BRENDA - Enzyme Database
show all sequences of 1.1.98.2

Discovery and characterization of an F420-dependent glucose-6-phosphate dehydrogenase (Rh-FGD1) from Rhodococcus jostii RHA1

Nguyen, Q.T.; Trinco, G.; Binda, C.; Mattevi, A.; Fraaije, M.W.; Appl. Microbiol. Biotechnol. 101, 2831-2842 (2016)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expressed in Escherichia coli C41(DE3) cells
Rhodococcus jostii
Engineering
Amino acid exchange
Commentary
Organism
K197N
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
Rhodococcus jostii
K258N
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
Rhodococcus jostii
R282Q
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
Rhodococcus jostii
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.31
-
D-glucose 6-phosphate
wild type enzyme, at pH 7.5 and 25°C
Rhodococcus jostii
61
-
D-glucose 6-phosphate
mutant enzyme K258N, at pH 7.5 and 25°C
Rhodococcus jostii
95
-
D-glucose 6-phosphate
mutant enzyme K197N, at pH 7.5 and 25°C
Rhodococcus jostii
100
-
D-glucose 6-phosphate
Km above 100 mM, mutant enzyme R282Q, at pH 7.5 and 25°C
Rhodococcus jostii
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-glucose 6-phosphate + oxidized coenzyme F420
Rhodococcus jostii
-
6-phospho-D-glucono-1,5-lactone + reduced coenzyme F420
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Rhodococcus jostii
-
-
-
Purification (Commentary)
Commentary
Organism
HisTrap column chromatography and Superdex 200 gel filtration
Rhodococcus jostii
Storage Stability
Storage Stability
Organism
-80°C, phosphate-based buffer with both NaCl and glycerol as additives, 1 year, less than 10% loss of activity
Rhodococcus jostii
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-fructose 6-phosphate + oxidized coenzyme F420
4.8% activity compared to D-glucose 6-phosphate
739925
Rhodococcus jostii
? + reduced coenzyme F420
-
-
-
?
D-glucosamine 6-phosphate + oxidized coenzyme F420
2.8% activity compared to D-glucose 6-phosphate
739925
Rhodococcus jostii
?
-
-
-
?
D-glucose 6-phosphate + oxidized coenzyme F420
-
739925
Rhodococcus jostii
6-phospho-D-glucono-1,5-lactone + reduced coenzyme F420
-
-
-
?
D-glucose 6-phosphate + oxidized coenzyme F420
100% activity
739925
Rhodococcus jostii
6-phospho-D-glucono-1,5-lactone + reduced coenzyme F420
-
-
-
?
D-mannose 6-phosphate + oxidized coenzyme F420
1.1% activity compared to D-glucose 6-phosphate
739925
Rhodococcus jostii
6-phospho-D-mannono-1,5-lactone + reduced coenzyme F420
-
-
-
?
additional information
there is no detectable enzyme activity with alpha-Dglucose 1-phosphate and alpha-D-galactose 1-phosphate. The enzyme also accepts D-glucose as substrate, although with very low catalytic activity
739925
Rhodococcus jostii
?
-
-
-
-
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
35
-
the enzyme exhibits melting temperature values above 35°C in most common buffer systems like HEPES, citrate, and phosphate
Rhodococcus jostii
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.047
-
D-glucose 6-phosphate
kcat above 0.047 s-1, mutant enzyme R282Q, at pH 7.5 and 25°C
Rhodococcus jostii
0.57
-
D-glucose 6-phosphate
mutant enzyme K258N, at pH 7.5 and 25°C
Rhodococcus jostii
3.8
-
D-glucose 6-phosphate
mutant enzyme K197N, at pH 7.5 and 25°C
Rhodococcus jostii
17
-
D-glucose 6-phosphate
wild type enzyme, at pH 7.5 and 25°C
Rhodococcus jostii
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
8
-
Rhodococcus jostii
Cofactor
Cofactor
Commentary
Organism
Structure
coenzyme F420
the enzyme is strictly dependent on F420 as coenzyme
Rhodococcus jostii
additional information
the enzyme shows no significant activity when NAD+, NADP+, FAD, or FMN is used as alternative electron acceptor
Rhodococcus jostii
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli C41(DE3) cells
Rhodococcus jostii
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
coenzyme F420
the enzyme is strictly dependent on F420 as coenzyme
Rhodococcus jostii
additional information
the enzyme shows no significant activity when NAD+, NADP+, FAD, or FMN is used as alternative electron acceptor
Rhodococcus jostii
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
K197N
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
Rhodococcus jostii
K258N
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
Rhodococcus jostii
R282Q
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
Rhodococcus jostii
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.31
-
D-glucose 6-phosphate
wild type enzyme, at pH 7.5 and 25°C
Rhodococcus jostii
61
-
D-glucose 6-phosphate
mutant enzyme K258N, at pH 7.5 and 25°C
Rhodococcus jostii
95
-
D-glucose 6-phosphate
mutant enzyme K197N, at pH 7.5 and 25°C
Rhodococcus jostii
100
-
D-glucose 6-phosphate
Km above 100 mM, mutant enzyme R282Q, at pH 7.5 and 25°C
Rhodococcus jostii
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-glucose 6-phosphate + oxidized coenzyme F420
Rhodococcus jostii
-
6-phospho-D-glucono-1,5-lactone + reduced coenzyme F420
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
HisTrap column chromatography and Superdex 200 gel filtration
Rhodococcus jostii
Storage Stability (protein specific)
Storage Stability
Organism
-80°C, phosphate-based buffer with both NaCl and glycerol as additives, 1 year, less than 10% loss of activity
Rhodococcus jostii
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-fructose 6-phosphate + oxidized coenzyme F420
4.8% activity compared to D-glucose 6-phosphate
739925
Rhodococcus jostii
? + reduced coenzyme F420
-
-
-
?
D-glucosamine 6-phosphate + oxidized coenzyme F420
2.8% activity compared to D-glucose 6-phosphate
739925
Rhodococcus jostii
?
-
-
-
?
D-glucose 6-phosphate + oxidized coenzyme F420
-
739925
Rhodococcus jostii
6-phospho-D-glucono-1,5-lactone + reduced coenzyme F420
-
-
-
?
D-glucose 6-phosphate + oxidized coenzyme F420
100% activity
739925
Rhodococcus jostii
6-phospho-D-glucono-1,5-lactone + reduced coenzyme F420
-
-
-
?
D-mannose 6-phosphate + oxidized coenzyme F420
1.1% activity compared to D-glucose 6-phosphate
739925
Rhodococcus jostii
6-phospho-D-mannono-1,5-lactone + reduced coenzyme F420
-
-
-
?
additional information
there is no detectable enzyme activity with alpha-Dglucose 1-phosphate and alpha-D-galactose 1-phosphate. The enzyme also accepts D-glucose as substrate, although with very low catalytic activity
739925
Rhodococcus jostii
?
-
-
-
-
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
35
-
the enzyme exhibits melting temperature values above 35°C in most common buffer systems like HEPES, citrate, and phosphate
Rhodococcus jostii
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.047
-
D-glucose 6-phosphate
kcat above 0.047 s-1, mutant enzyme R282Q, at pH 7.5 and 25°C
Rhodococcus jostii
0.57
-
D-glucose 6-phosphate
mutant enzyme K258N, at pH 7.5 and 25°C
Rhodococcus jostii
3.8
-
D-glucose 6-phosphate
mutant enzyme K197N, at pH 7.5 and 25°C
Rhodococcus jostii
17
-
D-glucose 6-phosphate
wild type enzyme, at pH 7.5 and 25°C
Rhodococcus jostii
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
8
-
Rhodococcus jostii
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.00067
-
D-glucose 6-phosphate
mutant enzyme R282Q, at pH 7.5 and 25°C
Rhodococcus jostii
0.0094
-
D-glucose 6-phosphate
mutant enzyme K258N, at pH 7.5 and 25°C
Rhodococcus jostii
0.04
-
D-glucose 6-phosphate
mutant enzyme K197N, at pH 7.5 and 25°C
Rhodococcus jostii
57
-
D-glucose 6-phosphate
wild type enzyme, at pH 7.5 and 25°C
Rhodococcus jostii
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.00067
-
D-glucose 6-phosphate
mutant enzyme R282Q, at pH 7.5 and 25°C
Rhodococcus jostii
0.0094
-
D-glucose 6-phosphate
mutant enzyme K258N, at pH 7.5 and 25°C
Rhodococcus jostii
0.04
-
D-glucose 6-phosphate
mutant enzyme K197N, at pH 7.5 and 25°C
Rhodococcus jostii
57
-
D-glucose 6-phosphate
wild type enzyme, at pH 7.5 and 25°C
Rhodococcus jostii
Other publictions for EC 1.1.98.2
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)
739925
Nguyen
Discovery and characterization ...
Rhodococcus jostii
Appl. Microbiol. Biotechnol.
101
2831-2842
2016
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1
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3
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1
6
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1
4
1
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4
4
740083
Oyugi
Investigating the reaction mec ...
Mycobacterium tuberculosis
Biochemistry
55
5566-5577
2016
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1
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5
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12
-
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1
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3
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1
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1
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12
1
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1
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1
1
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5
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12
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1
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1
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1
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12
1
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-
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11
11
723589
Bashiri
Tat-dependent translocation of ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
PLoS ONE
7
e45003
2012
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1
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2
2
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160
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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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2
1
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-
1
-
-
-
-
1
1
-
-
-
699008
Hasan
Glucose-6-phosphate accumulati ...
Mycolicibacterium smegmatis
J. Biol. Chem.
285
19135-19144
2010
-
-
-
-
-
-
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-
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1
-
6
-
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1
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1
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1
-
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-
-
-
-
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-
-
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698764
Bashiri
Crystal structures of F420-dep ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
J. Biol. Chem.
283
17531-17541
2008
-
-
1
1
-
-
1
-
-
-
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5
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1
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-
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1
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1
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1
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1
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1
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-
701052
Bashiri
Expression, purification and c ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Protein Expr. Purif.
54
38-44
2007
-
-
1
1
-
-
-
-
-
-
-
2
-
160
-
-
1
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2
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1
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1
1
1
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2
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1
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2
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-
-
-
-
-
1
1
-
-
-
700931
Manjunatha
Identification of a nitroimida ...
Mycobacterium tuberculosis
Proc. Natl. Acad. Sci. USA
103
431-436
2006
-
1
-
-
-
-
-
-
-
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1
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1
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-
698551
Purwantini
Molecular analysis of the gene ...
Mycolicibacterium smegmatis
J. Bacteriol.
180
2212-2219
1998
-
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1
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6
-
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1
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-
697967
Purwantini
Presence of F420-dependent glu ...
Gordonia amarae, Mycobacterium avium, Mycobacterium gordonae, Mycobacterium kansasii, Mycobacterium leprae, Mycobacterium scrofulaceum, Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Ra / ATCC 25177, Mycobacterium tuberculosis H37Rv, Mycolicibacterium fortuitum, Mycolicibacterium smegmatis, no activity in Actinomadura kijaniata, no activity in Corynebacterium ammoniagenes, no activity in Corynebacterium glutamicum, no activity in Corynebacterium matruchotii, no activity in Methanobacterium thermoautotrophicum, no activity in Methanobacterium thermoautotrophicum Marburg / DSM 2133, no activity in Methanosarcina barkeri, no activity in Methanosarcina barkeri Fusaro, no activity in Methanospirillum hungateii, no activity in Streptomyces achromogenes, no activity in Streptomyces aureofaciens, no activity in Streptomyces avermitilis, no activity in Streptomyces lincolnensis, no activity in Streptomyces lividans, no activity in Streptomyces rimosus, Nocardia asteroides, Nocardia brasiliensis, Nocardia otitidiscaviarum, Nocardia tartaricans
FEMS Microbiol. Lett.
146
129-134
1997
-
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1
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33
-
203
-
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14
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33
-
13
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13
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13
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13
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1
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33
-
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14
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33
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13
-
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13
-
-
-
-
-
-
-
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698547
Purwantini
Purification of a novel coenzy ...
Mycolicibacterium smegmatis
J. Bacteriol.
178
2861-2866
1996
-
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-
-
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1
2
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2
1
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4
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1
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1
1
4
1
1
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1
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2
1
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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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1
1
4
1
1
-
1
-
2
1
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