BMRB Entry 16892
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR16892
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Title: NS2 [60-99] PubMed: 21187906
Deposition date: 2010-04-22 Original release date: 2011-05-19
Authors: Montserret, Roland; Bartenschlager, Ralf; Penin, Francois
Citation: Jirasko, Vlastimil; Montserret, Roland; Lee, Ji Young; Gouttenoire, Jerome; Moradpour, Darius; Penin, Francois; Bartenschlager, Ralf. "Structural and functional studies of nonstructural protein 2 of the hepatitis C virus reveal its key role as organizer of virion assembly." PLoS Pathog. 6, .-. (2010).
Assembly members:
NS2[60-99], polymer, 40 residues, 4275.335 Da.
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: chemical synthesis Host organism: not applicable
Entity Sequences (FASTA):
NS2[60-99]: GRDAVILLTCAIHPELIFTI
TKILLAILGPLMVLQAGITK
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 297 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | NS2[60-99] | 1 |
Entities:
Entity 1, NS2[60-99] 40 residues - 4275.335 Da.
| 1 | GLY | ARG | ASP | ALA | VAL | ILE | LEU | LEU | THR | CYS | |
| 2 | ALA | ILE | HIS | PRO | GLU | LEU | ILE | PHE | THR | ILE | |
| 3 | THR | LYS | ILE | LEU | LEU | ALA | ILE | LEU | GLY | PRO | |
| 4 | LEU | MET | VAL | LEU | GLN | ALA | GLY | ILE | THR | LYS |
Samples:
sample_1: NS2[60-99] 0.4 mM; TFE, [U-2H], 50 % v/v; H2O 50 % v/v; DSS 0.2 uM
sample_conditions_1: pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection
SPARKY, Goddard - data analysis
X-PLOR NIH v2.24, Schwieters, Kuszewski, Tjandra and Clore - structure solution
NMR spectrometers:
- Bruker Avance 500 MHz