+Open data
-Basic information
Entry | Database: PDB / ID: 8fmn | ||||||
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Title | Complex structure of K210 deletion Troponin complex | ||||||
Components |
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Keywords | STRUCTURAL PROTEIN / Ca sensing complex / troponin complex / K210 deletion | ||||||
Function / homology | Function and homology information regulation of systemic arterial blood pressure by ischemic conditions / troponin C binding / regulation of muscle filament sliding speed / troponin T binding / diaphragm contraction / regulation of ATP-dependent activity / cardiac Troponin complex / cardiac myofibril / troponin complex / transition between fast and slow fiber ...regulation of systemic arterial blood pressure by ischemic conditions / troponin C binding / regulation of muscle filament sliding speed / troponin T binding / diaphragm contraction / regulation of ATP-dependent activity / cardiac Troponin complex / cardiac myofibril / troponin complex / transition between fast and slow fiber / regulation of smooth muscle contraction / regulation of muscle contraction / muscle filament sliding / negative regulation of ATP-dependent activity / regulation of cardiac muscle contraction by calcium ion signaling / positive regulation of ATP-dependent activity / Striated Muscle Contraction / response to metal ion / ventricular cardiac muscle tissue morphogenesis / sarcomere organization / regulation of heart contraction / tropomyosin binding / heart contraction / troponin I binding / striated muscle thin filament / skeletal muscle contraction / vasculogenesis / calcium channel inhibitor activity / Ion homeostasis / cardiac muscle contraction / sarcomere / intracellular calcium ion homeostasis / response to calcium ion / calcium-dependent protein binding / actin filament binding / heart development / actin binding / protein domain specific binding / calcium ion binding / protein kinase binding / protein homodimerization activity / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.101 Å | ||||||
Authors | Wang, P. / Ahmed, M. / Sadek, H. | ||||||
Funding support | United States, 1items
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Citation | Journal: To Be Published Title: Structural and Phenotypic Correction of K210del Genetic Cardiomyopathy by an FDA Approved drug Authors: Wang, P. / Ahmed, M. / Sadek, H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8fmn.cif.gz | 149 KB | Display | PDBx/mmCIF format |
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PDB format | pdb8fmn.ent.gz | 114.6 KB | Display | PDB format |
PDBx/mmJSON format | 8fmn.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 8fmn_validation.pdf.gz | 1.9 MB | Display | wwPDB validaton report |
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Full document | 8fmn_full_validation.pdf.gz | 1.9 MB | Display | |
Data in XML | 8fmn_validation.xml.gz | 23.4 KB | Display | |
Data in CIF | 8fmn_validation.cif.gz | 31.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fm/8fmn ftp://data.pdbj.org/pub/pdb/validation_reports/fm/8fmn | HTTPS FTP |
-Related structure data
Related structure data | 8fmmC 8fmoC 8fmpC 8fmqC 8fmrC 8fmsC 8fmtC C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 18673.635 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: TNNC1, TNNC / Production host: Escherichia coli (E. coli) / References: UniProt: P63316 #2: Protein | Mass: 12971.820 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: TNNT2 / Production host: Escherichia coli (E. coli) / References: UniProt: P45379 #3: Protein | Mass: 15405.877 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: TNNI3, TNNC1 / Production host: Escherichia coli (E. coli) / References: UniProt: P19429 #4: Chemical | ChemComp-CA / Has ligand of interest | Y | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.68 Å3/Da / Density % sol: 54.16 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / Details: 0.2M sodium acetate, 20% PEG3350 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.97973 Å |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Aug 20, 2019 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97973 Å / Relative weight: 1 |
Reflection | Resolution: 3.1→50 Å / Num. obs: 15584 / % possible obs: 94.2 % / Redundancy: 4.7 % / Rmerge(I) obs: 0.076 / Net I/σ(I): 17.7 |
Reflection shell | Resolution: 3.1→3.21 Å / Rmerge(I) obs: 0.458 / Mean I/σ(I) obs: 2.7 / Num. unique obs: 1342 |
-Processing
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 3.101→43.612 Å / SU ML: 0.44 / Cross valid method: THROUGHOUT / σ(F): 1.36 / Phase error: 29.1 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.101→43.612 Å
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Refine LS restraints |
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LS refinement shell |
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