Header list of 1mbe.pdb file
Complete list - 25 201 Bytes
HEADER DNA BINDING PROTEIN 19-MAY-95 1MBE
TITLE MOUSE C-MYB DNA-BINDING DOMAIN REPEAT 1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MYB PROTO-ONCOGENE PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 OTHER_DETAILS: GENE C-MYB, NMR, MINIMIZED AVERAGE STRUCTURE;
COMPND 5 ENGINEERED
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090
KEYWDS PROTOONCOGENE PRODUCT, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
AUTHOR K.OGATA,S.MORIKAWA,H.NAKAMURA,H.HOJO,S.YOSHIMURA,R.ZHANG,S.AIMOTO,
AUTHOR 2 Y.AMETANI,Z.HIRATA,A.SARAI,S.ISHII,Y.NISHIMURA
REVDAT 4 29-FEB-12 1MBE 1 JRNL VERSN
REVDAT 3 24-FEB-09 1MBE 1 VERSN
REVDAT 2 01-APR-03 1MBE 1 JRNL
REVDAT 1 31-JUL-95 1MBE 0
JRNL AUTH K.OGATA,S.MORIKAWA,H.NAKAMURA,H.HOJO,S.YOSHIMURA,R.ZHANG,
JRNL AUTH 2 S.AIMOTO,Y.AMETANI,Z.HIRATA,A.SARAI,S.ISHII,Y.NISHIMURA
JRNL TITL COMPARISON OF THE FREE AND DNA-COMPLEXED FORMS OF THE
JRNL TITL 2 DNA-BINDING DOMAIN FROM C-MYB.
JRNL REF NAT.STRUCT.BIOL. V. 2 309 1995
JRNL REFN ISSN 1072-8368
JRNL PMID 7796266
JRNL DOI 10.1038/NSB0495-309
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH K.OGATA,S.MORIKAWA,H.NAKAMURA,A.SEKIKAWA,T.INOUE,H.KANAI,
REMARK 1 AUTH 2 A.SARAI,S.ISHII,Y.NISHIMURA
REMARK 1 TITL SOLUTION STRUCTURE OF A SPECIFIC DNA COMPLEX OF THE MYB
REMARK 1 TITL 2 DNA-BINDING DOMAIN WITH COOPERATIVE RECOGNITION HELICES
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 79 639 1994
REMARK 1 REFN ISSN 0092-8674
REMARK 1 REFERENCE 2
REMARK 1 AUTH K.OGATA,H.HOJO,S.AIMOTO,T.NAKAI,H.NAKAMURA,A.SARAI,S.ISHII,
REMARK 1 AUTH 2 Y.NISHIMURA
REMARK 1 TITL SOLUTION STRUCTURE OF A DNA-BINDING UNIT OF MYB: A
REMARK 1 TITL 2 HELIX-TURN-HELIX-RELATED MOTIF WITH CONSERVED TRYPTOPHANS
REMARK 1 TITL 3 FORMING A HYDROPHOBIC CORE
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 89 6428 1992
REMARK 1 REFN ISSN 0027-8424
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : EMBOSS, PRESTO
REMARK 3 AUTHORS : NAKAI,KIDERA,NAKAMURA (EMBOSS), MORIKAMI,NAKAI,
REMARK 3 KIDERA,SAITO,NAKAMURA (PRESTO)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 A TOTAL OF 50 STRUCTURES WERE CALCULATED. THE COORDINATES
REMARK 3 OF THE RESTRAINED MINIMIZED AVERAGED STRUCTURE WERE
REMARK 3 OBTAINED BY AVERAGING THE COORDINATES OF THE INDIVIDUAL
REMARK 3 STRUCTURES AND THEN BY SUBJECTING THE RESULTING
REMARK 3 COORDINATES TO THE RESTRAINED ENERGY MINIMIZATION BY
REMARK 3 PRESTO.
REMARK 4
REMARK 4 1MBE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 290; 300
REMARK 210 PH : 6.8; 6.8
REMARK 210 IONIC STRENGTH : NULL; NULL
REMARK 210 PRESSURE : NULL; 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 : 1
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: 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 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 ASN A 58 -79.11 -90.15
REMARK 500 THR A 60 48.96 -83.83
REMARK 500 ASP A 61 -134.11 -90.45
REMARK 500 ASN A 72 -44.60 76.96
REMARK 500 TRP A 82 -75.55 -84.91
REMARK 500 VAL A 85 -75.08 -134.88
REMARK 500 ASN A 87 79.70 -153.75
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 A 90
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1MBF RELATED DB: PDB
DBREF 1MBE A 38 89 UNP P06876 MYB_MOUSE 38 89
SEQRES 1 A 53 LEU GLY LYS THR ARG TRP THR ARG GLU GLU ASP GLU LYS
SEQRES 2 A 53 LEU LYS LYS LEU VAL GLU GLN ASN GLY THR ASP ASP TRP
SEQRES 3 A 53 LYS VAL ILE ALA ASN TYR LEU PRO ASN ARG THR ASP VAL
SEQRES 4 A 53 GLN CYS GLN HIS ARG TRP GLN LYS VAL LEU ASN PRO GLU
SEQRES 5 A 53 NH2
HET NH2 A 90 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
HELIX 1 H1 ARG A 45 ASN A 58 1 14
HELIX 2 H2 TRP A 63 TYR A 69 1 7
HELIX 3 H3 ASP A 75 LYS A 84 1 10
LINK C GLU A 89 N NH2 A 90 1555 1555 1.33
SITE 1 AC1 1 GLU A 89
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 - 25 201 Bytes