BMRB Entry 11053
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11053
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Chemical shifts assignment for the West Nile virus NS2B(K96A)-NS3 protease PubMed: 19583774
Deposition date: 2008-07-24 Original release date: 2009-07-14
Authors: Yagi, Hiromasa
Citation: Su, Xun-Cheng; Ozawa, Kiyoshi; Yagi, Hiromasa; Lim, Siew; Wen, Daying; Ekonomiuk, Dariusz; Huang, Danzhi; Keller, Thomas; Sonntag, Sebastian; Caflisch, Amedeo; Vasudevan, Subhash; Otting, Gottfried. "NMR study of complexes between low molecular mass inhibitors and the West Nile virus NS2B-NS3 protease" FEBS J. 276, 4244-4255 (2009).
Assembly members:
the West Nile virus NS2B(K96A)-NS3 protease, polymer, 243 residues, Formula weight is not available
2,5-methylenisothiourea-PXY, non-polymer, 284.444 Da.
Natural source: Common Name: West Nile virus Taxonomy ID: 11082 Superkingdom: not available Kingdom: not available Genus/species: Flavivirus West Nile virus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
the West Nile virus NS2B(K96A)-NS3 protease: TDMWIERTADITWESDAEIT
GSSERVDVRLDDDGNFQLMN
DPGAPWAGGGGSGGGGGGVL
WDTPSPKEYKKGDTTTGVYR
IMTRGLLGSYQAGAGVMVEG
VFHTLWHTTKGAALMSGEGR
LDPYWGSVKEDRLCYGGPWK
LQHKWNGHDEVQMIVVEPGK
NVKNVQTKPGVFKTPEGEIG
AVTLDYPTGTSGSPIVDKNG
DVIGLYGNGVIMPNGSYISA
IVQGERMEEPAPAGFEPEML
RKK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 543 |
| 15N chemical shifts | 197 |
| 1H chemical shifts | 1223 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | the West Nile virus NS2B(K96A)-NS3 protease | 1 |
| 2 | 2,5-methylenisothiourea-PXY | 2 |
Entities:
Entity 1, the West Nile virus NS2B(K96A)-NS3 protease 243 residues - Formula weight is not available
The construction of this protein is composed of two domain (NS2B and NS3) jointed short linker. The numbering of amino acid is as follows. (550 - 605) NS2B domain and linker : The domain of the entry is a part of original NS2B (See reference_citation). TDMWIERTADITWESDAEIT GSSERVDVRLDDDGNFQLMN DPGAPWAGGGGSGGGG ( 1 - 187) NS3 domain : This numbering is based on reference_citation. GGVLWDTPSPKEYKKGDTTT GVYRIMTRGLLGSYQAGAGV MVEGVFHTLWHTTKGAALMS GEGRLDPYWGSVKEDRLCYG GPWKLQHKWNGHDEVQMIVV EPGKNVKNVQTKPGVFKTPE GEIGAVTLDYPTGTSGSPIV DKNGDVIGLYGNGVIMPNGS YISAIVQGERMEEPAPAGFE PEMLRKK
| 1 | THR | ASP | MET | TRP | ILE | GLU | ARG | THR | ALA | ASP | ||||
| 2 | ILE | THR | TRP | GLU | SER | ASP | ALA | GLU | ILE | THR | ||||
| 3 | GLY | SER | SER | GLU | ARG | VAL | ASP | VAL | ARG | LEU | ||||
| 4 | ASP | ASP | ASP | GLY | ASN | PHE | GLN | LEU | MET | ASN | ||||
| 5 | ASP | PRO | GLY | ALA | PRO | TRP | ALA | GLY | GLY | GLY | ||||
| 6 | GLY | SER | GLY | GLY | GLY | GLY | GLY | GLY | VAL | LEU | ||||
| 7 | TRP | ASP | THR | PRO | SER | PRO | LYS | GLU | TYR | LYS | ||||
| 8 | LYS | GLY | ASP | THR | THR | THR | GLY | VAL | TYR | ARG | ||||
| 9 | ILE | MET | THR | ARG | GLY | LEU | LEU | GLY | SER | TYR | ||||
| 10 | GLN | ALA | GLY | ALA | GLY | VAL | MET | VAL | GLU | GLY | ||||
| 11 | VAL | PHE | HIS | THR | LEU | TRP | HIS | THR | THR | LYS | ||||
| 12 | GLY | ALA | ALA | LEU | MET | SER | GLY | GLU | GLY | ARG | ||||
| 13 | LEU | ASP | PRO | TYR | TRP | GLY | SER | VAL | LYS | GLU | ||||
| 14 | ASP | ARG | LEU | CYS | TYR | GLY | GLY | PRO | TRP | LYS | ||||
| 15 | LEU | GLN | HIS | LYS | TRP | ASN | GLY | HIS | ASP | GLU | ||||
| 16 | VAL | GLN | MET | ILE | VAL | VAL | GLU | PRO | GLY | LYS | ||||
| 17 | ASN | VAL | LYS | ASN | VAL | GLN | THR | LYS | PRO | GLY | ||||
| 18 | VAL | PHE | LYS | THR | PRO | GLU | GLY | GLU | ILE | GLY | ||||
| 19 | ALA | VAL | THR | LEU | ASP | TYR | PRO | THR | GLY | THR | ||||
| 20 | SER | GLY | SER | PRO | ILE | VAL | ASP | LYS | ASN | GLY | ||||
| 21 | ASP | VAL | ILE | GLY | LEU | TYR | GLY | ASN | GLY | VAL | ||||
| 22 | ILE | MET | PRO | ASN | GLY | SER | TYR | ILE | SER | ALA | ||||
| 23 | ILE | VAL | GLN | GLY | GLU | ARG | MET | GLU | GLU | PRO | ||||
| 24 | ALA | PRO | ALA | GLY | PHE | GLU | PRO | GLU | MET | LEU | ||||
| 25 | ARG | LYS | LYS |
Entity 2, 2,5-methylenisothiourea-PXY - C12 H20 N4 S2 - 284.444 Da.
| 1 | 1 |
Samples:
sample_1: the West Nile virus NS2B(K96A)-NS3 protease, [U-98% 13C; U-98% 15N], 0.9 mM; 2,5-methylenisothiourea-PXY 3 mM
sample_conditions_1: ionic strength: 0 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 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D CC(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D (H)CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 13C-HMQC-NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - chemical shift assignment
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
| PDB | |
| EMBL | CAS03096 |
| 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