BMRB Entry 27270
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27270
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Title: Backbone assignments of NS5A-D2 from Hepatitis C virus (JFH-1) phosphorylated by Casein Kinase II PubMed: 29876401
Deposition date: 2017-10-03 Original release date: 2017-10-31
Authors: Hanoulle, Xavier
Citation: Bessa, Luiza; Schneider, Robert; Hanoulle, Xavier. "NMR and circular dichroism data for domain 2 of the HCV NS5A protein phosphorylated by the Casein Kinase II" Data Brief 17, .-325 (333).
Assembly members:
pNS5A-D2, polymer, 103 residues, Formula weight is not available
Natural source: Common Name: Hepatitis C Taxonomy ID: 11103 Superkingdom: Viruses Kingdom: not available Genus/species: Hepacivirus Hepatitis C
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pT7.7
Entity Sequences (FASTA):
pNS5A-D2: MNTYDVDMVDANLLMEGGVA
QTEPESRVPVLDFLEPMAEE
EXDLEPSIPSECMLPRSGFP
RALPAWARPDYNPPLVESWR
RPDYQPPTVAGCALPLQHHH
HHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 278 |
| 15N chemical shifts | 80 |
| 1H chemical shifts | 80 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | pNS5A-D2 | 1 |
Entities:
Entity 1, pNS5A-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 | SEP | 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: pNS5A-D2, [U-100% 13C; U-100% 15N], 250 uM; sodium phosphate 20 mM; sodium chloride 30 mM; THP 1 mM; sodium azide 0.02%
sample_conditions_1: ionic strength: 0.03 M; pH: 6.3; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)NNH | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection
In_house_product_plane_algorithm, in-house software - chemical shift calculation, data analysis
NMR spectrometers:
- Bruker AvanceIII 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts