BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 50105

Title: Nipah virus phosphoprotein residues 588-650   PubMed: 32348724

Deposition date: 2019-11-29 Original release date: 2020-01-10

Authors: Jensen, Malene; Blackledge, Martin

Citation: Jensen, Malene Ringkjybing; Yabukarski, Filip; Communie, Guillaume; Condamine, Eric; Mas, Caroline; Volchkova, Valentina; Tarbouriech, Nicolas; Bourhis, Jean-Marie; Volchkov, Viktor; Blackledge, Martin; Jamin, Marc. "Structural Description of the Nipah Virus Phosphoprotein and Its Interaction With STAT1"  Biophys. J. 118, 2470-2488 (2020).

Assembly members:
entity_1, polymer, 72 residues, Formula weight is not available

Natural source:   Common Name: Nipah virus   Taxonomy ID: 121791   Superkingdom: Virus   Kingdom: not available   Genus/species: henipavirus Nipah virus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28

Entity Sequences (FASTA):
entity_1: MGKNNPELKPVIGRDILEQQ SLFSFDNVKNFRDGSLTNEP YGAAVQLREDLILPELNFEE TNASLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts183
15N chemical shifts58
1H chemical shifts57

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1Nipah virus phosphoprotein1

Entities:

Entity 1, Nipah virus phosphoprotein 72 residues - Formula weight is not available

1   METGLYLYSASNASNPROGLULEULYSPRO
2   VALILEGLYARGASPILELEUGLUGLNGLN
3   SERLEUPHESERPHEASPASNVALLYSASN
4   PHEARGASPGLYSERLEUTHRASNGLUPRO
5   TYRGLYALAALAVALGLNLEUARGGLUASP
6   LEUILELEUPROGLULEUASNPHEGLUGLU
7   THRASNALASERLEUGLUHISHISHISHIS
8   HISHIS

Samples:

sample_1: entity_1, [U-13C; U-15N], 0.5 mM; Bis-Tris ph 6.0 20 mM; NaCl 150 mM; Arginine 50 mM; glutamate 50 mM; TCEP 0.5 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HNCOCAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOCACBsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - peak picking

NMR spectrometers:

  • Agilent Unity 800 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts