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- PDB-1im1: NMR SOLUTION STRUCTURE OF ALPHA-CONOTOXIN IM1, 20 STRUCTURES -

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Basic information

Entry
Database: PDB / ID: 1im1
TitleNMR SOLUTION STRUCTURE OF ALPHA-CONOTOXIN IM1, 20 STRUCTURES
ComponentsALPHA-CONOTOXIN IM1
KeywordsPEPTIDE TOXIN / NEUROTOXIN / NICOTINIC ACETYLCHOLINE RECEPTOR ANTAGONIST / ALPHA-CONOTOXIN
Function / homologyConotoxin, alpha-type, conserved site / Alpha-conotoxin family signature. / host cell postsynaptic membrane / acetylcholine receptor inhibitor activity / ion channel regulator activity / toxin activity / extracellular region / Alpha-conotoxin ImI
Function and homology information
Biological speciesConus imperialis (invertebrata)
MethodSOLUTION NMR / DISTANCE GEOMETRY, RESTRAINED ENERGY REFINEMENT
AuthorsRogers, J.P. / Luginbuhl, P. / Shen, G.S. / Mccabe, R.T. / Stevens, R.C. / Wemmer, D.E.
Citation
Journal: Biochemistry / Year: 1999
Title: NMR solution structure of alpha-conotoxin ImI and comparison to other conotoxins specific for neuronal nicotinic acetylcholine receptors.
Authors: Rogers, J.P. / Luginbuhl, P. / Shen, G.S. / McCabe, R.T. / Stevens, R.C. / Wemmer, D.E.
#1: Journal: Mol.Pharmacol. / Year: 1995
Title: Alpha-Conotoxin Imi Exhibits Subtype-Specific Nicotinic Acetylcholine Receptor Blockade: Preferential Inhibition of Homomeric Alpha 7 and Alpha 9 Receptors
Authors: Johnson, D.S. / Martinez, J. / Elgoyhen, A.B. / Heinemann, S.F. / Mcintosh, J.M.
#2: Journal: J.Biol.Chem. / Year: 1994
Title: A Nicotinic Acetylcholine Receptor Ligand of Unique Specificity, Alpha-Conotoxin Imi
Authors: Mcintosh, J.M. / Yoshikami, D. / Mahe, E. / Nielsen, D.B. / Rivier, J.E. / Gray, W.R. / Olivera, B.M.
History
DepositionNov 18, 1998Processing site: BNL
Revision 1.0Jun 15, 1999Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3May 25, 2016Group: Source and taxonomy
Revision 1.4Feb 23, 2022Group: Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site
Revision 1.5Oct 23, 2024Group: Data collection / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: ALPHA-CONOTOXIN IM1


Theoretical massNumber of molelcules
Total (without water)1,3591
Polymers1,3591
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 / 20LOWEST RESIDUAL TARGET FUNCTION
RepresentativeModel #3

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Components

#1: Protein/peptide ALPHA-CONOTOXIN IM1


Mass: 1358.594 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: NEUROTOXIN / Source: (gene. exp.) Conus imperialis (invertebrata) / References: UniProt: P50983
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111TOCSY
121ROESY
131DQF-COSY

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Sample preparation

DetailsContents: 90% H2O/10% D2O OR 100% D2O
Sample conditionspH: 3 / Temperature: 298 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker DRX500BrukerDRX5005001
Bruker DRX300BrukerDRX3003002

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Processing

Software
NameClassification
DYANAmodel building
DYANArefinement
NMR software
NameDeveloperClassification
OPALLUGINBUHL,GUNTERT,BILLETER, WUTHRICHrefinement
DYANAstructure solution
OPALstructure solution
RefinementMethod: DISTANCE GEOMETRY, RESTRAINED ENERGY REFINEMENT / Software ordinal: 1
Details: FOR THE PRESENT STRUCTURES THE NMR DISTANCE CONSTRAINTS WERE WEIGHTED SUCH THAT A VIOLATION OF AN UPPER DISTANCE LIMIT OF 0.1 ANGSTROM CORRESPONDS TO AN ENERGY OF KT/2. THE CONSTRAINTS ON ...Details: FOR THE PRESENT STRUCTURES THE NMR DISTANCE CONSTRAINTS WERE WEIGHTED SUCH THAT A VIOLATION OF AN UPPER DISTANCE LIMIT OF 0.1 ANGSTROM CORRESPONDS TO AN ENERGY OF KT/2. THE CONSTRAINTS ON DIHEDRAL ANGLES RESULTING FROM MEASUREMENTS OF VICINAL COUPLING CONSTANTS WERE WEIGHTED SUCH THAT A VIOLATION OF 2.5 DEGREES CORRESPONDS TO AN ENERGY OF KT/2.
NMR ensembleConformer selection criteria: LOWEST RESIDUAL TARGET FUNCTION
Conformers calculated total number: 20 / Conformers submitted total number: 20

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