CNRS Nantes University US2B US2B
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CA distance fluctuations for 2607171153561942151

---  normal mode 16  ---

This matrix displays the maximum distance fluctuations between all pairs of CA atoms and between the two extreme conformations that were computed for this mode (DQMIN/DQMAX). Distance increases are plotted in blue and decreases in red for the strongest 10% of the residue pair distance changes. Every pixel corresponds to a single residue. Grey lines are drawn every 10 residues, yellow lines every 100 residues (counting from the upper left corner).

The following table indicates for every residue the two corresponding residues with the strongest CA distance fluctuations.

[HELP on distance fluctuations]

GD ok
largest increasereflargest decrease
PRO 700 0.18 MET 1 -0.15 LYS 122
PRO 700 0.19 SER 2 -0.13 LYS 122
PRO 700 0.20 ARG 3 -0.10 LYS 122
PRO 700 0.21 ILE 4 -0.09 LYS 112
PRO 700 0.22 GLU 5 -0.08 GLU 160
LEU 699 0.23 LYS 6 -0.09 GLU 160
LEU 699 0.24 MET 7 -0.09 GLU 160
LEU 699 0.25 SER 8 -0.09 GLU 160
LEU 699 0.26 ILE 9 -0.07 GLU 160
LEU 699 0.27 LEU 10 -0.06 LYS 20
LEU 699 0.27 GLY 11 -0.07 ASP 19
LEU 699 0.26 VAL 12 -0.06 GLU 160
LEU 699 0.27 ARG 13 -0.06 ALA 135
LEU 699 0.29 SER 14 -0.05 ALA 135
LEU 699 0.29 PHE 15 -0.05 GLU 160
LEU 699 0.30 GLY 16 -0.07 LYS 20
LEU 699 0.30 ILE 17 -0.10 ALA 80
LEU 699 0.31 GLU 18 -0.10 ALA 80
LEU 699 0.30 ASP 19 -0.11 ALA 80
LEU 699 0.33 LYS 20 -0.08 ALA 80
LEU 699 0.31 ASP 21 -0.07 LYS 20
LEU 699 0.29 LYS 22 -0.06 GLN 81
LEU 699 0.30 GLN 23 -0.07 GLU 160
LEU 699 0.28 ILE 24 -0.08 GLU 160
LEU 699 0.27 ILE 25 -0.11 GLU 160
LEU 699 0.25 THR 26 -0.11 GLU 160
PRO 700 0.25 PHE 27 -0.10 GLU 160
PRO 700 0.26 PHE 28 -0.10 GLU 160
PRO 700 0.24 SER 29 -0.11 HIS 733
PRO 700 0.24 PRO 30 -0.11 HIS 733
PRO 700 0.26 LEU 31 -0.08 VAL 159
PRO 700 0.27 THR 32 -0.10 VAL 159
PRO 700 0.28 ILE 33 -0.11 THR 133
LEU 699 0.29 LEU 34 -0.13 GLY 134
LEU 699 0.31 VAL 35 -0.17 GLY 134
LEU 699 0.32 GLY 36 -0.18 ALA 135
LEU 699 0.31 PRO 37 -0.19 ALA 135
LEU 699 0.29 ASN 38 -0.16 ALA 135
LEU 699 0.28 GLY 39 -0.14 ALA 135
LEU 699 0.30 ALA 40 -0.14 ALA 135
LEU 699 0.28 GLY 41 -0.12 ALA 135
LEU 699 0.27 LYS 42 -0.13 ALA 135
LEU 699 0.25 THR 43 -0.12 ALA 135
LEU 699 0.25 THR 44 -0.10 ALA 135
LEU 699 0.24 ILE 45 -0.11 ALA 135
LEU 699 0.23 ILE 46 -0.10 ALA 135
LEU 699 0.22 GLU 47 -0.09 ALA 135
LEU 699 0.22 CYS 48 -0.09 ALA 135
LEU 699 0.21 LEU 49 -0.09 GLU 160
LEU 699 0.20 LYS 50 -0.11 GLY 63
LEU 699 0.20 TYR 51 -0.13 LYS 112
LEU 699 0.20 ILE 52 -0.12 LYS 112
PRO 700 0.18 CYS 53 -0.14 LYS 112
LEU 699 0.18 THR 54 -0.18 LYS 112
LEU 699 0.19 GLY 55 -0.23 LYS 112
LEU 699 0.19 ASP 56 -0.26 GLY 63
LEU 699 0.20 PHE 57 -0.14 ASN 152
LEU 699 0.20 PRO 58 -0.10 ARG 69
LEU 699 0.20 PRO 59 -0.12 LYS 108
LEU 699 0.20 GLY 60 -0.14 LYS 108
LEU 699 0.22 THR 61 -0.12 LYS 108
LEU 699 0.21 LYS 62 -0.20 ASP 56
LEU 750 0.22 GLY 63 -0.26 ASP 56
LEU 699 0.24 ASN 64 -0.17 ASP 56
LEU 699 0.25 THR 65 -0.12 ASP 56
LEU 699 0.24 PHE 66 -0.11 ASP 56
LEU 699 0.25 VAL 67 -0.09 ASP 56
LEU 699 0.28 HIS 68 -0.06 ASP 56
LEU 699 0.30 ASP 69 -0.11 THR 65
LEU 699 0.31 PRO 70 -0.11 CYS 133
ASP 1294 0.37 LYS 71 -0.10 CYS 133
GLN 1295 0.47 VAL 72 -0.07 GLY 60
ASP 1294 0.45 ALA 73 -0.08 CYS 133
ASP 1294 0.43 GLN 74 -0.09 CYS 133
LEU 699 0.33 GLU 75 -0.11 CYS 133
LEU 699 0.31 THR 76 -0.14 CYS 133
LEU 699 0.28 ASP 77 -0.14 CYS 133
LEU 750 0.28 VAL 78 -0.12 MET 100
LEU 750 0.34 ARG 79 -0.14 MET 100
LEU 750 0.31 ALA 80 -0.11 ASP 19
LEU 750 0.31 GLN 81 -0.10 ASP 19
LEU 750 0.23 ILE 82 -0.07 GLU 160
LEU 699 0.22 HIS 83 -0.07 GLU 160
LEU 699 0.21 LEU 84 -0.08 LYS 112
PRO 700 0.20 GLN 85 -0.07 LYS 112
PRO 700 0.20 PHE 86 -0.09 LYS 112
PRO 700 0.19 ARG 87 -0.12 LYS 122
PRO 700 0.18 ASP 88 -0.14 LYS 122
PRO 700 0.18 VAL 89 -0.15 ASN 1224
PRO 700 0.17 ASN 90 -0.18 LYS 122
PRO 700 0.17 GLY 91 -0.17 LYS 122
PRO 700 0.17 GLU 92 -0.23 LYS 122
PRO 700 0.18 LEU 93 -0.11 LYS 122
PRO 700 0.18 ILE 94 -0.09 LYS 112
LEU 699 0.19 ALA 95 -0.08 LYS 112
LEU 699 0.19 VAL 96 -0.11 LYS 112
LEU 750 0.22 GLN 97 -0.08 LYS 112
LEU 750 0.27 ARG 98 -0.11 LYS 112
LEU 750 0.35 SER 99 -0.07 ASP 19
LEU 750 0.31 MET 100 -0.14 VAL 101
LEU 750 0.31 VAL 101 -0.15 CYS 133
LEU 699 0.26 CYS 102 -0.16 CYS 133
LEU 699 0.27 THR 103 -0.17 CYS 133
LEU 699 0.29 GLN 104 -0.15 CYS 133
LEU 699 0.29 LYS 105 -0.18 ALA 134
ASP 1294 0.31 SER 106 -0.18 ALA 134
ASP 1294 0.31 LYS 107 -0.17 ALA 134
LEU 699 0.28 LYS 108 -0.20 ALA 134
LEU 699 0.27 THR 109 -0.16 ALA 134
LEU 699 0.24 GLU 110 -0.21 CYS 133
LEU 699 0.22 PHE 111 -0.24 CYS 133
LEU 750 0.23 LYS 112 -0.34 CYS 133
LEU 750 0.26 THR 113 -0.26 LYS 112
LEU 750 0.34 LEU 114 -0.13 CYS 133
LEU 750 0.31 GLU 115 -0.09 LYS 132
LEU 750 0.25 GLY 116 -0.09 VAL 117
LEU 750 0.19 VAL 117 -0.09 GLY 116
LEU 699 0.18 ILE 118 -0.09 LYS 112
LEU 699 0.18 THR 119 -0.08 GLN 1259
PRO 700 0.17 ARG 120 -0.11 GLU 92
PRO 700 0.16 THR 121 -0.17 GLU 92
PRO 700 0.14 LYS 122 -0.23 GLU 92
PRO 700 0.14 HIS 123 -0.18 GLU 92
PRO 700 0.15 GLY 124 -0.16 GLN 1259
LEU 699 0.15 GLU 125 -0.15 GLU 92
LEU 699 0.17 LYS 126 -0.13 GLU 92
LEU 699 0.16 VAL 127 -0.12 GLU 92
LEU 699 0.17 SER 128 -0.08 GLN 1259
LEU 699 0.16 LEU 129 -0.07 GLN 1259
LEU 699 0.17 SER 130 -0.06 GLN 1259
LEU 699 0.17 SER 131 -0.13 LYS 112
LEU 699 0.17 LYS 132 -0.22 LYS 112
LEU 699 0.18 CYS 133 -0.34 LYS 112
LEU 699 0.16 ALA 134 -0.26 LYS 112
LEU 699 0.16 GLU 135 -0.20 LYS 112
LEU 699 0.17 ILE 136 -0.20 LYS 112
PRO 700 0.17 ASP 137 -0.23 LYS 112
PRO 700 0.16 ARG 138 -0.20 LYS 112
PRO 700 0.17 GLU 139 -0.17 LYS 112
PRO 700 0.17 MET 140 -0.16 LYS 112
PRO 700 0.17 ILE 141 -0.17 LYS 112
PRO 700 0.16 SER 142 -0.15 LYS 112
PRO 700 0.17 SER 143 -0.13 LYS 112
PRO 700 0.18 LEU 144 -0.13 LYS 112
PRO 700 0.17 GLY 145 -0.13 LYS 112
PRO 700 0.18 VAL 146 -0.14 LYS 112
PRO 700 0.17 SER 147 -0.17 LYS 108
PRO 700 0.17 LYS 148 -0.19 LYS 108
PRO 700 0.17 ALA 149 -0.19 LYS 108
PRO 700 0.18 VAL 150 -0.15 LYS 108
PRO 700 0.19 LEU 151 -0.13 LYS 108
PRO 700 0.18 ASN 152 -0.15 LYS 62
PRO 700 0.19 ASN 153 -0.14 LYS 108
PRO 700 0.19 VAL 154 -0.11 LYS 108
PRO 700 0.20 ILE 155 -0.09 GLY 63
PRO 700 0.20 PHE 156 -0.09 SER 68
PRO 700 0.20 CYS 157 -0.11 SER 68
LEU 699 0.21 HIS 158 -0.12 ARG 69
LEU 699 0.22 GLN 159 -0.14 ARG 69
LEU 699 0.21 GLU 160 -0.14 ARG 69
LEU 699 0.19 ASP 161 -0.14 ARG 69
PRO 700 0.20 SER 162 -0.14 ASP 1270
PRO 700 0.20 ASN 163 -0.13 ARG 69
PRO 700 0.19 TRP 164 -0.11 ARG 69
PRO 700 0.19 PRO 165 -0.11 LYS 108
PRO 700 0.19 LEU 166 -0.11 ASP 1238
ASN 38 0.22 SER 1202 -0.19 ASP 1238
ASN 38 0.25 ALA 1203 -0.20 ASP 1238
ASN 38 0.23 GLY 1204 -0.26 ASP 1238
PRO 700 0.21 GLN 1205 -0.18 ASP 1238
PRO 700 0.21 LYS 1206 -0.16 ASP 1238
PRO 700 0.22 VAL 1207 -0.14 ASP 1238
PRO 700 0.22 LEU 1208 -0.14 ASP 1238
PRO 700 0.21 ALA 1209 -0.12 ASP 1238
PRO 700 0.20 SER 1210 -0.12 ASP 1238
PRO 700 0.21 LEU 1211 -0.10 ASP 1238
PRO 700 0.21 ILE 1212 -0.12 GLN 1205
PRO 700 0.20 ILE 1213 -0.10 ASP 1238
PRO 700 0.20 ARG 1214 -0.10 ASN 1241
PRO 700 0.20 LEU 1215 -0.12 ASN 1241
PRO 700 0.19 ALA 1216 -0.13 ASN 1241
PRO 700 0.19 LEU 1217 -0.11 VAL 146
PRO 700 0.19 ALA 1218 -0.11 ASN 1241
PRO 700 0.19 GLU 1219 -0.13 ASN 1241
PRO 700 0.18 THR 1220 -0.12 ASN 1241
PRO 700 0.18 PHE 1221 -0.12 LYS 108
PRO 700 0.18 CYS 1222 -0.11 ASN 1241
PRO 700 0.18 LEU 1223 -0.12 LYS 122
PRO 700 0.18 ASN 1224 -0.15 VAL 89
PRO 700 0.19 CYS 1225 -0.11 LYS 122
PRO 700 0.20 GLY 1226 -0.11 LYS 122
PRO 700 0.21 ILE 1227 -0.08 LYS 112
PRO 700 0.21 ILE 1228 -0.08 SER 68
PRO 700 0.22 ALA 1229 -0.09 SER 68
PRO 700 0.23 LEU 1230 -0.12 VAL 1274
LEU 699 0.23 ASP 1231 -0.13 SER 68
LEU 699 0.25 GLU 1232 -0.18 ASP 1270
PRO 700 0.24 PRO 1233 -0.14 ASP 1270
PRO 700 0.26 THR 1234 -0.15 SER 68
ASN 38 0.26 THR 1235 -0.17 SER 68
ASN 38 0.27 ASN 1236 -0.17 ARG 69
PRO 700 0.25 LEU 1237 -0.14 SER 68
PRO 700 0.28 ASP 1238 -0.26 GLY 1204
PRO 700 0.29 ARG 1239 -0.15 GLY 1204
PRO 700 0.27 GLU 1240 -0.18 SER 273
PRO 700 0.25 ASN 1241 -0.13 ALA 1248
PRO 700 0.27 ILE 1242 -0.11 LEU 1237
PRO 700 0.27 GLU 1243 -0.11 THR 272
PRO 700 0.25 SER 1244 -0.13 ASN 1241
PRO 700 0.24 LEU 1245 -0.09 GLU 1219
PRO 700 0.26 ALA 1246 -0.08 ARG 1279
PRO 700 0.24 HIS 1247 -0.10 ASN 227
PRO 700 0.23 ALA 1248 -0.13 ASN 1241
PRO 700 0.24 LEU 1249 -0.09 HIS 733
PRO 700 0.24 VAL 1250 -0.09 HIS 733
PRO 700 0.22 GLU 1251 -0.11 HIS 733
PRO 700 0.22 ILE 1252 -0.12 HIS 733
PRO 700 0.23 ILE 1253 -0.12 HIS 733
PRO 700 0.22 LYS 1254 -0.13 HIS 733
PRO 700 0.20 SER 1255 -0.13 HIS 733
PRO 700 0.20 ARG 1256 -0.14 HIS 733
PRO 700 0.21 SER 1257 -0.16 HIS 733
PRO 700 0.19 GLN 1258 -0.17 HIS 733
PRO 700 0.18 GLN 1259 -0.19 GLN 732
PRO 700 0.19 ARG 1260 -0.17 HIS 733
PRO 700 0.20 ASN 1261 -0.16 HIS 733
PRO 700 0.21 PHE 1262 -0.13 HIS 733
PRO 700 0.23 GLN 1263 -0.10 HIS 733
PRO 700 0.24 LEU 1264 -0.08 HIS 733
PRO 700 0.24 LEU 1265 -0.09 VAL 159
PRO 700 0.26 VAL 1266 -0.10 THR 133
LEU 699 0.26 ILE 1267 -0.12 GLY 134
LEU 699 0.28 THR 1268 -0.13 SER 68
LEU 699 0.30 HIS 1269 -0.16 LYS 66
PRO 700 0.32 ASP 1270 -0.18 GLU 1232
PRO 700 0.35 GLU 1271 -0.17 SER 68
PRO 700 0.33 ASP 1272 -0.17 SER 68
PRO 700 0.31 PHE 1273 -0.12 SER 68
PRO 700 0.33 VAL 1274 -0.13 GLU 1232
PRO 700 0.34 GLU 1275 -0.11 ASN 65
PRO 700 0.31 LEU 1276 -0.09 LEU 1237
PRO 700 0.29 LEU 1277 -0.10 GLY 1278
PRO 700 0.32 GLY 1278 -0.10 LEU 1277
PRO 700 0.32 ARG 1279 -0.08 LEU 1237
PRO 700 0.29 SER 1280 -0.08 ALA 1246
PRO 700 0.31 GLU 1281 -0.06 PRO 185
PRO 700 0.29 TYR 1282 -0.08 ARG 188
PRO 700 0.31 VAL 1283 -0.10 VAL 159
PRO 700 0.33 GLU 1284 -0.14 VAL 159
PRO 700 0.33 LYS 1285 -0.14 VAL 159
PRO 700 0.32 PHE 1286 -0.13 VAL 159
LEU 699 0.31 TYR 1287 -0.12 VAL 159
LEU 699 0.33 ARG 1288 -0.16 ALA 135
LEU 699 0.32 ILE 1289 -0.13 ALA 135
LEU 699 0.34 LYS 1290 -0.12 ALA 135
LEU 699 0.34 LYS 1291 -0.10 ALA 135
LEU 699 0.35 ASN 1292 -0.09 SER 158
VAL 72 0.37 ILE 1293 -0.08 SER 158
VAL 72 0.46 ASP 1294 -0.08 LYS 20
VAL 72 0.47 GLN 1295 -0.07 SER 158
VAL 72 0.40 CYS 1296 -0.07 SER 158
LEU 699 0.31 SER 1297 -0.07 SER 158
LEU 699 0.32 GLU 1298 -0.09 GLU 160
LEU 699 0.32 ILE 1299 -0.10 GLU 160
LEU 699 0.34 VAL 1300 -0.12 GLU 160
LEU 699 0.33 LYS 1301 -0.14 GLU 160
LEU 699 0.37 CYS 1302 -0.16 VAL 159
PRO 700 0.37 SER 1303 -0.20 VAL 159
PRO 700 0.38 VAL 1304 -0.15 VAL 159
PRO 700 0.43 SER 1305 -0.14 MET 157
PRO 700 0.47 SER 1306 -0.13 MET 157
ARG 87 0.07 GLU 10 -0.52 LYS 698
SER 209 0.07 ASN 11 -0.51 LYS 698
SER 209 0.06 THR 12 -0.37 LYS 698
ASP 53 0.07 PHE 13 -0.27 PRO 694
ILE 289 0.07 LYS 14 -0.27 PRO 694
PRO 700 0.08 ILE 15 -0.21 PRO 694
PRO 700 0.13 LEU 16 -0.17 PRO 694
PRO 700 0.16 VAL 17 -0.14 PRO 694
PRO 700 0.20 ALA 18 -0.11 PRO 694
PRO 700 0.24 THR 19 -0.09 LEU 1237
PRO 700 0.28 ASP 20 -0.10 LEU 1237
PRO 700 0.28 ILE 21 -0.10 LEU 1237
PRO 700 0.31 HIS 22 -0.11 LEU 1237
PRO 700 0.34 LEU 23 -0.12 ASN 1236
PRO 700 0.34 GLY 24 -0.14 ASN 1236
PRO 700 0.30 PHE 25 -0.15 ARG 1239
PRO 700 0.29 MET 26 -0.15 ARG 1239
PRO 700 0.31 GLU 27 -0.13 ASN 1236
PRO 700 0.31 LYS 28 -0.14 ALA 1203
PRO 700 0.27 ASP 29 -0.11 SER 1202
PRO 700 0.25 ALA 30 -0.10 SER 1202
PRO 700 0.22 VAL 31 -0.08 SER 1202
PRO 700 0.24 ARG 32 -0.10 ARG 1239
PRO 700 0.27 GLY 33 -0.11 ALA 1203
PRO 700 0.26 ASN 34 -0.11 ALA 1203
PRO 700 0.23 ASP 35 -0.11 ARG 1239
PRO 700 0.26 THR 36 -0.11 ARG 1239
PRO 700 0.28 PHE 37 -0.11 ASN 1236
PRO 700 0.23 VAL 38 -0.10 ASN 1236
PRO 700 0.21 THR 39 -0.09 ARG 1239
PRO 700 0.25 LEU 40 -0.10 ASN 1236
PRO 700 0.23 ASP 41 -0.10 ASN 1236
PRO 700 0.17 GLU 42 -0.11 PRO 694
PRO 700 0.18 ILE 43 -0.12 PRO 694
PRO 700 0.20 LEU 44 -0.11 PRO 694
PRO 700 0.15 ARG 45 -0.13 PRO 694
PRO 700 0.11 LEU 46 -0.16 PRO 694
PRO 700 0.13 ALA 47 -0.17 PRO 694
PRO 700 0.12 GLN 48 -0.17 PRO 694
PRO 700 0.06 GLU 49 -0.18 PRO 694
ARG 288 0.06 ASN 50 -0.20 PRO 694
LYS 290 0.05 GLU 51 -0.24 PRO 694
PRO 700 0.06 VAL 52 -0.23 PRO 694
PRO 700 0.07 ASP 53 -0.27 PRO 694
PRO 700 0.19 PHE 54 -0.19 PRO 694
PRO 700 0.23 ILE 55 -0.14 PRO 694
PRO 700 0.25 LEU 56 -0.12 PRO 694
PRO 700 0.29 LEU 57 -0.08 PRO 694
PRO 700 0.28 GLY 58 -0.08 PRO 694
PRO 700 0.34 GLY 59 -0.08 LEU 1237
PRO 700 0.35 ASP 60 -0.09 LEU 1237
PRO 700 0.36 LEU 61 -0.09 ASN 1236
PRO 700 0.38 PHE 62 -0.10 ASN 1236
PRO 700 0.34 HIS 63 -0.11 LEU 1237
PRO 700 0.38 GLU 64 -0.16 ASP 1272
PRO 700 0.42 ASN 65 -0.15 ASP 1272
PRO 700 0.44 LYS 66 -0.16 HIS 1269
PRO 700 0.43 PRO 67 -0.15 GLU 1271
PRO 700 0.42 SER 68 -0.17 THR 1235
PRO 700 0.45 ARG 69 -0.17 ASN 1236
PRO 700 0.38 LYS 70 -0.15 ASN 1236
PRO 700 0.38 THR 71 -0.13 ASN 1236
PRO 700 0.44 LEU 72 -0.14 HIS 1269
PRO 700 0.42 HIS 73 -0.13 ASN 1236
PRO 700 0.36 THR 74 -0.11 ASN 1236
PRO 700 0.38 CYS 75 -0.11 HIS 1269
PRO 700 0.43 LEU 76 -0.12 HIS 1269
PRO 700 0.36 GLU 77 -0.10 HIS 1269
PRO 700 0.31 LEU 78 -0.09 ASN 1236
PRO 700 0.35 LEU 79 -0.10 HIS 1269
PRO 700 0.36 ARG 80 -0.10 HIS 1269
PRO 700 0.28 LYS 81 -0.09 HIS 1269
PRO 700 0.24 TYR 82 -0.09 PRO 694
PRO 700 0.29 CYS 83 -0.08 HIS 1269
GLY 697 0.31 MET 84 -0.08 PRO 37
GLY 697 0.25 GLY 85 -0.07 PRO 37
GLY 697 0.20 ASP 86 -0.09 GLY 705
ALA 696 0.13 ARG 87 -0.14 PRO 694
ALA 696 0.10 PRO 88 -0.20 PRO 694
PRO 700 0.10 VAL 89 -0.29 PRO 694
VAL 89 0.08 GLN 90 -0.44 PRO 694
GLU 205 0.06 PHE 91 -0.38 PRO 694
ARG 69 0.07 GLU 92 -0.18 GLY 695
PRO 700 0.25 ILE 93 -0.14 GLY 704
PRO 700 0.11 LEU 94 -0.16 ALA 696
PRO 700 0.37 SER 95 -0.24 GLY 704
PRO 700 0.65 ASP 96 -0.27 GLY 705
PRO 700 0.87 GLN 97 -0.18 GLY 705
PRO 700 1.02 SER 98 -0.13 GLY 705
PRO 700 0.73 VAL 99 -0.12 ILE 709
PRO 700 0.63 ASN 100 -0.11 SER 165
PRO 700 0.77 PHE 101 -0.11 GLY 102
PRO 700 0.90 GLY 102 -0.11 PHE 101
PRO 700 0.79 PHE 103 -0.09 PRO 37
PRO 700 0.84 SER 104 -0.09 PRO 37
PRO 700 0.93 LYS 105 -0.08 PRO 37
PRO 700 1.00 PHE 106 -0.09 GLY 705
PRO 700 1.08 PRO 107 -0.10 GLY 705
PRO 700 1.04 TRP 108 -0.15 GLY 705
PRO 700 0.72 VAL 109 -0.12 GLY 705
PRO 700 0.60 ASN 110 -0.12 GLY 705
PRO 700 0.47 TYR 111 -0.11 GLY 705
ALA 696 0.66 GLN 112 -0.15 GLY 705
LYS 698 0.73 ASP 113 -0.16 GLY 114
GLY 697 0.91 GLY 114 -0.18 GLY 705
GLY 697 0.69 ASN 115 -0.14 GLY 705
GLY 697 0.55 LEU 116 -0.12 GLY 705
GLY 697 0.41 ASN 117 -0.11 GLY 705
ALA 696 0.35 ILE 118 -0.08 GLY 705
PRO 700 0.22 SER 119 -0.12 PRO 694
PRO 700 0.23 ILE 120 -0.14 PRO 694
PRO 700 0.33 PRO 121 -0.11 PRO 694
PRO 700 0.36 VAL 122 -0.09 PRO 694
PRO 700 0.39 PHE 123 -0.08 PRO 37
PRO 700 0.40 SER 124 -0.08 HIS 1269
PRO 700 0.41 ILE 125 -0.08 HIS 1269
PRO 700 0.43 HIS 126 -0.09 HIS 1269
PRO 700 0.36 GLY 127 -0.08 HIS 1269
PRO 700 0.35 ASN 128 -0.08 LEU 1237
PRO 700 0.36 HIS 129 -0.10 ASP 1272
PRO 700 0.42 ASP 130 -0.11 HIS 1269
PRO 700 0.44 ASP 131 -0.11 HIS 1269
PRO 700 0.50 PRO 132 -0.12 HIS 1269
PRO 700 0.48 THR 133 -0.15 HIS 1269
PRO 700 0.50 GLY 134 -0.17 PRO 37
LEU 699 0.54 ALA 135 -0.19 PRO 37
PRO 700 0.60 ASP 136 -0.17 PRO 37
PRO 700 0.56 ALA 137 -0.14 PRO 37
PRO 700 0.58 LEU 138 -0.14 PRO 37
PRO 700 0.53 CYS 139 -0.12 HIS 1269
PRO 700 0.51 ALA 140 -0.12 HIS 1269
PRO 700 0.54 LEU 141 -0.10 HIS 1269
PRO 700 0.62 ASP 142 -0.11 PRO 37
PRO 700 0.59 ILE 143 -0.11 PRO 37
PRO 700 0.55 LEU 144 -0.10 HIS 1269
PRO 700 0.65 SER 145 -0.10 PRO 37
PRO 700 0.69 CYS 146 -0.11 PRO 37
PRO 700 0.60 ALA 147 -0.11 PRO 37
PRO 700 0.62 GLY 148 -0.09 PRO 37
PRO 700 0.49 PHE 149 -0.08 PRO 37
PRO 700 0.50 VAL 150 -0.08 PRO 37
PRO 700 0.57 ASN 151 -0.08 PRO 37
PRO 700 0.57 HIS 152 -0.09 PRO 37
PRO 700 0.54 PHE 153 -0.09 PRO 37
PRO 700 0.46 GLY 154 -0.09 SER 1305
PRO 700 0.51 ARG 155 -0.12 SER 1305
PRO 700 0.49 SER 156 -0.14 SER 1305
PRO 700 0.55 MET 157 -0.14 SER 1305
PRO 700 0.48 SER 158 -0.18 SER 1303
PRO 700 0.41 VAL 159 -0.20 SER 1303
PRO 700 0.37 GLU 160 -0.16 SER 1303
PRO 700 0.36 LYS 161 -0.13 SER 1303
PRO 700 0.37 ILE 162 -0.12 SER 1303
PRO 700 0.36 ASP 163 -0.10 SER 1303
PRO 700 0.33 ILE 164 -0.09 SER 1305
PRO 700 0.36 SER 165 -0.11 ASN 100
PRO 700 0.27 PRO 166 -0.08 ASN 100
PRO 700 0.33 VAL 167 -0.07 PRO 37
PRO 700 0.15 LEU 168 -0.07 GLY 695
PRO 700 0.08 LEU 169 -0.14 GLY 695
GLU 205 0.06 GLN 170 -0.37 HIS 701
VAL 89 0.05 LYS 171 -0.43 GLY 695
SER 209 0.06 GLY 172 -0.61 LYS 698
SER 209 0.09 SER 173 -0.64 LEU 699
SER 209 0.07 THR 174 -0.47 HIS 701
SER 209 0.06 LYS 175 -0.43 HIS 701
GLN 74 0.05 ILE 176 -0.25 HIS 701
PRO 700 0.07 ALA 177 -0.13 HIS 701
PRO 700 0.19 LEU 178 -0.09 PRO 694
PRO 700 0.24 TYR 179 -0.07 PRO 37
PRO 700 0.33 GLY 180 -0.08 SER 1305
PRO 700 0.35 LEU 181 -0.09 SER 1305
PRO 700 0.40 GLY 182 -0.09 SER 1305
PRO 700 0.35 SER 183 -0.08 HIS 1269
PRO 700 0.35 ILE 184 -0.08 GLU 1284
PRO 700 0.32 PRO 185 -0.08 TYR 1282
PRO 700 0.27 ASP 186 -0.08 HIS 1247
PRO 700 0.26 GLU 187 -0.07 HIS 1247
PRO 700 0.30 ARG 188 -0.08 TYR 1282
PRO 700 0.27 LEU 189 -0.08 ALA 713
PRO 700 0.23 TYR 190 -0.07 HIS 1247
PRO 700 0.25 ARG 191 -0.07 SER 738
PRO 700 0.26 MET 192 -0.09 ALA 713
PRO 700 0.20 PHE 193 -0.10 ALA 713
PRO 700 0.19 VAL 194 -0.09 ALA 734
PRO 700 0.22 ASN 195 -0.11 SER 738
GLY 705 0.22 LYS 196 -0.11 ALA 713
PRO 700 0.26 LYS 197 -0.10 SER 1303
PRO 700 0.24 VAL 198 -0.10 SER 1303
GLY 705 0.25 THR 199 -0.09 ALA 713
GLY 705 0.22 MET 200 -0.08 SER 1303
GLY 705 0.26 LEU 201 -0.10 ASN 100
GLY 705 0.14 ARG 202 -0.10 GLY 697
GLY 704 0.09 PRO 203 -0.20 HIS 701
GLY 704 0.08 LYS 204 -0.23 HIS 701
SER 173 0.07 GLU 205 -0.41 HIS 701
SER 173 0.07 ASP 206 -0.52 HIS 701
SER 173 0.06 GLU 207 -0.37 HIS 701
SER 173 0.07 ASN 208 -0.39 HIS 701
SER 173 0.09 SER 209 -0.47 HIS 701
LEU 201 0.05 TRP 210 -0.37 HIS 701
GLN 74 0.04 PHE 211 -0.28 HIS 701
GLY 705 0.06 ASN 212 -0.17 HIS 701
PRO 700 0.08 LEU 213 -0.12 PRO 694
PRO 700 0.15 PHE 214 -0.09 PRO 694
PRO 700 0.23 VAL 215 -0.08 PRO 694
PRO 700 0.25 ILE 216 -0.07 LEU 1237
PRO 700 0.28 HIS 217 -0.08 LEU 1237
PRO 700 0.26 GLN 218 -0.08 GLU 1243
PRO 700 0.22 ASN 219 -0.10 GLU 1243
PRO 700 0.17 ARG 220 -0.10 GLU 1240
PRO 700 0.14 SER 221 -0.10 GLU 1240
PRO 700 0.16 LYS 222 -0.10 GLU 1240
PRO 700 0.17 HIS 223 -0.10 GLU 1240
PRO 700 0.19 GLY 224 -0.10 SER 1244
PRO 700 0.18 SER 225 -0.12 VAL 729
PRO 700 0.20 THR 226 -0.10 VAL 729
PRO 700 0.23 ASN 227 -0.10 HIS 1247
PRO 700 0.21 PHE 228 -0.09 HIS 1247
PRO 700 0.19 ILE 229 -0.08 SER 1244
PRO 700 0.14 PRO 230 -0.08 GLU 1240
PRO 700 0.10 GLU 231 -0.08 ASN 208
GLY 705 0.10 GLN 232 -0.09 ASN 208
GLY 705 0.13 PHE 233 -0.08 ASN 208
GLY 705 0.13 LEU 234 -0.07 LEU 189
GLY 705 0.12 ASP 235 -0.08 ASN 208
GLY 705 0.08 ASP 236 -0.14 HIS 701
GLY 705 0.06 PHE 237 -0.19 HIS 701
GLY 705 0.07 ILE 238 -0.15 HIS 701
MET 296 0.05 ASP 239 -0.20 HIS 701
MET 296 0.05 LEU 240 -0.14 HIS 701
PRO 700 0.10 VAL 241 -0.10 PRO 694
PRO 700 0.15 ILE 242 -0.11 PRO 694
PRO 700 0.18 TRP 243 -0.09 PRO 694
PRO 700 0.23 GLY 244 -0.09 GLU 1243
PRO 700 0.26 HIS 245 -0.10 GLU 1243
PRO 700 0.20 GLU 246 -0.11 GLU 1240
PRO 700 0.20 HIS 247 -0.12 GLU 1240
PRO 700 0.15 GLU 248 -0.12 GLU 1240
PRO 700 0.12 CYS 249 -0.11 PRO 694
PRO 700 0.09 LYS 250 -0.11 PRO 694
PRO 700 0.08 ILE 251 -0.13 PRO 694
LYS 298 0.06 ALA 252 -0.14 PRO 694
GLY 285 0.05 PRO 253 -0.14 PRO 694
LYS 298 0.06 THR 254 -0.13 LEU 699
VAL 72 0.04 LYS 255 -0.16 LEU 699
GLY 705 0.05 ASN 256 -0.13 LEU 699
GLN 1259 0.05 GLU 257 -0.17 LEU 699
ARG 714 0.05 GLN 258 -0.16 LEU 699
GLY 705 0.06 GLN 259 -0.14 HIS 701
ALA 713 0.05 LEU 260 -0.21 LEU 699
TYR 262 0.05 PHE 261 -0.18 HIS 701
PHE 261 0.05 TYR 262 -0.15 HIS 701
GLY 705 0.06 ILE 263 -0.11 PRO 694
PRO 700 0.08 SER 264 -0.12 PRO 694
PRO 700 0.13 GLN 265 -0.10 PRO 694
PRO 700 0.14 PRO 266 -0.11 PRO 694
PRO 700 0.17 GLY 267 -0.10 GLU 1240
PRO 700 0.21 SER 268 -0.11 ARG 1239
PRO 700 0.21 SER 269 -0.11 ARG 1239
PRO 700 0.22 VAL 270 -0.12 ARG 1239
PRO 700 0.21 VAL 271 -0.13 GLU 1240
PRO 700 0.25 THR 272 -0.16 GLU 1240
PRO 700 0.23 SER 273 -0.18 GLU 1240
PRO 700 0.20 LEU 274 -0.16 GLU 1240
LYS 1254 0.19 SER 275 -0.14 GLU 1240
SER 1255 0.18 PRO 276 -0.12 GLU 1240
PRO 700 0.15 GLY 277 -0.11 GLU 1240
PRO 700 0.17 GLU 278 -0.13 GLU 1240
PRO 700 0.13 ALA 279 -0.11 GLU 1240
PRO 700 0.11 VAL 280 -0.10 PRO 694
PRO 700 0.10 LYS 281 -0.11 PRO 694
PRO 700 0.13 LYS 282 -0.10 ARG 1239
PRO 700 0.11 HIS 283 -0.13 PRO 694
PRO 700 0.12 VAL 284 -0.14 PRO 694
PRO 700 0.07 GLY 285 -0.17 PRO 694
ASN 295 0.05 LEU 286 -0.19 PRO 694
MET 294 0.04 LEU 287 -0.20 PRO 694
ASN 50 0.06 ARG 288 -0.24 LYS 698
LYS 14 0.07 ILE 289 -0.30 LEU 699
THR 12 0.06 LYS 290 -0.41 LEU 699
ASN 208 0.05 GLY 291 -0.46 LEU 699
LYS 14 0.04 ARG 292 -0.38 LEU 699
LYS 14 0.05 LYS 293 -0.35 LEU 699
ASN 50 0.05 MET 294 -0.28 LEU 699
GLU 49 0.05 ASN 295 -0.25 LEU 699
LEU 240 0.05 MET 296 -0.18 PRO 694
PHE 261 0.05 HIS 297 -0.18 PRO 694
ALA 252 0.06 LYS 298 -0.17 PRO 694
GLN 1259 0.05 ILE 299 -0.17 PRO 694
PRO 700 0.08 PRO 300 -0.14 PRO 694
PRO 700 0.12 LEU 301 -0.12 PRO 694
PRO 700 0.10 HIS 302 -0.13 PRO 694
PRO 700 0.15 THR 303 -0.10 PRO 694
PRO 700 0.16 VAL 304 -0.10 ARG 1239
PRO 700 0.17 ARG 305 -0.10 ARG 1239
GLY 697 0.41 LYS 690 -0.17 GLY 705
ALA 696 0.26 VAL 691 -0.15 GLY 705
ALA 696 0.22 THR 692 -0.14 GLY 705
ILE 118 0.13 TYR 693 -0.15 PRO 694
GLY 114 0.13 PRO 694 -0.44 GLN 90
GLN 112 0.43 GLY 695 -0.54 GLY 172
GLY 114 0.72 ALA 696 -0.30 GLY 172
GLY 114 0.91 GLY 697 -0.35 GLY 172
PHE 106 0.83 LYS 698 -0.62 SER 173
LYS 105 0.90 LEU 699 -0.64 SER 173
PRO 107 1.08 PRO 700 -0.43 SER 173
SER 98 0.75 HIS 701 -0.60 SER 173
ASP 96 0.50 ILE 702 -0.25 GLY 697
SER 98 0.15 ILE 703 -0.19 GLY 697
SER 165 0.25 GLY 704 -0.24 SER 95
ASP 163 0.33 GLY 705 -0.27 ASP 96
LYS 197 0.14 SER 706 -0.15 GLY 697
LYS 197 0.09 ASP 707 -0.18 GLY 697
GLY 705 0.20 LEU 708 -0.12 GLY 697
GLY 705 0.15 ILE 709 -0.12 VAL 99
GLY 705 0.22 ALA 710 -0.10 VAL 99
GLY 705 0.14 HIS 711 -0.09 SER 1303
GLY 705 0.13 HIS 712 -0.09 SER 1303
GLY 705 0.11 ALA 713 -0.11 LYS 196
GLN 258 0.05 ARG 714 -0.15 HIS 701
GLY 705 0.05 LYS 715 -0.14 HIS 701
GLY 705 0.07 ASN 716 -0.12 HIS 701
GLY 705 0.07 THR 717 -0.09 ASN 208
GLY 705 0.08 GLU 718 -0.11 ASN 208
GLY 705 0.11 LEU 719 -0.09 ASN 208
GLY 705 0.12 GLU 720 -0.10 ALA 734
GLY 705 0.12 GLU 721 -0.08 GLY 124
GLY 705 0.13 TRP 722 -0.07 GLY 124
GLY 705 0.16 LEU 723 -0.10 ALA 734
GLY 705 0.15 ARG 724 -0.11 ALA 734
GLY 705 0.14 GLN 725 -0.09 GLY 124
PRO 700 0.16 GLU 726 -0.10 SER 225
PRO 700 0.18 MET 727 -0.13 ALA 734
PRO 700 0.16 GLU 728 -0.13 GLN 1258
PRO 700 0.18 VAL 729 -0.16 GLN 1258
PRO 700 0.21 GLN 730 -0.14 GLN 1258
PRO 700 0.20 ASN 731 -0.16 ALA 734
PRO 700 0.19 GLN 732 -0.19 GLN 1259
PRO 700 0.21 HIS 733 -0.18 GLN 1259
PRO 700 0.22 ALA 734 -0.16 ASN 731
PRO 700 0.20 LYS 735 -0.14 GLN 1259
PRO 700 0.20 GLU 736 -0.14 GLN 1259
PRO 700 0.22 GLU 737 -0.10 GLN 1259
PRO 700 0.21 SER 738 -0.11 ASN 195
PRO 700 0.19 LEU 739 -0.10 GLN 1259
PRO 700 0.20 ALA 740 -0.08 GLN 1259
LEU 699 0.22 ASP 741 -0.10 ASN 195
LEU 699 0.20 ASP 742 -0.09 ASN 195
LEU 699 0.19 LEU 743 -0.08 TYR 746
LEU 699 0.22 PHE 744 -0.08 LYS 197
LEU 699 0.23 ARG 745 -0.08 ALA 713
LEU 699 0.21 TYR 746 -0.08 ALA 713
LEU 699 0.22 ASN 747 -0.07 ALA 713
LEU 699 0.20 PRO 748 -0.07 ALA 713
ARG 79 0.22 TYR 749 -0.07 ALA 713
SER 99 0.35 LEU 750 -0.11 VAL 127

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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Between 2015 and 2025, it was hosted by US2B (Nantes).
Last modification: april 24th, 2026.