BMRB Entry 51846

Name: MEG 2.1, isoform 1, peptide C
Published: 2024-02-16

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51846

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

MEG 2.1, isoform 1, peptide C

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:

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).
PubMed: 37535563

Assembly members:

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

Natural source:

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

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: STPDLLLGNYQRHQR

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	26
15N chemical shifts	16
1H chemical shifts	101

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	MEG 2.1	1

Entities:

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

1

SER

THR

PRO

ASP

LEU

GLY

ASN

TYR

2

GLN

ARG

HIS

GLN

ARG

Samples:

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

sample_conditions_1: pressure: 1 atm; temperature: 300 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_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 peaks
SPARKY: Backbone or all simulated peaks