HEADER DNA BINDING PROTEIN/DNA 11-AUG-10 3ODA
TITLE HUMAN PARP-1 ZINC FINGER 1 (ZN1) BOUND TO DNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY [ADP-RIBOSE] POLYMERASE 1;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 FRAGMENT: PARP-1 ZINC FINGER 1, ZN1, UNP RESIDUES 2-96;
COMPND 5 SYNONYM: PARP-1, NAD(+) ADP-RIBOSYLTRANSFERASE 1, ADPRT 1, POLY[ADP-
COMPND 6 RIBOSE] SYNTHASE 1;
COMPND 7 EC: 2.4.2.30;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: 5'-D(*GP*CP*CP*TP*GP*CP*AP*GP*GP*C)-3';
COMPND 11 CHAIN: I, J, K, L, M, N, O, P;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ADPRT, PARP1, PPOL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) ROSETTA2;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 OTHER_DETAILS: CHEMICALLY SYNTHESIZED DNA
KEYWDS PROTEIN-DNA COMPLEX, PARP ZINC FINGER, DNA BINDING PROTEIN-DNA
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.M.PASCAL,M.-F.LANGELIER
REVDAT 5 21-FEB-24 3ODA 1 REMARK SEQADV LINK
REVDAT 4 08-NOV-17 3ODA 1 REMARK
REVDAT 3 08-JUN-11 3ODA 1 MTRIX1 MTRIX2 MTRIX3
REVDAT 2 13-APR-11 3ODA 1 JRNL
REVDAT 1 12-JAN-11 3ODA 0
JRNL AUTH M.F.LANGELIER,J.L.PLANCK,S.ROY,J.M.PASCAL
JRNL TITL CRYSTAL STRUCTURES OF POLY(ADP-RIBOSE) POLYMERASE-1 (PARP-1)
JRNL TITL 2 ZINC FINGERS BOUND TO DNA: STRUCTURAL AND FUNCTIONAL
JRNL TITL 3 INSIGHTS INTO DNA-DEPENDENT PARP-1 ACTIVITY.
JRNL REF J.BIOL.CHEM. V. 286 10690 2011
JRNL REFN ISSN 0021-9258
JRNL PMID 21233213
JRNL DOI 10.1074/JBC.M110.202507
REMARK 2
REMARK 2 RESOLUTION. 2.64 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.6.1_357
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.64
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.42
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 33211
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 1677
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 42.4267 - 5.6859 0.99 3183 187 0.1634 0.1764
REMARK 3 2 5.6859 - 4.5147 1.00 3194 168 0.1517 0.1817
REMARK 3 3 4.5147 - 3.9445 1.00 3147 176 0.1616 0.2219
REMARK 3 4 3.9445 - 3.5840 1.00 3180 164 0.1820 0.2432
REMARK 3 5 3.5840 - 3.3273 1.00 3154 165 0.1920 0.2675
REMARK 3 6 3.3273 - 3.1312 0.99 3145 160 0.1981 0.2669
REMARK 3 7 3.1312 - 2.9744 1.00 3127 187 0.2295 0.2798
REMARK 3 8 2.9744 - 2.8449 1.00 3159 174 0.2424 0.3523
REMARK 3 9 2.8449 - 2.7354 1.00 3161 156 0.2514 0.3029
REMARK 3 10 2.7354 - 2.6411 0.97 3084 140 0.2556 0.3271
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.33
REMARK 3 B_SOL : 36.35
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.360
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.02
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 8.34840
REMARK 3 B22 (A**2) : -9.96490
REMARK 3 B33 (A**2) : 1.61650
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 2.14620
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.011 7731
REMARK 3 ANGLE : 1.288 10687
REMARK 3 CHIRALITY : 0.072 1092
REMARK 3 PLANARITY : 0.005 1084
REMARK 3 DIHEDRAL : 21.881 2991
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 4
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'A' AND (RESSEQ 7:9 OR RESSEQ 11:38
REMARK 3 OR RESSEQ 48:59 OR RESSEQ 68:91 OR
REMARK 3 (RESSEQ 10 AND BACKBONE) ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 SELECTION : CHAIN 'C' AND (RESSEQ 7:9 OR RESSEQ 11:38
REMARK 3 OR RESSEQ 48:59 OR RESSEQ 68:91 OR
REMARK 3 (RESSEQ 10 AND BACKBONE) ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 ATOM PAIRS NUMBER : 556
REMARK 3 RMSD : 0.040
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN 'A' AND (RESSEQ 7:9 OR RESSEQ 11:38
REMARK 3 OR RESSEQ 48:59 OR RESSEQ 68:91 OR
REMARK 3 (RESSEQ 10 AND BACKBONE) ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 SELECTION : CHAIN 'E' AND (RESSEQ 7:9 OR RESSEQ 11:38
REMARK 3 OR RESSEQ 48:59 OR RESSEQ 68:91 OR
REMARK 3 (RESSEQ 10 AND BACKBONE) ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 ATOM PAIRS NUMBER : 557
REMARK 3 RMSD : 0.051
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN 'A' AND (RESSEQ 7:9 OR RESSEQ 11:38
REMARK 3 OR RESSEQ 48:59 OR RESSEQ 68:91 OR
REMARK 3 (RESSEQ 10 AND BACKBONE) ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 SELECTION : CHAIN 'G' AND (RESSEQ 7:9 OR RESSEQ 11:38
REMARK 3 OR RESSEQ 48:59 OR RESSEQ 68:91 OR
REMARK 3 (RESSEQ 10 AND BACKBONE) ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 ATOM PAIRS NUMBER : 548
REMARK 3 RMSD : 0.046
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'B' AND (RESSEQ 7:9 OR RESSEQ 11:38
REMARK 3 OR RESSEQ 48:59 OR RESSEQ 68:82 OR RESSEQ
REMARK 3 84:91 OR (RESSEQ 83 AND BACKBONE) OR
REMARK 3 (RESSEQ 10 AND BACKBONE) ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 SELECTION : CHAIN 'D' AND (RESSEQ 7:9 OR RESSEQ 11:38
REMARK 3 OR RESSEQ 48:59 OR RESSEQ 68:82 OR RESSEQ
REMARK 3 84:91 OR (RESSEQ 83 AND BACKBONE) OR
REMARK 3 (RESSEQ 10 AND BACKBONE) ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 ATOM PAIRS NUMBER : 551
REMARK 3 RMSD : 0.051
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN 'B' AND (RESSEQ 7:9 OR RESSEQ 11:38
REMARK 3 OR RESSEQ 48:59 OR RESSEQ 68:82 OR RESSEQ
REMARK 3 84:91 OR (RESSEQ 83 AND BACKBONE) OR
REMARK 3 (RESSEQ 10 AND BACKBONE) ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 SELECTION : CHAIN 'F' AND (RESSEQ 7:9 OR RESSEQ 11:38
REMARK 3 OR RESSEQ 48:59 OR RESSEQ 68:82 OR RESSEQ
REMARK 3 84:91 OR (RESSEQ 83 AND BACKBONE) OR
REMARK 3 (RESSEQ 10 AND BACKBONE) ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 ATOM PAIRS NUMBER : 552
REMARK 3 RMSD : 0.055
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN 'B' AND (RESSEQ 7:9 OR RESSEQ 11:38
REMARK 3 OR RESSEQ 48:59 OR RESSEQ 68:82 OR RESSEQ
REMARK 3 84:91 OR (RESSEQ 83 AND BACKBONE) OR
REMARK 3 (RESSEQ 10 AND BACKBONE) ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 SELECTION : CHAIN 'H' AND (RESSEQ 7:9 OR RESSEQ 11:38
REMARK 3 OR RESSEQ 48:59 OR RESSEQ 68:82 OR RESSEQ
REMARK 3 84:91 OR (RESSEQ 83 AND BACKBONE) OR
REMARK 3 (RESSEQ 10 AND BACKBONE) ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 ATOM PAIRS NUMBER : 552
REMARK 3 RMSD : 0.052
REMARK 3 NCS GROUP : 3
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'B' AND (RESSEQ 39:47) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D) AND
REMARK 3 BACKBONE
REMARK 3 SELECTION : CHAIN 'A' AND (RESSEQ 39:47) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D) AND
REMARK 3 BACKBONE
REMARK 3 ATOM PAIRS NUMBER : 36
REMARK 3 RMSD : 0.264
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN 'B' AND (RESSEQ 39:47) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D) AND
REMARK 3 BACKBONE
REMARK 3 SELECTION : CHAIN 'D' AND (RESSEQ 39:47) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D) AND
REMARK 3 BACKBONE
REMARK 3 ATOM PAIRS NUMBER : 36
REMARK 3 RMSD : 0.182
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN 'B' AND (RESSEQ 39:47) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D) AND
REMARK 3 BACKBONE
REMARK 3 SELECTION : CHAIN 'F' AND (RESSEQ 39:47) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D) AND
REMARK 3 BACKBONE
REMARK 3 ATOM PAIRS NUMBER : 36
REMARK 3 RMSD : 0.245
REMARK 3 NCS OPERATOR : 4
REMARK 3 REFERENCE SELECTION: CHAIN 'B' AND (RESSEQ 39:47) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D) AND
REMARK 3 BACKBONE
REMARK 3 SELECTION : CHAIN 'H' AND (RESSEQ 39:47) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D) AND
REMARK 3 BACKBONE
REMARK 3 ATOM PAIRS NUMBER : 36
REMARK 3 RMSD : 0.186
REMARK 3 NCS GROUP : 4
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'C' AND (RESSEQ 39:47) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D) AND
REMARK 3 BACKBONE
REMARK 3 SELECTION : CHAIN 'E' AND (RESSEQ 39:47) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D) AND
REMARK 3 BACKBONE
REMARK 3 ATOM PAIRS NUMBER : 36
REMARK 3 RMSD : 0.253
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN 'C' AND (RESSEQ 39:47) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D) AND
REMARK 3 BACKBONE
REMARK 3 SELECTION : CHAIN 'G' AND (RESSEQ 39:47) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D) AND
REMARK 3 BACKBONE
REMARK 3 ATOM PAIRS NUMBER : 36
REMARK 3 RMSD : 0.199
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3ODA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-AUG-10.
REMARK 100 THE DEPOSITION ID IS D_1000060970.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-SEP-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X12C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.99
REMARK 200 MONOCHROMATOR : SILICON(111) CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33279
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.640
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.64
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.30
REMARK 200 R MERGE FOR SHELL (I) : 0.50900
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 3350, 100 MM NAACETATE, 100 MM
REMARK 280 TRIS PH 8.5, 0.1 MM TCEP, 20% ETHYLENE GLYCOL, VAPOR DIFFUSION,
REMARK 280 TEMPERATURE 298K
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 53.66700
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, 3, 4
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, B, I, J
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: C, D, K, L
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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, 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 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, O, P
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 -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 GLU A 3
REMARK 465 SER A 4
REMARK 465 GLY A 92
REMARK 465 GLY A 93
REMARK 465 VAL A 94
REMARK 465 THR A 95
REMARK 465 GLY A 96
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 GLU B 3
REMARK 465 SER B 4
REMARK 465 SER B 5
REMARK 465 GLY B 92
REMARK 465 GLY B 93
REMARK 465 VAL B 94
REMARK 465 THR B 95
REMARK 465 GLY B 96
REMARK 465 MET C -19
REMARK 465 GLY C -18
REMARK 465 SER C -17
REMARK 465 SER C -16
REMARK 465 HIS C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 HIS C -10
REMARK 465 SER C -9
REMARK 465 SER C -8
REMARK 465 GLY C -7
REMARK 465 LEU C -6
REMARK 465 VAL C -5
REMARK 465 PRO C -4
REMARK 465 ARG C -3
REMARK 465 GLY C -2
REMARK 465 SER C -1
REMARK 465 HIS C 0
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 GLU C 3
REMARK 465 SER C 4
REMARK 465 GLY C 92
REMARK 465 GLY C 93
REMARK 465 VAL C 94
REMARK 465 THR C 95
REMARK 465 GLY C 96
REMARK 465 MET D -19
REMARK 465 GLY D -18
REMARK 465 SER D -17
REMARK 465 SER D -16
REMARK 465 HIS D -15
REMARK 465 HIS D -14
REMARK 465 HIS D -13
REMARK 465 HIS D -12
REMARK 465 HIS D -11
REMARK 465 HIS D -10
REMARK 465 SER D -9
REMARK 465 SER D -8
REMARK 465 GLY D -7
REMARK 465 LEU D -6
REMARK 465 VAL D -5
REMARK 465 PRO D -4
REMARK 465 ARG D -3
REMARK 465 GLY D -2
REMARK 465 SER D -1
REMARK 465 HIS D 0
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 GLU D 3
REMARK 465 SER D 4
REMARK 465 VAL D 94
REMARK 465 THR D 95
REMARK 465 GLY D 96
REMARK 465 MET E -19
REMARK 465 GLY E -18
REMARK 465 SER E -17
REMARK 465 SER E -16
REMARK 465 HIS E -15
REMARK 465 HIS E -14
REMARK 465 HIS E -13
REMARK 465 HIS E -12
REMARK 465 HIS E -11
REMARK 465 HIS E -10
REMARK 465 SER E -9
REMARK 465 SER E -8
REMARK 465 GLY E -7
REMARK 465 LEU E -6
REMARK 465 VAL E -5
REMARK 465 PRO E -4
REMARK 465 ARG E -3
REMARK 465 GLY E -2
REMARK 465 SER E -1
REMARK 465 HIS E 0
REMARK 465 MET E 1
REMARK 465 ALA E 2
REMARK 465 GLU E 3
REMARK 465 SER E 4
REMARK 465 SER E 5
REMARK 465 GLY E 92
REMARK 465 GLY E 93
REMARK 465 VAL E 94
REMARK 465 THR E 95
REMARK 465 GLY E 96
REMARK 465 MET F -19
REMARK 465 GLY F -18
REMARK 465 SER F -17
REMARK 465 SER F -16
REMARK 465 HIS F -15
REMARK 465 HIS F -14
REMARK 465 HIS F -13
REMARK 465 HIS F -12
REMARK 465 HIS F -11
REMARK 465 HIS F -10
REMARK 465 SER F -9
REMARK 465 SER F -8
REMARK 465 GLY F -7
REMARK 465 LEU F -6
REMARK 465 VAL F -5
REMARK 465 PRO F -4
REMARK 465 ARG F -3
REMARK 465 GLY F -2
REMARK 465 SER F -1
REMARK 465 HIS F 0
REMARK 465 MET F 1
REMARK 465 ALA F 2
REMARK 465 GLU F 3
REMARK 465 SER F 4
REMARK 465 THR F 95
REMARK 465 GLY F 96
REMARK 465 MET G -19
REMARK 465 GLY G -18
REMARK 465 SER G -17
REMARK 465 SER G -16
REMARK 465 HIS G -15
REMARK 465 HIS G -14
REMARK 465 HIS G -13
REMARK 465 HIS G -12
REMARK 465 HIS G -11
REMARK 465 HIS G -10
REMARK 465 SER G -9
REMARK 465 SER G -8
REMARK 465 GLY G -7
REMARK 465 LEU G -6
REMARK 465 VAL G -5
REMARK 465 PRO G -4
REMARK 465 ARG G -3
REMARK 465 GLY G -2
REMARK 465 SER G -1
REMARK 465 HIS G 0
REMARK 465 MET G 1
REMARK 465 ALA G 2
REMARK 465 GLU G 3
REMARK 465 SER G 4
REMARK 465 GLY G 92
REMARK 465 GLY G 93
REMARK 465 VAL G 94
REMARK 465 THR G 95
REMARK 465 GLY G 96
REMARK 465 MET H -19
REMARK 465 GLY H -18
REMARK 465 SER H -17
REMARK 465 SER H -16
REMARK 465 HIS H -15
REMARK 465 HIS H -14
REMARK 465 HIS H -13
REMARK 465 HIS H -12
REMARK 465 HIS H -11
REMARK 465 HIS H -10
REMARK 465 SER H -9
REMARK 465 SER H -8
REMARK 465 GLY H -7
REMARK 465 LEU H -6
REMARK 465 VAL H -5
REMARK 465 PRO H -4
REMARK 465 ARG H -3
REMARK 465 GLY H -2
REMARK 465 SER H -1
REMARK 465 HIS H 0
REMARK 465 MET H 1
REMARK 465 ALA H 2
REMARK 465 GLU H 3
REMARK 465 SER H 4
REMARK 465 GLY H 93
REMARK 465 VAL H 94
REMARK 465 THR H 95
REMARK 465 GLY H 96
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 NZ LYS E 23 OE1 GLU G 26 2657 2.11
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 DT I 4 O3' DT I 4 C3' -0.037
REMARK 500 DG I 5 O3' DG I 5 C3' -0.038
REMARK 500 DC I 6 O3' DC I 6 C3' -0.047
REMARK 500 DC J 6 O3' DC J 6 C3' -0.044
REMARK 500 DT K 4 O3' DT K 4 C3' -0.041
REMARK 500 DG P 9 O3' DG P 9 C3' -0.040
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 DT I 4 C3' - C2' - C1' ANGL. DEV. = -5.1 DEGREES
REMARK 500 DT I 4 N3 - C4 - O4 ANGL. DEV. = 3.7 DEGREES
REMARK 500 DG I 5 C3' - C2' - C1' ANGL. DEV. = -5.5 DEGREES
REMARK 500 DG I 5 O4' - C1' - N9 ANGL. DEV. = -4.3 DEGREES
REMARK 500 DC I 6 C3' - C2' - C1' ANGL. DEV. = -6.8 DEGREES
REMARK 500 DC I 6 O4' - C1' - N1 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DC I 10 O4' - C4' - C3' ANGL. DEV. = -3.6 DEGREES
REMARK 500 DC I 10 O4' - C1' - N1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 DC J 3 O4' - C4' - C3' ANGL. DEV. = -3.7 DEGREES
REMARK 500 DT K 4 O4' - C1' - N1 ANGL. DEV. = -4.7 DEGREES
REMARK 500 DG K 5 C3' - C2' - C1' ANGL. DEV. = -6.6 DEGREES
REMARK 500 DA K 7 O4' - C1' - N9 ANGL. DEV. = -5.5 DEGREES
REMARK 500 DG K 8 O4' - C1' - N9 ANGL. DEV. = -5.6 DEGREES
REMARK 500 DG K 9 O4' - C1' - N9 ANGL. DEV. = 3.0 DEGREES
REMARK 500 DC K 10 O4' - C1' - N1 ANGL. DEV. = 2.7 DEGREES
REMARK 500 DG L 1 O4' - C1' - N9 ANGL. DEV. = 3.8 DEGREES
REMARK 500 DT L 4 O4' - C1' - N1 ANGL. DEV. = -5.4 DEGREES
REMARK 500 DC L 6 C3' - C2' - C1' ANGL. DEV. = -5.6 DEGREES
REMARK 500 DG L 9 O4' - C1' - N9 ANGL. DEV. = 2.7 DEGREES
REMARK 500 DC L 10 O4' - C1' - N1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 DG M 1 C3' - C2' - C1' ANGL. DEV. = -5.3 DEGREES
REMARK 500 DG M 1 O4' - C1' - N9 ANGL. DEV. = 3.2 DEGREES
REMARK 500 DT M 4 O4' - C1' - N1 ANGL. DEV. = -7.0 DEGREES
REMARK 500 DC M 6 C3' - C2' - C1' ANGL. DEV. = -5.6 DEGREES
REMARK 500 DC M 6 O4' - C1' - N1 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DG M 8 C1' - O4' - C4' ANGL. DEV. = -6.3 DEGREES
REMARK 500 DG N 1 O4' - C1' - N9 ANGL. DEV. = 3.3 DEGREES
REMARK 500 DC N 2 C3' - C2' - C1' ANGL. DEV. = -6.0 DEGREES
REMARK 500 DC N 3 O4' - C1' - N1 ANGL. DEV. = -5.4 DEGREES
REMARK 500 DG N 5 O4' - C1' - N9 ANGL. DEV. = -4.5 DEGREES
REMARK 500 DG N 8 O4' - C1' - N9 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DG N 9 O4' - C1' - C2' ANGL. DEV. = 3.8 DEGREES
REMARK 500 DT O 4 N3 - C4 - O4 ANGL. DEV. = 3.9 DEGREES
REMARK 500 DG O 5 P - O5' - C5' ANGL. DEV. = -9.7 DEGREES
REMARK 500 DG O 5 O4' - C4' - C3' ANGL. DEV. = -3.8 DEGREES
REMARK 500 DC O 6 C3' - C2' - C1' ANGL. DEV. = -5.4 DEGREES
REMARK 500 DC O 10 O4' - C1' - N1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 DG P 1 O4' - C4' - C3' ANGL. DEV. = -2.5 DEGREES
REMARK 500 DG P 1 C3' - C2' - C1' ANGL. DEV. = -4.9 DEGREES
REMARK 500 DT P 4 C3' - C2' - C1' ANGL. DEV. = -5.1 DEGREES
REMARK 500 DC P 6 C3' - C2' - C1' ANGL. DEV. = -5.6 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 ASP A 31 -13.25 75.93
REMARK 500 SER A 63 60.08 -100.30
REMARK 500 SER B 25 -11.16 78.27
REMARK 500 ASP B 31 -7.06 69.38
REMARK 500 ASP C 31 -14.15 74.98
REMARK 500 ASP D 6 40.38 -93.93
REMARK 500 SER D 25 -13.81 77.49
REMARK 500 ASP D 31 -8.76 69.93
REMARK 500 SER E 25 -0.16 73.50
REMARK 500 ASP E 31 -14.53 75.52
REMARK 500 MET E 43 -77.62 -71.16
REMARK 500 PHE E 44 -161.77 -107.51
REMARK 500 HIS E 66 75.79 -105.55
REMARK 500 ASP E 68 -31.94 -35.30
REMARK 500 SER F 25 -14.83 78.12
REMARK 500 ASP F 31 -9.42 70.11
REMARK 500 SER G 25 -0.16 74.01
REMARK 500 ASP G 31 -13.95 74.57
REMARK 500 SER H 25 -13.98 77.24
REMARK 500 ASP H 31 -8.84 69.94
REMARK 500 ALA H 91 -12.88 -45.57
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 200 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 21 SG
REMARK 620 2 CYS A 24 SG 109.8
REMARK 620 3 HIS A 53 ND1 106.4 92.6
REMARK 620 4 CYS A 56 SG 113.1 116.5 116.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 200 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 21 SG
REMARK 620 2 CYS B 24 SG 107.1
REMARK 620 3 HIS B 53 ND1 99.4 95.1
REMARK 620 4 CYS B 56 SG 108.5 125.0 118.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 200 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 21 SG
REMARK 620 2 CYS C 24 SG 110.9
REMARK 620 3 HIS C 53 ND1 106.6 94.0
REMARK 620 4 CYS C 56 SG 110.9 117.4 115.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 200 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 21 SG
REMARK 620 2 CYS D 24 SG 107.8
REMARK 620 3 HIS D 53 ND1 98.4 98.9
REMARK 620 4 CYS D 56 SG 107.5 122.5 118.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN E 200 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E 21 SG
REMARK 620 2 CYS E 24 SG 116.0
REMARK 620 3 HIS E 53 ND1 103.1 98.9
REMARK 620 4 CYS E 56 SG 103.4 120.9 113.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN F 200 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS F 21 SG
REMARK 620 2 CYS F 24 SG 106.2
REMARK 620 3 HIS F 53 ND1 99.3 100.1
REMARK 620 4 CYS F 56 SG 109.2 121.4 118.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN G 200 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS G 21 SG
REMARK 620 2 CYS G 24 SG 108.3
REMARK 620 3 HIS G 53 ND1 106.9 97.8
REMARK 620 4 CYS G 56 SG 106.6 114.0 122.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN H 200 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS H 21 SG
REMARK 620 2 CYS H 24 SG 108.4
REMARK 620 3 HIS H 53 ND1 101.2 101.3
REMARK 620 4 CYS H 56 SG 106.9 119.1 118.3
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 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN G 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H 200
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3OD8 RELATED DB: PDB
REMARK 900 HUMAN PARP-1 ZINC FINGER 1 (ZN1) BOUND TO DNA
REMARK 900 RELATED ID: 3ODC RELATED DB: PDB
REMARK 900 HUMAN PARP-1 ZINC FINGER 1 (ZN1) BOUND TO DNA
REMARK 900 RELATED ID: 3ODE RELATED DB: PDB
REMARK 900 HUMAN PARP-1 ZINC FINGER 2 (ZN2) BOUND TO DNA
DBREF 3ODA A 2 96 UNP P09874 PARP1_HUMAN 2 96
DBREF 3ODA B 2 96 UNP P09874 PARP1_HUMAN 2 96
DBREF 3ODA C 2 96 UNP P09874 PARP1_HUMAN 2 96
DBREF 3ODA D 2 96 UNP P09874 PARP1_HUMAN 2 96
DBREF 3ODA E 2 96 UNP P09874 PARP1_HUMAN 2 96
DBREF 3ODA F 2 96 UNP P09874 PARP1_HUMAN 2 96
DBREF 3ODA G 2 96 UNP P09874 PARP1_HUMAN 2 96
DBREF 3ODA H 2 96 UNP P09874 PARP1_HUMAN 2 96
DBREF 3ODA I 1 10 PDB 3ODA 3ODA 1 10
DBREF 3ODA J 1 10 PDB 3ODA 3ODA 1 10
DBREF 3ODA K 1 10 PDB 3ODA 3ODA 1 10
DBREF 3ODA L 1 10 PDB 3ODA 3ODA 1 10
DBREF 3ODA M 1 10 PDB 3ODA 3ODA 1 10
DBREF 3ODA N 1 10 PDB 3ODA 3ODA 1 10
DBREF 3ODA O 1 10 PDB 3ODA 3ODA 1 10
DBREF 3ODA P 1 10 PDB 3ODA 3ODA 1 10
SEQADV 3ODA MET A -19 UNP P09874 EXPRESSION TAG
SEQADV 3ODA GLY A -18 UNP P09874 EXPRESSION TAG
SEQADV 3ODA SER A -17 UNP P09874 EXPRESSION TAG
SEQADV 3ODA SER A -16 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS A -15 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS A -14 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS A -13 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS A -12 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS A -11 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS A -10 UNP P09874 EXPRESSION TAG
SEQADV 3ODA SER A -9 UNP P09874 EXPRESSION TAG
SEQADV 3ODA SER A -8 UNP P09874 EXPRESSION TAG
SEQADV 3ODA GLY A -7 UNP P09874 EXPRESSION TAG
SEQADV 3ODA LEU A -6 UNP P09874 EXPRESSION TAG
SEQADV 3ODA VAL A -5 UNP P09874 EXPRESSION TAG
SEQADV 3ODA PRO A -4 UNP P09874 EXPRESSION TAG
SEQADV 3ODA ARG A -3 UNP P09874 EXPRESSION TAG
SEQADV 3ODA GLY A -2 UNP P09874 EXPRESSION TAG
SEQADV 3ODA SER A -1 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS A 0 UNP P09874 EXPRESSION TAG
SEQADV 3ODA MET A 1 UNP P09874 EXPRESSION TAG
SEQADV 3ODA MET B -19 UNP P09874 EXPRESSION TAG
SEQADV 3ODA GLY B -18 UNP P09874 EXPRESSION TAG
SEQADV 3ODA SER B -17 UNP P09874 EXPRESSION TAG
SEQADV 3ODA SER B -16 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS B -15 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS B -14 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS B -13 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS B -12 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS B -11 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS B -10 UNP P09874 EXPRESSION TAG
SEQADV 3ODA SER B -9 UNP P09874 EXPRESSION TAG
SEQADV 3ODA SER B -8 UNP P09874 EXPRESSION TAG
SEQADV 3ODA GLY B -7 UNP P09874 EXPRESSION TAG
SEQADV 3ODA LEU B -6 UNP P09874 EXPRESSION TAG
SEQADV 3ODA VAL B -5 UNP P09874 EXPRESSION TAG
SEQADV 3ODA PRO B -4 UNP P09874 EXPRESSION TAG
SEQADV 3ODA ARG B -3 UNP P09874 EXPRESSION TAG
SEQADV 3ODA GLY B -2 UNP P09874 EXPRESSION TAG
SEQADV 3ODA SER B -1 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS B 0 UNP P09874 EXPRESSION TAG
SEQADV 3ODA MET B 1 UNP P09874 EXPRESSION TAG
SEQADV 3ODA MET C -19 UNP P09874 EXPRESSION TAG
SEQADV 3ODA GLY C -18 UNP P09874 EXPRESSION TAG
SEQADV 3ODA SER C -17 UNP P09874 EXPRESSION TAG
SEQADV 3ODA SER C -16 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS C -15 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS C -14 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS C -13 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS C -12 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS C -11 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS C -10 UNP P09874 EXPRESSION TAG
SEQADV 3ODA SER C -9 UNP P09874 EXPRESSION TAG
SEQADV 3ODA SER C -8 UNP P09874 EXPRESSION TAG
SEQADV 3ODA GLY C -7 UNP P09874 EXPRESSION TAG
SEQADV 3ODA LEU C -6 UNP P09874 EXPRESSION TAG
SEQADV 3ODA VAL C -5 UNP P09874 EXPRESSION TAG
SEQADV 3ODA PRO C -4 UNP P09874 EXPRESSION TAG
SEQADV 3ODA ARG C -3 UNP P09874 EXPRESSION TAG
SEQADV 3ODA GLY C -2 UNP P09874 EXPRESSION TAG
SEQADV 3ODA SER C -1 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS C 0 UNP P09874 EXPRESSION TAG
SEQADV 3ODA MET C 1 UNP P09874 EXPRESSION TAG
SEQADV 3ODA MET D -19 UNP P09874 EXPRESSION TAG
SEQADV 3ODA GLY D -18 UNP P09874 EXPRESSION TAG
SEQADV 3ODA SER D -17 UNP P09874 EXPRESSION TAG
SEQADV 3ODA SER D -16 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS D -15 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS D -14 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS D -13 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS D -12 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS D -11 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS D -10 UNP P09874 EXPRESSION TAG
SEQADV 3ODA SER D -9 UNP P09874 EXPRESSION TAG
SEQADV 3ODA SER D -8 UNP P09874 EXPRESSION TAG
SEQADV 3ODA GLY D -7 UNP P09874 EXPRESSION TAG
SEQADV 3ODA LEU D -6 UNP P09874 EXPRESSION TAG
SEQADV 3ODA VAL D -5 UNP P09874 EXPRESSION TAG
SEQADV 3ODA PRO D -4 UNP P09874 EXPRESSION TAG
SEQADV 3ODA ARG D -3 UNP P09874 EXPRESSION TAG
SEQADV 3ODA GLY D -2 UNP P09874 EXPRESSION TAG
SEQADV 3ODA SER D -1 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS D 0 UNP P09874 EXPRESSION TAG
SEQADV 3ODA MET D 1 UNP P09874 EXPRESSION TAG
SEQADV 3ODA MET E -19 UNP P09874 EXPRESSION TAG
SEQADV 3ODA GLY E -18 UNP P09874 EXPRESSION TAG
SEQADV 3ODA SER E -17 UNP P09874 EXPRESSION TAG
SEQADV 3ODA SER E -16 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS E -15 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS E -14 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS E -13 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS E -12 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS E -11 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS E -10 UNP P09874 EXPRESSION TAG
SEQADV 3ODA SER E -9 UNP P09874 EXPRESSION TAG
SEQADV 3ODA SER E -8 UNP P09874 EXPRESSION TAG
SEQADV 3ODA GLY E -7 UNP P09874 EXPRESSION TAG
SEQADV 3ODA LEU E -6 UNP P09874 EXPRESSION TAG
SEQADV 3ODA VAL E -5 UNP P09874 EXPRESSION TAG
SEQADV 3ODA PRO E -4 UNP P09874 EXPRESSION TAG
SEQADV 3ODA ARG E -3 UNP P09874 EXPRESSION TAG
SEQADV 3ODA GLY E -2 UNP P09874 EXPRESSION TAG
SEQADV 3ODA SER E -1 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS E 0 UNP P09874 EXPRESSION TAG
SEQADV 3ODA MET E 1 UNP P09874 EXPRESSION TAG
SEQADV 3ODA MET F -19 UNP P09874 EXPRESSION TAG
SEQADV 3ODA GLY F -18 UNP P09874 EXPRESSION TAG
SEQADV 3ODA SER F -17 UNP P09874 EXPRESSION TAG
SEQADV 3ODA SER F -16 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS F -15 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS F -14 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS F -13 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS F -12 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS F -11 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS F -10 UNP P09874 EXPRESSION TAG
SEQADV 3ODA SER F -9 UNP P09874 EXPRESSION TAG
SEQADV 3ODA SER F -8 UNP P09874 EXPRESSION TAG
SEQADV 3ODA GLY F -7 UNP P09874 EXPRESSION TAG
SEQADV 3ODA LEU F -6 UNP P09874 EXPRESSION TAG
SEQADV 3ODA VAL F -5 UNP P09874 EXPRESSION TAG
SEQADV 3ODA PRO F -4 UNP P09874 EXPRESSION TAG
SEQADV 3ODA ARG F -3 UNP P09874 EXPRESSION TAG
SEQADV 3ODA GLY F -2 UNP P09874 EXPRESSION TAG
SEQADV 3ODA SER F -1 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS F 0 UNP P09874 EXPRESSION TAG
SEQADV 3ODA MET F 1 UNP P09874 EXPRESSION TAG
SEQADV 3ODA MET G -19 UNP P09874 EXPRESSION TAG
SEQADV 3ODA GLY G -18 UNP P09874 EXPRESSION TAG
SEQADV 3ODA SER G -17 UNP P09874 EXPRESSION TAG
SEQADV 3ODA SER G -16 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS G -15 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS G -14 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS G -13 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS G -12 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS G -11 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS G -10 UNP P09874 EXPRESSION TAG
SEQADV 3ODA SER G -9 UNP P09874 EXPRESSION TAG
SEQADV 3ODA SER G -8 UNP P09874 EXPRESSION TAG
SEQADV 3ODA GLY G -7 UNP P09874 EXPRESSION TAG
SEQADV 3ODA LEU G -6 UNP P09874 EXPRESSION TAG
SEQADV 3ODA VAL G -5 UNP P09874 EXPRESSION TAG
SEQADV 3ODA PRO G -4 UNP P09874 EXPRESSION TAG
SEQADV 3ODA ARG G -3 UNP P09874 EXPRESSION TAG
SEQADV 3ODA GLY G -2 UNP P09874 EXPRESSION TAG
SEQADV 3ODA SER G -1 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS G 0 UNP P09874 EXPRESSION TAG
SEQADV 3ODA MET G 1 UNP P09874 EXPRESSION TAG
SEQADV 3ODA MET H -19 UNP P09874 EXPRESSION TAG
SEQADV 3ODA GLY H -18 UNP P09874 EXPRESSION TAG
SEQADV 3ODA SER H -17 UNP P09874 EXPRESSION TAG
SEQADV 3ODA SER H -16 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS H -15 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS H -14 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS H -13 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS H -12 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS H -11 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS H -10 UNP P09874 EXPRESSION TAG
SEQADV 3ODA SER H -9 UNP P09874 EXPRESSION TAG
SEQADV 3ODA SER H -8 UNP P09874 EXPRESSION TAG
SEQADV 3ODA GLY H -7 UNP P09874 EXPRESSION TAG
SEQADV 3ODA LEU H -6 UNP P09874 EXPRESSION TAG
SEQADV 3ODA VAL H -5 UNP P09874 EXPRESSION TAG
SEQADV 3ODA PRO H -4 UNP P09874 EXPRESSION TAG
SEQADV 3ODA ARG H -3 UNP P09874 EXPRESSION TAG
SEQADV 3ODA GLY H -2 UNP P09874 EXPRESSION TAG
SEQADV 3ODA SER H -1 UNP P09874 EXPRESSION TAG
SEQADV 3ODA HIS H 0 UNP P09874 EXPRESSION TAG
SEQADV 3ODA MET H 1 UNP P09874 EXPRESSION TAG
SEQRES 1 A 116 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 116 LEU VAL PRO ARG GLY SER HIS MET ALA GLU SER SER ASP
SEQRES 3 A 116 LYS LEU TYR ARG VAL GLU TYR ALA LYS SER GLY ARG ALA
SEQRES 4 A 116 SER CYS LYS LYS CYS SER GLU SER ILE PRO LYS ASP SER
SEQRES 5 A 116 LEU ARG MET ALA ILE MET VAL GLN SER PRO MET PHE ASP
SEQRES 6 A 116 GLY LYS VAL PRO HIS TRP TYR HIS PHE SER CYS PHE TRP
SEQRES 7 A 116 LYS VAL GLY HIS SER ILE ARG HIS PRO ASP VAL GLU VAL
SEQRES 8 A 116 ASP GLY PHE SER GLU LEU ARG TRP ASP ASP GLN GLN LYS
SEQRES 9 A 116 VAL LYS LYS THR ALA GLU ALA GLY GLY VAL THR GLY
SEQRES 1 B 116 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 116 LEU VAL PRO ARG GLY SER HIS MET ALA GLU SER SER ASP
SEQRES 3 B 116 LYS LEU TYR ARG VAL GLU TYR ALA LYS SER GLY ARG ALA
SEQRES 4 B 116 SER CYS LYS LYS CYS SER GLU SER ILE PRO LYS ASP SER
SEQRES 5 B 116 LEU ARG MET ALA ILE MET VAL GLN SER PRO MET PHE ASP
SEQRES 6 B 116 GLY LYS VAL PRO HIS TRP TYR HIS PHE SER CYS PHE TRP
SEQRES 7 B 116 LYS VAL GLY HIS SER ILE ARG HIS PRO ASP VAL GLU VAL
SEQRES 8 B 116 ASP GLY PHE SER GLU LEU ARG TRP ASP ASP GLN GLN LYS
SEQRES 9 B 116 VAL LYS LYS THR ALA GLU ALA GLY GLY VAL THR GLY
SEQRES 1 C 116 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 116 LEU VAL PRO ARG GLY SER HIS MET ALA GLU SER SER ASP
SEQRES 3 C 116 LYS LEU TYR ARG VAL GLU TYR ALA LYS SER GLY ARG ALA
SEQRES 4 C 116 SER CYS LYS LYS CYS SER GLU SER ILE PRO LYS ASP SER
SEQRES 5 C 116 LEU ARG MET ALA ILE MET VAL GLN SER PRO MET PHE ASP
SEQRES 6 C 116 GLY LYS VAL PRO HIS TRP TYR HIS PHE SER CYS PHE TRP
SEQRES 7 C 116 LYS VAL GLY HIS SER ILE ARG HIS PRO ASP VAL GLU VAL
SEQRES 8 C 116 ASP GLY PHE SER GLU LEU ARG TRP ASP ASP GLN GLN LYS
SEQRES 9 C 116 VAL LYS LYS THR ALA GLU ALA GLY GLY VAL THR GLY
SEQRES 1 D 116 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 116 LEU VAL PRO ARG GLY SER HIS MET ALA GLU SER SER ASP
SEQRES 3 D 116 LYS LEU TYR ARG VAL GLU TYR ALA LYS SER GLY ARG ALA
SEQRES 4 D 116 SER CYS LYS LYS CYS SER GLU SER ILE PRO LYS ASP SER
SEQRES 5 D 116 LEU ARG MET ALA ILE MET VAL GLN SER PRO MET PHE ASP
SEQRES 6 D 116 GLY LYS VAL PRO HIS TRP TYR HIS PHE SER CYS PHE TRP
SEQRES 7 D 116 LYS VAL GLY HIS SER ILE ARG HIS PRO ASP VAL GLU VAL
SEQRES 8 D 116 ASP GLY PHE SER GLU LEU ARG TRP ASP ASP GLN GLN LYS
SEQRES 9 D 116 VAL LYS LYS THR ALA GLU ALA GLY GLY VAL THR GLY
SEQRES 1 E 116 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 E 116 LEU VAL PRO ARG GLY SER HIS MET ALA GLU SER SER ASP
SEQRES 3 E 116 LYS LEU TYR ARG VAL GLU TYR ALA LYS SER GLY ARG ALA
SEQRES 4 E 116 SER CYS LYS LYS CYS SER GLU SER ILE PRO LYS ASP SER
SEQRES 5 E 116 LEU ARG MET ALA ILE MET VAL GLN SER PRO MET PHE ASP
SEQRES 6 E 116 GLY LYS VAL PRO HIS TRP TYR HIS PHE SER CYS PHE TRP
SEQRES 7 E 116 LYS VAL GLY HIS SER ILE ARG HIS PRO ASP VAL GLU VAL
SEQRES 8 E 116 ASP GLY PHE SER GLU LEU ARG TRP ASP ASP GLN GLN LYS
SEQRES 9 E 116 VAL LYS LYS THR ALA GLU ALA GLY GLY VAL THR GLY
SEQRES 1 F 116 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 F 116 LEU VAL PRO ARG GLY SER HIS MET ALA GLU SER SER ASP
SEQRES 3 F 116 LYS LEU TYR ARG VAL GLU TYR ALA LYS SER GLY ARG ALA
SEQRES 4 F 116 SER CYS LYS LYS CYS SER GLU SER ILE PRO LYS ASP SER
SEQRES 5 F 116 LEU ARG MET ALA ILE MET VAL GLN SER PRO MET PHE ASP
SEQRES 6 F 116 GLY LYS VAL PRO HIS TRP TYR HIS PHE SER CYS PHE TRP
SEQRES 7 F 116 LYS VAL GLY HIS SER ILE ARG HIS PRO ASP VAL GLU VAL
SEQRES 8 F 116 ASP GLY PHE SER GLU LEU ARG TRP ASP ASP GLN GLN LYS
SEQRES 9 F 116 VAL LYS LYS THR ALA GLU ALA GLY GLY VAL THR GLY
SEQRES 1 G 116 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 G 116 LEU VAL PRO ARG GLY SER HIS MET ALA GLU SER SER ASP
SEQRES 3 G 116 LYS LEU TYR ARG VAL GLU TYR ALA LYS SER GLY ARG ALA
SEQRES 4 G 116 SER CYS LYS LYS CYS SER GLU SER ILE PRO LYS ASP SER
SEQRES 5 G 116 LEU ARG MET ALA ILE MET VAL GLN SER PRO MET PHE ASP
SEQRES 6 G 116 GLY LYS VAL PRO HIS TRP TYR HIS PHE SER CYS PHE TRP
SEQRES 7 G 116 LYS VAL GLY HIS SER ILE ARG HIS PRO ASP VAL GLU VAL
SEQRES 8 G 116 ASP GLY PHE SER GLU LEU ARG TRP ASP ASP GLN GLN LYS
SEQRES 9 G 116 VAL LYS LYS THR ALA GLU ALA GLY GLY VAL THR GLY
SEQRES 1 H 116 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 H 116 LEU VAL PRO ARG GLY SER HIS MET ALA GLU SER SER ASP
SEQRES 3 H 116 LYS LEU TYR ARG VAL GLU TYR ALA LYS SER GLY ARG ALA
SEQRES 4 H 116 SER CYS LYS LYS CYS SER GLU SER ILE PRO LYS ASP SER
SEQRES 5 H 116 LEU ARG MET ALA ILE MET VAL GLN SER PRO MET PHE ASP
SEQRES 6 H 116 GLY LYS VAL PRO HIS TRP TYR HIS PHE SER CYS PHE TRP
SEQRES 7 H 116 LYS VAL GLY HIS SER ILE ARG HIS PRO ASP VAL GLU VAL
SEQRES 8 H 116 ASP GLY PHE SER GLU LEU ARG TRP ASP ASP GLN GLN LYS
SEQRES 9 H 116 VAL LYS LYS THR ALA GLU ALA GLY GLY VAL THR GLY
SEQRES 1 I 10 DG DC DC DT DG DC DA DG DG DC
SEQRES 1 J 10 DG DC DC DT DG DC DA DG DG DC
SEQRES 1 K 10 DG DC DC DT DG DC DA DG DG DC
SEQRES 1 L 10 DG DC DC DT DG DC DA DG DG DC
SEQRES 1 M 10 DG DC DC DT DG DC DA DG DG DC
SEQRES 1 N 10 DG DC DC DT DG DC DA DG DG DC
SEQRES 1 O 10 DG DC DC DT DG DC DA DG DG DC
SEQRES 1 P 10 DG DC DC DT DG DC DA DG DG DC
HET ZN A 200 1
HET ZN B 200 1
HET ZN C 200 1
HET ZN D 200 1
HET ZN E 200 1
HET ZN F 200 1
HET ZN G 200 1
HET ZN H 200 1
HETNAM ZN ZINC ION
FORMUL 17 ZN 8(ZN 2+)
FORMUL 25 HOH *233(H2 O)
HELIX 1 1 PHE A 54 VAL A 60 1 7
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 PHE B 54 LYS B 59 1 6
HELIX 5 5 HIS B 66 GLU B 70 1 5
HELIX 6 6 GLY B 73 LEU B 77 5 5
HELIX 7 7 ARG B 78 ALA B 91 1 14
HELIX 8 8 PHE C 54 VAL C 60 1 7
HELIX 9 9 HIS C 66 GLU C 70 1 5
HELIX 10 10 ARG C 78 ALA C 91 1 14
HELIX 11 11 PHE D 54 VAL D 60 1 7
HELIX 12 12 HIS D 66 GLU D 70 1 5
HELIX 13 13 GLY D 73 LEU D 77 5 5
HELIX 14 14 ARG D 78 GLY D 92 1 15
HELIX 15 15 PHE E 54 VAL E 60 1 7
HELIX 16 16 HIS E 66 GLU E 70 1 5
HELIX 17 17 ARG E 78 ALA E 91 1 14
HELIX 18 18 PHE F 54 VAL F 60 1 7
HELIX 19 19 HIS F 66 GLU F 70 1 5
HELIX 20 20 GLY F 73 LEU F 77 5 5
HELIX 21 21 ARG F 78 GLY F 92 1 15
HELIX 22 22 PHE G 54 VAL G 60 1 7
HELIX 23 23 HIS G 66 GLU G 70 1 5
HELIX 24 24 ARG G 78 ALA G 91 1 14
HELIX 25 25 PHE H 54 LYS H 59 1 6
HELIX 26 26 HIS H 66 GLU H 70 1 5
HELIX 27 27 GLY H 73 LEU H 77 5 5
HELIX 28 28 ARG H 78 ALA H 91 1 14
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 4 LYS B 47 HIS B 53 0
SHEET 2 B 4 LEU B 33 GLN B 40 -1 N VAL B 39 O VAL B 48
SHEET 3 B 4 TYR B 9 TYR B 13 -1 N ARG B 10 O ALA B 36
SHEET 4 B 4 VAL B 71 ASP B 72 1 O ASP B 72 N TYR B 9
SHEET 1 C 4 LYS C 47 HIS C 53 0
SHEET 2 C 4 LEU C 33 GLN C 40 -1 N VAL C 39 O VAL C 48
SHEET 3 C 4 TYR C 9 TYR C 13 -1 N ARG C 10 O ALA C 36
SHEET 4 C 4 VAL C 71 ASP C 72 1 O ASP C 72 N VAL C 11
SHEET 1 D 4 LYS D 47 HIS D 53 0
SHEET 2 D 4 LEU D 33 GLN D 40 -1 N VAL D 39 O VAL D 48
SHEET 3 D 4 TYR D 9 TYR D 13 -1 N ARG D 10 O ALA D 36
SHEET 4 D 4 VAL D 71 ASP D 72 1 O ASP D 72 N TYR D 9
SHEET 1 E 4 LYS E 47 HIS E 53 0
SHEET 2 E 4 LEU E 33 GLN E 40 -1 N VAL E 39 O VAL E 48
SHEET 3 E 4 TYR E 9 TYR E 13 -1 N ARG E 10 O ALA E 36
SHEET 4 E 4 VAL E 71 ASP E 72 1 O ASP E 72 N VAL E 11
SHEET 1 F 4 LYS F 47 HIS F 53 0
SHEET 2 F 4 LEU F 33 GLN F 40 -1 N VAL F 39 O VAL F 48
SHEET 3 F 4 TYR F 9 TYR F 13 -1 N ARG F 10 O ALA F 36
SHEET 4 F 4 VAL F 71 ASP F 72 1 O ASP F 72 N TYR F 9
SHEET 1 G 4 LYS G 47 HIS G 53 0
SHEET 2 G 4 LEU G 33 GLN G 40 -1 N VAL G 39 O VAL G 48
SHEET 3 G 4 TYR G 9 TYR G 13 -1 N ARG G 10 O ALA G 36
SHEET 4 G 4 VAL G 71 ASP G 72 1 O ASP G 72 N VAL G 11
SHEET 1 H 4 LYS H 47 HIS H 53 0
SHEET 2 H 4 LEU H 33 GLN H 40 -1 N VAL H 39 O VAL H 48
SHEET 3 H 4 TYR H 9 TYR H 13 -1 N ARG H 10 O ALA H 36
SHEET 4 H 4 VAL H 71 ASP H 72 1 O ASP H 72 N TYR H 9
LINK SG CYS A 21 ZN ZN A 200 1555 1555 2.20
LINK SG CYS A 24 ZN ZN A 200 1555 1555 2.35
LINK ND1 HIS A 53 ZN ZN A 200 1555 1555 2.11
LINK SG CYS A 56 ZN ZN A 200 1555 1555 2.15
LINK SG CYS B 21 ZN ZN B 200 1555 1555 2.18
LINK SG CYS B 24 ZN ZN B 200 1555 1555 2.30
LINK ND1 HIS B 53 ZN ZN B 200 1555 1555 2.27
LINK SG CYS B 56 ZN ZN B 200 1555 1555 2.12
LINK SG CYS C 21 ZN ZN C 200 1555 1555 2.26
LINK SG CYS C 24 ZN ZN C 200 1555 1555 2.36
LINK ND1 HIS C 53 ZN ZN C 200 1555 1555 2.12
LINK SG CYS C 56 ZN ZN C 200 1555 1555 2.19
LINK SG CYS D 21 ZN ZN D 200 1555 1555 2.19
LINK SG CYS D 24 ZN ZN D 200 1555 1555 2.33
LINK ND1 HIS D 53 ZN ZN D 200 1555 1555 2.19
LINK SG CYS D 56 ZN ZN D 200 1555 1555 2.21
LINK SG CYS E 21 ZN ZN E 200 1555 1555 2.30
LINK SG CYS E 24 ZN ZN E 200 1555 1555 2.17
LINK ND1 HIS E 53 ZN ZN E 200 1555 1555 2.09
LINK SG CYS E 56 ZN ZN E 200 1555 1555 2.24
LINK SG CYS F 21 ZN ZN F 200 1555 1555 2.19
LINK SG CYS F 24 ZN ZN F 200 1555 1555 2.37
LINK ND1 HIS F 53 ZN ZN F 200 1555 1555 2.11
LINK SG CYS F 56 ZN ZN F 200 1555 1555 2.22
LINK SG CYS G 21 ZN ZN G 200 1555 1555 2.31
LINK SG CYS G 24 ZN ZN G 200 1555 1555 2.28
LINK ND1 HIS G 53 ZN ZN G 200 1555 1555 2.00
LINK SG CYS G 56 ZN ZN G 200 1555 1555 2.15
LINK SG CYS H 21 ZN ZN H 200 1555 1555 2.15
LINK SG CYS H 24 ZN ZN H 200 1555 1555 2.34
LINK ND1 HIS H 53 ZN ZN H 200 1555 1555 2.08
LINK SG CYS H 56 ZN ZN H 200 1555 1555 2.16
SITE 1 AC1 4 CYS A 21 CYS A 24 HIS A 53 CYS A 56
SITE 1 AC2 4 CYS B 21 CYS B 24 HIS B 53 CYS B 56
SITE 1 AC3 4 CYS C 21 CYS C 24 HIS C 53 CYS C 56
SITE 1 AC4 4 CYS D 21 CYS D 24 HIS D 53 CYS D 56
SITE 1 AC5 4 CYS E 21 CYS E 24 HIS E 53 CYS E 56
SITE 1 AC6 4 CYS F 21 CYS F 24 HIS F 53 CYS F 56
SITE 1 AC7 4 CYS G 21 CYS G 24 HIS G 53 CYS G 56
SITE 1 AC8 4 CYS H 21 CYS H 24 HIS H 53 CYS H 56
CRYST1 62.812 107.334 86.998 90.00 100.61 90.00 P 1 21 1 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 0.015921 0.000000 0.002983 0.00000
SCALE2 0.000000 0.009317 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011695 0.00000
MTRIX1 1 0.991952 0.042233 0.119362 21.92130 1
MTRIX2 1 0.053830 -0.993957 -0.095665 93.54500 1
MTRIX3 1 0.114600 0.101321 -0.988231 76.98280 1
MTRIX1 2 0.990774 -0.016573 0.134504 -1.87424 1
MTRIX2 2 -0.001120 -0.993461 -0.114164 88.97620 1
MTRIX3 2 0.135516 0.112960 -0.984315 115.93600 1
MTRIX1 3 0.998634 -0.019534 -0.048460 45.68270 1
MTRIX2 3 0.020387 0.999645 0.017160 -11.55540 1
MTRIX3 3 0.048107 -0.018124 0.998678 -40.96580 1
MTRIX1 4 0.992906 -0.006149 0.118743 26.98810 1
MTRIX2 4 -0.020396 -0.992668 0.119137 84.34870 1
MTRIX3 4 0.117140 -0.120713 -0.985752 90.02240 1
MTRIX1 5 0.987538 0.035505 0.153321 -6.26136 1
MTRIX2 5 0.013307 -0.989569 0.143446 67.20540 1
MTRIX3 5 0.156815 -0.139618 -0.977710 127.36700 1
MTRIX1 6 0.998995 -0.012840 -0.042939 41.99480 1
MTRIX2 6 0.012574 0.999900 -0.006471 -9.41443 1
MTRIX3 6 0.043017 0.005925 0.999057 -43.10660 1
MTRIX1 7 -0.683511 -0.095243 0.723700 9.09951 1
MTRIX2 7 0.356998 -0.908401 0.217623 43.79700 1
MTRIX3 7 0.636683 0.407107 0.654903 -10.94090 1
MTRIX1 8 0.995769 -0.008054 0.091537 28.48330 1
MTRIX2 8 -0.018791 -0.992949 0.117045 84.28500 1
MTRIX3 8 0.089949 -0.118270 -0.988899 90.01200 1
MTRIX1 9 0.992458 0.026306 0.119730 -3.00526 1
MTRIX2 9 0.008147 -0.988698 0.149697 66.61850 1
MTRIX3 9 0.122314 -0.147592 -0.981456 128.67200 1
MTRIX1 10 0.998884 -0.030340 -0.036193 42.52590 1
MTRIX2 10 0.027916 0.997449 -0.065701 -4.50145 1
MTRIX3 10 0.038094 0.064617 0.997183 -46.69900 1
MTRIX1 11 0.998226 -0.058976 -0.008158 -17.42910 1
MTRIX2 11 0.059068 0.998186 0.011619 8.06851 1
MTRIX3 11 0.007458 -0.012080 0.999899 -41.61560 1
MTRIX1 12 0.966180 0.101086 0.237228 -12.92450 1
MTRIX2 12 0.077696 -0.991329 0.105976 92.26580 1
MTRIX3 12 0.245883 -0.083960 -0.965656 130.36700 1
(ATOM LINES ARE NOT SHOWN.)
END
