BMRB Entry 51840
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51840
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Title: 1H, 13C and 15N resonance assignments of four MEF2D b-domain peptide constructs (wild type) PubMed: 36898987
Deposition date: 2023-02-18 Original release date: 2023-02-21
Authors: Nagy, Tamas Milan; Feher, Krisztina; Kover, Katalin
Citation: Gonczi, Monika; Teixeira, Joao; Barrera-Vilarmau, Susana; Mediani, Laura; Antoniani, Francesco; Nagy, Tamas Milan; Feher, Krisztina; Raduly, Zsolt; Ambrus, Viktor; Tozser, Jozsef; Barta, Endre; Kover, Katalin; Csernoch, Laszlo; Carra, Serena; Fuxreiter, Monika. "Alternatively spliced exon regulates context-dependent MEF2D higher-order assembly during myogenesis" Nat. Commun. 14, 1329-1329 (2023).
Assembly members:
entity_1, polymer, 37 residues, Formula weight is not available
Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available
Experimental source: Production method: chemical synthesis
Entity Sequences (FASTA):
entity_1: SRKPDLRVITSQAGKGLMHH
LTEDHLDLNNAQRLGVS
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 73 |
15N chemical shifts | 5 |
1H chemical shifts | 234 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | MEF2D wt | 1 |
Entities:
Entity 1, MEF2D wt 37 residues - Formula weight is not available
1 | SER | ARG | LYS | PRO | ASP | LEU | ARG | VAL | ILE | THR | ||||
2 | SER | GLN | ALA | GLY | LYS | GLY | LEU | MET | HIS | HIS | ||||
3 | LEU | THR | GLU | ASP | HIS | LEU | ASP | LEU | ASN | ASN | ||||
4 | ALA | GLN | ARG | LEU | GLY | VAL | SER |
Samples:
sample_1: MEF2D wild-type construct, [U-15N]-Leu, 1 mM; DSS 8 ug; Na2HPO4/NaH2PO4 20 mM; sodium chloride 100 mM
sample_conditions_1: pH: 6; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-1H ROESY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC-TOCSY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC-TOCSY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC-ROESY | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v4.0.5 - data collection and analysis
CARA v1.9 - chemical shift assignment
NMR spectrometers:
- Bruker AVANCE NEO 700 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts