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:
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