BMRB Entry 30100
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30100
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Title: The NMR structure of the m domain tri-helix bundle and C2 of human cardiac Myosin Binding Protein C PubMed: 27720588
Deposition date: 2016-05-25 Original release date: 2016-11-04
Authors: Michie, K.; Kwan, A.; Tung, C.; Guss, J.; Trewhella, J.
Citation: Michie, K.; Kwan, A.; Tung, C.; Guss, J.; Trewhella, J.. "A Highly Conserved Yet Flexible Linker Is Part of a Polymorphic Protein-Binding Domain in Myosin-Binding Protein C" Structure 24, 2000-2007 (2016).
Assembly members:
Myosin-binding protein C, cardiac-type, polymer, 137 residues, 15497.698 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):
Myosin-binding protein C, cardiac-type: GPGSEDVWEILRQAPPSEYE
RIAFQYGVTDLRGMLKRLKG
MRRDEKKSTAFQKKLEPAYQ
VSKGHKIRLTVELADHDAEV
KWLKNGQEIQMSGSKYIFES
IGAKRTLTISQCSLADDAAY
QCVVGGEKCSTELFVKE
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 582 |
| 15N chemical shifts | 147 |
| 1H chemical shifts | 972 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 137 residues - 15497.698 Da.
| 1 | GLY | PRO | GLY | SER | GLU | ASP | VAL | TRP | GLU | ILE | ||||
| 2 | LEU | ARG | GLN | ALA | PRO | PRO | SER | GLU | TYR | GLU | ||||
| 3 | ARG | ILE | ALA | PHE | GLN | TYR | GLY | VAL | THR | ASP | ||||
| 4 | LEU | ARG | GLY | MET | LEU | LYS | ARG | LEU | LYS | GLY | ||||
| 5 | MET | ARG | ARG | ASP | GLU | LYS | LYS | SER | THR | ALA | ||||
| 6 | PHE | GLN | LYS | LYS | LEU | GLU | PRO | ALA | TYR | GLN | ||||
| 7 | VAL | SER | LYS | GLY | HIS | LYS | ILE | ARG | LEU | THR | ||||
| 8 | VAL | GLU | LEU | ALA | ASP | HIS | ASP | ALA | GLU | VAL | ||||
| 9 | LYS | TRP | LEU | LYS | ASN | GLY | GLN | GLU | ILE | GLN | ||||
| 10 | MET | SER | GLY | SER | LYS | TYR | ILE | PHE | GLU | SER | ||||
| 11 | ILE | GLY | ALA | LYS | ARG | THR | LEU | THR | ILE | SER | ||||
| 12 | GLN | CYS | SER | LEU | ALA | ASP | ASP | ALA | ALA | TYR | ||||
| 13 | GLN | CYS | VAL | VAL | GLY | GLY | GLU | LYS | CYS | SER | ||||
| 14 | THR | GLU | LEU | PHE | VAL | LYS | GLU |
Samples:
sample_2: CaCl2 1 mM; DSS 10 mM; MES 10 mM; Na azide 1 mM; NaCl 50 mM; TCEP 2 mM; human cMyBP-C (319-451), [U-99% 13C; U-99% 15N], 412 uM; H2O 95%; D2O 5%
sample_3: CaCl2 1 mM; DSS 10 mM; MES 10 mM; Na azide 1 mM; NaCl 50 mM; TCEP 2 mM; human cMyBP-C (319-451), [U-99% 13C; U-99% 15N], 920 uM; H2O 95%; D2O 5%
sample_4: CaCl2 1 mM; DSS 10 mM; MES 10 mM; Na azide 1 mM; NaCl 50 mM; TCEP 2 mM; human cMyBP-C (319-451), [U-99% 13C; U-99% 15N], 550 uM; H2O 95%; D2O 5%
sample_5: CaCl2 1 mM; DSS 10 mM; MES 10 mM; Na azide 1 mM; NaCl 50 mM; TCEP 2 mM; human cMyBP-C (319-451), [U-99% 13C; U-99% 15N], 500 uM; H2O 1%; D2O 99%
sample_6: CaCl2 1 mM; DSS 10 mM; MES 10 mM; Na azide 1 mM; NaCl 50 mM; TCEP 2 mM; human cMyBP-C (319-451), [U-99% 13C; U-99% 15N], 800 uM; H2O 1%; D2O 99%
sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| HCC(CO)NH TOCSY | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 2D HBCBCGCDCEHE | sample_5 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_4 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_3 | isotropic | sample_conditions_1 |
| CC(CO)NH-TOCSY | sample_3 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_3 | isotropic | sample_conditions_1 |
| 3D 13C NOESY aromatic | sample_4 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_6 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_4 | isotropic | sample_conditions_1 |
| 3D 13C NOESY aliphatic | sample_5 | isotropic | sample_conditions_1 |
| 3D HCC TOCSY aromatic | sample_6 | isotropic | sample_conditions_1 |
| 2D HBCBCGCDHD | sample_5 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_3 | isotropic | sample_conditions_1 |
| 3D hCCH-TOCSY | sample_6 | isotropic | sample_conditions_1 |
| 3D HcCH-TOCSY | sample_4 | isotropic | sample_conditions_1 |
Software:
Analysis, CCPN - chemical shift assignment, peak picking
CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts