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Open data
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Basic information
Entry | Database: PDB / ID: 1kke | ||||||
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Title | Crystal Structure of Reovirus Attachment Protein Sigma1 Trimer | ||||||
![]() | SIGMA 1 PROTEIN | ||||||
![]() | VIRAL PROTEIN / reovirus / sigma1 / fiber / beta-spiral / beta-barrel / trimer / receptor-binding | ||||||
Function / homology | ![]() viral outer capsid / cell adhesion / symbiont entry into host cell / virion attachment to host cell Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Chappell, J.D. / Prota, A.E. / Dermody, T.S. / Stehle, T. | ||||||
![]() | ![]() Title: Crystal structure of reovirus attachment protein sigma1 reveals evolutionary relationship to adenovirus fiber. Authors: Chappell, J.D. / Prota, A.E. / Dermody, T.S. / Stehle, T. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 127.9 KB | Display | ![]() |
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PDB format | ![]() | 101 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 438.3 KB | Display | ![]() |
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Full document | ![]() | 445.9 KB | Display | |
Data in XML | ![]() | 25 KB | Display | |
Data in CIF | ![]() | 34 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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Unit cell |
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Details | The asymmetric unit contains a biologically active trimer |
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Components
#1: Protein | Mass: 22687.412 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.06 Å3/Da / Density % sol: 40.37 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: PEG4000, Isopropanol, Hepes, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / Method: vapor diffusion | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Feb 1, 2001 / Details: mirror |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.541789 Å / Relative weight: 1 |
Reflection | Resolution: 2.6→20 Å / Num. all: 17954 / Num. obs: 16338 / % possible obs: 91 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Rmerge(I) obs: 0.087 / Net I/σ(I): 9 |
Reflection shell | Resolution: 2.6→2.7 Å / Rmerge(I) obs: 0.284 / Mean I/σ(I) obs: 2.2 / % possible all: 64 |
Reflection | *PLUS Lowest resolution: 20 Å / % possible obs: 91 % / Num. measured all: 56260 |
Reflection shell | *PLUS % possible obs: 64 % |
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Processing
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Refinement | Method to determine structure: ![]() Stereochemistry target values: xplor parameter set (Engh & Huber)
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Refinement step | Cycle: LAST / Resolution: 2.6→20 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.6 Å / Lowest resolution: 20 Å / σ(F): 1 / % reflection Rfree: 5 % / Rfactor all: 0.172 / Rfactor Rfree: 0.235 | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_deg / Dev ideal: 1.4 |