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- PDB-3c8r: Contributions of all 20 amino acids at site 96 to stability and s... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3c8r | |||||||||
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Title | Contributions of all 20 amino acids at site 96 to stability and structure of T4 lysozyme | |||||||||
![]() | Lysozyme![]() | |||||||||
![]() | ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() | |||||||||
Function / homology | ![]() viral release from host cell by cytolysis / peptidoglycan catabolic process / cell wall macromolecule catabolic process / ![]() ![]() Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() | |||||||||
![]() | Mooers, B.H.M. | |||||||||
![]() | ![]() Title: Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme. Authors: Mooers, B.H. / Baase, W.A. / Wray, J.W. / Matthews, B.W. #1: ![]() Title: Evaluation at atomic resolution of the role of strain in destabilizing the temperature-sensitive T4 lysozyme mutant Arg 96 --> His. Authors: Mooers, B.H. / Tronrud, D.E. / 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 | ![]() | 46.7 KB | Display | ![]() |
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PDB format | ![]() | 32 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 3c7wC ![]() 3c7yC ![]() 3c7zC ![]() 3c80C ![]() 3c81C ![]() 3c82C ![]() 3c83C ![]() 3c8qC ![]() 3c8sC ![]() 3cdoC ![]() 3cdqC ![]() 3cdrC ![]() 3cdtC ![]() 3cdvC ![]() 3fi5C ![]() 1l63S S: Starting model for refinement 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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Unit cell |
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Components
#1: Protein | ![]() Mass: 18562.324 Da / Num. of mol.: 1 / Mutation: R96G Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() | ||||
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#2: Chemical | ![]() #3: Chemical | ChemComp-BME / | ![]() #4: Water | ChemComp-HOH / | ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.84 Å3/Da / Density % sol: 56.67 % |
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Crystal grow![]() | pH: 6.7 Details: 2M NA/K PHOSPHATE 50 MM REDUCED BME 50 MM OXIDIZED BME, PH 6.7, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 276K, PH 6.70 |
-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU / Detector: IMAGE PLATE / Date: Jun 1, 1998 |
Radiation | Monochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 1.8→30.5 Å / Num. obs: 18258 / % possible obs: 92.2 % / Observed criterion σ(I): 2 / Redundancy: 5 % / Biso Wilson estimate: 22.58 Å2 / Rmerge(I) obs: 0.067 / Rsym value: 0.067 / Net I/σ(I): 21.8 |
Reflection shell | Resolution: 1.8→1.9 Å / Redundancy: 3.5 % / Rmerge(I) obs: 0.322 / Mean I/σ(I) obs: 4.5 / Rsym value: 0.322 / % possible all: 96.2 |
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Processing
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Refinement | Method to determine structure![]() ![]() Starting model: 1L63 Resolution: 1.8→30.5 Å / Isotropic thermal model: ISOTROPIC / Cross valid method: FWT-FMUT MAPS / σ(F): 0 / Stereochemistry target values: TNT
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Solvent computation | Bsol: 165.22 Å2 / ksol: 0.84 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→30.5 Å
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Refine LS restraints |
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