BMRB Entry 50308
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50308
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
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: 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:
entity_1, polymer, 154 residues, Formula weight is not available
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
Entity Sequences (FASTA):
entity_1: GPMSQVLFHQLVPLQVKCKD
CEERRVSIRMSIELQSVSNP
VHRKDLVIRLTDDTDPFFLY
NLVISEEDFQSLKFQQGLLV
DFLAFPQKFIDLLQQCTQEH
AKEIPRFLLQLVSPAAILDN
SPAFLNVVETNPDKHLTHLS
LKLLPGNDVEIKKF
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 224 |
| 15N chemical shifts | 110 |
| 1H chemical shifts | 110 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | hsSAS-6 | 1 |
Entities:
Entity 1, hsSAS-6 154 residues - Formula weight is not available
First two residues are cloning artifacts
| 1 | GLY | PRO | MET | SER | GLN | VAL | LEU | PHE | HIS | GLN | ||||
| 2 | LEU | VAL | PRO | LEU | GLN | VAL | LYS | CYS | LYS | ASP | ||||
| 3 | CYS | GLU | GLU | ARG | ARG | VAL | SER | ILE | ARG | MET | ||||
| 4 | SER | ILE | GLU | LEU | GLN | SER | VAL | SER | ASN | PRO | ||||
| 5 | VAL | HIS | ARG | LYS | ASP | LEU | VAL | ILE | ARG | LEU | ||||
| 6 | THR | ASP | ASP | THR | ASP | PRO | PHE | PHE | LEU | TYR | ||||
| 7 | ASN | LEU | VAL | ILE | SER | GLU | GLU | ASP | PHE | GLN | ||||
| 8 | SER | LEU | LYS | PHE | GLN | GLN | GLY | LEU | LEU | VAL | ||||
| 9 | ASP | PHE | LEU | ALA | PHE | PRO | GLN | LYS | PHE | ILE | ||||
| 10 | ASP | LEU | LEU | GLN | GLN | CYS | THR | GLN | GLU | HIS | ||||
| 11 | ALA | LYS | GLU | ILE | PRO | ARG | PHE | LEU | LEU | GLN | ||||
| 12 | LEU | VAL | SER | PRO | ALA | ALA | ILE | LEU | ASP | ASN | ||||
| 13 | SER | PRO | ALA | PHE | LEU | ASN | VAL | VAL | GLU | THR | ||||
| 14 | ASN | PRO | ASP | LYS | HIS | LEU | THR | HIS | LEU | SER | ||||
| 15 | LEU | LYS | LEU | LEU | PRO | GLY | ASN | ASP | VAL | GLU | ||||
| 16 | ILE | LYS | LYS | PHE |
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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N 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 HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN - collection
NMRPipe - processing
SPARKY - data analysis
PINE - chemical shift assignment
NMR spectrometers:
- Bruker AVANCE III 17.6 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts