BMRB Entry 15513

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15513

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Title:
1H, 13C and 15N Resonance Assignemnt of HIV-1 VpU cytoplasmic domain
Deposition date:
2007-10-09
Original release date:
2008-07-29
Authors:
Wittlich, Marc; Koenig, Bernd; Willbold, Dieter
Citation:

Citation: Wittlich, Marc; Koenig, Bernd; Willbold, Dieter. "Structural consequences of phosphorylation of two serine residues in the cytoplasmic domain of HIV-1 VpU"  J. Pept. Sci. 14, 804-810 (2008).
PubMed: 18186541

Assembly members:

Assembly members:
VpUcyt, polymer, 45 residues, 5009.3 Da.

Natural source:

Natural source:   Common Name: HIV   Taxonomy ID: 11676   Superkingdom: Viruses   Kingdom: not available   Genus/species: Lentivirus HIV

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEX-2T

Entity Sequences (FASTA):

Entity Sequences (FASTA):
VpUcyt: GSIDRLIDRITERAEDSGNE SEGDQEELSALVERGHLAPW DVDDL

Data sets:
Data typeCount
13C chemical shifts185
15N chemical shifts50
1H chemical shifts297

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1VpU polypeptide1

Entities:

Entity 1, VpU polypeptide 45 residues - 5009.3 Da.

1   GLYSERILEASPARGLEUILEASPARGILE
2   THRGLUARGALAGLUASPSERGLYASNGLU
3   SERGLUGLYASPGLNGLUGLULEUSERALA
4   LEUVALGLUARGGLYHISLEUALAPROTRP
5   ASPVALASPASPLEU

Samples:

sample_1: VpUcyt, [U-100% 13C; U-100% 15N], 1 mM; DPC, [U-100% 2H], 100 mM; sodium chloride 100 mM; sodium phosphate 20 mM; sodium azide 0.02 % w/v

sample_conditions_1: ionic strength: 100 mM; pH: 6.2; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

CARA v1.8.4a.5, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Keller and Wuthrich - chemical shift assignment, data analysis, processing

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
GB AAA45071 AEL00701 AEL00706 AEL00711 AEL00716
SP P19554
AlphaFold P19554

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks