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Open data
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Basic information
Entry | Database: PDB / ID: 1hxx | ||||||
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Title | OMPF PORIN MUTANT Y106F | ||||||
![]() | OUTER MEMBRANE PROTEIN F | ||||||
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Function / homology | ![]() colicin transmembrane transporter activity / monoatomic ion channel complex / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Phale, P.S. / Philippsen, A. / Widmer, C. / Phale, V.P. / Rosenbusch, J.P. / Schirmer, T. | ||||||
![]() | ![]() Title: Role of charged residues at the OmpF porin channel constriction probed by mutagenesis and simulation. Authors: Phale, P.S. / Philippsen, A. / Widmer, C. / Phale, V.P. / Rosenbusch, J.P. / Schirmer, T. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 82.2 KB | Display | ![]() |
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PDB format | ![]() | 61.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-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: 37098.250 Da / Num. of mol.: 1 / Mutation: Y106F Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() | ||
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#2: Chemical | ChemComp-C8E / ( #3: Water | ChemComp-HOH / | ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.85 Å3/Da / Density % sol: 56.88 % | |||||||||||||||
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Crystal grow![]() | *PLUS Method: microdialysis / Details: Pauptit, R.A., (1991) J. Mol. Biol., 218, 505. | |||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MACSCIENCE / Detector: IMAGE PLATE / Date: Jan 1, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 2.2→30 Å / Num. all: 71614 / Num. obs: 19807 / % possible obs: 79.9 % / Observed criterion σ(F): 6 / Observed criterion σ(I): 0 / Redundancy: 3.4 % / Biso Wilson estimate: 28 Å2 / Rmerge(I) obs: 0.065 / Net I/σ(I): 7 |
Reflection | *PLUS % possible obs: 97.9 % / Num. measured all: 71614 |
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Processing
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Refinement | Method to determine structure![]()
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Refinement step | Cycle: LAST / Resolution: 2.2→8 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.174 / Rfactor Rfree![]() | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||
Refine LS restraints | *PLUS Type: p_bond_d / Dev ideal: 0.08 |