Header list of 1wid.pdb file
Complete list - r 2 2 Bytes
HEADER DNA BINDING PROTEIN 28-MAY-04 1WID
TITLE SOLUTION STRUCTURE OF THE B3 DNA-BINDING DOMAIN OF RAV1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA-BINDING PROTEIN RAV1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: B3 DNA-BINDING DOMAIN;
COMPND 5 SYNONYM: TRANSCRIPTION FACTOR RAV1;
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: RAV1;
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 1WID 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1WID 1 VERSN
REVDAT 2 21-DEC-04 1WID 1 JRNL
REVDAT 1 28-NOV-04 1WID 0
JRNL AUTH K.YAMASAKI,T.KIGAWA,M.INOUE,M.TATENO,T.YAMASAKI,T.YABUKI,
JRNL AUTH 2 M.AOKI,E.SEKI,T.MATSUDA,Y.TOMO,N.HAYAMI,T.TERADA,M.SHIROUZU,
JRNL AUTH 3 T.OSANAI,A.TANAKA,M.SEKI,K.SHINOZAKI,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE B3 DNA BINDING DOMAIN OF THE
JRNL TITL 2 ARABIDOPSIS COLD-RESPONSIVE TRANSCRIPTION FACTOR RAV1
JRNL REF PLANT CELL V. 16 3448 2004
JRNL REFN ISSN 1040-4651
JRNL PMID 15548737
JRNL DOI 10.1105/TPC.104.026112
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 1WID 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_1000023612.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 500MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1MM RAV1-B3; 20MM KPI; 500MM
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 : 15
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 175
REMARK 465 SER A 176
REMARK 465 SER A 177
REMARK 465 GLY A 178
REMARK 465 SER A 179
REMARK 465 SER A 180
REMARK 465 GLY A 181
REMARK 465 SER A 299
REMARK 465 GLY A 300
REMARK 465 PRO A 301
REMARK 465 SER A 302
REMARK 465 SER A 303
REMARK 465 GLY A 304
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 PRO A 215 -168.73 -75.50
REMARK 500 1 SER A 218 34.65 -98.45
REMARK 500 1 SER A 219 -47.04 -144.42
REMARK 500 1 SER A 222 -70.72 -160.14
REMARK 500 1 VAL A 223 -43.75 -139.42
REMARK 500 1 LYS A 224 -178.05 -56.44
REMARK 500 1 ASN A 234 37.72 -94.48
REMARK 500 1 ASN A 246 90.01 43.69
REMARK 500 1 SER A 247 -63.36 70.82
REMARK 500 1 SER A 248 -57.55 170.40
REMARK 500 1 LYS A 255 128.25 63.52
REMARK 500 2 SER A 183 106.95 -161.94
REMARK 500 2 LEU A 187 -63.34 -91.04
REMARK 500 2 ASN A 201 124.18 63.71
REMARK 500 2 ARG A 202 122.56 -178.55
REMARK 500 2 HIS A 213 -71.85 -106.48
REMARK 500 2 PRO A 215 -167.82 -69.17
REMARK 500 2 PRO A 217 162.37 -49.43
REMARK 500 2 VAL A 221 -46.00 -157.96
REMARK 500 2 SER A 222 -49.01 -145.61
REMARK 500 2 ASN A 234 36.04 -93.60
REMARK 500 2 LYS A 255 118.86 61.13
REMARK 500 2 GLN A 280 66.75 60.35
REMARK 500 2 ASP A 281 160.60 59.90
REMARK 500 2 SER A 292 -48.04 -147.85
REMARK 500 3 SER A 183 -39.25 -178.10
REMARK 500 3 PRO A 206 174.48 -53.20
REMARK 500 3 ASN A 220 44.72 -93.31
REMARK 500 3 ASN A 234 33.23 -94.57
REMARK 500 3 ASN A 246 50.66 70.83
REMARK 500 3 SER A 247 -71.04 67.69
REMARK 500 3 SER A 248 28.22 -165.84
REMARK 500 3 GLN A 249 -65.13 -90.44
REMARK 500 3 LYS A 255 120.96 61.94
REMARK 500 3 GLN A 282 51.48 -90.13
REMARK 500 4 PRO A 194 81.47 -58.09
REMARK 500 4 SER A 195 -35.86 173.75
REMARK 500 4 PRO A 215 -159.31 -58.18
REMARK 500 4 SER A 219 139.28 64.48
REMARK 500 4 SER A 222 -49.59 -135.72
REMARK 500 4 ASN A 234 34.79 -94.30
REMARK 500 4 ASN A 246 92.20 45.09
REMARK 500 4 SER A 248 -58.98 70.98
REMARK 500 4 LYS A 255 97.04 57.64
REMARK 500 4 SER A 275 -169.54 -117.91
REMARK 500 4 SER A 290 101.86 -160.07
REMARK 500 4 SER A 292 -50.16 -147.22
REMARK 500 5 SER A 183 112.58 61.14
REMARK 500 5 ASN A 201 84.47 61.64
REMARK 500 5 PRO A 206 172.67 -52.78
REMARK 500
REMARK 500 THIS ENTRY HAS 233 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: ATR001006482.1 RELATED DB: TARGETDB
DBREF 1WID A 182 298 UNP Q9ZWM9 RAV1_ARATH 182 298
SEQADV 1WID GLY A 175 UNP Q9ZWM9 CLONING ARTIFACT
SEQADV 1WID SER A 176 UNP Q9ZWM9 CLONING ARTIFACT
SEQADV 1WID SER A 177 UNP Q9ZWM9 CLONING ARTIFACT
SEQADV 1WID GLY A 178 UNP Q9ZWM9 CLONING ARTIFACT
SEQADV 1WID SER A 179 UNP Q9ZWM9 CLONING ARTIFACT
SEQADV 1WID SER A 180 UNP Q9ZWM9 CLONING ARTIFACT
SEQADV 1WID GLY A 181 UNP Q9ZWM9 CLONING ARTIFACT
SEQADV 1WID SER A 299 UNP Q9ZWM9 CLONING ARTIFACT
SEQADV 1WID GLY A 300 UNP Q9ZWM9 CLONING ARTIFACT
SEQADV 1WID PRO A 301 UNP Q9ZWM9 CLONING ARTIFACT
SEQADV 1WID SER A 302 UNP Q9ZWM9 CLONING ARTIFACT
SEQADV 1WID SER A 303 UNP Q9ZWM9 CLONING ARTIFACT
SEQADV 1WID GLY A 304 UNP Q9ZWM9 CLONING ARTIFACT
SEQRES 1 A 130 GLY SER SER GLY SER SER GLY ARG SER ALA GLU ALA LEU
SEQRES 2 A 130 PHE GLU LYS ALA VAL THR PRO SER ASP VAL GLY LYS LEU
SEQRES 3 A 130 ASN ARG LEU VAL ILE PRO LYS HIS HIS ALA GLU LYS HIS
SEQRES 4 A 130 PHE PRO LEU PRO SER SER ASN VAL SER VAL LYS GLY VAL
SEQRES 5 A 130 LEU LEU ASN PHE GLU ASP VAL ASN GLY LYS VAL TRP ARG
SEQRES 6 A 130 PHE ARG TYR SER TYR TRP ASN SER SER GLN SER TYR VAL
SEQRES 7 A 130 LEU THR LYS GLY TRP SER ARG PHE VAL LYS GLU LYS ASN
SEQRES 8 A 130 LEU ARG ALA GLY ASP VAL VAL SER PHE SER ARG SER ASN
SEQRES 9 A 130 GLY GLN ASP GLN GLN LEU TYR ILE GLY TRP LYS SER ARG
SEQRES 10 A 130 SER GLY SER ASP LEU ASP ALA SER GLY PRO SER SER GLY
HELIX 1 1 PRO A 206 GLU A 211 1 6
HELIX 2 2 GLY A 256 LYS A 264 1 9
SHEET 1 A 7 GLU A 185 ALA A 191 0
SHEET 2 A 7 VAL A 271 ARG A 276 -1 O VAL A 272 N LYS A 190
SHEET 3 A 7 LEU A 284 LYS A 289 -1 O GLY A 287 N SER A 273
SHEET 4 A 7 VAL A 226 ASP A 232 1 N ASN A 229 O LEU A 284
SHEET 5 A 7 LYS A 236 TRP A 245 -1 O TYR A 242 N VAL A 226
SHEET 6 A 7 SER A 250 THR A 254 -1 O SER A 250 N TRP A 245
SHEET 7 A 7 LEU A 203 ILE A 205 -1 N ILE A 205 O TYR A 251
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