BRENDA - Enzyme Database
show all sequences of 3.2.1.145

An exo-beta-(1->3)-D-galactanase from Streptomyces sp. provides insights into type II arabinogalactan structure

Ling, N.; Lee, J.; Ellis, M.; Liao, M.; Mau, S.; Guest, D.; Janssen, P.; Kovac, P.; Bacic, A.; Pettolino, F.; Carbohydr. Res. 352, 70-81 (2012)

Data extracted from this reference:

Application
Application
Commentary
Organism
analysis
the activity of the enzyme is well suited for the study of type II galactan structures and provides an important tool for the investigation of the biological role of arabinogalactan proteins in plants; the activity of the enzyme is well suited for the study of type II galactan structures and provides an important tool for the investigation of the biological role of arabinogalactan proteins in plants
Streptomyces sp.
Cloned(Commentary)
Cloned (Commentary)
Organism
SGalase1, DNA and amino acid equence determination and analysis, sequence comparison, phylogenetic analysis and tree; SGalase2, DNA and amino acid equence determination and analysis, sequence comparison, phylogenetic analysis and tree
Streptomyces sp.
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
45000
-
x * 45000, about, SDS-PAGE, x * 48200, about, sequence calculation
Streptomyces sp.
47900
-
x * 47900, about, sequence calculation
Streptomyces sp.
48200
-
x * 45000, about, SDS-PAGE, x * 48200, about, sequence calculation
Streptomyces sp.
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
additional information
Streptomyces sp.
the enzyme specifically cleaves the beta-(1->3)-D-galactan backbone of arabinogalactan-proteins
?
-
-
-
additional information
Streptomyces sp. 19(2012)
the enzyme specifically cleaves the beta-(1->3)-D-galactan backbone of arabinogalactan-proteins
?
-
-
-
Organism
Organism
UniProt
Commentary
Textmining
Streptomyces sp.
I0B0S9
SGalase1; isolated from culture filtrates of soil
-
Streptomyces sp.
I0B0T0
SGalase2; isolated from culture filtrates of soil
-
Streptomyces sp. 19(2012)
I0B0S9
SGalase1; isolated from culture filtrates of soil
-
Streptomyces sp. 19(2012)
I0B0T0
SGalase2; isolated from culture filtrates of soil
-
Purification (Commentary)
Purification (Commentary)
Organism
native enzyme 1.8fold from culture supernatant by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration; native enzyme 1.8fold from culture supernatant by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration
Streptomyces sp.
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
40
-
purified native enzyme, pH 3.8, 48°C; purified native enzyme, pH 5.0, 48°C
Streptomyces sp.
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
dearabinosylated gum arabic + H2O
de-arabinosylated gum arabic is used as a model to investigate the use of the enzyme in defining type II galactan structure, kinetics, overview. Exhaustive hydrolysis of dearabinosylated gum arabic resultes in a limited number of oligosaccharide products with a trisaccharide of Gal2GlcA1 predominating, mass spectrometric analysis
731581
Streptomyces sp.
?
-
-
-
?
dearabinosylated gum arabic + H2O
de-arabinosylated gum arabic is used as a model to investigate the use of the enzyme in defining type II galactan structure, kinetics, overview. Exhaustive hydrolysis of dearabinosylated gum arabic resultes in a limited number of oligosaccharide products with a trisaccharide of Gal2GlcA1 predominating., mass spectrometric analysis
731581
Streptomyces sp.
?
-
-
-
?
dearabinosylated gum arabic + H2O
de-arabinosylated gum arabic is used as a model to investigate the use of the enzyme in defining type II galactan structure, kinetics, overview. Exhaustive hydrolysis of dearabinosylated gum arabic resultes in a limited number of oligosaccharide products with a trisaccharide of Gal2GlcA1 predominating., mass spectrometric analysis
731581
Streptomyces sp. 19(2012)
?
-
-
-
?
dearabinosylated gum arabic + H2O
de-arabinosylated gum arabic is used as a model to investigate the use of the enzyme in defining type II galactan structure, kinetics, overview. Exhaustive hydrolysis of dearabinosylated gum arabic resultes in a limited number of oligosaccharide products with a trisaccharide of Gal2GlcA1 predominating, mass spectrometric analysis
731581
Streptomyces sp. 19(2012)
?
-
-
-
?
additional information
the enzyme specifically cleaves the beta-(1->3)-D-galactan backbone of arabinogalactan-proteins
731581
Streptomyces sp.
?
-
-
-
-
additional information
the enzyme specifically hydrolyses beta-(1->3)-D-galacto-oligo- or poly-saccharides from the upstream (non-reducing) end, typical of an exo-acting enzyme. Substrate specificity, overview. No or negligible activity on 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl beta-D-fucopyranoside,4-nitrophenyl alpha-L-arabinofuranosidase 4-nitrophenyl alpha-D-galactopyranoside, 4-nitrophenyl alpha/beta-D-glucopyranoside, 4-nitrophenyl alpha/beta-L-fucopyranoside, 4-nitrophenyl beta-D-cellobioside, 4-nitrophenyl alpha-D-mannopyranoside, or 4-nitrophenyl beta-D-xylopyranoside
731581
Streptomyces sp.
?
-
-
-
-
additional information
the enzyme specifically cleaves the beta-(1->3)-D-galactan backbone of arabinogalactan-proteins
731581
Streptomyces sp. 19(2012)
?
-
-
-
-
additional information
the enzyme specifically hydrolyses beta-(1->3)-D-galacto-oligo- or poly-saccharides from the upstream (non-reducing) end, typical of an exo-acting enzyme. Substrate specificity, overview. No or negligible activity on 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl beta-D-fucopyranoside,4-nitrophenyl alpha-L-arabinofuranosidase 4-nitrophenyl alpha-D-galactopyranoside, 4-nitrophenyl alpha/beta-D-glucopyranoside, 4-nitrophenyl alpha/beta-L-fucopyranoside, 4-nitrophenyl beta-D-cellobioside, 4-nitrophenyl alpha-D-mannopyranoside, or 4-nitrophenyl beta-D-xylopyranoside
731581
Streptomyces sp. 19(2012)
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
?
x * 45000, about, SDS-PAGE, x * 48200, about, sequence calculation; x * 47900, about, sequence calculation
Streptomyces sp.
Synonyms
Synonyms
Commentary
Organism
exo-beta-(1->3)-D-galactanase
-
Streptomyces sp.
SGalase1
-
Streptomyces sp.
SGalase2
-
Streptomyces sp.
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
48
-
;
Streptomyces sp.
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
3.8
-
-
Streptomyces sp.
5
-
-
Streptomyces sp.
pI Value
Organism
Commentary
pI Value Maximum
pI Value
Streptomyces sp.
about, sequence calculation; about, sequence calculation
-
7.45
Application (protein specific)
Application
Commentary
Organism
analysis
the activity of the enzyme is well suited for the study of type II galactan structures and provides an important tool for the investigation of the biological role of arabinogalactan proteins in plants
Streptomyces sp.
Cloned(Commentary) (protein specific)
Commentary
Organism
SGalase1, DNA and amino acid equence determination and analysis, sequence comparison, phylogenetic analysis and tree
Streptomyces sp.
SGalase2, DNA and amino acid equence determination and analysis, sequence comparison, phylogenetic analysis and tree
Streptomyces sp.
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
45000
-
x * 45000, about, SDS-PAGE, x * 48200, about, sequence calculation
Streptomyces sp.
47900
-
x * 47900, about, sequence calculation
Streptomyces sp.
48200
-
x * 45000, about, SDS-PAGE, x * 48200, about, sequence calculation
Streptomyces sp.
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
additional information
Streptomyces sp.
the enzyme specifically cleaves the beta-(1->3)-D-galactan backbone of arabinogalactan-proteins
?
-
-
-
additional information
Streptomyces sp. 19(2012)
the enzyme specifically cleaves the beta-(1->3)-D-galactan backbone of arabinogalactan-proteins
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
native enzyme 1.8fold from culture supernatant by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration
Streptomyces sp.
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
40
-
purified native enzyme, pH 3.8, 48°C
Streptomyces sp.
40
-
purified native enzyme, pH 5.0, 48°C
Streptomyces sp.
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
dearabinosylated gum arabic + H2O
de-arabinosylated gum arabic is used as a model to investigate the use of the enzyme in defining type II galactan structure, kinetics, overview. Exhaustive hydrolysis of dearabinosylated gum arabic resultes in a limited number of oligosaccharide products with a trisaccharide of Gal2GlcA1 predominating, mass spectrometric analysis
731581
Streptomyces sp.
?
-
-
-
?
dearabinosylated gum arabic + H2O
de-arabinosylated gum arabic is used as a model to investigate the use of the enzyme in defining type II galactan structure, kinetics, overview. Exhaustive hydrolysis of dearabinosylated gum arabic resultes in a limited number of oligosaccharide products with a trisaccharide of Gal2GlcA1 predominating., mass spectrometric analysis
731581
Streptomyces sp.
?
-
-
-
?
dearabinosylated gum arabic + H2O
de-arabinosylated gum arabic is used as a model to investigate the use of the enzyme in defining type II galactan structure, kinetics, overview. Exhaustive hydrolysis of dearabinosylated gum arabic resultes in a limited number of oligosaccharide products with a trisaccharide of Gal2GlcA1 predominating., mass spectrometric analysis
731581
Streptomyces sp. 19(2012)
?
-
-
-
?
dearabinosylated gum arabic + H2O
de-arabinosylated gum arabic is used as a model to investigate the use of the enzyme in defining type II galactan structure, kinetics, overview. Exhaustive hydrolysis of dearabinosylated gum arabic resultes in a limited number of oligosaccharide products with a trisaccharide of Gal2GlcA1 predominating, mass spectrometric analysis
731581
Streptomyces sp. 19(2012)
?
-
-
-
?
additional information
the enzyme specifically cleaves the beta-(1->3)-D-galactan backbone of arabinogalactan-proteins
731581
Streptomyces sp.
?
-
-
-
-
additional information
the enzyme specifically hydrolyses beta-(1->3)-D-galacto-oligo- or poly-saccharides from the upstream (non-reducing) end, typical of an exo-acting enzyme. Substrate specificity, overview. No or negligible activity on 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl beta-D-fucopyranoside,4-nitrophenyl alpha-L-arabinofuranosidase 4-nitrophenyl alpha-D-galactopyranoside, 4-nitrophenyl alpha/beta-D-glucopyranoside, 4-nitrophenyl alpha/beta-L-fucopyranoside, 4-nitrophenyl beta-D-cellobioside, 4-nitrophenyl alpha-D-mannopyranoside, or 4-nitrophenyl beta-D-xylopyranoside
731581
Streptomyces sp.
?
-
-
-
-
additional information
the enzyme specifically cleaves the beta-(1->3)-D-galactan backbone of arabinogalactan-proteins
731581
Streptomyces sp. 19(2012)
?
-
-
-
-
additional information
the enzyme specifically hydrolyses beta-(1->3)-D-galacto-oligo- or poly-saccharides from the upstream (non-reducing) end, typical of an exo-acting enzyme. Substrate specificity, overview. No or negligible activity on 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl beta-D-fucopyranoside,4-nitrophenyl alpha-L-arabinofuranosidase 4-nitrophenyl alpha-D-galactopyranoside, 4-nitrophenyl alpha/beta-D-glucopyranoside, 4-nitrophenyl alpha/beta-L-fucopyranoside, 4-nitrophenyl beta-D-cellobioside, 4-nitrophenyl alpha-D-mannopyranoside, or 4-nitrophenyl beta-D-xylopyranoside
731581
Streptomyces sp. 19(2012)
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 45000, about, SDS-PAGE, x * 48200, about, sequence calculation
Streptomyces sp.
?
x * 47900, about, sequence calculation
Streptomyces sp.
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
48
-
-
Streptomyces sp.
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
3.8
-
-
Streptomyces sp.
5
-
-
Streptomyces sp.
pI Value (protein specific)
Organism
Commentary
pI Value Maximum
pI Value
Streptomyces sp.
about, sequence calculation
-
7.45
General Information
General Information
Commentary
Organism
evolution
the enzyme belongs to the glycoside hydrolase family 43, GH43, phylogenetic analysis and tree; the enzyme belongs to the glycoside hydrolase family 43, GH43, phylogenetic analysis and tree
Streptomyces sp.
General Information (protein specific)
General Information
Commentary
Organism
evolution
the enzyme belongs to the glycoside hydrolase family 43, GH43, phylogenetic analysis and tree
Streptomyces sp.
Other publictions for EC
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
Synonyms
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)
752571
Fujita
Degradative enzymes for type ...
Bifidobacterium longum subsp. Longum
Appl. Microbiol. Biotechnol.
103
1299-1310
2019
-
-
1
-
-
-
-
-
-
-
-
-
-
3
-
-
1
-
-
-
-
-
6
1
6
1
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
6
1
1
-
-
-
1
-
-
-
-
3
3
-
-
-
752397
Godoy
Crystal structure of a putati ...
Bifidobacterium bifidum, Bifidobacterium bifidum NCIMB 41171, Bifidobacterium bifidum S17
Acta Crystallogr. Sect. F
72
288-293
2016
-
-
1
1
-
-
-
-
-
-
1
-
-
5
-
-
1
-
-
-
-
-
3
2
2
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
3
2
-
-
-
-
-
-
-
-
-
1
1
-
-
-
731184
Fujita
Bifidobacterium longum subsp. ...
Bifidobacterium longum, Bifidobacterium longum JCM 1217
Appl. Environ. Microbiol.
80
4577-4584
2014
-
-
1
-
1
-
-
1
-
-
1
-
-
6
-
-
-
-
-
-
9
-
14
-
2
1
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
9
-
14
-
1
-
-
-
1
-
-
-
1
2
2
1
-
-
731202
Okawa
Identification of an exo-beta- ...
Fusarium oxysporum 12S, Fusarium oxysporum
Appl. Microbiol. Biotechnol.
97
9685-9694
2013
-
-
1
-
-
-
-
-
-
-
-
-
-
5
-
-
1
-
-
-
1
-
12
1
2
1
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
12
1
1
-
-
-
1
-
-
-
-
1
1
-
-
-
731581
Ling
An exo-beta-(1->3)-D-galactana ...
Streptomyces sp. 19(2012), Streptomyces sp.
Carbohydr. Res.
352
70-81
2012
-
1
1
-
-
-
-
-
-
-
3
4
-
6
-
-
1
-
-
-
1
-
12
1
4
1
-
-
-
2
-
-
-
-
1
-
-
2
2
-
-
-
-
-
-
-
-
-
-
3
4
-
-
-
2
-
-
2
-
12
2
2
-
-
-
2
-
-
2
-
1
2
-
-
-
732396
Jiang
Crystal structure of 1,3Gal43A ...
Hungateiclostridium thermocellum
J. Struct. Biol.
180
447-457
2012
-
-
1
1
2
-
-
-
-
-
2
-
-
4
-
-
1
-
-
-
-
-
1
2
3
1
-
-
-
1
-
-
-
-
-
-
-
-
1
-
1
2
-
-
-
-
-
-
-
2
-
-
-
-
1
-
-
-
-
1
2
1
-
-
-
1
-
-
-
-
2
2
-
-
-
713904
Sakamoto
Characterization of an exo-bet ...
Sphingomonas sp., Sphingomonas sp. 24T
Appl. Microbiol. Biotechnol.
90
1701-1710
2011
1
-
-
-
-
-
-
-
-
-
1
-
-
3
-
-
1
-
-
1
2
-
12
1
2
1
-
1
-
1
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
1
2
-
12
1
1
-
1
-
1
-
1
-
-
-
-
-
-
-
703061
Ling
Preparation of a new chromogen ...
Irpex lacteus
Carbohydr. Res.
344
1941-1946
2009
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
1
-
2
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
1
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
706965
Ishida
Crystallization of selenomethi ...
Phanerochaete chrysosporium
Acta Crystallogr. Sect. F
65
1274-1276
2009
-
-
1
1
-
-
-
-
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
1
3
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
707784
Kotake
Molecular cloning and expressi ...
Irpex lacteus, Irpex lacteus NBRC 5367
Biosci. Biotechnol. Biochem.
73
2303-2309
2009
-
-
1
-
-
-
-
-
-
-
1
-
-
2
-
-
1
-
-
-
1
-
4
1
2
1
1
-
-
1
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
1
-
4
1
1
1
-
-
1
1
-
-
-
-
-
-
-
-
677662
Ichinose
Characterization of an exo-bet ...
Hungateiclostridium thermocellum
Appl. Environ. Microbiol.
72
3515-3523
2006
-
-
1
-
-
-
-
-
-
-
1
-
-
4
-
-
1
-
-
-
1
-
5
-
2
2
-
-
-
1
1
-
-
-
-
-
-
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1
-
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1
-
-
-
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1
-
-
1
-
5
-
2
-
-
-
1
1
-
-
-
-
-
-
-
-
678786
Ichinose
Characterization of an exo-bet ...
Streptomyces avermitilis, Streptomyces avermitilis NBRC 14893
Biosci. Biotechnol. Biochem.
70
2745-2750
2006
-
-
1
-
-
-
-
-
-
-
1
-
-
4
-
1
1
-
-
-
1
-
10
-
2
1
-
-
-
1
-
-
-
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-
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1
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1
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1
1
-
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1
-
10
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
666634
Kotake
Molecular cloning of a b-galac ...
Raphanus sativus
Plant Physiol.
138
1563-1576
2005
-
-
1
-
-
-
4
3
-
-
2
-
-
4
-
-
1
-
-
-
1
-
10
1
1
1
-
1
3
1
1
-
-
-
-
-
-
-
1
-
-
-
-
-
4
-
3
-
-
2
-
-
-
-
1
-
-
1
-
10
1
1
-
1
3
1
1
-
-
-
-
-
-
-
-
171335
Tsumuraya
Purification of an exo-beta-(1 ...
Irpex lacteus
J. Biol. Chem.
265
7207-7215
1990
-
-
-
-
-
-
-
2
-
-
2
1
-
1
-
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1
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1
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4
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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2
1
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1
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4
1
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1
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