BMRB Entry 16800
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16800
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Title: 1H, 15N and 13C backbone resonance assignments of domain 3 of the non-structural 5A (NS5A) protein from Hepatitis C Virus (Con1) in presence of 50%TFE PubMed: 21489988
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: 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).
Assembly members:
HCV_(Con1)_NS5A-D3, polymer, 96 residues, Formula weight is not available
Natural source: Common Name: Hepatitis C Virus Taxonomy ID: 11103 Superkingdom: Virus Kingdom: not available Genus/species: Hepacivirus Hepatitis C Virus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
HCV_(Con1)_NS5A-D3: MRTVVLSESTVSSALAELAT
KTFGSSESSAVDSGTATASP
DQPSDDGDAGSDVESYSSMP
PLEGEPGDPDLSDGSWSTVS
EEASEDVVLQHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 252 |
| 15N chemical shifts | 82 |
| 1H chemical shifts | 82 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | NS5A-D3 | 1 |
Entities:
Entity 1, NS5A-D3 96 residues - Formula weight is not available
| 1 | MET | ARG | THR | VAL | VAL | LEU | SER | GLU | SER | THR | ||||
| 2 | VAL | SER | SER | ALA | LEU | ALA | GLU | LEU | ALA | THR | ||||
| 3 | LYS | THR | PHE | GLY | SER | SER | GLU | SER | SER | ALA | ||||
| 4 | VAL | ASP | SER | GLY | THR | ALA | THR | ALA | SER | PRO | ||||
| 5 | ASP | GLN | PRO | SER | ASP | ASP | GLY | ASP | ALA | GLY | ||||
| 6 | SER | ASP | VAL | GLU | SER | TYR | SER | SER | MET | PRO | ||||
| 7 | PRO | LEU | GLU | GLY | GLU | PRO | GLY | ASP | PRO | ASP | ||||
| 8 | LEU | SER | ASP | GLY | SER | TRP | SER | THR | VAL | SER | ||||
| 9 | GLU | GLU | ALA | SER | GLU | ASP | VAL | VAL | LEU | GLN | ||||
| 10 | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: HCV (Con1) NS5A-D3, [U-95% 13C; U-98% 15N], 360 uM; sodium phosphate 20 mM; sodium chloride 30 mM; sodium azide 0.02%; THP 1 mM; D2O, [U-99.9% 2H], 5%; H2O 95%; TFE, [U-100% 2H], 50%
sample_conditions_1: ionic strength: 30 mM; pH: 6.4; pressure: 1 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 HNCACO | 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 v1.5, Dries Verdegem & Guy Lippens - data analysis
NMR spectrometers:
- Bruker Avance 800 MHz
Related Database Links:
| BMRB | 16166 |
| DBJ | BAD73972 BAD73974 BAD73975 BAD73984 BAD73985 |
| EMBL | CAB46677 CAB46911 CAB46913 CAB46915 CAB46917 |
| GB | AAL55821 AAY23099 AAY23100 AAY23101 AAY23102 |
| SP | Q9WMX2 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts