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- PDB-1qth: THE INTRODUCTION OF STRAIN AND ITS EFFECTS ON THE STRUCTURE AND S... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1qth | ||||||
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Title | THE INTRODUCTION OF STRAIN AND ITS EFFECTS ON THE STRUCTURE AND STABILITY OF T4 LYSOZYME | ||||||
![]() | LYSOZYME | ||||||
![]() | HYDROLASE / STRAIN / STABILITY / MUTANT / T4 LYSOZYME | ||||||
Function / homology | ![]() viral release from host cell by cytolysis / peptidoglycan catabolic process / cell wall macromolecule catabolic process / lysozyme / lysozyme activity / host cell cytoplasm / defense response to bacterium Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Liu, R. / Baase, W.A. / Matthews, B.W. | ||||||
![]() | ![]() Title: The introduction of strain and its effects on the structure and stability of T4 lysozyme. Authors: Liu, R. / Baase, W.A. / Matthews, B.W. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 77.3 KB | Display | ![]() |
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PDB format | ![]() | 58.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 423.5 KB | Display | ![]() |
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Full document | ![]() | 464 KB | Display | |
Data in XML | ![]() | 20 KB | Display | |
Data in CIF | ![]() | 27.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1qs5C ![]() 1qs9C ![]() 1qsbC ![]() 1qtbC ![]() 1qtcC ![]() 1qtdC C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Details | The biological assembly is a dimer constructed from chain A a symmetry partner generated by the noncrystallographic two-fold |
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Components
#1: Protein | Mass: 18688.480 Da / Num. of mol.: 2 / Mutation: C54T, C97A, A98M 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: 2.26 Å3/Da / Density % sol: 45.51 % | |||||||||||||||||||||||||
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 7.4 Details: PEG3.4K, magnesium chloride, Hepes, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 277K | |||||||||||||||||||||||||
Crystal grow | *PLUS Method: unknown | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: Oct 29, 1997 |
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→46.4 Å / Num. all: 25769 / Num. obs: 23171 / % possible obs: 89.92 % / Observed criterion σ(I): 0 / Biso Wilson estimate: 26.4 Å2 / Rmerge(I) obs: 0.048 |
Reflection shell | Resolution: 1.9→2 Å / Rmerge(I) obs: 0.459 / Num. unique all: 3677 / % possible all: 86.4 |
Reflection | *PLUS % possible obs: 85 % |
Reflection shell | *PLUS % possible obs: 86.4 % |
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Processing
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Refinement | Resolution: 1.9→20 Å / Stereochemistry target values: TNT PROTGEO
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Refinement step | Cycle: LAST / Resolution: 1.9→20 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Classification: refinement | ||||||||||||||||||
Refine LS restraints | *PLUS
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