Header list of 2gcc.pdb file
Complete list - 9 202 Bytes
HEADER TRANSCRIPTION FACTOR 13-MAR-98 2GCC
TITLE SOLUTION STRUCTURE OF THE GCC-BOX BINDING DOMAIN, NMR, MINIMIZED MEAN
TITLE 2 STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ATERF1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: GCC-BOX BINDING DOMAIN;
COMPND 5 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 CELL_LINE: BL21;
SOURCE 6 GENE: ATERF1;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PAF104;
SOURCE 11 OTHER_DETAILS: DNA-BINDING DOMAIN OF ATERF1
KEYWDS TRANSCRIPTION FACTOR, ETHLENE INDUCIBLE
EXPDTA SOLUTION NMR
AUTHOR M.D.ALLEN,K.YAMASAKI,M.OHME-TAKAGI,M.TATENO,M.SUZUKI
REVDAT 3 09-MAR-22 2GCC 1 REMARK
REVDAT 2 24-FEB-09 2GCC 1 VERSN
REVDAT 1 23-MAR-99 2GCC 0
JRNL AUTH M.D.ALLEN,K.YAMASAKI,M.OHME-TAKAGI,M.TATENO,M.SUZUKI
JRNL TITL A NOVEL MODE OF DNA RECOGNITION BY A BETA-SHEET REVEALED BY
JRNL TITL 2 THE SOLUTION STRUCTURE OF THE GCC-BOX BINDING DOMAIN IN
JRNL TITL 3 COMPLEX WITH DNA.
JRNL REF EMBO J. V. 17 5484 1998
JRNL REFN ISSN 0261-4189
JRNL PMID 9736626
JRNL DOI 10.1093/EMBOJ/17.18.5484
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: SEE REMARK 210
REMARK 4
REMARK 4 2GCC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000178126.
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 : 90 MM
REMARK 210 PRESSURE : 1 ATMOSPHERE
REMARK 210 SAMPLE CONTENTS : POTASIUM PHOSPHATE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; DQF-COSY; 1H-15N
REMARK 210 HSQC; 3D 1H-15N NOESY-HMQC; 3D
REMARK 210 1H-15N TOCSY-HMQC; 13C; 15N-
REMARK 210 FILTERED NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : DMX750; DMX500
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.1
REMARK 210 METHOD USED : SIMULATED ANEALING PROTOCOL IN X
REMARK 210 -PLOR 3.1 WAS CARRIED OUT TO
REMARK 210 OBTAIN 46 STRUCTURES.
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 1
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NO NOE VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: SIGNALS DUE TO PROTEINS WERE OBTAINED BY NOESY, TOCSY, DQF
REMARK 210 -COSY FOR UNLABELED SAMPLE AND 1H-15N HSQC, 3D 1H-15N NOESY-HMQC
REMARK 210 AND 3D 1H-15N TOCSY-HMQC FOR THE SAMPLE WITH 15N-LABELED PROTEIN.
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 RES C SSSEQI
REMARK 465 ALA A 141
REMARK 465 LYS A 142
REMARK 465 GLY A 143
REMARK 465 ASN A 207
REMARK 465 SER A 208
REMARK 465 GLY A 209
REMARK 465 GLU A 210
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 PRO A 153 35.16 -81.05
REMARK 500 TRP A 154 -33.63 -140.23
REMARK 500 LYS A 166 38.63 -93.78
REMARK 500 ARG A 197 141.32 55.14
REMARK 500 ARG A 205 44.10 -172.44
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 147 0.31 SIDE CHAIN
REMARK 500 ARG A 150 0.31 SIDE CHAIN
REMARK 500 ARG A 152 0.30 SIDE CHAIN
REMARK 500 ARG A 162 0.31 SIDE CHAIN
REMARK 500 ARG A 170 0.19 SIDE CHAIN
REMARK 500 ARG A 188 0.27 SIDE CHAIN
REMARK 500 ARG A 192 0.30 SIDE CHAIN
REMARK 500 ARG A 194 0.29 SIDE CHAIN
REMARK 500 ARG A 197 0.28 SIDE CHAIN
REMARK 500 ARG A 205 0.31 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2GCC A 141 210 UNP O80337 ERF1A_ARATH 141 210
SEQRES 1 A 70 ALA LYS GLY LYS HIS TYR ARG GLY VAL ARG GLN ARG PRO
SEQRES 2 A 70 TRP GLY LYS PHE ALA ALA GLU ILE ARG ASP PRO ALA LYS
SEQRES 3 A 70 ASN GLY ALA ARG VAL TRP LEU GLY THR PHE GLU THR ALA
SEQRES 4 A 70 GLU ASP ALA ALA LEU ALA TYR ASP ARG ALA ALA PHE ARG
SEQRES 5 A 70 MET ARG GLY SER ARG ALA LEU LEU ASN PHE PRO LEU ARG
SEQRES 6 A 70 VAL ASN SER GLY GLU
HELIX 1 1 ALA A 179 ARG A 192 1 14
SHEET 1 A 3 VAL A 149 GLN A 151 0
SHEET 2 A 3 PHE A 157 ASP A 163 -1 N ALA A 158 O ARG A 150
SHEET 3 A 3 ALA A 169 PHE A 176 -1 N PHE A 176 O PHE A 157
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
Complete list - 9 202 Bytes