BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 27607

Title: Sequence specific chemical shift assignments of the Caenorhabditis elegans SAS-6 N-terminal domain   PubMed: 30837637

Deposition date: 2018-09-13 Original release date: 2019-02-15

Authors: Erat, Michele; Vakonakis, Ioannis

Citation: Busch, Julia; Erat, Michele; Blank, Iris; Musgaard, Maria; Biggin, Philip; Vakonakis, Ioannis. "A dynamically interacting flexible loop assists oligomerisation of the Caenorhabditis elegans centriolar protein SAS-6"  Sci. Rep. 9, 3526-3526 (2019).

Assembly members:
CeSAS-6N, polymer, 170 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
CeSAS-6N: GSMTSKIALFDQTLIASLLQ PLSLNQPDFKAYKTKVKLKI SEQRNETSGEKELKFEISRS DDFEFLFSETLNNEKYQILA RDHDLTVDFDAFPKVIIQHL LCKNIVKNLEEDGEVDARKK AGYHEIADPGKPTEINIILD AEKNFCSFELFSKTPESKGK IFSIKLHAVR

Data sets:
Data typeCount
13C chemical shifts320
15N chemical shifts153
1H chemical shifts153

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1CeSAS-6N1

Entities:

Entity 1, CeSAS-6N 170 residues - Formula weight is not available

Residues 1 and 2 are cloning artefacts. Entry includes two mutations, S123E and I154E, compared to database sequence.

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: CeSAS-6N, [U-98% 13C; U-98% 15N], 0.75 mM; sodium chloride 150 mM; sodium phosphate 20 mM; DTT 2 mM; D2O 5 % v/v; sodium azide 0.02 % w/v; DSS 50 uM

sample_conditions_1: ionic strength: 0.38 M; pH: 7; pressure: 1 atm; temperature: 273 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

Software:

TOPSPIN, Bruker Biospin - collection

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

SPARKY, Goddard - data analysis

PIPP, Garrett - data analysis

NMR spectrometers:

  • Bruker Avance 500 MHz

Related Database Links:

UNP O62479

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