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CA distance fluctuations for 2607171440351968437

---  normal mode 23  ---

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
ASN 1224 0.13 MET 1 -0.19 LYS 107
CYS 1225 0.14 SER 2 -0.20 LYS 107
GLU 736 0.14 ARG 3 -0.20 LYS 107
GLU 737 0.14 ILE 4 -0.21 LYS 107
GLU 737 0.18 GLU 5 -0.18 LYS 107
ASN 1292 0.21 LYS 6 -0.18 LYS 107
ASN 1292 0.17 MET 7 -0.20 LYS 108
GLU 1298 0.23 SER 8 -0.20 LYS 108
ASN 747 0.14 ILE 9 -0.24 LYS 108
VAL 101 0.18 LEU 10 -0.22 LYS 108
ARG 79 0.24 GLY 11 -0.27 LYS 108
THR 44 0.17 VAL 12 -0.37 LYS 108
ALA 73 0.35 ARG 13 -0.50 LYS 108
ALA 73 0.38 SER 14 -0.48 LYS 107
GLY 39 0.24 PHE 15 -0.35 LYS 107
CYS 1296 0.31 GLY 16 -0.39 VAL 72
CYS 1296 0.32 ILE 17 -0.38 VAL 72
ARG 79 0.42 GLU 18 -0.47 VAL 72
ARG 79 0.46 ASP 19 -0.33 VAL 72
ASN 747 0.57 LYS 20 -0.41 VAL 72
ASN 747 0.38 ASP 21 -0.41 VAL 72
ASN 747 0.41 LYS 22 -0.31 VAL 72
ARG 745 0.34 GLN 23 -0.24 LYS 107
ARG 745 0.35 ILE 24 -0.25 ILE 25
ASP 741 0.27 ILE 25 -0.25 ILE 24
GLU 737 0.37 THR 26 -0.22 LYS 107
GLU 737 0.30 PHE 27 -0.23 LYS 107
GLU 737 0.33 PHE 28 -0.22 LYS 107
ALA 734 0.25 SER 29 -0.22 LYS 107
ALA 734 0.21 PRO 30 -0.22 LYS 107
ALA 734 0.22 LEU 31 -0.24 LYS 107
GLU 737 0.25 THR 32 -0.26 LYS 107
GLU 737 0.24 ILE 33 -0.27 LYS 107
GLU 737 0.24 LEU 34 -0.30 LYS 107
GLU 737 0.23 VAL 35 -0.35 THR 1235
ALA 73 0.26 GLY 36 -0.39 ALA 1203
ALA 73 0.33 PRO 37 -0.56 ALA 1203
ALA 73 0.46 ASN 38 -0.62 ALA 1203
ALA 73 0.55 GLY 39 -0.60 GLU 160
ALA 73 0.38 ALA 40 -0.46 LYS 107
ALA 73 0.31 GLY 41 -0.41 LYS 107
ALA 73 0.25 LYS 42 -0.37 LYS 107
ALA 73 0.27 THR 43 -0.40 LYS 107
ALA 73 0.25 THR 44 -0.40 LYS 107
GLU 737 0.14 ILE 45 -0.34 LYS 107
ASP 1231 0.16 ILE 46 -0.35 LYS 107
ASP 1231 0.15 GLU 47 -0.38 LYS 107
ASP 1231 0.10 CYS 48 -0.31 LYS 108
ALA 30 0.11 LEU 49 -0.28 LYS 107
THR 1235 0.13 LYS 50 -0.31 LYS 107
THR 1235 0.13 TYR 51 -0.31 LYS 108
ASP 19 0.14 ILE 52 -0.24 LYS 108
ASP 19 0.12 CYS 53 -0.24 LYS 108
ASP 19 0.12 THR 54 -0.25 LYS 108
ASP 19 0.15 GLY 55 -0.27 LYS 108
ASN 1236 0.16 ASP 56 -0.35 LYS 108
THR 1235 0.16 PHE 57 -0.41 LYS 108
THR 1235 0.20 PRO 58 -0.47 LYS 107
THR 1235 0.24 PRO 59 -0.50 LYS 107
VAL 72 0.27 GLY 60 -0.61 LYS 107
VAL 72 0.30 THR 61 -0.63 LYS 108
ASP 69 0.25 LYS 62 -0.60 LYS 108
ASP 69 0.22 GLY 63 -0.46 LYS 108
ASP 69 0.28 ASN 64 -0.60 LYS 108
ASP 69 0.39 THR 65 -0.82 LYS 108
ASP 69 0.24 PHE 66 -0.57 LYS 108
ASP 69 0.19 VAL 67 -0.46 LYS 108
ALA 73 0.25 HIS 68 -0.42 LYS 108
THR 65 0.39 ASP 69 -0.39 ASP 1294
GLY 39 0.25 PRO 70 -0.16 LEU 750
GLY 39 0.27 LYS 71 -0.33 ASP 1294
GLY 39 0.42 VAL 72 -0.47 GLU 18
GLY 39 0.55 ALA 73 -0.42 GLU 18
GLY 39 0.46 GLN 74 -0.26 GLU 18
GLY 39 0.39 GLU 75 -0.24 LEU 750
SER 106 0.29 THR 76 -0.18 LEU 750
LYS 105 0.38 ASP 77 -0.20 VAL 101
GLU 18 0.30 VAL 78 -0.18 ALA 73
ASP 19 0.46 ARG 79 -0.19 LEU 750
ASP 19 0.29 ALA 80 -0.20 GLN 81
ASP 19 0.34 GLN 81 -0.20 ALA 80
ASP 19 0.19 ILE 82 -0.21 LYS 108
ASN 1292 0.18 ILE 83 -0.18 LYS 108
ASN 1292 0.15 LEU 84 -0.19 LYS 108
ASN 1292 0.19 GLN 85 -0.17 LYS 108
ASN 1292 0.14 PHE 86 -0.17 LYS 108
ASN 1292 0.13 ARG 87 -0.16 LYS 108
PRO 165 0.11 ASP 88 -0.17 LYS 108
PRO 165 0.12 VAL 89 -0.17 LYS 108
LEU 274 0.10 ASN 90 -0.15 LYS 108
ASN 1292 0.13 GLY 91 -0.15 LYS 108
ASN 1292 0.16 GLU 92 -0.14 LYS 108
ASN 1292 0.20 LEU 93 -0.13 LYS 108
ASN 1292 0.18 ILE 94 -0.14 LYS 108
LYS 20 0.21 ALA 95 -0.15 LYS 108
LYS 20 0.20 VAL 96 -0.17 LYS 108
ASP 19 0.29 GLN 97 -0.15 LYS 108
ASP 19 0.30 ARG 98 -0.17 LYS 108
ASP 19 0.40 SER 99 -0.16 ARG 79
ASP 19 0.34 MET 100 -0.17 LYS 108
ASP 19 0.38 VAL 101 -0.20 ASP 77
ASP 19 0.21 CYS 102 -0.16 LYS 108
LYS 105 0.35 THR 103 -0.15 GLU 110
ASP 77 0.19 GLN 104 -0.15 ASP 1294
ASP 77 0.38 LYS 105 -0.30 THR 65
THR 76 0.29 SER 106 -0.44 THR 65
THR 76 0.24 LYS 107 -0.68 THR 65
THR 76 0.17 LYS 108 -0.82 THR 65
ASP 19 0.08 THR 109 -0.35 THR 65
ASP 19 0.16 GLU 110 -0.26 THR 65
ASP 19 0.20 PHE 111 -0.19 LYS 108
ASP 19 0.31 LYS 112 -0.12 ASP 77
ASP 19 0.33 THR 113 -0.14 LYS 108
ASP 19 0.43 LEU 114 -0.17 LEU 750
ASP 19 0.41 GLU 115 -0.17 LEU 750
ASP 19 0.37 GLY 116 -0.21 VAL 117
ASP 19 0.35 VAL 117 -0.21 GLY 116
LYS 20 0.26 ILE 118 -0.13 LYS 108
LYS 20 0.30 THR 119 -0.11 LYS 108
LYS 20 0.25 ARG 120 -0.11 LYS 108
LYS 20 0.27 THR 121 -0.10 LYS 108
LYS 20 0.25 LYS 122 -0.18 LEU 129
LYS 20 0.27 HIS 123 -0.21 LEU 129
ILE 1293 0.31 GLY 124 -0.14 LEU 129
LYS 20 0.32 GLU 125 -0.09 GLU 75
LYS 20 0.34 LYS 126 -0.11 GLU 75
LYS 20 0.33 VAL 127 -0.17 LEU 129
LYS 20 0.34 SER 128 -0.16 GLU 75
LYS 20 0.32 LEU 129 -0.21 HIS 123
ASP 19 0.38 SER 130 -0.15 HIS 123
ASP 19 0.33 SER 131 -0.15 HIS 123
ASP 19 0.31 LYS 132 -0.13 HIS 123
ASP 19 0.26 CYS 133 -0.15 LYS 108
ASP 19 0.22 ALA 134 -0.14 LYS 108
ASP 19 0.23 GLU 135 -0.16 HIS 123
ASP 19 0.22 ILE 136 -0.15 LYS 108
ASP 19 0.17 ASP 137 -0.19 LYS 108
ASP 19 0.16 ARG 138 -0.16 LYS 108
ASP 19 0.17 GLU 139 -0.15 LYS 108
ASP 19 0.14 MET 140 -0.18 LYS 108
PRO 165 0.13 ILE 141 -0.20 LYS 108
PRO 165 0.12 SER 142 -0.17 LYS 108
PRO 165 0.11 SER 143 -0.17 LYS 108
PRO 165 0.13 LEU 144 -0.20 LYS 108
PRO 165 0.13 GLY 145 -0.20 LYS 107
PRO 165 0.16 VAL 146 -0.22 LYS 107
PRO 165 0.18 SER 147 -0.23 LYS 107
PRO 165 0.16 LYS 148 -0.26 LYS 107
PRO 165 0.20 ALA 149 -0.29 LYS 107
PRO 165 0.19 VAL 150 -0.28 LYS 107
PRO 165 0.14 LEU 151 -0.29 LYS 107
ASN 1236 0.15 ASN 152 -0.34 LYS 107
PRO 165 0.16 ASN 153 -0.35 LYS 107
PRO 165 0.15 VAL 154 -0.32 LYS 107
GLU 737 0.13 ILE 155 -0.31 LYS 107
ALA 30 0.13 PHE 156 -0.34 LYS 107
THR 1235 0.18 CYS 157 -0.38 LYS 107
THR 1235 0.22 HIS 158 -0.46 GLY 39
THR 1235 0.31 GLN 159 -0.59 GLY 39
THR 1235 0.37 GLU 160 -0.60 GLY 39
ASN 1236 0.24 ASP 161 -0.53 GLY 39
ASN 1236 0.27 SER 162 -0.53 ASN 38
ASN 1236 0.23 ASN 163 -0.52 ASN 38
ASN 1236 0.18 TRP 164 -0.44 ASN 38
ALA 149 0.20 PRO 165 -0.41 ASN 38
ALA 149 0.15 LEU 166 -0.48 ASN 38
ALA 1248 0.14 SER 1202 -0.53 ASN 38
ALA 30 0.12 ALA 1203 -0.62 ASN 38
ALA 30 0.14 GLY 1204 -0.51 ASN 38
ALA 1248 0.19 GLN 1205 -0.44 ASN 38
ALA 30 0.13 LYS 1206 -0.51 ASN 38
ALA 30 0.13 VAL 1207 -0.52 ASN 38
ALA 1248 0.18 LEU 1208 -0.39 ASN 38
ILE 1252 0.17 ALA 1209 -0.40 ASN 38
ALA 30 0.13 SER 1210 -0.42 ASN 38
ALA 30 0.14 LEU 1211 -0.37 ASN 38
ILE 1252 0.17 ILE 1212 -0.30 ASN 38
ALA 1216 0.17 ILE 1213 -0.32 ASN 38
ALA 30 0.14 ARG 1214 -0.31 LYS 107
GLY 1226 0.14 LEU 1215 -0.29 LYS 107
ILE 1213 0.17 ALA 1216 -0.27 LYS 107
CYS 1222 0.16 LEU 1217 -0.28 LYS 107
LEU 1217 0.15 ALA 1218 -0.28 LYS 107
VAL 31 0.13 GLU 1219 -0.25 LYS 107
PRO 165 0.13 THR 1220 -0.25 LYS 107
PRO 165 0.14 PHE 1221 -0.25 LYS 107
LEU 1217 0.16 CYS 1222 -0.25 LYS 107
PRO 165 0.12 LEU 1223 -0.22 LYS 107
MET 1 0.13 ASN 1224 -0.21 LYS 107
SER 2 0.14 CYS 1225 -0.23 LYS 107
LEU 1215 0.14 GLY 1226 -0.23 LYS 107
GLU 737 0.15 ILE 1227 -0.26 LYS 107
GLU 737 0.15 ILE 1228 -0.28 LYS 107
GLU 737 0.16 ALA 1229 -0.31 LYS 107
ALA 73 0.16 LEU 1230 -0.30 LYS 107
ALA 73 0.21 ASP 1231 -0.35 ASN 38
ALA 73 0.22 GLU 1232 -0.38 ASN 38
GLN 159 0.22 PRO 1233 -0.31 ASN 38
GLU 160 0.25 THR 1234 -0.30 HIS 1269
GLU 160 0.37 THR 1235 -0.54 HIS 1269
GLU 160 0.32 ASN 1236 -0.47 PRO 37
GLU 160 0.23 LEU 1237 -0.33 PRO 37
VAL 72 0.21 ASP 1238 -0.23 ILE 1293
ALA 73 0.21 ARG 1239 -0.27 SER 273
ALA 30 0.23 GLU 1240 -0.27 SER 273
ALA 30 0.21 ASN 1241 -0.23 LYS 107
ALA 73 0.19 ILE 1242 -0.22 LYS 107
ASP 29 0.23 GLU 1243 -0.26 SER 273
ASP 29 0.28 SER 1244 -0.22 LYS 107
ALA 30 0.21 LEU 1245 -0.23 LYS 107
ASP 29 0.20 ALA 1246 -0.22 LYS 107
ASP 29 0.27 HIS 1247 -0.21 LYS 107
ALA 30 0.25 ALA 1248 -0.22 LYS 107
ALA 30 0.20 LEU 1249 -0.23 LYS 107
ASP 29 0.21 VAL 1250 -0.22 LYS 107
LEU 274 0.28 GLU 1251 -0.22 LYS 107
LEU 274 0.22 ILE 1252 -0.23 LYS 107
LEU 274 0.21 ILE 1253 -0.22 LYS 107
LEU 274 0.29 LYS 1254 -0.21 LYS 107
LEU 274 0.28 SER 1255 -0.21 LYS 107
LEU 274 0.22 ARG 1256 -0.22 LYS 107
LEU 274 0.22 SER 1257 -0.21 LYS 107
LEU 274 0.23 GLN 1258 -0.19 LYS 107
LEU 274 0.20 GLN 1259 -0.18 LYS 107
LEU 274 0.18 ARG 1260 -0.19 LYS 107
LEU 274 0.16 ASN 1261 -0.20 LYS 107
LEU 274 0.17 PHE 1262 -0.22 LYS 107
GLU 737 0.19 GLN 1263 -0.24 LYS 107
GLU 737 0.18 LEU 1264 -0.26 LYS 107
GLU 737 0.19 LEU 1265 -0.28 LYS 107
GLU 737 0.18 VAL 1266 -0.28 LYS 107
ALA 73 0.21 ILE 1267 -0.31 LYS 107
ALA 73 0.24 THR 1268 -0.38 THR 1235
ALA 73 0.28 HIS 1269 -0.54 THR 1235
ALA 73 0.23 ASP 1270 -0.39 THR 1235
ALA 73 0.20 GLU 1271 -0.27 ASN 1236
ALA 73 0.18 ASP 1272 -0.23 LYS 107
ALA 73 0.18 PHE 1273 -0.24 LYS 107
ALA 734 0.18 VAL 1274 -0.24 LYS 107
ALA 734 0.17 GLU 1275 -0.23 LYS 107
MET 26 0.19 LEU 1276 -0.22 LYS 107
ALA 734 0.17 LEU 1277 -0.22 LYS 107
ALA 734 0.21 GLY 1278 -0.22 LYS 107
ALA 734 0.18 ARG 1279 -0.21 LYS 107
SER 273 0.19 SER 1280 -0.20 LYS 107
ALA 734 0.21 GLU 1281 -0.20 LYS 107
ALA 734 0.24 TYR 1282 -0.22 LYS 107
ALA 734 0.28 VAL 1283 -0.23 LYS 107
ALA 734 0.32 GLU 1284 -0.22 LYS 107
ALA 734 0.36 LYS 1285 -0.23 LYS 107
ALA 734 0.32 PHE 1286 -0.26 LYS 107
GLU 737 0.32 TYR 1287 -0.29 LYS 107
GLU 737 0.29 ARG 1288 -0.31 LYS 107
ASP 741 0.26 ILE 1289 -0.35 LYS 107
SER 738 0.27 LYS 1290 -0.42 ALA 1203
ARG 745 0.30 LYS 1291 -0.48 LYS 107
ARG 745 0.42 ASN 1292 -0.46 LYS 107
ARG 745 0.41 ILE 1293 -0.50 LYS 107
ARG 745 0.35 ASP 1294 -0.52 LYS 107
GLU 75 0.29 GLN 1295 -0.60 LYS 107
ILE 17 0.32 CYS 1296 -0.48 LYS 107
ARG 745 0.24 SER 1297 -0.41 LYS 107
ARG 745 0.37 GLU 1298 -0.36 LYS 107
ASP 741 0.36 ILE 1299 -0.33 LYS 107
SER 738 0.40 VAL 1300 -0.30 LYS 107
GLU 737 0.43 LYS 1301 -0.27 LYS 20
ALA 734 0.36 CYS 1302 -0.27 LYS 107
ALA 734 0.32 SER 1303 -0.25 LYS 20
ALA 734 0.28 VAL 1304 -0.23 LYS 107
ALA 734 0.22 SER 1305 -0.21 LYS 107
PRO 37 0.22 SER 1306 -0.24 LYS 20
VAL 691 0.09 GLU 10 -0.12 LYS 107
ARG 714 0.08 ASN 11 -0.12 LYS 107
GLY 124 0.07 THR 12 -0.13 LYS 107
GLY 124 0.08 PHE 13 -0.14 LYS 107
ALA 734 0.08 LYS 14 -0.14 LYS 107
ALA 734 0.09 ILE 15 -0.15 LYS 107
ALA 734 0.09 LEU 16 -0.15 LYS 107
ALA 734 0.10 VAL 17 -0.16 LYS 107
ALA 734 0.11 ALA 18 -0.16 LYS 107
ALA 734 0.12 THR 19 -0.17 LYS 107
ALA 734 0.14 ASP 20 -0.18 LYS 107
ALA 734 0.13 ILE 21 -0.18 LYS 107
ALA 734 0.15 HIS 22 -0.19 LYS 107
ALA 734 0.14 LEU 23 -0.19 LYS 107
ALA 734 0.15 GLY 24 -0.19 LYS 107
ALA 734 0.16 PHE 25 -0.22 ARG 1239
HIS 1247 0.25 MET 26 -0.18 LYS 107
HIS 1247 0.19 GLU 27 -0.19 LYS 107
SER 1244 0.23 LYS 28 -0.19 LYS 107
SER 1244 0.28 ASP 29 -0.17 LYS 107
SER 1244 0.27 ALA 30 -0.15 LYS 107
ALA 1248 0.23 VAL 31 -0.16 VAL 38
GLU 1251 0.22 ARG 32 -0.17 VAL 38
HIS 1247 0.20 GLY 33 -0.17 LYS 107
GLU 1251 0.14 ASN 34 -0.17 LYS 107
ALA 734 0.14 ASP 35 -0.19 VAL 38
ALA 734 0.14 THR 36 -0.18 LYS 107
ALA 734 0.12 PHE 37 -0.17 LYS 107
ALA 734 0.12 VAL 38 -0.19 ASP 35
ALA 734 0.12 THR 39 -0.16 LYS 107
ALA 734 0.12 LEU 40 -0.17 LYS 107
ALA 734 0.11 ASP 41 -0.16 LYS 107
ALA 734 0.11 GLU 42 -0.16 LYS 107
ALA 734 0.11 ILE 43 -0.16 LYS 107
ALA 734 0.11 LEU 44 -0.16 LYS 107
ALA 734 0.10 ARG 45 -0.15 LYS 107
ALA 734 0.10 LEU 46 -0.15 LYS 107
ALA 734 0.10 ALA 47 -0.15 LYS 107
ALA 734 0.09 GLN 48 -0.15 LYS 107
ALA 734 0.09 GLU 49 -0.14 LYS 107
GLY 85 0.09 ASN 50 -0.14 LYS 107
GLY 85 0.10 GLU 51 -0.14 LYS 107
ALA 734 0.09 VAL 52 -0.14 LYS 107
ALA 734 0.08 ASP 53 -0.14 LYS 107
ALA 734 0.09 PHE 54 -0.15 LYS 107
ALA 734 0.10 ILE 55 -0.16 LYS 107
ALA 734 0.11 LEU 56 -0.16 LYS 107
ALA 734 0.12 LEU 57 -0.17 LYS 107
ALA 734 0.12 GLY 58 -0.17 LYS 107
ALA 734 0.14 GLY 59 -0.18 LYS 107
ALA 734 0.15 ASP 60 -0.19 LYS 107
ALA 734 0.14 LEU 61 -0.19 LYS 107
ALA 734 0.15 PHE 62 -0.19 LYS 107
ALA 734 0.16 HIS 63 -0.21 ARG 1239
ALA 734 0.16 GLU 64 -0.21 LYS 107
ALA 734 0.16 ASN 65 -0.22 LYS 107
ALA 734 0.15 LYS 66 -0.22 LYS 107
ALA 734 0.14 PRO 67 -0.21 LYS 107
ALA 734 0.13 SER 68 -0.22 LYS 107
ALA 734 0.12 ARG 69 -0.21 LYS 107
ALA 734 0.12 LYS 70 -0.20 LYS 107
ALA 734 0.13 THR 71 -0.20 LYS 107
ALA 734 0.12 LEU 72 -0.20 LYS 107
ALA 734 0.11 HIS 73 -0.19 LYS 107
ALA 734 0.11 THR 74 -0.19 LYS 107
ALA 734 0.12 CYS 75 -0.18 LYS 107
ALA 734 0.11 LEU 76 -0.18 LYS 107
ALA 734 0.10 GLU 77 -0.18 LYS 107
ALA 734 0.11 LEU 78 -0.17 LYS 107
ALA 734 0.11 LEU 79 -0.17 LYS 107
ALA 734 0.10 ARG 80 -0.17 ASN 117
ALA 734 0.10 LYS 81 -0.19 ASP 86
ALA 734 0.10 TYR 82 -0.16 LYS 107
ALA 734 0.10 CYS 83 -0.16 LYS 107
ALA 734 0.09 MET 84 -0.16 LYS 107
GLU 51 0.10 GLY 85 -0.35 ASP 86
ASN 117 0.09 ASP 86 -0.35 GLY 85
ALA 734 0.08 ARG 87 -0.15 LYS 81
ALA 734 0.08 PRO 88 -0.14 HIS 701
ALA 734 0.09 VAL 89 -0.15 HIS 701
LYS 735 0.08 GLN 90 -0.15 HIS 701
GLY 124 0.09 PHE 91 -0.16 HIS 701
GLY 124 0.10 GLU 92 -0.21 HIS 701
GLY 695 0.11 ILE 93 -0.16 HIS 701
GLY 695 0.15 LEU 94 -0.12 LYS 107
GLY 697 0.13 SER 95 -0.13 GLY 704
PRO 700 0.14 ASP 96 -0.13 GLY 705
GLY 697 0.12 GLN 97 -0.13 LYS 107
ILE 1293 0.13 SER 98 -0.13 LYS 107
ILE 1293 0.15 VAL 99 -0.13 LYS 107
ALA 734 0.12 ASN 100 -0.14 LYS 107
ALA 734 0.12 PHE 101 -0.15 LYS 107
PRO 37 0.13 GLY 102 -0.15 LYS 20
PRO 37 0.14 PHE 103 -0.17 LYS 20
PRO 37 0.11 SER 104 -0.18 LYS 20
PRO 37 0.11 LYS 105 -0.19 LYS 20
ALA 734 0.10 PHE 106 -0.16 LYS 20
PRO 37 0.11 PRO 107 -0.15 LYS 107
ALA 734 0.10 TRP 108 -0.14 LYS 107
ALA 734 0.10 VAL 109 -0.15 LYS 107
ALA 734 0.10 ASN 110 -0.16 LYS 107
ALA 734 0.09 TYR 111 -0.15 LYS 107
ALA 734 0.09 GLN 112 -0.17 PRO 700
ALA 734 0.09 ASP 113 -0.15 LYS 107
ALA 734 0.09 GLY 114 -0.15 LYS 107
ALA 734 0.08 ASN 115 -0.16 LYS 107
ALA 734 0.08 LEU 116 -0.16 LYS 107
ASP 86 0.09 ASN 117 -0.17 ARG 80
ALA 734 0.09 ILE 118 -0.16 LYS 107
ALA 734 0.08 SER 119 -0.15 LYS 107
ALA 734 0.09 ILE 120 -0.15 LYS 107
ALA 734 0.10 PRO 121 -0.16 LYS 107
ALA 734 0.10 VAL 122 -0.16 LYS 107
ALA 734 0.11 PHE 123 -0.16 LYS 107
ALA 734 0.12 SER 124 -0.17 LYS 107
ALA 734 0.13 ILE 125 -0.17 LYS 107
ALA 734 0.14 HIS 126 -0.18 LYS 107
ALA 734 0.16 GLY 127 -0.19 LYS 107
ALA 734 0.18 ASN 128 -0.20 LYS 107
ALA 734 0.18 HIS 129 -0.20 LYS 107
ALA 734 0.16 ASP 130 -0.20 LYS 107
ALA 734 0.18 ASP 131 -0.20 LYS 107
ALA 734 0.17 PRO 132 -0.20 LYS 107
ALA 734 0.18 THR 133 -0.21 LYS 107
PRO 37 0.20 GLY 134 -0.23 LYS 20
PRO 37 0.25 ALA 135 -0.26 LYS 20
PRO 37 0.21 ASP 136 -0.24 LYS 20
PRO 37 0.17 ALA 137 -0.21 LYS 20
ALA 734 0.14 LEU 138 -0.20 LYS 20
ALA 734 0.14 CYS 139 -0.20 LYS 107
ALA 734 0.13 ALA 140 -0.20 LYS 107
ALA 734 0.13 LEU 141 -0.19 LYS 107
ALA 734 0.12 ASP 142 -0.19 LYS 107
ALA 734 0.11 ILE 143 -0.20 LYS 107
ALA 734 0.11 LEU 144 -0.19 LYS 107
ALA 734 0.11 SER 145 -0.18 LYS 107
ALA 734 0.10 CYS 146 -0.18 LYS 107
ALA 734 0.10 ALA 147 -0.18 LYS 107
ALA 734 0.09 GLY 148 -0.17 LYS 107
ALA 734 0.10 PHE 149 -0.17 LYS 107
ALA 734 0.10 VAL 150 -0.17 LYS 107
ALA 734 0.11 ASN 151 -0.16 LYS 107
ALA 734 0.12 HIS 152 -0.17 LYS 107
ALA 734 0.12 PHE 153 -0.16 LYS 107
ALA 734 0.13 GLY 154 -0.16 LYS 107
ALA 734 0.14 ARG 155 -0.17 LYS 107
ALA 734 0.15 SER 156 -0.16 LYS 107
ILE 1293 0.18 MET 157 -0.16 ASP 19
ILE 1293 0.23 SER 158 -0.16 ASP 19
SER 1303 0.28 VAL 159 -0.16 ASP 19
ILE 1293 0.27 GLU 160 -0.14 ASP 19
ILE 1293 0.24 LYS 161 -0.13 LYS 107
ILE 1293 0.19 ILE 162 -0.14 LYS 107
ILE 1293 0.18 ASP 163 -0.13 LYS 107
ILE 1293 0.14 ILE 164 -0.14 LYS 107
GLY 704 0.16 SER 165 -0.14 LYS 107
SER 165 0.14 PRO 166 -0.13 LYS 107
LYS 735 0.11 VAL 167 -0.14 LYS 107
GLY 695 0.12 LEU 168 -0.13 LYS 107
GLY 695 0.12 LEU 169 -0.13 LYS 107
GLY 695 0.10 GLN 170 -0.13 LYS 107
ARG 714 0.09 LYS 171 -0.14 HIS 701
ARG 714 0.09 GLY 172 -0.14 HIS 701
ARG 714 0.10 SER 173 -0.12 LYS 107
ARG 714 0.10 THR 174 -0.12 LYS 107
ARG 714 0.10 LYS 175 -0.12 LYS 107
GLY 124 0.09 ILE 176 -0.13 LYS 107
GLY 124 0.10 ALA 177 -0.13 LYS 107
LYS 735 0.10 LEU 178 -0.14 LYS 107
LYS 735 0.11 TYR 179 -0.14 LYS 107
ALA 734 0.12 GLY 180 -0.15 LYS 107
ALA 734 0.14 LEU 181 -0.16 LYS 107
ALA 734 0.15 GLY 182 -0.17 LYS 107
ALA 734 0.16 SER 183 -0.19 LYS 107
ALA 734 0.19 ILE 184 -0.18 LYS 107
ALA 734 0.21 PRO 185 -0.19 LYS 107
ALA 734 0.18 ASP 186 -0.18 LYS 107
ALA 734 0.23 GLU 187 -0.18 LYS 107
ALA 734 0.24 ARG 188 -0.18 LYS 107
ALA 734 0.18 LEU 189 -0.17 LYS 107
SER 275 0.16 TYR 190 -0.16 LYS 107
GLN 730 0.22 ARG 191 -0.15 LYS 107
ILE 1293 0.18 MET 192 -0.15 LYS 107
ILE 1293 0.16 PHE 193 -0.14 LYS 107
ILE 1293 0.18 VAL 194 -0.13 LYS 107
ILE 1293 0.23 ASN 195 -0.14 ARG 714
ILE 1293 0.22 LYS 196 -0.19 ARG 714
ILE 1293 0.23 LYS 197 -0.16 ARG 714
ILE 1293 0.19 VAL 198 -0.15 ARG 714
ILE 1293 0.18 THR 199 -0.12 LYS 107
ILE 1293 0.15 MET 200 -0.13 LYS 107
GLY 704 0.20 LEU 201 -0.12 LYS 107
GLU 720 0.16 ARG 202 -0.12 LYS 107
GLU 720 0.15 PRO 203 -0.11 LYS 107
ARG 714 0.17 LYS 204 -0.10 LYS 107
ARG 714 0.17 GLU 205 -0.10 LYS 107
ARG 714 0.17 ASP 206 -0.10 LYS 107
ARG 714 0.20 GLU 207 -0.11 LYS 107
ARG 714 0.20 ASN 208 -0.11 LYS 107
ARG 714 0.15 SER 209 -0.11 LYS 107
ARG 714 0.13 TRP 210 -0.12 LYS 107
ARG 714 0.10 PHE 211 -0.13 LYS 107
GLY 124 0.09 ASN 212 -0.13 LYS 107
GLY 124 0.09 LEU 213 -0.14 LYS 107
LYS 735 0.09 PHE 214 -0.15 LYS 107
ALA 734 0.11 VAL 215 -0.16 LYS 107
ALA 734 0.13 ILE 216 -0.16 LYS 107
ALA 734 0.14 HIS 217 -0.18 LYS 107
ALA 734 0.15 GLN 218 -0.18 LYS 107
SER 275 0.20 ASN 219 -0.18 LYS 107
SER 275 0.20 ARG 220 -0.17 LYS 107
SER 275 0.22 SER 221 -0.17 LYS 107
SER 275 0.33 LYS 222 -0.18 LYS 107
SER 275 0.35 HIS 223 -0.18 LYS 107
SER 275 0.28 GLY 224 -0.18 LYS 107
SER 275 0.23 SER 225 -0.17 LYS 107
SER 275 0.20 THR 226 -0.17 LYS 107
SER 275 0.21 ASN 227 -0.19 LYS 107
SER 275 0.21 PHE 228 -0.18 LYS 107
SER 275 0.17 ILE 229 -0.17 LYS 107
SER 275 0.16 PRO 230 -0.16 LYS 107
SER 275 0.14 GLU 231 -0.15 LYS 107
SER 275 0.13 GLN 232 -0.14 LYS 107
LEU 234 0.15 PHE 233 -0.15 LYS 107
PHE 233 0.15 LEU 234 -0.14 LYS 107
GLU 720 0.11 ASP 235 -0.13 LYS 107
ILE 1293 0.11 ASP 236 -0.13 LYS 107
ARG 714 0.12 PHE 237 -0.13 LYS 107
ILE 1293 0.09 ILE 238 -0.13 LYS 107
GLY 124 0.08 ASP 239 -0.13 LYS 107
GLY 124 0.07 LEU 240 -0.14 LYS 107
LYS 735 0.08 VAL 241 -0.15 LYS 107
ALA 734 0.10 ILE 242 -0.16 LYS 107
ALA 734 0.11 TRP 243 -0.17 LYS 107
ALA 734 0.13 GLY 244 -0.18 LYS 107
ALA 734 0.14 HIS 245 -0.19 LYS 107
ALA 734 0.14 GLU 246 -0.18 LYS 107
ALA 734 0.13 HIS 247 -0.18 ARG 1239
ALA 734 0.12 GLU 248 -0.18 LYS 107
ALA 734 0.11 CYS 249 -0.17 LYS 107
ALA 734 0.09 LYS 250 -0.16 LYS 107
ALA 734 0.09 ILE 251 -0.16 LYS 107
ALA 734 0.07 ALA 252 -0.15 LYS 107
LYS 735 0.06 PRO 253 -0.15 LYS 107
GLY 277 0.07 THR 254 -0.15 LYS 107
SER 275 0.07 LYS 255 -0.14 LYS 107
SER 275 0.09 ASN 256 -0.15 LYS 107
SER 275 0.08 GLU 257 -0.14 LYS 107
SER 275 0.09 GLN 258 -0.14 LYS 107
SER 275 0.09 GLN 259 -0.14 LYS 107
ILE 1293 0.08 LEU 260 -0.13 LYS 107
SER 275 0.07 PHE 261 -0.14 LYS 107
SER 275 0.06 TYR 262 -0.15 LYS 107
SER 275 0.07 ILE 263 -0.15 LYS 107
ALA 734 0.08 SER 264 -0.16 LYS 107
ALA 734 0.10 GLN 265 -0.16 LYS 107
ALA 734 0.10 PRO 266 -0.16 LYS 107
ALA 734 0.12 GLY 267 -0.17 LYS 107
ALA 734 0.13 SER 268 -0.18 LYS 107
ALA 734 0.13 SER 269 -0.17 LYS 107
ALA 734 0.15 VAL 270 -0.17 LYS 107
ALA 734 0.16 VAL 271 -0.20 ARG 1239
LYS 1254 0.19 THR 272 -0.25 ARG 1239
LYS 1254 0.25 SER 273 -0.27 ARG 1239
HIS 223 0.30 LEU 274 -0.25 GLU 1240
HIS 223 0.35 SER 275 -0.25 GLU 1240
HIS 223 0.27 PRO 276 -0.19 GLU 1240
LYS 222 0.22 GLY 277 -0.20 GLU 1243
LYS 222 0.18 GLU 278 -0.19 ARG 1239
LYS 222 0.15 ALA 279 -0.17 LYS 107
LYS 222 0.12 VAL 280 -0.16 LYS 107
ALA 734 0.11 LYS 281 -0.16 LYS 107
ALA 734 0.11 LYS 282 -0.16 LYS 107
ALA 734 0.10 HIS 283 -0.16 LYS 107
ALA 734 0.10 VAL 284 -0.16 LYS 107
ALA 734 0.09 GLY 285 -0.15 LYS 107
ALA 734 0.08 LEU 286 -0.15 LYS 107
ALA 734 0.08 LEU 287 -0.14 LYS 107
LYS 735 0.07 ARG 288 -0.14 LYS 107
GLY 124 0.07 ILE 289 -0.13 LYS 107
ARG 714 0.07 LYS 290 -0.13 LYS 107
ARG 714 0.09 GLY 291 -0.12 LYS 107
ARG 714 0.09 ARG 292 -0.12 LYS 107
ARG 714 0.08 LYS 293 -0.13 LYS 107
GLY 124 0.06 MET 294 -0.14 LYS 107
GLY 124 0.06 ASN 295 -0.14 LYS 107
ALA 734 0.07 MET 296 -0.14 LYS 107
ALA 734 0.07 HIS 297 -0.14 LYS 107
ALA 734 0.08 LYS 298 -0.15 LYS 107
ALA 734 0.08 ILE 299 -0.15 LYS 107
ALA 734 0.09 PRO 300 -0.15 LYS 107
ALA 734 0.10 LEU 301 -0.16 LYS 107
ALA 734 0.11 HIS 302 -0.15 LYS 107
ALA 734 0.12 THR 303 -0.15 LYS 107
ALA 734 0.13 VAL 304 -0.16 LYS 107
ALA 734 0.14 ARG 305 -0.16 LYS 107
ALA 734 0.08 LYS 690 -0.16 GLY 85
GLU 10 0.09 VAL 691 -0.24 GLY 85
GLY 124 0.09 THR 692 -0.19 ALA 696
GLU 92 0.10 TYR 693 -0.18 GLY 85
GLY 124 0.10 PRO 694 -0.17 HIS 701
LEU 94 0.15 GLY 695 -0.20 PRO 700
LEU 94 0.12 ALA 696 -0.19 THR 692
LEU 94 0.14 GLY 697 -0.16 GLY 85
LEU 94 0.14 LYS 698 -0.16 GLY 85
GLY 124 0.13 LEU 699 -0.18 GLY 695
ILE 702 0.20 PRO 700 -0.20 GLY 695
ILE 703 0.19 HIS 701 -0.21 GLU 92
PRO 700 0.20 ILE 702 -0.10 LYS 107
HIS 701 0.19 ILE 703 -0.10 LYS 107
LEU 201 0.20 GLY 704 -0.13 SER 95
ILE 1293 0.19 GLY 705 -0.13 ASP 96
ILE 1293 0.20 SER 706 -0.09 ASP 96
HIS 701 0.18 ASP 707 -0.10 LYS 107
GLU 720 0.18 LEU 708 -0.10 LYS 107
GLU 720 0.22 ILE 709 -0.10 LYS 107
GLU 720 0.20 ALA 710 -0.10 LYS 107
GLU 720 0.21 HIS 711 -0.11 LYS 107
GLU 720 0.28 HIS 712 -0.11 LYS 107
GLU 720 0.30 ALA 713 -0.20 ARG 714
GLU 207 0.20 ARG 714 -0.20 ALA 713
ILE 709 0.16 LYS 715 -0.14 LYS 196
ALA 713 0.18 ASN 716 -0.12 LYS 107
ALA 713 0.17 THR 717 -0.11 LYS 107
ALA 713 0.19 GLU 718 -0.13 GLN 258
ALA 713 0.25 LEU 719 -0.12 LYS 107
ALA 713 0.30 GLU 720 -0.11 LYS 107
HIS 712 0.21 GLU 721 -0.11 LYS 107
ALA 713 0.19 TRP 722 -0.12 LYS 107
HIS 712 0.20 LEU 723 -0.12 LYS 107
ILE 1293 0.21 ARG 724 -0.10 LYS 107
ILE 1293 0.19 GLN 725 -0.11 LYS 107
ILE 1293 0.18 GLU 726 -0.13 LYS 107
ILE 1293 0.23 MET 727 -0.11 LYS 107
ILE 1293 0.24 GLU 728 -0.09 LYS 107
ILE 1293 0.20 VAL 729 -0.12 LYS 107
LYS 1301 0.25 GLN 730 -0.12 LYS 107
LYS 1301 0.30 ASN 731 -0.09 LYS 108
LYS 1301 0.29 GLN 732 -0.09 LYS 108
LYS 1301 0.30 HIS 733 -0.12 LYS 107
LYS 1301 0.41 ALA 734 -0.10 LYS 108
LYS 1301 0.37 LYS 735 -0.09 LYS 108
LYS 1301 0.34 GLU 736 -0.10 LYS 108
LYS 1301 0.43 GLU 737 -0.11 LYS 108
LYS 1301 0.41 SER 738 -0.10 LYS 108
ASN 1292 0.33 LEU 739 -0.11 LYS 108
ASN 1292 0.31 ALA 740 -0.12 LYS 108
ASN 1292 0.39 ASP 741 -0.11 LYS 108
ASN 1292 0.38 ASP 742 -0.11 LYS 108
ASN 1292 0.30 LEU 743 -0.13 LYS 108
ASN 1292 0.33 PHE 744 -0.13 LYS 108
ASN 1292 0.42 ARG 745 -0.13 VAL 72
LYS 20 0.46 TYR 746 -0.12 GLN 74
LYS 20 0.57 ASN 747 -0.15 ALA 73
LYS 20 0.46 PRO 748 -0.16 GLU 75
LYS 20 0.51 TYR 749 -0.20 GLU 75
LYS 20 0.41 LEU 750 -0.24 GLU 75

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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.