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- PDB-4j0o: Structure of the Y246A Mutant of the PANTON-VALENTINE LEUCOCIDIN ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4j0o | ||||||
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Title | Structure of the Y246A Mutant of the PANTON-VALENTINE LEUCOCIDIN S Component from STAPHYLOCOCCUS AUREUS | ||||||
![]() | LukS-PV | ||||||
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Function / homology | ![]() | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Maveyraud, L. / Laventie, B.J. / Prevost, G. / Mourey, L. | ||||||
![]() | ![]() Title: Residues essential for panton-valentine leukocidin s component binding to its cell receptor suggest both plasticity and adaptability in its interaction surface Authors: Laventie, B.J. / Guerin, F. / Mourey, L. / Tawk, M.Y. / Jover, E. / Maveyraud, L. / Prevost, G. #1: ![]() Title: Crystallization and preliminary crystallographic data of a leucotoxin S component from Staphylococcus aureus Authors: Guillet, V. / Keller, D. / Prevost, G. / Mourey, L. #2: ![]() Title: Crystal Structure of Leucotoxin S Component NEW INSIGHT INTO THE STAPHYLOCOCCAL beta-BARREL PORE-FORMING TOXINS Authors: Guillet, V. / Roblin, P. / Werner, S. / Coraiola, M. / Menestrina, G. / Monteil, H. / Prevost, G. / Mourey, L. #3: ![]() Title: The structure of a Staphylococcus aureus leucocidin component (LukF-PV) reveals the fold of the water-soluble species of a family of transmembrane pore-forming toxins Authors: Pedelacq, J.D. / Maveyraud, L. / Prevost, G. / Baba-Moussa, L. / Gonzalez, A. / Courcelle, E. / Shepard, W. / Monteil, H. / Samama, J.P. / Mourey, L. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 451.1 KB | Display | ![]() |
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PDB format | ![]() | 373 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 4iyaC ![]() 4iycC ![]() 4iytC ![]() 4izlC ![]() 1t5rS 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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2 | ![]()
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3 | ![]()
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4 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 32933.293 Da / Num. of mol.: 4 / Fragment: UNP residues 30-312 / Mutation: Y246A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Water | ChemComp-HOH / | ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.58 Å3/Da / Density % sol: 52.24 % |
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Crystal grow![]() | Temperature: 285 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: 40 % PEG 200, 0.1M NaMES, pH 7.50, VAPOR DIFFUSION, SITTING DROP, temperature 285K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 210 / Detector: CCD / Date: Feb 7, 2010 |
Radiation | Monochromator: Diamond (111), Ge(220) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 2.5→47.05 Å / Num. all: 46924 / Num. obs: 46924 / % possible obs: 96.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.6 % / Biso Wilson estimate: 49.67 Å2 / Rmerge(I) obs: 0.149 / Rsym value: 0.149 / Net I/σ(I): 10 |
Reflection shell | Resolution: 2.5→2.64 Å / Redundancy: 4.3 % / Rmerge(I) obs: 0.827 / Mean I/σ(I) obs: 1.9 / Num. unique all: 6622 / Rsym value: 0.827 / % possible all: 95.7 |
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Processing
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Refinement | Method to determine structure![]() ![]() Starting model: 1T5R Resolution: 2.5→46.51 Å / Cor.coef. Fo:Fc: 0.932 / Cor.coef. Fo:Fc free: 0.9075 / SU R Cruickshank DPI: 0.444 / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: BUSTER/TNT
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Displacement parameters | Biso mean: 42.75 Å2
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Refine analyze | Luzzati coordinate error obs: 0.291 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→46.51 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.5→2.56 Å / Total num. of bins used: 20
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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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