Header list of 1v9x.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSFERASE 04-FEB-04 1V9X TITLE SOLUTION STRUCTURE OF THE FIRST ZN-FINGER DOMAIN OF POLY(ADP-RIBOSE) TITLE 2 POLYMERASE-1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: POLY (ADP-RIBOSE) POLYMERASE; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: ZN-FINGER DOMAIN; COMPND 5 EC: 2.4.2.30; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA; SOURCE 3 ORGANISM_COMMON: THALE CRESS; SOURCE 4 ORGANISM_TAXID: 3702; SOURCE 5 GENE: RIKEN CDNA RAFL09-59-L22; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P021118-12; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS PARP, DNA REPAIR, INFLAMMATION, CELL DEATH, STRUCTURAL GENOMICS, KEYWDS 2 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, TRANSFERASE EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS AUTHOR 2 INITIATIVE (RSGI) REVDAT 3 02-MAR-22 1V9X 1 REMARK SEQADV LINK REVDAT 2 24-FEB-09 1V9X 1 VERSN REVDAT 1 22-FEB-05 1V9X 0 JRNL AUTH T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE FIRST 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), GUENTERT, P. (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1V9X COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-FEB-04. REMARK 100 THE DEPOSITION ID IS D_1000006390. 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 : 1.14MM ZF-PARP DOMAIN U-13C,15N; REMARK 210 20MM TRISHCL, 100MM NACL, 0.02% REMARK 210 NAN3, 0.1MM ZNCL2 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N 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 2002045, NMRVIEW 5.0.4, REMARK 210 KUJIRA 0.861, 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 : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS, TARGET REMARK 210 FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL 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 GLU A 14 146.65 -174.54 REMARK 500 1 ASP A 47 136.82 -173.30 REMARK 500 1 MET A 52 96.29 -66.12 REMARK 500 1 THR A 98 52.39 34.83 REMARK 500 1 SER A 108 43.02 37.10 REMARK 500 1 PRO A 111 2.41 -69.80 REMARK 500 1 SER A 112 120.90 -34.29 REMARK 500 2 GLU A 14 147.80 -173.19 REMARK 500 2 SER A 18 -179.20 -175.18 REMARK 500 2 LYS A 27 43.23 70.51 REMARK 500 2 ASP A 47 46.82 -83.80 REMARK 500 2 MET A 52 96.06 -65.92 REMARK 500 2 THR A 104 157.11 -39.27 REMARK 500 2 SER A 112 145.70 -172.93 REMARK 500 3 SER A 3 171.22 -52.40 REMARK 500 3 GLU A 14 149.92 -175.18 REMARK 500 3 SER A 19 40.36 -103.15 REMARK 500 3 SER A 43 -74.81 -125.61 REMARK 500 3 PHE A 46 48.30 -107.85 REMARK 500 3 MET A 52 96.87 -66.16 REMARK 500 3 SER A 92 -174.93 -53.95 REMARK 500 3 THR A 100 154.61 -38.16 REMARK 500 3 SER A 101 -61.55 -121.83 REMARK 500 3 SER A 113 99.13 -43.46 REMARK 500 4 SER A 6 -61.06 -95.79 REMARK 500 4 GLU A 14 145.04 -175.08 REMARK 500 4 LYS A 27 37.86 70.53 REMARK 500 4 MET A 52 96.34 -69.28 REMARK 500 4 ALA A 94 171.63 -46.58 REMARK 500 4 SER A 107 117.22 -164.45 REMARK 500 4 SER A 108 45.70 -98.51 REMARK 500 5 GLU A 14 147.88 -173.63 REMARK 500 5 SER A 19 33.67 -92.76 REMARK 500 5 THR A 44 38.28 -82.56 REMARK 500 5 PHE A 46 168.00 -47.52 REMARK 500 5 ASP A 47 106.59 -36.68 REMARK 500 5 MET A 52 97.11 -68.93 REMARK 500 5 SER A 92 -174.61 -51.58 REMARK 500 6 GLU A 14 147.61 -174.97 REMARK 500 6 SER A 19 34.95 -97.70 REMARK 500 6 THR A 44 90.49 -59.75 REMARK 500 6 PHE A 46 95.93 -63.28 REMARK 500 6 MET A 52 97.78 -67.98 REMARK 500 6 THR A 98 64.46 -102.16 REMARK 500 6 THR A 104 39.49 36.55 REMARK 500 6 SER A 109 -57.27 -128.84 REMARK 500 7 SER A 2 -61.42 -99.66 REMARK 500 7 SER A 19 36.70 -87.65 REMARK 500 7 SER A 43 40.34 -95.05 REMARK 500 7 THR A 44 39.15 33.96 REMARK 500 REMARK 500 THIS ENTRY HAS 130 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 23 SG REMARK 620 2 CYS A 26 SG 104.3 REMARK 620 3 HIS A 55 ND1 107.9 106.7 REMARK 620 4 CYS A 58 SG 110.8 110.4 116.0 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: ATR001011678 RELATED DB: TARGETDB DBREF 1V9X A 8 108 UNP Q9ZP54 PARP1_ARATH 5 105 SEQADV 1V9X GLY A 1 UNP Q9ZP54 CLONING ARTIFACT SEQADV 1V9X SER A 2 UNP Q9ZP54 CLONING ARTIFACT SEQADV 1V9X SER A 3 UNP Q9ZP54 CLONING ARTIFACT SEQADV 1V9X GLY A 4 UNP Q9ZP54 CLONING ARTIFACT SEQADV 1V9X SER A 5 UNP Q9ZP54 CLONING ARTIFACT SEQADV 1V9X SER A 6 UNP Q9ZP54 CLONING ARTIFACT SEQADV 1V9X GLY A 7 UNP Q9ZP54 CLONING ARTIFACT SEQADV 1V9X SER A 109 UNP Q9ZP54 CLONING ARTIFACT SEQADV 1V9X GLY A 110 UNP Q9ZP54 CLONING ARTIFACT SEQADV 1V9X PRO A 111 UNP Q9ZP54 CLONING ARTIFACT SEQADV 1V9X SER A 112 UNP Q9ZP54 CLONING ARTIFACT SEQADV 1V9X SER A 113 UNP Q9ZP54 CLONING ARTIFACT SEQADV 1V9X GLY A 114 UNP Q9ZP54 CLONING ARTIFACT SEQRES 1 A 114 GLY SER SER GLY SER SER GLY HIS LYS PRO TRP ARG ALA SEQRES 2 A 114 GLU TYR ALA LYS SER SER ARG SER SER CYS LYS THR CYS SEQRES 3 A 114 LYS SER VAL ILE ASN LYS GLU ASN PHE ARG LEU GLY LYS SEQRES 4 A 114 LEU VAL GLN SER THR HIS PHE ASP GLY ILE MET PRO MET SEQRES 5 A 114 TRP ASN HIS ALA SER CYS ILE LEU LYS LYS THR LYS GLN SEQRES 6 A 114 ILE LYS SER VAL ASP ASP VAL GLU GLY ILE GLU SER LEU SEQRES 7 A 114 ARG TRP GLU ASP GLN GLN LYS ILE ARG LYS TYR VAL GLU SEQRES 8 A 114 SER GLY ALA GLY SER ASN THR SER THR SER THR GLY THR SEQRES 9 A 114 SER THR SER SER SER GLY PRO SER SER GLY HET ZN A 200 1 HETNAM ZN ZINC ION FORMUL 2 ZN ZN 2+ HELIX 1 1 ALA A 56 LYS A 61 1 6 HELIX 2 2 SER A 68 ASP A 70 5 3 HELIX 3 3 ARG A 79 GLU A 91 1 13 SHEET 1 A 4 MET A 52 HIS A 55 0 SHEET 2 A 4 PHE A 35 LYS A 39 -1 N LEU A 37 O ASN A 54 SHEET 3 A 4 TRP A 11 TYR A 15 -1 N ARG A 12 O GLY A 38 SHEET 4 A 4 VAL A 72 GLU A 73 1 O GLU A 73 N ALA A 13 LINK SG CYS A 23 ZN ZN A 200 1555 1555 2.33 LINK SG CYS A 26 ZN ZN A 200 1555 1555 2.34 LINK ND1 HIS A 55 ZN ZN A 200 1555 1555 2.01 LINK SG CYS A 58 ZN ZN A 200 1555 1555 2.35 SITE 1 AC1 4 CYS A 23 CYS A 26 HIS A 55 CYS A 58 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 2 2 Bytes