HEADER TRANSFERASE/TRANSFERASE INHIBITOR 22-AUG-14 4R5W
TITLE HUMAN ARTD1 (PARP1) - CATALYTIC DOMAIN IN COMPLEX WITH INHIBITOR
TITLE 2 XAV939
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY [ADP-RIBOSE] POLYMERASE 1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN (UNP RESIDUES 662-1011);
COMPND 5 SYNONYM: PARP-1, ADP-RIBOSYLTRANSFERASE DIPHTHERIA TOXIN-LIKE 1,
COMPND 6 ARTD1, NAD(+) ADP-RIBOSYLTRANSFERASE 1, ADPRT 1, POLY[ADP-RIBOSE]
COMPND 7 SYNTHASE 1;
COMPND 8 EC: 2.4.2.30;
COMPND 9 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: ADPRT, PARP1, PPOL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA2(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNIC-CH
KEYWDS ADP-RIBOSYLATION, DNA REPAIR, ADP-RIBOSYL TRANSFERASE, TRANSFERASE-
KEYWDS 2 TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR T.KARLBERG,A.G.THORSELL,H.SCHULER
REVDAT 5 20-SEP-23 4R5W 1 REMARK
REVDAT 4 24-AUG-22 4R5W 1 JRNL REMARK SEQADV
REVDAT 3 22-NOV-17 4R5W 1 REMARK
REVDAT 2 18-JAN-17 4R5W 1 JRNL
REVDAT 1 02-SEP-15 4R5W 0
JRNL AUTH A.G.THORSELL,T.EKBLAD,T.KARLBERG,M.LOW,A.F.PINTO,
JRNL AUTH 2 L.TRESAUGUES,M.MOCHE,M.S.COHEN,H.SCHULER
JRNL TITL STRUCTURAL BASIS FOR POTENCY AND PROMISCUITY IN
JRNL TITL 2 POLY(ADP-RIBOSE) POLYMERASE (PARP) AND TANKYRASE INHIBITORS.
JRNL REF J.MED.CHEM. V. 60 1262 2017
JRNL REFN ISSN 0022-2623
JRNL PMID 28001384
JRNL DOI 10.1021/ACS.JMEDCHEM.6B00990
REMARK 2
REMARK 2 RESOLUTION. 2.84 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.5
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.84
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.46
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 20249
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) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1013
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.84
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.98
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.22
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2813
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2351
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2672
REMARK 3 BIN R VALUE (WORKING SET) : 0.2345
REMARK 3 BIN FREE R VALUE : 0.2466
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.01
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 141
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5556
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 77
REMARK 3 SOLVENT ATOMS : 11
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 71.39
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.28
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.02300
REMARK 3 B22 (A**2) : -8.14950
REMARK 3 B33 (A**2) : 8.12650
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.33000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.371
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.919
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.855
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 5738 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 7750 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2684 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 154 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 806 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 5738 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 736 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 6293 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.17
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.92
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 3.40
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|661 - A|1013 }
REMARK 3 ORIGIN FOR THE GROUP (A): -18.7029 -8.9618 -20.5941
REMARK 3 T TENSOR
REMARK 3 T11: -0.1495 T22: -0.0806
REMARK 3 T33: -0.0706 T12: -0.0248
REMARK 3 T13: -0.0042 T23: -0.0249
REMARK 3 L TENSOR
REMARK 3 L11: 1.2957 L22: 1.8794
REMARK 3 L33: 1.5505 L12: 0.0418
REMARK 3 L13: -0.0158 L23: -0.0089
REMARK 3 S TENSOR
REMARK 3 S11: -0.0035 S12: -0.0532 S13: -0.0273
REMARK 3 S21: 0.1638 S22: -0.0013 S23: 0.0992
REMARK 3 S31: -0.0135 S32: -0.2250 S33: 0.0048
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|661 - B|1017 }
REMARK 3 ORIGIN FOR THE GROUP (A): 17.6242 -3.7586 -24.1646
REMARK 3 T TENSOR
REMARK 3 T11: -0.0872 T22: -0.0659
REMARK 3 T33: -0.0965 T12: -0.0267
REMARK 3 T13: 0.0310 T23: -0.0179
REMARK 3 L TENSOR
REMARK 3 L11: 0.8557 L22: 1.4923
REMARK 3 L33: 1.8068 L12: 0.3139
REMARK 3 L13: -0.0922 L23: -0.7642
REMARK 3 S TENSOR
REMARK 3 S11: 0.0655 S12: -0.1099 S13: 0.0335
REMARK 3 S21: 0.1324 S22: -0.0031 S23: -0.0550
REMARK 3 S31: -0.2274 S32: 0.2597 S33: -0.0624
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4R5W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-AUG-14.
REMARK 100 THE DEPOSITION ID IS D_1000086938.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-JUN-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91841
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL (SI-111)
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-225
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20249
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.840
REMARK 200 RESOLUTION RANGE LOW (A) : 48.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.16800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.84
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.01
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.92100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 4GV7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 21% PEG-3350, 0.17M AMMONIUM SULFATE,
REMARK 280 0.09M BIS-TRIS, 1MM XAV939, PH 5.5, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 33.83100
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 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 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 ASP A 783
REMARK 465 ASP A 784
REMARK 465 HIS A 1014
REMARK 465 HIS A 1015
REMARK 465 HIS A 1016
REMARK 465 HIS A 1017
REMARK 465 HIS A 1018
REMARK 465 ASP B 783
REMARK 465 ASP B 784
REMARK 465 HIS B 1018
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 ASN A 980 C - N - CA ANGL. DEV. = 16.1 DEGREES
REMARK 500 ASN B 980 C - N - CA ANGL. DEV. = 16.0 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 SER A 939 -60.83 -96.36
REMARK 500 ASN A 980 100.56 76.50
REMARK 500 ASP A 981 78.92 59.92
REMARK 500 ASN B 980 100.68 76.03
REMARK 500 ASP B 981 78.72 59.49
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 SO4 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 XAV A 1106
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XAV B 1103
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4UND RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH BMN673
REMARK 900 RELATED ID: 4UXB RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH PJ34
REMARK 900 RELATED ID: 4R6E RELATED DB: PDB
DBREF 4R5W A 662 1011 UNP P09874 PARP1_HUMAN 662 1011
DBREF 4R5W B 662 1011 UNP P09874 PARP1_HUMAN 662 1011
SEQADV 4R5W MET A 661 UNP P09874 INITIATING METHIONINE
SEQADV 4R5W ALA A 762 UNP P09874 VAL 762 VARIANT
SEQADV 4R5W ALA A 1012 UNP P09874 EXPRESSION TAG
SEQADV 4R5W HIS A 1013 UNP P09874 EXPRESSION TAG
SEQADV 4R5W HIS A 1014 UNP P09874 EXPRESSION TAG
SEQADV 4R5W HIS A 1015 UNP P09874 EXPRESSION TAG
SEQADV 4R5W HIS A 1016 UNP P09874 EXPRESSION TAG
SEQADV 4R5W HIS A 1017 UNP P09874 EXPRESSION TAG
SEQADV 4R5W HIS A 1018 UNP P09874 EXPRESSION TAG
SEQADV 4R5W MET B 661 UNP P09874 INITIATING METHIONINE
SEQADV 4R5W ALA B 762 UNP P09874 VAL 762 VARIANT
SEQADV 4R5W ALA B 1012 UNP P09874 EXPRESSION TAG
SEQADV 4R5W HIS B 1013 UNP P09874 EXPRESSION TAG
SEQADV 4R5W HIS B 1014 UNP P09874 EXPRESSION TAG
SEQADV 4R5W HIS B 1015 UNP P09874 EXPRESSION TAG
SEQADV 4R5W HIS B 1016 UNP P09874 EXPRESSION TAG
SEQADV 4R5W HIS B 1017 UNP P09874 EXPRESSION TAG
SEQADV 4R5W HIS B 1018 UNP P09874 EXPRESSION TAG
SEQRES 1 A 358 MET LYS SER LYS LEU PRO LYS PRO VAL GLN ASP LEU ILE
SEQRES 2 A 358 LYS MET ILE PHE ASP VAL GLU SER MET LYS LYS ALA MET
SEQRES 3 A 358 VAL GLU TYR GLU ILE ASP LEU GLN LYS MET PRO LEU GLY
SEQRES 4 A 358 LYS LEU SER LYS ARG GLN ILE GLN ALA ALA TYR SER ILE
SEQRES 5 A 358 LEU SER GLU VAL GLN GLN ALA VAL SER GLN GLY SER SER
SEQRES 6 A 358 ASP SER GLN ILE LEU ASP LEU SER ASN ARG PHE TYR THR
SEQRES 7 A 358 LEU ILE PRO HIS ASP PHE GLY MET LYS LYS PRO PRO LEU
SEQRES 8 A 358 LEU ASN ASN ALA ASP SER VAL GLN ALA LYS ALA GLU MET
SEQRES 9 A 358 LEU ASP ASN LEU LEU ASP ILE GLU VAL ALA TYR SER LEU
SEQRES 10 A 358 LEU ARG GLY GLY SER ASP ASP SER SER LYS ASP PRO ILE
SEQRES 11 A 358 ASP VAL ASN TYR GLU LYS LEU LYS THR ASP ILE LYS VAL
SEQRES 12 A 358 VAL ASP ARG ASP SER GLU GLU ALA GLU ILE ILE ARG LYS
SEQRES 13 A 358 TYR VAL LYS ASN THR HIS ALA THR THR HIS ASN ALA TYR
SEQRES 14 A 358 ASP LEU GLU VAL ILE ASP ILE PHE LYS ILE GLU ARG GLU
SEQRES 15 A 358 GLY GLU CYS GLN ARG TYR LYS PRO PHE LYS GLN LEU HIS
SEQRES 16 A 358 ASN ARG ARG LEU LEU TRP HIS GLY SER ARG THR THR ASN
SEQRES 17 A 358 PHE ALA GLY ILE LEU SER GLN GLY LEU ARG ILE ALA PRO
SEQRES 18 A 358 PRO GLU ALA PRO VAL THR GLY TYR MET PHE GLY LYS GLY
SEQRES 19 A 358 ILE TYR PHE ALA ASP MET VAL SER LYS SER ALA ASN TYR
SEQRES 20 A 358 CYS HIS THR SER GLN GLY ASP PRO ILE GLY LEU ILE LEU
SEQRES 21 A 358 LEU GLY GLU VAL ALA LEU GLY ASN MET TYR GLU LEU LYS
SEQRES 22 A 358 HIS ALA SER HIS ILE SER LYS LEU PRO LYS GLY LYS HIS
SEQRES 23 A 358 SER VAL LYS GLY LEU GLY LYS THR THR PRO ASP PRO SER
SEQRES 24 A 358 ALA ASN ILE SER LEU ASP GLY VAL ASP VAL PRO LEU GLY
SEQRES 25 A 358 THR GLY ILE SER SER GLY VAL ASN ASP THR SER LEU LEU
SEQRES 26 A 358 TYR ASN GLU TYR ILE VAL TYR ASP ILE ALA GLN VAL ASN
SEQRES 27 A 358 LEU LYS TYR LEU LEU LYS LEU LYS PHE ASN PHE LYS THR
SEQRES 28 A 358 ALA HIS HIS HIS HIS HIS HIS
SEQRES 1 B 358 MET LYS SER LYS LEU PRO LYS PRO VAL GLN ASP LEU ILE
SEQRES 2 B 358 LYS MET ILE PHE ASP VAL GLU SER MET LYS LYS ALA MET
SEQRES 3 B 358 VAL GLU TYR GLU ILE ASP LEU GLN LYS MET PRO LEU GLY
SEQRES 4 B 358 LYS LEU SER LYS ARG GLN ILE GLN ALA ALA TYR SER ILE
SEQRES 5 B 358 LEU SER GLU VAL GLN GLN ALA VAL SER GLN GLY SER SER
SEQRES 6 B 358 ASP SER GLN ILE LEU ASP LEU SER ASN ARG PHE TYR THR
SEQRES 7 B 358 LEU ILE PRO HIS ASP PHE GLY MET LYS LYS PRO PRO LEU
SEQRES 8 B 358 LEU ASN ASN ALA ASP SER VAL GLN ALA LYS ALA GLU MET
SEQRES 9 B 358 LEU ASP ASN LEU LEU ASP ILE GLU VAL ALA TYR SER LEU
SEQRES 10 B 358 LEU ARG GLY GLY SER ASP ASP SER SER LYS ASP PRO ILE
SEQRES 11 B 358 ASP VAL ASN TYR GLU LYS LEU LYS THR ASP ILE LYS VAL
SEQRES 12 B 358 VAL ASP ARG ASP SER GLU GLU ALA GLU ILE ILE ARG LYS
SEQRES 13 B 358 TYR VAL LYS ASN THR HIS ALA THR THR HIS ASN ALA TYR
SEQRES 14 B 358 ASP LEU GLU VAL ILE ASP ILE PHE LYS ILE GLU ARG GLU
SEQRES 15 B 358 GLY GLU CYS GLN ARG TYR LYS PRO PHE LYS GLN LEU HIS
SEQRES 16 B 358 ASN ARG ARG LEU LEU TRP HIS GLY SER ARG THR THR ASN
SEQRES 17 B 358 PHE ALA GLY ILE LEU SER GLN GLY LEU ARG ILE ALA PRO
SEQRES 18 B 358 PRO GLU ALA PRO VAL THR GLY TYR MET PHE GLY LYS GLY
SEQRES 19 B 358 ILE TYR PHE ALA ASP MET VAL SER LYS SER ALA ASN TYR
SEQRES 20 B 358 CYS HIS THR SER GLN GLY ASP PRO ILE GLY LEU ILE LEU
SEQRES 21 B 358 LEU GLY GLU VAL ALA LEU GLY ASN MET TYR GLU LEU LYS
SEQRES 22 B 358 HIS ALA SER HIS ILE SER LYS LEU PRO LYS GLY LYS HIS
SEQRES 23 B 358 SER VAL LYS GLY LEU GLY LYS THR THR PRO ASP PRO SER
SEQRES 24 B 358 ALA ASN ILE SER LEU ASP GLY VAL ASP VAL PRO LEU GLY
SEQRES 25 B 358 THR GLY ILE SER SER GLY VAL ASN ASP THR SER LEU LEU
SEQRES 26 B 358 TYR ASN GLU TYR ILE VAL TYR ASP ILE ALA GLN VAL ASN
SEQRES 27 B 358 LEU LYS TYR LEU LEU LYS LEU LYS PHE ASN PHE LYS THR
SEQRES 28 B 358 ALA HIS HIS HIS HIS HIS HIS
HET SO4 A1101 5
HET SO4 A1102 5
HET SO4 A1103 5
HET SO4 A1104 5
HET SO4 A1105 5
HET XAV A1106 21
HET SO4 B1101 5
HET SO4 B1102 5
HET XAV B1103 21
HETNAM SO4 SULFATE ION
HETNAM XAV 2-[4-(TRIFLUOROMETHYL)PHENYL]-7,8-DIHYDRO-5H-
HETNAM 2 XAV THIOPYRANO[4,3-D]PYRIMIDIN-4-OL
FORMUL 3 SO4 7(O4 S 2-)
FORMUL 8 XAV 2(C14 H11 F3 N2 O S)
FORMUL 12 HOH *11(H2 O)
HELIX 1 1 PRO A 666 PHE A 677 1 12
HELIX 2 2 ASP A 678 TYR A 689 1 12
HELIX 3 3 PRO A 697 LEU A 701 5 5
HELIX 4 4 SER A 702 GLN A 722 1 21
HELIX 5 5 SER A 725 ILE A 740 1 16
HELIX 6 6 ASN A 754 GLY A 780 1 27
HELIX 7 7 ASP A 788 LEU A 797 1 10
HELIX 8 8 SER A 808 THR A 821 1 14
HELIX 9 9 GLY A 843 GLN A 853 1 11
HELIX 10 10 ARG A 865 THR A 867 5 3
HELIX 11 11 ASN A 868 GLY A 876 1 9
HELIX 12 12 PRO A 885 TYR A 889 5 5
HELIX 13 13 MET A 900 ASN A 906 1 7
HELIX 14 14 PRO A 958 ASN A 961 5 4
HELIX 15 15 SER A 963 VAL A 967 5 5
HELIX 16 16 ASP A 993 ALA A 995 5 3
HELIX 17 17 PRO B 666 ASP B 678 1 13
HELIX 18 18 ASP B 678 TYR B 689 1 12
HELIX 19 19 PRO B 697 LEU B 701 5 5
HELIX 20 20 SER B 702 GLN B 722 1 21
HELIX 21 21 SER B 725 ILE B 740 1 16
HELIX 22 22 ASN B 754 GLY B 780 1 27
HELIX 23 23 ASP B 788 LEU B 797 1 10
HELIX 24 24 SER B 808 THR B 821 1 14
HELIX 25 25 GLY B 843 GLN B 853 1 11
HELIX 26 26 ARG B 865 THR B 867 5 3
HELIX 27 27 ASN B 868 GLY B 876 1 9
HELIX 28 28 PRO B 885 TYR B 889 5 5
HELIX 29 29 MET B 900 ASN B 906 1 7
HELIX 30 30 PRO B 958 ASN B 961 5 4
HELIX 31 31 SER B 963 VAL B 967 5 5
HELIX 32 32 ASP B 993 ALA B 995 5 3
SHEET 1 A 5 THR A 799 VAL A 803 0
SHEET 2 A 5 TYR A 829 ARG A 841 -1 O LYS A 838 N LYS A 802
SHEET 3 A 5 VAL A 997 PHE A1009 -1 O ASN A1008 N ASP A 830
SHEET 4 A 5 ILE A 916 ALA A 925 -1 N ILE A 919 O LEU A1003
SHEET 5 A 5 ARG A 857 SER A 864 -1 N ARG A 858 O VAL A 924
SHEET 1 B 4 ILE A 895 PHE A 897 0
SHEET 2 B 4 GLU A 988 VAL A 991 -1 O VAL A 991 N ILE A 895
SHEET 3 B 4 SER A 947 GLY A 950 -1 N GLY A 950 O GLU A 988
SHEET 4 B 4 MET A 929 LEU A 932 1 N TYR A 930 O SER A 947
SHEET 1 C 2 THR A 954 PRO A 956 0
SHEET 2 C 2 GLY A 974 SER A 976 -1 O ILE A 975 N THR A 955
SHEET 1 D 5 THR B 799 VAL B 803 0
SHEET 2 D 5 TYR B 829 ARG B 841 -1 O LYS B 838 N LYS B 802
SHEET 3 D 5 VAL B 997 PHE B1009 -1 O LYS B1006 N GLU B 832
SHEET 4 D 5 ILE B 916 ALA B 925 -1 N ILE B 919 O LEU B1003
SHEET 5 D 5 ARG B 857 SER B 864 -1 N ARG B 858 O VAL B 924
SHEET 1 E 4 ILE B 895 PHE B 897 0
SHEET 2 E 4 GLU B 988 VAL B 991 -1 O VAL B 991 N ILE B 895
SHEET 3 E 4 SER B 947 GLY B 950 -1 N GLY B 950 O GLU B 988
SHEET 4 E 4 MET B 929 LEU B 932 1 N TYR B 930 O SER B 947
SHEET 1 F 2 THR B 954 PRO B 956 0
SHEET 2 F 2 GLY B 974 SER B 976 -1 O ILE B 975 N THR B 955
CISPEP 1 VAL A 979 ASN A 980 0 -7.62
CISPEP 2 VAL B 979 ASN B 980 0 -6.74
SITE 1 AC1 6 SER A 702 LYS A 703 ARG A 704 GLU A 772
SITE 2 AC1 6 LYS B 798 GLN B 875
SITE 1 AC2 4 LYS A 903 LEU A 985 TYR A 986 HIS B1016
SITE 1 AC3 4 THR A1011 HIS A1013 ARG B 865 HIS B 909
SITE 1 AC4 3 ARG A 865 HIS A 909 HIS B1013
SITE 1 AC5 4 ASP A 766 ALA A 880 TYR A 889 GLY A 894
SITE 1 AC6 11 ASP A 766 ASN A 767 HIS A 862 GLY A 863
SITE 2 AC6 11 SER A 864 ASN A 868 TYR A 896 PHE A 897
SITE 3 AC6 11 LYS A 903 SER A 904 TYR A 907
SITE 1 AC7 6 LYS A 798 GLN A 875 SER B 702 LYS B 703
SITE 2 AC7 6 ARG B 704 GLU B 772
SITE 1 AC8 3 LYS B 903 LEU B 985 TYR B 986
SITE 1 AC9 10 ASP B 766 ASN B 767 HIS B 862 GLY B 863
SITE 2 AC9 10 SER B 864 ASN B 868 TYR B 896 PHE B 897
SITE 3 AC9 10 SER B 904 TYR B 907
CRYST1 74.525 67.662 91.165 90.00 111.28 90.00 P 1 21 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.013418 0.000000 0.005226 0.00000
SCALE2 0.000000 0.014779 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011772 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
