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- PDB-1p1p: [PRO7,13] AA-CONOTOXIN PIVA, NMR, 12 STRUCTURES -

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Basic information

Entry
Database: PDB / ID: 1p1p
Title[PRO7,13] AA-CONOTOXIN PIVA, NMR, 12 STRUCTURES
ComponentsAA-CONOTOXIN PIVA
KeywordsNEUROTOXIN / CONOTOXIN / ACETYLCHOLINE RECEPTOR BINDING / TRANSCRIPTION REGULATION
Function / homology
Function and homology information


host cell postsynaptic membrane / acetylcholine receptor inhibitor activity / : / toxin activity / extracellular region
Similarity search - Function
Alpha-A conotoxin PIVA-like / Alpha-A conotoxin PIVA-like protein / Conotoxin, alpha-type / Alpha conotoxin precursor
Similarity search - Domain/homology
Alpha-conotoxin PIVA
Similarity search - Component
Biological speciesConus purpurascens (invertebrata)
MethodSOLUTION NMR / distance geometry
AuthorsHan, K.-H. / Hwang, K.-J. / Kim, S.-M. / Kim, S.-K. / Gray, W.R. / Olivera, B.M. / Rivier, J. / Shon, K.J.
CitationJournal: Biochemistry / Year: 1997
Title: NMR structure determination of a novel conotoxin, [Pro 7,13] alpha A-conotoxin PIVA.
Authors: Han, K.H. / Hwang, K.J. / Kim, S.M. / Kim, S.K. / Gray, W.R. / Olivera, B.M. / Rivier, J. / Shon, K.J.
History
DepositionDec 6, 1996Processing site: BNL
Revision 1.0Jul 7, 1997Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 23, 2022Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_oper_list / struct_conn / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site / _pdbx_nmr_software.name / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: AA-CONOTOXIN PIVA


Theoretical massNumber of molelcules
Total (without water)2,6251
Polymers2,6251
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)12 / 50RMSD
Representative

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Components

#1: Protein/peptide AA-CONOTOXIN PIVA


Mass: 2624.956 Da / Num. of mol.: 1 / Mutation: PRO 7, PRO 13
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Conus purpurascens (invertebrata) / References: UniProt: P55963

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111COSY
121TOCSY
131NOESY
141P.E.COSY

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Sample preparation

Sample conditionspH: 3.4 / Temperature: 287 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Varian UNITY 500 / Manufacturer: Varian / Model: UNITY 500 / Field strength: 500 MHz

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Processing

NMR software
NameVersionDeveloperClassification
DGII, DISCOVERDISCOVERBIOSYM TECHNOLOGIESrefinement
VNMRstructure solution
Felixstructure solution
DGIIstructure solution
Discoverstructure solution
RefinementMethod: distance geometry / Software ordinal: 1
Details: THE TOTAL OF 324 NOE-DERIVED INTERPROTON DISTANCE RESTRAINTS INCLUDING 33 LONG-RANGE NOE RESTRAINTS AS WELL AS 11 PHI AND 7 CHI1 TORSION ANGLE RESTRAINTS WERE USED FOR STRUCTURE ...Details: THE TOTAL OF 324 NOE-DERIVED INTERPROTON DISTANCE RESTRAINTS INCLUDING 33 LONG-RANGE NOE RESTRAINTS AS WELL AS 11 PHI AND 7 CHI1 TORSION ANGLE RESTRAINTS WERE USED FOR STRUCTURE DETERMINATION. BACK CALCULATION OF EXPERIMENTAL NOE SPECTRUM YIELDED THE FINAL R-FACTORS OF RA=0.641 AND RB=0.157. THE FINAL RMSD VALUES ARE 0.90A AND 1.16A FOR THE BACKBONE AND THE HEAVY ATOMS, RESPECTIVELY. RESIDUES 12 - 24 ARE EXTREMELY WELL-DEFINED WITH A BACKBONE RMSD OF 0.56 A WHEREAS THE N-TERMINAL 3 - 11 DISULFIDE LOOP IS FLEXIBLE POSSESSING A BACKBONE RMSD OF 1.09 A.
NMR ensembleConformer selection criteria: RMSD / Conformers calculated total number: 50 / Conformers submitted total number: 12

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