+Open data
-Basic information
Entry | Database: PDB / ID: 2okw | ||||||
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Title | A non-invasive GFP-based biosensor for mercury ions | ||||||
Components | Green fluorescent protein | ||||||
Keywords | LUMINESCENT PROTEIN / mercury / biosensor | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Aequorea victoria (jellyfish) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.9 Å | ||||||
Authors | Chapleau, R.R. / Blomberg, R. / Ford, P.C. / Sagermann, M. | ||||||
Citation | Journal: Protein Sci. / Year: 2008 Title: Design of a highly specific and noninvasive biosensor suitable for real-time in vivo imaging of mercury (II) uptake. Authors: Chapleau, R.R. / Blomberg, R. / Ford, P.C. / Sagermann, M. #1: Journal: Proc.Natl.Acad.Sci.USA / Year: 2004 Title: Local complexity of amino acid interactions in a protein core. Authors: Jain, R.K. / Ranganathan, R. #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 | 2okw.cif.gz | 293.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2okw.ent.gz | 237.9 KB | Display | PDB format |
PDBx/mmJSON format | 2okw.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ok/2okw ftp://data.pdbj.org/pub/pdb/validation_reports/ok/2okw | HTTPS FTP |
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-Related structure data
Related structure data | 2okyC 1embS C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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Unit cell |
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-Components
#1: Protein | Mass: 26898.365 Da / Num. of mol.: 6 / Mutation: S65T, R80Q, S205C Source method: isolated from a genetically manipulated source Source: (gene. exp.) Aequorea victoria (jellyfish) / Gene: GFP / Plasmid: pET151 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): Bl21 / References: UniProt: P42212 #2: Water | ChemComp-HOH / | Sequence details | AUTHORS STATE THAT RESIDUE 64 IS A LEUCINE. RESIDUE 65 HAS BEEN MUTATED FROM SER TO THR AND RESIDUE ...AUTHORS STATE THAT RESIDUE 64 IS A LEUCINE. RESIDUE 65 HAS BEEN MUTATED FROM SER TO THR AND RESIDUE 80 IS AN ARG TO GLN MUTATION. RESIDUE 80 IS LISTED AS A GLN IN THE DATABASE REFERENCE BUT IS AN ARG ACCORDING TO ROUWENDAL ET AL., 1997 PLANT MOL. BIOL. 33, 989-999. RESIDUES THR 65, TYR 66, GLY 67 CONSTITUTE | |
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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: 2.6 Å3/Da / Density % sol: 52.75 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 100mM Pipes, 30% PEG 8000, 200mM Na-acetate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 150 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRL / Beamline: BL11-1 / Wavelength: 0.979454 Å |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Jun 3, 2006 / Details: single SI crystal flat mirror |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.979454 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→19.83 Å / Num. all: 156061 / Num. obs: 155659 / % possible obs: 99.7 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 7.16 % / Rmerge(I) obs: 0.073 / Net I/σ(I): 15.7 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1EMB Resolution: 1.9→19.83 Å / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber Details: First 6 residues and the last c-terminal residues could not be modeled into the density. These residues were therefore omitted in the final model
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Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 1.9→19.83 Å
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Refine LS restraints |
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