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- PDB-2eql: CRYSTALLOGRAPHIC STUDIES OF A CALCIUM BINDING LYSOZYME FROM EQUIN... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2eql | ||||||
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Title | CRYSTALLOGRAPHIC STUDIES OF A CALCIUM BINDING LYSOZYME FROM EQUINE MILK AT 2.5 ANGSTROMS RESOLUTION | ||||||
![]() | HORSE MILK LYSOZYME | ||||||
![]() | HYDROLASE(O-GLYCOSYL) | ||||||
Function / homology | ![]() lysozyme / lysozyme activity / killing of cells of another organism / defense response to bacterium / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Tsuge, H. / Ago, H. / Miyano, M. | ||||||
![]() | ![]() Title: Crystallographic studies of a calcium binding lysozyme from equine milk at 2.5 A resolution. Authors: Tsuge, H. / Ago, H. / Noma, M. / Nitta, K. / Sugai, S. / Miyano, M. #1: ![]() Title: A Structural Study of Calcium-Binding Equine Lysozyme by Two-Dimensional 1H-NMR Authors: Tsuge, H. / Koseki, K. / Miyano, M. / Shimazaki, K. / Chuman, T. / Matsumoto, T. / Noma, M. / Nitta, K. / Sugai, S. #2: ![]() Title: Calcium-Binding Lysozymes Authors: Nitta, K. / Tsuge, H. / Shimazaki, K. / Sugai, S. #3: ![]() Title: The Calcium-Binding Property of Equine Lysozyme Authors: Nitta, K. / Tsuge, H. / Sugai, S. / Shimazaki, K. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 36.2 KB | Display | ![]() |
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PDB format | ![]() | 25.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 411.5 KB | Display | ![]() |
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Full document | ![]() | 420 KB | Display | |
Data in XML | ![]() | 7.9 KB | Display | |
Data in CIF | ![]() | 9.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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: 14673.627 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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Has protein modification | Y |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.04 Å3/Da / Density % sol: 39.71 % | ||||||||||||||||||||
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Crystal grow | *PLUS pH: 5.6 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 2.3 Å / Num. obs: 4842 / Rmerge(I) obs: 0.039 |
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Processing
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Refinement | Resolution: 2.5→7 Å / σ(F): 3 /
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Refinement step | Cycle: LAST / Resolution: 2.5→7 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.234 / Rfactor Rwork: 0.234 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 4.08 |