Header list of 1a93.pdb file
Complete list - 16 20 Bytes
HEADER LEUCINE ZIPPER 15-APR-98 1A93
TITLE NMR SOLUTION STRUCTURE OF THE C-MYC-MAX HETERODIMERIC LEUCINE ZIPPER,
TITLE 2 NMR, MINIMIZED AVERAGE STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MYC PROTO-ONCOGENE PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: HETERODIMERIC LEUCINE ZIPPER;
COMPND 5 SYNONYM: COILED COIL, LZ;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: BOTH C-MYC (CHAIN A) AND MAX (CHAIN B) HAVE A NON-
COMPND 8 BIOLOGICAL CGG LINKER AT THE N-TERMINUS OF THE PROTEIN;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: MAX PROTEIN;
COMPND 11 CHAIN: B;
COMPND 12 FRAGMENT: HETERODIMERIC LEUCINE ZIPPER;
COMPND 13 SYNONYM: COILED COIL, LZ;
COMPND 14 ENGINEERED: YES;
COMPND 15 OTHER_DETAILS: BOTH C-MYC (CHAIN A) AND MAX (CHAIN B) HAVE A NON-
COMPND 16 BIOLOGICAL CGG LINKER AT THE N-TERMINUS OF THE PROTEIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 7 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 8 ORGANISM_TAXID: 10090
KEYWDS LEUCINE ZIPPER, 2D NMR, SOLUTION STRUCTURE, H-BONDS, BURIED SALT
KEYWDS 2 BRIDGE, PROTO-ONCOGENE, NUCLEAR PROTEIN
EXPDTA SOLUTION NMR
AUTHOR P.LAVIGNE,M.P.CRUMP,S.M.GAGNE,R.S.HODGES,C.M.KAY,B.D.SYKES
REVDAT 4 16-FEB-22 1A93 1 REMARK LINK
REVDAT 3 24-FEB-09 1A93 1 VERSN
REVDAT 2 18-NOV-98 1A93 2 SOURCE COMPND REMARK TITLE
REVDAT 2 2 2 DBREF SEQADV JRNL EXPDTA
REVDAT 2 3 2 KEYWDS HEADER CONECT SLTBRG
REVDAT 1 21-OCT-98 1A93 0
JRNL AUTH P.LAVIGNE,M.P.CRUMP,S.M.GAGNE,R.S.HODGES,C.M.KAY,B.D.SYKES
JRNL TITL INSIGHTS INTO THE MECHANISM OF HETERODIMERIZATION FROM THE
JRNL TITL 2 1H-NMR SOLUTION STRUCTURE OF THE C-MYC-MAX HETERODIMERIC
JRNL TITL 3 LEUCINE ZIPPER.
JRNL REF J.MOL.BIOL. V. 281 165 1998
JRNL REFN ISSN 0022-2836
JRNL PMID 9680483
JRNL DOI 10.1006/JMBI.1998.1914
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: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE.
REMARK 4
REMARK 4 1A93 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_1000170546.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 4.8
REMARK 210 IONIC STRENGTH : 10MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : WATER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : VXR-500; UNITY 600
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION ONLY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING 1H 2D NMR SPECTROSCOPY
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 ILE B 17 -74.01 -62.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 A 35
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 B 35
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2A93 RELATED DB: PDB
DBREF 1A93 A 6 34 UNP P01106 MYC_HUMAN 406 434
DBREF 1A93 B 6 34 UNP P28574 MAX_MOUSE 74 102
SEQRES 1 A 34 ACE CYS GLY GLY VAL GLN ALA GLU GLU GLN LYS LEU ILE
SEQRES 2 A 34 SER GLU GLU ASP LEU LEU ARG LYS ARG ARG GLU GLN LEU
SEQRES 3 A 34 LYS HIS LYS LEU GLU GLN LEU NH2
SEQRES 1 B 34 ACE CYS GLY GLY MET ARG ARG LYS ASN ASP THR HIS GLN
SEQRES 2 B 34 GLN ASP ILE ASP ASP LEU LYS ARG GLN ASN ALA LEU LEU
SEQRES 3 B 34 GLU GLN GLN VAL ARG ALA LEU NH2
HET ACE A 2 6
HET NH2 A 35 3
HET ACE B 2 6
HET NH2 B 35 3
HETNAM ACE ACETYL GROUP
HETNAM NH2 AMINO GROUP
FORMUL 1 ACE 2(C2 H4 O)
FORMUL 1 NH2 2(H2 N)
HELIX 1 1 VAL A 6 GLU A 32 1 27
HELIX 2 2 MET B 6 ARG B 32 1 27
SSBOND 1 CYS A 3 CYS B 3 1555 1555 2.02
LINK C ACE A 2 N CYS A 3 1555 1555 1.33
LINK C LEU A 34 N NH2 A 35 1555 1555 1.31
LINK C ACE B 2 N CYS B 3 1555 1555 1.33
LINK C LEU B 34 N NH2 B 35 1555 1555 1.31
SITE 1 AC3 1 LEU A 34
SITE 1 AC4 1 LEU B 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 - 16 20 Bytes