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Open data
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Basic information
Entry | Database: PDB / ID: 1qq1 | ||||||
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Title | TAILSPIKE PROTEIN, MUTANT E359G | ||||||
![]() | TAILSPIKE PROTEIN | ||||||
![]() | VIRAL PROTEIN / BETA-HELIX | ||||||
Function / homology | ![]() endo-1,3-alpha-L-rhamnosidase activity / symbiont entry into host cell via disruption of host cell envelope lipopolysaccharide / virus tail, fiber / symbiont entry into host cell via disruption of host cell envelope / symbiont entry into host / Hydrolases; Glycosylases; Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds / adhesion receptor-mediated virion attachment to host cell / metabolic process / virion attachment to host cell Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Schuler, B. / Furst, F. / Osterroth, F. / Steinbacher, S. / Huber, R. / Seckler, R. | ||||||
![]() | ![]() Title: Plasticity and steric strain in a parallel beta-helix: rational mutations in the P22 tailspike protein. Authors: Schuler, B. / Furst, F. / Osterroth, F. / Steinbacher, S. / Huber, R. / Seckler, R. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 118 KB | Display | ![]() |
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PDB format | ![]() | 89.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 363.3 KB | Display | ![]() |
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Full document | ![]() | 367.6 KB | Display | |
Data in XML | ![]() | 11.2 KB | Display | |
Data in CIF | ![]() | 18.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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: 60193.207 Da / Num. of mol.: 1 / Fragment: C-TERMINAL FRAGMENT / Mutation: E359G 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: 2.45 Å3/Da / Density % sol: 49.71 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 10 Details: 1M AMMONIUM SULPHATE, 0.1M SODIUM PHOSPHATE, pH 10.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K | |||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Details: Steinbacher, S., (1994) Science, 265, 383. | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 287 K |
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Diffraction source | Source: ![]() |
Detector | Type: MARRESEARCH / Detector: AREA DETECTOR / Date: Aug 12, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→8 Å / Num. all: 53301 / Num. obs: 53301 / % possible obs: 98.8 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.3 % / Biso Wilson estimate: 20.4 Å2 / Rmerge(I) obs: 0.071 / Net I/σ(I): 10.3 |
Reflection shell | Resolution: 1.8→1.84 Å / Redundancy: 4.5 % / Rmerge(I) obs: 0.324 / % possible all: 98.3 |
Reflection | *PLUS Num. measured all: 232408 |
Reflection shell | *PLUS % possible obs: 98.3 % |
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Processing
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Refinement | Resolution: 1.8→8 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: ENGH & HUBER
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Refinement step | Cycle: LAST / Resolution: 1.8→8 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 8 Å / σ(F): 0 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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