BMRB Entry 50300

Title:
Sequence-specific resonance assignments of the Chlamydomonas reinhardtii SAS-6 N-terminal domain, F145E variant   PubMed: 32873708
Deposition date:
2020-05-28
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, 161 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: green algae   Taxonomy ID: 3055   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Chlamydomonas reinhardtii

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pSTCm1

Experimental source:

Natural source:   Common Name: green algae   Taxonomy ID: 3055   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Chlamydomonas reinhardtii

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pSTCm1

Data sets:
Data typeCount
13C chemical shifts410
15N chemical shifts133
1H chemical shifts133

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CrSAS-6N F145E1

Entities:

Entity 1, CrSAS-6N F145E 161 residues - Formula weight is not available

First two residues are cloning artefact. E147 in assignment numbering is an engineered mutation.

1   GLYPROMETPROLEULEULEUASPASPGLY
2   ASPPROLYSALAGLNTHRGLYPHEASPLEU
3   SERTHRALATHRTHRLEUPHETRPARGPRO
4   VALPROVALHISVALLYSGLNGLNASPARG
5   GLUASPVALLEUGLUGLULEUTHRPHEARG
6   ILELEUTHRGLYVALALALYSGLNASNHIS
7   ASNLEUARGILELEUARGILEHISILESER
8   SERASPSERASPLEUPHEPHELEUHISTHR
9   LEUGLUVALSERGLUGLUASPPHEGLNSER
10   LEULYSASNASPGLNGLYILELEUVALASP
11   PHEALASERPHEPROGLYLYSILEILESER
12   LEULEUGLULYSCYSILELEUALAGLNPRO
13   GLYASPSERPROARGPHEGLNALAVALLEU
14   THRILEARGGLYGLYGLUSERVALPHELYS
15   ILEVALGLUILEASNASPGLULYSGLNLEU
16   PROHISILETHRLEUALAPHEARGPROGLY
17   ASN

Samples:

sample_1: CrSAS-6N F145E, [U-99% 13C; U-99% 15N], 0.5 mM; sodium chloride 150 mM; sodium phosphate 20 mM; D2O 5%; DSS 50 uM; 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 HNCOsample_1isotropicsample_conditions_1

Software:

TOPSPIN - collection

NMRPipe - processing

SPARKY - data analysis

PIPP - data analysis

NMR spectrometers:

  • Bruker Avance II 500 MHz

Related Database Links:

UNP A9CQL4

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