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Open data
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Basic information
Entry | Database: PDB / ID: 4z8u | |||||||||||||||
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Title | CRYSTAL STRUCTURE OF AvrRxo1-ORF1:-ORF2 WITH ATP | |||||||||||||||
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![]() | PROTEIN BINDING / AVRRXO1-ORF2 AVRRXO1-ORF1 AVRRXO1 AVRRXO1 REQUIRED CHAPERONE 1 / EFFECTOR PROTEINS AND MOLECULAR CHAPERONE / ATP | |||||||||||||||
Function / homology | Zeta toxin domain / Zeta toxin / kinase activity / P-loop containing nucleoside triphosphate hydrolase / ATP binding / ACETATE ION / AvrRxo1-ORF1 / AvrRxo1-ORF2![]() | |||||||||||||||
Biological species | ![]() | |||||||||||||||
Method | ![]() ![]() ![]() | |||||||||||||||
![]() | Han, Q. / Zhou, C. / Wu, S. / Liu, Y. / Yang, Z. / Miao, J. / Triplett, L. / Cheng, Q. / Tokuhisa, J. / Deblais, L. ...Han, Q. / Zhou, C. / Wu, S. / Liu, Y. / Yang, Z. / Miao, J. / Triplett, L. / Cheng, Q. / Tokuhisa, J. / Deblais, L. / Robinson, H. / Leach, J.E. / Li, J. / Zhao, B. | |||||||||||||||
Funding support | ![]() ![]()
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![]() | ![]() Title: Crystal Structure of Xanthomonas AvrRxo1-ORF1, a Type III Effector with a Polynucleotide Kinase Domain, and Its Interactor AvrRxo1-ORF2. Authors: Han, Q. / Zhou, C. / Wu, S. / Liu, Y. / Triplett, L. / Miao, J. / Tokuhisa, J. / Deblais, L. / Robinson, H. / Leach, J.E. / Li, J. / Zhao, B. | |||||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 108.4 KB | Display | ![]() |
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PDB format | ![]() | 79.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 471.4 KB | Display | ![]() |
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Full document | ![]() | 478 KB | Display | |
Data in XML | ![]() | 21.3 KB | Display | |
Data in CIF | ![]() | 31.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4z8qC ![]() 4z8tC ![]() 4z8vC ![]() 4pdbS 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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1 | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
-Protein , 2 types, 2 molecules AB
#1: Protein | Mass: 36303.531 Da / Num. of mol.: 1 / Fragment: UNP RESIDUES 90-421 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() ![]() |
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#2: Protein | Mass: 11523.586 Da / Num. of mol.: 1 / Fragment: UNP RESIDUES 1-98 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() ![]() |
-Non-polymers , 4 types, 327 molecules ![](data/chem/img/SO4.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/ACT.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/ACT.gif)
![](data/chem/img/HOH.gif)
#3: Chemical | ChemComp-SO4 / #4: Chemical | ChemComp-GOL / | #5: Chemical | ChemComp-ACT / | #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.65 Å3/Da / Density % sol: 53.65 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 5 Details: 1.6M (NH4)2SO4, 18% GLYCEROL, 8 MM DTT, 100 MM NA-CITRATE, 30 MM ATP AND 60 MM MAGNESIUM ACETATE, PH 5.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K PH range: 5 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Mar 21, 2012 |
Radiation | Monochromator: SI 111 CHANNEL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.075 Å / Relative weight: 1 |
Reflection | Resolution: 1.64→50 Å / Num. obs: 58250 / % possible obs: 98.6 % / Redundancy: 7.9 % / Rmerge(I) obs: 0.087 / Rsym value: 0.09 / Net I/σ(I): 20.1 |
Reflection shell | Resolution: 1.64→1.7 Å / Redundancy: 5.5 % / Rmerge(I) obs: 0.618 / Mean I/σ(I) obs: 1.5 / Rsym value: 0.771 / % possible all: 85.7 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 4PDB ENTRY Q5L Resolution: 1.65→45.82 Å / Cor.coef. Fo:Fc: 0.963 / Cor.coef. Fo:Fc free: 0.946 / Cross valid method: THROUGHOUT / ESU R: 0.098 / ESU R Free: 0.1 / Stereochemistry target values: MAXIMUM LIKELIHOOD
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 32.44 Å2
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Refinement step | Cycle: LAST / Resolution: 1.65→45.82 Å
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Refine LS restraints |
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