Header list of 1omn.pdb file
Complete list - 29 20 Bytes
HEADER NEUROTOXIN 20-DEC-94 1OMN
TITLE SOLUTION STRUCTURE OF OMEGA-CONOTOXIN MVIIC, A HIGH AFFINITY OF P-TYPE
TITLE 2 CALCIUM CHANNELS, USING 1H NMR SPECTROSCOPY AND COMPLETE RELAXATION
TITLE 3 MATRIX ANALYSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OMEGA-CONOTOXIN M VII C (M SEVEN C);
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SNX-230
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CONUS MAGUS;
SOURCE 3 ORGANISM_COMMON: MAGUS CONE;
SOURCE 4 ORGANISM_TAXID: 6492;
SOURCE 5 ORGAN: VENOM DUCT
KEYWDS P-TYPE CALCIUM CHANNEL BLOCKER, CONUS VENOM, PRESYNAPTIC NEUROTOXIN,
KEYWDS 2 CONOTOXIN, NEUROTOXIN
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR S.FARR-JONES,V.J.BASUS
REVDAT 4 29-NOV-17 1OMN 1 REMARK HELIX
REVDAT 3 24-FEB-09 1OMN 1 VERSN
REVDAT 2 01-APR-03 1OMN 1 JRNL
REVDAT 1 01-DEC-95 1OMN 0
JRNL AUTH S.FARR-JONES,G.P.MILJANICH,L.NADASDI,J.RAMACHANDRAN,
JRNL AUTH 2 V.J.BASUS
JRNL TITL SOLUTION STRUCTURE OF OMEGA-CONOTOXIN MVIIC, A HIGH AFFINITY
JRNL TITL 2 LIGAND OF P-TYPE CALCIUM CHANNELS, USING 1H NMR SPECTROSCOPY
JRNL TITL 3 AND COMPLETE RELAXATION MATRIX ANALYSIS.
JRNL REF J.MOL.BIOL. V. 248 106 1995
JRNL REFN ISSN 0022-2836
JRNL PMID 7731037
JRNL DOI 10.1006/JMBI.1995.0205
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.R.HILLYARD,V.D.MONJE,I.M.MINTZ,L.J.CRUZ,J.S.IMPERIAL,
REMARK 1 AUTH 2 B.M.OLIVERA
REMARK 1 TITL A NEW CONUS PEPTIDE LIGAND FOR MAMMALIAN PRESYNAPTIC CA2+
REMARK 1 TITL 2 CHANNELS
REMARK 1 REF NEURON V. 9 69 1992
REMARK 1 REFN ISSN 0896-6273
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AMBER
REMARK 3 AUTHORS : PEARLMAN,CASE,CALDWELL,SEIBEL,SINGH,WEINER,KOLLMAN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1OMN 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_1000175475.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
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 : 15
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 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 A 27
DBREF 1OMN A 1 26 UNP P37300 CXO7C_CONMA 3 28
SEQRES 1 A 27 CYS LYS GLY LYS GLY ALA PRO CYS ARG LYS THR MET TYR
SEQRES 2 A 27 ASP CYS CYS SER GLY SER CYS GLY ARG ARG GLY LYS CYS
SEQRES 3 A 27 NH2
HET NH2 A 27 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
HELIX 1 1 LYS A 10 MET A 12 5 3
SHEET 1 1 3 ALA A 6 CYS A 8 0
SHEET 2 1 3 GLY A 24 CYS A 26 -1
SHEET 3 1 3 SER A 19 GLY A 21 -1
SSBOND 1 CYS A 1 CYS A 16 1555 1555 2.09
SSBOND 2 CYS A 8 CYS A 20 1555 1555 2.07
SSBOND 3 CYS A 15 CYS A 26 1555 1555 2.08
LINK C CYS A 26 N NH2 A 27 1555 1555 1.33
SITE 1 AC1 4 CYS A 15 SER A 19 LYS A 25 CYS A 26
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 - 29 20 Bytes