BMRB Entry 50765
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50765
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Title: Assignments of free human Tsg101 UEV domain PubMed: 36740661
Deposition date: 2021-02-16 Original release date: 2023-09-11
Authors: Moschidi, Danai; Cantrelle, Francois-Xavier; Hanoulle, Xavier
Citation: Moschidi, Danai; Cantrelle, Francois-Xavier; Boll, Emmanuelle; Hanoulle, Xavier. "Backbone NMR resonance assignment of the apo human Tsg101-UEV domain" Biomol. NMR Assignm. 17, 49-54 (2023).
Assembly members:
entity_1, polymer, 147 residues, Formula weight is not available
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 Vector: pET28a
Entity Sequences (FASTA):
entity_1: GAMAVSESQLKKMVSKYKYR
DLTVRETVNVITLYKDLKPV
LDSYVFNDGSSRELMNLTGT
IPVPYRGNTYNIPICLWLLD
TYPYNPPICFVKPTSSMTIK
TGKHVDANGKIYLPYLHEWK
HPQSDLLGLIQVMIVVFGDE
PPVFSRP
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 441 |
| 15N chemical shifts | 156 |
| 1H chemical shifts | 308 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Tsg101_UEV | 1 |
Entities:
Entity 1, Tsg101_UEV 147 residues - Formula weight is not available
The author sequence numbering is the Uniprot Q99816 numbering without the 2 first residues from polymer sequence due to cloning tag.
| 1 | GLY | ALA | MET | ALA | VAL | SER | GLU | SER | GLN | LEU | ||||
| 2 | LYS | LYS | MET | VAL | SER | LYS | TYR | LYS | TYR | ARG | ||||
| 3 | ASP | LEU | THR | VAL | ARG | GLU | THR | VAL | ASN | VAL | ||||
| 4 | ILE | THR | LEU | TYR | LYS | ASP | LEU | LYS | PRO | VAL | ||||
| 5 | LEU | ASP | SER | TYR | VAL | PHE | ASN | ASP | GLY | SER | ||||
| 6 | SER | ARG | GLU | LEU | MET | ASN | LEU | THR | GLY | THR | ||||
| 7 | ILE | PRO | VAL | PRO | TYR | ARG | GLY | ASN | THR | TYR | ||||
| 8 | ASN | ILE | PRO | ILE | CYS | LEU | TRP | LEU | LEU | ASP | ||||
| 9 | THR | TYR | PRO | TYR | ASN | PRO | PRO | ILE | CYS | PHE | ||||
| 10 | VAL | LYS | PRO | THR | SER | SER | MET | THR | ILE | LYS | ||||
| 11 | THR | GLY | LYS | HIS | VAL | ASP | ALA | ASN | GLY | LYS | ||||
| 12 | ILE | TYR | LEU | PRO | TYR | LEU | HIS | GLU | TRP | LYS | ||||
| 13 | HIS | PRO | GLN | SER | ASP | LEU | LEU | GLY | LEU | ILE | ||||
| 14 | GLN | VAL | MET | ILE | VAL | VAL | PHE | GLY | ASP | GLU | ||||
| 15 | PRO | PRO | VAL | PHE | SER | ARG | PRO |
Samples:
sample_1: Tsg101_UEV, [U-99% 13C; U-99% 15N], 330 uM; sodium phosphate 50 mM; sodium chloride 50 mM; EDTA 0.1 mM
sample_conditions_1: ionic strength: 0.05 M; pH: 6.1; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCANH | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)NNH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCAN | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D (H)CACON | sample_1 | isotropic | sample_conditions_1 |
| 2D CON | sample_1 | isotropic | sample_conditions_1 |
| 2D CACO | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRFAM-SPARKY - chemical shift assignment, data analysis, peak picking
TOPSPIN - collection
NMRPipe - processing
qMDD - processing
NMR spectrometers:
- Bruker AVANCE III HD 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts