BMRB Entry 16165
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16165
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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
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 277 |
| 15N chemical shifts | 80 |
| 1H chemical shifts | 80 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | HCV (JFH1) NS5A-D2 | 1 |
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 | MET | ASN | THR | TYR | ASP | VAL | ASP | MET | VAL | ASP | ||||
| 2 | ALA | ASN | LEU | LEU | MET | GLU | GLY | GLY | VAL | ALA | ||||
| 3 | GLN | THR | GLU | PRO | GLU | SER | ARG | VAL | PRO | VAL | ||||
| 4 | LEU | ASP | PHE | LEU | GLU | PRO | MET | ALA | GLU | GLU | ||||
| 5 | GLU | SER | ASP | LEU | GLU | PRO | SER | ILE | PRO | SER | ||||
| 6 | GLU | CYS | MET | LEU | PRO | ARG | SER | GLY | PHE | PRO | ||||
| 7 | ARG | ALA | LEU | PRO | ALA | TRP | ALA | ARG | PRO | ASP | ||||
| 8 | TYR | ASN | PRO | PRO | LEU | VAL | GLU | SER | TRP | ARG | ||||
| 9 | ARG | PRO | ASP | TYR | GLN | PRO | PRO | THR | VAL | ALA | ||||
| 10 | GLY | CYS | ALA | LEU | PRO | LEU | GLN | HIS | HIS | HIS | ||||
| 11 | HIS | HIS | HIS |
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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCACO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCANNH | sample_1 | isotropic | sample_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