BMRB Entry 10338

Title:
Solution Structure of the First UBA Domain in the Human Ubiquitin Specific Protease 5 (Isopeptidase 5)
Deposition date:
2011-01-13
Original release date:
2019-09-04
Authors:
Zhao, C.; Kigawa, T.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Yokoyama, S.
Citation:

Citation: Zhao, C.; Kigawa, T.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Yokoyama, S.. "Solution Structure of the First UBA Domain in the Human Ubiquitin Specific Protease 5 (Isopeptidase 5)"  .

Assembly members:

Assembly members:
UBA domain, polymer, 54 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: cell free synthesis   Host organism: Escherichia coli   Vector: P050613-08

Entity Sequences (FASTA):

Entity Sequences (FASTA):
UBA domain: GLDESVIIQLVEMGFPMDAC RKAVYYTGNSGAEAAMNWVM SHMDDPDFANPLIL

Data sets:
Data typeCount
13C chemical shifts235
15N chemical shifts53
1H chemical shifts368

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1UBA domain1

Entities:

Entity 1, UBA domain 54 residues - Formula weight is not available

1   GLYLEUASPGLUSERVALILEILEGLNLEU
2   VALGLUMETGLYPHEPROMETASPALACYS
3   ARGLYSALAVALTYRTYRTHRGLYASNSER
4   GLYALAGLUALAALAMETASNTRPVALMET
5   SERHISMETASPASPPROASPPHEALAASN
6   PROLEUILELEU

Samples:

sample_1: UBA domain, [U-13C; U-15N], 1.05 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 296.0 K

Experiments:

NameSampleSample stateSample conditions
3D 15N-separated NOESYsample_1isotropiccondition_1
3D 13C-separated NOESYsample_1isotropiccondition_1

Software:

TOPSPIN v2.1, Bruker - collection

NMRPipe, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B. A. - data analysis

Kujira v0.9843, Kobayashi, N. - data analysis

CYANA v1.0.8, Guntert, P. - structure solution

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