BMRB Entry 16798

Title:
1H, 15N and 13C backbone resonance assignments of domain 3 of the non-structural 5A (NS5A) protein from Hepatitis C Virus (JFH-1)
Deposition date:
2010-03-29
Original release date:
2011-05-02
Authors:
Verdegem, Dries; Badillo, Aurelie; Wieruszeski, Jean-Michel; Landrieu, Isabelle; Bartenschlager, Ralf; Penin, Francois; Lippens, Guy; Hanoulle, Xavier
Citation:

Citation: Verdegem, Dries; Badillo, Aurelie; Wieruszeski, Jean-Michel; Landrieu, Isabelle; Leroy, Arnaud; Bartenschlager, Ralf; Penin, Francois; Lippens, Guy; Hanoulle, Xavier. "Domain 3 of NS5A Protein from the Hepatitis C Virus Has Intrinsic {alpha}-Helical Propensity and Is a Substrate of Cyclophilin A."  J. Biol. Chem. 286, 20441-20454 (2011).
PubMed: 21489988

Assembly members:

Assembly members:
NS5A-D3, polymer, 119 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Hepatitis C Virus   Taxonomy ID: 11103   Superkingdom: Virus   Kingdom: not available   Genus/species: Hepacivirus Hepatitis C Virus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pT7.7

Data sets:
Data typeCount
13C chemical shifts306
15N chemical shifts97
1H chemical shifts97

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NS5A-D31

Entities:

Entity 1, NS5A-D3 119 residues - Formula weight is not available

1   METARGTHRVALGLYLEUSERGLUSERTHR
2   ILESERGLUALALEUGLNGLNLEUALAILE
3   LYSTHRPHEGLYGLNPROPROSERSERGLY
4   ASPALAGLYSERSERTHRGLYALAGLYALA
5   ALAGLUSERGLYGLYPROTHRSERPROGLY
6   GLUPROALAPROSERGLUTHRGLYSERALA
7   SERSERMETPROPROLEUGLUGLYGLUPRO
8   GLYASPPROASPLEUGLUSERASPGLNVAL
9   GLULEUGLNPROPROPROGLNGLYGLYGLY
10   VALALAPROGLYSERGLYSERGLYSERTRP
11   SERTHRCYSSERGLUGLUASPASPTHRTHR
12   VALLEUGLNHISHISHISHISHISHIS

Samples:

sample_1: HCV (JFH-1) NS5A-D3, [U-95% 13C; U-98% 15N], 500 uM; sodium phosphate 20 mM; sodium chloride 30 mM; sodium azide 0.02%; THP 1 mM; D2O, [U-99.9% 2H], 5%; H2O 95%

sample_conditions_1: ionic strength: 30 mM; pH: 6.3; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCANNHsample_1isotropicsample_conditions_1

Software:

TOPSPIN v1.3, Bruker Biospin - collection, processing

In_house_product_plane_algorithm v1.5, Dries Verdegem & Guy Lippens - data analysis

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

UniProt Q99IB8
Genbank AB047639
EuHCVdb AB047639
BMRB 16799
DBJ BAB32872 BAD06942 BAF34893
GB ABX82715 ABY68009 ABY68010 ABY68011 ABY68012
SP Q99IB8
AlphaFold Q99IB8 Q99IB8

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