BMRB Entry 26873

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26873

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Title:
Backbone assignment of NS2B-NS3 Protease from Zika Virus
Deposition date:
2016-08-09
Original release date:
2016-11-21
Authors:
Li, Yan; Phoo, Wint Wint; Zhang, Zhenzhen; Lee, Michelle Yueqi; Loh, Ying Ru; Tan, Yaw Bia; Ng, Elizabeth Yihui; Lescar, Julien; Kang, CongBao; Luo, Dahai
Citation:

Citation: Phoo, Wint Wint; Li, Yan; Zhang, Zhenzhen; Lee, Michelle Yueqi; Loh, Ying Ru; Tan, Yaw Bia; Ng, Elizabeth Yihui; Lescar, Julien; Kang, CongBao; Luo, Dahai. "Structure of the NS2B-NS3 protease from Zika virus after self-cleavage"  Nat. Commun. 7, 13410-13410 (2016).
PubMed: 27845325

Assembly members:

Assembly members:
NS2B fragment (45-96), polymer, 78 residues, Formula weight is not available
NS3 fragment (1-177), polymer, 177 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Zika virus   Taxonomy ID: 64320   Superkingdom: Viruses   Kingdom: not available   Genus/species: Zika virus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NS2B fragment (45-96): MGSSHHHHHHSSGLVPRGSH MTGKSVDMYIERAGDITWEK DAEVTGNSPRLDVALDESGD FSLVEEDGPPMREKTGKR
NS3 fragment (1-177): SGALWDVPAPKEVKKGETTD GVYRVMTRRLLGSTQVGVGV MQEGVFHTMWHVTKGAALRS GEGRLDPYWGDVKQDLVSYC GPWKLDAAWDGLSEVQLLAV PPGERAKNIQTLPGIFKTKD GDIGAVALDYPAGTSGSPIL DKCGRVIGLYGNGVVIKNGS YVSAITQGKREEETPVE

Data typeCount
13C chemical shifts641
15N chemical shifts214
1H chemical shifts214

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NS2B fragment (45-96)1
2NS3 fragment (1-177)2

Entities:

Entity 1, NS2B fragment (45-96) 78 residues - Formula weight is not available

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METTHRGLYLYSSERVALASPMETTYRILE
4   GLUARGALAGLYASPILETHRTRPGLULYS
5   ASPALAGLUVALTHRGLYASNSERPROARG
6   LEUASPVALALALEUASPGLUSERGLYASP
7   PHESERLEUVALGLUGLUASPGLYPROPRO
8   METARGGLULYSTHRGLYLYSARG

Entity 2, NS3 fragment (1-177) 177 residues - Formula weight is not available

1   SERGLYALALEUTRPASPVALPROALAPRO
2   LYSGLUVALLYSLYSGLYGLUTHRTHRASP
3   GLYVALTYRARGVALMETTHRARGARGLEU
4   LEUGLYSERTHRGLNVALGLYVALGLYVAL
5   METGLNGLUGLYVALPHEHISTHRMETTRP
6   HISVALTHRLYSGLYALAALALEUARGSER
7   GLYGLUGLYARGLEUASPPROTYRTRPGLY
8   ASPVALLYSGLNASPLEUVALSERTYRCYS
9   GLYPROTRPLYSLEUASPALAALATRPASP
10   GLYLEUSERGLUVALGLNLEULEUALAVAL
11   PROPROGLYGLUARGALALYSASNILEGLN
12   THRLEUPROGLYILEPHELYSTHRLYSASP
13   GLYASPILEGLYALAVALALALEUASPTYR
14   PROALAGLYTHRSERGLYSERPROILELEU
15   ASPLYSCYSGLYARGVALILEGLYLEUTYR
16   GLYASNGLYVALVALILELYSASNGLYSER
17   TYRVALSERALAILETHRGLNGLYLYSARG
18   GLUGLUGLUTHRPROVALGLU

Samples:

sample_1: NS2B fragment (45-96), [U-13C; U-15N; U-2H], 0.8 mM; NS3 fragment (1-177), [U-13C; U-15N; U-2H], 0.8 mM; HEPES 20 mM; sodium chloride 150 mM; DTT 1 mM

sample_conditions_1: ionic strength: 170 mM; pH: 7.3; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

NMRPipe, Bruker Biospin, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Johnson, One Moon Scientific, Keller and Wuthrich - chemical shift assignment, 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