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- PDB-1v46: Solution Structure of CCAP (Crustacean Cardioactive Peptide) from... -

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Basic information

Entry
Database: PDB / ID: 1v46
TitleSolution Structure of CCAP (Crustacean Cardioactive Peptide) from Drosophila melanogaster
ComponentsCardioactive Peptide
KeywordsNEUROPEPTIDE
Function / homologyCrustacean cardioactive peptide / Arthropod cardioacceleratory peptide 2a / positive regulation of heart contraction / neuropeptide hormone activity / neuropeptide signaling pathway / extracellular region / : / Cardioactive peptide
Function and homology information
MethodSOLUTION NMR / torsion angle dynamics using DYANA ver. 1.4
AuthorsNagata, K. / Tanokura, M.
CitationJournal: To be Published
Title: Solution structure of CCAP from Drosophila melanogaster
Authors: Nagata, K. / Tanokura, M.
History
DepositionNov 10, 2003Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Dec 14, 2004Provider: repository / Type: Initial release
Revision 1.1Oct 21, 2007Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 2, 2022Group: Database references / Derived calculations
Category: database_2 / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 1.4Dec 27, 2023Group: Data collection / Category: chem_comp_atom / chem_comp_bond
Revision 1.5Oct 30, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Cardioactive Peptide


Theoretical massNumber of molelcules
Total (without water)9591
Polymers9591
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)10 / 100target function
Representative

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Components

#1: Protein/peptide Cardioactive Peptide / CCAP


Mass: 959.099 Da / Num. of mol.: 1 / Source method: obtained synthetically
Details: This sequence occurs naturally in Drosophila melanogaster.
References: GenBank: 21355713, UniProt: Q8WRC7*PLUS
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D NOESY
1212D TOCSY
131DQF-COSY
141E-COSY
NMR detailsText: This structure was determined using standard 2D homonuclear techniques.

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Sample preparation

DetailsContents: 5mM CCAP; DMSO-d6 / Solvent system: DMSO-d6
Sample conditionsIonic strength: almost zero / pH: 6 / Pressure: ambient / Temperature: 298 K

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometerType: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 500 MHz

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Processing

NMR software
NameVersionDeveloperClassification
VNMR6.1CVarian, Inc.collection
NMRPipe2002.113.19.37Delaglio, F.processing
Sparky3.106Goddard, T. D. and Kneller, D. G.data analysis
DYANA1.4Guentert, P.structure solution
DYANA1.4Guentert, P.refinement
RefinementMethod: torsion angle dynamics using DYANA ver. 1.4 / Software ordinal: 1
Details: The structures are based on a total of 79 restraints, of which 65 are NOE-derived distance restraints, 8 dihedral angle restraints, and 6 distance restraints for the disulfide bond (Cys3-Cys9).
NMR ensembleConformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 10

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