Header list of 1gcc.pdb file
Complete list - 23 20 Bytes
HEADER TRANSCRIPTION/DNA 13-MAR-98 1GCC
TITLE SOLUTION NMR STRUCTURE OF THE COMPLEX OF GCC-BOX BINDING DOMAIN OF
TITLE 2 ATERF1 AND GCC-BOX DNA, MINIMIZED AVERAGE STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA (5'-D(*TP*AP*GP*CP*CP*GP*CP*CP*AP*GP*C)-3');
COMPND 3 CHAIN: B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: DNA (5'-D(*GP*CP*TP*GP*GP*CP*GP*GP*CP*TP*A)-3');
COMPND 7 CHAIN: C;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: ETHYLENE RESPONSIVE ELEMENT BINDING FACTOR 1;
COMPND 11 CHAIN: A;
COMPND 12 FRAGMENT: GCC-BOX BINDING DOMAIN;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 SYNTHETIC: YES;
SOURCE 5 MOL_ID: 3;
SOURCE 6 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 7 ORGANISM_COMMON: THALE CRESS;
SOURCE 8 ORGANISM_TAXID: 3702;
SOURCE 9 CELL_LINE: BL21;
SOURCE 10 GENE: ATERF1;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 13 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 14 EXPRESSION_SYSTEM_PLASMID: PAF104;
SOURCE 15 OTHER_DETAILS: DNA-BINDING DOMAIN OF ATERF1
KEYWDS TRANSCRIPTION FACTOR, PROTEIN-DNA COMPLEX, ETHYLENE INDUCIBLE,
KEYWDS 2 COMPLEX (TRANSCRIPTION FACTOR-DNA), TRANSCRIPTION-DNA COMPLEX
EXPDTA SOLUTION NMR
AUTHOR K.YAMASAKI,M.D.ALLEN,M.OHME-TAKAGI,M.TATENO,M.SUZUKI
REVDAT 3 23-FEB-22 1GCC 1 REMARK LINK
REVDAT 2 24-FEB-09 1GCC 1 VERSN
REVDAT 1 23-MAR-99 1GCC 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 OTHER PROGRAMS USED:
REMARK 3 AMBER 4.1 AUTHORS: PEARLMAN,CASE,CALDWELL,ROSS,CHEATHAM III,
REMARK 3 FERGUSON,SEIBEL,SINGH,WEINER,KOLLMAN
REMARK 4
REMARK 4 1GCC 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_1000173514.
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, AMBER 4.1
REMARK 210 METHOD USED : SIMULATED ANNEALING PROTOCOL IN
REMARK 210 X-PLOR 3.1 WAS CARRIED OUT TO
REMARK 210 OBTAIN 25 STRUCTURES. MINIMIZED
REMARK 210 MEAN STRUCTURE OF THEM WAS
REMARK 210 FURTHER REVISED BY A 300 PS
REMARK 210 RESTRAINED MOLECULAR DYNAMICAL
REMARK 210 CALCULATION IN THE PRESENCE OF
REMARK 210 APPROXIMATELY 5000 TIP3P WATER
REMARK 210 MOLSCULES, USING CORNELL FORCE
REMARK 210 FIELD IN AMBER 4.1. THE MEAN CO-
REMARK 210 ORDINATE OF 200 STRUCTURES
REMARK 210 OBTAINED AFTER THE EQUILIBRIUM
REMARK 210 (100 PS) WAS ENERGY-MINIMIZED.
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 1
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
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
REMARK 210 PROTEIN. SIGNALS DUE TO DNA WERE OBTAINED BY NOESY, TOCSY, AND
REMARK 210 DQF-COSY FOR UNLABELED SAMPLE AND 13C,15N-FILTERED NOESY FOR
REMARK 210 SAMPLE WITH 13C, 15N-LABELED PROTEIN. INTERMOLECULAR NOES WERE
REMARK 210 IDENTIFIED USING NOESY SPECTRA INCLUDING THOSE WITH AND WITHOUT
REMARK 210 13C- OR 15N-DECOUPLING FOR SAMPLE WITH 13C,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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, 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: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 DC B 6 O4' - C4' - C3' ANGL. DEV. = 3.7 DEGREES
REMARK 500 DC B 10 O4' - C4' - C3' ANGL. DEV. = 3.7 DEGREES
REMARK 500 DC C 15 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DT C 16 O4' - C4' - C3' ANGL. DEV. = 4.0 DEGREES
REMARK 500 DG C 18 O4' - C1' - N9 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DG C 20 O4' - C1' - N9 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DC C 22 O4' - C4' - C3' ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG A 147 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG A 150 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG A 150 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 ARG A 197 74.04 51.83
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 DC B 7 0.07 SIDE CHAIN
REMARK 500 DT C 16 0.07 SIDE CHAIN
REMARK 500 DG C 17 0.06 SIDE CHAIN
REMARK 500 DC C 19 0.09 SIDE CHAIN
REMARK 500 DC C 22 0.07 SIDE CHAIN
REMARK 500 ARG A 147 0.14 SIDE CHAIN
REMARK 500 ARG A 170 0.08 SIDE CHAIN
REMARK 500 TYR A 186 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1GCC A 144 206 UNP O80337 ERF1A_ARATH 144 206
DBREF 1GCC B 3 13 PDB 1GCC 1GCC 3 13
DBREF 1GCC C 14 24 PDB 1GCC 1GCC 14 24
SEQRES 1 B 11 DT DA DG DC DC DG DC DC DA DG DC
SEQRES 1 C 11 DG DC DT DG DG DC DG DG DC DT DA
SEQRES 1 A 63 LYS HIS TYR ARG GLY VAL ARG GLN ARG PRO TRP GLY LYS
SEQRES 2 A 63 PHE ALA ALA GLU ILE ARG ASP PRO ALA LYS ASN GLY ALA
SEQRES 3 A 63 ARG VAL TRP LEU GLY THR PHE GLU THR ALA GLU ASP ALA
SEQRES 4 A 63 ALA LEU ALA TYR ASP ARG ALA ALA PHE ARG MET ARG GLY
SEQRES 5 A 63 SER ARG ALA LEU LEU ASN PHE PRO LEU ARG VAL
HELIX 1 1 ALA A 179 ARG A 194 1 16
SHEET 1 A 3 VAL A 149 ARG A 152 0
SHEET 2 A 3 LYS A 156 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
LINK C LYS A 144 N HIS A 145 1555 1555 1.34
LINK C HIS A 145 N TYR A 146 1555 1555 1.34
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 - 23 20 Bytes