Table 2.
Distances for BSL-AC, BSL-CD, and BSL-AJ P450cam in Various Conformational States, Measured from DEER, Crystal Structures, and MD Simulationsa
| state | BSL-CD distance (Å) |
BSL-AC distance (Å) |
BSL-AJ distance (Å) |
|||||
|---|---|---|---|---|---|---|---|---|
| crystal | DEER | MD | crystal | DEER | MD | crystal | DEER | |
| P450cam with cam | 36.7 | 44.6(4) | 45.2(3) | 43.1 | 54.7(4) | 54.2(6) | 32.84 | 40.1(1) |
| P450cam | 36.4 | 41.3(2) | 43.4(4) | 42.4 | 54.6(3) | 53.5(3) | 32.54 | 40.0(0) |
| P450cam with cam and Pdx | 35.8 | 39.4(9) | 41.0(3) | 42.9 | 55.5(6) | 55.8(9) | 32.76 | 40.0(0) |
a
DEER distance standard deviations (shown in parentheses) were calculated from three separate measurements, two from different protein batches and one from a repeated measurement of the same sample. The standard deviations for MD distances are based on three separate production runs, with the distances measured between the two nitrogen atoms of the spin-label. The distances from crystal structures are the distances between Cα atoms at Q110 and S35 (BSL-AC), at Q110 and C136 (BSL-CD), or at S35 and E276 (BSL-AJ) using PDB entries 3L61, 3L63, and 4JWS.