BMRB Entry 26599
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26599
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Title: 1H, 13Ca, 13Cb and 15N chemical shift assignment of coiled-coil motif from human Thanatos-associated protein 11 PubMed: 26975212
Deposition date: 2015-07-06 Original release date: 2016-05-09
Authors: Cukier, Cyprian; Milon, Alain; Gervais, Virginie
Citation: Cukier, Cyprian; Gervais, Virginie. "The C-terminal region of the transcriptional regulator THAP11 forms a parallel coiled-coil domain involved in protein dimerization" J. Struct. Biol. 194, 337-346 (2016).
Assembly members:
THAP11, polymer, 68 residues, 8038 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
Entity Sequences (FASTA):
THAP11: GAMGTTEEELLRKLNEQRDI
LALMEVKMKEMKGSIRHLRL
TEAKLREELREKDRLLAMAV
IRKKHGMY
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 130 |
| 15N chemical shifts | 66 |
| 1H chemical shifts | 66 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | THAP11 coiled-coil, chain A | 1 |
| 2 | THAP11 coiled-coil, chain B | 1 |
Entities:
Entity 1, THAP11 coiled-coil, chain A 68 residues - 8038 Da.
N-terminal GAM residues are the result of clonic procedure. The C-terminal Y residue was introduced to facilitate protein quantification. This is a coiled-coil motif of THAP11 protein.
| 1 | GLY | ALA | MET | GLY | THR | THR | GLU | GLU | GLU | LEU | ||||
| 2 | LEU | ARG | LYS | LEU | ASN | GLU | GLN | ARG | ASP | ILE | ||||
| 3 | LEU | ALA | LEU | MET | GLU | VAL | LYS | MET | LYS | GLU | ||||
| 4 | MET | LYS | GLY | SER | ILE | ARG | HIS | LEU | ARG | LEU | ||||
| 5 | THR | GLU | ALA | LYS | LEU | ARG | GLU | GLU | LEU | ARG | ||||
| 6 | GLU | LYS | ASP | ARG | LEU | LEU | ALA | MET | ALA | VAL | ||||
| 7 | ILE | ARG | LYS | LYS | HIS | GLY | MET | TYR |
Samples:
sample_1: THAP11, [U-15N], 0.28 – 0.46 mM; sodium/potassium phosphate 10 mM; sodium chloride 50 mM; H2O 90%; D2O 10%
sample_2: THAP11, [U-13C; U-15N], 0.3 – 0.5 mM; sodium/potassium phosphate 10 mM; sodium chloride 50 mM; DTT 2 mM; H2O 90%; D2O 10%
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 CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_2 | 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 HNCACB | 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
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts