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- PDB-4phn: The Structural Basis of Differential Inhibition of Human Calpain ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4phn | |||||||||
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Title | The Structural Basis of Differential Inhibition of Human Calpain by Indole and Phenyl alpha-Mercaptoacrylic Acids | |||||||||
![]() | Calpain small subunit 1![]() | |||||||||
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Function / homology | ![]() Degradation of the extracellular matrix / ![]() ![]() ![]() ![]() ![]() Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Allemann, R.K. / Rizkallah, P.J. / Adams, S.E. / Miller, D.J. / Hallett, M.B. | |||||||||
Funding support | ![]()
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![]() | ![]() Title: The structural basis of differential inhibition of human calpain by indole and phenyl alpha-mercaptoacrylic acids. Authors: Adams, S.E. / Rizkallah, P.J. / Miller, D.J. / Robinson, E.J. / Hallett, M.B. / Allemann, R.K. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 163.5 KB | Display | ![]() |
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PDB format | ![]() | 126.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 4phjC ![]() 4phkC ![]() 4phmC ![]() 1alvS C: citing same article ( S: Starting model for refinement |
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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: 19883.477 Da / Num. of mol.: 2 / Fragment: PEF(S) domain VI, residues 94-266 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() #2: Chemical | ChemComp-CA / #3: Water | ChemComp-HOH / | ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.44 Å3/Da / Density % sol: 49.6 % |
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Crystal grow![]() | Temperature: 293 K / Method: vapor diffusion, sitting drop Details: PROTEIN WAS CRYSTALLIZED FROM 12% PEG6000, 20 MM CACL2, 50 MM CACODYLATE BUFFER, PH7.4 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 2M / Detector: PIXEL / Date: Mar 17, 2013 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 1.79→39.05 Å / Num. all: 35505 / Num. obs: 35505 / % possible obs: 98.4 % / Redundancy: 3.7 % / Rmerge(I) obs: 0.041 / Net I/σ(I): 16.6 |
Reflection shell | Resolution: 1.79→1.84 Å / Redundancy: 3.9 % / Rmerge(I) obs: 0.622 / Mean I/σ(I) obs: 2.1 / % possible all: 99.9 |
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Processing
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Refinement | Method to determine structure![]() ![]() Starting model: 1ALV Resolution: 1.79→39.05 Å / Cor.coef. Fo:Fc: 0.963 / Cor.coef. Fo:Fc free: 0.945 / SU B: 6.773 / SU ML: 0.106 / Cross valid method: THROUGHOUT / ESU R: 0.128 / ESU R Free: 0.127 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 31.919 Å2
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Refinement step | Cycle: LAST / Resolution: 1.79→39.05 Å
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Refine LS restraints |
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