BMRB Entry 16363
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16363
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Title: Solution structure of the Nuclear coactivator binding domain of CBP PubMed: 20616042
Deposition date: 2009-06-24 Original release date: 2010-08-16
Authors: Kjaergaard, Magnus; Teilum, Kaare; Poulsen, Flemming
Citation: Kjaergaard, Magnus; Teilum, Kaare; Poulsen, Flemming. "Conformational selection in the molten globule state of the nuclear coactivator binding domain of CBP" Proc. Natl. Acad. Sci. U S A. 107, 12535-12540 (2010).
Assembly members:
CBP, polymer, 59 residues, 6568.623 Da.
Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
CBP: PNRSISPSALQDLLRTLKSP
SSPQQQQQVLNILKSNPQLM
AAFIKQRTAKYVANQPGMQ
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 236 |
| 15N chemical shifts | 49 |
| 1H chemical shifts | 372 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | CBP | 1 |
Entities:
Entity 1, CBP 59 residues - 6568.623 Da.
| 1 | PRO | ASN | ARG | SER | ILE | SER | PRO | SER | ALA | LEU | ||||
| 2 | GLN | ASP | LEU | LEU | ARG | THR | LEU | LYS | SER | PRO | ||||
| 3 | SER | SER | PRO | GLN | GLN | GLN | GLN | GLN | VAL | LEU | ||||
| 4 | ASN | ILE | LEU | LYS | SER | ASN | PRO | GLN | LEU | MET | ||||
| 5 | ALA | ALA | PHE | ILE | LYS | GLN | ARG | THR | ALA | LYS | ||||
| 6 | TYR | VAL | ALA | ASN | GLN | PRO | GLY | MET | GLN |
Samples:
sample_1: D2O 10%; sodium chloride 20 mM; sodium phosphate 20 mM; protein, [U-100% 13C; U-100% 15N], 2 mM; H2O 90%
sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 304 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
ARIA v2.2, Linge, O, . - structure solution
NMR spectrometers:
- Varian INOVA 750 MHz
- Bruker Avance 800 MHz
Related Database Links:
| BMRB | 15398 17073 |
| PDB | |
| DBJ | BAE06125 BAI45616 |
| GB | AAB28651 AAC17736 AAC51331 AAC51340 AAC51770 |
| PRF | 1923401A |
| REF | NP_001020603 NP_001073315 NP_001247644 NP_004371 NP_596872 |
| SP | P45481 Q6JHU9 Q92793 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts