BMRB Entry 18582

Title:
1H, 13C, 15N chemical shifts of gp78CUE bound to ubiquitin AND backbone amide shifts of ubiquitin bound to gp78CUE
Deposition date:
2012-07-09
Original release date:
2012-11-19
Authors:
Liu, Shan; Chen, Yinghua; Huang, Tao; Tarasov, Sergey; King, Aaren; Li, Jess; Weissman, Allan; Byrd, Robert; Das, Ranabir
Citation:

Citation: Liu, Shan; Chen, Yinghua; Li, Jess; Huang, Tao; Tarasov, Sergey; King, Aaren; Weissman, Allan; Byrd, R. Andrew; Das, Ranabir. "Promiscuous interactions of gp78 E3 ligase CUE domain with polyubiquitin chains."  Structure 20, 2138-2150 (2012).
PubMed: 23123110

Assembly members:

Assembly members:
ubiquitin, polymer, 76 residues, 8576.914 Da.
gp78CUE, polymer, 52 residues, 5966.808 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: pET3a

Data sets:
Data typeCount
13C chemical shifts228
15N chemical shifts121
1H chemical shifts443

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ubiquitin1
2gp78CUE2

Entities:

Entity 1, ubiquitin 76 residues - 8576.914 Da.

1   METGLNILEPHEVALLYSTHRLEUTHRGLY
2   LYSTHRILETHRLEUGLUVALGLUPROSER
3   ASPTHRILEGLUASNVALLYSALALYSILE
4   GLNASPLYSGLUGLYILEPROPROASPGLN
5   GLNARGLEUILEPHEALAGLYLYSGLNLEU
6   GLUASPGLYARGTHRLEUSERASPTYRASN
7   ILEGLNLYSGLUSERTHRLEUHISLEUVAL
8   LEUARGLEUARGGLYGLY

Entity 2, gp78CUE 52 residues - 5966.808 Da.

1   SERASNSERGLNLEUASNALAMETALAHIS
2   GLNILEGLNGLUMETPHEPROGLNVALPRO
3   TYRHISLEUVALLEUGLNASPLEUGLNLEU
4   THRARGSERVALGLUILETHRTHRASPASN
5   ILELEUGLUGLYARGILEGLNVALPROPHE
6   PROTHR

Samples:

sample_1: TRIS 50 mM; sodium chloride 50 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 7.2; 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 HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment, peak picking

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

CNS, Alexandre Bonvin - structure solution

NMR spectrometers:

  • Bruker INOVA 600 MHz
  • Bruker INOVA 700 MHz
  • Varian INOVA 600 MHz
  • Varian INOVA 800 MHz

Related Database Links:

BMRB 11505 11547 15047 15410 15689 15907 16228 16582 16626 16895 17181 17439 17769 17919 18583 18584 18610 18611 18737 19406 19412 25070 25123 25601 26604 4245 4375 18581 18583 18584
PDB
DBJ BAA03983 BAA09860 BAA11842 BAA11843 BAA23486 BAE01277 BAE34049 BAE41974 BAK63135
EMBL CAA25706 CAA26488 CAA28495 CAA30183 CAA30815
GB AAA02769 AAA28154 AAA28997 AAA28998 AAA28999 AAD56721 AAD56722 AAH03256 AAH17043 AAH34538
PIR I50437 I51568 I65237 JN0790 S13928
PRF 0412265A 1101405A 1212243A 1212243B 1212243C
REF NP_001005123 NP_001006688 NP_001009117 NP_001009202 NP_001009286 NP_001039439 NP_001135 NP_001267243 NP_035917 XP_001091030
SP P0C273 P0C275 P0C276 P0CG47 P0CG48 Q9R049 Q9UKV5
TPD FAA00319
TPE CEL68433 CEL70397 CEL75964 CEL78064
TPG DAA18802 DAA20663 DAA20672 DAA24675 DAA28295 DAA20037
AlphaFold P0C273 P0C275 P0C276 P0CG47 P0CG48 Q9R049 Q9UKV5

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