BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 16461

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

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

Data sets:
  • assigned_chemical_shifts
  • binding_constants
Data typeCount
binding constants6

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Vpr(52-96)11
2Vpr(52-96)21

Entities:

Entity 1, Vpr(52-96)1 45 residues - Formula weight is not available

1   ASPTHRTRPTHRPHEVALGLUALALEUILE
2   ARGILELEUGLNGLNLEULEUPHEILEHIS
3   PHEARGILEGLYCYSARGHISSERARGILE
4   GLYILEILEGLNGLNARGARGTHRARGASN
5   GLYALASERLYSSER

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_2
2D 1H-15N HSQCsample_1isotropicsample_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

Related Database Links:

BMRB 4257 4257
PDB
GB AAA81039
SP Q73369