Header list of 1wj0.pdb file
Complete list - r 2 2 Bytes
HEADER DNA BINDING PROTEIN 28-MAY-04 1WJ0 TITLE SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN OF SQUAMOSA PROMOTER TITLE 2 BINDING PROTEIN-LIKE 12 LACKING THE SECOND ZINC-BINDING SITE COMPND MOL_ID: 1; COMPND 2 MOLECULE: SQUAMOSA PROMOTER-BINDING PROTEIN-LIKE 12; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: DNA-BINDING DOMAIN (SHORT FRAGMENT); COMPND 5 SYNONYM: SPL12, TRANSCRIPTION FACTOR SPL12; 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: SPL12; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PCR2.1; SOURCE 8 OTHER_DETAILS: CELL-FREE SYNTHESIS KEYWDS DNA-BINDING DOMAIN, STRUCTURAL GENOMICS, RIKEN STRUCTURAL KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, DNA BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR K.YAMASAKI,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN STRUCTURAL AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 4 02-MAR-22 1WJ0 1 REMARK SEQADV LINK REVDAT 3 24-FEB-09 1WJ0 1 VERSN REVDAT 2 21-DEC-04 1WJ0 1 JRNL REVDAT 1 28-NOV-04 1WJ0 0 JRNL AUTH K.YAMASAKI,T.KIGAWA,M.INOUE,T.YAMASAKI,T.YABUKI,M.AOKI, JRNL AUTH 2 E.SEKI,T.MATSUDA,Y.TOMO,T.TERADA,M.SHIROUZU,A.TANAKA,M.SEKI, JRNL AUTH 3 K.SHINOZAKI,S.YOKOYAMA JRNL TITL STRUCTURE OF THE SBP DOMAIN THAT LACKS THE SECOND JRNL TITL 2 ZINC-BINDING SITE JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : FELIX 2000, CNS 1.1 REMARK 3 AUTHORS : MSI (FELIX), REMARK 3 BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI, REMARK 3 NILGES, PANNU,READ,RICE,SIMONSON,WARREN (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1WJ0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-JUN-04. REMARK 100 THE DEPOSITION ID IS D_1000023630. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 293 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : 0.3M REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 1MM SPL12-DBD FRAGMENT; 20MM REMARK 210 KPI; 300MM KCL; 0.02MM ZNCL2; REMARK 210 1MM DTT; 95% H2O; 5% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ REMARK 210 SPECTROMETER MODEL : DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : CNS 1.1 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 9 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 MODELS 1-20 REMARK 465 RES C SSSEQI REMARK 465 GLY A 122 REMARK 465 SER A 123 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 141 -174.84 -175.90 REMARK 500 1 TYR A 142 -67.51 68.55 REMARK 500 1 LYS A 147 86.99 50.20 REMARK 500 1 VAL A 148 136.65 -178.63 REMARK 500 1 ILE A 151 -70.01 -62.29 REMARK 500 1 SER A 172 69.58 62.08 REMARK 500 1 ARG A 173 149.20 -175.06 REMARK 500 1 LEU A 177 38.61 -95.98 REMARK 500 2 CYS A 132 -66.89 -159.78 REMARK 500 2 LYS A 138 38.31 -96.39 REMARK 500 2 LYS A 140 -79.73 -98.12 REMARK 500 2 TYR A 142 -65.44 69.41 REMARK 500 2 ARG A 144 -61.79 -152.19 REMARK 500 2 LYS A 147 81.39 64.85 REMARK 500 2 VAL A 148 133.24 -178.91 REMARK 500 2 ILE A 151 -68.45 -104.41 REMARK 500 2 VAL A 176 179.38 -51.79 REMARK 500 2 LEU A 177 30.60 -96.77 REMARK 500 3 LYS A 140 -78.18 -75.44 REMARK 500 3 ASP A 141 -42.10 -167.63 REMARK 500 3 HIS A 143 34.45 -99.75 REMARK 500 3 ARG A 144 -63.18 -124.58 REMARK 500 3 LYS A 147 64.41 61.49 REMARK 500 3 CYS A 149 -167.53 -67.56 REMARK 500 4 LEU A 136 50.47 -91.49 REMARK 500 4 VAL A 139 173.13 -57.31 REMARK 500 4 LYS A 140 -74.07 -71.27 REMARK 500 4 ASP A 141 -41.91 -169.71 REMARK 500 4 HIS A 143 37.62 -98.82 REMARK 500 4 ARG A 144 -64.86 -130.40 REMARK 500 4 LYS A 154 30.16 -148.49 REMARK 500 4 VAL A 176 174.38 -49.17 REMARK 500 4 LEU A 177 40.56 -95.35 REMARK 500 5 LEU A 136 45.11 -107.72 REMARK 500 5 LYS A 138 41.36 -107.22 REMARK 500 5 LYS A 140 -82.71 -68.16 REMARK 500 5 ASP A 141 -43.85 178.39 REMARK 500 5 SER A 172 70.03 59.92 REMARK 500 5 ARG A 173 133.60 -176.54 REMARK 500 5 VAL A 176 178.76 -53.86 REMARK 500 5 GLU A 178 31.57 -99.83 REMARK 500 5 GLU A 179 -43.09 -164.86 REMARK 500 5 PHE A 180 105.20 -59.21 REMARK 500 6 GLN A 128 40.94 -94.64 REMARK 500 6 LYS A 138 32.00 -96.69 REMARK 500 6 ASP A 141 -177.77 -174.44 REMARK 500 6 HIS A 143 -45.41 -161.80 REMARK 500 6 LYS A 147 75.66 66.24 REMARK 500 6 VAL A 148 134.76 -179.40 REMARK 500 6 HIS A 152 33.72 -96.40 REMARK 500 REMARK 500 THIS ENTRY HAS 191 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 182 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 127 SG REMARK 620 2 CYS A 132 SG 107.2 REMARK 620 3 CYS A 149 SG 111.3 111.4 REMARK 620 4 HIS A 152 ND1 112.2 108.4 106.4 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 182 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: ATR001004282.1 RELATED DB: TARGETDB DBREF 1WJ0 A 124 181 UNP Q9S7P5 SPL12_ARATH 124 181 SEQADV 1WJ0 GLY A 122 UNP Q9S7P5 CLONING ARTIFACT SEQADV 1WJ0 SER A 123 UNP Q9S7P5 CLONING ARTIFACT SEQRES 1 A 60 GLY SER ALA ILE CYS CYS GLN VAL ASP ASN CYS GLY ALA SEQRES 2 A 60 ASP LEU SER LYS VAL LYS ASP TYR HIS ARG ARG HIS LYS SEQRES 3 A 60 VAL CYS GLU ILE HIS SER LYS ALA THR THR ALA LEU VAL SEQRES 4 A 60 GLY GLY ILE MET GLN ARG PHE CYS GLN GLN CYS SER ARG SEQRES 5 A 60 PHE HIS VAL LEU GLU GLU PHE ASP HET ZN A 182 1 HETNAM ZN ZINC ION FORMUL 2 ZN ZN 2+ HELIX 1 1 CYS A 149 LYS A 154 1 6 SHEET 1 A 2 ILE A 125 CYS A 126 0 SHEET 2 A 2 ASP A 135 LEU A 136 -1 O LEU A 136 N ILE A 125 SHEET 1 B 2 ALA A 158 VAL A 160 0 SHEET 2 B 2 ILE A 163 GLN A 165 -1 O GLN A 165 N ALA A 158 LINK SG CYS A 127 ZN ZN A 182 1555 1555 2.47 LINK SG CYS A 132 ZN ZN A 182 1555 1555 2.47 LINK SG CYS A 149 ZN ZN A 182 1555 1555 2.47 LINK ND1 HIS A 152 ZN ZN A 182 1555 1555 2.14 SITE 1 AC1 4 CYS A 127 CYS A 132 CYS A 149 HIS A 152 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