BRENDA - Enzyme Database
show all sequences of 6.1.1.12

Amino acid substrate specificity of asparaginyl-, aspartyl- and glutaminyl-tRNA synthetase isolated from higher plants

Lea, P.J.; Fowden, L.; Phytochemistry 12, 1903-1916 (1973)
No PubMed abstract available

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
putrescine
can replace Mg2+ in activation with 27% efficiency in aminoacylation
Vigna radiata var. radiata
spermidine
can replace Mg2+ in activation with 16% efficiency in aminoacylation
Vigna radiata var. radiata
spermine
can replace Mg2+ in activation with 32% efficiency in aminoacylation
Vigna radiata var. radiata
Inhibitors
Inhibitors
Commentary
Organism
Structure
2-aminomalonic acid
inhibits transfer of Asp to tRNA
Vigna radiata var. radiata
Br-
0.7 M, 50% inhibition of ATP-diphosphate exchange
Vigna radiata var. radiata
CH3COO-
2.0 M, 50% inhibition of ATP-diphosphate exchange
Vigna radiata var. radiata
Cl-
2.2 M, 50% inhibition of ATP-diphosphate exchange
Vigna radiata var. radiata
ClO3-
0.1 M, 50% inhibition of ATP-diphosphate exchange
Vigna radiata var. radiata
CNS-
0.1 M, 50% inhibition of ATP-diphosphate exchange
Vigna radiata var. radiata
Cs+
1.1 M, 50% inhibition of ATP-diphosphate exchange, 0.16 M, 50% inhibition of aminoacylation
Vigna radiata var. radiata
erythro-3-hydroxyaspartic acid
inhibits transfer of Asp to tRNA
Vigna radiata var. radiata
I-
0.1 M, 50% inhibition of ATP-diphosphate exchange
Vigna radiata var. radiata
IO3-
0.04 M, 50% inhibition of ATP-diphosphate exchange
Vigna radiata var. radiata
K+
2.3 M, 50% inhibition of ATP-diphosphate exchange, 0.22 M, 50% inhibition of aminoacylation
Vigna radiata var. radiata
Li+
0.6 M, 50% inhibition of ATP-diphosphate exchange, 0.11 M, 50% inhibition of aminoacylation
Vigna radiata var. radiata
Na+
1.4 M, 50% inhibition of ATP-diphosphate exchange, 0.18 M , 50% inhibition of aminoacylation
Vigna radiata var. radiata
NH4+
0.9 M, 50% inhibition of ATP-diphosphate exchange, 0.14 M, 50% inhibition of aminoacylation
Vigna radiata var. radiata
NO3-
0.7 M, 50% inhibition of ATP-diphosphate exchange
Vigna radiata var. radiata
p-chloromercuribenzoate
-
Vigna radiata var. radiata
threo-3-hydroxyaspartic acid
inhibits transfer of Asp to tRNA
Vigna radiata var. radiata
threo-3-Methylaspartic acid
inhibits transfer of Asp to tRNA
Vigna radiata var. radiata
tRNA
above 0.4 mg/ml
Vigna radiata var. radiata
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
4.6
-
Asp
ATP-diphosphate exchange
Vigna radiata var. radiata
8
-
2-aminomalonic acid
ATP-diphosphate exchange
Vigna radiata var. radiata
24
-
threo-3-hydroxyaspartic acid
ATP-diphosphate exchange
Vigna radiata var. radiata
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Co2+
can replace Mg2+, with 12% efficiency in activation of ATP-diphosphate exchange, with 34% efficiency in aminoacylation
Vigna radiata var. radiata
Mg2+
Km: 1.1 mM , aminoacylation; Km: 6.9 mM , ATP-diphosphate exchange; optimal concentration: 12 mM, ATP-diphosphate exchange, 5 mM, aminoacylation; required
Vigna radiata var. radiata
Mn2+
can replace Mg2+, with 35% efficiency in activation of ATP-diphosphate exchange, with 56% efficiency in aminoacylation
Vigna radiata var. radiata
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Vigna radiata var. radiata
-
-
-
Purification (Commentary)
Commentary
Organism
-
Vigna radiata var. radiata
Renatured (Commentary)
Commentary
Organism
denaturation by 4 M urea, 30% recovery after dialysis
Vigna radiata var. radiata
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.326
-
-
Vigna radiata var. radiata
Storage Stability
Storage Stability
Organism
-20°C, 40% w/v glycerol, SH-group stabilizing reagent, 50% loss of activity after 72 h
Vigna radiata var. radiata
in a dry form, e.g. as acetone precipitate, stable for 1 month
Vigna radiata var. radiata
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + L-aspartate + tRNAAsp
-
114
Vigna radiata var. radiata
AMP + diphosphate + L-aspartyl-tRNAAsp
-
114
Vigna radiata var. radiata
-
additional information
enzyme can also utilize 2-aminomalonic acid and threo-3-hydroxyaspartic acid in ATP-diphosphate exchange
114
Vigna radiata var. radiata
?
-
-
-
-
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
50
-
half-life: 7 min without stabilizing reagents, 12 min in presence of 0.004 mM ATP, 23 min in presence of 0.004 mM ATP and 0.1 mM Asp
Vigna radiata var. radiata
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
ATP-diphosphate exchange
Vigna radiata var. radiata
pH Range
pH Minimum
pH Maximum
Commentary
Organism
7.8
9.1
7.8: sharp loss of activity below, 9.1: plateau of high activity up to pH 9.1
Vigna radiata var. radiata
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
6000
-
Li+
ATP-diphosphate exchange
Vigna radiata var. radiata
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
putrescine
can replace Mg2+ in activation with 27% efficiency in aminoacylation
Vigna radiata var. radiata
spermidine
can replace Mg2+ in activation with 16% efficiency in aminoacylation
Vigna radiata var. radiata
spermine
can replace Mg2+ in activation with 32% efficiency in aminoacylation
Vigna radiata var. radiata
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
2-aminomalonic acid
inhibits transfer of Asp to tRNA
Vigna radiata var. radiata
Br-
0.7 M, 50% inhibition of ATP-diphosphate exchange
Vigna radiata var. radiata
CH3COO-
2.0 M, 50% inhibition of ATP-diphosphate exchange
Vigna radiata var. radiata
Cl-
2.2 M, 50% inhibition of ATP-diphosphate exchange
Vigna radiata var. radiata
ClO3-
0.1 M, 50% inhibition of ATP-diphosphate exchange
Vigna radiata var. radiata
CNS-
0.1 M, 50% inhibition of ATP-diphosphate exchange
Vigna radiata var. radiata
Cs+
1.1 M, 50% inhibition of ATP-diphosphate exchange, 0.16 M, 50% inhibition of aminoacylation
Vigna radiata var. radiata
erythro-3-hydroxyaspartic acid
inhibits transfer of Asp to tRNA
Vigna radiata var. radiata
I-
0.1 M, 50% inhibition of ATP-diphosphate exchange
Vigna radiata var. radiata
IO3-
0.04 M, 50% inhibition of ATP-diphosphate exchange
Vigna radiata var. radiata
K+
2.3 M, 50% inhibition of ATP-diphosphate exchange, 0.22 M, 50% inhibition of aminoacylation
Vigna radiata var. radiata
Li+
0.6 M, 50% inhibition of ATP-diphosphate exchange, 0.11 M, 50% inhibition of aminoacylation
Vigna radiata var. radiata
Na+
1.4 M, 50% inhibition of ATP-diphosphate exchange, 0.18 M , 50% inhibition of aminoacylation
Vigna radiata var. radiata
NH4+
0.9 M, 50% inhibition of ATP-diphosphate exchange, 0.14 M, 50% inhibition of aminoacylation
Vigna radiata var. radiata
NO3-
0.7 M, 50% inhibition of ATP-diphosphate exchange
Vigna radiata var. radiata
p-chloromercuribenzoate
-
Vigna radiata var. radiata
threo-3-hydroxyaspartic acid
inhibits transfer of Asp to tRNA
Vigna radiata var. radiata
threo-3-Methylaspartic acid
inhibits transfer of Asp to tRNA
Vigna radiata var. radiata
tRNA
above 0.4 mg/ml
Vigna radiata var. radiata
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
6000
-
Li+
ATP-diphosphate exchange
Vigna radiata var. radiata
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
4.6
-
Asp
ATP-diphosphate exchange
Vigna radiata var. radiata
8
-
2-aminomalonic acid
ATP-diphosphate exchange
Vigna radiata var. radiata
24
-
threo-3-hydroxyaspartic acid
ATP-diphosphate exchange
Vigna radiata var. radiata
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Co2+
can replace Mg2+, with 12% efficiency in activation of ATP-diphosphate exchange, with 34% efficiency in aminoacylation
Vigna radiata var. radiata
Mg2+
Km: 1.1 mM , aminoacylation; Km: 6.9 mM , ATP-diphosphate exchange; optimal concentration: 12 mM, ATP-diphosphate exchange, 5 mM, aminoacylation; required
Vigna radiata var. radiata
Mn2+
can replace Mg2+, with 35% efficiency in activation of ATP-diphosphate exchange, with 56% efficiency in aminoacylation
Vigna radiata var. radiata
Purification (Commentary) (protein specific)
Commentary
Organism
-
Vigna radiata var. radiata
Renatured (Commentary) (protein specific)
Commentary
Organism
denaturation by 4 M urea, 30% recovery after dialysis
Vigna radiata var. radiata
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.326
-
-
Vigna radiata var. radiata
Storage Stability (protein specific)
Storage Stability
Organism
-20°C, 40% w/v glycerol, SH-group stabilizing reagent, 50% loss of activity after 72 h
Vigna radiata var. radiata
in a dry form, e.g. as acetone precipitate, stable for 1 month
Vigna radiata var. radiata
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + L-aspartate + tRNAAsp
-
114
Vigna radiata var. radiata
AMP + diphosphate + L-aspartyl-tRNAAsp
-
114
Vigna radiata var. radiata
-
additional information
enzyme can also utilize 2-aminomalonic acid and threo-3-hydroxyaspartic acid in ATP-diphosphate exchange
114
Vigna radiata var. radiata
?
-
-
-
-
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
50
-
half-life: 7 min without stabilizing reagents, 12 min in presence of 0.004 mM ATP, 23 min in presence of 0.004 mM ATP and 0.1 mM Asp
Vigna radiata var. radiata
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
ATP-diphosphate exchange
Vigna radiata var. radiata
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
7.8
9.1
7.8: sharp loss of activity below, 9.1: plateau of high activity up to pH 9.1
Vigna radiata var. radiata
Other publictions for EC 6.1.1.12
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)
743965
Songsiriritthigul
Crystal structure of the N-te ...
Helicobacter pylori, Helicobacter pylori ATCC 700392
Acta Crystallogr. Sect. F
73
62-69
2017
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745554
Nair
The Bacillus subtilis and Bac ...
Mycoplasma pneumoniae
J. Mol. Biol.
428
618-630
2016
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744436
Schwenzer
Released selective pressure o ...
Homo sapiens, Mus musculus
Biochimie
100
18-26
2014
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2
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2
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2
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7
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40
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40
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745833
Luna
Plant perception of gamma-ami ...
Arabidopsis thaliana
Nat. Chem. Biol.
10
450-456
2014
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746254
Gurcha
Biochemical and structural ch ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv, Mycolicibacterium smegmatis
PLoS ONE
9
e113568
2014
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2
1
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2
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8
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7
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726911
van Berge
Pathogenic mutations causing L ...
Homo sapiens
Biochem. J.
450
345-350
2013
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8
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727335
Kron
Nematode asparaginyl-tRNA synt ...
Brugia malayi
Clin. Vaccine Immunol.
20
276-281
2013
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1
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1
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1
1
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728404
Neuenfeldt
Thermodynamic properties disti ...
Escherichia coli, Homo sapiens
Nucleic Acids Res.
41
2698-2708
2013
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2
1
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3
2
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3
3
728743
Fuengfuloy
Overproduction of the N-termin ...
Helicobacter pylori
Protein Expr. Purif.
89
25-32
2013
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1
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7
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728778
Kim
Crystal structure of human cyt ...
Homo sapiens
Proteins
81
1840-1846
2013
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714091
Messmer
A human pathology-related muta ...
Homo sapiens
Biochem. J.
433
441-446
2011
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2
2
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705213
Ul-Haq
Template-based structure predi ...
Homo sapiens, Mus musculus
J. Mol. Graph. Model.
28
401-412
2010
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2
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705605
Merritt
Crystal structure of the aspar ...
Entamoeba histolytica
Mol. Biochem. Parasitol.
169
95-100
2010
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1
1
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5
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702481
Messmer
Peculiar inhibition of human m ...
Bos taurus, Escherichia coli, Homo sapiens, Pseudomonas aeruginosa
Biochimie
91
596-603
2009
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4
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8
5
3
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4
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8
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4
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4
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4
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4
9
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4
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4
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8
9
5
3
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4
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4
-
4
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4
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704488
Charriere
Dual targeting of a tRNAAsp re ...
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2
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2
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Plasmodial aspartyl-tRNA synth ...
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3
1
2
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6
2
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3
4
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2
3
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1
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4
4
7
2
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3
3
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2
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3
1
2
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6
2
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Guzzo
Lysyl-tRNA synthetase interact ...
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2
-
1
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1
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Petit
Collision induced dissociation ...
Escherichia coli, Escherichia coli TG1
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2008
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692852
Kazakov
Escherichia coli peptidase A, ...
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J. Bacteriol.
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1
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1
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693741
Uluc
Leukoencephalopathy with brain ...
Homo sapiens
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2
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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
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1
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1
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694002
Bailly
tRNA-dependent asparagine form ...
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Methods
44
146-163
2008
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1
1
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1
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11
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1
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1
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1
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1
1
1
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1
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6
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1
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11
-
1
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1
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695032
Thompson
Probing electrostatic interact ...
Escherichia coli
Proteins
71
1450-1460
2008
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1
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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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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
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696373
Ryckelynck
Post-translational modificatio ...
Saccharomyces cerevisiae
Biochemistry
47
12476-12482
2008
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1
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2
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1
1
1
1
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2
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2
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2
1
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4
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1
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1
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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2
1
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-
4
-
-
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674863
Thompson
Ammonium scanning in an enzyme ...
Escherichia coli
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282
30856-30868
2007
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1
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1
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3
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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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3
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676127
Scheper
Mitochondrial aspartyl-tRNA sy ...
Homo sapiens
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534-539
2007
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1
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6
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3
1
1
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1
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1
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4
6
-
2
-
1
-
-
3
1
-
-
1
-
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-
1
1
-
6
-
-
-
-
3
1
1
-
1
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-
4
6
-
2
-
1
-
-
3
1
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676987
Guzzo
Systematic analysis of fusion ...
Homo sapiens
Protein Expr. Purif.
54
166-175
2007
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1
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1
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1
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4
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1
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5
-
1
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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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1
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1
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1
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5
-
1
-
1
-
-
-
1
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674587
Metlitskaya
Aspartyl-tRNA synthetase is th ...
Francisella tularensis
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281
18033-18042
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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
1
1
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1
1
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1
-
1
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1
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-
-
-
2
-
1
-
-
-
1
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674621
Thompson
Molecular dynamics simulations ...
Escherichia coli
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281
23792-23803
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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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1
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1
1
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1
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1
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-
-
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1
-
-
-
-
-
-
-
-
-
-
-
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-
657471
Moreno
Effects of macromolecular impu ...
Thermus thermophilus
Acta Crystallogr. Sect. D
61
789-792
2005
-
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-
1
-
-
-
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3
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1
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1
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-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
658121
Bonnefond
Toward the full set of human m ...
Homo sapiens
Biochemistry
44
4805-4816
2005
-
-
1
-
-
-
-
2
2
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3
-
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1
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1
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2
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1
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2
2
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1
-
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
658271
Bernier
Synthesis and aminoacyl-tRNA s ...
Escherichia coli
Bioorg. Med. Chem.
13
69-75
2005
-
-
-
-
-
-
4
-
-
-
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-
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2
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1
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-
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1
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3
-
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-
-
-
-
-
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4
3
-
-
-
-
-
-
-
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1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
659731
Ryckelynck
An intricate RNA structure wit ...
Saccharomyces cerevisiae
J. Mol. Biol.
354
614-629
2005
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-
-
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-
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3
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1
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-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
660032
Martin
Single amino acid changes in A ...
Escherichia coli
Nucleic Acids Res.
32
4081-4089
2004
-
-
-
-
9
-
-
8
-
-
-
-
-
3
-
-
-
-
-
-
-
-
1
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
9
-
-
-
-
8
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
650996
Charron
Non-discriminating and discrim ...
Thermococcus kodakarensis, Thermus thermophilus
EMBO J.
22
1632-1643
2003
-
-
2
1
1
-
-
5
-
-
-
4
-
6
-
-
2
2
-
-
1
-
6
-
2
-
-
5
2
-
-
-
-
-
-
-
-
2
-
1
1
-
-
-
-
5
-
-
-
4
-
-
-
2
-
-
1
-
6
-
2
-
-
5
2
-
-
-
-
-
-
-
-
-
651530
Cheong
Structure of the N-terminal ex ...
Homo sapiens
Int. J. Biochem. Cell Biol.
35
1548-1557
2003
-
-
-
-
-
-
-
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2
-
2
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-
-
-
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2
1
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-
-
-
-
-
-
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-
-
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-
-
-
-
-
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-
-
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2
-
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-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
652511
Ryckelynck
Yeast tRNA(Asp) charging accur ...
Saccharomyces cerevisiae
J. Biol. Chem.
278
9683-9690
2003
-
-
1
-
-
-
-
1
-
-
-
1
-
2
-
-
-
-
-
-
1
-
2
1
1
-
-
1
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
-
-
1
-
2
1
1
-
-
1
1
-
-
-
-
-
-
-
-
-
652920
Frugier
Yeast aspartyl-tRNA synthetase ...
Saccharomyces cerevisiae
J. Mol. Biol.
331
375-383
2003
-
-
1
-
1
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-
-
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2
-
2
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-
-
1
-
-
-
-
2
2
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
653872
Choi
Recognition of acceptor-stem s ...
Escherichia coli
RNA
9
386-393
2003
-
-
-
-
-
-
-
-
-
-
-
1
-
3
-
-
-
1
-
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-
-
3
-
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-
-
-
-
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-
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-
-
-
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-
-
-
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-
-
-
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-
-
1
-
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-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
659236
Brevet
Anticodon Recognition in Evolu ...
Escherichia coli
J. Biol. Chem.
278
30927-30935
2003
-
-
-
-
1
-
-
2
-
-
-
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1
-
-
1
-
-
-
-
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2
-
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-
-
2
-
-
-
-
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-
-
-
-
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-
1
-
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-
-
2
-
-
-
-
-
-
-
1
-
-
-
-
2
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
660355
Feng
Expanding tRNA recognition of ...
Thermococcus kodakarensis
Proc. Natl. Acad. Sci. USA
100
5676-5681
2003
-
-
-
-
3
-
-
7
-
-
-
-
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5
-
-
-
-
-
-
-
-
4
-
1
-
-
6
1
-
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
14
-
-
-
-
-
-
-
-
-
-
-
-
4
-
2
-
-
12
1
-
-
-
-
-
-
-
6
6
440091
Tumbula-Hansen
Evolutionary divergence of the ...
Ferroplasma acidarmanus, Methanothermobacter thermautotrophicus, Thermococcus kodakarensis
J. Biol. Chem.
277
37184-37190
2002
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3
-
-
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-
-
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8
-
9
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3
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-
-
-
-
13
-
2
1
-
-
3
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
8
-
-
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4
-
-
-
-
13
-
2
1
-
-
3
-
-
-
-
-
-
-
-
-
649182
Charron
Crystal contacts engineering o ...
Thermus thermophilus
Acta Crystallogr. Sect. D
58
1729-1733
2002
-
-
-
1
1
-
-
-
-
-
1
1
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2
-
-
-
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-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
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-
1
1
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
649141
Charron
Crystallization and preliminar ...
Thermus thermophilus
Acta Crystallogr. Sect. D
57
1177-1179
2001
-
-
-
1
-
-
-
-
-
-
1
1
-
3
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
649163
Zhu
Growth kinetics, diffraction p ...
Thermus thermophilus
Acta Crystallogr. Sect. D
57
552-558
2001
-
-
1
1
-
-
-
-
-
-
-
1
-
1
-
-
1
-
-
-
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
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Aspartyl tRNA-synthetase from ...
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The free yeast aspartyl-tRNA s ...
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Mimics of yeast tRNAAsp and th ...
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Yeast aspartyl-tRNA synthetase ...
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Existence of two distinct aspa ...
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Crystal structure of a prokary ...
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Yeast aspartyl-tRNA synthetase ...
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Sequence, overproduction and c ...
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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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-
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-
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-
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-
1
-
1
-
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1
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-
1
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Low molecular weight aspartyl- ...
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6
3
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1
3
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1
2
-
-
1
-
-
2
-
1
1
1
-
-
-
1
1
-
-
-
2
-
-
-
-
-
-
-
-
-
-
6
2
3
-
1
3
-
1
-
-
1
-
2
-
1
1
1
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1
1
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-
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5
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2
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1
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-
1
-
1
1
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-
-
-
-
-
-
-
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-
-
-
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5
-
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1
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1
-
1
1
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3
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3
2
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1
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1
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1
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1
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-
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-
3
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-
3
2
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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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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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1
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1
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1
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3
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4
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1
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1
1
2
1
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1
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1
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3
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4
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1
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1
1
2
1
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1
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1
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Amino acid substrate specifici ...
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19
3
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3
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1
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1
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1
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1
2
2
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1
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1
1
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1
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3
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19
1
3
-
3
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1
1
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1
2
2
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1
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1
1
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Gangloff
Studies on aspartyl-tRNA synth ...
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3
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2
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4
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1
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1
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1
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1
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3
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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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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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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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1
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1
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