+Open data
-Basic information
Entry | Database: PDB / ID: 1b9c | ||||||
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Title | Green Fluorescent Protein Mutant F99S, M153T and V163A | ||||||
Components | PROTEIN (GREEN FLUORESCENT PROTEIN) | ||||||
Keywords | LUMINESCENT PROTEIN / FLUORESCENT PROTEIN / CHROMOPHORE / GREEN FLUORESCENT PROTEIN / LUMINESCENCE / F99S M153T V163A MUTANT | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Aequorea victoria (jellyfish) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å | ||||||
Authors | Battistutta, R. / Negro, A. / Zanotti, G. | ||||||
Citation | Journal: Proteins / Year: 2000 Title: Crystal structure and refolding properties of the mutant F99S/M153T/V163A of the green fluorescent protein. Authors: Battistutta, R. / Negro, A. / Zanotti, G. #1: Journal: Nat.Biotechnol. / Year: 1996 Title: The Molecular Structure of Green Fluorescent Protein Authors: Yang, F. / Moss, L.G. / Phillips Jr., G.N. #2: Journal: Science / Year: 1996 Title: Crystal Structure of the Aequorea Victoria Green Fluorescent Protein Authors: Ormo, M. / Cubitt, A.B. / Kallio, K. / Gross, L.A. / Tsien, R.Y. / Remington, S.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1b9c.cif.gz | 193 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1b9c.ent.gz | 153.9 KB | Display | PDB format |
PDBx/mmJSON format | 1b9c.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/b9/1b9c ftp://data.pdbj.org/pub/pdb/validation_reports/b9/1b9c | HTTPS FTP |
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-Related structure data
Related structure data | 1gflS 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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Noncrystallographic symmetry (NCS) | NCS oper:
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-Components
#1: Protein | Mass: 26737.959 Da / Num. of mol.: 4 / Mutation: F99S, M153T, V163A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Aequorea victoria (jellyfish) / Description: THE N-TERMINAL HIS-TAG HAS BEEN REMOVED / Plasmid: PRSETB (INVITROGEN) / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P42212 #2: Water | ChemComp-HOH / | Sequence details | THE FLUOROPHORE IS FORMED BY SER 65, TYR 66 AND GLY 67. THE CARBONYL CARBON OF TYR 66 IS BONDED TO ...THE FLUOROPHOR | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 2 |
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-Sample preparation
Crystal | Density Matthews: 2.3 Å3/Da / Density % sol: 50 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 8.3 Details: 22% PEG 4000, 50 MM HEPES PH 8.5, 50 MM MGCL2, 10 MM 2-MERCAPTOETHANOL, 23% MG/ ML PROTEINA, pH 8.3 | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / pH: 7.4 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ELETTRA / Beamline: 5.2R / Wavelength: 1 |
Detector | Type: MAR scanner 345 mm plate / Detector: IMAGE PLATE |
Radiation | Monochromator: SI (111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.37→30 Å / Num. obs: 36746 / % possible obs: 83.9 % / Observed criterion σ(I): 0 / Redundancy: 4.6 % / Rmerge(I) obs: 0.062 / Net I/σ(I): 6.9 |
Reflection shell | Resolution: 2.37→2.64 Å / Redundancy: 3.9 % / Rmerge(I) obs: 0.146 / Mean I/σ(I) obs: 4.2 / % possible all: 45 |
Reflection | *PLUS Num. measured all: 165357 |
Reflection shell | *PLUS % possible obs: 45 % / Num. unique obs: 5445 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1GFL Resolution: 2.4→30 Å / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 2 / Details: APPLIED DATA CUTOFF: F(CALC)/F (OBS) < = 3.5
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Refinement step | Cycle: LAST / Resolution: 2.4→30 Å
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Refine LS restraints |
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Refine LS restraints NCS | NCS model details: RESTRAINTS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: X-PLOR / Version: 3.8.5 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.4 Å / Lowest resolution: 30 Å / σ(F): 2 / % reflection Rfree: 10 % / Rfactor Rfree: 0.28 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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