BMRB Entry 11053

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11053

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Title:
Chemical shifts assignment for the West Nile virus NS2B(K96A)-NS3 protease
Deposition date:
2008-07-24
Original release date:
2009-07-14
Authors:
Yagi, Hiromasa
Citation:

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).
PubMed: 19583774

Assembly members:

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:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
the West Nile virus NS2B(K96A)-NS3 protease: TDMWIERTADITWESDAEIT GSSERVDVRLDDDGNFQLMN DPGAPWAGGGGSGGGGGGVL WDTPSPKEYKKGDTTTGVYR IMTRGLLGSYQAGAGVMVEG VFHTLWHTTKGAALMSGEGR LDPYWGSVKEDRLCYGGPWK LQHKWNGHDEVQMIVVEPGK NVKNVQTKPGVFKTPEGEIG AVTLDYPTGTSGSPIVDKNG DVIGLYGNGVIMPNGSYISA IVQGERMEEPAPAGFEPEML RKK

Data sets:
Data typeCount
13C chemical shifts543
15N chemical shifts197
1H chemical shifts1223

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1the West Nile virus NS2B(K96A)-NS3 protease1
22,5-methylenisothiourea-PXY2

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   THRASPMETTRPILEGLUARGTHRALAASP
2   ILETHRTRPGLUSERASPALAGLUILETHR
3   GLYSERSERGLUARGVALASPVALARGLEU
4   ASPASPASPGLYASNPHEGLNLEUMETASN
5   ASPPROGLYALAPROTRPALAGLYGLYGLY
6   GLYSERGLYGLYGLYGLYGLYGLYVALLEU
7   TRPASPTHRPROSERPROLYSGLUTYRLYS
8   LYSGLYASPTHRTHRTHRGLYVALTYRARG
9   ILEMETTHRARGGLYLEULEUGLYSERTYR
10   GLNALAGLYALAGLYVALMETVALGLUGLY
11   VALPHEHISTHRLEUTRPHISTHRTHRLYS
12   GLYALAALALEUMETSERGLYGLUGLYARG
13   LEUASPPROTYRTRPGLYSERVALLYSGLU
14   ASPARGLEUCYSTYRGLYGLYPROTRPLYS
15   LEUGLNHISLYSTRPASNGLYHISASPGLU
16   VALGLNMETILEVALVALGLUPROGLYLYS
17   ASNVALLYSASNVALGLNTHRLYSPROGLY
18   VALPHELYSTHRPROGLUGLYGLUILEGLY
19   ALAVALTHRLEUASPTYRPROTHRGLYTHR
20   SERGLYSERPROILEVALASPLYSASNGLY
21   ASPVALILEGLYLEUTYRGLYASNGLYVAL
22   ILEMETPROASNGLYSERTYRILESERALA
23   ILEVALGLNGLYGLUARGMETGLUGLUPRO
24   ALAPROALAGLYPHEGLUPROGLUMETLEU
25   ARGLYSLYS

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CC(CO)NHsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 13C-HMQC-NOESYsample_1isotropicsample_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 HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks