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 51846

Title: MEG 2.1, isoform 1, peptide C   PubMed: 37535563

Deposition date: 2023-02-20 Original release date: 2024-02-16

Authors: Nedvedova, Stepanka; Guilliere, Florence; Miele, Adriana Erica; Dvorak, Jan; Walker, Olivier; Hologne, Maggy

Citation: Nedvedova, Stepanka; Guilliere, Florence; Miele, Adriana Erica; Cantrelle, Francis-Xavier; Dvorak, Jan; Walker, Olivier; Hologne, Maggy. "Divide, conquer and reconstruct: How to solve the 3D structure of recalcitrant Micro-Exon Gene (MEG) protein from Schistosoma mansoni"  PLoS One 18, e0289444-e0289444 (2023).

Assembly members:
entity_1, polymer, 15 residues, Formula weight is not available

Natural source:   Common Name: Schistosoma mansoni   Taxonomy ID: 6183   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Schistosoma mansoni

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):
entity_1: STPDLLLGNYQRHQR

Data sets:
Data typeCount
13C chemical shifts26
15N chemical shifts16
1H chemical shifts101

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1MEG 2.11

Entities:

Entity 1, MEG 2.1 15 residues - Formula weight is not available

1   SERTHRPROASPLEULEULEUGLYASNTYR
2   GLNARGHISGLNARG

Samples:

sample_1: MEG 2.1 isoform 1, peptide 1C 2 mM

sample_conditions_1: pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1

Software:

SPARKY - chemical shift assignment

NMR spectrometers:

  • Agilent INOVA 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts