BMRB Entry 4257

Title:
(52-96)C-Terminal Domain of the HIV-1 Regulatory Protein VPR
Deposition date:
1998-10-28
Original release date:
1999-11-23
Authors:
Schuler, W.; de Rocquigny, H.; Baudat, Y.; Sire, J.; Roques, B.
Citation:

Citation: Schuler, W.; Wecker, K.; de Rocquigny, H.; Baudat, Y.; Sire, J.; Roques, B.. "NMR Structure of the (52-96) C-Terminal Domain of the HIV-1 Regulatory Protein Vpr : Molecular Insights into its Biological Functions"  J. Mol. Biol. 285, 2105-2117 (1999).

Assembly members:

Assembly members:
Vpr_HIV-1_(LAI), polymer, 45 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: HIV-1   Taxonomy ID: 11706   Superkingdom: not available   Kingdom: not available   Genus/species: Lentivirus HIV-1

Experimental source:

Experimental source:   Production method: chemically synthesized

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Vpr_HIV-1_(LAI): DTWTGVEALIRILQQLLFIH FRIGCRHSRIGIIQQRRTRN GASKS

Data sets:
Data typeCount
1H chemical shifts377
coupling constants26

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Vpr_HIV-1_(LAI)1

Entities:

Entity 1, Vpr_HIV-1_(LAI) 45 residues - Formula weight is not available

1   ASPTHRTRPTHRGLYVALGLUALALEUILE
2   ARGILELEUGLNGLNLEULEUPHEILEHIS
3   PHEARGILEGLYCYSARGHISSERARGILE
4   GLYILEILEGLNGLNARGARGTHRARGASN
5   GLYALASERLYSSER

Samples:

sample_one: Vpr_HIV-1_(LAI) 2.0 mM; DTT 10.0 mM; TFE, [U-2H], 4.1 M; D2O 5.6 M; H2O 33.3 M; TMSP 0.1 mM

sample_conditions_one: pH: 3.4; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
NOESYsample_onenot availablesample_conditions_one
TOCSYsample_onenot availablesample_conditions_one
E.COSYsample_onenot availablesample_conditions_one

Software:

UXNMR - Data acquisition, Processing

FELIX - Data evaluation, Data processing, Structure calculations

NMRchitect - Data evaluation, Data processing, Structure calculations

INSIGHTII - Data evaluation, Data processing, Structure calculations

NMR spectrometers:

  • Bruker AMX 600 MHz

Related Database Links:

BMRB 16461
PDB
GB AAA81039 AAX22726 AET05947 AGC36856
SP Q73369
AlphaFold Q73369 Q73369