CNRS Nantes University US2B US2B
home |  start a new run |  job status |  references&downloads |  examples |  help  

Should you encounter any unexpected behaviour,
please let us know.
 elNémo has been hacked on november 27th.
It has been moved away and runs again.
**Still some additional cleaning from time to time**
Sorry for the inconvenience.


***  SIGNALING PROTEIN 20-OCT-09 3KB3  ***

CA distance fluctuations for 2602031626281395717

---  normal mode 8  ---

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
VAL 310 0.61 CYS 186 -0.13 ASP 370
VAL 310 0.62 ILE 187 -0.13 SER 336
VAL 310 0.58 PRO 188 -0.11 ASP 370
VAL 310 0.51 LEU 189 -0.11 ASP 370
VAL 310 0.44 TRP 190 -0.08 ASP 370
VAL 310 0.37 GLY 191 -0.05 ASP 370
VAL 310 0.28 THR 192 -0.06 VAL 208
VAL 310 0.18 VAL 193 -0.06 VAL 208
VAL 193 0.17 SER 194 -0.07 VAL 208
GLN 386 0.18 ILE 195 -0.07 ASP 256
GLN 386 0.25 GLN 196 -0.14 VAL 309
GLN 386 0.25 GLY 197 -0.12 VAL 309
GLN 386 0.34 ASN 198 -0.18 VAL 310
GLN 386 0.40 ARG 199 -0.23 VAL 310
GLN 386 0.43 SER 200 -0.32 VAL 310
GLN 386 0.34 GLU 201 -0.31 VAL 310
GLN 386 0.24 MET 202 -0.20 VAL 309
VAL 393 0.20 GLU 203 -0.17 VAL 309
VAL 393 0.16 ASP 204 -0.08 VAL 309
GLY 469 0.19 ALA 205 -0.10 ARG 255
VAL 310 0.22 PHE 206 -0.07 SER 194
VAL 310 0.37 ALA 207 -0.08 ALA 263
VAL 310 0.51 VAL 208 -0.07 SER 194
VAL 310 0.66 SER 209 -0.09 PHE 212
VAL 310 0.70 PRO 210 -0.06 ASP 370
VAL 310 0.79 HIS 211 -0.07 ASP 370
VAL 310 0.80 PHE 212 -0.09 SER 209
VAL 310 0.78 LEU 213 -0.08 GLU 267
VAL 310 0.76 LYS 214 -0.08 ASP 370
VAL 310 0.64 LEU 215 -0.10 ASP 370
VAL 310 0.60 PRO 216 -0.10 ASP 370
VAL 310 0.55 ILE 217 -0.12 ASP 370
VAL 310 0.48 LYS 218 -0.13 ASP 370
VAL 310 0.46 MET 219 -0.15 ASP 370
VAL 310 0.42 LEU 220 -0.17 ASP 370
VAL 310 0.66 LEU 234 -0.12 ASP 370
VAL 310 0.70 THR 235 -0.11 ASP 370
VAL 310 0.64 GLY 236 -0.11 ASP 370
VAL 310 0.61 HIS 237 -0.09 ASP 370
VAL 310 0.54 PHE 238 -0.07 ASP 370
VAL 310 0.42 PHE 239 -0.06 ASP 370
VAL 310 0.30 GLY 240 -0.05 SER 194
VAL 310 0.18 VAL 241 -0.04 SER 194
GLY 469 0.13 TYR 242 -0.04 ARG 255
ALA 395 0.15 ASP 243 -0.08 ASP 432
VAL 393 0.16 GLY 244 -0.12 ASP 432
VAL 393 0.23 HIS 245 -0.18 VAL 310
VAL 393 0.29 GLY 246 -0.29 VAL 310
VAL 393 0.21 GLY 247 -0.31 VAL 310
GLY 469 0.20 HIS 248 -0.24 VAL 310
GLY 469 0.23 LYS 249 -0.29 VAL 309
GLY 469 0.19 VAL 250 -0.15 VAL 309
GLY 469 0.19 ALA 251 -0.07 VAL 309
GLY 469 0.25 ASP 252 -0.12 MET 202
GLY 469 0.24 TYR 253 -0.09 MET 202
GLY 469 0.19 CYS 254 -0.07 MET 202
GLY 469 0.25 ARG 255 -0.10 ALA 205
VAL 310 0.34 ASP 256 -0.11 MET 202
VAL 310 0.38 ARG 257 -0.08 MET 202
VAL 310 0.35 LEU 258 -0.07 ARG 255
VAL 310 0.52 HIS 259 -0.06 GLN 196
VAL 310 0.66 PHE 260 -0.08 GLN 196
ALA 308 0.52 ALA 261 -0.06 MET 202
VAL 310 0.50 LEU 262 -0.06 ALA 207
VAL 310 0.65 ALA 263 -0.08 ALA 207
SER 313 0.64 GLU 264 -0.06 MET 202
SER 313 0.52 GLU 265 -0.05 ALA 207
SER 313 0.57 ILE 266 -0.06 LEU 213
SER 313 0.62 GLU 267 -0.08 LEU 213
SER 313 0.53 ARG 268 -0.06 PRO 216
SER 313 0.34 ARG 282 -0.17 ASP 370
SER 313 0.31 GLN 283 -0.20 ASP 370
SER 313 0.30 VAL 284 -0.17 ARG 374
SER 313 0.36 GLN 285 -0.12 ARG 374
SER 313 0.36 TRP 286 -0.12 ASP 370
SER 313 0.29 ASP 287 -0.14 ARG 374
SER 313 0.31 LYS 288 -0.08 LYS 304
SER 313 0.38 VAL 289 -0.05 ASP 370
SER 313 0.31 PHE 290 -0.06 ASP 370
SER 313 0.24 THR 291 -0.09 LYS 304
SER 313 0.29 SER 292 -0.08 LYS 304
SER 313 0.32 CYS 293 -0.04 LYS 249
ALA 308 0.21 PHE 294 -0.06 LYS 304
ALA 308 0.18 LEU 295 -0.11 LYS 304
ALA 308 0.25 THR 296 -0.06 LYS 249
ALA 308 0.19 VAL 297 -0.07 LYS 249
GLY 469 0.12 ASP 298 -0.08 ALA 319
GLY 469 0.12 GLY 299 -0.10 LEU 295
GLY 469 0.17 GLU 300 -0.08 LYS 249
GLY 469 0.18 ILE 301 -0.13 VAL 310
GLY 469 0.16 GLU 302 -0.18 VAL 310
GLY 469 0.18 GLY 303 -0.23 VAL 310
GLY 469 0.14 LYS 304 -0.14 LEU 317
GLY 469 0.14 ILE 305 -0.07 LYS 249
LYS 468 0.19 GLY 306 -0.10 LYS 249
PHE 260 0.34 ARG 307 -0.16 LYS 249
PHE 260 0.61 ALA 308 -0.24 LYS 249
PHE 260 0.57 VAL 309 -0.32 VAL 320
PHE 212 0.80 VAL 310 -0.42 SER 322
LEU 213 0.68 SER 312 -0.34 SER 322
LYS 214 0.65 SER 313 -0.22 SER 200
GLU 264 0.38 ASP 314 -0.16 GLU 201
GLU 264 0.37 LYS 315 -0.18 VAL 320
PHE 260 0.29 VAL 316 -0.21 SER 312
LYS 468 0.23 LEU 317 -0.20 VAL 310
GLY 469 0.26 GLU 318 -0.35 VAL 310
GLY 469 0.21 ALA 319 -0.33 VAL 310
GLY 469 0.23 VAL 320 -0.32 VAL 309
GLY 469 0.21 ALA 321 -0.38 VAL 310
GLY 469 0.19 SER 322 -0.42 VAL 310
GLY 469 0.16 GLU 323 -0.32 VAL 310
GLY 469 0.14 THR 324 -0.30 VAL 310
GLY 469 0.16 VAL 325 -0.26 VAL 310
VAL 393 0.14 GLY 326 -0.16 VAL 310
GLY 469 0.13 SER 327 -0.09 ASP 432
ALA 395 0.10 THR 328 -0.09 SER 327
VAL 310 0.12 ALA 329 -0.05 ALA 319
VAL 310 0.18 VAL 330 -0.04 ASP 370
VAL 310 0.29 VAL 331 -0.06 ASP 370
VAL 310 0.37 ALA 332 -0.11 ASP 370
VAL 310 0.47 LEU 333 -0.11 ASP 370
VAL 310 0.50 VAL 334 -0.14 ASP 370
VAL 310 0.55 CYS 335 -0.14 ASP 370
VAL 310 0.54 SER 336 -0.15 ASP 370
VAL 310 0.49 SER 337 -0.18 ASP 370
VAL 310 0.45 HIS 338 -0.18 ASP 370
VAL 310 0.41 ILE 339 -0.18 ASP 370
VAL 310 0.37 VAL 340 -0.16 ASP 370
VAL 310 0.30 VAL 341 -0.15 ASP 370
VAL 310 0.25 SER 342 -0.10 ASP 370
SER 313 0.16 ASN 343 -0.07 ASP 370
SER 313 0.12 CYS 344 -0.11 SER 361
ARG 268 0.08 GLY 345 -0.13 PRO 359
ASP 492 0.10 ASP 346 -0.14 PRO 359
ARG 268 0.07 SER 347 -0.12 ARG 348
VAL 310 0.12 ARG 348 -0.12 SER 347
VAL 310 0.20 ALA 349 -0.13 VAL 362
VAL 310 0.21 VAL 350 -0.21 VAL 362
VAL 310 0.27 LEU 351 -0.22 GLU 369
VAL 310 0.26 PHE 352 -0.23 GLU 369
VAL 310 0.28 ARG 353 -0.27 GLU 369
VAL 310 0.28 GLY 354 -0.27 GLU 369
VAL 310 0.23 LYS 355 -0.26 GLU 369
VAL 310 0.21 GLU 356 -0.29 GLU 369
VAL 310 0.19 ALA 357 -0.28 ARG 368
VAL 310 0.21 MET 358 -0.30 ARG 368
VAL 310 0.17 PRO 359 -0.34 VAL 362
VAL 310 0.21 LEU 360 -0.22 ASP 370
SER 313 0.15 SER 361 -0.25 VAL 362
SER 313 0.12 VAL 362 -0.34 PRO 359
LYS 491 0.12 ASP 363 -0.24 PRO 359
LYS 491 0.12 HIS 364 -0.23 PRO 359
SER 200 0.17 LYS 365 -0.25 PRO 359
SER 200 0.20 PRO 366 -0.24 PRO 359
SER 200 0.21 ASP 367 -0.28 GLU 356
LYS 491 0.18 ARG 368 -0.30 MET 358
LYS 491 0.16 GLU 369 -0.30 MET 358
SER 200 0.13 ASP 370 -0.28 MET 358
SER 200 0.15 GLU 371 -0.24 MET 358
SER 200 0.18 TYR 372 -0.24 MET 358
SER 200 0.15 ALA 373 -0.22 GLU 356
SER 200 0.13 ARG 374 -0.20 THR 416
SER 200 0.16 ILE 375 -0.18 MET 358
SER 200 0.17 GLU 376 -0.19 GLU 356
SER 200 0.14 ASN 377 -0.18 GLN 283
SER 200 0.13 ALA 378 -0.16 GLN 283
SER 200 0.15 GLY 379 -0.15 GLU 356
SER 200 0.17 GLY 380 -0.16 GLU 356
SER 200 0.21 LYS 381 -0.18 GLU 356
SER 200 0.24 VAL 382 -0.21 GLU 356
SER 200 0.27 ILE 383 -0.21 GLU 356
SER 200 0.31 GLN 384 -0.23 GLU 356
SER 200 0.37 TRP 385 -0.20 ASN 439
SER 200 0.43 GLN 386 -0.24 ASN 439
SER 200 0.36 GLY 387 -0.25 ASN 439
SER 200 0.29 ALA 388 -0.23 GLU 356
SER 200 0.29 ARG 389 -0.19 GLU 356
SER 200 0.23 VAL 390 -0.17 PRO 359
SER 200 0.25 PHE 391 -0.16 GLU 356
SER 200 0.31 GLY 392 -0.17 GLU 356
SER 200 0.32 VAL 393 -0.16 ASN 439
SER 200 0.26 LEU 394 -0.16 ASN 439
SER 200 0.27 ALA 395 -0.19 ASN 439
SER 200 0.18 MET 396 -0.19 PRO 359
SER 200 0.15 SER 397 -0.18 PRO 359
SER 200 0.11 ARG 398 -0.14 PRO 359
ARG 268 0.10 SER 399 -0.11 PRO 359
GLY 469 0.12 ILE 400 -0.10 ALA 319
GLY 469 0.14 GLY 401 -0.15 ALA 319
GLY 469 0.13 ASP 402 -0.18 VAL 310
GLY 469 0.13 ARG 403 -0.20 VAL 310
GLY 469 0.12 TYR 404 -0.24 VAL 310
SER 200 0.13 LEU 405 -0.17 VAL 310
SER 200 0.10 LYS 406 -0.13 VAL 310
ARG 268 0.10 PRO 407 -0.12 PRO 359
SER 200 0.13 TYR 408 -0.15 PRO 359
SER 200 0.12 VAL 409 -0.14 PRO 359
ARG 268 0.10 ILE 410 -0.12 ALA 319
ARG 268 0.12 PRO 411 -0.12 GLU 302
SER 313 0.14 GLU 412 -0.12 GLU 302
SER 313 0.17 PRO 413 -0.10 THR 416
SER 313 0.18 GLU 414 -0.15 GLU 371
SER 313 0.24 VAL 415 -0.16 ASP 370
VAL 310 0.26 THR 416 -0.25 ASP 370
VAL 310 0.32 PHE 417 -0.23 ASP 370
VAL 310 0.34 MET 418 -0.26 ASP 370
VAL 310 0.39 PRO 419 -0.23 ASP 370
VAL 310 0.40 ARG 420 -0.23 ASP 370
VAL 310 0.38 SER 421 -0.24 GLU 369
VAL 310 0.40 ARG 422 -0.23 GLU 369
VAL 310 0.34 GLU 423 -0.25 GLU 369
VAL 310 0.35 ASP 424 -0.23 GLU 369
VAL 310 0.34 GLU 425 -0.20 GLU 369
VAL 310 0.34 CYS 426 -0.17 GLU 369
VAL 310 0.32 LEU 427 -0.16 ASP 370
VAL 310 0.25 ILE 428 -0.11 ASP 370
VAL 310 0.22 LEU 429 -0.08 ASP 370
VAL 310 0.13 ALA 430 -0.05 GLY 246
SER 347 0.06 SER 431 -0.08 HIS 245
ASP 363 0.10 ASP 432 -0.16 HIS 245
GLY 387 0.10 GLY 433 -0.13 HIS 245
LEU 360 0.05 LEU 434 -0.10 GLY 246
LEU 360 0.07 TRP 435 -0.14 HIS 245
VAL 362 0.11 ASP 436 -0.17 GLY 246
LEU 360 0.07 VAL 437 -0.14 GLY 246
LEU 360 0.06 MET 438 -0.16 GLN 386
LEU 360 0.08 ASN 439 -0.25 GLY 387
VAL 310 0.12 ASN 440 -0.24 GLY 387
VAL 310 0.14 GLN 441 -0.24 GLY 387
VAL 310 0.13 GLU 442 -0.19 GLY 387
VAL 310 0.15 VAL 443 -0.14 GLY 387
VAL 310 0.21 CYS 444 -0.17 ARG 368
VAL 310 0.20 GLU 445 -0.16 ASP 367
VAL 310 0.18 ILE 446 -0.12 ASP 367
VAL 310 0.23 ALA 447 -0.12 GLU 369
VAL 310 0.27 ARG 448 -0.15 GLU 369
VAL 310 0.24 ARG 449 -0.13 GLU 369
VAL 310 0.25 ARG 450 -0.10 GLU 369
VAL 310 0.31 ILE 451 -0.11 GLU 369
VAL 310 0.31 LEU 452 -0.13 GLU 369
VAL 310 0.28 MET 453 -0.11 GLU 369
VAL 310 0.32 TRP 454 -0.09 GLU 369
VAL 310 0.37 HIS 455 -0.11 GLU 369
VAL 310 0.33 LYS 456 -0.11 GLU 369
VAL 310 0.33 LYS 457 -0.08 GLU 369
VAL 310 0.38 ASN 458 -0.08 GLU 369
VAL 310 0.42 GLY 459 -0.10 GLU 369
VAL 310 0.48 ALA 460 -0.10 GLN 504
VAL 310 0.52 PRO 461 -0.09 ALA 503
VAL 310 0.59 PRO 462 -0.12 ALA 503
VAL 310 0.65 LEU 463 -0.14 SER 336
VAL 310 0.69 ALA 464 -0.12 SER 336
VAL 310 0.67 GLU 465 -0.10 SER 336
VAL 310 0.63 ARG 466 -0.10 SER 336
VAL 310 0.67 GLY 467 -0.09 SER 336
VAL 310 0.73 LYS 468 -0.07 LEU 234
VAL 310 0.63 GLY 469 -0.07 PRO 472
VAL 310 0.50 ILE 470 -0.05 THR 235
VAL 310 0.47 ASP 471 -0.07 ASP 370
VAL 310 0.41 PRO 472 -0.07 GLY 469
VAL 310 0.37 ALA 473 -0.08 ASP 370
VAL 310 0.35 CYS 474 -0.08 ASP 370
VAL 310 0.32 GLN 475 -0.05 ASP 370
VAL 310 0.27 ALA 476 -0.05 ASP 370
VAL 310 0.25 ALA 477 -0.07 ASP 370
VAL 310 0.22 ALA 478 -0.04 GLY 191
VAL 310 0.17 ASP 479 -0.05 PRO 210
VAL 310 0.15 TYR 480 -0.03 PRO 210
VAL 310 0.12 LEU 481 -0.03 ASP 370
VAL 310 0.07 SER 482 -0.05 VAL 208
GLN 386 0.07 MET 483 -0.04 VAL 208
VAL 310 0.05 LEU 484 -0.05 GLY 246
GLY 387 0.04 ALA 485 -0.07 GLY 246
GLY 387 0.12 LEU 486 -0.06 VAL 309
GLY 387 0.08 GLN 487 -0.06 GLY 246
ARG 368 0.07 LYS 488 -0.09 GLY 246
GLY 387 0.14 GLY 489 -0.09 VAL 309
GLY 387 0.17 SER 490 -0.10 GLY 246
GLY 387 0.31 LYS 491 -0.15 VAL 310
GLY 387 0.28 ASP 492 -0.13 VAL 310
GLN 386 0.22 ASN 493 -0.11 VAL 309
GLY 387 0.14 ILE 494 -0.05 ASP 256
GLN 386 0.10 SER 495 -0.05 PHE 212
VAL 310 0.17 ILE 496 -0.04 VAL 208
VAL 310 0.27 ILE 497 -0.05 ASP 370
VAL 310 0.31 VAL 498 -0.09 ASP 370
VAL 310 0.39 ILE 499 -0.12 ASP 370
VAL 310 0.41 ASP 500 -0.14 ASP 370
VAL 310 0.43 LEU 501 -0.17 ASP 370
VAL 310 0.43 LYS 502 -0.18 GLU 369
VAL 310 0.49 ALA 503 -0.16 GLU 369
VAL 310 0.47 GLN 504 -0.15 GLU 369
VAL 310 0.42 ARG 505 -0.16 GLU 369
VAL 310 0.40 LYS 506 -0.17 GLU 369

If you find results from this site helpful for your research, please cite one of our papers:

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: december 26th, 2025.