BMRB Entry 16799
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16799
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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 (JFH-1) 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_(JFH-1)_NS5A-D3, polymer, 119 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_(JFH-1)_NS5A-D3: MRTVGLSESTISEALQQLAI
KTFGQPPSSGDAGSSTGAGA
AESGGPTSPGEPAPSETGSA
SSMPPLEGEPGDPDLESDQV
ELQPPPQGGGVAPGSGSGSW
STCSEEDDTTVLQHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 299 |
| 15N chemical shifts | 97 |
| 1H chemical shifts | 97 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | NS5A-D3 | 1 |
Entities:
Entity 1, NS5A-D3 119 residues - Formula weight is not available
| 1 | MET | ARG | THR | VAL | GLY | LEU | SER | GLU | SER | THR | ||||
| 2 | ILE | SER | GLU | ALA | LEU | GLN | GLN | LEU | ALA | ILE | ||||
| 3 | LYS | THR | PHE | GLY | GLN | PRO | PRO | SER | SER | GLY | ||||
| 4 | ASP | ALA | GLY | SER | SER | THR | GLY | ALA | GLY | ALA | ||||
| 5 | ALA | GLU | SER | GLY | GLY | PRO | THR | SER | PRO | GLY | ||||
| 6 | GLU | PRO | ALA | PRO | SER | GLU | THR | GLY | SER | ALA | ||||
| 7 | SER | SER | MET | PRO | PRO | LEU | GLU | GLY | GLU | PRO | ||||
| 8 | GLY | ASP | PRO | ASP | LEU | GLU | SER | ASP | GLN | VAL | ||||
| 9 | GLU | LEU | GLN | PRO | PRO | PRO | GLN | GLY | GLY | GLY | ||||
| 10 | VAL | ALA | PRO | GLY | SER | GLY | SER | GLY | SER | TRP | ||||
| 11 | SER | THR | CYS | SER | GLU | GLU | ASP | ASP | THR | THR | ||||
| 12 | VAL | LEU | GLN | HIS | HIS | HIS | HIS | HIS | HIS |
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 2 mM; D2O, [U-99.9% 2H], 5%; H2O 95%; TFE, [U-100% 2H], 50%
sample_conditions_1: ionic strength: 30 mM; pH: 6.35; 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:
| UniProt | Q99IB8 |
| Genbank | AB047639 |
| EuHCVdb | AB047639 |
| BMRB | 16798 |
| DBJ | BAB32872 BAD06942 BAF34893 |
| GB | ABX82715 ABY68009 ABY68010 ABY68011 ABY68012 |
| SP | Q99IB8 |
Download simulated HSQC data in one of the following formats:
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