Header list of 2ezd.pdb file
Complete list - 9 20 Bytes
HEADER DNA BINDING PROTEIN/DNA 04-JUN-97 2EZD
TITLE SOLUTION STRUCTURE OF A COMPLEX OF THE SECOND DNA BINDING DOMAIN OF
TITLE 2 HUMAN HMG-I(Y) BOUND TO DNA DODECAMER CONTAINING THE PRDII SITE OF
TITLE 3 THE INTERFERON-BETA PROMOTER, NMR, MINIMIZED AVERAGE STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA (5'-D(*GP*GP*GP*AP*AP*AP*TP*TP*CP*CP*TP*C)-3');
COMPND 3 CHAIN: B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: DNA (5'-D(*GP*AP*GP*GP*AP*AP*TP*TP*TP*CP*CP*C)-3');
COMPND 7 CHAIN: C;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: HIGH MOBILITY GROUP PROTEIN HMG-I/HMG-Y;
COMPND 11 CHAIN: A;
COMPND 12 SYNONYM: HIGH MOBILITY GROUP PROTEIN HMG;
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: HOMO SAPIENS;
SOURCE 7 ORGANISM_COMMON: HUMAN;
SOURCE 8 ORGANISM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DNA BINDING PROTEIN, MINOR GROOVE DNA BINDING, TRANSCRIPTIONAL CO-
KEYWDS 2 ACTIVATOR, ARCHITECTURAL FACTOR, COMPLEX (DNA-BINDING PROTEIN-DNA),
KEYWDS 3 DNA BINDING PROTEIN-DNA COMPLEX
EXPDTA SOLUTION NMR
AUTHOR G.M.CLORE,J.R.HUTH,C.BEWLEY,A.M.GRONENBORN
REVDAT 3 09-MAR-22 2EZD 1 REMARK
REVDAT 2 24-FEB-09 2EZD 1 VERSN
REVDAT 1 15-OCT-97 2EZD 0
JRNL AUTH J.R.HUTH,C.A.BEWLEY,M.S.NISSEN,J.N.EVANS,R.REEVES,
JRNL AUTH 2 A.M.GRONENBORN,G.M.CLORE
JRNL TITL THE SOLUTION STRUCTURE OF AN HMG-I(Y)-DNA COMPLEX DEFINES A
JRNL TITL 2 NEW ARCHITECTURAL MINOR GROOVE BINDING MOTIF.
JRNL REF NAT.STRUCT.BIOL. V. 4 657 1997
JRNL REFN ISSN 1072-8368
JRNL PMID 9253416
JRNL DOI 10.1038/NSB0897-657
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:
REMARK 3 THE STRUCTURES WERE CALCULATED USING THE SIMULATED
REMARK 3 ANNEALING PROTOCOL OF NILGES ET AL. (1988) FEBS LETT.
REMARK 3 229, 129 - 136 USING THE PROGRAM X-PLOR 3.1 (BRUNGER)
REMARK 3 MODIFIED TO INCORPORATE COUPLING CONSTANT (GARRETT ET AL.
REMARK 3 (1984) J. MAGN RESON. SERIES B 104, 99 - 103), CARBON
REMARK 3 CHEMICAL SHIFT (KUSZEWSKI ET AL. (1995) J. MAGN. RESON.
REMARK 3 SERIES B 106, 92 - 96) RESTRAINTS AND A CONFORMATIONAL
REMARK 3 DATABASE
REMARK 3 POTENTIAL (KUSZEWSKI ET AL. (1996) PROTEIN SCI 5, 1067 -
REMARK 3 1080
REMARK 3 AND (1997) J. MAGN. RESON. 125, 171-177)
REMARK 3 THE 3D STRUCTURE OF THE COMPLEX OF THE SECOND DNA BINDING
REMARK 3 DOMAIN OF HMG-I(Y)
REMARK 3 COMPLEXED TO DNA WAS SOLVED BY
REMARK 3 MULTI-DIMENSIONAL HETERONUCLEAR-EDITED AND -FILTERED NMR
REMARK 3 (A) PROTEIN: 71 SEQUENTIAL (|I-J|=1), 4 MEDIUM
REMARK 3 RANGE (1 < |I-J| >=5) AND 64 INTRARESIDUE
REMARK 3 APPROXIMATE INTERPROTON DISTANCE RESTRAINTS; NULL
REMARK 3 36 TORSION ANGLE RESTRAINTS
REMARK 3 13 THREE-BOND HN-HA AND 8 THREE_BOND COCO COUPLING
REMARK 3 CONSTANT RESTRAINTS; 39 (21 CALPHA AND 18 CBETA) 13C
REMARK 3 SHIFT RESTRAINTS.
REMARK 3 (B) DNA: 249 INTRARESIDUE, 119 SEQUENTIAL INTRASTRAND AND
REMARK 3 33 INTERSTRAND INTERPROTON DISTANCE RESTRAINTS; 42
REMARK 3 DISTANCES FOR WATSON-CRICK BASE PAIR HYDROGEN BONDS; 136
REMARK 3 TORSION ANGLE RESTRAINTS
REMARK 3 (C) 73 INTERMOLECULAR INTERPROTON DISTANCE RESTRAINTS
REMARK 3 (D) 5 INTERMOLECULAR DISTANCE RESTRAINTS TO PHOSPHATES
REMARK 3 (E) 20 'REPULSIVE' RESTRAINTS
REMARK 3
REMARK 3 THE STRUCTURE IN THIS ENTRY IS THE RESTRAINED REGULARIZED
REMARK 3 MEAN STRUCTURE. THE LAST NUMERIC COLUMN REPRESENTS THE
REMARK 3 RMS OF THE 35 INDIVIDUAL SIMULATED ANNEALING STRUCTURES
REMARK 3 FOUND IN PDB ENTRY 2EZE ABOUT THE MEAN COORDINATE
REMARK 3 POSITIONS. THE LAST NUMERIC COLUMN IN THE INDIVIDUAL SA
REMARK 3 STRUCTURES HAS NO MEANING.
REMARK 3
REMARK 3 RESIDUES 3 - 27 OF THE PROTEIN CORRESPOND TO RESIDUES 51 -
REMARK 3 75 OF INTACT HMG-I(Y). RESIDUES 3 - 5 AND 20 - 27 ARE
REMARK 3 DISORDERED. ONLY RESIDUES 3 - 23 ARE PROVIDED FOR THE
REMARK 3 RESTRAINED REGULARIZED MEAN STRUCTURE.
REMARK 4
REMARK 4 2EZD 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_1000178055.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 306
REMARK 210 PH : 6.1
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : AMX500; AMX600; DMX600; DMX750
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XPLOR MODIFIED MODIFIED
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 35
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: DATA WERE RECORDED ON A 2:1 COMPLEX OF DNA DODECAMER TO
REMARK 210 HMG-I(Y) 50-91 WHICH CONTAINS THE SECOND AND THIRD DNA
REMARK 210 DNA BINDING DOMAINS. EACH DNA BINDING DOMAIN BINDS TO
REMARK 210 1 MOLECULE OF DNA.
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 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 THR A 24
REMARK 465 ARG A 25
REMARK 465 LYS A 26
REMARK 465 THR A 27
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 6 81.01 -49.94
REMARK 500 PRO A 13 153.61 -42.71
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2EZE RELATED DB: PDB
REMARK 900 ENSEMBLE OF 35 STRUCTURES
DBREF 2EZD A 3 23 UNP P17096 HMGIY_HUMAN 39 59
DBREF 2EZD B 201 212 PDB 2EZD 2EZD 201 212
DBREF 2EZD C 213 224 PDB 2EZD 2EZD 213 224
SEQRES 1 B 12 DG DG DG DA DA DA DT DT DC DC DT DC
SEQRES 1 C 12 DG DA DG DG DA DA DT DT DT DC DC DC
SEQRES 1 A 25 VAL PRO THR PRO LYS ARG PRO ARG GLY ARG PRO LYS GLY
SEQRES 2 A 25 SER LYS ASN LYS GLY ALA ALA LYS THR ARG LYS THR
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 20 Bytes