BMRB Entry 15679
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15679
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Title: 3D NMR structure of domain cC0 of cardiac myosin bonding protein C (MyBP-C) PubMed: 21297165
Deposition date: 2008-03-10 Original release date: 2009-10-13
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
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 281 |
| 15N chemical shifts | 85 |
| 1H chemical shifts | 601 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | cC0_MyBPC | 1 |
Entities:
Entity 1, cC0_MyBPC 95 residues - 10045.401 Da.
| 1 | PRO | GLU | PRO | GLY | LYS | LYS | PRO | VAL | SER | ALA | ||||
| 2 | PHE | SER | LYS | LYS | PRO | ARG | SER | VAL | GLU | VAL | ||||
| 3 | ALA | ALA | GLY | SER | PRO | ALA | VAL | PHE | GLU | ALA | ||||
| 4 | GLU | THR | GLU | ARG | ALA | GLY | VAL | LYS | VAL | ARG | ||||
| 5 | TRP | GLN | ARG | GLY | GLY | SER | ASP | ILE | SER | ALA | ||||
| 6 | SER | ASN | LYS | TYR | GLY | LEU | ALA | THR | GLU | GLY | ||||
| 7 | THR | ARG | HIS | THR | LEU | THR | VAL | ARG | GLU | VAL | ||||
| 8 | GLY | PRO | ALA | ASP | GLN | GLY | SER | TYR | ALA | VAL | ||||
| 9 | ILE | ALA | GLY | SER | SER | LYS | VAL | LYS | PHE | ASP | ||||
| 10 | LEU | LYS | VAL | ILE | GLU |
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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-13C NOESY | cC0_13C_15N | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | cC0_15N | isotropic | sample_conditions_1 |
| 3D HNCACB | cC0_13C_15N | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | cC0_13C_15N | isotropic | sample_conditions_1 |
| 3D HNCO | cC0_13C_15N | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | cC0_13C_15N | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | cC0 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | cC0_13C_15N | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | cC0_13C_15N | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | cC0_15N | isotropic | sample_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
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts