BMRB Entry 27527
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27527
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Title: Backbone resonance assignments of the N-terminal domain of FAT10 PubMed: 30127417
Deposition date: 2018-06-26 Original release date: 2018-07-31
Authors: Aichem, Annette; Anders, Samira; Catone, Nicola; Roessler, Philip; Stotz, Sophie; Berg, Andrej; Schwab, Ricarda; Scheuermann, Sophia; Bialas, Johanna; Schuetz-Stoffregen, Mira; Schmidtke, Gunter; Peter, Christine; Groettrup, Marcus; Wiesner, Silke
Citation: Aichem, Annette; Anders, Samira; Catone, Nicola; Roessler, Philip; Stotz, Sophie; Berg, Andrej; Schwab, Ricarda; Scheuermann, Sophia; Bialas, Johanna; Schuetz-Stoffregen, Mira; Schmidtke, Gunter; Peter, Christine; Groettrup, Marcus; Wiesner, Silke. "The structure of the ubiquitin-like modifier FAT10 reveals an alternative targeting mechanism for proteasomal degradation" Nat. Commun. 9, 3321-3321 (2018).
Assembly members:
ndomain, polymer, 83 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: pET-M30
Entity Sequences (FASTA):
ndomain: GASTLTVHVRSEEWDLMTFD
ANPYDSVKKIKEHVRSKTKV
PVQDQVLLLGSKILKPRRSL
SSYGIDKEKTIHLTLKVVKP
SDE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 159 |
| 15N chemical shifts | 74 |
| 1H chemical shifts | 74 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | ndomain | 1 |
Entities:
Entity 1, ndomain 83 residues - Formula weight is not available
Residue 1 is a cloning artefact, residues 4 and 6 are Cys in the native protein sequence. Numbering of the residues compared to the native protein is off by -3.
| 1 | GLY | ALA | SER | THR | LEU | THR | VAL | HIS | VAL | ARG | ||||
| 2 | SER | GLU | GLU | TRP | ASP | LEU | MET | THR | PHE | ASP | ||||
| 3 | ALA | ASN | PRO | TYR | ASP | SER | VAL | LYS | LYS | ILE | ||||
| 4 | LYS | GLU | HIS | VAL | ARG | SER | LYS | THR | LYS | VAL | ||||
| 5 | PRO | VAL | GLN | ASP | GLN | VAL | LEU | LEU | LEU | GLY | ||||
| 6 | SER | LYS | ILE | LEU | LYS | PRO | ARG | ARG | SER | LEU | ||||
| 7 | SER | SER | TYR | GLY | ILE | ASP | LYS | GLU | LYS | THR | ||||
| 8 | ILE | HIS | LEU | THR | LEU | LYS | VAL | VAL | LYS | PRO | ||||
| 9 | SER | ASP | GLU |
Samples:
sample_1: ndomain, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 20 mM; sodium chloride 150 mM
sample_conditions_1: ionic strength: 0.1 M; pH: 7.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
XEASY, Bartels et al. - chemical shift assignment
NMR spectrometers:
- Bruker Avance 600 MHz
Related Database Links:
| NCBI | AAD52982.1 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts