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- PDB-1dte: THE STRUCTURAL ORIGINS OF INTERFACIAL ACTIVATION IN THERMOMYCES (... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1dte | ||||||
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Title | THE STRUCTURAL ORIGINS OF INTERFACIAL ACTIVATION IN THERMOMYCES (HUMICOLA) LANUGINOSA LIPASE | ||||||
![]() | LIPASE | ||||||
![]() | HYDROLASE / lipase / thermomyces linuginosa / interfacial activation / alpa-beta structure | ||||||
Function / homology | ![]() triacylglycerol lipase / triacylglycerol lipase activity / lipid catabolic process Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Brozozowski, A.M. / Savage, H. | ||||||
![]() | ![]() Title: Structural origins of the interfacial activation in Thermomyces (Humicola) lanuginosa lipase. Authors: Brzozowski, A.M. / Savage, H. / Verma, C.S. / Turkenburg, J.P. / Lawson, D.M. / Svendsen, A. / Patkar, S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 116.1 KB | Display | ![]() |
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PDB format | ![]() | 95 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 381.3 KB | Display | ![]() |
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Full document | ![]() | 415.3 KB | Display | |
Data in XML | ![]() | 16.1 KB | Display | |
Data in CIF | ![]() | 24.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Details | The biological assembly is a monomer |
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Components
#1: Protein | Mass: 29342.484 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.41 Å3/Da / Density % sol: 48.97 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | Method: vapor diffusion, hanging drop / pH: 8.1 Details: PEG 5000, magnesium chloride, c8e5, pH 8.1, VAPOR DIFFUSION, HANGING DROP, temperature 110K | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: unknown | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 110 K |
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Diffraction source | Source: ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jun 1, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.35→20 Å / Num. all: 65466 / Num. obs: 24301 / % possible obs: 89.2 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 2.7 % / Biso Wilson estimate: 35 Å2 / Rmerge(I) obs: 0.067 / Net I/σ(I): 5 |
Reflection shell | Resolution: 2.35→2.39 Å / Redundancy: 2 % / Rmerge(I) obs: 0.116 / Num. unique all: 21108 / % possible all: 49.9 |
Reflection | *PLUS Highest resolution: 2.4 Å / Num. obs: 91415 / % possible obs: 98.4 % / Redundancy: 2.75 % / Rmerge(I) obs: 0.062 |
Reflection shell | *PLUS Highest resolution: 2.4 Å / Lowest resolution: 2.44 Å / % possible obs: 98.6 % / Redundancy: 2.75 % / Rmerge(I) obs: 0.424 / Mean I/σ(I) obs: 8.31 |
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Processing
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Refinement | Resolution: 2.35→20 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber Details: data was twinned and detwinned. Thus, probably the reason for higher than normal R-factors.
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Refinement step | Cycle: LAST / Resolution: 2.35→20 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | |||||||||||||||||||||||||
Refinement | *PLUS Rfactor Rfree: 0.315 / Rfactor Rwork: 0.244 / Highest resolution: 2.4 Å | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 61 Å2 | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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