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Open data
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Basic information
| Entry | Database: PDB / ID: 2yh3 | ||||||
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| Title | The structure of BamB from E. coli | ||||||
Components | LIPOPROTEIN YFGL | ||||||
Keywords | LIPID BINDING PROTEIN / BAM COMPLEX / PROPELLER FOLD | ||||||
| Function / homology | Function and homology informationBam protein complex / Gram-negative-bacterium-type cell outer membrane assembly / protein insertion into membrane / cell outer membrane / identical protein binding / membrane Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.6 Å | ||||||
Authors | Albrecht, R. / Zeth, K. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2011Title: Structural Basis of Outer Membrane Protein Biogenesis in Bacteria. Authors: Albrecht, R. / Zeth, K. | ||||||
| History |
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 2yh3.cif.gz | 146.3 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb2yh3.ent.gz | 117.4 KB | Display | PDB format |
| PDBx/mmJSON format | 2yh3.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 2yh3_validation.pdf.gz | 423.9 KB | Display | wwPDB validaton report |
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| Full document | 2yh3_full_validation.pdf.gz | 434.1 KB | Display | |
| Data in XML | 2yh3_validation.xml.gz | 16.4 KB | Display | |
| Data in CIF | 2yh3_validation.cif.gz | 22.1 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/yh/2yh3 ftp://data.pdbj.org/pub/pdb/validation_reports/yh/2yh3 | HTTPS FTP |
-Related 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
| #1: Protein | Mass: 40663.070 Da / Num. of mol.: 1 / Fragment: RESIDUES 22-392 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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| #2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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Sample preparation
| Crystal | Density Matthews: 3.53 Å3/Da / Density % sol: 65.12 % / Description: NONE |
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| Crystal grow | pH: 4.6 / Details: 3.5M NH4CL, 0.1M NA-ACETATE PH 4.6 |
-Data collection
| Diffraction | Mean temperature: 100 K |
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| Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 1 |
| Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
| Reflection | Resolution: 2.6→50 Å / Num. obs: 17551 / % possible obs: 99.8 % / Observed criterion σ(I): 2 / Redundancy: 8.9 % / Rmerge(I) obs: 0.07 / Net I/σ(I): 20.6 |
| Reflection shell | Resolution: 2.6→2.66 Å / Rmerge(I) obs: 0.91 / Mean I/σ(I) obs: 2.2 / % possible all: 99.1 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.6→50 Å / Cor.coef. Fo:Fc: 0.946 / Cor.coef. Fo:Fc free: 0.903 / SU B: 24.557 / SU ML: 0.246 / Cross valid method: THROUGHOUT / ESU R: 0.367 / ESU R Free: 0.284 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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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 mean: 66.593 Å2
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| Refinement step | Cycle: LAST / Resolution: 2.6→50 Å
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| Refine LS restraints |
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