BMRB Entry 25010
Click here to enlarge.
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/BMR25010
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Structural Characterization of the Hypertrophic Cardiomyopathy-Related R502W Mutant of the C3 Domain of Cardiac Myosin Binding Protein-C PubMed: 25058872
Deposition date: 2014-06-12 Original release date: 2014-07-28
Authors: Zhang, Xiaolu Linda; De, Soumya; McIntosh, Lawrence; Paetzel, Mark
Citation: Zhang, Xiaolu Linda; De, Soumya; McIntosh, Lawrence; Paetzel, Mark. "Structural Characterization of the C3 Domain of Cardiac Myosin Binding Protein C and Its Hypertrophic Cardiomyopathy-Related R502W Mutant." Biochemistry 53, 5332-5342 (2014).
Assembly members:
entity, polymer, 95 residues, 10856.431 Da.
Natural source: Common Name: Humans Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: GSHMPVLITRPLEDQLVMVG
QRVEFECEVSEEGAQVKWLK
DGVELTREETFKYWFKKDGQ
RHHLIINEAMLEDAGHYALC
TSGGQALAELIVQEK
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 670 |
| 13C chemical shifts | 326 |
| 15N chemical shifts | 100 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 95 residues - 10856.431 Da.
| 1 | GLY | SER | HIS | MET | PRO | VAL | LEU | ILE | THR | ARG | ||||
| 2 | PRO | LEU | GLU | ASP | GLN | LEU | VAL | MET | VAL | GLY | ||||
| 3 | GLN | ARG | VAL | GLU | PHE | GLU | CYS | GLU | VAL | SER | ||||
| 4 | GLU | GLU | GLY | ALA | GLN | VAL | LYS | TRP | LEU | LYS | ||||
| 5 | ASP | GLY | VAL | GLU | LEU | THR | ARG | GLU | GLU | THR | ||||
| 6 | PHE | LYS | TYR | TRP | PHE | LYS | LYS | ASP | GLY | GLN | ||||
| 7 | ARG | HIS | HIS | LEU | ILE | ILE | ASN | GLU | ALA | MET | ||||
| 8 | LEU | GLU | ASP | ALA | GLY | HIS | TYR | ALA | LEU | CYS | ||||
| 9 | THR | SER | GLY | GLY | GLN | ALA | LEU | ALA | GLU | LEU | ||||
| 10 | ILE | VAL | GLN | GLU | LYS |
Samples:
sample_1: sodium phosphate 50 mM; sodium chloride 100 mM; entity, [U-100% 13C; U-100% 15N], 0.8 mM; H2O 90%; D2O 10%
sample_conditions_1: temperature: 298 K; pH: 6.5; pressure: 1 atm; ionic strength: 0.4 M
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - chemical shift assignment
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMR spectrometers:
- Bruker Avance 500 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