BMRB Entry 36272

Title:
Solution Structure of the CS2 Domain of USP19
Deposition date:
2019-07-16
Original release date:
2025-09-15
Authors:
Xue, W.; Hu, H.
Citation:

Citation: Xue, Wei; Zhang, Shu-Xian; He, Wen-Tian; Hong, Jun-Ye; Jiang, Lei-Lei; Hu, Hong-Yu. "Domain interactions reveal auto-inhibition of the deubiquitinating enzyme USP19 and its activation by HSP90 in the modulation of huntingtin aggregation."  Biochem. J. 477, 4295-4312 (2020).
PubMed: 33094816

Assembly members:

Assembly members:
Ubiquitin carboxyl-terminal hydrolase 19, polymer, 114 residues, 13338.205 Da.

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

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts378
15N chemical shifts110
1H chemical shifts491

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 114 residues - 13338.205 Da.

1   VALASPGLUPROGLUSERMETVALASNLEU
2   ALAPHEVALLYSASNASPSERTYRGLULYS
3   GLYPROASPSERVALVALVALHISVALTYR
4   VALLYSGLUILECYSARGASPTHRSERARG
5   VALLEUPHEARGGLUGLNASPPHETHRLEU
6   ILEPHEGLNTHRARGASPGLYASNPHELEU
7   ARGLEUHISPROGLYCYSGLYPROHISTHR
8   THRPHEARGTRPGLNVALLYSLEUARGASN
9   LEUILEGLUPROGLUGLNCYSTHRPHECYS
10   PHETHRALASERARGILEASPILECYSLEU
11   ARGLYSARGGLNSERGLNARGTRPGLYGLY
12   LEUGLUALAPRO

Samples:

15N_13C_sample: Ubiquitin carboxyl-terminal hydrolase 19, [U-13C; U-15N], mM; sodium azide 0.05 mM; sodium chloride 50 mM; sodium phosphate 20 mM; H2O 90 % v/v; D2O, [U-2H], 10 % v/v

15N_sample: Ubiquitin carboxyl-terminal hydrolase 19, [U-13C; U-15N], mM; sodium azide 0.05 mM; sodium chloride 50 mM; sodium phosphate 20 mM; H2O 90 % v/v; D2O, [U-2H], 10 % v/v

sample_conditions_1: ionic strength: 0.08 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC15N_sampleisotropicsample_conditions_1
3D CBCA(CO)NH15N_13C_sampleisotropicsample_conditions_1
3D HNCACB15N_13C_sampleisotropicsample_conditions_1
3D H(CCO)NH15N_13C_sampleisotropicsample_conditions_1
3D HNHA15N_sampleisotropicsample_conditions_1
3D HCCH-TOCSY15N_13C_sampleisotropicsample_conditions_1
3D 1H-13C NOESY15N_13C_sampleisotropicsample_conditions_1
3D 1H-15N NOESY15N_sampleisotropicsample_conditions_1
3D HNCO15N_13C_sampleisotropicsample_conditions_1

Software:

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

Sparky, Goddard - data analysis

Sparky, Goddard - chemical shift assignment

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure calculation

ARIA, Linge, O'Donoghue and Nilges - structure calculation

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

ARIA, Linge, O'Donoghue and Nilges - refinement

NMR spectrometers:

  • Bruker AVANCE 600 MHz

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