOM   1029  CD  PRO A 129      34.856  69.484   4.481  1.00  7.07           C  
ATOM   1030  N   VAL A 130      31.588  67.292   7.119  1.00  9.18           N  
ATOM   1031  CA  VAL A 130      30.130  67.089   7.411  1.00  8.16           C  
ATOM   1032  C   VAL A 130      29.935  67.228   8.940  1.00  4.27           C  
ATOM   1033  O   VAL A 130      30.690  66.774   9.742  1.00  7.64           O  
ATOM   1034  CB  VAL A 130      29.649  65.698   6.928  1.00 13.67           C  
ATOM   1035  CG1 VAL A 130      28.257  65.278   7.281  1.00  6.55           C  
ATOM   1036  CG2 VAL A 130      29.805  65.418   5.395  1.00 10.00           C  
ATOM   1037  N   SER A 131      28.734  67.739   9.273  1.00 10.68           N  
ATOM   1038  CA  SER A 131      28.302  67.860  10.654  1.00  3.64           C  
ATOM   1039  C   SER A 131      27.547  66.584  11.039  1.00  2.17           C  
ATOM   1040  O   SER A 131      26.597  66.126  10.383  1.00  9.53           O  
ATOM   1041  CB  SER A 131      27.260  68.986  10.670  1.00  8.86           C  
ATOM   1042  OG  SER A 131      26.781  69.046  11.989  1.00 18.12           O  
ATOM   1043  N   VAL A 132      27.953  65.994  12.187  1.00  4.67           N  
ATOM   1044  CA  VAL A 132      27.410  64.765  12.733  1.00  9.50           C  
ATOM   1045  C   VAL A 132      27.201  64.915  14.274  1.00  9.92           C  
ATOM   1046  O   VAL A 132      27.688  65.826  14.857  1.00  6.68           O  
ATOM   1047  CB  VAL A 132      28.347  63.578  12.413  1.00  5.67           C  
ATOM   1048  CG1 VAL A 132      28.677  63.464  10.883  1.00  7.48           C  
ATOM   1049  CG2 VAL A 132      29.590  63.621  13.218  1.00  5.36           C  
ATOM   1050  N   VAL A 133      26.351  64.042  14.798  1.00  9.14           N  
ATOM   1051  CA  VAL A 133      26.014  63.934  16.224  1.00 11.47           C  
ATOM   1052  C   VAL A 133      26.411  62.521  16.685  1.00  9.75           C  
ATOM   1053  O   VAL A 133      26.609  61.561  15.967  1.00  7.57           O  
ATOM   1054  CB  VAL A 133      24.523  64.276  16.475  1.00 12.66           C  
ATOM   1055  CG1 VAL A 133      24.161  65.651  15.991  1.00 11.50           C  
ATOM   1056  CG2 VAL A 133      23.507  63.191  15.970  1.00  5.37           C  
ATOM   1057  N   LEU A 134      26.607  62.416  18.048  1.00  7.86           N  
ATOM   1058  CA  LEU A 134      26.989  61.234  18.776  1.00  5.52           C  
ATOM   1059  C   LEU A 134      26.686  61.472  20.256  1.00 10.56           C  
ATOM   1060  O   LEU A 134      26.312  62.604  20.650  1.00  7.67           O  
ATOM   1061  CB  LEU A 134      28.508  60.907  18.536  1.00  8.55           C  
ATOM   1062  CG  LEU A 134      29.432  62.086  18.747  1.00  9.50           C  
ATOM   1063  CD1 LEU A 134      29.398  62.539  20.181  1.00 21.32           C  
ATOM   1064  CD2 LEU A 134      30.839  61.721  18.285  1.00 23.06           C  
ATOM   1065  N   GLN A 135      26.699  60.363  20.970  1.00  7.01           N  
ATOM   1066  CA  GLN A 135      26.501  60.344  22.436  1.00  5.28           C  
ATOM   1067  C   GLN A 135      27.839  60.702  23.064  1.00  7.76           C  
ATOM   1068  O   GLN A 135      28.761  59.843  23.017  1.00 13.60           O  
ATOM   1069  CB  GLN A 135      26.061  58.945  22.777  1.00 12.55           C  
ATOM   1070  CG  GLN A 135      25.593  59.034  24.183  1.00 13.21           C  
ATOM   1071  CD  GLN A 135      25.444  57.610  24.787  1.00  9.52           C  
ATOM   1072  OE1 GLN A 135      26.448  57.043  25.227  1.00 12.83           O  
ATOM   1073  NE2 GLN A 135      24.295  57.131  24.775  1.00  9.69           N  
ATOM   1074  N   ALA A 136      27.909  61.813  23.759  1.00 11.69           N  
ATOM   1075  CA  ALA A 136      29.202  62.178  24.394  1.00  9.71           C  
ATOM   1076  C   ALA A 136      29.134  62.028  25.919  1.00  7.63           C  
ATOM   1077  O   ALA A 136      30.177  62.258  26.559  1.00 16.27           O  
ATOM   1078  CB  ALA A 136      29.583  63.641  24.018  1.00  7.58           C  
ATOM   1079  N   ALA A 137      27.948  61.745  26.419  1.00 12.68           N  
ATOM   1080  CA  ALA A 137      27.747  61.799  27.896  1.00 28.07           C  
ATOM   1081  C   ALA A 137      28.426  60.664  28.607  1.00 19.44           C  
ATOM   1082  O   ALA A 137      28.632  60.785  29.865  1.00 20.35           O  
ATOM   1083  CB  ALA A 137      26.257  61.802  28.169  1.00 19.02           C  
ATOM   1084  N   GLY A 138      28.771  59.565  27.969  1.00 10.75           N  
ATOM   1085  CA  GLY A 138      29.431  58.408  28.575  1.00  7.59           C  
ATOM   1086  C   GLY A 138      30.846  58.780  29.000  1.00 17.57           C  
ATOM   1087  O   GLY A 138      31.529  59.630  28.421  1.00 13.96           O  
ATOM   1088  N   LYS A 139      31.283  58.188  30.117  1.00 14.49           N  
ATOM   1089  CA  LYS A 139      32.564  58.487  30.779  1.00 17.45           C  
ATOM   1090  C   LYS A 139      33.723  58.160  29.831  1.00 11.15           C  
ATOM   1091  O   LYS A 139      34.714  58.817  29.901  1.00 12.78           O  
ATOM   1092  CB  LYS A 139      32.673  57.701  32.079  1.00 32.08           C  
ATOM   1093  CG  LYS A 139      32.019  58.259  33.257  1.00 42.20           C  
ATOM   1094  N   ASP A 140      33.511  57.119  29.010  1.00  7.79           N  
ATOM   1095  CA  ASP A 140      34.577  56.639  28.139  1.00 10.57           C  
ATOM   1096  C   ASP A 140      34.890  57.699  27.053  1.00  8.77           C  
ATOM   1097  O   ASP A 140      36.085  57.888  26.823  1.00  7.65           O  
ATOM   1098  CB  ASP A 140      34.040  55.362  27.457  1.00 12.56           C  
ATOM   1099  CG  ASP A 140      33.664  54.413  28.585  1.00 30.00           C  
ATOM   1100  OD1 ASP A 140      34.544  53.793  29.136  1.00 15.62           O  
ATOM   1101  OD2 ASP A 140      32.516  54.287  28.917  1.00 14.85           O  
ATOM   1102  N   PHE A 141      33.828  58.224  26.515  1.00  7.45           N  
ATOM   1103  CA  PHE A 141      34.004  59.308  25.495  1.00  6.33           C  
ATOM   1104  C   PHE A 141      34.667  60.559  26.095  1.00 10.69           C  
ATOM   1105  O   PHE A 141      35.719  61.010  25.536  1.00 13.16           O  
ATOM   1106  CB  PHE A 141      32.646  59.643  24.884  1.00 11.34           C  
ATOM   1107  CG  PHE A 141      32.859  60.626  23.761  1.00  8.67           C  
ATOM   1108  CD1 PHE A 141      32.956  60.127  22.500  1.00 13.65           C  
ATOM   1109  CD2 PHE A 141      32.946  61.980  24.017  1.00 10.38           C  
ATOM   1110  CE1 PHE A 141      33.160  60.987  21.405  1.00  8.32           C  
ATOM   1111  CE2 PHE A 141      33.148  62.835  22.880  1.00 14.22           C  
ATOM   1112  CZ  PHE A 141      33.240  62.297  21.606  1.00  5.80           C  
ATOM   1113  N   GLN A 142      34.155  60.925  27.286  1.00 16.39           N  
ATOM   1114  CA  GLN A 142      34.824  62.030  28.043  1.00 17.58           C  
ATOM   1115  C   GLN A 142      36.253  61.902  28.455  1.00 10.11           C  
ATOM   1116  O   GLN A 142      37.039  62.881  28.375  1.00 12.64           O  
ATOM   1117  CB  GLN A 142      33.923  62.244  29.268  1.00 10.64           C  
ATOM   1118  CG  GLN A 142      32.805  63.006  28.626  1.00 23.59           C  
ATOM   1119  CD  GLN A 142      32.017  63.784  29.670  1.00 60.71           C  
ATOM   1120  OE1 GLN A 142      32.120  63.368  30.869  1.00 37.18           O  
ATOM   1121  NE2 GLN A 142      31.334  64.763  29.262  1.00 73.08           N  
ATOM   1122  N   LEU A 143      36.717  60.734  28.824  1.00 12.61           N  
ATOM   1123  CA  LEU A 143      38.077  60.439  29.285  1.00 12.32           C  
ATOM   1124  C   LEU A 143      38.981  59.933  28.180  1.00 20.80           C  
ATOM   1125  O   LEU A 143      40.147  59.612  28.441  1.00 18.03           O  
ATOM   1126  CB  LEU A 143      38.011  59.380  30.442  1.00 14.24           C  
ATOM   1127  CG  LEU A 143      37.309  59.833  31.706  1.00 18.55           C  
ATOM   1128  CD1 LEU A 143      37.450  58.830  32.809  1.00 21.96           C  
ATOM   1129  CD2 LEU A 143      37.797  61.139  32.199  1.00 19.25           C  
ATOM   1130  N   TYR A 144      38.558  59.974  26.925  1.00 16.90           N  
ATOM   1131  CA  TYR A 144      39.358  59.505  25.772  1.00 15.21           C  
ATOM   1132  C   TYR A 144      40.577  60.429  25.571  1.00 11.57           C  
ATOM   1133  O   TYR A 144      40.523  61.686  25.631  1.00 11.07           O  
ATOM   1134  CB  TYR A 144      38.490  59.544  24.525  1.00 13.57           C  
ATOM   1135  CG  TYR A 144      39.217  59.348  23.206  1.00  9.29           C  
ATOM   1136  CD1 TYR A 144      39.514  60.493  22.444  1.00  9.74           C  
ATOM   1137  CD2 TYR A 144      39.582  58.135  22.731  1.00  9.02           C  
ATOM   1138  CE1 TYR A 144      40.188  60.293  21.188  1.00  8.08           C  
ATOM   1139  CE2 TYR A 144      40.238  57.935  21.520  1.00  5.79           C  
ATOM   1140  CZ  TYR A 144      40.514  59.077  20.775  1.00  6.57           C  
ATOM   1141  OH  TYR A 144      41.162  58.962  19.539  1.00  9.10           O  
ATOM   1142  N   ARG A 145      41.668  59.723  25.381  1.00 13.34           N  
ATOM   1143  CA  ARG A 145      42.982  60.286  25.184  1.00 15.76           C  
ATOM   1144  C   ARG A 145      43.677  59.774  23.960  1.00 13.17           C  
ATOM   1145  O   ARG A 145      44.809  60.218  23.836  1.00 21.15           O  
ATOM   1146  CB  ARG A 145      43.873  60.029  26.463  1.00 22.42           C  
ATOM   1147  CG  ARG A 145      43.193  60.754  27.691  1.00 23.08           C  
ATOM   1148  CD  ARG A 145      43.490  59.915  28.959  1.00 48.35           C  
ATOM   1149  NE  ARG A 145      44.359  60.690  29.775  1.00 66.93           N  
ATOM   1150  CZ  ARG A 145      45.287  60.467  30.716  1.00 70.88           C  
ATOM   1151  NH1 ARG A 145      45.294  59.201  31.144  1.00 65.61           N  
ATOM   1152  NH2 ARG A 145      46.109  61.458  31.064  1.00 50.84           N  
ATOM   1153  N   GLY A 146      43.160  58.898  23.142  1.00 14.25           N  
ATOM   1154  CA  GLY A 146      43.820  58.557  21.876  1.00  9.18           C  
ATOM   1155  C   GLY A 146      43.455  57.114  21.531  1.00 19.48           C  
ATOM   1156  O   GLY A 146      42.969  56.342  22.372  1.00 21.65           O  
ATOM   1157  N   GLY A 147      43.732  56.763  20.265  1.00 21.93           N  
ATOM   1158  CA  GLY A 147      43.438  55.384  19.756  1.00 18.86           C  
ATOM   1159  C   GLY A 147      42.056  55.391  19.087  1.00 18.18           C  
ATOM   1160  O   GLY A 147      41.411  56.460  18.926  1.00 21.88           O  
ATOM   1161  N   ILE A 148      41.756  54.231  18.457  1.00 12.19           N  
ATOM   1162  CA  ILE A 148      40.470  54.123  17.753  1.00 12.05           C  
ATOM   1163  C   ILE A 148      39.463  53.785  18.800  1.00 16.35           C  
ATOM   1164  O   ILE A 148      39.594  52.803  19.563  1.00 14.81           O  
ATOM   1165  CB  ILE A 148      40.651  53.035  16.654  1.00 10.92           C  
ATOM   1166  CG1 ILE A 148      41.821  53.561  15.765  1.00 17.25           C  
ATOM   1167  CG2 ILE A 148      39.233  52.955  16.087  1.00 11.97           C  
ATOM   1168  CD1 ILE A 148      41.768  53.134  14.328  1.00 19.46           C  
ATOM   1169  N   PHE A 149      38.479  54.659  18.915  1.00 10.09           N  
ATOM   1170  CA  PHE A 149      37.413  54.559  19.940  1.00 17.90           C  
ATOM   1171  C   PHE A 149      36.313  53.663  19.402  1.00  9.28           C  
ATOM   1172  O   PHE A 149      35.646  53.807  18.400  1.00 13.65           O  
ATOM   1173  CB  PHE A 149      36.925  55.969  20.250  1.00 10.63           C  
ATOM   1174  CG  PHE A 149      35.865  55.986  21.326  1.00 12.73           C  
ATOM   1175  CD1 PHE A 149      36.339  55.969  22.619  1.00 16.75           C  
ATOM   1176  CD2 PHE A 149      34.504  56.010  21.048  1.00 18.30           C  
ATOM   1177  CE1 PHE A 149      35.389  55.983  23.712  1.00 14.34           C  
ATOM   1178  CE2 PHE A 149      33.640  56.024  22.170  1.00 14.13           C  
ATOM   1179  CZ  PHE A 149      34.072  56.016  23.461  1.00 14.09           C  
ATOM   1180  N   VAL A 150      36.086  52.700  20.294  1.00 13.51           N  
ATOM   1181  CA  VAL A 150      35.173  51.546  20.034  1.00 13.65           C  
ATOM   1182  C   VAL A 150      34.019  51.572  21.028  1.00 21.20           C  
ATOM   1183  O   VAL A 150      33.030  50.796  20.854  1.00 23.75           O  
ATOM   1184  CB  VAL A 150      36.166  50.377  20.127  1.00 23.03           C  
ATOM   1185  CG1 VAL A 150      35.990  49.359  21.191  1.00 25.62           C  
ATOM   1186  CG2 VAL A 150      36.631  49.775  18.772  1.00 14.90           C  
ATOM   1187  N   GLY A 151      33.971  52.608  21.873  1.00 12.28           N  
ATOM   1188  CA  GLY A 151      32.938  52.607  22.937  1.00  7.03           C  
ATOM   1189  C   GLY A 151      33.532  52.112  24.239  1.00 13.37           C  
ATOM   1190  O   GLY A 151      34.751  51.985  24.460  1.00 16.48           O  
ATOM   1191  N   PRO A 152      32.680  51.737  25.161  1.00  8.76           N  
ATOM   1192  CA  PRO A 152      31.229  51.671  25.149  1.00  8.17           C  
ATOM   1193  C   PRO A 152      30.585  53.061  25.093  1.00 17.28           C  
ATOM   1194  O   PRO A 152      31.088  54.076  25.591  1.00 22.07           O  
ATOM   1195  CB  PRO A 152      30.871  51.044  26.491  1.00 10.19           C  
ATOM   1196  CG  PRO A 152      32.147  50.815  27.256  1.00 11.54           C  
ATOM   1197  CD  PRO A 152      33.291  51.382  26.458  1.00 11.58           C  
ATOM   1198  N   CYS A 153      29.414  53.064  24.467  1.00 15.47           N  
ATOM   1199  CA  CYS A 153      28.546  54.232  24.312  1.00 15.54           C  
ATOM   1200  C   CYS A 153      27.262  53.719  23.651  1.00 19.46           C  
ATOM   1201  O   CYS A 153      27.206  52.608  23.025  1.00 21.58           O  
ATOM   1202  CB  CYS A 153      29.208  55.308  23.502  1.00 10.27           C  
ATOM   1203  SG  CYS A 153      29.735  54.685  21.836  1.00 13.17           S  
ATOM   1204  N   GLY A 154      26.163  54.428  23.981  1.00 18.01           N  
ATOM   1205  CA  GLY A 154      24.833  54.060  23.463  1.00 15.88           C  
ATOM   1206  C   GLY A 154      24.636  54.935  22.181  1.00 10.24           C  
ATOM   1207  O   GLY A 154      25.609  55.489  21.703  1.00 12.55           O  
ATOM   1208  N   ASN A 155      23.387  55.239  22.047  1.00  7.84           N  
ATOM   1209  CA  ASN A 155      22.905  56.065  20.937  1.00 25.04           C  
ATOM   1210  C   ASN A 155      21.989  57.225  21.309  1.00 12.21           C  
ATOM   1211  O   ASN A 155      21.207  57.744  20.463  1.00 17.39           O  
ATOM   1212  CB  ASN A 155      22.138  55.285  19.900  1.00 34.77           C  
ATOM   1213  CG  ASN A 155      22.275  53.890  19.514  1.00 60.34           C  
ATOM   1214  OD1 ASN A 155      21.308  53.122  19.471  1.00 33.55           O  
ATOM   1215  ND2 ASN A 155      23.558  53.486  19.193  1.00 44.01           N  
ATOM   1216  N   LYS A 156      22.151  57.735  22.528  1.00 12.56           N  
ATOM   1217  CA  LYS A 156      21.367  58.851  23.019  1.00 13.82           C  
ATOM   1218  C   LYS A 156      22.253  60.095  22.666  1.00  9.45           C  
ATOM   1219  O   LYS A 156      22.942  60.626  23.506  1.00 13.48           O  
ATOM   1220  CB  LYS A 156      21.159  58.742  24.512  1.00 29.67           C  
ATOM   1221  CG  LYS A 156      21.076  57.413  25.227  1.00 62.91           C  
ATOM   1222  CD  LYS A 156      21.860  57.318  26.547  1.00 70.39           C  
ATOM   1223  CE  LYS A 156      22.766  56.060  26.633  1.00 17.23           C  
ATOM   1224  NZ  LYS A 156      21.911  54.867  26.369  1.00 55.21           N  
ATOM   1225  N   VAL A 157      22.212  60.346  21.337  1.00 16.26           N  
ATOM   1226  CA  VAL A 157      23.050  61.418  20.771  1.00  9.33           C  
ATOM   1227  C   VAL A 157      22.728  62.720  21.476  1.00 10.30           C  
ATOM   1228  O   VAL A 157      21.543  63.145  21.664  1.00 12.18           O  
ATOM   1229  CB  VAL A 157      22.923  61.476  19.225  1.00  7.96           C  
ATOM   1230  CG1 VAL A 157      23.281  60.192  18.480  1.00  6.82           C  
ATOM   1231  CG2 VAL A 157      21.584  62.019  18.816  1.00 13.90           C  
ATOM   1232  N   ASP A 158      23.771  63.446  21.883  1.00  8.13           N  
ATOM   1233  CA  ASP A 158      23.649  64.703  22.580  1.00 12.32           C  
ATOM   1234  C   ASP A 158      24.701  65.731  22.277  1.00 19.51           C  
ATOM   1235  O   ASP A 158      24.838  66.710  23.029  1.00 16.05           O  
ATOM   1236  CB  ASP A 158      23.649  64.426  24.118  1.00  6.21           C  
ATOM   1237  CG  ASP A 158      24.892  63.669  24.472  1.00 24.21           C  
ATOM   1238  OD1 ASP A 158      25.888  63.663  23.745  1.00 12.63           O  
ATOM   1239  OD2 ASP A 158      24.908  63.044  25.513  1.00 27.65           O  
ATOM   1240  N   HIS A 159      25.592  65.493  21.338  1.00 14.54           N  
ATOM   1241  CA  HIS A 159      26.713  66.378  21.046  1.00  3.57           C  
ATOM   1242  C   HIS A 159      26.942  66.469  19.553  1.00 15.86           C  
ATOM   1243  O   HIS A 159      26.838  65.437  18.889  1.00 12.72           O  
ATOM   1244  CB  HIS A 159      27.895  65.686  21.747  1.00  9.07           C  
ATOM   1245  CG  HIS A 159      29.115  66.576  21.748  1.00 17.09           C  
ATOM   1246  ND1 HIS A 159      29.140  67.820  22.342  1.00 18.34           N  
ATOM   1247  CD2 HIS A 159      30.343  66.404  21.220  1.00 13.00           C  
ATOM   1248  CE1 HIS A 159      30.326  68.375  22.176  1.00 19.98           C  
ATOM   1249  NE2 HIS A 159      31.075  67.534  21.503  1.00 15.03           N  
ATOM   1250  N   ALA A 160      27.190  67.687  19.074  1.00  8.81           N  
ATOM   1251  CA  ALA A 160      27.418  67.878  17.621  1.00  7.63           C  
ATOM   1252  C   ALA A 160      28.906  68.165  17.431  1.00  9.05           C  
ATOM   1253  O   ALA A 160      29.520  69.055  18.058  1.00 10.00           O  
ATOM   1254  CB  ALA A 160      26.551  69.047  17.208  1.00  4.83           C  
ATOM   1255  N   VAL A 161      29.502  67.475  16.434  1.00  9.89           N  
ATOM   1256  CA  VAL A 161      30.935  67.487  16.086  1.00  7.48           C  
ATOM   1257  C   VAL A 161      31.051  67.463  14.530  1.00 11.46           C  
ATOM   1258  O   VAL A 161      30.000  67.658  13.892  1.00  7.50           O  
ATOM   1259  CB  VAL A 161      31.733  66.345  16.710  1.00 10.22           C  
ATOM   1260  CG1 VAL A 161      31.905  66.577  18.188  1.00  9.26           C  
ATOM   1261  CG2 VAL A 161      31.148  64.948  16.421  1.00  1.92           C  
ATOM   1262  N   ALA A 162      32.260  67.449  14.036  1.00  5.96           N  
ATOM   1263  CA  ALA A 162      32.421  67.534  12.541  1.00  4.60           C  
ATOM   1264  C   ALA A 162      33.278  66.389  12.097  1.00  7.11           C  
ATOM   1265  O   ALA A 162      34.334  66.114  12.714  1.00 12.61           O  
ATOM   1266  CB  ALA A 162      32.867  68.906  12.117  1.00  7.08           C  
ATOM   1267  N   ALA A 163      32.882  65.654  11.030  1.00  4.28           N  
ATOM   1268  CA  ALA A 163      33.635  64.544  10.516  1.00  1.00           C  
ATOM   1269  C   ALA A 163      34.537  65.121   9.399  1.00  6.66           C  
ATOM   1270  O   ALA A 163      33.979  65.782   8.500  1.00  7.99           O  
ATOM   1271  CB  ALA A 163      32.774  63.424   9.938  1.00  3.96           C  
ATOM   1272  N   VAL A 164      35.857  64.981   9.559  1.00  5.63           N  
ATOM   1273  CA  VAL A 164      36.759  65.637   8.634  1.00  6.45           C  
ATOM   1274  C   VAL A 164      37.620  64.621   7.873  1.00 11.06           C  
ATOM   1275  O   VAL A 164      38.591  65.070   7.205  1.00 12.85           O  
ATOM   1276  CB  VAL A 164      37.661  66.700   9.356  1.00 11.57           C  
ATOM   1277  CG1 VAL A 164      36.844  67.915   9.789  1.00  9.58           C  
ATOM   1278  CG2 VAL A 164      38.588  66.133  10.436  1.00  7.34           C  
ATOM   1279  N   GLY A 165      37.242  63.315   8.018  1.00  8.14           N  
ATOM   1280  CA  GLY A 165      38.072  62.339   7.286  1.00  6.61           C  
ATOM   1281  C   GLY A 165      37.637  60.943   7.705  1.00  8.79           C  
ATOM   1282  O   GLY A 165      36.760  60.771   8.535  1.00  9.07           O  
ATOM   1283  N   TYR A 166      38.385  59.992   7.100  1.00  8.73           N  
ATOM   1284  CA  TYR A 166      38.189  58.552   7.364  1.00  5.02           C  
ATOM   1285  C   TYR A 166      39.442  57.824   6.866  1.00  7.41           C  
ATOM   1286  O   TYR A 166      40.293  58.268   6.114  1.00  8.76           O  
ATOM   1287  CB  TYR A 166      36.857  58.014   6.851  1.00  4.76           C  
ATOM   1288  CG  TYR A 166      36.786  58.116   5.309  1.00  6.29           C  
ATOM   1289  CD1 TYR A 166      37.393  57.003   4.662  1.00  6.73           C  
ATOM   1290  CD2 TYR A 166      36.218  59.155   4.617  1.00 16.45           C  
ATOM   1291  CE1 TYR A 166      37.398  56.983   3.183  1.00  9.46           C  
ATOM   1292  CE2 TYR A 166      36.228  59.114   3.187  1.00 14.54           C  
ATOM   1293  CZ  TYR A 166      36.816  58.025   2.534  1.00  9.39           C  
ATOM   1294  OH  TYR A 166      36.821  58.012   1.154  1.00 12.18           O  
ATOM   1295  N   GLY A 167      39.416  56.560   7.366  1.00 15.91           N  
ATOM   1296  CA  GLY A 167      40.381  55.531   6.973  1.00 15.34           C  
ATOM   1297  C   GLY A 167      39.658  54.188   7.072  1.00  7.01           C  
ATOM   1298  O   GLY A 167      38.470  54.077   7.308  1.00 13.21           O  
ATOM   1299  N   PRO A 168      40.457  53.151   6.900  1.00 13.01           N  
ATOM   1300  CA  PRO A 168      39.966  51.769   6.718  1.00 20.97           C  
ATOM   1301  C   PRO A 168      39.050  51.393   7.847  1.00 16.15           C  
ATOM   1302  O   PRO A 168      38.094  50.622   7.698  1.00 16.18           O  
ATOM   1303  CB  PRO A 168      41.281  51.034   6.562  1.00 17.19           C  
ATOM   1304  CG  PRO A 168      42.248  52.051   6.077  1.00 10.86           C  
ATOM   1305  CD  PRO A 168      41.889  53.320   6.853  1.00  7.69           C  
ATOM   1306  N   ASN A 169      39.377  51.787   9.094  1.00 10.94           N  
ATOM   1307  CA  ASN A 169      38.651  51.391  10.287  1.00  9.43           C  
ATOM   1308  C   ASN A 169      38.172  52.563  11.112  1.00  8.08           C  
ATOM   1309  O   ASN A 169      37.886  52.256  12.334  1.00  9.80           O  
ATOM   1310  CB  ASN A 169      39.660  50.560  11.128  1.00 25.72           C  
ATOM   1311  CG  ASN A 169      41.027  51.160  11.192  1.00 34.00           C  
ATOM   1312  OD1 ASN A 169      41.847  51.627  10.375  1.00 35.82           O  
ATOM   1313  ND2 ASN A 169      41.434  51.160  12.539  1.00 70.88           N  
ATOM   1314  N   TYR A 170      38.187  53.806  10.702  1.00  9.80           N  
ATOM   1315  CA  TYR A 170      37.801  54.875  11.663  1.00 10.75           C  
ATOM   1316  C   TYR A 170      37.144  55.971  10.837  1.00 18.83           C  
ATOM   1317  O   TYR A 170      37.292  56.010   9.622  1.00 12.00           O  
ATOM   1318  CB  TYR A 170      39.026  55.332  12.575  1.00  8.98           C  
ATOM   1319  CG  TYR A 170      40.051  55.983  11.666  1.00  3.84           C  
ATOM   1320  CD1 TYR A 170      41.030  55.114  11.196  1.00 17.51           C  
ATOM   1321  CD2 TYR A 170      40.003  57.330  11.316  1.00  3.63           C  
ATOM   1322  CE1 TYR A 170      42.051  55.687  10.290  1.00 14.99           C  
ATOM   1323  CE2 TYR A 170      40.980  57.841  10.457  1.00 10.77           C  
ATOM   1324  CZ  TYR A 170      41.970  56.977   9.986  1.00 17.31           C  
ATOM   1325  OH  TYR A 170      42.929  57.470   9.142  1.00 18.43           O  
ATOM   1326  N   ILE A 171      36.447  56.890  11.512  1.00 11.15           N  
ATOM   1327  CA  ILE A 171      35.964  58.146  10.919  1.00  9.33           C  
ATOM   1328  C   ILE A 171      36.677  59.195  11.793  1.00 11.95           C  
ATOM   1329  O   ILE A 171      36.677  58.958  13.049  1.00  8.05           O  
ATOM   1330  CB  ILE A 171      34.398  58.244  10.924  1.00 12.26           C  
ATOM   1331  CG1 ILE A 171      33.817  57.303   9.813  1.00  6.25           C  
ATOM   1332  CG2 ILE A 171      34.026  59.740  10.763  1.00 12.48           C  
ATOM   1333  CD1 ILE A 171      32.342  57.055   9.948  1.00 13.36           C  
ATOM   1334  N   LEU A 172      37.250  60.184  11.166  1.00  6.92           N  
ATOM   1335  CA  LEU A 172      38.037  61.185  11.904  1.00  4.66           C  
ATOM   1336  C   LEU A 172      37.160  62.362  12.244  1.00  1.93           C  
ATOM   1337  O   LEU A 172      36.554  62.986  11.377  1.00  5.05           O  
ATOM   1338  CB  LEU A 172      39.259  61.656  11.107  1.00  6.16           C  
ATOM   1339  CG  LEU A 172      40.153  62.852  11.556  1.00  4.43           C  
ATOM   1340  CD1 LEU A 172      40.937  62.436  12.722  1.00  7.18           C  
ATOM   1341  CD2 LEU A 172      41.057  63.250  10.437  1.00  7.12           C  
ATOM   1342  N   ILE A 173      37.063  62.595  13.564  1.00  1.97           N  
ATOM   1343  CA  ILE A 173      36.152  63.669  14.083  1.00 11.12           C  
ATOM   1344  C   ILE A 173      36.908  64.829  14.717  1.00  6.84           C  
ATOM   1345  O   ILE A 173      37.753  64.607  15.608  1.00 12.15           O  
ATOM   1346  CB  ILE A 173      35.204  63.053  15.143  1.00  6.24           C  
ATOM   1347  CG1 ILE A 173      34.222  61.953  14.598  1.00 16.36           C  
ATOM   1348  CG2 ILE A 173      34.571  64.149  15.997  1.00  6.06           C  
ATOM   1349  CD1 ILE A 173      33.384  62.381  13.416  1.00 14.43           C  
ATOM   1350  N   LYS A 174      36.540  66.092  14.360  1.00  3.80           N  
ATOM   1351  CA  LYS A 174      37.068  67.259  15.018  1.00  2.80           C  
ATOM   1352  C   LYS A 174      36.053  67.648  16.114  1.00  5.28           C  
ATOM   1353  O   LYS A 174      34.911  67.959  15.916  1.00  6.75           O  
ATOM   1354  CB  LYS A 174      37.123  68.442  14.012  1.00  8.12           C  
ATOM   1355  CG  LYS A 174      37.928  69.594  14.578  1.00  6.57           C  
ATOM   1356  CD  LYS A 174      37.807  70.858  13.689  1.00  4.42           C  
ATOM   1357  CE  LYS A 174      38.699  71.971  13.982  1.00 10.25           C  
ATOM   1358  NZ  LYS A 174      38.552  73.267  13.147  1.00  5.27           N  
ATOM   1359  N   ASN A 175      36.503  67.613  17.378  1.00  8.42           N  
ATOM   1360  CA  ASN A 175      35.703  68.042  18.522  1.00  8.56           C  
ATOM   1361  C   ASN A 175      36.015  69.511  18.842  1.00 10.80           C  
ATOM   1362  O   ASN A 175      36.953  70.116  18.273  1.00 12.02           O  
ATOM   1363  CB  ASN A 175      35.917  67.058  19.693  1.00  6.79           C  
ATOM   1364  CG  ASN A 175      34.772  67.076  20.672  1.00 17.58           C  
ATOM   1365  OD1 ASN A 175      33.720  67.662  20.695  1.00  4.08           O  
ATOM   1366  ND2 ASN A 175      34.980  66.242  21.762  1.00 14.50           N  
ATOM   1367  N   SER A 176      35.190  70.016  19.821  1.00  4.06           N  
ATOM   1368  CA  SER A 176      35.339  71.438  20.190  1.00  5.17           C  
ATOM   1369  C   SER A 176      35.590  71.475  21.719  1.00 10.01           C  
ATOM   1370  O   SER A 176      35.095  72.388  22.416  1.00  8.66           O  
ATOM   1371  CB  SER A 176      34.169  72.246  19.822  1.00  5.87           C  
ATOM   1372  OG  SER A 176      32.927  71.665  20.138  1.00 12.44           O  
ATOM   1373  N   TRP A 177      36.450  70.578  22.171  1.00 14.64           N  
ATOM   1374  CA  TRP A 177      36.828  70.613  23.581  1.00  4.62           C  
ATOM   1375  C   TRP A 177      38.285  70.942  23.760  1.00 13.40           C  
ATOM   1376  O   TRP A 177      38.738  70.644  24.872  1.00 11.94           O  
ATOM   1377  CB  TRP A 177      36.594  69.211  24.165  1.00  7.30           C  
ATOM   1378  CG  TRP A 177      35.070  68.930  24.370  1.00  8.24           C  
ATOM   1379  CD1 TRP A 177      34.014  69.747  24.150  1.00  6.01           C  
ATOM   1380  CD2 TRP A 177      34.491  67.705  24.842  1.00 10.05           C  
ATOM   1381  NE1 TRP A 177      32.772  69.071  24.478  1.00 14.58           N  
ATOM   1382  CE2 TRP A 177      33.081  67.879  24.881  1.00 15.29           C  
ATOM   1383  CE3 TRP A 177      35.085  66.536  25.214  1.00 10.79           C  
ATOM   1384  CZ2 TRP A 177      32.151  66.916  25.289  1.00 13.67           C  
ATOM   1385  CZ3 TRP A 177      34.118  65.566  25.634  1.00 15.74           C  
ATOM   1386  CH2 TRP A 177      32.747  65.736  25.672  1.00 15.67           C  
ATOM   1387  N   GLY A 178      38.898  71.727  22.906  1.00  9.38           N  
ATOM   1388  CA  GLY A 178      40.249  72.119  22.961  1.00  9.60           C  
ATOM   1389  C   GLY A 178      41.196  70.938  22.696  1.00  7.09           C  
ATOM   1390  O   GLY A 178      40.829  69.870  22.296  1.00 11.81           O  
ATOM   1391  N   THR A 179      42.505  71.291  22.811  1.00 10.51           N  
ATOM   1392  CA  THR A 179      43.649  70.437  22.496  1.00  7.60           C  
ATOM   1393  C   THR A 179      43.844  69.319  23.540  1.00  8.90           C  
ATOM   1394  O   THR A 179      44.590  68.382  23.207  1.00 15.49           O  
ATOM   1395  CB  THR A 179      44.962  71.180  22.269  1.00 17.02           C  
ATOM   1396  OG1 THR A 179      45.203  72.187  23.245  1.00 13.06           O  
ATOM   1397  CG2 THR A 179      44.922  71.850  20.929  1.00 20.10           C  
ATOM   1398  N   GLY A 180      43.373  69.647  24.702  1.00 10.72           N  
ATOM   1399  CA  GLY A 180      43.579  68.845  25.883  1.00  8.86           C  
ATOM   1400  C   GLY A 180      42.747  67.573  25.931  1.00 30.84           C  
ATOM   1401  O   GLY A 180      42.663  66.946  27.001  1.00 28.69           O  
ATOM   1402  N   TRP A 181      41.976  67.276  24.881  1.00 17.45           N  
ATOM   1403  CA  TRP A 181      41.122  66.098  24.815  1.00 11.70           C  
ATOM   1404  C   TRP A 181      41.411  65.298  23.526  1.00  8.71           C  
ATOM   1405  O   TRP A 181      41.735  65.851  22.493  1.00 10.91           O  
ATOM   1406  CB  TRP A 181      39.652  66.577  24.853  1.00 14.13           C  
ATOM   1407  CG  TRP A 181      38.646  65.364  24.780  1.00 11.87           C  
ATOM   1408  CD1 TRP A 181      38.097  64.643  25.743  1.00  7.78           C  
ATOM   1409  CD2 TRP A 181      38.154  64.825  23.588  1.00  9.47           C  
ATOM   1410  NE1 TRP A 181      37.247  63.642  25.187  1.00 17.84           N  
ATOM   1411  CE2 TRP A 181      37.281  63.752  23.894  1.00 11.78           C  
ATOM   1412  CE3 TRP A 181      38.358  65.147  22.239  1.00  6.90           C  
ATOM   1413  CZ2 TRP A 181      36.604  62.981  22.975  1.00  6.72           C  
ATOM   1414  CZ3 TRP A 181      37.666  64.365  21.347  1.00 12.22           C  
ATOM   1415  CH2 TRP A 181      36.822  63.327  21.661  1.00 10.34           C  
ATOM   1416  N   GLY A 182      41.412  63.981  23.691  1.00 13.40           N  
ATOM   1417  CA  GLY A 182      41.595  63.106  22.501  1.00 10.92           C  
ATOM   1418  C   GLY A 182      42.965  63.267  21.952  1.00 11.15           C  
ATOM   1419  O   GLY A 182      43.947  63.470  22.689  1.00 14.15           O  
ATOM   1420  N   GLU A 183      43.086  63.138  20.664  1.00  8.53           N  
ATOM   1421  CA  GLU A 183      44.364  63.272  19.932  1.00  6.88           C  
ATOM   1422  C   GLU A 183      44.512  64.689  19.402  1.00 10.38           C  
ATOM   1423  O   GLU A 183      44.085  64.955  18.253  1.00  9.54           O  
ATOM   1424  CB  GLU A 183      44.261  62.311  18.710  1.00  8.54           C  
ATOM   1425  CG  GLU A 183      43.957  60.886  19.137  1.00 11.37           C  
ATOM   1426  CD  GLU A 183      44.111  59.743  18.076  1.00 19.85           C  
ATOM   1427  OE1 GLU A 183      43.767  60.056  16.976  1.00 16.32           O  
ATOM   1428  OE2 GLU A 183      44.546  58.782  18.617  1.00 19.13           O  
ATOM   1429  N   ASN A 184      44.904  65.584  20.296  1.00 13.51           N  
ATOM   1430  CA  ASN A 184      45.026  67.020  20.034  1.00 10.58           C  
ATOM   1431  C   ASN A 184      43.704  67.622  19.659  1.00  9.84           C  
ATOM   1432  O   ASN A 184      43.678  68.496  18.784  1.00 13.04           O  
ATOM   1433  CB  ASN A 184      46.146  67.342  19.007  1.00 10.28           C  
ATOM   1434  CG  ASN A 184      47.500  67.270  19.700  1.00 28.60           C  
ATOM   1435  OD1 ASN A 184      48.123  66.268  19.927  1.00 35.64           O  
ATOM   1436  ND2 ASN A 184      48.051  68.475  20.107  1.00 65.19           N  
ATOM   1437  N   GLY A 185      42.642  67.152  20.268  1.00  7.07           N  
ATOM   1438  CA  GLY A 185      41.286  67.669  19.987  1.00  5.48           C  
ATOM   1439  C   GLY A 185      40.461  66.814  19.003  1.00  5.92           C  
ATOM   1440  O   GLY A 185      39.295  67.155  18.806  1.00  7.96           O  
ATOM   1441  N   TYR A 186      40.954  65.767  18.435  1.00  7.59           N  
ATOM   1442  CA  TYR A 186      40.348  64.906  17.442  1.00  6.40           C  
ATOM   1443  C   TYR A 186      40.012  63.586  18.081  1.00  4.44           C  
ATOM   1444  O   TYR A 186      40.711  63.196  19.076  1.00  6.80           O  
ATOM   1445  CB  TYR A 186      41.319  64.617  16.300  1.00  8.94           C  
ATOM   1446  CG  TYR A 186      41.454  65.860  15.429  1.00  9.71           C  
ATOM   1447  CD1 TYR A 186      40.554  65.967  14.347  1.00 10.95           C  
ATOM   1448  CD2 TYR A 186      42.391  66.811  15.698  1.00  7.68           C  
ATOM   1449  CE1 TYR A 186      40.701  67.178  13.521  1.00 17.06           C  
ATOM   1450  CE2 TYR A 186      42.526  67.965  14.905  1.00  8.30           C  
ATOM   1451  CZ  TYR A 186      41.627  68.091  13.809  1.00 19.99           C  
ATOM   1452  OH  TYR A 186      41.710  69.197  13.000  1.00 16.58           O  
ATOM   1453  N   ILE A 187      39.081  62.824  17.444  1.00 11.66           N  
ATOM   1454  CA  ILE A 187      38.850  61.434  17.919  1.00  6.52           C  
ATOM   1455  C   ILE A 187      38.792  60.625  16.629  1.00  6.09           C  
ATOM   1456  O   ILE A 187      38.211  61.057  15.670  1.00  8.21           O  
ATOM   1457  CB  ILE A 187      37.669  61.228  18.851  1.00 10.89           C  
ATOM   1458  CG1 ILE A 187      37.257  59.708  19.155  1.00  2.74           C  
ATOM   1459  CG2 ILE A 187      36.463  61.973  18.337  1.00  9.70           C  
ATOM   1460  CD1 ILE A 187      36.328  59.657  20.369  1.00  8.15           C  
ATOM   1461  N   ARG A 188      39.337  59.415  16.668  1.00  4.67           N  
ATOM   1462  CA  ARG A 188      39.070  58.406  15.609  1.00  8.45           C  
ATOM   1463  C   ARG A 188      38.059  57.380  16.119  1.00 10.66           C  
ATOM   1464  O   ARG A 188      38.368  56.694  17.123  1.00 10.21           O  
ATOM   1465  CB  ARG A 188      40.386  57.718  15.172  1.00 11.80           C  
ATOM   1466  CG  ARG A 188      41.309  58.801  14.511  1.00  9.63           C  
ATOM   1467  CD  ARG A 188      42.591  58.036  14.142  1.00 10.29           C  
ATOM   1468  NE  ARG A 188      43.334  57.671  15.346  1.00 24.69           N  
ATOM   1469  CZ  ARG A 188      44.244  56.674  15.421  1.00 52.30           C  
ATOM   1470  NH1 ARG A 188      44.557  56.049  14.271  1.00 41.93           N  
ATOM   1471  NH2 ARG A 188      44.909  56.454  16.562  1.00 16.62           N  
ATOM   1472  N   ILE A 189      36.888  57.364  15.466  1.00  6.77           N  
ATOM   1473  CA  ILE A 189      35.779  56.471  15.995  1.00  7.37           C  
ATOM   1474  C   ILE A 189      35.736  55.261  15.078  1.00  6.54           C  
ATOM   1475  O   ILE A 189      35.795  55.430  13.822  1.00  9.43           O  
ATOM   1476  CB  ILE A 189      34.440  57.184  16.167  1.00 11.69           C  
ATOM   1477  CG1 ILE A 189      34.490  58.309  17.291  1.00 20.72           C  
ATOM   1478  CG2 ILE A 189      33.293  56.254  16.633  1.00 15.23           C  
ATOM   1479  CD1 ILE A 189      33.137  59.030  17.505  1.00 35.11           C  
ATOM   1480  N   LYS A 190      35.653  54.069  15.652  1.00  7.62           N  
ATOM   1481  CA  LYS A 190      35.521  52.854  14.842  1.00  7.16           C  
ATOM   1482  C   LYS A 190      34.329  52.949  13.865  1.00  7.95           C  
ATOM   1483  O   LYS A 190      33.174  53.277  14.201  1.00 12.31           O  
ATOM   1484  CB  LYS A 190      35.252  51.630  15.763  1.00 10.59           C  
ATOM   1485  CG  LYS A 190      35.303  50.389  14.895  1.00 23.92           C  
ATOM   1486  CD  LYS A 190      36.509  49.510  14.881  1.00 32.20           C  
ATOM   1487  CE  LYS A 190      36.734  48.837  13.551  1.00 64.99           C  
ATOM   1488  NZ  LYS A 190      36.660  47.410  13.386  1.00 35.23           N  
ATOM   1489  N   ARG A 191      34.642  52.390  12.632  1.00  7.17           N  
ATOM   1490  CA  ARG A 191      33.545  52.184  11.661  1.00  8.13           C  
ATOM   1491  C   ARG A 191      33.580  50.715  11.217  1.00  6.80           C  
ATOM   1492  O   ARG A 191      34.440  49.974  11.600  1.00 12.56           O  
ATOM   1493  CB  ARG A 191      33.753  53.071  10.444  1.00  8.61           C  
ATOM   1494  CG  ARG A 191      34.967  52.765   9.570  1.00  9.47           C  
ATOM   1495  CD  ARG A 191      34.859  53.686   8.385  1.00 10.04           C  
ATOM   1496  NE  ARG A 191      35.668  53.332   7.253  1.00 12.47           N  
ATOM   1497  CZ  ARG A 191      35.325  52.537   6.184  1.00  7.01           C  
ATOM   1498  NH1 ARG A 191      34.148  51.941   6.137  1.00  9.83           N  
ATOM   1499  NH2 ARG A 191      36.156  52.450   5.212  1.00  8.38           N  
ATOM   1500  N   GLY A 192      32.617  50.399  10.360  1.00 11.90           N  
ATOM   1501  CA  GLY A 192      32.539  49.155   9.618  1.00 14.54           C  
ATOM   1502  C   GLY A 192      32.268  47.944  10.448  1.00 20.70           C  
ATOM   1503  O   GLY A 192      32.897  46.917  10.171  1.00 27.18           O  
ATOM   1504  N   THR A 193      31.433  48.077  11.437  1.00 18.72           N  
ATOM   1505  CA  THR A 193      31.051  47.006  12.338  1.00 35.12           C  
ATOM   1506  C   THR A 193      29.639  46.520  12.015  1.00 44.69           C  
ATOM   1507  O   THR A 193      29.225  45.616  12.767  1.00 41.48           O  
ATOM   1508  CB  THR A 193      31.086  47.462  13.810  1.00 22.08           C  
ATOM   1509  OG1 THR A 193      30.079  48.475  13.863  1.00 28.58           O  
ATOM   1510  CG2 THR A 193      32.418  47.990  14.204  1.00 60.77           C  
ATOM   1511  N   GLY A 194      28.979  47.094  11.026  1.00 27.98           N  
ATOM   1512  CA  GLY A 194      27.618  46.633  10.677  1.00 29.77           C  
ATOM   1513  C   GLY A 194      26.527  47.239  11.519  1.00 17.06           C  
ATOM   1514  O   GLY A 194      25.313  47.059  11.224  1.00 34.07           O  
ATOM   1515  N   ASN A 195      26.855  47.985  12.550  1.00 19.30           N  
ATOM   1516  CA  ASN A 195      25.917  48.760  13.389  1.00 34.76           C  
ATOM   1517  C   ASN A 195      25.405  49.972  12.567  1.00 26.37           C  
ATOM   1518  O   ASN A 195      26.217  50.796  12.113  1.00 22.84           O  
ATOM   1519  CB  ASN A 195      26.586  49.326  14.663  1.00 28.57           C  
ATOM   1520  CG  ASN A 195      25.552  49.914  15.586  1.00 31.78           C  
ATOM   1521  OD1 ASN A 195      24.360  49.975  15.347  1.00 38.47           O  
ATOM   1522  ND2 ASN A 195      25.991  50.408  16.801  1.00 41.43           N  
ATOM   1523  N   SER A 196      24.084  50.040  12.383  1.00 35.18           N  
ATOM   1524  CA  SER A 196      23.339  51.050  11.668  1.00 28.16           C  
ATOM   1525  C   SER A 196      23.245  52.451  12.237  1.00  9.92           C  
ATOM   1526  O   SER A 196      23.175  53.468  11.489  1.00 15.55           O  
ATOM   1527  CB  SER A 196      21.875  50.524  11.562  1.00 23.53           C  
ATOM   1528  OG  SER A 196      21.732  50.379  10.135  1.00 56.88           O  
ATOM   1529  N   TYR A 197      23.196  52.511  13.590  1.00 18.49           N  
ATOM   1530  CA  TYR A 197      23.266  53.747  14.322  1.00 12.50           C  
ATOM   1531  C   TYR A 197      24.660  54.351  14.182  1.00  7.70           C  
ATOM   1532  O   TYR A 197      24.771  55.567  14.425  1.00 15.82           O  
ATOM   1533  CB  TYR A 197      23.068  53.578  15.869  1.00 15.51           C  
ATOM   1534  CG  TYR A 197      21.739  52.818  16.007  1.00 24.35           C  
ATOM   1535  CD1 TYR A 197      20.569  53.468  15.589  1.00 33.32           C  
ATOM   1536  CD2 TYR A 197      21.720  51.555  16.518  1.00 40.48           C  
ATOM   1537  CE1 TYR A 197      19.306  52.744  15.720  1.00 69.11           C  
ATOM   1538  CE2 TYR A 197      20.489  50.839  16.653  1.00 64.52           C  
ATOM   1539  CZ  TYR A 197      19.317  51.485  16.235  1.00 66.71           C  
ATOM   1540  OH  TYR A 197      18.138  50.767  16.376  1.00 63.31           O  
ATOM   1541  N   GLY A 198      25.664  53.469  14.041  1.00  9.30           N  
ATOM   1542  CA  GLY A 198      27.077  53.902  14.048  1.00  8.58           C  
ATOM   1543  C   GLY A 198      27.476  53.892  15.542  1.00  5.85           C  
ATOM   1544  O   GLY A 198      26.602  53.807  16.396  1.00  8.60           O  
ATOM   1545  N   VAL A 199      28.773  53.803  15.789  1.00 10.64           N  
ATOM   1546  CA  VAL A 199      29.274  53.809  17.165  1.00 14.56           C  
ATOM   1547  C   VAL A 199      28.976  55.183  17.760  1.00  9.54           C  
ATOM   1548  O   VAL A 199      29.154  56.186  17.096  1.00  6.88           O  
ATOM   1549  CB  VAL A 199      30.645  53.244  17.497  1.00 26.90           C  
ATOM   1550  CG1 VAL A 199      31.229  52.233  16.524  1.00 19.16           C  
ATOM   1551  CG2 VAL A 199      31.721  54.117  18.175  1.00 29.21           C  
ATOM   1552  N   CYS A 200      28.374  55.113  18.979  1.00 10.58           N  
ATOM   1553  CA  CYS A 200      27.837  56.280  19.688  1.00 21.27           C  
ATOM   1554  C   CYS A 200      26.785  57.098  18.868  1.00 14.61           C  
ATOM   1555  O   CYS A 200      26.503  58.249  19.269  1.00  8.71           O  
ATOM   1556  CB  CYS A 200      28.815  57.278  20.254  1.00 11.62           C  
ATOM   1557  SG  CYS A 200      30.292  56.461  20.977  1.00 14.45           S  
ATOM   1558  N   GLY A 201      26.021  56.373  18.084  1.00 10.36           N  
ATOM   1559  CA  GLY A 201      24.981  56.757  17.258  1.00 10.61           C  
ATOM   1560  C   GLY A 201      25.400  57.762  16.148  1.00 13.07           C  
ATOM   1561  O   GLY A 201      24.644  58.722  15.885  1.00 11.36           O  
ATOM   1562  N   LEU A 202      26.602  57.633  15.648  1.00 11.57           N  
ATOM   1563  CA  LEU A 202      27.215  58.588  14.723  1.00 11.53           C  
ATOM   1564  C   LEU A 202      26.429  58.722  13.432  1.00  7.04           C  
ATOM   1565  O   LEU A 202      26.655  59.807  12.765  1.00  8.52           O  
ATOM   1566  CB  LEU A 202      28.652  58.013  14.446  1.00  6.89           C  
ATOM   1567  CG  LEU A 202      29.582  58.770  13.522  1.00 21.63           C  
ATOM   1568  CD1 LEU A 202      29.781  60.188  14.059  1.00 14.91           C  
ATOM   1569  CD2 LEU A 202      30.890  57.977  13.473  1.00 17.51           C  
ATOM   1570  N   TYR A 203      25.582  57.731  13.070  1.00  8.08           N  
ATOM   1571  CA  TYR A 203      24.880  57.906  11.730  1.00  3.81           C  
ATOM   1572  C   TYR A 203      23.461  58.388  11.852  1.00  9.05           C  
ATOM   1573  O   TYR A 203      22.662  58.386  10.925  1.00 12.06           O  
ATOM   1574  CB  TYR A 203      24.976  56.639  10.890  1.00  7.97           C  
ATOM   1575  CG  TYR A 203      26.369  55.994  10.844  1.00 11.41           C  
ATOM   1576  CD1 TYR A 203      26.435  54.596  10.766  1.00 13.98           C  
ATOM   1577  CD2 TYR A 203      27.505  56.759  10.893  1.00 11.58           C  
ATOM   1578  CE1 TYR A 203      27.760  53.995  10.743  1.00  6.79           C  
ATOM   1579  CE2 TYR A 203      28.804  56.181  10.864  1.00 13.60           C  
ATOM   1580  CZ  TYR A 203      28.848  54.768  10.784  1.00 12.05           C  
ATOM   1581  OH  TYR A 203      30.073  54.167  10.755  1.00 13.01           O  
ATOM   1582  N   THR A 204      23.156  59.111  12.958  1.00  8.20           N  
ATOM   1583  CA  THR A 204      21.867  59.583  13.356  1.00 12.86           C  
ATOM   1584  C   THR A 204      21.422  60.825  12.543  1.00 10.78           C  
ATOM   1585  O   THR A 204      20.281  60.804  12.034  1.00 13.89           O  
ATOM   1586  CB  THR A 204      21.745  59.917  14.873  1.00 16.89           C  
ATOM   1587  OG1 THR A 204      21.904  58.619  15.519  1.00 10.19           O  
ATOM   1588  CG2 THR A 204      20.365  60.442  15.125  1.00 13.09           C  
ATOM   1589  N   SER A 205      22.273  61.831  12.534  1.00  9.02           N  
ATOM   1590  CA  SER A 205      21.817  63.072  11.873  1.00  9.35           C  
ATOM   1591  C   SER A 205      23.003  63.851  11.364  1.00 10.74           C  
ATOM   1592  O   SER A 205      23.602  64.520  12.212  1.00 15.05           O  
ATOM   1593  CB  SER A 205      21.056  63.794  12.930  1.00 10.36           C  
ATOM   1594  OG  SER A 205      20.346  64.909  12.363  1.00 21.42           O  
ATOM   1595  N   SER A 206      23.153  63.835   9.998  1.00  9.29           N  
ATOM   1596  CA  SER A 206      24.352  64.460   9.397  1.00  6.11           C  
ATOM   1597  C   SER A 206      23.945  65.355   8.229  1.00  9.40           C  
ATOM   1598  O   SER A 206      23.015  65.046   7.507  1.00 11.53           O  
ATOM   1599  CB  SER A 206      25.198  63.311   8.873  1.00 14.42           C  
ATOM   1600  OG  SER A 206      25.454  62.386   9.953  1.00 15.28           O  
ATOM   1601  N   PHE A 207      24.509  66.563   8.253  1.00 12.21           N  
ATOM   1602  CA  PHE A 207      24.153  67.659   7.315  1.00 12.69           C  
ATOM   1603  C   PHE A 207      25.478  68.253   6.805  1.00 17.20           C  
ATOM   1604  O   PHE A 207      26.493  68.224   7.498  1.00  7.36           O  
ATOM   1605  CB  PHE A 207      23.393  68.805   8.009  1.00  4.05           C  
ATOM   1606  CG  PHE A 207      21.990  68.468   8.383  1.00  9.23           C  
ATOM   1607  CD1 PHE A 207      21.789  67.977   9.642  1.00 14.65           C  
ATOM   1608  CD2 PHE A 207      20.947  68.634   7.489  1.00  6.40           C  
ATOM   1609  CE1 PHE A 207      20.480  67.609  10.097  1.00 13.72           C  
ATOM   1610  CE2 PHE A 207      19.646  68.257   7.958  1.00 10.92           C  
ATOM   1611  CZ  PHE A 207      19.464  67.772   9.220  1.00 11.64           C  
ATOM   1612  N   TYR A 208      25.330  69.071   5.703  1.00 14.34           N  
ATOM   1613  CA  TYR A 208      26.470  69.820   5.148  1.00 13.30           C  
ATOM   1614  C   TYR A 208      25.836  70.917   4.248  1.00  1.98           C  
ATOM   1615  O   TYR A 208      24.734  70.752   3.705  1.00 11.32           O  
ATOM   1616  CB  TYR A 208      27.448  68.949   4.350  1.00 10.88           C  
ATOM   1617  CG  TYR A 208      26.693  68.257   3.228  1.00  9.23           C  
ATOM   1618  CD1 TYR A 208      26.126  66.986   3.500  1.00  9.93           C  
ATOM   1619  CD2 TYR A 208      26.538  68.842   1.973  1.00 15.69           C  
ATOM   1620  CE1 TYR A 208      25.399  66.271   2.498  1.00 13.81           C  
ATOM   1621  CE2 TYR A 208      25.813  68.156   0.949  1.00 15.44           C  
ATOM   1622  CZ  TYR A 208      25.281  66.894   1.277  1.00 16.66           C  
ATOM   1623  OH  TYR A 208      24.590  66.220   0.324  1.00 16.44           O  
ATOM   1624  N   PRO A 209      26.548  71.994   4.211  1.00 11.41           N  
ATOM   1625  CA  PRO A 209      26.235  73.149   3.357  1.00 12.36           C  
ATOM   1626  C   PRO A 209      26.528  72.799   1.898  1.00 10.68           C  
ATOM   1627  O   PRO A 209      27.422  72.020   1.563  1.00 15.21           O  
ATOM   1628  CB  PRO A 209      27.185  74.190   3.924  1.00 10.16           C  
ATOM   1629  CG  PRO A 209      28.423  73.482   4.414  1.00  6.99           C  
ATOM   1630  CD  PRO A 209      27.896  72.083   4.812  1.00  6.08           C  
ATOM   1631  N   VAL A 210      25.872  73.472   0.977  1.00  8.42           N  
ATOM   1632  CA  VAL A 210      25.981  73.468  -0.477  1.00  9.97           C  
ATOM   1633  C   VAL A 210      26.465  74.876  -0.859  1.00 12.89           C  
ATOM   1634  O   VAL A 210      26.060  75.938  -0.293  1.00 10.37           O  
ATOM   1635  CB  VAL A 210      24.525  73.172  -0.999  1.00  6.09           C  
ATOM   1636  CG1 VAL A 210      24.408  73.351  -2.474  1.00 31.20           C  
ATOM   1637  CG2 VAL A 210      24.089  71.775  -0.505  1.00 17.56           C  
ATOM   1638  N   LYS A 211      27.472  74.879  -1.716  1.00 14.85           N  
ATOM   1639  CA  LYS A 211      28.020  76.126  -2.248  1.00 11.73           C  
ATOM   1640  C   LYS A 211      28.344  75.874  -3.710  1.00 26.83           C  
ATOM   1641  O   LYS A 211      29.158  74.994  -3.976  1.00 21.43           O  
ATOM   1642  CB  LYS A 211      29.295  76.411  -1.488  1.00 13.36           C  
ATOM   1643  CG  LYS A 211      29.949  77.730  -1.804  1.00 16.42           C  
ATOM   1644  CD  LYS A 211      29.014  78.901  -1.553  1.00 16.59           C  
ATOM   1645  CE  LYS A 211      29.802  80.171  -1.869  1.00 23.46           C  
ATOM   1646  NZ  LYS A 211      28.820  81.215  -2.231  1.00 41.82           N  
ATOM   1647  N   ASN A 212      27.763  76.613  -4.617  1.00 20.22           N  
ATOM   1648  CA  ASN A 212      27.901  76.625  -6.054  1.00 22.34           C  
ATOM   1649  C   ASN A 212      29.192  77.323  -6.538  1.00 25.26           C  
ATOM   1650  O   ASN A 212      29.586  76.876  -7.654  1.00 52.91           O  
ATOM   1651  CB  ASN A 212      26.737  77.444  -6.755  1.00 24.69           C  
ATOM   1652  CG  ASN A 212      25.438  76.681  -6.709  1.00 62.61           C  
ATOM   1653  OD1 ASN A 212      25.369  75.458  -6.623  1.00 39.30           O  
ATOM   1654  ND2 ASN A 212      24.266  77.441  -6.763  1.00 57.82           N  
ATOM   1655  OXT ASN A 212      29.688  78.197  -5.848  1.00 27.70           O  
TER    1656      ASN A 212                                                      
HETATM 1657  C   MOH A 214      44.699  68.604  -3.792  1.00 34.21           C  
HETATM 1658  O   MOH A 214      45.059  69.119  -2.471  1.00 28.01           O  
HETATM 1659  C   MOH A 215      41.741  56.759  26.822  1.00 47.76           C  
HETATM 1660  O   MOH A 215      42.225  56.578  25.467  1.00 27.75           O  
HETATM 1661  C   MOH A 216      34.867  73.138  -6.348  1.00 45.86           C  
HETATM 1662  O   MOH A 216      35.644  71.914  -6.142  1.00 64.58           O  
HETATM 1663  C   MOH A 217      34.195  61.876  -4.706  1.00 62.81           C  
HETATM 1664  O   MOH A 217      34.817  62.221  -3.449  1.00 60.39           O  
HETATM 1665  C   MOH A 218      25.260  91.948   8.019  1.00 36.28           C  
HETATM 1666  O   MOH A 218      25.050  92.208   6.607  1.00 44.79           O  
HETATM 1667  C   MOH A 219      27.620  51.266  20.025  1.00 36.61           C  
HETATM 1668  O   MOH A 219      27.215  52.633  20.226  1.00 22.41           O  
HETATM 1669  C   MOH A 220      28.492  65.889  -1.107  1.00 42.70           C  
HETATM 1670  O   MOH A 220      28.745  65.953   0.321  1.00 30.93           O  
HETATM 1671  C   MOH A 221      23.198  70.041  22.119  1.00 52.42           C  
HETATM 1672  O   MOH A 221      23.460  70.424  20.769  1.00 26.97           O  
HETATM 1673  C   MOH A 222      40.029  48.046  16.924  1.00 36.52           C  
HETATM 1674  O   MOH A 222      40.415  49.235  16.211  1.00 42.21           O  
HETATM 1675  C   MOH A 223      42.166  58.615  32.003  1.00 64.31           C  
HETATM 1676  O   MOH A 223      41.596  57.560  32.836  1.00 48.11           O  
HETATM 1677  C   MOH A 224      18.111  67.556   2.167  1.00 49.09           C  
HETATM 1678  O   MOH A 224      18.999  66.672   1.457  1.00 52.95           O  
HETATM 1679  C   MOH A 225      20.775  68.325  16.309  1.00 31.98           C  
HETATM 1680  O   MOH A 225      20.628  67.508  15.126  1.00 32.10           O  
HETATM 1681  C   MOH A 226      33.671  94.364  31.979  1.00 60.13           C  
HETATM 1682  O   MOH A 226      32.716  93.356  32.436  1.00 63.47           O  
HETATM 1683  C   MOH A 227      38.991  93.870  30.417  1.00 50.36           C  
HETATM 1684  O   MOH A 227      39.688  94.959  31.102  1.00 68.97           O  
HETATM 1685  C   MOH A 228      36.687  52.560  26.947  1.00 42.17           C  
HETATM 1686  O   MOH A 228      36.811  53.413  28.132  1.00 47.58           O  
HETATM 1687  C   MOH A 229      45.257  78.339  10.320  1.00 62.03           C  
HETATM 1688  O   MOH A 229      45.684  77.051   9.823  1.00 58.53           O  
HETATM 1689  C   MOH A 230      34.319  78.396  30.035  1.00 55.21           C  
HETATM 1690  O   MOH A 230      33.624  79.168  29.003  1.00 60.10           O  
HETATM 1691  C   MOH A 231      14.959  83.304   9.897  1.00 66.92           C  
HETATM 1692  O   MOH A 231      15.219  84.730  10.036  1.00 68.35           O  
HETATM 1693  C   MOH A 232      33.843  71.438  27.768  1.00 61.58           C  
HETATM 1694  O   MOH A 232      34.912  72.149  27.072  1.00 42.14           O  
HETATM 1695  C   MOH A 233      48.026  54.930  16.696  1.00 46.55           C  
HETATM 1696  O   MOH A 233      46.757  54.229  16.578  1.00 50.27           O  
HETATM 1697  C   MOH A 234      19.762  73.264  29.645  1.00 61.24           C  
HETATM 1698  O   MOH A 234      19.740  72.131  28.712  1.00 65.62           O  
HETATM 1699  C   MOH A 235      47.830  57.691  19.039  1.00 37.49           C  
HETATM 1700  O   MOH A 235      46.488  57.139  18.814  1.00 79.42           O  
HETATM 1701  C   MOH A 236      23.310  66.620  -3.264  1.00 64.59           C  
HETATM 1702  O   MOH A 236      24.631  66.909  -2.740  1.00 54.82           O  
HETATM 1703  C   MOH A 237      36.852  83.513   0.307  1.00 41.06           C  
HETATM 1704  O   MOH A 237      37.365  84.262   1.445  1.00 50.35           O  
HETATM 1705  C   MOH A 238      35.451  89.161   2.550  1.00 63.00           C  
HETATM 1706  O   MOH A 238      36.900  89.057   2.394  1.00 60.21           O  
HETATM 1707  C   MOH A 239      31.754  69.331  -3.604  1.00 63.77           C  
HETATM 1708  O   MOH A 239      32.006  69.574  -2.193  1.00 47.33           O  
HETATM 1709  C   MOH A 240      19.415  51.131   8.170  1.00 63.75           C  
HETATM 1710  O   MOH A 240      20.277  51.346   7.002  1.00 63.23           O  
HETATM 1711  C   MOH A 241      37.945  65.506  30.187  1.00 49.26           C  
HETATM 1712  O   MOH A 241      38.534  66.589  29.419  1.00 62.14           O  
HETATM 1713  C   MOH A 242      35.841  81.513  33.285  1.00 51.28           C  
HETATM 1714  O   MOH A 242      36.060  82.904  33.653  1.00 56.61           O  
HETATM 1715  O   HOH A 243      36.842  72.392   8.126  1.00  6.65           O  
HETATM 1716  O   HOH A 244      38.434  68.845  21.154  1.00  7.19           O  
HETATM 1717  O   HOH A 245      34.433  75.747  14.786  1.00  8.13           O  
HETATM 1718  O   HOH A 246      37.812  73.937  10.291  1.00  9.04           O  
HETATM 1719  O   HOH A 247      31.589  71.080   4.139  1.00  9.10           O  
HETATM 1720  O   HOH A 248      36.609  78.686  13.724  1.00  9.45           O  
HETATM 1721  O   HOH A 249      36.646  75.326  13.384  1.00  9.60           O  
HETATM 1722  O   HOH A 250      37.421  72.645  17.157  1.00 10.09           O  
HETATM 1723  O   HOH A 251      44.497  75.974   2.649  1.00 10.12           O  
HETATM 1724  O   HOH A 252      33.069  83.198  17.188  1.00 10.12           O  
HETATM 1725  O   HOH A 253      25.047  62.049  12.821  1.00 10.46           O  
HETATM 1726  O   HOH A 254      28.931  58.228  25.336  1.00 10.59           O  
HETATM 1727  O   HOH A 255      33.457  70.590  15.666  1.00 10.81           O  
HETATM 1728  O   HOH A 256      37.552  78.755   4.472  1.00 10.97           O  
HETATM 1729  O   HOH A 257      44.077  72.214   7.236  1.00 11.79           O  
HETATM 1730  O   HOH A 258      31.952  70.492  18.056  1.00 11.92           O  
HETATM 1731  O   HOH A 259      21.006  80.216  19.857  1.00 12.18           O  
HETATM 1732  O   HOH A 260      21.603  61.906   8.512  1.00 12.51           O  
HETATM 1733  O   HOH A 261      24.439  58.028   7.339  1.00 13.12           O  
HETATM 1734  O   HOH A 262      24.499  76.205   4.494  1.00 13.20           O  
HETATM 1735  O   HOH A 263      30.976  56.953  26.112  1.00 13.50           O  
HETATM 1736  O   HOH A 264      38.771  53.252   3.874  1.00 13.60           O  
HETATM 1737  O   HOH A 265      46.605  74.319  23.273  1.00 14.43           O  
HETATM 1738  O   HOH A 266      33.504  89.570   8.760  1.00 14.51           O  
HETATM 1739  O   HOH A 267      31.599  88.686  19.980  1.00 14.87           O  
HETATM 1740  O   HOH A 268      37.207  83.970  19.104  1.00 15.05           O  
HETATM 1741  O   HOH A 269      30.624  53.677  13.437  1.00 15.33           O  
HETATM 1742  O   HOH A 270      35.336  72.935  16.127  1.00 15.91           O  
HETATM 1743  O   HOH A 271      24.133  67.386  12.347  1.00 17.46           O  
HETATM 1744  O   HOH A 272      38.825  50.457   2.947  1.00 17.79           O  
HETATM 1745  O   HOH A 273      22.068  80.421  26.530  1.00 18.27           O  
HETATM 1746  O   HOH A 274      38.870  85.246  11.067  1.00 18.58           O  
HETATM 1747  O   HOH A 275      23.975  60.139   9.128  1.00 18.70           O  
HETATM 1748  O   HOH A 276      18.145  81.270  21.539  1.00 19.48           O  
HETATM 1749  O   HOH A 277      43.256  71.148  13.493  1.00 19.66           O  
HETATM 1750  O   HOH A 278      22.816  60.693   1.496  1.00 19.89           O  
HETATM 1751  O   HOH A 279      37.498  52.620  22.844  1.00 20.19           O  
HETATM 1752  O   HOH A 280      23.166  61.231  26.187  1.00 20.83           O  
HETATM 1753  O   HOH A 281      28.090  72.320  -2.729  1.00 21.57           O  
HETATM 1754  O   HOH A 282      21.737  67.353  13.423  1.00 21.90           O  
HETATM 1755  O   HOH A 283      29.746  50.888  12.546  1.00 22.18           O  
HETATM 1756  O   HOH A 284      27.166  67.817  24.664  1.00 24.02           O  
HETATM 1757  O   HOH A 285      29.966  69.723  25.413  1.00 24.36           O  
HETATM 1758  O   HOH A 286      31.995  91.336  19.026  1.00 24.42           O  
HETATM 1759  O   HOH A 287      34.898  84.466   2.999  1.00 24.54           O  
HETATM 1760  O   HOH A 288      29.646  55.896  30.880  1.00 24.54           O  
HETATM 1761  O   HOH A 289      40.847  49.072   2.204  1.00 25.15           O  
HETATM 1762  O   HOH A 290      25.230  51.228   7.325  1.00 26.57           O  
HETATM 1763  O   HOH A 291      41.083  76.023  26.095  1.00 26.99           O  
HETATM 1764  O   HOH A 292      42.468  79.839  15.897  1.00 27.20           O  
HETATM 1765  O   HOH A 293      18.623  85.258   0.707  1.00 27.71           O  
HETATM 1766  O   HOH A 294      23.114  86.965  11.067  1.00 28.04           O  
HETATM 1767  O   HOH A 295      27.919  70.249  -1.589  1.00 28.05           O  
HETATM 1768  O   HOH A 296      18.844  85.574  24.589  1.00 28.14           O  
HETATM 1769  O   HOH A 297      19.069  89.612  19.126  1.00 28.46           O  
HETATM 1770  O   HOH A 298      19.981  82.653  27.102  1.00 28.49           O  
HETATM 1771  O   HOH A 299      25.359  52.105  19.036  1.00 29.39           O  
HETATM 1772  O   HOH A 300      39.589  84.315   8.693  1.00 30.55           O  
HETATM 1773  O   HOH A 301      44.785  72.973  16.741  1.00 30.69           O  
HETATM 1774  O   HOH A 302      42.209  60.024   8.014  1.00 30.76           O  
HETATM 1775  O   HOH A 303      44.962  70.210  16.933  1.00 30.95           O  
HETATM 1776  O   HOH A 304      20.402  74.319  -2.764  1.00 31.93           O  
HETATM 1777  O   HOH A 305      26.294  51.171   4.195  1.00 32.65           O  
HETATM 1778  O   HOH A 306      45.269  64.499  15.603  1.00 33.12           O  
HETATM 1779  O   HOH A 307      40.276  82.347  16.247  1.00 33.41           O  
HETATM 1780  O   HOH A 308      23.896  84.727  10.293  1.00 33.48           O  
HETATM 1781  O   HOH A 309      34.799  81.049  26.389  1.00 33.56           O  
HETATM 1782  O   HOH A 310      39.736  77.812  22.056  1.00 33.80           O  
HETATM 1783  O   HOH A 311      46.390  66.377  23.497  1.00 34.01           O  
HETATM 1784  O   HOH A 312      44.679  62.052  14.731  1.00 35.17           O  
HETATM 1785  O   HOH A 313      44.043  57.112  -0.317  1.00 35.46           O  
HETATM 1786  O   HOH A 314      29.379  83.399  -0.333  1.00 35.96           O  
HETATM 1787  O   HOH A 315      42.435  61.431   0.585  1.00 36.39           O  
HETATM 1788  O   HOH A 316      32.511  86.208  28.163  1.00 36.59           O  
HETATM 1789  O   HOH A 317      19.492  81.666  29.049  1.00 36.71           O  
HETATM 1790  O   HOH A 318      43.750  52.791  11.130  1.00 36.91           O  
HETATM 1791  O   HOH A 319      47.848  75.821  21.272  1.00 37.12           O  
HETATM 1792  O   HOH A 320      40.763  50.616  20.202  1.00 37.29           O  
HETATM 1793  O   HOH A 321      38.267  63.245  -1.709  1.00 37.35           O  
HETATM 1794  O   HOH A 322      31.309  82.731   0.029  1.00 37.78           O  
HETATM 1795  O   HOH A 323      25.967  91.566   3.282  1.00 38.45           O  
HETATM 1796  O   HOH A 324      41.767  47.635   4.658  1.00 38.78           O  
HETATM 1797  O   HOH A 325      43.387  52.381  18.897  1.00 39.56           O  
HETATM 1798  O   HOH A 326      44.576  60.621   8.455  1.00 39.57           O  
HETATM 1799  O   HOH A 327      38.092  56.307  27.178  1.00 39.58           O  
HETATM 1800  O   HOH A 328      16.628  71.658  -2.056  1.00 40.07           O  
HETATM 1801  O   HOH A 329      37.140  79.200  20.963  1.00 40.44           O  
HETATM 1802  O   HOH A 330      28.856  49.632   9.456  1.00 40.64           O  
HETATM 1803  O   HOH A 331      26.938  63.197  -0.551  1.00 41.05           O  
HETATM 1804  O   HOH A 332      17.727  65.126  12.082  1.00 41.15           O  
HETATM 1805  O   HOH A 333      45.113  57.330  33.794  1.00 41.20           O  
HETATM 1806  O   HOH A 334      44.431  71.510  11.028  1.00 41.71           O  
HETATM 1807  O   HOH A 335      28.444  80.599  29.467  1.00 42.30           O  
HETATM 1808  O   HOH A 336      17.355  70.020   1.728  1.00 42.73           O  
HETATM 1809  O   HOH A 337      18.557  51.521  12.566  1.00 42.95           O  
HETATM 1810  O   HOH A 338      47.534  57.935  23.389  1.00 43.63           O  
HETATM 1811  O   HOH A 339      27.527  66.302  26.027  1.00 43.86           O  
HETATM 1812  O   HOH A 340      33.678  90.589   6.033  1.00 44.01           O  
HETATM 1813  O   HOH A 341      24.501  88.400   0.443  1.00 44.05           O  
HETATM 1814  O   HOH A 342      30.491  72.092  27.521  1.00 44.18           O  
HETATM 1815  O   HOH A 343      36.865  78.939  25.385  1.00 44.34           O  
HETATM 1816  O   HOH A 344      24.560  71.074  25.182  1.00 44.59           O  
HETATM 1817  O   HOH A 345      28.715  49.356  17.340  1.00 44.64           O  
HETATM 1818  O   HOH A 346      42.572  78.134  18.520  1.00 44.77           O  
HETATM 1819  O   HOH A 347      16.371  82.809  13.878  1.00 45.48           O  
HETATM 1820  O   HOH A 348      44.210  63.898  26.004  1.00 45.52           O  
HETATM 1821  O   HOH A 349      40.107  46.981   6.414  1.00 45.62           O  
HETATM 1822  O   HOH A 350      17.674  62.205   3.760  1.00 45.79           O  
HETATM 1823  O   HOH A 351      35.194  67.839  -3.629  1.00 45.85           O  
HETATM 1824  O   HOH A 352      19.308  95.427  15.470  1.00 45.96           O  
HETATM 1825  O   HOH A 353      19.140  54.446   5.449  1.00 45.96           O  
HETATM 1826  O   HOH A 354      17.028  67.427  14.560  1.00 46.02           O  
HETATM 1827  O   HOH A 355      25.427  82.970  -2.081  1.00 46.42           O  
HETATM 1828  O   HOH A 356      40.220  63.379  -0.351  1.00 47.40           O  
HETATM 1829  O   HOH A 357      32.647  83.010  29.057  1.00 47.40           O  
HETATM 1830  O   HOH A 358      44.525  74.772  18.810  1.00 47.70           O  
HETATM 1831  O   HOH A 359      25.344  61.337   0.663  1.00 47.87           O  
HETATM 1832  O   HOH A 360      19.840  87.098  11.281  1.00 47.88           O  
HETATM 1833  O   HOH A 361      28.717  64.541  -4.827  1.00 48.06           O  
HETATM 1834  O   HOH A 362      16.450  60.622  15.899  1.00 48.15           O  
HETATM 1835  O   HOH A 363      18.829  60.963  21.591  1.00 48.67           O  
HETATM 1836  O   HOH A 364      45.789  66.469  25.743  1.00 48.76           O  
HETATM 1837  O   HOH A 365      17.128  61.472  12.187  1.00 49.11           O  
HETATM 1838  O   HOH A 366      21.192  46.958  11.771  1.00 49.78           O  
HETATM 1839  O   HOH A 367      21.569  54.084  23.793  1.00 50.39           O  
HETATM 1840  O   HOH A 368      25.436  49.812  22.004  1.00 50.46           O  
HETATM 1841  O   HOH A 369      42.870  80.343   8.860  1.00 50.73           O  
HETATM 1842  O   HOH A 370      17.197  66.641  17.484  1.00 50.99           O  
HETATM 1843  O   HOH A 371      23.631  49.977  19.080  1.00 51.32           O  
HETATM 1844  O   HOH A 372      20.879  90.149   9.251  1.00 51.38           O  
HETATM 1845  O   HOH A 373      30.353  44.544  15.300  1.00 51.38           O  
HETATM 1846  O   HOH A 374      20.213  54.596  21.505  1.00 51.53           O  
HETATM 1847  O   HOH A 375      14.856  81.334  21.665  1.00 51.59           O  
HETATM 1848  O   HOH A 376      18.088  86.931  14.957  1.00 52.05           O  
HETATM 1849  O   HOH A 377      21.911  67.159  19.224  1.00 52.25           O  
HETATM 1850  O   HOH A 378      18.693  94.520  13.115  1.00 52.56           O  
HETATM 1851  O   HOH A 379      44.865  74.541  10.498  1.00 52.74           O  
HETATM 1852  O   HOH A 380      22.650  63.877   0.401  1.00 52.75           O  
HETATM 1853  O   HOH A 381      41.204  67.461  28.868  1.00 53.30           O  
HETATM 1854  O   HOH A 382      46.883  73.365  13.948  1.00 53.73           O  
HETATM 1855  O   HOH A 383      40.403  48.226  13.525  1.00 54.14           O  
HETATM 1856  O   HOH A 384      40.216  84.932   6.176  1.00 54.61           O  
HETATM 1857  O   HOH A 385      25.459  65.054  30.083  1.00 54.76           O  
HETATM 1858  O   HOH A 386      22.538  51.451  22.249  1.00 55.49           O  
HETATM 1859  O   HOH A 387      30.047  54.724  -0.664  1.00 56.22           O  
HETATM 1860  O   HOH A 388      29.120  68.621  -3.252  1.00 57.19           O  
HETATM 1861  O   HOH A 389      46.754  55.070  22.123  1.00 57.24           O  
HETATM 1862  O   HOH A 390      30.667  49.626   5.290  1.00 57.72           O  
HETATM 1863  O   HOH A 391      33.374  83.593  -0.541  1.00 57.94           O  
HETATM 1864  O   HOH A 392      47.679  63.607  16.812  1.00 57.96           O  
HETATM 1865  O   HOH A 393      28.955  74.050  -8.632  1.00 58.14           O  
HETATM 1866  O   HOH A 394      28.620  82.682  -6.076  1.00 58.90           O  
HETATM 1867  O   HOH A 395      26.869  72.722  -5.151  1.00 59.08           O  
HETATM 1868  O   HOH A 396      19.982  56.625  17.138  1.00 59.11           O  
HETATM 1869  O   HOH A 397      18.390  57.481  18.602  1.00 59.44           O  
HETATM 1870  O   HOH A 398      24.501  81.771  -6.529  1.00 59.58           O  
HETATM 1871  O   HOH A 399      33.652  91.070  22.619  1.00 59.73           O  
HETATM 1872  O   HOH A 400      40.484  80.971  20.069  1.00 59.90           O  
HETATM 1873  O   HOH A 401      27.159  70.943  26.162  1.00 60.15           O  
HETATM 1874  O   HOH A 402      27.366  80.144  -4.579  1.00 60.20           O  
HETATM 1875  O   HOH A 403      16.664  60.325  -5.628  1.00 60.35           O  
HETATM 1876  O   HOH A 404      47.285  53.826  19.110  1.00 60.39           O  
HETATM 1877  O   HOH A 405      17.730  63.634  15.691  1.00 60.42           O  
HETATM 1878  O   HOH A 406      37.576  58.559  -6.321  1.00 60.55           O  
HETATM 1879  O   HOH A 407      31.782  88.618  27.091  1.00 60.59           O  
HETATM 1880  O   HOH A 408      39.395  88.847   9.809  1.00 60.89           O  
HETATM 1881  O   HOH A 409      47.841  71.188   5.499  1.00 61.31           O  
HETATM 1882  O   HOH A 410      18.507  47.705  11.233  1.00 61.35           O  
HETATM 1883  O   HOH A 411      40.147  83.917  12.796  1.00 61.45           O  
HETATM 1884  O   HOH A 412      27.438  62.269  31.951  1.00 61.49           O  
HETATM 1885  O   HOH A 413      37.827  53.667  -4.559  1.00 61.93           O  
HETATM 1886  O   HOH A 414      14.678  79.135  21.154  1.00 62.12           O  
HETATM 1887  O   HOH A 415      24.672  77.658  29.819  1.00 62.22           O  
HETATM 1888  O   HOH A 416      16.946  67.174  -2.337  1.00 62.47           O  
HETATM 1889  O   HOH A 417      18.786  87.296  18.138  1.00 62.94           O  
HETATM 1890  O   HOH A 418      48.315  59.334  27.592  1.00 62.96           O  
HETATM 1891  O   HOH A 419      32.999  96.433  -2.613  1.00 62.97           O  
HETATM 1892  O   HOH A 420      40.046  87.054   7.922  1.00 63.67           O  
HETATM 1893  O   HOH A 421      39.645  44.869  10.066  1.00 64.06           O  
HETATM 1894  O   HOH A 422      19.730  47.679  14.340  1.00 64.17           O  
HETATM 1895  O   HOH A 423      31.114  95.411  17.172  1.00 64.19           O  
HETATM 1896  O   HOH A 424      45.044  60.757  11.274  1.00 64.26           O  
HETATM 1897  O   HOH A 425      29.855  94.345  18.956  1.00 64.30           O  
HETATM 1898  O   HOH A 426      32.173  74.846  -7.205  1.00 64.68           O  
HETATM 1899  O   HOH A 427      19.249  96.880  12.875  1.00 65.08           O  
HETATM 1900  O   HOH A 428      34.742  44.875  12.689  1.00 65.13           O  
HETATM 1901  O   HOH A 429      14.839  52.068  14.669  1.00 65.82           O  
HETATM 1902  O   HOH A 430      44.783  80.090  19.276  1.00 66.35           O  
HETATM 1903  O   HOH A 431      43.397  45.432   4.821  1.00 66.61           O  
HETATM 1904  O   HOH A 432      22.915  91.201   3.531  1.00 67.13           O  
HETATM 1905  O   HOH A 433      20.029  65.286  24.267  1.00 67.41           O  
HETATM 1906  O   HOH A 434      12.633  50.226  17.422  1.00 68.01           O  
HETATM 1907  O   HOH A 435      39.743  78.260  24.711  1.00 68.69           O  
HETATM 1908  O   HOH A 436      39.376  61.000  -4.843  1.00 69.00           O  
HETATM 1909  O   HOH A 437      32.824  98.004  15.869  1.00 76.84           O  
CONECT  173  496                                                                
CONECT  180  184                                                                
CONECT  184  180  185                                                           
CONECT  185  184  186  188                                                      
CONECT  186  185  187                                                           
CONECT  187  186  190  191  192                                                 
CONECT  188  185  189  193                                                      
CONECT  189  188                                                                
CONECT  190  187                                                                
CONECT  191  187                                                                
CONECT  192  187                                                                
CONECT  193  188                                                                
CONECT  438  763                                                                
CONECT  496  173                                                                
CONECT  763  438                                                                
CONECT 1203 1557                                                                
CONECT 1557 1203                                                                
CONECT 1657 1658                                                                
CONECT 1658 1657                                                                
CONECT 1659 1660                                                                
CONECT 1660 1659                                                                
CONECT 1661 1662                                                                
CONECT 1662 1661                                                                
CONECT 1663 1664                                                                
CONECT 1664 1663                                                                
CONECT 1665 1666                                                                
CONECT 1666 1665                                                                
CONECT 1667 1668                                                                
CONECT 1668 1667                                                                
CONECT 1669 1670                                                                
CONECT 1670 1669                                                                
CONECT 1671 1672                                                                
CONECT 1672 1671                                                                
CONECT 1673 1674                                                                
CONECT 1674 1673                                                                
CONECT 1675 1676                                                                
CONECT 1676 1675                                                                
CONECT 1677 1678                                                                
CONECT 1678 1677                                                                
CONECT 1679 1680                                                                
CONECT 1680 1679                                                                
CONECT 1681 1682                                                                
CONECT 1682 1681                                                                
CONECT 1683 1684                                                                
CONECT 1684 1683                                                                
CONECT 1685 1686                                                                
CONECT 1686 1685                                                                
CONECT 1687 1688                                                                
CONECT 1688 1687                                                                
CONECT 1689 1690                                                                
CONECT 1690 1689                                                                
CONECT 1691 1692                                                                
CONECT 1692 1691                                                                
CONECT 1693 1694                                                                
CONECT 1694 1693                                                                
CONECT 1695 1696                                                                
CONECT 1696 1695                                                                
CONECT 1697 1698                                                                
CONECT 1698 1697                                                                
CONECT 1699 1700                                                                
CONECT 1700 1699                                                                
CONECT 1701 1702                                                                
CONECT 1702 1701                                                                
CONECT 1703 1704                                                                
CONECT 1704 1703                                                                
CONECT 1705 1706                                                                
CONECT 1706 1705                                                                
CONECT 1707 1708                                                                
CONECT 1708 1707                                                                
CONECT 1709 1710                                                                
CONECT 1710 1709                                                                
CONECT 1711 1712                                                                
CONECT 1712 1711                                                                
CONECT 1713 1714                                                                
CONECT 1714 1713                                                                
MASTER      507    0   30    5    8    0   32    6 1908    1   75   17          
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.