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- PDB-173l: PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 173l | ||||||
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Title | PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME | ||||||
![]() | T4 LYSOZYME | ||||||
![]() | HYDROLASE (O-GLYCOSYL) | ||||||
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 | ![]() | ||||||
![]() | Xiong, X.-P. / Zhang, X.-J. / Sun, D. / Matthews, B.W. | ||||||
![]() | ![]() Title: Protein flexibility and adaptability seen in 25 crystal forms of T4 lysozyme. Authors: Zhang, X.J. / Wozniak, J.A. / Matthews, B.W. #1: ![]() Title: Structure of Bacteriophage T4 Lysozyme Refined at 1.7 Angstroms Resolution Authors: Weaver, L.H. / 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 | ![]() | 46.4 KB | Display | ![]() |
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PDB format | ![]() | 32.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 431.1 KB | Display | ![]() |
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Full document | ![]() | 436.9 KB | Display | |
Data in XML | ![]() | 10.4 KB | Display | |
Data in CIF | ![]() | 13.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 167lC ![]() 168lC ![]() 169lC ![]() 170lC ![]() 171lC ![]() 172lC ![]() 174lC ![]() 175lC ![]() 176lC ![]() 177lC ![]() 178lC ![]() 180lC 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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Unit cell |
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Atom site foot note | 1: ASN 163 - LEU 164 OMEGA = 9.44 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION |
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Components
#1: Protein | Mass: 18634.188 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() | ||
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#2: Chemical | #3: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.39 Å3/Da / Density % sol: 48.52 % | ||||||||||||||||||||||||||||||
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Crystal | *PLUS Density % sol: 48 % | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7.1 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Ambient pressure: 101 kPa / Mean temperature: 298 K |
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Diffraction source | Source: rotating-anode X-ray tube / Type: RIGAKU RU200 / Target: Cu |
Detector | Type: AREA DETECTOR / Detector: AREA DETECTOR / Details: Xuong-Hamlin |
Radiation | Monochromator: graphite / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray / Wavelength: 1.5418 Å |
Radiation wavelength | Relative weight: 1 |
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Processing
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Refinement | Resolution: 1.7→20 Å / Rfactor obs: 0.183 | ||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.7→20 Å
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Refine LS restraints |
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