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- PDB-1eyo: SOLUTION STRUCTURE OF CONOTOXIN TVIIA FROM CONUS TULIPA -

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Basic information

Entry
Database: PDB / ID: 1eyo
TitleSOLUTION STRUCTURE OF CONOTOXIN TVIIA FROM CONUS TULIPA
ComponentsCONOTOXIN TVIIA
KeywordsTOXIN / cystine knot motif
Function / homologyConotoxin TVIIAGS / Conotoxin TVIIA/GS family / sodium channel inhibitor activity / toxin activity / extracellular region / Conotoxin TVIIA
Function and homology information
MethodSOLUTION NMR / simulated annealing
AuthorsHill, J.M. / Alewood, P.F. / Craik, D.J.
Citation
Journal: Eur.J.Biochem. / Year: 2000
Title: Conotoxin TVIIA, a novel peptide from the venom of Conus tulipa 2. Three-dimensional solution structure.
Authors: Hill, J.M. / Alewood, P.F. / Craik, D.J.
#1: Journal: Eur.J.Biochem. / Year: 2000
Title: Conotoxin TVIIA, a novel peptide from the venom of Conus tulipa 1. Isolation, characterisation and chemical synthesis
Authors: Hill, J.M. / Atkins, A.R. / Loughnan, M.L. / Jones, A. / Adams, D.A. / Martin, R. / Lewis, R.J. / Craik, D.J. / Alewood, P.F.
#2: Journal: Structure / Year: 1997
Title: Solution structure of the sodium channel antagonist conotoxin GS: a new molecular caliper for probing sodium channel geometry
Authors: Hill, J.M. / Alewood, P.F. / Craik, D.J.
History
DepositionMay 7, 2000Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 6, 2000Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 16, 2022Group: Database references / Derived calculations
Category: database_2 / pdbx_struct_assembly ...database_2 / pdbx_struct_assembly / pdbx_struct_oper_list / struct_conn
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: CONOTOXIN TVIIA


Theoretical massNumber of molelcules
Total (without water)3,2221
Polymers3,2221
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 50structures with the least restraint violations,structures with the lowest energy
RepresentativeModel #1fewest violations,lowest energy

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Components

#1: Protein/peptide CONOTOXIN TVIIA


Mass: 3221.803 Da / Num. of mol.: 1 / Source method: obtained synthetically
Details: THIS PEPTIDE WAS CHEMICALLY SYNTHESIZED. THIS SEQUENCE OCCURS NATURALLY IN CONUS TULIPA (TULIP CONE)
References: UniProt: P58923

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D NOESY
121DQF-COSY
131E-COSY
141TOCSY
NMR detailsText: This structure was determined using standard 2D homonuclear techniques.

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Sample preparation

DetailsContents: 2mM conotoxin TVIIA / Solvent system: 90% H2O/10% D2O or 99.99% D2O
Sample conditionsIonic strength: 0 / pH: 3 / Pressure: ambient / Temperature: 283 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker ARXBrukerARX5001
Bruker DMXBrukerDMX7502

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Processing

NMR softwareName: X-PLOR / Version: 3.1 / Developer: Brunger / Classification: refinement
RefinementMethod: simulated annealing / Software ordinal: 1
Details: The structures are based on a total of 562 interproton distance restraints, and 18 backbone and 9 side chain dihedral angle restraints derived from spin-spin coupling constants.
NMR representativeSelection criteria: fewest violations,lowest energy
NMR ensembleConformer selection criteria: structures with the least restraint violations,structures with the lowest energy
Conformers calculated total number: 50 / Conformers submitted total number: 20

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