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Yorodumi- PDB-6ogc: Crystal structure of Green Fluorescent Protein (GFP); S65T, Y66(2... -
+Open data
-Basic information
Entry | Database: PDB / ID: 6ogc | ||||||
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Title | Crystal structure of Green Fluorescent Protein (GFP); S65T, Y66(2,3-F2Y), H148D; circular permutant (50-51) | ||||||
Components | Crystal structure of Green Fluorescent Protein (GFP); S65T, Y66(2,3-F2Y), H148D; circular permutant (50-51) | ||||||
Keywords | FLUORESCENT PROTEIN / GFP | ||||||
Function / homology | Green fluorescent protein, GFP / Green fluorescent protein-related / Green fluorescent protein / Green fluorescent protein / bioluminescence / generation of precursor metabolites and energy / Green fluorescent protein Function and homology information | ||||||
Biological species | Aequorea victoria (jellyfish) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.178 Å | ||||||
Authors | Lin, C.-Y. / Boxer, S.G. | ||||||
Funding support | United States, 1items
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Citation | Journal: J.Phys.Chem.B / Year: 2020 Title: Unusual Spectroscopic and Electric Field Sensitivity of Chromophores with Short Hydrogen Bonds: GFP and PYP as Model Systems. Authors: Lin, C.Y. / Boxer, S.G. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6ogc.cif.gz | 220 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6ogc.ent.gz | 175 KB | Display | PDB format |
PDBx/mmJSON format | 6ogc.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/og/6ogc ftp://data.pdbj.org/pub/pdb/validation_reports/og/6ogc | HTTPS FTP |
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-Related structure data
Related structure data | 6og8C 6og9C 6ogaC 6ogbC 6un5C 6un6C 6un7C 4zf3S S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 28096.254 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Aequorea victoria (jellyfish) / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P42212*PLUS #2: Water | ChemComp-HOH / | |
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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: 1.92 Å3/Da / Density % sol: 35.98 % |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 5 Details: 50 mM sodium acetate, pH 5.0, 100 mM NaCl, 7-8% PEG 3350 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: SSRL / Beamline: BL9-2 / Wavelength: 0.9795 Å |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Nov 21, 2017 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9795 Å / Relative weight: 1 |
Reflection | Resolution: 1.178→36.5 Å / Num. obs: 134742 / % possible obs: 95 % / Redundancy: 13.1 % / Biso Wilson estimate: 9.91 Å2 / CC1/2: 1 / Rmerge(I) obs: 0.04828 / Rpim(I) all: 0.01365 / Rrim(I) all: 0.05023 / Net I/σ(I): 29.19 |
Reflection shell | Resolution: 1.178→1.221 Å / Redundancy: 10.5 % / Rmerge(I) obs: 0.5514 / Mean I/σ(I) obs: 3.65 / Num. unique obs: 11199 / CC1/2: 0.905 / Rpim(I) all: 0.1726 / Rrim(I) all: 0.5796 / % possible all: 80.44 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 4zf3 Resolution: 1.178→36.5 Å / SU ML: 0.09 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 15.48
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.178→36.5 Å
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Refine LS restraints |
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LS refinement shell |
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