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Table 2 Comparison of KD values for the wild type and mutant 6 × His-ATD2B proteins.

From: Structural insights into phenylethanolamines high-affinity binding site in NR2B from binding and molecular modeling studies

Protein

KD (nM)

Fold Shift

WT

60 ± 18

1

F176A

331 ± 122

5.5

D101A

173 ± 52

2.9

F176A/D101A

627 ± 295

10.5

I150A

139 ± 28

2.3

D113A

48 ± 15

0.8

  1. Values are mean ± S.E. of the KD values from five experiments using proteins obtained from at least two independent batches of bacteria induction. The fold shift in KD values for each mutant is the ratio of KD(mutant) to KD(WT).