BMRB Entry 27991

Title:
Assignment of 1H, 13C and 15N resonances of Influenza A virus (H1N1) Non structural protein 2 (NS2)
Deposition date:
2019-07-30
Original release date:
2021-07-20
Authors:
Jaiswal, Nancy; Kumar, Dinesh
Citation:

Citation: Jaiswal, Nancy; Agarwal, Nipanshu; Poluri, Krishna Mohan; Kumar, Dinesh. "Effect of urea concentration on instant refolding of Nuclear Export Protein (NEP) from Influenza-A virus H1N1: A solution NMR based investigation"  Int. J. Biol. Macromol. 165, 2508-2519 (2020).
PubMed: 33470198

Assembly members:

Assembly members:
H1N1-NS2, polymer, 119 residues, 14322 Da.

Natural source:

Natural source:   Common Name: Influenza A   Taxonomy ID: 11320   Superkingdom: Viruses   Kingdom: not available   Genus/species: Alphainfluenzavirus Influenza A

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pet28b

Data sets:
Data typeCount
13C chemical shifts349
15N chemical shifts118
1H chemical shifts503

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1H1N1-NS21

Entities:

Entity 1, H1N1-NS2 119 residues - 14322 Da.

protein has 6XHis tag with TEV cleavage site at N terminus

1   METASPSERASNTHRMETSERSERPHEGLN
2   ASPILELEUMETARGMETSERLYSMETGLN
3   LEUGLYSERSERSERGLUASPLEUASNGLY
4   METVALTHRARGPHEGLUSERLEULYSILE
5   TYRARGASPSERLEUGLYGLUTHRVALMET
6   ARGMETGLYASPLEUHISTYRLEUGLNSER
7   ARGASNGLULYSTRPARGGLUGLNLEUGLY
8   GLNLYSPHEGLUGLUILEARGTRPLEUILE
9   GLUGLUMETARGHISARGLEULYSPROTHR
10   GLUASNSERPHEGLUGLNILETHRPHEMET
11   GLNALALEUGLNLEULEULEUGLUVALGLU
12   GLNGLUILEARGTHRPHESERPHEGLN

Samples:

sample_1: H1N1-NS2, [U-99% 13C; U-99% 15N], 0.8 ± 0.2 mM; D2O, [U-100% 2H], 10%; H2O 90%; urea 9.7 M; sodium chloride 300 mM; sodium phosphate 50 mM

condition_1: pH*: 6.0; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropiccondition_1
3D HNCAsample_1isotropiccondition_1
3D CBCA(CO)NHsample_1isotropiccondition_1
3D H(CCO)NHsample_1isotropiccondition_1
3D HNCACBsample_1isotropiccondition_1
3D HNCACOsample_1isotropiccondition_1
3D hNCAnHsample_1isotropiccondition_1
3D 1H-15N TOCSYsample_1isotropiccondition_1

Software:

CARA v1.9.1, Freely Available - chemical shift assignment, data analysis, structure solution

NMR spectrometers:

  • Bruker Avance 800 MHz

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