BMRB Entry 11173

Title:
Solution Structure of the First UBA Domain in the Human Ubiquitin Specific Protease 5 (Isopeptidase 5)
Deposition date:
2010-05-20
Original release date:
2010-06-16
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, 74 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: E. coli - cell free   Vector: P050613-08

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts249
15N chemical shifts57
1H chemical shifts387

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1UBA domain1

Entities:

Entity 1, UBA domain 74 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYLEUASPGLU
2   SERVALILEILEGLNLEUVALGLUMETGLY
3   PHEPROMETASPALACYSARGLYSALAVAL
4   TYRTYRTHRGLYASNSERGLYALAGLUALA
5   ALAMETASNTRPVALMETSERHISMETASP
6   ASPPROASPPHEALAASNPROLEUILELEU
7   PROGLYSERSERGLYPROGLYSERSERGLY
8   PROSERSERGLY

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:

xwinnmr v2.6, Bruker - collection

NMRPipe v20030801, Delaglio, F. - processing

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

Kujira v0.9321, Kobayashi, N. - data analysis

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

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB

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