BRENDA - Enzyme Database show
show all sequences of 2.7.1.127

Interaction of the catalytic domain of inositol 1,4,5-trisphosphate 3-kinase A with inositol phosphate analogues

Poinas, A.; Backers, K.; Riley, A.M.; Mills, S.J.; Moreau, C.; Potter, B.V.; Erneux, C.; Chembiochem 6, 1449-1457 (2005)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
stable expression of the C-terminal catalytic domain 3KA-cat30, comprising residues Ser185-Arg459, as N-terminally His-tagged and S-tagged protein in Escherichia coli strain BL21(DE3)
Rattus norvegicus
Inhibitors
Inhibitors
Commentary
Organism
Structure
(2'S)-1D-1,2-O-[(2'-phosphoryloxy)propane-1',3'-diyl]-myo-inositol 4,5-bisphosphate
synthetic bicyclic inositol trisphosphate S epimer, IC50 is 0.156 mM
Rattus norvegicus
1D-myo-inositol 1,3,4,5-tetrakisphosphate
product inhibition, IC50 is 0.013 mM
Rattus norvegicus
D-2-deoxyinositol 1,3,4,5-tetrakisphosphate
strong inhibition of isozyme A, IC50 is 0.0054 mM
Rattus norvegicus
D-2-deoxyinositol 1,4,5-trisphosphate
strong inhibition of isozyme A, IC50 is 0.0017 mM
Rattus norvegicus
D-3-deoxyinositol 1,4,6-trisphosphate
strong inhibition of isozyme A, IC50 is 0.0014 mM
Rattus norvegicus
D-6-deoxyinositol 1,3,4,5-tetrakisphosphate
strong inhibition of isozyme A, IC50 is 0.0051 mM
Rattus norvegicus
D-myo-inositol 2,4,5-trisphosphate
IC50 is 0.117 mM
Rattus norvegicus
additional information
poor inhibition by adenophostin analogues xylo-furanophostin and furanophostin, by L-myo-inositol 2,4,5-trisphosphate, synthetic bicyclic inositol trisphosphate R epimer, and by epi-1D-myo-inositol 1,3,6-trisphosphate
Rattus norvegicus
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
-
Rattus norvegicus
additional information
assay in presence of Triton X-100 and ethylene glycol bis-(beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid
Rattus norvegicus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + 1D-myo-inositol 1,4,5-trisphosphate
Rattus norvegicus
-
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Rattus norvegicus
-
isozyme A
-
Purification (Commentary)
Commentary
Organism
recombinant N-terminally His-tagged and S-tagged C-terminal catalytic domain 3KA-cat30, comprising residues Ser185-Arg459, from Escherichia coli strain BL21(DE3) by nickel and S-protein affinity chromatography, and gel filtration
Rattus norvegicus
Reaction
Reaction
Commentary
Organism
ATP + 1D-myo-inositol 1,4,5-trisphosphate = ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
catalytic mechanism involving the 3-hydroxygroup of the substrate, substrate recognition
Rattus norvegicus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + 1D-myo-inositol 1,4,5-trisphosphate
-
661488
Rattus norvegicus
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + D-2-deoxy-myo-inositol 1,4,5-trisphosphate
-
661488
Rattus norvegicus
ADP + D-2-deoxy-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Rattus norvegicus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Rattus norvegicus
Cofactor
Cofactor
Commentary
Organism
Structure
ATP
-
Rattus norvegicus
IC50 Value
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
0.0014
-
strong inhibition of isozyme A, IC50 is 0.0014 mM
Rattus norvegicus
D-3-deoxyinositol 1,4,6-trisphosphate
0.0017
-
strong inhibition of isozyme A, IC50 is 0.0017 mM
Rattus norvegicus
D-2-deoxyinositol 1,4,5-trisphosphate
0.0051
-
strong inhibition of isozyme A, IC50 is 0.0051 mM
Rattus norvegicus
D-6-deoxyinositol 1,3,4,5-tetrakisphosphate
0.0054
-
strong inhibition of isozyme A, IC50 is 0.0054 mM
Rattus norvegicus
D-2-deoxyinositol 1,3,4,5-tetrakisphosphate
0.013
-
product inhibition, IC50 is 0.013 mM
Rattus norvegicus
1D-myo-inositol 1,3,4,5-tetrakisphosphate
0.117
-
IC50 is 0.117 mM
Rattus norvegicus
D-myo-inositol 2,4,5-trisphosphate
0.156
-
synthetic bicyclic inositol trisphosphate S epimer, IC50 is 0.156 mM
Rattus norvegicus
(2'S)-1D-1,2-O-[(2'-phosphoryloxy)propane-1',3'-diyl]-myo-inositol 4,5-bisphosphate
Cloned(Commentary) (protein specific)
Commentary
Organism
stable expression of the C-terminal catalytic domain 3KA-cat30, comprising residues Ser185-Arg459, as N-terminally His-tagged and S-tagged protein in Escherichia coli strain BL21(DE3)
Rattus norvegicus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
ATP
-
Rattus norvegicus
IC50 Value (protein specific)
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
0.0014
-
strong inhibition of isozyme A, IC50 is 0.0014 mM
Rattus norvegicus
D-3-deoxyinositol 1,4,6-trisphosphate
0.0017
-
strong inhibition of isozyme A, IC50 is 0.0017 mM
Rattus norvegicus
D-2-deoxyinositol 1,4,5-trisphosphate
0.0051
-
strong inhibition of isozyme A, IC50 is 0.0051 mM
Rattus norvegicus
D-6-deoxyinositol 1,3,4,5-tetrakisphosphate
0.0054
-
strong inhibition of isozyme A, IC50 is 0.0054 mM
Rattus norvegicus
D-2-deoxyinositol 1,3,4,5-tetrakisphosphate
0.013
-
product inhibition, IC50 is 0.013 mM
Rattus norvegicus
1D-myo-inositol 1,3,4,5-tetrakisphosphate
0.117
-
IC50 is 0.117 mM
Rattus norvegicus
D-myo-inositol 2,4,5-trisphosphate
0.156
-
synthetic bicyclic inositol trisphosphate S epimer, IC50 is 0.156 mM
Rattus norvegicus
(2'S)-1D-1,2-O-[(2'-phosphoryloxy)propane-1',3'-diyl]-myo-inositol 4,5-bisphosphate
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
(2'S)-1D-1,2-O-[(2'-phosphoryloxy)propane-1',3'-diyl]-myo-inositol 4,5-bisphosphate
synthetic bicyclic inositol trisphosphate S epimer, IC50 is 0.156 mM
Rattus norvegicus
1D-myo-inositol 1,3,4,5-tetrakisphosphate
product inhibition, IC50 is 0.013 mM
Rattus norvegicus
D-2-deoxyinositol 1,3,4,5-tetrakisphosphate
strong inhibition of isozyme A, IC50 is 0.0054 mM
Rattus norvegicus
D-2-deoxyinositol 1,4,5-trisphosphate
strong inhibition of isozyme A, IC50 is 0.0017 mM
Rattus norvegicus
D-3-deoxyinositol 1,4,6-trisphosphate
strong inhibition of isozyme A, IC50 is 0.0014 mM
Rattus norvegicus
D-6-deoxyinositol 1,3,4,5-tetrakisphosphate
strong inhibition of isozyme A, IC50 is 0.0051 mM
Rattus norvegicus
D-myo-inositol 2,4,5-trisphosphate
IC50 is 0.117 mM
Rattus norvegicus
additional information
poor inhibition by adenophostin analogues xylo-furanophostin and furanophostin, by L-myo-inositol 2,4,5-trisphosphate, synthetic bicyclic inositol trisphosphate R epimer, and by epi-1D-myo-inositol 1,3,6-trisphosphate
Rattus norvegicus
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
-
Rattus norvegicus
additional information
assay in presence of Triton X-100 and ethylene glycol bis-(beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid
Rattus norvegicus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + 1D-myo-inositol 1,4,5-trisphosphate
Rattus norvegicus
-
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant N-terminally His-tagged and S-tagged C-terminal catalytic domain 3KA-cat30, comprising residues Ser185-Arg459, from Escherichia coli strain BL21(DE3) by nickel and S-protein affinity chromatography, and gel filtration
Rattus norvegicus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + 1D-myo-inositol 1,4,5-trisphosphate
-
661488
Rattus norvegicus
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
ATP + D-2-deoxy-myo-inositol 1,4,5-trisphosphate
-
661488
Rattus norvegicus
ADP + D-2-deoxy-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Rattus norvegicus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Rattus norvegicus
Other publictions for EC 2.7.1.127
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)
737402
Erneux
Inositol(1,4,5)P3 3-kinase iso ...
Homo sapiens, Mus musculus, Rattus norvegicus
Adv. Biol. Regul.
60
135-143
2016
6
-
3
-
-
-
-
-
4
6
3
9
-
12
-
4
1
-
-
27
-
-
9
6
-
-
-
-
-
-
-
3
-
-
-
16
-
9
9
-
-
-
-
-
-
-
7
18
3
9
-
-
5
1
-
67
-
-
9
9
-
-
-
-
-
-
-
-
-
13
31
-
-
-
737403
Scoumanne
Specific expression and functi ...
Mus musculus
Adv. Biol. Regul.
62
1-10
2016
-
-
1
-
-
-
-
-
3
-
1
1
-
3
-
-
-
-
-
20
-
-
1
1
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
3
-
1
1
-
-
-
-
-
20
-
-
1
1
-
-
-
-
-
-
-
-
-
2
2
-
-
-
738022
Koester
Inositol-1,4,5-trisphosphate-3 ...
Mus musculus, Mus musculus C57BL/6
Cell. Signal.
28
83-90
2016
-
-
1
-
-
-
-
-
1
2
-
2
-
3
-
-
1
-
-
3
-
-
2
-
-
-
-
-
1
-
-
1
-
-
-
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-
1
1
-
-
-
-
-
-
-
1
2
-
2
-
-
-
1
-
3
-
-
2
-
-
-
-
-
1
-
-
-
-
2
2
-
-
-
739679
Chung
The role of inositol 1,4,5-tri ...
Mus musculus, Mus musculus C57BL/6N
Sci. Rep.
6
23757
2016
-
-
1
-
-
-
-
-
1
2
-
2
-
4
-
-
-
-
-
3
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
1
2
-
2
-
-
-
-
-
3
-
-
2
-
-
-
-
-
-
-
-
-
-
3
3
-
-
-
738088
Ashour
The catalytic domain of inosit ...
Homo sapiens
Cytoskeleton (Hoboken)
72
93-100
2015
-
-
-
-
1
-
-
-
-
1
-
1
-
1
-
-
-
-
-
-
-
-
1
1
1
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
1
1
-
-
-
1
-
-
-
-
1
1
-
-
-
738216
Koenig
Regulation of NGF-driven neuri ...
Rattus norvegicus
FEBS J.
282
2553-2569
2015
-
-
-
-
1
-
-
-
1
1
-
3
-
4
-
-
-
-
-
2
-
-
3
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
3
-
3
-
-
-
-
-
3
3
-
3
-
-
-
-
-
6
-
-
3
-
-
-
-
-
-
-
-
-
-
3
8
-
-
-
737647
Franco-Echevarria
A new calmodulin-binding motif ...
Homo sapiens
Biochem. J.
463
319-328
2014
1
-
-
1
-
-
-
-
-
2
-
1
-
2
-
-
-
-
-
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1
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1
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1
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1
1
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-
-
-
-
-
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2
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
737961
Stygelbout
Inositol trisphosphate 3-kinas ...
Homo sapiens, Mus musculus
Brain
137
537-552
2014
-
-
-
-
-
-
-
-
-
4
-
2
-
4
-
-
-
-
-
4
-
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2
-
-
-
-
-
-
-
-
2
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-
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2
-
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4
-
2
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4
-
-
2
-
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-
-
-
-
-
-
-
-
-
-
-
-
-
737400
Pouillon
-
Inositol 1,4,5-trisphosphate 3 ...
Mus musculus
Adv. Biol. Regul.
53
39-50
2013
-
-
-
-
1
-
-
-
-
2
-
1
-
1
-
-
-
-
-
9
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
2
-
1
-
-
-
-
-
9
-
-
1
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
737593
Schroeder
Identification of a new membra ...
Homo sapiens
Biochem. Biophys. Res. Commun.
439
228-234
2013
-
-
1
-
-
-
4
1
-
1
-
1
-
1
-
-
1
-
-
3
-
-
1
-
1
-
-
-
1
-
-
1
-
-
3
-
-
1
1
-
-
-
3
4
-
1
-
1
-
1
-
-
-
1
-
3
-
-
1
-
1
-
-
-
1
-
-
-
-
1
1
-
-
-
722003
Windhorst
Inositol-1,4,5-trisphosphate 3 ...
Homo sapiens
Cell. Signal.
24
750-757
2012
-
-
-
-
-
-
-
-
-
-
-
-
-
1
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1
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-
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-
-
-
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-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
722753
Lee
Inositol 1,4,5-trisphosphate 3 ...
Rattus norvegicus
J. Biol. Chem.
287
15981-15995
2012
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
-
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1
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-
-
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1
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
722735
Nalaskowski
Human inositol 1,4,5-trisphosp ...
Homo sapiens
J. Biol. Chem.
286
4500-4510
2011
-
-
-
-
-
-
-
-
2
-
-
-
-
2
-
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-
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-
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2
-
-
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-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
722002
Terhzaz
Cell-specific inositol 1,4,5 t ...
Drosophila melanogaster
Cell. Signal.
22
737-748
2010
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
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-
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-
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-
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-
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-
-
-
-
-
-
-
-
-
-
1
2
-
-
-
722381
Marechal
Inositol 1,4,5-trisphosphate 3 ...
Mus musculus
Immunobiology
216
103-109
2010
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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2
1
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2
2
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5
2
2
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2
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4
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6
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1
4
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4
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2
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2
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3
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5
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1
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1
2
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3
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1
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2
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3
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1
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3
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1
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1
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2
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-
-
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1
2
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-
-
-
-
-
2
1
1
1
2
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1
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2
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3
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2
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1
1
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Morris
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Irvine
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