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 25592

Title: Solution-state NMR structure of Vpu cytoplasmic domain   PubMed: 26362058

Deposition date: 2015-05-01 Original release date: 2015-09-28

Authors: Zhang, H.; Lin, E.; Tian, Y.; Das, B.; Opella, S.

Citation: Zhang, H.; Lin, E.; Tian, Y.; Das, B.; Opella, S.. "Structural determination of virus protein U from HIV-1 by NMR in membrane environments"  Biochim. Biophys. Acta 1848, 3007-3018 (2015).

Assembly members:
HIV-1_Virus_protein_U, polymer, 54 residues, 6266.018 Da.
4-(trifluoromethyl)aniline, non-polymer, 161.124 Da.

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
HIV-1_Virus_protein_U: EYRKILRQRKIDRLIDRLIE RAEDSGNESEGEISALVELG VELGHHAPWDVDDL

Data sets:
Data typeCount
13C chemical shifts142
15N chemical shifts52
1H chemical shifts104

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1HIV-1 Virus protein U1
24-(TRIFLUOROMETHYL)ANILINE2

Entities:

Entity 1, HIV-1 Virus protein U 54 residues - 6266.018 Da.

1   GLUTYRARGLYSILELEUARGGLNARGLYS
2   ILEASPARGLEUILEASPARGLEUILEGLU
3   ARGALAGLUASPSERGLYASNGLUSERGLU
4   GLYGLUILESERALALEUVALGLULEUGLY
5   VALGLULEUGLYHISHISALAPROTRPASP
6   VALASPASPLEU

Entity 2, 4-(TRIFLUOROMETHYL)ANILINE - C7 H6 F3 N - 161.124 Da.

1   ANI

Samples:

sample_1: Vpu Cytoplasmic domain, [U-100% 15N], 0.5 mM; DHPC 100 mM; H20 90%; D2O 10%

sample_2: Vpu Cytoplasmic domain, [U-100% 13C; U-100% 15N], 0.5 mM; DHPC 100 mM; H20 90%; D2O 10%

sample_conditions_1: ionic strength: 5 mM; pH: 4.0; pressure: 1 atm; temperature: 323 K

Experiments:

NameSampleSample stateSample conditions
3D_15N-separated_NOESYsample_1isotropicsample_conditions_1
2D_15N/1N_HSQCsample_1isotropicsample_conditions_1
2D_15N/1N_HSQCIPAPsample_1isotropicsample_conditions_1
3D_HNCAsample_1isotropicsample_conditions_1
3D_HCCCONHsample_1isotropicsample_conditions_1
3D_CCCONHsample_1isotropicsample_conditions_1
3D_15N/13C'/13Csample_1isotropicsample_conditions_1
3D_HNCOsample_1isotropicsample_conditions_1
3D_HNCACBsample_1isotropicsample_conditions_1

Software:

CNS, Brunger A. T. et.al. - refinement

NMR spectrometers:

  • Bruker AVANCE 600 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts