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
MolProbity Validation Chart

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Title:
Chemical shift assignments of the C-terminal domain of human FAT10
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:

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).
PubMed: 30127417

Assembly members:

Assembly members:
fat10_c, polymer, 85 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: pETM-41

Entity Sequences (FASTA):

Entity Sequences (FASTA):
fat10_c: GAMGDEELPLFLVESGDEAK RHLLQVRRSSSVAQVKAMIE TKTGIIPETQIVTLNGKRLE DGKMMADYGIRKGNLLFLAS YSIGG

Data sets:
Data typeCount
13C chemical shifts6
15N chemical shifts1
1H chemical shifts5

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1FAT10 C-terminal domain1

Entities:

Entity 1, FAT10 C-terminal domain 85 residues - Formula weight is not available

1   GLYALAMETGLYASPGLUGLULEUPROLEU
2   PHELEUVALGLUSERGLYASPGLUALALYS
3   ARGHISLEULEUGLNVALARGARGSERSER
4   SERVALALAGLNVALLYSALAMETILEGLU
5   THRLYSTHRGLYILEILEPROGLUTHRGLN
6   ILEVALTHRLEUASNGLYLYSARGLEUGLU
7   ASPGLYLYSMETMETALAASPTYRGLYILE
8   ARGLYSGLYASNLEULEUPHELEUALASER
9   TYRSERILEGLYGLY

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1

Software:

XEASY, (Xeasy) W thrich - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

GB AAD52982.1

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks