BMRB Entry 27093
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27093
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Title: Chemical shift assignment of human MOZART1 protein (mitotic-spindle organizing protein associated with a ring of gamma-tubulin 1) PubMed: 28851027
Deposition date: 2017-05-04 Original release date: 2017-09-15
Authors: Cukier, Cyprian; Gervais, Virginie; Milon, Alain
Citation: Cukier, Cyprian; Tourdes, Audrey; El-Mazouni, Dounia; Guillet, Valerie; Nomme, Julian; Mourey, Lionel; Milon, Alain; Merdes, Andreas; Gervais, Virginie. "NMR secondary structure and interactions of recombinant human MOZART1 protein, a component of the gamma-tubulin complex" Protein Sci. 26, 2240-2248 (2017).
Assembly members:
MOZART1, polymer, 85 residues, 8760 Da.
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: pET28a
Entity Sequences (FASTA):
MOZART1: GSHMASSSGAGAAAAAAAAN
LNAVRETMDVLLEISRILNT
GLDMETLSICVRLCEQGINP
EALSSVIKELRKATEALKAA
ENMTS
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 298 |
15N chemical shifts | 77 |
1H chemical shifts | 471 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | MOZART1 | 1 |
Entities:
Entity 1, MOZART1 85 residues - 8760 Da.
N-terminal GSH residues are the result of clonic procedure. This is a full-length MOZART1 protein.
1 | GLY | SER | HIS | MET | ALA | SER | SER | SER | GLY | ALA | ||||
2 | GLY | ALA | ALA | ALA | ALA | ALA | ALA | ALA | ALA | ASN | ||||
3 | LEU | ASN | ALA | VAL | ARG | GLU | THR | MET | ASP | VAL | ||||
4 | LEU | LEU | GLU | ILE | SER | ARG | ILE | LEU | ASN | THR | ||||
5 | GLY | LEU | ASP | MET | GLU | THR | LEU | SER | ILE | CYS | ||||
6 | VAL | ARG | LEU | CYS | GLU | GLN | GLY | ILE | ASN | PRO | ||||
7 | GLU | ALA | LEU | SER | SER | VAL | ILE | LYS | GLU | LEU | ||||
8 | ARG | LYS | ALA | THR | GLU | ALA | LEU | LYS | ALA | ALA | ||||
9 | GLU | ASN | MET | THR | SER |
Samples:
sample_1: MOZART1, [U-99% 13C; U-99% 15N], 0.55 mM; sodium phosphate pH 6.0 10 mM; sodium chloride 50 mM; DTT 2 mM; sulfobetaine-12 30-50 mM; DSS 10 uM
sample_2: MOZART1, [U-99% 13C; U-99% 15N], 0.56 mM; sodium phosphate pH 6.0 10 mM; sodium chloride 50 mM; DTT 2 mM; sulfobetaine-12, d25 (25 protons substituted by deuters), 50 mM; DSS 10 uM
sample_conditions_1: pH: 6; pressure: 1 atm; temperature: 310 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D BEST-HN(CO)CACB | sample_1 | isotropic | sample_conditions_1 |
3D BEST-HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D BEST-HNCO | sample_1 | isotropic | sample_conditions_1 |
3D BEST-HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
3D HC(C)H-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D (H)CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection, processing
SPARKY, Goddard - chemical shift assignment, data analysis
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 950 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts