Header list of 1mf6.pdb file
Complete list - 23 20 Bytes
HEADER SIGNALING PROTEIN 09-AUG-02 1MF6
TITLE TRANSDUCIN GAMMA SUBUNIT, C-TERMINAL DOMAIN 60-71, RHODOPSIN-BOUND
TITLE 2 STATE: ENSEMBLE OF 15 MODELS DETERMINED BY TRNOE SPECTROSCOPY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(T)GAMMA-T1 SUBUNIT;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 60-71;
COMPND 5 SYNONYM: TRANSDUCIN GAMMA CHAIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913
KEYWDS G-PROTEIN, TRANSDUCIN, RHODOPSIN, GPCR, GAMMA SUBUNIT, BOUND
KEYWDS 2 CONFORMATION, C-TERMINAL DOMAIN, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR O.G.KISSELEV
REVDAT 3 23-FEB-22 1MF6 1 REMARK
REVDAT 2 24-FEB-09 1MF6 1 VERSN
REVDAT 1 15-APR-03 1MF6 0
JRNL AUTH O.G.KISSELEV,M.A.DOWNS
JRNL TITL RHODOPSIN CONTROLS A CONFORMATIONAL SWITCH ON THE TRANSDUCIN
JRNL TITL 2 GAMMA SUBUNIT
JRNL REF STRUCTURE V. 11 367 2003
JRNL REFN ISSN 0969-2126
JRNL PMID 12679015
JRNL DOI 10.1016/S0969-2126(03)00045-5
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 5.2, TINKER 3.9
REMARK 3 AUTHORS : VARIAN (VNMR), PONDER, J.W. (TINKER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1MF6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-AUG-02.
REMARK 100 THE DEPOSITION ID IS D_1000016867.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 277
REMARK 210 PH : 7
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 0.1 MM RHODOPSIN, 2 MM PEPTIDE
REMARK 210 DKNPFKELKGGC-FARNESYL.
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VNMR 5.2, TINKER 3.9
REMARK 210 METHOD USED : DISTANCE GEOMERTY, HIGH
REMARK 210 -TEMPERATURE MOLECULAR DYNAMICS,
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 15
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES
REMARK 210 SUBMITTED
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 1 LYS A 2 -72.18 -131.76
REMARK 500 2 LYS A 2 -69.64 -155.15
REMARK 500 2 PRO A 4 0.33 -61.66
REMARK 500 3 LYS A 2 -76.45 -141.62
REMARK 500 3 PRO A 4 7.28 -63.30
REMARK 500 4 LYS A 2 -71.26 -136.36
REMARK 500 5 LYS A 2 -73.45 -144.67
REMARK 500 6 LYS A 2 -78.58 -119.70
REMARK 500 7 LYS A 2 -70.42 -129.19
REMARK 500 8 LYS A 2 -77.79 -115.99
REMARK 500 9 LYS A 2 -78.01 -123.86
REMARK 500 10 LYS A 2 -73.84 -132.06
REMARK 500 11 LYS A 2 -65.82 -129.90
REMARK 500 12 LYS A 2 -79.67 -130.28
REMARK 500 13 LYS A 2 -68.73 -139.97
REMARK 500 14 LYS A 2 -76.30 -127.10
REMARK 500 15 LYS A 2 -73.49 -132.36
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1MF6 A 1 12 UNP P02698 GBG1_BOVIN 60 71
SEQRES 1 A 12 ASP LYS ASN PRO PHE LYS GLU LEU LYS GLY GLY CYS
HELIX 1 1 LYS A 2 CYS A 12 1 11
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