BMRB Entry 11256

Title:
Solution Structure of the N-terminal Ubiquitin-like Domain of Mouse Ubiquitin Specific Protease 14 (USP14)
Deposition date:
2010-08-09
Original release date:
2011-08-17
Authors:
Zhao, C.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.
Citation:

Citation: Zhao, C.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution Structure of the N-terminal Ubiquitin-like Domain of Mouse Ubiquitin Specific Protease 14 (USP14)"  .

Assembly members:

Assembly members:
ubiquitin-like domain, polymer, 96 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: house mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

Experimental source:   Production method: cell free synthesis   Host organism: E. coli - cell free   Vector: P0302212-91

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts408
15N chemical shifts96
1H chemical shifts634

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ubiquitin-like domain1

Entities:

Entity 1, ubiquitin-like domain 96 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYTYRSERVAL
2   THRVALLYSTRPGLYLYSGLULYSPHEGLU
3   GLYVALGLULEUASNTHRASPGLUPROPRO
4   METVALPHELYSALAGLNLEUPHEALALEU
5   THRGLYVALGLNPROALAARGGLNLYSVAL
6   METVALLYSGLYGLYTHRLEULYSASPASP
7   ASPTRPGLYASNILELYSMETLYSASNGLY
8   METTHRVALLEUMETMETGLYSERALAASP
9   ALALEUPROGLUGLUPROSERALALYSTHR
10   SERGLYPROSERSERGLY

Samples:

sample_1: ubiquitin-like domain mM; PiNa 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 6.0; pressure: 1 atm; temperature: 298.0 K

Experiments:

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

Software:

xwinnmr v2.6, Bruker - collection

NMRPipe v20020425, Delaglio, F. - processing

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

Kujira v0.8996, Kobayashi, N. - data analysis

CYANA v1.0.7, Guntert, P. - refinement, structure solution

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAA93551 BAB27544 BAC26713 BAC32528 BAE89403
GB AAB60365 AAH03556 AAH05571 AAH50197 AAH85947
REF NP_001008302 NP_001032411 NP_001033678 NP_001038961 NP_001068657
SP P54578 P60051 Q0IIF7 Q9JMA1
TPG DAA15782
AlphaFold P54578 Q9JMA1 Q0IIF7 P60051

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