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- PDB-2oyv: Neurotensin in DPC micelles -

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Basic information

Entry
Database: PDB / ID: 2oyv
TitleNeurotensin in DPC micelles
Componentsneurotensin
KeywordsNEUROPEPTIDE / type I turn
Function / homology
Function and homology information


neuropeptide receptor binding / neuropeptide hormone activity / neuropeptide signaling pathway / axon terminus / transport vesicle / blood vessel diameter maintenance / Peptide ligand-binding receptors / positive regulation of NF-kappaB transcription factor activity / G alpha (q) signalling events / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction ...neuropeptide receptor binding / neuropeptide hormone activity / neuropeptide signaling pathway / axon terminus / transport vesicle / blood vessel diameter maintenance / Peptide ligand-binding receptors / positive regulation of NF-kappaB transcription factor activity / G alpha (q) signalling events / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / receptor ligand activity / negative regulation of gene expression / intracellular membrane-bounded organelle / positive regulation of gene expression / signal transduction / extracellular region
Similarity search - Function
Neurotensin/neuromedin N / Neurotensin/neuromedin N precursor
Similarity search - Domain/homology
Neurotensin/neuromedin N
Similarity search - Component
MethodSOLUTION NMR / simulated annealing
AuthorsMonti, J.P. / Coutant, J. / Curmi, P.A.
CitationJournal: Biochemistry / Year: 2007
Title: NMR Solution Structure of Neurotensin in Membrane-Mimetic Environments: Molecular Basis for Neurotensin Receptor Recognition.
Authors: Coutant, J. / Curmi, P.A. / Toma, F. / Monti, J.P.
History
DepositionFeb 23, 2007Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 8, 2007Provider: repository / Type: Initial release
Revision 1.1May 1, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 2.0Dec 25, 2019Group: Data collection / Derived calculations / Polymer sequence
Category: entity_poly / pdbx_nmr_software ...entity_poly / pdbx_nmr_software / pdbx_nmr_spectrometer / pdbx_struct_assembly / pdbx_struct_mod_residue / pdbx_struct_oper_list / struct_conn
Item: _entity_poly.pdbx_seq_one_letter_code_can / _pdbx_nmr_software.name ..._entity_poly.pdbx_seq_one_letter_code_can / _pdbx_nmr_software.name / _pdbx_nmr_spectrometer.model / _pdbx_struct_mod_residue.parent_comp_id / _struct_conn.pdbx_leaving_atom_flag
Revision 2.1Oct 30, 2024Group: Data collection / Database references / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: neurotensin


Theoretical massNumber of molelcules
Total (without water)1,6761
Polymers1,6761
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)14 / 100structures with the least restraint violations,structures with the lowest energy
RepresentativeModel #1closest to the average

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Components

#1: Protein/peptide neurotensin


Mass: 1675.948 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: This sequence occurs naturally in humans. / References: UniProt: P30990*PLUS
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experimentType: 2D NOESY
NMR detailsText: This structure was determined using standard 2D homonuclear techniques.

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Sample preparation

DetailsContents: 5 mM neurotensin, 30 mg DPC, H2O:D2O 12:1, pH 6.4 / Solvent system: H2O:D2O (12:1) pH = 6.4
Sample conditionspH: 6.4 / Pressure: 1 atm / Temperature: 283 K

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometerType: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 600 MHz

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Processing

NMR softwareName: Discover / Classification: refinement
RefinementMethod: simulated annealing / Software ordinal: 1
Details: the structures are based on a total of 204 NOE-derived distance constraints.
NMR representativeSelection criteria: closest to the average
NMR ensembleConformer selection criteria: structures with the least restraint violations,structures with the lowest energy
Conformers calculated total number: 100 / Conformers submitted total number: 14

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