BMRB Entry 25426
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25426
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Title: MBD2 intrinsically disordered region PubMed: 25753662
Deposition date: 2015-01-12 Original release date: 2018-02-23
Authors: Williams, David
Citation: Desai, Megha; Webb, Heather; Sinanan, Leander; Scarsdale, Neel; Walavalkar, Ninad; Ginder, Gordon; Williams, David. "An intrinsically disordered region of methyl-CpG binding domain protein 2 (MBD2) recruits the histone deacetylase core of the NuRD complex" Nucleic Acids Res. 43, 3100-3113 (2015).
Assembly members:
MBD2, polymer, 121 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: pet32a
Entity Sequences (FASTA):
MBD2: GSDLNTTLPIRQTASIFKQP
VTKVTNHPSNKVKSDPQRMN
EQPRQLFWEKRLQGLSASDV
TEQIIKTMELPKGLQGVGPG
SNDETLLSAVASALHTSSAP
ITGQVSAAVEKNPAVWLNTS
Q
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 331 |
| 15N chemical shifts | 106 |
| 1H chemical shifts | 366 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | MBD2 IDR | 1 |
Entities:
Entity 1, MBD2 IDR 121 residues - Formula weight is not available
Residue 1-2 represent residual from non-native affinity tag.
| 1 | GLY | SER | ASP | LEU | ASN | THR | THR | LEU | PRO | ILE | ||||
| 2 | ARG | GLN | THR | ALA | SER | ILE | PHE | LYS | GLN | PRO | ||||
| 3 | VAL | THR | LYS | VAL | THR | ASN | HIS | PRO | SER | ASN | ||||
| 4 | LYS | VAL | LYS | SER | ASP | PRO | GLN | ARG | MET | ASN | ||||
| 5 | GLU | GLN | PRO | ARG | GLN | LEU | PHE | TRP | GLU | LYS | ||||
| 6 | ARG | LEU | GLN | GLY | LEU | SER | ALA | SER | ASP | VAL | ||||
| 7 | THR | GLU | GLN | ILE | ILE | LYS | THR | MET | GLU | LEU | ||||
| 8 | PRO | LYS | GLY | LEU | GLN | GLY | VAL | GLY | PRO | GLY | ||||
| 9 | SER | ASN | ASP | GLU | THR | LEU | LEU | SER | ALA | VAL | ||||
| 10 | ALA | SER | ALA | LEU | HIS | THR | SER | SER | ALA | PRO | ||||
| 11 | ILE | THR | GLY | GLN | VAL | SER | ALA | ALA | VAL | GLU | ||||
| 12 | LYS | ASN | PRO | ALA | VAL | TRP | LEU | ASN | THR | SER | ||||
| 13 | GLN |
Samples:
sample_1: MBD2, [U-99% 13C; U-99% 15N], 0.5 – 1 mM; H2O 90%; D2O 10%; NaH2PO4 10 mM; sodium azide 0.02%; DTT 1 mM
sample_conditions_1: ionic strength: 25 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N 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 HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CcpNMR, CCPN - chemical shift assignment
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Bruker Avance 700 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts