BMRB Entry 50308

Title:
Sequence-specific resonance assignments of the human SAS-6 F131D head domain   PubMed: 32873708
Deposition date:
2020-06-07
Original release date:
2020-09-01
Authors:
Busch, Julia; Vakonakis, Ioannis
Citation:

Citation: Busch, Julia; Matsoukas, Minos-Timotheos; Musgaard, Maria; Spyroulias, Georgios; Biggin, Philip; Vakonakis, Ioannis. "Identification of compounds that bind the centriolar protein SAS-6 and inhibit its oligomerization"  J. Biol. Chem. 295, 17922-17934 (2020).

Assembly members:

Assembly members:
entity_1, polymer, 154 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

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

Experimental source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

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

Data sets:
Data typeCount
13C chemical shifts224
15N chemical shifts110
1H chemical shifts110

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hsSAS-61

Entities:

Entity 1, hsSAS-6 154 residues - Formula weight is not available

First two residues are cloning artifacts

1   GLYPROMETSERGLNVALLEUPHEHISGLN
2   LEUVALPROLEUGLNVALLYSCYSLYSASP
3   CYSGLUGLUARGARGVALSERILEARGMET
4   SERILEGLULEUGLNSERVALSERASNPRO
5   VALHISARGLYSASPLEUVALILEARGLEU
6   THRASPASPTHRASPPROPHEPHELEUTYR
7   ASNLEUVALILESERGLUGLUASPPHEGLN
8   SERLEULYSPHEGLNGLNGLYLEULEUVAL
9   ASPPHELEUALAPHEPROGLNLYSPHEILE
10   ASPLEULEUGLNGLNCYSTHRGLNGLUHIS
11   ALALYSGLUILEPROARGPHELEULEUGLN
12   LEUVALSERPROALAALAILELEUASPASN
13   SERPROALAPHELEUASNVALVALGLUTHR
14   ASNPROASPLYSHISLEUTHRHISLEUSER
15   LEULYSLEULEUPROGLYASNASPVALGLU
16   ILELYSLYSPHE

Samples:

sample_1: hsSAS-6, [U-99% 13C; U-99% 15N], 0.5 mM; D2O 5%; DSS 50 uM; sodium chloride 150 mM; sodium phosphate 20 mM; sodium azide 0.02%

sample_conditions_1: ionic strength: 0.38 M; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

TOPSPIN - collection

NMRPipe - processing

SPARKY - data analysis

PINE - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 17.6 MHz

Related Database Links:

UNP Q6UVJ0

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts