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
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:

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).
PubMed: 30127417

Assembly members:

Assembly members:
ndomain, polymer, 83 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-M30

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ndomain: GASTLTVHVRSEEWDLMTFD ANPYDSVKKIKEHVRSKTKV PVQDQVLLLGSKILKPRRSL SSYGIDKEKTIHLTLKVVKP SDE

Data sets:
Data typeCount
13C chemical shifts159
15N chemical shifts74
1H chemical shifts74

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1ndomain1

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   GLYALASERTHRLEUTHRVALHISVALARG
2   SERGLUGLUTRPASPLEUMETTHRPHEASP
3   ALAASNPROTYRASPSERVALLYSLYSILE
4   LYSGLUHISVALARGSERLYSTHRLYSVAL
5   PROVALGLNASPGLNVALLEULEULEUGLY
6   SERLYSILELEULYSPROARGARGSERLEU
7   SERSERTYRGLYILEASPLYSGLULYSTHR
8   ILEHISLEUTHRLEULYSVALVALLYSPRO
9   SERASPGLU

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_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 peaks
SPARKY: Backbone or all simulated peaks