BMRB Entry 12009

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR12009

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Title:
Backbone assignment of the N-terminal ubiquitin C-terminal hydrolase domain of UCH37
Deposition date:
2017-02-07
Original release date:
2018-12-11
Authors:
Lee, Yun-Tzai; Chang, Chia-Yun; Hsu, Shang-Te Danny
Citation:

Citation: Lee, Yun-Tzai; Chang, Chia-Yun; Chen, Szu-Yu; Pan, Yun-Ru; Ho, Meng-Ru; Hsu, Shang-Te. "Entropic stabilization of a deubiquitinase provides conformational plasticity and slow unfolding kinetics beneficial for functioning on the proteasome."  Sci. Rep. 7, 45174-45174 (2017).
PubMed: 28338014

Assembly members:

Assembly members:
UCHL5N240, polymer, 245 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: pGEX-6P1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
UCHL5N240: GPLGSMTGNAGEWCLMESDP GVFTELIKGFGCRGAQVEEI WSLEPENFEKLKPVHGLIFL FKWQPGEEPAGSVVQDSRLD TIFFAKQVINNACATQAIVS VLLNCTHQDVHLGETLSEFK EFSQSFDAAMKGLALSNSDV IRQVHNSFARQQMFEFDTKT SAKEEDAFHFVSYVPVNGRL YELDGLREGPIDLGACNQDD WISAVRPVIEKRIQKYSEGE IRFNLMAIVSDRKMIYEQKI AELQR

Data sets:
Data typeCount
13C chemical shifts576
15N chemical shifts220
1H chemical shifts220

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1UCHL5N2401

Entities:

Entity 1, UCHL5N240 245 residues - Formula weight is not available

1   GLYPROLEUGLYSERMETTHRGLYASNALA
2   GLYGLUTRPCYSLEUMETGLUSERASPPRO
3   GLYVALPHETHRGLULEUILELYSGLYPHE
4   GLYCYSARGGLYALAGLNVALGLUGLUILE
5   TRPSERLEUGLUPROGLUASNPHEGLULYS
6   LEULYSPROVALHISGLYLEUILEPHELEU
7   PHELYSTRPGLNPROGLYGLUGLUPROALA
8   GLYSERVALVALGLNASPSERARGLEUASP
9   THRILEPHEPHEALALYSGLNVALILEASN
10   ASNALACYSALATHRGLNALAILEVALSER
11   VALLEULEUASNCYSTHRHISGLNASPVAL
12   HISLEUGLYGLUTHRLEUSERGLUPHELYS
13   GLUPHESERGLNSERPHEASPALAALAMET
14   LYSGLYLEUALALEUSERASNSERASPVAL
15   ILEARGGLNVALHISASNSERPHEALAARG
16   GLNGLNMETPHEGLUPHEASPTHRLYSTHR
17   SERALALYSGLUGLUASPALAPHEHISPHE
18   VALSERTYRVALPROVALASNGLYARGLEU
19   TYRGLULEUASPGLYLEUARGGLUGLYPRO
20   ILEASPLEUGLYALACYSASNGLNASPASP
21   TRPILESERALAVALARGPROVALILEGLU
22   LYSARGILEGLNLYSTYRSERGLUGLYGLU
23   ILEARGPHEASNLEUMETALAILEVALSER
24   ASPARGLYSMETILETYRGLUGLNLYSILE
25   ALAGLULEUGLNARG

Samples:

sample_1: UCHL5N240, [U-98% 13C; U-98% 15N], 0.5 mM; TRIS 20 mM; sodium chloride 100 mM; DTT 5 mM; H2O 95%; D2O, [U-2H], 5%

sample_conditions_1: ionic strength: 0.1 M; pH: 7.6; 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 CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

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

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 850 MHz

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