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 16165

Title: 1H, 15N and 13C backbone resonance assignments of domain 2 (D2) of the non-structural 5A protein (NS5A) from the JFH1 Hepatitis C virus (HCV) strain.   PubMed: 19297321

Deposition date: 2009-02-11 Original release date: 2009-03-20

Authors: Hanoulle, Xavier; Badillo, Aurelie; Wieruszeski, Jean-Michel; Verdegem, Dries; Landrieu, Isabelle; Bartenschlager, Ralf; Penin, Francois; Lippens, Guy

Citation: Hanoulle, Xavier; Badillo, Aurelie; Wieruszeski, Jean-Michel; Verdegem, Dries; Landrieu, Isabelle; Bartenschlager, Ralf; Penin, Francois; Lippens, Guy. "Hepatitis C Virus NS5A protein is a substrate for the Peptidyl-Prolyl cis/trans Isomerase activity of Cyclophilins A and B."  J. Biol. Chem. ., .-. (2009).

Assembly members:
HCV_(JFH1)_NS5A-D2, polymer, 103 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
HCV_(JFH1)_NS5A-D2: MNTYDVDMVDANLLMEGGVA QTEPESRVPVLDFLEPMAEE ESDLEPSIPSECMLPRSGFP RALPAWARPDYNPPLVESWR RPDYQPPTVAGCALPLQHHH HHH

Data sets:
Data typeCount
13C chemical shifts277
15N chemical shifts80
1H chemical shifts80

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1HCV (JFH1) NS5A-D21

Entities:

Entity 1, HCV (JFH1) NS5A-D2 103 residues - Formula weight is not available

The first Methionine residue is a cloning artifact. The last 8 residues represent a non-native affinity tag. This is the domain 2 of the HCV (JFH1, genotype 2a) NS5A protein.

1   METASNTHRTYRASPVALASPMETVALASP
2   ALAASNLEULEUMETGLUGLYGLYVALALA
3   GLNTHRGLUPROGLUSERARGVALPROVAL
4   LEUASPPHELEUGLUPROMETALAGLUGLU
5   GLUSERASPLEUGLUPROSERILEPROSER
6   GLUCYSMETLEUPROARGSERGLYPHEPRO
7   ARGALALEUPROALATRPALAARGPROASP
8   TYRASNPROPROLEUVALGLUSERTRPARG
9   ARGPROASPTYRGLNPROPROTHRVALALA
10   GLYCYSALALEUPROLEUGLNHISHISHIS
11   HISHISHIS

Samples:

sample_1: HCV (JFH1) NS5A-D2, [U-95% 13C; U-98% 15N], 350 uM; sodium phosphate 20 mM; sodium chloride 30 mM; DTT 1 mM; sodium azide 0.02%; D2O 5%; H2O 95%

sample_conditions_1: ionic strength: 30 mM; pH: 6.4; pressure: 1.0 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCACOsample_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, Dries Verdegem & Guy Lippens - chemical shift assignment, data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

Swiss-Prot Q99IB8
Genbank AB047639
euHCVdb AB047639
DBJ BAB32872 BAD06942 BAF34893
GB ABX82715 ABY68009 ABY68010 ABY68011 ABY68012
SP Q99IB8

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