+Open data
-Basic information
Entry | Database: PDB / ID: 3evp | ||||||
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Title | crystal structure of circular-permutated EGFP | ||||||
Components | Green fluorescent protein,Green fluorescent protein | ||||||
Keywords | SIGNALING PROTEIN / circular-permutated / EGFP / Chromophore / Luminescence / Photoprotein | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Aequorea victoria (jellyfish) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.453 Å | ||||||
Authors | Wang, Q. / Shui, B. / Kotlikoff, M.I. / Sondermann, H. | ||||||
Citation | Journal: Structure / Year: 2008 Title: Structural Basis for Calcium Sensing by GCaMP2. Authors: Wang, Q. / Shui, B. / Kotlikoff, M.I. / Sondermann, H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3evp.cif.gz | 122.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3evp.ent.gz | 93.7 KB | Display | PDB format |
PDBx/mmJSON format | 3evp.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ev/3evp ftp://data.pdbj.org/pub/pdb/validation_reports/ev/3evp | 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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-Components
#1: Protein | Mass: 27348.896 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: protein contains the M13 fragment of myosin light chain kinase, circular permuted EGFP from Aequorea victoria (Jellyfish), calmodulin from Rattus norvegicus (Rat) Source: (gene. exp.) Aequorea victoria (jellyfish) / Gene: GFP / Plasmid: pET21 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P42212 |
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#2: Water | ChemComp-HOH / |
Sequence details | RESIDUE SER65 HAS BEEN MUTATED TO GLY. RESIDUES GLY65, TYR66, AND GLY67 CONSTITUTE THE CHROMOPHORE ...RESIDUE SER65 HAS BEEN MUTATED TO GLY. RESIDUES GLY65, TYR66, AND GLY67 CONSTITUTE |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 5 |
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-Sample preparation
Crystal | Density Matthews: 2.02 Å3/Da / Density % sol: 39.01 % |
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-Data collection
Diffraction source | Source: SYNCHROTRON / Site: CHESS / Beamline: A1 |
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Detector | Type: ADSC QUANTUM 210 / Detector: CCD / Date: Jul 14, 2007 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 1.45→50 Å / Num. obs: 39659 / Observed criterion σ(I): 9.9 / Redundancy: 7.6 % / Biso Wilson estimate: 13.4 Å2 / Rsym value: 0.042 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.453→41.138 Å / SU ML: 0.15 / σ(F): 0.21 / Phase error: 14.32 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 68.075 Å2 / ksol: 0.396 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.453→41.138 Å
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Refine LS restraints |
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LS refinement shell |
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