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- PDB-6qqh: Cryogenic temperature structure of the ground state of AtPhot2LOV... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6qqh | ||||||
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Title | Cryogenic temperature structure of the ground state of AtPhot2LOV2 recorded after an accumulated dose of 2.68 MGy | ||||||
![]() | Phototropin-2 | ||||||
![]() | PLANT PROTEIN / Room temperature macromolecular crystallography / cryo-crystallography / specific radiation damage / time-resolved crystallography | ||||||
Function / homology | ![]() chloroplast relocation / negative regulation of anion channel activity by blue light / phototropism / stomatal movement / response to blue light / blue light photoreceptor activity / plastid / circadian rhythm / FMN binding / kinase activity ...chloroplast relocation / negative regulation of anion channel activity by blue light / phototropism / stomatal movement / response to blue light / blue light photoreceptor activity / plastid / circadian rhythm / FMN binding / kinase activity / protein autophosphorylation / non-specific serine/threonine protein kinase / protein serine kinase activity / protein serine/threonine kinase activity / Golgi apparatus / ATP binding / identical protein binding / membrane / nucleus / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Aumonier, S. / Gotthard, G. / Royant, A. | ||||||
![]() | ![]() Title: Specific radiation damage is a lesser concern at room temperature. Authors: Gotthard, G. / Aumonier, S. / De Sanctis, D. / Leonard, G. / von Stetten, D. / Royant, A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 74.8 KB | Display | ![]() |
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PDB format | ![]() | 54.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 728.2 KB | Display | ![]() |
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Full document | ![]() | 728.6 KB | Display | |
Data in XML | ![]() | 8.5 KB | Display | |
Data in CIF | ![]() | 11.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6qq8C ![]() 6qq9C ![]() 6qqaC ![]() 6qqbC ![]() 6qqcC ![]() 6qqdC ![]() 6qqeC ![]() 6qqfC ![]() 6qqiC ![]() 6qqjC ![]() 6qqkC ![]() 6qsaC ![]() 4eepS S: Starting model for refinement C: citing same article ( |
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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: 15007.909 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P93025, non-specific serine/threonine protein kinase |
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#2: Chemical | ChemComp-FMN / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.94 Å3/Da / Density % sol: 36.55 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6 / Details: 12-17 % PEG8000 0.2 M Calcium acetate 0.1 M MES |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS3 2M / Detector: PIXEL / Date: Sep 23, 2015 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.968 Å / Relative weight: 1 |
Reflection | Resolution: 1.38→38.4 Å / Num. obs: 23065 / % possible obs: 99.8 % / Redundancy: 7.18 % / Biso Wilson estimate: 18.75 Å2 / CC1/2: 0.999 / Net I/σ(I): 16.84 |
Reflection shell | Resolution: 1.38→1.43 Å / Redundancy: 6.32 % / Mean I/σ(I) obs: 1.68 / Num. unique obs: 2265 / CC1/2: 0.568 / % possible all: 99.8 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 4eep Resolution: 1.38→38.4 Å / Cor.coef. Fo:Fc: 0.977 / Cor.coef. Fo:Fc free: 0.971 / SU B: 2.412 / SU ML: 0.042 / Cross valid method: THROUGHOUT / ESU R: 0.066 / ESU R Free: 0.057 / 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: 1.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 16.625 Å2
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Refinement step | Cycle: LAST / Resolution: 1.38→38.4 Å
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Refine LS restraints |
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