BMRB Entry 18022
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR18022
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Title: Structure of the Cx43 C-terminal domain bound to tubulin PubMed: 22558917
Deposition date: 2011-10-26 Original release date: 2012-05-22
Authors: Saidi Brikci-Nigassa, Amal; Clement, Marie-Jeanne; Ha-Duong, Tap; Benmansour, Kamal; Adjadj, Elisabeth; Ziani, Latifa; Pastre, David; Curmi, Patrick
Citation: Saidi Brikci-Nigassa, Amal; Clement, Marie-Jeanne; Ha-Duong, Tap; Adjadj, Elisabeth; Ziani, Latifa; Pastre, David; Curmi, Patrick; Savarin, Philippe. "Phosphorylation controls the interaction of the connexin43 C-terminal domain with tubulin and microtubules." Biochemistry 51, 4331-4342 (2012).
Assembly members:
entity, polymer, 26 residues, 2720.094 Da.
Natural source: Common Name: Rat Taxonomy ID: 10116 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rattus norvegicus
Experimental source: Production method: chemical synthesis
Entity Sequences (FASTA):
entity: KGVKDRVKGKSDPYHATSGA
LSPAKD
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 164 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Cx43 | 1 |
Entities:
Entity 1, Cx43 26 residues - 2720.094 Da.
Swiss-Prot: P08050.2
| 1 | LYS | GLY | VAL | LYS | ASP | ARG | VAL | LYS | GLY | LYS | ||||
| 2 | SER | ASP | PRO | TYR | HIS | ALA | THR | SER | GLY | ALA | ||||
| 3 | LEU | SER | PRO | ALA | LYS | ASP |
Samples:
sample_1: Cx43 0.8 mM; D2O, [U-100% 15N], 0.04 mM; PIPES, [U-100% 15N], 50 mM; H2O 95%; D2O 5%
sample_2: Cx43 0.8 mM; D2O, [U-100% 15N], 0.04 mM; PIPES, [U-100% 15N], 50 mM; tubulin 0.04 mM; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 0 M; pH: 6.9; pressure: 1 atm; temperature: 282 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions_1 |
| 1D STD | sample_2 | isotropic | sample_conditions_1 |
| 1D STD | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRView v5.2, Johnson, One Moon Scientific - chemical shift assignment, peak picking
NMR spectrometers:
- Bruker Avance 600 MHz