BMRB Entry 52105

Title:
1H and 15N chemical shift assignments of K6-linked di-ubiquitin with chain-terminating mutations
Deposition date:
2023-08-28
Original release date:
2023-08-30
Authors:
Kurbah, Iladeiti; Fushman, David
Citation:

Citation: Kurbah, Iladeiti; Fushman, David. "1H and 15N chemical shift assignments of K6-linked di-ubiquitin with chain-terminating mutations"  Biomol. NMR Assignments ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 77 residues, 8707.95 Da.
entity_2, polymer, 76 residues, 8620.87 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: pET-3a

Data sets:
Data typeCount
15N chemical shifts142
1H chemical shifts142

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ubiquitin, Chain A1
2ubiquitin, Chain B2

Entities:

Entity 1, ubiquitin, Chain A 77 residues - 8707.95 Da.

Proximal domain of K6-linked di-ubiquitin

1   METGLNILEPHEVALLYSTHRLEUTHRGLY
2   LYSTHRILETHRLEUGLUVALGLUPROSER
3   ASPTHRILEGLUASNVALLYSALALYSILE
4   GLNASPLYSGLUGLYILEPROPROASPGLN
5   GLNARGLEUILEPHEALAGLYARGGLNLEU
6   GLUASPGLYARGTHRLEUSERASPTYRASN
7   ILEGLNLYSGLUSERTHRLEUHISLEUVAL
8   LEUARGLEUARGGLYGLYASP

Entity 2, ubiquitin, Chain B 76 residues - 8620.87 Da.

Distal domain of K6-linked di-ubiquitin

1   METGLNILEPHEVALARGTHRLEUTHRGLY
2   LYSTHRILETHRLEUGLUVALGLUPROSER
3   ASPTHRILEGLUASNVALLYSALALYSILE
4   GLNASPLYSGLUGLYILEPROPROASPGLN
5   GLNARGLEUILEPHEALAGLYARGGLNLEU
6   GLUASPGLYARGTHRLEUSERASPTYRASN
7   ILEGLNLYSGLUSERTHRLEUHISLEUVAL
8   LEUARGLEUARGGLYGLY

Samples:

sample_1: entity_1, [U-100% 15N], 150 uM; entity_2 150 uM; sodium phosphate 20 mM

sample_2: entity_1 50 uM; entity_2, [U-100% 15N], 50 uM; sodium phosphate 20 mM

sample_conditions_1: ionic strength: 20 mM; pH: 6.8; pressure: 1 atm; temperature: 296 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1

Software:

NMRFAM-SPARKY v1.470 - chemical shift assignment, peak picking

TOPSPIN v4.1.4 - processing of raw NMR data

NMR spectrometers:

  • Bruker AVANCE III HD 800 MHz
  • Bruker AVANCE III 600 MHz

Related Database Links:

UNP P0CG47 P0CG47

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