BMRB Entry 27539
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27539
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Title: Influenza A virus non-structural protein 1 (NS1) effector domain PubMed: 30076219
Deposition date: 2018-07-11 Original release date: 2018-11-15
Authors: Kleinpeter, Alex; Petit, Chad
Citation: Kleinpeter, Alex; Jureka, Alex; Fallahat, Sally; Green, Todd; Petit, Chad. "Structural analyses reveal the mechanism of inhibition of influenza virus NS1 by two antiviral compounds" J. Biol. Chem. 293, 14659-14668 (2018).
Assembly members:
NS1_Effector_Domain, polymer, 120 residues, Formula weight is not available
Natural source: Common Name: Influenza A virus Taxonomy ID: 11320 Superkingdom: Viruses Kingdom: not available Genus/species: Alphainfluenzavirus Influenza A virus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-SUMO
Entity Sequences (FASTA):
NS1_Effector_Domain: ASRYLTDMTLEEMSRDWFML
MPKQKVAGSLCIRMDQAIMD
KNIILKANFSVIFDRLETLI
LLRAFTEEGAIVGEISPLPS
LPGHTDEDVKNAVGVLIGGL
EANDNTVRVSETLQRFAWRS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 185 |
| 15N chemical shifts | 99 |
| 1H chemical shifts | 99 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | NS1 Effector Domain | 1 |
Entities:
Entity 1, NS1 Effector Domain 120 residues - Formula weight is not available
Construct consists of residues 86-205. The sequence provided begins and ends at these positions.
| 1 | ALA | SER | ARG | TYR | LEU | THR | ASP | MET | THR | LEU | |
| 2 | GLU | GLU | MET | SER | ARG | ASP | TRP | PHE | MET | LEU | |
| 3 | MET | PRO | LYS | GLN | LYS | VAL | ALA | GLY | SER | LEU | |
| 4 | CYS | ILE | ARG | MET | ASP | GLN | ALA | ILE | MET | ASP | |
| 5 | LYS | ASN | ILE | ILE | LEU | LYS | ALA | ASN | PHE | SER | |
| 6 | VAL | ILE | PHE | ASP | ARG | LEU | GLU | THR | LEU | ILE | |
| 7 | LEU | LEU | ARG | ALA | PHE | THR | GLU | GLU | GLY | ALA | |
| 8 | ILE | VAL | GLY | GLU | ILE | SER | PRO | LEU | PRO | SER | |
| 9 | LEU | PRO | GLY | HIS | THR | ASP | GLU | ASP | VAL | LYS | |
| 10 | ASN | ALA | VAL | GLY | VAL | LEU | ILE | GLY | GLY | LEU | |
| 11 | GLU | ALA | ASN | ASP | ASN | THR | VAL | ARG | VAL | SER | |
| 12 | GLU | THR | LEU | GLN | ARG | PHE | ALA | TRP | ARG | SER |
Samples:
sample_1: NS1 Effector Domain, [U-99% 13C; U-99% 15N], 0.6 mM; NaCl 100 mM; NaPO4 20 mM
sample_conditions_1: ionic strength: 0.1 M; pH: 6.8; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection
CARA, Keller and Wuthrich - chemical shift assignment
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView, Johnson, One Moon Scientific - data analysis
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 850 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts