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.
Deposition date:
2012-09-20
Original release date:
2013-02-12
Authors:
Gayen, Shovanlal; Chen, Angela; Kang, Congbao
Citation:

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).
PubMed: 23211132

Assembly members:

Assembly members:
West_nile_protease, polymer, 248 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Escherichia coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21

Entity Sequences (FASTA):

Entity Sequences (FASTA):
West_nile_protease: MAGSHHHHHHGSTDMWIERT ADISWESDAEITGSSERVDV RLDDDGNFQLMNDPGAGGGG SGGGGGVLWDTPSPKEYKKG DTTTGVYRIMTRGLLGSYQA GAGVMVEGVFHTLWHTTKGA ALMSGEGRLDPYWGSVKEDR LCYGGPWKLQHKWNGQDEVQ MIVVEPGKNVKNVQTKPGVF KTPEGEIGAVTLDFPTGTSG SPIVDKNGDVIGLYGNGVIM PNGSYISAIVQGERMDEPIP AGFEPEML

Data sets:
Data typeCount
13C chemical shifts557
15N chemical shifts187
1H chemical shifts189

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1West_nile_protease1

Entities:

Entity 1, West_nile_protease 248 residues - Formula weight is not available

1   METALAGLYSERHISHISHISHISHISHIS
2   GLYSERTHRASPMETTRPILEGLUARGTHR
3   ALAASPILESERTRPGLUSERASPALAGLU
4   ILETHRGLYSERSERGLUARGVALASPVAL
5   ARGLEUASPASPASPGLYASNPHEGLNLEU
6   METASNASPPROGLYALAGLYGLYGLYGLY
7   SERGLYGLYGLYGLYGLYVALLEUTRPASP
8   THRPROSERPROLYSGLUTYRLYSLYSGLY
9   ASPTHRTHRTHRGLYVALTYRARGILEMET
10   THRARGGLYLEULEUGLYSERTYRGLNALA
11   GLYALAGLYVALMETVALGLUGLYVALPHE
12   HISTHRLEUTRPHISTHRTHRLYSGLYALA
13   ALALEUMETSERGLYGLUGLYARGLEUASP
14   PROTYRTRPGLYSERVALLYSGLUASPARG
15   LEUCYSTYRGLYGLYPROTRPLYSLEUGLN
16   HISLYSTRPASNGLYGLNASPGLUVALGLN
17   METILEVALVALGLUPROGLYLYSASNVAL
18   LYSASNVALGLNTHRLYSPROGLYVALPHE
19   LYSTHRPROGLUGLYGLUILEGLYALAVAL
20   THRLEUASPPHEPROTHRGLYTHRSERGLY
21   SERPROILEVALASPLYSASNGLYASPVAL
22   ILEGLYLEUTYRGLYASNGLYVALILEMET
23   PROASNGLYSERTYRILESERALAILEVAL
24   GLNGLYGLUARGMETASPGLUPROILEPRO
25   ALAGLYPHEGLUPROGLUMETLEU

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_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

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