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Yorodumi- PDB-1f00: CRYSTAL STRUCTURE OF C-TERMINAL 282-RESIDUE FRAGMENT OF ENTEROPAT... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1f00 | ||||||
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Title | CRYSTAL STRUCTURE OF C-TERMINAL 282-RESIDUE FRAGMENT OF ENTEROPATHOGENIC E. COLI INTIMIN | ||||||
Components | INTIMIN | ||||||
Keywords | CELL ADHESION / Immunoglobulin-like fold / C-type lectin-like fold | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.9 Å | ||||||
Authors | Luo, Y. / Frey, E.A. / Pfuetzner, R.A. / Creagh, A.L. / Knoechel, D.G. / Haynes, C.A. / Finlay, B.B. / Strynadka, N.C.J. | ||||||
Citation | Journal: Nature / Year: 2000 Title: Crystal structure of enteropathogenic Escherichia coli intimin-receptor complex. Authors: Luo, Y. / Frey, E.A. / Pfuetzner, R.A. / Creagh, A.L. / Knoechel, D.G. / Haynes, C.A. / Finlay, B.B. / Strynadka, N.C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1f00.cif.gz | 67.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1f00.ent.gz | 50.2 KB | Display | PDB format |
PDBx/mmJSON format | 1f00.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1f00_validation.pdf.gz | 409.6 KB | Display | wwPDB validaton report |
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Full document | 1f00_full_validation.pdf.gz | 415 KB | Display | |
Data in XML | 1f00_validation.xml.gz | 14 KB | Display | |
Data in CIF | 1f00_validation.cif.gz | 19.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/f0/1f00 ftp://data.pdbj.org/pub/pdb/validation_reports/f0/1f00 | HTTPS FTP |
-Related structure data
Related structure data | 1f02C 1inm 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: 30084.533 Da / Num. of mol.: 1 / Fragment: C-TERMINAL DOMAIN (282 RESIDUES) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Plasmid: PET21A / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P19809 |
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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: 2.92 Å3/Da / Density % sol: 57.84 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: 1.8 M potassium phosphate, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 291.0K |
Crystal grow | *PLUS |
Components of the solutions | *PLUS Conc.: 1.8 M / Details: or 2.5M ammonium sulfate / Chemical formula: K2HPO4 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418 |
Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: Jan 5, 2000 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→20 Å / Num. all: 27521 / Num. obs: 24955 / % possible obs: 90.7 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 3 / Redundancy: 3.73 % / Biso Wilson estimate: 21.1 Å2 / Rmerge(I) obs: 0.097 / Net I/σ(I): 15.1 |
Reflection shell | Resolution: 1.9→1.94 Å / Redundancy: 2.5 % / Rmerge(I) obs: 0.261 / Num. unique all: 875 / % possible all: 51.5 |
Reflection shell | *PLUS % possible obs: 51.5 % |
-Processing
Software |
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Refinement | Resolution: 1.9→20 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 1.9→20 Å
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Refine LS restraints |
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