BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 26927

Title: Backbone assignment of unlinked NS2B-NS3 Protease of Zika Virus in complex with acetyl-lysine-arginine   PubMed: 27940580

Deposition date: 2016-10-28 Original release date: 2016-12-15

Authors: Li, Yan; Zhang, Zhenzhen; Loh, Ying Ru; Phoo, Wint Wint; Kang, CongBao; Luo, Dahai

Citation: Zhang, Zhenzhen; Li, Yan; Loh, Ying Ru; Phoo, Wint Wint; Hung, Alvin; Kang, CongBao; Luo, Dahai. "Crystal structure of unlinked NS2B-NS3 protease from Zika virus"  Science 354, 1597-1600 (2016).

Assembly members:
NS2B_fragment, polymer, 73 residues, Formula weight is not available
NS3_fragment, polymer, 177 residues, Formula weight is not available
acetyl-lysine-arginine, polymer, 3 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
NS2B_fragment: MGSSHHHHHHSSGLVPRGSH MTGKSVDMYIERAGDITWEK DAEVTGNSPRLDVALDESGD FSLVEEDGPPMRE
NS3_fragment: SGALWDVPAPKEVKKGETTD GVYRVMTRRLLGSTQVGVGV MQEGVFHTMWHVTKGAALRS GEGRLDPYWGDVKQDLVSYC GPWKLDAAWDGLSEVQLLAV PPGERAKNIQTLPGIFKTKD GDIGAVALDYPAGTSGSPIL DKCGRVIGLYGNGVVIKNGS YVSAITQGKREEETPVE
acetyl-lysine-arginine: XKR

Data typeCount
13C chemical shifts663
15N chemical shifts221
1H chemical shifts221

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
3acetyl-lysine-arginine3

Entities:

Entity 1, NS2B fragment (45-96) 73 residues - Formula weight is not available

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

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

Entity 3, acetyl-lysine-arginine 3 residues - Formula weight is not available

1   ACELYSARG

Samples:

sample_1: NS2B fragment, [U-13C; U-15N; U-2H], 0.8 mM; NS3 fragment, [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: 298 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 simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts