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Yorodumi- PDB-3cbe: Development of a family of redox-sensitive green fluorescent prot... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 3cbe | ||||||
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| Title | Development of a family of redox-sensitive green fluorescent protein indicators for use in relatively oxidizing subcellular environments | ||||||
Components | Green fluorescent protein | ||||||
Keywords | LUMINESCENT PROTEIN / GFP / redox | ||||||
| Function / homology | Function and homology information | ||||||
| Biological species | ![]() | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.488 Å | ||||||
Authors | Lohman, J.R. | ||||||
Citation | Journal: Biochemistry / Year: 2008Title: Development of a family of redox-sensitive green fluorescent protein indicators for use in relatively oxidizing subcellular environments Authors: Lohman, J.R. / Remington, S.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 | 3cbe.cif.gz | 112.1 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb3cbe.ent.gz | 85.4 KB | Display | PDB format |
| PDBx/mmJSON format | 3cbe.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 3cbe_validation.pdf.gz | 429.4 KB | Display | wwPDB validaton report |
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| Full document | 3cbe_full_validation.pdf.gz | 430.7 KB | Display | |
| Data in XML | 3cbe_validation.xml.gz | 13.1 KB | Display | |
| Data in CIF | 3cbe_validation.cif.gz | 19.5 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cb/3cbe ftp://data.pdbj.org/pub/pdb/validation_reports/cb/3cbe | HTTPS FTP |
-Related 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: 28136.545 Da / Num. of mol.: 1 Mutation: C48S,F64L,F99S,S147CR,H148S,M153T,V163A,I167T,Q204C Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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| #2: Chemical | ChemComp-MG / |
| #3: Water | ChemComp-HOH / |
| 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: 1.94 Å3/Da / Density % sol: 36.64 % |
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| Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: 0.1M tris, 22% PEG 1550, 0.02M magnesium chloride. After crystal formation TCEP added to 20mM., pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
| Diffraction | Mean temperature: 100 K |
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| Diffraction source | Source: SYNCHROTRON / Site: ALS / Beamline: 5.0.1 / Wavelength: 1 Å |
| Detector | Type: ADSC QUANTUM 210 / Detector: CCD / Date: Aug 11, 2007 |
| Radiation | Monochromator: Single crystal, cylindrically bent, Si(220) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
| Reflection | Resolution: 1.4→50 Å / Num. all: 41093 / Num. obs: 41093 / % possible obs: 93.3 % / Observed criterion σ(I): 2 |
| Reflection shell | Resolution: 1.4→1.45 Å / % possible all: 93.6 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.488→30 Å / Cor.coef. Fo:Fc: 0.967 / Cor.coef. Fo:Fc free: 0.962 / SU B: 2.997 / SU ML: 0.05 / Cross valid method: THROUGHOUT / σ(F): 2 / ESU R: 0.101 / ESU R Free: 0.075 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE 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 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | Biso mean: 11.465 Å2
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| Refinement step | Cycle: LAST / Resolution: 1.488→30 Å
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| Refine LS restraints |
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| LS refinement shell | Resolution: 1.488→1.527 Å / Total num. of bins used: 20
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