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Yorodumi- PDB-7sej: Structure-based design of prefusion-stabilized human metapneumovi... -
+Open data
-Basic information
Entry | Database: PDB / ID: 7sej | |||||||||
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Title | Structure-based design of prefusion-stabilized human metapneumovirus fusion proteins | |||||||||
Components |
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Keywords | VIRAL PROTEIN / human metapneumovirus / fusion protein | |||||||||
Function / homology | Precursor fusion glycoprotein F0, Paramyxoviridae / Fusion glycoprotein F0 / fusion of virus membrane with host plasma membrane / host cell plasma membrane / virion membrane / plasma membrane / Fusion glycoprotein F0 Function and homology information | |||||||||
Biological species | Human metapneumovirus | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.51 Å | |||||||||
Authors | Hsieh, C.-L. / Rush, S.A. / McLellan, J.S. | |||||||||
Funding support | United States, 2items
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Citation | Journal: Nat Commun / Year: 2022 Title: Structure-based design of prefusion-stabilized human metapneumovirus fusion proteins. Authors: Hsieh, C.L. / Rush, S.A. / Palomo, C. / Chou, C.W. / Pickens, W. / Mas, V. / McLellan, J.S. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 7sej.cif.gz | 199.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7sej.ent.gz | 141.3 KB | Display | PDB format |
PDBx/mmJSON format | 7sej.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 7sej_validation.pdf.gz | 489.2 KB | Display | wwPDB validaton report |
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Full document | 7sej_full_validation.pdf.gz | 497.4 KB | Display | |
Data in XML | 7sej_validation.xml.gz | 31.7 KB | Display | |
Data in CIF | 7sej_validation.cif.gz | 43.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/se/7sej ftp://data.pdbj.org/pub/pdb/validation_reports/se/7sej | HTTPS FTP |
-Related structure data
Related structure data | 7semC 5wb0S 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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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 11015.444 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Human metapneumovirus / Cell (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: H6X1Z0 #2: Protein | Mass: 49456.418 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: the protein is cleaved into the two subunits (entities 1 and 2) as it transported through ER-Golgi Source: (gene. exp.) Human metapneumovirus / Cell (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: H6X1Z0 #3: Sugar | ChemComp-NAG / #4: Water | ChemComp-HOH / | Has ligand of interest | N | Has protein modification | Y | |
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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: 2.43 Å3/Da / Density % sol: 49.49 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6 Details: 500 nl of hMPV F (10 mg/ml) with 500 nl of reservoir solution containing 0.1 M MES pH 6.0 and 12%(v/v) PEK 20k. |
-Data collection
Diffraction | Mean temperature: 80 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.9792 Å |
Detector | Type: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Nov 1, 2020 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9792 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→45.4 Å / Num. obs: 35650 / % possible obs: 97.6 % / Redundancy: 3.2 % / Biso Wilson estimate: 40.37 Å2 / CC1/2: 0.994 / Rmerge(I) obs: 0.078 / Rpim(I) all: 0.073 / Net I/σ(I): 8.3 |
Reflection shell | Resolution: 2.51→2.6 Å / Rmerge(I) obs: 0.038 / Mean I/σ(I) obs: 15.5 / Num. unique obs: 801 / CC1/2: 0.994 / Rpim(I) all: 0.037 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 5wb0 Resolution: 2.51→45.31 Å / SU ML: 0.3247 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 26.5753 Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 42.77 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.51→45.31 Å
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Refine LS restraints |
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LS refinement shell |
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