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Yorodumi- PDB-1ih0: Structure of the C-domain of Human Cardiac Troponin C in Complex ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1ih0 | ||||||
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Title | Structure of the C-domain of Human Cardiac Troponin C in Complex with Ca2+ Sensitizer EMD 57033 | ||||||
Components | TROPONIN C, SLOW SKELETAL AND CARDIAC MUSCLES | ||||||
Keywords | CONTRACTILE PROTEIN / Ca2+ binding protein / Ca2+ Sensitizer | ||||||
Function / homology | Function and homology information regulation of muscle filament sliding speed / troponin T binding / diaphragm contraction / regulation of ATP-dependent activity / cardiac Troponin complex / troponin complex / regulation of muscle contraction / transition between fast and slow fiber / Striated Muscle Contraction / response to metal ion ...regulation of muscle filament sliding speed / troponin T binding / diaphragm contraction / regulation of ATP-dependent activity / cardiac Troponin complex / troponin complex / regulation of muscle contraction / transition between fast and slow fiber / Striated Muscle Contraction / response to metal ion / ventricular cardiac muscle tissue morphogenesis / myosin II complex / troponin I binding / skeletal muscle contraction / cardiac muscle contraction / calcium-dependent protein binding / actin filament binding / calcium ion binding / protein homodimerization activity / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Wang, X. / Li, M.X. / Spyracopoulos, L. / Beier, N. / Chandra, M. / Solaro, R.J. / Sykes, B.D. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2001 Title: Structure of the C-domain of human cardiac troponin C in complex with the Ca2+ sensitizing drug EMD 57033. Authors: Wang, X. / Li, M.X. / Spyracopoulos, L. / Beier, N. / Chandra, M. / Solaro, R.J. / Sykes, B.D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ih0.cif.gz | 683.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ih0.ent.gz | 573.6 KB | Display | PDB format |
PDBx/mmJSON format | 1ih0.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1ih0_validation.pdf.gz | 439.1 KB | Display | wwPDB validaton report |
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Full document | 1ih0_full_validation.pdf.gz | 686.5 KB | Display | |
Data in XML | 1ih0_validation.xml.gz | 57.8 KB | Display | |
Data in CIF | 1ih0_validation.cif.gz | 83.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ih/1ih0 ftp://data.pdbj.org/pub/pdb/validation_reports/ih/1ih0 | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 8252.034 Da / Num. of mol.: 1 / Fragment: C-TERMINAL DOMAIN (RESIDUES 91-161) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: cTnC / Plasmid: pET3C / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)pLys / References: UniProt: P63316 | ||
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#2: Chemical | #3: Chemical | ChemComp-EMD / | |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: The structure of the protein was determined using multidimensional NMR spectroscopy. The structure of EMD 57033 in the complex was determined using 15N/13C-filtered-NOESY and DIPSI experiments. ...Text: The structure of the protein was determined using multidimensional NMR spectroscopy. The structure of EMD 57033 in the complex was determined using 15N/13C-filtered-NOESY and DIPSI experiments. The contacts between protein and EMD 57033 were determined using 15N/13C-filtered/edited experiments. |
-Sample preparation
Details | Contents: ~1mM C-domain of Cardiac Troponin C. 100mM KCl 10mM Imidazole 1mM DSS ~1mM EMD 57033 trace DMSO-d6 Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 0.1 / pH: 6.7 / Pressure: ambient / Temperature: 303 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | ||||||||||||||||||||
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Radiation wavelength | Relative weight: 1 | ||||||||||||||||||||
NMR spectrometer |
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-Processing
NMR software | Name: X-PLOR / Version: 3.851 / Developer: Brunger, A. / Classification: refinement |
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Refinement | Method: simulated annealing / Software ordinal: 1 Details: ~1000 NOE restraints were used. 61 dihedral restraints as well as 14 NOE restraints between drug and protein. |
NMR representative | Selection criteria: closest to the minimized average structure |
NMR ensemble | Conformer selection criteria: all calculated structures submitted Conformers calculated total number: 30 / Conformers submitted total number: 30 |