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Yorodumi- PDB-1col: REFINED STRUCTURE OF THE PORE-FORMING DOMAIN OF COLICIN A AT 2.4 ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1col | ||||||
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Title | REFINED STRUCTURE OF THE PORE-FORMING DOMAIN OF COLICIN A AT 2.4 ANGSTROMS RESOLUTION | ||||||
Components | COLICIN A | ||||||
Keywords | ANTIBACTERIAL PROTEIN | ||||||
Function / homology | Function and homology information cytolysis / defense response to Gram-negative bacterium / membrane => GO:0016020 / plasma membrane Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.4 Å | ||||||
Authors | Parker, M.W. / Postma, J.P.M. / Pattus, F. / Tucker, A.D. / Tsernoglou, D. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1992 Title: Refined structure of the pore-forming domain of colicin A at 2.4 A resolution. Authors: Parker, M.W. / Postma, J.P. / Pattus, F. / Tucker, A.D. / Tsernoglou, D. #1: Journal: J.Mol.Biol. / Year: 1991 Title: Fluorescence Energy Transfer Distance Measurements Using Site-Directed Single Cysteine Mutants Authors: Lakey, J.H. / Baty, D. / Pattus, F. #2: Journal: Experientia / Year: 1990 Title: Colicins: Prokaryotic Killer-Pores Authors: Pattus, F. / Massotte, D. / Wilmsen, H.U. / Lakey, J. / Tsernoglou, D. / Tucker, A. / Parker, M.W. #3: Journal: Nature / Year: 1989 Title: Structure of the Membrane-Pore-Forming Fragment of Colicin A Authors: Parker, M.W. / Pattus, F. / Tucker, A.D. / Tsernoglou, D. #4: Journal: Biochim.Biophys.Acta / Year: 1988 Title: The Membrane Channel-Forming Colicin A: Synthesis, Secretion, Structure, Action and Immunity Authors: Lazdunski, C.J. / Baty, D. / Geli, V. / Cavard, D. / Morlon, J. / Howard, R.Lloubes.S.P. / Knibiehler, M. / Chartier, M. / Varenne, S. / Frenette, M. / Dasseux, J.-L. / Pattus, F. #5: Journal: Eur.Biophys.J. / Year: 1987 Title: Gating Processes of Channels Induced by Colicin A, its C-Terminal Fragment and Colicin E1 in Planar Lipid Bilayers Authors: Collarini, M. / Amblard, G. / Lazdunski, C. / Pattus, F. #6: Journal: J.Mol.Biol. / Year: 1986 Title: Crystallization of the C-Terminal Domain of Colicin A Carrying the Voltage-Dependent Pore Activity of the Protein Authors: Tucker, A.D. / Pattus, F. / Tsernoglou, D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1col.cif.gz | 84.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1col.ent.gz | 65.6 KB | Display | PDB format |
PDBx/mmJSON format | 1col.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1col_validation.pdf.gz | 378.1 KB | Display | wwPDB validaton report |
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Full document | 1col_full_validation.pdf.gz | 398.2 KB | Display | |
Data in XML | 1col_validation.xml.gz | 11.1 KB | Display | |
Data in CIF | 1col_validation.cif.gz | 16.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/co/1col ftp://data.pdbj.org/pub/pdb/validation_reports/co/1col | 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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2 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.47345, -0.01458, 0.88043), Vector: |
-Components
#1: Protein | Mass: 21818.148 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / References: UniProt: Q47108 #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.62 Å3/Da / Density % sol: 53.04 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Method: vapor diffusion, hanging drop / Details: referred to J.Mol.Biol. 190.133-134 1986 | ||||||||||||||||||||||||||||||||||||
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: 2.5 Å / Lowest resolution: 6 Å / Num. obs: 10024 / Observed criterion σ(F): 3 / Rmerge F obs: 0.244 |
-Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 2.4→6 Å / Rfactor obs: 0.18 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.4→6 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 6 Å / σ(F): 2 / Rfactor obs: 0.26 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |