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Database: PDB
Entry: 4TVJ
LinkDB: 4TVJ
Original site: 4TVJ 
HEADER    TRANSFERASE                             27-JUN-14   4TVJ              
TITLE     HUMAN ARTD2 (PARP2) - CATALYTIC DOMAIN IN COMPLEX WITH OLAPARIB       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: POLY [ADP-RIBOSE] POLYMERASE 2;                            
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: HPARP-2,ADP-RIBOSYLTRANSFERASE DIPHTHERIA TOXIN-LIKE 2,     
COMPND   5 ARTD2,NAD(+) ADP-RIBOSYLTRANSFERASE 2,ADPRT-2,POLY[ADP-RIBOSE]       
COMPND   6 SYNTHASE 2,PADPRT-2;                                                 
COMPND   7 EC: 2.4.2.30;                                                        
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PARP2, ADPRT2, ADPRTL2;                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: R3 PRARE;                                  
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4                               
KEYWDS    POLY(ADP-RIBOSE) TRANSFERASE, INHIBITOR, ADP-RIBOSYLATION,            
KEYWDS   2 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.KARLBERG,A.G.THORSELL,T.EKBLAD,A.F.PINTO,H.SCHULER                  
REVDAT   3   22-MAR-17 4TVJ    1       JRNL                                     
REVDAT   2   18-JAN-17 4TVJ    1       JRNL                                     
REVDAT   1   08-JUL-15 4TVJ    0                                                
JRNL        AUTH   A.G.THORSELL,T.EKBLAD,T.KARLBERG,M.LOW,A.F.PINTO,            
JRNL        AUTH 2 L.TRESAUGUES,M.MOCHE,M.S.COHEN,H.SCHULER                     
JRNL        TITL   STRUCTURAL BASIS FOR POTENCY AND PROMISCUITY IN              
JRNL        TITL 2 POLY(ADP-RIBOSE) POLYMERASE (PARP) AND TANKYRASE INHIBITORS. 
JRNL        REF    J. MED. CHEM.                 V.  60  1262 2017              
JRNL        REFN                   ISSN 1520-4804                               
JRNL        PMID   28001384                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.6B00990                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.28                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 43558                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.190                           
REMARK   3   R VALUE            (WORKING SET) : 0.188                           
REMARK   3   FREE R VALUE                     : 0.231                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2293                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3174                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2320                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 167                          
REMARK   3   BIN FREE R VALUE                    : 0.2980                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5609                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 82                                      
REMARK   3   SOLVENT ATOMS            : 267                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.88                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.97000                                              
REMARK   3    B22 (A**2) : 0.37000                                              
REMARK   3    B33 (A**2) : -0.83000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.54000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.220         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.183         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.127         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.101        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.949                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.924                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5815 ; 0.017 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  3993 ; 0.004 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7851 ; 1.530 ; 1.987       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9765 ; 1.027 ; 3.002       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   705 ; 6.212 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   259 ;36.227 ;24.363       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1042 ;14.919 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    30 ;16.891 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   853 ; 0.088 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6371 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1125 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3522 ; 0.805 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1429 ; 0.190 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5657 ; 1.471 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2293 ; 2.319 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2188 ; 3.724 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   223        A   579                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.9670  -0.0870  16.2690              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0291 T22:   0.0161                                     
REMARK   3      T33:   0.0412 T12:  -0.0058                                     
REMARK   3      T13:   0.0087 T23:  -0.0144                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6516 L22:   0.1652                                     
REMARK   3      L33:   0.5152 L12:  -0.0854                                     
REMARK   3      L13:  -0.1402 L23:  -0.0845                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0649 S12:   0.0280 S13:  -0.0070                       
REMARK   3      S21:   0.0367 S22:   0.0267 S23:  -0.0038                       
REMARK   3      S31:   0.0012 S32:  -0.0050 S33:   0.0381                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   226        B   579                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.8520 -32.7100   9.0590              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0760 T22:   0.0343                                     
REMARK   3      T33:   0.0145 T12:  -0.0277                                     
REMARK   3      T13:   0.0160 T23:   0.0036                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4920 L22:   0.5129                                     
REMARK   3      L33:   0.6167 L12:   0.1372                                     
REMARK   3      L13:  -0.2594 L23:   0.3170                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0358 S12:  -0.0192 S13:  -0.0569                       
REMARK   3      S21:  -0.1095 S22:   0.0628 S23:  -0.0548                       
REMARK   3      S31:  -0.0699 S32:   0.0127 S33:  -0.0271                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4TVJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-JUN-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000202357.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-JUL-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.99190                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 45851                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 7.500                              
REMARK 200  R MERGE                    (I) : 0.10900                            
REMARK 200  R SYM                      (I) : 0.10700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.15                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.66900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3KCZ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.74                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG3350, 0.1M TRIS, PH 8.5, VAPOR    
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 277K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       67.06150            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   212                                                      
REMARK 465     HIS A   213                                                      
REMARK 465     HIS A   214                                                      
REMARK 465     HIS A   215                                                      
REMARK 465     HIS A   216                                                      
REMARK 465     HIS A   217                                                      
REMARK 465     HIS A   218                                                      
REMARK 465     SER A   219                                                      
REMARK 465     SER A   220                                                      
REMARK 465     GLY A   221                                                      
REMARK 465     VAL A   222                                                      
REMARK 465     MET B   212                                                      
REMARK 465     HIS B   213                                                      
REMARK 465     HIS B   214                                                      
REMARK 465     HIS B   215                                                      
REMARK 465     HIS B   216                                                      
REMARK 465     HIS B   217                                                      
REMARK 465     HIS B   218                                                      
REMARK 465     SER B   219                                                      
REMARK 465     SER B   220                                                      
REMARK 465     GLY B   221                                                      
REMARK 465     VAL B   222                                                      
REMARK 465     ASP B   223                                                      
REMARK 465     LEU B   224                                                      
REMARK 465     GLY B   225                                                      
REMARK 465     GLU B   350                                                      
REMARK 465     LEU B   351                                                      
REMARK 465     GLN B   352                                                      
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     ASP A 223    CG   OD1  OD2                                       
REMARK 470     GLN A 510    CD   OE1  NE2                                       
REMARK 470     TYR A 552    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASN B 228    CG   OD1  ND2                                       
REMARK 470     GLN B 232    CG   CD   OE1  NE2                                  
REMARK 470     TYR B 552    CG   CD1  CD2  CE1  CE2  CZ   OH                    
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 B 316   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    HIS A 394       50.70   -107.71                                   
REMARK 500    ARG A 570      -43.95   -138.33                                   
REMARK 500    GLN B 232       78.98     64.53                                   
REMARK 500    HIS B 294      -30.04   -143.36                                   
REMARK 500    ARG B 322       -5.08   -141.25                                   
REMARK 500    HIS B 394       55.36   -109.48                                   
REMARK 500    ASP B 410      117.57    -38.01                                   
REMARK 500    ASP B 550      -84.26   -103.86                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 09L A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 09L B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 602                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3KCZ   RELATED DB: PDB                                   
REMARK 900 3KCZ CONTAINS THE SAME PROTEIN COMPLEXED WITH 3-AMINOBENZAMIDE.      
REMARK 900 RELATED ID: 3KJD   RELATED DB: PDB                                   
REMARK 900 3KJD CONTAINS THE SAME PROTEIN COMPLEXED WITH ABT-888 (VELIPARIB).   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE SEQUENCE MISMATCH IS DUE TO SEQUENCE CONFLICTS BETWEEN UNIPROT   
REMARK 999 AND GENBANK (ID AF085734.1). IN THIS CASE AUTHORS HAVE USED THE      
REMARK 999 SEQUENCE FROM GENBANK (HTTP://WWW.NCBI.NLM.NIH.GOV/NUCCORE/4808556), 
REMARK 999 HERE RESIDUE 447 IS HISTIDINE.                                       
DBREF  4TVJ A  235   579  UNP    Q9UGN5   PARP2_HUMAN    235    579             
DBREF  4TVJ B  235   579  UNP    Q9UGN5   PARP2_HUMAN    235    579             
SEQADV 4TVJ MET A  212  UNP  Q9UGN5              INITIATING METHIONINE          
SEQADV 4TVJ HIS A  213  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4TVJ HIS A  214  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4TVJ HIS A  215  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4TVJ HIS A  216  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4TVJ HIS A  217  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4TVJ HIS A  218  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4TVJ SER A  219  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4TVJ SER A  220  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4TVJ GLY A  221  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4TVJ VAL A  222  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4TVJ ASP A  223  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4TVJ LEU A  224  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4TVJ GLY A  225  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4TVJ THR A  226  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4TVJ GLU A  227  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4TVJ ASN A  228  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4TVJ LEU A  229  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4TVJ TYR A  230  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4TVJ PHE A  231  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4TVJ GLN A  232  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4TVJ SER A  233  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4TVJ MET A  234  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4TVJ HIS A  447  UNP  Q9UGN5    PRO   447 CONFLICT                       
SEQADV 4TVJ MET B  212  UNP  Q9UGN5              INITIATING METHIONINE          
SEQADV 4TVJ HIS B  213  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4TVJ HIS B  214  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4TVJ HIS B  215  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4TVJ HIS B  216  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4TVJ HIS B  217  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4TVJ HIS B  218  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4TVJ SER B  219  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4TVJ SER B  220  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4TVJ GLY B  221  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4TVJ VAL B  222  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4TVJ ASP B  223  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4TVJ LEU B  224  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4TVJ GLY B  225  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4TVJ THR B  226  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4TVJ GLU B  227  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4TVJ ASN B  228  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4TVJ LEU B  229  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4TVJ TYR B  230  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4TVJ PHE B  231  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4TVJ GLN B  232  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4TVJ SER B  233  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4TVJ MET B  234  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4TVJ HIS B  447  UNP  Q9UGN5    PRO   447 CONFLICT                       
SEQRES   1 A  368  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 A  368  GLY THR GLU ASN LEU TYR PHE GLN SER MET ASP LEU ARG          
SEQRES   3 A  368  VAL GLN GLU LEU ILE LYS LEU ILE CYS ASN VAL GLN ALA          
SEQRES   4 A  368  MET GLU GLU MET MET MET GLU MET LYS TYR ASN THR LYS          
SEQRES   5 A  368  LYS ALA PRO LEU GLY LYS LEU THR VAL ALA GLN ILE LYS          
SEQRES   6 A  368  ALA GLY TYR GLN SER LEU LYS LYS ILE GLU ASP CYS ILE          
SEQRES   7 A  368  ARG ALA GLY GLN HIS GLY ARG ALA LEU MET GLU ALA CYS          
SEQRES   8 A  368  ASN GLU PHE TYR THR ARG ILE PRO HIS ASP PHE GLY LEU          
SEQRES   9 A  368  ARG THR PRO PRO LEU ILE ARG THR GLN LYS GLU LEU SER          
SEQRES  10 A  368  GLU LYS ILE GLN LEU LEU GLU ALA LEU GLY ASP ILE GLU          
SEQRES  11 A  368  ILE ALA ILE LYS LEU VAL LYS THR GLU LEU GLN SER PRO          
SEQRES  12 A  368  GLU HIS PRO LEU ASP GLN HIS TYR ARG ASN LEU HIS CYS          
SEQRES  13 A  368  ALA LEU ARG PRO LEU ASP HIS GLU SER TYR GLU PHE LYS          
SEQRES  14 A  368  VAL ILE SER GLN TYR LEU GLN SER THR HIS ALA PRO THR          
SEQRES  15 A  368  HIS SER ASP TYR THR MET THR LEU LEU ASP LEU PHE GLU          
SEQRES  16 A  368  VAL GLU LYS ASP GLY GLU LYS GLU ALA PHE ARG GLU ASP          
SEQRES  17 A  368  LEU HIS ASN ARG MET LEU LEU TRP HIS GLY SER ARG MET          
SEQRES  18 A  368  SER ASN TRP VAL GLY ILE LEU SER HIS GLY LEU ARG ILE          
SEQRES  19 A  368  ALA HIS PRO GLU ALA PRO ILE THR GLY TYR MET PHE GLY          
SEQRES  20 A  368  LYS GLY ILE TYR PHE ALA ASP MET SER SER LYS SER ALA          
SEQRES  21 A  368  ASN TYR CYS PHE ALA SER ARG LEU LYS ASN THR GLY LEU          
SEQRES  22 A  368  LEU LEU LEU SER GLU VAL ALA LEU GLY GLN CYS ASN GLU          
SEQRES  23 A  368  LEU LEU GLU ALA ASN PRO LYS ALA GLU GLY LEU LEU GLN          
SEQRES  24 A  368  GLY LYS HIS SER THR LYS GLY LEU GLY LYS MET ALA PRO          
SEQRES  25 A  368  SER SER ALA HIS PHE VAL THR LEU ASN GLY SER THR VAL          
SEQRES  26 A  368  PRO LEU GLY PRO ALA SER ASP THR GLY ILE LEU ASN PRO          
SEQRES  27 A  368  ASP GLY TYR THR LEU ASN TYR ASN GLU TYR ILE VAL TYR          
SEQRES  28 A  368  ASN PRO ASN GLN VAL ARG MET ARG TYR LEU LEU LYS VAL          
SEQRES  29 A  368  GLN PHE ASN PHE                                              
SEQRES   1 B  368  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 B  368  GLY THR GLU ASN LEU TYR PHE GLN SER MET ASP LEU ARG          
SEQRES   3 B  368  VAL GLN GLU LEU ILE LYS LEU ILE CYS ASN VAL GLN ALA          
SEQRES   4 B  368  MET GLU GLU MET MET MET GLU MET LYS TYR ASN THR LYS          
SEQRES   5 B  368  LYS ALA PRO LEU GLY LYS LEU THR VAL ALA GLN ILE LYS          
SEQRES   6 B  368  ALA GLY TYR GLN SER LEU LYS LYS ILE GLU ASP CYS ILE          
SEQRES   7 B  368  ARG ALA GLY GLN HIS GLY ARG ALA LEU MET GLU ALA CYS          
SEQRES   8 B  368  ASN GLU PHE TYR THR ARG ILE PRO HIS ASP PHE GLY LEU          
SEQRES   9 B  368  ARG THR PRO PRO LEU ILE ARG THR GLN LYS GLU LEU SER          
SEQRES  10 B  368  GLU LYS ILE GLN LEU LEU GLU ALA LEU GLY ASP ILE GLU          
SEQRES  11 B  368  ILE ALA ILE LYS LEU VAL LYS THR GLU LEU GLN SER PRO          
SEQRES  12 B  368  GLU HIS PRO LEU ASP GLN HIS TYR ARG ASN LEU HIS CYS          
SEQRES  13 B  368  ALA LEU ARG PRO LEU ASP HIS GLU SER TYR GLU PHE LYS          
SEQRES  14 B  368  VAL ILE SER GLN TYR LEU GLN SER THR HIS ALA PRO THR          
SEQRES  15 B  368  HIS SER ASP TYR THR MET THR LEU LEU ASP LEU PHE GLU          
SEQRES  16 B  368  VAL GLU LYS ASP GLY GLU LYS GLU ALA PHE ARG GLU ASP          
SEQRES  17 B  368  LEU HIS ASN ARG MET LEU LEU TRP HIS GLY SER ARG MET          
SEQRES  18 B  368  SER ASN TRP VAL GLY ILE LEU SER HIS GLY LEU ARG ILE          
SEQRES  19 B  368  ALA HIS PRO GLU ALA PRO ILE THR GLY TYR MET PHE GLY          
SEQRES  20 B  368  LYS GLY ILE TYR PHE ALA ASP MET SER SER LYS SER ALA          
SEQRES  21 B  368  ASN TYR CYS PHE ALA SER ARG LEU LYS ASN THR GLY LEU          
SEQRES  22 B  368  LEU LEU LEU SER GLU VAL ALA LEU GLY GLN CYS ASN GLU          
SEQRES  23 B  368  LEU LEU GLU ALA ASN PRO LYS ALA GLU GLY LEU LEU GLN          
SEQRES  24 B  368  GLY LYS HIS SER THR LYS GLY LEU GLY LYS MET ALA PRO          
SEQRES  25 B  368  SER SER ALA HIS PHE VAL THR LEU ASN GLY SER THR VAL          
SEQRES  26 B  368  PRO LEU GLY PRO ALA SER ASP THR GLY ILE LEU ASN PRO          
SEQRES  27 B  368  ASP GLY TYR THR LEU ASN TYR ASN GLU TYR ILE VAL TYR          
SEQRES  28 B  368  ASN PRO ASN GLN VAL ARG MET ARG TYR LEU LEU LYS VAL          
SEQRES  29 B  368  GLN PHE ASN PHE                                              
HET    09L  A 601      32                                                       
HET    GOL  A 602       6                                                       
HET    GOL  A 603       6                                                       
HET    09L  B 601      32                                                       
HET    GOL  B 602       6                                                       
HETNAM     09L 4-(3-{[4-(CYCLOPROPYLCARBONYL)PIPERAZIN-1-YL]CARBONYL}-          
HETNAM   2 09L  4-FLUOROBENZYL)PHTHALAZIN-1(2H)-ONE                             
HETNAM     GOL GLYCEROL                                                         
HETSYN     09L OLAPARIB                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  09L    2(C24 H23 F N4 O3)                                           
FORMUL   4  GOL    3(C3 H8 O3)                                                  
FORMUL   8  HOH   *267(H2 O)                                                    
HELIX    1 AA1 ASP A  223  GLN A  232  1                                  10    
HELIX    2 AA2 ASP A  235  CYS A  246  1                                  12    
HELIX    3 AA3 ASN A  247  MET A  258  1                                  12    
HELIX    4 AA4 PRO A  266  LEU A  270  5                                   5    
HELIX    5 AA5 THR A  271  ALA A  291  1                                  21    
HELIX    6 AA6 GLY A  295  ILE A  309  1                                  15    
HELIX    7 AA7 THR A  323  VAL A  347  1                                  25    
HELIX    8 AA8 HIS A  356  HIS A  366  1                                  11    
HELIX    9 AA9 SER A  376  THR A  389  1                                  14    
HELIX   10 AB1 GLY A  411  PHE A  416  1                                   6    
HELIX   11 AB2 ARG A  431  SER A  433  5                                   3    
HELIX   12 AB3 ASN A  434  GLY A  442  1                                   9    
HELIX   13 AB4 PRO A  451  TYR A  455  5                                   5    
HELIX   14 AB5 MET A  466  ASN A  472  1                                   7    
HELIX   15 AB6 TYR A  473  PHE A  475  5                                   3    
HELIX   16 AB7 LYS A  504  LEU A  509  5                                   6    
HELIX   17 AB8 SER A  525  PHE A  528  5                                   4    
HELIX   18 AB9 ASN A  563  ASN A  565  5                                   3    
HELIX   19 AC1 GLU B  227  GLN B  232  1                                   6    
HELIX   20 AC2 ASP B  235  CYS B  246  1                                  12    
HELIX   21 AC3 ASN B  247  MET B  258  1                                  12    
HELIX   22 AC4 PRO B  266  LEU B  270  5                                   5    
HELIX   23 AC5 THR B  271  GLY B  292  1                                  22    
HELIX   24 AC6 GLY B  295  ILE B  309  1                                  15    
HELIX   25 AC7 THR B  323  VAL B  347  1                                  25    
HELIX   26 AC8 HIS B  356  HIS B  366  1                                  11    
HELIX   27 AC9 SER B  376  THR B  389  1                                  14    
HELIX   28 AD1 GLY B  411  PHE B  416  1                                   6    
HELIX   29 AD2 ARG B  431  SER B  433  5                                   3    
HELIX   30 AD3 ASN B  434  GLY B  442  1                                   9    
HELIX   31 AD4 PRO B  451  TYR B  455  5                                   5    
HELIX   32 AD5 MET B  466  TYR B  473  1                                   8    
HELIX   33 AD6 LYS B  504  LEU B  509  5                                   6    
HELIX   34 AD7 SER B  525  PHE B  528  5                                   4    
HELIX   35 AD8 ASN B  563  ASN B  565  5                                   3    
SHEET    1 AA1 5 CYS A 367  PRO A 371  0                                        
SHEET    2 AA1 5 THR A 398  LYS A 409 -1  O  GLU A 406   N  ARG A 370           
SHEET    3 AA1 5 VAL A 567  ASN A 578 -1  O  ASN A 578   N  THR A 398           
SHEET    4 AA1 5 THR A 482  ALA A 491 -1  N  LEU A 487   O  TYR A 571           
SHEET    5 AA1 5 ARG A 423  GLY A 429 -1  N  HIS A 428   O  LEU A 486           
SHEET    1 AA2 4 ILE A 461  PHE A 463  0                                        
SHEET    2 AA2 4 GLU A 558  VAL A 561 -1  O  VAL A 561   N  ILE A 461           
SHEET    3 AA2 4 SER A 514  GLY A 517 -1  N  GLY A 517   O  GLU A 558           
SHEET    4 AA2 4 CYS A 495  LEU A 498  1  N  ASN A 496   O  SER A 514           
SHEET    1 AA3 3 ALA A 541  ASP A 543  0                                        
SHEET    2 AA3 3 GLY A 519  PRO A 523 -1  N  ALA A 522   O  SER A 542           
SHEET    3 AA3 3 LEU A 554  TYR A 556  1  O  ASN A 555   N  MET A 521           
SHEET    1 AA4 2 VAL A 529  LEU A 531  0                                        
SHEET    2 AA4 2 SER A 534  VAL A 536 -1  O  VAL A 536   N  VAL A 529           
SHEET    1 AA5 5 CYS B 367  PRO B 371  0                                        
SHEET    2 AA5 5 THR B 398  LYS B 409 -1  O  GLU B 406   N  ARG B 370           
SHEET    3 AA5 5 VAL B 567  ASN B 578 -1  O  ASN B 578   N  THR B 398           
SHEET    4 AA5 5 THR B 482  ALA B 491 -1  N  GLU B 489   O  ARG B 568           
SHEET    5 AA5 5 ARG B 423  GLY B 429 -1  N  MET B 424   O  VAL B 490           
SHEET    1 AA6 4 ILE B 461  PHE B 463  0                                        
SHEET    2 AA6 4 GLU B 558  VAL B 561 -1  O  VAL B 561   N  ILE B 461           
SHEET    3 AA6 4 SER B 514  GLY B 517 -1  N  THR B 515   O  ILE B 560           
SHEET    4 AA6 4 CYS B 495  LEU B 498  1  N  ASN B 496   O  SER B 514           
SHEET    1 AA7 3 ALA B 541  ASP B 543  0                                        
SHEET    2 AA7 3 GLY B 519  PRO B 523 -1  N  ALA B 522   O  SER B 542           
SHEET    3 AA7 3 LEU B 554  TYR B 556  1  O  ASN B 555   N  MET B 521           
SHEET    1 AA8 2 VAL B 529  LEU B 531  0                                        
SHEET    2 AA8 2 SER B 534  VAL B 536 -1  O  VAL B 536   N  VAL B 529           
CISPEP   1 GLY A  539    PRO A  540          0         2.48                     
CISPEP   2 GLY B  539    PRO B  540          0         5.15                     
SITE     1 AC1 13 GLU A 335  HIS A 428  GLY A 429  ARG A 444                    
SITE     2 AC1 13 TYR A 455  GLY A 460  ILE A 461  TYR A 462                    
SITE     3 AC1 13 PHE A 463  SER A 470  TYR A 473  GOL A 603                    
SITE     4 AC1 13 HOH A 723                                                     
SITE     1 AC2  6 ASP A 396  TYR A 397  ALA A 471  ASN A 472                    
SITE     2 AC2  6 PHE A 475  ALA A 476                                          
SITE     1 AC3  7 SER A 328  ILE A 331  GLU A 335  GLY A 454                    
SITE     2 AC3  7 TYR A 455  09L A 601  HOH A 854                               
SITE     1 AC4 11 GLU B 335  HIS B 428  GLY B 429  ARG B 444                    
SITE     2 AC4 11 TYR B 455  GLY B 460  ILE B 461  TYR B 462                    
SITE     3 AC4 11 SER B 470  TYR B 473  HOH B 719                               
SITE     1 AC5  7 ASP B 396  TYR B 397  ALA B 471  ASN B 472                    
SITE     2 AC5  7 CYS B 474  PHE B 475  ALA B 476                               
CRYST1   58.083  134.123   58.348  90.00 117.96  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.017217  0.000000  0.009140        0.00000                         
SCALE2      0.000000  0.007456  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019404        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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