BMRB Entry 27466
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR27466
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Title: Chemical shift assignments of the C-terminal domain of human FAT10 PubMed: 30127417
Deposition date: 2018-04-25 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; Schmidtke, Gunter; Peter, Christine; Groettrup, Marcus; Wiesner, Silke
Citation: Aichem, Annette; Anders, Samira; Catone, Nicola; Rossler, Philip; Stotz, Sophie; Berg, Andrej; Schwab, Ricarda; Scheuermann, Sophia; Bialas, Johanna; Schutz-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:
fat10_c, polymer, 85 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
Entity Sequences (FASTA):
fat10_c: GAMGDEELPLFLVESGDEAK
RHLLQVRRSSSVAQVKAMIE
TKTGIIPETQIVTLNGKRLE
DGKMMADYGIRKGNLLFLAS
YSIGG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 6 |
| 15N chemical shifts | 1 |
| 1H chemical shifts | 5 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | FAT10 C-terminal domain | 1 |
Entities:
Entity 1, FAT10 C-terminal domain 85 residues - Formula weight is not available
| 1 | GLY | ALA | MET | GLY | ASP | GLU | GLU | LEU | PRO | LEU | ||||
| 2 | PHE | LEU | VAL | GLU | SER | GLY | ASP | GLU | ALA | LYS | ||||
| 3 | ARG | HIS | LEU | LEU | GLN | VAL | ARG | ARG | SER | SER | ||||
| 4 | SER | VAL | ALA | GLN | VAL | LYS | ALA | MET | ILE | GLU | ||||
| 5 | THR | LYS | THR | GLY | ILE | ILE | PRO | GLU | THR | GLN | ||||
| 6 | ILE | VAL | THR | LEU | ASN | GLY | LYS | ARG | LEU | GLU | ||||
| 7 | ASP | GLY | LYS | MET | MET | ALA | ASP | TYR | GLY | ILE | ||||
| 8 | ARG | LYS | GLY | ASN | LEU | LEU | PHE | LEU | ALA | SER | ||||
| 9 | TYR | SER | ILE | GLY | GLY |
Samples:
sample_1: fat10_c, [U-100% 13C; U-100% 15N], 2 mM; sodium chloride 150 mM; sodium phosphate 20 mM
sample_conditions_1: ionic strength: 0.2 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 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | 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 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
XEASY, (Xeasy) W thrich - chemical shift assignment, peak picking
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts