BMRB Entry 36175

Title:
A-ubiquitin like protein from the trypanosoma brucei
Deposition date:
2018-04-02
Original release date:
2018-12-07
Authors:
Mi, J.; Tu, X.
Citation:

Citation: Mi, J.; Zhang, J.; Liao, S.; Tu, X.. "Solution structure of a ubiquitin-like protein from Trypanosoma brucei"  Protein Sci. 27, 1831-1836 (2018).
PubMed: 30058168

Assembly members:

Assembly members:
ubiquintin-like protein, polymer, 81 residues, 9141.467 Da.

Natural source:

Natural source:   Common Name: Trypanosoma brucei   Taxonomy ID: 185431   Superkingdom: Metazoa   Kingdom: not available   Genus/species: Trypanosoma brucei

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli 'BL21-Gold(DE3)pLysS AG'

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts236
15N chemical shifts81
1H chemical shifts497

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 81 residues - 9141.467 Da.

1   METSERGLUTHRILEPROVALSERVALGLN
2   CYSCYSGLUGLYARGPHEGLULEUSERVAL
3   ASPSERASNHISTHRLEUARGASPVALLEU
4   ARGGLNPHELYSARGGLUVALALAALALEU
5   ASPPROILEASNLEUGLUGLUTYRVALVAL
6   ASNHISGLUGLYLYSLEULEULEUASPASP
7   SERVALTHRLEUGLNTHRVALGLYVALLYS
8   LYSASPSERVALPHEVALLEUVALARGLYS
9   ALA

Samples:

sample_1: ubiquitin-like protein, [U-99% 13C; U-99% 15N], 0.5 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 120 mM; pH: 6.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure calculation

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

SPARKY, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker DMX 600 MHz

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