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- PDB-1cmr: NMR SOLUTION STRUCTURE OF A CHIMERIC PROTEIN, DESIGNED BY TRANSFE... -

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Basic information

Entry
Database: PDB / ID: 1cmr
TitleNMR SOLUTION STRUCTURE OF A CHIMERIC PROTEIN, DESIGNED BY TRANSFERRING A FUNCTIONAL SNAKE BETA-HAIRPIN INTO A SCORPION ALPHA/BETA SCAFFOLD (PH 3.5, 20C), NMR, 18 STRUCTURES
ComponentsCHARYBDOTOXIN, ALPHA CHIMERA
KeywordsCURAREMIMETIC PROTEIN / ANTAGONIST OF NICOTINIC ACETYLCHOLINE RECEPTOR
Function / homology
Function and homology information


ion channel inhibitor activity / potassium channel regulator activity / defense response to fungus / toxin activity / killing of cells of another organism / defense response to bacterium / extracellular region
Similarity search - Function
Scorpion short toxins signature. / Scorpion short chain toxin, potassium channel inhibitor / Scorpion short toxin, BmKK2 / Knottin, scorpion toxin-like superfamily
Similarity search - Domain/homology
Potassium channel toxin alpha-KTx 1.1
Similarity search - Component
MethodSOLUTION NMR
AuthorsZinn-Justin, S. / Guenneugues, M. / Drakopoulou, E. / Gilquin, B. / Vita, C. / Menez, A.
Citation
Journal: Biochemistry / Year: 1996
Title: Transfer of a beta-hairpin from the functional site of snake curaremimetic toxins to the alpha/beta scaffold of scorpion toxins: three-dimensional solution structure of the chimeric protein.
Authors: Zinn-Justin, S. / Guenneugues, M. / Drakopoulou, E. / Gilquin, B. / Vita, C. / Menez, A.
#1: Journal: To be Published
Title: Changing the Structural Context of a Functional Beta-Hairpin. Synthesis and Characterization of a Chimera Containing the Curaremimetic Loop of a Snake Toxin in the Scorpion Alpha/Beta Scaffold
Authors: Drakopoulou, E. / Zinn-Justin, S. / Guenneugues, M. / Gilquin, B. / Vita, C. / Menez, A.
History
DepositionMar 15, 1996Processing site: BNL
Revision 1.0Aug 1, 1996Provider: 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 / struct_conf_type
Item: _pdbx_database_status.process_site
Revision 1.4Nov 3, 2021Group: Database references / Category: database_2 / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: CHARYBDOTOXIN, ALPHA CHIMERA


Theoretical massNumber of molelcules
Total (without water)3,5651
Polymers3,5651
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)18 / -
Representative

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Components

#1: Protein/peptide CHARYBDOTOXIN, ALPHA CHIMERA /


Mass: 3565.052 Da / Num. of mol.: 1 / Mutation: R19K, K21W, M23D, N24H, K25R, K26G, R28I, Y30E / Source method: obtained synthetically / Details: THE CHIMERA WAS PREPARED BY SOLID PHASE SYNTHESIS / References: UniProt: P13487

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Sample conditionspH: 3.5 / Temperature: 293 K
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: 18

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