BMRB Entry 18768
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18768
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Title: Structural study of NS2(2-32) GBVB protein PubMed: 24741107
Deposition date: 2012-10-08 Original release date: 2014-04-07
Authors: Montserret, Roland; Penin, Francois; Martin, Annette
Citation: Boukadida, Celia; Marnata, Caroline; Montserret, Roland; Cohen, Lisette; Blumen, Brigitte; Gouttenoire, Jerome; Moradpour, Darius; Penin, Francois; Martin, Annette. "NS2 proteins of GB virus B and hepatitis C virus share common protease activities and membrane topologies." J. Virol. 88, 7426-7444 (2014).
Assembly members:
NS2_2-32_GBVB, polymer, 31 residues, 3370.069 Da.
Natural source: Common Name: Hepatitis GB virus B Taxonomy ID: 39113 Superkingdom: Viruses Kingdom: not available Genus/species: not available not available
Experimental source: Production method: chemical synthesis Host organism: none
Entity Sequences (FASTA):
NS2_2-32_GBVB: DTEIIGGLTIPPVVALVVMS
RFGFFAHLLPR
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 102 |
| 1H chemical shifts | 230 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | NS2_2-32_GBVB | 1 |
Entities:
Entity 1, NS2_2-32_GBVB 31 residues - 3370.069 Da.
| 1 | ASP | THR | GLU | ILE | ILE | GLY | GLY | LEU | THR | ILE | ||||
| 2 | PRO | PRO | VAL | VAL | ALA | LEU | VAL | VAL | MET | SER | ||||
| 3 | ARG | PHE | GLY | PHE | PHE | ALA | HIS | LEU | LEU | PRO | ||||
| 4 | ARG |
Samples:
sample_1: NS2_2-32_GBVB, [U-99% 2H], 2 ± 0.1 mM; TFE 50 % v/v; H2O 50 % v/v
sample_conditions_1: pH: 6; pressure: 1 atm; temperature: 273 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection, processing
SPARKY, Goddard - chemical shift assignment, data analysis
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution
Molmol, Koradi, Billeter and Wuthrich - data analysis, structure solution
NMR spectrometers:
- Bruker Avance 500 MHz