BMRB Entry 26783

Title:
APC11 binding Ubiquitin Variant
Deposition date:
2016-04-21
Original release date:
2018-06-19
Authors:
Brown, Nicholas; Grace, Christy; Schulman, Brenda
Citation:

Citation: Brown, Nicholas; VanderLinden, Ryan; Watson, Edmond; Weissmann, Florian; Ordureau, Alban; Wu, Kuen-Phon; Zhang, Wei; Yu, Shanshan; Mercredi, Peter; Harrison, Joseph; Davidson, Iain; Qiao, Renping; Lu, Ying; Dube, Prakash; Brunner, Michael; Grace, Christy; Miller, Darcie; Haselbach, David; Jarvis, Marc; Yamaguchi, Masaya; Yanishevski, David; Petzold, Georg; Sidhu, Sachdev; Kuhlman, Brian; Kirschner, Marc; Harper, J Wade; Peters, Jan-Michael; Stark, Holger; Schulman, Brenda. "Dual RING E3 Architectures Regulate Multiubiquitination and Ubiquitin Chain Elongation by APC/C."  Cell 165, 1440-1453 (2016).
PubMed: 27259151

Assembly members:

Assembly members:
UBv, polymer, 84 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: BL21

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts231
15N chemical shifts75
1H chemical shifts75

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1UBv1

Entities:

Entity 1, UBv 84 residues - Formula weight is not available

1   GLYSERGLYGLYSERGLYMETGLNILELEU
2   VALLYSTHRPROARGGLYLYSTHRILETHR
3   LEUGLUVALGLUPROSERASPTHRILEGLU
4   ASNVALLYSALALYSILEGLNASPLYSGLU
5   GLYILEPROPROASPGLNGLNILELEUPHE
6   PHEALAVALLYSARGLEUGLUASPGLYARG
7   THRLEUSERASPTYRASNILEGLNLYSLYS
8   SERSERLEULEULEUALAMETARGVALPRO
9   GLYLYSMETLYS

Samples:

sample_1: UBv, [U-100% 13C; U-100% 15N], 1.0 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

CARA, Keller and Wuthrich - chemical shift assignment, data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz

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