BMRB Entry 18807

Title:
Chemical shifts for the N-terminal head group of ceSAS-6   PubMed: 23798409
Deposition date:
2012-10-25
Original release date:
2019-08-30
Authors:
Erat, Michele; Vakonakis, Ioannis
Citation:

Citation: Hilbert, Manuel; Erat, Michele; Hachet, Virginie; Guichard, Paul; Blank, Iris; Fluckiger, Isabelle; Slater, Leanne; Lowe, Edward; Hatzopoulos, Georgios; Steinmetz, Michel; Gonczy, Pierre; Vakonakis, Ioannis. "Caenorhabditis elegans centriolar protein SAS-6 forms a spiral that is consistent with imparting a ninefold symmetry"  Proc. Natl. Acad. Sci. U.S.A. 110, 11373-11378 (2013).

Assembly members:

Assembly members:
ce_SAS-6, polymer, 170 residues, 19425 Da.

Natural source:

Natural source:   Common Name: Nematodes   Taxonomy ID: 6239   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Caenorhabditis elegans

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: modified p15b

Experimental source:

Natural source:   Common Name: Nematodes   Taxonomy ID: 6239   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Caenorhabditis elegans

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: modified p15b

Data sets:
Data typeCount
13C chemical shifts472
15N chemical shifts153
1H chemical shifts153

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ceN SAS-61

Entities:

Entity 1, ceN SAS-6 170 residues - 19425 Da.

GS N-terminal cloning artefact, S123E, I154E

1   GLYSERMETTHRSERLYSILEALALEUPHE
2   ASPGLNTHRLEUILEALASERLEULEUGLN
3   PROLEUSERLEUASNGLNPROASPPHELYS
4   ALATYRLYSTHRLYSVALLYSLEULYSILE
5   SERGLUGLNARGASNGLUTHRSERGLYGLU
6   LYSGLULEULYSPHEGLUILESERARGSER
7   ASPASPPHEGLUPHELEUPHESERGLUTHR
8   LEUASNASNGLULYSTYRGLNILELEUALA
9   ARGASPHISASPLEUTHRVALASPPHEASP
10   ALAPHEPROLYSVALILEILEGLNHISLEU
11   LEUCYSLYSASNILEVALLYSASNLEUGLU
12   GLUASPGLYGLUVALASPALAARGLYSLYS
13   ALAGLYTYRHISGLUILEALAASPPROGLY
14   LYSPROTHRGLUILEASNILEILELEUASP
15   ALAGLULYSASNPHECYSSERPHEGLULEU
16   PHESERLYSTHRPROGLUSERLYSGLYLYS
17   ILEPHESERILELYSLEUHISALAVALARG

Samples:

sample_1: ce SAS-6, [U-15N], 0.5 mM; H2O 95%; D2O, [U-100% 2H], 5%; DSS 0.1 mM; sodium chloride 100 mM; sodium phosphate 20 mM

sample_2: ce SAS-6, [U-100% 13C; U-100% 15N], 0.5 mM; H2O 95%; D2O, [U-100% 2H], 5%; DSS 0.1 mM; sodium chloride 100 mM; potassium phosphate 20 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D CBCANHsample_2isotropicsample_conditions_1
HNCOsample_2isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TOPSPIN, Bruker Biospin - collection

Omega_Spectrometer_Operating_Software_Beta_6.03b2, GE - collection

NMR spectrometers:

  • GE/home-built OMEGA 600 MHz
  • Bruker Avance 500 MHz

Related Database Links:

UNP O62479
PDB

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