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- PDB-1lhl: ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A SCANNING ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1lhl | ||||||
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Title | ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A SCANNING CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE ANALYSIS OF PROLINE MUTANTS | ||||||
![]() | HUMAN LYSOZYME | ||||||
![]() | HYDROLASE(O-GLYCOSYL) | ||||||
Function / homology | ![]() antimicrobial humoral response / Antimicrobial peptides / specific granule lumen / azurophil granule lumen / tertiary granule lumen / lysozyme / lysozyme activity / defense response to Gram-negative bacterium / killing of cells of another organism / defense response to Gram-positive bacterium ...antimicrobial humoral response / Antimicrobial peptides / specific granule lumen / azurophil granule lumen / tertiary granule lumen / lysozyme / lysozyme activity / defense response to Gram-negative bacterium / killing of cells of another organism / defense response to Gram-positive bacterium / defense response to bacterium / inflammatory response / Amyloid fiber formation / Neutrophil degranulation / extracellular space / extracellular exosome / extracellular region / identical protein binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Inaka, K. / Matsushima, M. / Herning, T. / Kuroki, R. / Yutani, K. / Kikuchi, M. | ||||||
![]() | ![]() Title: Role of proline residues in human lysozyme stability: a scanning calorimetric study combined with X-ray structure analysis of proline mutants. Authors: Herning, T. / Yutani, K. / Inaka, K. / Kuroki, R. / Matsushima, M. / Kikuchi, M. #1: ![]() Title: Crystal Structures of the Apo-and Holomutant Human Lysozymes with an Introduced Ca Binding Site Authors: Inaka, K. / Kuroki, R. / Kikuchi, M. / Matsushima, M. #2: ![]() Title: Effects of Proline Mutations on the Unfolding and Refolding of Human Lysozyme: The Slow Refolding Kinetic Phase Does not Result from Proline Cis-Trans Isomerization Authors: Herning, T. / Yutani, K. / Taniyama, Y. / Kikuchi, M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 35.3 KB | Display | ![]() |
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PDB format | ![]() | 27.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related 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: 14746.730 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.98 Å3/Da / Density % sol: 37.92 % | ||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 13 ℃ / pH: 5.8 / Method: unknown | ||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 1.8 Å / Num. obs: 10426 / % possible obs: 91.4 % / Num. measured all: 38695 / Rmerge(I) obs: 0.0564 |
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Processing
Software | Name: PROLSQ / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 1.8→5 Å /
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Refinement step | Cycle: LAST / Resolution: 1.8→5 Å
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Refine LS restraints |
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Software | *PLUS Name: PROLSQ / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 1.8 Å / Lowest resolution: 5 Å / Num. reflection obs: 10426 / Rfactor obs: 0.154 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Highest resolution: 1.8 Å / Lowest resolution: 1.89 Å / Rfactor obs: 0.185 |