BMRB Entry 11566
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11566
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Title: L105P-RPEL1 motif of MKL1 PubMed: 24909411
Deposition date: 2014-04-18 Original release date: 2017-03-08
Authors: Mizuguchi, Mineyuki; Fuju, Takahiro; Obita, Takayuki
Citation: Mizuguchi, Mineyuki; Fuju, Takahiro; Obita, Takayuki; Ishikawa, Mitsuru; Tsuda, Masaaki; Tabuchi, Akiko. "Transient alpha-helices in the disordered RPEL motifs of the serum response factor coactivator MKL1" Sci. Rep. 4, 5224-5224 (2014).
Assembly members:
L105P-MKL1, polymer, 36 residues, Formula weight is not available
Natural source: Common Name: Rat Taxonomy ID: 10116 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rattus norvegicus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pOP3C
Entity Sequences (FASTA):
L105P-MKL1: GPHMLSERKNVLQLKLQQRR
TREEPVSQGIMPPLKS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 61 |
| 15N chemical shifts | 28 |
| 1H chemical shifts | 28 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | L105P-RPEL1 | 1 |
Entities:
Entity 1, L105P-RPEL1 36 residues - Formula weight is not available
This is the L105P-RPEL motif of rat MKL1 protein.
| 1 | GLY | PRO | HIS | MET | LEU | SER | GLU | ARG | LYS | ASN | ||||
| 2 | VAL | LEU | GLN | LEU | LYS | LEU | GLN | GLN | ARG | ARG | ||||
| 3 | THR | ARG | GLU | GLU | PRO | VAL | SER | GLN | GLY | ILE | ||||
| 4 | MET | PRO | PRO | LEU | LYS | SER |
Samples:
sample_1: L105P-MKL1, [U-100% 13C; U-100% 15N], 0.12 – 0.50 mM; sodium phosphate 10 mM; sodium chloride 50 mM; D2O, [U-100% 2H], 7%; sodium azide 1 mM; DSS 20 uM; H2O 93%
sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 288 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 CBCANH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRView v8.0.3, Johnson, One Moon Scientific - chemical shift assignment
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