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Open data
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Basic information
Entry | Database: PDB / ID: 1jmy | ||||||
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Title | Truncated Recombinant Human Bile Salt Stimulated Lipase | ||||||
![]() | BILE-SALT-ACTIVATED LIPASE | ||||||
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Function / homology | ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Moore, S.A. / Kingston, R.L. / Loomes, K.M. / Hernell, O. / Blackberg, L. / Baker, H.M. / Baker, E.N. | ||||||
![]() | ![]() Title: The structure of truncated recombinant human bile salt-stimulated lipase reveals bile salt-independent conformational flexibility at the active-site loop and provides insights into heparin binding. Authors: Moore, S.A. / Kingston, R.L. / Loomes, K.M. / Hernell, O. / Blackberg, L. / Baker, H.M. / Baker, E.N. #1: ![]() Title: Crystallization and preliminary X-ray analysis of native and recombinant human bile-salt dependent lipase: strategies for improvement of diffraction quality | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 111.4 KB | Display | ![]() |
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PDB format | ![]() | 86.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-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: 57479.176 Da / Num. of mol.: 1 / Fragment: 1-518 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-SO4 / ![]() |
#3: Water | ChemComp-HOH / ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.37 Å3/Da / Density % sol: 48.12 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow![]() | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.7 Details: PEG-6000, PIPES/KOH, Glycerol, pH 6.7, VAPOR DIFFUSION, HANGING DROP, temperature 293K | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 3 Details: Kingston, R.L., (2000) Acta Crystallogr., Sect.D, 56, 478. | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 113 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: 1996 / Details: Graphite Monochromator |
Radiation | Monochromator: Graphite plus 0.1 mm collimator / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 2.6→100 Å / Num. all: 17429 / Num. obs: 15613 / % possible obs: 89.6 % / Redundancy: 3.2 % / Biso Wilson estimate: 45 Å2 / Rmerge(I) obs: 0.1 / Rsym value: 0.1 / Net I/σ(I): 6.3 |
Reflection shell | Highest resolution: 2.6 Å / Redundancy: 2.5 % / Rmerge(I) obs: 0.35 / Mean I/σ(I) obs: 2 / Rsym value: 0.35 / % possible all: 74.9 |
Reflection | *PLUS Lowest resolution: 100 Å / % possible obs: 90.7 % / Rmerge(I) obs: 0.1 |
Reflection shell | *PLUS % possible obs: 74.9 % / Rmerge(I) obs: 0.35 |
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Processing
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Refinement | Method to determine structure![]() ![]() Starting model: Truncated core of acetylcholinesterase Resolution: 2.6→100 Å / Isotropic thermal model: Tightly restrained individual B's / Cross valid method: Freer / σ(F): 0 / Stereochemistry target values: Engh and Huber
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Displacement parameters | Biso mean: 45 Å2
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Refinement step | Cycle: LAST / Resolution: 2.6→100 Å
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Refine LS restraints |
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Software | *PLUS Name: CNS / Version: 1 / Classification: refinement | |||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 100 Å / σ(F): 0 / % reflection Rfree: 10 % / Rfactor obs: 0.236 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 45 Å2 | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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