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Open data
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Basic information
Entry | Database: PDB / ID: 2ec6 | ||||||
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Title | Placopecten Striated Muscle Myosin II | ||||||
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![]() | CONTRACTILE PROTEIN / muscle / rigor-like / actin binding | ||||||
Function / homology | ![]() cytoskeletal motor regulator activity / muscle myosin complex / actomyosin structure organization / locomotion / myosin complex / myosin II complex / myofibril / myosin heavy chain binding / cytoskeletal motor activity / mitotic cytokinesis ...cytoskeletal motor regulator activity / muscle myosin complex / actomyosin structure organization / locomotion / myosin complex / myosin II complex / myofibril / myosin heavy chain binding / cytoskeletal motor activity / mitotic cytokinesis / post-embryonic development / actin filament binding / calcium ion binding / ATP binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Yang, Y. / Brown, J. / Samudrala, G. / Reutzel, R. / Szent-Gyorgyi, A. | ||||||
![]() | ![]() Title: Rigor-like structures from muscle myosins reveal key mechanical elements in the transduction pathways of this allosteric motor. Authors: Yang, Y. / Gourinath, S. / Kovacs, M. / Nyitray, L. / Reutzel, R. / Himmel, D.M. / O'Neall-Hennessey, E. / Reshetnikova, L. / Szent-Gyorgyi, A.G. / Brown, J.H. / Cohen, C. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 230 KB | Display | ![]() |
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PDB format | ![]() | 177.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 462.8 KB | Display | ![]() |
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Full document | ![]() | 686.9 KB | Display | |
Data in XML | ![]() | 70.6 KB | Display | |
Data in CIF | ![]() | 93.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2os8C ![]() 2otgC ![]() 3i5fC ![]() 3i5gC ![]() 3i5hC ![]() 3i5iC C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 95832.875 Da / Num. of mol.: 1 / Fragment: residues 1-838 Source method: isolated from a genetically manipulated source Details: The source was obtained from the Marine Biological Laboratory (MBL) Source: (gene. exp.) ![]() |
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#2: Protein | Mass: 15354.388 Da / Num. of mol.: 1 / Fragment: residues 23-156 / Mutation: Y84F, T151A Source method: isolated from a genetically manipulated source Details: The source was obtained from the Marine Biological Laboratory (MBL) Source: (gene. exp.) ![]() |
#3: Protein | Mass: 17620.557 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: The source was obtained from the Marine Biological Laboratory (MBL) Source: (gene. exp.) ![]() |
#4: Chemical | ChemComp-CA / |
#5: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.56 Å3/Da / Density % sol: 52.04 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 90mM CaCl2, 8.5% PEG 6K, 100mM HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
-Data collection
Diffraction source | Source: ![]() ![]() ![]() |
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Detector | Type: ADSC QUANTUM 315 / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 3.25→20 Å / Num. all: 21051 / Num. obs: 18825 / % possible obs: 94.7 % / Observed criterion σ(F): 1.5 / Observed criterion σ(I): 2 / Redundancy: 2.8 % / Rmerge(I) obs: 0.073 / Net I/σ(I): 12.4 |
Reflection shell | Resolution: 3.25→20 Å / Redundancy: 2.6 % / Rmerge(I) obs: 0.458 / Mean I/σ(I) obs: 2 / Num. unique all: 1852 / Rsym value: 0.458 / % possible all: 87.8 |
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Processing
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Refinement | Method to determine structure: ![]()
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Displacement parameters | Biso mean: 39.7 Å2 | |||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.25→20 Å
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