BMRB Entry 34217

Title:
Solution structure of the RING domain of the E3 ubiquitin ligase HRD1
Deposition date:
2017-12-14
Original release date:
2019-01-28
Authors:
Kniss, A.; Kazemi, S.; Lohr, F.; Guntert, P.; Dotsch, V.
Citation:

Citation: Kniss, A.. "Solution structure of the RING domain of the E3 ubiquitin ligase HRD1"  .

Assembly members:

Assembly members:
entity_1, polymer, 78 residues, 8985.388 Da.
entity_ZN, non-polymer, 65.409 Da.

Natural source:

Natural source:   Common Name: Baker's yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

Experimental source:

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

Entity Sequences (FASTA):

Data typeCount
13C chemical shifts328
15N chemical shifts73
1H chemical shifts513

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_2, 12
3entity_2, 22

Entities:

Entity 1, entity_1 78 residues - 8985.388 Da.

1   GLYALAGLUGLNLEUGLNASNSERALAASN
2   ASPASPASNILECYSILEILECYSMETASP
3   GLULEUILEHISSERPROASNGLNGLNTHR
4   TRPLYSASNLYSASNLYSLYSPROLYSARG
5   LEUPROCYSGLYHISILELEUHISLEUSER
6   CYSLEULYSASNTRPMETGLUARGSERGLN
7   THRCYSPROILECYSARGLEUPROVALPHE
8   ASPGLULYSGLYASNVALVALGLN

Entity 2, entity_2, 1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: E3 ubiquitin ligase Hrd1, [U-98% 13C; U-98% 15N], 0.8 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.0; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H TOCSYsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
2D HCBCGCDH TOCSYsample_1isotropicsample_conditions_1

Software:

SPARKY v3.13, Goddard - chemical shift assignment

CYANA v3.9, Peter Guntert - structure calculation

OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 950 MHz

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