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Open data
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Basic information
Entry | Database: PDB / ID: 4oxf | ||||||
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Title | Structure of ECP in complex with citrate ions at 1.50 Angstroms | ||||||
![]() | Eosinophil cationic protein![]() | ||||||
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Function / homology | ![]() induction of bacterial agglutination / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Blanco, J.A. / Boix, E. / Moussaoui, M. / Salazar, V.A. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Structure of ECP in complex with citrate ions at 1.50 Angstroms Authors: Blanco, J.A. / Boix, E. / Moussaoui, M. / Salazar, V.A. #1: ![]() Title: Three-dimensional crystal structure of human eosinophil cationic protein (RNase 3) at 1.75 A resolution. Authors: Mallorqui-Fernandez, G. / Pous, J. / Peracaula, R. / Aymami, J. / Maeda, T. / Tada, H. / Yamada, H. / Seno, M. / de Llorens, R. / Gomis-Ruth, F.X. / Coll, M. #2: ![]() Title: The sulfate-binding site structure of the human eosinophil cationic protein as revealed by a new crystal form. Authors: Boix, E. / Pulido, D. / Moussaoui, M. / Nogues, M.V. / Russi, 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 | ![]() | 84 KB | Display | ![]() |
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PDB format | ![]() | 63.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | |
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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: 15730.072 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() References: UniProt: P12724, ![]() #2: Chemical | ChemComp-CIT / ![]() #3: Chemical | ![]() #4: Water | ChemComp-HOH / | ![]() Nonpolymer details | AUTHORS STATE THAT BOTH IRON AND CITRATE ATOMS HAVE BEEN ADJUSTED TO THE CORRESPONDING ELECTRON ...AUTHORS STATE THAT BOTH IRON AND CITRATE ATOMS HAVE BEEN ADJUSTED TO THE CORRESPOND | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.73 Å3/Da / Density % sol: 54.97 % |
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Crystal grow![]() | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 5.2 Details: Protein resuspended in sodium cacodylate buffer (20mM, pH5.0). 1 uL of protein sample was mixed with 1 uL of crystallisation buffer (0.1M sodium citrate pH5.2, 8% Jeffamine M-600, 10mM iron(III) chloride) PH range: 5.0 - 5.2 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jul 10, 2013 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 1.5→52.53 Å / Num. obs: 61922 / % possible obs: 99.3 % / Redundancy: 8.6 % / Rmerge(I) obs: 0.03 / Net I/σ(I): 32.3 |
Reflection shell | Resolution: 1.5→1.62 Å / Mean I/σ(I) obs: 3.8 / % possible all: 100 |
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Processing
Software | Name: PHENIX / Version: (phenix.refine: 1.8.4_1496) / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 1.5→50.882 Å / SU ML: 0.15 / σ(F): 1.35 / Phase error: 22.6 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.5→50.882 Å
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Refine LS restraints |
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LS refinement shell |
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