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- PDB-1prn: REFINED STRUCTURE OF PORIN FROM RHODOPSEUDOMONAS BLASTICA AND COM... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1prn | ||||||
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Title | REFINED STRUCTURE OF PORIN FROM RHODOPSEUDOMONAS BLASTICA AND COMPARISON WITH THE PORIN FROM RHODOBACTER CAPSULATUS | ||||||
![]() | PORIN | ||||||
![]() | INTEGRAL MEMBRANE PROTEIN PORIN | ||||||
Function / homology | ![]() porin activity / pore complex / monoatomic ion transport / cell outer membrane Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Kreusch, A. / Schulz, G.E. | ||||||
![]() | ![]() Title: Refined structure of the porin from Rhodopseudomonas blastica. Comparison with the porin from Rhodobacter capsulatus. Authors: Kreusch, A. / Schulz, G.E. #1: ![]() Title: The Structure of the Membrane Channel Porin from Rhodopseudomonas Blastica at 2.0 Angstroms Resolution Authors: Kreusch, A. / Neubueser, A. / Schiltz, E. / Weckesser, J. / Schulz, G.E. | ||||||
History |
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Remark 700 | SHEET THE SHEET PRESENTED AS *S1* ON SHEET RECORDS BELOW IS ACTUALLY A SIXTEEN-STRANDED BETA-BARREL. ...SHEET THE SHEET PRESENTED AS *S1* ON SHEET RECORDS BELOW IS ACTUALLY A SIXTEEN-STRANDED BETA-BARREL. THIS IS REPRESENTED BY A SEVENTEEN-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 72.6 KB | Display | ![]() |
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PDB format | ![]() | 54.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 895.2 KB | Display | ![]() |
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Full document | ![]() | 894.1 KB | Display | |
Data in XML | ![]() | 15.9 KB | Display | |
Data in CIF | ![]() | 23.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar 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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Atom site foot note | 1: RESIDUES ILE 139 - SER 140 HAVE WEAK DENSITY. 2: THE STRUCTURE OF THE DETERGENT MOLECULES COULD NOT BE IDENTIFIED FROM THE ELECTRON DENSITY AND HAS THEREFORE BEEN PRELIMINARILY MODELED AS N-OCTYLTETRAOXYETHYLENE USED IN CRYSTALLIZATION. |
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Components
#1: Protein | Mass: 30608.854 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() | ||||||
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#2: Chemical | #3: Water | ChemComp-HOH / | Nonpolymer details | THE STRUCTURE OF THE DETERGENT MOLECULES COULD NOT BE IDENTIFIED FROM THE ELECTRON DENSITY AND HAS ...THE STRUCTURE OF THE DETERGENT MOLECULES COULD NOT BE IDENTIFIED | Sequence details | THE SEQUENCE IS DESCRIBED IN THE JRNL ARTICLE AND IN REFERENCE 1 ABOVE. | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 4.26 Å3/Da / Density % sol: 71.13 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 20 ℃ / pH: 7.2 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 1.96 Å / Lowest resolution: 100 Å / Num. obs: 35847 / % possible obs: 75 % / Observed criterion σ(I): 3 / Num. measured all: 291952 / Rmerge(I) obs: 0.078 |
Reflection shell | *PLUS Highest resolution: 1.96 Å / Lowest resolution: 2 Å |
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Processing
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Refinement | Resolution: 1.96→10 Å / σ(F): 0 / Details: RESIDUES ILE 139 - SER 140 HAVE WEAK DENSITY. /
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Refinement step | Cycle: LAST / Resolution: 1.96→10 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Num. reflection all: 35620 / Rfactor obs: 0.176 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 18 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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