CNRS Nantes University US2B US2B
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***  ABCDE  ***

CA distance fluctuations for 240415173241498793

---  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
VAL 533 0.19 LEU 306 -0.25 ARG 548
VAL 533 0.21 ALA 307 -0.22 ARG 548
CYS 530 0.15 LEU 308 -0.20 ARG 548
VAL 533 0.18 SER 309 -0.19 ARG 548
VAL 533 0.23 LEU 310 -0.17 ARG 548
VAL 533 0.23 THR 311 -0.15 ARG 548
VAL 533 0.25 ALA 312 -0.13 ARG 548
VAL 533 0.30 ASP 313 -0.12 ARG 548
VAL 533 0.31 GLN 314 -0.14 ARG 548
VAL 533 0.30 MET 315 -0.15 ARG 548
VAL 533 0.35 VAL 316 -0.13 ALA 551
VAL 533 0.40 SER 317 -0.14 ALA 551
VAL 533 0.39 ALA 318 -0.17 ALA 551
VAL 533 0.41 LEU 319 -0.17 ALA 551
VAL 533 0.47 LEU 320 -0.16 ALA 551
VAL 533 0.51 ASP 321 -0.18 ALA 551
VAL 533 0.53 ALA 322 -0.21 ALA 551
VAL 533 0.58 GLU 323 -0.18 ALA 551
VAL 533 0.70 PRO 324 -0.20 ALA 551
VAL 533 0.80 PRO 325 -0.20 ALA 551
VAL 533 0.82 ILE 326 -0.17 ALA 551
VAL 533 0.98 LEU 327 -0.16 ALA 551
VAL 533 1.02 TYR 328 -0.14 ALA 551
CYS 530 1.11 SER 329 -0.13 ALA 551
CYS 530 1.23 GLU 330 -0.12 ALA 551
CYS 530 1.14 TYR 331 -0.11 ALA 551
LYS 531 1.13 ASP 332 -0.11 ALA 551
ASN 532 1.00 PRO 333 -0.12 ALA 551
ASN 532 1.06 THR 334 -0.10 ALA 551
LYS 531 1.07 ARG 335 -0.09 ALA 551
LYS 531 0.94 PRO 336 -0.10 ALA 551
LYS 531 0.85 PHE 337 -0.10 ALA 551
LYS 531 0.78 SER 338 -0.09 ALA 551
LYS 531 0.92 GLU 339 -0.10 ALA 551
CYS 530 0.97 ALA 340 -0.10 ALA 551
CYS 530 0.97 SER 341 -0.09 ALA 551
CYS 530 0.90 MET 342 -0.10 ALA 551
CYS 530 0.92 MET 343 -0.09 ALA 551
CYS 530 1.27 GLY 344 -0.09 ALA 551
CYS 530 1.25 LEU 345 -0.11 ALA 551
CYS 530 1.08 LEU 346 -0.11 ALA 551
CYS 530 1.22 THR 347 -0.10 ALA 551
CYS 530 1.50 ASN 348 -0.11 ALA 551
CYS 530 1.19 LEU 349 -0.13 ALA 551
CYS 530 1.00 ALA 350 -0.12 ALA 551
CYS 530 1.09 ASP 351 -0.11 ALA 551
VAL 533 1.18 ARG 352 -0.14 ALA 551
VAL 533 0.92 GLU 353 -0.15 ALA 551
VAL 533 0.78 LEU 354 -0.14 ALA 551
VAL 533 0.86 VAL 355 -0.16 ALA 551
VAL 533 0.81 HIS 356 -0.20 ALA 551
VAL 533 0.64 MET 357 -0.18 ALA 551
VAL 533 0.56 ILE 358 -0.19 ALA 551
VAL 533 0.61 ASN 359 -0.25 ALA 551
VAL 533 0.55 TRP 360 -0.22 ALA 551
VAL 533 0.41 ALA 361 -0.20 ALA 551
VAL 533 0.40 LYS 362 -0.24 ALA 551
VAL 533 0.42 ARG 363 -0.25 ALA 551
VAL 533 0.34 VAL 364 -0.20 ARG 548
VAL 533 0.27 PRO 365 -0.22 ARG 548
VAL 533 0.19 GLY 366 -0.24 ARG 548
VAL 533 0.21 PHE 367 -0.23 ARG 548
VAL 533 0.23 VAL 368 -0.30 ARG 548
CYS 530 0.15 ASP 369 -0.29 ARG 548
CYS 530 0.10 LEU 370 -0.25 ARG 548
TYR 526 0.10 THR 371 -0.25 HIS 547
TYR 526 0.12 LEU 372 -0.23 HIS 547
TYR 526 0.13 HIS 373 -0.26 LYS 531
TYR 526 0.11 ASP 374 -0.28 LYS 531
CYS 530 0.14 GLN 375 -0.17 ARG 548
TYR 526 0.15 VAL 376 -0.17 PRO 535
TYR 526 0.14 HIS 377 -0.30 LYS 531
TYR 526 0.11 LEU 378 -0.23 LYS 531
CYS 530 0.23 LEU 379 -0.12 ALA 551
TYR 526 0.18 GLU 380 -0.18 LYS 531
TYR 526 0.12 CYS 381 -0.27 LYS 531
TYR 526 0.12 CYS 381 -0.28 LYS 531
CYS 530 0.22 ALA 382 -0.14 LYS 531
CYS 530 0.38 TRP 383 -0.12 ALA 551
CYS 530 0.41 LEU 384 -0.11 ALA 551
CYS 530 0.32 GLU 385 -0.12 ALA 551
CYS 530 0.42 ILE 386 -0.13 ALA 551
CYS 530 0.57 LEU 387 -0.13 ALA 551
CYS 530 0.49 MET 388 -0.12 ALA 551
CYS 530 0.43 ILE 389 -0.12 ALA 551
CYS 530 0.55 GLY 390 -0.14 ALA 551
CYS 530 0.59 LEU 391 -0.13 ALA 551
CYS 530 0.48 VAL 392 -0.12 ALA 551
CYS 530 0.49 TRP 393 -0.12 ALA 551
CYS 530 0.57 ARG 394 -0.13 ALA 551
CYS 530 0.54 SER 395 -0.11 ALA 551
CYS 530 0.46 MET 396 -0.11 ALA 551
CYS 530 0.48 GLU 397 -0.10 ALA 551
CYS 530 0.51 HIS 398 -0.10 ALA 551
CYS 530 0.43 PRO 399 -0.09 ALA 551
CYS 530 0.43 GLY 400 -0.09 ALA 551
CYS 530 0.52 LYS 401 -0.10 ALA 551
CYS 530 0.59 LEU 402 -0.11 ALA 551
CYS 530 0.68 LEU 403 -0.12 ALA 551
CYS 530 0.79 PHE 404 -0.12 ALA 551
CYS 530 0.85 ALA 405 -0.13 ALA 551
VAL 533 0.79 PRO 406 -0.13 ALA 551
CYS 530 0.85 ASN 407 -0.12 ALA 551
CYS 530 0.84 LEU 408 -0.12 ALA 551
CYS 530 0.71 LEU 409 -0.11 ALA 551
CYS 530 0.64 LEU 410 -0.10 ALA 551
CYS 530 0.52 ASP 411 -0.09 ALA 551
CYS 530 0.43 ARG 412 -0.09 ALA 551
CYS 530 0.42 ASN 413 -0.09 ALA 551
CYS 530 0.53 GLN 414 -0.09 ALA 551
CYS 530 0.50 GLY 415 -0.09 ALA 551
CYS 530 0.38 LYS 416 -0.10 SER 527
CYS 530 0.46 CYS 417 -0.09 ALA 551
CYS 530 0.55 VAL 418 -0.09 ALA 551
CYS 530 0.43 GLU 419 -0.09 ALA 551
CYS 530 0.31 GLY 420 -0.14 SER 527
CYS 530 0.37 MET 421 -0.12 SER 527
CYS 530 0.24 VAL 422 -0.19 SER 527
CYS 530 0.19 GLU 423 -0.19 SER 527
CYS 530 0.28 ILE 424 -0.13 SER 527
CYS 530 0.39 PHE 425 -0.09 ALA 551
CYS 530 0.31 ASP 426 -0.11 SER 527
CYS 530 0.26 MET 427 -0.11 SER 527
CYS 530 0.37 LEU 428 -0.10 ALA 551
CYS 530 0.38 LEU 429 -0.10 ALA 551
CYS 530 0.29 ALA 430 -0.09 ALA 551
CYS 530 0.31 THR 431 -0.10 ALA 551
CYS 530 0.39 SER 432 -0.10 ALA 551
CYS 530 0.34 SER 433 -0.13 SER 433
CYS 530 0.34 SER 433 -0.13 SER 433
CYS 530 0.28 ARG 434 -0.09 ALA 551
CYS 530 0.33 PHE 435 -0.10 ALA 551
CYS 530 0.35 ARG 436 -0.10 ALA 551
CYS 530 0.29 MET 437 -0.09 ALA 551
CYS 530 0.28 MET 438 -0.09 ALA 551
VAL 533 0.33 ASN 439 -0.09 ALA 551
VAL 533 0.34 LEU 440 -0.10 ALA 551
VAL 533 0.38 GLN 441 -0.10 ALA 551
VAL 533 0.43 GLY 442 -0.12 ALA 551
VAL 533 0.38 GLU 443 -0.12 ALA 551
VAL 533 0.32 GLU 444 -0.12 ALA 551
VAL 533 0.37 PHE 445 -0.12 ALA 551
VAL 533 0.39 VAL 446 -0.14 ALA 551
VAL 533 0.30 CYS 447 -0.13 ALA 551
CYS 530 0.28 LEU 448 -0.13 ALA 551
CYS 530 0.34 LYS 449 -0.14 ALA 551
CYS 530 0.29 SER 450 -0.15 ALA 551
CYS 530 0.21 ILE 451 -0.13 ALA 551
CYS 530 0.21 ILE 452 -0.13 LYS 531
CYS 530 0.23 LEU 453 -0.14 ALA 551
CYS 530 0.15 LEU 454 -0.19 LYS 531
CYS 530 0.08 ASN 455 -0.27 LYS 531
CYS 530 0.08 SER 456 -0.29 LYS 531
SER 527 0.07 GLY 457 -0.40 LYS 531
HIS 516 0.07 VAL 458 -0.41 LYS 531
HIS 516 0.08 TYR 459 -0.53 LYS 531
GLU 523 0.10 THR 460 -0.60 LYS 531
SER 527 0.10 PHE 461 -0.56 LYS 531
SER 527 0.11 LEU 462 -0.64 LYS 531
SER 527 0.10 SER 463 -0.67 ASN 532
SER 527 0.08 SER 464 -0.62 ASN 532
SER 527 0.08 THR 465 -0.57 ASN 532
SER 527 0.08 LEU 466 -0.48 ASN 532
SER 527 0.08 LYS 467 -0.41 ASN 532
SER 527 0.08 SER 468 -0.45 LYS 531
SER 527 0.07 LEU 469 -0.45 LYS 531
SER 527 0.07 GLU 470 -0.36 LYS 531
SER 527 0.07 GLU 471 -0.33 LYS 531
SER 527 0.06 LYS 472 -0.38 LYS 531
SER 512 0.05 ASP 473 -0.34 LYS 531
TYR 526 0.06 HIS 474 -0.26 LYS 531
CYS 530 0.07 ILE 475 -0.25 LYS 531
SER 512 0.06 HIS 476 -0.29 LYS 531
CYS 530 0.08 ARG 477 -0.23 LYS 531
CYS 530 0.13 VAL 478 -0.18 ARG 548
CYS 530 0.13 LEU 479 -0.19 LYS 531
CYS 530 0.11 ASP 480 -0.20 LYS 531
CYS 530 0.16 LYS 481 -0.15 ARG 548
CYS 530 0.19 ILE 482 -0.14 ARG 548
CYS 530 0.16 THR 483 -0.14 LYS 531
CYS 530 0.16 ASP 484 -0.13 ARG 548
VAL 533 0.22 THR 485 -0.13 ARG 548
VAL 533 0.22 LEU 486 -0.11 ARG 548
CYS 530 0.18 ILE 487 -0.11 ARG 548
VAL 533 0.22 HIS 488 -0.11 ARG 548
VAL 533 0.27 LEU 489 -0.09 ARG 548
VAL 533 0.24 MET 490 -0.08 ARG 548
VAL 533 0.21 ALA 491 -0.09 ARG 548
VAL 533 0.26 LYS 492 -0.08 ARG 548
VAL 533 0.28 ALA 493 -0.06 ALA 551
VAL 533 0.24 GLY 494 -0.07 ARG 548
VAL 533 0.21 LEU 495 -0.07 ARG 548
VAL 533 0.16 THR 496 -0.08 ARG 548
CYS 530 0.13 LEU 497 -0.12 LYS 531
CYS 530 0.11 GLN 498 -0.15 LYS 531
CYS 530 0.15 GLN 499 -0.10 LYS 531
CYS 530 0.16 GLN 500 -0.10 LYS 531
CYS 530 0.11 HIS 501 -0.17 LYS 531
CYS 530 0.12 GLN 502 -0.16 LYS 531
CYS 530 0.17 ARG 503 -0.10 LYS 531
CYS 530 0.15 LEU 504 -0.13 LYS 531
CYS 530 0.11 ALA 505 -0.20 LYS 531
CYS 530 0.15 GLN 506 -0.14 LYS 531
CYS 530 0.20 LEU 507 -0.10 ALA 551
CYS 530 0.14 LEU 508 -0.18 LYS 531
CYS 530 0.11 LEU 509 -0.22 LYS 531
CYS 530 0.18 ILE 510 -0.13 LYS 531
CYS 530 0.16 LEU 511 -0.17 LYS 531
CYS 530 0.08 SER 512 -0.27 LYS 531
CYS 530 0.14 HIS 513 -0.19 LYS 531
CYS 530 0.14 HIS 513 -0.19 LYS 531
CYS 530 0.22 ILE 514 -0.12 LYS 531
CYS 530 0.11 ARG 515 -0.24 LYS 531
TYR 459 0.08 HIS 516 -0.27 LYS 531
CYS 530 0.19 MET 517 -0.13 LYS 531
CYS 530 0.20 SER 518 -0.14 LYS 531
THR 460 0.09 ASN 519 -0.30 LYS 531
THR 460 0.09 LYS 520 -0.22 LYS 531
CYS 530 0.24 GLY 521 -0.09 ALA 551
CYS 530 0.10 MET 522 -0.18 LYS 531
CYS 530 0.10 MET 522 -0.18 LYS 531
THR 460 0.10 GLU 523 -0.28 LYS 531
PRO 535 0.11 HIS 524 -0.12 GLY 420
CYS 530 0.22 LEU 525 -0.05 ALA 551
THR 347 0.30 TYR 526 -0.25 GLU 523
PRO 535 0.29 SER 527 -0.19 VAL 422
GLY 344 0.32 MET 528 -0.08 GLU 523
THR 347 0.53 LYS 529 -0.24 TYR 526
ASN 348 1.50 CYS 530 -0.25 SER 463
ASP 332 1.13 LYS 531 -0.66 SER 463
ASP 332 1.12 ASN 532 -0.67 SER 463
GLU 330 1.20 VAL 533 -0.40 SER 463
ASP 351 0.52 VAL 534 -0.23 LEU 462
LYS 529 0.44 PRO 535 -0.34 TYR 537
TYR 526 0.28 LEU 536 -0.08 LEU 539
TYR 526 0.24 TYR 537 -0.34 PRO 535
LYS 529 0.23 ASP 538 -0.09 LEU 462
VAL 534 0.40 LEU 539 -0.08 LEU 536
VAL 533 0.31 LEU 540 -0.07 ALA 551
CYS 530 0.19 LEU 541 -0.07 ALA 551
VAL 534 0.35 GLU 542 -0.04 GLU 419
VAL 533 0.50 MET 543 -0.06 ALA 551
VAL 533 0.35 LEU 544 -0.13 ALA 551
VAL 533 0.26 ASP 545 -0.08 ALA 551
VAL 533 0.41 ALA 546 -0.09 ALA 551
VAL 533 0.46 HIS 547 -0.25 THR 371
VAL 533 0.45 ARG 548 -0.30 VAL 368
VAL 533 0.59 LEU 549 -0.22 ASP 369
VAL 533 0.60 HIS 550 -0.08 LYS 467
VAL 533 0.44 ALA 551 -0.25 ARG 363

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.