BMRB Entry 25792
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR25792
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Title: p65dd PubMed: 26647230
Deposition date: 2015-09-02 Original release date: 2016-09-02
Authors: Dyson, Jane; Mukherjee, Sulakshana; Borin, Brendan; Quintas, Pedro
Citation: Mukherjee, Sulakshana; Borin, Brendan; Quintas, Pedro; Dyson, Jane. "NMR characterization of a 72 kDa transcription factor using differential isotopic labeling" Protein Sci. 25, 597-604 (2016).
Assembly members:
p65dd, polymer, 132 residues, Formula weight is not available
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):
p65dd: NTAELKICRVNRNSGSCLGG
DEIFLLCDKVQKEDIEVYFT
GPGWEARGSFSQADVHRQVA
IVFRTPPYADPSLQAPVRVS
MQLRRPSDRELSEPMEFQYL
PDTDDRHRIEEKRKRTYETF
KSIMKKSPFNGP
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 255 |
| 15N chemical shifts | 125 |
| 1H chemical shifts | 125 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | p65 dimerization domain | 1 |
Entities:
Entity 1, p65 dimerization domain 132 residues - Formula weight is not available
| 1 | ASN | THR | ALA | GLU | LEU | LYS | ILE | CYS | ARG | VAL | ||||
| 2 | ASN | ARG | ASN | SER | GLY | SER | CYS | LEU | GLY | GLY | ||||
| 3 | ASP | GLU | ILE | PHE | LEU | LEU | CYS | ASP | LYS | VAL | ||||
| 4 | GLN | LYS | GLU | ASP | ILE | GLU | VAL | TYR | PHE | THR | ||||
| 5 | GLY | PRO | GLY | TRP | GLU | ALA | ARG | GLY | SER | PHE | ||||
| 6 | SER | GLN | ALA | ASP | VAL | HIS | ARG | GLN | VAL | ALA | ||||
| 7 | ILE | VAL | PHE | ARG | THR | PRO | PRO | TYR | ALA | ASP | ||||
| 8 | PRO | SER | LEU | GLN | ALA | PRO | VAL | ARG | VAL | SER | ||||
| 9 | MET | GLN | LEU | ARG | ARG | PRO | SER | ASP | ARG | GLU | ||||
| 10 | LEU | SER | GLU | PRO | MET | GLU | PHE | GLN | TYR | LEU | ||||
| 11 | PRO | ASP | THR | ASP | ASP | ARG | HIS | ARG | ILE | GLU | ||||
| 12 | GLU | LYS | ARG | LYS | ARG | THR | TYR | GLU | THR | PHE | ||||
| 13 | LYS | SER | ILE | MET | LYS | LYS | SER | PRO | PHE | ASN | ||||
| 14 | GLY | PRO |
Samples:
sample_1: p65dd, [U-100% 13C; U-100% 15N; U-80% 2H], 0.3 ± 0.1 mM; p50dd, [U-100% 2H], 0.3 ± 0.1 mM; TRIS, [U-2H], 20 mM; sodium chloride 50 mM; DTT, [U-2H], 2 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.05 M; pH: 6.8; pressure: 1 atm; temperature: 298 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 HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRView, Johnson, One Moon Scientific - data analysis
NMR spectrometers:
- Bruker DRX 600 MHz
- Bruker Avance 750 MHz
- Bruker Avance 900 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts