+Open data
-Basic information
Entry | Database: PDB / ID: 1bt9 | ||||||
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Title | OMPF PORIN MUTANT D74A | ||||||
Components | PROTEIN (MATRIX PORIN OUTER MEMBRANE PROTEIN F) | ||||||
Keywords | MEMBRANE PROTEIN / INTEGRAL MEMBRANE PROTEIN PORIN / PORIN | ||||||
Function / homology | Function and homology information colicin transmembrane transporter activity / monoatomic ion channel complex / porin activity / pore complex / protein homotrimerization / monoatomic ion transmembrane transport / lipopolysaccharide binding / cell outer membrane / disordered domain specific binding / protein transport ...colicin transmembrane transporter activity / monoatomic ion channel complex / porin activity / pore complex / protein homotrimerization / monoatomic ion transmembrane transport / lipopolysaccharide binding / cell outer membrane / disordered domain specific binding / protein transport / monoatomic ion channel activity / lipid binding / identical protein binding / membrane Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / OTHER / Resolution: 3 Å | ||||||
Authors | Philippsen, A. / Schirmer, T. | ||||||
Citation | Journal: Biochemistry / Year: 1998 Title: Stability of trimeric OmpF porin: the contributions of the latching loop L2. Authors: Phale, P.S. / Philippsen, A. / Kiefhaber, T. / Koebnik, R. / Phale, V.P. / Schirmer, T. / Rosenbusch, J.P. #1: Journal: Nature / Year: 1992 Title: Crystal Structures Explain Functional Properties of Two E.Coli Porins Authors: Cowan, S.W. / Schirmer, T. / Rummel, G. / Steiert, M. / Ghosh, R. / Pauptit, R.A. / Jansonius, J.N. / Rosenbusch, J.P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1bt9.cif.gz | 76.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1bt9.ent.gz | 58.3 KB | Display | PDB format |
PDBx/mmJSON format | 1bt9.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1bt9_validation.pdf.gz | 370.3 KB | Display | wwPDB validaton report |
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Full document | 1bt9_full_validation.pdf.gz | 384.3 KB | Display | |
Data in XML | 1bt9_validation.xml.gz | 9.6 KB | Display | |
Data in CIF | 1bt9_validation.cif.gz | 13.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bt/1bt9 ftp://data.pdbj.org/pub/pdb/validation_reports/bt/1bt9 | 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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Unit cell |
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-Components
#1: Protein | Mass: 37070.242 Da / Num. of mol.: 1 / Mutation: D74A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: B / Species (production host): Escherichia coli / Production host: Escherichia coli B (bacteria) / Strain (production host): B / References: UniProt: P02931 |
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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: 2.88 Å3/Da / Density % sol: 57 % | |||||||||||||||
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Crystal grow | pH: 7 / Details: pH 7.0 | |||||||||||||||
Crystal | *PLUS | |||||||||||||||
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: 276 K |
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Diffraction source | Wavelength: 1.5418 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 3→20 Å / Num. obs: 8162 / % possible obs: 92 % / Redundancy: 3.9 % / Rmerge(I) obs: 0.082 |
-Processing
Software |
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Refinement | Method to determine structure: OTHER / Resolution: 3→20 Å / Cross valid method: THROUGHOUT / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 3→20 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 3 Å / σ(F): 0 / % reflection Rfree: 10 % / Rfactor obs: 0.191 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |