BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 26996

Title: Backbone assignments for NS2b, NS3 complex   PubMed: 28751017

Deposition date: 2017-01-18 Original release date: 2017-08-10

Authors: Agback, Peter; Woestenenk, Esmeralda

Citation: Woestenenk, Esmeralda; Agback, Peter; Unnerstale, Sofia; Henderson, Ian; Agback, Tatiana. "Co-refolding of a functional complex of Dengue NS3 protease and NS2B co-factor domain and backbone resonance assignment by solution NMR"  Protein Expr. Purif. 140, 16-27 (2017).

Assembly members:
NS2B, polymer, 70 residues, Formula weight is not available
NS3, polymer, 194 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
NS2B: MGSSHHHHHHSSGLVPRGSH MLEADLELERAADVRWEEQA EISGSSPILSITISEDGSMS IKNEEEEQTL
NS3: MSHHHHHHSAGVLWDVPSPP PVGKAELEDGAYRIKQKGIL GYSQIGAGVYKEGTFHTMWH VTRGAVLMHKGKRIEPSWAD VKKDLISYGGGWKLEGEWKE GEEVQVLALEPGKNPRAVQT KPGLFKTNTGTIGAVSLDFS PGTSGSPIVDKKGKVVGLYG NGVVTRSGAYVSAIAQTEKS IEDNPEIEDDIFRK

Data sets:
Data typeCount
13C chemical shifts332
15N chemical shifts193
1H chemical shifts193

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NS2B1
2NS32

Entities:

Entity 1, NS2B 70 residues - Formula weight is not available

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METLEUGLUALAASPLEUGLULEUGLUARG
4   ALAALAASPVALARGTRPGLUGLUGLNALA
5   GLUILESERGLYSERSERPROILELEUSER
6   ILETHRILESERGLUASPGLYSERMETSER
7   ILELYSASNGLUGLUGLUGLUGLNTHRLEU

Entity 2, NS3 194 residues - Formula weight is not available

1   METSERHISHISHISHISHISHISSERALA
2   GLYVALLEUTRPASPVALPROSERPROPRO
3   PROVALGLYLYSALAGLULEUGLUASPGLY
4   ALATYRARGILELYSGLNLYSGLYILELEU
5   GLYTYRSERGLNILEGLYALAGLYVALTYR
6   LYSGLUGLYTHRPHEHISTHRMETTRPHIS
7   VALTHRARGGLYALAVALLEUMETHISLYS
8   GLYLYSARGILEGLUPROSERTRPALAASP
9   VALLYSLYSASPLEUILESERTYRGLYGLY
10   GLYTRPLYSLEUGLUGLYGLUTRPLYSGLU
11   GLYGLUGLUVALGLNVALLEUALALEUGLU
12   PROGLYLYSASNPROARGALAVALGLNTHR
13   LYSPROGLYLEUPHELYSTHRASNTHRGLY
14   THRILEGLYALAVALSERLEUASPPHESER
15   PROGLYTHRSERGLYSERPROILEVALASP
16   LYSLYSGLYLYSVALVALGLYLEUTYRGLY
17   ASNGLYVALVALTHRARGSERGLYALATYR
18   VALSERALAILEALAGLNTHRGLULYSSER
19   ILEGLUASPASNPROGLUILEGLUASPASP
20   ILEPHEARGLYS

Samples:

sample_1: NS2B, [U-13C; U-15N; U-2H], 0.3 mM; NS3, [U-13C; U-15N; U-2H], 0.3 mM; Boronic acid 1.0 mM; MES, [U-100% 2H], 20 mM; sodium chloride 100 mM; sodium azide 0.02%; calcium chloride 5 mM

sample_2: NS2B 0.3 mM; NS3, [U-13C; U-15N; U-2H], 0.3 mM; Boronic acid 1.0 mM; MES, [U-100% 2H], 20 mM; sodium chloride 100 mM; sodium azide 0.02%; calcium chloride 5 mM

sample_3: NS2B, [U-13C; U-15N; U-2H], 0.3 mM; NS3 0.3 mM; Boronic acid 1.0 mM; MES, [U-100% 2H], 20 mM; sodium chloride 100 mM; sodium azide 0.02%; calcium chloride 5 mM

sample_conditions_1: pH: 6.5; 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 HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
3D HNCAsample_3isotropicsample_conditions_1
3D HN(CO)CAsample_3isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

CCPN, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts