HEADER    TRANSFERASE                             22-MAY-00   1E2F              
TITLE     HUMAN THYMIDYLATE KINASE COMPLEXED WITH THYMIDINE MONOPHOSPHATE,      
TITLE    2 ADENOSINE DIPHOSPHATE AND A MAGNESIUM-ION                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: THYMIDYLATE KINASE;                                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: TMPK;                                                       
COMPND   5 EC: 2.7.4.9;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TRANSFERASE, TREANSFERASE, P-LOOP                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.OSTERMANN,I.SCHLICHTING,R.BRUNDIERS,M.KONRAD,J.REINSTEIN,T.VEIT,    
AUTHOR   2 R.S.GOODY,A.LAVIE                                                    
REVDAT   6   24-JUL-19 1E2F    1       REMARK                                   
REVDAT   5   06-MAR-19 1E2F    1       REMARK                                   
REVDAT   4   15-DEC-10 1E2F    1       VERSN                                    
REVDAT   3   24-FEB-09 1E2F    1       VERSN                                    
REVDAT   2   24-JUN-03 1E2F    1       REMARK HET    HETSYN HETNAM              
REVDAT   2 2                   1       FORMUL LINK   SITE   HETATM              
REVDAT   1   17-MAY-01 1E2F    0                                                
JRNL        AUTH   N.OSTERMANN,I.SCHLICHTING,R.BRUNDIERS,M.KONRAD,J.REINSTEIN,  
JRNL        AUTH 2 T.VEIT,R.S.GOODY,A.LAVIE                                     
JRNL        TITL   INSIGHTS INTO THE PHOSPHORYLTRANSFER MECHANISM OF HUMAN      
JRNL        TITL 2 THYMIDYLATE KINASE GAINED FROM CRYSTAL STRUCTURES OF ENZYME  
JRNL        TITL 3 COMPLEXES ALONG THE REACTION COORDINATE                      
JRNL        REF    STRUCTURE                     V.   8   629 2000              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   10873853                                                     
JRNL        DOI    10.1016/S0969-2126(00)00149-0                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 71.70                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 33305                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.210                           
REMARK   3   FREE R VALUE                     : 0.264                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 3365                            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1642                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 81                                      
REMARK   3   SOLVENT ATOMS            : 297                                     
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.011 ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : 1.700 ; 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 1E2F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-MAY-00.                  
REMARK 100 THE DEPOSITION ID IS D_1290004978.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 8.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : BW7B                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.847                              
REMARK 200  MONOCHROMATOR                  : YES                                
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33305                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 71.700                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY                : 3.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.04600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.70                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.15500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.22                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION AT 293 K MIXING 2        
REMARK 280  MICROLITERS OF A SOLUTION CONTAINING THE ENZYME, NUCLEOTIDES,       
REMARK 280  AND 50 MM MGCL2 WITH 2 MICROLITERS OF A SOLUTION CONTAINING 21%     
REMARK 280  PEG 3350, 100 MM TRIS HCL PH 8.0 AND 50 MICROLITERS OF DEAD SEA     
REMARK 280  WATER., PH 8.00                                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       24.65000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       50.65000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       50.65000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       36.97500            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       50.65000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       50.65000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       12.32500            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       50.65000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       50.65000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       36.97500            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       50.65000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       50.65000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       12.32500            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       24.65000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6080 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16920 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -71.0 KCAL/MOL                        
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 350   BIOMT1   2  0.000000 -1.000000  0.000000      101.30000            
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000      101.30000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       24.65000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 MG    MG A 402  LIES ON A SPECIAL POSITION.                          
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 CHAIN A ENGINEERED MUTATION ARG200ALA                                
REMARK 400 GLY, SER, HIS INSERTED AT THE N-TERMINUS                             
REMARK 400 THE ACTIVE SITE CONTAINS A MIXTURE OF NUCLEOTIDES: TMP               
REMARK 400 ADP AND TMP + ANP, THE ORIENTATION OF TMP DIFFERS.                   
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
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     GLN A 136    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 142    CG   CD   CE   NZ                                   
REMARK 470     HIS A 148    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS A 205    CG   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   O    ALA A   140     N    ARG A   143              1.82            
REMARK 500   C    ALA A   140     N    LYS A   142              2.13            
REMARK 500   O    ASP A   139     O    HOH A  2186              2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A  2197     O    HOH A  2198     8666     1.91            
REMARK 500   CD1  ILE A   184     O    HOH A  2018     4455     2.02            
REMARK 500   O    HOH A  2026     O    HOH A  2026     8665     2.08            
REMARK 500   O    HOH A  2032     O    HOH A  2043     8665     2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A   4   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ARG A   4   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    ARG A  16   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG A  16   NE  -  CZ  -  NH2 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG A  24   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ARG A  97   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES          
REMARK 500    ARG A  97   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ALA A 141   CA  -  C   -  N   ANGL. DEV. = -25.6 DEGREES          
REMARK 500    LYS A 142   C   -  N   -  CA  ANGL. DEV. =  16.3 DEGREES          
REMARK 500    LYS A 142   C   -  N   -  CA  ANGL. DEV. = -15.0 DEGREES          
REMARK 500    ARG A 159   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    ARG A 192   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 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    VAL A  14     -179.54    -67.06                                   
REMARK 500    ARG A  97      146.98     74.83                                   
REMARK 500    TYR A  98     -148.25   -151.03                                   
REMARK 500    ALA A 138      -70.82    -68.04                                   
REMARK 500    ALA A 141      -32.61    -37.44                                   
REMARK 500    TYR A 151       -2.79     72.16                                   
REMARK 500    ALA A 202      -34.07    -37.84                                   
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  16        -14.00                                           
REMARK 500    ALA A 141        -24.73                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A2008        DISTANCE =  6.55 ANGSTROMS                       
REMARK 525    HOH A2010        DISTANCE =  6.97 ANGSTROMS                       
REMARK 525    HOH A2011        DISTANCE =  6.11 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 401  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A  20   OG                                                     
REMARK 620 2 ANP A 302   O2B  89.6                                              
REMARK 620 3 ADP A 303   O2B  89.4   3.5                                        
REMARK 620 4 HOH A2277   O    86.6  97.6  94.1                                  
REMARK 620 5 ANP A 302   O3G 173.4  86.2  86.1  89.0                            
REMARK 620 6 HOH A2276   O    89.9 173.6 177.1  88.7  94.8                      
REMARK 620 7 HOH A2286   O    89.7  86.2  89.7 174.7  95.1  87.5                
REMARK 620 8 HOH A2293   O   171.8  97.8  98.2  95.9  14.4  82.4  87.3          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 402  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2161   O                                                      
REMARK 620 2 HOH A2161   O    84.2                                              
REMARK 620 3 HOH A2163   O    95.8  85.2                                        
REMARK 620 4 HOH A2163   O    86.4  97.8 176.5                                  
REMARK 620 5 HOH A2067   O   173.2  93.4  90.3  87.6                            
REMARK 620 6 HOH A2067   O    92.7 170.1  85.8  91.4  90.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TMP A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 402                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1E2D   RELATED DB: PDB                                   
REMARK 900 HUMAN THYMIDYLATE KINASE COMPLEXED WITH THYMIDINE MONOPHOSPHATE,     
REMARK 900 ADENOSINE DIPHOSPHATE AND A MAGNESIUM-ION                            
REMARK 900 RELATED ID: 1E2G   RELATED DB: PDB                                   
REMARK 900 HUMAN THYMIDYLATE KINASE COMPLEXED WITH ADP, TDP AND A MAGNESIUM-ION 
REMARK 900 RELATED ID: 1E9A   RELATED DB: PDB                                   
REMARK 900 HUMAN THYMIDYLATE KINASE COMPLEXED WITH THE BISUBSTRATE INHIBITOR    
REMARK 900 AZTP5A                                                               
REMARK 900 RELATED ID: 1E9B   RELATED DB: PDB                                   
REMARK 900 HUMAN THYMIDYLATE KINASE COMPLEXED WITH AZTMP AND APPNP              
REMARK 900 RELATED ID: 1NN3   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN THYMIDYLATE KINASE WITH D4TMP +ADP        
REMARK 900 RELATED ID: 1E98   RELATED DB: PDB                                   
REMARK 900 WILD TYPE HUMAN THYMIDYLATE KINASE COMPLEXED WITH AZTMP AND ADP      
REMARK 900 RELATED ID: 1E9E   RELATED DB: PDB                                   
REMARK 900 MUTANT HUMAN THYMIDYLATE KINASE (F105Y) COMPLEXED WITH DTMP AND ADP  
REMARK 900 RELATED ID: 1E2E   RELATED DB: PDB                                   
REMARK 900 HUMAN THYMIDYLATE KINASE COMPLEXED WITH THYMIDINE MONOPHOSPHATE,     
REMARK 900 ADENOSINE DIPHOSPHATE,A MAGNESIUM-ION AND ALF3                       
REMARK 900 RELATED ID: 1E2Q   RELATED DB: PDB                                   
REMARK 900 HUMAN THYMIDYLATE KINASE COMPLEXED WITH TP5A AND A MAGNESIUM-ION     
REMARK 900 RELATED ID: 1NMX   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN THYMIDYLATE KINASE WITH FLTMPAND ADP      
REMARK 900 RELATED ID: 1E99   RELATED DB: PDB                                   
REMARK 900 HUMAN THYMIDYLATE KINASE COMPLEXED WITH AZTMP AND ADP                
REMARK 900 RELATED ID: 1NN5   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN THYMIDYLATE KINASE WITH D4TMP +APPNHP     
REMARK 900 RELATED ID: 1NN1   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN THYMIDYLATE KINASE WITH DDTMPAND APPNHP   
REMARK 900 RELATED ID: 1NMZ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN THYMIDYLATE KINASE WITH NH2TMPAND APPNHP  
REMARK 900 RELATED ID: 2XX3   RELATED DB: PDB                                   
REMARK 900 HUMAN THYMIDYLATE KINASE COMPLEXED WITH THYMIDINE BUTENYL            
REMARK 900 PHOSPHONATE MONOPHOSPHATE AND ADP                                    
REMARK 900 RELATED ID: 1E9D   RELATED DB: PDB                                   
REMARK 900 MUTANT HUMAN THYMIDYLATE KINASE (F105Y) COMPLEXED WITH AZTMP AND ADP 
REMARK 900 RELATED ID: 1NMY   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN THYMIDYLATE KINASE WITH FLTMPAND APPNHP   
REMARK 900 RELATED ID: 1NN0   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN THYMIDYLATE KINASE WITH DDTMPAND ADP      
REMARK 900 RELATED ID: 1E9F   RELATED DB: PDB                                   
REMARK 900 MUTANT HUMAN THYMIDYLATE KINASE COMPLEXED WITH TMP AND ADP           
REMARK 900 RELATED ID: 1E9C   RELATED DB: PDB                                   
REMARK 900 MUTANT HUMAN THYMIDYLATE KINASE COMPLEXED WITH TMP AND APPNP         
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 SAMPLE COMTAINS SER183, ILE184, ASP190, AND A ILE191                 
REMARK 999 (CONFIRMED BY THE DNA SEQUENCE AND ELECTRON DENSITY OF               
REMARK 999 SIDE-CHAINS). POSSIBLE ERROR IN SWISSPROT ENTRY.                     
DBREF  1E2F A   -2     0  PDB    1E2F     1E2F            -2      0             
DBREF  1E2F A    1   212  UNP    P23919   KTHY_HUMAN       1    212             
SEQADV 1E2F ALA A  200  UNP  P23919    ARG   200 ENGINEERED MUTATION            
SEQADV 1E2F SER A  183  UNP  P23919    ARG   183 CONFLICT                       
SEQADV 1E2F ILE A  184  UNP  P23919    LEU   184 CONFLICT                       
SEQADV 1E2F ASP A  190  UNP  P23919    GLU   190 CONFLICT                       
SEQADV 1E2F ILE A  191  UNP  P23919    LEU   191 CONFLICT                       
SEQRES   1 A  215  GLY SER HIS MET ALA ALA ARG ARG GLY ALA LEU ILE VAL          
SEQRES   2 A  215  LEU GLU GLY VAL ASP ARG ALA GLY LYS SER THR GLN SER          
SEQRES   3 A  215  ARG LYS LEU VAL GLU ALA LEU CYS ALA ALA GLY HIS ARG          
SEQRES   4 A  215  ALA GLU LEU LEU ARG PHE PRO GLU ARG SER THR GLU ILE          
SEQRES   5 A  215  GLY LYS LEU LEU SER SER TYR LEU GLN LYS LYS SER ASP          
SEQRES   6 A  215  VAL GLU ASP HIS SER VAL HIS LEU LEU PHE SER ALA ASN          
SEQRES   7 A  215  ARG TRP GLU GLN VAL PRO LEU ILE LYS GLU LYS LEU SER          
SEQRES   8 A  215  GLN GLY VAL THR LEU VAL VAL ASP ARG TYR ALA PHE SER          
SEQRES   9 A  215  GLY VAL ALA PHE THR GLY ALA LYS GLU ASN PHE SER LEU          
SEQRES  10 A  215  ASP TRP CYS LYS GLN PRO ASP VAL GLY LEU PRO LYS PRO          
SEQRES  11 A  215  ASP LEU VAL LEU PHE LEU GLN LEU GLN LEU ALA ASP ALA          
SEQRES  12 A  215  ALA LYS ARG GLY ALA PHE GLY HIS GLU ARG TYR GLU ASN          
SEQRES  13 A  215  GLY ALA PHE GLN GLU ARG ALA LEU ARG CYS PHE HIS GLN          
SEQRES  14 A  215  LEU MET LYS ASP THR THR LEU ASN TRP LYS MET VAL ASP          
SEQRES  15 A  215  ALA SER LYS SER ILE GLU ALA VAL HIS GLU ASP ILE ARG          
SEQRES  16 A  215  VAL LEU SER GLU ASP ALA ILE ALA THR ALA THR GLU LYS          
SEQRES  17 A  215  PRO LEU GLY GLU LEU TRP LYS                                  
HET    TMP  A 301      42                                                       
HET    ANP  A 302      31                                                       
HET    ADP  A 303      27                                                       
HET     MG  A 401       1                                                       
HET     MG  A 402       1                                                       
HETNAM     TMP THYMIDINE-5'-PHOSPHATE                                           
HETNAM     ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER                      
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   2  TMP    C10 H15 N2 O8 P                                              
FORMUL   3  ANP    C10 H17 N6 O12 P3                                            
FORMUL   4  ADP    C10 H15 N5 O10 P2                                            
FORMUL   5   MG    2(MG 2+)                                                     
FORMUL   7  HOH   *297(H2 O)                                                    
HELIX    1   1 GLY A   18  ALA A   33  1                                  16    
HELIX    2   2 THR A   47  GLN A   58  1                                  12    
HELIX    3   3 GLU A   64  GLU A   78  1                                  15    
HELIX    4   4 GLN A   79  GLN A   89  1                                  11    
HELIX    5   5 TYR A   98  ALA A  108  1                                  11    
HELIX    6   6 SER A  113  GLN A  119  1                                   7    
HELIX    7   7 PRO A  120  VAL A  122  5                                   3    
HELIX    8   8 GLN A  136  ALA A  141  1                                   6    
HELIX    9   9 ASN A  153  MET A  168  1                                  16    
HELIX   10  10 SER A  183  THR A  201  1                                  19    
HELIX   11  11 ALA A  202  LYS A  205  5                                   4    
SHEET    1   A 5 TRP A 175  ASP A 179  0                                        
SHEET    2   A 5 LEU A 129  GLN A 134  1  N  VAL A 130   O  LYS A 176           
SHEET    3   A 5 LEU A   8  GLU A  12  1  N  VAL A  10   O  LEU A 129           
SHEET    4   A 5 THR A  92  ASP A  96  1  N  LEU A  93   O  ILE A   9           
SHEET    5   A 5 ALA A  37  ARG A  41  1  N  GLU A  38   O  THR A  92           
LINK        MG    MG A 401                 OG  SER A  20     1555   1555  2.10  
LINK        MG    MG A 401                 O2BAANP A 302     1555   1555  1.98  
LINK        MG    MG A 401                 O2BBADP A 303     1555   1555  2.15  
LINK        MG    MG A 401                 O   HOH A2277     1555   1555  2.06  
LINK        MG    MG A 401                 O3GAANP A 302     1555   1555  2.13  
LINK        MG    MG A 401                 O   HOH A2276     1555   1555  2.02  
LINK        MG    MG A 401                 O   HOH A2286     1555   1555  2.11  
LINK        MG    MG A 401                 O   HOH A2293     1555   1555  2.17  
LINK        MG    MG A 402                 O   HOH A2161     1555   8665  2.09  
LINK        MG    MG A 402                 O   HOH A2161     1555   1555  2.08  
LINK        MG    MG A 402                 O   HOH A2163     1555   1555  2.18  
LINK        MG    MG A 402                 O   HOH A2163     1555   8665  2.13  
LINK        MG    MG A 402                 O   HOH A2067     1555   8665  2.10  
LINK        MG    MG A 402                 O   HOH A2067     1555   1555  2.12  
CISPEP   1 PHE A   42    PRO A   43          0        -3.38                     
SITE     1 AC1 22 PHE A  42  PRO A  43  ARG A  45  LEU A  57                    
SITE     2 AC1 22 PHE A  72  ARG A  76  ARG A  97  GLY A 102                    
SITE     3 AC1 22 PHE A 105  TYR A 151  ANP A 302  HOH A2021                    
SITE     4 AC1 22 HOH A2078  HOH A2276  HOH A2277  HOH A2278                    
SITE     5 AC1 22 HOH A2279  HOH A2280  HOH A2281  HOH A2282                    
SITE     6 AC1 22 HOH A2292  HOH A2293                                          
SITE     1 AC2 31 ASP A  15  ARG A  16  ALA A  17  GLY A  18                    
SITE     2 AC2 31 LYS A  19  SER A  20  THR A  21  ARG A  97                    
SITE     3 AC2 31 ARG A 143  LYS A 182  SER A 183  ILE A 184                    
SITE     4 AC2 31 ARG A 192  TMP A 301   MG A 401  HOH A2276                    
SITE     5 AC2 31 HOH A2277  HOH A2278  HOH A2283  HOH A2285                    
SITE     6 AC2 31 HOH A2286  HOH A2288  HOH A2289  HOH A2290                    
SITE     7 AC2 31 HOH A2291  HOH A2292  HOH A2293  HOH A2294                    
SITE     8 AC2 31 HOH A2295  HOH A2296  HOH A2297                               
SITE     1 AC3 26 ARG A  16  ALA A  17  GLY A  18  LYS A  19                    
SITE     2 AC3 26 SER A  20  THR A  21  ARG A 143  LYS A 182                    
SITE     3 AC3 26 SER A 183  ILE A 184  ARG A 192   MG A 401                    
SITE     4 AC3 26 HOH A2277  HOH A2283  HOH A2284  HOH A2285                    
SITE     5 AC3 26 HOH A2286  HOH A2288  HOH A2289  HOH A2290                    
SITE     6 AC3 26 HOH A2291  HOH A2293  HOH A2294  HOH A2295                    
SITE     7 AC3 26 HOH A2296  HOH A2297                                          
SITE     1 AC4  7 SER A  20  ANP A 302  ADP A 303  HOH A2276                    
SITE     2 AC4  7 HOH A2277  HOH A2286  HOH A2293                               
SITE     1 AC5  3 HOH A2067  HOH A2161  HOH A2163                               
CRYST1  101.300  101.300   49.300  90.00  90.00  90.00 P 43 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009872  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009872  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020284        0.00000                         
ATOM      1  N   ALA A   3      -9.272  65.783   0.347  1.00 55.36           N  
ATOM      2  CA  ALA A   3      -8.702  64.792   1.339  1.00 55.07           C  
ATOM      3  C   ALA A   3      -8.370  65.500   2.653  1.00 51.92           C  
ATOM      4  O   ALA A   3      -7.524  66.388   2.687  1.00 52.22           O  
ATOM      5  CB  ALA A   3      -7.413  64.204   0.739  1.00 56.88           C  
ATOM      6  N   ARG A   4      -8.994  65.156   3.754  1.00 46.23           N  
ATOM      7  CA  ARG A   4      -8.896  65.774   5.058  1.00 38.38           C  
ATOM      8  C   ARG A   4      -7.518  65.969   5.665  1.00 28.88           C  
ATOM      9  O   ARG A   4      -6.766  65.039   5.948  1.00 30.81           O  
ATOM     10  CB  ARG A   4      -9.786  64.890   5.967  1.00 39.55           C  
ATOM     11  CG  ARG A   4     -10.888  64.307   5.052  1.00 41.79           C  
ATOM     12  CD  ARG A   4     -11.571  63.148   5.767  1.00 39.74           C  
ATOM     13  NE  ARG A   4     -12.066  63.594   7.064  1.00 41.39           N  
ATOM     14  CZ  ARG A   4     -13.157  64.320   7.281  1.00 45.07           C  
ATOM     15  NH1 ARG A   4     -13.973  64.741   6.331  1.00 46.46           N  
ATOM     16  NH2 ARG A   4     -13.406  64.600   8.560  1.00 47.28           N  
ATOM     17  N   ARG A   5      -7.202  67.254   5.910  1.00 24.66           N  
ATOM     18  CA  ARG A   5      -5.878  67.549   6.473  1.00 21.32           C  
ATOM     19  C   ARG A   5      -5.815  67.177   7.959  1.00 19.90           C  
ATOM     20  O   ARG A   5      -6.804  67.212   8.697  1.00 20.15           O  
ATOM     21  CB  ARG A   5      -5.523  69.034   6.294  1.00 21.86           C  
ATOM     22  CG  ARG A   5      -6.132  70.032   7.245  1.00 18.91           C  
ATOM     23  CD  ARG A   5      -5.621  71.450   7.049  1.00 22.42           C  
ATOM     24  NE  ARG A   5      -6.238  72.465   7.863  1.00 22.36           N  
ATOM     25  CZ  ARG A   5      -5.940  72.813   9.115  1.00 20.18           C  
ATOM     26  NH1 ARG A   5      -4.983  72.117   9.751  1.00 17.53           N  
ATOM     27  NH2 ARG A   5      -6.577  73.790   9.730  1.00 19.59           N  
ATOM     28  N   GLY A   6      -4.580  66.995   8.447  1.00 19.73           N  
ATOM     29  CA  GLY A   6      -4.332  66.792   9.871  1.00 18.63           C  
ATOM     30  C   GLY A   6      -4.370  68.130  10.604  1.00 19.72           C  
ATOM     31  O   GLY A   6      -4.355  69.201   9.982  1.00 18.55           O  
ATOM     32  N   ALA A   7      -4.467  68.099  11.924  1.00 16.59           N  
ATOM     33  CA  ALA A   7      -4.433  69.258  12.778  1.00 14.90           C  
ATOM     34  C   ALA A   7      -3.006  69.514  13.285  1.00 16.08           C  
ATOM     35  O   ALA A   7      -2.267  68.578  13.556  1.00 16.52           O  
ATOM     36  CB  ALA A   7      -5.306  69.088  14.022  1.00 16.69           C  
ATOM     37  N   LEU A   8      -2.680  70.785  13.496  1.00 14.74           N  
ATOM     38  CA  LEU A   8      -1.397  71.165  14.098  1.00 14.26           C  
ATOM     39  C   LEU A   8      -1.698  71.542  15.542  1.00 15.71           C  
ATOM     40  O   LEU A   8      -2.359  72.546  15.835  1.00 16.21           O  
ATOM     41  CB  LEU A   8      -0.848  72.368  13.330  1.00 15.65           C  
ATOM     42  CG  LEU A   8       0.528  72.832  13.892  1.00 13.27           C  
ATOM     43  CD1 LEU A   8       1.558  71.724  13.807  1.00 15.91           C  
ATOM     44  CD2 LEU A   8       0.962  74.030  13.038  1.00 15.72           C  
ATOM     45  N   ILE A   9      -1.252  70.714  16.473  1.00 13.96           N  
ATOM     46  CA  ILE A   9      -1.511  70.912  17.887  1.00 13.89           C  
ATOM     47  C   ILE A   9      -0.206  71.221  18.599  1.00 14.08           C  
ATOM     48  O   ILE A   9       0.727  70.405  18.515  1.00 14.84           O  
ATOM     49  CB  ILE A   9      -2.153  69.636  18.503  1.00 15.42           C  
ATOM     50  CG1 ILE A   9      -3.521  69.410  17.808  1.00 15.32           C  
ATOM     51  CG2 ILE A   9      -2.356  69.811  19.998  1.00 17.23           C  
ATOM     52  CD1 ILE A   9      -4.125  68.053  18.276  1.00 17.81           C  
ATOM     53  N   VAL A  10      -0.153  72.338  19.314  1.00 13.97           N  
ATOM     54  CA  VAL A  10       1.044  72.689  20.067  1.00 14.41           C  
ATOM     55  C   VAL A  10       0.802  72.610  21.549  1.00 15.19           C  
ATOM     56  O   VAL A  10      -0.262  73.037  22.078  1.00 15.72           O  
ATOM     57  CB  VAL A  10       1.447  74.142  19.680  1.00 14.45           C  
ATOM     58  CG1 VAL A  10       2.496  74.738  20.633  1.00 16.71           C  
ATOM     59  CG2 VAL A  10       1.935  74.163  18.236  1.00 16.53           C  
ATOM     60  N   LEU A  11       1.794  72.125  22.296  1.00 14.64           N  
ATOM     61  CA  LEU A  11       1.762  72.141  23.753  1.00 13.38           C  
ATOM     62  C   LEU A  11       2.833  73.148  24.231  1.00 15.30           C  
ATOM     63  O   LEU A  11       3.998  73.090  23.848  1.00 16.32           O  
ATOM     64  CB  LEU A  11       2.032  70.809  24.470  1.00 14.85           C  
ATOM     65  CG  LEU A  11       0.899  69.773  24.438  1.00 14.88           C  
ATOM     66  CD1 LEU A  11       0.759  69.150  23.055  1.00 20.21           C  
ATOM     67  CD2 LEU A  11       1.121  68.692  25.489  1.00 13.77           C  
ATOM     68  N   GLU A  12       2.386  74.099  25.042  1.00 16.16           N  
ATOM     69  CA  GLU A  12       3.252  75.090  25.684  1.00 18.16           C  
ATOM     70  C   GLU A  12       3.030  75.052  27.195  1.00 16.35           C  
ATOM     71  O   GLU A  12       2.092  74.405  27.714  1.00 17.84           O  
ATOM     72  CB  GLU A  12       2.949  76.497  25.133  1.00 16.59           C  
ATOM     73  CG  GLU A  12       3.420  76.818  23.727  1.00 15.09           C  
ATOM     74  CD  GLU A  12       4.933  76.967  23.553  1.00 16.17           C  
ATOM     75  OE1 GLU A  12       5.659  76.751  24.531  1.00 17.46           O  
ATOM     76  OE2 GLU A  12       5.332  77.288  22.415  1.00 16.48           O  
ATOM     77  N  AGLY A  13       3.944  75.726  27.895  0.66 18.89           N  
ATOM     78  N  BGLY A  13       3.833  75.728  28.023  0.33 17.76           N  
ATOM     79  CA AGLY A  13       3.929  75.813  29.343  0.66 23.47           C  
ATOM     80  CA BGLY A  13       3.493  75.618  29.452  0.33 18.83           C  
ATOM     81  C  AGLY A  13       5.337  76.132  29.852  0.66 26.06           C  
ATOM     82  C  BGLY A  13       4.655  75.977  30.340  0.33 20.61           C  
ATOM     83  O  AGLY A  13       6.335  76.050  29.126  0.66 22.70           O  
ATOM     84  O  BGLY A  13       5.779  76.192  29.879  0.33 21.15           O  
ATOM     85  N  AVAL A  14       5.392  76.587  31.110  0.66 26.20           N  
ATOM     86  N  BVAL A  14       4.339  76.071  31.635  0.33 18.80           N  
ATOM     87  CA AVAL A  14       6.674  76.809  31.744  0.66 28.22           C  
ATOM     88  CA BVAL A  14       5.404  76.432  32.572  0.33 16.91           C  
ATOM     89  C  AVAL A  14       7.323  75.429  31.921  0.66 29.30           C  
ATOM     90  C  BVAL A  14       6.337  75.262  32.825  0.33 20.05           C  
ATOM     91  O  AVAL A  14       6.775  74.372  31.615  0.66 27.46           O  
ATOM     92  O  BVAL A  14       6.000  74.099  32.591  0.33 17.83           O  
ATOM     93  CB AVAL A  14       6.576  77.494  33.115  0.66 27.30           C  
ATOM     94  CB BVAL A  14       4.847  76.974  33.897  0.33 17.81           C  
ATOM     95  CG1AVAL A  14       5.929  78.864  32.949  0.66 31.19           C  
ATOM     96  CG1BVAL A  14       3.944  78.160  33.622  0.33 18.61           C  
ATOM     97  CG2AVAL A  14       5.784  76.668  34.116  0.66 31.28           C  
ATOM     98  CG2BVAL A  14       4.127  75.859  34.639  0.33 18.68           C  
ATOM     99  N  AASP A  15       8.515  75.487  32.507  0.66 30.40           N  
ATOM    100  N  BASP A  15       7.539  75.580  33.293  0.33 19.74           N  
ATOM    101  CA AASP A  15       9.208  74.214  32.730  0.66 31.47           C  
ATOM    102  CA BASP A  15       8.575  74.583  33.510  0.33 22.96           C  
ATOM    103  C  AASP A  15       8.612  73.362  33.833  0.66 29.81           C  
ATOM    104  C  BASP A  15       8.081  73.385  34.299  0.33 25.28           C  
ATOM    105  O  AASP A  15       8.154  73.826  34.864  0.66 29.51           O  
ATOM    106  O  BASP A  15       7.334  73.467  35.272  0.33 22.77           O  
ATOM    107  CB AASP A  15      10.669  74.527  32.990  0.66 36.51           C  
ATOM    108  CB BASP A  15       9.820  75.211  34.139  0.33 24.95           C  
ATOM    109  CG AASP A  15      11.255  75.198  31.757  0.66 41.46           C  
ATOM    110  CG BASP A  15      11.040  74.323  33.964  0.33 25.93           C  
ATOM    111  OD1AASP A  15      10.566  75.453  30.754  0.66 44.65           O  
ATOM    112  OD1BASP A  15      11.213  73.742  32.869  0.33 28.16           O  
ATOM    113  OD2AASP A  15      12.468  75.479  31.810  0.66 47.43           O  
ATOM    114  OD2BASP A  15      11.809  74.201  34.936  0.33 29.64           O  
ATOM    115  N  AARG A  16       8.621  72.062  33.517  0.66 27.62           N  
ATOM    116  N  BARG A  16       8.460  72.203  33.803  0.33 26.38           N  
ATOM    117  CA AARG A  16       8.135  71.012  34.385  0.66 28.07           C  
ATOM    118  CA BARG A  16       8.075  70.950  34.427  0.33 26.83           C  
ATOM    119  C  AARG A  16       6.628  70.930  34.500  0.66 22.49           C  
ATOM    120  C  BARG A  16       6.557  70.785  34.457  0.33 24.01           C  
ATOM    121  O  AARG A  16       6.124  70.300  35.404  0.66 24.94           O  
ATOM    122  O  BARG A  16       6.097  69.717  34.867  0.33 24.29           O  
ATOM    123  CB AARG A  16       8.796  71.114  35.773  0.66 28.33           C  
ATOM    124  CB BARG A  16       8.595  70.878  35.865  0.33 27.33           C  
ATOM    125  CG AARG A  16      10.292  70.815  35.700  0.66 32.90           C  
ATOM    126  CG BARG A  16      10.036  70.410  35.966  0.33 31.24           C  
ATOM    127  CD AARG A  16      10.923  70.782  37.084  0.66 36.01           C  
ATOM    128  CD BARG A  16      10.594  70.648  37.364  0.33 33.03           C  
ATOM    129  NE AARG A  16      11.237  72.121  37.574  0.66 36.81           N  
ATOM    130  NE BARG A  16      11.172  71.979  37.491  0.33 34.77           N  
ATOM    131  CZ AARG A  16      11.579  72.355  38.840  0.66 39.79           C  
ATOM    132  CZ BARG A  16      11.714  72.475  38.596  0.33 37.76           C  
ATOM    133  NH1AARG A  16      11.618  71.308  39.658  0.66 40.04           N  
ATOM    134  NH1BARG A  16      11.759  71.755  39.706  0.33 38.56           N  
ATOM    135  NH2AARG A  16      11.867  73.555  39.317  0.66 38.65           N  
ATOM    136  NH2BARG A  16      12.205  73.709  38.576  0.33 38.36           N  
ATOM    137  N   ALA A  17       5.917  71.549  33.561  1.00 25.56           N  
ATOM    138  CA  ALA A  17       4.471  71.521  33.478  1.00 29.14           C  
ATOM    139  C   ALA A  17       3.954  70.191  32.943  1.00 26.73           C  
ATOM    140  O   ALA A  17       2.819  69.806  33.186  1.00 31.01           O  
ATOM    141  CB  ALA A  17       4.047  72.660  32.556  1.00 30.09           C  
ATOM    142  N   GLY A  18       4.816  69.462  32.217  1.00 21.53           N  
ATOM    143  CA  GLY A  18       4.420  68.187  31.654  1.00 17.14           C  
ATOM    144  C   GLY A  18       4.326  68.169  30.120  1.00 17.63           C  
ATOM    145  O   GLY A  18       3.715  67.265  29.529  1.00 16.10           O  
ATOM    146  N   LYS A  19       4.897  69.162  29.436  1.00 17.49           N  
ATOM    147  CA  LYS A  19       4.790  69.245  27.988  1.00 17.22           C  
ATOM    148  C   LYS A  19       5.270  67.984  27.278  1.00 15.52           C  
ATOM    149  O   LYS A  19       4.565  67.476  26.389  1.00 14.83           O  
ATOM    150  CB  LYS A  19       5.552  70.468  27.415  1.00 16.35           C  
ATOM    151  CG  LYS A  19       5.077  71.780  28.052  1.00 16.47           C  
ATOM    152  CD  LYS A  19       5.955  72.940  27.593  1.00 17.92           C  
ATOM    153  CE  LYS A  19       7.396  72.791  28.089  1.00 20.63           C  
ATOM    154  NZ  LYS A  19       7.499  72.920  29.566  1.00 20.07           N  
ATOM    155  N   SER A  20       6.444  67.500  27.674  1.00 15.79           N  
ATOM    156  CA  SER A  20       6.946  66.341  26.894  1.00 13.24           C  
ATOM    157  C   SER A  20       6.207  65.056  27.233  1.00 13.95           C  
ATOM    158  O   SER A  20       5.886  64.283  26.312  1.00 14.74           O  
ATOM    159  CB  SER A  20       8.452  66.181  27.134  1.00 13.51           C  
ATOM    160  OG  SER A  20       9.079  67.435  26.823  1.00 14.82           O  
ATOM    161  N   THR A  21       5.898  64.881  28.517  1.00 14.78           N  
ATOM    162  CA  THR A  21       5.133  63.689  28.900  1.00 14.42           C  
ATOM    163  C   THR A  21       3.764  63.687  28.204  1.00 16.47           C  
ATOM    164  O   THR A  21       3.370  62.665  27.635  1.00 15.76           O  
ATOM    165  CB  THR A  21       4.893  63.639  30.421  1.00 13.31           C  
ATOM    166  OG1 THR A  21       6.152  63.525  31.080  1.00 16.54           O  
ATOM    167  CG2 THR A  21       4.031  62.449  30.852  1.00 14.51           C  
ATOM    168  N   GLN A  22       3.064  64.829  28.244  1.00 13.22           N  
ATOM    169  CA  GLN A  22       1.744  64.853  27.606  1.00 14.80           C  
ATOM    170  C   GLN A  22       1.819  64.812  26.095  1.00 14.29           C  
ATOM    171  O   GLN A  22       0.926  64.245  25.445  1.00 15.37           O  
ATOM    172  CB  GLN A  22       1.002  66.126  28.108  1.00 15.98           C  
ATOM    173  CG  GLN A  22       0.735  66.122  29.608  1.00 16.56           C  
ATOM    174  CD  GLN A  22      -0.097  64.926  30.056  1.00 16.19           C  
ATOM    175  OE1 GLN A  22      -0.832  64.294  29.323  1.00 17.46           O  
ATOM    176  NE2 GLN A  22      -0.008  64.508  31.322  1.00 16.51           N  
ATOM    177  N   SER A  23       2.870  65.366  25.461  1.00 13.47           N  
ATOM    178  CA  SER A  23       2.972  65.256  24.014  1.00 13.87           C  
ATOM    179  C   SER A  23       3.152  63.793  23.590  1.00 13.85           C  
ATOM    180  O   SER A  23       2.474  63.363  22.655  1.00 13.67           O  
ATOM    181  CB  SER A  23       4.087  66.144  23.447  1.00 15.38           C  
ATOM    182  OG ASER A  23       3.918  67.520  23.673  0.50 13.26           O  
ATOM    183  OG BSER A  23       5.337  65.813  23.969  0.50 15.92           O  
ATOM    184  N   ARG A  24       3.991  63.040  24.334  1.00 15.00           N  
ATOM    185  CA  ARG A  24       4.185  61.633  23.996  1.00 13.96           C  
ATOM    186  C   ARG A  24       2.888  60.825  24.213  1.00 13.20           C  
ATOM    187  O   ARG A  24       2.564  60.053  23.325  1.00 15.55           O  
ATOM    188  CB  ARG A  24       5.239  61.018  24.943  1.00 13.34           C  
ATOM    189  CG  ARG A  24       6.655  61.513  24.647  1.00 14.01           C  
ATOM    190  CD  ARG A  24       7.677  60.729  25.480  1.00 15.24           C  
ATOM    191  NE  ARG A  24       7.476  60.850  26.897  1.00 15.92           N  
ATOM    192  CZ  ARG A  24       8.075  61.699  27.732  1.00 13.85           C  
ATOM    193  NH1 ARG A  24       8.936  62.602  27.275  1.00 16.23           N  
ATOM    194  NH2 ARG A  24       7.760  61.587  29.015  1.00 17.04           N  
ATOM    195  N   LYS A  25       2.240  61.065  25.328  1.00 13.88           N  
ATOM    196  CA  LYS A  25       1.013  60.300  25.608  1.00 14.88           C  
ATOM    197  C   LYS A  25      -0.086  60.638  24.623  1.00 14.87           C  
ATOM    198  O   LYS A  25      -0.915  59.774  24.260  1.00 15.14           O  
ATOM    199  CB  LYS A  25       0.516  60.541  27.040  1.00 15.23           C  
ATOM    200  CG  LYS A  25       1.430  59.920  28.101  1.00 15.51           C  
ATOM    201  CD  LYS A  25       0.930  60.017  29.519  1.00 16.24           C  
ATOM    202  CE  LYS A  25      -0.384  59.301  29.819  1.00 17.06           C  
ATOM    203  NZ  LYS A  25      -0.156  57.804  29.727  1.00 22.13           N  
ATOM    204  N   LEU A  26      -0.126  61.920  24.219  1.00 14.15           N  
ATOM    205  CA  LEU A  26      -1.169  62.306  23.257  1.00 13.36           C  
ATOM    206  C   LEU A  26      -1.018  61.580  21.938  1.00 14.49           C  
ATOM    207  O   LEU A  26      -1.989  61.043  21.376  1.00 15.36           O  
ATOM    208  CB  LEU A  26      -1.189  63.829  23.020  1.00 14.82           C  
ATOM    209  CG  LEU A  26      -2.229  64.322  22.011  1.00 14.59           C  
ATOM    210  CD1 LEU A  26      -3.659  63.933  22.422  1.00 15.20           C  
ATOM    211  CD2 LEU A  26      -2.111  65.863  21.963  1.00 16.19           C  
ATOM    212  N   VAL A  27       0.193  61.566  21.361  1.00 14.62           N  
ATOM    213  CA  VAL A  27       0.403  60.869  20.087  1.00 15.27           C  
ATOM    214  C   VAL A  27       0.076  59.386  20.250  1.00 15.61           C  
ATOM    215  O   VAL A  27      -0.629  58.847  19.395  1.00 15.14           O  
ATOM    216  CB  VAL A  27       1.837  61.076  19.585  1.00 15.95           C  
ATOM    217  CG1 VAL A  27       2.109  60.166  18.377  1.00 16.99           C  
ATOM    218  CG2 VAL A  27       2.035  62.549  19.263  1.00 17.09           C  
ATOM    219  N   GLU A  28       0.494  58.794  21.350  1.00 14.57           N  
ATOM    220  CA  GLU A  28       0.196  57.374  21.581  1.00 16.84           C  
ATOM    221  C   GLU A  28      -1.311  57.132  21.547  1.00 15.74           C  
ATOM    222  O   GLU A  28      -1.750  56.149  20.933  1.00 17.77           O  
ATOM    223  CB  GLU A  28       0.814  56.976  22.921  1.00 18.53           C  
ATOM    224  CG  GLU A  28       0.523  55.553  23.397  1.00 24.94           C  
ATOM    225  CD  GLU A  28       1.032  55.313  24.807  1.00 29.66           C  
ATOM    226  OE1 GLU A  28       1.310  56.184  25.651  1.00 29.77           O  
ATOM    227  OE2 GLU A  28       1.163  54.109  25.147  1.00 39.48           O  
ATOM    228  N   ALA A  29      -2.026  57.949  22.290  1.00 14.52           N  
ATOM    229  CA  ALA A  29      -3.480  57.734  22.382  1.00 14.03           C  
ATOM    230  C   ALA A  29      -4.182  57.972  21.054  1.00 14.78           C  
ATOM    231  O   ALA A  29      -5.168  57.276  20.712  1.00 15.75           O  
ATOM    232  CB  ALA A  29      -4.113  58.614  23.433  1.00 16.20           C  
ATOM    233  N   LEU A  30      -3.765  59.008  20.351  1.00 14.35           N  
ATOM    234  CA  LEU A  30      -4.429  59.317  19.082  1.00 14.40           C  
ATOM    235  C   LEU A  30      -4.228  58.169  18.110  1.00 15.94           C  
ATOM    236  O   LEU A  30      -5.178  57.747  17.435  1.00 17.32           O  
ATOM    237  CB  LEU A  30      -3.887  60.639  18.499  1.00 15.45           C  
ATOM    238  CG  LEU A  30      -4.272  61.901  19.261  1.00 14.62           C  
ATOM    239  CD1 LEU A  30      -3.558  63.141  18.665  1.00 15.22           C  
ATOM    240  CD2 LEU A  30      -5.791  62.148  19.229  1.00 16.92           C  
ATOM    241  N   CYS A  31      -2.999  57.638  18.028  1.00 16.41           N  
ATOM    242  CA  CYS A  31      -2.729  56.528  17.121  1.00 16.73           C  
ATOM    243  C   CYS A  31      -3.505  55.272  17.523  1.00 19.14           C  
ATOM    244  O   CYS A  31      -4.008  54.573  16.630  1.00 19.27           O  
ATOM    245  CB  CYS A  31      -1.223  56.240  17.110  1.00 15.14           C  
ATOM    246  SG  CYS A  31      -0.286  57.494  16.244  1.00 17.32           S  
ATOM    247  N   ALA A  32      -3.668  55.066  18.829  1.00 17.23           N  
ATOM    248  CA  ALA A  32      -4.421  53.895  19.278  1.00 16.09           C  
ATOM    249  C   ALA A  32      -5.900  54.023  18.957  1.00 18.56           C  
ATOM    250  O   ALA A  32      -6.584  52.990  18.935  1.00 18.02           O  
ATOM    251  CB  ALA A  32      -4.186  53.627  20.755  1.00 18.22           C  
ATOM    252  N   ALA A  33      -6.379  55.240  18.759  1.00 15.67           N  
ATOM    253  CA  ALA A  33      -7.760  55.517  18.424  1.00 17.72           C  
ATOM    254  C   ALA A  33      -7.944  55.693  16.930  1.00 16.15           C  
ATOM    255  O   ALA A  33      -8.977  56.229  16.478  1.00 16.50           O  
ATOM    256  CB  ALA A  33      -8.315  56.724  19.165  1.00 18.10           C  
ATOM    257  N   GLY A  34      -6.992  55.240  16.119  1.00 16.66           N  
ATOM    258  CA  GLY A  34      -7.103  55.242  14.691  1.00 17.19           C  
ATOM    259  C   GLY A  34      -6.683  56.477  13.922  1.00 16.51           C  
ATOM    260  O   GLY A  34      -6.876  56.497  12.708  1.00 16.95           O  
ATOM    261  N   HIS A  35      -6.175  57.493  14.664  1.00 16.98           N  
ATOM    262  CA  HIS A  35      -5.686  58.649  13.903  1.00 15.74           C  
ATOM    263  C   HIS A  35      -4.245  58.381  13.448  1.00 16.93           C  
ATOM    264  O   HIS A  35      -3.506  57.592  14.029  1.00 18.89           O  
ATOM    265  CB  HIS A  35      -5.600  59.868  14.830  1.00 14.11           C  
ATOM    266  CG  HIS A  35      -6.917  60.293  15.400  1.00 16.91           C  
ATOM    267  ND1 HIS A  35      -7.807  61.050  14.647  1.00 20.18           N  
ATOM    268  CD2 HIS A  35      -7.488  60.101  16.609  1.00 19.02           C  
ATOM    269  CE1 HIS A  35      -8.866  61.320  15.396  1.00 18.79           C  
ATOM    270  NE2 HIS A  35      -8.694  60.770  16.591  1.00 19.94           N  
ATOM    271  N   ARG A  36      -3.877  59.098  12.391  1.00 17.78           N  
ATOM    272  CA  ARG A  36      -2.491  59.226  11.976  1.00 20.27           C  
ATOM    273  C   ARG A  36      -1.936  60.484  12.705  1.00 18.42           C  
ATOM    274  O   ARG A  36      -2.465  61.561  12.456  1.00 20.67           O  
ATOM    275  CB  ARG A  36      -2.378  59.436  10.468  1.00 26.71           C  
ATOM    276  CG  ARG A  36      -2.693  58.125   9.710  1.00 31.94           C  
ATOM    277  CD  ARG A  36      -2.562  58.397   8.209  1.00 41.47           C  
ATOM    278  NE  ARG A  36      -1.232  58.913   7.877  1.00 50.91           N  
ATOM    279  CZ  ARG A  36      -0.947  59.545   6.740  1.00 55.08           C  
ATOM    280  NH1 ARG A  36      -1.909  59.737   5.846  1.00 57.44           N  
ATOM    281  NH2 ARG A  36       0.284  59.978   6.500  1.00 57.21           N  
ATOM    282  N   ALA A  37      -1.043  60.259  13.637  1.00 17.74           N  
ATOM    283  CA  ALA A  37      -0.500  61.409  14.382  1.00 16.32           C  
ATOM    284  C   ALA A  37       0.975  61.155  14.637  1.00 19.31           C  
ATOM    285  O   ALA A  37       1.398  60.020  14.837  1.00 19.57           O  
ATOM    286  CB  ALA A  37      -1.264  61.550  15.701  1.00 18.82           C  
ATOM    287  N   GLU A  38       1.760  62.236  14.609  1.00 17.55           N  
ATOM    288  CA  GLU A  38       3.183  62.125  14.861  1.00 16.03           C  
ATOM    289  C   GLU A  38       3.700  63.253  15.774  1.00 15.49           C  
ATOM    290  O   GLU A  38       3.031  64.288  15.832  1.00 17.11           O  
ATOM    291  CB  GLU A  38       3.969  62.228  13.533  1.00 19.17           C  
ATOM    292  CG  GLU A  38       3.684  61.034  12.646  1.00 20.25           C  
ATOM    293  CD  GLU A  38       4.447  61.064  11.336  1.00 28.30           C  
ATOM    294  OE1 GLU A  38       5.604  61.534  11.366  1.00 34.37           O  
ATOM    295  OE2 GLU A  38       3.917  60.593  10.305  1.00 28.43           O  
ATOM    296  N   LEU A  39       4.759  62.973  16.499  1.00 16.03           N  
ATOM    297  CA  LEU A  39       5.345  63.945  17.423  1.00 15.55           C  
ATOM    298  C   LEU A  39       6.505  64.759  16.863  1.00 15.66           C  
ATOM    299  O   LEU A  39       7.415  64.217  16.201  1.00 18.28           O  
ATOM    300  CB  LEU A  39       5.865  63.111  18.607  1.00 16.06           C  
ATOM    301  CG  LEU A  39       6.521  63.870  19.757  1.00 18.39           C  
ATOM    302  CD1 LEU A  39       5.546  64.801  20.458  1.00 20.08           C  
ATOM    303  CD2 LEU A  39       7.086  62.858  20.759  1.00 20.30           C  
ATOM    304  N   LEU A  40       6.476  66.057  17.158  1.00 16.30           N  
ATOM    305  CA  LEU A  40       7.585  66.967  16.821  1.00 15.11           C  
ATOM    306  C   LEU A  40       7.919  67.733  18.079  1.00 16.60           C  
ATOM    307  O   LEU A  40       7.122  67.805  19.025  1.00 17.13           O  
ATOM    308  CB  LEU A  40       7.174  67.961  15.740  1.00 16.90           C  
ATOM    309  CG  LEU A  40       6.874  67.390  14.351  1.00 20.92           C  
ATOM    310  CD1 LEU A  40       6.507  68.528  13.406  1.00 26.29           C  
ATOM    311  CD2 LEU A  40       8.025  66.566  13.799  1.00 27.72           C  
ATOM    312  N   ARG A  41       9.137  68.314  18.135  1.00 17.80           N  
ATOM    313  CA  ARG A  41       9.478  69.134  19.309  1.00 17.38           C  
ATOM    314  C   ARG A  41      10.386  70.274  18.837  1.00 18.32           C  
ATOM    315  O   ARG A  41      11.086  70.093  17.832  1.00 19.02           O  
ATOM    316  CB  ARG A  41      10.174  68.330  20.393  1.00 20.16           C  
ATOM    317  CG  ARG A  41      11.645  68.056  20.121  1.00 22.34           C  
ATOM    318  CD  ARG A  41      11.895  67.169  18.919  1.00 24.34           C  
ATOM    319  NE  ARG A  41      11.021  65.986  19.031  1.00 27.13           N  
ATOM    320  CZ  ARG A  41      10.647  65.269  17.975  1.00 30.15           C  
ATOM    321  NH1 ARG A  41      11.064  65.551  16.740  1.00 30.52           N  
ATOM    322  NH2 ARG A  41       9.832  64.245  18.183  1.00 26.43           N  
ATOM    323  N   PHE A  42      10.375  71.379  19.573  1.00 15.52           N  
ATOM    324  CA  PHE A  42      11.337  72.459  19.255  1.00 14.92           C  
ATOM    325  C   PHE A  42      11.992  72.812  20.574  1.00 14.93           C  
ATOM    326  O   PHE A  42      11.302  72.860  21.603  1.00 17.08           O  
ATOM    327  CB  PHE A  42      10.591  73.646  18.619  1.00 13.68           C  
ATOM    328  CG  PHE A  42      10.191  73.296  17.199  1.00 15.69           C  
ATOM    329  CD1 PHE A  42      11.161  73.191  16.196  1.00 13.40           C  
ATOM    330  CD2 PHE A  42       8.860  73.000  16.921  1.00 14.39           C  
ATOM    331  CE1 PHE A  42      10.773  72.803  14.915  1.00 15.63           C  
ATOM    332  CE2 PHE A  42       8.491  72.637  15.631  1.00 17.07           C  
ATOM    333  CZ  PHE A  42       9.438  72.529  14.616  1.00 17.27           C  
ATOM    334  N   PRO A  43      13.304  73.079  20.586  1.00 14.91           N  
ATOM    335  CA  PRO A  43      14.111  72.968  19.396  1.00 15.52           C  
ATOM    336  C   PRO A  43      14.306  71.537  18.937  1.00 16.75           C  
ATOM    337  O   PRO A  43      14.256  70.599  19.775  1.00 16.92           O  
ATOM    338  CB  PRO A  43      15.514  73.471  19.836  1.00 16.73           C  
ATOM    339  CG  PRO A  43      15.493  73.306  21.295  1.00 16.37           C  
ATOM    340  CD  PRO A  43      14.071  73.419  21.794  1.00 18.00           C  
ATOM    341  N   GLU A  44      14.496  71.395  17.651  1.00 16.78           N  
ATOM    342  CA  GLU A  44      14.762  70.106  17.001  1.00 17.27           C  
ATOM    343  C   GLU A  44      16.298  70.025  16.964  1.00 19.17           C  
ATOM    344  O   GLU A  44      16.893  70.682  16.111  1.00 18.53           O  
ATOM    345  CB  GLU A  44      14.113  70.068  15.635  1.00 18.25           C  
ATOM    346  CG  GLU A  44      14.524  68.856  14.789  1.00 20.71           C  
ATOM    347  CD  GLU A  44      14.349  67.547  15.527  1.00 28.70           C  
ATOM    348  OE1 GLU A  44      13.164  67.251  15.840  1.00 28.34           O  
ATOM    349  OE2 GLU A  44      15.365  66.887  15.797  1.00 29.58           O  
ATOM    350  N   ARG A  45      16.849  69.305  17.925  1.00 19.51           N  
ATOM    351  CA  ARG A  45      18.322  69.369  18.070  1.00 22.70           C  
ATOM    352  C   ARG A  45      19.102  68.551  17.088  1.00 23.13           C  
ATOM    353  O   ARG A  45      20.355  68.594  17.201  1.00 27.70           O  
ATOM    354  CB  ARG A  45      18.682  69.008  19.510  1.00 22.58           C  
ATOM    355  CG  ARG A  45      18.057  69.866  20.583  1.00 23.20           C  
ATOM    356  CD  ARG A  45      18.467  69.349  21.966  1.00 31.13           C  
ATOM    357  NE  ARG A  45      17.721  70.097  22.979  1.00 29.95           N  
ATOM    358  CZ  ARG A  45      18.303  70.524  24.108  1.00 30.64           C  
ATOM    359  NH1 ARG A  45      19.575  70.290  24.394  1.00 36.95           N  
ATOM    360  NH2 ARG A  45      17.588  71.190  24.997  1.00 30.64           N  
ATOM    361  N   SER A  46      18.490  67.875  16.142  1.00 21.51           N  
ATOM    362  CA  SER A  46      19.252  67.015  15.246  1.00 26.03           C  
ATOM    363  C   SER A  46      19.867  67.726  14.052  1.00 28.38           C  
ATOM    364  O   SER A  46      20.748  67.140  13.412  1.00 26.83           O  
ATOM    365  CB  SER A  46      18.364  65.874  14.726  1.00 26.45           C  
ATOM    366  OG  SER A  46      17.285  66.379  13.944  1.00 30.66           O  
ATOM    367  N   THR A  47      19.382  68.908  13.706  1.00 20.30           N  
ATOM    368  CA  THR A  47      19.904  69.569  12.499  1.00 18.74           C  
ATOM    369  C   THR A  47      21.152  70.351  12.859  1.00 17.36           C  
ATOM    370  O   THR A  47      21.502  70.435  14.028  1.00 19.79           O  
ATOM    371  CB  THR A  47      18.838  70.512  11.927  1.00 20.13           C  
ATOM    372  OG1 THR A  47      18.575  71.560  12.890  1.00 19.50           O  
ATOM    373  CG2 THR A  47      17.531  69.830  11.550  1.00 20.18           C  
ATOM    374  N   GLU A  48      21.790  70.952  11.849  1.00 19.63           N  
ATOM    375  CA  GLU A  48      23.004  71.738  12.131  1.00 18.77           C  
ATOM    376  C   GLU A  48      22.684  72.898  13.056  1.00 17.46           C  
ATOM    377  O   GLU A  48      23.344  73.167  14.059  1.00 19.03           O  
ATOM    378  CB  GLU A  48      23.582  72.240  10.801  1.00 20.63           C  
ATOM    379  CG  GLU A  48      24.056  71.081   9.915  1.00 22.70           C  
ATOM    380  CD  GLU A  48      24.272  71.520   8.482  1.00 21.18           C  
ATOM    381  OE1 GLU A  48      23.276  71.694   7.747  1.00 23.42           O  
ATOM    382  OE2 GLU A  48      25.459  71.651   8.070  1.00 26.14           O  
ATOM    383  N   ILE A  49      21.553  73.569  12.747  1.00 18.95           N  
ATOM    384  CA  ILE A  49      21.140  74.651  13.636  1.00 17.72           C  
ATOM    385  C   ILE A  49      20.776  74.121  15.015  1.00 18.74           C  
ATOM    386  O   ILE A  49      21.075  74.643  16.083  1.00 18.08           O  
ATOM    387  CB  ILE A  49      19.918  75.383  13.018  1.00 18.93           C  
ATOM    388  CG1 ILE A  49      20.336  76.192  11.776  1.00 19.94           C  
ATOM    389  CG2 ILE A  49      19.273  76.254  14.082  1.00 18.27           C  
ATOM    390  CD1 ILE A  49      19.150  76.787  11.024  1.00 18.88           C  
ATOM    391  N   GLY A  50      20.082  72.960  15.000  1.00 18.85           N  
ATOM    392  CA  GLY A  50      19.679  72.328  16.256  1.00 19.66           C  
ATOM    393  C   GLY A  50      20.867  72.032  17.162  1.00 18.34           C  
ATOM    394  O   GLY A  50      20.793  72.133  18.383  1.00 17.03           O  
ATOM    395  N   LYS A  51      21.969  71.616  16.543  1.00 20.57           N  
ATOM    396  CA  LYS A  51      23.196  71.353  17.315  1.00 21.51           C  
ATOM    397  C   LYS A  51      23.765  72.594  17.984  1.00 21.32           C  
ATOM    398  O   LYS A  51      24.234  72.565  19.134  1.00 21.18           O  
ATOM    399  CB  LYS A  51      24.227  70.682  16.392  1.00 23.94           C  
ATOM    400  CG  LYS A  51      23.867  69.256  16.058  1.00 24.98           C  
ATOM    401  CD  LYS A  51      24.905  68.604  15.157  1.00 29.16           C  
ATOM    402  CE  LYS A  51      24.655  67.104  15.078  1.00 37.60           C  
ATOM    403  NZ  LYS A  51      23.541  66.781  14.144  1.00 41.64           N  
ATOM    404  N   LEU A  52      23.720  73.737  17.269  1.00 19.83           N  
ATOM    405  CA  LEU A  52      24.164  74.989  17.859  1.00 18.75           C  
ATOM    406  C   LEU A  52      23.310  75.359  19.074  1.00 18.24           C  
ATOM    407  O   LEU A  52      23.779  75.832  20.100  1.00 20.54           O  
ATOM    408  CB  LEU A  52      24.060  76.133  16.813  1.00 18.98           C  
ATOM    409  CG  LEU A  52      24.842  75.893  15.525  1.00 19.34           C  
ATOM    410  CD1 LEU A  52      24.702  77.106  14.598  1.00 22.95           C  
ATOM    411  CD2 LEU A  52      26.322  75.620  15.792  1.00 24.58           C  
ATOM    412  N   LEU A  53      21.985  75.123  18.926  1.00 16.59           N  
ATOM    413  CA  LEU A  53      21.046  75.451  19.988  1.00 18.19           C  
ATOM    414  C   LEU A  53      21.219  74.548  21.206  1.00 17.82           C  
ATOM    415  O   LEU A  53      21.168  75.001  22.347  1.00 19.54           O  
ATOM    416  CB  LEU A  53      19.605  75.326  19.435  1.00 17.32           C  
ATOM    417  CG  LEU A  53      19.223  76.396  18.407  1.00 18.58           C  
ATOM    418  CD1 LEU A  53      17.839  76.038  17.849  1.00 19.53           C  
ATOM    419  CD2 LEU A  53      19.218  77.787  19.020  1.00 18.12           C  
ATOM    420  N   SER A  54      21.525  73.268  20.910  1.00 20.30           N  
ATOM    421  CA  SER A  54      21.724  72.325  22.003  1.00 20.15           C  
ATOM    422  C   SER A  54      22.973  72.685  22.804  1.00 21.69           C  
ATOM    423  O   SER A  54      22.934  72.709  24.024  1.00 20.16           O  
ATOM    424  CB  SER A  54      21.860  70.890  21.460  1.00 21.16           C  
ATOM    425  OG  SER A  54      21.855  70.024  22.600  1.00 22.29           O  
ATOM    426  N   SER A  55      24.032  73.055  22.077  1.00 20.12           N  
ATOM    427  CA  SER A  55      25.259  73.445  22.794  1.00 23.27           C  
ATOM    428  C   SER A  55      25.024  74.684  23.618  1.00 21.99           C  
ATOM    429  O   SER A  55      25.381  74.731  24.797  1.00 22.66           O  
ATOM    430  CB  SER A  55      26.380  73.592  21.755  1.00 20.90           C  
ATOM    431  OG  SER A  55      27.481  74.229  22.415  1.00 26.31           O  
ATOM    432  N   TYR A  56      24.290  75.682  23.089  1.00 20.51           N  
ATOM    433  CA  TYR A  56      23.964  76.889  23.842  1.00 21.01           C  
ATOM    434  C   TYR A  56      23.169  76.599  25.109  1.00 22.78           C  
ATOM    435  O   TYR A  56      23.435  77.134  26.193  1.00 25.56           O  
ATOM    436  CB  TYR A  56      23.100  77.813  22.955  1.00 20.24           C  
ATOM    437  CG  TYR A  56      22.536  79.032  23.652  1.00 18.27           C  
ATOM    438  CD1 TYR A  56      23.366  80.062  24.063  1.00 19.05           C  
ATOM    439  CD2 TYR A  56      21.173  79.164  23.906  1.00 20.23           C  
ATOM    440  CE1 TYR A  56      22.869  81.186  24.693  1.00 20.14           C  
ATOM    441  CE2 TYR A  56      20.658  80.294  24.533  1.00 21.80           C  
ATOM    442  CZ  TYR A  56      21.515  81.294  24.923  1.00 20.95           C  
ATOM    443  OH  TYR A  56      21.049  82.427  25.561  1.00 21.27           O  
ATOM    444  N   LEU A  57      22.133  75.760  24.980  1.00 19.99           N  
ATOM    445  CA  LEU A  57      21.273  75.464  26.121  1.00 21.49           C  
ATOM    446  C   LEU A  57      22.019  74.699  27.212  1.00 23.90           C  
ATOM    447  O   LEU A  57      21.699  74.879  28.385  1.00 26.94           O  
ATOM    448  CB  LEU A  57      20.036  74.666  25.670  1.00 18.78           C  
ATOM    449  CG  LEU A  57      19.010  75.534  24.908  1.00 20.97           C  
ATOM    450  CD1 LEU A  57      17.946  74.620  24.280  1.00 21.31           C  
ATOM    451  CD2 LEU A  57      18.369  76.558  25.819  1.00 19.70           C  
ATOM    452  N   GLN A  58      23.003  73.914  26.820  1.00 24.63           N  
ATOM    453  CA  GLN A  58      23.818  73.166  27.777  1.00 27.46           C  
ATOM    454  C   GLN A  58      24.931  74.007  28.392  1.00 31.33           C  
ATOM    455  O   GLN A  58      25.691  73.527  29.240  1.00 29.88           O  
ATOM    456  CB  GLN A  58      24.467  71.985  27.034  1.00 26.36           C  
ATOM    457  CG  GLN A  58      23.471  70.892  26.690  1.00 28.83           C  
ATOM    458  CD  GLN A  58      24.186  69.769  25.953  1.00 32.91           C  
ATOM    459  OE1 GLN A  58      25.097  69.181  26.540  1.00 36.15           O  
ATOM    460  NE2 GLN A  58      23.832  69.508  24.707  1.00 36.57           N  
ATOM    461  N   LYS A  59      25.043  75.259  27.964  1.00 31.34           N  
ATOM    462  CA  LYS A  59      26.039  76.209  28.435  1.00 34.34           C  
ATOM    463  C   LYS A  59      27.434  75.785  27.984  1.00 33.13           C  
ATOM    464  O   LYS A  59      28.447  76.157  28.584  1.00 34.28           O  
ATOM    465  CB  LYS A  59      26.024  76.396  29.951  1.00 36.64           C  
ATOM    466  CG  LYS A  59      24.641  76.383  30.576  1.00 41.15           C  
ATOM    467  CD  LYS A  59      24.212  77.780  30.983  1.00 46.66           C  
ATOM    468  CE  LYS A  59      24.971  78.243  32.214  1.00 49.22           C  
ATOM    469  NZ  LYS A  59      24.525  77.526  33.442  1.00 54.34           N  
ATOM    470  N   LYS A  60      27.490  75.007  26.915  1.00 28.33           N  
ATOM    471  CA  LYS A  60      28.759  74.555  26.356  1.00 29.96           C  
ATOM    472  C   LYS A  60      29.285  75.628  25.410  1.00 29.52           C  
ATOM    473  O   LYS A  60      30.432  75.647  24.972  1.00 30.91           O  
ATOM    474  CB  LYS A  60      28.631  73.202  25.669  1.00 28.58           C  
ATOM    475  CG  LYS A  60      28.420  72.061  26.677  1.00 31.29           C  
ATOM    476  CD  LYS A  60      28.368  70.714  25.968  1.00 35.63           C  
ATOM    477  CE  LYS A  60      28.729  69.582  26.916  1.00 41.83           C  
ATOM    478  NZ  LYS A  60      27.562  68.864  27.484  1.00 41.94           N  
ATOM    479  N   SER A  61      28.383  76.564  25.073  1.00 28.13           N  
ATOM    480  CA  SER A  61      28.773  77.666  24.202  1.00 29.00           C  
ATOM    481  C   SER A  61      27.897  78.864  24.537  1.00 27.88           C  
ATOM    482  O   SER A  61      26.816  78.691  25.093  1.00 26.34           O  
ATOM    483  CB  SER A  61      28.627  77.304  22.725  1.00 30.10           C  
ATOM    484  OG  SER A  61      27.239  77.132  22.433  1.00 26.83           O  
ATOM    485  N   ASP A  62      28.433  80.051  24.261  1.00 25.30           N  
ATOM    486  CA  ASP A  62      27.684  81.284  24.454  1.00 28.87           C  
ATOM    487  C   ASP A  62      27.321  81.799  23.064  1.00 24.62           C  
ATOM    488  O   ASP A  62      28.091  81.627  22.108  1.00 25.67           O  
ATOM    489  CB  ASP A  62      28.470  82.305  25.280  1.00 33.40           C  
ATOM    490  CG  ASP A  62      28.713  81.768  26.686  1.00 40.41           C  
ATOM    491  OD1 ASP A  62      27.793  81.171  27.292  1.00 41.75           O  
ATOM    492  OD2 ASP A  62      29.847  81.944  27.174  1.00 46.31           O  
ATOM    493  N   VAL A  63      26.141  82.357  22.950  1.00 20.37           N  
ATOM    494  CA  VAL A  63      25.621  82.879  21.691  1.00 19.56           C  
ATOM    495  C   VAL A  63      24.944  84.224  21.982  1.00 20.75           C  
ATOM    496  O   VAL A  63      24.220  84.375  22.959  1.00 21.97           O  
ATOM    497  CB  VAL A  63      24.597  81.946  20.994  1.00 20.51           C  
ATOM    498  CG1 VAL A  63      24.198  82.432  19.597  1.00 19.87           C  
ATOM    499  CG2 VAL A  63      25.212  80.548  20.867  1.00 23.21           C  
ATOM    500  N   GLU A  64      25.243  85.204  21.131  1.00 19.86           N  
ATOM    501  CA  GLU A  64      24.651  86.533  21.247  1.00 18.59           C  
ATOM    502  C   GLU A  64      23.126  86.405  21.252  1.00 19.54           C  
ATOM    503  O   GLU A  64      22.615  85.585  20.489  1.00 17.90           O  
ATOM    504  CB  GLU A  64      25.193  87.405  20.102  1.00 18.33           C  
ATOM    505  CG  GLU A  64      24.949  88.887  20.321  1.00 17.93           C  
ATOM    506  CD  GLU A  64      23.567  89.380  19.951  1.00 18.00           C  
ATOM    507  OE1 GLU A  64      22.924  88.695  19.129  1.00 17.71           O  
ATOM    508  OE2 GLU A  64      23.152  90.414  20.513  1.00 21.02           O  
ATOM    509  N   ASP A  65      22.452  87.155  22.121  1.00 18.09           N  
ATOM    510  CA  ASP A  65      21.018  86.923  22.343  1.00 18.58           C  
ATOM    511  C   ASP A  65      20.130  87.061  21.133  1.00 19.73           C  
ATOM    512  O   ASP A  65      19.102  86.363  20.968  1.00 18.20           O  
ATOM    513  CB  ASP A  65      20.450  87.826  23.439  1.00 19.28           C  
ATOM    514  CG  ASP A  65      20.908  87.484  24.836  1.00 23.55           C  
ATOM    515  OD1 ASP A  65      21.103  86.307  25.167  1.00 22.68           O  
ATOM    516  OD2 ASP A  65      21.072  88.469  25.599  1.00 29.41           O  
ATOM    517  N   HIS A  66      20.403  88.040  20.266  1.00 16.76           N  
ATOM    518  CA  HIS A  66      19.590  88.203  19.058  1.00 17.10           C  
ATOM    519  C   HIS A  66      19.871  87.049  18.107  1.00 15.93           C  
ATOM    520  O   HIS A  66      18.958  86.494  17.488  1.00 16.12           O  
ATOM    521  CB  HIS A  66      19.866  89.544  18.363  1.00 16.68           C  
ATOM    522  CG  HIS A  66      19.672  90.769  19.223  1.00 17.35           C  
ATOM    523  ND1 HIS A  66      20.583  91.190  20.157  1.00 18.86           N  
ATOM    524  CD2 HIS A  66      18.606  91.608  19.248  1.00 18.76           C  
ATOM    525  CE1 HIS A  66      20.081  92.282  20.737  1.00 19.58           C  
ATOM    526  NE2 HIS A  66      18.919  92.580  20.211  1.00 20.78           N  
ATOM    527  N   SER A  67      21.156  86.711  17.893  1.00 15.97           N  
ATOM    528  CA  SER A  67      21.502  85.581  17.053  1.00 15.95           C  
ATOM    529  C   SER A  67      20.811  84.288  17.503  1.00 17.33           C  
ATOM    530  O   SER A  67      20.239  83.611  16.627  1.00 16.29           O  
ATOM    531  CB  SER A  67      23.034  85.337  17.120  1.00 16.43           C  
ATOM    532  OG  SER A  67      23.331  84.208  16.295  1.00 19.24           O  
ATOM    533  N   VAL A  68      20.850  84.018  18.805  1.00 16.60           N  
ATOM    534  CA  VAL A  68      20.252  82.748  19.241  1.00 17.31           C  
ATOM    535  C   VAL A  68      18.733  82.753  19.057  1.00 17.05           C  
ATOM    536  O   VAL A  68      18.178  81.740  18.618  1.00 15.80           O  
ATOM    537  CB  VAL A  68      20.685  82.369  20.650  1.00 19.09           C  
ATOM    538  CG1 VAL A  68      19.893  83.041  21.743  1.00 20.27           C  
ATOM    539  CG2 VAL A  68      20.604  80.833  20.724  1.00 20.03           C  
ATOM    540  N   HIS A  69      18.132  83.916  19.234  1.00 15.79           N  
ATOM    541  CA  HIS A  69      16.680  84.002  19.000  1.00 14.87           C  
ATOM    542  C   HIS A  69      16.326  83.643  17.571  1.00 16.83           C  
ATOM    543  O   HIS A  69      15.378  82.922  17.232  1.00 16.91           O  
ATOM    544  CB  HIS A  69      16.259  85.453  19.329  1.00 16.54           C  
ATOM    545  CG  HIS A  69      14.776  85.590  19.110  1.00 17.04           C  
ATOM    546  ND1 HIS A  69      13.909  85.112  20.050  1.00 18.32           N  
ATOM    547  CD2 HIS A  69      14.057  86.131  18.101  1.00 15.93           C  
ATOM    548  CE1 HIS A  69      12.672  85.334  19.629  1.00 17.20           C  
ATOM    549  NE2 HIS A  69      12.735  85.964  18.475  1.00 17.64           N  
ATOM    550  N   LEU A  70      17.139  84.172  16.611  1.00 15.41           N  
ATOM    551  CA  LEU A  70      16.929  83.929  15.192  1.00 14.16           C  
ATOM    552  C   LEU A  70      17.231  82.472  14.839  1.00 16.76           C  
ATOM    553  O   LEU A  70      16.501  81.902  14.047  1.00 17.26           O  
ATOM    554  CB  LEU A  70      17.795  84.894  14.370  1.00 16.47           C  
ATOM    555  CG  LEU A  70      17.430  86.371  14.604  1.00 16.37           C  
ATOM    556  CD1 LEU A  70      18.375  87.261  13.788  1.00 16.97           C  
ATOM    557  CD2 LEU A  70      16.023  86.690  14.111  1.00 20.33           C  
ATOM    558  N   LEU A  71      18.218  81.859  15.510  1.00 16.80           N  
ATOM    559  CA  LEU A  71      18.461  80.413  15.272  1.00 14.81           C  
ATOM    560  C   LEU A  71      17.258  79.585  15.759  1.00 14.89           C  
ATOM    561  O   LEU A  71      16.881  78.676  14.995  1.00 16.34           O  
ATOM    562  CB  LEU A  71      19.714  79.948  16.029  1.00 14.51           C  
ATOM    563  CG  LEU A  71      21.073  80.466  15.526  1.00 19.20           C  
ATOM    564  CD1 LEU A  71      22.179  79.894  16.399  1.00 18.02           C  
ATOM    565  CD2 LEU A  71      21.344  80.105  14.070  1.00 24.12           C  
ATOM    566  N   PHE A  72      16.682  79.935  16.894  1.00 16.00           N  
ATOM    567  CA  PHE A  72      15.464  79.187  17.333  1.00 16.42           C  
ATOM    568  C   PHE A  72      14.366  79.279  16.286  1.00 15.64           C  
ATOM    569  O   PHE A  72      13.668  78.293  15.985  1.00 15.80           O  
ATOM    570  CB  PHE A  72      14.985  79.697  18.690  1.00 16.43           C  
ATOM    571  CG  PHE A  72      15.662  79.082  19.882  1.00 15.51           C  
ATOM    572  CD1 PHE A  72      15.449  77.740  20.179  1.00 18.71           C  
ATOM    573  CD2 PHE A  72      16.469  79.841  20.720  1.00 16.89           C  
ATOM    574  CE1 PHE A  72      16.016  77.145  21.284  1.00 18.14           C  
ATOM    575  CE2 PHE A  72      17.053  79.260  21.836  1.00 19.31           C  
ATOM    576  CZ  PHE A  72      16.831  77.898  22.113  1.00 20.45           C  
ATOM    577  N   SER A  73      14.172  80.484  15.699  1.00 15.36           N  
ATOM    578  CA  SER A  73      13.129  80.616  14.668  1.00 13.69           C  
ATOM    579  C   SER A  73      13.468  79.860  13.394  1.00 14.98           C  
ATOM    580  O   SER A  73      12.668  79.180  12.736  1.00 15.81           O  
ATOM    581  CB  SER A  73      12.833  82.109  14.415  1.00 14.12           C  
ATOM    582  OG  SER A  73      11.845  82.205  13.403  1.00 15.37           O  
ATOM    583  N   ALA A  74      14.740  79.966  12.921  1.00 14.34           N  
ATOM    584  CA  ALA A  74      15.161  79.237  11.746  1.00 13.64           C  
ATOM    585  C   ALA A  74      15.003  77.727  11.937  1.00 15.62           C  
ATOM    586  O   ALA A  74      14.695  77.072  10.925  1.00 15.60           O  
ATOM    587  CB  ALA A  74      16.621  79.557  11.407  1.00 16.72           C  
ATOM    588  N   ASN A  75      15.171  77.274  13.177  1.00 15.82           N  
ATOM    589  CA  ASN A  75      15.003  75.848  13.486  1.00 15.67           C  
ATOM    590  C   ASN A  75      13.562  75.426  13.235  1.00 16.59           C  
ATOM    591  O   ASN A  75      13.311  74.261  12.921  1.00 17.53           O  
ATOM    592  CB  ASN A  75      15.447  75.645  14.934  1.00 16.46           C  
ATOM    593  CG  ASN A  75      15.471  74.213  15.431  1.00 18.14           C  
ATOM    594  OD1 ASN A  75      14.776  73.904  16.385  1.00 17.74           O  
ATOM    595  ND2 ASN A  75      16.294  73.340  14.829  1.00 19.45           N  
ATOM    596  N   ARG A  76      12.605  76.338  13.454  1.00 14.43           N  
ATOM    597  CA  ARG A  76      11.213  76.006  13.100  1.00 15.77           C  
ATOM    598  C   ARG A  76      10.993  76.050  11.606  1.00 16.68           C  
ATOM    599  O   ARG A  76      10.418  75.155  10.952  1.00 16.22           O  
ATOM    600  CB  ARG A  76      10.225  76.971  13.814  1.00 15.02           C  
ATOM    601  CG  ARG A  76      10.057  76.567  15.273  1.00 13.16           C  
ATOM    602  CD  ARG A  76       9.163  77.566  15.986  1.00 14.29           C  
ATOM    603  NE  ARG A  76       9.768  78.906  16.235  1.00 15.04           N  
ATOM    604  CZ  ARG A  76      10.577  79.124  17.265  1.00 15.59           C  
ATOM    605  NH1 ARG A  76      11.005  78.132  18.052  1.00 15.29           N  
ATOM    606  NH2 ARG A  76      10.998  80.378  17.503  1.00 16.75           N  
ATOM    607  N   TRP A  77      11.508  77.109  10.914  1.00 15.46           N  
ATOM    608  CA  TRP A  77      11.309  77.251   9.489  1.00 16.38           C  
ATOM    609  C   TRP A  77      11.854  76.072   8.676  1.00 15.60           C  
ATOM    610  O   TRP A  77      11.246  75.710   7.683  1.00 16.27           O  
ATOM    611  CB  TRP A  77      11.926  78.597   9.012  1.00 16.33           C  
ATOM    612  CG  TRP A  77      11.029  79.777   9.269  1.00 15.98           C  
ATOM    613  CD1 TRP A  77      11.201  80.757  10.221  1.00 15.58           C  
ATOM    614  CD2 TRP A  77       9.810  80.075   8.568  1.00 14.09           C  
ATOM    615  NE1 TRP A  77      10.170  81.666  10.133  1.00 17.42           N  
ATOM    616  CE2 TRP A  77       9.320  81.270   9.128  1.00 14.65           C  
ATOM    617  CE3 TRP A  77       9.098  79.468   7.541  1.00 15.55           C  
ATOM    618  CZ2 TRP A  77       8.134  81.884   8.687  1.00 15.96           C  
ATOM    619  CZ3 TRP A  77       7.933  80.069   7.086  1.00 17.32           C  
ATOM    620  CH2 TRP A  77       7.451  81.251   7.674  1.00 18.15           C  
ATOM    621  N   GLU A  78      13.001  75.530   9.086  1.00 16.70           N  
ATOM    622  CA  GLU A  78      13.596  74.404   8.370  1.00 14.56           C  
ATOM    623  C   GLU A  78      12.696  73.171   8.433  1.00 17.83           C  
ATOM    624  O   GLU A  78      12.828  72.293   7.560  1.00 19.98           O  
ATOM    625  CB  GLU A  78      15.041  74.147   8.822  1.00 16.99           C  
ATOM    626  CG  GLU A  78      15.186  73.625  10.245  1.00 19.77           C  
ATOM    627  CD  GLU A  78      16.644  73.446  10.662  1.00 18.31           C  
ATOM    628  OE1 GLU A  78      17.531  73.449   9.777  1.00 20.68           O  
ATOM    629  OE2 GLU A  78      16.879  73.333  11.867  1.00 18.21           O  
ATOM    630  N   GLN A  79      11.754  73.147   9.370  1.00 15.53           N  
ATOM    631  CA  GLN A  79      10.811  72.013   9.398  1.00 18.63           C  
ATOM    632  C   GLN A  79       9.489  72.329   8.720  1.00 17.80           C  
ATOM    633  O   GLN A  79       8.571  71.473   8.746  1.00 19.21           O  
ATOM    634  CB  GLN A  79      10.516  71.664  10.859  1.00 18.52           C  
ATOM    635  CG  GLN A  79      11.726  71.192  11.656  1.00 20.58           C  
ATOM    636  CD  GLN A  79      12.232  69.832  11.225  1.00 28.27           C  
ATOM    637  OE1 GLN A  79      11.667  69.104  10.421  1.00 29.00           O  
ATOM    638  NE2 GLN A  79      13.383  69.465  11.788  1.00 39.87           N  
ATOM    639  N   VAL A  80       9.300  73.549   8.196  1.00 16.53           N  
ATOM    640  CA  VAL A  80       7.986  73.907   7.602  1.00 18.21           C  
ATOM    641  C   VAL A  80       7.630  73.073   6.408  1.00 19.14           C  
ATOM    642  O   VAL A  80       6.468  72.631   6.347  1.00 18.42           O  
ATOM    643  CB  VAL A  80       7.907  75.428   7.390  1.00 16.66           C  
ATOM    644  CG1 VAL A  80       6.746  75.869   6.498  1.00 18.11           C  
ATOM    645  CG2 VAL A  80       7.726  76.065   8.762  1.00 15.60           C  
ATOM    646  N   PRO A  81       8.504  72.740   5.479  1.00 18.02           N  
ATOM    647  CA  PRO A  81       8.124  71.894   4.342  1.00 18.69           C  
ATOM    648  C   PRO A  81       7.622  70.530   4.839  1.00 19.06           C  
ATOM    649  O   PRO A  81       6.524  70.149   4.398  1.00 21.56           O  
ATOM    650  CB  PRO A  81       9.395  71.819   3.512  1.00 20.14           C  
ATOM    651  CG  PRO A  81      10.052  73.127   3.833  1.00 20.29           C  
ATOM    652  CD  PRO A  81       9.872  73.312   5.337  1.00 19.99           C  
ATOM    653  N   LEU A  82       8.257  69.963   5.828  1.00 17.69           N  
ATOM    654  CA  LEU A  82       7.785  68.689   6.398  1.00 17.60           C  
ATOM    655  C   LEU A  82       6.439  68.854   7.090  1.00 19.40           C  
ATOM    656  O   LEU A  82       5.545  68.007   6.926  1.00 20.82           O  
ATOM    657  CB  LEU A  82       8.768  68.165   7.448  1.00 21.43           C  
ATOM    658  CG  LEU A  82       8.294  66.981   8.299  1.00 26.74           C  
ATOM    659  CD1 LEU A  82       8.175  65.751   7.401  1.00 31.54           C  
ATOM    660  CD2 LEU A  82       9.260  66.678   9.438  1.00 34.12           C  
ATOM    661  N   ILE A  83       6.273  69.918   7.862  1.00 16.68           N  
ATOM    662  CA  ILE A  83       5.019  70.128   8.572  1.00 16.14           C  
ATOM    663  C   ILE A  83       3.870  70.237   7.590  1.00 20.48           C  
ATOM    664  O   ILE A  83       2.800  69.634   7.761  1.00 18.42           O  
ATOM    665  CB  ILE A  83       5.120  71.419   9.436  1.00 17.29           C  
ATOM    666  CG1 ILE A  83       6.035  71.114  10.624  1.00 17.01           C  
ATOM    667  CG2 ILE A  83       3.751  71.929   9.869  1.00 18.52           C  
ATOM    668  CD1 ILE A  83       6.484  72.392  11.364  1.00 18.41           C  
ATOM    669  N   LYS A  84       4.079  71.046   6.540  1.00 18.12           N  
ATOM    670  CA  LYS A  84       2.992  71.204   5.558  1.00 21.71           C  
ATOM    671  C   LYS A  84       2.705  69.905   4.822  1.00 21.88           C  
ATOM    672  O   LYS A  84       1.516  69.620   4.600  1.00 21.54           O  
ATOM    673  CB  LYS A  84       3.337  72.349   4.580  1.00 20.45           C  
ATOM    674  CG  LYS A  84       3.239  73.724   5.224  1.00 22.39           C  
ATOM    675  CD  LYS A  84       3.538  74.768   4.127  1.00 25.07           C  
ATOM    676  CE  LYS A  84       3.577  76.152   4.745  1.00 29.87           C  
ATOM    677  NZ  LYS A  84       3.276  77.198   3.710  1.00 37.75           N  
ATOM    678  N   GLU A  85       3.731  69.128   4.511  1.00 19.10           N  
ATOM    679  CA  GLU A  85       3.531  67.868   3.807  1.00 23.19           C  
ATOM    680  C   GLU A  85       2.738  66.898   4.700  1.00 21.88           C  
ATOM    681  O   GLU A  85       1.718  66.387   4.218  1.00 23.33           O  
ATOM    682  CB  GLU A  85       4.863  67.264   3.417  1.00 26.60           C  
ATOM    683  CG  GLU A  85       4.742  66.025   2.538  1.00 34.46           C  
ATOM    684  CD  GLU A  85       6.124  65.539   2.124  1.00 40.31           C  
ATOM    685  OE1 GLU A  85       6.732  64.825   2.943  1.00 42.28           O  
ATOM    686  OE2 GLU A  85       6.576  65.885   1.012  1.00 44.94           O  
ATOM    687  N   LYS A  86       3.190  66.750   5.938  1.00 19.49           N  
ATOM    688  CA  LYS A  86       2.446  65.812   6.799  1.00 19.50           C  
ATOM    689  C   LYS A  86       1.002  66.229   7.002  1.00 20.71           C  
ATOM    690  O   LYS A  86       0.084  65.383   6.901  1.00 18.98           O  
ATOM    691  CB  LYS A  86       3.168  65.726   8.140  1.00 18.90           C  
ATOM    692  CG  LYS A  86       4.492  65.001   8.045  1.00 21.44           C  
ATOM    693  CD  LYS A  86       4.332  63.499   7.969  1.00 25.70           C  
ATOM    694  CE  LYS A  86       5.688  62.806   7.932  1.00 30.63           C  
ATOM    695  NZ  LYS A  86       5.486  61.327   8.079  1.00 32.95           N  
ATOM    696  N   LEU A  87       0.742  67.495   7.295  1.00 19.11           N  
ATOM    697  CA  LEU A  87      -0.636  67.939   7.501  1.00 19.19           C  
ATOM    698  C   LEU A  87      -1.472  67.713   6.242  1.00 21.56           C  
ATOM    699  O   LEU A  87      -2.595  67.206   6.304  1.00 21.26           O  
ATOM    700  CB  LEU A  87      -0.701  69.416   7.933  1.00 19.50           C  
ATOM    701  CG  LEU A  87      -0.017  69.724   9.278  1.00 18.56           C  
ATOM    702  CD1 LEU A  87       0.125  71.245   9.385  1.00 18.03           C  
ATOM    703  CD2 LEU A  87      -0.817  69.158  10.455  1.00 19.01           C  
ATOM    704  N   SER A  88      -0.887  67.985   5.069  1.00 20.60           N  
ATOM    705  CA  SER A  88      -1.679  67.819   3.838  1.00 23.83           C  
ATOM    706  C   SER A  88      -1.982  66.350   3.591  1.00 25.96           C  
ATOM    707  O   SER A  88      -2.977  66.066   2.909  1.00 26.11           O  
ATOM    708  CB  SER A  88      -0.959  68.475   2.665  1.00 22.66           C  
ATOM    709  OG  SER A  88       0.133  67.689   2.225  1.00 27.88           O  
ATOM    710  N   GLN A  89      -1.173  65.457   4.117  1.00 20.01           N  
ATOM    711  CA  GLN A  89      -1.399  64.019   3.963  1.00 22.37           C  
ATOM    712  C   GLN A  89      -2.396  63.460   4.979  1.00 23.77           C  
ATOM    713  O   GLN A  89      -2.688  62.258   4.917  1.00 25.83           O  
ATOM    714  CB  GLN A  89      -0.080  63.276   4.079  1.00 25.14           C  
ATOM    715  CG  GLN A  89       0.808  63.481   2.857  1.00 28.69           C  
ATOM    716  CD  GLN A  89       2.246  63.113   3.144  1.00 34.19           C  
ATOM    717  OE1 GLN A  89       2.623  62.839   4.295  1.00 37.66           O  
ATOM    718  NE2 GLN A  89       3.080  63.122   2.107  1.00 38.09           N  
ATOM    719  N   GLY A  90      -2.892  64.279   5.869  1.00 20.82           N  
ATOM    720  CA  GLY A  90      -3.881  63.848   6.866  1.00 20.66           C  
ATOM    721  C   GLY A  90      -3.264  63.450   8.192  1.00 22.17           C  
ATOM    722  O   GLY A  90      -3.966  62.902   9.056  1.00 22.27           O  
ATOM    723  N   VAL A  91      -1.984  63.798   8.390  1.00 20.38           N  
ATOM    724  CA  VAL A  91      -1.296  63.439   9.626  1.00 18.36           C  
ATOM    725  C   VAL A  91      -1.407  64.579  10.630  1.00 18.08           C  
ATOM    726  O   VAL A  91      -1.009  65.708  10.286  1.00 20.47           O  
ATOM    727  CB  VAL A  91       0.191  63.148   9.383  1.00 18.12           C  
ATOM    728  CG1 VAL A  91       0.862  62.754  10.707  1.00 18.07           C  
ATOM    729  CG2 VAL A  91       0.412  62.040   8.347  1.00 19.42           C  
ATOM    730  N   THR A  92      -1.964  64.348  11.792  1.00 16.06           N  
ATOM    731  CA  THR A  92      -2.034  65.358  12.846  1.00 15.59           C  
ATOM    732  C   THR A  92      -0.659  65.411  13.493  1.00 16.29           C  
ATOM    733  O   THR A  92      -0.010  64.383  13.787  1.00 17.99           O  
ATOM    734  CB  THR A  92      -3.105  64.959  13.885  1.00 16.43           C  
ATOM    735  OG1 THR A  92      -4.350  65.331  13.245  1.00 18.35           O  
ATOM    736  CG2 THR A  92      -2.956  65.696  15.200  1.00 17.50           C  
ATOM    737  N   LEU A  93      -0.156  66.614  13.762  1.00 14.82           N  
ATOM    738  CA  LEU A  93       1.145  66.792  14.382  1.00 13.47           C  
ATOM    739  C   LEU A  93       0.980  67.409  15.763  1.00 14.72           C  
ATOM    740  O   LEU A  93       0.294  68.413  15.952  1.00 18.63           O  
ATOM    741  CB  LEU A  93       2.025  67.736  13.519  1.00 15.80           C  
ATOM    742  CG  LEU A  93       2.313  67.209  12.112  1.00 15.39           C  
ATOM    743  CD1 LEU A  93       2.988  68.329  11.289  1.00 17.25           C  
ATOM    744  CD2 LEU A  93       3.133  65.932  12.147  1.00 17.65           C  
ATOM    745  N   VAL A  94       1.596  66.733  16.727  1.00 15.74           N  
ATOM    746  CA  VAL A  94       1.619  67.168  18.123  1.00 14.43           C  
ATOM    747  C   VAL A  94       3.009  67.740  18.390  1.00 17.23           C  
ATOM    748  O   VAL A  94       3.980  66.991  18.222  1.00 15.51           O  
ATOM    749  CB  VAL A  94       1.316  66.002  19.087  1.00 15.98           C  
ATOM    750  CG1 VAL A  94       1.455  66.417  20.545  1.00 17.37           C  
ATOM    751  CG2 VAL A  94      -0.091  65.485  18.764  1.00 16.72           C  
ATOM    752  N   VAL A  95       3.091  69.006  18.750  1.00 14.98           N  
ATOM    753  CA  VAL A  95       4.396  69.704  18.827  1.00 14.46           C  
ATOM    754  C   VAL A  95       4.683  70.205  20.228  1.00 15.19           C  
ATOM    755  O   VAL A  95       3.928  70.990  20.817  1.00 16.26           O  
ATOM    756  CB  VAL A  95       4.287  70.907  17.860  1.00 15.39           C  
ATOM    757  CG1 VAL A  95       5.669  71.564  17.792  1.00 17.66           C  
ATOM    758  CG2 VAL A  95       3.807  70.412  16.490  1.00 16.03           C  
ATOM    759  N   ASP A  96       5.792  69.712  20.790  1.00 14.43           N  
ATOM    760  CA  ASP A  96       6.262  70.061  22.124  1.00 13.51           C  
ATOM    761  C   ASP A  96       7.096  71.340  22.051  1.00 14.79           C  
ATOM    762  O   ASP A  96       8.272  71.278  21.671  1.00 15.32           O  
ATOM    763  CB  ASP A  96       7.121  68.880  22.598  1.00 15.74           C  
ATOM    764  CG  ASP A  96       7.645  68.938  24.002  1.00 15.64           C  
ATOM    765  OD1 ASP A  96       7.412  69.945  24.726  1.00 16.58           O  
ATOM    766  OD2 ASP A  96       8.346  67.946  24.365  1.00 18.51           O  
ATOM    767  N   ARG A  97       6.472  72.464  22.349  1.00 13.77           N  
ATOM    768  CA  ARG A  97       6.969  73.826  22.203  1.00 16.20           C  
ATOM    769  C   ARG A  97       6.980  74.305  20.743  1.00 16.01           C  
ATOM    770  O   ARG A  97       7.190  73.544  19.793  1.00 16.61           O  
ATOM    771  CB  ARG A  97       8.371  74.097  22.768  1.00 16.68           C  
ATOM    772  CG  ARG A  97       8.505  73.823  24.270  1.00 16.00           C  
ATOM    773  CD  ARG A  97       9.892  74.405  24.637  1.00 17.51           C  
ATOM    774  NE  ARG A  97      10.279  74.136  26.011  1.00 20.34           N  
ATOM    775  CZ  ARG A  97       9.972  74.925  27.042  1.00 19.17           C  
ATOM    776  NH1 ARG A  97       9.228  76.037  26.957  1.00 20.18           N  
ATOM    777  NH2 ARG A  97      10.435  74.564  28.248  1.00 25.42           N  
ATOM    778  N   TYR A  98       6.736  75.633  20.612  1.00 13.66           N  
ATOM    779  CA  TYR A  98       6.726  76.224  19.269  1.00 16.20           C  
ATOM    780  C   TYR A  98       7.152  77.692  19.351  1.00 16.50           C  
ATOM    781  O   TYR A  98       7.958  78.012  20.217  1.00 16.19           O  
ATOM    782  CB  TYR A  98       5.365  76.088  18.622  1.00 16.04           C  
ATOM    783  CG  TYR A  98       5.157  76.214  17.131  1.00 14.72           C  
ATOM    784  CD1 TYR A  98       5.886  75.471  16.210  1.00 13.59           C  
ATOM    785  CD2 TYR A  98       4.170  77.063  16.616  1.00 14.99           C  
ATOM    786  CE1 TYR A  98       5.656  75.535  14.847  1.00 15.22           C  
ATOM    787  CE2 TYR A  98       3.921  77.154  15.259  1.00 15.16           C  
ATOM    788  CZ  TYR A  98       4.672  76.403  14.364  1.00 12.64           C  
ATOM    789  OH  TYR A  98       4.409  76.421  13.009  1.00 16.98           O  
ATOM    790  N   ALA A  99       6.626  78.529  18.473  1.00 16.21           N  
ATOM    791  CA  ALA A  99       7.052  79.939  18.446  1.00 13.65           C  
ATOM    792  C   ALA A  99       6.773  80.688  19.729  1.00 17.10           C  
ATOM    793  O   ALA A  99       7.412  81.702  20.070  1.00 17.73           O  
ATOM    794  CB  ALA A  99       6.317  80.610  17.282  1.00 14.89           C  
ATOM    795  N   PHE A 100       5.758  80.247  20.491  1.00 14.74           N  
ATOM    796  CA  PHE A 100       5.371  80.921  21.736  1.00 15.92           C  
ATOM    797  C   PHE A 100       6.508  80.829  22.738  1.00 15.17           C  
ATOM    798  O   PHE A 100       6.847  81.827  23.394  1.00 16.16           O  
ATOM    799  CB  PHE A 100       4.048  80.327  22.294  1.00 16.80           C  
ATOM    800  CG  PHE A 100       3.057  80.195  21.167  1.00 15.99           C  
ATOM    801  CD1 PHE A 100       2.446  81.322  20.621  1.00 18.41           C  
ATOM    802  CD2 PHE A 100       2.769  78.939  20.623  1.00 16.65           C  
ATOM    803  CE1 PHE A 100       1.571  81.178  19.549  1.00 19.91           C  
ATOM    804  CE2 PHE A 100       1.918  78.820  19.546  1.00 18.09           C  
ATOM    805  CZ  PHE A 100       1.303  79.943  19.006  1.00 21.31           C  
ATOM    806  N   SER A 101       7.146  79.655  22.888  1.00 14.77           N  
ATOM    807  CA  SER A 101       8.319  79.529  23.756  1.00 15.29           C  
ATOM    808  C   SER A 101       9.448  80.450  23.205  1.00 15.75           C  
ATOM    809  O   SER A 101      10.155  81.050  24.023  1.00 16.80           O  
ATOM    810  CB  SER A 101       8.865  78.109  23.753  1.00 14.97           C  
ATOM    811  OG  SER A 101       8.157  77.308  24.719  1.00 17.64           O  
ATOM    812  N   GLY A 102       9.565  80.464  21.895  1.00 15.10           N  
ATOM    813  CA  GLY A 102      10.568  81.322  21.229  1.00 16.90           C  
ATOM    814  C   GLY A 102      10.438  82.768  21.708  1.00 18.09           C  
ATOM    815  O   GLY A 102      11.446  83.385  22.112  1.00 17.94           O  
ATOM    816  N   VAL A 103       9.219  83.281  21.674  1.00 15.11           N  
ATOM    817  CA  VAL A 103       8.992  84.674  22.098  1.00 16.42           C  
ATOM    818  C   VAL A 103       9.090  84.878  23.586  1.00 18.96           C  
ATOM    819  O   VAL A 103       9.678  85.847  24.103  1.00 17.29           O  
ATOM    820  CB  VAL A 103       7.620  85.138  21.551  1.00 16.72           C  
ATOM    821  CG1 VAL A 103       7.225  86.517  22.088  1.00 18.01           C  
ATOM    822  CG2 VAL A 103       7.635  85.164  20.023  1.00 19.64           C  
ATOM    823  N   ALA A 104       8.467  83.964  24.372  1.00 16.48           N  
ATOM    824  CA  ALA A 104       8.486  84.095  25.820  1.00 17.29           C  
ATOM    825  C   ALA A 104       9.874  84.028  26.438  1.00 19.22           C  
ATOM    826  O   ALA A 104      10.149  84.790  27.378  1.00 20.63           O  
ATOM    827  CB  ALA A 104       7.581  83.007  26.423  1.00 17.22           C  
ATOM    828  N   PHE A 105      10.744  83.156  25.948  1.00 17.82           N  
ATOM    829  CA  PHE A 105      12.085  83.019  26.484  1.00 19.16           C  
ATOM    830  C   PHE A 105      12.987  84.193  26.087  1.00 20.41           C  
ATOM    831  O   PHE A 105      13.648  84.736  26.991  1.00 21.84           O  
ATOM    832  CB  PHE A 105      12.668  81.618  26.199  1.00 18.19           C  
ATOM    833  CG  PHE A 105      12.078  80.663  27.217  1.00 19.46           C  
ATOM    834  CD1 PHE A 105      10.796  80.178  27.074  1.00 22.06           C  
ATOM    835  CD2 PHE A 105      12.824  80.257  28.304  1.00 24.03           C  
ATOM    836  CE1 PHE A 105      10.250  79.323  28.026  1.00 22.05           C  
ATOM    837  CE2 PHE A 105      12.293  79.394  29.250  1.00 25.44           C  
ATOM    838  CZ  PHE A 105      11.006  78.934  29.108  1.00 24.65           C  
ATOM    839  N   THR A 106      12.985  84.633  24.835  1.00 17.70           N  
ATOM    840  CA  THR A 106      13.857  85.798  24.523  1.00 16.60           C  
ATOM    841  C   THR A 106      13.236  87.059  25.106  1.00 21.62           C  
ATOM    842  O   THR A 106      13.927  87.965  25.610  1.00 20.48           O  
ATOM    843  CB  THR A 106      14.046  85.926  23.000  1.00 17.51           C  
ATOM    844  OG1 THR A 106      14.791  84.787  22.528  1.00 18.68           O  
ATOM    845  CG2 THR A 106      14.825  87.171  22.596  1.00 17.00           C  
ATOM    846  N   GLY A 107      11.907  87.080  25.129  1.00 20.52           N  
ATOM    847  CA  GLY A 107      11.182  88.263  25.639  1.00 21.75           C  
ATOM    848  C   GLY A 107      11.406  88.454  27.125  1.00 22.26           C  
ATOM    849  O   GLY A 107      11.156  89.551  27.648  1.00 23.57           O  
ATOM    850  N   ALA A 108      11.855  87.456  27.862  1.00 22.04           N  
ATOM    851  CA  ALA A 108      12.204  87.534  29.258  1.00 22.90           C  
ATOM    852  C   ALA A 108      13.555  88.198  29.518  1.00 23.70           C  
ATOM    853  O   ALA A 108      13.950  88.387  30.673  1.00 25.05           O  
ATOM    854  CB  ALA A 108      12.258  86.136  29.882  1.00 24.18           C  
ATOM    855  N   LYS A 109      14.334  88.382  28.462  1.00 23.17           N  
ATOM    856  CA  LYS A 109      15.650  89.023  28.575  1.00 21.34           C  
ATOM    857  C   LYS A 109      15.427  90.521  28.521  1.00 23.83           C  
ATOM    858  O   LYS A 109      14.446  90.993  27.949  1.00 26.05           O  
ATOM    859  CB  LYS A 109      16.574  88.587  27.420  1.00 20.25           C  
ATOM    860  CG  LYS A 109      16.871  87.087  27.544  1.00 21.19           C  
ATOM    861  CD  LYS A 109      17.716  86.598  26.366  1.00 22.83           C  
ATOM    862  CE  LYS A 109      17.892  85.092  26.531  1.00 22.16           C  
ATOM    863  NZ  LYS A 109      18.810  84.510  25.497  1.00 20.66           N  
ATOM    864  N   GLU A 110      16.360  91.285  29.119  1.00 24.66           N  
ATOM    865  CA  GLU A 110      16.172  92.733  29.120  1.00 32.41           C  
ATOM    866  C   GLU A 110      16.329  93.333  27.735  1.00 25.99           C  
ATOM    867  O   GLU A 110      17.117  92.834  26.934  1.00 28.22           O  
ATOM    868  CB  GLU A 110      17.181  93.350  30.110  1.00 34.94           C  
ATOM    869  CG  GLU A 110      16.815  93.033  31.553  1.00 41.40           C  
ATOM    870  CD  GLU A 110      15.557  93.697  32.063  1.00 45.25           C  
ATOM    871  OE1 GLU A 110      14.939  94.564  31.404  1.00 50.29           O  
ATOM    872  OE2 GLU A 110      15.163  93.326  33.191  1.00 50.12           O  
ATOM    873  N   ASN A 111      15.535  94.344  27.425  1.00 29.11           N  
ATOM    874  CA  ASN A 111      15.629  95.052  26.158  1.00 32.75           C  
ATOM    875  C   ASN A 111      15.224  94.259  24.935  1.00 27.95           C  
ATOM    876  O   ASN A 111      15.789  94.446  23.858  1.00 27.32           O  
ATOM    877  CB  ASN A 111      17.071  95.569  25.989  1.00 39.79           C  
ATOM    878  CG  ASN A 111      17.507  96.341  27.225  1.00 47.76           C  
ATOM    879  OD1 ASN A 111      17.360  97.562  27.271  1.00 52.38           O  
ATOM    880  ND2 ASN A 111      18.027  95.642  28.232  1.00 50.84           N  
ATOM    881  N   PHE A 112      14.304  93.302  25.097  1.00 21.55           N  
ATOM    882  CA  PHE A 112      13.745  92.558  23.981  1.00 21.15           C  
ATOM    883  C   PHE A 112      12.231  92.745  23.931  1.00 22.29           C  
ATOM    884  O   PHE A 112      11.554  92.288  24.874  1.00 27.62           O  
ATOM    885  CB  PHE A 112      14.045  91.065  24.086  1.00 20.76           C  
ATOM    886  CG  PHE A 112      15.414  90.713  23.558  1.00 19.32           C  
ATOM    887  CD1 PHE A 112      16.531  90.734  24.382  1.00 19.78           C  
ATOM    888  CD2 PHE A 112      15.568  90.367  22.227  1.00 20.01           C  
ATOM    889  CE1 PHE A 112      17.785  90.418  23.894  1.00 21.52           C  
ATOM    890  CE2 PHE A 112      16.826  90.044  21.737  1.00 20.91           C  
ATOM    891  CZ  PHE A 112      17.934  90.083  22.566  1.00 22.57           C  
ATOM    892  N   SER A 113      11.725  93.471  22.948  1.00 20.06           N  
ATOM    893  CA  SER A 113      10.274  93.697  22.920  1.00 20.50           C  
ATOM    894  C   SER A 113       9.554  92.462  22.366  1.00 22.16           C  
ATOM    895  O   SER A 113      10.125  91.724  21.564  1.00 20.78           O  
ATOM    896  CB  SER A 113       9.897  94.874  22.045  1.00 22.45           C  
ATOM    897  OG  SER A 113      10.150  94.674  20.667  1.00 22.47           O  
ATOM    898  N   LEU A 114       8.309  92.291  22.782  1.00 22.54           N  
ATOM    899  CA  LEU A 114       7.558  91.137  22.241  1.00 21.48           C  
ATOM    900  C   LEU A 114       7.404  91.282  20.742  1.00 20.21           C  
ATOM    901  O   LEU A 114       7.451  90.278  20.004  1.00 20.36           O  
ATOM    902  CB  LEU A 114       6.204  91.051  22.958  1.00 24.96           C  
ATOM    903  CG  LEU A 114       5.795  89.712  23.567  1.00 36.60           C  
ATOM    904  CD1 LEU A 114       6.932  88.990  24.261  1.00 36.99           C  
ATOM    905  CD2 LEU A 114       4.680  89.968  24.592  1.00 37.12           C  
ATOM    906  N   ASP A 115       7.181  92.480  20.196  1.00 19.53           N  
ATOM    907  CA  ASP A 115       7.058  92.696  18.779  1.00 18.11           C  
ATOM    908  C   ASP A 115       8.301  92.191  18.032  1.00 17.16           C  
ATOM    909  O   ASP A 115       8.129  91.411  17.086  1.00 17.36           O  
ATOM    910  CB  ASP A 115       6.850  94.188  18.413  1.00 20.71           C  
ATOM    911  CG  ASP A 115       6.654  94.348  16.915  1.00 25.67           C  
ATOM    912  OD1 ASP A 115       5.563  94.038  16.398  1.00 26.94           O  
ATOM    913  OD2 ASP A 115       7.572  94.747  16.143  1.00 26.83           O  
ATOM    914  N   TRP A 116       9.493  92.624  18.439  1.00 17.44           N  
ATOM    915  CA  TRP A 116      10.704  92.164  17.748  1.00 16.45           C  
ATOM    916  C   TRP A 116      10.848  90.623  17.840  1.00 16.07           C  
ATOM    917  O   TRP A 116      11.209  89.983  16.860  1.00 17.98           O  
ATOM    918  CB  TRP A 116      11.947  92.784  18.404  1.00 17.89           C  
ATOM    919  CG  TRP A 116      13.173  92.546  17.562  1.00 18.07           C  
ATOM    920  CD1 TRP A 116      13.659  93.291  16.537  1.00 20.85           C  
ATOM    921  CD2 TRP A 116      14.052  91.427  17.721  1.00 16.16           C  
ATOM    922  NE1 TRP A 116      14.805  92.700  16.038  1.00 19.51           N  
ATOM    923  CE2 TRP A 116      15.062  91.540  16.735  1.00 17.27           C  
ATOM    924  CE3 TRP A 116      14.083  90.322  18.594  1.00 17.03           C  
ATOM    925  CZ2 TRP A 116      16.062  90.592  16.608  1.00 16.86           C  
ATOM    926  CZ3 TRP A 116      15.109  89.396  18.467  1.00 17.75           C  
ATOM    927  CH2 TRP A 116      16.092  89.509  17.466  1.00 17.07           C  
ATOM    928  N   CYS A 117      10.506  90.113  19.027  1.00 16.27           N  
ATOM    929  CA  CYS A 117      10.659  88.653  19.191  1.00 14.47           C  
ATOM    930  C   CYS A 117       9.715  87.878  18.270  1.00 15.96           C  
ATOM    931  O   CYS A 117      10.083  86.793  17.800  1.00 16.66           O  
ATOM    932  CB  CYS A 117      10.419  88.312  20.665  1.00 17.40           C  
ATOM    933  SG  CYS A 117      11.775  88.848  21.730  1.00 17.89           S  
ATOM    934  N   LYS A 118       8.507  88.410  18.091  1.00 16.38           N  
ATOM    935  CA  LYS A 118       7.562  87.693  17.233  1.00 17.13           C  
ATOM    936  C   LYS A 118       7.908  87.640  15.767  1.00 17.89           C  
ATOM    937  O   LYS A 118       7.584  86.660  15.050  1.00 15.24           O  
ATOM    938  CB  LYS A 118       6.149  88.325  17.357  1.00 15.42           C  
ATOM    939  CG  LYS A 118       5.457  87.990  18.672  1.00 17.69           C  
ATOM    940  CD  LYS A 118       4.238  88.871  18.938  1.00 21.88           C  
ATOM    941  CE  LYS A 118       3.243  88.861  17.803  1.00 23.62           C  
ATOM    942  NZ  LYS A 118       2.006  89.625  18.250  1.00 26.85           N  
ATOM    943  N   GLN A 119       8.551  88.693  15.215  1.00 17.60           N  
ATOM    944  CA  GLN A 119       8.684  88.815  13.780  1.00 16.86           C  
ATOM    945  C   GLN A 119       9.250  87.650  12.984  1.00 14.66           C  
ATOM    946  O   GLN A 119       8.718  87.339  11.918  1.00 15.13           O  
ATOM    947  CB  GLN A 119       9.375  90.138  13.377  1.00 15.90           C  
ATOM    948  CG  GLN A 119       8.659  91.382  13.945  1.00 16.99           C  
ATOM    949  CD  GLN A 119       7.184  91.427  13.595  1.00 18.08           C  
ATOM    950  OE1 GLN A 119       6.756  91.393  12.451  1.00 18.51           O  
ATOM    951  NE2 GLN A 119       6.330  91.449  14.609  1.00 21.18           N  
ATOM    952  N   PRO A 120      10.377  87.054  13.372  1.00 16.23           N  
ATOM    953  CA  PRO A 120      10.926  85.969  12.617  1.00 14.16           C  
ATOM    954  C   PRO A 120       9.947  84.815  12.399  1.00 12.91           C  
ATOM    955  O   PRO A 120      10.002  84.171  11.365  1.00 16.85           O  
ATOM    956  CB  PRO A 120      12.127  85.511  13.461  1.00 15.50           C  
ATOM    957  CG  PRO A 120      12.331  86.538  14.491  1.00 23.61           C  
ATOM    958  CD  PRO A 120      11.123  87.434  14.601  1.00 16.46           C  
ATOM    959  N   ASP A 121       9.046  84.628  13.381  1.00 15.36           N  
ATOM    960  CA  ASP A 121       8.103  83.512  13.302  1.00 16.57           C  
ATOM    961  C   ASP A 121       6.819  83.916  12.593  1.00 18.65           C  
ATOM    962  O   ASP A 121       5.974  83.030  12.354  1.00 16.54           O  
ATOM    963  CB  ASP A 121       7.816  82.969  14.704  1.00 15.87           C  
ATOM    964  CG  ASP A 121       8.923  82.119  15.331  1.00 14.21           C  
ATOM    965  OD1 ASP A 121       9.583  81.385  14.560  1.00 15.68           O  
ATOM    966  OD2 ASP A 121       9.051  82.207  16.562  1.00 16.24           O  
ATOM    967  N   VAL A 122       6.658  85.184  12.232  1.00 16.29           N  
ATOM    968  CA  VAL A 122       5.446  85.536  11.467  1.00 15.02           C  
ATOM    969  C   VAL A 122       5.379  84.772  10.171  1.00 16.65           C  
ATOM    970  O   VAL A 122       6.311  84.716   9.360  1.00 15.58           O  
ATOM    971  CB  VAL A 122       5.515  87.051  11.174  1.00 14.80           C  
ATOM    972  CG1 VAL A 122       4.512  87.400  10.080  1.00 17.83           C  
ATOM    973  CG2 VAL A 122       5.216  87.813  12.477  1.00 15.39           C  
ATOM    974  N   GLY A 123       4.212  84.118   9.935  1.00 15.85           N  
ATOM    975  CA  GLY A 123       4.053  83.309   8.753  1.00 15.95           C  
ATOM    976  C   GLY A 123       4.203  81.794   8.898  1.00 15.75           C  
ATOM    977  O   GLY A 123       3.897  81.048   7.944  1.00 16.92           O  
ATOM    978  N   LEU A 124       4.700  81.360  10.076  1.00 15.73           N  
ATOM    979  CA  LEU A 124       4.798  79.900  10.255  1.00 15.91           C  
ATOM    980  C   LEU A 124       3.388  79.294  10.179  1.00 18.46           C  
ATOM    981  O   LEU A 124       2.370  79.997  10.361  1.00 18.09           O  
ATOM    982  CB  LEU A 124       5.333  79.606  11.654  1.00 16.06           C  
ATOM    983  CG  LEU A 124       6.838  79.770  11.939  1.00 13.94           C  
ATOM    984  CD1 LEU A 124       7.086  79.474  13.425  1.00 15.94           C  
ATOM    985  CD2 LEU A 124       7.647  78.850  11.044  1.00 15.64           C  
ATOM    986  N   PRO A 125       3.362  77.994   9.950  1.00 16.59           N  
ATOM    987  CA  PRO A 125       2.054  77.307  10.021  1.00 16.74           C  
ATOM    988  C   PRO A 125       1.399  77.652  11.350  1.00 15.53           C  
ATOM    989  O   PRO A 125       1.958  77.536  12.454  1.00 16.06           O  
ATOM    990  CB  PRO A 125       2.455  75.834   9.966  1.00 16.00           C  
ATOM    991  CG  PRO A 125       3.702  75.837   9.105  1.00 17.80           C  
ATOM    992  CD  PRO A 125       4.448  77.047   9.676  1.00 15.06           C  
ATOM    993  N   LYS A 126       0.123  78.038  11.316  1.00 16.72           N  
ATOM    994  CA  LYS A 126      -0.606  78.428  12.503  1.00 14.73           C  
ATOM    995  C   LYS A 126      -1.223  77.224  13.224  1.00 15.73           C  
ATOM    996  O   LYS A 126      -1.936  76.481  12.539  1.00 16.58           O  
ATOM    997  CB  LYS A 126      -1.764  79.378  12.105  1.00 18.04           C  
ATOM    998  CG  LYS A 126      -2.454  80.003  13.311  1.00 17.11           C  
ATOM    999  CD  LYS A 126      -3.595  80.909  12.836  1.00 20.48           C  
ATOM   1000  CE  LYS A 126      -4.291  81.642  13.966  1.00 23.39           C  
ATOM   1001  NZ  LYS A 126      -5.362  82.504  13.340  1.00 28.10           N  
ATOM   1002  N   PRO A 127      -0.923  77.004  14.471  1.00 14.47           N  
ATOM   1003  CA  PRO A 127      -1.545  75.928  15.235  1.00 14.78           C  
ATOM   1004  C   PRO A 127      -3.075  76.057  15.234  1.00 15.22           C  
ATOM   1005  O   PRO A 127      -3.649  77.156  15.241  1.00 17.18           O  
ATOM   1006  CB  PRO A 127      -1.042  76.082  16.666  1.00 15.56           C  
ATOM   1007  CG  PRO A 127       0.264  76.833  16.474  1.00 18.12           C  
ATOM   1008  CD  PRO A 127      -0.072  77.827  15.370  1.00 17.45           C  
ATOM   1009  N   ASP A 128      -3.696  74.862  15.097  1.00 14.99           N  
ATOM   1010  CA  ASP A 128      -5.157  74.814  15.208  1.00 17.45           C  
ATOM   1011  C   ASP A 128      -5.584  74.807  16.673  1.00 17.85           C  
ATOM   1012  O   ASP A 128      -6.752  75.097  16.954  1.00 18.12           O  
ATOM   1013  CB  ASP A 128      -5.658  73.497  14.562  1.00 17.08           C  
ATOM   1014  CG  ASP A 128      -5.360  73.493  13.068  1.00 16.19           C  
ATOM   1015  OD1 ASP A 128      -5.941  74.422  12.406  1.00 19.22           O  
ATOM   1016  OD2 ASP A 128      -4.600  72.685  12.545  1.00 19.28           O  
ATOM   1017  N   LEU A 129      -4.679  74.432  17.573  1.00 16.45           N  
ATOM   1018  CA  LEU A 129      -4.980  74.345  18.998  1.00 15.76           C  
ATOM   1019  C   LEU A 129      -3.674  74.609  19.763  1.00 15.14           C  
ATOM   1020  O   LEU A 129      -2.670  74.003  19.379  1.00 16.79           O  
ATOM   1021  CB  LEU A 129      -5.484  72.945  19.330  1.00 15.41           C  
ATOM   1022  CG  LEU A 129      -5.610  72.566  20.784  1.00 17.35           C  
ATOM   1023  CD1 LEU A 129      -6.590  73.459  21.532  1.00 19.26           C  
ATOM   1024  CD2 LEU A 129      -6.023  71.086  20.895  1.00 17.55           C  
ATOM   1025  N   VAL A 130      -3.662  75.519  20.692  1.00 14.73           N  
ATOM   1026  CA  VAL A 130      -2.471  75.740  21.497  1.00 18.79           C  
ATOM   1027  C   VAL A 130      -2.847  75.425  22.938  1.00 18.70           C  
ATOM   1028  O   VAL A 130      -3.603  76.188  23.534  1.00 18.54           O  
ATOM   1029  CB  VAL A 130      -1.927  77.160  21.418  1.00 18.45           C  
ATOM   1030  CG1 VAL A 130      -0.587  77.213  22.152  1.00 19.36           C  
ATOM   1031  CG2 VAL A 130      -1.764  77.550  19.948  1.00 18.72           C  
ATOM   1032  N   LEU A 131      -2.342  74.326  23.480  1.00 15.18           N  
ATOM   1033  CA  LEU A 131      -2.650  73.982  24.858  1.00 16.25           C  
ATOM   1034  C   LEU A 131      -1.629  74.652  25.763  1.00 17.54           C  
ATOM   1035  O   LEU A 131      -0.437  74.525  25.480  1.00 19.61           O  
ATOM   1036  CB  LEU A 131      -2.522  72.454  25.031  1.00 15.48           C  
ATOM   1037  CG  LEU A 131      -3.554  71.694  24.169  1.00 18.18           C  
ATOM   1038  CD1 LEU A 131      -3.059  70.312  23.761  1.00 17.97           C  
ATOM   1039  CD2 LEU A 131      -4.841  71.583  24.980  1.00 19.92           C  
ATOM   1040  N   PHE A 132      -2.031  75.317  26.818  1.00 15.31           N  
ATOM   1041  CA  PHE A 132      -1.066  75.883  27.758  1.00 15.65           C  
ATOM   1042  C   PHE A 132      -1.216  75.149  29.087  1.00 16.89           C  
ATOM   1043  O   PHE A 132      -2.292  75.229  29.736  1.00 17.73           O  
ATOM   1044  CB  PHE A 132      -1.283  77.404  27.920  1.00 16.40           C  
ATOM   1045  CG  PHE A 132      -0.168  78.011  28.748  1.00 18.22           C  
ATOM   1046  CD1 PHE A 132       1.044  78.284  28.117  1.00 19.36           C  
ATOM   1047  CD2 PHE A 132      -0.326  78.249  30.096  1.00 20.86           C  
ATOM   1048  CE1 PHE A 132       2.082  78.847  28.842  1.00 19.50           C  
ATOM   1049  CE2 PHE A 132       0.741  78.797  30.813  1.00 23.74           C  
ATOM   1050  CZ  PHE A 132       1.941  79.079  30.197  1.00 23.53           C  
ATOM   1051  N   LEU A 133      -0.210  74.396  29.439  1.00 16.42           N  
ATOM   1052  CA  LEU A 133      -0.203  73.598  30.671  1.00 17.61           C  
ATOM   1053  C   LEU A 133       0.157  74.454  31.881  1.00 19.34           C  
ATOM   1054  O   LEU A 133       1.313  74.763  32.128  1.00 19.68           O  
ATOM   1055  CB  LEU A 133       0.779  72.432  30.502  1.00 17.35           C  
ATOM   1056  CG  LEU A 133       0.201  71.232  29.744  1.00 17.09           C  
ATOM   1057  CD1 LEU A 133      -0.247  71.532  28.323  1.00 19.78           C  
ATOM   1058  CD2 LEU A 133       1.270  70.135  29.749  1.00 17.88           C  
ATOM   1059  N   GLN A 134      -0.877  74.843  32.634  1.00 19.47           N  
ATOM   1060  CA  GLN A 134      -0.647  75.730  33.793  1.00 22.07           C  
ATOM   1061  C   GLN A 134      -0.345  74.974  35.068  1.00 26.06           C  
ATOM   1062  O   GLN A 134      -0.986  73.966  35.382  1.00 25.94           O  
ATOM   1063  CB  GLN A 134      -1.851  76.619  34.036  1.00 25.29           C  
ATOM   1064  CG  GLN A 134      -2.383  77.408  32.869  1.00 28.74           C  
ATOM   1065  CD  GLN A 134      -3.456  78.363  33.411  1.00 34.22           C  
ATOM   1066  OE1 GLN A 134      -3.173  79.527  33.705  1.00 36.64           O  
ATOM   1067  NE2 GLN A 134      -4.635  77.788  33.557  1.00 31.56           N  
ATOM   1068  N   LEU A 135       0.579  75.507  35.856  1.00 26.54           N  
ATOM   1069  CA  LEU A 135       1.025  74.874  37.079  1.00 29.25           C  
ATOM   1070  C   LEU A 135       1.668  75.942  37.985  1.00 32.64           C  
ATOM   1071  O   LEU A 135       2.399  76.788  37.495  1.00 35.54           O  
ATOM   1072  CB  LEU A 135       2.108  73.833  36.739  1.00 31.38           C  
ATOM   1073  CG  LEU A 135       2.591  72.879  37.821  1.00 32.28           C  
ATOM   1074  CD1 LEU A 135       1.481  71.947  38.282  1.00 33.82           C  
ATOM   1075  CD2 LEU A 135       3.790  72.061  37.337  1.00 33.98           C  
ATOM   1076  N  AGLN A 136       1.336  75.991  39.270  0.66 33.68           N  
ATOM   1077  N  BGLN A 136       1.384  75.703  39.249  0.33 32.50           N  
ATOM   1078  CA AGLN A 136       2.003  77.048  40.068  0.66 36.69           C  
ATOM   1079  CA BGLN A 136       1.834  76.435  40.407  0.33 33.96           C  
ATOM   1080  C  AGLN A 136       3.506  76.867  39.879  0.66 36.51           C  
ATOM   1081  C  BGLN A 136       3.169  75.850  40.878  0.33 34.20           C  
ATOM   1082  O  AGLN A 136       3.994  75.735  39.981  0.66 36.51           O  
ATOM   1083  O  BGLN A 136       3.387  74.647  40.898  0.33 32.93           O  
ATOM   1084  CB AGLN A 136       1.549  76.966  41.502  0.66 39.35           C  
ATOM   1085  CB BGLN A 136       0.797  76.383  41.527  0.33 33.00           C  
ATOM   1086  N  ALEU A 137       4.262  77.937  39.581  0.66 35.17           N  
ATOM   1087  N  BLEU A 137       4.073  76.760  41.209  0.33 35.38           N  
ATOM   1088  CA ALEU A 137       5.708  77.742  39.427  0.66 35.10           C  
ATOM   1089  CA BLEU A 137       5.430  76.467  41.617  0.33 37.95           C  
ATOM   1090  C  ALEU A 137       6.218  76.973  40.643  0.66 36.43           C  
ATOM   1091  C  BLEU A 137       5.602  75.401  42.685  0.33 36.62           C  
ATOM   1092  O  ALEU A 137       7.250  76.312  40.599  0.66 34.18           O  
ATOM   1093  O  BLEU A 137       6.547  74.613  42.614  0.33 36.41           O  
ATOM   1094  CB ALEU A 137       6.491  79.040  39.214  0.66 32.54           C  
ATOM   1095  CB BLEU A 137       6.115  77.770  42.071  0.33 38.82           C  
ATOM   1096  CG ALEU A 137       6.554  79.491  37.737  0.66 32.90           C  
ATOM   1097  CG BLEU A 137       7.222  78.278  41.146  0.33 40.32           C  
ATOM   1098  CD1ALEU A 137       7.012  80.942  37.626  0.66 32.32           C  
ATOM   1099  CD1BLEU A 137       8.026  79.391  41.787  0.33 40.56           C  
ATOM   1100  CD2ALEU A 137       7.486  78.572  36.945  0.66 31.48           C  
ATOM   1101  CD2BLEU A 137       8.107  77.127  40.706  0.33 42.31           C  
ATOM   1102  N  AALA A 138       5.423  77.011  41.712  0.66 41.61           N  
ATOM   1103  N  BALA A 138       4.744  75.410  43.696  0.33 37.75           N  
ATOM   1104  CA AALA A 138       5.753  76.314  42.946  0.66 46.20           C  
ATOM   1105  CA BALA A 138       4.836  74.435  44.780  0.33 37.61           C  
ATOM   1106  C  AALA A 138       5.717  74.796  42.849  0.66 47.65           C  
ATOM   1107  C  BALA A 138       4.680  73.020  44.233  0.33 37.14           C  
ATOM   1108  O  AALA A 138       6.812  74.222  42.939  0.66 48.44           O  
ATOM   1109  O  BALA A 138       5.339  72.089  44.693  0.33 38.67           O  
ATOM   1110  CB AALA A 138       4.854  76.797  44.080  0.66 47.14           C  
ATOM   1111  CB BALA A 138       3.782  74.732  45.832  0.33 37.46           C  
ATOM   1112  N  AASP A 139       4.558  74.147  42.726  0.66 50.02           N  
ATOM   1113  N  BASP A 139       3.805  72.877  43.239  0.33 36.56           N  
ATOM   1114  CA AASP A 139       4.548  72.684  42.684  0.66 51.19           C  
ATOM   1115  CA BASP A 139       3.574  71.565  42.635  0.33 33.92           C  
ATOM   1116  C  AASP A 139       5.262  72.165  41.436  0.66 49.88           C  
ATOM   1117  C  BASP A 139       4.673  71.215  41.642  0.33 32.27           C  
ATOM   1118  O  AASP A 139       5.598  70.979  41.370  0.66 50.83           O  
ATOM   1119  O  BASP A 139       4.941  70.033  41.413  0.33 32.65           O  
ATOM   1120  CB AASP A 139       3.211  72.019  42.907  0.66 52.17           C  
ATOM   1121  CB BASP A 139       2.182  71.501  42.012  0.33 36.08           C  
ATOM   1122  CG AASP A 139       1.936  72.679  42.476  0.66 53.54           C  
ATOM   1123  CG BASP A 139       1.091  71.572  43.069  0.33 37.33           C  
ATOM   1124  OD1AASP A 139       1.703  73.852  42.838  0.66 52.52           O  
ATOM   1125  OD1BASP A 139       1.309  71.093  44.200  0.33 38.75           O  
ATOM   1126  OD2AASP A 139       1.119  72.021  41.786  0.66 53.80           O  
ATOM   1127  OD2BASP A 139       0.011  72.115  42.756  0.33 38.65           O  
ATOM   1128  N  AALA A 140       5.538  73.067  40.500  0.66 47.27           N  
ATOM   1129  N  BALA A 140       5.365  72.224  41.118  0.33 30.13           N  
ATOM   1130  CA AALA A 140       6.313  72.676  39.318  0.66 48.34           C  
ATOM   1131  CA BALA A 140       6.452  71.985  40.180  0.33 30.77           C  
ATOM   1132  C  AALA A 140       7.719  72.377  39.854  0.66 48.22           C  
ATOM   1133  C  BALA A 140       7.816  71.744  40.818  0.33 33.30           C  
ATOM   1134  O  AALA A 140       8.441  71.481  39.454  0.66 48.94           O  
ATOM   1135  O  BALA A 140       8.515  70.788  40.507  0.33 32.52           O  
ATOM   1136  CB AALA A 140       6.363  73.780  38.289  0.66 46.69           C  
ATOM   1137  CB BALA A 140       6.587  73.196  39.256  0.33 28.60           C  
ATOM   1138  N  AALA A 141       8.048  73.206  40.845  0.66 49.14           N  
ATOM   1139  N  BALA A 141       8.266  72.718  41.618  0.33 38.40           N  
ATOM   1140  CA AALA A 141       9.302  73.071  41.571  0.66 50.15           C  
ATOM   1141  CA BALA A 141       9.588  72.686  42.275  0.33 42.38           C  
ATOM   1142  C  AALA A 141       9.318  71.817  42.432  0.66 50.32           C  
ATOM   1143  C  BALA A 141       9.661  71.165  42.607  0.33 45.84           C  
ATOM   1144  O  AALA A 141      10.402  71.386  42.849  0.66 50.45           O  
ATOM   1145  O  BALA A 141      10.169  70.354  41.827  0.33 46.12           O  
ATOM   1146  CB AALA A 141       9.532  74.325  42.408  0.66 50.02           C  
ATOM   1147  CB BALA A 141       9.594  73.489  43.559  0.33 42.06           C  
ATOM   1148  N   LYS A 142       8.279  71.100  42.790  1.00 49.58           N  
ATOM   1149  CA  LYS A 142       8.014  69.882  43.532  1.00 49.55           C  
ATOM   1150  C   LYS A 142       8.337  68.778  42.528  1.00 51.43           C  
ATOM   1151  O   LYS A 142       8.589  67.653  42.930  1.00 54.33           O  
ATOM   1152  CB  LYS A 142       6.603  69.799  44.058  1.00 52.99           C  
ATOM   1153  N   ARG A 143       8.358  69.128  41.244  1.00 48.91           N  
ATOM   1154  CA  ARG A 143       8.670  68.123  40.229  1.00 47.44           C  
ATOM   1155  C   ARG A 143      10.182  68.034  40.063  1.00 47.53           C  
ATOM   1156  O   ARG A 143      10.812  68.424  39.092  1.00 48.34           O  
ATOM   1157  CB  ARG A 143       7.936  68.370  38.912  1.00 42.42           C  
ATOM   1158  CG  ARG A 143       6.462  68.010  39.056  1.00 42.06           C  
ATOM   1159  CD  ARG A 143       5.605  68.667  37.980  1.00 37.73           C  
ATOM   1160  NE  ARG A 143       4.209  68.574  38.420  1.00 36.76           N  
ATOM   1161  CZ  ARG A 143       3.186  68.631  37.564  1.00 35.47           C  
ATOM   1162  NH1 ARG A 143       3.473  68.773  36.278  1.00 33.30           N  
ATOM   1163  NH2 ARG A 143       1.953  68.543  38.003  1.00 35.46           N  
ATOM   1164  N   GLY A 144      10.762  67.466  41.123  1.00 50.68           N  
ATOM   1165  CA  GLY A 144      12.219  67.291  41.173  1.00 54.55           C  
ATOM   1166  C   GLY A 144      12.854  68.680  41.306  1.00 56.01           C  
ATOM   1167  O   GLY A 144      12.277  69.577  41.930  1.00 53.94           O  
ATOM   1168  N   ALA A 145      14.023  68.864  40.698  1.00 55.15           N  
ATOM   1169  CA  ALA A 145      14.657  70.173  40.793  1.00 55.99           C  
ATOM   1170  C   ALA A 145      15.235  70.621  39.457  1.00 55.80           C  
ATOM   1171  O   ALA A 145      15.184  69.913  38.457  1.00 54.65           O  
ATOM   1172  CB  ALA A 145      15.753  70.168  41.846  1.00 56.99           C  
ATOM   1173  N   PHE A 146      15.819  71.817  39.520  1.00 55.88           N  
ATOM   1174  CA  PHE A 146      16.405  72.405  38.335  1.00 58.15           C  
ATOM   1175  C   PHE A 146      17.660  71.695  37.830  1.00 59.36           C  
ATOM   1176  O   PHE A 146      18.489  71.120  38.520  1.00 59.11           O  
ATOM   1177  CB  PHE A 146      16.709  73.892  38.525  1.00 56.73           C  
ATOM   1178  CG  PHE A 146      15.492  74.743  38.266  1.00 56.83           C  
ATOM   1179  CD1 PHE A 146      14.727  74.562  37.124  1.00 56.04           C  
ATOM   1180  CD2 PHE A 146      15.117  75.712  39.175  1.00 56.07           C  
ATOM   1181  CE1 PHE A 146      13.616  75.345  36.892  1.00 56.24           C  
ATOM   1182  CE2 PHE A 146      14.001  76.500  38.951  1.00 56.40           C  
ATOM   1183  CZ  PHE A 146      13.252  76.317  37.805  1.00 55.74           C  
ATOM   1184  N   GLY A 147      17.737  71.791  36.500  1.00 60.32           N  
ATOM   1185  CA  GLY A 147      18.850  71.239  35.746  1.00 58.00           C  
ATOM   1186  C   GLY A 147      19.944  72.313  35.748  1.00 56.76           C  
ATOM   1187  O   GLY A 147      19.824  73.362  36.377  1.00 57.35           O  
ATOM   1188  N   HIS A 148      20.996  71.974  35.018  1.00 53.97           N  
ATOM   1189  CA  HIS A 148      22.141  72.861  34.880  1.00 52.63           C  
ATOM   1190  C   HIS A 148      22.005  73.636  33.569  1.00 48.68           C  
ATOM   1191  O   HIS A 148      22.870  74.440  33.230  1.00 50.00           O  
ATOM   1192  CB  HIS A 148      23.425  72.044  34.876  1.00 51.39           C  
ATOM   1193  N   GLU A 149      20.917  73.370  32.845  1.00 45.07           N  
ATOM   1194  CA  GLU A 149      20.711  74.023  31.563  1.00 41.45           C  
ATOM   1195  C   GLU A 149      20.304  75.488  31.700  1.00 37.61           C  
ATOM   1196  O   GLU A 149      19.825  76.018  32.696  1.00 34.99           O  
ATOM   1197  CB  GLU A 149      19.732  73.301  30.638  1.00 46.10           C  
ATOM   1198  CG  GLU A 149      20.319  72.109  29.894  1.00 50.70           C  
ATOM   1199  CD  GLU A 149      19.718  71.885  28.524  1.00 54.31           C  
ATOM   1200  OE1 GLU A 149      18.769  72.600  28.120  1.00 58.04           O  
ATOM   1201  OE2 GLU A 149      20.161  70.983  27.779  1.00 56.32           O  
ATOM   1202  N   ARG A 150      20.531  76.182  30.580  1.00 31.47           N  
ATOM   1203  CA  ARG A 150      20.200  77.598  30.509  1.00 31.58           C  
ATOM   1204  C   ARG A 150      18.724  77.806  30.853  1.00 30.80           C  
ATOM   1205  O   ARG A 150      17.911  76.908  30.653  1.00 32.48           O  
ATOM   1206  CB  ARG A 150      20.499  78.090  29.087  1.00 35.13           C  
ATOM   1207  CG  ARG A 150      20.999  79.534  29.121  1.00 37.77           C  
ATOM   1208  CD  ARG A 150      21.594  79.975  27.811  1.00 36.36           C  
ATOM   1209  NE  ARG A 150      22.906  79.497  27.453  1.00 35.41           N  
ATOM   1210  CZ  ARG A 150      24.077  80.019  27.796  1.00 36.92           C  
ATOM   1211  NH1 ARG A 150      24.125  81.093  28.578  1.00 38.51           N  
ATOM   1212  NH2 ARG A 150      25.197  79.479  27.359  1.00 38.23           N  
ATOM   1213  N   TYR A 151      18.413  78.937  31.438  1.00 29.05           N  
ATOM   1214  CA  TYR A 151      17.082  79.403  31.769  1.00 29.52           C  
ATOM   1215  C   TYR A 151      16.448  78.646  32.934  1.00 30.13           C  
ATOM   1216  O   TYR A 151      15.321  78.974  33.295  1.00 30.31           O  
ATOM   1217  CB  TYR A 151      16.130  79.347  30.564  1.00 24.08           C  
ATOM   1218  CG  TYR A 151      16.598  80.042  29.300  1.00 24.45           C  
ATOM   1219  CD1 TYR A 151      17.340  81.223  29.364  1.00 24.73           C  
ATOM   1220  CD2 TYR A 151      16.317  79.523  28.049  1.00 25.04           C  
ATOM   1221  CE1 TYR A 151      17.762  81.850  28.211  1.00 23.74           C  
ATOM   1222  CE2 TYR A 151      16.732  80.139  26.878  1.00 24.85           C  
ATOM   1223  CZ  TYR A 151      17.470  81.318  26.976  1.00 25.60           C  
ATOM   1224  OH  TYR A 151      17.854  81.886  25.791  1.00 23.56           O  
ATOM   1225  N   GLU A 152      17.154  77.648  33.441  1.00 33.68           N  
ATOM   1226  CA  GLU A 152      16.604  76.855  34.542  1.00 39.99           C  
ATOM   1227  C   GLU A 152      16.737  77.513  35.908  1.00 38.67           C  
ATOM   1228  O   GLU A 152      17.453  77.008  36.782  1.00 43.10           O  
ATOM   1229  CB  GLU A 152      17.264  75.469  34.557  1.00 44.28           C  
ATOM   1230  CG  GLU A 152      17.174  74.784  33.201  1.00 51.24           C  
ATOM   1231  CD  GLU A 152      16.650  73.366  33.331  1.00 54.89           C  
ATOM   1232  OE1 GLU A 152      16.465  72.912  34.482  1.00 56.63           O  
ATOM   1233  OE2 GLU A 152      16.420  72.740  32.277  1.00 55.81           O  
ATOM   1234  N   ASN A 153      16.064  78.630  36.115  1.00 34.44           N  
ATOM   1235  CA  ASN A 153      16.047  79.332  37.389  1.00 33.44           C  
ATOM   1236  C   ASN A 153      14.694  80.015  37.539  1.00 30.87           C  
ATOM   1237  O   ASN A 153      14.081  80.424  36.551  1.00 30.31           O  
ATOM   1238  CB  ASN A 153      17.165  80.341  37.611  1.00 33.46           C  
ATOM   1239  CG  ASN A 153      17.122  81.566  36.739  1.00 29.10           C  
ATOM   1240  OD1 ASN A 153      16.425  82.565  36.944  1.00 30.62           O  
ATOM   1241  ND2 ASN A 153      17.944  81.506  35.679  1.00 35.50           N  
ATOM   1242  N   GLY A 154      14.258  80.191  38.782  1.00 27.00           N  
ATOM   1243  CA  GLY A 154      12.977  80.797  39.068  1.00 29.24           C  
ATOM   1244  C   GLY A 154      12.705  82.187  38.561  1.00 24.45           C  
ATOM   1245  O   GLY A 154      11.606  82.550  38.127  1.00 24.76           O  
ATOM   1246  N   ALA A 155      13.736  83.076  38.627  1.00 24.56           N  
ATOM   1247  CA  ALA A 155      13.501  84.433  38.213  1.00 21.18           C  
ATOM   1248  C   ALA A 155      13.226  84.538  36.697  1.00 18.05           C  
ATOM   1249  O   ALA A 155      12.373  85.293  36.251  1.00 21.48           O  
ATOM   1250  CB  ALA A 155      14.779  85.232  38.571  1.00 21.93           C  
ATOM   1251  N   PHE A 156      14.015  83.727  35.994  1.00 22.33           N  
ATOM   1252  CA  PHE A 156      13.845  83.750  34.531  1.00 25.48           C  
ATOM   1253  C   PHE A 156      12.510  83.092  34.148  1.00 21.68           C  
ATOM   1254  O   PHE A 156      11.824  83.664  33.319  1.00 22.27           O  
ATOM   1255  CB  PHE A 156      14.977  83.018  33.833  1.00 25.34           C  
ATOM   1256  CG  PHE A 156      15.010  83.326  32.358  1.00 24.99           C  
ATOM   1257  CD1 PHE A 156      15.684  84.428  31.867  1.00 30.90           C  
ATOM   1258  CD2 PHE A 156      14.344  82.483  31.484  1.00 27.65           C  
ATOM   1259  CE1 PHE A 156      15.717  84.690  30.509  1.00 33.59           C  
ATOM   1260  CE2 PHE A 156      14.376  82.743  30.124  1.00 30.08           C  
ATOM   1261  CZ  PHE A 156      15.056  83.842  29.646  1.00 31.43           C  
ATOM   1262  N   GLN A 157      12.197  81.993  34.834  1.00 23.13           N  
ATOM   1263  CA  GLN A 157      10.908  81.355  34.492  1.00 25.23           C  
ATOM   1264  C   GLN A 157       9.724  82.271  34.715  1.00 25.05           C  
ATOM   1265  O   GLN A 157       8.762  82.276  33.913  1.00 22.05           O  
ATOM   1266  CB  GLN A 157      10.752  80.054  35.280  1.00 21.86           C  
ATOM   1267  CG  GLN A 157      11.712  78.952  34.893  1.00 24.23           C  
ATOM   1268  CD  GLN A 157      11.488  78.405  33.500  1.00 26.11           C  
ATOM   1269  OE1 GLN A 157      10.350  78.093  33.162  1.00 27.08           O  
ATOM   1270  NE2 GLN A 157      12.546  78.257  32.718  1.00 25.46           N  
ATOM   1271  N   GLU A 158       9.722  83.083  35.774  1.00 23.80           N  
ATOM   1272  CA  GLU A 158       8.639  84.008  36.041  1.00 26.65           C  
ATOM   1273  C   GLU A 158       8.494  85.046  34.931  1.00 24.17           C  
ATOM   1274  O   GLU A 158       7.396  85.409  34.536  1.00 25.45           O  
ATOM   1275  CB  GLU A 158       8.870  84.684  37.403  1.00 30.95           C  
ATOM   1276  CG  GLU A 158       7.664  85.377  37.991  1.00 39.15           C  
ATOM   1277  CD  GLU A 158       7.369  86.787  37.551  1.00 45.12           C  
ATOM   1278  OE1 GLU A 158       8.267  87.496  37.043  1.00 44.78           O  
ATOM   1279  OE2 GLU A 158       6.203  87.232  37.716  1.00 47.89           O  
ATOM   1280  N   ARG A 159       9.648  85.585  34.451  1.00 22.87           N  
ATOM   1281  CA  ARG A 159       9.542  86.549  33.364  1.00 26.16           C  
ATOM   1282  C   ARG A 159       8.983  85.902  32.084  1.00 21.37           C  
ATOM   1283  O   ARG A 159       8.194  86.528  31.377  1.00 23.62           O  
ATOM   1284  CB  ARG A 159      10.889  87.210  33.051  1.00 29.55           C  
ATOM   1285  CG  ARG A 159      11.382  88.155  34.130  1.00 34.49           C  
ATOM   1286  CD  ARG A 159      12.730  88.747  33.789  1.00 36.09           C  
ATOM   1287  NE  ARG A 159      12.779  89.654  32.658  1.00 38.24           N  
ATOM   1288  CZ  ARG A 159      12.880  90.980  32.733  1.00 41.46           C  
ATOM   1289  NH1 ARG A 159      12.928  91.520  33.948  1.00 41.41           N  
ATOM   1290  NH2 ARG A 159      12.944  91.721  31.639  1.00 39.37           N  
ATOM   1291  N   ALA A 160       9.365  84.637  31.842  1.00 22.23           N  
ATOM   1292  CA  ALA A 160       8.853  83.981  30.627  1.00 18.36           C  
ATOM   1293  C   ALA A 160       7.342  83.785  30.753  1.00 19.62           C  
ATOM   1294  O   ALA A 160       6.621  83.969  29.767  1.00 20.42           O  
ATOM   1295  CB  ALA A 160       9.585  82.670  30.396  1.00 18.43           C  
ATOM   1296  N   LEU A 161       6.947  83.369  31.952  1.00 21.74           N  
ATOM   1297  CA  LEU A 161       5.525  83.185  32.246  1.00 23.99           C  
ATOM   1298  C   LEU A 161       4.758  84.478  32.012  1.00 24.84           C  
ATOM   1299  O   LEU A 161       3.710  84.468  31.363  1.00 21.68           O  
ATOM   1300  CB  LEU A 161       5.298  82.674  33.664  1.00 24.85           C  
ATOM   1301  CG  LEU A 161       3.824  82.382  34.011  1.00 23.03           C  
ATOM   1302  CD1 LEU A 161       3.204  81.465  32.971  1.00 20.88           C  
ATOM   1303  CD2 LEU A 161       3.811  81.799  35.419  1.00 27.72           C  
ATOM   1304  N   ARG A 162       5.284  85.645  32.418  1.00 25.30           N  
ATOM   1305  CA  ARG A 162       4.595  86.902  32.116  1.00 26.02           C  
ATOM   1306  C   ARG A 162       4.431  87.122  30.624  1.00 25.22           C  
ATOM   1307  O   ARG A 162       3.386  87.584  30.136  1.00 24.36           O  
ATOM   1308  CB  ARG A 162       5.367  88.072  32.739  1.00 28.25           C  
ATOM   1309  CG  ARG A 162       5.424  87.997  34.265  1.00 33.14           C  
ATOM   1310  CD  ARG A 162       4.030  88.285  34.835  1.00 39.56           C  
ATOM   1311  NE  ARG A 162       3.299  87.044  35.042  1.00 45.52           N  
ATOM   1312  CZ  ARG A 162       2.014  86.816  34.809  1.00 47.35           C  
ATOM   1313  NH1 ARG A 162       1.233  87.776  34.320  1.00 47.50           N  
ATOM   1314  NH2 ARG A 162       1.522  85.606  35.061  1.00 48.53           N  
ATOM   1315  N   CYS A 163       5.487  86.788  29.850  1.00 21.64           N  
ATOM   1316  CA  CYS A 163       5.398  86.889  28.397  1.00 20.87           C  
ATOM   1317  C   CYS A 163       4.348  85.933  27.831  1.00 19.92           C  
ATOM   1318  O   CYS A 163       3.637  86.362  26.925  1.00 21.57           O  
ATOM   1319  CB  CYS A 163       6.743  86.617  27.729  1.00 21.19           C  
ATOM   1320  SG  CYS A 163       8.016  87.849  28.130  1.00 22.81           S  
ATOM   1321  N   PHE A 164       4.301  84.686  28.318  1.00 18.97           N  
ATOM   1322  CA  PHE A 164       3.270  83.782  27.825  1.00 19.53           C  
ATOM   1323  C   PHE A 164       1.873  84.405  28.031  1.00 20.03           C  
ATOM   1324  O   PHE A 164       1.076  84.283  27.107  1.00 20.52           O  
ATOM   1325  CB  PHE A 164       3.359  82.418  28.502  1.00 19.05           C  
ATOM   1326  CG  PHE A 164       4.350  81.431  27.910  1.00 17.96           C  
ATOM   1327  CD1 PHE A 164       4.185  80.995  26.612  1.00 20.07           C  
ATOM   1328  CD2 PHE A 164       5.384  80.938  28.674  1.00 20.27           C  
ATOM   1329  CE1 PHE A 164       5.056  80.045  26.079  1.00 18.21           C  
ATOM   1330  CE2 PHE A 164       6.264  79.984  28.134  1.00 20.66           C  
ATOM   1331  CZ  PHE A 164       6.102  79.546  26.846  1.00 21.23           C  
ATOM   1332  N   HIS A 165       1.592  85.008  29.170  1.00 24.89           N  
ATOM   1333  CA  HIS A 165       0.242  85.583  29.366  1.00 26.57           C  
ATOM   1334  C   HIS A 165       0.013  86.747  28.423  1.00 24.35           C  
ATOM   1335  O   HIS A 165      -1.112  86.903  27.946  1.00 26.00           O  
ATOM   1336  CB  HIS A 165      -0.016  85.935  30.837  1.00 30.35           C  
ATOM   1337  CG  HIS A 165      -0.133  84.717  31.708  1.00 35.63           C  
ATOM   1338  ND1 HIS A 165      -1.267  83.932  31.743  1.00 39.19           N  
ATOM   1339  CD2 HIS A 165       0.740  84.133  32.563  1.00 36.07           C  
ATOM   1340  CE1 HIS A 165      -1.081  82.918  32.574  1.00 38.11           C  
ATOM   1341  NE2 HIS A 165       0.132  83.024  33.090  1.00 36.08           N  
ATOM   1342  N   GLN A 166       1.058  87.495  28.020  1.00 22.04           N  
ATOM   1343  CA  GLN A 166       0.839  88.525  27.006  1.00 26.03           C  
ATOM   1344  C   GLN A 166       0.428  87.888  25.687  1.00 25.25           C  
ATOM   1345  O   GLN A 166      -0.457  88.369  24.997  1.00 26.98           O  
ATOM   1346  CB  GLN A 166       2.082  89.393  26.800  1.00 30.00           C  
ATOM   1347  CG  GLN A 166       2.301  90.333  27.984  1.00 34.22           C  
ATOM   1348  CD  GLN A 166       0.973  91.010  28.324  1.00 43.13           C  
ATOM   1349  OE1 GLN A 166       0.541  91.911  27.606  1.00 43.42           O  
ATOM   1350  NE2 GLN A 166       0.310  90.551  29.385  1.00 43.76           N  
ATOM   1351  N   LEU A 167       1.049  86.751  25.311  1.00 21.35           N  
ATOM   1352  CA  LEU A 167       0.716  86.101  24.053  1.00 22.27           C  
ATOM   1353  C   LEU A 167      -0.682  85.480  24.020  1.00 24.07           C  
ATOM   1354  O   LEU A 167      -1.276  85.272  22.954  1.00 25.84           O  
ATOM   1355  CB  LEU A 167       1.777  85.000  23.804  1.00 19.72           C  
ATOM   1356  CG  LEU A 167       3.191  85.556  23.545  1.00 21.70           C  
ATOM   1357  CD1 LEU A 167       4.182  84.396  23.389  1.00 22.18           C  
ATOM   1358  CD2 LEU A 167       3.202  86.421  22.306  1.00 21.16           C  
ATOM   1359  N   MET A 168      -1.212  85.211  25.199  1.00 27.08           N  
ATOM   1360  CA  MET A 168      -2.529  84.589  25.282  1.00 29.67           C  
ATOM   1361  C   MET A 168      -3.646  85.597  25.052  1.00 31.94           C  
ATOM   1362  O   MET A 168      -4.792  85.180  24.913  1.00 32.52           O  
ATOM   1363  CB  MET A 168      -2.741  83.907  26.614  1.00 31.58           C  
ATOM   1364  CG  MET A 168      -1.828  82.721  26.875  1.00 35.60           C  
ATOM   1365  SD  MET A 168      -2.057  82.279  28.621  1.00 39.26           S  
ATOM   1366  CE  MET A 168      -0.478  81.518  28.959  1.00 32.28           C  
ATOM   1367  N   LYS A 169      -3.281  86.872  25.054  1.00 35.55           N  
ATOM   1368  CA  LYS A 169      -4.286  87.906  24.787  1.00 38.55           C  
ATOM   1369  C   LYS A 169      -4.624  87.855  23.302  1.00 38.48           C  
ATOM   1370  O   LYS A 169      -5.617  88.410  22.832  1.00 42.32           O  
ATOM   1371  CB  LYS A 169      -3.758  89.287  25.174  1.00 38.74           C  
ATOM   1372  CG  LYS A 169      -3.447  89.452  26.654  1.00 42.66           C  
ATOM   1373  CD  LYS A 169      -2.777  90.791  26.921  1.00 48.81           C  
ATOM   1374  CE  LYS A 169      -2.555  91.013  28.409  1.00 52.83           C  
ATOM   1375  NZ  LYS A 169      -1.855  92.304  28.667  1.00 56.20           N  
ATOM   1376  N   ASP A 170      -3.760  87.171  22.540  1.00 35.56           N  
ATOM   1377  CA  ASP A 170      -3.963  87.077  21.101  1.00 32.02           C  
ATOM   1378  C   ASP A 170      -5.121  86.145  20.767  1.00 35.44           C  
ATOM   1379  O   ASP A 170      -4.943  84.930  20.699  1.00 35.87           O  
ATOM   1380  CB  ASP A 170      -2.669  86.591  20.427  1.00 30.51           C  
ATOM   1381  CG  ASP A 170      -2.673  86.889  18.939  1.00 31.24           C  
ATOM   1382  OD1 ASP A 170      -3.760  86.840  18.323  1.00 33.88           O  
ATOM   1383  OD2 ASP A 170      -1.575  87.168  18.396  1.00 35.53           O  
ATOM   1384  N   THR A 171      -6.302  86.717  20.530  1.00 35.11           N  
ATOM   1385  CA  THR A 171      -7.471  85.913  20.199  1.00 35.04           C  
ATOM   1386  C   THR A 171      -7.467  85.419  18.766  1.00 35.81           C  
ATOM   1387  O   THR A 171      -8.443  84.783  18.356  1.00 39.02           O  
ATOM   1388  CB  THR A 171      -8.757  86.680  20.575  1.00 41.04           C  
ATOM   1389  OG1 THR A 171      -8.824  87.877  19.793  1.00 40.33           O  
ATOM   1390  CG2 THR A 171      -8.726  87.087  22.044  1.00 42.01           C  
ATOM   1391  N   THR A 172      -6.394  85.617  17.974  1.00 32.01           N  
ATOM   1392  CA  THR A 172      -6.383  85.036  16.628  1.00 32.22           C  
ATOM   1393  C   THR A 172      -6.052  83.538  16.796  1.00 29.34           C  
ATOM   1394  O   THR A 172      -6.188  82.776  15.833  1.00 33.68           O  
ATOM   1395  CB  THR A 172      -5.360  85.631  15.653  1.00 32.08           C  
ATOM   1396  OG1 THR A 172      -4.012  85.565  16.152  1.00 36.43           O  
ATOM   1397  CG2 THR A 172      -5.662  87.105  15.362  1.00 35.52           C  
ATOM   1398  N   LEU A 173      -5.693  83.148  18.017  1.00 25.55           N  
ATOM   1399  CA  LEU A 173      -5.231  81.785  18.266  1.00 22.02           C  
ATOM   1400  C   LEU A 173      -6.145  80.977  19.174  1.00 23.52           C  
ATOM   1401  O   LEU A 173      -6.726  81.553  20.103  1.00 26.06           O  
ATOM   1402  CB  LEU A 173      -3.822  81.877  18.900  1.00 22.54           C  
ATOM   1403  CG  LEU A 173      -2.725  82.202  17.869  1.00 23.46           C  
ATOM   1404  CD1 LEU A 173      -1.512  82.821  18.539  1.00 27.27           C  
ATOM   1405  CD2 LEU A 173      -2.346  80.964  17.076  1.00 22.96           C  
ATOM   1406  N   ASN A 174      -6.291  79.680  18.903  1.00 19.75           N  
ATOM   1407  CA  ASN A 174      -7.183  78.827  19.715  1.00 18.73           C  
ATOM   1408  C   ASN A 174      -6.452  78.312  20.942  1.00 21.13           C  
ATOM   1409  O   ASN A 174      -5.999  77.166  21.036  1.00 20.37           O  
ATOM   1410  CB  ASN A 174      -7.704  77.686  18.837  1.00 21.64           C  
ATOM   1411  CG  ASN A 174      -8.673  76.733  19.508  1.00 20.89           C  
ATOM   1412  OD1 ASN A 174      -9.390  77.163  20.431  1.00 25.04           O  
ATOM   1413  ND2 ASN A 174      -8.694  75.485  19.075  1.00 23.22           N  
ATOM   1414  N   TRP A 175      -6.314  79.167  21.942  1.00 19.71           N  
ATOM   1415  CA  TRP A 175      -5.678  78.851  23.200  1.00 19.97           C  
ATOM   1416  C   TRP A 175      -6.624  78.087  24.117  1.00 21.59           C  
ATOM   1417  O   TRP A 175      -7.794  78.470  24.285  1.00 21.60           O  
ATOM   1418  CB  TRP A 175      -5.257  80.132  23.929  1.00 19.90           C  
ATOM   1419  CG  TRP A 175      -4.060  80.859  23.406  1.00 23.84           C  
ATOM   1420  CD1 TRP A 175      -4.086  81.917  22.537  1.00 27.30           C  
ATOM   1421  CD2 TRP A 175      -2.671  80.612  23.705  1.00 23.64           C  
ATOM   1422  NE1 TRP A 175      -2.802  82.346  22.303  1.00 27.79           N  
ATOM   1423  CE2 TRP A 175      -1.917  81.571  22.991  1.00 27.47           C  
ATOM   1424  CE3 TRP A 175      -2.009  79.707  24.519  1.00 25.17           C  
ATOM   1425  CZ2 TRP A 175      -0.527  81.597  23.061  1.00 27.65           C  
ATOM   1426  CZ3 TRP A 175      -0.624  79.748  24.599  1.00 28.98           C  
ATOM   1427  CH2 TRP A 175       0.103  80.699  23.865  1.00 26.75           C  
ATOM   1428  N   LYS A 176      -6.133  77.026  24.733  1.00 19.89           N  
ATOM   1429  CA  LYS A 176      -6.882  76.295  25.743  1.00 18.84           C  
ATOM   1430  C   LYS A 176      -6.001  76.122  26.975  1.00 21.25           C  
ATOM   1431  O   LYS A 176      -4.926  75.504  26.894  1.00 20.41           O  
ATOM   1432  CB  LYS A 176      -7.360  74.916  25.288  1.00 18.96           C  
ATOM   1433  CG  LYS A 176      -8.310  74.873  24.108  1.00 22.25           C  
ATOM   1434  CD  LYS A 176      -9.649  75.502  24.485  1.00 24.69           C  
ATOM   1435  CE  LYS A 176     -10.655  75.294  23.368  1.00 28.78           C  
ATOM   1436  NZ  LYS A 176     -11.977  75.887  23.776  1.00 31.79           N  
ATOM   1437  N   MET A 177      -6.489  76.511  28.140  1.00 19.70           N  
ATOM   1438  CA  MET A 177      -5.752  76.349  29.381  1.00 20.89           C  
ATOM   1439  C   MET A 177      -5.982  74.918  29.887  1.00 22.75           C  
ATOM   1440  O   MET A 177      -7.099  74.393  29.885  1.00 24.50           O  
ATOM   1441  CB  MET A 177      -6.163  77.318  30.484  1.00 22.94           C  
ATOM   1442  CG  MET A 177      -6.014  78.793  30.200  1.00 24.40           C  
ATOM   1443  SD  MET A 177      -4.349  79.286  29.696  1.00 25.05           S  
ATOM   1444  CE  MET A 177      -4.463  79.229  27.925  1.00 27.75           C  
ATOM   1445  N   VAL A 178      -4.929  74.297  30.367  1.00 19.10           N  
ATOM   1446  CA  VAL A 178      -4.995  72.968  30.947  1.00 17.30           C  
ATOM   1447  C   VAL A 178      -4.475  72.972  32.367  1.00 17.93           C  
ATOM   1448  O   VAL A 178      -3.421  73.560  32.639  1.00 20.00           O  
ATOM   1449  CB  VAL A 178      -4.104  71.995  30.128  1.00 19.93           C  
ATOM   1450  CG1 VAL A 178      -4.071  70.607  30.733  1.00 19.14           C  
ATOM   1451  CG2 VAL A 178      -4.576  72.016  28.671  1.00 21.24           C  
ATOM   1452  N   ASP A 179      -5.232  72.405  33.300  1.00 19.66           N  
ATOM   1453  CA  ASP A 179      -4.775  72.360  34.689  1.00 19.37           C  
ATOM   1454  C   ASP A 179      -3.777  71.218  34.850  1.00 21.52           C  
ATOM   1455  O   ASP A 179      -4.144  70.045  34.982  1.00 21.42           O  
ATOM   1456  CB  ASP A 179      -5.987  72.129  35.605  1.00 22.28           C  
ATOM   1457  CG  ASP A 179      -5.553  71.969  37.047  1.00 22.97           C  
ATOM   1458  OD1 ASP A 179      -4.364  72.061  37.417  1.00 24.61           O  
ATOM   1459  OD2 ASP A 179      -6.496  71.769  37.864  1.00 29.42           O  
ATOM   1460  N   ALA A 180      -2.507  71.608  34.694  1.00 22.26           N  
ATOM   1461  CA  ALA A 180      -1.426  70.612  34.711  1.00 23.67           C  
ATOM   1462  C   ALA A 180      -1.009  70.170  36.090  1.00 24.79           C  
ATOM   1463  O   ALA A 180      -0.098  69.351  36.230  1.00 25.04           O  
ATOM   1464  CB  ALA A 180      -0.266  71.194  33.901  1.00 22.28           C  
ATOM   1465  N   SER A 181      -1.720  70.619  37.131  1.00 25.11           N  
ATOM   1466  CA  SER A 181      -1.441  70.173  38.494  1.00 26.82           C  
ATOM   1467  C   SER A 181      -2.021  68.817  38.840  1.00 27.66           C  
ATOM   1468  O   SER A 181      -1.645  68.250  39.889  1.00 28.42           O  
ATOM   1469  CB  SER A 181      -1.986  71.230  39.486  1.00 28.47           C  
ATOM   1470  OG  SER A 181      -3.397  71.105  39.587  1.00 29.24           O  
ATOM   1471  N   LYS A 182      -2.909  68.256  38.012  1.00 25.64           N  
ATOM   1472  CA  LYS A 182      -3.492  66.947  38.264  1.00 23.90           C  
ATOM   1473  C   LYS A 182      -2.556  65.790  37.905  1.00 23.77           C  
ATOM   1474  O   LYS A 182      -1.407  66.047  37.539  1.00 26.82           O  
ATOM   1475  CB  LYS A 182      -4.833  66.838  37.517  1.00 26.82           C  
ATOM   1476  CG  LYS A 182      -5.656  68.113  37.786  1.00 30.28           C  
ATOM   1477  CD  LYS A 182      -7.088  67.921  37.329  1.00 33.64           C  
ATOM   1478  CE  LYS A 182      -7.229  67.820  35.826  1.00 32.05           C  
ATOM   1479  NZ  LYS A 182      -8.632  68.101  35.361  1.00 28.39           N  
ATOM   1480  N   SER A 183      -3.058  64.559  38.016  1.00 22.48           N  
ATOM   1481  CA  SER A 183      -2.209  63.413  37.746  1.00 22.73           C  
ATOM   1482  C   SER A 183      -1.844  63.393  36.254  1.00 21.02           C  
ATOM   1483  O   SER A 183      -2.539  63.986  35.435  1.00 20.05           O  
ATOM   1484  CB  SER A 183      -2.879  62.096  38.109  1.00 23.94           C  
ATOM   1485  OG  SER A 183      -3.974  61.790  37.257  1.00 24.13           O  
ATOM   1486  N   ILE A 184      -0.798  62.638  35.944  1.00 21.30           N  
ATOM   1487  CA  ILE A 184      -0.425  62.508  34.527  1.00 19.19           C  
ATOM   1488  C   ILE A 184      -1.610  61.983  33.717  1.00 16.92           C  
ATOM   1489  O   ILE A 184      -1.884  62.480  32.612  1.00 18.73           O  
ATOM   1490  CB  ILE A 184       0.788  61.571  34.380  1.00 18.73           C  
ATOM   1491  CG1 ILE A 184       2.013  62.296  34.933  1.00 20.69           C  
ATOM   1492  CG2 ILE A 184       0.974  61.120  32.938  1.00 20.57           C  
ATOM   1493  CD1 ILE A 184       3.268  61.457  34.953  1.00 21.41           C  
ATOM   1494  N   GLU A 185      -2.321  60.957  34.230  1.00 20.72           N  
ATOM   1495  CA  GLU A 185      -3.464  60.439  33.503  1.00 18.79           C  
ATOM   1496  C   GLU A 185      -4.631  61.413  33.416  1.00 16.99           C  
ATOM   1497  O   GLU A 185      -5.261  61.427  32.353  1.00 17.82           O  
ATOM   1498  CB  GLU A 185      -4.015  59.160  34.198  1.00 22.88           C  
ATOM   1499  CG  GLU A 185      -3.047  58.013  33.950  1.00 28.26           C  
ATOM   1500  CD  GLU A 185      -2.791  57.672  32.501  1.00 36.15           C  
ATOM   1501  OE1 GLU A 185      -3.650  57.773  31.592  1.00 34.15           O  
ATOM   1502  OE2 GLU A 185      -1.645  57.252  32.189  1.00 37.78           O  
ATOM   1503  N   ALA A 186      -4.894  62.200  34.451  1.00 18.20           N  
ATOM   1504  CA  ALA A 186      -6.014  63.124  34.387  1.00 20.08           C  
ATOM   1505  C   ALA A 186      -5.745  64.262  33.398  1.00 19.83           C  
ATOM   1506  O   ALA A 186      -6.618  64.707  32.676  1.00 18.17           O  
ATOM   1507  CB  ALA A 186      -6.295  63.755  35.748  1.00 22.21           C  
ATOM   1508  N   VAL A 187      -4.493  64.756  33.485  1.00 18.96           N  
ATOM   1509  CA  VAL A 187      -4.130  65.848  32.557  1.00 17.46           C  
ATOM   1510  C   VAL A 187      -4.213  65.301  31.130  1.00 17.21           C  
ATOM   1511  O   VAL A 187      -4.677  65.988  30.224  1.00 16.06           O  
ATOM   1512  CB  VAL A 187      -2.718  66.341  32.880  1.00 17.27           C  
ATOM   1513  CG1 VAL A 187      -2.229  67.379  31.852  1.00 18.05           C  
ATOM   1514  CG2 VAL A 187      -2.673  66.966  34.271  1.00 18.05           C  
ATOM   1515  N   HIS A 188      -3.729  64.073  30.930  1.00 16.70           N  
ATOM   1516  CA  HIS A 188      -3.753  63.442  29.611  1.00 15.94           C  
ATOM   1517  C   HIS A 188      -5.176  63.385  29.068  1.00 16.40           C  
ATOM   1518  O   HIS A 188      -5.465  63.740  27.933  1.00 18.07           O  
ATOM   1519  CB  HIS A 188      -3.142  62.016  29.662  1.00 16.34           C  
ATOM   1520  CG  HIS A 188      -3.432  61.234  28.430  1.00 16.35           C  
ATOM   1521  ND1 HIS A 188      -2.957  61.593  27.190  1.00 16.16           N  
ATOM   1522  CD2 HIS A 188      -4.170  60.104  28.244  1.00 17.92           C  
ATOM   1523  CE1 HIS A 188      -3.369  60.708  26.284  1.00 16.65           C  
ATOM   1524  NE2 HIS A 188      -4.120  59.788  26.912  1.00 18.22           N  
ATOM   1525  N   GLU A 189      -6.126  62.935  29.878  1.00 16.91           N  
ATOM   1526  CA  GLU A 189      -7.514  62.867  29.397  1.00 19.42           C  
ATOM   1527  C   GLU A 189      -8.074  64.219  29.009  1.00 17.90           C  
ATOM   1528  O   GLU A 189      -8.732  64.337  27.958  1.00 17.65           O  
ATOM   1529  CB  GLU A 189      -8.372  62.128  30.423  1.00 20.89           C  
ATOM   1530  CG  GLU A 189      -9.807  61.943  29.912  1.00 24.77           C  
ATOM   1531  CD  GLU A 189      -9.896  60.922  28.789  1.00 28.63           C  
ATOM   1532  OE1 GLU A 189      -8.879  60.275  28.411  1.00 29.05           O  
ATOM   1533  OE2 GLU A 189     -11.004  60.797  28.239  1.00 29.95           O  
ATOM   1534  N   ASP A 190      -7.788  65.283  29.770  1.00 17.83           N  
ATOM   1535  CA  ASP A 190      -8.258  66.608  29.366  1.00 16.64           C  
ATOM   1536  C   ASP A 190      -7.707  67.001  27.997  1.00 15.25           C  
ATOM   1537  O   ASP A 190      -8.408  67.470  27.077  1.00 17.90           O  
ATOM   1538  CB  ASP A 190      -7.815  67.651  30.402  1.00 18.94           C  
ATOM   1539  CG  ASP A 190      -8.572  67.585  31.712  1.00 26.92           C  
ATOM   1540  OD1 ASP A 190      -9.604  66.878  31.785  1.00 25.87           O  
ATOM   1541  OD2 ASP A 190      -8.132  68.270  32.668  1.00 27.67           O  
ATOM   1542  N   ILE A 191      -6.380  66.767  27.841  1.00 15.75           N  
ATOM   1543  CA  ILE A 191      -5.705  67.130  26.599  1.00 17.55           C  
ATOM   1544  C   ILE A 191      -6.191  66.314  25.410  1.00 15.75           C  
ATOM   1545  O   ILE A 191      -6.445  66.838  24.322  1.00 16.95           O  
ATOM   1546  CB  ILE A 191      -4.183  66.955  26.779  1.00 16.13           C  
ATOM   1547  CG1 ILE A 191      -3.663  68.134  27.605  1.00 16.03           C  
ATOM   1548  CG2 ILE A 191      -3.475  66.905  25.423  1.00 18.04           C  
ATOM   1549  CD1 ILE A 191      -2.255  67.923  28.143  1.00 16.50           C  
ATOM   1550  N   ARG A 192      -6.429  65.025  25.644  1.00 16.47           N  
ATOM   1551  CA  ARG A 192      -6.885  64.120  24.592  1.00 15.74           C  
ATOM   1552  C   ARG A 192      -8.258  64.508  24.062  1.00 14.93           C  
ATOM   1553  O   ARG A 192      -8.465  64.598  22.866  1.00 16.62           O  
ATOM   1554  CB  ARG A 192      -6.836  62.683  25.114  1.00 16.79           C  
ATOM   1555  CG  ARG A 192      -7.150  61.668  24.035  1.00 17.14           C  
ATOM   1556  CD  ARG A 192      -7.435  60.279  24.608  1.00 17.13           C  
ATOM   1557  NE  ARG A 192      -8.656  60.264  25.399  1.00 18.42           N  
ATOM   1558  CZ  ARG A 192      -9.830  60.260  24.771  1.00 21.40           C  
ATOM   1559  NH1 ARG A 192      -9.846  60.252  23.453  1.00 21.70           N  
ATOM   1560  NH2 ARG A 192     -10.923  60.262  25.529  1.00 22.93           N  
ATOM   1561  N   VAL A 193      -9.170  64.853  24.983  1.00 14.84           N  
ATOM   1562  CA  VAL A 193     -10.517  65.267  24.532  1.00 17.49           C  
ATOM   1563  C   VAL A 193     -10.469  66.571  23.755  1.00 16.18           C  
ATOM   1564  O   VAL A 193     -11.119  66.665  22.701  1.00 18.53           O  
ATOM   1565  CB  VAL A 193     -11.425  65.345  25.773  1.00 21.21           C  
ATOM   1566  CG1 VAL A 193     -12.725  66.046  25.403  1.00 21.89           C  
ATOM   1567  CG2 VAL A 193     -11.698  63.946  26.298  1.00 21.09           C  
ATOM   1568  N   LEU A 194      -9.679  67.540  24.247  1.00 16.09           N  
ATOM   1569  CA  LEU A 194      -9.552  68.801  23.475  1.00 17.56           C  
ATOM   1570  C   LEU A 194      -8.975  68.551  22.086  1.00 17.16           C  
ATOM   1571  O   LEU A 194      -9.403  69.126  21.069  1.00 17.87           O  
ATOM   1572  CB  LEU A 194      -8.654  69.790  24.244  1.00 18.17           C  
ATOM   1573  CG  LEU A 194      -9.258  70.362  25.542  1.00 19.52           C  
ATOM   1574  CD1 LEU A 194      -8.159  71.079  26.317  1.00 18.03           C  
ATOM   1575  CD2 LEU A 194     -10.403  71.322  25.219  1.00 21.14           C  
ATOM   1576  N   SER A 195      -7.969  67.681  22.011  1.00 15.65           N  
ATOM   1577  CA  SER A 195      -7.318  67.330  20.764  1.00 14.21           C  
ATOM   1578  C   SER A 195      -8.253  66.634  19.758  1.00 16.74           C  
ATOM   1579  O   SER A 195      -8.279  66.978  18.586  1.00 17.82           O  
ATOM   1580  CB  SER A 195      -6.059  66.494  21.044  1.00 15.31           C  
ATOM   1581  OG  SER A 195      -5.170  67.251  21.883  1.00 15.71           O  
ATOM   1582  N   GLU A 196      -9.038  65.656  20.211  1.00 17.26           N  
ATOM   1583  CA  GLU A 196     -10.013  65.044  19.306  1.00 16.60           C  
ATOM   1584  C   GLU A 196     -10.973  66.102  18.738  1.00 17.84           C  
ATOM   1585  O   GLU A 196     -11.263  66.015  17.546  1.00 18.87           O  
ATOM   1586  CB  GLU A 196     -10.826  63.953  20.029  1.00 18.55           C  
ATOM   1587  CG  GLU A 196      -9.952  62.731  20.348  1.00 22.92           C  
ATOM   1588  CD  GLU A 196     -10.138  61.649  19.310  1.00 25.61           C  
ATOM   1589  OE1 GLU A 196     -10.774  61.892  18.244  1.00 30.58           O  
ATOM   1590  OE2 GLU A 196      -9.674  60.523  19.582  1.00 22.70           O  
ATOM   1591  N   ASP A 197     -11.398  67.057  19.563  1.00 19.07           N  
ATOM   1592  CA  ASP A 197     -12.313  68.084  19.002  1.00 21.72           C  
ATOM   1593  C   ASP A 197     -11.639  68.907  17.922  1.00 21.01           C  
ATOM   1594  O   ASP A 197     -12.206  69.137  16.847  1.00 23.37           O  
ATOM   1595  CB  ASP A 197     -12.763  68.980  20.143  1.00 25.06           C  
ATOM   1596  CG  ASP A 197     -13.903  69.903  19.757  1.00 36.00           C  
ATOM   1597  OD1 ASP A 197     -14.889  69.367  19.202  1.00 37.91           O  
ATOM   1598  OD2 ASP A 197     -13.767  71.107  20.043  1.00 41.03           O  
ATOM   1599  N   ALA A 198     -10.398  69.333  18.193  1.00 19.58           N  
ATOM   1600  CA  ALA A 198      -9.682  70.122  17.175  1.00 21.92           C  
ATOM   1601  C   ALA A 198      -9.425  69.369  15.892  1.00 20.50           C  
ATOM   1602  O   ALA A 198      -9.532  69.904  14.784  1.00 22.72           O  
ATOM   1603  CB  ALA A 198      -8.370  70.622  17.784  1.00 21.84           C  
ATOM   1604  N   ILE A 199      -9.072  68.085  15.959  1.00 18.08           N  
ATOM   1605  CA  ILE A 199      -8.790  67.274  14.784  1.00 17.40           C  
ATOM   1606  C   ILE A 199     -10.013  67.230  13.867  1.00 21.42           C  
ATOM   1607  O   ILE A 199      -9.914  67.347  12.654  1.00 22.03           O  
ATOM   1608  CB  ILE A 199      -8.379  65.835  15.168  1.00 16.42           C  
ATOM   1609  CG1 ILE A 199      -6.977  65.907  15.815  1.00 17.79           C  
ATOM   1610  CG2 ILE A 199      -8.368  64.920  13.966  1.00 19.25           C  
ATOM   1611  CD1 ILE A 199      -6.672  64.624  16.594  1.00 18.54           C  
ATOM   1612  N   ALA A 200     -11.140  67.056  14.538  1.00 22.01           N  
ATOM   1613  CA  ALA A 200     -12.403  66.980  13.777  1.00 28.07           C  
ATOM   1614  C   ALA A 200     -12.800  68.337  13.199  1.00 33.72           C  
ATOM   1615  O   ALA A 200     -12.977  68.452  11.980  1.00 38.61           O  
ATOM   1616  CB  ALA A 200     -13.520  66.507  14.680  1.00 23.25           C  
ATOM   1617  N   THR A 201     -12.926  69.320  14.073  1.00 31.21           N  
ATOM   1618  CA  THR A 201     -13.437  70.629  13.694  1.00 38.63           C  
ATOM   1619  C   THR A 201     -12.427  71.588  13.116  1.00 40.44           C  
ATOM   1620  O   THR A 201     -12.542  72.028  11.960  1.00 45.13           O  
ATOM   1621  CB  THR A 201     -14.114  71.315  14.908  1.00 36.78           C  
ATOM   1622  OG1 THR A 201     -13.155  71.556  15.943  1.00 45.56           O  
ATOM   1623  CG2 THR A 201     -15.233  70.443  15.450  1.00 41.72           C  
ATOM   1624  N   ALA A 202     -11.475  71.979  13.957  1.00 39.72           N  
ATOM   1625  CA  ALA A 202     -10.443  72.922  13.521  1.00 36.85           C  
ATOM   1626  C   ALA A 202     -10.008  72.672  12.089  1.00 36.02           C  
ATOM   1627  O   ALA A 202      -9.755  73.648  11.362  1.00 36.81           O  
ATOM   1628  CB  ALA A 202      -9.281  72.845  14.513  1.00 33.99           C  
ATOM   1629  N   THR A 203      -9.976  71.427  11.615  1.00 33.61           N  
ATOM   1630  CA  THR A 203      -9.541  71.117  10.255  1.00 31.50           C  
ATOM   1631  C   THR A 203     -10.441  71.474   9.082  1.00 39.01           C  
ATOM   1632  O   THR A 203      -9.940  71.392   7.942  1.00 41.30           O  
ATOM   1633  CB  THR A 203      -9.216  69.608  10.185  1.00 36.04           C  
ATOM   1634  OG1 THR A 203     -10.337  68.857  10.660  1.00 34.86           O  
ATOM   1635  CG2 THR A 203      -8.040  69.295  11.116  1.00 35.29           C  
ATOM   1636  N   GLU A 204     -11.700  71.848   9.217  1.00 34.65           N  
ATOM   1637  CA  GLU A 204     -12.590  72.238   8.136  1.00 33.01           C  
ATOM   1638  C   GLU A 204     -12.133  73.486   7.379  1.00 33.93           C  
ATOM   1639  O   GLU A 204     -12.680  73.924   6.361  1.00 35.59           O  
ATOM   1640  CB  GLU A 204     -13.985  72.588   8.709  1.00 32.05           C  
ATOM   1641  CG  GLU A 204     -14.847  71.377   9.012  1.00 35.60           C  
ATOM   1642  CD  GLU A 204     -16.107  71.717   9.789  1.00 35.03           C  
ATOM   1643  OE1 GLU A 204     -16.760  72.739   9.495  1.00 34.96           O  
ATOM   1644  OE2 GLU A 204     -16.460  70.962  10.718  1.00 35.34           O  
ATOM   1645  N   LYS A 205     -11.164  74.183   7.946  1.00 32.57           N  
ATOM   1646  CA  LYS A 205     -10.627  75.423   7.373  1.00 30.11           C  
ATOM   1647  C   LYS A 205      -9.180  75.151   6.981  1.00 30.50           C  
ATOM   1648  O   LYS A 205      -8.569  74.283   7.588  1.00 25.47           O  
ATOM   1649  CB  LYS A 205     -10.699  76.502   8.445  1.00 31.70           C  
ATOM   1650  N   PRO A 206      -8.641  75.867   6.009  1.00 28.64           N  
ATOM   1651  CA  PRO A 206      -7.267  75.697   5.603  1.00 26.47           C  
ATOM   1652  C   PRO A 206      -6.294  76.042   6.746  1.00 22.92           C  
ATOM   1653  O   PRO A 206      -6.651  76.779   7.659  1.00 23.42           O  
ATOM   1654  CB  PRO A 206      -7.056  76.739   4.499  1.00 27.61           C  
ATOM   1655  CG  PRO A 206      -8.427  77.137   4.063  1.00 32.66           C  
ATOM   1656  CD  PRO A 206      -9.348  76.919   5.239  1.00 32.24           C  
ATOM   1657  N   LEU A 207      -5.107  75.475   6.589  1.00 23.95           N  
ATOM   1658  CA  LEU A 207      -4.043  75.780   7.562  1.00 21.95           C  
ATOM   1659  C   LEU A 207      -3.786  77.281   7.497  1.00 20.80           C  
ATOM   1660  O   LEU A 207      -3.647  77.812   6.378  1.00 23.46           O  
ATOM   1661  CB  LEU A 207      -2.829  74.964   7.162  1.00 23.25           C  
ATOM   1662  CG  LEU A 207      -1.537  75.159   7.965  1.00 22.83           C  
ATOM   1663  CD1 LEU A 207      -1.708  74.634   9.372  1.00 23.06           C  
ATOM   1664  CD2 LEU A 207      -0.407  74.459   7.221  1.00 24.12           C  
ATOM   1665  N   GLY A 208      -3.729  77.948   8.635  1.00 20.13           N  
ATOM   1666  CA  GLY A 208      -3.476  79.366   8.723  1.00 17.15           C  
ATOM   1667  C   GLY A 208      -1.969  79.719   8.817  1.00 18.75           C  
ATOM   1668  O   GLY A 208      -1.105  78.854   8.831  1.00 19.13           O  
ATOM   1669  N   GLU A 209      -1.747  81.014   8.848  1.00 19.12           N  
ATOM   1670  CA  GLU A 209      -0.398  81.584   8.992  1.00 18.83           C  
ATOM   1671  C   GLU A 209      -0.345  82.320  10.309  1.00 15.53           C  
ATOM   1672  O   GLU A 209      -1.193  83.135  10.683  1.00 20.99           O  
ATOM   1673  CB  GLU A 209      -0.130  82.593   7.859  1.00 21.00           C  
ATOM   1674  CG  GLU A 209      -0.310  81.914   6.495  1.00 31.49           C  
ATOM   1675  CD  GLU A 209      -0.434  82.992   5.413  1.00 36.26           C  
ATOM   1676  OE1 GLU A 209      -1.520  83.522   5.130  1.00 44.62           O  
ATOM   1677  OE2 GLU A 209       0.653  83.266   4.882  1.00 40.11           O  
ATOM   1678  N   LEU A 210       0.705  82.022  11.101  1.00 14.64           N  
ATOM   1679  CA  LEU A 210       0.857  82.622  12.407  1.00 15.48           C  
ATOM   1680  C   LEU A 210       1.167  84.115  12.417  1.00 18.68           C  
ATOM   1681  O   LEU A 210       2.078  84.583  11.727  1.00 17.25           O  
ATOM   1682  CB  LEU A 210       2.005  81.860  13.114  1.00 17.43           C  
ATOM   1683  CG  LEU A 210       2.348  82.322  14.519  1.00 15.32           C  
ATOM   1684  CD1 LEU A 210       1.146  82.104  15.452  1.00 18.33           C  
ATOM   1685  CD2 LEU A 210       3.618  81.650  15.045  1.00 15.69           C  
ATOM   1686  N   TRP A 211       0.405  84.867  13.209  1.00 19.11           N  
ATOM   1687  CA  TRP A 211       0.732  86.293  13.430  1.00 20.10           C  
ATOM   1688  C   TRP A 211       0.652  87.134  12.171  1.00 23.05           C  
ATOM   1689  O   TRP A 211       1.320  88.180  12.020  1.00 23.59           O  
ATOM   1690  CB  TRP A 211       2.034  86.411  14.248  1.00 18.11           C  
ATOM   1691  CG  TRP A 211       1.958  85.873  15.653  1.00 18.99           C  
ATOM   1692  CD1 TRP A 211       0.850  85.857  16.473  1.00 19.52           C  
ATOM   1693  CD2 TRP A 211       3.003  85.320  16.458  1.00 16.53           C  
ATOM   1694  NE1 TRP A 211       1.167  85.323  17.700  1.00 19.56           N  
ATOM   1695  CE2 TRP A 211       2.494  84.957  17.709  1.00 18.57           C  
ATOM   1696  CE3 TRP A 211       4.366  85.066  16.194  1.00 16.77           C  
ATOM   1697  CZ2 TRP A 211       3.248  84.396  18.730  1.00 16.96           C  
ATOM   1698  CZ3 TRP A 211       5.115  84.494  17.191  1.00 18.27           C  
ATOM   1699  CH2 TRP A 211       4.574  84.132  18.436  1.00 18.45           C  
ATOM   1700  N   LYS A 212      -0.191  86.695  11.239  1.00 22.72           N  
ATOM   1701  CA  LYS A 212      -0.472  87.533  10.063  1.00 29.20           C  
ATOM   1702  C   LYS A 212      -1.907  87.254   9.627  1.00 34.97           C  
ATOM   1703  O   LYS A 212      -2.513  86.321  10.201  1.00 34.91           O  
ATOM   1704  CB  LYS A 212       0.532  87.428   8.936  1.00 31.39           C  
ATOM   1705  CG  LYS A 212       0.939  86.053   8.504  1.00 32.09           C  
ATOM   1706  CD  LYS A 212       1.953  86.075   7.377  1.00 33.13           C  
ATOM   1707  CE  LYS A 212       1.362  86.730   6.135  1.00 37.77           C  
ATOM   1708  NZ  LYS A 212       2.237  86.516   4.947  1.00 39.57           N  
ATOM   1709  OXT LYS A 212      -2.379  88.031   8.775  1.00 37.50           O  
TER    1710      LYS A 212                                                      
HETATM 1711  P  ATMP A 301      14.460  71.208  26.179  0.66 30.95           P  
HETATM 1712  P  BTMP A 301      12.513  72.074  26.646  0.33 19.73           P  
HETATM 1713  O1PATMP A 301      15.310  70.489  27.171  0.66 33.88           O  
HETATM 1714  O1PBTMP A 301      12.037  72.641  27.964  0.33 18.10           O  
HETATM 1715  O2PATMP A 301      12.991  71.028  26.244  0.66 28.80           O  
HETATM 1716  O2PBTMP A 301      11.440  71.637  25.727  0.33 12.03           O  
HETATM 1717  O3PATMP A 301      14.970  70.974  24.685  0.66 32.95           O  
HETATM 1718  O3PBTMP A 301      13.572  70.938  27.066  0.33 12.29           O  
HETATM 1719  O5'ATMP A 301      14.641  72.773  26.403  0.66 27.46           O  
HETATM 1720  O5'BTMP A 301      13.375  73.140  25.879  0.33 19.46           O  
HETATM 1721  C5'ATMP A 301      14.247  73.734  25.390  0.66 21.34           C  
HETATM 1722  C5'BTMP A 301      14.713  73.588  26.202  0.33 18.54           C  
HETATM 1723  C4'ATMP A 301      14.683  75.119  25.881  0.66 20.69           C  
HETATM 1724  C4'BTMP A 301      14.718  75.126  26.258  0.33 13.93           C  
HETATM 1725  O4'ATMP A 301      14.821  76.175  24.930  0.66 18.48           O  
HETATM 1726  O4'BTMP A 301      14.744  75.914  25.061  0.33 16.00           O  
HETATM 1727  C3'ATMP A 301      13.892  75.645  27.065  0.66 20.52           C  
HETATM 1728  C3'BTMP A 301      13.660  75.695  27.191  0.33 14.15           C  
HETATM 1729  O3'ATMP A 301      14.803  76.237  27.988  0.66 22.88           O  
HETATM 1730  O3'BTMP A 301      14.211  76.507  28.224  0.33 12.35           O  
HETATM 1731  C2'ATMP A 301      13.021  76.721  26.393  0.66 20.00           C  
HETATM 1732  C2'BTMP A 301      12.831  76.588  26.242  0.33 14.61           C  
HETATM 1733  C1'ATMP A 301      13.900  77.181  25.229  0.66 18.68           C  
HETATM 1734  C1'BTMP A 301      13.892  77.009  25.224  0.33 14.46           C  
HETATM 1735  N1 ATMP A 301      13.358  77.757  24.019  0.66 18.21           N  
HETATM 1736  N1 BTMP A 301      13.553  77.618  23.961  0.33 13.52           N  
HETATM 1737  C2 ATMP A 301      13.761  79.059  23.621  0.66 20.41           C  
HETATM 1738  C2 BTMP A 301      14.000  78.911  23.608  0.33 14.11           C  
HETATM 1739  O2 ATMP A 301      14.392  79.848  24.342  0.66 19.59           O  
HETATM 1740  O2 BTMP A 301      14.740  79.613  24.298  0.33 13.44           O  
HETATM 1741  N3 ATMP A 301      13.340  79.395  22.363  0.66 17.91           N  
HETATM 1742  N3 BTMP A 301      13.474  79.331  22.412  0.33 13.11           N  
HETATM 1743  C4 ATMP A 301      12.637  78.567  21.494  0.66 15.67           C  
HETATM 1744  C4 BTMP A 301      12.640  78.575  21.601  0.33 12.80           C  
HETATM 1745  O4 ATMP A 301      12.273  78.957  20.219  0.66 20.08           O  
HETATM 1746  O4 BTMP A 301      12.172  79.060  20.396  0.33 11.03           O  
HETATM 1747  C5 ATMP A 301      12.279  77.213  21.990  0.66 15.72           C  
HETATM 1748  C5 BTMP A 301      12.235  77.223  22.056  0.33 12.14           C  
HETATM 1749  C5MATMP A 301      11.525  76.305  21.085  0.66 16.80           C  
HETATM 1750  C5MBTMP A 301      11.343  76.374  21.238  0.33 15.09           C  
HETATM 1751  C6 ATMP A 301      12.676  76.881  23.250  0.66 18.21           C  
HETATM 1752  C6 BTMP A 301      12.741  76.814  23.250  0.33 13.73           C  
HETATM 1753  PG AANP A 302      10.685  71.086  30.451  0.66 21.41           P  
HETATM 1754  O1GAANP A 302      11.894  70.989  31.331  0.66 25.26           O  
HETATM 1755  O2GAANP A 302       9.999  72.424  30.582  0.66 25.77           O  
HETATM 1756  O3GAANP A 302      10.888  70.443  29.157  0.66 20.09           O  
HETATM 1757  PB AANP A 302       8.276  69.375  30.587  0.66 21.21           P  
HETATM 1758  O1BAANP A 302       7.115  70.258  30.726  0.66 21.98           O  
HETATM 1759  O2BAANP A 302       8.569  68.866  29.258  0.66 18.96           O  
HETATM 1760  N3BAANP A 302       9.604  70.149  31.287  0.66 22.39           N  
HETATM 1761  PA AANP A 302       8.012  66.707  31.631  0.66 19.75           P  
HETATM 1762  O1AAANP A 302       6.861  66.168  30.886  0.66 20.96           O  
HETATM 1763  O2AAANP A 302       9.382  66.301  31.180  0.66 20.50           O  
HETATM 1764  O3AAANP A 302       7.922  68.300  31.698  0.66 20.50           O  
HETATM 1765  O5'AANP A 302       7.884  66.341  33.178  0.66 22.07           O  
HETATM 1766  C5'AANP A 302       8.789  66.905  34.179  0.66 21.31           C  
HETATM 1767  C4'AANP A 302       8.878  65.949  35.360  0.66 22.20           C  
HETATM 1768  O4'AANP A 302       7.642  66.034  36.065  0.66 22.12           O  
HETATM 1769  C3'AANP A 302       9.040  64.499  34.894  0.66 24.33           C  
HETATM 1770  O3'AANP A 302       9.830  63.691  35.821  0.66 25.51           O  
HETATM 1771  C2'AANP A 302       7.628  63.993  34.823  0.66 24.27           C  
HETATM 1772  O2'AANP A 302       7.526  62.573  35.146  0.66 24.97           O  
HETATM 1773  C1'AANP A 302       6.950  64.783  35.962  0.66 22.07           C  
HETATM 1774  N9 AANP A 302       5.518  65.018  35.670  0.66 20.12           N  
HETATM 1775  C8 AANP A 302       4.901  65.297  34.480  0.66 21.43           C  
HETATM 1776  N7 AANP A 302       3.613  65.499  34.603  0.66 18.92           N  
HETATM 1777  C5 AANP A 302       3.374  65.328  35.947  0.66 22.56           C  
HETATM 1778  C6 AANP A 302       2.191  65.422  36.730  0.66 24.61           C  
HETATM 1779  N6 AANP A 302       0.987  65.680  36.186  0.66 22.13           N  
HETATM 1780  N1 AANP A 302       2.330  65.197  38.039  0.66 27.28           N  
HETATM 1781  C2 AANP A 302       3.533  64.926  38.562  0.66 29.41           C  
HETATM 1782  N3 AANP A 302       4.697  64.831  37.943  0.66 27.80           N  
HETATM 1783  C4 AANP A 302       4.525  65.051  36.617  0.66 23.21           C  
HETATM 1784  PB BADP A 303       8.154  69.545  30.634  0.33 13.45           P  
HETATM 1785  O1BBADP A 303       7.140  70.620  30.698  0.33 12.52           O  
HETATM 1786  O2BBADP A 303       8.380  68.957  29.294  0.33 13.60           O  
HETATM 1787  O3BBADP A 303       9.579  69.956  31.238  0.33 15.81           O  
HETATM 1788  PA BADP A 303       8.014  66.791  31.714  0.33 13.71           P  
HETATM 1789  O1ABADP A 303       9.419  66.569  31.319  0.33 14.46           O  
HETATM 1790  O2ABADP A 303       6.961  66.040  30.951  0.33 15.26           O  
HETATM 1791  O3ABADP A 303       7.597  68.382  31.635  0.33 10.98           O  
HETATM 1792  O5'BADP A 303       7.738  66.538  33.235  0.33 17.12           O  
HETATM 1793  C5'BADP A 303       8.728  66.965  34.196  0.33 18.67           C  
HETATM 1794  C4'BADP A 303       8.829  65.958  35.336  0.33 20.71           C  
HETATM 1795  O4'BADP A 303       7.592  66.001  36.047  0.33 21.11           O  
HETATM 1796  C3'BADP A 303       9.100  64.509  34.966  0.33 22.61           C  
HETATM 1797  O3'BADP A 303       9.771  63.935  36.079  0.33 22.41           O  
HETATM 1798  C2'BADP A 303       7.646  63.986  34.854  0.33 22.96           C  
HETATM 1799  O2'BADP A 303       7.475  62.622  35.076  0.33 23.41           O  
HETATM 1800  C1'BADP A 303       6.946  64.764  35.973  0.33 22.12           C  
HETATM 1801  N9 BADP A 303       5.521  65.027  35.685  0.33 22.07           N  
HETATM 1802  C8 BADP A 303       4.934  65.293  34.472  0.33 22.95           C  
HETATM 1803  N7 BADP A 303       3.630  65.494  34.579  0.33 22.12           N  
HETATM 1804  C5 BADP A 303       3.362  65.342  35.957  0.33 23.68           C  
HETATM 1805  C6 BADP A 303       2.186  65.437  36.701  0.33 24.66           C  
HETATM 1806  N6 BADP A 303       1.026  65.687  36.190  0.33 23.35           N  
HETATM 1807  N1 BADP A 303       2.363  65.221  38.019  0.33 26.05           N  
HETATM 1808  C2 BADP A 303       3.532  64.951  38.612  0.33 27.13           C  
HETATM 1809  N3 BADP A 303       4.690  64.855  37.958  0.33 26.34           N  
HETATM 1810  C4 BADP A 303       4.499  65.062  36.671  0.33 23.80           C  
HETATM 1811 MG    MG A 401      10.080  68.864  27.983  1.00 16.95          MG  
HETATM 1812 MG    MG A 402       5.852  95.486  12.314  0.50 25.06          MG  
HETATM 1813  O   HOH A2001      -5.913  62.926   4.259  1.00 52.61           O  
HETATM 1814  O   HOH A2002      -7.784  63.063   7.844  1.00 34.05           O  
HETATM 1815  O   HOH A2003     -11.820  67.860   4.115  1.00 51.03           O  
HETATM 1816  O   HOH A2004     -10.468  63.351  11.062  1.00 40.74           O  
HETATM 1817  O   HOH A2005      -7.449  66.544  11.228  1.00 35.07           O  
HETATM 1818  O   HOH A2006      -7.794  64.335  10.300  1.00 31.86           O  
HETATM 1819  O   HOH A2007      -8.682  69.468   4.766  1.00 31.50           O  
HETATM 1820  O   HOH A2008       6.255  56.611  19.132  1.00 58.99           O  
HETATM 1821  O   HOH A2009       1.493  54.413  15.682  1.00 49.52           O  
HETATM 1822  O   HOH A2010       4.136  53.253  18.575  1.00 47.97           O  
HETATM 1823  O   HOH A2011      29.002  69.208  15.409  1.00 49.70           O  
HETATM 1824  O   HOH A2012       3.235  57.075  19.471  1.00 38.54           O  
HETATM 1825  O   HOH A2013       5.876  59.349  19.152  1.00 39.84           O  
HETATM 1826  O   HOH A2014      10.080  61.878  22.545  1.00 34.63           O  
HETATM 1827  O   HOH A2015      12.002  64.784  25.665  1.00 40.39           O  
HETATM 1828  O   HOH A2016       4.294  75.312   0.224  1.00 60.35           O  
HETATM 1829  O   HOH A2017       6.280  76.372  27.295  0.33 18.33           O  
HETATM 1830  O   HOH A2018      -9.232  54.900  21.827  1.00 69.40           O  
HETATM 1831  O   HOH A2019       3.119  76.835  32.293  0.66 24.98           O  
HETATM 1832  O   HOH A2020      -9.381  59.622   9.794  1.00 35.89           O  
HETATM 1833  O   HOH A2021      12.979  76.299  30.467  0.33 15.47           O  
HETATM 1834  O   HOH A2022      -0.334  55.526  12.728  1.00 48.90           O  
HETATM 1835  O   HOH A2023       3.351  56.250  17.053  1.00 37.39           O  
HETATM 1836  O   HOH A2024      18.027  65.172  19.168  1.00 38.65           O  
HETATM 1837  O   HOH A2025      26.695  70.369  12.263  1.00 42.31           O  
HETATM 1838  O   HOH A2026      26.911  73.314  11.613  1.00 41.02           O  
HETATM 1839  O   HOH A2027      27.829  71.938  15.804  1.00 27.60           O  
HETATM 1840  O   HOH A2028      26.269  67.619   8.834  1.00 51.93           O  
HETATM 1841  O   HOH A2029      27.012  65.756  12.137  1.00 72.61           O  
HETATM 1842  O   HOH A2030      13.173  65.581  44.734  1.00 57.28           O  
HETATM 1843  O   HOH A2031      -3.579  55.833  37.022  1.00 60.52           O  
HETATM 1844  O   HOH A2032      25.986  94.149  22.108  1.00 37.22           O  
HETATM 1845  O   HOH A2033      26.891  89.823  23.932  1.00 65.17           O  
HETATM 1846  O   HOH A2034     -16.376  70.765  23.656  1.00 51.03           O  
HETATM 1847  O   HOH A2035      -1.602  63.989  26.729  1.00 15.84           O  
HETATM 1848  O   HOH A2036       9.605  63.586  24.635  1.00 20.88           O  
HETATM 1849  O   HOH A2037       4.321  58.958  21.347  1.00 34.20           O  
HETATM 1850  O   HOH A2038      20.824  75.182   8.182  1.00 20.91           O  
HETATM 1851  O   HOH A2039      13.688  72.693   2.690  1.00 39.03           O  
HETATM 1852  O   HOH A2040      15.484  69.765   8.351  1.00 44.50           O  
HETATM 1853  O   HOH A2041       3.264  70.377   1.003  1.00 41.18           O  
HETATM 1854  O   HOH A2042       7.463  69.582   0.846  1.00 54.66           O  
HETATM 1855  O   HOH A2043       6.551  73.789   1.131  1.00 59.39           O  
HETATM 1856  O   HOH A2044      -3.005  71.383   4.825  1.00 30.69           O  
HETATM 1857  O   HOH A2045       0.054  73.992   3.129  1.00 33.82           O  
HETATM 1858  O   HOH A2046      -1.094  57.528  26.237  1.00 27.36           O  
HETATM 1859  O   HOH A2047       1.532  55.916  28.221  1.00 25.63           O  
HETATM 1860  O   HOH A2048       3.423  53.479  26.507  1.00 48.24           O  
HETATM 1861  O   HOH A2049      -0.367  53.968  19.990  1.00 22.61           O  
HETATM 1862  O   HOH A2050      -4.201  70.199   2.513  1.00 43.29           O  
HETATM 1863  O   HOH A2051      -6.672  55.668  22.395  1.00 25.52           O  
HETATM 1864  O   HOH A2052      -2.397  55.205  24.462  1.00 42.78           O  
HETATM 1865  O   HOH A2053      -7.608  53.214  21.725  1.00 34.95           O  
HETATM 1866  O   HOH A2054      -5.009  55.094  10.385  1.00 45.82           O  
HETATM 1867  O   HOH A2055      -6.924  57.051  10.460  1.00 49.47           O  
HETATM 1868  O   HOH A2056      -7.533  61.645  12.074  1.00 35.97           O  
HETATM 1869  O   HOH A2057      -6.433  59.645  10.353  1.00 39.65           O  
HETATM 1870  O   HOH A2058       8.014  92.146  28.519  1.00 65.40           O  
HETATM 1871  O   HOH A2059       3.476  58.483  15.548  1.00 24.17           O  
HETATM 1872  O   HOH A2060       0.745  57.824  12.675  1.00 29.94           O  
HETATM 1873  O   HOH A2061      11.626  96.764  18.027  1.00 44.80           O  
HETATM 1874  O   HOH A2062       7.753  63.609  11.291  1.00 47.87           O  
HETATM 1875  O   HOH A2063       7.039  60.164  13.851  1.00 40.63           O  
HETATM 1876  O   HOH A2064       1.731  59.051  10.322  1.00 32.87           O  
HETATM 1877  O   HOH A2065       3.846  94.220  20.729  1.00 44.63           O  
HETATM 1878  O   HOH A2066       6.174  97.041  20.863  1.00 49.98           O  
HETATM 1879  O   HOH A2067       4.010  95.743  11.295  1.00 32.87           O  
HETATM 1880  O   HOH A2068       2.299  90.184  22.244  1.00 52.11           O  
HETATM 1881  O   HOH A2069      -1.401  91.890  18.470  1.00 67.07           O  
HETATM 1882  O   HOH A2070       8.058  62.929  13.875  1.00 42.64           O  
HETATM 1883  O   HOH A2071       5.648  60.140  16.378  1.00 22.26           O  
HETATM 1884  O   HOH A2072       9.997  64.508  21.450  1.00 34.34           O  
HETATM 1885  O   HOH A2073      10.625  69.126  15.037  1.00 25.51           O  
HETATM 1886  O   HOH A2074       9.836  60.650  17.515  1.00 50.82           O  
HETATM 1887  O   HOH A2075      -6.137  78.381  11.857  1.00 41.91           O  
HETATM 1888  O   HOH A2076      -7.397  79.067  14.624  1.00 41.06           O  
HETATM 1889  O   HOH A2077      -7.815  88.696  13.151  1.00 65.97           O  
HETATM 1890  O   HOH A2078      13.594  70.001  22.281  1.00 30.98           O  
HETATM 1891  O   HOH A2079      13.905  65.130  13.091  1.00 61.17           O  
HETATM 1892  O   HOH A2080      -8.032  75.070  33.580  1.00 42.65           O  
HETATM 1893  O   HOH A2081      15.557  67.560  19.557  1.00 32.32           O  
HETATM 1894  O   HOH A2082      22.398  67.716  18.960  1.00 37.32           O  
HETATM 1895  O   HOH A2083       4.491  83.162  39.332  1.00 48.43           O  
HETATM 1896  O   HOH A2084      22.705  67.646  11.458  1.00 45.93           O  
HETATM 1897  O   HOH A2085      17.561  66.143  11.209  1.00 39.54           O  
HETATM 1898  O   HOH A2086      13.738  63.773  42.345  1.00 46.63           O  
HETATM 1899  O   HOH A2087      26.040  72.394  13.818  1.00 23.49           O  
HETATM 1900  O   HOH A2088      26.167  72.970   5.640  1.00 26.49           O  
HETATM 1901  O   HOH A2089      20.958  70.865   8.946  1.00 23.33           O  
HETATM 1902  O   HOH A2090      27.634  71.621   9.526  1.00 29.92           O  
HETATM 1903  O   HOH A2091      25.427  75.474  12.346  0.50 52.02           O  
HETATM 1904  O   HOH A2092      22.339  73.821   6.422  1.00 23.10           O  
HETATM 1905  O   HOH A2093      27.586  72.608  18.408  1.00 30.90           O  
HETATM 1906  O   HOH A2094      25.475  70.228  20.158  1.00 33.05           O  
HETATM 1907  O   HOH A2095      25.513  68.182  11.758  1.00 46.27           O  
HETATM 1908  O   HOH A2096      30.161  74.624  20.544  1.00 48.51           O  
HETATM 1909  O   HOH A2097      -2.382  81.682  37.003  1.00 55.40           O  
HETATM 1910  O   HOH A2098      22.885  84.357  25.635  1.00 34.71           O  
HETATM 1911  O   HOH A2099      -7.988  85.454  26.722  1.00 56.01           O  
HETATM 1912  O   HOH A2100      -5.396  82.636  29.668  1.00 52.40           O  
HETATM 1913  O   HOH A2101      23.293  69.257  30.884  1.00 66.99           O  
HETATM 1914  O   HOH A2102     -10.516  71.077  29.317  1.00 34.34           O  
HETATM 1915  O   HOH A2103      26.387  76.987  19.834  1.00 21.74           O  
HETATM 1916  O   HOH A2104      -1.595  54.128  27.604  1.00 63.77           O  
HETATM 1917  O   HOH A2105      -3.237  58.192  37.722  1.00 59.67           O  
HETATM 1918  O   HOH A2106      31.157  80.104  23.296  1.00 33.27           O  
HETATM 1919  O   HOH A2107      27.947  81.941  18.791  1.00 69.12           O  
HETATM 1920  O   HOH A2108      30.244  83.844  22.027  1.00 51.85           O  
HETATM 1921  O   HOH A2109      27.511  80.014  29.921  1.00 50.03           O  
HETATM 1922  O   HOH A2110      26.505  85.991  25.103  1.00 44.47           O  
HETATM 1923  O   HOH A2111     -13.177  69.440  26.790  1.00 33.17           O  
HETATM 1924  O   HOH A2112      27.259  84.554  19.100  1.00 23.43           O  
HETATM 1925  O   HOH A2113      24.320  92.687  20.699  1.00 43.28           O  
HETATM 1926  O   HOH A2114      24.070  88.704  24.098  1.00 28.48           O  
HETATM 1927  O   HOH A2115      21.341  87.028  28.281  1.00 54.57           O  
HETATM 1928  O   HOH A2116      21.254  90.980  25.541  1.00 38.03           O  
HETATM 1929  O   HOH A2117     -13.520  69.064  24.103  1.00 46.79           O  
HETATM 1930  O   HOH A2118      15.820  93.158  19.875  1.00 26.42           O  
HETATM 1931  O   HOH A2119     -16.700  66.253  12.590  1.00 44.80           O  
HETATM 1932  O   HOH A2120      25.892  83.302  16.775  1.00 19.86           O  
HETATM 1933  O   HOH A2121      -2.536  74.856   2.949  1.00 68.06           O  
HETATM 1934  O   HOH A2122      -6.377  72.239   3.080  1.00 44.38           O  
HETATM 1935  O   HOH A2123      -0.409  77.382   4.406  1.00 51.68           O  
HETATM 1936  O   HOH A2124      -6.510  81.561   9.990  1.00 61.57           O  
HETATM 1937  O   HOH A2125      13.212  75.993  17.647  1.00 17.39           O  
HETATM 1938  O   HOH A2126      14.733  71.850  12.949  1.00 24.99           O  
HETATM 1939  O   HOH A2127      12.890  82.237  18.585  1.00 16.28           O  
HETATM 1940  O   HOH A2128      11.252  70.282   6.373  1.00 22.99           O  
HETATM 1941  O   HOH A2129      14.518  72.417   5.521  1.00 26.59           O  
HETATM 1942  O   HOH A2130      17.482  71.186   7.966  1.00 39.04           O  
HETATM 1943  O   HOH A2131      20.231  73.218  10.222  1.00 19.93           O  
HETATM 1944  O   HOH A2132      12.571  68.276   7.876  1.00 31.35           O  
HETATM 1945  O   HOH A2133       5.747  71.008   1.952  1.00 30.37           O  
HETATM 1946  O   HOH A2134      10.483  67.753   3.796  1.00 55.64           O  
HETATM 1947  O   HOH A2135       6.052  78.748   4.349  1.00 40.03           O  
HETATM 1948  O   HOH A2136      -0.346  71.790   4.736  1.00 32.73           O  
HETATM 1949  O   HOH A2137       6.529  63.735   4.868  1.00 48.30           O  
HETATM 1950  O   HOH A2138      -5.106  67.892   2.352  1.00 38.67           O  
HETATM 1951  O   HOH A2139       3.086  60.978   5.673  1.00 58.81           O  
HETATM 1952  O   HOH A2140       6.108  61.552   2.192  1.00 58.82           O  
HETATM 1953  O   HOH A2141      -5.843  61.078   8.330  1.00 25.22           O  
HETATM 1954  O   HOH A2142      -5.295  63.491  11.481  1.00 26.96           O  
HETATM 1955  O   HOH A2143      11.212  68.129  23.970  1.00 25.91           O  
HETATM 1956  O   HOH A2144       8.130  65.488  23.249  1.00 25.02           O  
HETATM 1957  O   HOH A2145      14.212  67.232  28.877  1.00 43.26           O  
HETATM 1958  O   HOH A2146      10.333  90.577  30.180  1.00 33.07           O  
HETATM 1959  O   HOH A2147      16.193  88.472  32.245  1.00 39.74           O  
HETATM 1960  O   HOH A2148      12.449  92.484  27.525  1.00 35.64           O  
HETATM 1961  O   HOH A2149      17.561  85.083  23.031  1.00 20.04           O  
HETATM 1962  O   HOH A2150      18.098  94.519  34.299  1.00 63.64           O  
HETATM 1963  O   HOH A2151      19.207  95.909  31.546  1.00 58.24           O  
HETATM 1964  O   HOH A2152      17.752  94.474  22.041  1.00 39.24           O  
HETATM 1965  O   HOH A2153      13.822  97.000  22.505  1.00 53.60           O  
HETATM 1966  O   HOH A2154       9.403  91.320  26.079  1.00 30.88           O  
HETATM 1967  O   HOH A2155      13.751  94.633  21.209  1.00 26.53           O  
HETATM 1968  O   HOH A2156      10.014  96.997  19.548  1.00 35.33           O  
HETATM 1969  O   HOH A2157       7.225  94.272  24.696  1.00 30.44           O  
HETATM 1970  O   HOH A2158       7.453  98.149  15.031  1.00 45.01           O  
HETATM 1971  O   HOH A2159      10.298  95.443  16.442  1.00 27.28           O  
HETATM 1972  O   HOH A2160       3.373  92.593  17.829  1.00 36.25           O  
HETATM 1973  O   HOH A2161       7.500  94.949  13.461  1.00 28.82           O  
HETATM 1974  O   HOH A2162       6.267  94.940  21.770  1.00 26.94           O  
HETATM 1975  O   HOH A2163       4.688  94.415  13.815  1.00 32.80           O  
HETATM 1976  O   HOH A2164      12.332  91.056  14.607  1.00 22.51           O  
HETATM 1977  O   HOH A2165       0.553  88.131  20.060  1.00 35.59           O  
HETATM 1978  O   HOH A2166       0.237  89.798  16.055  1.00 40.72           O  
HETATM 1979  O   HOH A2167       3.942  91.603  10.673  1.00 35.25           O  
HETATM 1980  O   HOH A2168       3.436  91.490  14.338  1.00 36.10           O  
HETATM 1981  O   HOH A2169       7.487  90.054  10.099  1.00 21.23           O  
HETATM 1982  O   HOH A2170      10.400  83.836  18.184  1.00 20.18           O  
HETATM 1983  O   HOH A2171       6.172  85.268   6.588  1.00 24.52           O  
HETATM 1984  O   HOH A2172       3.606  78.557   6.754  1.00 26.06           O  
HETATM 1985  O   HOH A2173       3.559  82.045   5.415  1.00 29.50           O  
HETATM 1986  O   HOH A2174      -8.052  84.359  13.074  1.00 70.26           O  
HETATM 1987  O   HOH A2175      -4.285  76.627  11.228  1.00 21.42           O  
HETATM 1988  O   HOH A2176      -5.460  78.819  16.432  1.00 21.85           O  
HETATM 1989  O   HOH A2177      -8.485  76.579  15.249  1.00 27.89           O  
HETATM 1990  O   HOH A2178      -5.676  75.603  34.648  1.00 38.34           O  
HETATM 1991  O   HOH A2179       1.756  78.258  34.598  1.00 38.54           O  
HETATM 1992  O   HOH A2180      -0.667  74.300  40.185  1.00 43.59           O  
HETATM 1993  O   HOH A2181      -0.628  79.724  40.844  1.00 51.30           O  
HETATM 1994  O   HOH A2182       9.360  76.562  38.712  1.00 41.70           O  
HETATM 1995  O   HOH A2183       3.317  81.017  39.240  1.00 36.83           O  
HETATM 1996  O   HOH A2184       1.895  77.285  44.423  1.00 63.58           O  
HETATM 1997  O   HOH A2185       4.127  80.082  42.193  1.00 40.05           O  
HETATM 1998  O   HOH A2186       3.683  68.331  41.156  1.00 49.55           O  
HETATM 1999  O   HOH A2187      12.442  66.236  37.858  1.00 42.86           O  
HETATM 2000  O   HOH A2188      15.633  66.182  40.487  1.00 46.10           O  
HETATM 2001  O   HOH A2189      18.908  68.701  40.042  1.00 61.65           O  
HETATM 2002  O   HOH A2190      19.255  68.723  27.314  1.00 54.39           O  
HETATM 2003  O   HOH A2191      20.656  76.468  34.727  1.00 54.14           O  
HETATM 2004  O   HOH A2192      22.138  82.453  30.266  1.00 43.27           O  
HETATM 2005  O   HOH A2193      20.517  81.263  32.581  1.00 45.73           O  
HETATM 2006  O   HOH A2194      14.206  71.982  35.136  1.00 50.51           O  
HETATM 2007  O   HOH A2195      15.743  70.837  30.453  1.00 44.65           O  
HETATM 2008  O   HOH A2196      18.208  77.314  39.621  1.00 58.29           O  
HETATM 2009  O   HOH A2197      18.729  82.796  32.897  1.00 41.96           O  
HETATM 2010  O   HOH A2198      16.789  82.555  40.221  1.00 50.87           O  
HETATM 2011  O   HOH A2199       9.468  81.957  40.573  1.00 52.10           O  
HETATM 2012  O   HOH A2200      15.643  79.346  41.073  1.00 34.84           O  
HETATM 2013  O   HOH A2201      11.155  87.294  37.502  1.00 37.29           O  
HETATM 2014  O   HOH A2202       8.541  79.461  32.334  0.33 41.34           O  
HETATM 2015  O   HOH A2203      11.295  90.715  36.676  0.50 27.58           O  
HETATM 2016  O   HOH A2204       8.191  89.360  31.331  1.00 32.28           O  
HETATM 2017  O   HOH A2205       1.763  89.193  31.481  1.00 32.43           O  
HETATM 2018  O   HOH A2206      -3.491  86.548  29.506  1.00 36.23           O  
HETATM 2019  O   HOH A2207      -0.207  80.321  34.567  1.00 23.55           O  
HETATM 2020  O   HOH A2208      -0.457  89.670  22.320  1.00 48.04           O  
HETATM 2021  O   HOH A2209       0.421  85.307  20.569  1.00 32.82           O  
HETATM 2022  O   HOH A2210      -6.018  82.444  26.925  1.00 45.55           O  
HETATM 2023  O   HOH A2211      -7.044  83.014  24.650  1.00 64.01           O  
HETATM 2024  O   HOH A2212      -2.494  95.216  27.124  1.00 60.91           O  
HETATM 2025  O   HOH A2213      -1.832  88.471  15.693  1.00 38.88           O  
HETATM 2026  O   HOH A2214      -8.341  80.813  15.643  1.00 56.72           O  
HETATM 2027  O   HOH A2215      -8.245  81.561  22.561  1.00 62.66           O  
HETATM 2028  O   HOH A2216     -10.772  73.649  19.794  1.00 26.30           O  
HETATM 2029  O   HOH A2217      -8.915  79.856  26.753  1.00 54.44           O  
HETATM 2030  O   HOH A2218     -11.850  78.412  24.122  1.00 41.57           O  
HETATM 2031  O   HOH A2219     -13.447  73.535  24.802  1.00 46.44           O  
HETATM 2032  O   HOH A2220     -12.896  75.296  20.644  1.00 47.30           O  
HETATM 2033  O   HOH A2221      -8.110  71.541  29.776  1.00 38.07           O  
HETATM 2034  O   HOH A2222      -9.137  73.769  28.305  1.00 45.10           O  
HETATM 2035  O   HOH A2223      -9.191  77.774  28.321  1.00 24.68           O  
HETATM 2036  O   HOH A2224      -8.939  71.933  37.373  1.00 44.60           O  
HETATM 2037  O   HOH A2225      -3.136  74.566  37.445  1.00 44.53           O  
HETATM 2038  O   HOH A2226      -2.828  74.141  41.242  1.00 56.38           O  
HETATM 2039  O   HOH A2227      -4.387  69.728  42.046  1.00 47.38           O  
HETATM 2040  O   HOH A2228      -2.078  65.482  41.219  1.00 52.30           O  
HETATM 2041  O   HOH A2229       0.811  69.207  41.006  1.00 53.43           O  
HETATM 2042  O   HOH A2230      -9.949  70.258  35.927  1.00 65.61           O  
HETATM 2043  O   HOH A2231     -11.465  68.171  34.114  1.00 65.19           O  
HETATM 2044  O   HOH A2232      -9.920  65.387  35.851  1.00 37.83           O  
HETATM 2045  O   HOH A2233      -5.487  59.846  38.126  1.00 44.13           O  
HETATM 2046  O   HOH A2234      -5.705  64.058  39.455  1.00 27.55           O  
HETATM 2047  O   HOH A2235       0.782  61.350  38.193  1.00 30.76           O  
HETATM 2048  O   HOH A2236      -2.930  56.383  28.957  1.00 43.13           O  
HETATM 2049  O   HOH A2237      -0.804  54.440  32.022  1.00 46.76           O  
HETATM 2050  O   HOH A2238       0.295  57.742  34.994  1.00 37.81           O  
HETATM 2051  O   HOH A2239      -1.332  59.183  36.457  1.00 26.18           O  
HETATM 2052  O   HOH A2240      -8.486  60.572  34.589  1.00 51.83           O  
HETATM 2053  O   HOH A2241      -9.242  64.301  33.364  1.00 28.44           O  
HETATM 2054  O   HOH A2242      -5.789  57.570  26.621  1.00 27.49           O  
HETATM 2055  O   HOH A2243     -11.170  57.911  27.639  1.00 37.38           O  
HETATM 2056  O   HOH A2244     -13.361  61.677  28.876  1.00 35.19           O  
HETATM 2057  O   HOH A2245      -7.476  58.445  29.019  1.00 31.92           O  
HETATM 2058  O   HOH A2246     -11.790  66.732  29.959  1.00 36.94           O  
HETATM 2059  O   HOH A2247     -10.931  68.405  28.108  1.00 26.32           O  
HETATM 2060  O   HOH A2248      -7.574  70.956  32.566  1.00 25.20           O  
HETATM 2061  O   HOH A2249      -7.846  56.828  24.670  1.00 34.10           O  
HETATM 2062  O   HOH A2250     -13.652  65.515  22.247  1.00 26.71           O  
HETATM 2063  O   HOH A2251     -10.491  71.688  21.580  1.00 25.82           O  
HETATM 2064  O   HOH A2252     -14.222  64.831  18.983  1.00 36.74           O  
HETATM 2065  O   HOH A2253     -11.477  63.516  16.253  1.00 26.55           O  
HETATM 2066  O   HOH A2254      -7.801  59.691  21.370  1.00 19.71           O  
HETATM 2067  O   HOH A2255     -12.947  71.581  22.561  1.00 29.55           O  
HETATM 2068  O   HOH A2256     -16.013  67.323  18.263  1.00 51.82           O  
HETATM 2069  O   HOH A2257     -14.296  67.486  20.778  1.00 40.41           O  
HETATM 2070  O   HOH A2258     -11.682  63.574  13.574  1.00 31.94           O  
HETATM 2071  O   HOH A2259     -15.577  68.203  11.087  1.00 39.88           O  
HETATM 2072  O   HOH A2260      -8.959  72.126   5.724  1.00 37.75           O  
HETATM 2073  O   HOH A2261      -9.937  69.008   8.051  1.00 44.29           O  
HETATM 2074  O   HOH A2262     -12.500  68.003   8.999  1.00 33.00           O  
HETATM 2075  O   HOH A2263     -10.254  73.448   3.793  1.00 53.68           O  
HETATM 2076  O   HOH A2264     -16.053  72.693  12.870  1.00 55.01           O  
HETATM 2077  O   HOH A2265      -4.574  73.795   4.316  1.00 29.01           O  
HETATM 2078  O   HOH A2266       0.797  77.990   6.699  1.00 25.50           O  
HETATM 2079  O   HOH A2267      -3.287  85.172   6.225  1.00 63.88           O  
HETATM 2080  O   HOH A2268      -4.197  82.768   8.833  1.00 31.28           O  
HETATM 2081  O   HOH A2269       2.048  90.455  11.051  1.00 32.61           O  
HETATM 2082  O   HOH A2270      -2.064  84.177  14.530  1.00 23.68           O  
HETATM 2083  O   HOH A2271       4.628  84.120   4.909  1.00 34.64           O  
HETATM 2084  O   HOH A2272      -2.427  87.903  13.460  1.00 39.82           O  
HETATM 2085  O   HOH A2273       4.945  87.618   5.861  1.00 35.85           O  
HETATM 2086  O   HOH A2274      -4.144  85.116   8.435  1.00 45.87           O  
HETATM 2087  O   HOH A2275      -3.428  84.475  11.977  1.00 28.27           O  
HETATM 2088  O   HOH A2276      11.702  68.687  26.796  1.00 20.19           O  
HETATM 2089  O   HOH A2277       9.334  70.268  26.674  1.00 18.19           O  
HETATM 2090  O   HOH A2278      13.659  72.929  30.202  1.00 36.69           O  
HETATM 2091  O   HOH A2279      16.654  75.326  29.200  1.00 36.35           O  
HETATM 2092  O   HOH A2280      15.723  82.154  24.019  1.00 23.56           O  
HETATM 2093  O   HOH A2281      13.853  82.014  21.349  1.00 18.41           O  
HETATM 2094  O   HOH A2282      10.854  70.701  23.354  1.00 40.08           O  
HETATM 2095  O   HOH A2283       6.925  64.355  39.863  1.00 37.95           O  
HETATM 2096  O   HOH A2284       9.471  64.753  38.968  1.00 36.47           O  
HETATM 2097  O   HOH A2285       7.466  61.658  32.665  1.00 20.92           O  
HETATM 2098  O   HOH A2286      10.891  67.320  29.165  1.00 19.79           O  
HETATM 2099  O   HOH A2287       3.520  61.489  38.676  1.00 35.69           O  
HETATM 2100  O   HOH A2288      12.213  64.082  34.882  1.00 35.40           O  
HETATM 2101  O   HOH A2289       6.252  61.276  37.273  1.00 27.41           O  
HETATM 2102  O   HOH A2290      11.712  65.052  32.090  1.00 38.62           O  
HETATM 2103  O   HOH A2291      11.629  68.712  32.915  0.50 25.66           O  
HETATM 2104  O   HOH A2292      13.529  69.374  29.703  1.00 44.15           O  
HETATM 2105  O   HOH A2293      11.378  70.233  29.061  0.33 19.07           O  
HETATM 2106  O   HOH A2294       0.576  65.759  39.916  1.00 40.92           O  
HETATM 2107  O   HOH A2295       9.460  63.729  30.108  1.00 23.55           O  
HETATM 2108  O   HOH A2296       1.489  66.231  33.143  1.00 20.86           O  
HETATM 2109  O   HOH A2297      10.005  72.423  30.576  0.33 27.53           O  
CONECT  160 1811                                                                
CONECT 1711 1713 1715 1717 1719                                                 
CONECT 1712 1714 1716 1718 1720                                                 
CONECT 1713 1711                                                                
CONECT 1714 1712                                                                
CONECT 1715 1711                                                                
CONECT 1716 1712                                                                
CONECT 1717 1711                                                                
CONECT 1718 1712                                                                
CONECT 1719 1711 1721                                                           
CONECT 1720 1712 1722                                                           
CONECT 1721 1719 1723                                                           
CONECT 1722 1720 1724                                                           
CONECT 1723 1721 1725 1727                                                      
CONECT 1724 1722 1726 1728                                                      
CONECT 1725 1723 1733                                                           
CONECT 1726 1724 1734                                                           
CONECT 1727 1723 1729 1731                                                      
CONECT 1728 1724 1730 1732                                                      
CONECT 1729 1727                                                                
CONECT 1730 1728                                                                
CONECT 1731 1727 1733                                                           
CONECT 1732 1728 1734                                                           
CONECT 1733 1725 1731 1735                                                      
CONECT 1734 1726 1732 1736                                                      
CONECT 1735 1733 1737 1751                                                      
CONECT 1736 1734 1738 1752                                                      
CONECT 1737 1735 1739 1741                                                      
CONECT 1738 1736 1740 1742                                                      
CONECT 1739 1737                                                                
CONECT 1740 1738                                                                
CONECT 1741 1737 1743                                                           
CONECT 1742 1738 1744                                                           
CONECT 1743 1741 1745 1747                                                      
CONECT 1744 1742 1746 1748                                                      
CONECT 1745 1743                                                                
CONECT 1746 1744                                                                
CONECT 1747 1743 1749 1751                                                      
CONECT 1748 1744 1750 1752                                                      
CONECT 1749 1747                                                                
CONECT 1750 1748                                                                
CONECT 1751 1735 1747                                                           
CONECT 1752 1736 1748                                                           
CONECT 1753 1754 1755 1756 1760                                                 
CONECT 1754 1753                                                                
CONECT 1755 1753                                                                
CONECT 1756 1753 1811                                                           
CONECT 1757 1758 1759 1760 1764                                                 
CONECT 1758 1757                                                                
CONECT 1759 1757 1811                                                           
CONECT 1760 1753 1757                                                           
CONECT 1761 1762 1763 1764 1765                                                 
CONECT 1762 1761                                                                
CONECT 1763 1761                                                                
CONECT 1764 1757 1761                                                           
CONECT 1765 1761 1766                                                           
CONECT 1766 1765 1767                                                           
CONECT 1767 1766 1768 1769                                                      
CONECT 1768 1767 1773                                                           
CONECT 1769 1767 1770 1771                                                      
CONECT 1770 1769                                                                
CONECT 1771 1769 1772 1773                                                      
CONECT 1772 1771                                                                
CONECT 1773 1768 1771 1774                                                      
CONECT 1774 1773 1775 1783                                                      
CONECT 1775 1774 1776                                                           
CONECT 1776 1775 1777                                                           
CONECT 1777 1776 1778 1783                                                      
CONECT 1778 1777 1779 1780                                                      
CONECT 1779 1778                                                                
CONECT 1780 1778 1781                                                           
CONECT 1781 1780 1782                                                           
CONECT 1782 1781 1783                                                           
CONECT 1783 1774 1777 1782                                                      
CONECT 1784 1785 1786 1787 1791                                                 
CONECT 1785 1784                                                                
CONECT 1786 1784 1811                                                           
CONECT 1787 1784                                                                
CONECT 1788 1789 1790 1791 1792                                                 
CONECT 1789 1788                                                                
CONECT 1790 1788                                                                
CONECT 1791 1784 1788                                                           
CONECT 1792 1788 1793                                                           
CONECT 1793 1792 1794                                                           
CONECT 1794 1793 1795 1796                                                      
CONECT 1795 1794 1800                                                           
CONECT 1796 1794 1797 1798                                                      
CONECT 1797 1796                                                                
CONECT 1798 1796 1799 1800                                                      
CONECT 1799 1798                                                                
CONECT 1800 1795 1798 1801                                                      
CONECT 1801 1800 1802 1810                                                      
CONECT 1802 1801 1803                                                           
CONECT 1803 1802 1804                                                           
CONECT 1804 1803 1805 1810                                                      
CONECT 1805 1804 1806 1807                                                      
CONECT 1806 1805                                                                
CONECT 1807 1805 1808                                                           
CONECT 1808 1807 1809                                                           
CONECT 1809 1808 1810                                                           
CONECT 1810 1801 1804 1809                                                      
CONECT 1811  160 1756 1759 1786                                                 
CONECT 1811 2088 2089 2098 2105                                                 
CONECT 1812 1879 1973 1975                                                      
CONECT 1879 1812                                                                
CONECT 1973 1812                                                                
CONECT 1975 1812                                                                
CONECT 2088 1811                                                                
CONECT 2089 1811                                                                
CONECT 2098 1811                                                                
CONECT 2105 1811                                                                
MASTER      469    0    5   11    5    0   24    6 2020    1  111   17          
END                                                                             
