BMRB Entry 25150

Title:
Solution structure of the human ubiquitin conjugating enzyme Ube2w
Deposition date:
2014-08-14
Original release date:
2014-11-24
Authors:
Vittal, Vinayak; Shi, Lei; Wenzel, Dawn; Brzovic, Peter; Klevit, Rachel
Citation:

Citation: Vittal, Vinayak; Shi, Lei; Wenzel, Dawn; Scaglione, K. Matthew; Duncan, Emily; Basrur, Venkatesha; Elenitoba-Johnson, Kojo; Baker, David; Paulson, Henry; Brzovic, Peter; Klevit, Rachel. "Intrinsic disorder drives N-terminal ubiquitination by Ube2w"  Nat. Chem. Biol. 11, 83-89 (2015).
PubMed: 25436519

Assembly members:

Assembly members:
entity, polymer, 151 residues, 17350.973 Da.

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: pET24

Data sets:
Data typeCount
13C chemical shifts367
15N chemical shifts113
1H chemical shifts230

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 151 residues - 17350.973 Da.

1   METALASERMETGLNLYSARGLEUGLNLYS
2   GLULEULEUALALEUGLNASNASPPROPRO
3   PROGLYMETTHRLEUASNGLULYSSERVAL
4   GLNASNSERILETHRGLNTRPILEVALASP
5   METGLUGLYALAPROGLYTHRLEUTYRGLU
6   GLYGLULYSPHEGLNLEULEUPHELYSPHE
7   SERSERARGTYRPROPHEASPSERPROGLN
8   VALMETPHETHRGLYGLUASNILEPROVAL
9   HISPROHISVALTYRSERASNGLYHISILE
10   CYSLEUSERILELEUTHRGLUASPTRPSER
11   PROALALEUSERVALGLNSERVALCYSLEU
12   SERILEILESERMETLEUSERSERCYSLYS
13   GLULYSARGARGPROPROASPASNSERPHE
14   TYRVALARGTHRCYSASNLYSASNPROLYS
15   LYSTHRLYSTRPTRPTYRHISASPASPTHR
16   CYS

Samples:

sample_1: Ube2w, [U-100% 13C; U-100% 15N], 200 – 400 uM; H20 90%; D20 10%

sample_conditions_1: ionic strength: 150 mM; pH: 7.0; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

CS-ROSETTA, Shen, Vernon, Baker and Bax - refinement, structure solution

NMR spectrometers:

  • Bruker DMX 500 MHz
  • Bruker INOVA 600 MHz

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