BMRB Entry 27991
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27991
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Title: Assignment of 1H, 13C and 15N resonances of Influenza A virus (H1N1) Non structural protein 2 (NS2) PubMed: 33470198
Deposition date: 2019-07-30 Original release date: 2021-07-20
Authors: Jaiswal, Nancy; Kumar, Dinesh
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).
Assembly members:
H1N1-NS2, polymer, 119 residues, 14322 Da.
Natural source: Common Name: Influenza A Taxonomy ID: 11320 Superkingdom: Viruses Kingdom: not available Genus/species: Alphainfluenzavirus Influenza A
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pet28b
Entity Sequences (FASTA):
H1N1-NS2: MDSNTMSSFQDILMRMSKMQ
LGSSSEDLNGMVTRFESLKI
YRDSLGETVMRMGDLHYLQS
RNEKWREQLGQKFEEIRWLI
EEMRHRLKPTENSFEQITFM
QALQLLLEVEQEIRTFSFQ
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 349 |
| 15N chemical shifts | 118 |
| 1H chemical shifts | 503 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | H1N1-NS2 | 1 |
Entities:
Entity 1, H1N1-NS2 119 residues - 14322 Da.
protein has 6XHis tag with TEV cleavage site at N terminus
| 1 | MET | ASP | SER | ASN | THR | MET | SER | SER | PHE | GLN | ||||
| 2 | ASP | ILE | LEU | MET | ARG | MET | SER | LYS | MET | GLN | ||||
| 3 | LEU | GLY | SER | SER | SER | GLU | ASP | LEU | ASN | GLY | ||||
| 4 | MET | VAL | THR | ARG | PHE | GLU | SER | LEU | LYS | ILE | ||||
| 5 | TYR | ARG | ASP | SER | LEU | GLY | GLU | THR | VAL | MET | ||||
| 6 | ARG | MET | GLY | ASP | LEU | HIS | TYR | LEU | GLN | SER | ||||
| 7 | ARG | ASN | GLU | LYS | TRP | ARG | GLU | GLN | LEU | GLY | ||||
| 8 | GLN | LYS | PHE | GLU | GLU | ILE | ARG | TRP | LEU | ILE | ||||
| 9 | GLU | GLU | MET | ARG | HIS | ARG | LEU | LYS | PRO | THR | ||||
| 10 | GLU | ASN | SER | PHE | GLU | GLN | ILE | THR | PHE | MET | ||||
| 11 | GLN | ALA | LEU | GLN | LEU | LEU | LEU | GLU | VAL | GLU | ||||
| 12 | GLN | GLU | ILE | ARG | THR | PHE | SER | PHE | GLN |
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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCO | sample_1 | isotropic | condition_1 |
| 3D HNCA | sample_1 | isotropic | condition_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | condition_1 |
| 3D H(CCO)NH | sample_1 | isotropic | condition_1 |
| 3D HNCACB | sample_1 | isotropic | condition_1 |
| 3D HNCACO | sample_1 | isotropic | condition_1 |
| 3D hNCAnH | sample_1 | isotropic | condition_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | condition_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 shifts
SPARKY: Backbone
or all simulated shifts