BMRB Entry 53250
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53250
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
All files associated with the entry
Citation: Iyer, Aishwarya. "Structural and biochemical alterations in the MYBPC1 M-domain underlie Myotrem pathogenicity" PNAS ., .-..
Assembly members:
entity_1, polymer, 103 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
Entity Sequences (FASTA):
entity_1: MHHHHHHESTGTTPNIDIRS
AFKRSGEGQEDAGELDFSGL
LKRREVKQQEEEPQVDVWEL
LKNAKPSEYEKIAFQYGITD
LRGMLKRLKRMRREEKKSAA
FAK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 390 |
| 15N chemical shifts | 93 |
| 1H chemical shifts | 370 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | M-domain | 1 |
Entities:
Entity 1, M-domain 103 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 | MET | ARG | ARG | GLU | GLU | LYS | LYS | SER | ALA | ALA | ||||
| 11 | PHE | ALA | LYS |
Samples:
sample_1: sMyBP-C wild-type M-domain, [U-99% 13C; U-99% 15N], 0.5 mM; HEPES 20 mM; NaCl 50 mM; TCEP 1 mM; EGTA 1 mM; NaN3 0.01%
sample_conditions_1: ionic strength: 0.05 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 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe - processing
CcpNMR v3.0.4 - chemical shift assignment
NMR spectrometers:
- Bruker AVANCE III 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks