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- PDB-2jt8: Solution structure of the F153-to-5-flurotryptophan mutant of hum... -
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Basic information
Entry | Database: PDB / ID: 2jt8 | |||||||||
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Title | Solution structure of the F153-to-5-flurotryptophan mutant of human cardiac troponin C | |||||||||
![]() | Troponin C, slow skeletal and cardiac muscles | |||||||||
![]() | STRUCTURAL PROTEIN / EF-hand protein / Calcium-bind protein / Phe-to-Trp mutation / Acetylation / Muscle protein / Polymorphism | |||||||||
Function / homology | ![]() 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 | ![]() | |||||||||
Method | SOLUTION NMR / simulated annealing | |||||||||
![]() | Wang, X. / Mercier, P. / Letourneau, P. / Sykes, B.D. | |||||||||
![]() | ![]() 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. | |||||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 486.8 KB | Display | ![]() |
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PDB format | ![]() | 411.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 471.8 KB | Display | ![]() |
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Full document | ![]() | 607.7 KB | Display | |
Data in XML | ![]() | 52.8 KB | Display | |
Data in CIF | ![]() | 52.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2jt0C ![]() 2jt3C ![]() 2jtzC C: citing same article ( |
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Similar structure data | |
Other databases |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 18444.379 Da / Num. of mol.: 1 / Mutation: F153(FTR), C35S, C84S Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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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 F153(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 |