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Open data
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Basic information
| Entry | Database: PDB / ID: 6j11 | |||||||||
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| Title | MERS-CoV spike N-terminal domain and 7D10 scFv complex | |||||||||
Components |
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Keywords | VIRAL PROTEIN / MERS-CoV / Antibody | |||||||||
| Function / homology | Function and homology informationmembrane fusion / host cell endoplasmic reticulum-Golgi intermediate compartment membrane / positive regulation of viral entry into host cell / receptor-mediated virion attachment to host cell / 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 / host cell plasma membrane / virion membrane / membrane Similarity search - Function | |||||||||
| Biological species | ![]() ![]() | |||||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3 Å | |||||||||
Authors | Zhou, H. / Zhang, S. / Zhang, S. / Tang, W. / Wang, X. | |||||||||
| Funding support | China, 2items
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Citation | Journal: Nat Commun / Year: 2019Title: Structural definition of a neutralization epitope on the N-terminal domain of MERS-CoV spike glycoprotein. Authors: Zhou, H. / Chen, Y. / Zhang, S. / Niu, P. / Qin, K. / Jia, W. / Huang, B. / Zhang, S. / Lan, J. / Zhang, L. / Tan, W. / Wang, X. | |||||||||
| History |
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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 | 6j11.cif.gz | 711.9 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb6j11.ent.gz | 593.4 KB | Display | PDB format |
| PDBx/mmJSON format | 6j11.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 6j11_validation.pdf.gz | 5.1 MB | Display | wwPDB validaton report |
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| Full document | 6j11_full_validation.pdf.gz | 5.1 MB | Display | |
| Data in XML | 6j11_validation.xml.gz | 63.7 KB | Display | |
| Data in CIF | 6j11_validation.cif.gz | 85.8 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/j1/6j11 ftp://data.pdbj.org/pub/pdb/validation_reports/j1/6j11 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 5x4rS S: Starting model for refinement |
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| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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| 1 | ![]()
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| 2 | ![]()
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| 3 | ![]()
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| Unit cell |
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Components
-Protein , 1 types, 3 molecules ABC
| #1: Protein | Mass: 37724.180 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: Mammalian expression vector Flag-MCS-pcDNA3.1 (others) References: UniProt: A0A2D0YPK3, UniProt: K9N5Q8*PLUS |
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-Antibody , 2 types, 6 molecules HDFLEG
| #2: Antibody | Mass: 13812.137 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() #3: Antibody | Mass: 12200.607 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() |
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-Sugars , 6 types, 24 molecules 
| #4: Polysaccharide | Source method: isolated from a genetically manipulated source #5: Polysaccharide | alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1- ...alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | Source method: isolated from a genetically manipulated source #6: 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 #7: Polysaccharide | Source method: isolated from a genetically manipulated source #8: Polysaccharide | alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2- ...alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | Source method: isolated from a genetically manipulated source #9: Sugar | ChemComp-NAG / |
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-Details
| 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: 6.22 Å3/Da / Density % sol: 80.22 % |
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| Crystal grow | Temperature: 291.15 K / Method: vapor diffusion, sitting drop Details: 0.2 M potassium sodium tartrate, 0.1 M Sodium citrate pH 5.6, 2.0 M Ammonium sulfate and 10% (v/v) of the additive Acetonitrile (40% v/v) |
-Data collection
| Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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| Diffraction source | Source: SYNCHROTRON / Site: SSRF / Beamline: BL17U / Wavelength: 0.9796 Å |
| Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Mar 17, 2018 |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 0.9796 Å / Relative weight: 1 |
| Reflection | Resolution: 3→50 Å / Num. obs: 96015 / % possible obs: 99.9 % / Redundancy: 13.3 % / Net I/σ(I): 21.2 |
| Reflection shell | Resolution: 3→3.07 Å / Num. unique obs: 9478 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: 5x4r Resolution: 3→47.314 Å / SU ML: 0.37 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 21.48
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| Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement step | Cycle: LAST / Resolution: 3→47.314 Å
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| Refine LS restraints |
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| LS refinement shell |
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| Refinement TLS params. | Method: refined / Origin x: 21.0227 Å / Origin y: -15.4383 Å / Origin z: -30.4158 Å
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| Refinement TLS group | Selection details: all |
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X-RAY DIFFRACTION
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