BMRB Entry 10338
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR10338
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Title: Solution Structure of the First UBA Domain in the Human Ubiquitin Specific Protease 5 (Isopeptidase 5)
Deposition date: 2011-01-13 Original release date: 2019-09-04
Authors: Zhao, C.; Kigawa, T.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Yokoyama, S.
Citation: Zhao, C.; Kigawa, T.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Yokoyama, S.. "Solution Structure of the First UBA Domain in the Human Ubiquitin Specific Protease 5 (Isopeptidase 5)" .
Assembly members:
UBA domain, polymer, 54 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: cell free synthesis Host organism: Escherichia coli Vector: P050613-08
Entity Sequences (FASTA):
UBA domain: GLDESVIIQLVEMGFPMDAC
RKAVYYTGNSGAEAAMNWVM
SHMDDPDFANPLIL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 235 |
| 15N chemical shifts | 53 |
| 1H chemical shifts | 368 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | UBA domain | 1 |
Entities:
Entity 1, UBA domain 54 residues - Formula weight is not available
| 1 | GLY | LEU | ASP | GLU | SER | VAL | ILE | ILE | GLN | LEU | ||||
| 2 | VAL | GLU | MET | GLY | PHE | PRO | MET | ASP | ALA | CYS | ||||
| 3 | ARG | LYS | ALA | VAL | TYR | TYR | THR | GLY | ASN | SER | ||||
| 4 | GLY | ALA | GLU | ALA | ALA | MET | ASN | TRP | VAL | MET | ||||
| 5 | SER | HIS | MET | ASP | ASP | PRO | ASP | PHE | ALA | ASN | ||||
| 6 | PRO | LEU | ILE | LEU |
Samples:
sample_1: UBA domain, [U-13C; U-15N], 1.05 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%
condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 296.0 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 15N-separated NOESY | sample_1 | isotropic | condition_1 |
| 3D 13C-separated NOESY | sample_1 | isotropic | condition_1 |
Software:
TOPSPIN v2.1, Bruker - collection
NMRPipe, Delaglio, F. - processing
NMRView v5.0.4, Johnson, B. A. - data analysis
Kujira v0.9843, Kobayashi, N. - data analysis
CYANA v1.0.8, Guntert, P. - structure solution
NMR spectrometers:
- Bruker AVANCE 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts