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Yorodumi- PDB-3s06: The crystal structure of the periplasmic domain of Helicobacter p... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3s06 | ||||||
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Title | The crystal structure of the periplasmic domain of Helicobacter pylori MotB (residues 97-256, P3121). | ||||||
Components | Motility protein B | ||||||
Keywords | MOTOR PROTEIN / peptidoglycan binding / flagellar rotation / chemotaxis / bacterial flagellar motor / membrane | ||||||
Function / homology | Function and homology information archaeal or bacterial-type flagellum-dependent cell motility / chemotaxis / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | Helicobacter pylori (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.8 Å | ||||||
Authors | Roujeinikova, A.R. | ||||||
Citation | Journal: Acta Crystallogr.,Sect.D / Year: 2011 Title: Role of the MotB linker in the assembly and activation of the bacterial flagellar motor. Authors: O'Neill, J. / Xie, M. / Hijnen, M. / Roujeinikova, A. #1: Journal: To be published Title: Cloning, purification and crystallization of MotB, a stator component of the proton-driven bacterial flagellar motor. Authors: O'Neill, J. / Roujeinikova, A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3s06.cif.gz | 87.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3s06.ent.gz | 68.5 KB | Display | PDB format |
PDBx/mmJSON format | 3s06.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 3s06_validation.pdf.gz | 446.1 KB | Display | wwPDB validaton report |
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Full document | 3s06_full_validation.pdf.gz | 447.9 KB | Display | |
Data in XML | 3s06_validation.xml.gz | 18.6 KB | Display | |
Data in CIF | 3s06_validation.cif.gz | 28 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/s0/3s06 ftp://data.pdbj.org/pub/pdb/validation_reports/s0/3s06 | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 18876.377 Da / Num. of mol.: 2 / Fragment: C-terminal fragment (UNP residues 98-257) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Helicobacter pylori (bacteria) / Strain: 26695 / Gene: HP_0816, motB / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / References: UniProt: P56427 #2: Chemical | ChemComp-SO4 / | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.74 Å3/Da / Density % sol: 55.14 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 9 Details: 100 mM Bicine pH 9.0, 2 M Ammonium Sulphate , VAPOR DIFFUSION, SITTING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID23-2 / Wavelength: 0.87 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Apr 8, 2009 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 0.87 Å / Relative weight: 1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Redundancy: 5.6 % / Av σ(I) over netI: 7.6 / Number: 214679 / Rmerge(I) obs: 0.066 / Rsym value: 0.066 / D res high: 1.7 Å / D res low: 56.344 Å / Num. obs: 38287 / % possible obs: 98.1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Diffraction reflection shell |
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Reflection | Resolution: 1.8→61.24 Å / Num. all: 38287 / Num. obs: 38287 / % possible obs: 98.1 % / Redundancy: 5.6 % / Rmerge(I) obs: 0.066 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.8→30 Å / Cor.coef. Fo:Fc: 0.959 / Cor.coef. Fo:Fc free: 0.946 / Occupancy max: 1 / Occupancy min: 0.3 / SU B: 4.701 / SU ML: 0.068 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.114 / ESU R Free: 0.111 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : RESIDUAL ONLY
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 56.16 Å2 / Biso mean: 15.9676 Å2 / Biso min: 3.15 Å2
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Refinement step | Cycle: LAST / Resolution: 1.8→30 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.8→1.847 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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