BMRB Entry 27106
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27106
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Human BRM AT-hook and Bromodomain PubMed: 28706277
Deposition date: 2017-05-15 Original release date: 2017-06-01
Authors: Morrison, Emma
Citation: Morrison, Emma; Sanchez, Julio; Ronan, Jehnna; Farrell, Daniel; Varzavand, Katayoun; Johnson, Jenna; Gu, Brian; Crabtree, Gerald; Musselman, Catherine. "DNA binding drives the association of BRG1/hBRM bromodomains with nucleosomes" Nat Commun. 8, 16080-16080 (2017).
Assembly members:
BRM_AT-BRD, polymer, 153 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: pDEST15
Entity Sequences (FASTA):
BRM_AT-BRD: GPKEDVEKAKKRRGRPPAEK
LSPNPPKLTKQMNAIIDTVI
NYKDRCNVEKVPSNSQLEIE
GNSSGRQLSEVFIQLPSRKE
LPEYYELIRKPVDFKKIKER
IRNHKYRSLGDLEKDVMLLC
HNAQTFNLEGSQIYEDSIVL
QSVFKSARQKIAK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 190 |
| 15N chemical shifts | 131 |
| 1H chemical shifts | 131 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | AT-BRD | 1 |
Entities:
Entity 1, AT-BRD 153 residues - Formula weight is not available
| 1 | GLY | PRO | LYS | GLU | ASP | VAL | GLU | LYS | ALA | LYS | ||||
| 2 | LYS | ARG | ARG | GLY | ARG | PRO | PRO | ALA | GLU | LYS | ||||
| 3 | LEU | SER | PRO | ASN | PRO | PRO | LYS | LEU | THR | LYS | ||||
| 4 | GLN | MET | ASN | ALA | ILE | ILE | ASP | THR | VAL | ILE | ||||
| 5 | ASN | TYR | LYS | ASP | ARG | CYS | ASN | VAL | GLU | LYS | ||||
| 6 | VAL | PRO | SER | ASN | SER | GLN | LEU | GLU | ILE | GLU | ||||
| 7 | GLY | ASN | SER | SER | GLY | ARG | GLN | LEU | SER | GLU | ||||
| 8 | VAL | PHE | ILE | GLN | LEU | PRO | SER | ARG | LYS | GLU | ||||
| 9 | LEU | PRO | GLU | TYR | TYR | GLU | LEU | ILE | ARG | LYS | ||||
| 10 | PRO | VAL | ASP | PHE | LYS | LYS | ILE | LYS | GLU | ARG | ||||
| 11 | ILE | ARG | ASN | HIS | LYS | TYR | ARG | SER | LEU | GLY | ||||
| 12 | ASP | LEU | GLU | LYS | ASP | VAL | MET | LEU | LEU | CYS | ||||
| 13 | HIS | ASN | ALA | GLN | THR | PHE | ASN | LEU | GLU | GLY | ||||
| 14 | SER | GLN | ILE | TYR | GLU | ASP | SER | ILE | VAL | LEU | ||||
| 15 | GLN | SER | VAL | PHE | LYS | SER | ALA | ARG | GLN | LYS | ||||
| 16 | ILE | ALA | LYS |
Samples:
sample_1: BRM, [U-100% 13C; U-100% 15N], 0.5 mM; KPi 50 mM; KCl 50 mM
sample_conditions_1: ionic strength: 129 mM; pH: 7.0; pressure: 1 atm; temperature: 293 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 |
| HNCA | sample_1 | isotropic | sample_conditions_1 |
Software:
CCPNMR, CCPN - chemical shift assignment
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Varian INOVA 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts