BMRB Entry 31260

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31260
MolProbity Validation Chart

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NMR-STAR v3 text file.
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Title:
NMR structure of slow skeletal Myosin Binding Protein-C M-domain tri-helix bundle
Deposition date:
2025-07-04
Original release date:
2026-05-07
Authors:
Iyer, A.; Wright, N.; Kontrogianni-Konstantopoulos, A.
Citation:

Citation: Iyer, A.; Wright, N.; Cook, M.; Takagi, Y.; Johnson, B.; Biancalana, V.; Massier, M.; Spodenkiewicz, M.; Poirsier, C.; Vallecillo, B.; Boyer, F.; Pineau, C.; Hensley, L.; Sellers, J.; Varney, K.; Weber, D.; Kontrigianni-Konstantopoulos, A.. "Structural and biochemical alterations in the MYBPC1 M-domain underlie Myotrem pathogenicity"  .

Assembly members:

Assembly members:
entity_1, polymer, 45 residues, 5507.521 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MPQVDVWELLKNAKPSEYEK IAFQYGITDLRGMLKRLKRM RREEK

Data sets:
Data typeCount
13C chemical shifts113
15N chemical shifts37
1H chemical shifts240

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 45 residues - 5507.521 Da.

1   METPROGLNVALASPVALTRPGLULEULEU
2   LYSASNALALYSPROSERGLUTYRGLULYS
3   ILEALAPHEGLNTYRGLYILETHRASPLEU
4   ARGGLYMETLEULYSARGLEULYSARGMET
5   ARGARGGLUGLULYS

Samples:

sample_1: M-domain tri-helix bundle of slow skeletal MyBP-C, [U-15N], 2 mM; TRIS, d-11, 20 mM; sodium chloride 50 mM; sodium azide 350 uM; D2O 10%

sample_2: M-domain tri-helix bundle of slow skeletal MyBP-C, [U-13C; U-15N], 2 mM; TRIS, d-11, 20 mM; sodium chloride 50 mM; sodium azide 350 uM; D20 10%

sample_conditions_1: ionic strength: 70 mM; pH: 7.5; pressure: 1 atm; temperature: 289 K

sample_conditions_2: ionic strength: 70 mM; pH: 7.5; pressure: 1 atm; temperature: 289 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_2
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_2

Software:

NMRFAM-SPARKY, Lee, Tonelli, and Markley - peak picking

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE 600 MHz

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