BMRB Entry 15579
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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/BMR15579
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Title: NS2(1-27) PubMed: 18644781
Deposition date: 2007-12-04 Original release date: 2008-06-04
Authors: Montserret, Roland; Penin, Francois
Citation: Jirasko, Vlastimil; Montserret, Roland; Appel, Nicole; Janvier, Anne; Eustachi, Leah; Brohm, Christiane; Steinmann, Eike; Pietschmann, Thomas; Penin, Francois; Bartenschlager, Ralf. "Structural and functional characterization of non-structural protein 2 for its role in hepatitis C virus assembly" J. Biol. Chem. 283, 28546-28562 (2008).
Assembly members:
NS2(1-27), polymer, 27 residues, 2834.36 Da.
Natural source: Common Name: not available Taxonomy ID: 11103 Superkingdom: Viruses Kingdom: not available Genus/species: Hepatitis C virus
Experimental source: Production method: chemical synthesis Host organism: none
Entity Sequences (FASTA):
NS2(1-27): MDREMAASAGGAVFVGLVLL
TLSPHYK
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 83 |
1H chemical shifts | 187 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | NS2(1-27) | 1 |
Entities:
Entity 1, NS2(1-27) 27 residues - 2834.36 Da.
1 | MET | ASP | ARG | GLU | MET | ALA | ALA | SER | ALA | GLY | ||||
2 | GLY | ALA | VAL | PHE | VAL | GLY | LEU | VAL | LEU | LEU | ||||
3 | THR | LEU | SER | PRO | HIS | TYR | LYS |
Samples:
sample_1: NS2(1-27) 0.9 ± 0.1 mM; Trifluoro ethanol D2OH, [U-100% 2H], 50 % v/v; H2O 90 % v/v
sample_conditions_1: pH: .; pressure: 1 atm; temperature: 298 K
sample_conditions_2: temperature: 308 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 |
2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_2 |
2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_2 |
2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_2 |
Software:
VNMR, Varian - collection, processing
SPARKY, Goddard - chemical shift assignment, data analysis, peak picking
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution
NMR spectrometers:
- Varian UnityPlus 500 MHz
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