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Open data
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Basic information
Entry | Database: PDB / ID: 7ptd | ||||||
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Title | PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C MUTANT R163K | ||||||
![]() | PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C![]() | ||||||
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Function / homology | ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Heinz, D.W. | ||||||
![]() | ![]() Title: Probing the roles of active site residues in phosphatidylinositol-specific phospholipase C from Bacillus cereus by site-directed mutagenesis. Authors: Gassler, C.S. / Ryan, M. / Liu, T. / Griffith, O.H. / Heinz, D.W. #1: ![]() Title: Crystal Structure of the Phosphatidylinositol-Specific Phospholipase C from Bacillus Cereus in Complex with Myo-Inositol Authors: Heinz, D.W. / Ryan, M. / Bullock, T.L. / Griffith, O.H. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 72.6 KB | Display | ![]() |
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PDB format | ![]() | 54.9 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: 34540.648 Da / Num. of mol.: 1 / Mutation: R163K Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() |
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#2: Water | ChemComp-HOH / ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.4 Å3/Da / Density % sol: 45 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow![]() | pH: 7.5 / Details: pH 7.5 | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Wavelength: 1.5418 |
Detector | Type: XENTRONICS / Detector: AREA DETECTOR / Date: Oct 13, 1996 / Details: COLLIMATOR |
Radiation | Monochromator: NI FILTER / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 2.52→18.7 Å / Num. obs: 9137 / % possible obs: 76.3 % / Observed criterion σ(I): 0 / Redundancy: 1.96 % / Biso Wilson estimate: 20.2 Å2 / Rmerge(I) obs: 0.073 / Rsym value: 0.08 / Net I/σ(I): 9.9 |
Reflection shell | Resolution: 2.52→2.6 Å / Redundancy: 1.3 % / Rmerge(I) obs: 0.179 / Mean I/σ(I) obs: 3.7 / Rsym value: 0.202 / % possible all: 26.2 |
Reflection | *PLUS Num. measured all: 17915 |
Reflection shell | *PLUS % possible obs: 26.2 % |
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Processing
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Refinement | Method to determine structure![]()
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Displacement parameters | Biso mean: 22.7 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.6→18.7 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.6→2.72 Å / Rfactor Rfree error: 0.06 / Total num. of bins used: 8
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor obs: 0.262 |