+ Open data
Open data
- Basic information
Basic information
| Entry | Database: PDB / ID: 9w76 | |||||||||||||||||||||
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| Title | sarbecovirus Rc-o319 S-trimer in a locked-2 conformation | |||||||||||||||||||||
|  Components | Spike protein S1 | |||||||||||||||||||||
|  Keywords | VIRAL PROTEIN / spike protein / VIRUS | |||||||||||||||||||||
| Function / homology | BILIVERDINE IX ALPHA  Function and homology information | |||||||||||||||||||||
| Biological species |  Sarbecovirus | |||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.3 Å | |||||||||||||||||||||
|  Authors | Wang, J. / Li, Z.X. / Li, Z.M. / Huang, Y. / Xiong, X. | |||||||||||||||||||||
| Funding support |  China, 1items 
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|  Citation |  Journal: To Be Published Title: sarbecovirus Rc-o319 S-trimer in a locked-2 conformation Authors: Wang, J. / Li, Z. / Li, Z.M. / Yuan, H. / Xiong, X. | |||||||||||||||||||||
| History | 
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- Structure visualization
Structure visualization
| Structure viewer | Molecule:  Molmil  Jmol/JSmol | 
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- Downloads & links
Downloads & links
- Download
Download
| PDBx/mmCIF format |  9w76.cif.gz | 656.2 KB | Display |  PDBx/mmCIF format | 
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| PDB format |  pdb9w76.ent.gz | Display |  PDB format | |
| PDBx/mmJSON format |  9w76.json.gz | Tree view |  PDBx/mmJSON format | |
| Others |  Other downloads | 
-Validation report
| Summary document |  9w76_validation.pdf.gz | 3.1 MB | Display |  wwPDB validaton report | 
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| Full document |  9w76_full_validation.pdf.gz | 3.2 MB | Display | |
| Data in XML |  9w76_validation.xml.gz | 89 KB | Display | |
| Data in CIF |  9w76_validation.cif.gz | 136.2 KB | Display | |
| Arichive directory |  https://data.pdbj.org/pub/pdb/validation_reports/w7/9w76  ftp://data.pdbj.org/pub/pdb/validation_reports/w7/9w76 | HTTPS FTP | 
-Related structure data
| Related structure data |  65718MC 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 | 
- Links
Links
- Assembly
Assembly
| Deposited unit |  
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| 1 | 
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- Components
Components
| #1: Protein | Mass: 138931.375 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.)  Sarbecovirus / Strain: Rc-o319 / Production host:  Homo sapiens (human) #2: Polysaccharide | Source method: isolated from a genetically manipulated source #3: Polysaccharide | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source #4: Sugar | ChemComp-NAG / #5: Chemical | Has ligand of interest | Y | 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 | 
- Sample preparation
Sample preparation
| Component | Name: the spike protein of Rc-o319 / Type: ORGANELLE OR CELLULAR COMPONENT / Entity ID: #1 / Source: RECOMBINANT | 
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| Source (natural) | Organism:  Sarbecovirus / Strain: Rc-o319 | 
| Source (recombinant) | Organism:  Homo sapiens (human) | 
| Buffer solution | pH: 7.4 Details: 137 mM NaCl, 2.7 mM KCl, 10 mM Na2HPO4, and 1.8 mM KH2PO4. | 
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | 
| Vitrification | Cryogen name: ETHANE | 
- Electron microscopy imaging
Electron microscopy imaging
| Experimental equipment |  Model: Talos Arctica / Image courtesy: FEI Company | 
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| Microscopy | Model: FEI TALOS ARCTICA | 
| Electron gun | Electron source:  FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: OTHER | 
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2200 nm / Nominal defocus min: 800 nm / Cs: 2.7 mm | 
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) | 
- Processing
Processing
| EM software | 
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 2.3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 86709 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refinement | Highest resolution: 2.3 Å Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS) | ||||||||||||||||||||||||
| Refine LS restraints | 
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