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Open data
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Basic information
Entry | Database: PDB / ID: 6fsb | ||||||
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Title | Influenza B/Memphis/13/03 endonuclease with I38T mutation | ||||||
![]() | Polymerase acidic protein | ||||||
![]() | VIRAL PROTEIN / Influenza polymerase / endonuclease | ||||||
Function / homology | ![]() cap snatching / symbiont-mediated suppression of host mRNA transcription via inhibition of RNA polymerase II activity / endonuclease activity / host cell cytoplasm / Hydrolases; Acting on ester bonds / viral RNA genome replication / DNA-templated transcription / host cell nucleus / RNA binding / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Cusack, S. / Speranzini, V. | ||||||
![]() | ![]() Title: Characterization of influenza virus variants induced by treatment with the endonuclease inhibitor baloxavir marboxil. Authors: Omoto, S. / Speranzini, V. / Hashimoto, T. / Noshi, T. / Yamaguchi, H. / Kawai, M. / Kawaguchi, K. / Uehara, T. / Shishido, T. / Naito, A. / Cusack, S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 98.9 KB | Display | ![]() |
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PDB format | ![]() | 75 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 436.1 KB | Display | ![]() |
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Full document | ![]() | 436.8 KB | Display | |
Data in XML | ![]() | 16.7 KB | Display | |
Data in CIF | ![]() | 23.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6fs6C ![]() 6fs7C ![]() 6fs8C ![]() 6fs9C ![]() 5fmlS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 23506.596 Da / Num. of mol.: 2 / Mutation: I38T Source method: isolated from a genetically manipulated source Details: N-terminal GAMGSGMA linkerI38T mutation / Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q5V8Z9, Hydrolases; Acting on ester bonds #2: Chemical | #3: Chemical | ChemComp-MG / | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.29 Å3/Da / Density % sol: 46.26 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop Details: Protein, at 15-17 mg/ml, was incubated with 10-fold molar excess of BXA for 30 min at RT, mixtures were centrifuged at RT for 5 minutes at 12000 g, and soluble fraction was used for ...Details: Protein, at 15-17 mg/ml, was incubated with 10-fold molar excess of BXA for 30 min at RT, mixtures were centrifuged at RT for 5 minutes at 12000 g, and soluble fraction was used for crystallization trials (final protein concentration 8-10 mg/ml). Mother liquor was |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS3 2M / Detector: PIXEL / Date: Oct 4, 2017 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.966 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→50 Å / Num. obs: 39336 / % possible obs: 91.3 % / Redundancy: 1.7 % / CC1/2: 0.996 / Rsym value: 0.055 / Net I/σ(I): 7.55 |
Reflection shell | Resolution: 1.8→1.85 Å / Redundancy: 1.7 % / Mean I/σ(I) obs: 1.17 / Num. unique obs: 5269 / CC1/2: 0.596 / Rsym value: 0.58 / % possible all: 92.4 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 5FML Resolution: 1.8→46.104 Å / SU ML: 0.27 / Cross valid method: FREE R-VALUE / σ(F): 1.37 / Phase error: 26.69
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→46.104 Å
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Refine LS restraints |
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LS refinement shell |
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