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- PDB-1vni: CHLOROPEROXIDASE FROM THE FUNGUS CURVULARIA INAEQUALIS: RECOMBINA... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1vni | ||||||
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Title | CHLOROPEROXIDASE FROM THE FUNGUS CURVULARIA INAEQUALIS: RECOMBINANT HOLO-CHLOROPEROXIDASE | ||||||
![]() | VANADIUM CHLOROPEROXIDASE | ||||||
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Function / homology | ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Macedo-Ribeiro, S. / Messerschmidt, A. | ||||||
![]() | ![]() Title: X-ray crystal structures of active site mutants of the vanadium-containing chloroperoxidase from the fungus Curvularia inaequalis. Authors: Macedo-Ribeiro, S. / Hemrika, W. / Renirie, R. / Wever, R. / Messerschmidt, A. #1: ![]() Title: X-Ray Structure of a Vanadium-Containing Enzyme: Chloroperoxidase from the Fungus Curvularia Inaequalis Authors: Messerschmidt, A. / Wever, R. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 127 KB | Display | ![]() |
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PDB format | ![]() | 98.6 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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1 |
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 67627.445 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-VO4 / ![]() |
#3: Water | ChemComp-HOH / ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.79 Å3/Da / Density % sol: 56 % | ||||||||||||||||||||||||||||||||||||||||
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Crystal grow![]() | pH: 8 / Details: pH 8.0 | ||||||||||||||||||||||||||||||||||||||||
Crystal | *PLUS | ||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / pH: 7.5 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 287 K |
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Diffraction source | Wavelength: 1.5418 |
Detector | Date: Jun 1, 1998 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 2.15→15 Å / Num. obs: 39327 / % possible obs: 99.2 % / Observed criterion σ(I): 0 / Redundancy: 2.7 % / Rmerge(I) obs: 0.07 / Net I/σ(I): 6.2 |
Reflection shell | Resolution: 2.15→2.27 Å / Rmerge(I) obs: 0.28 / Mean I/σ(I) obs: 2.4 / % possible all: 95.6 |
Reflection | *PLUS Num. measured all: 164218 / Rmerge(I) obs: 0.069 |
Reflection shell | *PLUS % possible obs: 95.6 % / Rmerge(I) obs: 0.278 |
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Processing
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Refinement | Method to determine structure![]()
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Displacement parameters | Biso mean: 31.22 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.23 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.15→8 Å
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Refine LS restraints |
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Refinement | *PLUS Rfactor obs: 0.181 / Rfactor Rfree![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | *PLUS Highest resolution: 2.15 Å / Lowest resolution: 2.27 Å / Rfactor Rfree: 0.243 / Rfactor obs: 0.258 |