Mutations to Proline
| Codon | Amino acid | Number of Mutations |
Secondary Structure |
Phi | Psi | Disallowed? |
|---|---|---|---|---|---|---|
| 96 | ser | 1 | - | - | -157.73 | YES |
| 110 | arg | 4 | E | -144.137 | 151.752 | YES |
| 111 | leu | 2 | E | -113.239 | 147.026 | YES |
| 116 | ser | 1 | - | -76.39 | -39.217 | YES |
| 127 | ser | 3 | E | -109.949 | 100.816 | YES |
| 136 | gln | 2 | - | -100.488 | 152.672 | YES |
| 137 | leu | 3 | T | -56.519 | 131.157 | YES |
| 138 | ala | 14 | T | 71.046 | -6.909 | YES |
| 140 | thr | 2 | - | -66.207 | 125.858 | |
| 144 | gln | 5 | E | -92.668 | 136.71 | YES |
| 145 | leu | 8 | E | -100.898 | 118.692 | YES |
| 149 | ser | 3 | S | -146.477 | 133.016 | YES |
| 155 | thr | 11 | - | -61.553 | 129.245 | |
| 156 | arg | 22 | E | -119.194 | 161.537 | YES |
| 158 | arg | 13 | E | -127.57 | 139.746 | YES |
| 159 | ala | 21 | E | -119.554 | 146.868 | YES |
| 161 | ala | 1 | E | -106.536 | 157.296 | YES |
| 165 | gln | 3 | S | -71.981 | 138.63 | YES |
| 166 | ser | 1 | T | -40.607 | -64.889 | YES |
| 168 | his | 3 | G | -66.524 | -13.923 | YES |
| 170 | thr | 1 | G | -88.444 | -18.605 | YES |
| 175 | arg | 4 | - | -65.109 | 147.266 | YES |
| 178 | his | 7 | H | -56.791 | -61.784 | YES |
| 179 | his | 3 | H | -57.75 | -31.935 | YES |
| 181 | arg | 11 | H | -62.976 | -43.551 | YES |
| 183 | ser | 2 | - | -62.278 | 154.117 | YES |
| 189 | ala | 3 | - | -63.187 | 129.726 | |
| 193 | his | 7 | - | -70.794 | 133.586 | YES |
| 194 | leu | 9 | S | -81.987 | -44.986 | YES |
| 196 | arg | 11 | E | -122.688 | 161.578 | YES |
| 202 | arg | 3 | T | -115.442 | 7.853 | YES |
| 213 | arg | 3 | - | -37.348 | 132.738 | YES |
| 214 | his | 1 | E | -102.983 | 146.49 | YES |
| 241 | ser | 6 | T | -92.341 | 12.954 | YES |
| 247 | asn | 1 | T | 44.311 | 28.416 | YES |
| 248 | arg | 11 | T | 86.753 | 7.922 | YES |
| 252 | leu | 8 | E | -118.307 | 137.257 | YES |
| 253 | thr | 2 | E | -103.296 | 127.718 | YES |
| 257 | leu | 10 | E | -83.297 | 136.58 | YES |
| 260 | ser | 1 | T | -47.916 | -18.882 | YES |
| 264 | leu | 1 | E | -63.609 | 126.162 | YES |
| 265 | leu | 10 | E | -114.011 | -21.378 | YES |
| 267 | arg | 8 | E | -158.106 | 140.954 | YES |
| 271 | glu | 1 | E | -89.422 | 163.063 | YES |
| 273 | arg | 20 | E | -126.608 | 110.838 | YES |
| 276 | ala | 15 | S | -90.697 | 143.622 | YES |
| 282 | arg | 10 | H | -80.193 | -38.59 | YES |
| 283 | arg | 21 | H | -50.147 | -57.613 | YES |
| 284 | thr | 4 | H | -52.739 | -57.402 | YES |
| 289 | leu | 3 | - | 90.022 | -- | YES |
Mutations to proline occurring in the DNA binding domain of p53. Allowed backbone torsion angles for proline are defined as -70≤phi≤-50 and (-70≤psi≤-50 or 110≤psi≤130). Secondary structure as assigned by DSSP in the parent is indicated (C: coil, E: β-strand, H: α-helix, T: turn, S: bend, G: 310-helix). Mutations where the parent amino acid was in a region disallowed for proline are flagged, as are prolines in alpha-helices or non-edge-strands of beta sheets.