BMRB Entry 16359
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR16359
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Title: chemical shift assignment of West Nile protease in the absence of inhibitor PubMed: 19997625
Deposition date: 2009-06-19 Original release date: 2009-12-16
Authors: Su, Xun-Cheng
Citation: Su, Xun-Cheng; Ozawa, Kiyoshi; Qi, Ruhu; Vasudevan, Subhash; Lim, Siew; Otting, Gottfried. "NMR analysis of the dynamic exchange of the NS2B cofactor between open and closed conformations of the West Nile virus NS2B-NS3 protease." PLoS Negl. Trop. Dis. 3, .-. (2009).
Assembly members:
West_Nile_virus_protease, polymer, 226 residues, Formula weight is not available
Natural source: Common Name: west nile virus Taxonomy ID: 11082 Superkingdom: virus Kingdom: not available Genus/species: Flavivirus west nile virus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
West_Nile_virus_protease: GDTTTGVYRIMTRGLLGSYQ
AGAGVMVEGVFHTLWHTTKG
AALMSGEGRLDPYWGSVKED
RLCYGGPWKLQHKWNGHDEV
QMIVVEPGKNVKNVQTKPGV
FKTPEGEIGAVTLDYPTGTS
GSPIVDKNGDVIGLYGNGVI
MPNGSYISAIVQGERMEEPA
PAGFEPEMLRKKGSHMLETD
MWIERTADITWESDAEITGS
SERVDVRLDDDGNFQLMNDP
GAPWAG
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 200 |
| 1H chemical shifts | 200 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | NS2B_NS3pro | 1 |
Entities:
Entity 1, NS2B_NS3pro 226 residues - Formula weight is not available
| 1 | GLY | ASP | THR | THR | THR | GLY | VAL | TYR | ARG | ILE | ||||
| 2 | MET | THR | ARG | GLY | LEU | LEU | GLY | SER | TYR | GLN | ||||
| 3 | ALA | GLY | ALA | GLY | VAL | MET | VAL | GLU | GLY | VAL | ||||
| 4 | PHE | HIS | THR | LEU | TRP | HIS | THR | THR | LYS | GLY | ||||
| 5 | ALA | ALA | LEU | MET | SER | GLY | GLU | GLY | ARG | LEU | ||||
| 6 | ASP | PRO | TYR | TRP | GLY | SER | VAL | LYS | GLU | ASP | ||||
| 7 | ARG | LEU | CYS | TYR | GLY | GLY | PRO | TRP | LYS | LEU | ||||
| 8 | GLN | HIS | LYS | TRP | ASN | GLY | HIS | ASP | GLU | VAL | ||||
| 9 | GLN | MET | ILE | VAL | VAL | GLU | PRO | GLY | LYS | ASN | ||||
| 10 | VAL | LYS | ASN | VAL | GLN | THR | LYS | PRO | GLY | VAL | ||||
| 11 | PHE | LYS | THR | PRO | GLU | GLY | GLU | ILE | GLY | ALA | ||||
| 12 | VAL | THR | LEU | ASP | TYR | PRO | THR | GLY | THR | SER | ||||
| 13 | GLY | SER | PRO | ILE | VAL | ASP | LYS | ASN | GLY | ASP | ||||
| 14 | VAL | ILE | GLY | LEU | TYR | GLY | ASN | GLY | VAL | ILE | ||||
| 15 | MET | PRO | ASN | GLY | SER | TYR | ILE | SER | ALA | ILE | ||||
| 16 | VAL | GLN | GLY | GLU | ARG | MET | GLU | GLU | PRO | ALA | ||||
| 17 | PRO | ALA | GLY | PHE | GLU | PRO | GLU | MET | LEU | ARG | ||||
| 18 | LYS | LYS | GLY | SER | HIS | MET | LEU | GLU | THR | ASP | ||||
| 19 | MET | TRP | ILE | GLU | ARG | THR | ALA | ASP | ILE | THR | ||||
| 20 | TRP | GLU | SER | ASP | ALA | GLU | ILE | THR | GLY | SER | ||||
| 21 | SER | GLU | ARG | VAL | ASP | VAL | ARG | LEU | ASP | ASP | ||||
| 22 | ASP | GLY | ASN | PHE | GLN | LEU | MET | ASN | ASP | PRO | ||||
| 23 | GLY | ALA | PRO | TRP | ALA | GLY |
Samples:
sample_1: West Nile virus protease, [U-15N], 0.9 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.02 M; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - chemical shift assignment
NMR spectrometers:
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts