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Open data
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Basic information
Entry | Database: PDB / ID: 5lfk | ||||||
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Title | Crystal structure of CpxAHDC (hemiphosphorylated form) | ||||||
![]() | (Sensor histidine kinase CpxA) x 2 | ||||||
![]() | TRANSFERASE / Two-Componet Systems / Histidine Kinase | ||||||
Function / homology | ![]() cell adhesion involved in biofilm formation / cellular response to cell envelope stress / histidine kinase / phosphoprotein phosphatase activity / phosphorelay sensor kinase activity / response to radiation / signal transduction / ATP binding / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Mechaly, A.E. / Alzari, P.M. | ||||||
![]() | ![]() Title: Structural Coupling between Autokinase and Phosphotransferase Reactions in a Bacterial Histidine Kinase. Authors: Mechaly, A.E. / Soto Diaz, S. / Sassoon, N. / Buschiazzo, A. / Betton, J.M. / Alzari, P.M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 212.2 KB | Display | ![]() |
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PDB format | ![]() | 170 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
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Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 20 KB | Display | |
Data in CIF | ![]() | 26.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4uhjC ![]() 4uhkC ![]() 4biwS 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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1 | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 33314.422 Da / Num. of mol.: 1 / Fragment: UNP residues 188-457 / Mutation: M228V Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() | ||||
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#2: Protein | Mass: 33393.395 Da / Num. of mol.: 1 / Fragment: UNP residues 188-457 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() | ||||
#3: Chemical | ChemComp-SO4 / #4: Chemical | #5: Chemical | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 5.17 Å3/Da / Density % sol: 76.23 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion Details: 100 mM Tris (pH 8.5), 1.5 M ammonium sulphate and 12 % v/v glycerol |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Apr 23, 2015 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97934 Å / Relative weight: 1 |
Reflection | Resolution: 3.09→48.3 Å / Num. obs: 26453 / % possible obs: 99.6 % / Redundancy: 11.9 % / CC1/2: 0.999 / Rmerge(I) obs: 0.094 / Rsym value: 0.103 / Net I/σ(I): 9.4 |
Reflection shell | Resolution: 3.09→3.31 Å / Redundancy: 11.8 % / Rmerge(I) obs: 0.774 / Mean I/σ(I) obs: 1.8 / CC1/2: 0.921 / % possible all: 98.1 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 4BIW Resolution: 3.094→47.703 Å / SU ML: 0.44 / Cross valid method: FREE R-VALUE / σ(F): 0.96 / Phase error: 26.77
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.094→47.703 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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