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Open data
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Basic information
Entry | Database: PDB / ID: 1a87 | ||||||
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Title | COLICIN N | ||||||
![]() | COLICIN N | ||||||
![]() | BACTERIOCIN / TOXIN / PORE-FORMING ACTIVITY | ||||||
Function / homology | ![]() negative regulation of ion transmembrane transporter activity / pore-forming activity / defense response to Gram-negative bacterium / killing of cells of another organism / transmembrane transporter binding / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Vetter, I.R. / Parker, M.W. / Tucker, A.D. / Lakey, J.H. / Pattus, F. / Tsernoglou, D. | ||||||
![]() | ![]() Title: Crystal structure of a colicin N fragment suggests a model for toxicity. Authors: Vetter, I.R. / Parker, M.W. / Tucker, A.D. / Lakey, J.H. / Pattus, F. / Tsernoglou, D. #1: ![]() Title: Insights Into Membrane Insertion Based on Studies of Colicins Authors: Vetter, I.R. / Parker, M.W. / Pattus, F. / Tsernoglou, D. #2: ![]() Title: Characterization of the Receptor and Translocator Domains of Colicin N Authors: El Kouhen, R. / Fierobe, H.P. / Scianimanico, S. / Steiert, M. / Pattus, F. / Pages, J.M. #3: ![]() Title: Colicin N Forms Voltage-and Ph-Dependent Channels in Planar Lipid Bilayer Membranes Authors: Wilmsen, H.U. / Pugsley, A.P. / Pattus, F. #4: ![]() Title: Involvement of Ompf During Reception and Translocation Steps of Colicin N Entry Authors: Bourdineaud, J.P. / Fierobe, H.P. / Lazdunski, C. / Pages, J.M. #5: ![]() Title: Nucleotide Sequencing of the Structural Gene for Colicin N Reveals Homology between the Catalytic, C-Terminal Domains of Colicins a and N Authors: Pugsley, A.P. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 70.5 KB | Display | ![]() |
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PDB format | ![]() | 53.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 378.1 KB | Display | ![]() |
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Full document | ![]() | 395.7 KB | Display | |
Data in XML | ![]() | 9.1 KB | Display | |
Data in CIF | ![]() | 13.3 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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Components
#1: Protein | Mass: 35146.270 Da / Num. of mol.: 1 / Fragment: RECEPTOR-BINDING AND PORE-FORMING DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 4.17 Å3/Da / Density % sol: 65 % | ||||||||||||||||||||
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Crystal grow | *PLUS Method: vapor diffusion, hanging drop / PH range low: 7 / PH range high: 5.6 | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 283 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jun 1, 1990 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.009 Å / Relative weight: 1 |
Reflection | Resolution: 3.1→22.7 Å / Num. obs: 10644 / % possible obs: 93.5 % / Biso Wilson estimate: 57.5 Å2 / Rsym value: 0.083 / Net I/σ(I): 33.07 |
Reflection shell | Resolution: 3.1→3.2 Å / Mean I/σ(I) obs: 6.3 / % possible all: 100 |
Reflection | *PLUS Rmerge(I) obs: 0.083 |
Reflection shell | *PLUS % possible obs: 100 % |
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Processing
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Refinement | Method to determine structure: ![]()
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Solvent computation | Bsol: 300 Å2 / ksol: 0.8 e/Å3 | ||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.1→23 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Version: 5EB / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.173 | ||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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