BMRB Entry 19765
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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/BMR19765
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
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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).
PubMed: 24741107
Assembly members:
entity, polymer, 25 residues, 3116.649 Da.
Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: GBVB virus
Experimental source: Production method: chemical synthesis Host organism: none Vector: none
Entity Sequences (FASTA):
entity: HAWYSHYVLKFFLLVFGENG
VFFYK
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 175 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | gbvb5 | 1 |
Entities:
Entity 1, gbvb5 25 residues - 3116.649 Da.
| 1 | HIS | ALA | TRP | TYR | SER | HIS | TYR | VAL | LEU | LYS | ||||
| 2 | PHE | PHE | LEU | LEU | VAL | PHE | GLY | GLU | ASN | GLY | ||||
| 3 | VAL | PHE | PHE | TYR | LYS |
Samples:
sample_1: entity 2 mM; TFE, [U-99% 2H], 50 % v/v; H2O 50 % v/v
sample_conditions_1: ionic strength: 0 M; pH: 6; pressure: 1 atm; temperature: 273 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection, processing
SPARKY, Goddard - chemical shift assignment, data analysis
X-PLOR_NIH v2.34, Schwieters, Kuszewski, Tjandra and Clore - structure solution
Molmol, Koradi, Billeter and Wuthrich - data analysis, structure solution
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker Avance 1000 MHz