BRENDA - Enzyme Database show
show all sequences of 1.13.11.50

Exploring the cupin-type metal-coordinating signature of acetylacetone dioxygenase Dke1 with site-directed mutagenesis: Catalytic reaction profile and Fe2+ binding stability of Glu-69->Gln mutant

Straganz, G.D.; Egger, S.; Aquino, G.; DAuria, S.; Nidetzky, B.; J. Mol. Catal. B 39, 171-178 (2006)
No PubMed abstract available

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expressed in Escherichia coli BL21(DE3) cells
Acinetobacter johnsonii
Engineering
Amino acid exchange
Commentary
Organism
E69Q
lower thermal stability of beta-sheet secondary structure, half catalytic center activity and remarkably silent difference in apparent substrate binding compared to the wild type enzyme
Acinetobacter johnsonii
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.006
-
Pentane-2,4-dione
wild type enzyme, using 0.2 mM pentane-2,4-dione in 20 mM Tris/HCl buffer at pH 7.5 and 25°C
Acinetobacter johnsonii
0.0065
-
Pentane-2,4-dione
mutant enzyme E69Q, using 0.2 mM pentane-2,4-dione in 20 mM Tris/HCl buffer at pH 7.5 and 25°C
Acinetobacter johnsonii
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe2+
Fe2+-dependent enzyme, 1 molecule per subunit
Acinetobacter johnsonii
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
18000
-
SDS-PAGE, Strep-tagged full length enzyme
Acinetobacter johnsonii
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Acinetobacter johnsonii
-
-
-
Purification (Commentary)
Commentary
Organism
affinity column chromatography
Acinetobacter johnsonii
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1,1,1-trifluoro-pentane-2,4-dione + O2
-
675466
Acinetobacter johnsonii
?
-
-
-
?
pentane-2,4-dione + O2
-
675466
Acinetobacter johnsonii
acetate + 2-oxopropanal
-
-
-
?
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.0043
-
1,1,1-trifluoro-pentane-2,4-dione
native enzyme, using 0.09 mM 1,1,1-trifluoro-pentane-2,4-dione in 20 mM Tris/HCl buffer at pH 7.5 and 25°C
Acinetobacter johnsonii
3.6
-
Pentane-2,4-dione
mutant enzyme E69Q, using 0.2 mM pentane-2,4-dione in 20 mM Tris/HCl buffer at pH 7.5 and 25°C
Acinetobacter johnsonii
6.6
-
Pentane-2,4-dione
wild type enzyme, using 0.2 mM pentane-2,4-dione in 20 mM Tris/HCl buffer at pH 7.5 and 25°C
Acinetobacter johnsonii
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
-
Acinetobacter johnsonii
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli BL21(DE3) cells
Acinetobacter johnsonii
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
E69Q
lower thermal stability of beta-sheet secondary structure, half catalytic center activity and remarkably silent difference in apparent substrate binding compared to the wild type enzyme
Acinetobacter johnsonii
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.006
-
Pentane-2,4-dione
wild type enzyme, using 0.2 mM pentane-2,4-dione in 20 mM Tris/HCl buffer at pH 7.5 and 25°C
Acinetobacter johnsonii
0.0065
-
Pentane-2,4-dione
mutant enzyme E69Q, using 0.2 mM pentane-2,4-dione in 20 mM Tris/HCl buffer at pH 7.5 and 25°C
Acinetobacter johnsonii
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
Fe2+-dependent enzyme, 1 molecule per subunit
Acinetobacter johnsonii
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
18000
-
SDS-PAGE, Strep-tagged full length enzyme
Acinetobacter johnsonii
Purification (Commentary) (protein specific)
Commentary
Organism
affinity column chromatography
Acinetobacter johnsonii
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1,1,1-trifluoro-pentane-2,4-dione + O2
-
675466
Acinetobacter johnsonii
?
-
-
-
?
pentane-2,4-dione + O2
-
675466
Acinetobacter johnsonii
acetate + 2-oxopropanal
-
-
-
?
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.0043
-
1,1,1-trifluoro-pentane-2,4-dione
native enzyme, using 0.09 mM 1,1,1-trifluoro-pentane-2,4-dione in 20 mM Tris/HCl buffer at pH 7.5 and 25°C
Acinetobacter johnsonii
3.6
-
Pentane-2,4-dione
mutant enzyme E69Q, using 0.2 mM pentane-2,4-dione in 20 mM Tris/HCl buffer at pH 7.5 and 25°C
Acinetobacter johnsonii
6.6
-
Pentane-2,4-dione
wild type enzyme, using 0.2 mM pentane-2,4-dione in 20 mM Tris/HCl buffer at pH 7.5 and 25°C
Acinetobacter johnsonii
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
-
Acinetobacter johnsonii
Other publictions for EC 1.13.11.50
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
742322
Brkic
-
Insight of the iron binding a ...
Acinetobacter johnsonii
Croat. Chem. Acta
88
297-306
2015
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1
3
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1
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1
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3
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1
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725553
Brkic
Dke1--structure, dynamics, and ...
Acinetobacter johnsonii
J. Biol. Inorg. Chem.
17
801-815
2012
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-
1
-
4
-
-
1
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2
-
1
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1
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1
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2
1
1
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10
1
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1
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4
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-
1
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2
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1
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1
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2
1
1
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10
1
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2
2
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725198
Diebold
Spectroscopic and computationa ...
Acinetobacter johnsonii
J. Am. Chem. Soc.
133
15979-15991
2011
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1
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1
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3
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1
1
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711258
Diebold
The three-his triad in Dke1: c ...
Acinetobacter johnsonii
Biochemistry
49
6945-6952
2010
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2
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1
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1
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1
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2
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711267
Straganz
Kinetic and CD/MCD spectroscop ...
Acinetobacter johnsonii
Biochemistry
49
996-1004
2010
-
-
-
-
9
-
-
1
-
1
-
1
-
1
-
-
-
-
-
-
-
-
3
-
1
-
-
10
1
1
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-
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9
-
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-
1
-
1
-
1
-
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-
-
-
-
-
3
-
1
-
-
10
1
1
-
-
-
-
-
-
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-
696107
Leitgeb
Biochemical characterization a ...
Acinetobacter johnsonii
Biochem. J.
418
403-411
2009
-
-
1
-
8
-
6
-
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6
1
1
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2
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-
1
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-
1
-
4
1
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1
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1
1
-
8
-
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6
-
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6
1
1
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-
1
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1
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4
1
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-
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-
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-
675466
Straganz
-
Exploring the cupin-type metal ...
Acinetobacter johnsonii
J. Mol. Catal. B
39
171-178
2006
-
-
1
-
1
-
-
2
-
1
1
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-
1
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1
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2
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3
1
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1
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1
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2
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1
1
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2
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3
1
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-
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-
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-
657614
Hofer
Fast determination of operatio ...
Acinetobacter johnsonii
Appl. Microbiol. Biotechnol.
1
1-12
2005
-
1
1
-
-
1
-
2
1
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1
-
1
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-
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-
-
1
1
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1
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1
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2
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1
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1
1
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1
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2
1
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1
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1
1
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1
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1
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2
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1
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-
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657866
Grogan
Emergent mechanistic diversity ...
Acinetobacter johnsonii
Biochem. J.
388
721-730
2005
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-
1
1
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-
-
1
-
1
1
1
-
1
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1
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1
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6
1
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1
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1
-
1
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1
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1
1
1
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1
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6
1
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1
-
-
-
-
-
-
-
-
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-
671683
Straganz
-
Integrated approach for produc ...
Acinetobacter johnsonii
Biocatal. Biotransform.
23
261-269
2005
-
-
1
-
-
-
-
3
-
1
4
-
-
1
-
-
1
-
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1
1
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-
3
-
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1
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3
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1
4
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1
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1
1
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3
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674150
Straganz
Reaction coordinate analysis f ...
Acinetobacter johnsonii
J. Am. Chem. Soc.
127
12306-12314
2005
-
-
-
-
-
-
-
4
-
1
2
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3
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4
1
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4
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4
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1
2
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4
1
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4
-
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-
636327
Straganz
Acetylacetone-cleaving enzyme ...
Acinetobacter johnsonii
Biochem. J.
369
573-581
2003
-
-
1
-
-
-
5
1
-
1
1
1
-
3
-
-
1
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11
1
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1
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1
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5
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1
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1
1
1
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1
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11
1
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-
-
-
1
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-
-
-
-
-
-
-
636328
Straganz
A novel beta-diketone-cleaving ...
Acinetobacter johnsonii
Biochem. Biophys. Res. Commun.
297
232-236
2002
-
-
-
-
-
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-
2
1
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1
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1
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2
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5
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2
1
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1
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2
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5
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