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CA distance fluctuations for 2604262204102534339

---  normal mode 13  ---

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 351 0.12 SER 1 -0.08 GLY 134
PRO 351 0.11 THR 2 -0.10 GLY 134
LYS 39 0.09 ALA 3 -0.10 GLY 134
PRO 351 0.08 GLY 4 -0.12 GLY 134
PRO 351 0.08 LYS 5 -0.15 GLY 134
PHE 352 0.09 VAL 6 -0.17 GLY 134
PHE 352 0.11 ILE 7 -0.12 GLY 134
PHE 352 0.13 LYS 8 -0.09 GLY 134
PHE 352 0.16 CYS 9 -0.06 CYS 100
PHE 352 0.18 LYS 10 -0.06 CYS 100
PHE 352 0.11 ALA 11 -0.07 LEU 112
LYS 135 0.13 ALA 12 -0.08 ASP 115
LYS 135 0.16 VAL 13 -0.09 CYS 100
LYS 135 0.15 LEU 14 -0.10 ASP 115
LYS 135 0.20 TRP 15 -0.10 CYS 100
LYS 135 0.15 GLU 16 -0.11 LYS 247
LYS 135 0.11 GLU 17 -0.12 LYS 247
PRO 295 0.12 LYS 18 -0.12 LYS 247
LYS 135 0.13 LYS 19 -0.10 SER 117
LYS 135 0.13 PRO 20 -0.10 GLU 353
LYS 135 0.14 PHE 21 -0.11 GLU 353
LYS 135 0.17 SER 22 -0.07 ASP 115
ASN 356 0.16 ILE 23 -0.08 ASP 115
ARG 133 0.18 GLU 24 -0.08 CYS 100
PHE 352 0.13 GLU 25 -0.09 CYS 100
PHE 352 0.11 VAL 26 -0.10 CYS 100
PHE 352 0.10 GLU 27 -0.13 GLY 134
PHE 352 0.09 VAL 28 -0.12 GLY 134
GLN 148 0.08 ALA 29 -0.17 GLY 134
ASP 125 0.09 PRO 30 -0.14 GLY 134
ASP 125 0.13 PRO 31 -0.12 LYS 99
ASP 125 0.23 LYS 32 -0.17 LYS 99
ASP 125 0.24 ALA 33 -0.19 GLY 98
ASP 125 0.17 HIS 34 -0.17 GLY 98
ASP 125 0.14 GLU 35 -0.11 GLY 98
ASP 125 0.09 VAL 36 -0.09 GLY 134
ASP 125 0.09 ARG 37 -0.08 GLY 134
PRO 305 0.08 ILE 38 -0.08 GLN 244
THR 2 0.11 LYS 39 -0.07 GLN 244
THR 2 0.09 MET 40 -0.07 GLN 244
SER 1 0.11 VAL 41 -0.08 ASN 225
PRO 106 0.10 ALA 42 -0.09 ASN 225
PRO 106 0.09 THR 43 -0.10 ASN 225
PRO 106 0.10 GLY 44 -0.12 SER 117
GLY 175 0.10 ILE 45 -0.14 SER 117
GLY 175 0.16 CYS 46 -0.20 LEU 116
VAL 203 0.14 ARG 47 -0.25 SER 117
GLY 316 0.14 SER 48 -0.30 LEU 116
GLY 316 0.12 ASP 49 -0.20 SER 117
GLY 316 0.12 ASP 50 -0.19 SER 117
GLY 316 0.15 HIS 51 -0.24 SER 117
GLY 316 0.12 VAL 52 -0.19 SER 117
GLY 316 0.12 VAL 53 -0.15 SER 117
PRO 295 0.14 SER 54 -0.16 LYS 247
GLY 316 0.12 GLY 55 -0.17 LYS 247
PRO 296 0.19 THR 56 -0.20 LYS 247
ILE 318 0.18 LEU 57 -0.24 SER 117
ILE 318 0.14 VAL 58 -0.15 LYS 247
ASN 304 0.10 THR 59 -0.14 PRO 119
ASN 304 0.10 PRO 60 -0.14 CYS 100
GLY 55 0.11 LEU 61 -0.13 CYS 100
LYS 135 0.12 PRO 62 -0.12 CYS 100
LYS 135 0.09 VAL 63 -0.12 CYS 100
LYS 135 0.09 ILE 64 -0.10 ASP 115
PRO 305 0.09 ALA 65 -0.12 ASP 115
PHE 319 0.09 GLY 66 -0.12 ASP 115
PHE 322 0.10 HIS 67 -0.13 ASP 115
PHE 322 0.11 GLU 68 -0.12 ILE 224
PRO 106 0.11 ALA 69 -0.10 ASN 225
PRO 106 0.12 ALA 70 -0.10 ASN 225
GLY 98 0.10 GLY 71 -0.08 ASN 225
GLY 98 0.11 ILE 72 -0.08 ASN 225
GLY 98 0.09 VAL 73 -0.07 ILE 224
PRO 305 0.08 GLU 74 -0.08 GLY 134
ASP 125 0.08 SER 75 -0.09 GLY 134
ASP 125 0.10 ILE 76 -0.08 GLY 134
ASP 125 0.15 GLY 77 -0.10 ASP 326
ASP 125 0.17 GLU 78 -0.12 GLY 98
ASP 125 0.14 GLY 79 -0.15 ASP 326
ASP 125 0.11 VAL 80 -0.16 ASP 326
CYS 97 0.16 THR 81 -0.15 ASP 326
CYS 97 0.23 THR 82 -0.15 ASP 326
GLY 98 0.16 VAL 83 -0.09 PRO 329
GLY 98 0.12 ARG 84 -0.08 ILE 224
GLY 98 0.09 PRO 85 -0.07 GLY 134
GLY 98 0.12 GLY 86 -0.07 ASN 225
GLY 98 0.16 ASP 87 -0.08 ASN 225
GLY 98 0.17 LYS 88 -0.09 ASN 225
GLY 98 0.17 VAL 89 -0.09 ASN 225
GLY 98 0.15 ILE 90 -0.10 ASN 225
PRO 305 0.10 PRO 91 -0.10 ILE 224
PRO 305 0.12 LEU 92 -0.10 ILE 224
PRO 305 0.12 PHE 93 -0.12 GLN 244
PRO 305 0.13 THR 94 -0.16 GLY 293
PRO 305 0.12 PRO 95 -0.17 GLN 124
LYS 325 0.18 GLN 96 -0.18 GLN 124
THR 82 0.23 CYS 97 -0.38 GLN 124
ASP 326 0.39 GLY 98 -0.31 ASP 125
ASP 326 0.30 LYS 99 -0.38 ASP 125
ASP 326 0.24 CYS 100 -0.35 ASP 125
ASP 326 0.23 ARG 101 -0.29 ASP 125
ASP 326 0.23 VAL 102 -0.24 LEU 301
ASP 326 0.36 CYS 103 -0.25 ASP 125
ASP 326 0.38 LYS 104 -0.26 ASP 125
ASP 326 0.32 HIS 105 -0.21 LEU 301
LYS 185 0.30 PRO 106 -0.19 ASP 125
PRO 305 0.25 GLU 107 -0.16 ASP 125
PRO 305 0.22 GLY 108 -0.18 LEU 301
PRO 305 0.20 ASN 109 -0.15 ASP 125
PRO 305 0.17 PHE 110 -0.21 GLY 293
PRO 305 0.15 CYS 111 -0.21 ASP 125
ASP 326 0.13 LEU 112 -0.26 ARG 120
ILE 155 0.14 LYS 113 -0.24 ARG 120
ILE 155 0.13 ASN 114 -0.27 PRO 296
ASP 153 0.16 ASP 115 -0.34 PRO 296
PRO 119 0.13 LEU 116 -0.44 PRO 296
GLN 124 0.12 SER 117 -0.58 PRO 296
ALA 33 0.11 MET 118 -0.40 PRO 296
LEU 116 0.13 PRO 119 -0.29 PRO 296
LYS 32 0.10 ARG 120 -0.26 LEU 112
LYS 32 0.09 GLY 121 -0.20 CYS 100
LYS 32 0.11 THR 122 -0.23 CYS 100
LYS 32 0.13 MET 123 -0.25 CYS 97
ASP 115 0.15 GLN 124 -0.38 CYS 97
ALA 33 0.24 ASP 125 -0.38 LYS 99
LYS 32 0.17 GLY 126 -0.32 LYS 99
LYS 32 0.16 THR 127 -0.27 LYS 99
LYS 32 0.10 SER 128 -0.21 LYS 99
LYS 32 0.06 ARG 129 -0.18 LYS 99
PHE 352 0.07 PHE 130 -0.15 LYS 99
PHE 352 0.08 THR 131 -0.14 LYS 99
ARG 133 0.11 CYS 132 -0.12 CYS 100
GLU 24 0.18 ARG 133 -0.13 LYS 99
TRP 15 0.14 GLY 134 -0.18 LYS 99
TRP 15 0.20 LYS 135 -0.16 LYS 99
SER 22 0.07 PRO 136 -0.18 CYS 100
LYS 135 0.08 ILE 137 -0.14 CYS 100
LYS 32 0.08 HIS 138 -0.16 CYS 100
LYS 32 0.08 HIS 139 -0.14 CYS 100
PRO 305 0.09 PHE 140 -0.14 ASP 115
PRO 305 0.10 LEU 141 -0.16 ASP 115
PRO 305 0.10 GLY 142 -0.13 CYS 97
PRO 305 0.10 THR 143 -0.10 GLN 244
PRO 305 0.09 SER 144 -0.09 GLN 244
PRO 305 0.09 THR 145 -0.09 GLN 244
ILE 45 0.09 PHE 146 -0.08 LYS 247
PRO 305 0.08 SER 147 -0.07 LYS 247
THR 2 0.09 GLN 148 -0.06 GLN 244
ALA 29 0.08 TYR 149 -0.07 GLN 244
PRO 305 0.08 THR 150 -0.08 GLN 244
PRO 305 0.08 VAL 151 -0.09 GLY 134
PRO 305 0.09 VAL 152 -0.09 GLN 244
ASP 115 0.16 ASP 153 -0.12 CYS 97
ASP 115 0.12 GLU 154 -0.12 LYS 325
LYS 113 0.14 ILE 155 -0.14 LYS 323
PRO 305 0.10 SER 156 -0.11 LEU 301
GLY 98 0.13 VAL 157 -0.10 ILE 224
GLY 98 0.25 ALA 158 -0.10 SER 177
GLY 98 0.25 LYS 159 -0.10 ASN 225
GLY 98 0.25 ILE 160 -0.11 ILE 172
GLY 98 0.22 ASP 161 -0.10 LYS 228
GLY 98 0.19 ALA 162 -0.09 ASN 225
LYS 104 0.17 ALA 163 -0.09 LYS 228
LYS 104 0.18 SER 164 -0.10 LYS 228
PRO 106 0.16 PRO 165 -0.10 ASN 225
PRO 106 0.14 LEU 166 -0.10 ASN 225
PRO 106 0.13 GLU 167 -0.11 ASN 225
PRO 106 0.15 LYS 168 -0.12 ASN 225
PRO 106 0.17 VAL 169 -0.11 ASN 225
PRO 106 0.14 CYS 170 -0.11 ASN 225
PRO 106 0.15 LEU 171 -0.12 ASN 225
PRO 106 0.18 ILE 172 -0.11 ILE 160
PRO 106 0.14 GLY 173 -0.10 ILE 224
PRO 106 0.12 CYS 174 -0.14 LEU 116
CYS 46 0.16 GLY 175 -0.15 SER 117
PRO 106 0.14 PHE 176 -0.12 SER 117
PRO 106 0.16 SER 177 -0.13 VAL 328
SER 48 0.14 THR 178 -0.14 SER 117
ARG 47 0.13 GLY 179 -0.13 SER 117
PRO 106 0.17 TYR 180 -0.12 LEU 331
PRO 106 0.20 GLY 181 -0.09 VAL 80
PRO 106 0.15 SER 182 -0.10 SER 117
PRO 106 0.18 ALA 183 -0.09 SER 117
PRO 106 0.26 VAL 184 -0.08 VAL 80
PRO 106 0.30 LYS 185 -0.08 GLY 79
PRO 305 0.21 VAL 186 -0.10 LEU 301
THR 313 0.19 ALA 187 -0.09 LEU 301
PRO 106 0.25 LYS 188 -0.07 LEU 301
PRO 106 0.20 VAL 189 -0.07 GLY 79
PRO 106 0.21 THR 190 -0.06 GLY 79
PRO 106 0.19 GLN 191 -0.06 GLY 79
PRO 106 0.16 GLY 192 -0.06 SER 117
PRO 106 0.14 SER 193 -0.08 SER 117
LEU 254 0.12 THR 194 -0.10 SER 117
PRO 106 0.11 CYS 195 -0.12 SER 117
ILE 250 0.09 ALA 196 -0.15 SER 117
ASN 300 0.10 VAL 197 -0.17 SER 117
ASN 300 0.08 PHE 198 -0.21 SER 117
SER 364 0.10 GLY 199 -0.22 SER 117
SER 364 0.12 LEU 200 -0.19 SER 117
SER 364 0.14 GLY 201 -0.20 SER 117
LEU 362 0.17 GLY 202 -0.17 SER 117
LEU 362 0.15 VAL 203 -0.17 SER 117
ARG 363 0.11 GLY 204 -0.17 SER 117
LEU 362 0.13 LEU 205 -0.14 PHE 340
PRO 106 0.13 SER 206 -0.13 PHE 340
PRO 106 0.13 VAL 207 -0.13 SER 117
PRO 106 0.13 ILE 208 -0.11 SER 117
PRO 106 0.16 MET 209 -0.10 PHE 340
PRO 106 0.19 GLY 210 -0.08 THR 82
PRO 106 0.17 CYS 211 -0.09 SER 117
PRO 106 0.18 LYS 212 -0.07 SER 117
PRO 106 0.21 ALA 213 -0.07 THR 82
PRO 106 0.23 ALA 214 -0.07 GLY 79
PRO 106 0.20 GLY 215 -0.06 GLY 79
PRO 106 0.16 ALA 216 -0.07 SER 117
PRO 106 0.14 ALA 217 -0.08 SER 117
TYR 246 0.13 ARG 218 -0.10 ASN 304
PRO 106 0.11 ILE 219 -0.14 SER 258
VAL 241 0.13 ILE 220 -0.23 SER 258
PRO 106 0.08 GLY 221 -0.19 MET 257
ILE 220 0.06 VAL 222 -0.19 ASN 304
ASN 225 0.05 ASP 223 -0.22 SER 117
PRO 249 0.06 ILE 224 -0.23 SER 117
ASP 223 0.05 ASN 225 -0.24 GLU 366
PRO 106 0.04 LYS 226 -0.18 SER 117
PRO 106 0.05 ASP 227 -0.19 PRO 344
SER 364 0.10 LYS 228 -0.23 PRO 344
SER 364 0.08 PHE 229 -0.16 MET 257
GLU 366 0.12 ALA 230 -0.14 MET 257
ILE 368 0.19 LYS 231 -0.15 PHE 340
ILE 368 0.11 ALA 232 -0.13 MET 257
ILE 368 0.11 LYS 233 -0.13 MET 257
ILE 368 0.14 GLU 234 -0.13 PHE 340
LEU 345 0.17 VAL 235 -0.17 PHE 340
PRO 106 0.13 GLY 236 -0.10 SER 258
PRO 106 0.11 ALA 237 -0.14 SER 258
PRO 106 0.12 THR 238 -0.17 SER 258
TYR 246 0.13 GLU 239 -0.24 MET 257
TYR 246 0.11 CYS 240 -0.24 MET 257
ILE 220 0.13 VAL 241 -0.24 ASN 304
TYR 246 0.08 ASN 242 -0.26 ASN 304
TYR 246 0.07 PRO 243 -0.33 ASN 304
GLU 239 0.05 GLN 244 -0.32 ASN 304
GLU 239 0.10 ASP 245 -0.33 ASN 304
ARG 218 0.13 TYR 246 -0.39 ASN 304
VAL 253 0.14 LYS 247 -0.46 ASN 304
VAL 253 0.14 LYS 248 -0.53 ASN 304
THR 194 0.07 PRO 249 -0.55 ASN 304
THR 194 0.10 ILE 250 -0.42 ASN 304
THR 194 0.05 GLN 251 -0.45 ASN 304
THR 194 0.07 GLU 252 -0.46 ASN 304
LYS 248 0.14 VAL 253 -0.38 ASN 304
THR 194 0.12 LEU 254 -0.33 ASN 304
PRO 106 0.07 THR 255 -0.32 ASN 304
LYS 247 0.13 GLU 256 -0.30 ASN 304
LYS 247 0.13 MET 257 -0.26 ASN 304
PRO 106 0.10 SER 258 -0.23 ILE 220
PRO 106 0.10 ASN 259 -0.20 ASN 304
PRO 106 0.10 GLY 260 -0.19 ASN 304
PRO 106 0.09 GLY 261 -0.20 ASN 304
PRO 106 0.10 VAL 262 -0.13 ASN 304
PRO 106 0.13 ASP 263 -0.08 SER 117
ASN 300 0.12 PHE 264 -0.11 SER 117
ASN 300 0.13 SER 265 -0.15 SER 117
ASN 300 0.14 PHE 266 -0.18 SER 117
ASN 300 0.14 GLU 267 -0.23 SER 117
ASN 300 0.12 VAL 268 -0.25 SER 117
SER 364 0.09 ILE 269 -0.29 SER 117
ASN 300 0.11 GLY 270 -0.35 SER 117
LEU 301 0.08 ARG 271 -0.32 SER 117
LEU 301 0.13 LEU 272 -0.32 SER 117
LEU 301 0.09 ASP 273 -0.31 MET 303
ALA 196 0.05 THR 274 -0.26 SER 117
ASN 300 0.16 MET 275 -0.26 SER 117
ASN 300 0.13 VAL 276 -0.24 MET 303
ASN 300 0.05 THR 277 -0.34 ASN 304
ASN 300 0.11 ALA 278 -0.19 SER 117
ASN 300 0.15 LEU 279 -0.16 SER 117
ASN 300 0.09 SER 280 -0.33 ASN 304
ASN 300 0.07 CYS 281 -0.28 ASN 304
ASN 300 0.10 CYS 282 -0.16 ASN 304
ASN 300 0.10 GLN 283 -0.11 ASN 304
ASN 300 0.12 GLU 284 -0.11 ALA 285
GLU 107 0.12 ALA 285 -0.11 LEU 301
PRO 106 0.13 TYR 286 -0.11 LEU 301
ASN 300 0.11 GLY 287 -0.10 LEU 301
ALA 187 0.14 VAL 288 -0.12 LEU 301
ASN 300 0.17 SER 289 -0.13 SER 117
ASN 300 0.19 VAL 290 -0.15 SER 117
ASN 300 0.21 ILE 291 -0.23 SER 117
ASN 300 0.16 VAL 292 -0.23 SER 117
ASN 300 0.15 GLY 293 -0.37 SER 117
ASN 300 0.17 VAL 294 -0.45 SER 117
SER 54 0.14 PRO 295 -0.46 SER 117
THR 56 0.19 PRO 296 -0.58 SER 117
SER 54 0.12 ASP 297 -0.43 SER 117
SER 54 0.12 SER 298 -0.46 SER 117
GLY 316 0.16 GLN 299 -0.24 LYS 247
MET 303 0.33 ASN 300 -0.19 SER 117
LEU 272 0.13 LEU 301 -0.33 SER 117
VAL 276 0.07 SER 302 -0.24 PRO 305
ASN 300 0.33 MET 303 -0.40 PRO 249
ASN 300 0.28 ASN 304 -0.55 PRO 249
LYS 315 0.25 PRO 305 -0.35 PRO 249
GLU 107 0.19 MET 306 -0.30 PRO 249
TRP 314 0.21 LEU 307 -0.28 GLN 251
THR 313 0.22 LEU 308 -0.26 LEU 301
GLU 107 0.18 LEU 309 -0.19 LEU 301
GLU 107 0.15 SER 310 -0.13 PRO 249
GLU 107 0.16 GLY 311 -0.17 LEU 301
ALA 187 0.15 ARG 312 -0.18 LEU 301
LEU 308 0.22 THR 313 -0.21 LEU 301
PRO 305 0.25 TRP 314 -0.24 LEU 301
PRO 305 0.25 LYS 315 -0.19 LEU 301
ASN 300 0.25 GLY 316 -0.14 VAL 102
PRO 305 0.21 ALA 317 -0.16 PHE 110
LEU 57 0.18 ILE 318 -0.20 PHE 110
PRO 305 0.15 PHE 319 -0.10 ASN 114
PRO 305 0.16 GLY 320 -0.09 VAL 80
PRO 305 0.19 GLY 321 -0.10 LEU 301
PRO 106 0.18 PHE 322 -0.11 VAL 80
CYS 103 0.22 LYS 323 -0.14 ILE 155
CYS 103 0.18 SER 324 -0.14 ILE 155
GLY 98 0.34 LYS 325 -0.15 VAL 80
GLY 98 0.39 ASP 326 -0.16 VAL 80
LYS 104 0.30 SER 327 -0.13 THR 82
LYS 104 0.22 VAL 328 -0.13 SER 177
GLY 98 0.27 PRO 329 -0.14 THR 82
PRO 106 0.30 LYS 330 -0.12 THR 82
PRO 106 0.27 LEU 331 -0.12 SER 206
PRO 106 0.22 VAL 332 -0.10 LYS 228
PRO 106 0.25 ALA 333 -0.10 LYS 228
PRO 106 0.27 ASP 334 -0.11 SER 206
PRO 106 0.22 PHE 335 -0.13 LYS 228
PRO 106 0.21 MET 336 -0.12 LYS 228
PRO 106 0.23 ALA 337 -0.11 LYS 228
PRO 106 0.21 LYS 338 -0.13 LYS 231
PRO 106 0.24 LYS 339 -0.13 VAL 235
PRO 106 0.22 PHE 340 -0.17 VAL 235
PRO 106 0.19 ALA 341 -0.15 LYS 228
PRO 106 0.17 LEU 342 -0.15 LYS 228
PRO 106 0.15 ASP 343 -0.17 LYS 228
PRO 106 0.14 PRO 344 -0.23 LYS 228
VAL 235 0.17 LEU 345 -0.18 LYS 228
PRO 106 0.12 ILE 346 -0.15 ASN 225
VAL 235 0.13 THR 347 -0.16 ASN 225
VAL 235 0.10 HIS 348 -0.14 ASN 225
PRO 106 0.10 VAL 349 -0.11 ASN 225
LYS 10 0.11 LEU 350 -0.10 SER 117
CYS 9 0.14 PRO 351 -0.08 SER 117
LYS 10 0.18 PHE 352 -0.08 GLN 244
LYS 10 0.14 GLU 353 -0.11 PHE 21
ARG 133 0.12 LYS 354 -0.11 SER 117
ILE 23 0.13 ILE 355 -0.12 SER 117
ILE 23 0.16 ASN 356 -0.14 SER 117
ILE 23 0.14 GLU 357 -0.12 SER 117
ARG 133 0.11 GLY 358 -0.13 SER 117
ILE 23 0.12 PHE 359 -0.16 SER 117
GLY 202 0.12 ASP 360 -0.15 SER 117
LYS 231 0.13 LEU 361 -0.15 SER 117
GLY 202 0.17 LEU 362 -0.18 SER 117
GLY 202 0.15 ARG 363 -0.19 SER 117
GLY 201 0.14 SER 364 -0.17 SER 117
LYS 231 0.15 GLY 365 -0.21 SER 117
LYS 231 0.18 GLU 366 -0.24 ASN 225
LYS 231 0.15 SER 367 -0.19 ASN 225
LYS 231 0.19 ILE 368 -0.19 SER 117
SER 206 0.13 ARG 369 -0.16 ASN 225
VAL 235 0.10 THR 370 -0.13 SER 117
PRO 106 0.10 ILE 371 -0.11 ASN 225
LYS 10 0.11 LEU 372 -0.10 SER 117
CYS 9 0.11 THR 373 -0.09 ASN 225

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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.