BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 51842

Title: 1H, 13C and 15N resonance assignments of four MEF2D b-domain peptide constructs (var4)   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 LTEDHLDNNNHQRLGTS

Data sets:
Data typeCount
13C chemical shifts73
15N chemical shifts4
1H chemical shifts210

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1MEF2D var41

Entities:

Entity 1, MEF2D var4 37 residues - Formula weight is not available

1   SERARGLYSPROASPLEUARGVALILETHR
2   SERGLNALAGLYLYSGLYLEUMETHISHIS
3   LEUTHRGLUASPHISLEUASPASNASNASN
4   HISGLNARGLEUGLYTHRSER

Samples:

sample_1: MEF2D construct var4, [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:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H ROESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC-TOCSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQC-TOCSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQC-ROESYsample_1isotropicsample_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