Header list of 1wij.pdb file
Complete list - r 2 2 Bytes
HEADER DNA BINDING PROTEIN 28-MAY-04 1WIJ
TITLE SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN OF ETHYLENE-INSENSITIVE3-
TITLE 2 LIKE3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ETHYLENE-INSENSITIVE3-LIKE 3 PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DNA-BINDING DOMAIN;
COMPND 5 SYNONYM: TRANSCRIPTION FACTOR EIL3;
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: EIL3;
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 5 02-MAR-22 1WIJ 1 REMARK SEQADV
REVDAT 4 24-FEB-09 1WIJ 1 VERSN
REVDAT 3 05-JUL-05 1WIJ 1 JRNL
REVDAT 2 21-DEC-04 1WIJ 1 JRNL
REVDAT 1 28-NOV-04 1WIJ 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 SOLUTION STRUCTURE OF THE MAJOR DNA-BINDING DOMAIN OF
JRNL TITL 2 ARABIDOPSIS THALIANA ETHYLENE-INSENSITIVE3-LIKE3.
JRNL REF J.MOL.BIOL. V. 348 253 2005
JRNL REFN ISSN 0022-2836
JRNL PMID 15811366
JRNL DOI 10.1016/J.JMB.2005.02.065
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : FELIX 2000, CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE
REMARK 3 -KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE,
REMARK 3 SIMONSON,WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WIJ 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_1000023618.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 200MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1MM EIL3-DBD; 20MM KPI; 200MM
REMARK 210 KCL; 95% H2O; 5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_NOESY; DQF-COSY; HMQC-J
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 500 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 : 17
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 155
REMARK 465 SER A 156
REMARK 465 SER A 157
REMARK 465 GLY A 158
REMARK 465 SER A 159
REMARK 465 SER A 160
REMARK 465 GLY A 161
REMARK 465 SER A 289
REMARK 465 GLY A 290
REMARK 465 PRO A 291
REMARK 465 SER A 292
REMARK 465 SER A 293
REMARK 465 GLY A 294
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 MET A 182 63.30 -107.77
REMARK 500 1 GLN A 183 -38.26 -170.08
REMARK 500 1 GLN A 189 43.81 -90.39
REMARK 500 1 PRO A 193 170.96 -46.38
REMARK 500 1 LYS A 196 -63.63 -90.24
REMARK 500 1 TRP A 202 74.94 -170.22
REMARK 500 1 ASN A 207 33.71 -164.77
REMARK 500 1 PRO A 217 103.49 -52.08
REMARK 500 1 GLN A 220 53.96 -152.20
REMARK 500 1 PRO A 223 -176.71 -64.75
REMARK 500 1 ARG A 225 -167.17 -125.99
REMARK 500 1 ASP A 229 38.68 -96.84
REMARK 500 1 ASP A 249 65.64 -115.39
REMARK 500 1 SER A 260 173.93 -59.73
REMARK 500 1 LEU A 263 -43.48 -153.44
REMARK 500 1 ALA A 269 -55.22 -172.67
REMARK 500 1 GLN A 287 -78.06 -71.37
REMARK 500 2 GLN A 183 -42.29 -170.15
REMARK 500 2 GLN A 189 30.88 -90.40
REMARK 500 2 LYS A 191 31.27 -163.33
REMARK 500 2 PRO A 193 171.35 -46.11
REMARK 500 2 LYS A 196 -68.78 -90.27
REMARK 500 2 TRP A 202 72.40 -170.70
REMARK 500 2 ASN A 207 51.47 -145.94
REMARK 500 2 GLN A 220 57.78 -152.23
REMARK 500 2 PRO A 223 -178.65 -60.76
REMARK 500 2 ASP A 249 57.50 -103.86
REMARK 500 2 MET A 267 46.48 -108.83
REMARK 500 2 ALA A 269 -166.21 -173.61
REMARK 500 2 ILE A 286 -67.53 -90.01
REMARK 500 3 GLN A 163 101.48 60.58
REMARK 500 3 PRO A 188 -178.71 -53.26
REMARK 500 3 ARG A 190 50.72 -90.05
REMARK 500 3 LYS A 191 -45.33 -147.51
REMARK 500 3 PRO A 193 -178.60 -50.73
REMARK 500 3 TRP A 202 77.12 -170.35
REMARK 500 3 ASN A 207 65.50 -105.20
REMARK 500 3 GLN A 220 56.20 -151.65
REMARK 500 3 PRO A 223 173.29 -58.30
REMARK 500 3 ASP A 249 57.96 -111.47
REMARK 500 3 CYS A 262 -39.11 -177.80
REMARK 500 3 ASP A 265 -43.58 -166.49
REMARK 500 3 LYS A 266 31.23 -153.04
REMARK 500 3 MET A 267 30.67 -98.71
REMARK 500 3 ALA A 269 -167.94 -105.95
REMARK 500 4 PRO A 193 -166.25 -56.12
REMARK 500 4 LEU A 194 -54.69 -127.12
REMARK 500 4 TRP A 202 75.63 -170.58
REMARK 500 4 ASN A 207 42.71 -170.03
REMARK 500 4 GLN A 220 54.99 -143.53
REMARK 500
REMARK 500 THIS ENTRY HAS 252 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: ATR001003609.1 RELATED DB: TARGETDB
DBREF 1WIJ A 162 288 UNP O23116 EIL3_ARATH 162 288
SEQADV 1WIJ GLY A 155 UNP O23116 CLONING ARTIFACT
SEQADV 1WIJ SER A 156 UNP O23116 CLONING ARTIFACT
SEQADV 1WIJ SER A 157 UNP O23116 CLONING ARTIFACT
SEQADV 1WIJ GLY A 158 UNP O23116 CLONING ARTIFACT
SEQADV 1WIJ SER A 159 UNP O23116 CLONING ARTIFACT
SEQADV 1WIJ SER A 160 UNP O23116 CLONING ARTIFACT
SEQADV 1WIJ GLY A 161 UNP O23116 CLONING ARTIFACT
SEQADV 1WIJ SER A 289 UNP O23116 CLONING ARTIFACT
SEQADV 1WIJ GLY A 290 UNP O23116 CLONING ARTIFACT
SEQADV 1WIJ PRO A 291 UNP O23116 CLONING ARTIFACT
SEQADV 1WIJ SER A 292 UNP O23116 CLONING ARTIFACT
SEQADV 1WIJ SER A 293 UNP O23116 CLONING ARTIFACT
SEQADV 1WIJ GLY A 294 UNP O23116 CLONING ARTIFACT
SEQRES 1 A 140 GLY SER SER GLY SER SER GLY SER GLN PHE VAL LEU GLN
SEQRES 2 A 140 ASP LEU GLN ASP ALA THR LEU GLY SER LEU LEU SER SER
SEQRES 3 A 140 LEU MET GLN HIS CYS ASP PRO PRO GLN ARG LYS TYR PRO
SEQRES 4 A 140 LEU GLU LYS GLY THR PRO PRO PRO TRP TRP PRO THR GLY
SEQRES 5 A 140 ASN GLU GLU TRP TRP VAL LYS LEU GLY LEU PRO LYS SER
SEQRES 6 A 140 GLN SER PRO PRO TYR ARG LYS PRO HIS ASP LEU LYS LYS
SEQRES 7 A 140 MET TRP LYS VAL GLY VAL LEU THR ALA VAL ILE ASN HIS
SEQRES 8 A 140 MET LEU PRO ASP ILE ALA LYS ILE LYS ARG HIS VAL ARG
SEQRES 9 A 140 GLN SER LYS CYS LEU GLN ASP LYS MET THR ALA LYS GLU
SEQRES 10 A 140 SER ALA ILE TRP LEU ALA VAL LEU ASN GLN GLU GLU SER
SEQRES 11 A 140 LEU ILE GLN GLN SER GLY PRO SER SER GLY
HELIX 1 1 GLN A 170 MET A 182 1 13
HELIX 2 2 THR A 198 TRP A 203 1 6
HELIX 3 3 GLU A 208 GLY A 215 1 8
HELIX 4 4 LYS A 226 LEU A 230 5 5
HELIX 5 5 LYS A 231 MET A 246 1 16
HELIX 6 6 ASP A 249 HIS A 256 1 8
HELIX 7 7 ALA A 269 ASN A 280 1 12
CISPEP 1 ASP A 186 PRO A 187 1 0.00
CISPEP 2 ASP A 186 PRO A 187 2 -0.05
CISPEP 3 ASP A 186 PRO A 187 3 -0.12
CISPEP 4 ASP A 186 PRO A 187 4 -0.02
CISPEP 5 ASP A 186 PRO A 187 5 0.31
CISPEP 6 ASP A 186 PRO A 187 6 0.11
CISPEP 7 ASP A 186 PRO A 187 7 0.02
CISPEP 8 ASP A 186 PRO A 187 8 -0.08
CISPEP 9 ASP A 186 PRO A 187 9 0.12
CISPEP 10 ASP A 186 PRO A 187 10 0.03
CISPEP 11 ASP A 186 PRO A 187 11 -0.04
CISPEP 12 ASP A 186 PRO A 187 12 -0.07
CISPEP 13 ASP A 186 PRO A 187 13 -0.11
CISPEP 14 ASP A 186 PRO A 187 14 0.17
CISPEP 15 ASP A 186 PRO A 187 15 0.11
CISPEP 16 ASP A 186 PRO A 187 16 0.12
CISPEP 17 ASP A 186 PRO A 187 17 0.05
CISPEP 18 ASP A 186 PRO A 187 18 0.13
CISPEP 19 ASP A 186 PRO A 187 19 0.02
CISPEP 20 ASP A 186 PRO A 187 20 -0.05
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