BMRB Entry 50101

Title:
Nipah virus phosphoprotein residues 223-319
Deposition date:
2019-11-29
Original release date:
2020-01-10
Authors:
Jensen, Malene; Blackledge, Martin
Citation:

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).
PubMed: 32348724

Assembly members:

Assembly members:
Nipah virus phosphoprotein residues 223-319, polymer, 106 residues, Formula weight is not available

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts279
15N chemical shifts90
1H chemical shifts90

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Nipah virus phosphoprotein1

Entities:

Entity 1, Nipah virus phosphoprotein 106 residues - Formula weight is not available

1   METGLYPROGLNTHRSERARGASNVALASN
2   LEUASPSERILELYSLEUTYRTHRSERASP
3   ASPGLUGLUALAASPGLNLEUGLUPHEGLU
4   ASPGLUPHEALAGLYSERSERSERGLUVAL
5   ILEVALGLYILESERPROGLUASPGLUGLU
6   PROSERSERVALGLYGLYLYSPROASNGLU
7   SERILEGLYARGTHRILEGLUGLYGLNSER
8   ILEARGASPASNLEUGLNALALYSASPASN
9   LYSSERTHRASPVALPROGLYALAGLYPRO
10   LYSASPSERALAVALLYSGLUGLULEUGLU
11   HISHISHISHISHISHIS

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 peaks
SPARKY: Backbone or all simulated peaks