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- PDB-1l5d: Solution Structure of the Monomeric Form of a Mutant Unliganded B... -

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Basic information

Entry
Database: PDB / ID: 1l5d
TitleSolution Structure of the Monomeric Form of a Mutant Unliganded Bovine Neurophysin, Minimized Average Structure
ComponentsNEUROPHYSIN 1Neurophysins
KeywordsHORMONE/GROWTH FACTOR / Two 4-strand beta sheet / 3 / 10-helix / HORMONE-GROWTH FACTOR COMPLEX
Function / homology
Function and homology information


Vasopressin-like receptors / oxytocin receptor binding / neurohypophyseal hormone activity / V1A vasopressin receptor binding / neuropeptide hormone activity / G alpha (q) signalling events / secretory granule / response to estrogen / positive regulation of cold-induced thermogenesis / extracellular space
Similarity search - Function
Neurophysin II; Chain A / Neurohypophysial hormone domain / Neurohypophysial hormone / Neurohypophysial hormone, conserved site / Neurohypophysial hormone domain superfamily / Neurohypophysial hormones, C-terminal Domain / Neurohypophysial hormones, N-terminal Domain / Neurohypophysial hormones signature. / Neurohypophysial hormones / Sandwich / Mainly Beta
Similarity search - Domain/homology
Oxytocin-neurophysin 1
Similarity search - Component
Biological speciesBos taurus (cattle)
MethodSOLUTION NMR / simulated annealing
Model type detailsminimized average
AuthorsNguyen, T.L. / Breslow, E.
CitationJournal: Biochemistry / Year: 2002
Title: NMR analysis of the monomeric form of a mutant unliganded bovine neurophysin: comparison with the crystal structure of a neurophysin dimer.
Authors: Nguyen, T.L. / Breslow, E.
History
DepositionMar 6, 2002Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 20, 2002Provider: repository / Type: Initial release
Revision 1.1Apr 28, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Oct 27, 2021Group: Database references / Derived calculations
Category: database_2 / pdbx_struct_assembly ...database_2 / pdbx_struct_assembly / pdbx_struct_oper_list / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: NEUROPHYSIN 1


Theoretical massNumber of molelcules
Total (without water)9,2861
Polymers9,2861
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)1 / -
Representativeminimized average structure

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Components

#1: Protein NEUROPHYSIN 1 / Neurophysins


Mass: 9286.441 Da / Num. of mol.: 1 / Mutation: H80E
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bos taurus (cattle) / Plasmid: T7 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE)pLyS-S / References: UniProt: P01175

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D 15N-separated NOESY
2213D 15N-separated NOESY
332HNHA
1423D 13C-separated NOESY
3523D 13C-separated NOESY

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Sample preparation

Details
Solution-IDContentsSolvent system
11.4 mM H80E of bovine neurophysin I U-15N; 90% H2O, 10% D2O90% H2O/10% D2O
21.4 mM H80E of bovine neurophysin I U-15N, 13C; 90% H2O, 10% D2O90% H2O/10% D2O
Sample conditions
Conditions-IDpHPressure (kPa)Temperature (K)
17.5 ambient 283 K
27.5 ambient 298 K
37.5 ambient 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: 600 MHz

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Processing

NMR software
NameVersionDeveloperClassification
NMRPipebaxdata analysis
NMRView4.1johnsondata analysis
CNS0.9brungerstructure solution
TALOSbaxdata analysis
CNS0.9brungerrefinement
RefinementMethod: simulated annealing / Software ordinal: 1
Details: The structures are based on 811 NOE-derived distance constraints, 50 hydrogen bond distance restraints, 72 torsion angle constraints, 46 JNHA coupling constants, 157 CA/CB and 108 1H ...Details: The structures are based on 811 NOE-derived distance constraints, 50 hydrogen bond distance restraints, 72 torsion angle constraints, 46 JNHA coupling constants, 157 CA/CB and 108 1H chemical shift restraints and the pairing of the protein's 7 disulfides
NMR representativeSelection criteria: minimized average structure
NMR ensembleConformers submitted total number: 1

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