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Open data
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Basic information
Entry | Database: PDB / ID: 1b9c | ||||||
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Title | Green Fluorescent Protein Mutant F99S, M153T and V163A | ||||||
![]() | PROTEIN (GREEN FLUORESCENT PROTEIN) | ||||||
![]() | LUMINESCENT PROTEIN / FLUORESCENT PROTEIN / CHROMOPHORE / GREEN FLUORESCENT PROTEIN / LUMINESCENCE / F99S M153T V163A MUTANT | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Battistutta, R. / Negro, A. / Zanotti, G. | ||||||
![]() | ![]() 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: ![]() Title: The Molecular Structure of Green Fluorescent Protein Authors: Yang, F. / Moss, L.G. / Phillips Jr., G.N. #2: ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 193 KB | Display | ![]() |
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PDB format | ![]() | 153.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 471.2 KB | Display | ![]() |
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Full document | ![]() | 513 KB | Display | |
Data in XML | ![]() | 42.3 KB | Display | |
Data in CIF | ![]() | 56.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1gflS S: Starting model for refinement |
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Similar structure data |
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Links
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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.) ![]() ![]() ![]() ![]() #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: ![]() |
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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: ![]() ![]() ![]() |
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 |
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Processing
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Refinement | Method to determine structure: ![]() 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: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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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