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Yorodumi- PDB-4uf7: Ghanaian henipavirus (Gh-M74a) attachment glycoprotein in complex... -
+Open data
-Basic information
Entry | Database: PDB / ID: 4uf7 | ||||||
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Title | Ghanaian henipavirus (Gh-M74a) attachment glycoprotein in complex with human ephrinB2 | ||||||
Components |
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Keywords | VIRAL PROTEIN/IMMUNE SYSTEM / VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX / GH-M74A / HENDRA VIRUS / NIPAH VIRUS / VIRAL ATTACHMENT / GLYCOPROTEIN / PARAMYXOVIRUS / GHV-G / NIV-G / HEV-G / HNV / HNV-G | ||||||
Function / homology | Function and homology information venous blood vessel morphogenesis / nephric duct morphogenesis / positive regulation of aorta morphogenesis / positive regulation of cardiac muscle cell differentiation / lymph vessel development / regulation of chemotaxis / cell migration involved in sprouting angiogenesis / regulation of postsynaptic neurotransmitter receptor internalization / adherens junction organization / EPH-Ephrin signaling ...venous blood vessel morphogenesis / nephric duct morphogenesis / positive regulation of aorta morphogenesis / positive regulation of cardiac muscle cell differentiation / lymph vessel development / regulation of chemotaxis / cell migration involved in sprouting angiogenesis / regulation of postsynaptic neurotransmitter receptor internalization / adherens junction organization / EPH-Ephrin signaling / Ephrin signaling / blood vessel morphogenesis / regulation of postsynaptic membrane neurotransmitter receptor levels / keratinocyte proliferation / EPH-ephrin mediated repulsion of cells / anatomical structure morphogenesis / negative regulation of keratinocyte proliferation / ephrin receptor signaling pathway / EPHB-mediated forward signaling / T cell costimulation / ephrin receptor binding / axon guidance / animal organ morphogenesis / postsynaptic density membrane / adherens junction / Schaffer collateral - CA1 synapse / virus receptor activity / cell-cell signaling / negative regulation of neuron projection development / presynaptic membrane / membrane => GO:0016020 / cell adhesion / host cell surface receptor binding / focal adhesion / viral envelope / glutamatergic synapse / positive regulation of cell population proliferation / virion attachment to host cell / virion membrane / plasma membrane Similarity search - Function | ||||||
Biological species | BAT PARAMYXOVIRUS EID_HEL/GH-M74A/GHA/2009 Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.7 Å | ||||||
Authors | Lee, B. / Pernet, O. / Ahmed, A.A. / Zeltina, A. / Beaty, S.M. / Bowden, T.A. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2015 Title: Molecular Recognition of Human Ephrinb2 Cell Surface Receptor by an Emergent African Henipavirus. Authors: Lee, B. / Pernet, O. / Ahmed, A.A. / Zeltina, A. / Beaty, S.M. / Bowden, T.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4uf7.cif.gz | 480.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4uf7.ent.gz | 396 KB | Display | PDB format |
PDBx/mmJSON format | 4uf7.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/uf/4uf7 ftp://data.pdbj.org/pub/pdb/validation_reports/uf/4uf7 | HTTPS FTP |
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-Related structure data
Related structure data | 2vsmS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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2 |
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Unit cell |
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-Components
-Protein , 2 types, 4 molecules ABCE
#1: Protein | Mass: 52333.727 Da / Num. of mol.: 2 Fragment: RECEPTOR-BINDING B-PROPELLER DOMAIN, RESIDUES 199-632 Source method: isolated from a genetically manipulated source Details: N-ACETYLGLUCOSAMINE LINKAGES OBSERVED IN STRUCTURE. ASN207, ASN255, ASN327, AND ASN396 Source: (gene. exp.) BAT PARAMYXOVIRUS EID_HEL/GH-M74A/GHA/2009 Description: SYNTHETICALLY OPTIMIZED CDNA / Plasmid: PHLSEC / Cell line (production host): HEK293T / Production host: Homo sapiens (human) / References: UniProt: I0E093 #2: Protein | Mass: 17506.854 Da / Num. of mol.: 2 / Fragment: RECEPTOR-BINDING DOMAIN, RESIDUES 27-167 Source method: isolated from a genetically manipulated source Details: N-ACETYLGLUCOSAMINE LINKAGES OBSERVED IN STRUCTURE. ASN39, ASN142 Source: (gene. exp.) Homo sapiens (human) / Plasmid: PHLSEC / Cell line (production host): HEK293T / Production host: Homo sapiens (human) / References: UniProt: P52799 |
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-Sugars , 1 types, 11 molecules
#6: Sugar | ChemComp-NAG / |
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-Non-polymers , 4 types, 1042 molecules
#3: Chemical | ChemComp-SO4 / #4: Chemical | ChemComp-ACT / #5: Chemical | #7: 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: 3.1 Å3/Da / Density % sol: 60.7 % / Description: NONE |
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Crystal grow | pH: 5.5 Details: 12% PEG 4000, 0.1 M SODIUM ACETATE PH 5.5, 0.1 M LISO4, AND 0.1 M NACL |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: Diamond / Beamline: I04 / Wavelength: 0.97949 |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jun 24, 2013 / Details: MIRRORS |
Radiation | Monochromator: SINGLE BOUNCE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97949 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→100 Å / Num. obs: 172833 / % possible obs: 99.8 % / Observed criterion σ(I): -3 / Redundancy: 4.9 % / Rmerge(I) obs: 0.04 / Net I/σ(I): 18.2 |
Reflection shell | Resolution: 1.7→1.74 Å / Redundancy: 4.8 % / Rmerge(I) obs: 0.88 / Mean I/σ(I) obs: 1.8 / % possible all: 99.3 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 2VSM Resolution: 1.7→111.47 Å / Cor.coef. Fo:Fc: 0.969 / Cor.coef. Fo:Fc free: 0.96 / SU B: 4.068 / SU ML: 0.067 / Cross valid method: THROUGHOUT / ESU R: 0.088 / ESU R Free: 0.087 / 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: 34.222 Å2
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Refinement step | Cycle: LAST / Resolution: 1.7→111.47 Å
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Refine LS restraints |
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