HEADER TRANSFERASE/DNA/TRANSFERASE INHIBITOR 07-FEB-14 4OQA
TITLE STRUCTURE OF HUMAN PARP-1 BOUND TO A DNA DOUBLE STRAND BREAK IN
TITLE 2 COMPLEX WITH (2Z)-2-(2,4-DIHYDROXYBENZYLIDENE)-3-OXO-2,3-DIHYDRO-1-
TITLE 3 BENZOFURAN-7-CARBOXAMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY [ADP-RIBOSE] POLYMERASE 1;
COMPND 3 CHAIN: A, D;
COMPND 4 FRAGMENT: N-TERMINUS (ZN1-ZN3, SEE REMARK 999);
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 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: POLY [ADP-RIBOSE] POLYMERASE 1;
COMPND 11 CHAIN: C, F;
COMPND 12 FRAGMENT: C-TERMINUS (WGR-CAT, UNP RESIDUES 518-1014);
COMPND 13 SYNONYM: PARP-1, ADP-RIBOSYLTRANSFERASE DIPHTHERIA TOXIN-LIKE 1,
COMPND 14 ARTD1, NAD(+) ADP-RIBOSYLTRANSFERASE 1, ADPRT 1, POLY[ADP-RIBOSE]
COMPND 15 SYNTHASE 1;
COMPND 16 EC: 2.4.2.30;
COMPND 17 ENGINEERED: YES;
COMPND 18 MOL_ID: 3;
COMPND 19 MOLECULE: DNA (26-MER);
COMPND 20 CHAIN: M, N;
COMPND 21 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 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: PARP1, ADPRT, PPOL;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 MOL_ID: 3;
SOURCE 16 SYNTHETIC: YES
KEYWDS ZINC FINGER, DNA BINDING, PARP, POLYMERASE, DNA REPAIR, POLY(ADP-
KEYWDS 2 RIBOSYL)ATION, TRANSFERASE-DNA-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.M.PASCAL,J.D.STEFFEN
REVDAT 6 20-SEP-23 4OQA 1 REMARK SEQADV LINK
REVDAT 5 24-JAN-18 4OQA 1 AUTHOR
REVDAT 4 26-JUL-17 4OQA 1 SOURCE
REVDAT 3 23-JUL-14 4OQA 1 JRNL
REVDAT 2 09-JUL-14 4OQA 1 JRNL
REVDAT 1 02-JUL-14 4OQA 0
JRNL AUTH M.R.PATEL,A.BHATT,J.D.STEFFEN,A.CHERGUI,J.MURAI,Y.POMMIER,
JRNL AUTH 2 J.M.PASCAL,L.D.TROMBETTA,F.R.FRONCZEK,T.T.TALELE
JRNL TITL DISCOVERY AND STRUCTURE-ACTIVITY RELATIONSHIP OF NOVEL
JRNL TITL 2 2,3-DIHYDROBENZOFURAN-7-CARBOXAMIDE AND
JRNL TITL 3 2,3-DIHYDROBENZOFURAN-3(2H)-ONE-7-CARBOXAMIDE DERIVATIVES AS
JRNL TITL 4 POLY(ADP-RIBOSE)POLYMERASE-1 INHIBITORS.
JRNL REF J.MED.CHEM. V. 57 5579 2014
JRNL REFN ISSN 0022-2623
JRNL PMID 24922587
JRNL DOI 10.1021/JM5002502
REMARK 2
REMARK 2 RESOLUTION. 3.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
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) : 3.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 23595
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) : 0.300
REMARK 3 R VALUE (WORKING SET) : 0.298
REMARK 3 FREE R VALUE : 0.334
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1250
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) : 3.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1564
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.53
REMARK 3 BIN R VALUE (WORKING SET) : 0.4640
REMARK 3 BIN FREE R VALUE SET COUNT : 78
REMARK 3 BIN FREE R VALUE : 0.4820
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10666
REMARK 3 NUCLEIC ACID ATOMS : 1060
REMARK 3 HETEROGEN ATOMS : 26
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) : 257.2
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.03000
REMARK 3 B22 (A**2) : 9.67000
REMARK 3 B33 (A**2) : -8.64000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.882
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.998
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 164.771
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.931
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.911
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 12134 ; 0.004 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 11123 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 16603 ; 0.774 ; 1.882
REMARK 3 BOND ANGLES OTHERS (DEGREES): 25737 ; 0.860 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1350 ; 4.338 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 464 ;32.131 ;24.828
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2014 ;14.893 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 44 ;11.394 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1772 ; 0.059 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 12894 ; 0.003 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2644 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 5420 ; 1.126 ;16.866
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 5421 ; 1.126 ;16.866
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6757 ; 2.114 ;25.293
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 6757 ; 2.114 ;25.293
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 6714 ; 0.605 ;16.346
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 6715 ; 0.605 ;16.347
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 9831 ; 1.226 ;24.491
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 13556 ; 4.105 ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 13557 ; 4.105 ; 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 : 4
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 6 91 D 6 91 5107 0.00 0.05
REMARK 3 2 A 224 359 D 224 359 7577 0.00 0.05
REMARK 3 3 C 531 1011 F 531 1011 28501 0.02 0.05
REMARK 3 4 M 1 26 N 1 26 1989 0.14 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 6 A 91
REMARK 3 ORIGIN FOR THE GROUP (A): -18.8051 69.5900 7.4726
REMARK 3 T TENSOR
REMARK 3 T11: 0.3913 T22: 0.6078
REMARK 3 T33: 1.1598 T12: -0.1003
REMARK 3 T13: -0.2839 T23: -0.3860
REMARK 3 L TENSOR
REMARK 3 L11: 6.2703 L22: 2.4715
REMARK 3 L33: 10.2324 L12: -3.4658
REMARK 3 L13: -4.1198 L23: 0.7921
REMARK 3 S TENSOR
REMARK 3 S11: 0.3392 S12: 0.2521 S13: 0.4602
REMARK 3 S21: -0.3899 S22: 0.0454 S23: 0.0050
REMARK 3 S31: -0.7285 S32: -0.4369 S33: -0.3846
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 224 A 359
REMARK 3 ORIGIN FOR THE GROUP (A): -25.9944 51.9685 20.8909
REMARK 3 T TENSOR
REMARK 3 T11: 0.8533 T22: 1.2474
REMARK 3 T33: 0.9657 T12: -0.3314
REMARK 3 T13: 0.1451 T23: -0.4110
REMARK 3 L TENSOR
REMARK 3 L11: 3.8659 L22: 3.7221
REMARK 3 L33: 3.0493 L12: -3.4623
REMARK 3 L13: -0.3837 L23: -0.5348
REMARK 3 S TENSOR
REMARK 3 S11: -0.4691 S12: -0.7762 S13: 0.0542
REMARK 3 S21: 0.1230 S22: 0.5409 S23: 0.5648
REMARK 3 S31: 1.5417 S32: -0.4076 S33: -0.0718
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 531 C 1011
REMARK 3 ORIGIN FOR THE GROUP (A): -4.7279 34.8069 -25.9125
REMARK 3 T TENSOR
REMARK 3 T11: 1.1365 T22: 0.7604
REMARK 3 T33: 0.7276 T12: 0.1884
REMARK 3 T13: -0.1570 T23: -0.1394
REMARK 3 L TENSOR
REMARK 3 L11: 0.8392 L22: 1.5782
REMARK 3 L33: 4.2032 L12: -0.2511
REMARK 3 L13: -0.5655 L23: 2.4615
REMARK 3 S TENSOR
REMARK 3 S11: -0.2044 S12: -0.3497 S13: 0.0147
REMARK 3 S21: 0.0479 S22: 0.2796 S23: -0.0431
REMARK 3 S31: 0.7046 S32: 0.5670 S33: -0.0752
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 6 D 91
REMARK 3 ORIGIN FOR THE GROUP (A): 51.5843 80.3819 72.3722
REMARK 3 T TENSOR
REMARK 3 T11: 0.6647 T22: 1.9552
REMARK 3 T33: 0.3484 T12: -0.3873
REMARK 3 T13: -0.1319 T23: -0.0069
REMARK 3 L TENSOR
REMARK 3 L11: 9.2123 L22: 1.4569
REMARK 3 L33: 10.6135 L12: 2.2499
REMARK 3 L13: -4.4813 L23: 0.8410
REMARK 3 S TENSOR
REMARK 3 S11: 0.3299 S12: 1.2977 S13: 0.7872
REMARK 3 S21: 0.3097 S22: 0.0111 S23: 0.2322
REMARK 3 S31: -1.0491 S32: 0.8238 S33: -0.3411
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 224 D 359
REMARK 3 ORIGIN FOR THE GROUP (A): 58.7951 62.1604 59.5420
REMARK 3 T TENSOR
REMARK 3 T11: 0.3185 T22: 2.1895
REMARK 3 T33: 0.4598 T12: 0.1579
REMARK 3 T13: 0.1657 T23: -0.7723
REMARK 3 L TENSOR
REMARK 3 L11: 4.3019 L22: 4.0596
REMARK 3 L33: 2.7349 L12: 1.7539
REMARK 3 L13: 2.2558 L23: -1.0712
REMARK 3 S TENSOR
REMARK 3 S11: 0.1829 S12: 1.7000 S13: -0.2696
REMARK 3 S21: -0.1898 S22: -0.2835 S23: 0.0609
REMARK 3 S31: 0.5409 S32: 1.0815 S33: 0.1005
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 531 F 1011
REMARK 3 ORIGIN FOR THE GROUP (A): 37.1037 45.9173 106.5225
REMARK 3 T TENSOR
REMARK 3 T11: 0.9532 T22: 0.6489
REMARK 3 T33: 1.3754 T12: 0.0119
REMARK 3 T13: 0.0351 T23: -0.3714
REMARK 3 L TENSOR
REMARK 3 L11: 1.0567 L22: 2.0025
REMARK 3 L33: 2.0713 L12: 0.6364
REMARK 3 L13: -0.3769 L23: -1.2937
REMARK 3 S TENSOR
REMARK 3 S11: -0.1987 S12: 0.6632 S13: -0.8186
REMARK 3 S21: 0.5037 S22: 0.4631 S23: 0.0820
REMARK 3 S31: 0.1836 S32: -0.5245 S33: -0.2645
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : M 1 M 26
REMARK 3 ORIGIN FOR THE GROUP (A): 16.6388 63.9664 40.4401
REMARK 3 T TENSOR
REMARK 3 T11: 0.8107 T22: 1.4081
REMARK 3 T33: 0.8147 T12: 0.0021
REMARK 3 T13: -0.2285 T23: -0.3366
REMARK 3 L TENSOR
REMARK 3 L11: 4.0604 L22: 0.2857
REMARK 3 L33: 7.6984 L12: 0.8995
REMARK 3 L13: 4.8743 L23: 1.4319
REMARK 3 S TENSOR
REMARK 3 S11: 0.0757 S12: -0.1645 S13: 0.0967
REMARK 3 S21: 0.2519 S22: -0.0793 S23: 0.0750
REMARK 3 S31: 1.1766 S32: 0.4008 S33: 0.0036
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : N 1 N 26
REMARK 3 ORIGIN FOR THE GROUP (A): 15.2868 64.0303 40.7260
REMARK 3 T TENSOR
REMARK 3 T11: 1.4481 T22: 1.7487
REMARK 3 T33: 0.7988 T12: 0.0060
REMARK 3 T13: -0.3931 T23: -0.5123
REMARK 3 L TENSOR
REMARK 3 L11: 7.2329 L22: 0.1811
REMARK 3 L33: 1.2907 L12: 0.3953
REMARK 3 L13: 2.6873 L23: 0.1501
REMARK 3 S TENSOR
REMARK 3 S11: 0.4486 S12: -0.3465 S13: 0.6599
REMARK 3 S21: 0.0195 S22: -0.5739 S23: 0.2287
REMARK 3 S31: 0.7937 S32: -0.0975 S33: 0.1253
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 4OQA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-FEB-14.
REMARK 100 THE DEPOSITION ID IS D_1000084815.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JUL-13
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 : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.075
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : XIA2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24937
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.650
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
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: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 4DQY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25 MM HEPES, 150 MM SODIUM CHLORIDE, 1
REMARK 280 MM EDTA, 0.1 MM TCEP, 6.8% PEG3350, 2% ETHYLENE GLYCOL, PH 7.5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 32.58000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 147.12000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 57.11500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 147.12000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.58000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 57.11500
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, C, M, N
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, F, M, N
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 1
REMARK 465 ALA A 2
REMARK 465 GLU A 3
REMARK 465 SER A 4
REMARK 465 SER A 5
REMARK 465 GLY A 199
REMARK 465 GLY A 200
REMARK 465 VAL A 201
REMARK 465 THR A 202
REMARK 465 GLY A 203
REMARK 465 LYS A 204
REMARK 465 ASP A 205
REMARK 465 ILE A 206
REMARK 465 LYS A 207
REMARK 465 ARG A 208
REMARK 465 LYS A 209
REMARK 465 GLY A 210
REMARK 465 ASP A 211
REMARK 465 GLU A 212
REMARK 465 VAL A 213
REMARK 465 ASP A 214
REMARK 465 GLY A 215
REMARK 465 VAL A 216
REMARK 465 ASP A 217
REMARK 465 GLU A 218
REMARK 465 VAL A 219
REMARK 465 ALA A 220
REMARK 465 LYS A 221
REMARK 465 LYS A 222
REMARK 465 LYS A 223
REMARK 465 GLU A 360
REMARK 465 THR A 361
REMARK 465 SER A 362
REMARK 465 ALA A 363
REMARK 465 SER A 364
REMARK 465 VAL A 365
REMARK 465 ALA A 366
REMARK 465 LEU A 367
REMARK 465 GLU A 368
REMARK 465 HIS A 369
REMARK 465 HIS A 370
REMARK 465 HIS A 371
REMARK 465 HIS A 372
REMARK 465 HIS A 373
REMARK 465 HIS A 374
REMARK 465 LYS C 518
REMARK 465 SER C 519
REMARK 465 GLU C 520
REMARK 465 LYS C 521
REMARK 465 ARG C 522
REMARK 465 MET C 523
REMARK 465 LYS C 524
REMARK 465 LEU C 525
REMARK 465 THR C 526
REMARK 465 LEU C 527
REMARK 465 LYS C 528
REMARK 465 GLY C 529
REMARK 465 GLY C 530
REMARK 465 GLU C 576
REMARK 465 ASP C 577
REMARK 465 ASP C 578
REMARK 465 LYS C 579
REMARK 465 GLU C 580
REMARK 465 ASN C 581
REMARK 465 ARG C 582
REMARK 465 TYR C 583
REMARK 465 TYR C 645
REMARK 465 GLY C 646
REMARK 465 GLN C 647
REMARK 465 ASP C 648
REMARK 465 GLU C 649
REMARK 465 GLU C 650
REMARK 465 ALA C 651
REMARK 465 VAL C 652
REMARK 465 LYS C 653
REMARK 465 LYS C 654
REMARK 465 LEU C 655
REMARK 465 THR C 656
REMARK 465 VAL C 657
REMARK 465 ASN C 658
REMARK 465 PRO C 659
REMARK 465 GLY C 660
REMARK 465 THR C 661
REMARK 465 SER C 1012
REMARK 465 LEU C 1013
REMARK 465 TRP C 1014
REMARK 465 LEU C 1015
REMARK 465 GLU C 1016
REMARK 465 HIS C 1017
REMARK 465 HIS C 1018
REMARK 465 HIS C 1019
REMARK 465 HIS C 1020
REMARK 465 HIS C 1021
REMARK 465 HIS C 1022
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 GLU D 3
REMARK 465 SER D 4
REMARK 465 SER D 5
REMARK 465 GLY D 199
REMARK 465 GLY D 200
REMARK 465 VAL D 201
REMARK 465 THR D 202
REMARK 465 GLY D 203
REMARK 465 LYS D 204
REMARK 465 ASP D 205
REMARK 465 ILE D 206
REMARK 465 LYS D 207
REMARK 465 ARG D 208
REMARK 465 LYS D 209
REMARK 465 GLY D 210
REMARK 465 ASP D 211
REMARK 465 GLU D 212
REMARK 465 VAL D 213
REMARK 465 ASP D 214
REMARK 465 GLY D 215
REMARK 465 VAL D 216
REMARK 465 ASP D 217
REMARK 465 GLU D 218
REMARK 465 VAL D 219
REMARK 465 ALA D 220
REMARK 465 LYS D 221
REMARK 465 LYS D 222
REMARK 465 LYS D 223
REMARK 465 GLU D 360
REMARK 465 THR D 361
REMARK 465 SER D 362
REMARK 465 ALA D 363
REMARK 465 SER D 364
REMARK 465 VAL D 365
REMARK 465 ALA D 366
REMARK 465 LEU D 367
REMARK 465 GLU D 368
REMARK 465 HIS D 369
REMARK 465 HIS D 370
REMARK 465 HIS D 371
REMARK 465 HIS D 372
REMARK 465 HIS D 373
REMARK 465 HIS D 374
REMARK 465 LYS F 518
REMARK 465 SER F 519
REMARK 465 GLU F 520
REMARK 465 LYS F 521
REMARK 465 ARG F 522
REMARK 465 MET F 523
REMARK 465 LYS F 524
REMARK 465 LEU F 525
REMARK 465 THR F 526
REMARK 465 LEU F 527
REMARK 465 LYS F 528
REMARK 465 GLY F 529
REMARK 465 GLY F 530
REMARK 465 GLU F 576
REMARK 465 ASP F 577
REMARK 465 ASP F 578
REMARK 465 LYS F 579
REMARK 465 GLU F 580
REMARK 465 ASN F 581
REMARK 465 ARG F 582
REMARK 465 TYR F 583
REMARK 465 TYR F 645
REMARK 465 GLY F 646
REMARK 465 GLN F 647
REMARK 465 ASP F 648
REMARK 465 GLU F 649
REMARK 465 GLU F 650
REMARK 465 ALA F 651
REMARK 465 VAL F 652
REMARK 465 LYS F 653
REMARK 465 LYS F 654
REMARK 465 LEU F 655
REMARK 465 THR F 656
REMARK 465 VAL F 657
REMARK 465 ASN F 658
REMARK 465 PRO F 659
REMARK 465 GLY F 660
REMARK 465 THR F 661
REMARK 465 SER F 1012
REMARK 465 LEU F 1013
REMARK 465 TRP F 1014
REMARK 465 LEU F 1015
REMARK 465 GLU F 1016
REMARK 465 HIS F 1017
REMARK 465 HIS F 1018
REMARK 465 HIS F 1019
REMARK 465 HIS F 1020
REMARK 465 HIS F 1021
REMARK 465 HIS F 1022
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 PHE A 339 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A 340 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 341 CG CD OE1 OE2
REMARK 470 ILE A 342 CG1 CG2 CD1
REMARK 470 SER A 343 OG
REMARK 470 TYR A 344 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU A 345 CG CD1 CD2
REMARK 470 LYS A 346 CG CD CE NZ
REMARK 470 LYS A 347 CG CD CE NZ
REMARK 470 LEU A 348 CG CD1 CD2
REMARK 470 LYS A 349 CG CD CE NZ
REMARK 470 VAL A 350 CG1 CG2
REMARK 470 LYS A 351 CG CD CE NZ
REMARK 470 VAL C 762 CG1 CG2
REMARK 470 SER C 782 OG
REMARK 470 ASP C 783 CG OD1 OD2
REMARK 470 ASP C 784 CG OD1 OD2
REMARK 470 SER C 785 OG
REMARK 470 SER C 786 OG
REMARK 470 LYS C 787 CG CD CE NZ
REMARK 470 ASP C 788 CG OD1 OD2
REMARK 470 PHE D 339 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG D 340 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 341 CG CD OE1 OE2
REMARK 470 ILE D 342 CG1 CG2 CD1
REMARK 470 SER D 343 OG
REMARK 470 TYR D 344 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU D 345 CG CD1 CD2
REMARK 470 LYS D 346 CG CD CE NZ
REMARK 470 LYS D 347 CG CD CE NZ
REMARK 470 LEU D 348 CG CD1 CD2
REMARK 470 LYS D 349 CG CD CE NZ
REMARK 470 VAL D 350 CG1 CG2
REMARK 470 LYS D 351 CG CD CE NZ
REMARK 470 VAL F 762 CG1 CG2
REMARK 470 SER F 782 OG
REMARK 470 ASP F 783 CG OD1 OD2
REMARK 470 ASP F 784 CG OD1 OD2
REMARK 470 SER F 785 OG
REMARK 470 SER F 786 OG
REMARK 470 LYS F 787 CG CD CE NZ
REMARK 470 ASP F 788 CG OD1 OD2
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 DG M 1 C5' - C4' - C3' ANGL. DEV. = 7.2 DEGREES
REMARK 500 DG M 1 C5' - C4' - O4' ANGL. DEV. = 8.2 DEGREES
REMARK 500 DG N 1 C5' - C4' - C3' ANGL. DEV. = 7.6 DEGREES
REMARK 500 DG N 1 C5' - C4' - O4' ANGL. DEV. = 10.1 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 306 -73.50 65.23
REMARK 500 PHE A 339 89.85 -164.08
REMARK 500 HIS C 541 65.90 -103.37
REMARK 500 SER C 542 -58.98 -151.85
REMARK 500 SER C 554 124.28 -170.32
REMARK 500 ASN C 567 87.82 -156.24
REMARK 500 LYS C 636 3.65 59.76
REMARK 500 LYS C 664 75.68 -100.38
REMARK 500 SER C 786 -63.83 -154.38
REMARK 500 THR C 821 47.06 -94.02
REMARK 500 GLU C 832 105.90 -163.34
REMARK 500 ASN C 856 70.03 52.53
REMARK 500 HIS C 909 74.12 56.41
REMARK 500 ASP C 981 41.61 -99.42
REMARK 500 SER D 306 -73.39 65.15
REMARK 500 PHE D 339 90.06 -163.61
REMARK 500 HIS F 541 65.66 -103.17
REMARK 500 SER F 542 -58.88 -151.95
REMARK 500 SER F 554 123.82 -170.13
REMARK 500 ASN F 567 87.77 -156.03
REMARK 500 LYS F 636 4.06 58.88
REMARK 500 LYS F 664 75.66 -100.43
REMARK 500 SER F 786 -63.93 -154.30
REMARK 500 THR F 821 47.15 -94.02
REMARK 500 GLU F 832 105.90 -163.25
REMARK 500 HIS F 909 74.29 56.25
REMARK 500 ASP F 981 41.93 -99.64
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 21 SG
REMARK 620 2 CYS A 24 SG 93.9
REMARK 620 3 HIS A 53 ND1 93.7 97.1
REMARK 620 4 CYS A 56 SG 116.2 117.7 130.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 402 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 295 SG
REMARK 620 2 CYS A 298 SG 109.5
REMARK 620 3 CYS A 311 SG 92.6 88.2
REMARK 620 4 CYS A 321 SG 140.7 109.4 94.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 21 SG
REMARK 620 2 CYS D 24 SG 93.9
REMARK 620 3 HIS D 53 ND1 93.7 97.1
REMARK 620 4 CYS D 56 SG 116.3 117.6 130.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 402 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 295 SG
REMARK 620 2 CYS D 298 SG 109.5
REMARK 620 3 CYS D 311 SG 92.5 88.2
REMARK 620 4 CYS D 321 SG 140.8 109.3 94.0
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2US C 1101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4DQY RELATED DB: PDB
REMARK 900 RELATED ID: 4OPX RELATED DB: PDB
REMARK 900 RELATED ID: 4OQB RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 CHAINS A AND D EACH COMPRISE UNP RESIDUES 1-97 AND 207-366 OF PARP-
REMARK 999 1 CONNECTED BY A ASP-ILE LINKER.
DBREF 4OQA A 1 204 UNP P09874 PARP1_HUMAN 1 97
DBREF 4OQA A 207 366 UNP P09874 PARP1_HUMAN 207 366
DBREF 4OQA C 518 1014 UNP P09874 PARP1_HUMAN 518 1014
DBREF 4OQA D 1 204 UNP P09874 PARP1_HUMAN 1 97
DBREF 4OQA D 207 366 UNP P09874 PARP1_HUMAN 207 366
DBREF 4OQA F 518 1014 UNP P09874 PARP1_HUMAN 518 1014
DBREF 4OQA M 1 26 PDB 4OQA 4OQA 1 26
DBREF 4OQA N 1 26 PDB 4OQA 4OQA 1 26
SEQADV 4OQA ASP A 205 UNP P09874 LINKER
SEQADV 4OQA ILE A 206 UNP P09874 LINKER
SEQADV 4OQA LEU A 367 UNP P09874 EXPRESSION TAG
SEQADV 4OQA GLU A 368 UNP P09874 EXPRESSION TAG
SEQADV 4OQA HIS A 369 UNP P09874 EXPRESSION TAG
SEQADV 4OQA HIS A 370 UNP P09874 EXPRESSION TAG
SEQADV 4OQA HIS A 371 UNP P09874 EXPRESSION TAG
SEQADV 4OQA HIS A 372 UNP P09874 EXPRESSION TAG
SEQADV 4OQA HIS A 373 UNP P09874 EXPRESSION TAG
SEQADV 4OQA HIS A 374 UNP P09874 EXPRESSION TAG
SEQADV 4OQA LEU C 1015 UNP P09874 EXPRESSION TAG
SEQADV 4OQA GLU C 1016 UNP P09874 EXPRESSION TAG
SEQADV 4OQA HIS C 1017 UNP P09874 EXPRESSION TAG
SEQADV 4OQA HIS C 1018 UNP P09874 EXPRESSION TAG
SEQADV 4OQA HIS C 1019 UNP P09874 EXPRESSION TAG
SEQADV 4OQA HIS C 1020 UNP P09874 EXPRESSION TAG
SEQADV 4OQA HIS C 1021 UNP P09874 EXPRESSION TAG
SEQADV 4OQA HIS C 1022 UNP P09874 EXPRESSION TAG
SEQADV 4OQA ASP D 205 UNP P09874 LINKER
SEQADV 4OQA ILE D 206 UNP P09874 LINKER
SEQADV 4OQA LEU D 367 UNP P09874 EXPRESSION TAG
SEQADV 4OQA GLU D 368 UNP P09874 EXPRESSION TAG
SEQADV 4OQA HIS D 369 UNP P09874 EXPRESSION TAG
SEQADV 4OQA HIS D 370 UNP P09874 EXPRESSION TAG
SEQADV 4OQA HIS D 371 UNP P09874 EXPRESSION TAG
SEQADV 4OQA HIS D 372 UNP P09874 EXPRESSION TAG
SEQADV 4OQA HIS D 373 UNP P09874 EXPRESSION TAG
SEQADV 4OQA HIS D 374 UNP P09874 EXPRESSION TAG
SEQADV 4OQA LEU F 1015 UNP P09874 EXPRESSION TAG
SEQADV 4OQA GLU F 1016 UNP P09874 EXPRESSION TAG
SEQADV 4OQA HIS F 1017 UNP P09874 EXPRESSION TAG
SEQADV 4OQA HIS F 1018 UNP P09874 EXPRESSION TAG
SEQADV 4OQA HIS F 1019 UNP P09874 EXPRESSION TAG
SEQADV 4OQA HIS F 1020 UNP P09874 EXPRESSION TAG
SEQADV 4OQA HIS F 1021 UNP P09874 EXPRESSION TAG
SEQADV 4OQA HIS F 1022 UNP P09874 EXPRESSION TAG
SEQRES 1 A 267 MET ALA GLU SER SER ASP LYS LEU TYR ARG VAL GLU TYR
SEQRES 2 A 267 ALA LYS SER GLY ARG ALA SER CYS LYS LYS CYS SER GLU
SEQRES 3 A 267 SER ILE PRO LYS ASP SER LEU ARG MET ALA ILE MET VAL
SEQRES 4 A 267 GLN SER PRO MET PHE ASP GLY LYS VAL PRO HIS TRP TYR
SEQRES 5 A 267 HIS PHE SER CYS PHE TRP LYS VAL GLY HIS SER ILE ARG
SEQRES 6 A 267 HIS PRO ASP VAL GLU VAL ASP GLY PHE SER GLU LEU ARG
SEQRES 7 A 267 TRP ASP ASP GLN GLN LYS VAL LYS LYS THR ALA GLU ALA
SEQRES 8 A 267 GLY GLY VAL THR GLY LYS ASP ILE LYS ARG LYS GLY ASP
SEQRES 9 A 267 GLU VAL ASP GLY VAL ASP GLU VAL ALA LYS LYS LYS SER
SEQRES 10 A 267 LYS LYS GLU LYS ASP LYS ASP SER LYS LEU GLU LYS ALA
SEQRES 11 A 267 LEU LYS ALA GLN ASN ASP LEU ILE TRP ASN ILE LYS ASP
SEQRES 12 A 267 GLU LEU LYS LYS VAL CYS SER THR ASN ASP LEU LYS GLU
SEQRES 13 A 267 LEU LEU ILE PHE ASN LYS GLN GLN VAL PRO SER GLY GLU
SEQRES 14 A 267 SER ALA ILE LEU ASP ARG VAL ALA ASP GLY MET VAL PHE
SEQRES 15 A 267 GLY ALA LEU LEU PRO CYS GLU GLU CYS SER GLY GLN LEU
SEQRES 16 A 267 VAL PHE LYS SER ASP ALA TYR TYR CYS THR GLY ASP VAL
SEQRES 17 A 267 THR ALA TRP THR LYS CYS MET VAL LYS THR GLN THR PRO
SEQRES 18 A 267 ASN ARG LYS GLU TRP VAL THR PRO LYS GLU PHE ARG GLU
SEQRES 19 A 267 ILE SER TYR LEU LYS LYS LEU LYS VAL LYS LYS GLN ASP
SEQRES 20 A 267 ARG ILE PHE PRO PRO GLU THR SER ALA SER VAL ALA LEU
SEQRES 21 A 267 GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 C 505 LYS SER GLU LYS ARG MET LYS LEU THR LEU LYS GLY GLY
SEQRES 2 C 505 ALA ALA VAL ASP PRO ASP SER GLY LEU GLU HIS SER ALA
SEQRES 3 C 505 HIS VAL LEU GLU LYS GLY GLY LYS VAL PHE SER ALA THR
SEQRES 4 C 505 LEU GLY LEU VAL ASP ILE VAL LYS GLY THR ASN SER TYR
SEQRES 5 C 505 TYR LYS LEU GLN LEU LEU GLU ASP ASP LYS GLU ASN ARG
SEQRES 6 C 505 TYR TRP ILE PHE ARG SER TRP GLY ARG VAL GLY THR VAL
SEQRES 7 C 505 ILE GLY SER ASN LYS LEU GLU GLN MET PRO SER LYS GLU
SEQRES 8 C 505 ASP ALA ILE GLU HIS PHE MET LYS LEU TYR GLU GLU LYS
SEQRES 9 C 505 THR GLY ASN ALA TRP HIS SER LYS ASN PHE THR LYS TYR
SEQRES 10 C 505 PRO LYS LYS PHE TYR PRO LEU GLU ILE ASP TYR GLY GLN
SEQRES 11 C 505 ASP GLU GLU ALA VAL LYS LYS LEU THR VAL ASN PRO GLY
SEQRES 12 C 505 THR LYS SER LYS LEU PRO LYS PRO VAL GLN ASP LEU ILE
SEQRES 13 C 505 LYS MET ILE PHE ASP VAL GLU SER MET LYS LYS ALA MET
SEQRES 14 C 505 VAL GLU TYR GLU ILE ASP LEU GLN LYS MET PRO LEU GLY
SEQRES 15 C 505 LYS LEU SER LYS ARG GLN ILE GLN ALA ALA TYR SER ILE
SEQRES 16 C 505 LEU SER GLU VAL GLN GLN ALA VAL SER GLN GLY SER SER
SEQRES 17 C 505 ASP SER GLN ILE LEU ASP LEU SER ASN ARG PHE TYR THR
SEQRES 18 C 505 LEU ILE PRO HIS ASP PHE GLY MET LYS LYS PRO PRO LEU
SEQRES 19 C 505 LEU ASN ASN ALA ASP SER VAL GLN ALA LYS VAL GLU MET
SEQRES 20 C 505 LEU ASP ASN LEU LEU ASP ILE GLU VAL ALA TYR SER LEU
SEQRES 21 C 505 LEU ARG GLY GLY SER ASP ASP SER SER LYS ASP PRO ILE
SEQRES 22 C 505 ASP VAL ASN TYR GLU LYS LEU LYS THR ASP ILE LYS VAL
SEQRES 23 C 505 VAL ASP ARG ASP SER GLU GLU ALA GLU ILE ILE ARG LYS
SEQRES 24 C 505 TYR VAL LYS ASN THR HIS ALA THR THR HIS ASN ALA TYR
SEQRES 25 C 505 ASP LEU GLU VAL ILE ASP ILE PHE LYS ILE GLU ARG GLU
SEQRES 26 C 505 GLY GLU CYS GLN ARG TYR LYS PRO PHE LYS GLN LEU HIS
SEQRES 27 C 505 ASN ARG ARG LEU LEU TRP HIS GLY SER ARG THR THR ASN
SEQRES 28 C 505 PHE ALA GLY ILE LEU SER GLN GLY LEU ARG ILE ALA PRO
SEQRES 29 C 505 PRO GLU ALA PRO VAL THR GLY TYR MET PHE GLY LYS GLY
SEQRES 30 C 505 ILE TYR PHE ALA ASP MET VAL SER LYS SER ALA ASN TYR
SEQRES 31 C 505 CYS HIS THR SER GLN GLY ASP PRO ILE GLY LEU ILE LEU
SEQRES 32 C 505 LEU GLY GLU VAL ALA LEU GLY ASN MET TYR GLU LEU LYS
SEQRES 33 C 505 HIS ALA SER HIS ILE SER LYS LEU PRO LYS GLY LYS HIS
SEQRES 34 C 505 SER VAL LYS GLY LEU GLY LYS THR THR PRO ASP PRO SER
SEQRES 35 C 505 ALA ASN ILE SER LEU ASP GLY VAL ASP VAL PRO LEU GLY
SEQRES 36 C 505 THR GLY ILE SER SER GLY VAL ASN ASP THR SER LEU LEU
SEQRES 37 C 505 TYR ASN GLU TYR ILE VAL TYR ASP ILE ALA GLN VAL ASN
SEQRES 38 C 505 LEU LYS TYR LEU LEU LYS LEU LYS PHE ASN PHE LYS THR
SEQRES 39 C 505 SER LEU TRP LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 D 267 MET ALA GLU SER SER ASP LYS LEU TYR ARG VAL GLU TYR
SEQRES 2 D 267 ALA LYS SER GLY ARG ALA SER CYS LYS LYS CYS SER GLU
SEQRES 3 D 267 SER ILE PRO LYS ASP SER LEU ARG MET ALA ILE MET VAL
SEQRES 4 D 267 GLN SER PRO MET PHE ASP GLY LYS VAL PRO HIS TRP TYR
SEQRES 5 D 267 HIS PHE SER CYS PHE TRP LYS VAL GLY HIS SER ILE ARG
SEQRES 6 D 267 HIS PRO ASP VAL GLU VAL ASP GLY PHE SER GLU LEU ARG
SEQRES 7 D 267 TRP ASP ASP GLN GLN LYS VAL LYS LYS THR ALA GLU ALA
SEQRES 8 D 267 GLY GLY VAL THR GLY LYS ASP ILE LYS ARG LYS GLY ASP
SEQRES 9 D 267 GLU VAL ASP GLY VAL ASP GLU VAL ALA LYS LYS LYS SER
SEQRES 10 D 267 LYS LYS GLU LYS ASP LYS ASP SER LYS LEU GLU LYS ALA
SEQRES 11 D 267 LEU LYS ALA GLN ASN ASP LEU ILE TRP ASN ILE LYS ASP
SEQRES 12 D 267 GLU LEU LYS LYS VAL CYS SER THR ASN ASP LEU LYS GLU
SEQRES 13 D 267 LEU LEU ILE PHE ASN LYS GLN GLN VAL PRO SER GLY GLU
SEQRES 14 D 267 SER ALA ILE LEU ASP ARG VAL ALA ASP GLY MET VAL PHE
SEQRES 15 D 267 GLY ALA LEU LEU PRO CYS GLU GLU CYS SER GLY GLN LEU
SEQRES 16 D 267 VAL PHE LYS SER ASP ALA TYR TYR CYS THR GLY ASP VAL
SEQRES 17 D 267 THR ALA TRP THR LYS CYS MET VAL LYS THR GLN THR PRO
SEQRES 18 D 267 ASN ARG LYS GLU TRP VAL THR PRO LYS GLU PHE ARG GLU
SEQRES 19 D 267 ILE SER TYR LEU LYS LYS LEU LYS VAL LYS LYS GLN ASP
SEQRES 20 D 267 ARG ILE PHE PRO PRO GLU THR SER ALA SER VAL ALA LEU
SEQRES 21 D 267 GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 F 505 LYS SER GLU LYS ARG MET LYS LEU THR LEU LYS GLY GLY
SEQRES 2 F 505 ALA ALA VAL ASP PRO ASP SER GLY LEU GLU HIS SER ALA
SEQRES 3 F 505 HIS VAL LEU GLU LYS GLY GLY LYS VAL PHE SER ALA THR
SEQRES 4 F 505 LEU GLY LEU VAL ASP ILE VAL LYS GLY THR ASN SER TYR
SEQRES 5 F 505 TYR LYS LEU GLN LEU LEU GLU ASP ASP LYS GLU ASN ARG
SEQRES 6 F 505 TYR TRP ILE PHE ARG SER TRP GLY ARG VAL GLY THR VAL
SEQRES 7 F 505 ILE GLY SER ASN LYS LEU GLU GLN MET PRO SER LYS GLU
SEQRES 8 F 505 ASP ALA ILE GLU HIS PHE MET LYS LEU TYR GLU GLU LYS
SEQRES 9 F 505 THR GLY ASN ALA TRP HIS SER LYS ASN PHE THR LYS TYR
SEQRES 10 F 505 PRO LYS LYS PHE TYR PRO LEU GLU ILE ASP TYR GLY GLN
SEQRES 11 F 505 ASP GLU GLU ALA VAL LYS LYS LEU THR VAL ASN PRO GLY
SEQRES 12 F 505 THR LYS SER LYS LEU PRO LYS PRO VAL GLN ASP LEU ILE
SEQRES 13 F 505 LYS MET ILE PHE ASP VAL GLU SER MET LYS LYS ALA MET
SEQRES 14 F 505 VAL GLU TYR GLU ILE ASP LEU GLN LYS MET PRO LEU GLY
SEQRES 15 F 505 LYS LEU SER LYS ARG GLN ILE GLN ALA ALA TYR SER ILE
SEQRES 16 F 505 LEU SER GLU VAL GLN GLN ALA VAL SER GLN GLY SER SER
SEQRES 17 F 505 ASP SER GLN ILE LEU ASP LEU SER ASN ARG PHE TYR THR
SEQRES 18 F 505 LEU ILE PRO HIS ASP PHE GLY MET LYS LYS PRO PRO LEU
SEQRES 19 F 505 LEU ASN ASN ALA ASP SER VAL GLN ALA LYS VAL GLU MET
SEQRES 20 F 505 LEU ASP ASN LEU LEU ASP ILE GLU VAL ALA TYR SER LEU
SEQRES 21 F 505 LEU ARG GLY GLY SER ASP ASP SER SER LYS ASP PRO ILE
SEQRES 22 F 505 ASP VAL ASN TYR GLU LYS LEU LYS THR ASP ILE LYS VAL
SEQRES 23 F 505 VAL ASP ARG ASP SER GLU GLU ALA GLU ILE ILE ARG LYS
SEQRES 24 F 505 TYR VAL LYS ASN THR HIS ALA THR THR HIS ASN ALA TYR
SEQRES 25 F 505 ASP LEU GLU VAL ILE ASP ILE PHE LYS ILE GLU ARG GLU
SEQRES 26 F 505 GLY GLU CYS GLN ARG TYR LYS PRO PHE LYS GLN LEU HIS
SEQRES 27 F 505 ASN ARG ARG LEU LEU TRP HIS GLY SER ARG THR THR ASN
SEQRES 28 F 505 PHE ALA GLY ILE LEU SER GLN GLY LEU ARG ILE ALA PRO
SEQRES 29 F 505 PRO GLU ALA PRO VAL THR GLY TYR MET PHE GLY LYS GLY
SEQRES 30 F 505 ILE TYR PHE ALA ASP MET VAL SER LYS SER ALA ASN TYR
SEQRES 31 F 505 CYS HIS THR SER GLN GLY ASP PRO ILE GLY LEU ILE LEU
SEQRES 32 F 505 LEU GLY GLU VAL ALA LEU GLY ASN MET TYR GLU LEU LYS
SEQRES 33 F 505 HIS ALA SER HIS ILE SER LYS LEU PRO LYS GLY LYS HIS
SEQRES 34 F 505 SER VAL LYS GLY LEU GLY LYS THR THR PRO ASP PRO SER
SEQRES 35 F 505 ALA ASN ILE SER LEU ASP GLY VAL ASP VAL PRO LEU GLY
SEQRES 36 F 505 THR GLY ILE SER SER GLY VAL ASN ASP THR SER LEU LEU
SEQRES 37 F 505 TYR ASN GLU TYR ILE VAL TYR ASP ILE ALA GLN VAL ASN
SEQRES 38 F 505 LEU LYS TYR LEU LEU LYS LEU LYS PHE ASN PHE LYS THR
SEQRES 39 F 505 SER LEU TRP LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 M 26 DG DC DC DT DA DC DC DG DG DT DT DC DG
SEQRES 2 M 26 DC DG DA DA DC DC DG DG DT DA DG DG DC
SEQRES 1 N 26 DG DC DC DT DA DC DC DG DG DT DT DC DG
SEQRES 2 N 26 DC DG DA DA DC DC DG DG DT DA DG DG DC
HET ZN A 401 1
HET ZN A 402 1
HET 2US C1101 22
HET ZN D 401 1
HET ZN D 402 1
HETNAM ZN ZINC ION
HETNAM 2US (2Z)-2-(2,4-DIHYDROXYBENZYLIDENE)-3-OXO-2,3-DIHYDRO-1-
HETNAM 2 2US BENZOFURAN-7-CARBOXAMIDE
FORMUL 7 ZN 4(ZN 2+)
FORMUL 9 2US C16 H11 N O5
HELIX 1 1 SER A 55 LYS A 59 5 5
HELIX 2 2 HIS A 66 GLU A 70 1 5
HELIX 3 3 ARG A 78 ALA A 91 1 14
HELIX 4 4 LYS A 225 CYS A 256 1 32
HELIX 5 5 SER A 257 ASN A 268 1 12
HELIX 6 6 GLY A 275 PHE A 289 1 15
HELIX 7 7 GLU A 341 LYS A 346 1 6
HELIX 8 8 SER C 606 GLY C 623 1 18
HELIX 9 9 PRO C 666 PHE C 677 1 12
HELIX 10 10 ASP C 678 GLU C 688 1 11
HELIX 11 11 SER C 702 GLN C 722 1 21
HELIX 12 12 SER C 725 ILE C 740 1 16
HELIX 13 13 ASN C 754 ARG C 779 1 26
HELIX 14 14 ASP C 788 LYS C 798 1 11
HELIX 15 15 SER C 808 THR C 821 1 14
HELIX 16 16 GLY C 843 LYS C 849 1 7
HELIX 17 17 PRO C 850 GLN C 853 5 4
HELIX 18 18 ASN C 868 GLY C 876 1 9
HELIX 19 19 MET C 900 ASN C 906 1 7
HELIX 20 20 TYR C 907 HIS C 909 5 3
HELIX 21 21 PRO C 958 ASN C 961 5 4
HELIX 22 22 SER D 55 LYS D 59 5 5
HELIX 23 23 HIS D 66 GLU D 70 1 5
HELIX 24 24 ARG D 78 ALA D 91 1 14
HELIX 25 25 LYS D 225 CYS D 256 1 32
HELIX 26 26 SER D 257 ASN D 268 1 12
HELIX 27 27 GLY D 275 PHE D 289 1 15
HELIX 28 28 GLU D 341 LYS D 346 1 6
HELIX 29 29 SER F 606 GLY F 623 1 18
HELIX 30 30 PRO F 666 PHE F 677 1 12
HELIX 31 31 ASP F 678 GLU F 688 1 11
HELIX 32 32 SER F 702 GLN F 722 1 21
HELIX 33 33 SER F 725 ILE F 740 1 16
HELIX 34 34 ASN F 754 ARG F 779 1 26
HELIX 35 35 ASP F 788 LYS F 798 1 11
HELIX 36 36 SER F 808 THR F 821 1 14
HELIX 37 37 GLY F 843 LYS F 849 1 7
HELIX 38 38 PRO F 850 GLN F 853 5 4
HELIX 39 39 ASN F 868 GLY F 876 1 9
HELIX 40 40 MET F 900 ASN F 906 1 7
HELIX 41 41 TYR F 907 HIS F 909 5 3
HELIX 42 42 PRO F 958 ASN F 961 5 4
SHEET 1 A 4 LYS A 47 HIS A 53 0
SHEET 2 A 4 LEU A 33 GLN A 40 -1 N VAL A 39 O VAL A 48
SHEET 3 A 4 TYR A 9 TYR A 13 -1 N ARG A 10 O ALA A 36
SHEET 4 A 4 VAL A 71 ASP A 72 1 O ASP A 72 N VAL A 11
SHEET 1 B 2 ALA A 291 LEU A 292 0
SHEET 2 B 2 ARG A 330 LYS A 331 -1 O LYS A 331 N ALA A 291
SHEET 1 C 3 LEU A 302 LYS A 305 0
SHEET 2 C 3 ALA A 308 CYS A 311 -1 O ALA A 308 N LYS A 305
SHEET 3 C 3 LYS A 324 THR A 325 -1 O THR A 325 N TYR A 309
SHEET 1 D 2 GLU C 547 LYS C 548 0
SHEET 2 D 2 LYS C 551 VAL C 552 -1 O LYS C 551 N LYS C 548
SHEET 1 E 5 GLY C 597 GLU C 602 0
SHEET 2 E 5 ILE C 585 ARG C 591 -1 N ILE C 585 O GLU C 602
SHEET 3 E 5 ASN C 567 GLN C 573 -1 N LYS C 571 O SER C 588
SHEET 4 E 5 SER C 554 VAL C 560 -1 N ALA C 555 O LEU C 572
SHEET 5 E 5 TYR C 639 LEU C 641 -1 O LEU C 641 N THR C 556
SHEET 1 F 5 THR C 799 VAL C 803 0
SHEET 2 F 5 ASP C 830 ARG C 841 -1 O GLU C 840 N ASP C 800
SHEET 3 F 5 LEU C 999 ASN C1008 -1 O LEU C1002 N PHE C 837
SHEET 4 F 5 ILE C 916 ALA C 925 -1 N GLY C 917 O LEU C1005
SHEET 5 F 5 ARG C 857 GLY C 863 -1 N HIS C 862 O LEU C 920
SHEET 1 G 4 ILE C 895 PHE C 897 0
SHEET 2 G 4 GLU C 988 VAL C 991 -1 O TYR C 989 N PHE C 897
SHEET 3 G 4 SER C 947 GLY C 950 -1 N GLY C 950 O GLU C 988
SHEET 4 G 4 MET C 929 LEU C 932 1 N LEU C 932 O LYS C 949
SHEET 1 H 2 THR C 954 PRO C 956 0
SHEET 2 H 2 GLY C 974 SER C 976 -1 O ILE C 975 N THR C 955
SHEET 1 I 2 ILE C 962 SER C 963 0
SHEET 2 I 2 ASP C 968 VAL C 969 -1 O VAL C 969 N ILE C 962
SHEET 1 J 4 LYS D 47 HIS D 53 0
SHEET 2 J 4 LEU D 33 GLN D 40 -1 N VAL D 39 O VAL D 48
SHEET 3 J 4 TYR D 9 TYR D 13 -1 N ARG D 10 O ALA D 36
SHEET 4 J 4 VAL D 71 ASP D 72 1 O ASP D 72 N VAL D 11
SHEET 1 K 2 ALA D 291 LEU D 292 0
SHEET 2 K 2 ARG D 330 LYS D 331 -1 O LYS D 331 N ALA D 291
SHEET 1 L 3 LEU D 302 LYS D 305 0
SHEET 2 L 3 ALA D 308 CYS D 311 -1 O ALA D 308 N LYS D 305
SHEET 3 L 3 LYS D 324 THR D 325 -1 O THR D 325 N TYR D 309
SHEET 1 M 2 GLU F 547 LYS F 548 0
SHEET 2 M 2 LYS F 551 VAL F 552 -1 O LYS F 551 N LYS F 548
SHEET 1 N 5 GLY F 597 GLU F 602 0
SHEET 2 N 5 ILE F 585 ARG F 591 -1 N ILE F 585 O GLU F 602
SHEET 3 N 5 ASN F 567 GLN F 573 -1 N LYS F 571 O SER F 588
SHEET 4 N 5 SER F 554 VAL F 560 -1 N ALA F 555 O LEU F 572
SHEET 5 N 5 TYR F 639 LEU F 641 -1 O LEU F 641 N THR F 556
SHEET 1 O 5 THR F 799 VAL F 803 0
SHEET 2 O 5 ASP F 830 ARG F 841 -1 O GLU F 840 N ASP F 800
SHEET 3 O 5 LEU F 999 ASN F1008 -1 O LEU F1002 N PHE F 837
SHEET 4 O 5 ILE F 916 ALA F 925 -1 N GLY F 917 O LEU F1005
SHEET 5 O 5 ARG F 857 GLY F 863 -1 N HIS F 862 O LEU F 920
SHEET 1 P 4 ILE F 895 PHE F 897 0
SHEET 2 P 4 GLU F 988 VAL F 991 -1 O TYR F 989 N PHE F 897
SHEET 3 P 4 SER F 947 GLY F 950 -1 N GLY F 950 O GLU F 988
SHEET 4 P 4 MET F 929 LEU F 932 1 N LEU F 932 O LYS F 949
SHEET 1 Q 2 THR F 954 PRO F 956 0
SHEET 2 Q 2 GLY F 974 SER F 976 -1 O ILE F 975 N THR F 955
SHEET 1 R 2 ILE F 962 SER F 963 0
SHEET 2 R 2 ASP F 968 VAL F 969 -1 O VAL F 969 N ILE F 962
LINK SG CYS A 21 ZN ZN A 401 1555 1555 2.34
LINK SG CYS A 24 ZN ZN A 401 1555 1555 2.34
LINK ND1 HIS A 53 ZN ZN A 401 1555 1555 2.07
LINK SG CYS A 56 ZN ZN A 401 1555 1555 2.34
LINK SG CYS A 295 ZN ZN A 402 1555 1555 2.34
LINK SG CYS A 298 ZN ZN A 402 1555 1555 2.34
LINK SG CYS A 311 ZN ZN A 402 1555 1555 2.34
LINK SG CYS A 321 ZN ZN A 402 1555 1555 2.34
LINK SG CYS D 21 ZN ZN D 401 1555 1555 2.34
LINK SG CYS D 24 ZN ZN D 401 1555 1555 2.34
LINK ND1 HIS D 53 ZN ZN D 401 1555 1555 2.07
LINK SG CYS D 56 ZN ZN D 401 1555 1555 2.34
LINK SG CYS D 295 ZN ZN D 402 1555 1555 2.34
LINK SG CYS D 298 ZN ZN D 402 1555 1555 2.34
LINK SG CYS D 311 ZN ZN D 402 1555 1555 2.34
LINK SG CYS D 321 ZN ZN D 402 1555 1555 2.34
SITE 1 AC1 4 CYS A 21 CYS A 24 HIS A 53 CYS A 56
SITE 1 AC2 4 CYS A 295 CYS A 298 CYS A 311 CYS A 321
SITE 1 AC3 8 HIS C 862 GLY C 863 TYR C 889 TYR C 896
SITE 2 AC3 8 ALA C 898 SER C 904 TYR C 907 GLU C 988
SITE 1 AC4 4 CYS D 21 CYS D 24 HIS D 53 CYS D 56
SITE 1 AC5 4 CYS D 295 CYS D 298 CYS D 311 CYS D 321
CRYST1 65.160 114.230 294.240 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.015347 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008754 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003399 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
