CNRS Nantes University US2B US2B
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CA distance fluctuations for 2607170838011899107

---  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
HIS 733 0.12 MET 1 -0.19 PRO 700
HIS 733 0.10 SER 2 -0.20 PRO 700
HIS 733 0.11 ARG 3 -0.22 PRO 700
LYS 112 0.08 ILE 4 -0.23 PRO 700
GLU 160 0.09 GLU 5 -0.24 PRO 700
GLU 160 0.10 LYS 6 -0.25 LEU 699
GLU 160 0.09 MET 7 -0.25 LEU 699
GLU 160 0.09 SER 8 -0.27 LEU 699
GLU 160 0.07 ILE 9 -0.28 LEU 699
GLU 160 0.06 LEU 10 -0.29 LEU 699
ASP 19 0.06 GLY 11 -0.29 LEU 699
GLU 160 0.06 VAL 12 -0.27 LEU 699
ALA 135 0.06 ARG 13 -0.28 LEU 699
SER 158 0.06 SER 14 -0.31 LEU 699
GLU 160 0.06 PHE 15 -0.31 LEU 699
LYS 20 0.07 GLY 16 -0.32 LEU 699
ALA 80 0.10 ILE 17 -0.32 LEU 699
ALA 80 0.09 GLU 18 -0.33 LEU 699
GLN 81 0.09 ASP 19 -0.32 LEU 699
ASP 1294 0.09 LYS 20 -0.35 LEU 699
LYS 20 0.06 ASP 21 -0.33 LEU 699
GLU 160 0.06 LYS 22 -0.31 LEU 699
GLU 160 0.08 GLN 23 -0.31 LEU 699
GLU 160 0.09 ILE 24 -0.29 LEU 699
GLU 160 0.12 ILE 25 -0.28 LEU 699
GLU 160 0.12 THR 26 -0.27 PRO 700
GLU 160 0.11 PHE 27 -0.27 PRO 700
GLU 160 0.11 PHE 28 -0.27 PRO 700
HIS 733 0.11 SER 29 -0.26 PRO 700
HIS 733 0.11 PRO 30 -0.26 PRO 700
VAL 159 0.09 LEU 31 -0.28 PRO 700
VAL 159 0.11 THR 32 -0.29 PRO 700
VAL 159 0.12 ILE 33 -0.30 PRO 700
GLY 134 0.13 LEU 34 -0.30 LEU 699
GLY 134 0.17 VAL 35 -0.32 LEU 699
ALA 135 0.19 GLY 36 -0.33 LEU 699
ALA 135 0.20 PRO 37 -0.33 LEU 699
ALA 135 0.17 ASN 38 -0.31 LEU 699
ALA 135 0.14 GLY 39 -0.30 LEU 699
ALA 135 0.14 ALA 40 -0.31 LEU 699
ALA 135 0.13 GLY 41 -0.29 LEU 699
ALA 135 0.13 LYS 42 -0.29 LEU 699
ALA 135 0.12 THR 43 -0.26 LEU 699
ALA 135 0.11 THR 44 -0.27 LEU 699
ALA 135 0.11 ILE 45 -0.26 LEU 699
ALA 135 0.10 ILE 46 -0.24 LEU 699
ALA 135 0.09 GLU 47 -0.24 LEU 699
GLU 160 0.09 CYS 48 -0.24 LEU 699
GLU 160 0.10 LEU 49 -0.22 LEU 699
GLY 63 0.10 LYS 50 -0.21 LEU 699
LYS 112 0.12 TYR 51 -0.21 LEU 699
LYS 112 0.12 ILE 52 -0.21 LEU 699
LYS 112 0.14 CYS 53 -0.20 PRO 700
LYS 112 0.18 THR 54 -0.19 PRO 700
LYS 112 0.22 GLY 55 -0.20 LEU 699
GLY 63 0.23 ASP 56 -0.20 LEU 699
ASN 152 0.13 PHE 57 -0.21 LEU 699
ARG 69 0.11 PRO 58 -0.22 LEU 699
LYS 108 0.12 PRO 59 -0.21 LEU 699
LYS 108 0.14 GLY 60 -0.22 LEU 699
LYS 108 0.11 THR 61 -0.23 LEU 699
ASP 56 0.17 LYS 62 -0.22 LEU 699
ASP 56 0.23 GLY 63 -0.23 LEU 699
ASP 56 0.15 ASN 64 -0.25 LEU 699
ASP 56 0.09 THR 65 -0.26 LEU 699
ASP 56 0.09 PHE 66 -0.25 LEU 699
ASP 56 0.08 VAL 67 -0.27 LEU 699
ASP 56 0.05 HIS 68 -0.29 LEU 699
ASP 56 0.09 ASP 69 -0.31 LEU 699
CYS 133 0.11 PRO 70 -0.32 LEU 699
CYS 133 0.09 LYS 71 -0.36 ASP 1294
CYS 133 0.06 VAL 72 -0.47 GLN 1295
MET 100 0.09 ALA 73 -0.46 ASP 1294
CYS 133 0.09 GLN 74 -0.43 ASP 1294
ASP 77 0.11 GLU 75 -0.35 LEU 699
CYS 133 0.14 THR 76 -0.32 LEU 699
CYS 133 0.14 ASP 77 -0.30 LEU 699
MET 100 0.13 VAL 78 -0.30 LEU 699
MET 100 0.14 ARG 79 -0.27 LEU 699
ILE 17 0.10 ALA 80 -0.26 LEU 699
ASP 19 0.09 GLN 81 -0.25 LEU 699
GLU 160 0.08 ILE 82 -0.25 LEU 699
GLU 160 0.08 ARG 83 -0.24 LEU 699
GLU 160 0.08 LEU 84 -0.22 LEU 699
GLU 160 0.08 GLN 85 -0.22 PRO 700
LYS 112 0.08 PHE 86 -0.21 PRO 700
HIS 733 0.09 ARG 87 -0.20 PRO 700
LYS 112 0.10 ASP 88 -0.19 PRO 700
LYS 112 0.10 VAL 89 -0.19 PRO 700
LYS 122 0.09 ASN 90 -0.18 PRO 700
GLN 732 0.11 GLY 91 -0.19 PRO 700
LYS 122 0.12 GLU 92 -0.18 PRO 700
GLU 736 0.09 LEU 93 -0.19 PRO 700
LYS 112 0.08 ILE 94 -0.19 PRO 700
LYS 112 0.07 ALA 95 -0.20 LEU 699
LYS 112 0.10 VAL 96 -0.20 LEU 699
GLU 160 0.07 GLN 97 -0.22 LEU 699
LYS 112 0.10 ARG 98 -0.22 LEU 699
GLU 160 0.06 SER 99 -0.23 LEU 699
VAL 101 0.16 MET 100 -0.23 LEU 699
MET 100 0.16 VAL 101 -0.25 LEU 699
CYS 133 0.14 CYS 102 -0.27 LEU 699
CYS 133 0.16 THR 103 -0.28 LEU 699
CYS 133 0.13 GLN 104 -0.30 LEU 699
ALA 134 0.16 LYS 105 -0.30 LEU 699
ALA 134 0.16 SER 106 -0.31 LEU 699
ALA 149 0.16 LYS 107 -0.31 LEU 699
ASP 56 0.18 LYS 108 -0.28 LEU 699
ASP 56 0.15 THR 109 -0.28 LEU 699
CYS 133 0.19 GLU 110 -0.25 LEU 699
CYS 133 0.21 PHE 111 -0.24 LEU 699
CYS 133 0.31 LYS 112 -0.22 LEU 699
LYS 112 0.24 THR 113 -0.21 LEU 699
CYS 133 0.12 LEU 114 -0.21 LEU 699
LYS 132 0.09 GLU 115 -0.20 LEU 699
VAL 117 0.11 GLY 116 -0.20 LEU 699
GLY 116 0.11 VAL 117 -0.20 LEU 699
LYS 112 0.09 ILE 118 -0.19 LEU 699
ASN 731 0.06 THR 119 -0.19 LEU 699
GLN 1259 0.07 ARG 120 -0.18 PRO 700
GLU 92 0.09 THR 121 -0.17 PRO 700
GLU 92 0.12 LYS 122 -0.15 PRO 700
GLN 1259 0.11 HIS 123 -0.14 PRO 700
GLN 1259 0.11 GLY 124 -0.15 PRO 700
GLN 1259 0.09 GLU 125 -0.16 LEU 699
GLN 1259 0.08 LYS 126 -0.17 LEU 699
GLN 1259 0.07 VAL 127 -0.17 LEU 699
ASN 195 0.06 SER 128 -0.18 LEU 699
LYS 112 0.06 LEU 129 -0.17 LEU 699
LYS 112 0.06 SER 130 -0.18 LEU 699
LYS 112 0.12 SER 131 -0.18 LEU 699
LYS 112 0.20 LYS 132 -0.18 LEU 699
LYS 112 0.31 CYS 133 -0.19 LEU 699
LYS 112 0.24 ALA 134 -0.18 LEU 699
LYS 112 0.18 GLU 135 -0.17 LEU 699
LYS 112 0.18 ILE 136 -0.18 LEU 699
LYS 112 0.22 ASP 137 -0.18 PRO 700
LYS 112 0.19 ARG 138 -0.17 PRO 700
LYS 112 0.16 GLU 139 -0.17 PRO 700
LYS 112 0.15 MET 140 -0.18 PRO 700
LYS 112 0.16 ILE 141 -0.18 PRO 700
LYS 112 0.15 SER 142 -0.17 PRO 700
LYS 112 0.13 SER 143 -0.18 PRO 700
LYS 112 0.12 LEU 144 -0.19 PRO 700
LYS 112 0.13 GLY 145 -0.18 PRO 700
LYS 112 0.14 VAL 146 -0.19 PRO 700
LYS 112 0.16 SER 147 -0.18 PRO 700
LYS 112 0.18 LYS 148 -0.19 PRO 700
LYS 108 0.18 ALA 149 -0.18 PRO 700
LYS 108 0.14 VAL 150 -0.19 PRO 700
LYS 112 0.13 LEU 151 -0.20 PRO 700
LYS 108 0.14 ASN 152 -0.20 PRO 700
LYS 108 0.13 ASN 153 -0.20 PRO 700
LYS 108 0.10 VAL 154 -0.21 PRO 700
LYS 112 0.09 ILE 155 -0.21 PRO 700
SER 68 0.10 PHE 156 -0.22 PRO 700
SER 68 0.11 CYS 157 -0.21 PRO 700
ARG 69 0.12 HIS 158 -0.22 LEU 699
ARG 69 0.14 GLN 159 -0.23 LEU 699
ARG 69 0.14 GLU 160 -0.22 LEU 699
ARG 69 0.14 ASP 161 -0.21 LEU 699
ARG 69 0.14 SER 162 -0.21 PRO 700
ARG 69 0.13 ASN 163 -0.21 PRO 700
ARG 69 0.11 TRP 164 -0.20 PRO 700
LYS 108 0.11 PRO 165 -0.20 PRO 700
ARG 69 0.11 LEU 166 -0.20 PRO 700
ASP 1238 0.18 SER 1202 -0.21 PRO 700
ASP 1238 0.18 ALA 1203 -0.23 PRO 700
ASP 1238 0.24 GLY 1204 -0.23 PRO 700
ASP 1238 0.17 GLN 1205 -0.22 PRO 700
ASP 1238 0.15 LYS 1206 -0.22 PRO 700
ASP 1238 0.14 VAL 1207 -0.23 PRO 700
ASP 1238 0.14 LEU 1208 -0.23 PRO 700
ASP 1238 0.12 ALA 1209 -0.22 PRO 700
ASP 1238 0.11 SER 1210 -0.22 PRO 700
ASP 1238 0.10 LEU 1211 -0.23 PRO 700
ASN 1241 0.12 ILE 1212 -0.22 PRO 700
ASP 1238 0.10 ILE 1213 -0.21 PRO 700
ASN 1241 0.10 ARG 1214 -0.21 PRO 700
ASN 1241 0.12 LEU 1215 -0.22 PRO 700
ASN 1241 0.12 ALA 1216 -0.20 PRO 700
LYS 108 0.11 LEU 1217 -0.20 PRO 700
ASN 1241 0.10 ALA 1218 -0.21 PRO 700
ASN 1241 0.12 GLU 1219 -0.20 PRO 700
ASN 1241 0.11 THR 1220 -0.19 PRO 700
LYS 112 0.11 PHE 1221 -0.19 PRO 700
LYS 112 0.10 CYS 1222 -0.20 PRO 700
LYS 112 0.10 LEU 1223 -0.19 PRO 700
LYS 112 0.11 ASN 1224 -0.19 PRO 700
LYS 112 0.10 CYS 1225 -0.20 PRO 700
HIS 733 0.10 GLY 1226 -0.21 PRO 700
HIS 733 0.09 ILE 1227 -0.22 PRO 700
SER 68 0.08 ILE 1228 -0.23 PRO 700
SER 68 0.09 ALA 1229 -0.24 PRO 700
VAL 1274 0.11 LEU 1230 -0.24 PRO 700
SER 68 0.13 ASP 1231 -0.25 PRO 700
ASP 1270 0.18 GLU 1232 -0.26 PRO 700
ASP 1270 0.13 PRO 1233 -0.26 PRO 700
SER 68 0.15 THR 1234 -0.27 PRO 700
SER 68 0.17 THR 1235 -0.26 PRO 700
ARG 69 0.18 ASN 1236 -0.25 PRO 700
SER 68 0.15 LEU 1237 -0.26 PRO 700
GLY 1204 0.24 ASP 1238 -0.29 PRO 700
GLY 1204 0.14 ARG 1239 -0.30 PRO 700
SER 273 0.14 GLU 1240 -0.28 PRO 700
ALA 1216 0.12 ASN 1241 -0.27 PRO 700
SER 68 0.10 ILE 1242 -0.28 PRO 700
HIS 245 0.09 GLU 1243 -0.28 PRO 700
ALA 1248 0.11 SER 1244 -0.26 PRO 700
GLU 1219 0.09 LEU 1245 -0.26 PRO 700
ARG 1279 0.08 ALA 1246 -0.27 PRO 700
VAL 729 0.09 HIS 1247 -0.26 PRO 700
ASN 1241 0.12 ALA 1248 -0.24 PRO 700
HIS 733 0.09 LEU 1249 -0.25 PRO 700
VAL 729 0.09 VAL 1250 -0.26 PRO 700
VAL 729 0.11 GLU 1251 -0.24 PRO 700
HIS 733 0.11 ILE 1252 -0.23 PRO 700
HIS 733 0.12 ILE 1253 -0.24 PRO 700
VAL 729 0.13 LYS 1254 -0.23 PRO 700
VAL 729 0.12 SER 1255 -0.21 PRO 700
HIS 733 0.13 ARG 1256 -0.21 PRO 700
HIS 733 0.15 SER 1257 -0.22 PRO 700
VAL 729 0.17 GLN 1258 -0.20 PRO 700
GLN 732 0.18 GLN 1259 -0.19 PRO 700
HIS 733 0.16 ARG 1260 -0.20 PRO 700
HIS 733 0.16 ASN 1261 -0.22 PRO 700
HIS 733 0.13 PHE 1262 -0.23 PRO 700
HIS 733 0.11 GLN 1263 -0.24 PRO 700
HIS 733 0.08 LEU 1264 -0.25 PRO 700
VAL 159 0.09 LEU 1265 -0.26 PRO 700
SER 68 0.10 VAL 1266 -0.27 PRO 700
GLY 134 0.13 ILE 1267 -0.28 LEU 699
SER 68 0.14 THR 1268 -0.29 LEU 699
LYS 66 0.16 HIS 1269 -0.31 LEU 699
GLU 1232 0.18 ASP 1270 -0.34 PRO 700
SER 68 0.17 GLU 1271 -0.36 PRO 700
SER 68 0.18 ASP 1272 -0.35 PRO 700
SER 68 0.13 PHE 1273 -0.32 PRO 700
GLU 1232 0.13 VAL 1274 -0.34 PRO 700
ASN 65 0.11 GLU 1275 -0.36 PRO 700
THR 1234 0.08 LEU 1276 -0.33 PRO 700
GLY 1278 0.10 LEU 1277 -0.31 PRO 700
LEU 1277 0.10 GLY 1278 -0.34 PRO 700
LEU 1237 0.08 ARG 1279 -0.34 PRO 700
ALA 1246 0.07 SER 1280 -0.30 PRO 700
PRO 185 0.06 GLU 1281 -0.33 PRO 700
ARG 188 0.08 TYR 1282 -0.31 PRO 700
VAL 159 0.10 VAL 1283 -0.33 PRO 700
VAL 159 0.15 GLU 1284 -0.36 PRO 700
VAL 159 0.15 LYS 1285 -0.35 PRO 700
VAL 159 0.15 PHE 1286 -0.34 PRO 700
VAL 159 0.14 TYR 1287 -0.33 LEU 699
ALA 135 0.16 ARG 1288 -0.35 LEU 699
ALA 135 0.14 ILE 1289 -0.33 LEU 699
ALA 135 0.13 LYS 1290 -0.35 LEU 699
ALA 135 0.10 LYS 1291 -0.35 LEU 699
SER 158 0.10 ASN 1292 -0.37 LEU 699
SER 158 0.09 ILE 1293 -0.37 LEU 699
LYS 20 0.09 ASP 1294 -0.46 ALA 73
SER 158 0.08 GLN 1295 -0.47 VAL 72
GLU 160 0.08 CYS 1296 -0.40 ALA 73
GLU 160 0.08 SER 1297 -0.33 LEU 699
GLU 160 0.10 GLU 1298 -0.34 LEU 699
GLU 160 0.11 ILE 1299 -0.33 LEU 699
GLU 160 0.13 VAL 1300 -0.36 LEU 699
GLU 160 0.15 LYS 1301 -0.35 LEU 699
VAL 159 0.17 CYS 1302 -0.39 LEU 699
VAL 159 0.22 SER 1303 -0.39 PRO 700
VAL 159 0.17 VAL 1304 -0.40 PRO 700
SER 158 0.17 SER 1305 -0.45 PRO 700
MET 157 0.15 SER 1306 -0.49 PRO 700
LYS 698 0.54 GLU 10 -0.08 ARG 87
LYS 698 0.53 ASN 11 -0.07 SER 209
LYS 698 0.39 THR 12 -0.07 SER 209
PRO 694 0.28 PHE 13 -0.07 ASP 53
PRO 694 0.28 LYS 14 -0.07 ILE 289
PRO 694 0.23 ILE 15 -0.08 PRO 700
PRO 694 0.18 LEU 16 -0.13 PRO 700
PRO 694 0.15 VAL 17 -0.16 PRO 700
PRO 694 0.12 ALA 18 -0.21 PRO 700
PRO 694 0.09 THR 19 -0.25 PRO 700
LEU 1237 0.09 ASP 20 -0.29 PRO 700
ASN 1236 0.09 ILE 21 -0.30 PRO 700
ASN 1236 0.10 HIS 22 -0.33 PRO 700
ASN 1236 0.11 LEU 23 -0.35 PRO 700
ASN 1236 0.13 GLY 24 -0.35 PRO 700
ARG 1239 0.14 PHE 25 -0.32 PRO 700
ARG 1239 0.14 MET 26 -0.30 PRO 700
ASN 1236 0.13 GLU 27 -0.32 PRO 700
ALA 1203 0.14 LYS 28 -0.32 PRO 700
SER 1202 0.10 ASP 29 -0.28 PRO 700
SER 1202 0.09 ALA 30 -0.26 PRO 700
SER 1202 0.07 VAL 31 -0.23 PRO 700
ARG 1239 0.10 ARG 32 -0.25 PRO 700
ARG 1239 0.10 GLY 33 -0.28 PRO 700
ASN 1236 0.10 ASN 34 -0.27 PRO 700
ARG 1239 0.10 ASP 35 -0.24 PRO 700
ARG 1239 0.10 THR 36 -0.27 PRO 700
ASN 1236 0.11 PHE 37 -0.29 PRO 700
ASN 1236 0.10 VAL 38 -0.23 PRO 700
PRO 694 0.09 THR 39 -0.22 PRO 700
ASN 1236 0.10 LEU 40 -0.26 PRO 700
ASN 1236 0.09 ASP 41 -0.23 PRO 700
PRO 694 0.12 GLU 42 -0.18 PRO 700
PRO 694 0.13 ILE 43 -0.19 PRO 700
PRO 694 0.12 LEU 44 -0.21 PRO 700
PRO 694 0.14 ARG 45 -0.15 PRO 700
PRO 694 0.16 LEU 46 -0.11 PRO 700
PRO 694 0.18 ALA 47 -0.13 PRO 700
PRO 694 0.18 GLN 48 -0.12 PRO 700
PRO 694 0.19 GLU 49 -0.06 PRO 700
PRO 694 0.21 ASN 50 -0.07 ARG 288
PRO 694 0.25 GLU 51 -0.06 LYS 290
PRO 694 0.25 VAL 52 -0.06 PRO 700
PRO 694 0.29 ASP 53 -0.07 PRO 700
PRO 694 0.21 PHE 54 -0.19 PRO 700
PRO 694 0.15 ILE 55 -0.24 PRO 700
PRO 694 0.12 LEU 56 -0.26 PRO 700
PRO 694 0.09 LEU 57 -0.31 PRO 700
PRO 694 0.08 GLY 58 -0.29 PRO 700
HIS 1269 0.08 GLY 59 -0.36 PRO 700
ASP 1272 0.09 ASP 60 -0.36 PRO 700
ASN 1236 0.09 LEU 61 -0.38 PRO 700
ASN 1236 0.10 PHE 62 -0.40 PRO 700
ASP 1272 0.11 HIS 63 -0.36 PRO 700
ASP 1272 0.16 GLU 64 -0.40 PRO 700
ASP 1272 0.15 ASN 65 -0.44 PRO 700
GLU 1271 0.16 LYS 66 -0.46 PRO 700
GLU 1271 0.15 PRO 67 -0.45 PRO 700
ASP 1272 0.18 SER 68 -0.44 PRO 700
ASN 1236 0.18 ARG 69 -0.46 PRO 700
ASN 1236 0.15 LYS 70 -0.40 PRO 700
ASN 1236 0.13 THR 71 -0.40 PRO 700
HIS 1269 0.14 LEU 72 -0.46 PRO 700
ASN 1236 0.13 HIS 73 -0.44 PRO 700
ASN 1236 0.11 THR 74 -0.37 PRO 700
HIS 1269 0.11 CYS 75 -0.39 PRO 700
HIS 1269 0.12 LEU 76 -0.44 PRO 700
HIS 1269 0.11 GLU 77 -0.37 PRO 700
ASN 1236 0.10 LEU 78 -0.32 PRO 700
HIS 1269 0.10 LEU 79 -0.36 PRO 700
HIS 1269 0.10 ARG 80 -0.37 PRO 700
HIS 1269 0.09 LYS 81 -0.28 PRO 700
PRO 694 0.09 TYR 82 -0.24 PRO 700
PRO 694 0.08 CYS 83 -0.29 PRO 700
PRO 37 0.08 MET 84 -0.32 GLY 697
PRO 37 0.08 GLY 85 -0.26 GLY 697
GLY 705 0.09 ASP 86 -0.21 GLY 697
PRO 694 0.15 ARG 87 -0.13 ALA 696
PRO 694 0.21 PRO 88 -0.10 ALA 696
PRO 694 0.31 VAL 89 -0.10 ALA 696
PRO 694 0.46 GLN 90 -0.08 VAL 89
PRO 694 0.40 PHE 91 -0.06 GLU 205
GLY 695 0.18 GLU 92 -0.06 ARG 69
GLY 704 0.14 ILE 93 -0.25 PRO 700
ALA 696 0.16 LEU 94 -0.11 PRO 700
GLY 704 0.26 SER 95 -0.37 PRO 700
GLY 705 0.30 ASP 96 -0.66 PRO 700
GLY 705 0.20 GLN 97 -0.88 PRO 700
GLY 705 0.14 SER 98 -1.06 PRO 700
ILE 709 0.13 VAL 99 -0.76 PRO 700
ILE 709 0.11 ASN 100 -0.65 PRO 700
GLY 102 0.11 PHE 101 -0.80 PRO 700
PHE 101 0.11 GLY 102 -0.94 PRO 700
PRO 37 0.10 PHE 103 -0.82 PRO 700
PRO 37 0.09 SER 104 -0.88 PRO 700
PRO 37 0.09 LYS 105 -0.97 PRO 700
GLY 705 0.10 PHE 106 -1.04 PRO 700
GLY 705 0.12 PRO 107 -1.13 PRO 700
GLY 705 0.16 TRP 108 -1.06 PRO 700
GLY 705 0.13 VAL 109 -0.74 PRO 700
GLY 705 0.13 ASN 110 -0.62 PRO 700
GLY 705 0.12 TYR 111 -0.48 PRO 700
GLY 705 0.16 GLN 112 -0.68 ALA 696
GLY 114 0.17 ASP 113 -0.76 GLY 697
GLY 705 0.19 GLY 114 -0.94 GLY 697
GLY 705 0.15 ASN 115 -0.72 GLY 697
GLY 705 0.13 LEU 116 -0.57 GLY 697
GLY 705 0.12 ASN 117 -0.42 GLY 697
GLY 705 0.09 ILE 118 -0.36 ALA 696
PRO 694 0.13 SER 119 -0.22 PRO 700
PRO 694 0.15 ILE 120 -0.24 PRO 700
PRO 694 0.11 PRO 121 -0.33 PRO 700
PRO 694 0.09 VAL 122 -0.37 PRO 700
PRO 37 0.08 PHE 123 -0.40 PRO 700
HIS 1269 0.08 SER 124 -0.42 PRO 700
SER 1305 0.09 ILE 125 -0.43 PRO 700
HIS 1269 0.09 HIS 126 -0.45 PRO 700
HIS 1269 0.08 GLY 127 -0.38 PRO 700
HIS 1269 0.08 ASN 128 -0.37 PRO 700
ASP 1272 0.10 HIS 129 -0.38 PRO 700
HIS 1269 0.11 ASP 130 -0.44 PRO 700
HIS 1269 0.11 ASP 131 -0.46 PRO 700
HIS 1269 0.12 PRO 132 -0.52 PRO 700
HIS 1269 0.15 THR 133 -0.50 PRO 700
PRO 37 0.18 GLY 134 -0.52 PRO 700
PRO 37 0.20 ALA 135 -0.56 LEU 699
PRO 37 0.18 ASP 136 -0.62 PRO 700
PRO 37 0.14 ALA 137 -0.58 PRO 700
PRO 37 0.14 LEU 138 -0.61 PRO 700
HIS 1269 0.13 CYS 139 -0.56 PRO 700
HIS 1269 0.12 ALA 140 -0.53 PRO 700
HIS 1269 0.10 LEU 141 -0.56 PRO 700
PRO 37 0.12 ASP 142 -0.65 PRO 700
PRO 37 0.12 ILE 143 -0.61 PRO 700
PRO 37 0.10 LEU 144 -0.57 PRO 700
PRO 37 0.10 SER 145 -0.67 PRO 700
PRO 37 0.11 CYS 146 -0.71 PRO 700
PRO 37 0.11 ALA 147 -0.62 PRO 700
PRO 37 0.09 GLY 148 -0.64 PRO 700
PRO 37 0.09 PHE 149 -0.51 PRO 700
PRO 37 0.08 VAL 150 -0.52 PRO 700
PRO 37 0.09 ASN 151 -0.59 PRO 700
PRO 37 0.09 HIS 152 -0.59 PRO 700
PRO 37 0.09 PHE 153 -0.56 PRO 700
SER 1305 0.10 GLY 154 -0.48 PRO 700
SER 1305 0.12 ARG 155 -0.54 PRO 700
SER 1305 0.16 SER 156 -0.52 PRO 700
SER 1305 0.15 MET 157 -0.58 PRO 700
SER 1303 0.20 SER 158 -0.51 PRO 700
SER 1303 0.22 VAL 159 -0.44 PRO 700
SER 1303 0.18 GLU 160 -0.40 PRO 700
SER 1303 0.15 LYS 161 -0.38 PRO 700
SER 1303 0.13 ILE 162 -0.39 PRO 700
SER 1303 0.11 ASP 163 -0.38 PRO 700
SER 1305 0.10 ILE 164 -0.34 PRO 700
ASN 100 0.11 SER 165 -0.38 PRO 700
ASN 100 0.08 PRO 166 -0.28 PRO 700
PRO 37 0.07 VAL 167 -0.34 PRO 700
GLY 695 0.07 LEU 168 -0.16 PRO 700
HIS 701 0.14 LEU 169 -0.08 PRO 700
HIS 701 0.38 GLN 170 -0.06 GLU 205
GLY 695 0.45 LYS 171 -0.06 VAL 89
LYS 698 0.63 GLY 172 -0.07 SER 209
LEU 699 0.66 SER 173 -0.10 SER 209
HIS 701 0.49 THR 174 -0.08 SER 209
HIS 701 0.45 LYS 175 -0.06 SER 209
HIS 701 0.26 ILE 176 -0.04 GLN 74
HIS 701 0.14 ALA 177 -0.07 PRO 700
PRO 694 0.10 LEU 178 -0.20 PRO 700
SER 1305 0.08 TYR 179 -0.25 PRO 700
SER 1305 0.09 GLY 180 -0.35 PRO 700
SER 1305 0.10 LEU 181 -0.37 PRO 700
SER 1305 0.10 GLY 182 -0.42 PRO 700
HIS 1269 0.08 SER 183 -0.37 PRO 700
GLU 1284 0.08 ILE 184 -0.38 PRO 700
TYR 1282 0.07 PRO 185 -0.34 PRO 700
HIS 1247 0.07 ASP 186 -0.29 PRO 700
TYR 1282 0.07 GLU 187 -0.28 PRO 700
GLU 1284 0.09 ARG 188 -0.32 PRO 700
ALA 713 0.09 LEU 189 -0.29 PRO 700
ALA 713 0.06 TYR 190 -0.24 PRO 700
SER 29 0.08 ARG 191 -0.27 PRO 700
ALA 713 0.10 MET 192 -0.28 PRO 700
ALA 713 0.11 PHE 193 -0.22 PRO 700
ALA 734 0.09 VAL 194 -0.20 PRO 700
SER 738 0.11 ASN 195 -0.24 PRO 700
ALA 713 0.12 LYS 196 -0.24 GLY 705
SER 1303 0.11 LYS 197 -0.29 GLY 705
ALA 713 0.11 VAL 198 -0.25 PRO 700
ALA 713 0.11 THR 199 -0.27 GLY 705
SER 1303 0.09 MET 200 -0.24 GLY 705
ASN 100 0.10 LEU 201 -0.29 GLY 705
GLY 697 0.10 ARG 202 -0.15 GLY 705
HIS 701 0.20 PRO 203 -0.10 GLY 704
HIS 701 0.23 LYS 204 -0.08 GLY 704
HIS 701 0.41 GLU 205 -0.08 SER 173
HIS 701 0.53 ASP 206 -0.08 SER 173
HIS 701 0.38 GLU 207 -0.06 SER 173
HIS 701 0.40 ASN 208 -0.08 SER 173
HIS 701 0.49 SER 209 -0.10 SER 173
HIS 701 0.38 TRP 210 -0.05 LEU 201
HIS 701 0.29 PHE 211 -0.04 LYS 14
HIS 701 0.18 ASN 212 -0.06 GLY 705
PRO 694 0.13 LEU 213 -0.08 PRO 700
PRO 694 0.10 PHE 214 -0.16 PRO 700
PRO 694 0.08 VAL 215 -0.24 PRO 700
SER 1305 0.07 ILE 216 -0.27 PRO 700
LEU 1237 0.07 HIS 217 -0.30 PRO 700
GLU 1243 0.07 GLN 218 -0.27 PRO 700
GLU 1243 0.08 ASN 219 -0.24 PRO 700
GLU 1240 0.08 ARG 220 -0.18 PRO 700
GLU 1240 0.08 SER 221 -0.15 PRO 700
GLU 1240 0.09 LYS 222 -0.17 PRO 700
VAL 729 0.09 HIS 223 -0.18 PRO 700
VAL 729 0.09 GLY 224 -0.21 PRO 700
VAL 729 0.12 SER 225 -0.19 PRO 700
VAL 729 0.11 THR 226 -0.22 PRO 700
HIS 1247 0.09 ASN 227 -0.24 PRO 700
HIS 1247 0.08 PHE 228 -0.22 PRO 700
SER 1244 0.07 ILE 229 -0.20 PRO 700
ASN 208 0.07 PRO 230 -0.15 PRO 700
ASN 208 0.08 GLU 231 -0.11 PRO 700
ASN 208 0.09 GLN 232 -0.11 GLY 705
ASN 208 0.08 PHE 233 -0.15 GLY 705
LEU 189 0.08 LEU 234 -0.14 GLY 705
SER 1303 0.08 ASP 235 -0.13 GLY 705
HIS 701 0.14 ASP 236 -0.09 GLY 705
HIS 701 0.19 PHE 237 -0.07 GLY 705
HIS 701 0.16 ILE 238 -0.08 GLY 705
HIS 701 0.21 ASP 239 -0.05 MET 296
HIS 701 0.15 LEU 240 -0.05 MET 296
PRO 694 0.11 VAL 241 -0.11 PRO 700
PRO 694 0.11 ILE 242 -0.16 PRO 700
PRO 694 0.09 TRP 243 -0.19 PRO 700
LEU 1237 0.08 GLY 244 -0.25 PRO 700
GLU 1243 0.09 HIS 245 -0.27 PRO 700
GLU 1240 0.09 GLU 246 -0.21 PRO 700
GLU 1240 0.10 HIS 247 -0.21 PRO 700
GLU 1240 0.10 GLU 248 -0.16 PRO 700
PRO 694 0.11 CYS 249 -0.13 PRO 700
PRO 694 0.12 LYS 250 -0.09 PRO 700
PRO 694 0.14 ILE 251 -0.08 PRO 700
PRO 694 0.15 ALA 252 -0.07 LYS 298
PRO 694 0.15 PRO 253 -0.05 GLY 285
HIS 701 0.14 THR 254 -0.06 LYS 298
LEU 699 0.17 LYS 255 -0.05 LYS 298
LEU 699 0.13 ASN 256 -0.05 GLY 705
LEU 699 0.18 GLU 257 -0.05 THR 1220
LEU 699 0.16 GLN 258 -0.06 GLY 705
HIS 701 0.15 GLN 259 -0.06 GLY 705
LEU 699 0.21 LEU 260 -0.06 ALA 713
HIS 701 0.19 PHE 261 -0.06 TYR 262
HIS 701 0.16 TYR 262 -0.06 PHE 261
PRO 694 0.12 ILE 263 -0.06 GLY 705
PRO 694 0.13 SER 264 -0.08 PRO 700
PRO 694 0.11 GLN 265 -0.13 PRO 700
PRO 694 0.12 PRO 266 -0.15 PRO 700
PRO 694 0.10 GLY 267 -0.18 PRO 700
ARG 1239 0.09 SER 268 -0.22 PRO 700
ARG 1239 0.10 SER 269 -0.22 PRO 700
ARG 1239 0.11 VAL 270 -0.23 PRO 700
ARG 1239 0.11 VAL 271 -0.22 PRO 700
GLU 1240 0.13 THR 272 -0.26 PRO 700
GLU 1240 0.14 SER 273 -0.24 PRO 700
GLU 1240 0.12 LEU 274 -0.21 PRO 700
GLU 1240 0.10 SER 275 -0.19 PRO 700
GLU 1240 0.09 PRO 276 -0.18 SER 1255
GLU 1240 0.09 GLY 277 -0.16 PRO 700
GLU 1240 0.10 GLU 278 -0.17 PRO 700
PRO 694 0.09 ALA 279 -0.14 PRO 700
PRO 694 0.11 VAL 280 -0.12 PRO 700
PRO 694 0.12 LYS 281 -0.11 PRO 700
PRO 694 0.11 LYS 282 -0.14 PRO 700
PRO 694 0.13 HIS 283 -0.12 PRO 700
PRO 694 0.15 VAL 284 -0.12 PRO 700
PRO 694 0.18 GLY 285 -0.07 PRO 700
PRO 694 0.21 LEU 286 -0.05 ASN 295
PRO 694 0.21 LEU 287 -0.05 ASP 239
LYS 698 0.25 ARG 288 -0.07 ASN 50
LEU 699 0.31 ILE 289 -0.07 LYS 14
LEU 699 0.42 LYS 290 -0.06 THR 12
LEU 699 0.47 GLY 291 -0.06 ASN 208
LEU 699 0.40 ARG 292 -0.05 LYS 14
LEU 699 0.36 LYS 293 -0.06 LYS 14
LEU 699 0.29 MET 294 -0.05 PHE 237
LEU 699 0.26 ASN 295 -0.05 GLU 49
PRO 694 0.19 MET 296 -0.05 PHE 261
PRO 694 0.19 HIS 297 -0.05 PHE 261
PRO 694 0.18 LYS 298 -0.07 ALA 252
PRO 694 0.18 ILE 299 -0.05 THR 254
PRO 694 0.15 PRO 300 -0.08 PRO 700
PRO 694 0.13 LEU 301 -0.12 PRO 700
PRO 694 0.13 HIS 302 -0.11 PRO 700
PRO 694 0.10 THR 303 -0.16 PRO 700
PRO 694 0.10 VAL 304 -0.17 PRO 700
ARG 1239 0.09 ARG 305 -0.17 PRO 700
GLY 705 0.17 LYS 690 -0.42 GLY 697
GLY 705 0.15 VAL 691 -0.26 ALA 696
GLY 705 0.14 THR 692 -0.23 ALA 696
PRO 694 0.15 TYR 693 -0.13 ILE 118
GLN 90 0.46 PRO 694 -0.14 TRP 108
GLY 172 0.57 GLY 695 -0.45 GLN 112
GLY 172 0.32 ALA 696 -0.75 GLY 114
GLY 172 0.37 GLY 697 -0.94 GLY 114
SER 173 0.64 LYS 698 -0.86 PHE 106
SER 173 0.66 LEU 699 -0.93 LYS 105
SER 173 0.45 PRO 700 -1.13 PRO 107
SER 173 0.63 HIS 701 -0.77 SER 98
ALA 696 0.26 ILE 702 -0.52 ASP 96
GLY 697 0.20 ILE 703 -0.15 SER 98
SER 95 0.26 GLY 704 -0.27 SER 165
ASP 96 0.30 GLY 705 -0.35 ASP 163
GLY 697 0.15 SER 706 -0.16 LYS 197
GLY 697 0.18 ASP 707 -0.10 LYS 197
VAL 99 0.13 LEU 708 -0.21 GLY 705
VAL 99 0.13 ILE 709 -0.16 GLY 705
VAL 99 0.11 ALA 710 -0.24 GLY 705
SER 1303 0.10 HIS 711 -0.16 GLY 705
THR 199 0.11 HIS 712 -0.14 GLY 705
LYS 196 0.12 ALA 713 -0.12 GLY 705
HIS 701 0.14 ARG 714 -0.06 GLY 705
LEU 699 0.13 LYS 715 -0.06 GLY 705
HIS 701 0.11 ASN 716 -0.08 GLY 705
LEU 699 0.09 THR 717 -0.09 GLY 705
ASN 208 0.10 GLU 718 -0.10 GLY 705
ASN 208 0.08 LEU 719 -0.12 GLY 705
ALA 734 0.11 GLU 720 -0.14 GLY 705
ALA 734 0.08 GLU 721 -0.13 GLY 705
ALA 734 0.07 TRP 722 -0.14 GLY 705
ALA 734 0.11 LEU 723 -0.18 GLY 705
ALA 734 0.12 ARG 724 -0.18 GLY 705
GLN 1258 0.09 GLN 725 -0.16 GLY 705
GLN 1258 0.11 GLU 726 -0.17 PRO 700
ALA 734 0.14 MET 727 -0.20 GLY 705
GLN 1258 0.13 GLU 728 -0.18 GLY 705
GLN 1258 0.17 VAL 729 -0.19 PRO 700
GLN 1258 0.14 GLN 730 -0.22 PRO 700
ALA 734 0.16 ASN 731 -0.22 PRO 700
GLN 1259 0.18 GLN 732 -0.20 PRO 700
GLN 1259 0.17 HIS 733 -0.23 PRO 700
ASN 731 0.16 ALA 734 -0.23 PRO 700
ASN 731 0.13 LYS 735 -0.21 PRO 700
GLN 1259 0.12 GLU 736 -0.21 PRO 700
ASN 195 0.09 GLU 737 -0.23 PRO 700
ASN 195 0.11 SER 738 -0.22 PRO 700
ASN 195 0.08 LEU 739 -0.20 PRO 700
ASN 195 0.08 ALA 740 -0.21 PRO 700
ASN 195 0.10 ASP 741 -0.23 LEU 699
ASN 195 0.09 ASP 742 -0.22 LEU 699
ASN 195 0.08 LEU 743 -0.21 LEU 699
GLU 160 0.08 PHE 744 -0.23 LEU 699
ALA 713 0.09 ARG 745 -0.24 LEU 699
ALA 713 0.08 TYR 746 -0.22 LEU 699
ALA 713 0.08 ASN 747 -0.23 LEU 699
ALA 713 0.07 PRO 748 -0.21 LEU 699
ALA 713 0.07 TYR 749 -0.21 LEU 699
ALA 713 0.07 LEU 750 -0.20 LEU 699

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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.