+Open data
-Basic information
Entry | Database: PDB / ID: 2ptu | ||||||
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Title | Structure of NK cell receptor 2B4 (CD244) | ||||||
Components | Natural killer cell receptor 2B4CD244 | ||||||
Keywords | IMMUNE SYSTEM / 2B4 / CD244 / NK cell receptor | ||||||
Function / homology | Function and homology information positive regulation of granzyme B production / myeloid dendritic cell activation / natural killer cell activation involved in immune response / Cell surface interactions at the vascular wall / positive regulation of inositol phosphate biosynthetic process / positive regulation of natural killer cell proliferation / positive regulation of CD8-positive, alpha-beta T cell proliferation / MHC class I protein binding / positive regulation of interleukin-8 production / positive regulation of type II interferon production ...positive regulation of granzyme B production / myeloid dendritic cell activation / natural killer cell activation involved in immune response / Cell surface interactions at the vascular wall / positive regulation of inositol phosphate biosynthetic process / positive regulation of natural killer cell proliferation / positive regulation of CD8-positive, alpha-beta T cell proliferation / MHC class I protein binding / positive regulation of interleukin-8 production / positive regulation of type II interferon production / adaptive immune response / external side of plasma membrane / innate immune response Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.38 Å | ||||||
Authors | Deng, L. / Velikovsky, C.A. / Mariuzza, R.A. | ||||||
Citation | Journal: Immunity / Year: 2007 Title: Structure of natural killer receptor 2B4 bound to CD48 reveals basis for heterophilic recognition in signaling lymphocyte activation molecule family. Authors: Velikovsky, C.A. / Deng, L. / Chlewicki, L.K. / Fernandez, M.M. / Kumar, V. / Mariuzza, R.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2ptu.cif.gz | 94.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2ptu.ent.gz | 73.9 KB | Display | PDB format |
PDBx/mmJSON format | 2ptu.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/pt/2ptu ftp://data.pdbj.org/pub/pdb/validation_reports/pt/2ptu | HTTPS FTP |
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-Related structure data
Related structure data | 2pttSC 2ptvC S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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Unit cell |
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Details | The biological assembly is one of the monomers in the asymmetric unit. |
-Components
#1: Protein | Mass: 12526.927 Da / Num. of mol.: 4 / Fragment: Ig-like 1, D1, CD48-binding domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Strain: C57BL/6 / Gene: Cd244, 2b4, Nmrk / Plasmid: pT7.7 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21-CodonPlus(DE3)-RIL / References: UniProt: Q07763 #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 4.38 Å3/Da / Density % sol: 71.91 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: 2.0 M ammonium dihydrogen phosphate, 0.1 mM Tris-HCl, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X29A / Wavelength: 1 Å |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Nov 1, 2004 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.38→50 Å / Num. obs: 57316 / % possible obs: 85.1 % / Redundancy: 1.8 % / Biso Wilson estimate: 50.5 Å2 / Rmerge(I) obs: 0.03 / Net I/σ(I): 20.9 |
Reflection shell | Resolution: 2.38→2.47 Å / Redundancy: 1.6 % / Rmerge(I) obs: 0.14 / Mean I/σ(I) obs: 3.5 / Num. unique all: 4034 / % possible all: 60 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 2PTT Resolution: 2.38→50 Å / Cor.coef. Fo:Fc: 0.932 / Cor.coef. Fo:Fc free: 0.906 / SU B: 6.767 / SU ML: 0.161 / Cross valid method: THROUGHOUT / ESU R: 0.247 / ESU R Free: 0.222 / Stereochemistry target values: MAXIMUM LIKELIHOOD
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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: 47.35 Å2
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Refinement step | Cycle: LAST / Resolution: 2.38→50 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.381→2.443 Å / Total num. of bins used: 20
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