Header list of 1fv5.pdb file
Complete list - 23 20 Bytes
HEADER TRANSCRIPTION 18-SEP-00 1FV5
TITLE SOLUTION STRUCTURE OF THE FIRST ZINC FINGER FROM THE DROSOPHILA U-
TITLE 2 SHAPED TRANSCRIPTION FACTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FIRST ZINC FINGER OF U-SHAPED;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: FIRST ZINC FINGER DOMAIN (RESIDUES 202-235);
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 3 ORGANISM_COMMON: FRUIT FLY;
SOURCE 4 ORGANISM_TAXID: 7227;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PGEX-2T
KEYWDS ZINC FINGER, CCHC, PROTEIN INTERACTION, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR C.K.LIEW,K.KOWALSKI,A.H.FOX,A.NEWTON,B.K.SHARPE,M.CROSSLEY,J.P.MACKAY
REVDAT 4 23-FEB-22 1FV5 1 REMARK LINK
REVDAT 3 24-FEB-09 1FV5 1 VERSN
REVDAT 2 10-JAN-01 1FV5 1 JRNL
REVDAT 1 04-OCT-00 1FV5 0
JRNL AUTH C.K.LIEW,K.KOWALSKI,A.H.FOX,A.NEWTON,B.K.SHARPE,M.CROSSLEY,
JRNL AUTH 2 J.P.MACKAY
JRNL TITL SOLUTION STRUCTURES OF TWO CCHC ZINC FINGERS FROM THE FOG
JRNL TITL 2 FAMILY PROTEIN U-SHAPED THAT MEDIATE PROTEIN-PROTEIN
JRNL TITL 3 INTERACTIONS.
JRNL REF STRUCTURE FOLD.DES. V. 8 1157 2000
JRNL REFN ISSN 0969-2126
JRNL PMID 11080638
JRNL DOI 10.1016/S0969-2126(00)00527-X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CNS 1.0
REMARK 3 AUTHORS : GUENTHER (XWINNMR), WARREN, NILGES, KUSZEWSKI,
REMARK 3 CLORE, BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 356 RESTRAINTS, 324 ARE NOE-DERIVED DISTANCE CONSTRAINTS AND 32
REMARK 3 ARE DIHEDRAL ANGLE RESTRAINTS
REMARK 4
REMARK 4 1FV5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-SEP-00.
REMARK 100 THE DEPOSITION ID IS D_1000011927.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : 0
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.7MM U-SHAPED FIRST FINGER; 95%
REMARK 210 H2O, 5% D2O; 0.7MM U-SHAPED
REMARK 210 FIRST FINGER 15N-LABELLED; 95%
REMARK 210 H2O, 5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; HNHA; HNHB
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.2, DYANA 1.5
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING CARTESIAN DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 500
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 : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING 2D HOMONUCLEAR AND
REMARK 210 HETERONUCLEAR TECHNIQUES ON UNLABELLED AND 15N-LABELLED PEPTIDE.
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 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 37 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 11 SG
REMARK 620 2 CYS A 14 SG 110.2
REMARK 620 3 HIS A 27 NE2 110.0 109.8
REMARK 620 4 CYS A 32 SG 108.8 110.1 107.9
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 37
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FU9 RELATED DB: PDB
REMARK 900 1FU9 CONTAINS THE NINTH ZINC FINGER OF U-SHAPED
DBREF 1FV5 A 3 36 UNP Q9VPQ6 USH_DROME 186 219
SEQADV 1FV5 GLY A 1 UNP Q9VPQ6 CLONING ARTIFACT
SEQADV 1FV5 SER A 2 UNP Q9VPQ6 CLONING ARTIFACT
SEQRES 1 A 36 GLY SER LEU LEU LYS PRO ALA ARG PHE MET CYS LEU PRO
SEQRES 2 A 36 CYS GLY ILE ALA PHE SER SER PRO SER THR LEU GLU ALA
SEQRES 3 A 36 HIS GLN ALA TYR TYR CYS SER HIS ARG ILE
HET ZN A 37 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 1 SER A 20 TYR A 31 1 12
LINK SG CYS A 11 ZN ZN A 37 1555 1555 2.30
LINK SG CYS A 14 ZN ZN A 37 1555 1555 2.30
LINK NE2 HIS A 27 ZN ZN A 37 1555 1555 2.00
LINK SG CYS A 32 ZN ZN A 37 1555 1555 2.30
SITE 1 AC1 4 CYS A 11 CYS A 14 HIS A 27 CYS A 32
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 - 23 20 Bytes