+Open data
-Basic information
Entry | Database: PDB / ID: 6fls | ||||||
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Title | Pentapeptide repeat family protein from Clostridium botulinum | ||||||
Components | Pentapeptide repeat family protein | ||||||
Keywords | UNKNOWN FUNCTION / Pentapeptide repeat protein Clostridium botulinum | ||||||
Function / homology | Pentapeptide repeats (8 copies) / Pentapeptide repeats (9 copies) / Pentapeptide repeat / Uncharacterized protein Function and homology information | ||||||
Biological species | Clostridium botulinum (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.8 Å | ||||||
Authors | Martinez-Carranza, M. / Stenmark, P. | ||||||
Citation | Journal: J. Mol. Biol. / Year: 2018 Title: Cotranslational Folding of a Pentarepeat beta-Helix Protein. Authors: Notari, L. / Martinez-Carranza, M. / Farias-Rico, J.A. / Stenmark, P. / von Heijne, G. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6fls.cif.gz | 187.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6fls.ent.gz | 149.6 KB | Display | PDB format |
PDBx/mmJSON format | 6fls.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6fls_validation.pdf.gz | 472.6 KB | Display | wwPDB validaton report |
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Full document | 6fls_full_validation.pdf.gz | 481.9 KB | Display | |
Data in XML | 6fls_validation.xml.gz | 33.4 KB | Display | |
Data in CIF | 6fls_validation.cif.gz | 46 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fl/6fls ftp://data.pdbj.org/pub/pdb/validation_reports/fl/6fls | HTTPS FTP |
-Related structure data
Similar structure data |
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-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
#1: Protein | Mass: 27369.889 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Clostridium botulinum (bacteria) / Gene: ACP52_06880 / Production host: Escherichia coli (E. coli) / References: UniProt: A0A0M0A2X5 #2: Chemical | ChemComp-GOL / #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: 5.8 Å3/Da / Density % sol: 78.79 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / Details: 0.1 M Bis-Tris pH 5.5, 25% PEG 3350 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: Diamond / Beamline: I04-1 / Wavelength: 0.9282 Å |
Detector | Type: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Apr 16, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9282 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→112.53 Å / Num. obs: 63384 / % possible obs: 99.2 % / Redundancy: 3.8 % / Net I/σ(I): 10.1 |
Reflection shell | Resolution: 2.8→2.87 Å |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.8→112.53 Å / Cor.coef. Fo:Fc: 0.96 / Cor.coef. Fo:Fc free: 0.945 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.232 / ESU R Free: 0.202 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
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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 max: 149 Å2 / Biso mean: 59.071 Å2 / Biso min: 28 Å2
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Refinement step | Cycle: final / Resolution: 2.8→112.53 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.8→2.873 Å / Total num. of bins used: 20
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