HEADER TRANSFERASE/TRANSFERASE INHIBITOR 23-JAN-19 6NRJ
TITLE CRYSTAL STRUCTURE OF HUMAN PARP-1 ART DOMAIN BOUND TO INHIBITOR UTT93
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY [ADP-RIBOSE] POLYMERASE 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ADP-RIBOSYLTRANSFERASE (ART) DOMAIN;
COMPND 5 SYNONYM: PARP-1,ADP-RIBOSYLTRANSFERASE DIPHTHERIA TOXIN-LIKE 1,ARTD1,
COMPND 6 NAD(+) ADP-RIBOSYLTRANSFERASE 1,ADPRT 1,POLY[ADP-RIBOSE] SYNTHASE 1;
COMPND 7 EC: 2.4.2.30,2.4.2.-;
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: PARP1, ADPRT, PPOL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA2(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28
KEYWDS PARP-1, POLY(ADP-RIBOSE) POLYMERASE, PARP INHIBITOR, PARP1, ARTD1,
KEYWDS 2 TRANSFERASE, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.F.LANGELIER,J.M.PASCAL
REVDAT 3 11-OCT-23 6NRJ 1 REMARK
REVDAT 2 08-JAN-20 6NRJ 1 REMARK
REVDAT 1 14-AUG-19 6NRJ 0
JRNL AUTH U.K.VELAGAPUDI,M.F.LANGELIER,C.DELGADO-MARTIN,M.E.DIOLAITI,
JRNL AUTH 2 S.BAKKER,A.ASHWORTH,B.A.PATEL,X.SHAO,J.M.PASCAL,T.T.TALELE
JRNL TITL DESIGN AND SYNTHESIS OF POLY(ADP-RIBOSE) POLYMERASE
JRNL TITL 2 INHIBITORS: IMPACT OF ADENOSINE POCKET-BINDING MOTIF
JRNL TITL 3 APPENDAGE TO THE 3-OXO-2,3-DIHYDROBENZOFURAN-7-CARBOXAMIDE
JRNL TITL 4 ON POTENCY AND SELECTIVITY.
JRNL REF J.MED.CHEM. V. 62 5330 2019
JRNL REFN ISSN 0022-2623
JRNL PMID 31042381
JRNL DOI 10.1021/ACS.JMEDCHEM.8B01709
REMARK 2
REMARK 2 RESOLUTION. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.98
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 35588
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) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.191
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.300
REMARK 3 FREE R VALUE TEST SET COUNT : 1975
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1895
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 67
REMARK 3 SOLVENT ATOMS : 127
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.03
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.41000
REMARK 3 B22 (A**2) : 0.41000
REMARK 3 B33 (A**2) : -0.83000
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): 0.079
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.078
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.051
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.955
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 6NRJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JAN-19.
REMARK 100 THE DEPOSITION ID IS D_1000239292.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-FEB-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CLSI
REMARK 200 BEAMLINE : 08ID-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : ACCEL/BRUKER DOUBLE CRYSTAL
REMARK 200 MONOCHROMATOR (DCM), SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.6.2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37738
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 47.980
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 27.80
REMARK 200 R MERGE (I) : 0.07700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.7000
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) : 1.68
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 26.80
REMARK 200 R MERGE FOR SHELL (I) : 1.73800
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: PDBID 6BHV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: ~20% PEG 3350, 0.2 M AMMONIUM SULFATE
REMARK 280 OR SODIUM CITRATE, 100 MM HEPES PH 7.5, EVAPORATION, TEMPERATURE
REMARK 280 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 3555 -Y,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X,Z+3/4
REMARK 290 5555 -X+1/2,Y,-Z+3/4
REMARK 290 6555 X,-Y+1/2,-Z+1/4
REMARK 290 7555 Y+1/2,X+1/2,-Z+1/2
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 X+1/2,Y+1/2,Z+1/2
REMARK 290 10555 -X,-Y,Z
REMARK 290 11555 -Y+1/2,X,Z+3/4
REMARK 290 12555 Y,-X+1/2,Z+1/4
REMARK 290 13555 -X,Y+1/2,-Z+1/4
REMARK 290 14555 X+1/2,-Y,-Z+3/4
REMARK 290 15555 Y,X,-Z
REMARK 290 16555 -Y+1/2,-X+1/2,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 47.23250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 47.23250
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.81350
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 47.23250
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 34.40675
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 47.23250
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 103.22025
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 47.23250
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 103.22025
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 47.23250
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 34.40675
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 47.23250
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 47.23250
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 68.81350
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 47.23250
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 47.23250
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 68.81350
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 47.23250
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 103.22025
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 47.23250
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 34.40675
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 47.23250
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 34.40675
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 47.23250
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 103.22025
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 47.23250
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 47.23250
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 68.81350
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 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 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 742
REMARK 465 GLY A 743
REMARK 465 SER A 744
REMARK 465 SER A 745
REMARK 465 HIS A 746
REMARK 465 HIS A 747
REMARK 465 HIS A 748
REMARK 465 HIS A 749
REMARK 465 HIS A 750
REMARK 465 HIS A 751
REMARK 465 SER A 752
REMARK 465 SER A 753
REMARK 465 GLY A 754
REMARK 465 LEU A 755
REMARK 465 VAL A 756
REMARK 465 PRO A 757
REMARK 465 ARG A 758
REMARK 465 GLY A 759
REMARK 465 SER A 760
REMARK 465 HIS A 761
REMARK 465 MET A 762
REMARK 465 THR A 763
REMARK 465 SER A 781
REMARK 465 GLY A 782
REMARK 465 SER A 783
REMARK 465 GLY A 784
REMARK 465 SER A 785
REMARK 465 GLY A 786
REMARK 465 GLY A 787
REMARK 465 THR A 1011
REMARK 465 SER A 1012
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 A 1322 O HOH A 1324 1.69
REMARK 500 O HOH A 1319 O HOH A 1321 1.70
REMARK 500 O HOH A 1224 O HOH A 1317 1.73
REMARK 500 O HOH A 1317 O HOH A 1323 1.77
REMARK 500 O HOH A 1275 O HOH A 1314 1.97
REMARK 500 O HOH A 1202 O HOH A 1316 2.01
REMARK 500 O HOH A 1311 O HOH A 1316 2.15
REMARK 500 O HOH A 1258 O HOH A 1323 2.16
REMARK 500 O HOH A 1202 O HOH A 1274 2.19
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 826 64.58 -100.17
REMARK 500 SER A 936 117.85 -162.75
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 KYJ A 1101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1104
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1105
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1106
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 1107
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 1108
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6NRF RELATED DB: PDB
REMARK 900 RELATED ID: 6NRG RELATED DB: PDB
REMARK 900 RELATED ID: 6NRH RELATED DB: PDB
REMARK 900 RELATED ID: 6NRI RELATED DB: PDB
DBREF 6NRJ A 788 1012 UNP P09874 PARP1_HUMAN 788 1012
SEQADV 6NRJ MET A 742 UNP P09874 INITIATING METHIONINE
SEQADV 6NRJ GLY A 743 UNP P09874 EXPRESSION TAG
SEQADV 6NRJ SER A 744 UNP P09874 EXPRESSION TAG
SEQADV 6NRJ SER A 745 UNP P09874 EXPRESSION TAG
SEQADV 6NRJ HIS A 746 UNP P09874 EXPRESSION TAG
SEQADV 6NRJ HIS A 747 UNP P09874 EXPRESSION TAG
SEQADV 6NRJ HIS A 748 UNP P09874 EXPRESSION TAG
SEQADV 6NRJ HIS A 749 UNP P09874 EXPRESSION TAG
SEQADV 6NRJ HIS A 750 UNP P09874 EXPRESSION TAG
SEQADV 6NRJ HIS A 751 UNP P09874 EXPRESSION TAG
SEQADV 6NRJ SER A 752 UNP P09874 EXPRESSION TAG
SEQADV 6NRJ SER A 753 UNP P09874 EXPRESSION TAG
SEQADV 6NRJ GLY A 754 UNP P09874 EXPRESSION TAG
SEQADV 6NRJ LEU A 755 UNP P09874 EXPRESSION TAG
SEQADV 6NRJ VAL A 756 UNP P09874 EXPRESSION TAG
SEQADV 6NRJ PRO A 757 UNP P09874 EXPRESSION TAG
SEQADV 6NRJ ARG A 758 UNP P09874 EXPRESSION TAG
SEQADV 6NRJ GLY A 759 UNP P09874 EXPRESSION TAG
SEQADV 6NRJ SER A 760 UNP P09874 EXPRESSION TAG
SEQADV 6NRJ HIS A 761 UNP P09874 EXPRESSION TAG
SEQADV 6NRJ MET A 762 UNP P09874 EXPRESSION TAG
SEQADV 6NRJ THR A 763 UNP P09874 EXPRESSION TAG
SEQADV 6NRJ LYS A 764 UNP P09874 EXPRESSION TAG
SEQADV 6NRJ SER A 765 UNP P09874 EXPRESSION TAG
SEQADV 6NRJ LYS A 766 UNP P09874 EXPRESSION TAG
SEQADV 6NRJ LEU A 767 UNP P09874 EXPRESSION TAG
SEQADV 6NRJ PRO A 768 UNP P09874 EXPRESSION TAG
SEQADV 6NRJ LYS A 769 UNP P09874 EXPRESSION TAG
SEQADV 6NRJ PRO A 770 UNP P09874 EXPRESSION TAG
SEQADV 6NRJ VAL A 771 UNP P09874 EXPRESSION TAG
SEQADV 6NRJ GLN A 772 UNP P09874 EXPRESSION TAG
SEQADV 6NRJ ASP A 773 UNP P09874 EXPRESSION TAG
SEQADV 6NRJ LEU A 774 UNP P09874 EXPRESSION TAG
SEQADV 6NRJ ILE A 775 UNP P09874 EXPRESSION TAG
SEQADV 6NRJ LYS A 776 UNP P09874 EXPRESSION TAG
SEQADV 6NRJ MET A 777 UNP P09874 EXPRESSION TAG
SEQADV 6NRJ ILE A 778 UNP P09874 EXPRESSION TAG
SEQADV 6NRJ PHE A 779 UNP P09874 EXPRESSION TAG
SEQADV 6NRJ GLY A 780 UNP P09874 EXPRESSION TAG
SEQADV 6NRJ SER A 781 UNP P09874 EXPRESSION TAG
SEQADV 6NRJ GLY A 782 UNP P09874 EXPRESSION TAG
SEQADV 6NRJ SER A 783 UNP P09874 EXPRESSION TAG
SEQADV 6NRJ GLY A 784 UNP P09874 EXPRESSION TAG
SEQADV 6NRJ SER A 785 UNP P09874 EXPRESSION TAG
SEQADV 6NRJ GLY A 786 UNP P09874 EXPRESSION TAG
SEQADV 6NRJ GLY A 787 UNP P09874 EXPRESSION TAG
SEQRES 1 A 271 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 271 LEU VAL PRO ARG GLY SER HIS MET THR LYS SER LYS LEU
SEQRES 3 A 271 PRO LYS PRO VAL GLN ASP LEU ILE LYS MET ILE PHE GLY
SEQRES 4 A 271 SER GLY SER GLY SER GLY GLY ASP PRO ILE ASP VAL ASN
SEQRES 5 A 271 TYR GLU LYS LEU LYS THR ASP ILE LYS VAL VAL ASP ARG
SEQRES 6 A 271 ASP SER GLU GLU ALA GLU ILE ILE ARG LYS TYR VAL LYS
SEQRES 7 A 271 ASN THR HIS ALA THR THR HIS ASN ALA TYR ASP LEU GLU
SEQRES 8 A 271 VAL ILE ASP ILE PHE LYS ILE GLU ARG GLU GLY GLU CYS
SEQRES 9 A 271 GLN ARG TYR LYS PRO PHE LYS GLN LEU HIS ASN ARG ARG
SEQRES 10 A 271 LEU LEU TRP HIS GLY SER ARG THR THR ASN PHE ALA GLY
SEQRES 11 A 271 ILE LEU SER GLN GLY LEU ARG ILE ALA PRO PRO GLU ALA
SEQRES 12 A 271 PRO VAL THR GLY TYR MET PHE GLY LYS GLY ILE TYR PHE
SEQRES 13 A 271 ALA ASP MET VAL SER LYS SER ALA ASN TYR CYS HIS THR
SEQRES 14 A 271 SER GLN GLY ASP PRO ILE GLY LEU ILE LEU LEU GLY GLU
SEQRES 15 A 271 VAL ALA LEU GLY ASN MET TYR GLU LEU LYS HIS ALA SER
SEQRES 16 A 271 HIS ILE SER LYS LEU PRO LYS GLY LYS HIS SER VAL LYS
SEQRES 17 A 271 GLY LEU GLY LYS THR THR PRO ASP PRO SER ALA ASN ILE
SEQRES 18 A 271 SER LEU ASP GLY VAL ASP VAL PRO LEU GLY THR GLY ILE
SEQRES 19 A 271 SER SER GLY VAL ASN ASP THR SER LEU LEU TYR ASN GLU
SEQRES 20 A 271 TYR ILE VAL TYR ASP ILE ALA GLN VAL ASN LEU LYS TYR
SEQRES 21 A 271 LEU LEU LYS LEU LYS PHE ASN PHE LYS THR SER
HET KYJ A1101 34
HET SO4 A1102 5
HET SO4 A1103 5
HET SO4 A1104 5
HET SO4 A1105 5
HET SO4 A1106 5
HET DMS A1107 4
HET DMS A1108 4
HETNAM KYJ (2Z)-2-[(4-{[2-(1H-BENZIMIDAZOL-2-YL)
HETNAM 2 KYJ ETHYL]CARBAMOYL}PHENYL)METHYLIDENE]-3-OXO-2,3-DIHYDRO-
HETNAM 3 KYJ 1-BENZOFURAN-7-CARBOXAMIDE
HETNAM SO4 SULFATE ION
HETNAM DMS DIMETHYL SULFOXIDE
FORMUL 2 KYJ C26 H20 N4 O4
FORMUL 3 SO4 5(O4 S 2-)
FORMUL 8 DMS 2(C2 H6 O S)
FORMUL 10 HOH *127(H2 O)
HELIX 1 AA1 PRO A 768 GLY A 780 1 13
HELIX 2 AA2 PRO A 789 LEU A 797 1 9
HELIX 3 AA3 SER A 808 THR A 821 1 14
HELIX 4 AA4 GLY A 843 LYS A 849 1 7
HELIX 5 AA5 PRO A 850 LYS A 852 5 3
HELIX 6 AA6 ARG A 865 THR A 867 5 3
HELIX 7 AA7 ASN A 868 GLY A 876 1 9
HELIX 8 AA8 MET A 900 ASN A 906 1 7
HELIX 9 AA9 TYR A 907 HIS A 909 5 3
HELIX 10 AB1 PRO A 958 ASN A 961 5 4
HELIX 11 AB2 ASP A 993 ALA A 995 5 3
SHEET 1 AA1 5 THR A 799 VAL A 803 0
SHEET 2 AA1 5 TYR A 829 ARG A 841 -1 O LYS A 838 N LYS A 802
SHEET 3 AA1 5 VAL A 997 PHE A1009 -1 O LYS A1006 N GLU A 832
SHEET 4 AA1 5 ILE A 916 ALA A 925 -1 N ILE A 919 O LEU A1003
SHEET 5 AA1 5 ARG A 857 GLY A 863 -1 N HIS A 862 O LEU A 920
SHEET 1 AA2 4 ILE A 895 PHE A 897 0
SHEET 2 AA2 4 GLU A 988 VAL A 991 -1 O VAL A 991 N ILE A 895
SHEET 3 AA2 4 SER A 947 GLY A 950 -1 N VAL A 948 O ILE A 990
SHEET 4 AA2 4 MET A 929 LEU A 932 1 N TYR A 930 O SER A 947
SHEET 1 AA3 3 GLY A 974 SER A 976 0
SHEET 2 AA3 3 GLY A 952 PRO A 956 -1 N THR A 955 O ILE A 975
SHEET 3 AA3 3 LEU A 984 TYR A 986 1 O LEU A 985 N THR A 954
SHEET 1 AA4 2 ILE A 962 LEU A 964 0
SHEET 2 AA4 2 VAL A 967 VAL A 969 -1 O VAL A 969 N ILE A 962
SSBOND 1 CYS A 845 CYS A 845 1555 7545 2.05
SITE 1 AC1 16 HIS A 862 GLY A 863 ARG A 878 ALA A 880
SITE 2 AC1 16 PRO A 881 GLY A 888 TYR A 889 TYR A 896
SITE 3 AC1 16 PHE A 897 SER A 904 TYR A 907 DMS A1107
SITE 4 AC1 16 DMS A1108 HOH A1208 HOH A1218 HOH A1222
SITE 1 AC2 7 LYS A 764 LYS A 766 LYS A 903 LEU A 984
SITE 2 AC2 7 LEU A 985 TYR A 986 HOH A1233
SITE 1 AC3 3 ASN A 906 TYR A 907 HIS A 909
SITE 1 AC4 6 ARG A 806 LYS A 953 ASN A 980 ASP A 981
SITE 2 AC4 6 THR A 982 HOH A1221
SITE 1 AC5 5 GLU A 840 LYS A 849 ASN A 998 LYS A1000
SITE 2 AC5 5 HOH A1216
SITE 1 AC6 7 ARG A 858 MET A 929 LYS A 949 HOH A1205
SITE 2 AC6 7 HOH A1258 HOH A1274 HOH A1307
SITE 1 AC7 8 HIS A 862 ARG A 878 TYR A 889 GLY A 894
SITE 2 AC7 8 ILE A 895 TYR A 896 KYJ A1101 DMS A1108
SITE 1 AC8 4 KYJ A1101 DMS A1107 HOH A1234 HOH A1278
CRYST1 94.465 94.465 137.627 90.00 90.00 90.00 I 41 2 2 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 0.010586 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010586 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007266 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
