+Open data
-Basic information
Entry | Database: PDB / ID: 6prn | ||||||
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Title | E1M, K50A, R52A MUTANT OF RH. BLASTICA PORIN | ||||||
Components | PORIN | ||||||
Keywords | MEMBRANE PROTEIN / INTEGRAL MEMBRANE PROTEIN / PORIN / PORE EYELET MUTANT | ||||||
Function / homology | Function and homology information porin activity / pore complex / monoatomic ion transport / cell outer membrane Similarity search - Function | ||||||
Biological species | Rhodobacter blasticus (bacteria) | ||||||
Method | X-RAY DIFFRACTION / DIFFERENCE FOURIER / Resolution: 2.04 Å | ||||||
Authors | Maveyraud, L. / Schmid, B. / Schulz, G.E. | ||||||
Citation | Journal: Protein Sci. / Year: 1998 Title: Porin mutants with new channel properties. Authors: Schmid, B. / Maveyraud, L. / Kromer, M. / Schulz, G.E. #1: Journal: FEBS Lett. / Year: 1996 Title: Expression of Porin from Rhodopseudomonas Blastica in Escherichia Coli Inclusion Bodies and Folding Into Exact Native Structure Authors: Schmid, B. / Kromer, M. / Schulz, G.E. #2: Journal: J.Mol.Biol. / Year: 1994 Title: Refined Structure of the Porin from Rhodopseudomonas Blastica. Comparison with the Porin from Rhodobacter Capsulatus Authors: Kreusch, A. / Schulz, G.E. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6prn.cif.gz | 70.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6prn.ent.gz | 52.6 KB | Display | PDB format |
PDBx/mmJSON format | 6prn.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/pr/6prn ftp://data.pdbj.org/pub/pdb/validation_reports/pr/6prn | HTTPS FTP |
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-Related structure data
Related structure data | 1bh3C 2prnC 3prnC 5prnC 7prnC 8prnC 1prnS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 30466.717 Da / Num. of mol.: 1 / Mutation: E1M, K50A, R52A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rhodobacter blasticus (bacteria) / Cell line: BL21 / Cellular location: OUTER MEMBRANE / Plasmid: PET-3B / Cellular location (production host): INCLUSION BODIES / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 (DE3) PLYSS / References: UniProt: P39767 | ||
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#2: Chemical | #3: 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: 4.27 Å3/Da / Density % sol: 66 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 7.8 / Details: pH 7.8 | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / pH: 7.2 / Method: vapor diffusion, hanging drop / Details: Kreusch, A., (1994) J.Mol.Biol., 243, 891. | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RUH3R / Wavelength: 1.5418 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Aug 1, 1997 |
Radiation | Monochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.04→19.7 Å / Num. obs: 32038 / % possible obs: 99.8 % / Redundancy: 3.5 % / Rmerge(I) obs: 0.045 / Rsym value: 0.045 / Net I/σ(I): 19.3 |
Reflection shell | Resolution: 2.04→2.15 Å / Redundancy: 2.2 % / Rmerge(I) obs: 0.181 / Mean I/σ(I) obs: 5.1 / Rsym value: 0.181 / % possible all: 99.6 |
Reflection shell | *PLUS % possible obs: 100 % / Num. unique obs: 4676 |
-Processing
Software |
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Refinement | Method to determine structure: DIFFERENCE FOURIER Starting model: PDB ENTRY 1PRN Resolution: 2.04→19.68 Å / Cross valid method: THROUGHOUT / σ(F): 1
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Displacement parameters | Biso mean: 34.1 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.04→19.68 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.163 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |