BMRB Entry 16461
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR16461
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Title: The C-terminal domain of the HIV-1 regulatory protein Vpr adopts an antiparallel dimeric structure in solution via its leucine-zipper-like domain PubMed: 15571493
Deposition date: 2009-08-19 Original release date: 2010-03-08
Authors: Bourbigot, Sarah; Beltz, Herve; Denis, Jerome; Morellet, Nelly; Roques, Bernard; Mely, Yves; Bouaziz, Serge
Citation: Bourbigot, Sarah; Beltz, Herve; Denis, Jerome; Morellet, Nelly; Roques, Bernard; Mely, Yves; Bouaziz, Serge. "The C-terminal domain of the HIV-1 regulatory protein Vpr adopts an antiparallel dimeric structure in solution via its leucine-zipper-like domain" Biochem. J. 387, 333-341 (2005).
Assembly members:
Vpr(52-96), polymer, 45 residues, Formula weight is not available
Natural source: Common Name: HIV-1 Taxonomy ID: 11676 Superkingdom: Viruses Kingdom: not available Genus/species: Lentivirus HIV-1
Experimental source: Production method: chemical synthesis
Entity Sequences (FASTA):
Vpr(52-96): DTWTFVEALIRILQQLLFIH
FRIGCRHSRIGIIQQRRTRN
GASKS
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | Vpr(52-96)1 | 1 |
2 | Vpr(52-96)2 | 1 |
Entities:
Entity 1, Vpr(52-96)1 45 residues - Formula weight is not available
1 | ASP | THR | TRP | THR | PHE | VAL | GLU | ALA | LEU | ILE | ||||
2 | ARG | ILE | LEU | GLN | GLN | LEU | LEU | PHE | ILE | HIS | ||||
3 | PHE | ARG | ILE | GLY | CYS | ARG | HIS | SER | ARG | ILE | ||||
4 | GLY | ILE | ILE | GLN | GLN | ARG | ARG | THR | ARG | ASN | ||||
5 | GLY | ALA | SER | LYS | SER |
Samples:
sample_1: Vpr(52-96), [U-15% 13C; U-95% 15N], 0.03 2.0 mM; acetonitrile 30%; H2O 70%
sample_conditions_1: pH: 3.0; pressure: 1 atm; temperature: 293 K
sample_conditions_2: pH: 3.0; pressure: 1 atm; temperature: 308 K
sample_conditions_3: pH: 3.0; pressure: 1 atm; temperature: 313 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_2 |
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_3 |
Software:
xwinnmr, Bruker Biospin - processing
X-PLOR v3.84, Brunger - distance geometry
Procheck, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Tho - structure solution
InsightII, Accelrys Software Inc. - structure solution
NMR spectrometers:
- Bruker Avance 600 MHz