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Database: PDB
Entry: 4ZZX
LinkDB: 4ZZX
Original site: 4ZZX 
HEADER    TRANSFERASE                             15-APR-15   4ZZX              
TITLE     STRUCTURE OF PARP2 CATALYTIC DOMAIN BOUND TO AN ISOINDOLINONE         
TITLE    2 INHIBITOR                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: POLY [ADP-RIBOSE] POLYMERASE 2;                            
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, UNP RESIDUES 223-583;                    
COMPND   5 SYNONYM: PARP-2, HPARP-2, ADP-RIBOSYLTRANSFERASE DIPHTHERIA TOXIN-   
COMPND   6 LIKE 2, ARTD2, NAD(+) ADP-RIBOSYLTRANSFERASE 2, ADPRT-2, POLYADP-    
COMPND   7 RIBOSE SYNTHASE 2, PADPRT-2, PARP-2, HPARP-2, ADP-RIBOSYLTRANSFERASE 
COMPND   8 DIPHTHERIA TOXIN-LIKE 2, ARTD2, NAD(+) ADP-RIBOSYLTRANSFERASE 2, A   
COMPND   9 DPRT-2, POLYADP-RIBOSE SYNTHASE 2, PADPRT-2, POLY ADP-RIBOSE         
COMPND  10 POLYMERASE 2, POLY ADP-RIBOSE POLYMERASE 2;                          
COMPND  11 EC: 2.4.2.30;                                                        
COMPND  12 ENGINEERED: 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: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    TRANSFERASE                                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.CASALE,M.FASOLINI,G.PAPEO,H.POSTERI,D.BORGHI,A.A.BUSEL,F.CAPRERA,   
AUTHOR   2 M.CIOMEI,A.CIRLA,E.CORTI,M.DANELLO,M.FASOLINI,E.R.FELDER,B.FORTE,    
AUTHOR   3 A.GALVANI,A.ISACCHI,A.KHVAT,M.Y.KRASAVIN,R.LUPI,P.ORSINI,R.PEREGO,   
AUTHOR   4 E.PESENTI,D.PEZZETTA,S.RAINOLDI,F.RICCARDISIRTORI,A.SCOLARO,F.SOLA,  
AUTHOR   5 F.ZUCCOTTO,D.DONATI,A.MONTAGNOLI                                     
REVDAT   3   06-MAR-19 4ZZX    1       REMARK                                   
REVDAT   2   23-SEP-15 4ZZX    1       JRNL                                     
REVDAT   1   12-AUG-15 4ZZX    0                                                
JRNL        AUTH   G.M.E.PAPEO,H.POSTERI,D.BORGHI,A.A.BUSEL,F.CAPRERA,E.CASALE, 
JRNL        AUTH 2 M.CIOMEI,A.CIRLA,E.CORTI,M.D'ANELLO,M.FASOLINI,B.FORTE,      
JRNL        AUTH 3 A.GALVANI,A.ISACCHI,A.KHVAT,M.Y.KRASAVIN,R.LUPI,P.ORSINI,    
JRNL        AUTH 4 R.PEREGO,E.PESENTI,D.PEZZETTA,S.RAINOLDI,F.RICCARDI-SIRTORI, 
JRNL        AUTH 5 A.SCOLARO,F.SOLA,F.ZUCCOTTO,E.R.FELDER,D.DONATI,A.MONTAGNOLI 
JRNL        TITL   DISCOVERY OF                                                 
JRNL        TITL 2 2-[1-(4,4-DIFLUOROCYCLOHEXYL)                                
JRNL        TITL 3 PIPERIDIN-4-YL]-6-FLUORO-3-OXO-2,                            
JRNL        TITL 4 3-DIHYDRO-1H-ISOINDOLE-4-CARBOXAMIDE (NMS-P118): A POTENT,   
JRNL        TITL 5 ORALLY AVAILABLE AND HIGHLY SELECTIVE PARP- 1 INHIBITOR FOR  
JRNL        TITL 6 CANCER THERAPY.                                              
JRNL        REF    J.MED.CHEM.                   V.  58  6875 2015              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   26222319                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.5B00680                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.67                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 84921                          
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) : 0.214                           
REMARK   3   R VALUE            (WORKING SET) : 0.213                           
REMARK   3   FREE R VALUE                     : 0.244                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4478                            
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) : 1.65                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.70                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5818                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.01                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2750                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 293                          
REMARK   3   BIN FREE R VALUE                    : 0.3200                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5576                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 36                                      
REMARK   3   SOLVENT ATOMS            : 312                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.09                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.31000                                             
REMARK   3    B22 (A**2) : 0.12000                                              
REMARK   3    B33 (A**2) : 0.19000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.112         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.109         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.071         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.040         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.944                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.928                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5736 ; 0.008 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7746 ; 1.298 ; 1.980       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   698 ; 5.578 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   259 ;37.132 ;24.440       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1045 ;13.942 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    30 ;15.839 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   847 ; 0.084 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4288 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 4ZZX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-APR-15.                  
REMARK 100 THE DEPOSITION ID IS D_1290063595.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.07                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 89473                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.370                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3KCZ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG4000, 0.2M MAGNESIUM CHLORIDE,    
REMARK 280  0.1 M TRIS PH 8.5, 277K                                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       36.23000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       70.67000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.37000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       70.67000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.23000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       36.37000            
REMARK 290   SMTRY3   4  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     GLY A   221                                                      
REMARK 465     PRO A   222                                                      
REMARK 465     SER A   223                                                      
REMARK 465     LEU A   224                                                      
REMARK 465     LYS A   225                                                      
REMARK 465     SER A   226                                                      
REMARK 465     PRO A   227                                                      
REMARK 465     LEU A   228                                                      
REMARK 465     LYS A   229                                                      
REMARK 465     PRO A   230                                                      
REMARK 465     PRO A   549                                                      
REMARK 465     ASP A   550                                                      
REMARK 465     GLY B   221                                                      
REMARK 465     PRO B   222                                                      
REMARK 465     SER B   223                                                      
REMARK 465     LEU B   224                                                      
REMARK 465     LYS B   225                                                      
REMARK 465     SER B   226                                                      
REMARK 465     PRO B   227                                                      
REMARK 465     LEU B   228                                                      
REMARK 465     LYS B   229                                                      
REMARK 465     PRO B   230                                                      
REMARK 465     GLU B   231                                                      
REMARK 465     SER B   232                                                      
REMARK 465     PRO B   354                                                      
REMARK 465     GLU B   355                                                      
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    HOH B  2066     O    HOH B  2067              2.15            
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    LYS A 259        4.25     81.88                                   
REMARK 500    HIS A 394       60.94   -101.23                                   
REMARK 500    LYS A 480       79.45   -119.14                                   
REMARK 500    HIS B 394       60.88   -100.98                                   
REMARK 500    ASP B 550       84.82     53.14                                   
REMARK 500    ARG B 570      -42.93   -132.48                                   
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 FSU A 1584                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FSU B 1584                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4ZZY   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN PARP2 CATALYTIC DOMAIN BOUND TO AN ISOINDOLINONE  
REMARK 900 INHIBITOR                                                            
REMARK 900 RELATED ID: 4ZZZ   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN PARP1 CATALYTIC DOMAIN BOUND TO AN ISOINDOLINONE  
REMARK 900 INHIBITOR                                                            
REMARK 900 RELATED ID: 5A00   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN PARP1 CATALYTIC DOMAIN BOUND TO AN ISOINDOLINONE  
REMARK 900 INHIBITOR                                                            
DBREF  4ZZX A  223   583  UNP    Q9UGN5   PARP2_HUMAN    223    583             
DBREF  4ZZX B  223   583  UNP    Q9UGN5   PARP2_HUMAN    223    583             
SEQADV 4ZZX GLY A  221  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4ZZX PRO A  222  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4ZZX GLY B  221  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 4ZZX PRO B  222  UNP  Q9UGN5              EXPRESSION TAG                 
SEQRES   1 A  363  GLY PRO SER LEU LYS SER PRO LEU LYS PRO GLU SER GLN          
SEQRES   2 A  363  LEU ASP LEU ARG VAL GLN GLU LEU ILE LYS LEU ILE CYS          
SEQRES   3 A  363  ASN VAL GLN ALA MET GLU GLU MET MET MET GLU MET LYS          
SEQRES   4 A  363  TYR ASN THR LYS LYS ALA PRO LEU GLY LYS LEU THR VAL          
SEQRES   5 A  363  ALA GLN ILE LYS ALA GLY TYR GLN SER LEU LYS LYS ILE          
SEQRES   6 A  363  GLU ASP CYS ILE ARG ALA GLY GLN HIS GLY ARG ALA LEU          
SEQRES   7 A  363  MET GLU ALA CYS ASN GLU PHE TYR THR ARG ILE PRO HIS          
SEQRES   8 A  363  ASP PHE GLY LEU ARG THR PRO PRO LEU ILE ARG THR GLN          
SEQRES   9 A  363  LYS GLU LEU SER GLU LYS ILE GLN LEU LEU GLU ALA LEU          
SEQRES  10 A  363  GLY ASP ILE GLU ILE ALA ILE LYS LEU VAL LYS THR GLU          
SEQRES  11 A  363  LEU GLN SER PRO GLU HIS PRO LEU ASP GLN HIS TYR ARG          
SEQRES  12 A  363  ASN LEU HIS CYS ALA LEU ARG PRO LEU ASP HIS GLU SER          
SEQRES  13 A  363  TYR GLU PHE LYS VAL ILE SER GLN TYR LEU GLN SER THR          
SEQRES  14 A  363  HIS ALA PRO THR HIS SER ASP TYR THR MET THR LEU LEU          
SEQRES  15 A  363  ASP LEU PHE GLU VAL GLU LYS ASP GLY GLU LYS GLU ALA          
SEQRES  16 A  363  PHE ARG GLU ASP LEU HIS ASN ARG MET LEU LEU TRP HIS          
SEQRES  17 A  363  GLY SER ARG MET SER ASN TRP VAL GLY ILE LEU SER HIS          
SEQRES  18 A  363  GLY LEU ARG ILE ALA PRO PRO GLU ALA PRO ILE THR GLY          
SEQRES  19 A  363  TYR MET PHE GLY LYS GLY ILE TYR PHE ALA ASP MET SER          
SEQRES  20 A  363  SER LYS SER ALA ASN TYR CYS PHE ALA SER ARG LEU LYS          
SEQRES  21 A  363  ASN THR GLY LEU LEU LEU LEU SER GLU VAL ALA LEU GLY          
SEQRES  22 A  363  GLN CYS ASN GLU LEU LEU GLU ALA ASN PRO LYS ALA GLU          
SEQRES  23 A  363  GLY LEU LEU GLN GLY LYS HIS SER THR LYS GLY LEU GLY          
SEQRES  24 A  363  LYS MET ALA PRO SER SER ALA HIS PHE VAL THR LEU ASN          
SEQRES  25 A  363  GLY SER THR VAL PRO LEU GLY PRO ALA SER ASP THR GLY          
SEQRES  26 A  363  ILE LEU ASN PRO ASP GLY TYR THR LEU ASN TYR ASN GLU          
SEQRES  27 A  363  TYR ILE VAL TYR ASN PRO ASN GLN VAL ARG MET ARG TYR          
SEQRES  28 A  363  LEU LEU LYS VAL GLN PHE ASN PHE LEU GLN LEU TRP              
SEQRES   1 B  363  GLY PRO SER LEU LYS SER PRO LEU LYS PRO GLU SER GLN          
SEQRES   2 B  363  LEU ASP LEU ARG VAL GLN GLU LEU ILE LYS LEU ILE CYS          
SEQRES   3 B  363  ASN VAL GLN ALA MET GLU GLU MET MET MET GLU MET LYS          
SEQRES   4 B  363  TYR ASN THR LYS LYS ALA PRO LEU GLY LYS LEU THR VAL          
SEQRES   5 B  363  ALA GLN ILE LYS ALA GLY TYR GLN SER LEU LYS LYS ILE          
SEQRES   6 B  363  GLU ASP CYS ILE ARG ALA GLY GLN HIS GLY ARG ALA LEU          
SEQRES   7 B  363  MET GLU ALA CYS ASN GLU PHE TYR THR ARG ILE PRO HIS          
SEQRES   8 B  363  ASP PHE GLY LEU ARG THR PRO PRO LEU ILE ARG THR GLN          
SEQRES   9 B  363  LYS GLU LEU SER GLU LYS ILE GLN LEU LEU GLU ALA LEU          
SEQRES  10 B  363  GLY ASP ILE GLU ILE ALA ILE LYS LEU VAL LYS THR GLU          
SEQRES  11 B  363  LEU GLN SER PRO GLU HIS PRO LEU ASP GLN HIS TYR ARG          
SEQRES  12 B  363  ASN LEU HIS CYS ALA LEU ARG PRO LEU ASP HIS GLU SER          
SEQRES  13 B  363  TYR GLU PHE LYS VAL ILE SER GLN TYR LEU GLN SER THR          
SEQRES  14 B  363  HIS ALA PRO THR HIS SER ASP TYR THR MET THR LEU LEU          
SEQRES  15 B  363  ASP LEU PHE GLU VAL GLU LYS ASP GLY GLU LYS GLU ALA          
SEQRES  16 B  363  PHE ARG GLU ASP LEU HIS ASN ARG MET LEU LEU TRP HIS          
SEQRES  17 B  363  GLY SER ARG MET SER ASN TRP VAL GLY ILE LEU SER HIS          
SEQRES  18 B  363  GLY LEU ARG ILE ALA PRO PRO GLU ALA PRO ILE THR GLY          
SEQRES  19 B  363  TYR MET PHE GLY LYS GLY ILE TYR PHE ALA ASP MET SER          
SEQRES  20 B  363  SER LYS SER ALA ASN TYR CYS PHE ALA SER ARG LEU LYS          
SEQRES  21 B  363  ASN THR GLY LEU LEU LEU LEU SER GLU VAL ALA LEU GLY          
SEQRES  22 B  363  GLN CYS ASN GLU LEU LEU GLU ALA ASN PRO LYS ALA GLU          
SEQRES  23 B  363  GLY LEU LEU GLN GLY LYS HIS SER THR LYS GLY LEU GLY          
SEQRES  24 B  363  LYS MET ALA PRO SER SER ALA HIS PHE VAL THR LEU ASN          
SEQRES  25 B  363  GLY SER THR VAL PRO LEU GLY PRO ALA SER ASP THR GLY          
SEQRES  26 B  363  ILE LEU ASN PRO ASP GLY TYR THR LEU ASN TYR ASN GLU          
SEQRES  27 B  363  TYR ILE VAL TYR ASN PRO ASN GLN VAL ARG MET ARG TYR          
SEQRES  28 B  363  LEU LEU LYS VAL GLN PHE ASN PHE LEU GLN LEU TRP              
HET    FSU  A1584      18                                                       
HET    FSU  B1584      18                                                       
HETNAM     FSU 2-(3-METHOXYPROPYL)-3-OXO-2,3-DIHYDRO-1H-ISOINDOLE-4-            
HETNAM   2 FSU  CARBOXAMIDE                                                     
FORMUL   3  FSU    2(C13 H16 N2 O3)                                             
FORMUL   5  HOH   *312(H2 O)                                                    
HELIX    1   1 ASP A  235  CYS A  246  1                                  12    
HELIX    2   2 ASN A  247  MET A  258  1                                  12    
HELIX    3   3 PRO A  266  LEU A  270  5                                   5    
HELIX    4   4 THR A  271  ALA A  291  1                                  21    
HELIX    5   5 GLY A  295  ILE A  309  1                                  15    
HELIX    6   6 THR A  323  VAL A  347  1                                  25    
HELIX    7   7 HIS A  356  HIS A  366  1                                  11    
HELIX    8   8 SER A  376  THR A  389  1                                  14    
HELIX    9   9 GLY A  411  PHE A  416  1                                   6    
HELIX   10  10 ARG A  431  SER A  433  5                                   3    
HELIX   11  11 ASN A  434  GLY A  442  1                                   9    
HELIX   12  12 PRO A  451  TYR A  455  5                                   5    
HELIX   13  13 MET A  466  ASN A  472  1                                   7    
HELIX   14  14 TYR A  473  PHE A  475  5                                   3    
HELIX   15  15 LYS A  504  LEU A  509  5                                   6    
HELIX   16  16 SER A  525  PHE A  528  5                                   4    
HELIX   17  17 ASN A  563  ASN A  565  5                                   3    
HELIX   18  18 ASP B  235  CYS B  246  1                                  12    
HELIX   19  19 ASN B  247  MET B  258  1                                  12    
HELIX   20  20 PRO B  266  LEU B  270  5                                   5    
HELIX   21  21 THR B  271  ALA B  291  1                                  21    
HELIX   22  22 GLY B  295  ILE B  309  1                                  15    
HELIX   23  23 THR B  323  VAL B  347  1                                  25    
HELIX   24  24 HIS B  356  LEU B  365  1                                  10    
HELIX   25  25 SER B  376  THR B  389  1                                  14    
HELIX   26  26 GLY B  411  PHE B  416  1                                   6    
HELIX   27  27 ARG B  431  SER B  433  5                                   3    
HELIX   28  28 ASN B  434  GLY B  442  1                                   9    
HELIX   29  29 PRO B  451  TYR B  455  5                                   5    
HELIX   30  30 MET B  466  ASN B  472  1                                   7    
HELIX   31  31 TYR B  473  PHE B  475  5                                   3    
HELIX   32  32 LYS B  504  LEU B  509  5                                   6    
HELIX   33  33 SER B  525  PHE B  528  5                                   4    
HELIX   34  34 ASN B  563  ASN B  565  5                                   3    
SHEET    1  AA 5 CYS A 367  PRO A 371  0                                        
SHEET    2  AA 5 TYR A 397  LYS A 409 -1  O  GLU A 406   N  ARG A 370           
SHEET    3  AA 5 VAL A 567  PHE A 579 -1  O  ARG A 570   N  VAL A 407           
SHEET    4  AA 5 THR A 482  ALA A 491 -1  O  GLY A 483   N  VAL A 575           
SHEET    5  AA 5 ARG A 423  GLY A 429 -1  O  MET A 424   N  VAL A 490           
SHEET    1  AB 4 ILE A 461  PHE A 463  0                                        
SHEET    2  AB 4 GLU A 558  VAL A 561 -1  O  TYR A 559   N  PHE A 463           
SHEET    3  AB 4 SER A 514  GLY A 517 -1  O  THR A 515   N  ILE A 560           
SHEET    4  AB 4 CYS A 495  LEU A 498  1  O  ASN A 496   N  LYS A 516           
SHEET    1  AC 3 ALA A 541  ASP A 543  0                                        
SHEET    2  AC 3 GLY A 519  PRO A 523 -1  O  ALA A 522   N  SER A 542           
SHEET    3  AC 3 LEU A 554  TYR A 556  1  O  LEU A 554   N  LYS A 520           
SHEET    1  AD 2 VAL A 529  LEU A 531  0                                        
SHEET    2  AD 2 SER A 534  VAL A 536 -1  O  SER A 534   N  LEU A 531           
SHEET    1  BA 5 CYS B 367  PRO B 371  0                                        
SHEET    2  BA 5 TYR B 397  LYS B 409 -1  O  GLU B 406   N  ARG B 370           
SHEET    3  BA 5 VAL B 567  PHE B 579 -1  O  ARG B 570   N  VAL B 407           
SHEET    4  BA 5 THR B 482  ALA B 491 -1  O  GLY B 483   N  VAL B 575           
SHEET    5  BA 5 ARG B 423  GLY B 429 -1  O  MET B 424   N  VAL B 490           
SHEET    1  BB 4 ILE B 461  PHE B 463  0                                        
SHEET    2  BB 4 GLU B 558  VAL B 561 -1  O  TYR B 559   N  PHE B 463           
SHEET    3  BB 4 SER B 514  GLY B 517 -1  O  THR B 515   N  ILE B 560           
SHEET    4  BB 4 CYS B 495  LEU B 498  1  O  ASN B 496   N  LYS B 516           
SHEET    1  BC 3 ALA B 541  ASP B 543  0                                        
SHEET    2  BC 3 GLY B 519  PRO B 523 -1  O  ALA B 522   N  SER B 542           
SHEET    3  BC 3 LEU B 554  TYR B 556  1  O  LEU B 554   N  LYS B 520           
SHEET    1  BD 2 VAL B 529  LEU B 531  0                                        
SHEET    2  BD 2 SER B 534  VAL B 536 -1  O  SER B 534   N  LEU B 531           
CISPEP   1 GLY A  539    PRO A  540          0         3.86                     
CISPEP   2 GLY B  539    PRO B  540          0         5.95                     
SITE     1 AC1 10 SER A 328  HIS A 428  GLY A 429  GLY A 454                    
SITE     2 AC1 10 TYR A 462  PHE A 463  SER A 470  TYR A 473                    
SITE     3 AC1 10 HOH A2162  HOH A2163                                          
SITE     1 AC2 10 SER B 328  ILE B 331  HIS B 428  GLY B 429                    
SITE     2 AC2 10 GLY B 454  TYR B 462  PHE B 463  SER B 470                    
SITE     3 AC2 10 TYR B 473  HOH B2149                                          
CRYST1   72.460   72.740  141.340  90.00  90.00  90.00 P 21 21 21    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      0.013801  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013748  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007075        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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