BMRB Entry 50146
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50146
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: 1H, 15N, and 13C backbone chemical shift assignments for the second bromodomain of BRD4 (BRD4-BD2) PubMed: 33620209
Deposition date: 2019-12-31 Original release date: 2021-08-12
Authors: Patel, Karishma; Mackay, Joel; Solomon, Paul
Citation: Patel, Karishma; Solomon, Paul; Walshe, James; Ford, Daniel; Wilkinson-White, Lorna; Payne, Richard; Low, Jason; Mackay, Joel. "BET-Family Bromodomains Can Recognize Diacetylated Sequences from Transcription Factors Using a Conserved Mechanism" Biochemistry 60, 648-662 (2021).
Assembly members:
The second bromdomain of BRD4, polymer, 122 residues, Formula weight is not available
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 Vector: pGEX-6P
Entity Sequences (FASTA):
The second bromdomain of BRD4: GPLGSSKVSEQLKCCSGILK
EMFAKKHAAYAWPFYKPVDV
EALGLHDYCDIIKHPMDMST
IKSKLEAREYRDAQEFGADV
RLMFSNCYKYNPPDHEVVAM
ARKLQDVFEMRFAKMPDEPE
EP
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 143 |
| 15N chemical shifts | 84 |
| 1H chemical shifts | 84 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | The second bromodomain of BRD4 | 1 |
Entities:
Entity 1, The second bromodomain of BRD4 122 residues - Formula weight is not available
| 1 | GLY | PRO | LEU | GLY | SER | SER | LYS | VAL | SER | GLU | ||||
| 2 | GLN | LEU | LYS | CYS | CYS | SER | GLY | ILE | LEU | LYS | ||||
| 3 | GLU | MET | PHE | ALA | LYS | LYS | HIS | ALA | ALA | TYR | ||||
| 4 | ALA | TRP | PRO | PHE | TYR | LYS | PRO | VAL | ASP | VAL | ||||
| 5 | GLU | ALA | LEU | GLY | LEU | HIS | ASP | TYR | CYS | ASP | ||||
| 6 | ILE | ILE | LYS | HIS | PRO | MET | ASP | MET | SER | THR | ||||
| 7 | ILE | LYS | SER | LYS | LEU | GLU | ALA | ARG | GLU | TYR | ||||
| 8 | ARG | ASP | ALA | GLN | GLU | PHE | GLY | ALA | ASP | VAL | ||||
| 9 | ARG | LEU | MET | PHE | SER | ASN | CYS | TYR | LYS | TYR | ||||
| 10 | ASN | PRO | PRO | ASP | HIS | GLU | VAL | VAL | ALA | MET | ||||
| 11 | ALA | ARG | LYS | LEU | GLN | ASP | VAL | PHE | GLU | MET | ||||
| 12 | ARG | PHE | ALA | LYS | MET | PRO | ASP | GLU | PRO | GLU | ||||
| 13 | GLU | PRO |
Samples:
sample_1: DSS 0.01 mM; TRIS 10 mM; sodium chloride 100 mM; DTT 1 mM
sample_conditions_1: ionic strength: 100 mM; pH: 7.2; pressure: 1 atm; temperature: 298 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 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 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CcpNMR, CCPN - chemical shift assignment
TOPSPIN, Bruker Biospin - collection
NMR spectrometers:
- Bruker Avance 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts