BMRB Entry 16359

Title:
chemical shift assignment of West Nile protease in the absence of inhibitor
Deposition date:
2009-06-19
Original release date:
2009-12-16
Authors:
Su, Xun-Cheng
Citation:

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).
PubMed: 19997625

Assembly members:

Assembly members:
West_Nile_virus_protease, polymer, 226 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: west nile virus   Taxonomy ID: 11082   Superkingdom: virus   Kingdom: not available   Genus/species: Flavivirus west nile virus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET15b-WNV CF40GlyNS3pro187

Data sets:
  • assigned_chemical_shifts
Data typeCount
15N chemical shifts200
1H chemical shifts200

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1NS2B_NS3pro1

Entities:

Entity 1, NS2B_NS3pro 226 residues - Formula weight is not available

1   GLYASPTHRTHRTHRGLYVALTYRARGILE
2   METTHRARGGLYLEULEUGLYSERTYRGLN
3   ALAGLYALAGLYVALMETVALGLUGLYVAL
4   PHEHISTHRLEUTRPHISTHRTHRLYSGLY
5   ALAALALEUMETSERGLYGLUGLYARGLEU
6   ASPPROTYRTRPGLYSERVALLYSGLUASP
7   ARGLEUCYSTYRGLYGLYPROTRPLYSLEU
8   GLNHISLYSTRPASNGLYHISASPGLUVAL
9   GLNMETILEVALVALGLUPROGLYLYSASN
10   VALLYSASNVALGLNTHRLYSPROGLYVAL
11   PHELYSTHRPROGLUGLYGLUILEGLYALA
12   VALTHRLEUASPTYRPROTHRGLYTHRSER
13   GLYSERPROILEVALASPLYSASNGLYASP
14   VALILEGLYLEUTYRGLYASNGLYVALILE
15   METPROASNGLYSERTYRILESERALAILE
16   VALGLNGLYGLUARGMETGLUGLUPROALA
17   PROALAGLYPHEGLUPROGLUMETLEUARG
18   LYSLYSGLYSERHISMETLEUGLUTHRASP
19   METTRPILEGLUARGTHRALAASPILETHR
20   TRPGLUSERASPALAGLUILETHRGLYSER
21   SERGLUARGVALASPVALARGLEUASPASP
22   ASPGLYASNPHEGLNLEUMETASNASPPRO
23   GLYALAPROTRPALAGLY

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

PDB
GB AEL79849 AFX82689 AGC00412
REF NP_776018

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks