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- PDB-1lv4: Human catestatin 21-mer -

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Basic information

Entry
Database: PDB / ID: 1lv4
TitleHuman catestatin 21-mer
Componentscatestatin
KeywordsSIGNALING PROTEIN / Glycoprotein / Amidation / Phosphorylation
Function / homology
Function and homology information


protein localization to secretory granule / positive regulation of relaxation of cardiac muscle / adenylate cyclase-activating adrenergic receptor signaling pathway involved in cardiac muscle relaxation / negative regulation of catecholamine secretion / positive regulation of dense core granule biogenesis / organelle organization / mast cell chemotaxis / mast cell activation / chromaffin granule / regulation of the force of heart contraction ...protein localization to secretory granule / positive regulation of relaxation of cardiac muscle / adenylate cyclase-activating adrenergic receptor signaling pathway involved in cardiac muscle relaxation / negative regulation of catecholamine secretion / positive regulation of dense core granule biogenesis / organelle organization / mast cell chemotaxis / mast cell activation / chromaffin granule / regulation of the force of heart contraction / Antimicrobial peptides / mast cell degranulation / positive regulation of phospholipase C-activating G protein-coupled receptor signaling pathway / neuronal dense core vesicle / negative regulation of insulin secretion / defense response to fungus / adenylate cyclase-activating adrenergic receptor signaling pathway / transport vesicle / positive regulation of cardiac muscle contraction / secretory granule / regulation of blood pressure / defense response to Gram-negative bacterium / killing of cells of another organism / defense response to Gram-positive bacterium / defense response to bacterium / innate immune response / perinuclear region of cytoplasm / extracellular space / extracellular region
Similarity search - Function
Chromogranin A/B / Chromogranin A/B/C / Chromogranin, conserved site / Granin (chromogranin or secretogranin) / Granins signature 1. / Granins signature 2.
Similarity search - Domain/homology
MethodSOLUTION NMR / restrained molecular dynamics simulated annealing
AuthorsO'Connor, D.T. / Preece, N.E.
CitationJournal: Regul.Pept. / Year: 2004
Title: Conformational preferences and activities of peptides from the catecholamine release-inhibitory (catestatin) region of chromogranin A.
Authors: Preece, N.E. / Nguyen, M. / Mahata, M. / Mahata, S.K. / Mahapatra, N.R. / Tsigelny, I. / O'Connor, D.T.
History
DepositionMay 24, 2002Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 19, 2002Provider: repository / Type: Initial release
Revision 1.1Apr 28, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 23, 2022Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name
Revision 1.4May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: catestatin


Theoretical massNumber of molelcules
Total (without water)2,3311
Polymers2,3311
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)25 / 25
Representative

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Components

#1: Protein/peptide catestatin / Chromogranin A


Mass: 2330.712 Da / Num. of mol.: 1 / Fragment: Residues 370-390 / Source method: obtained synthetically
Details: solid-phase SYNTHESIS. THE SEQUENCE OF THE PROTEIN IS NATURALLY FOUND IN HOMO SAPIENS.
References: UniProt: P10645

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D NOESY
1212D TOCSY

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Sample preparation

DetailsContents: linear catestatin / Solvent system: 9:1 H2O:D2O
Sample conditionsIonic strength: 6.4 mM / pH: 4.9 / Pressure: 1 atm / Temperature: 303 K
Crystal grow
*PLUS
Method: other / Details: NMR

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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
VNMR5.3FVariancollection
Felix2000Accelrysdata analysis
DiscoverCAccelrysstructure solution
NMRARCHITECHTMSIrefinement
RefinementMethod: restrained molecular dynamics simulated annealing / Software ordinal: 1
NMR ensembleConformers calculated total number: 25 / Conformers submitted total number: 25

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