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Yorodumi- PDB-2c9i: Structure of the fluorescent protein asFP499 from Anemonia sulcata -
+Open data
-Basic information
Entry | Database: PDB / ID: 2c9i | |||||||||
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Title | Structure of the fluorescent protein asFP499 from Anemonia sulcata | |||||||||
Components | GREEN FLUORESCENT PROTEIN ASFP499 | |||||||||
Keywords | LUMINESCENT PROTEIN / FLUORESCENT PROTEIN / BETA-BARREL / BIOLUMINESCENCE / LUMINESCENCE | |||||||||
Function / homology | Green fluorescent protein-related / Green fluorescent protein / bioluminescence / Green Fluorescent Protein / Green fluorescent protein / Green fluorescent protein / Beta Barrel / Mainly Beta / Green fluorescent protein as(S)FP499 Function and homology information | |||||||||
Biological species | ANEMONIA SULCATA (snake-locks sea anemone) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.82 Å | |||||||||
Authors | Renzi, F. / Nienhaus, K. / Wiedenmann, J. / Vallone, B. / Nienhaus, G.U. | |||||||||
Citation | Journal: Biophys.J. / Year: 2006 Title: Chromophore-Protein Interactions in the Anthozoan Green Fluorescent Protein Asfp499 Authors: Nienhaus, K. / Renzi, F. / Vallone, B. / Wiedenmann, J. / Nienhaus, G.U. | |||||||||
History |
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Remark 700 | SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 14-STRANDED BARREL THIS IS REPRESENTED BY A 15-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "BA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 12-STRANDED BARREL THIS IS REPRESENTED BY A 13-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "CA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 12-STRANDED BARREL THIS IS REPRESENTED BY A 13-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "DA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 12-STRANDED BARREL THIS IS REPRESENTED BY A 13-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "EA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 12-STRANDED BARREL THIS IS REPRESENTED BY A 13-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "FA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 12-STRANDED BARREL THIS IS REPRESENTED BY A 13-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "GA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 12-STRANDED BARREL THIS IS REPRESENTED BY A 13-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "HA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 12-STRANDED BARREL THIS IS REPRESENTED BY A 13-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2c9i.cif.gz | 378.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2c9i.ent.gz | 311.9 KB | Display | PDB format |
PDBx/mmJSON format | 2c9i.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2c9i_validation.pdf.gz | 498.4 KB | Display | wwPDB validaton report |
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Full document | 2c9i_full_validation.pdf.gz | 533.1 KB | Display | |
Data in XML | 2c9i_validation.xml.gz | 85.6 KB | Display | |
Data in CIF | 2c9i_validation.cif.gz | 116.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/c9/2c9i ftp://data.pdbj.org/pub/pdb/validation_reports/c9/2c9i | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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-Components
#1: Protein | Mass: 25378.939 Da / Num. of mol.: 8 Source method: isolated from a genetically manipulated source Details: CHROMOPHORE\: AN IMIDAZOLINONE RING FROM THE CYCLIZATION BETWEEN GLN63 AND GLY65 AND COPLANAR TYR64 Source: (gene. exp.) ANEMONIA SULCATA (snake-locks sea anemone) Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q9GPI6 #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: 1.99 Å3/Da / Density % sol: 37.79 % / Description: 57 PERCENT SIMILARITY |
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Crystal grow | pH: 8.5 Details: 30 PERCENT PEG 4000, 0.1 M TRIS PH 8.5, 0.2 M MAGNESIUM CHLORIDE |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ELETTRA / Beamline: 5.2R / Wavelength: 1 |
Detector | Type: MARRESEARCH / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.85→30 Å / Num. obs: 128068 / % possible obs: 87.3 % / Observed criterion σ(I): 2 / Redundancy: 5.5 % / Rmerge(I) obs: 0.05 / Net I/σ(I): 17.5 |
Reflection shell | Highest resolution: 1.85 Å / Rmerge(I) obs: 0.19 / Mean I/σ(I) obs: 2 / % possible all: 81.4 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.82→50 Å / Cor.coef. Fo:Fc: 0.928 / Cor.coef. Fo:Fc free: 0.9 / SU B: 4.661 / SU ML: 0.143 / Cross valid method: THROUGHOUT / ESU R: 0.235 / ESU R Free: 0.199 / 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: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 23.37 Å2
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Refinement step | Cycle: LAST / Resolution: 1.82→50 Å
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Refine LS restraints |
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