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Open data
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Basic information
Entry | Database: PDB / ID: 3fpr | ||||||
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Title | Crystal Structure of Evasin-1 | ||||||
![]() | Evasin-1 | ||||||
![]() | IMMUNE SYSTEM / novel fold / Glycoprotein / Secreted | ||||||
Function / homology | ![]() negative regulation of chemokine activity / chemokine binding / C-C chemokine binding / extracellular region Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Dias, J.M. / Shaw, J.P. | ||||||
![]() | ![]() Title: Structural basis of chemokine sequestration by a tick chemokine binding protein: the crystal structure of the complex between Evasin-1 and CCL3 Authors: Dias, J.M. / Losberger, C. / Deruaz, M. / Power, C.A. / Proudfoot, A.E.I. / Shaw, J.P. #1: Journal: J.Biol.Chem. / Year: 2007 Title: Molecular cloning and characterization of a highly selective chemokine-binding protein from the tick Rhipicephalus sanguineus. Authors: Frauenschuh, A. / Power, C.A. / Deruaz, M. / Ferreira, B.R. / Silva, J.S. / Teixeira, M.M. / Dias, J.M. / Martin, T. / Wells, T.N.C. / Proudfoot, A.E.I. #2: Journal: J.Exp.Med. / Year: 2008 Title: Ticks produce highly selective chemokine binding proteins with antiinflammatory activity Authors: Deruaz, M. / Frauenschuh, A. / Alessandri, A.L. / Dias, J.M. / Coelho, F.M. / Russo, R.C. / Ferreira, B.R. / Graham, G.J. / Shaw, J.P. / Wells, T.N.C. / Teixeira, M.M. / Power, C.A. / Proudfoot, A.E.I. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 43.8 KB | Display | ![]() |
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PDB format | ![]() | 34.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 436.5 KB | Display | ![]() |
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Full document | ![]() | 438.1 KB | Display | |
Data in XML | ![]() | 10.6 KB | Display | |
Data in CIF | ![]() | 14.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 11306.446 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Plasmid: pFASTBAC / Production host: ![]() ![]() #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.01 Å3/Da / Density % sol: 38.9 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 3% (w/v) PEG 4000, 200mM Ammonium Sulfate, 10% (v/v) MPD, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MAR CCD 165 mm / Detector: CCD / Date: Aug 18, 2005 |
Radiation | Monochromator: SAGITALLY FOCUSED Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.6→39.6 Å / Num. obs: 23281 / % possible obs: 93.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 7.4 % / Rsym value: 0.065 / Net I/σ(I): 15.4 |
Reflection shell | Resolution: 1.6→1.8 Å / Mean I/σ(I) obs: 3.3 / Rsym value: 0.341 / % possible all: 65.3 |
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Processing
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Refinement | Method to determine structure: ![]()
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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: 30.206 Å2
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Refinement step | Cycle: LAST / Resolution: 1.63→25.73 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.63→1.672 Å / Total num. of bins used: 20
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