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- PDB-2lnf: Neurotensin 40 structures in DMPC/CHAPS(q=0.25) bicelle pH 5.5 & ... -

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Basic information

Entry
Database: PDB / ID: 2lnf
TitleNeurotensin 40 structures in DMPC/CHAPS(q=0.25) bicelle pH 5.5 & 298K. NMR data & Structures
ComponentsNeurotensin
KeywordsNEUROPEPTIDE / NT / DMPC:CHAPS Bicelle
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 / receptor ligand activity ...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 / receptor ligand activity / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / 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
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / simulated annealing
Model detailslowest energy, model 1
AuthorsMukhopadhyay, C. / Khatun, U.
CitationJournal: Biophys.Chem. / Year: 2012
Title: Modulation of the neurotensin solution structure in the presence of ganglioside GM1 bicelle.
Authors: Khatun, U.L. / Goswami, S.K. / Mukhopadhyay, C.
History
DepositionDec 27, 2011Deposition site: BMRB / Processing site: PDBJ
Revision 1.0Nov 14, 2012Provider: repository / Type: Initial release
Revision 1.1Jun 14, 2023Group: Data collection / Database references / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_nmr_software / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_nmr_data / _pdbx_nmr_software.name / _struct_ref_seq_dif.details
Revision 1.2May 15, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2 / Item: _database_2.pdbx_DOI

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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)1,6941
Polymers1,6941
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)40 / 100structures with the lowest energy
RepresentativeModel #1lowest energy

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Components

#1: Protein/peptide Neurotensin / / NT


Mass: 1693.964 Da / Num. of mol.: 1 / Fragment: UNP RESIDUES 151-163
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: NTS / Production host: Escherichia coli (E. coli) / References: UniProt: P30990

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experimentType: 2D 1H-1H TOCSY, 2D 1H-1H ROESY,2D DQF-COSY

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Sample preparation

DetailsContents: 4.5 mM Neurotensin-1, 90% H2O/10% D2O / Solvent system: 90% H2O/10% D2O
SampleConc.: 4.5 mM / Component: Neurotensin-1
Sample conditionsIonic strength: 4.5 / pH: 5.5 / Pressure: ambient / Temperature: 298 K

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NMR measurement

NMR spectrometerType: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 500 MHz

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Processing

NMR software
NameDeveloperClassification
X-PLOR NIHNIH,T.D.Goddard, D.G.Knellerrefinement
Sparkyrefinement
X-PLOR NIHNIH,T.D.Goddard, D.G.Knellerchemical shift assignment
Sparkychemical shift assignment
X-PLOR NIHNIH,T.D.Goddard, D.G.Knellerdata analysis
Sparkydata analysis
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: 40 / Representative conformer: 1

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