BRENDA - Enzyme Database
show all sequences of 6.3.2.49

A novel L-amino acid ligase from Bacillus licheniformis

Kino, K.; Noguchi, A.; Nakazawa, Y.; Yagasaki, M.; J. Biosci. Bioeng. 106, 313-315 (2008)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
Bacillus licheniformis
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
-
Bacillus licheniformis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + L-leucine + an L-amino acid
Bacillus licheniformis
the enzyme catalyzes the formation of an alpha-peptide bond in unprotected L-amino acids in an ATP-dependent manner, the substrate specificity of BL00235 is strict, only methionine or leucine are accepted as dipeptide N-terminal residues, overview
ADP + phosphate + L-leucyl-L-amino acid
-
-
?
ATP + L-leucine + an L-amino acid
Bacillus licheniformis NBRC12200
the enzyme catalyzes the formation of an alpha-peptide bond in unprotected L-amino acids in an ATP-dependent manner, the substrate specificity of BL00235 is strict, only methionine or leucine are accepted as dipeptide N-terminal residues, overview
ADP + phosphate + L-leucyl-L-amino acid
-
-
?
ATP + L-methionine + an L-amino acid
Bacillus licheniformis
the enzyme catalyzes the formation of an alpha-peptide bond in unprotected L-amino acids in an ATP-dependent manner, the substrate specificity of BL00235 is strict, only methionine or leucine are accepted as dipeptide N-terminal residues, overview
ADP + phosphate + L-methionyl-L-amino acid
-
-
?
ATP + L-methionine + an L-amino acid
Bacillus licheniformis NBRC12200
the enzyme catalyzes the formation of an alpha-peptide bond in unprotected L-amino acids in an ATP-dependent manner, the substrate specificity of BL00235 is strict, only methionine or leucine are accepted as dipeptide N-terminal residues, overview
ADP + phosphate + L-methionyl-L-amino acid
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Bacillus licheniformis
-
gene BL00235
-
Bacillus licheniformis NBRC12200
-
gene BL00235
-
Purification (Commentary)
Commentary
Organism
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
Bacillus licheniformis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + L-asparagine + L-methionine
-
693286
Bacillus licheniformis
ADP + phosphate + L-asparaginyl-L-methionine
-
-
-
?
ATP + L-asparagine + L-methionine
-
693286
Bacillus licheniformis NBRC12200
ADP + phosphate + L-asparaginyl-L-methionine
-
-
-
?
ATP + L-leucine + an L-amino acid
the enzyme catalyzes the formation of an alpha-peptide bond in unprotected L-amino acids in an ATP-dependent manner, the substrate specificity of BL00235 is strict, only methionine or leucine are accepted as dipeptide N-terminal residues, overview
693286
Bacillus licheniformis
ADP + phosphate + L-leucyl-L-amino acid
-
-
-
?
ATP + L-leucine + an L-amino acid
the enzyme catalyzes the formation of an alpha-peptide bond in unprotected L-amino acids in an ATP-dependent manner, the substrate specificity of BL00235 is strict, only methionine or leucine are accepted as dipeptide N-terminal residues, overview
693286
Bacillus licheniformis NBRC12200
ADP + phosphate + L-leucyl-L-amino acid
-
-
-
?
ATP + L-leucine + L-alanine
-
693286
Bacillus licheniformis
ADP + phosphate + L-leucyl-L-alanine
-
-
-
?
ATP + L-leucine + L-alanine
-
693286
Bacillus licheniformis NBRC12200
ADP + phosphate + L-leucyl-L-alanine
-
-
-
?
ATP + L-methionine + an L-amino acid
the enzyme catalyzes the formation of an alpha-peptide bond in unprotected L-amino acids in an ATP-dependent manner, the substrate specificity of BL00235 is strict, only methionine or leucine are accepted as dipeptide N-terminal residues, overview
693286
Bacillus licheniformis
ADP + phosphate + L-methionyl-L-amino acid
-
-
-
?
ATP + L-methionine + an L-amino acid
the enzyme catalyzes the formation of an alpha-peptide bond in unprotected L-amino acids in an ATP-dependent manner, the substrate specificity of BL00235 is strict, only methionine or leucine are accepted as dipeptide N-terminal residues, overview
693286
Bacillus licheniformis NBRC12200
ADP + phosphate + L-methionyl-L-amino acid
-
-
-
?
ATP + L-methionine + glycine
-
693286
Bacillus licheniformis
ADP + phosphate + L-methionyl-glycine
-
-
-
?
ATP + L-methionine + L-alanine
best substrate combination
693286
Bacillus licheniformis
ADP + phosphate + L-methionyl-L-alanine
-
-
-
?
ATP + L-methionine + L-cysteine
-
693286
Bacillus licheniformis
ADP + phosphate + L-methionyl-L-cysteine
-
-
-
?
ATP + L-methionine + L-leucine
-
693286
Bacillus licheniformis
ADP + phosphate + L-methionyl-L-leucine
-
-
-
?
ATP + L-methionine + L-methionine
-
693286
Bacillus licheniformis
ADP + phosphate + L-methionyl-L-methionine
-
-
-
?
ATP + L-serine + L-methionine
-
693286
Bacillus licheniformis
ADP + phosphate + L-seryl-L-methionine
-
-
-
?
ATP + L-threonine + L-methionine
-
693286
Bacillus licheniformis
ADP + phosphate + L-threonyl-L-methionine
-
-
-
?
additional information
the enzyme catalyzes the formation of an alpha-peptide bond in unprotected L-amino acids in an ATP-dependent manner, the substrate specificity of BL00235 is very strict, overview
693286
Bacillus licheniformis
?
-
-
-
-
additional information
the enzyme catalyzes the formation of an alpha-peptide bond in unprotected L-amino acids in an ATP-dependent manner, the substrate specificity of BL00235 is very strict, overview
693286
Bacillus licheniformis NBRC12200
?
-
-
-
-
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
-
Bacillus licheniformis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
9
-
-
Bacillus licheniformis
Cofactor
Cofactor
Commentary
Organism
Structure
ATP
-
Bacillus licheniformis
Cloned(Commentary) (protein specific)
Commentary
Organism
expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
Bacillus licheniformis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
ATP
-
Bacillus licheniformis
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
-
Bacillus licheniformis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + L-leucine + an L-amino acid
Bacillus licheniformis
the enzyme catalyzes the formation of an alpha-peptide bond in unprotected L-amino acids in an ATP-dependent manner, the substrate specificity of BL00235 is strict, only methionine or leucine are accepted as dipeptide N-terminal residues, overview
ADP + phosphate + L-leucyl-L-amino acid
-
-
?
ATP + L-leucine + an L-amino acid
Bacillus licheniformis NBRC12200
the enzyme catalyzes the formation of an alpha-peptide bond in unprotected L-amino acids in an ATP-dependent manner, the substrate specificity of BL00235 is strict, only methionine or leucine are accepted as dipeptide N-terminal residues, overview
ADP + phosphate + L-leucyl-L-amino acid
-
-
?
ATP + L-methionine + an L-amino acid
Bacillus licheniformis
the enzyme catalyzes the formation of an alpha-peptide bond in unprotected L-amino acids in an ATP-dependent manner, the substrate specificity of BL00235 is strict, only methionine or leucine are accepted as dipeptide N-terminal residues, overview
ADP + phosphate + L-methionyl-L-amino acid
-
-
?
ATP + L-methionine + an L-amino acid
Bacillus licheniformis NBRC12200
the enzyme catalyzes the formation of an alpha-peptide bond in unprotected L-amino acids in an ATP-dependent manner, the substrate specificity of BL00235 is strict, only methionine or leucine are accepted as dipeptide N-terminal residues, overview
ADP + phosphate + L-methionyl-L-amino acid
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
Bacillus licheniformis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + L-asparagine + L-methionine
-
693286
Bacillus licheniformis
ADP + phosphate + L-asparaginyl-L-methionine
-
-
-
?
ATP + L-asparagine + L-methionine
-
693286
Bacillus licheniformis NBRC12200
ADP + phosphate + L-asparaginyl-L-methionine
-
-
-
?
ATP + L-leucine + an L-amino acid
the enzyme catalyzes the formation of an alpha-peptide bond in unprotected L-amino acids in an ATP-dependent manner, the substrate specificity of BL00235 is strict, only methionine or leucine are accepted as dipeptide N-terminal residues, overview
693286
Bacillus licheniformis
ADP + phosphate + L-leucyl-L-amino acid
-
-
-
?
ATP + L-leucine + an L-amino acid
the enzyme catalyzes the formation of an alpha-peptide bond in unprotected L-amino acids in an ATP-dependent manner, the substrate specificity of BL00235 is strict, only methionine or leucine are accepted as dipeptide N-terminal residues, overview
693286
Bacillus licheniformis NBRC12200
ADP + phosphate + L-leucyl-L-amino acid
-
-
-
?
ATP + L-leucine + L-alanine
-
693286
Bacillus licheniformis
ADP + phosphate + L-leucyl-L-alanine
-
-
-
?
ATP + L-leucine + L-alanine
-
693286
Bacillus licheniformis NBRC12200
ADP + phosphate + L-leucyl-L-alanine
-
-
-
?
ATP + L-methionine + an L-amino acid
the enzyme catalyzes the formation of an alpha-peptide bond in unprotected L-amino acids in an ATP-dependent manner, the substrate specificity of BL00235 is strict, only methionine or leucine are accepted as dipeptide N-terminal residues, overview
693286
Bacillus licheniformis
ADP + phosphate + L-methionyl-L-amino acid
-
-
-
?
ATP + L-methionine + an L-amino acid
the enzyme catalyzes the formation of an alpha-peptide bond in unprotected L-amino acids in an ATP-dependent manner, the substrate specificity of BL00235 is strict, only methionine or leucine are accepted as dipeptide N-terminal residues, overview
693286
Bacillus licheniformis NBRC12200
ADP + phosphate + L-methionyl-L-amino acid
-
-
-
?
ATP + L-methionine + glycine
-
693286
Bacillus licheniformis
ADP + phosphate + L-methionyl-glycine
-
-
-
?
ATP + L-methionine + L-alanine
best substrate combination
693286
Bacillus licheniformis
ADP + phosphate + L-methionyl-L-alanine
-
-
-
?
ATP + L-methionine + L-cysteine
-
693286
Bacillus licheniformis
ADP + phosphate + L-methionyl-L-cysteine
-
-
-
?
ATP + L-methionine + L-leucine
-
693286
Bacillus licheniformis
ADP + phosphate + L-methionyl-L-leucine
-
-
-
?
ATP + L-methionine + L-methionine
-
693286
Bacillus licheniformis
ADP + phosphate + L-methionyl-L-methionine
-
-
-
?
ATP + L-serine + L-methionine
-
693286
Bacillus licheniformis
ADP + phosphate + L-seryl-L-methionine
-
-
-
?
ATP + L-threonine + L-methionine
-
693286
Bacillus licheniformis
ADP + phosphate + L-threonyl-L-methionine
-
-
-
?
additional information
the enzyme catalyzes the formation of an alpha-peptide bond in unprotected L-amino acids in an ATP-dependent manner, the substrate specificity of BL00235 is very strict, overview
693286
Bacillus licheniformis
?
-
-
-
-
additional information
the enzyme catalyzes the formation of an alpha-peptide bond in unprotected L-amino acids in an ATP-dependent manner, the substrate specificity of BL00235 is very strict, overview
693286
Bacillus licheniformis NBRC12200
?
-
-
-
-
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
-
Bacillus licheniformis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
9
-
-
Bacillus licheniformis
Other publictions for EC 6.3.2.49
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)
733347
Tsuda
Single mutation alters the sub ...
Bacillus subtilis
Biochemistry
53
2650-2660
2014
-
1
-
1
1
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
1
1
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
726743
Arai
L-amino acid ligase from Pseud ...
Pseudomonas syringae, Pseudomonas syringae NBRC 14081
Appl. Environ. Microbiol.
79
5023-5029
2013
-
1
1
-
-
-
-
-
-
1
-
4
-
4
-
-
-
-
-
-
-
-
100
-
1
1
-
-
1
1
-
1
-
-
-
-
1
1
1
-
-
-
-
-
-
-
-
1
-
4
-
-
-
-
-
-
-
-
100
-
1
1
-
-
1
1
-
-
-
-
-
-
-
-
729244
Parker
Action and timing of BacC and ...
Bacillus subtilis 168, Bacillus subtilis
Biochemistry
52
889-901
2013
-
-
1
-
-
-
-
-
-
-
-
2
-
6
-
-
1
-
-
-
-
-
8
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
1
-
-
-
-
8
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
726581
Suzuki
The structure of L-amino-acid ...
Bacillus licheniformis, Bacillus licheniformis NBRC 12200
Acta Crystallogr. Sect. D
68
1535-1540
2012
-
-
1
1
-
-
-
-
-
1
-
2
-
4
-
-
1
-
-
-
-
-
4
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
1
-
-
-
-
-
-
-
1
-
2
-
-
-
1
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
726615
Tsuda
Crystallization and preliminar ...
Bacillus subtilis 168, Bacillus subtilis
Acta Crystallogr. Sect. F
68
203-206
2012
-
-
-
1
1
-
-
-
-
-
2
-
-
7
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
2
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
730896
Shomura
Structural and enzymatic chara ...
Bacillus subtilis 168, Bacillus subtilis
Protein Sci.
21
707-716
2012
-
1
1
1
2
-
1
12
-
-
-
2
-
6
-
-
1
-
-
-
-
-
6
1
1
-
-
10
1
-
-
-
1
-
-
-
1
1
-
1
2
-
-
1
1
12
-
-
-
2
-
-
-
1
-
-
-
-
6
1
1
-
-
10
1
-
-
-
-
-
-
-
-
-
702768
Kino
A novel L-amino acid ligase fr ...
Bacillus subtilis, Bacillus subtilis NBRC3134
Biosci. Biotechnol. Biochem.
74
129-134
2010
-
-
1
-
-
-
-
-
-
1
-
-
-
4
-
-
-
-
-
-
-
-
2
-
1
1
-
-
1
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
2
-
1
1
-
-
1
1
-
-
-
1
1
-
-
-
702771
Senoo
Identification of novel L-amin ...
Actinobacillus pleuropneumoniae, Photorhabdus laumondii subsp. laumondii, Streptococcus mutans, Streptococcus pneumoniae, Treponema denticola
Biosci. Biotechnol. Biochem.
74
415-418
2010
-
-
5
-
-
-
-
-
-
-
-
-
-
5
-
-
5
-
-
-
-
-
115
-
5
-
-
-
5
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
5
-
-
-
-
115
-
5
-
-
-
5
-
-
-
-
-
-
-
-
-
690733
Kino
Dipeptide synthesis by L-amino ...
Ralstonia solanacearum, Ralstonia solanacearum JCM 10489
Biochem. Biophys. Res. Commun.
371
536-540
2008
-
-
1
-
-
-
-
1
-
1
1
2
-
4
-
-
1
-
-
-
-
-
4
1
1
-
-
-
1
1
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
1
-
1
1
2
-
-
-
1
-
-
-
-
4
1
1
-
-
-
1
1
-
-
-
-
-
-
-
-
693286
Kino
A novel L-amino acid ligase fr ...
Bacillus licheniformis, Bacillus licheniformis NBRC12200
J. Biosci. Bioeng.
106
313-315
2008
-
-
1
-
-
-
-
-
-
1
-
4
-
4
-
-
1
-
-
-
-
-
17
-
1
-
-
-
1
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
1
-
4
-
-
-
1
-
-
-
-
17
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
671498
Tabata
Fermentative production of L-a ...
Bacillus subtilis
Appl. Environ. Microbiol.
73
6378-6385
2007
-
1
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
662037
Tabata
ywf in Bacillus subtilis codes ...
Bacillus subtilis, Bacillus subtilis 168
J. Bacteriol.
187
5195-5202
2005
-
-
1
-
-
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2
3
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2
1
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7
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1
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-
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4
1
1
1
-
-
1
1
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-
-
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1
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2
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3
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2
1
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1
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4
1
1
1
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1
1
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733219
Steinborn
bac genes for recombinant baci ...
Bacillus amyloliquefaciens, Bacillus amyloliquefaciens ATCC 15841, Bacillus pumilus, Bacillus pumilus ATCC 7065, Bacillus subtilis, Bacillus subtilis 168, Bacillus subtilis A1/3, no activity in Bacillus amyloliquefaciens, no activity in Bacillus amyloliquefaciens GSB272, no activity in Bacillus coagulans, no activity in Bacillus licheniformis, no activity in Bacillus licheniformis ATCC 9789, no activity in Bacillus megaterium, no activity in Bacillus megaterium PV361, no activity in Bacillus pumilus, no activity in Bacillus pumilus ATCC 12140
Arch. Microbiol.
183
71-79
2005
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3
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1
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3
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8
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21
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8
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3
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4
4
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1
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4
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8
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8
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6
7
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