Table 2.
Estimation of the secondary structure content of the prepared proteins using the least-squares method (LSA)51 analysing amide I & II bands in infrared spectra (N marks values normalized to 100%).
| NKR-P1BWAG | Clr-11 | mouse Clr-g | |||
|---|---|---|---|---|---|
| Structure | LSA (%) | LSA N (%) | LSA (%) | LSA N (%) | crystal structure* |
| α-helix | 21 ± 10 | 20 | 23 ± 10 | 22 | 17 |
| β-sheet | 28 ± 9 | 27 | 25 ± 9 | 24 | 27 |
| β-turn | 14 ± 4 | 13 | 13 ± 4 | 12 | 12 |
| Bend | 15 ± 4 | 14 | 14 ± 4 | 13 | 15 |
| Disordered | 27 ± 6 | 26 | 30 ± 6 | 29 | 29 |
| Sum | 105% | 100% | 105% | 100% | 100% |
| NKR-P1BSD monomer | NKR-P1BSD dimer | NKR-P1BSD dimer | |||
| Structure | LSA (%) | LSA N (%) | LSA (%) | LSA N (%) | crystal structure* |
| α-helix | 23 ± 10 | 22 | 23 ± 10 | 22 | 19 |
| β-sheet | 28 ± 9 | 26 | 28 ± 9 | 26 | 28 |
| β-turn | 14 ± 4 | 13 | 14 ± 4 | 13 | 15 |
| Bend | 16 ± 4 | 15 | 16 ± 4 | 15 | 13 |
| Disordered | 26 ± 6 | 24 | 26 ± 6 | 24 | 25 |
| Sum | 107% | 100% | 107% | 100% | 100% |
Given standard deviations are calculated as standard deviations of the used reference set; therefore, they do not reflect the quality of the fits. *Calculated using DSSP58 on the crystal structures of mouse Clr-g (PDB ID 3RS1)29 and rat NKR-P1BSD dimer (PDB ID 5J2S). However, in the NKR-P1BSD crystal structure, only 118 amino acid residues are visible, i.e., 29 residues (20%), fewer than those present in the expressed protein construct.Given standard deviations are calculated as standard deviations of the used reference set; therefore, they do not reflect the quality of the fits.