Table 1.
RMSD analysis of mutants against their wild types
| Protein (ID) | Variants studied | No. of mutants (same/diff.*) | Most deviated residues† | Affected region‡ |
|---|---|---|---|---|
| T4 lysozyme (3lzm) | 62 | 191 (113/78) | Asn-40, Gly-77 | α-Helix termini, α-helix termini |
| Myoglobin (105m) | 54 | 104 (86/18) | Gly-121, His-48 | Coil, coil |
| Transthyretin (1bmz A) | 9 | 9 (6/3) | Ser-100, Gly-101 | Coil, coil |
| HIV aspartic proteinase (1dif A) | 5 | 7 (4/3) | Gly-51, Ser-37 | Coil, coil |
| Barnase | 10 | 13 (10/3) | Lys-66, Gly-40 | Coil, coil |
| Lactoferrin (1bka) | 4 | 4 (3/1) | Arg-313, Pro-284 | Coil, coil |
| Dihydrofolate reductase (4dfr A) | 5 | 6 (4/2) | Ser-135, Gly-67 | β-Strand, coil |
| α-1-antitrypsin (2psi) | 3 | 10 (5/5) | Ala-350 | Coil |
| BP-RNase A (1rph) | 3 | 5 (1/4) | Ser-21 | Coil |
| Adenylate kinase (1ake A) | 2 | 3 (1/2) | Glu-113, Thr-158 | Coil, β-strand termini |
| Calmodulin (4cln) | 2 | 2 (deletions) | Gly-113 | Coil |
Summary of the mutational analysis. The PDB codes (in parentheses) of only the wild-type proteins are listed. Mutant PDB codes are listed in Appendix A, (Supplemental Data).
Because a structure may contain several amino acid substitutions, the number of variants in the second column differs from the number of mutants in the third column.
*
Mutations of similar or different types of residues (hydrophobic/hydrophilic).
†
Residue positions of the highest and second-highest deviations.
‡
Regions in the structure where the highest and second-highest distance deviations fall, corresponding to column 3.