BMRB Entry 26770
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26770
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Citation: Launay, Helene; Barre, Patrick; Puppo, Carine; Manneville, Stephanie; Gontero-Meunier, Brigitte; Receveur-Brechot, Veronique. "Absence of residual structure in the intrinsically disordered regulatory protein CP12 in its reduced state" Biochem. Biophys. Res. Commun. 477, 20-26 (2016).
PubMed: 27268235
Assembly members:
CP12_reduced, polymer, 99 residues, Formula weight is not available
Natural source: Common Name: green algae Taxonomy ID: 3055 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Chlamydomonas reinhardtii
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEM-T
Entity Sequences (FASTA):
CP12_reduced: HHHHHHHHHSSGHIEGRHMS
GQPAVDLNKKVQDAVKEAED
ACAKGTSADCAVAWDTVEEL
SAAVSHKKDAVKADVTLTDP
LEAFCKDAPDADECRVYED
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 263 |
| 15N chemical shifts | 85 |
| 1H chemical shifts | 467 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | CP12 reduced | 1 |
Entities:
Entity 1, CP12 reduced 99 residues - Formula weight is not available
| 1 | HIS | HIS | HIS | HIS | HIS | HIS | HIS | HIS | HIS | SER | ||||
| 2 | SER | GLY | HIS | ILE | GLU | GLY | ARG | HIS | MET | SER | ||||
| 3 | GLY | GLN | PRO | ALA | VAL | ASP | LEU | ASN | LYS | LYS | ||||
| 4 | VAL | GLN | ASP | ALA | VAL | LYS | GLU | ALA | GLU | ASP | ||||
| 5 | ALA | CYS | ALA | LYS | GLY | THR | SER | ALA | ASP | CYS | ||||
| 6 | ALA | VAL | ALA | TRP | ASP | THR | VAL | GLU | GLU | LEU | ||||
| 7 | SER | ALA | ALA | VAL | SER | HIS | LYS | LYS | ASP | ALA | ||||
| 8 | VAL | LYS | ALA | ASP | VAL | THR | LEU | THR | ASP | PRO | ||||
| 9 | LEU | GLU | ALA | PHE | CYS | LYS | ASP | ALA | PRO | ASP | ||||
| 10 | ALA | ASP | GLU | CYS | ARG | VAL | TYR | GLU | ASP |
Samples:
sample_1: CP12 reduced, [U-100% 13C; U-100% 15N], 770 uM; DTT 20 mM; sodium phosphate 50 mM; sodium chloride 50 mM; sodium azide 2%
sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 273 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 HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCACO | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CcpNMR, CCPN - chemical shift assignment
NMR spectrometers:
- Bruker Avance 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks