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Database: PDB
Entry: 6F5F
LinkDB: 6F5F
Original site: 6F5F 
HEADER    DNA BINDING PROTEIN                     01-DEC-17   6F5F              
TITLE     STRUCTURE OF ARTD2/PARP2 WGR DOMAIN BOUND TO DOUBLE STRAND DNA WITH 5 
TITLE    2 NUCLEOTIDE OVERHANG AND 5'PHOSPHATE                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: POLY [ADP-RIBOSE] POLYMERASE 2;                            
COMPND   3 CHAIN: A, B, C, D;                                                   
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;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: DNA (5'-D(P*CP*GP*GP*TP*CP*GP*CP*CP*TP*AP*TP*AP*GP*GP*C)-  
COMPND  11 3');                                                                 
COMPND  12 CHAIN: E, F, G, H;                                                   
COMPND  13 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;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_TAXID: 9606                                                 
KEYWDS    ADP-RIBOSYLATION, DNA REPAIR, DNA END JOINING, ARTD2, NON-            
KEYWDS   2 PHOSPHORYLATED DNA, DNA BINDING PROTEIN                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.OBAJI,T.HAIKARAINEN,L.LEHTIO                                        
REVDAT   3   26-DEC-18 6F5F    1       JRNL                                     
REVDAT   2   24-OCT-18 6F5F    1       JRNL                                     
REVDAT   1   10-OCT-18 6F5F    0                                                
JRNL        AUTH   E.OBAJI,T.HAIKARAINEN,L.LEHTIO                               
JRNL        TITL   STRUCTURAL BASIS FOR DNA BREAK RECOGNITION BY ARTD2/PARP2.   
JRNL        REF    NUCLEIC ACIDS RES.            V.  46 12154 2018              
JRNL        REFN                   ESSN 1362-4962                               
JRNL        PMID   30321391                                                     
JRNL        DOI    10.1093/NAR/GKY927                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.98 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0158                                      
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) : 2.98                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.86                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 21936                          
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) : 0.231                           
REMARK   3   R VALUE            (WORKING SET) : 0.228                           
REMARK   3   FREE R VALUE                     : 0.275                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1155                            
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) : 2.98                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.06                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1553                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.70                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4830                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 82                           
REMARK   3   BIN FREE R VALUE                    : 0.4800                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3780                                    
REMARK   3   NUCLEIC ACID ATOMS       : 1232                                    
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 121.6                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.90000                                              
REMARK   3    B22 (A**2) : 7.42000                                              
REMARK   3    B33 (A**2) : -11.32000                                            
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): 1.130         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.400         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.404         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 25.197        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.936                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5236 ; 0.011 ; 0.017       
REMARK   3   BOND LENGTHS OTHERS               (A):  4155 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7308 ; 1.778 ; 1.717       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9731 ; 1.178 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   457 ; 6.826 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   210 ;38.531 ;25.619       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   723 ;18.868 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;15.417 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   705 ; 0.115 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5019 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1089 ; 0.002 ; 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):  1840 ; 9.410 ;12.641       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1839 ; 9.401 ;12.641       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2293 ;13.985 ;18.947       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  2294 ;13.982 ;18.949       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3396 ; 9.755 ;12.194       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  3395 ; 9.755 ;12.195       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  5015 ;14.351 ;18.116       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  6011 ;16.965 ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  6012 ;16.964 ;  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   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 12                                
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A    92    207       B    92    207    7378  0.09  0.05     
REMARK   3    2     A    92    205       C    92    205    7190  0.10  0.05     
REMARK   3    3     A    92    204       D    92    204    7148  0.09  0.05     
REMARK   3    4     B    92    205       C    92    205    7200  0.11  0.05     
REMARK   3    5     B    92    204       D    92    204    7108  0.11  0.05     
REMARK   3    6     C    92    204       D    92    204    7048  0.11  0.05     
REMARK   3    7     E     1     15       F     1     15    2310  0.16  0.05     
REMARK   3    8     E     1     15       G     1     15    2294  0.16  0.05     
REMARK   3    9     E     1     15       H     1     15    2282  0.17  0.05     
REMARK   3   10     F     1     15       G     1     15    2458  0.13  0.05     
REMARK   3   11     F     1     15       H     1     15    2554  0.12  0.05     
REMARK   3   12     G     1     15       H     1     15    2402  0.16  0.05     
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 ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 6F5F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-DEC-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200007639.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-JUL-16                          
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               : 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) : 0.97949                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23275                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.980                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 6.380                              
REMARK 200  R MERGE                    (I) : 0.06900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.2900                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.98                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
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 ID 6F1K                                          
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.48                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M NA-FORMATE 20 % PEG 3350 20 %      
REMARK 280  GLYCEROL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 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       34.07500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       92.63500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.57500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       92.63500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       34.07500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       43.57500            
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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E, F                               
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 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000      -34.07500            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000       43.57500            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D, G, H                            
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     SER A    88                                                      
REMARK 465     MET A    89                                                      
REMARK 465     GLY A    90                                                      
REMARK 465     LYS A    91                                                      
REMARK 465     TYR A   208                                                      
REMARK 465     ALA A   209                                                      
REMARK 465     THR A   210                                                      
REMARK 465     ASN A   211                                                      
REMARK 465     THR A   212                                                      
REMARK 465     GLN A   213                                                      
REMARK 465     ASP A   214                                                      
REMARK 465     GLU A   215                                                      
REMARK 465     GLU A   216                                                      
REMARK 465     GLU A   217                                                      
REMARK 465     THR A   218                                                      
REMARK 465     SER B    88                                                      
REMARK 465     MET B    89                                                      
REMARK 465     GLY B    90                                                      
REMARK 465     LYS B    91                                                      
REMARK 465     TYR B   208                                                      
REMARK 465     ALA B   209                                                      
REMARK 465     THR B   210                                                      
REMARK 465     ASN B   211                                                      
REMARK 465     THR B   212                                                      
REMARK 465     GLN B   213                                                      
REMARK 465     ASP B   214                                                      
REMARK 465     GLU B   215                                                      
REMARK 465     GLU B   216                                                      
REMARK 465     GLU B   217                                                      
REMARK 465     THR B   218                                                      
REMARK 465     SER C    88                                                      
REMARK 465     MET C    89                                                      
REMARK 465     GLY C    90                                                      
REMARK 465     LYS C    91                                                      
REMARK 465     ASP C   207                                                      
REMARK 465     TYR C   208                                                      
REMARK 465     ALA C   209                                                      
REMARK 465     THR C   210                                                      
REMARK 465     ASN C   211                                                      
REMARK 465     THR C   212                                                      
REMARK 465     GLN C   213                                                      
REMARK 465     ASP C   214                                                      
REMARK 465     GLU C   215                                                      
REMARK 465     GLU C   216                                                      
REMARK 465     GLU C   217                                                      
REMARK 465     THR C   218                                                      
REMARK 465     SER D    88                                                      
REMARK 465     MET D    89                                                      
REMARK 465     GLY D    90                                                      
REMARK 465     LYS D    91                                                      
REMARK 465     MET D   206                                                      
REMARK 465     ASP D   207                                                      
REMARK 465     TYR D   208                                                      
REMARK 465     ALA D   209                                                      
REMARK 465     THR D   210                                                      
REMARK 465     ASN D   211                                                      
REMARK 465     THR D   212                                                      
REMARK 465     GLN D   213                                                      
REMARK 465     ASP D   214                                                      
REMARK 465     GLU D   215                                                      
REMARK 465     GLU D   216                                                      
REMARK 465     GLU D   217                                                      
REMARK 465     THR D   218                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   C7    DT E     4     O6    DG G     3     4555     1.66            
REMARK 500   O6    DG E     2     N3    DC G     5     4555     2.06            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500     DC E   1   P      DC E   1   OP3    -0.123                       
REMARK 500     DC F   1   P      DC F   1   OP3    -0.117                       
REMARK 500     DC G   1   P      DC G   1   OP3    -0.105                       
REMARK 500     DC H   1   P      DC H   1   OP3    -0.132                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    MET B 157   CG  -  SD  -  CE  ANGL. DEV. =  10.8 DEGREES          
REMARK 500    ARG B 191   CG  -  CD  -  NE  ANGL. DEV. =  18.3 DEGREES          
REMARK 500     DG E   2   O4' -  C4' -  C3' ANGL. DEV. =  -3.7 DEGREES          
REMARK 500     DG E   2   C5' -  C4' -  O4' ANGL. DEV. =   7.8 DEGREES          
REMARK 500     DG E   2   C1' -  O4' -  C4' ANGL. DEV. =  -7.8 DEGREES          
REMARK 500     DG E   2   O4' -  C1' -  N9  ANGL. DEV. =   2.5 DEGREES          
REMARK 500     DG G   2   O5' -  P   -  OP1 ANGL. DEV. =  -8.6 DEGREES          
REMARK 500     DC G   5   C5' -  C4' -  C3' ANGL. DEV. =   8.2 DEGREES          
REMARK 500     DC G   8   O5' -  P   -  OP2 ANGL. DEV. =  -9.4 DEGREES          
REMARK 500     DC G   8   C5' -  C4' -  C3' ANGL. DEV. =   7.7 DEGREES          
REMARK 500     DG H  13   C5' -  C4' -  C3' ANGL. DEV. = -12.8 DEGREES          
REMARK 500     DG H  14   C5' -  C4' -  C3' ANGL. DEV. = -10.9 DEGREES          
REMARK 500     DG H  14   C5' -  C4' -  O4' ANGL. DEV. =   6.7 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    GLU A 110      100.93   -170.81                                   
REMARK 500    SER A 166     -124.58     41.75                                   
REMARK 500    LYS A 193       48.40   -104.12                                   
REMARK 500    GLU B 110      100.76   -165.89                                   
REMARK 500    SER B 166     -125.49     42.47                                   
REMARK 500    LYS B 193       47.43   -102.54                                   
REMARK 500    GLU C 110      107.20   -166.05                                   
REMARK 500    SER C 166     -124.59     41.19                                   
REMARK 500    LYS C 193       47.41   -104.34                                   
REMARK 500    GLU D 110      102.08   -170.59                                   
REMARK 500    SER D 166     -125.68     42.39                                   
REMARK 500    LYS D 193       47.68   -103.19                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  6F5F A   90   218  UNP    Q9UGN5   PARP2_HUMAN     90    218             
DBREF  6F5F B   90   218  UNP    Q9UGN5   PARP2_HUMAN     90    218             
DBREF  6F5F C   90   218  UNP    Q9UGN5   PARP2_HUMAN     90    218             
DBREF  6F5F D   90   218  UNP    Q9UGN5   PARP2_HUMAN     90    218             
DBREF  6F5F E    1    15  PDB    6F5F     6F5F             1     15             
DBREF  6F5F F    1    15  PDB    6F5F     6F5F             1     15             
DBREF  6F5F G    1    15  PDB    6F5F     6F5F             1     15             
DBREF  6F5F H    1    15  PDB    6F5F     6F5F             1     15             
SEQADV 6F5F SER A   88  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 6F5F MET A   89  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 6F5F SER B   88  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 6F5F MET B   89  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 6F5F SER C   88  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 6F5F MET C   89  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 6F5F SER D   88  UNP  Q9UGN5              EXPRESSION TAG                 
SEQADV 6F5F MET D   89  UNP  Q9UGN5              EXPRESSION TAG                 
SEQRES   1 A  131  SER MET GLY LYS ALA PRO VAL ASP PRO GLU CYS THR ALA          
SEQRES   2 A  131  LYS VAL GLY LYS ALA HIS VAL TYR CYS GLU GLY ASN ASP          
SEQRES   3 A  131  VAL TYR ASP VAL MET LEU ASN GLN THR ASN LEU GLN PHE          
SEQRES   4 A  131  ASN ASN ASN LYS TYR TYR LEU ILE GLN LEU LEU GLU ASP          
SEQRES   5 A  131  ASP ALA GLN ARG ASN PHE SER VAL TRP MET ARG TRP GLY          
SEQRES   6 A  131  ARG VAL GLY LYS MET GLY GLN HIS SER LEU VAL ALA CYS          
SEQRES   7 A  131  SER GLY ASN LEU ASN LYS ALA LYS GLU ILE PHE GLN LYS          
SEQRES   8 A  131  LYS PHE LEU ASP LYS THR LYS ASN ASN TRP GLU ASP ARG          
SEQRES   9 A  131  GLU LYS PHE GLU LYS VAL PRO GLY LYS TYR ASP MET LEU          
SEQRES  10 A  131  GLN MET ASP TYR ALA THR ASN THR GLN ASP GLU GLU GLU          
SEQRES  11 A  131  THR                                                          
SEQRES   1 B  131  SER MET GLY LYS ALA PRO VAL ASP PRO GLU CYS THR ALA          
SEQRES   2 B  131  LYS VAL GLY LYS ALA HIS VAL TYR CYS GLU GLY ASN ASP          
SEQRES   3 B  131  VAL TYR ASP VAL MET LEU ASN GLN THR ASN LEU GLN PHE          
SEQRES   4 B  131  ASN ASN ASN LYS TYR TYR LEU ILE GLN LEU LEU GLU ASP          
SEQRES   5 B  131  ASP ALA GLN ARG ASN PHE SER VAL TRP MET ARG TRP GLY          
SEQRES   6 B  131  ARG VAL GLY LYS MET GLY GLN HIS SER LEU VAL ALA CYS          
SEQRES   7 B  131  SER GLY ASN LEU ASN LYS ALA LYS GLU ILE PHE GLN LYS          
SEQRES   8 B  131  LYS PHE LEU ASP LYS THR LYS ASN ASN TRP GLU ASP ARG          
SEQRES   9 B  131  GLU LYS PHE GLU LYS VAL PRO GLY LYS TYR ASP MET LEU          
SEQRES  10 B  131  GLN MET ASP TYR ALA THR ASN THR GLN ASP GLU GLU GLU          
SEQRES  11 B  131  THR                                                          
SEQRES   1 C  131  SER MET GLY LYS ALA PRO VAL ASP PRO GLU CYS THR ALA          
SEQRES   2 C  131  LYS VAL GLY LYS ALA HIS VAL TYR CYS GLU GLY ASN ASP          
SEQRES   3 C  131  VAL TYR ASP VAL MET LEU ASN GLN THR ASN LEU GLN PHE          
SEQRES   4 C  131  ASN ASN ASN LYS TYR TYR LEU ILE GLN LEU LEU GLU ASP          
SEQRES   5 C  131  ASP ALA GLN ARG ASN PHE SER VAL TRP MET ARG TRP GLY          
SEQRES   6 C  131  ARG VAL GLY LYS MET GLY GLN HIS SER LEU VAL ALA CYS          
SEQRES   7 C  131  SER GLY ASN LEU ASN LYS ALA LYS GLU ILE PHE GLN LYS          
SEQRES   8 C  131  LYS PHE LEU ASP LYS THR LYS ASN ASN TRP GLU ASP ARG          
SEQRES   9 C  131  GLU LYS PHE GLU LYS VAL PRO GLY LYS TYR ASP MET LEU          
SEQRES  10 C  131  GLN MET ASP TYR ALA THR ASN THR GLN ASP GLU GLU GLU          
SEQRES  11 C  131  THR                                                          
SEQRES   1 D  131  SER MET GLY LYS ALA PRO VAL ASP PRO GLU CYS THR ALA          
SEQRES   2 D  131  LYS VAL GLY LYS ALA HIS VAL TYR CYS GLU GLY ASN ASP          
SEQRES   3 D  131  VAL TYR ASP VAL MET LEU ASN GLN THR ASN LEU GLN PHE          
SEQRES   4 D  131  ASN ASN ASN LYS TYR TYR LEU ILE GLN LEU LEU GLU ASP          
SEQRES   5 D  131  ASP ALA GLN ARG ASN PHE SER VAL TRP MET ARG TRP GLY          
SEQRES   6 D  131  ARG VAL GLY LYS MET GLY GLN HIS SER LEU VAL ALA CYS          
SEQRES   7 D  131  SER GLY ASN LEU ASN LYS ALA LYS GLU ILE PHE GLN LYS          
SEQRES   8 D  131  LYS PHE LEU ASP LYS THR LYS ASN ASN TRP GLU ASP ARG          
SEQRES   9 D  131  GLU LYS PHE GLU LYS VAL PRO GLY LYS TYR ASP MET LEU          
SEQRES  10 D  131  GLN MET ASP TYR ALA THR ASN THR GLN ASP GLU GLU GLU          
SEQRES  11 D  131  THR                                                          
SEQRES   1 E   15   DC  DG  DG  DT  DC  DG  DC  DC  DT  DA  DT  DA  DG          
SEQRES   2 E   15   DG  DC                                                      
SEQRES   1 F   15   DC  DG  DG  DT  DC  DG  DC  DC  DT  DA  DT  DA  DG          
SEQRES   2 F   15   DG  DC                                                      
SEQRES   1 G   15   DC  DG  DG  DT  DC  DG  DC  DC  DT  DA  DT  DA  DG          
SEQRES   2 G   15   DG  DC                                                      
SEQRES   1 H   15   DC  DG  DG  DT  DC  DG  DC  DC  DT  DA  DT  DA  DG          
SEQRES   2 H   15   DG  DC                                                      
HELIX    1 AA1 ASN A  168  LYS A  185  1                                  18    
HELIX    2 AA2 ASP A  190  PHE A  194  5                                   5    
HELIX    3 AA3 ASN B  168  LYS B  185  1                                  18    
HELIX    4 AA4 ASP B  190  PHE B  194  5                                   5    
HELIX    5 AA5 ASN C  168  LYS C  185  1                                  18    
HELIX    6 AA6 ASP C  190  PHE C  194  5                                   5    
HELIX    7 AA7 ASN D  168  LYS D  185  1                                  18    
HELIX    8 AA8 ASP D  190  PHE D  194  5                                   5    
SHEET    1 AA1 4 ALA A 105  VAL A 107  0                                        
SHEET    2 AA1 4 ASN A 128  ASP A 139 -1  O  GLU A 138   N  HIS A 106           
SHEET    3 AA1 4 PHE A 145  ARG A 153 -1  O  SER A 146   N  LEU A 137           
SHEET    4 AA1 4 GLN A 159  SER A 166 -1  O  SER A 166   N  PHE A 145           
SHEET    1 AA2 4 ALA A 105  VAL A 107  0                                        
SHEET    2 AA2 4 ASN A 128  ASP A 139 -1  O  GLU A 138   N  HIS A 106           
SHEET    3 AA2 4 ASP A 116  ASN A 123 -1  N  GLN A 121   O  LYS A 130           
SHEET    4 AA2 4 ASP A 202  LEU A 204 -1  O  ASP A 202   N  ASN A 120           
SHEET    1 AA3 2 CYS A 109  GLU A 110  0                                        
SHEET    2 AA3 2 ASP A 113  VAL A 114 -1  O  ASP A 113   N  GLU A 110           
SHEET    1 AA4 4 ALA B 105  VAL B 107  0                                        
SHEET    2 AA4 4 ASN B 128  ASP B 139 -1  O  GLU B 138   N  HIS B 106           
SHEET    3 AA4 4 PHE B 145  ARG B 153 -1  O  SER B 146   N  LEU B 137           
SHEET    4 AA4 4 GLN B 159  SER B 166 -1  O  SER B 166   N  PHE B 145           
SHEET    1 AA5 4 ALA B 105  VAL B 107  0                                        
SHEET    2 AA5 4 ASN B 128  ASP B 139 -1  O  GLU B 138   N  HIS B 106           
SHEET    3 AA5 4 ASP B 116  ASN B 123 -1  N  GLN B 121   O  LYS B 130           
SHEET    4 AA5 4 ASP B 202  MET B 203 -1  O  ASP B 202   N  ASN B 120           
SHEET    1 AA6 2 CYS B 109  GLU B 110  0                                        
SHEET    2 AA6 2 ASP B 113  VAL B 114 -1  O  ASP B 113   N  GLU B 110           
SHEET    1 AA7 4 ALA C 105  VAL C 107  0                                        
SHEET    2 AA7 4 ASN C 128  ASP C 139 -1  O  GLU C 138   N  HIS C 106           
SHEET    3 AA7 4 PHE C 145  ARG C 153 -1  O  SER C 146   N  LEU C 137           
SHEET    4 AA7 4 GLN C 159  SER C 166 -1  O  SER C 166   N  PHE C 145           
SHEET    1 AA8 4 ALA C 105  VAL C 107  0                                        
SHEET    2 AA8 4 ASN C 128  ASP C 139 -1  O  GLU C 138   N  HIS C 106           
SHEET    3 AA8 4 ASP C 116  ASN C 123 -1  N  ASN C 123   O  ASN C 128           
SHEET    4 AA8 4 ASP C 202  LEU C 204 -1  O  ASP C 202   N  ASN C 120           
SHEET    1 AA9 2 CYS C 109  GLU C 110  0                                        
SHEET    2 AA9 2 ASP C 113  VAL C 114 -1  O  ASP C 113   N  GLU C 110           
SHEET    1 AB1 4 ALA D 105  VAL D 107  0                                        
SHEET    2 AB1 4 ASN D 128  ASP D 139 -1  O  GLU D 138   N  HIS D 106           
SHEET    3 AB1 4 PHE D 145  ARG D 153 -1  O  SER D 146   N  LEU D 137           
SHEET    4 AB1 4 GLN D 159  SER D 166 -1  O  SER D 166   N  PHE D 145           
SHEET    1 AB2 4 ALA D 105  VAL D 107  0                                        
SHEET    2 AB2 4 ASN D 128  ASP D 139 -1  O  GLU D 138   N  HIS D 106           
SHEET    3 AB2 4 ASP D 116  ASN D 123 -1  N  GLN D 121   O  LYS D 130           
SHEET    4 AB2 4 ASP D 202  LEU D 204 -1  O  ASP D 202   N  ASN D 120           
SHEET    1 AB3 2 CYS D 109  GLU D 110  0                                        
SHEET    2 AB3 2 ASP D 113  VAL D 114 -1  O  ASP D 113   N  GLU D 110           
CRYST1   68.150   87.150  185.270  90.00  90.00  90.00 P 21 21 21   16          
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      0.014674  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011474  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005398        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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