BMRB Entry 18767

Title:
Hug1: an intrinsically disordered protein involved in the DNA damage response.
Deposition date:
2012-10-08
Original release date:
2019-09-05
Authors:
Ochsenbein, Francoise; Richet, Nicolas; Meurisse, Julie; Peyroche, Anne
Citation:

Citation: Meurisse, Julie; Bacquin, Agathe; Richet, Nicolas; Charbonnier, Jean-Baptiste; Ochsenbein, Francoise; Peyroche, Anne. "Hug1 is an intrinsically disordered protein that inhibits ribonucleotide reductase activity by directly binding Rnr2 subunit"  Nucleic Acids Res. 42, 13174-13185 (2014).
PubMed: 25378334

Assembly members:

Assembly members:
Hug1, polymer, 74 residues, Formula weight is not available

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   Vector: pGSTbis

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts211
15N chemical shifts70
1H chemical shifts317

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Hug11

Entities:

Entity 1, Hug1 74 residues - Formula weight is not available

1   GLYALAMETALAASPPROMETTHRMETASP
2   GLNGLYLEUASNPROLYSGLNPHEPHELEU
3   ASPASPVALVALLEUGLNASPTHRLEUCYS
4   SERMETSERASNARGVALASNLYSSERVAL
5   LYSTHRGLYTYRLEUPHEPROLYSASPHIS
6   VALPROSERALAASNILEILEALAVALGLU
7   ARGARGGLYGLYLEUSERASPILEGLYLYS
8   ASNTHRSERASN

Samples:

sample_1: Hug1, [U-13C; U-15N], 60 uM; sodium phosphate 20 mM; sodium chloride 50 mM; EDTA 0.1 mM; DSS 0.1 mM; sodium azide 0.1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 70 mM; pH: 5; pressure: 1 atm; temperature: 284 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

TOPSPIN_3.0, Bruker Biospin - collection, data analysis

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker DRX 600 MHz

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