+Open data
-Basic information
Entry | Database: PDB / ID: 2a52 | ||||||
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Title | fluorescent protein asFP595, S158V, on-state | ||||||
Components |
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Keywords | LUMINESCENT PROTEIN / asCP / fluorescent protein / chromoprotein / photochromic protein / reversible photoswitch | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Anemonia sulcata (snake-locks sea anemone) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.7 Å | ||||||
Authors | Andresen, M. / Wahl, M.C. / Stiel, A.C. / Graeter, F. / Schaefer, L. / Trowitzsch, S. / Weber, G. / Eggeling, C. / Grubmueller, H. / Hell, S.W. / Jakobs, S. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.Usa / Year: 2005 Title: Structure and mechanism of the reversible photoswitch of a fluorescent protein Authors: Andresen, M. / Wahl, M.C. / Stiel, A.C. / Graeter, F. / Schaefer, L. / Trowitzsch, S. / Weber, G. / Eggeling, C. / Grubmueller, H. / Hell, S.W. / Jakobs, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2a52.cif.gz | 112 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2a52.ent.gz | 91.7 KB | Display | PDB format |
PDBx/mmJSON format | 2a52.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/a5/2a52 ftp://data.pdbj.org/pub/pdb/validation_reports/a5/2a52 | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Details | The tetramer (biological assembly) is generated by the crystallographic twofold axis -x,y,-z+1/2 and translation by one unit cell length along x (alternative by the equivalent axis parallel to y located at 1/2x, 1/4z) |
-Components
#1: Protein | Mass: 8067.181 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Anemonia sulcata (snake-locks sea anemone) Plasmid: pQE30 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21CodonPlus / References: UniProt: Q9GZ28 #2: Protein | Mass: 19169.779 Da / Num. of mol.: 2 / Mutation: S158V Source method: isolated from a genetically manipulated source Source: (gene. exp.) Anemonia sulcata (snake-locks sea anemone) Plasmid: pQE30 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21CodonPlus / References: UniProt: Q9GZ28 #3: Water | ChemComp-HOH / | Sequence details | SEQUENCE RESIDUES MET 63, TYR 64 AND GLY 65 AUTOCATALYTICALLY FORM THE CHROMOPHORE NRQ LABELLED AS ...SEQUENCE RESIDUES MET 63, TYR 64 AND GLY 65 AUTOCATALY | |
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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: 2.1 Å3/Da / Density % sol: 40.4 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7.1 Details: PEG 3350, NaCl, pH 7.1, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: ENRAF-NONIUS FR591 / Wavelength: 1.5418 Å |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jun 9, 2004 |
Radiation | Monochromator: Mirrors / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→30 Å / Num. all: 48516 / Num. obs: 48031 / % possible obs: 99 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 |
Reflection shell | Resolution: 1.7→1.75 Å / % possible all: 98 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.7→20 Å / Cor.coef. Fo:Fc: 0.96 / Cor.coef. Fo:Fc free: 0.945 / SU B: 2.59 / SU ML: 0.083 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.12 / ESU R Free: 0.117 / 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: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 14.856 Å2
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Refinement step | Cycle: LAST / Resolution: 1.7→20 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.7→1.744 Å / Total num. of bins used: 20 /
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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