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- PDB-2bds: DETERMINATION OF THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE ... -

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Entry
Database: PDB / ID: 2bds
TitleDETERMINATION OF THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE ANTIHYPERTENSIVE AND ANTIVIRAL PROTEIN BDS-I FROM THE SEA ANEMONE ANEMONIA SULCATA. A STUDY USING NUCLEAR MAGNETIC RESONANCE AND HYBRID DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING
ComponentsBDS-I
KeywordsANTI-HYPERTENSIVE / ANTI-VIRAL PROTEIN
Function / homology
Function and homology information


nematocyst / ion channel inhibitor activity / sodium channel regulator activity / potassium channel regulator activity / regulation of blood pressure / toxin activity / extracellular region
Similarity search - Function
BDS potassium channel toxin / Potassium-channel blocking toxin / Anthopleurin-A / Myotoxin/Anemone neurotoxin domain superfamily / Anthopleurin-A / Single Sheet / Mainly Beta
Similarity search - Domain/homology
Delta/kappa-actitoxin-Avd4a
Similarity search - Component
Biological speciesAnemonia sulcata (snake-locks sea anemone)
MethodSOLUTION NMR
AuthorsClore, G.M. / Driscoll, P.C. / Gronenborn, A.M.
Citation
Journal: Biochemistry / Year: 1989
Title: Determination of the three-dimensional solution structure of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata: a study using nuclear magnetic resonance ...Title: Determination of the three-dimensional solution structure of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata: a study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing.
Authors: Driscoll, P.C. / Gronenborn, A.M. / Beress, L. / Clore, G.M.
#1: Journal: Biochemistry / Year: 1989
Title: A Proton Nuclear Magnetic Resonance Study of the Antihypertensive and Antiviral Protein Bds-I from the Sea Anemone Anemonia Sulcata. Sequential and Stereospecific Resonance Assignment and Secondary Structure
Authors: Driscoll, P.C. / Clore, G.M. / Beress, L. / Gronenborn, A.M.
#2: Journal: FEBS Lett. / Year: 1989
Title: The Influence of Stereospecific Assignments on the Determination of Three-Dimensional Structures of Proteins by Nuclear Magnetic Resonance Spectroscopy. Application to the Sea Anemone Protein Bds-I
Authors: Driscoll, P.C. / Gronenborn, A.M. / Clore, G.M.
History
DepositionNov 14, 1988Processing site: BNL
Revision 1.0Apr 19, 1989Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 29, 2017Group: Derived calculations / Other
Category: pdbx_database_status / pdbx_struct_assembly ...pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list / struct_conf
Item: _pdbx_database_status.process_site
Revision 1.4Oct 23, 2024Group: Data collection / Database references / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: BDS-I


Theoretical massNumber of molelcules
Total (without water)4,7191
Polymers4,7191
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
Atom site foot note1: RESIDUES PRO 36 AND PRO 42 ARE CIS PROLINES.
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)42 / -
Representative

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Components

#1: Protein/peptide BDS-I


Mass: 4719.434 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Anemonia sulcata (snake-locks sea anemone)
References: UniProt: P11494
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Crystal grow
*PLUS
Method: other / Details: NMR

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Processing

Software
NameClassification
X-PLORmodel building
X-PLORrefinement
X-PLORphasing
NMR softwareName: X-PLOR / Developer: BRUNGER / Classification: refinement
NMR ensembleConformers submitted total number: 42

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