BMRB Entry 27056
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27056
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Title: C. elegans SAS-5 N-term backbone assignments PubMed: 29367435
Deposition date: 2017-03-24 Original release date: 2018-02-02
Authors: Rogala, Kacper; Vakonakis, Ioannis
Citation: Bianchi, Sarah; Rogala, Kacper; Dynes, Nicola; Hilbert, Manuel; Leidel, Sebastian; Steinmetz, Michel; Gonczy, Pierre; Vakonakis, Ioannis. "Interaction between the C. elegans centriolar protein SAS-5 and microtubules facilitates organelle assembly" Mol. Biol. Cell 29, 722-735 (2018).
Assembly members:
sas-5N, polymer, 123 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 Vector: pFLOAT
Entity Sequences (FASTA):
sas-5N: GPNNYDDLPCSIYFKKPTVQ
EFVDQPRVFEDSEVPAFQEV
LQLPQERTKPPVPSTQPIVA
AVEVAKKKSCLSAPKPRKEP
PSHPALRQKTVAFGKTVNVS
QTVEGTSRNSKKVLASTMSA
QNT
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 356 |
| 15N chemical shifts | 107 |
| 1H chemical shifts | 430 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | sas-5N | 1 |
Entities:
Entity 1, sas-5N 123 residues - Formula weight is not available
Residues 1 and 2 are cloning artifacts. Numbering in assignments corresponds to uniprot Q20010 except for the cloning artefact.
| 1 | GLY | PRO | ASN | ASN | TYR | ASP | ASP | LEU | PRO | CYS | ||||
| 2 | SER | ILE | TYR | PHE | LYS | LYS | PRO | THR | VAL | GLN | ||||
| 3 | GLU | PHE | VAL | ASP | GLN | PRO | ARG | VAL | PHE | GLU | ||||
| 4 | ASP | SER | GLU | VAL | PRO | ALA | PHE | GLN | GLU | VAL | ||||
| 5 | LEU | GLN | LEU | PRO | GLN | GLU | ARG | THR | LYS | PRO | ||||
| 6 | PRO | VAL | PRO | SER | THR | GLN | PRO | ILE | VAL | ALA | ||||
| 7 | ALA | VAL | GLU | VAL | ALA | LYS | LYS | LYS | SER | CYS | ||||
| 8 | LEU | SER | ALA | PRO | LYS | PRO | ARG | LYS | GLU | PRO | ||||
| 9 | PRO | SER | HIS | PRO | ALA | LEU | ARG | GLN | LYS | THR | ||||
| 10 | VAL | ALA | PHE | GLY | LYS | THR | VAL | ASN | VAL | SER | ||||
| 11 | GLN | THR | VAL | GLU | GLY | THR | SER | ARG | ASN | SER | ||||
| 12 | LYS | LYS | VAL | LEU | ALA | SER | THR | MET | SER | ALA | ||||
| 13 | GLN | ASN | THR |
Samples:
sample_1: sas-5N, [U-100% 13C; U-100% 15N], 0.5 mM; Potassium PIPES (K-PIPES) 80 mM; EGTA 1 mM; MgCl2 1 mM; NaN3 0.02 % w/v; DSS 50 uM
sample_conditions_1: ionic strength: 0.16 M; pH: 6.8; pressure: 1 atm; temperature: 273 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHAHB | sample_1 | isotropic | sample_conditions_1 |
Software:
Omega_spectrometer_software vvBeta 6.0.3b2, GE - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CCPN_Analysis, CCPN - data analysis
NMR spectrometers:
- Home-built OMEGA 750 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts