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Open data
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Basic information
Entry | Database: PDB / ID: 1lcl | ||||||
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Title | CHARCOT-LEYDEN CRYSTAL PROTEIN | ||||||
![]() | LYSOPHOSPHOLIPASE![]() | ||||||
![]() | SERINE ESTERASE / CHARCOT-LEYDEN CRYSTAL PROTEIN | ||||||
Function / homology | ![]() regulation of activated T cell proliferation / regulation of T cell cytokine production / T cell apoptotic process / regulation of T cell anergy / cysteine-type endopeptidase activity involved in apoptotic process / ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Acharya, K.R. / Leonidas, D.D. | ||||||
![]() | ![]() Title: Crystal structure of human Charcot-Leyden crystal protein, an eosinophil lysophospholipase, identifies it as a new member of the carbohydrate-binding family of galectins. Authors: Leonidas, D.D. / Elbert, B.L. / Zhou, Z. / Leffler, H. / Ackerman, S.J. / Acharya, K.R. #1: ![]() Title: Molecular Cloning and Characterization of Human Eosinophil Charcot-Leyden Crystal Protein (Lysophospholipase). Similarities to Ige Binding Proteins and the S-Type Animal Lectin Superfamily Authors: Ackerman, S.J. / Corrette, S.E. / Rosenberg, H.F. / Bennett, J.C. / Mastrianni, D.M. / Nicholson-Weller, A. / Weller, P.F. / Chin, D.T. / Tenen, D.G. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 41.6 KB | Display | ![]() |
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PDB format | ![]() | 29.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Similar 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 on special symmetry positions |
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Components
#1: Protein | ![]() Mass: 16499.887 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() ![]() |
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#2: Water | ChemComp-HOH / ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.82 Å3/Da / Density % sol: 52 % | ||||||||||||||||||||
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Crystal grow![]() | pH: 7 / Details: pH 7.0 | ||||||||||||||||||||
Crystal | *PLUS | ||||||||||||||||||||
Crystal grow | *PLUS Temperature: 16 ℃ / pH: 10.5 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 289 K | |||||||||
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Diffraction source | Source: ![]() ![]() ![]() | |||||||||
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: 1994 | |||||||||
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||
Radiation wavelength |
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Reflection | Resolution: 1.8→40 Å / Num. obs: 18046 / % possible obs: 94.4 % / Observed criterion σ(I): -3 / Redundancy: 5.3 % / Rmerge(I) obs: 0.077 | |||||||||
Reflection | *PLUS Num. measured all: 75363 |
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Processing
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Refinement | Resolution: 1.8→8 Å / σ(F): 0
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Displacement parameters | Biso mean: 20.7 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→8 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.2 / Rfactor Rwork![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |