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Yorodumi- PDB-6yls: mEos4b - Directionality of Optical Properties of Fluorescent Proteins -
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Open data
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Basic information
| Entry | Database: PDB / ID: 6yls | |||||||||
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| Title | mEos4b - Directionality of Optical Properties of Fluorescent Proteins | |||||||||
Components | Green to red photoconvertible GFP-like protein EosFP | |||||||||
Keywords | FLUORESCENT PROTEIN / mEos4b | |||||||||
| Function / homology | Green fluorescent protein, GFP / Green fluorescent protein-related / Green fluorescent protein / Green fluorescent protein / bioluminescence / generation of precursor metabolites and energy / Green to red photoconvertible GFP-like protein EosFP Function and homology information | |||||||||
| Biological species | Lobophyllia hemprichii (invertebrata) | |||||||||
| Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.55 Å | |||||||||
Authors | Myskova, J. / Rybakova, O. / Brynda, J. / Lazar, J. | |||||||||
| Funding support | Czech Republic, 1items
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Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2020Title: Directionality of light absorption and emission in representative fluorescent proteins. Authors: Myskova, J. / Rybakova, O. / Brynda, J. / Khoroshyy, P. / Bondar, A. / Lazar, J. | |||||||||
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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 | 6yls.cif.gz | 67.8 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb6yls.ent.gz | 45.9 KB | Display | PDB format |
| PDBx/mmJSON format | 6yls.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 6yls_validation.pdf.gz | 437.3 KB | Display | wwPDB validaton report |
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| Full document | 6yls_full_validation.pdf.gz | 438.5 KB | Display | |
| Data in XML | 6yls_validation.xml.gz | 12.7 KB | Display | |
| Data in CIF | 6yls_validation.cif.gz | 18.3 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/yl/6yls ftp://data.pdbj.org/pub/pdb/validation_reports/yl/6yls | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 6ylmC ![]() 6ylnC ![]() 6yloC ![]() 6ylpC ![]() 6ylqC ![]() 3s05S ![]() 6yad C: citing same article ( 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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| Unit cell |
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Components
| #1: Protein | Mass: 26889.395 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Lobophyllia hemprichii (invertebrata) / Production host: ![]() |
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| #2: Chemical | ChemComp-CL / |
| #3: Chemical | ChemComp-NA / |
| #4: Water | ChemComp-HOH / |
| Has ligand of interest | Y |
| 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: 2.12 Å3/Da / Density % sol: 42.01 % Description: A - long axis of crystal B, C - diagonal to the faces of the crystal |
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| Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 5 / Details: PEG 6000, tri-sodium citrate |
-Data collection
| Diffraction | Mean temperature: 100 K / Serial crystal experiment: N | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Diffraction source | Source: ROTATING ANODE / Type: RIGAKU MICROMAX-007 HF / Wavelength: 1.54187 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Detector | Type: DECTRIS PILATUS 300K / Detector: PIXEL / Date: Nov 30, 2019 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Radiation wavelength | Wavelength: 1.54187 Å / Relative weight: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Reflection | Resolution: 1.55→35.44 Å / Num. obs: 61581 / % possible obs: 89 % / Redundancy: 2.456 % / Biso Wilson estimate: 20.974 Å2 / CC1/2: 0.997 / Rmerge(I) obs: 0.065 / Rrim(I) all: 0.076 / Χ2: 1.106 / Net I/σ(I): 9.15 / Num. measured all: 151232 / Scaling rejects: 461 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Reflection shell | Diffraction-ID: 1
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: 3s05 Resolution: 1.55→35.44 Å / Cor.coef. Fo:Fc: 0.956 / Cor.coef. Fo:Fc free: 0.921 / SU B: 2.275 / SU ML: 0.083 / SU R Cruickshank DPI: 0.0839 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.084 / ESU R Free: 0.084 Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
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| Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | Biso max: 193.88 Å2 / Biso mean: 21.084 Å2 / Biso min: 9.69 Å2
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| Refinement step | Cycle: final / Resolution: 1.55→35.44 Å
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| Refine LS restraints |
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| LS refinement shell | Resolution: 1.55→1.59 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
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Lobophyllia hemprichii (invertebrata)
X-RAY DIFFRACTION
Czech Republic, 1items
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