+Open data
-Basic information
Entry | Database: PDB / ID: 2wso | ||||||
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Title | Structure of Cerulean Fluorescent Protein at physiological pH | ||||||
Components | GREEN FLUORESCENT PROTEIN | ||||||
Keywords | FLUORESCENT PROTEIN / CHROMOPHORE / LUMINESCENCE / PHOTOPROTEIN | ||||||
Function / homology | Function and homology information serine-type endopeptidase inhibitor activity / extracellular space / metal ion binding Similarity search - Function | ||||||
Biological species | AEQUOREA VICTORIA (jellyfish) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.15 Å | ||||||
Authors | Lelimousin, M. / Noirclerc-Savoye, M. / Lazareno-Saez, C. / Paetzold, B. / Le Vot, S. / Chazal, R. / Macheboeuf, P. / Field, M.J. / Bourgeois, D. / Royant, A. | ||||||
Citation | Journal: Biochemistry / Year: 2009 Title: Intrinsic Dynamics in Ecfp and Cerulean Control Fluorescence Quantum Yield. Authors: Lelimousin, M. / Noirclerc-Savoye, M. / Lazareno-Saez, C. / Paetzold, B. / Le Vot, S. / Chazal, R. / Macheboeuf, P. / Field, M.J. / Bourgeois, D. / Royant, A. #1: Journal: Biochemistry / Year: 2007 Title: X-Ray Structure of Cerulean Gfp: A Tryptophan-Based Chromophore Useful for Fluorescence Lifetime Imaging. Authors: Malo, G.D. / Pouwels, L.J. / Wang, M. / Weichsel, A. / Montfort, W.R. / Rizzo, M.A. / Piston, D.W. / Wachter, R.M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2wso.cif.gz | 118.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2wso.ent.gz | 92.1 KB | Display | PDB format |
PDBx/mmJSON format | 2wso.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2wso_validation.pdf.gz | 426.1 KB | Display | wwPDB validaton report |
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Full document | 2wso_full_validation.pdf.gz | 427.1 KB | Display | |
Data in XML | 2wso_validation.xml.gz | 13.7 KB | Display | |
Data in CIF | 2wso_validation.cif.gz | 20.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ws/2wso ftp://data.pdbj.org/pub/pdb/validation_reports/ws/2wso | HTTPS FTP |
-Related structure data
Related structure data | 2wsnC 1oxeS C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 26789.236 Da / Num. of mol.: 1 / Fragment: RESIDUES 2-238 Source method: isolated from a genetically manipulated source Details: CHROMOPHORE RESULTING FROM AUTOCATALYTIC CYCLIZATION OF CONSECUTIVE AMINO ACID RESIDUES THR65, TRP66 AND GLY67. Source: (gene. exp.) AEQUOREA VICTORIA (jellyfish) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 CODONPLUS(DE3) RIL / References: UniProt: P42212 |
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#2: Water | ChemComp-HOH / |
Sequence details | GFP VARIANT |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2 Å3/Da / Density % sol: 40 % / Description: NONE |
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Crystal grow | pH: 7 / Details: 15% PEG 8000, 0.1M MGCL2, 0.1 M HEPES PH 7.0 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 0.984 |
Detector | Type: ADSC CCD / Detector: CCD / Date: Mar 2, 2007 / Details: TOROIDAL MIRROR |
Radiation | Monochromator: SI311 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.984 Å / Relative weight: 1 |
Reflection | Resolution: 1.15→50 Å / Num. obs: 78022 / % possible obs: 97.7 % / Observed criterion σ(I): 2 / Redundancy: 3.6 % / Biso Wilson estimate: 13.7 Å2 / Rmerge(I) obs: 0.04 / Net I/σ(I): 20.4 |
Reflection shell | Resolution: 1.15→1.22 Å / Redundancy: 3.2 % / Rmerge(I) obs: 0.45 / Mean I/σ(I) obs: 2.8 / % possible all: 92.1 |
-Processing
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1OXE Resolution: 1.15→46.57 Å / Cor.coef. Fo:Fc: 0.973 / Cor.coef. Fo:Fc free: 0.965 / SU B: 1.167 / SU ML: 0.024 / Cross valid method: THROUGHOUT / ESU R: 0.034 / ESU R Free: 0.036 / Stereochemistry target values: MAXIMUM LIKELIHOOD 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 / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 9.1 Å2
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Refinement step | Cycle: LAST / Resolution: 1.15→46.57 Å
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