BMRB Entry 16886
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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/BMR16886
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Title: NS2 [27-59] PubMed: 21187906
Deposition date: 2010-04-21 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:
HCV NS2 [27-59], polymer, 33 residues, 4054.897 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: none
Entity Sequences (FASTA):
HCV NS2 [27-59]: KLFLARLIWWLQYFITRAEA
HLQVWIPPLNVRG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 120 |
| 1H chemical shifts | 270 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | HCV NS2 [27-59] | 1 |
Entities:
Entity 1, HCV NS2 [27-59] 33 residues - 4054.897 Da.
| 1 | LYS | LEU | PHE | LEU | ALA | ARG | LEU | ILE | TRP | TRP | ||||
| 2 | LEU | GLN | TYR | PHE | ILE | THR | ARG | ALA | GLU | ALA | ||||
| 3 | HIS | LEU | GLN | VAL | TRP | ILE | PRO | PRO | LEU | ASN | ||||
| 4 | VAL | ARG | GLY |
Samples:
sample_1: NS2 1.2 mM; TFE, [U-2H], 50 % v/v; H2O 50 % v/v
sample_conditions_1: ionic strength: 0 M; pH: 6; 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:
VNMR, Varian - collection
SPARKY, Goddard - chemical shift assignment
X-PLOR NIH v2.19, Schwieters, Kuszewski, Tjandra and Clore - structure solution
NMR spectrometers:
- Varian UnityPlus 500 MHz