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Yorodumi- PDB-5jfb: Crystal structure of the scavenger receptor cysteine-rich domain ... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 5jfb | ||||||
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| Title | Crystal structure of the scavenger receptor cysteine-rich domain 5 (SRCR5) from porcine CD163 | ||||||
Components | Scavenger receptor cysteine-rich type 1 protein M130 | ||||||
Keywords | ENDOCYTOSIS / CD163 / SRCR / PRRSV | ||||||
| Function / homology | Function and homology informationacute-phase response / virus receptor activity / external side of plasma membrane / extracellular region Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å | ||||||
Authors | Ma, H. / Jiang, L. / Qiao, S. / Zhang, G. / Li, R. | ||||||
Citation | Journal: J. Virol. / Year: 2017Title: The Crystal Structure of the Fifth Scavenger Receptor Cysteine-Rich Domain of Porcine CD163 Reveals an Important Residue Involved in Porcine Reproductive and Respiratory Syndrome Virus Infection Authors: Ma, H. / Jiang, L. / Qiao, S. / Zhi, Y. / Chen, X.X. / Yang, Y. / Huang, X. / Huang, M. / Li, R. / Zhang, G.P. | ||||||
| History |
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 5jfb.cif.gz | 33 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb5jfb.ent.gz | 21.7 KB | Display | PDB format |
| PDBx/mmJSON format | 5jfb.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 5jfb_validation.pdf.gz | 424.3 KB | Display | wwPDB validaton report |
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| Full document | 5jfb_full_validation.pdf.gz | 424.3 KB | Display | |
| Data in XML | 5jfb_validation.xml.gz | 6.5 KB | Display | |
| Data in CIF | 5jfb_validation.cif.gz | 8.1 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jf/5jfb ftp://data.pdbj.org/pub/pdb/validation_reports/jf/5jfb | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 1by2S 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: 12083.336 Da / Num. of mol.: 1 / Fragment: SRCR 5 domain, UNP residues 477-577 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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| #2: Water | ChemComp-HOH / |
| Has protein modification | Y |
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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Sample preparation
| Crystal | Density Matthews: 1.99 Å3/Da / Density % sol: 38.16 % |
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| Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 4.6 Details: 25% (w/v) PEG 4000, 200mM (NH4)2SO4 in 100mM sodium acetate at pH 4.6 |
-Data collection
| Diffraction | Mean temperature: 100 K |
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| Diffraction source | Source: SYNCHROTRON / Site: SSRF / Beamline: BL19U1 / Wavelength: 0.979 Å |
| Detector | Type: Pilatus / Detector: CMOS / Date: Sep 14, 2015 |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 0.979 Å / Relative weight: 1 |
| Reflection | Resolution: 2→50 Å / Num. obs: 6682 / % possible obs: 97.1 % / Redundancy: 10 % / Rmerge(I) obs: 0.107 / Net I/σ(I): 17.7 |
| Reflection shell | Resolution: 2→2.07 Å |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: 1BY2 Resolution: 2→43.76 Å / Cor.coef. Fo:Fc: 0.936 / Cor.coef. Fo:Fc free: 0.927 / SU B: 4.562 / SU ML: 0.126 / Cross valid method: THROUGHOUT / ESU R: 0.221 / ESU R Free: 0.177 / 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: 23.6 Å2
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| Refinement step | Cycle: LAST / Resolution: 2→43.76 Å
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| Refine LS restraints |
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