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Open data
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Basic information
Entry | Database: PDB / ID: 1xm9 | ||||||
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Title | Structure of the armadillo repeat domain of plakophilin 1 | ||||||
![]() | plakophilin 1 | ||||||
![]() | CELL ADHESION / armadillo repeat | ||||||
Function / homology | ![]() negative regulation of mRNA catabolic process / intermediate filament bundle assembly / intermediate filament binding / structural constituent of skin epidermis / Keratinization / : / desmosome / Formation of the cornified envelope / lamin binding / cornified envelope ...negative regulation of mRNA catabolic process / intermediate filament bundle assembly / intermediate filament binding / structural constituent of skin epidermis / Keratinization / : / desmosome / Formation of the cornified envelope / lamin binding / cornified envelope / Apoptotic cleavage of cell adhesion proteins / cell-cell junction assembly / intermediate filament / ficolin-1-rich granule membrane / adherens junction / cell-cell adhesion / cell adhesion / cadherin binding / Neutrophil degranulation / positive regulation of gene expression / signal transduction / nucleoplasm / nucleus / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Choi, H.J. / Weis, W.I. | ||||||
![]() | ![]() Title: Structure of the armadillo repeat domain of plakophilin 1. Authors: Choi, H.J. / Weis, W.I. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 91.1 KB | Display | ![]() |
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PDB format | ![]() | 69.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 424.2 KB | Display | ![]() |
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Full document | ![]() | 452 KB | Display | |
Data in XML | ![]() | 19.9 KB | Display | |
Data in CIF | ![]() | 26.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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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Components
#1: Protein | Mass: 50489.098 Da / Num. of mol.: 1 / Fragment: Armadillo repeat domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.66 Å3/Da / Density % sol: 52 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8.6 Details: PEG 3350, Tris-Cl, potassium formate, pH 8.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 93 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Jul 20, 2003 |
Radiation | Monochromator: double crystal Si 111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.979 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→48 Å / Num. all: 14705 / Num. obs: 13069 / % possible obs: 89 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 1 / Biso Wilson estimate: 48.7 Å2 / Rsym value: 0.055 |
Reflection shell | Resolution: 2.8→2.9 Å / % possible all: 73 |
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Processing
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Refinement | Method to determine structure: ![]()
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 18.2814 Å2 / ksol: 0.287631 e/Å3 | ||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 70.3 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.8→29.92 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.8→2.98 Å / Rfactor Rfree error: 0.038 / Total num. of bins used: 6
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Xplor file | Serial no: 1 / Param file: PROTEIN_REP.PARAM / Topol file: PROTEIN.TOP |