BMRB Entry 53320
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53320
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
All files associated with the entry
Citation: Iyer, Aishwarya; Wright, Nathan; Cook, Mary; Takagi, Yasuharu; Johnson, Bruce; Biancalana, Valerie; Massier, Marie; Spodenkiewicz, Marta; Poirsier, Celine; Vallecillo, Brice; Boyer, Frances; Pineau, Charlotte; Hensley, Lindsey; Sellers, James; Varney, Kristen; Weber, David; Kontrogianni-Konstantopoulos, Aikaterini. "Structural and biochemical alterations in the MYBPC1 M-domain underlie Myotrem pathogenicity" PNAS ., .-..
Assembly members:
entity_1, polymer, 106 residues, Formula weight is not available
entity_2, polymer, 133 residues, Formula weight is not available
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 Vector: pET-11a
| Data type | Count |
| 15N chemical shifts | 576 |
| 1H chemical shifts | 576 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | sMyBP-C LKR-mutant M-domain | 1 |
| 2 | myosin S2delta, chain 1 | 2 |
| 3 | myosin S2delta, chain 2 | 2 |
Entities:
Entity 1, sMyBP-C LKR-mutant M-domain 106 residues - Formula weight is not available
| 1 | MET | HIS | HIS | HIS | HIS | HIS | HIS | GLU | SER | THR | ||||
| 2 | GLY | THR | THR | PRO | ASN | ILE | ASP | ILE | ARG | SER | ||||
| 3 | ALA | PHE | LYS | ARG | SER | GLY | GLU | GLY | GLN | GLU | ||||
| 4 | ASP | ALA | GLY | GLU | LEU | ASP | PHE | SER | GLY | LEU | ||||
| 5 | LEU | LYS | ARG | ARG | GLU | VAL | LYS | GLN | GLN | GLU | ||||
| 6 | GLU | GLU | PRO | GLN | VAL | ASP | VAL | TRP | GLU | LEU | ||||
| 7 | LEU | LYS | ASN | ALA | LYS | PRO | SER | GLU | TYR | GLU | ||||
| 8 | LYS | ILE | ALA | PHE | GLN | TYR | GLY | ILE | THR | ASP | ||||
| 9 | LEU | ARG | GLY | MET | LEU | LYS | ARG | LEU | LYS | ARG | ||||
| 10 | LEU | LYS | ARG | MET | ARG | ARG | GLU | GLU | LYS | LYS | ||||
| 11 | SER | ALA | ALA | PHE | ALA | LYS |
Entity 2, myosin S2delta, chain 1 133 residues - Formula weight is not available
| 1 | MET | HIS | HIS | HIS | HIS | HIS | HIS | PRO | LEU | LEU | ||||
| 2 | LYS | SER | ALA | GLU | ARG | GLU | LYS | GLU | MET | ALA | ||||
| 3 | SER | MET | LYS | GLU | GLU | PHE | THR | ARG | LEU | LYS | ||||
| 4 | GLU | ALA | LEU | GLU | LYS | SER | GLU | ALA | ARG | ARG | ||||
| 5 | LYS | GLU | LEU | GLU | GLU | LYS | MET | VAL | SER | LEU | ||||
| 6 | LEU | GLN | GLU | LYS | ASN | ASP | LEU | GLN | LEU | GLN | ||||
| 7 | VAL | GLN | ALA | GLU | GLN | ASP | ASN | LEU | ALA | ASP | ||||
| 8 | ALA | GLU | GLU | ARG | CYS | ASP | GLN | LEU | ILE | LYS | ||||
| 9 | ASN | LYS | ILE | GLN | LEU | GLU | ALA | LYS | VAL | LYS | ||||
| 10 | GLU | MET | ASN | GLU | ARG | LEU | GLU | ASP | GLU | GLU | ||||
| 11 | GLU | MET | ASN | ALA | GLU | LEU | THR | ALA | LYS | LYS | ||||
| 12 | ARG | LYS | LEU | GLU | ASP | GLU | CYS | SER | GLU | LEU | ||||
| 13 | LYS | ARG | ASP | ILE | ASP | ASP | LEU | GLU | LEU | THR | ||||
| 14 | LEU | ALA | LYS |
Samples:
sample_1: sMyBP-C LKR-mutant M-domain, [U-15N], 0.1 mM; myosin S2delta 0 mM; HEPES 20 mM; NaCl 150 mM; TCEP 1 mM; EGTA 1 mM; NaN3 0.01%; D2O 10%
sample_2: sMyBP-C LKR-mutant M-domain, [U-15N], 0.1 mM; myosin S2delta 0.01 mM; HEPES 20 mM; NaCl 150 mM; TCEP 1 mM; EGTA 1 mM; NaN3 0.01%; D2O 10%
sample_3: sMyBP-C LKR-mutant M-domain, [U-15N], 0.1 mM; myosin S2delta 0.025 mM; HEPES 20 mM; NaCl 150 mM; TCEP 1 mM; EGTA 1 mM; NaN3 0.01%; D2O 10%
sample_4: sMyBP-C LKR-mutant M-domain, [U-15N], 0.1 mM; myosin S2delta 0.05 mM; HEPES 20 mM; NaCl 150 mM; TCEP 1 mM; EGTA 1 mM; NaN3 0.01%; D2O 10%
sample_5: sMyBP-C LKR-mutant M-domain, [U-15N], 0.1 mM; myosin S2delta 0.1 mM; HEPES 20 mM; NaCl 150 mM; TCEP 1 mM; EGTA 1 mM; NaN3 0.01%; D2O 10%
sample_6: sMyBP-C LKR-mutant M-domain, [U-15N], 0.1 mM; myosin S2delta 0.2 mM; HEPES 20 mM; NaCl 150 mM; TCEP 1 mM; EGTA 1 mM; NaN3 0.01%; D2O 10%
sample_conditions_1: ionic strength: 0.150 M; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_4 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_5 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_6 | isotropic | sample_conditions_1 |
Software:
NMRPipe - processing
CcpNMR - chemical shift assignment
NMR spectrometers:
- Bruker AVANCE III 950 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks