Header list of 1jun.pdb file
Complete list - 23 20 Bytes
HEADER TRANSCRIPTION REGULATION 19-DEC-95 1JUN
TITLE NMR STUDY OF C-JUN HOMODIMER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: C-JUN HOMODIMER;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: LEUCINE ZIPPER DOMAIN, RESIDUES 272 - 315;
COMPND 5 SYNONYM: JUNLZ, JUNP1N;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS TRANSCRIPTION REGULATION, DNA-BINDING REGULATORY PROTEIN, ONCOGENE
KEYWDS 2 PROTEIN, TRANSCRIPTION ACTIVATION
EXPDTA SOLUTION NMR
NUMMDL 7
AUTHOR F.K.JUNIUS,S.I.O'DONOGHUE,M.NILGES,G.F.KING
REVDAT 4 23-FEB-22 1JUN 1 REMARK LINK
REVDAT 3 24-FEB-09 1JUN 1 VERSN
REVDAT 2 01-APR-03 1JUN 1 JRNL
REVDAT 1 20-JUN-96 1JUN 0
JRNL AUTH F.K.JUNIUS,S.I.O'DONOGHUE,M.NILGES,A.S.WEISS,G.F.KING
JRNL TITL HIGH RESOLUTION NMR SOLUTION STRUCTURE OF THE LEUCINE ZIPPER
JRNL TITL 2 DOMAIN OF THE C-JUN HOMODIMER.
JRNL REF J.BIOL.CHEM. V. 271 13663 1996
JRNL REFN ISSN 0021-9258
JRNL PMID 8662824
JRNL DOI 10.1074/JBC.271.23.13663
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.I.O'DONOGHUE,G.F.KING,M.NILGES
REMARK 1 TITL CALCULATION OF SYMMETRIC MULTIMER STRUCTURES FROM NMR DATA
REMARK 1 TITL 2 USING A PRIORI KNOWLEDGE OF THE MONOMER STRUCTURE,
REMARK 1 TITL 3 CO-MONOMER RESTRAINTS, AND INTERFACE MAPPING: THE CASE OF
REMARK 1 TITL 4 LEUCINE ZIPPERS
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
REMARK 1 REFERENCE 2
REMARK 1 AUTH F.K.JUNIUS
REMARK 1 TITL STRUCTURAL STUDIES OF THE LEUCINE ZIPPER DOMAIN OF THE
REMARK 1 TITL 2 ONCOPROTEIN C-JUN
REMARK 1 REF THESIS 1995
REMARK 1 PUBL SYDNEY : UNIVERSITY OF SYDNEY (THESIS)
REMARK 1 REFN
REMARK 1 REFERENCE 3
REMARK 1 AUTH F.K.JUNIUS,J.P.MACKAY,W.A.BUBB,S.A.JENSEN,A.S.WEISS,G.F.KING
REMARK 1 TITL NUCLEAR MAGNETIC RESONANCE CHARACTERIZATION OF THE JUN
REMARK 1 TITL 2 LEUCINE ZIPPER DOMAIN: UNUSUAL PROPERTIES OF COILED-COIL
REMARK 1 TITL 3 INTERFACIAL POLAR RESIDUES
REMARK 1 REF BIOCHEMISTRY V. 34 6164 1995
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 4
REMARK 1 AUTH F.K.JUNIUS,A.S.WEISS,G.F.KING
REMARK 1 TITL THE SOLUTION STRUCTURE OF THE LEUCINE ZIPPER MOTIF OF THE
REMARK 1 TITL 2 JUN ONCOPROTEIN HOMODIMER
REMARK 1 REF EUR.J.BIOCHEM. V. 214 415 1993
REMARK 1 REFN ISSN 0014-2956
REMARK 1 REFERENCE 5
REMARK 1 AUTH S.I.O'DONOGHUE,F.K.JUNIUS,G.F.KING
REMARK 1 TITL DETERMINATION OF THE STRUCTURE OF SYMMETRIC COILED-COIL
REMARK 1 TITL 2 PROTEINS FROM NMR DATA: APPLICATION OF THE LEUCINE ZIPPER
REMARK 1 TITL 3 PROTEINS JUN AND GCN4
REMARK 1 REF PROTEIN ENG. V. 6 557 1993
REMARK 1 REFN ISSN 0269-2139
REMARK 1 REFERENCE 6
REMARK 1 AUTH E.K.O'SHEA,R.RUTKOWSKI,W.F.STAFFORD III,P.S.KIM
REMARK 1 TITL PREFERENTIAL HETERODIMER FORMATION BY ISOLATED LEUCINE
REMARK 1 TITL 2 ZIPPERS FROM FOS AND JUN
REMARK 1 REF SCIENCE V. 245 646 1989
REMARK 1 REFN ISSN 0036-8075
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: NULL
REMARK 4
REMARK 4 1JUN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000174376.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 3.6
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 : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 7
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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: 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 MET A 313 92.69 -67.75
REMARK 500 1 ASN A 314 51.21 -176.46
REMARK 500 1 MET B 313 92.28 -67.42
REMARK 500 1 ASN B 314 51.46 -176.10
REMARK 500 2 GLU A 293 -75.92 -70.32
REMARK 500 2 ASN A 314 165.18 56.36
REMARK 500 2 GLU B 293 -75.43 -70.16
REMARK 500 2 ASN B 314 165.25 56.43
REMARK 500 3 GLU A 293 -70.61 -72.43
REMARK 500 3 GLU B 293 -70.59 -72.23
REMARK 500 4 ASN A 314 -84.02 -138.72
REMARK 500 4 ASN B 314 -83.11 -138.75
REMARK 500 5 ASN A 314 82.11 -162.00
REMARK 500 5 ASN B 314 81.77 -161.76
REMARK 500 6 MET A 313 71.50 -68.31
REMARK 500 6 MET B 313 71.59 -68.03
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 1 ARG A 276 0.21 SIDE CHAIN
REMARK 500 1 ARG A 279 0.31 SIDE CHAIN
REMARK 500 1 ARG A 302 0.31 SIDE CHAIN
REMARK 500 1 ARG B 276 0.21 SIDE CHAIN
REMARK 500 1 ARG B 279 0.31 SIDE CHAIN
REMARK 500 1 ARG B 302 0.31 SIDE CHAIN
REMARK 500 2 ARG A 276 0.31 SIDE CHAIN
REMARK 500 2 ARG A 279 0.21 SIDE CHAIN
REMARK 500 2 ARG A 302 0.25 SIDE CHAIN
REMARK 500 2 ARG B 276 0.31 SIDE CHAIN
REMARK 500 2 ARG B 279 0.21 SIDE CHAIN
REMARK 500 2 ARG B 302 0.25 SIDE CHAIN
REMARK 500 3 ARG A 276 0.27 SIDE CHAIN
REMARK 500 3 ARG A 279 0.30 SIDE CHAIN
REMARK 500 3 ARG A 302 0.20 SIDE CHAIN
REMARK 500 3 ARG B 276 0.27 SIDE CHAIN
REMARK 500 3 ARG B 279 0.30 SIDE CHAIN
REMARK 500 3 ARG B 302 0.20 SIDE CHAIN
REMARK 500 4 ARG A 276 0.27 SIDE CHAIN
REMARK 500 4 ARG A 279 0.12 SIDE CHAIN
REMARK 500 4 ARG A 302 0.31 SIDE CHAIN
REMARK 500 4 ARG B 276 0.27 SIDE CHAIN
REMARK 500 4 ARG B 279 0.13 SIDE CHAIN
REMARK 500 4 ARG B 302 0.31 SIDE CHAIN
REMARK 500 5 ARG A 276 0.20 SIDE CHAIN
REMARK 500 5 ARG A 279 0.12 SIDE CHAIN
REMARK 500 5 ARG A 302 0.25 SIDE CHAIN
REMARK 500 5 ARG B 276 0.21 SIDE CHAIN
REMARK 500 5 ARG B 279 0.13 SIDE CHAIN
REMARK 500 5 ARG B 302 0.25 SIDE CHAIN
REMARK 500 6 ARG A 276 0.30 SIDE CHAIN
REMARK 500 6 ARG A 279 0.29 SIDE CHAIN
REMARK 500 6 ARG A 302 0.27 SIDE CHAIN
REMARK 500 6 ARG B 276 0.30 SIDE CHAIN
REMARK 500 6 ARG B 279 0.29 SIDE CHAIN
REMARK 500 6 ARG B 302 0.27 SIDE CHAIN
REMARK 500 7 ARG A 276 0.27 SIDE CHAIN
REMARK 500 7 ARG A 279 0.31 SIDE CHAIN
REMARK 500 7 ARG A 302 0.15 SIDE CHAIN
REMARK 500 7 ARG B 276 0.26 SIDE CHAIN
REMARK 500 7 ARG B 279 0.31 SIDE CHAIN
REMARK 500 7 ARG B 302 0.15 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1JUN A 273 315 UNP P05412 AP1_HUMAN 2 44
DBREF 1JUN B 273 315 UNP P05412 AP1_HUMAN 2 44
SEQRES 1 A 44 ACE CYS GLY GLY ARG ILE ALA ARG LEU GLU GLU LYS VAL
SEQRES 2 A 44 LYS THR LEU LYS ALA GLN ASN SER GLU LEU ALA SER THR
SEQRES 3 A 44 ALA ASN MET LEU ARG GLU GLN VAL ALA GLN LEU LYS GLN
SEQRES 4 A 44 LYS VAL MET ASN TYR
SEQRES 1 B 44 ACE CYS GLY GLY ARG ILE ALA ARG LEU GLU GLU LYS VAL
SEQRES 2 B 44 LYS THR LEU LYS ALA GLN ASN SER GLU LEU ALA SER THR
SEQRES 3 B 44 ALA ASN MET LEU ARG GLU GLN VAL ALA GLN LEU LYS GLN
SEQRES 4 B 44 LYS VAL MET ASN TYR
HET ACE A 272 6
HET ACE B 272 6
HETNAM ACE ACETYL GROUP
FORMUL 1 ACE 2(C2 H4 O)
HELIX 1 1 ARG A 276 VAL A 312 1 37
HELIX 2 2 ARG B 276 VAL B 312 1 37
SSBOND 1 CYS A 273 CYS B 273 1555 1555 2.02
LINK C ACE A 272 N CYS A 273 1555 1555 1.30
LINK C ACE B 272 N CYS B 273 1555 1555 1.31
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