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Open data
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Basic information
Entry | Database: PDB / ID: 1dfk | ||||||
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Title | NUCLEOTIDE-FREE SCALLOP MYOSIN S1-NEAR RIGOR STATE | ||||||
![]() | (MYOSIN HEAD) x 3 | ||||||
![]() | CONTRACTILE PROTEIN / MYOSIN MOTOR / CONFORMATIONAL CHANGES | ||||||
Function / homology | ![]() cytoskeletal motor regulator activity / mitotic actomyosin contractile ring / mitotic actomyosin contractile ring contraction / muscle myosin complex / myosin filament / actomyosin structure organization / locomotion / myosin II complex / microfilament motor activity / myofibril ...cytoskeletal motor regulator activity / mitotic actomyosin contractile ring / mitotic actomyosin contractile ring contraction / muscle myosin complex / myosin filament / actomyosin structure organization / locomotion / myosin II complex / microfilament motor activity / myofibril / sarcomere organization / myosin heavy chain binding / mitotic cytokinesis / post-embryonic development / muscle contraction / actin filament binding / calmodulin binding / calcium ion binding / ATP binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Houdusse, A. / Szent-Gyorgyi, A.G. / Cohen, C. | ||||||
![]() | ![]() Title: Three conformational states of scallop myosin S1. Authors: Houdusse, A. / Szent-Gyorgyi, A.G. / Cohen, C. #1: ![]() Title: Atomic structure of scallop myosin subfragment S1 complexed with MgADP: a novel conformation of the myosin head. Authors: Houdusse, A. / Kalabokis, V.N. / Himmel, D. / Szent-Gyorgyi, A.G. / Cohen, C. #2: ![]() Title: Structure of the regulatory domain of scallop myosin at 2 A resolution: implications for regulation. Authors: Houdusse, A. / Cohen, C. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 156.6 KB | Display | ![]() |
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PDB format | ![]() | 98.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 362.2 KB | Display | ![]() |
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Full document | ![]() | 376.5 KB | Display | |
Data in XML | ![]() | 18.2 KB | Display | |
Data in CIF | ![]() | 28.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Components
#1: Protein | Mass: 94696.711 Da / Num. of mol.: 1 / Fragment: HEAVY CHAIN / Source method: isolated from a natural source / Source: (natural) ![]() |
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#2: Protein | Mass: 15914.102 Da / Num. of mol.: 1 / Fragment: REGULATORY LIGHT CHAIN / Source method: isolated from a natural source / Source: (natural) ![]() |
#3: Protein | Mass: 17165.070 Da / Num. of mol.: 1 / Fragment: ESSENTIAL LIGHT CHAIN / Source method: isolated from a natural source / Source: (natural) ![]() |
#4: Chemical | ChemComp-CA / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.85 Å3/Da / Density % sol: 56.92 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 7 Details: PEG8000, ammonium sulfate, cacodylate, glycerol , pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 4K | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, sitting dropDetails: drop consists of equal amounts of protein and reservoir solutions | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction |
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Diffraction source | Source: ![]() ![]() ![]() | |||||||||
Detector |
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Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||
Radiation wavelength | Wavelength: 0.9 Å / Relative weight: 1 | |||||||||
Reflection | Resolution: 4.2→30 Å / Num. all: 10676 / Num. obs: 139608 / % possible obs: 97.9 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 1 / Biso Wilson estimate: 40 Å2 / Rmerge(I) obs: 0.063 / Net I/σ(I): 27 | |||||||||
Reflection shell | Resolution: 4.2→4.27 Å / Redundancy: 1.61 % / Rmerge(I) obs: 0.308 / Num. unique all: 461 / % possible all: 85.2 | |||||||||
Reflection | *PLUS Num. obs: 10676 / Num. measured all: 139608 | |||||||||
Reflection shell | *PLUS % possible obs: 85.2 % |
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Processing
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Refinement | Resolution: 4.2→20 Å / σ(F): 1 / σ(I): 1 Details: At this resolution, we performed only a rigid body refinement. No positional refinement was done.
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Refinement step | Cycle: LAST / Resolution: 4.2→20 Å
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Refine LS restraints |
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