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 PubMed: 18186541
Deposition date: 2007-10-09 Original release date: 2008-07-29
Authors: Wittlich, Marc; Koenig, Bernd; Willbold, Dieter
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).
Assembly members:
VpUcyt, polymer, 45 residues, 5009.3 Da.
Natural source: Common Name: HIV Taxonomy ID: 11676 Superkingdom: Viruses Kingdom: not available Genus/species: Lentivirus HIV
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
VpUcyt: GSIDRLIDRITERAEDSGNE
SEGDQEELSALVERGHLAPW
DVDDL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 185 |
| 15N chemical shifts | 50 |
| 1H chemical shifts | 297 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | VpU polypeptide | 1 |
Entities:
Entity 1, VpU polypeptide 45 residues - 5009.3 Da.
| 1 | GLY | SER | ILE | ASP | ARG | LEU | ILE | ASP | ARG | ILE | ||||
| 2 | THR | GLU | ARG | ALA | GLU | ASP | SER | GLY | ASN | GLU | ||||
| 3 | SER | GLU | GLY | ASP | GLN | GLU | GLU | LEU | SER | ALA | ||||
| 4 | LEU | VAL | GLU | ARG | GLY | HIS | LEU | ALA | PRO | TRP | ||||
| 5 | ASP | VAL | ASP | ASP | LEU |
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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_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
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts