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- PDB-1k8v: The NMR-derived Conformation of Neuropeptide F from Moniezia expansa -

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Basic information

Entry
Database: PDB / ID: 1k8v
TitleThe NMR-derived Conformation of Neuropeptide F from Moniezia expansa
ComponentsNEUROPEPTIDE F
KeywordsUNKNOWN FUNCTION / neuropeptide F / Moniezia expansa / NPF
Function / homology
Function and homology information


neuropeptide signaling pathway / hormone activity / extracellular region
Similarity search - Function
Pancreatic hormone-like / Pancreatic hormone-like, conserved site / Pancreatic hormone peptide / Pancreatic hormone family signature. / Pancreatic hormone family profile. / Pancreatic hormones / neuropeptide F / peptide YY family
Similarity search - Domain/homology
MethodSOLUTION NMR / simulated annealing
AuthorsMiskolzie, M. / Kotovych, G.
CitationJournal: J.Biomol.Struct.Dyn. / Year: 2002
Title: The NMR-derived conformation of neuropeptide F from Moniezia expansa.
Authors: Miskolzie, M. / Kotovych, G.
History
DepositionOct 25, 2001Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 12, 2002Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 23, 2022Group: Database references / Derived calculations
Category: database_2 / pdbx_struct_assembly ...database_2 / pdbx_struct_assembly / pdbx_struct_oper_list / struct_conn / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag / _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: NEUROPEPTIDE F


Theoretical massNumber of molelcules
Total (without water)4,5981
Polymers4,5981
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)20 / 100structures with the lowest energy
RepresentativeModel #4lowest energy

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Components

#1: Protein/peptide NEUROPEPTIDE F


Mass: 4598.248 Da / Num. of mol.: 1 / Source method: obtained synthetically
Details: This sequence occurs naturally in Moniezia expansa (sheep tapeworm).
References: UniProt: P41967

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experimentType: 2D NOESY

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Sample preparation

DetailsContents: 1.4mM neuropeptide F / Solvent system: 60% CD3OH, 40% H2O by volume
Sample conditionspH: 4.85 / Pressure: ambient / Temperature: 298 K

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Varian INOVAVarianINOVA8001
Varian UNITYVarianUNITY5002

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Processing

NMR software
NameVersionDeveloperClassification
VNMR6.1bVarianprocessing
NMRView5.0.3Johnson, B.A.collection
CNS1Brunger, A.T.structure solution
CNS1Brunger, A.T.refinement
RefinementMethod: simulated annealing / Software ordinal: 1
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 100 / Conformers submitted total number: 20

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