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Yorodumi- EMDB-35789: Cryo-EM structure of SARS-CoV-2 BA.4/5 spike protein in complex w... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-35789 | |||||||||
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Title | Cryo-EM structure of SARS-CoV-2 BA.4/5 spike protein in complex with 1G11 (state 2) | |||||||||
Map data | ||||||||||
Sample |
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Keywords | SARS-CoV-2 / Neutralizing antibody / Cryo-EM / VIRAL PROTEIN | |||||||||
Biological species | Severe acute respiratory syndrome coronavirus 2 / Homo sapiens (human) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.81 Å | |||||||||
Authors | Sun H / Jiang Y / Zheng Z / Zheng Q / Li S | |||||||||
Funding support | 1 items
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Citation | Journal: J Virol / Year: 2023 Title: Structural basis for broad neutralization of human antibody against Omicron sublineages and evasion by XBB variant. Authors: Hui Sun / Yizhen Wang / Xiuting Chen / Yanan Jiang / Siling Wang / Yang Huang / Liqin Liu / Yu Li / Miaolin Lan / Huilin Guo / Quan Yuan / Yali Zhang / Tingting Li / Hai Yu / Ying Gu / Jun ...Authors: Hui Sun / Yizhen Wang / Xiuting Chen / Yanan Jiang / Siling Wang / Yang Huang / Liqin Liu / Yu Li / Miaolin Lan / Huilin Guo / Quan Yuan / Yali Zhang / Tingting Li / Hai Yu / Ying Gu / Jun Zhang / Shaowei Li / Zizheng Zheng / Qingbing Zheng / Ningshao Xia / Abstract: The ongoing COVID-19 pandemic has been characterized by the emergence of new SARS-CoV-2 variants including the highly transmissible Omicron XBB sublineages, which have shown significant resistance to ...The ongoing COVID-19 pandemic has been characterized by the emergence of new SARS-CoV-2 variants including the highly transmissible Omicron XBB sublineages, which have shown significant resistance to neutralizing antibodies (nAbs). This resistance has led to decreased vaccine effectiveness and therefore result in breakthrough infections and reinfections, which continuously threaten public health. To date, almost all available therapeutic nAbs, including those authorized under Emergency Use Authorization nAbs that were previously clinically useful against early strains, have recently been found to be ineffective against newly emerging variants. In this study, we provide a comprehensive structural basis about how the Class 3 nAbs, including 1G11 in this study and noted LY-CoV1404, are evaded by the newly emerged SARS-CoV-2 variants. | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_35789.map.gz | 361.5 MB | EMDB map data format | |
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Header (meta data) | emd-35789-v30.xml emd-35789.xml | 13.8 KB 13.8 KB | Display Display | EMDB header |
Images | emd_35789.png | 32.7 KB | ||
Filedesc metadata | emd-35789.cif.gz | 3.9 KB | ||
Others | emd_35789_half_map_1.map.gz emd_35789_half_map_2.map.gz | 677.4 MB 677.4 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-35789 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-35789 | HTTPS FTP |
-Validation report
Summary document | emd_35789_validation.pdf.gz | 1 MB | Display | EMDB validaton report |
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Full document | emd_35789_full_validation.pdf.gz | 1 MB | Display | |
Data in XML | emd_35789_validation.xml.gz | 20.6 KB | Display | |
Data in CIF | emd_35789_validation.cif.gz | 24.4 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-35789 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-35789 | HTTPS FTP |
-Related structure data
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_35789.map.gz / Format: CCP4 / Size: 729 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.778 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #1
File | emd_35789_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_35789_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : SARS-CoV-2 BA.4/5 spike protein in complex with 1G11
Entire | Name: SARS-CoV-2 BA.4/5 spike protein in complex with 1G11 |
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Components |
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-Supramolecule #1: SARS-CoV-2 BA.4/5 spike protein in complex with 1G11
Supramolecule | Name: SARS-CoV-2 BA.4/5 spike protein in complex with 1G11 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#3 |
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-Supramolecule #2: SARS-CoV-2 BA.4/5 spike protein
Supramolecule | Name: SARS-CoV-2 BA.4/5 spike protein / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1 |
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Source (natural) | Organism: Severe acute respiratory syndrome coronavirus 2 |
-Supramolecule #3: nAb 1G11
Supramolecule | Name: nAb 1G11 / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #2-#3 |
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Source (natural) | Organism: Homo sapiens (human) |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.4 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TECNAI F30 |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 60.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.8 µm |
Experimental equipment | Model: Tecnai F30 / Image courtesy: FEI Company |
-Image processing
Startup model | Type of model: OTHER |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.81 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 144396 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |