Header list of 2cs2.pdb file
Complete list - r 9 2 Bytes
HEADER TRANSFERASE 20-MAY-05 2CS2
TITLE SOLUTION STRUCTURE OF THE SECOND ZN-FINGER DOMAIN OF POLY(ADP-RIBOSE)
TITLE 2 POLYMERASE-1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY [ADP-RIBOSE] POLYMERASE-1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ZF-PARP;
COMPND 5 SYNONYM: PARP-1, ADPRT, NAD+, ADP-RIBOSYLTRANSFERASE-1, POLY[ADP-
COMPND 6 RIBOSE] SYNTHETASE-1;
COMPND 7 EC: 2.4.2.30;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PARP1, ADPRT, PPOL;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040809-08;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS DNA BIND, DNA REPAIR, NECROSIS, APOPTOSIS, STRUCTURAL GENOMICS,
KEYWDS 2 NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL
KEYWDS 3 ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI,
KEYWDS 4 TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS
AUTHOR 2 INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2CS2 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 2CS2 1 VERSN
REVDAT 1 20-NOV-05 2CS2 0
JRNL AUTH T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE SECOND ZN-FINGER DOMAIN OF
JRNL TITL 2 POLY(ADP-RIBOSE) POLYMERASE-1
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1C, CYANA 2.0.17
REMARK 3 AUTHORS : VARIAN (VNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2CS2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 31-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024559.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM ZF-PARP DOMAIN U-13C,15N;
REMARK 210 20MM TRISHCL, 100MM NACL, 1MM
REMARK 210 DTT, 0.02% NAN3, 0.1MM ZNCL2; 90%
REMARK 210 H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20020425, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.901, CYANA 2.0.17
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION,STRUCTURES WITH
REMARK 210 THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 1 ASP A 17 -39.35 -38.26
REMARK 500 1 ALA A 23 92.31 -65.44
REMARK 500 1 ASN A 26 45.67 -95.30
REMARK 500 1 ASN A 71 33.63 -99.08
REMARK 500 1 LEU A 92 167.75 -47.46
REMARK 500 1 PRO A 105 2.53 -69.78
REMARK 500 1 LYS A 108 132.72 -172.41
REMARK 500 1 PRO A 131 -174.76 -69.82
REMARK 500 2 SER A 9 60.29 -119.74
REMARK 500 2 LYS A 13 43.72 -82.85
REMARK 500 2 ASN A 26 42.56 -82.58
REMARK 500 2 SER A 28 144.82 -37.91
REMARK 500 2 MET A 34 47.82 70.37
REMARK 500 2 LYS A 36 153.08 -49.35
REMARK 500 2 LYS A 87 105.52 -55.91
REMARK 500 2 LEU A 92 165.57 -48.06
REMARK 500 2 LYS A 114 156.36 -38.82
REMARK 500 2 LYS A 126 149.98 -171.64
REMARK 500 2 PRO A 131 -174.82 -69.79
REMARK 500 3 ASN A 26 48.14 -82.99
REMARK 500 3 SER A 28 157.85 -38.37
REMARK 500 3 LYS A 53 75.04 -114.37
REMARK 500 3 LEU A 104 76.88 -112.08
REMARK 500 3 LYS A 128 111.23 -36.17
REMARK 500 3 SER A 129 172.80 -48.27
REMARK 500 3 PRO A 131 -172.59 -69.79
REMARK 500 4 ALA A 11 42.17 -95.63
REMARK 500 4 ASN A 26 45.33 -81.53
REMARK 500 4 ASN A 71 31.94 -87.89
REMARK 500 4 ARG A 78 156.19 -49.41
REMARK 500 4 LEU A 92 166.05 -44.47
REMARK 500 4 LEU A 104 76.23 -109.75
REMARK 500 4 PRO A 105 3.03 -69.75
REMARK 500 4 ALA A 125 104.05 -42.53
REMARK 500 4 SER A 133 116.79 -172.95
REMARK 500 5 SER A 9 122.57 -170.34
REMARK 500 5 LYS A 13 42.32 -83.52
REMARK 500 5 ASN A 26 40.32 -82.53
REMARK 500 5 LEU A 86 109.01 -52.05
REMARK 500 5 LYS A 108 136.64 -170.41
REMARK 500 5 GLU A 110 39.80 -99.66
REMARK 500 5 PRO A 131 -174.25 -69.80
REMARK 500 6 GLU A 12 -34.79 -130.44
REMARK 500 6 ASN A 26 39.64 -84.06
REMARK 500 6 LEU A 92 172.24 -49.69
REMARK 500 6 THR A 94 -33.36 -34.05
REMARK 500 6 VAL A 107 157.04 -38.14
REMARK 500 6 ASP A 116 112.44 -165.40
REMARK 500 6 GLU A 123 44.95 -106.31
REMARK 500 6 VAL A 124 54.46 33.18
REMARK 500
REMARK 500 THIS ENTRY HAS 189 RAMACHANDRAN OUTLIERS.
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 30 SG
REMARK 620 2 CYS A 33 SG 104.1
REMARK 620 3 HIS A 64 ND1 107.2 108.2
REMARK 620 4 CYS A 67 SG 111.3 109.3 116.0
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 200
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSS001003531.4 RELATED DB: TARGETDB
DBREF 2CS2 A 8 128 UNP P09874 PARP1_HUMAN 102 222
SEQADV 2CS2 GLY A 1 UNP P09874 CLONING ARTIFACT
SEQADV 2CS2 SER A 2 UNP P09874 CLONING ARTIFACT
SEQADV 2CS2 SER A 3 UNP P09874 CLONING ARTIFACT
SEQADV 2CS2 GLY A 4 UNP P09874 CLONING ARTIFACT
SEQADV 2CS2 SER A 5 UNP P09874 CLONING ARTIFACT
SEQADV 2CS2 SER A 6 UNP P09874 CLONING ARTIFACT
SEQADV 2CS2 GLY A 7 UNP P09874 CLONING ARTIFACT
SEQADV 2CS2 SER A 129 UNP P09874 CLONING ARTIFACT
SEQADV 2CS2 GLY A 130 UNP P09874 CLONING ARTIFACT
SEQADV 2CS2 PRO A 131 UNP P09874 CLONING ARTIFACT
SEQADV 2CS2 SER A 132 UNP P09874 CLONING ARTIFACT
SEQADV 2CS2 SER A 133 UNP P09874 CLONING ARTIFACT
SEQADV 2CS2 GLY A 134 UNP P09874 CLONING ARTIFACT
SEQRES 1 A 134 GLY SER SER GLY SER SER GLY GLY SER LYS ALA GLU LYS
SEQRES 2 A 134 THR LEU GLY ASP PHE ALA ALA GLU TYR ALA LYS SER ASN
SEQRES 3 A 134 ARG SER THR CYS LYS GLY CYS MET GLU LYS ILE GLU LYS
SEQRES 4 A 134 GLY GLN VAL ARG LEU SER LYS LYS MET VAL ASP PRO GLU
SEQRES 5 A 134 LYS PRO GLN LEU GLY MET ILE ASP ARG TRP TYR HIS PRO
SEQRES 6 A 134 GLY CYS PHE VAL LYS ASN ARG GLU GLU LEU GLY PHE ARG
SEQRES 7 A 134 PRO GLU TYR SER ALA SER GLN LEU LYS GLY PHE SER LEU
SEQRES 8 A 134 LEU ALA THR GLU ASP LYS GLU ALA LEU LYS LYS GLN LEU
SEQRES 9 A 134 PRO GLY VAL LYS SER GLU GLY LYS ARG LYS GLY ASP GLU
SEQRES 10 A 134 VAL ASP GLY VAL ASP GLU VAL ALA LYS LYS LYS SER GLY
SEQRES 11 A 134 PRO SER SER GLY
HET ZN A 200 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 1 HIS A 64 ASN A 71 1 8
HELIX 2 2 SER A 82 SER A 84 5 3
HELIX 3 3 ALA A 93 LYS A 102 1 10
SHEET 1 A 4 MET A 58 TYR A 63 0
SHEET 2 A 4 VAL A 42 VAL A 49 -1 N LEU A 44 O TYR A 63
SHEET 3 A 4 LEU A 15 TYR A 22 -1 N GLU A 21 O ARG A 43
SHEET 4 A 4 LEU A 86 LYS A 87 1 O LYS A 87 N ALA A 20
LINK SG CYS A 30 ZN ZN A 200 1555 1555 2.35
LINK SG CYS A 33 ZN ZN A 200 1555 1555 2.28
LINK ND1 HIS A 64 ZN ZN A 200 1555 1555 2.05
LINK SG CYS A 67 ZN ZN A 200 1555 1555 2.31
SITE 1 AC1 4 CYS A 30 CYS A 33 HIS A 64 CYS A 67
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - r 9 2 Bytes