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***  miprot  ***

CA distance fluctuations for 2404012111241946417

---  normal mode 10  ---

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 0.46 LEU 306 -0.05 CYS 530
ALA 551 0.33 ALA 307 -0.06 CYS 530
ALA 551 0.32 LEU 308 -0.06 SER 512
ALA 551 0.33 SER 309 -0.05 CYS 530
HIS 550 0.25 LEU 310 -0.07 CYS 530
HIS 550 0.20 THR 311 -0.07 CYS 530
HIS 550 0.15 ALA 312 -0.07 CYS 530
HIS 550 0.13 ASP 313 -0.10 CYS 530
HIS 550 0.17 GLN 314 -0.10 CYS 530
HIS 550 0.15 MET 315 -0.10 CYS 530
HIS 550 0.09 VAL 316 -0.12 CYS 530
HIS 550 0.10 SER 317 -0.14 VAL 533
HIS 550 0.14 ALA 318 -0.14 VAL 533
HIS 550 0.07 LEU 319 -0.14 VAL 533
ARG 394 0.09 LEU 320 -0.18 VAL 533
ARG 394 0.09 ASP 321 -0.20 VAL 533
ILE 326 0.08 ALA 322 -0.21 VAL 533
ILE 326 0.10 GLU 323 -0.23 VAL 533
TRP 360 0.10 PRO 324 -0.30 ALA 551
PRO 333 0.07 PRO 325 -0.34 ALA 551
GLU 323 0.10 ILE 326 -0.33 ASN 532
TYR 328 0.07 LEU 327 -0.42 ASN 532
LEU 327 0.07 TYR 328 -0.48 ASN 532
ASN 359 0.06 SER 329 -0.53 ASN 532
ASN 359 0.06 GLU 330 -0.64 ASN 532
ASN 359 0.06 TYR 331 -0.63 ASN 532
ASN 359 0.07 ASP 332 -0.62 ASN 532
PRO 325 0.07 PRO 333 -0.53 ASN 532
ASP 321 0.07 THR 334 -0.53 ASN 532
ASP 321 0.06 ARG 335 -0.56 ASN 532
ASP 321 0.06 PRO 336 -0.51 ASN 532
ASP 321 0.05 PHE 337 -0.49 ASN 532
ASP 321 0.04 SER 338 -0.47 ASN 532
TYR 331 0.04 GLU 339 -0.57 ASN 532
ASN 359 0.04 ALA 340 -0.57 ASN 532
ASN 359 0.02 SER 341 -0.55 CYS 530
GLY 344 0.05 MET 342 -0.46 CYS 530
THR 347 0.04 MET 343 -0.52 CYS 530
MET 342 0.05 GLY 344 -0.72 CYS 530
ASN 359 0.04 LEU 345 -0.59 CYS 530
VAL 355 0.03 LEU 346 -0.51 CYS 530
MET 343 0.04 THR 347 -0.66 CYS 530
VAL 355 0.04 ASN 348 -0.70 CYS 530
ASN 359 0.05 LEU 349 -0.53 CYS 530
LEU 346 0.03 ALA 350 -0.47 CYS 530
LEU 540 0.04 ASP 351 -0.57 VAL 533
VAL 355 0.07 ARG 352 -0.56 VAL 533
ILE 358 0.06 GLU 353 -0.41 VAL 533
ARG 352 0.04 LEU 354 -0.37 VAL 533
ARG 352 0.07 VAL 355 -0.43 ALA 551
ASN 359 0.08 HIS 356 -0.40 ALA 551
THR 371 0.05 MET 357 -0.27 ALA 551
HIS 356 0.06 ILE 358 -0.26 ALA 551
HIS 356 0.08 ASN 359 -0.30 ALA 551
PRO 324 0.10 TRP 360 -0.22 VAL 533
ILE 326 0.06 ALA 361 -0.15 CYS 530
HIS 550 0.09 LYS 362 -0.15 VAL 533
HIS 550 0.14 ARG 363 -0.15 VAL 533
HIS 550 0.12 VAL 364 -0.11 CYS 530
HIS 550 0.21 PRO 365 -0.09 CYS 530
ALA 551 0.25 GLY 366 -0.06 CYS 530
HIS 550 0.17 PHE 367 -0.06 CYS 530
HIS 550 0.28 VAL 368 -0.08 CYS 530
ALA 551 0.38 ASP 369 -0.05 ASN 519
ALA 551 0.29 LEU 370 -0.06 ASN 519
ALA 551 0.28 THR 371 -0.06 ASN 519
ARG 548 0.17 LEU 372 -0.07 TYR 526
ASN 532 0.23 HIS 373 -0.08 TYR 526
ASN 532 0.24 ASP 374 -0.09 ASN 519
ASN 532 0.13 GLN 375 -0.07 ASN 519
ASN 532 0.15 VAL 376 -0.09 TYR 526
ASN 532 0.26 HIS 377 -0.10 MET 522
ASN 532 0.18 LEU 378 -0.09 ASN 519
PRO 535 0.08 LEU 379 -0.09 ALA 551
ASN 532 0.16 GLU 380 -0.13 HIS 550
ASN 532 0.21 CYS 381 -0.10 ASN 519
ASN 532 0.09 ALA 382 -0.10 ALA 551
LYS 529 0.05 TRP 383 -0.17 ALA 551
LYS 529 0.07 LEU 384 -0.18 ALA 551
LYS 529 0.08 GLU 385 -0.13 ALA 551
ALA 505 0.04 ILE 386 -0.16 CYS 530
ALA 505 0.03 LEU 387 -0.23 CYS 530
GLU 523 0.04 MET 388 -0.18 CYS 530
GLU 523 0.04 ILE 389 -0.15 CYS 530
GLU 323 0.06 GLY 390 -0.22 CYS 530
GLU 323 0.06 LEU 391 -0.24 CYS 530
LEU 320 0.05 VAL 392 -0.18 CYS 530
LEU 320 0.06 TRP 393 -0.19 CYS 530
GLU 323 0.10 ARG 394 -0.23 CYS 530
LEU 320 0.07 SER 395 -0.22 CYS 530
LEU 320 0.08 MET 396 -0.18 CYS 530
LEU 320 0.08 GLU 397 -0.20 CYS 530
ASP 321 0.08 HIS 398 -0.20 CYS 530
ASP 321 0.06 PRO 399 -0.17 CYS 530
ASP 321 0.05 GLY 400 -0.17 CYS 530
ASP 321 0.06 LYS 401 -0.22 CYS 530
GLU 323 0.06 LEU 402 -0.24 CYS 530
GLU 323 0.07 LEU 403 -0.29 CYS 530
GLU 323 0.06 PHE 404 -0.34 CYS 530
GLU 323 0.07 ALA 405 -0.38 ASN 532
ASP 321 0.08 PRO 406 -0.37 ASN 532
ASP 321 0.07 ASN 407 -0.43 ASN 532
GLU 323 0.06 LEU 408 -0.39 ASN 532
ASP 321 0.07 LEU 409 -0.32 ASN 532
ASP 321 0.06 LEU 410 -0.28 ASN 532
ASP 321 0.05 ASP 411 -0.22 CYS 530
ASP 321 0.05 ARG 412 -0.18 CYS 530
ASP 321 0.04 ASN 413 -0.20 ASN 532
ASP 321 0.04 GLN 414 -0.26 ASN 532
ASP 321 0.04 GLY 415 -0.22 CYS 530
ASP 321 0.03 LYS 416 -0.18 CYS 530
ASP 321 0.03 CYS 417 -0.25 ASN 532
THR 347 0.03 VAL 418 -0.27 CYS 530
THR 347 0.03 GLU 419 -0.22 CYS 530
HIS 524 0.07 GLY 420 -0.19 ALA 551
HIS 524 0.06 MET 421 -0.18 ALA 551
SER 527 0.07 VAL 422 -0.16 ALA 551
SER 527 0.10 GLU 423 -0.14 ALA 551
SER 527 0.08 ILE 424 -0.15 ALA 551
GLU 523 0.05 PHE 425 -0.16 ALA 551
SER 527 0.06 ASP 426 -0.14 ALA 551
SER 527 0.07 MET 427 -0.13 ALA 551
GLU 523 0.06 LEU 428 -0.15 ALA 551
GLU 523 0.05 LEU 429 -0.14 ALA 551
GLU 523 0.07 ALA 430 -0.12 ALA 551
GLU 523 0.07 THR 431 -0.11 ALA 551
GLU 523 0.05 SER 432 -0.14 CYS 530
GLU 523 0.06 SER 433 -0.12 CYS 530
GLU 523 0.07 ARG 434 -0.09 ALA 551
GLU 523 0.06 PHE 435 -0.11 CYS 530
GLY 442 0.06 ARG 436 -0.13 CYS 530
GLU 523 0.06 MET 437 -0.09 CYS 530
GLU 523 0.06 MET 438 -0.08 CYS 530
ASP 313 0.05 ASN 439 -0.12 CYS 530
PHE 435 0.05 LEU 440 -0.12 CYS 530
ASP 313 0.07 GLN 441 -0.14 CYS 530
MET 396 0.07 GLY 442 -0.16 CYS 530
VAL 316 0.06 GLU 443 -0.13 CYS 530
ASP 313 0.03 GLU 444 -0.10 CYS 530
SER 317 0.04 PHE 445 -0.13 CYS 530
ARG 394 0.05 VAL 446 -0.14 CYS 530
HIS 550 0.04 CYS 447 -0.09 CYS 530
LYS 529 0.05 LEU 448 -0.08 CYS 530
LYS 529 0.04 LYS 449 -0.11 CYS 530
LYS 529 0.04 SER 450 -0.09 CYS 530
ASN 532 0.08 ILE 451 -0.06 SER 512
ASN 532 0.08 ILE 452 -0.05 ASN 455
PRO 535 0.07 LEU 453 -0.06 CYS 530
ASN 532 0.12 LEU 454 -0.07 SER 512
ASN 532 0.18 ASN 455 -0.12 SER 512
ASN 532 0.19 SER 456 -0.11 HIS 516
ASN 532 0.28 GLY 457 -0.13 ASN 519
ASN 532 0.29 VAL 458 -0.14 HIS 516
ASN 532 0.35 TYR 459 -0.17 HIS 516
ASN 532 0.42 THR 460 -0.18 ASN 519
ASN 532 0.39 PHE 461 -0.15 ASN 519
ASN 532 0.44 LEU 462 -0.15 GLU 523
ASN 532 0.42 SER 463 -0.15 ASN 519
ASN 532 0.38 SER 464 -0.15 ASN 519
ASN 532 0.35 THR 465 -0.12 ASN 519
ALA 551 0.31 LEU 466 -0.11 HIS 516
ALA 551 0.32 LYS 467 -0.10 HIS 516
ASN 532 0.30 SER 468 -0.11 ASN 519
ASN 532 0.28 LEU 469 -0.12 HIS 516
ALA 551 0.32 GLU 470 -0.10 HIS 516
ALA 551 0.27 GLU 471 -0.09 HIS 516
ASN 532 0.23 LYS 472 -0.11 SER 512
ALA 551 0.26 ASP 473 -0.11 SER 512
ALA 551 0.27 HIS 474 -0.08 SER 512
ALA 551 0.19 ILE 475 -0.09 SER 512
ALA 551 0.18 HIS 476 -0.12 SER 512
ALA 551 0.22 ARG 477 -0.09 SER 512
ALA 551 0.18 VAL 478 -0.07 SER 512
HIS 550 0.12 LEU 479 -0.09 SER 512
ALA 551 0.15 ASP 480 -0.08 SER 512
HIS 550 0.16 LYS 481 -0.06 SER 512
HIS 550 0.11 ILE 482 -0.04 CYS 530
HIS 550 0.10 THR 483 -0.05 LYS 481
HIS 550 0.12 ASP 484 -0.03 ALA 505
HIS 550 0.11 THR 485 -0.06 CYS 530
HIS 550 0.07 LEU 486 -0.05 CYS 530
HIS 550 0.08 ILE 487 -0.04 HIS 488
HIS 550 0.09 HIS 488 -0.06 CYS 530
HIS 550 0.06 LEU 489 -0.08 CYS 530
HIS 550 0.04 MET 490 -0.07 CYS 530
HIS 550 0.06 ALA 491 -0.06 PRO 325
HIS 550 0.05 LYS 492 -0.09 CYS 530
GLN 506 0.04 ALA 493 -0.10 PRO 325
ASP 480 0.04 GLY 494 -0.09 PRO 325
TYR 459 0.05 LEU 495 -0.07 PRO 325
TYR 459 0.07 THR 496 -0.06 GLU 397
TYR 459 0.09 LEU 497 -0.05 MET 437
LYS 531 0.10 GLN 498 -0.07 MET 437
TYR 526 0.07 GLN 499 -0.08 MET 437
LYS 531 0.07 GLN 500 -0.05 MET 437
LYS 531 0.11 HIS 501 -0.06 MET 437
LYS 531 0.11 GLN 502 -0.07 MET 437
TYR 526 0.08 ARG 503 -0.06 MET 437
LYS 531 0.09 LEU 504 -0.04 MET 437
LYS 531 0.13 ALA 505 -0.06 GLN 506
LYS 531 0.10 GLN 506 -0.06 ALA 505
TYR 526 0.08 LEU 507 -0.05 ASP 480
LYS 531 0.12 LEU 508 -0.08 ASP 480
LYS 531 0.15 LEU 509 -0.07 ASP 480
TYR 526 0.10 ILE 510 -0.07 SER 464
LYS 531 0.12 LEU 511 -0.08 HIS 476
LYS 531 0.18 SER 512 -0.13 TYR 459
LYS 531 0.13 HIS 513 -0.13 TYR 459
LYS 529 0.11 ILE 514 -0.10 TYR 459
LYS 531 0.17 ARG 515 -0.14 TYR 459
LYS 531 0.18 HIS 516 -0.17 TYR 459
TYR 526 0.12 MET 517 -0.14 THR 460
LYS 529 0.13 SER 518 -0.14 ALA 551
LYS 531 0.22 ASN 519 -0.18 THR 460
TYR 526 0.17 LYS 520 -0.17 THR 460
LYS 529 0.10 GLY 521 -0.17 ALA 551
LYS 529 0.20 MET 522 -0.18 HIS 550
TYR 526 0.26 GLU 523 -0.17 HIS 550
LYS 529 0.08 HIS 524 -0.19 HIS 550
LYS 529 0.12 LEU 525 -0.22 HIS 550
GLU 523 0.26 TYR 526 -0.26 HIS 550
GLU 523 0.17 SER 527 -0.24 HIS 550
GLU 523 0.12 MET 528 -0.25 GLY 344
MET 522 0.20 LYS 529 -0.30 GLY 344
THR 460 0.14 CYS 530 -0.72 GLY 344
THR 460 0.33 LYS 531 -0.60 GLY 344
LEU 462 0.44 ASN 532 -0.64 GLU 330
LEU 462 0.28 VAL 533 -0.63 ASN 348
THR 460 0.13 VAL 534 -0.42 HIS 550
VAL 533 0.19 PRO 535 -0.30 HIS 550
ASN 532 0.06 LEU 536 -0.25 HIS 550
ASN 532 0.20 TYR 537 -0.18 HIS 550
ASN 532 0.09 ASP 538 -0.25 HIS 550
ALA 505 0.03 LEU 539 -0.35 HIS 550
ARG 352 0.04 LEU 540 -0.23 HIS 550
ARG 352 0.04 LEU 541 -0.18 HIS 550
ASP 332 0.05 GLU 542 -0.30 HIS 550
ASP 332 0.06 MET 543 -0.34 HIS 550
THR 371 0.07 LEU 544 -0.16 VAL 533
THR 371 0.10 ASP 545 -0.12 VAL 533
THR 371 0.15 ALA 546 -0.31 VAL 533
THR 371 0.17 HIS 547 -0.30 VAL 533
ASP 369 0.28 ARG 548 -0.32 VAL 533
LEU 306 0.25 LEU 549 -0.39 VAL 533
LEU 306 0.40 HIS 550 -0.56 VAL 533
LEU 306 0.46 ALA 551 -0.47 VAL 533

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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).
Last modification: April 25th, 2023.