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Yorodumi- PDB-9fmw: Omicron BA.1 Spike protein with neutralizing NTD specific mAb K501SP6 -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9fmw | |||||||||||||||
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| Title | Omicron BA.1 Spike protein with neutralizing NTD specific mAb K501SP6 | |||||||||||||||
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Keywords | VIRAL PROTEIN / Neutralizing Antibody / Conserved Epitope / Covid-19 / Spike | |||||||||||||||
| Function / homology | Function and homology informationvirion component / symbiont-mediated disruption of host tissue / Maturation of spike protein / Translation of Structural Proteins / Virion Assembly and Release / host cell surface / viral translation / host extracellular space / symbiont-mediated-mediated suppression of host tetherin activity / Induction of Cell-Cell Fusion ...virion component / symbiont-mediated disruption of host tissue / Maturation of spike protein / Translation of Structural Proteins / Virion Assembly and Release / host cell surface / viral translation / host extracellular space / symbiont-mediated-mediated suppression of host tetherin activity / Induction of Cell-Cell Fusion / structural constituent of virion / membrane fusion / entry receptor-mediated virion attachment to host cell / Attachment and Entry / host cell endoplasmic reticulum-Golgi intermediate compartment membrane / positive regulation of viral entry into host cell / receptor-mediated virion attachment to host cell / host cell surface receptor binding / symbiont-mediated suppression of host innate immune response / receptor ligand activity / endocytosis involved in viral entry into host cell / fusion of virus membrane with host plasma membrane / fusion of virus membrane with host endosome membrane / viral envelope / symbiont entry into host cell / virion attachment to host cell / SARS-CoV-2 activates/modulates innate and adaptive immune responses / host cell plasma membrane / virion membrane / identical protein binding / membrane / plasma membrane Similarity search - Function | |||||||||||||||
| Biological species | ![]() Enterobacteria phage T4 (virus) Homo sapiens (human) | |||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.6 Å | |||||||||||||||
Authors | Bjoernsson, K.H. / Walker, M.R. / Raghavan, S.S.R. / Ward, A.B. / Barfod, L.K. | |||||||||||||||
| Funding support | Denmark, 1items
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Citation | Journal: To Be PublishedTitle: Omicron BA.1 Spike protein with neutralizing NTD specific mAb K501SP6 Authors: Bjoernsson, K.H. / Walker, M.R. / Raghavan, S.S.R. / Ward, A.B. / Barfod, L.K. | |||||||||||||||
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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 | 9fmw.cif.gz | 657.6 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9fmw.ent.gz | 532 KB | Display | PDB format |
| PDBx/mmJSON format | 9fmw.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fm/9fmw ftp://data.pdbj.org/pub/pdb/validation_reports/fm/9fmw | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 50574MC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
| #1: Protein | Mass: 141481.031 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Enterobacteria phage T4 (virus)Strain: BA.1 / Gene: S, 2, wac / Production host: Homo sapiens (human) / References: UniProt: P0DTC2, UniProt: P10104#2: Antibody | | Mass: 14387.906 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Homo sapiens (human)#3: Antibody | | Mass: 14002.314 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Homo sapiens (human)Has protein modification | Y | |
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-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
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| Molecular weight | Experimental value: NO | ||||||||||||||||||||||||||||
| Source (natural) |
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| Source (recombinant) |
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| Details of virus | Empty: NO / Enveloped: YES / Isolate: OTHER / Type: VIRION | ||||||||||||||||||||||||||||
| Natural host | Organism: Homo sapiens | ||||||||||||||||||||||||||||
| Buffer solution | pH: 7.5 / Details: TBS, pH 7.5 | ||||||||||||||||||||||||||||
| Specimen | Conc.: 1.2 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||||||
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277 K |
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Electron microscopy imaging
| Microscopy | Model: TFS GLACIOS |
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| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 195000 X / Nominal defocus max: 2000 nm / Nominal defocus min: 800 nm |
| Specimen holder | Cryogen: NITROGEN |
| Image recording | Electron dose: 60 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) |
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Processing
| EM software |
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||
| Particle selection | Num. of particles selected: 591736 | ||||||||||||||||
| 3D reconstruction | Resolution: 3.6 Å / Resolution method: FSC 0.5 CUT-OFF / Num. of particles: 87875 / Algorithm: FOURIER SPACE / Symmetry type: POINT |
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About Yorodumi




Homo sapiens (human)
Denmark, 1items
Citation



PDBj






FIELD EMISSION GUN