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- PDB-3c81: Mutant K85A of T4 lysozyme in wildtype background at room temperature -
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Open data
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Basic information
Entry | Database: PDB / ID: 3c81 | ||||||
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Title | Mutant K85A of T4 lysozyme in wildtype background at room temperature | ||||||
![]() | 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 | ![]() | 48.1 KB | Display | ![]() |
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PDB format | ![]() | 33.2 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 ![]() 3c82C ![]() 3c83C ![]() 3c8qC ![]() 3c8rC ![]() 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: 18604.365 Da / Num. of mol.: 1 / Mutation: K85A 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: 2.81 Å3/Da / Density % sol: 56.18 % |
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Crystal grow![]() | pH: 6.7 Details: 2 M NA/K PHOSPHATE PH 6.7 550 MM NACL 50 MM REDUCED BME, 50 MM OXIDIZED BME , VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K, pH 6.70 |
-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ![]() |
Detector | Type: SDMS / Detector: AREA DETECTOR / Date: Jun 24, 1998 / Details: MIRRORS |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 1.85→22.22 Å / Num. obs: 17772 / % possible obs: 93 % / Observed criterion σ(I): 0 / Rmerge(I) obs: 0.08 |
Reflection shell | Resolution: 1.85→1.94 Å / % possible all: 85.8 |
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Processing
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Refinement | Method to determine structure![]() ![]() Starting model: 1L63 Resolution: 1.85→22.22 Å / Cross valid method: FWT-FMUT DIFFERENCE MAPS / σ(F): 0 / Stereochemistry target values: TNT5G / Details: NATIVE K =1.7287, OVERALL = 0.0
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Solvent computation | Bsol: 623.72 Å2 / ksol: 0.9 e/Å3 | ||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.85→22.22 Å
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Refine LS restraints |
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