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.


***  miprot  ***

CA distance fluctuations for 2404012111241946417

---  normal mode 11  ---

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
ALA 551 0.40 LEU 306 -0.07 SER 512
ALA 551 0.30 ALA 307 -0.07 SER 512
ALA 551 0.28 LEU 308 -0.09 SER 512
ALA 551 0.28 SER 309 -0.08 SER 512
ALA 551 0.21 LEU 310 -0.06 SER 512
ALA 551 0.16 THR 311 -0.05 SER 512
HIS 550 0.12 ALA 312 -0.04 SER 512
GLU 397 0.11 ASP 313 -0.06 ALA 318
HIS 550 0.14 GLN 314 -0.05 ASP 545
HIS 550 0.13 MET 315 -0.04 LEU 372
GLU 397 0.11 VAL 316 -0.07 ALA 493
GLU 397 0.14 SER 317 -0.08 ALA 493
HIS 550 0.14 ALA 318 -0.07 ALA 493
CYS 530 0.12 LEU 319 -0.08 ALA 493
GLU 397 0.15 LEU 320 -0.12 ALA 493
VAL 533 0.15 ASP 321 -0.10 ALA 493
VAL 533 0.16 ALA 322 -0.09 ALA 493
VAL 533 0.19 GLU 323 -0.10 ALA 493
VAL 533 0.25 PRO 324 -0.10 ALA 493
ASN 532 0.30 PRO 325 -0.12 ALA 493
ASN 532 0.33 ILE 326 -0.11 ALA 493
ASN 532 0.41 LEU 327 -0.09 GLY 494
ASN 532 0.47 TYR 328 -0.10 GLY 494
ASN 532 0.54 SER 329 -0.09 ALA 551
ASN 532 0.68 GLU 330 -0.08 LEU 408
ASN 532 0.69 TYR 331 -0.10 LEU 408
ASN 532 0.73 ASP 332 -0.16 ASN 407
ASN 532 0.60 PRO 333 -0.25 LEU 409
ASN 532 0.63 THR 334 -0.25 HIS 398
ASN 532 0.68 ARG 335 -0.19 LEU 409
ASN 532 0.60 PRO 336 -0.15 ASP 411
ASN 532 0.55 PHE 337 -0.15 ASP 411
ASN 532 0.53 SER 338 -0.16 GLN 414
ASN 532 0.67 GLU 339 -0.09 LEU 409
ASN 532 0.63 ALA 340 -0.08 ALA 551
ASN 532 0.61 SER 341 -0.09 ALA 551
ASN 532 0.47 MET 342 -0.13 LEU 462
CYS 530 0.54 MET 343 -0.14 LEU 462
CYS 530 0.75 GLY 344 -0.11 ALA 551
CYS 530 0.60 LEU 345 -0.10 ALA 551
CYS 530 0.52 LEU 346 -0.12 LEU 462
CYS 530 0.67 THR 347 -0.12 ALA 551
CYS 530 0.68 ASN 348 -0.13 ALA 551
ASN 532 0.52 LEU 349 -0.11 ALA 551
CYS 530 0.46 ALA 350 -0.11 ALA 551
VAL 533 0.58 ASP 351 -0.14 ALA 551
VAL 533 0.53 ARG 352 -0.14 ALA 551
VAL 533 0.40 GLU 353 -0.11 ALA 551
VAL 533 0.35 LEU 354 -0.11 ALA 551
VAL 533 0.37 VAL 355 -0.16 ALA 551
VAL 533 0.31 HIS 356 -0.12 ALA 551
VAL 533 0.24 MET 357 -0.07 ALA 551
VAL 533 0.20 ILE 358 -0.06 ALA 551
VAL 533 0.20 ASN 359 -0.07 ALA 493
VAL 533 0.18 TRP 360 -0.07 ALA 493
VAL 533 0.12 ALA 361 -0.05 ALA 493
HIS 550 0.15 LYS 362 -0.05 ASP 545
HIS 550 0.17 ARG 363 -0.06 SER 317
HIS 550 0.14 VAL 364 -0.05 TYR 526
ALA 551 0.20 PRO 365 -0.06 TYR 526
ALA 551 0.26 GLY 366 -0.07 TYR 526
ALA 551 0.20 PHE 367 -0.08 TYR 526
ALA 551 0.30 VAL 368 -0.08 LEU 372
ALA 551 0.35 ASP 369 -0.10 ASN 532
ALA 551 0.29 LEU 370 -0.14 ASN 532
ALA 551 0.27 THR 371 -0.18 ASN 532
ALA 551 0.15 LEU 372 -0.16 ASN 532
ALA 551 0.10 HIS 373 -0.28 ASN 532
ALA 551 0.13 ASP 374 -0.28 ASN 532
ALA 551 0.11 GLN 375 -0.16 ASN 532
ASP 332 0.10 VAL 376 -0.17 ASN 532
HIS 501 0.07 HIS 377 -0.28 ASN 532
HIS 501 0.08 LEU 378 -0.18 ASN 532
ASP 332 0.07 LEU 379 -0.12 LYS 529
HIS 501 0.07 GLU 380 -0.17 LYS 529
HIS 501 0.09 CYS 381 -0.19 TYR 526
ALA 505 0.08 ALA 382 -0.12 LEU 462
CYS 530 0.15 TRP 383 -0.11 LEU 462
CYS 530 0.19 LEU 384 -0.15 THR 460
CYS 530 0.14 GLU 385 -0.13 THR 460
CYS 530 0.17 ILE 386 -0.08 THR 460
CYS 530 0.25 LEU 387 -0.09 THR 460
CYS 530 0.22 MET 388 -0.13 THR 460
CYS 530 0.18 ILE 389 -0.09 THR 460
CYS 530 0.22 GLY 390 -0.08 PRO 333
CYS 530 0.25 LEU 391 -0.10 THR 460
CYS 530 0.21 VAL 392 -0.12 THR 334
CYS 530 0.19 TRP 393 -0.13 PRO 333
CYS 530 0.23 ARG 394 -0.15 PRO 333
CYS 530 0.22 SER 395 -0.18 THR 334
CYS 530 0.19 MET 396 -0.20 THR 334
CYS 530 0.19 GLU 397 -0.24 THR 334
ASN 532 0.21 HIS 398 -0.25 THR 334
CYS 530 0.18 PRO 399 -0.23 THR 334
CYS 530 0.19 GLY 400 -0.21 THR 334
CYS 530 0.23 LYS 401 -0.22 THR 334
CYS 530 0.25 LEU 402 -0.18 THR 334
ASN 532 0.29 LEU 403 -0.19 PRO 333
CYS 530 0.34 PHE 404 -0.11 PRO 333
ASN 532 0.38 ALA 405 -0.12 PRO 333
ASN 532 0.37 PRO 406 -0.15 PRO 333
ASN 532 0.43 ASN 407 -0.22 PRO 333
ASN 532 0.40 LEU 408 -0.22 PRO 333
ASN 532 0.33 LEU 409 -0.25 PRO 333
ASN 532 0.30 LEU 410 -0.21 THR 334
ASN 532 0.24 ASP 411 -0.22 THR 334
CYS 530 0.19 ARG 412 -0.18 THR 334
ASN 532 0.21 ASN 413 -0.18 THR 334
ASN 532 0.27 GLN 414 -0.17 THR 334
CYS 530 0.23 GLY 415 -0.16 THR 460
ASN 532 0.19 LYS 416 -0.17 THR 460
ASN 532 0.27 CYS 417 -0.16 THR 460
CYS 530 0.28 VAL 418 -0.17 THR 460
CYS 530 0.23 GLU 419 -0.19 THR 460
CYS 530 0.18 GLY 420 -0.22 THR 460
CYS 530 0.20 MET 421 -0.20 THR 460
CYS 530 0.12 VAL 422 -0.21 THR 460
CYS 530 0.10 GLU 423 -0.21 THR 460
CYS 530 0.15 ILE 424 -0.21 THR 460
CYS 530 0.19 PHE 425 -0.17 THR 460
CYS 530 0.15 ASP 426 -0.16 THR 460
CYS 530 0.14 MET 427 -0.18 THR 460
CYS 530 0.18 LEU 428 -0.15 THR 460
CYS 530 0.18 LEU 429 -0.15 THR 334
CYS 530 0.14 ALA 430 -0.14 THR 334
CYS 530 0.15 THR 431 -0.12 THR 334
CYS 530 0.17 SER 432 -0.15 THR 334
CYS 530 0.15 SER 433 -0.17 THR 334
CYS 530 0.13 ARG 434 -0.15 THR 334
CYS 530 0.14 PHE 435 -0.15 THR 334
CYS 530 0.15 ARG 436 -0.18 THR 334
CYS 530 0.13 MET 437 -0.17 THR 334
CYS 530 0.12 MET 438 -0.16 THR 334
CYS 530 0.12 ASN 439 -0.18 THR 334
CYS 530 0.13 LEU 440 -0.15 THR 334
CYS 530 0.12 GLN 441 -0.14 THR 334
CYS 530 0.14 GLY 442 -0.12 ALA 493
CYS 530 0.12 GLU 443 -0.11 ALA 493
CYS 530 0.11 GLU 444 -0.09 THR 334
CYS 530 0.14 PHE 445 -0.09 THR 334
CYS 530 0.13 VAL 446 -0.07 ALA 493
CYS 530 0.10 CYS 447 -0.04 THR 334
CYS 530 0.10 LEU 448 -0.06 PRO 333
CYS 530 0.13 LYS 449 -0.04 SER 464
CYS 530 0.09 SER 450 -0.05 SER 512
HIS 550 0.08 ILE 451 -0.10 SER 512
HIS 501 0.08 ILE 452 -0.08 SER 464
HIS 501 0.07 LEU 453 -0.08 TYR 526
ALA 551 0.10 LEU 454 -0.11 HIS 516
HIS 501 0.11 ASN 455 -0.17 SER 512
HIS 501 0.10 SER 456 -0.17 ASN 519
HIS 501 0.11 GLY 457 -0.26 ASN 532
ALA 551 0.11 VAL 458 -0.28 ASN 532
LEU 497 0.12 TYR 459 -0.34 ASN 532
GLN 498 0.11 THR 460 -0.43 ASN 532
ALA 551 0.10 PHE 461 -0.43 ASN 532
ALA 551 0.10 LEU 462 -0.56 ASN 532
ALA 551 0.15 SER 463 -0.54 ASN 532
ALA 551 0.19 SER 464 -0.48 ASN 532
ALA 551 0.23 THR 465 -0.45 ASN 532
ALA 551 0.28 LEU 466 -0.38 ASN 532
ALA 551 0.30 LYS 467 -0.34 ASN 532
ALA 551 0.23 SER 468 -0.37 ASN 532
ALA 551 0.24 LEU 469 -0.33 ASN 532
ALA 551 0.30 GLU 470 -0.27 ASN 532
ALA 551 0.26 GLU 471 -0.24 ASN 532
ALA 551 0.20 LYS 472 -0.25 ASN 532
ALA 551 0.23 ASP 473 -0.22 ASN 532
ALA 551 0.25 HIS 474 -0.17 ASN 532
ALA 551 0.20 ILE 475 -0.16 ASN 532
ALA 551 0.18 HIS 476 -0.18 SER 512
ALA 551 0.21 ARG 477 -0.15 SER 512
ALA 551 0.19 VAL 478 -0.11 SER 512
ALA 551 0.14 LEU 479 -0.15 SER 512
ALA 551 0.15 ASP 480 -0.14 SER 512
ALA 551 0.16 LYS 481 -0.10 SER 512
ALA 551 0.12 ILE 482 -0.07 SER 512
ALA 551 0.11 THR 483 -0.07 SER 512
ALA 551 0.12 ASP 484 -0.06 SER 512
HIS 550 0.10 THR 485 -0.04 THR 334
CYS 530 0.08 LEU 486 -0.07 THR 334
ASP 480 0.08 ILE 487 -0.08 THR 334
HIS 550 0.08 HIS 488 -0.07 THR 334
CYS 530 0.08 LEU 489 -0.08 THR 334
CYS 530 0.08 MET 490 -0.11 THR 334
ASP 480 0.08 ALA 491 -0.11 THR 334
CYS 530 0.07 LYS 492 -0.11 THR 334
CYS 530 0.08 ALA 493 -0.14 THR 334
CYS 530 0.07 GLY 494 -0.16 THR 334
CYS 530 0.07 LEU 495 -0.15 THR 334
TYR 459 0.09 THR 496 -0.14 THR 334
TYR 459 0.12 LEU 497 -0.11 THR 334
TYR 459 0.12 GLN 498 -0.12 THR 334
TYR 459 0.08 GLN 499 -0.14 THR 334
TYR 459 0.09 GLN 500 -0.11 THR 334
TYR 459 0.12 HIS 501 -0.09 THR 334
LEU 509 0.09 GLN 502 -0.11 THR 334
CYS 530 0.09 ARG 503 -0.11 THR 334
CYS 530 0.08 LEU 504 -0.09 THR 334
LEU 508 0.09 ALA 505 -0.09 GLN 506
CYS 530 0.09 GLN 506 -0.10 THR 334
CYS 530 0.10 LEU 507 -0.09 THR 334
ALA 505 0.09 LEU 508 -0.11 ASP 480
GLN 502 0.09 LEU 509 -0.11 ASP 480
CYS 530 0.10 ILE 510 -0.11 SER 464
CYS 530 0.09 LEU 511 -0.13 HIS 476
GLN 502 0.08 SER 512 -0.21 TYR 459
CYS 530 0.09 HIS 513 -0.20 TYR 459
CYS 530 0.12 ILE 514 -0.17 TYR 459
ALA 505 0.08 ARG 515 -0.23 TYR 459
GLN 502 0.07 HIS 516 -0.28 TYR 459
CYS 530 0.12 MET 517 -0.23 THR 460
CYS 530 0.11 SER 518 -0.24 THR 460
GLN 502 0.07 ASN 519 -0.33 THR 460
GLY 344 0.07 LYS 520 -0.29 THR 460
CYS 530 0.15 GLY 521 -0.25 THR 460
ASN 348 0.07 MET 522 -0.28 THR 460
GLY 344 0.08 GLU 523 -0.30 THR 460
GLU 339 0.09 HIS 524 -0.25 THR 460
CYS 530 0.18 LEU 525 -0.26 LEU 462
GLY 344 0.18 TYR 526 -0.33 LEU 462
GLY 344 0.18 SER 527 -0.30 LEU 462
SER 341 0.25 MET 528 -0.28 LEU 462
GLY 344 0.32 LYS 529 -0.34 LEU 462
GLY 344 0.75 CYS 530 -0.34 LEU 462
GLY 344 0.63 LYS 531 -0.50 LEU 462
ASP 332 0.73 ASN 532 -0.56 LEU 462
ASN 348 0.66 VAL 533 -0.40 LEU 462
ASP 332 0.27 VAL 534 -0.23 LEU 462
ASP 332 0.20 PRO 535 -0.28 LEU 462
ASP 332 0.13 LEU 536 -0.16 LEU 462
ASP 332 0.12 TYR 537 -0.23 ASN 532
ASP 332 0.16 ASP 538 -0.14 ASN 532
ASP 332 0.17 LEU 539 -0.13 HIS 550
ASP 332 0.14 LEU 540 -0.10 HIS 550
ASP 332 0.14 LEU 541 -0.09 ALA 546
ASP 332 0.17 GLU 542 -0.15 HIS 550
VAL 533 0.18 MET 543 -0.14 HIS 550
ASP 332 0.14 LEU 544 -0.06 LYS 529
ASP 332 0.15 ASP 545 -0.06 SER 317
THR 371 0.16 ALA 546 -0.11 GLU 542
ASP 332 0.15 HIS 547 -0.10 ASP 538
LYS 467 0.24 ARG 548 -0.10 MET 543
LYS 467 0.20 LEU 549 -0.10 GLU 542
LEU 306 0.31 HIS 550 -0.15 GLU 542
LEU 306 0.40 ALA 551 -0.16 VAL 355

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).
Last modification: April 25th, 2023.