BMRB Entry 50143
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50143
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Title: 1H, 15N, and 13C backbone chemical shift assignments for the first bromodomain of BRD2 (BRD2-BD1) 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 first bromodomain of BRD2, polymer, 135 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 first bromodomain of BRD2: GPLGSEVSNPKKPGRVTNQL
QYLHKVVMKALWKHQFAWPF
RQPVDAVKLGLPDYHKIIKQ
PMDMGTIKRRLENNYYWAAS
ECMQDFNTMFTNCYIYNKPT
DDIVLMAQTLEKIFLQKVAS
MPQEEQELVVTIPKN
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 263 |
15N chemical shifts | 122 |
1H chemical shifts | 122 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | The first bromodomain of BRD2 (BRD2-BD1) | 1 |
Entities:
Entity 1, The first bromodomain of BRD2 (BRD2-BD1) 135 residues - Formula weight is not available
1 | GLY | PRO | LEU | GLY | SER | GLU | VAL | SER | ASN | PRO | ||||
2 | LYS | LYS | PRO | GLY | ARG | VAL | THR | ASN | GLN | LEU | ||||
3 | GLN | TYR | LEU | HIS | LYS | VAL | VAL | MET | LYS | ALA | ||||
4 | LEU | TRP | LYS | HIS | GLN | PHE | ALA | TRP | PRO | PHE | ||||
5 | ARG | GLN | PRO | VAL | ASP | ALA | VAL | LYS | LEU | GLY | ||||
6 | LEU | PRO | ASP | TYR | HIS | LYS | ILE | ILE | LYS | GLN | ||||
7 | PRO | MET | ASP | MET | GLY | THR | ILE | LYS | ARG | ARG | ||||
8 | LEU | GLU | ASN | ASN | TYR | TYR | TRP | ALA | ALA | SER | ||||
9 | GLU | CYS | MET | GLN | ASP | PHE | ASN | THR | MET | PHE | ||||
10 | THR | ASN | CYS | TYR | ILE | TYR | ASN | LYS | PRO | THR | ||||
11 | ASP | ASP | ILE | VAL | LEU | MET | ALA | GLN | THR | LEU | ||||
12 | GLU | LYS | ILE | PHE | LEU | GLN | LYS | VAL | ALA | SER | ||||
13 | MET | PRO | GLN | GLU | GLU | GLN | GLU | LEU | VAL | VAL | ||||
14 | THR | ILE | PRO | LYS | ASN |
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 HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
Software:
CcpNMR, CCPN - chemical shift assignment
TOPSPIN, Bruker Biospin - collection
NMR spectrometers:
- Bruker Avance 600 MHz
- 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