BMRB Entry 18730
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18730
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Title: Chemical shift assignment of West Nile Virus NS2B-NS3 protease in a complex with 4-phenyl-phenyl-KKR-aldehyde. PubMed: 23211132
Deposition date: 2012-09-20 Original release date: 2013-02-12
Authors: Gayen, Shovanlal; Chen, Angela; Kang, Congbao
Citation: Kang, Congbao; Gayen, Shovanlal; Wang, Weiling; Severin, Rene; Chen, Angela Shuyi; Lim, Huichang Annie; Chia, Cheng San Brian; Schuller, Andreas; Doan, Danny Ngoc Phouc; Poulsen, Anders; Hill, Jeffrey; Vasudevan, Subhash; Keller, Thomas. "Exploring the binding of peptidic West Nile virus NS2B-NS3 protease inhibitors by NMR." Antiviral Res. 97, 137-144 (2013).
Assembly members:
West_nile_protease, polymer, 248 residues, Formula weight is not available
Natural source: Common Name: Escherichia coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
West_nile_protease: MAGSHHHHHHGSTDMWIERT
ADISWESDAEITGSSERVDV
RLDDDGNFQLMNDPGAGGGG
SGGGGGVLWDTPSPKEYKKG
DTTTGVYRIMTRGLLGSYQA
GAGVMVEGVFHTLWHTTKGA
ALMSGEGRLDPYWGSVKEDR
LCYGGPWKLQHKWNGQDEVQ
MIVVEPGKNVKNVQTKPGVF
KTPEGEIGAVTLDFPTGTSG
SPIVDKNGDVIGLYGNGVIM
PNGSYISAIVQGERMDEPIP
AGFEPEML
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 557 |
| 15N chemical shifts | 187 |
| 1H chemical shifts | 189 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | West_nile_protease | 1 |
Entities:
Entity 1, West_nile_protease 248 residues - Formula weight is not available
| 1 | MET | ALA | GLY | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | GLY | SER | THR | ASP | MET | TRP | ILE | GLU | ARG | THR | ||||
| 3 | ALA | ASP | ILE | SER | TRP | GLU | SER | ASP | ALA | GLU | ||||
| 4 | ILE | THR | GLY | SER | SER | GLU | ARG | VAL | ASP | VAL | ||||
| 5 | ARG | LEU | ASP | ASP | ASP | GLY | ASN | PHE | GLN | LEU | ||||
| 6 | MET | ASN | ASP | PRO | GLY | ALA | GLY | GLY | GLY | GLY | ||||
| 7 | SER | GLY | GLY | GLY | GLY | GLY | VAL | LEU | TRP | ASP | ||||
| 8 | THR | PRO | SER | PRO | LYS | GLU | TYR | LYS | LYS | GLY | ||||
| 9 | ASP | THR | THR | THR | GLY | VAL | TYR | ARG | ILE | MET | ||||
| 10 | THR | ARG | GLY | LEU | LEU | GLY | SER | TYR | GLN | ALA | ||||
| 11 | GLY | ALA | GLY | VAL | MET | VAL | GLU | GLY | VAL | PHE | ||||
| 12 | HIS | THR | LEU | TRP | HIS | THR | THR | LYS | GLY | ALA | ||||
| 13 | ALA | LEU | MET | SER | GLY | GLU | GLY | ARG | LEU | ASP | ||||
| 14 | PRO | TYR | TRP | GLY | SER | VAL | LYS | GLU | ASP | ARG | ||||
| 15 | LEU | CYS | TYR | GLY | GLY | PRO | TRP | LYS | LEU | GLN | ||||
| 16 | HIS | LYS | TRP | ASN | GLY | GLN | ASP | GLU | VAL | GLN | ||||
| 17 | MET | ILE | VAL | VAL | GLU | PRO | GLY | LYS | ASN | VAL | ||||
| 18 | LYS | ASN | VAL | GLN | THR | LYS | PRO | GLY | VAL | PHE | ||||
| 19 | LYS | THR | PRO | GLU | GLY | GLU | ILE | GLY | ALA | VAL | ||||
| 20 | THR | LEU | ASP | PHE | PRO | THR | GLY | THR | SER | GLY | ||||
| 21 | SER | PRO | ILE | VAL | ASP | LYS | ASN | GLY | ASP | VAL | ||||
| 22 | ILE | GLY | LEU | TYR | GLY | ASN | GLY | VAL | ILE | MET | ||||
| 23 | PRO | ASN | GLY | SER | TYR | ILE | SER | ALA | ILE | VAL | ||||
| 24 | GLN | GLY | GLU | ARG | MET | ASP | GLU | PRO | ILE | PRO | ||||
| 25 | ALA | GLY | PHE | GLU | PRO | GLU | MET | LEU |
Samples:
sample_1: West nile protease, [U-13C; U-15N], 0.8 mM; 4-Phenyl-phenylacetyl-KKR aldehyde 2 mM; HEPES 20 mM; DTT 1 mM; D2O 10%; H2O 90%
sample_conditions_1: ionic strength: 0 M; pH: 7.3; pressure: 1 atm; temperature: 298 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 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v1.3, Bruker Biospin - collection
SPARKY, Goddard - chemical shift assignment
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Bruker Avance 700 MHz
Related Database Links:
| PDB | |
| GB | ADX89821 ADX89822 ADX89823 ADX89824 ADX89825 |
| REF | NP_776018 YP_001527884 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts