Instrument

#1 Model Bruker DMX (500 MHz)

#2 Model Bruker DMX Avance (600 MHz)

Sample #1

Temperature 300 (±1) K, pH 7.4 (±0.2), Details Every sample was fully 15N,13C labeled, only for definite experiments we used a only 15N-labeled sample (TOCSY-15N-HSQC;NOESY-15N-HSQC;HNHB). For each NMR experiment a new sample was neccessary. So we did approximatly 17 samples for the oxidized state. 1 to 5 mM oxydized Adx samples were obtained from E. coli and purified as described elsewhere [8]. For 15N-labelled samples, 15NH4CL was used and for 13C-labelled samples, both 13C6-glucose and 13C3-glycerol were introduced into the growth medium. Purity of the protein was checked by measuring A414/A290>0.9 in Tris/HCl (50mM, pH=7.4) buffer.

Sample #2

Temperature 300 (±1) K, pH 7.4 (±0.2), Details Every sample was fully 15N,13C labeled, only for definite experiments we used a only 15N-labeled sample (TOCSY-15N-HSQC;NOESY-15N-HSQC;HNHB). For each NMR experiment a new sample was neccessary. So we did approximatly 17 samples for the oxidized state. 1 to 5 mM oxydized Adx samples were obtained from E. coli and purified as described elsewhere [8]. For 15N-labelled samples, 15NH4CL was used and for 13C-labelled samples, both 13C6-glucose and 13C3-glycerol were introduced into the growth medium. Purity of the protein was checked by measuring A414/A290>0.9 in Tris/HCl (50mM, pH=7.4) buffer.

Instrument

#1 Model Bruker DMX (500 MHz)

#2 Model Bruker DMX Avance (600 MHz)

Sample #1

Temperature 300 (±1) K, pH 7.4 (±0.2), Details Every sample was fully 15N,13C labeled, only for definite experiments we used a only 15N-labeled sample (TOCSY-15N-HSQC;NOESY-15N-HSQC;HNHB). For each NMR experiment a new sample was neccessary. So we did approximatly 17 samples for the oxidized state. 1 to 5 mM oxydized Adx samples were obtained from E. coli and purified as described elsewhere [8]. For 15N-labelled samples, 15NH4CL was used and for 13C-labelled samples, both 13C6-glucose and 13C3-glycerol were introduced into the growth medium. Purity of the protein was checked by measuring A414/A290>0.9 in Tris/HCl (50mM, pH=7.4) buffer.

Sample #2

Temperature 300 (±1) K, pH 7.4 (±0.2), Details Every sample was fully 15N,13C labeled, only for definite experiments we used a only 15N-labeled sample (TOCSY-15N-HSQC;NOESY-15N-HSQC;HNHB). For each NMR experiment a new sample was neccessary. So we did approximatly 17 samples for the oxidized state. 1 to 5 mM oxydized Adx samples were obtained from E. coli and purified as described elsewhere [8]. For 15N-labelled samples, 15NH4CL was used and for 13C-labelled samples, both 13C6-glucose and 13C3-glycerol were introduced into the growth medium. Purity of the protein was checked by measuring A414/A290>0.9 in Tris/HCl (50mM, pH=7.4) buffer.

Instrument

#1 Model Bruker DMX (500 MHz)

#2 Model Bruker DMX Avance (600 MHz)

Sample #1

Temperature 300 (±1) K, pH 7.4 (±0.2), Details Every sample was fully 15N,13C labeled, only for definite experiments we used a only 15N-labeled sample (TOCSY-15N-HSQC;NOESY-15N-HSQC;HNHB). For each NMR experiment a new sample was neccessary. So we did approximatly 17 samples for the oxidized state. 1 to 5 mM oxydized Adx samples were obtained from E. coli and purified as described elsewhere [8]. For 15N-labelled samples, 15NH4CL was used and for 13C-labelled samples, both 13C6-glucose and 13C3-glycerol were introduced into the growth medium. Purity of the protein was checked by measuring A414/A290>0.9 in Tris/HCl (50mM, pH=7.4) buffer.

Sample #2

Temperature 300 (±1) K, pH 7.4 (±0.2), Details Every sample was fully 15N,13C labeled, only for definite experiments we used a only 15N-labeled sample (TOCSY-15N-HSQC;NOESY-15N-HSQC;HNHB). For each NMR experiment a new sample was neccessary. So we did approximatly 17 samples for the oxidized state. 1 to 5 mM oxydized Adx samples were obtained from E. coli and purified as described elsewhere [8]. For 15N-labelled samples, 15NH4CL was used and for 13C-labelled samples, both 13C6-glucose and 13C3-glycerol were introduced into the growth medium. Purity of the protein was checked by measuring A414/A290>0.9 in Tris/HCl (50mM, pH=7.4) buffer.

Instrument

#1 Model Bruker DMX (500 MHz)

#2 Model Bruker DMX Avance (600 MHz)

Sample #1

Temperature 300 (±1) K, pH 7.4 (±0.2), Details Every sample was fully 15N,13C labeled, only for definite experiments we used a only 15N-labeled sample (TOCSY-15N-HSQC;NOESY-15N-HSQC;HNHB). For each NMR experiment a new sample was neccessary. So we did approximatly 17 samples for the oxidized state. 1 to 5 mM oxydized Adx samples were obtained from E. coli and purified as described elsewhere [8]. For 15N-labelled samples, 15NH4CL was used and for 13C-labelled samples, both 13C6-glucose and 13C3-glycerol were introduced into the growth medium. Purity of the protein was checked by measuring A414/A290>0.9 in Tris/HCl (50mM, pH=7.4) buffer.

Sample #2

Temperature 300 (±1) K, pH 7.4 (±0.2), Details Every sample was fully 15N,13C labeled, only for definite experiments we used a only 15N-labeled sample (TOCSY-15N-HSQC;NOESY-15N-HSQC;HNHB). For each NMR experiment a new sample was neccessary. So we did approximatly 17 samples for the oxidized state. 1 to 5 mM oxydized Adx samples were obtained from E. coli and purified as described elsewhere [8]. For 15N-labelled samples, 15NH4CL was used and for 13C-labelled samples, both 13C6-glucose and 13C3-glycerol were introduced into the growth medium. Purity of the protein was checked by measuring A414/A290>0.9 in Tris/HCl (50mM, pH=7.4) buffer.

Instrument

#1 Model Bruker DMX (500 MHz)

#2 Model Bruker DMX Avance (600 MHz)

Sample #1

Temperature 300 (±1) K, pH 7.4 (±0.2), Details Every sample was fully 15N,13C labeled, only for definite experiments we used a only 15N-labeled sample (TOCSY-15N-HSQC;NOESY-15N-HSQC;HNHB). For each NMR experiment a new sample was neccessary. So we did approximatly 17 samples for the oxidized state. 1 to 5 mM oxydized Adx samples were obtained from E. coli and purified as described elsewhere [8]. For 15N-labelled samples, 15NH4CL was used and for 13C-labelled samples, both 13C6-glucose and 13C3-glycerol were introduced into the growth medium. Purity of the protein was checked by measuring A414/A290>0.9 in Tris/HCl (50mM, pH=7.4) buffer.

Sample #2

Temperature 300 (±1) K, pH 7.4 (±0.2), Details Every sample was fully 15N,13C labeled, only for definite experiments we used a only 15N-labeled sample (TOCSY-15N-HSQC;NOESY-15N-HSQC;HNHB). For each NMR experiment a new sample was neccessary. So we did approximatly 17 samples for the oxidized state. 1 to 5 mM oxydized Adx samples were obtained from E. coli and purified as described elsewhere [8]. For 15N-labelled samples, 15NH4CL was used and for 13C-labelled samples, both 13C6-glucose and 13C3-glycerol were introduced into the growth medium. Purity of the protein was checked by measuring A414/A290>0.9 in Tris/HCl (50mM, pH=7.4) buffer.

Instrument

#1 Model Bruker DMX (500 MHz)

#2 Model Bruker DMX Avance (600 MHz)

Sample #1

Temperature 300 (±1) K, pH 7.4 (±0.2), Details Every sample was fully 15N,13C labeled, only for definite experiments we used a only 15N-labeled sample (TOCSY-15N-HSQC;NOESY-15N-HSQC;HNHB). For each NMR experiment a new sample was neccessary. So we did approximatly 17 samples for the oxidized state. 1 to 5 mM oxydized Adx samples were obtained from E. coli and purified as described elsewhere [8]. For 15N-labelled samples, 15NH4CL was used and for 13C-labelled samples, both 13C6-glucose and 13C3-glycerol were introduced into the growth medium. Purity of the protein was checked by measuring A414/A290>0.9 in Tris/HCl (50mM, pH=7.4) buffer.

Sample #2

Temperature 300 (±1) K, pH 7.4 (±0.2), Details Every sample was fully 15N,13C labeled, only for definite experiments we used a only 15N-labeled sample (TOCSY-15N-HSQC;NOESY-15N-HSQC;HNHB). For each NMR experiment a new sample was neccessary. So we did approximatly 17 samples for the oxidized state. 1 to 5 mM oxydized Adx samples were obtained from E. coli and purified as described elsewhere [8]. For 15N-labelled samples, 15NH4CL was used and for 13C-labelled samples, both 13C6-glucose and 13C3-glycerol were introduced into the growth medium. Purity of the protein was checked by measuring A414/A290>0.9 in Tris/HCl (50mM, pH=7.4) buffer.

Instrument

#1 Model Bruker DMX (500 MHz)

#2 Model Bruker DMX Avance (600 MHz)

Sample #1

Temperature 300 (±1) K, pH 7.4 (±0.2), Details Every sample was fully 15N,13C labeled, only for definite experiments we used a only 15N-labeled sample (TOCSY-15N-HSQC;NOESY-15N-HSQC;HNHB). For each NMR experiment a new sample was neccessary. So we did approximatly 17 samples for the oxidized state. 1 to 5 mM oxydized Adx samples were obtained from E. coli and purified as described elsewhere [8]. For 15N-labelled samples, 15NH4CL was used and for 13C-labelled samples, both 13C6-glucose and 13C3-glycerol were introduced into the growth medium. Purity of the protein was checked by measuring A414/A290>0.9 in Tris/HCl (50mM, pH=7.4) buffer.

Sample #2

Temperature 300 (±1) K, pH 7.4 (±0.2), Details Every sample was fully 15N,13C labeled, only for definite experiments we used a only 15N-labeled sample (TOCSY-15N-HSQC;NOESY-15N-HSQC;HNHB). For each NMR experiment a new sample was neccessary. So we did approximatly 17 samples for the oxidized state. 1 to 5 mM oxydized Adx samples were obtained from E. coli and purified as described elsewhere [8]. For 15N-labelled samples, 15NH4CL was used and for 13C-labelled samples, both 13C6-glucose and 13C3-glycerol were introduced into the growth medium. Purity of the protein was checked by measuring A414/A290>0.9 in Tris/HCl (50mM, pH=7.4) buffer.

Instrument

#1 Model Bruker DMX (500 MHz)

#2 Model Bruker DMX Avance (600 MHz)

Sample #1

Temperature 300 (±1) K, pH 7.4 (±0.2), Details Every sample was fully 15N,13C labeled, only for definite experiments we used a only 15N-labeled sample (TOCSY-15N-HSQC;NOESY-15N-HSQC;HNHB). For each NMR experiment a new sample was neccessary. So we did approximatly 17 samples for the oxidized state. 1 to 5 mM oxydized Adx samples were obtained from E. coli and purified as described elsewhere [8]. For 15N-labelled samples, 15NH4CL was used and for 13C-labelled samples, both 13C6-glucose and 13C3-glycerol were introduced into the growth medium. Purity of the protein was checked by measuring A414/A290>0.9 in Tris/HCl (50mM, pH=7.4) buffer.

Sample #2

Temperature 300 (±1) K, pH 7.4 (±0.2), Details Every sample was fully 15N,13C labeled, only for definite experiments we used a only 15N-labeled sample (TOCSY-15N-HSQC;NOESY-15N-HSQC;HNHB). For each NMR experiment a new sample was neccessary. So we did approximatly 17 samples for the oxidized state. 1 to 5 mM oxydized Adx samples were obtained from E. coli and purified as described elsewhere [8]. For 15N-labelled samples, 15NH4CL was used and for 13C-labelled samples, both 13C6-glucose and 13C3-glycerol were introduced into the growth medium. Purity of the protein was checked by measuring A414/A290>0.9 in Tris/HCl (50mM, pH=7.4) buffer.

Instrument

#1 Model Bruker DMX (500 MHz)

#2 Model Bruker DMX Avance (600 MHz)

Sample #1

Temperature 300 (±1) K, pH 7.4 (±0.2), Details Every sample was fully 15N,13C labeled, only for definite experiments we used a only 15N-labeled sample (TOCSY-15N-HSQC;NOESY-15N-HSQC;HNHB). For each NMR experiment a new sample was neccessary. So we did approximatly 17 samples for the oxidized state. 1 to 5 mM oxydized Adx samples were obtained from E. coli and purified as described elsewhere [8]. For 15N-labelled samples, 15NH4CL was used and for 13C-labelled samples, both 13C6-glucose and 13C3-glycerol were introduced into the growth medium. Purity of the protein was checked by measuring A414/A290>0.9 in Tris/HCl (50mM, pH=7.4) buffer.

Sample #2

Temperature 300 (±1) K, pH 7.4 (±0.2), Details Every sample was fully 15N,13C labeled, only for definite experiments we used a only 15N-labeled sample (TOCSY-15N-HSQC;NOESY-15N-HSQC;HNHB). For each NMR experiment a new sample was neccessary. So we did approximatly 17 samples for the oxidized state. 1 to 5 mM oxydized Adx samples were obtained from E. coli and purified as described elsewhere [8]. For 15N-labelled samples, 15NH4CL was used and for 13C-labelled samples, both 13C6-glucose and 13C3-glycerol were introduced into the growth medium. Purity of the protein was checked by measuring A414/A290>0.9 in Tris/HCl (50mM, pH=7.4) buffer.

Instrument

#1 Model Bruker DMX (500 MHz)

#2 Model Bruker DMX Avance (600 MHz)

Sample #1

Temperature 300 (±1) K, pH 7.4 (±0.2), Details Every sample was fully 15N,13C labeled, only for definite experiments we used a only 15N-labeled sample (TOCSY-15N-HSQC;NOESY-15N-HSQC;HNHB). For each NMR experiment a new sample was neccessary. So we did approximatly 17 samples for the oxidized state. 1 to 5 mM oxydized Adx samples were obtained from E. coli and purified as described elsewhere [8]. For 15N-labelled samples, 15NH4CL was used and for 13C-labelled samples, both 13C6-glucose and 13C3-glycerol were introduced into the growth medium. Purity of the protein was checked by measuring A414/A290>0.9 in Tris/HCl (50mM, pH=7.4) buffer.

Sample #2

Temperature 300 (±1) K, pH 7.4 (±0.2), Details Every sample was fully 15N,13C labeled, only for definite experiments we used a only 15N-labeled sample (TOCSY-15N-HSQC;NOESY-15N-HSQC;HNHB). For each NMR experiment a new sample was neccessary. So we did approximatly 17 samples for the oxidized state. 1 to 5 mM oxydized Adx samples were obtained from E. coli and purified as described elsewhere [8]. For 15N-labelled samples, 15NH4CL was used and for 13C-labelled samples, both 13C6-glucose and 13C3-glycerol were introduced into the growth medium. Purity of the protein was checked by measuring A414/A290>0.9 in Tris/HCl (50mM, pH=7.4) buffer.

Instrument

#1 Model Bruker DMX (500 MHz)

#2 Model Bruker DMX Avance (600 MHz)

Sample #1

Temperature 300 (±1) K, pH 7.4 (±0.2), Details Every sample was fully 15N,13C labeled, only for definite experiments we used a only 15N-labeled sample (TOCSY-15N-HSQC;NOESY-15N-HSQC;HNHB). For each NMR experiment a new sample was neccessary. So we did approximatly 17 samples for the oxidized state. 1 to 5 mM oxydized Adx samples were obtained from E. coli and purified as described elsewhere [8]. For 15N-labelled samples, 15NH4CL was used and for 13C-labelled samples, both 13C6-glucose and 13C3-glycerol were introduced into the growth medium. Purity of the protein was checked by measuring A414/A290>0.9 in Tris/HCl (50mM, pH=7.4) buffer.

Sample #2

Temperature 300 (±1) K, pH 7.4 (±0.2), Details Every sample was fully 15N,13C labeled, only for definite experiments we used a only 15N-labeled sample (TOCSY-15N-HSQC;NOESY-15N-HSQC;HNHB). For each NMR experiment a new sample was neccessary. So we did approximatly 17 samples for the oxidized state. 1 to 5 mM oxydized Adx samples were obtained from E. coli and purified as described elsewhere [8]. For 15N-labelled samples, 15NH4CL was used and for 13C-labelled samples, both 13C6-glucose and 13C3-glycerol were introduced into the growth medium. Purity of the protein was checked by measuring A414/A290>0.9 in Tris/HCl (50mM, pH=7.4) buffer.

Instrument

#1 Model Bruker DMX (500 MHz)

#2 Model Bruker DMX Avance (600 MHz)

Sample #1

Temperature 300 (±1) K, pH 7.4 (±0.2), Details Every sample was fully 15N,13C labeled, only for definite experiments we used a only 15N-labeled sample (TOCSY-15N-HSQC;NOESY-15N-HSQC;HNHB). For each NMR experiment a new sample was neccessary. So we did approximatly 17 samples for the oxidized state. 1 to 5 mM oxydized Adx samples were obtained from E. coli and purified as described elsewhere [8]. For 15N-labelled samples, 15NH4CL was used and for 13C-labelled samples, both 13C6-glucose and 13C3-glycerol were introduced into the growth medium. Purity of the protein was checked by measuring A414/A290>0.9 in Tris/HCl (50mM, pH=7.4) buffer.

Sample #2

Temperature 300 (±1) K, pH 7.4 (±0.2), Details Every sample was fully 15N,13C labeled, only for definite experiments we used a only 15N-labeled sample (TOCSY-15N-HSQC;NOESY-15N-HSQC;HNHB). For each NMR experiment a new sample was neccessary. So we did approximatly 17 samples for the oxidized state. 1 to 5 mM oxydized Adx samples were obtained from E. coli and purified as described elsewhere [8]. For 15N-labelled samples, 15NH4CL was used and for 13C-labelled samples, both 13C6-glucose and 13C3-glycerol were introduced into the growth medium. Purity of the protein was checked by measuring A414/A290>0.9 in Tris/HCl (50mM, pH=7.4) buffer.

Instrument

#1 Model Bruker DMX (500 MHz)

#2 Model Bruker DMX Avance (600 MHz)

Sample #1

Temperature 300 (±1) K, pH 7.4 (±0.2), Details Every sample was fully 15N,13C labeled, only for definite experiments we used a only 15N-labeled sample (TOCSY-15N-HSQC;NOESY-15N-HSQC;HNHB). For each NMR experiment a new sample was neccessary. So we did approximatly 17 samples for the oxidized state. 1 to 5 mM oxydized Adx samples were obtained from E. coli and purified as described elsewhere [8]. For 15N-labelled samples, 15NH4CL was used and for 13C-labelled samples, both 13C6-glucose and 13C3-glycerol were introduced into the growth medium. Purity of the protein was checked by measuring A414/A290>0.9 in Tris/HCl (50mM, pH=7.4) buffer.

Sample #2

Temperature 300 (±1) K, pH 7.4 (±0.2), Details Every sample was fully 15N,13C labeled, only for definite experiments we used a only 15N-labeled sample (TOCSY-15N-HSQC;NOESY-15N-HSQC;HNHB). For each NMR experiment a new sample was neccessary. So we did approximatly 17 samples for the oxidized state. 1 to 5 mM oxydized Adx samples were obtained from E. coli and purified as described elsewhere [8]. For 15N-labelled samples, 15NH4CL was used and for 13C-labelled samples, both 13C6-glucose and 13C3-glycerol were introduced into the growth medium. Purity of the protein was checked by measuring A414/A290>0.9 in Tris/HCl (50mM, pH=7.4) buffer.