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Yorodumi- PDB-2jtz: Solution structure and chemical shift assignments of the F104-to-... -
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-Basic information
Entry | Database: PDB / ID: 2jtz | ||||||
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Title | Solution structure and chemical shift assignments of the F104-to-5-flurotryptophan mutant of cardiac troponin C | ||||||
Components | Troponin C, slow skeletal and cardiac muscles | ||||||
Keywords | CONTRACTILE PROTEIN / EF-hand protein / Calcium-binding protein / Phe-to-Trp mutation / Acetylation / Muscle protein / Polymorphism | ||||||
Function / homology | Function and homology information diaphragm contraction / regulation of ATP-dependent activity / regulation of muscle filament sliding speed / troponin T binding / cardiac Troponin complex / troponin complex / regulation of muscle contraction / transition between fast and slow fiber / Striated Muscle Contraction / response to metal ion ...diaphragm contraction / regulation of ATP-dependent activity / regulation of muscle filament sliding speed / troponin T binding / 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 / 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. / Mercier, P. / Letourneau, P. / Sykes, B.D. | ||||||
Citation | Journal: Protein Sci. / Year: 2005 Title: Effects of Phe-to-Trp mutation and fluorotryptophan incorporation on the solution structure of cardiac troponin C, and analysis of its suitability as a potential probe for in situ NMR studies Authors: Wang, X. / Mercier, P. / Letourneau, P. / Sykes, B. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2jtz.cif.gz | 492.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2jtz.ent.gz | 426.6 KB | Display | PDB format |
PDBx/mmJSON format | 2jtz.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jt/2jtz ftp://data.pdbj.org/pub/pdb/validation_reports/jt/2jtz | HTTPS FTP |
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-Related 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: 18444.377 Da / Num. of mol.: 1 / Mutation: F104(FTR), C35S, C84S Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: TNNC1, TNNC / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / Variant (production host): BL21(DE3)pLysS / References: UniProt: P63316 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 1.0 mM [U-100% 13C; U-100% 15N] F104(FTR), 10 mM Calcium, 100 mM potassium chloride, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 0.1 / pH: 6.7 / Pressure: ambient / Temperature: 303 K |
-NMR measurement
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | |||||||||||||||
NMR representative | Selection criteria: lowest energy | |||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 50 / Conformers submitted total number: 10 |