Table 5.
Escherichia coli residue | Atoma | rBfAvr ± rBfStdDev (count)b | E. coli residue | Atoma | rBfAvr ± rBfStdDev (count)b |
---|---|---|---|---|---|
Substrate | A1 (CB) | 0.990 ± 0.280 (120) | Thr89 | C2 (CB) | 0.658 ± 0.168 (95) |
A2 (OD1) | 0.913 ± 0.267 (120) | n2 (OG1) | 0.685 ± 0.169 (95) | ||
RC (CG) | 1.013 ± 0.302 (120) | Lys162 | CL (CE) | 0.700 ± 0.182 (88) | |
L (NH2,OH) | 1.009 ± 0.286 (120) | NZ (NZ) | 0.721 ± 0.190 (88) | ||
Thr12 | C1 (CB) | 1.024 ± 0.334 (111) | Tyr25 | CT (CZ) | 1.539 ± 0.633 (66) |
n1 (OG1) | 1.036 ± 0.361 (111) | OH (OH) | 1.503 ± 0.717 (66) |
The names of the atoms used in this analysis defined in Figure 2 are shown in bold and are followed by conventional names of these atoms (in parentheses).
For each included atom i the value of rBfAvr = rBf = Bfatom/<Bfstructure>, represents average over all structures of l‐asparaginases included here, followed by associated value of a standard deviation (± rBfStdDev) and number of independent active sites used in calculations (in parenthesis).