TABLE 2.
Secondary-structure analysis of RrgA recombinant proteins by CD spectroscopya
| Structure | Content (%) |
||||||
|---|---|---|---|---|---|---|---|
| RrgA clade I | RrgA D444A | RrgA clade II | NT | CP-1 | CP-2 | CT-long | |
| Helix | 23.60 | 25.70 | 21.30 | 19.80 | 26.80 | 29.90 | 10.90 |
| Antiparallel | 19.00 | 17.60 | 21.00 | 10.90 | 14.60 | 13.60 | 27.40 |
| Parallel | 6.10 | 6.20 | 6.20 | 4.10 | 5.70 | 5.90 | 5.20 |
| Beta turn | 15.30 | 15.00 | 15.50 | 28.60 | 16.70 | 15.50 | 22.20 |
| Random coil | 31.40 | 30.80 | 31.90 | 35.40 | 31.20 | 30.20 | 36.50 |
| Total | 95.40 | 95.20 | 95.80 | 98.90 | 95.20 | 95.00 | 102.10 |
a
Analysis of the CD spectra (see Fig. S1 in the supplemental material) was performed using CDNN v.2.1, including unit conversion to Δɛ units.