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- PDB-2hgy: Structure of S65A Y66F E222A GFP variant after cyclization and ca... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2hgy | ||||||
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Title | Structure of S65A Y66F E222A GFP variant after cyclization and carbon-carbon bond cleavage | ||||||
![]() | Green fluorescent protein | ||||||
![]() | LUMINESCENT PROTEIN / post-translational modification / cyclization / carbon-carbon bond cleavage / radical / GFP | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Barondeau, D.P. / Kassmann, C.J. / Tainer, J.A. / Getzoff, E.D. | ||||||
![]() | ![]() Title: The Case of the Missing Ring: Radical Cleavage of a Carbon-Carbon Bond and Implications for GFP Chromophore Biosynthesis Authors: Barondeau, D.P. / Kassmann, C.J. / Tainer, J.A. / Getzoff, E.D. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 60.9 KB | Display | ![]() |
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PDB format | ![]() | 43.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 430.3 KB | Display | ![]() |
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Full document | ![]() | 430.5 KB | Display | |
Data in XML | ![]() | 11.7 KB | Display | |
Data in CIF | ![]() | 16.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2hcgC ![]() 2hfcC ![]() 2hgdC ![]() 1emaS C: citing same article ( 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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Unit cell |
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Components
#1: Protein | Mass: 26676.986 Da / Num. of mol.: 1 / Mutation: S65A, Y66F, F99S, M153T, V163A, E222A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Water | ChemComp-HOH / |
Sequence details | RESIDUE AT POSITION 65 IS A S65A MUTATION, RESIDUE AT POSITION 66 IS A Y66F MUTATION. RESIDUES ALA ...RESIDUE AT POSITION 65 IS A S65A MUTATION, RESIDUE AT POSITION 66 IS A Y66F MUTATION. RESIDUES ALA 65, PHE 66 AND GLY 67 CONSTITUTE |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.08 Å3/Da / Density % sol: 40.77 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 8 Details: 19% PEG 4K, 50 mM MgCl2, 50 mM Hepes, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Mar 10, 2003 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.979 Å / Relative weight: 1 |
Reflection | Resolution: 2.05→20 Å / Num. obs: 13519 / % possible obs: 93.1 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Biso Wilson estimate: 25.2 Å2 / Rsym value: 0.07 / Net I/σ(I): 20.2 |
Reflection shell | Resolution: 2.05→2.1 Å / Mean I/σ(I) obs: 4.8 / Num. unique all: 1204 / Rsym value: 0.357 / % possible all: 85.2 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1ema Resolution: 2.05→20 Å / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.05→20 Å
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Refine LS restraints |
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