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 15679

Title: 3D NMR structure of domain cC0 of cardiac myosin bonding protein C (MyBP-C)   PubMed: 21297165

Authors: Ratti, Joyce; Gautel, Mathias; Pfuhl, Mark

Citation: Ratti, Joyce; Rostkova, Elena; Gautel, Mathias; Pfuhl, Mark. "Structure and interactions of myosin-binding protein C domain C0: cardiac-specific regulation of myosin at its neck?"  J. Biol. Chem. 286, 12650-12658 (2011).

Assembly members:
cC0_MyBPC, polymer, 95 residues, 10045.401 Da.

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

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

Entity Sequences (FASTA):
cC0_MyBPC: PEPGKKPVSAFSKKPRSVEV AAGSPAVFEAETERAGVKVR WQRGGSDISASNKYGLATEG TRHTLTVREVGPADQGSYAV IAGSSKVKFDLKVIE

Data sets:
Data typeCount
13C chemical shifts281
15N chemical shifts85
1H chemical shifts601

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1cC0_MyBPC1

Entities:

Entity 1, cC0_MyBPC 95 residues - 10045.401 Da.

1   PROGLUPROGLYLYSLYSPROVALSERALA
2   PHESERLYSLYSPROARGSERVALGLUVAL
3   ALAALAGLYSERPROALAVALPHEGLUALA
4   GLUTHRGLUARGALAGLYVALLYSVALARG
5   TRPGLNARGGLYGLYSERASPILESERALA
6   SERASNLYSTYRGLYLEUALATHRGLUGLY
7   THRARGHISTHRLEUTHRVALARGGLUVAL
8   GLYPROALAASPGLNGLYSERTYRALAVAL
9   ILEALAGLYSERSERLYSVALLYSPHEASP
10   LEULYSVALILEGLU

Samples:

cC0_13C_15N: cC0_MyBPC, [U-95% 13C; U-95% 15N], 1-1.5 ± 0.2 mM; D2O, [U-2H], 55.5 M; sodium phosphate 40 mM; sodium chloride 50 mM; DTT 2 mM

cC0_15N: cC0_MyBPC, [U-95% 15N], 1-1.5 ± 0.2 mM; H2O 55.5 M; sodium phosphate 40 mM; sodium chloride 50 mM; DTT 2 mM

cC0: cC0_MyBPC 1-1.5 ± 0.2 mM; H2O 55.5 M; sodium phosphate 40 mM; sodium chloride 50 mM; DTT 2 mM

sample_conditions_1: ionic strength: 185 mM; pH: 7; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-13C NOESYcC0_13C_15Nisotropicsample_conditions_1
2D 1H-15N HSQCcC0_15Nisotropicsample_conditions_1
3D HNCACBcC0_13C_15Nisotropicsample_conditions_1
3D CBCA(CO)NHcC0_13C_15Nisotropicsample_conditions_1
3D HNCOcC0_13C_15Nisotropicsample_conditions_1
3D HN(CO)CAcC0_13C_15Nisotropicsample_conditions_1
2D 1H-1H NOESYcC0isotropicsample_conditions_1
2D 1H-13C HSQCcC0_13C_15Nisotropicsample_conditions_1
3D HCCH-TOCSYcC0_13C_15Nisotropicsample_conditions_1
3D 1H-15N NOESYcC0_15Nisotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

TALOS, Cornilescu, Delaglio and Bax - dihedral angles

ANALYSIS v1.0 release 15, Wim F. Vranken, Wayne Boucher, Tim J. Stevens, Rasmus H. Fogh - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
GB ACH92817