Table 2. Structural superpositions of selected PR-10 proteins with the present MtN13 structure, represented by the protein chain from the MtN13–ZEA complex.
The superpositions were calculated with PDBeFold v.2.55 (Krissinel & Henrick, 2004 ▶).
| Protein structure | PDB code (chain ID)† | R.m.s.d. of Cα atoms (Å) | No. of aligned residues | Sequence identity (%) | Q score‡ |
|---|---|---|---|---|---|
| VrCSBP–ZEA | 2flh (A) | 1.45 | 135 | 22 | 0.63 |
| LlPR-10.1B | 1ifv (A) | 1.59 | 155 | 39 | 0.69 |
| LlPR-10.2B–ZEA | 2qim | 1.77 | 149 | 44 | 0.64 |
| LlPR-10.2B–DPU | 3e85 | 1.80 | 146 | 44 | 0.62 |
| Bet v 1a | 1bv1 | 1.80 | 152 | 44 | 0.65 |
| LlPR-10.1A | 1icx | 1.88 | 155 | 38 | 0.64 |
†
If more than one protein chain was present in the crystal structure, only the chain with the lowest r.m.s.d. was used in the analysis.
‡
The Q score represents the quality function of Cα alignment. It reduces the effect of the r.m.s.d./N algn (number of aligned residues) balance on the estimation of alignments: Q = (N algn·N algn)/{[1+(r.m.s.d./R 0)2]·N res1·N res2}, where N res1 and N res2 represent the number of residues in the aligned proteins and the empirical parameter R 0 is set to 3 Å.