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- PDB-1agy: The 1.15 angstrom refined structure of fusarium solani pisi cutinase -
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Open data
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Basic information
Entry | Database: PDB / ID: 1agy | ||||||
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Title | The 1.15 angstrom refined structure of fusarium solani pisi cutinase | ||||||
![]() | CUTINASE | ||||||
![]() | SERINE ESTERASE / HYDROLASE / GLYCOPROTEIN | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Nicolas, A. / Martinez, C. / Cambillau, C. | ||||||
![]() | ![]() Title: Atomic resolution (1.0 A) crystal structure of Fusarium solani cutinase: stereochemical analysis. Authors: Longhi, S. / Czjzek, M. / Lamzin, V. / Nicolas, A. / Cambillau, C. #1: ![]() Title: Fusarium Solani Cutinase is a Lipolytic Enzyme with a Catalytic Serine Accessible to Solvent Authors: Martinez, C. / De Geus, P. / Lauwereys, M. / Matthyssens, G. / Cambillau, C. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 105 KB | Display | ![]() |
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PDB format | ![]() | 84 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 415.7 KB | Display | ![]() |
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Full document | ![]() | 416.7 KB | Display | |
Data in XML | ![]() | 12.6 KB | Display | |
Data in CIF | ![]() | 19.1 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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Unit cell |
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Components
#1: Protein | Mass: 20828.400 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P00590, Hydrolases; Acting on ester bonds; Carboxylic-ester hydrolases |
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#2: Water | ChemComp-HOH / |
Sequence details | REGARDING IDENTITY OF RESIDUE ARG 32, UPON QUESTIONING OF TOMMY CARSTENSEN, AUTHORS SONIA LONGHI ...REGARDING IDENTITY OF RESIDUE ARG 32, UPON QUESTIONIN |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.98 Å3/Da / Density % sol: 38 % | ||||||||||||||||||||
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Crystal grow | pH: 7 Details: PROTEIN WAS CRYSTALLIZED FROM 15 - 20% PEG 6000, 0.1 M HEPES, PH 7.0 | ||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / Method: vapor diffusion, hanging drop / Details: Abergel, C., (1990) J. Mol. Biol., 215, 215. | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 288 K |
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Diffraction source | Source: ![]() |
Detector | Type: NICOLET / Detector: AREA DETECTOR / Date: Jan 1, 1993 / Details: NO |
Radiation | Monochromator: SI(111) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.15→20 Å / Num. obs: 60972 / % possible obs: 95.22 % / Observed criterion σ(I): 0 / Redundancy: 4.09 % / Biso Wilson estimate: 8.43 Å2 / Rmerge(I) obs: 0.01 / Rsym value: 0.01 / Net I/σ(I): 27.46 |
Reflection shell | Resolution: 1.15→1.2 Å / Redundancy: 2 % / Rmerge(I) obs: 0.03 / Mean I/σ(I) obs: 3.21 / Rsym value: 0.03 / % possible all: 84.2 |
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Processing
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Refinement | Method to determine structure: RESOLUTION EXTENSION Starting model: CUTINASE STRUCTURE AT 1.6 ANGSTROM RESOLUTION Resolution: 1.15→20 Å / Rfactor Rfree error: 0 / Data cutoff high absF: 1.15 / Data cutoff low absF: 6 / σ(F): 0
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Displacement parameters | Biso mean: 13.54 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati sigma a obs: 0.01 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.15→20 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.15→1.2 Å / Rfactor Rfree error: 0 / Total num. of bins used: 8
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Xplor file |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rfree: 0.4 / Rfactor Rwork: 0.4 |