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- PDB-1o97: Structure of electron transferring flavoprotein from Methylophilu... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1o97 | ||||||
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Title | Structure of electron transferring flavoprotein from Methylophilus methylotrophus, recognition loop removed by limited proteolysis | ||||||
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Function / homology | ![]() fatty acid beta-oxidation using acyl-CoA dehydrogenase / amino acid catabolic process / ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Leys, D. / Basran, J. / Talfournier, F. / Sutcliffe, M.J. / Scrutton, N.S. | ||||||
![]() | ![]() Title: Extensive Conformational Sampling in a Ternary Electron Transfer Complex. Authors: Leys, D. / Basran, J. / Talfournier, F. / Sutcliffe, M.J. / Scrutton, N.S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 137.3 KB | Display | ![]() |
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PDB format | ![]() | 105.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related 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: 28929.850 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() ![]() ![]() |
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#2: Protein | Mass: 33622.945 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() ![]() ![]() |
#3: Chemical | ChemComp-AMP / ![]() |
#4: Chemical | ChemComp-FAD / ![]() |
#5: Water | ChemComp-HOH / ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.75 Å3/Da / Density % sol: 55.26 % | ||||||||||||||||||||||||
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Crystal grow![]() | pH: 6.5 / Details: 2.5 M POTASSIUM PHOSPHATE PH 6.3 | ||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Date: May 15, 2002 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 1.6→20 Å / Num. obs: 85935 / % possible obs: 96.3 % / Redundancy: 5.2 % / Rmerge(I) obs: 0.069 / Net I/σ(I): 16.1 |
Reflection shell | Resolution: 1.6→1.65 Å / Redundancy: 4.9 % / Rmerge(I) obs: 0.28 / Mean I/σ(I) obs: 2.7 / % possible all: 95.5 |
Reflection | *PLUS Lowest resolution: 20 Å / Num. measured all: 876371 |
Reflection shell | *PLUS Highest resolution: 1.6 Å / Lowest resolution: 1.63 Å / % possible obs: 95.5 % / Rmerge(I) obs: 0.285 |
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Processing
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Refinement | Method to determine structure![]() ![]() Details: DISORDERED REGIONS AND SIDECHAINS WERE NOT INCLUDED IN THE MODEL.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 25.11 Å2
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Refinement step | Cycle: LAST / Resolution: 1.6→19.92 Å
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Refine LS restraints |
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