BMRB Entry 51763
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51763
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Title: MITF C-terminus backbone assignments
Deposition date: 2023-01-06 Original release date: 2023-08-31
Authors: Langelaan, David; Brown, Alexandra; Lynch, Kyle
Citation: Brown, Alexandra; Lynch, Kyle; Langelaan, David. "Structural analysis of the interactions between the C-terminal transactivation domain of MITF and the TAZ2 domain of CBP/p300" Biochemistry ., .-..
Assembly members:
entity_1, polymer, 133 residues, Formula weight is not available
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET21b
Entity Sequences (FASTA):
entity_1: GSEMQARAHGLSLIPSTGLC
SPDLVNRIIKQEPVLENCSQ
DLLQHHADLTCTTTLDLTDG
TITFNNNLGTGTEANQAYSV
PTKMGSKLEDILMDDTLSPV
GVTDPLLSSVSPGASKTSSR
RSSMSMEETEHTC
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 361 |
| 15N chemical shifts | 116 |
| 1H chemical shifts | 116 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | MITF | 1 |
Entities:
Entity 1, MITF 133 residues - Formula weight is not available
| 1 | GLY | SER | GLU | MET | GLN | ALA | ARG | ALA | HIS | GLY | ||||
| 2 | LEU | SER | LEU | ILE | PRO | SER | THR | GLY | LEU | CYS | ||||
| 3 | SER | PRO | ASP | LEU | VAL | ASN | ARG | ILE | ILE | LYS | ||||
| 4 | GLN | GLU | PRO | VAL | LEU | GLU | ASN | CYS | SER | GLN | ||||
| 5 | ASP | LEU | LEU | GLN | HIS | HIS | ALA | ASP | LEU | THR | ||||
| 6 | CYS | THR | THR | THR | LEU | ASP | LEU | THR | ASP | GLY | ||||
| 7 | THR | ILE | THR | PHE | ASN | ASN | ASN | LEU | GLY | THR | ||||
| 8 | GLY | THR | GLU | ALA | ASN | GLN | ALA | TYR | SER | VAL | ||||
| 9 | PRO | THR | LYS | MET | GLY | SER | LYS | LEU | GLU | ASP | ||||
| 10 | ILE | LEU | MET | ASP | ASP | THR | LEU | SER | PRO | VAL | ||||
| 11 | GLY | VAL | THR | ASP | PRO | LEU | LEU | SER | SER | VAL | ||||
| 12 | SER | PRO | GLY | ALA | SER | LYS | THR | SER | SER | ARG | ||||
| 13 | ARG | SER | SER | MET | SER | MET | GLU | GLU | THR | GLU | ||||
| 14 | HIS | THR | CYS |
Samples:
sample_1: MITF289-419, [U-99% 13C; U-99% 15N], 700 uM; D2O 5%; DTT 5 mM; MES 20 mM; NaCl 25 mM
sample_conditions_1: pH: 6.0; pressure: 1 atm; temperature: 308.15 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 CBCACONH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACO | sample_1 | isotropic | sample_conditions_1 |
Software:
CcpNMR - chemical shift assignment
NMR spectrometers:
- Bruker AVANCE III 700 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts