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Yorodumi- PDB-11yo: Single-conformation model re-refinement of 2F/S3-rich PSII interm... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 11yo | ||||||
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| Title | Single-conformation model re-refinement of 2F/S3-rich PSII intermediate structure at 2.09 Angstrom resolution | ||||||
Components |
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Keywords | PHOTOSYNTHESIS / Model bias Model anti-bias single-conformation model refinement CaMn4O5 composition | ||||||
| Function / homology | Function and homology informationphotosystem II oxygen evolving complex / photosystem II assembly / oxygen evolving activity / photosystem II stabilization / photosystem II reaction center / photosystem II / oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor / photosynthetic electron transport chain / response to herbicide / photosystem II ...photosystem II oxygen evolving complex / photosystem II assembly / oxygen evolving activity / photosystem II stabilization / photosystem II reaction center / photosystem II / oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor / photosynthetic electron transport chain / response to herbicide / photosystem II / extrinsic component of membrane / plasma membrane-derived thylakoid membrane / photosynthetic electron transport in photosystem II / chlorophyll binding / phosphate ion binding / photosynthesis, light reaction / photosynthesis / respiratory electron transport chain / manganese ion binding / electron transfer activity / protein stabilization / iron ion binding / heme binding / metal ion binding Similarity search - Function | ||||||
| Biological species | ![]() Thermosynechococcus vestitus BP-1 (bacteria) | ||||||
| Method | X-RAY DIFFRACTION / FREE ELECTRON LASER / MOLECULAR REPLACEMENT / Resolution: 2.09 Å | ||||||
Authors | Wang, J. / Armstrong, W.H. / Batista, V.S. | ||||||
| Funding support | 1items
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Citation | Journal: Proc. Natl. Acad. Sci. U.S.A. / Year: 2021Title: Do crystallographic XFEL data support binding of a water molecule to the oxygen-evolving complex of photosystem II exposed to two flashes of light? Authors: Wang, J. / Armstrong, W.H. / Batista, V.S. | ||||||
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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 | 11yo.cif.gz | 1.3 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb11yo.ent.gz | 1.1 MB | Display | PDB format |
| PDBx/mmJSON format | 11yo.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/1y/11yo ftp://data.pdbj.org/pub/pdb/validation_reports/1y/11yo | HTTPS FTP |
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-Related structure data
| Related structure data | |
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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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| 1 |
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| Unit cell |
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Components
-Photosystem II ... , 17 types, 34 molecules AaBbCcDdHhIiJjKkLlMmOoRrTtUuXx...
| #1: Protein | Mass: 38265.625 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() Thermosynechococcus vestitus BP-1 (bacteria)References: UniProt: P0A444, photosystem II #2: Protein | Mass: 56656.457 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() Thermosynechococcus vestitus BP-1 (bacteria)References: UniProt: Q8DIQ1 #3: Protein | Mass: 50287.500 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() Thermosynechococcus vestitus BP-1 (bacteria)References: UniProt: Q8DIF8 #4: Protein | Mass: 39388.156 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() Thermosynechococcus vestitus BP-1 (bacteria)References: UniProt: Q8CM25, photosystem II #7: Protein | Mass: 7358.754 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() Thermosynechococcus vestitus BP-1 (bacteria)References: UniProt: Q8DJ43 #8: Protein/peptide | Mass: 4438.255 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() Thermosynechococcus vestitus BP-1 (bacteria)References: UniProt: Q8DJZ6 #9: Protein/peptide | Mass: 4105.908 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() Thermosynechococcus vestitus BP-1 (bacteria)References: UniProt: P59087 #10: Protein/peptide | Mass: 5028.083 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() Thermosynechococcus vestitus BP-1 (bacteria)References: UniProt: Q9F1K9 #11: Protein/peptide | Mass: 4299.044 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() Thermosynechococcus vestitus BP-1 (bacteria)References: UniProt: Q8DIN8 #12: Protein/peptide | Mass: 4009.682 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() Thermosynechococcus vestitus BP-1 (bacteria)References: UniProt: Q8DHA7 #13: Protein | Mass: 29637.443 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() Thermosynechococcus vestitus BP-1 (bacteria)References: UniProt: P0A431 #14: Protein/peptide | Mass: 4590.648 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() Thermosynechococcus vestitus BP-1 (bacteria)References: UniProt: Q8DKM3 #15: Protein/peptide | Mass: 3906.738 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() Thermosynechococcus vestitus BP-1 (bacteria)References: UniProt: Q8DIQ0 #16: Protein | Mass: 15030.986 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() Thermosynechococcus vestitus BP-1 (bacteria)References: UniProt: Q9F1L5 #18: Protein/peptide | Mass: 4322.226 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() Thermosynechococcus vestitus BP-1 (bacteria)References: UniProt: Q9F1R6 #19: Protein/peptide | Mass: 5039.143 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() Thermosynechococcus vestitus BP-1 (bacteria)References: UniProt: Q8DJI1 #20: Protein | Mass: 6766.187 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() Thermosynechococcus vestitus BP-1 (bacteria)References: UniProt: Q8DHJ2 |
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-Cytochrome b559 subunit ... , 2 types, 4 molecules EeFf
| #5: Protein | Mass: 9580.840 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() Thermosynechococcus vestitus BP-1 (bacteria)References: UniProt: Q8DIP0 #6: Protein/peptide | Mass: 5067.900 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() Thermosynechococcus vestitus BP-1 (bacteria)References: UniProt: Q8DIN9 |
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-Protein / Sugars , 2 types, 11 molecules Vv

| #17: Protein | Mass: 18046.943 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() Thermosynechococcus vestitus BP-1 (bacteria)References: UniProt: P0A386 #27: Sugar | ChemComp-DGD / |
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-Non-polymers , 14 types, 2177 molecules 


























| #21: Chemical | | #22: Chemical | ChemComp-CLA / #23: Chemical | ChemComp-BCR / #24: Chemical | ChemComp-CL / #25: Chemical | ChemComp-PL9 / #26: Chemical | ChemComp-SQD / #28: Chemical | ChemComp-STE / #29: Chemical | #30: Chemical | ChemComp-LMG / #31: Chemical | ChemComp-LHG / #32: Chemical | #33: Chemical | ChemComp-PHO / #34: Chemical | ChemComp-HEC / #35: Water | ChemComp-HOH / | |
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-Details
| Has ligand of interest | N |
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| Has protein modification | Y |
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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Sample preparation
| Crystal | Density Matthews: 3.16 Å3/Da / Density % sol: 61.05 % |
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| Crystal grow | Temperature: 298 K / Method: batch mode / Details: 0.1 M MES pH 6.5, 0.1 M NH4Cl, 35% (w/v) PEG 5000 |
-Data collection
| Diffraction | Mean temperature: 298 K / Serial crystal experiment: Y |
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| Diffraction source | Source: FREE ELECTRON LASER / Site: SLAC LCLS / Beamline: MFX / Wavelength: 1.30192 Å |
| Detector | Type: RAYONIX MX340-HS / Detector: CCD / Date: Nov 28, 2019 |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 1.30192 Å / Relative weight: 1 |
| Reflection | Resolution: 2.09→33.65 Å / Num. obs: 468019 / % possible obs: 99.8 % / Redundancy: 81 % / CC1/2: 0.99 / Net I/σ(I): 12.8 |
| Reflection shell | Resolution: 2.09→2.13 Å / Num. unique obs: 23274 / CC1/2: 0.05 |
| Serial crystallography sample delivery | Method: injection |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.09→33.65 Å / Cor.coef. Fo:Fc: 0.96 / Cor.coef. Fo:Fc free: 0.938 / Cross valid method: FREE R-VALUE / ESU R: 0.193 / ESU R Free: 0.18 Details: Hydrogens have been added in their riding positions
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| Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK BULK SOLVENT | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | Biso mean: 40.956 Å2
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| Refinement step | Cycle: LAST / Resolution: 2.09→33.65 Å
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| Refine LS restraints |
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| LS refinement shell |
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Thermosynechococcus vestitus BP-1 (bacteria)
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