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 27282

Title: Backbone assignment of Zika Virus NS2B-NS3 Protease in complex with a covalent inhibitor   PubMed: 29526431

Deposition date: 2017-10-13 Original release date: 2018-03-16

Authors: Li, Yan; Zhang, Zhenzhen; Phoo, Wint Wint; Loh, Ying Ru; Li, Rong; Yeap, Yoon Sheng; Yang, Hai Yan; Jansson, Anna; Hill, Jeffrey; Keller, Thomas H; Nacro, Kassoum; Luo, Dahai; Kang, CongBao

Citation: Li, Yan; Zhang, Zhenzhen; Phoo, Wint Wint; Loh, Ying Ru; Li, Rong; Yeap, Yoon Sheng; Yang, Hai Yan; Jansson, Anna; Hill, Jeffrey; Keller, Thomas H; Nacro, Kassoum; Luo, Dahai; Kang, CongBao. "Structural Insights into the Inhibition of Zika Virus NS2B-NS3 Protease by a Small-Molecule Inhibitor"  Structure 26, 555-564 (2018).

Assembly members:
NS2B_fragment, polymer, 73 residues, Formula weight is not available
NS3_fragment, polymer, 178 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

Entity Sequences (FASTA):
NS2B_fragment: MGSSHHHHHHSSGLVPRGSH MTGKSVDMYIERAGDITWEK DAEVTGNSPRLDVALDESGD FSLVEEDGPPMRE
NS3_fragment: GSGALWDVPAPKEVKKGETT DGVYRVMTRRLLGSTQVGVG VMQEGVFHTMWHVTKGAALR SGEGRLDPYWGDVKQDLVSY CGPWKLDAAWDGLSEVQLLA VPPGERAKNIQTLPGIFKTK DGDIGAVALDYPAGTSGSPI LDKCGRVIGLYGNGVVIKNG SYVSAITQGKREEETPVE

Data sets:
Data typeCount
13C chemical shifts561
15N chemical shifts190
1H chemical shifts190

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) 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) 178 residues - Formula weight is not available

1   GLYSERGLYALALEUTRPASPVALPROALA
2   PROLYSGLUVALLYSLYSGLYGLUTHRTHR
3   ASPGLYVALTYRARGVALMETTHRARGARG
4   LEULEUGLYSERTHRGLNVALGLYVALGLY
5   VALMETGLNGLUGLYVALPHEHISTHRMET
6   TRPHISVALTHRLYSGLYALAALALEUARG
7   SERGLYGLUGLYARGLEUASPPROTYRTRP
8   GLYASPVALLYSGLNASPLEUVALSERTYR
9   CYSGLYPROTRPLYSLEUASPALAALATRP
10   ASPGLYLEUSERGLUVALGLNLEULEUALA
11   VALPROPROGLYGLUARGALALYSASNILE
12   GLNTHRLEUPROGLYILEPHELYSTHRLYS
13   ASPGLYASPILEGLYALAVALALALEUASP
14   TYRPROALAGLYTHRSERGLYSERPROILE
15   LEUASPLYSCYSGLYARGVALILEGLYLEU
16   TYRGLYASNGLYVALVALILELYSASNGLY
17   SERTYRVALSERALAILETHRGLNGLYLYS
18   ARGGLUGLUGLUTHRPROVALGLU

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: 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 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