Should you encounter any unexpected behaviour,
please let us know.

* 3pfq_allatom *

CA distance fluctuations for 240415112310379429

--- 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 increase ref largest decrease
ALA 621 0.17 LEU 339 -0.10 GLU 544

GLU 627 0.16 THR 340 -0.10 GLU 544

ALA 621 0.21 ASP 341 -0.10 GLU 544

GLU 627 0.22 PHE 342 -0.11 GLU 544

GLU 627 0.23 ASN 343 -0.13 GLU 544

GLU 627 0.20 PHE 344 -0.14 GLU 544

GLU 627 0.26 LEU 345 -0.17 LYS 620

ASP 630 0.22 MET 346 -0.19 LYS 620

ASP 630 0.09 VAL 347 -0.19 LYS 620

ASP 630 0.09 LEU 348 -0.20 LYS 620

LYS 668 0.02 GLY 349 -0.19 GLU 544

PRO 637 0.06 LYS 350 -0.20 GLU 646

LEU 640 0.09 GLY 351 -0.22 ASN 628

LEU 640 0.08 SER 352 -0.27 ASN 628

PRO 642 0.06 PHE 353 -0.21 ASN 628

LEU 640 0.05 GLY 354 -0.15 GLU 544

GLY 351 0.07 LYS 355 -0.15 GLU 544

ALA 626 0.08 VAL 356 -0.16 GLU 544

ASP 630 0.15 MET 357 -0.16 GLU 544

ASP 630 0.28 LEU 358 -0.16 GLU 544

GLU 627 0.27 SER 359 -0.14 GLU 544

GLU 627 0.33 GLU 360 -0.13 GLU 544

GLU 627 0.30 ARG 361 -0.11 GLU 544

GLU 627 0.28 LYS 362 -0.11 GLU 544

GLU 627 0.32 GLY 363 -0.10 GLU 544

ALA 621 0.37 THR 364 -0.11 ARG 610

GLU 627 0.43 ASP 365 -0.13 GLU 477

ALA 621 0.43 GLU 366 -0.13 LYS 611

ALA 626 0.42 LEU 367 -0.13 GLU 544

ALA 626 0.34 TYR 368 -0.13 GLU 544

ALA 626 0.27 ALA 369 -0.14 GLU 544

ALA 626 0.20 VAL 370 -0.13 GLU 544

ALA 621 0.12 LYS 371 -0.13 GLU 544

ALA 621 0.09 ILE 372 -0.12 GLU 544

ALA 621 0.05 LEU 373 -0.13 GLU 544

PRO 642 0.08 LYS 374 -0.13 ASN 628

PRO 642 0.07 LYS 375 -0.13 ASN 628

PRO 642 0.08 ASP 376 -0.17 ASN 628

PRO 642 0.09 VAL 377 -0.19 ASN 628

PRO 642 0.07 VAL 378 -0.17 ASN 628

PRO 642 0.06 ILE 379 -0.16 ASN 628

PRO 642 0.07 GLN 380 -0.21 ASN 628

PRO 642 0.07 ASP 381 -0.21 ASN 628

PRO 642 0.05 ASP 382 -0.16 ASN 628

PRO 642 0.05 ASP 383 -0.15 ASN 628

ALA 621 0.05 VAL 384 -0.11 ASN 628

ALA 621 0.06 GLU 385 -0.09 ASN 628

ALA 621 0.06 CYS 386 -0.09 ASN 628

ALA 621 0.08 THR 387 -0.08 ASN 628

ALA 621 0.11 MET 388 -0.06 GLU 544

ALA 621 0.11 VAL 389 -0.06 GLU 544

ALA 621 0.12 GLU 390 -0.07 GLU 544

ALA 621 0.16 LYS 391 -0.07 GLU 544

ALA 621 0.16 ARG 392 -0.06 GLU 544

ALA 621 0.16 VAL 393 -0.06 GLU 544

ALA 621 0.20 LEU 394 -0.08 GLU 544

ALA 621 0.22 ALA 395 -0.07 GLU 544

ALA 621 0.20 LEU 396 -0.06 GLU 544

ALA 621 0.23 PRO 397 -0.06 LEU 667

ALA 621 0.24 GLY 398 -0.09 LEU 667

ALA 621 0.23 LYS 399 -0.11 PRO 669

ALA 621 0.23 PRO 400 -0.15 PRO 669

ALA 621 0.27 PRO 401 -0.22 PRO 669

ALA 621 0.21 PHE 402 -0.14 PRO 669

ALA 621 0.22 LEU 403 -0.10 PRO 669

ALA 621 0.25 THR 404 -0.11 GLU 544

ALA 621 0.30 GLN 405 -0.10 GLU 544

ALA 621 0.27 LEU 406 -0.09 GLU 544

ALA 621 0.31 HSD 407 -0.09 GLU 544

ALA 621 0.25 SER 408 -0.09 GLU 544

ALA 621 0.21 CYS 409 -0.09 GLU 544

ALA 621 0.18 PHE 410 -0.09 GLU 544

ALA 621 0.14 GLN 411 -0.09 GLU 544

ALA 621 0.12 THR 412 -0.09 GLU 544

ARG 649 0.13 MET 413 -0.10 GLU 544

ALA 621 0.06 ASP 414 -0.13 HSD 636

ALA 621 0.08 ARG 415 -0.11 GLU 544

ALA 621 0.11 LEU 416 -0.10 GLU 544

ALA 621 0.15 TYR 417 -0.10 GLU 544

ALA 621 0.18 PHE 418 -0.10 GLU 544

ALA 621 0.24 VAL 419 -0.11 GLU 544

ALA 621 0.27 MET 420 -0.11 GLU 544

ALA 621 0.35 GLU 421 -0.12 GLU 544

ALA 626 0.38 TYR 422 -0.14 GLU 544

SER 622 0.39 VAL 423 -0.16 GLU 544

SER 622 0.54 ASN 424 -0.19 GLU 544

SER 622 0.41 GLY 425 -0.21 GLU 544

SER 622 0.19 GLY 426 -0.24 GLU 544

MET 473 0.08 ASP 427 -0.23 GLU 544

LEU 667 0.04 LEU 428 -0.21 GLU 544

ILE 432 0.08 MET 429 -0.29 GLU 544

GLY 426 0.10 TYR 430 -0.34 GLU 544

LEU 667 0.07 HSD 431 -0.28 ALA 621

MET 429 0.08 ILE 432 -0.30 ARG 624

LYS 668 0.08 GLN 433 -0.42 ARG 624

LYS 668 0.09 GLN 434 -0.49 GLY 623

MET 429 0.06 VAL 435 -0.45 ALA 621

MET 429 0.08 GLY 436 -0.43 GLY 623

LEU 469 0.05 ARG 437 -0.31 ARG 624

MET 429 0.03 PHE 438 -0.24 ALA 621

LEU 469 0.02 LYS 439 -0.21 ALA 621

GLY 658 0.02 GLU 440 -0.14 ALA 621

VAL 435 0.03 PRO 441 -0.09 ALA 621

HSD 431 0.03 HSD 442 -0.11 GLU 544

GLY 658 0.02 ALA 443 -0.10 GLU 544

LYS 618 0.04 VAL 444 -0.08 PRO 669

GLY 623 0.07 PHE 445 -0.10 PRO 669

ALA 626 0.06 TYR 446 -0.11 GLU 544

LYS 618 0.03 ALA 447 -0.08 GLU 544

SER 622 0.07 ALA 448 -0.11 PRO 669

GLY 623 0.11 GLU 449 -0.13 PRO 669

SER 622 0.08 ILE 450 -0.10 PRO 669

SER 622 0.06 ALA 451 -0.10 PRO 669

ALA 621 0.11 ILE 452 -0.12 PRO 669

ALA 621 0.13 GLY 453 -0.10 PRO 669

ALA 621 0.08 LEU 454 -0.08 PRO 669

ALA 621 0.09 PHE 455 -0.09 PRO 669

ALA 621 0.13 PHE 456 -0.09 PRO 669

ALA 621 0.12 LEU 457 -0.07 PRO 669

ALA 621 0.09 GLN 458 -0.06 PRO 669

ALA 621 0.11 SER 459 -0.07 PRO 669

ALA 621 0.13 LYS 460 -0.06 PRO 669

ALA 621 0.10 GLY 461 -0.05 PRO 669

ALA 621 0.09 ILE 462 -0.05 ASN 628

ALA 621 0.06 ILE 463 -0.08 ASN 628

ALA 621 0.05 TYR 464 -0.09 ASN 628

GLN 538 0.03 ARG 465 -0.13 ASN 628

GLN 538 0.05 ASP 466 -0.16 ASN 628

GLN 538 0.05 LEU 467 -0.13 ARG 624

GLN 538 0.08 LYS 468 -0.19 ARG 624

GLY 537 0.08 LEU 469 -0.20 ARG 624

GLY 537 0.06 ASP 470 -0.22 GLU 544

GLY 537 0.05 ASN 471 -0.16 GLU 544

ALA 626 0.06 VAL 472 -0.15 GLU 544

SER 622 0.14 MET 473 -0.18 GLU 544

SER 622 0.24 LEU 474 -0.17 GLU 544

SER 622 0.38 ASP 475 -0.16 GLU 544

ALA 621 0.56 SER 476 -0.17 GLU 544

GLY 623 0.41 GLU 477 -0.15 GLU 544

GLY 623 0.31 GLY 478 -0.16 GLU 544

GLY 623 0.26 HSD 479 -0.13 GLU 544

SER 622 0.17 ILE 480 -0.13 GLU 544

SER 622 0.21 LYS 481 -0.13 GLU 544

SER 622 0.14 ILE 482 -0.12 GLU 544

SER 622 0.14 ALA 483 -0.12 GLU 544

ALA 621 0.09 ASP 484 -0.12 GLU 544

ALA 621 0.09 PHE 485 -0.09 GLU 544

ALA 621 0.06 GLY 486 -0.10 ASN 628

GLN 538 0.04 MET 487 -0.12 ASN 628

ALA 621 0.06 CYS 488 -0.09 ASN 628

ALA 621 0.06 LYS 489 -0.09 ASN 628

ALA 621 0.09 GLU 490 -0.06 ASN 628

SER 654 0.10 ASN 491 -0.05 ASN 628

SER 654 0.08 ILE 492 -0.07 ASN 628

SER 654 0.08 TRP 493 -0.06 ASN 628

SER 654 0.07 ASP 494 -0.06 ASN 628

SER 654 0.07 GLY 495 -0.08 ASN 628

SER 654 0.07 VAL 496 -0.08 ASN 628

SER 654 0.06 THR 497 -0.10 ASN 628

SER 654 0.05 THR 498 -0.12 ASN 628

ASP 547 0.04 LYS 499 -0.15 ARG 624

ASP 547 0.02 GLU 500 -0.17 ASN 628

PRO 561 0.02 PHE 501 -0.21 ARG 624

PRO 561 0.03 CYS 502 -0.21 ASN 628

GLN 538 0.04 GLY 503 -0.21 ARG 624

GLN 538 0.06 THR 504 -0.28 ARG 624

PRO 561 0.04 PRO 505 -0.35 ARG 624

PRO 561 0.05 ASP 506 -0.36 ARG 624

PRO 561 0.04 TYR 507 -0.27 ARG 624

PRO 561 0.04 ILE 508 -0.26 ARG 624

PHE 550 0.03 ALA 509 -0.24 ARG 624

GLU 548 0.06 PRO 510 -0.25 ARG 624

GLU 548 0.06 GLU 511 -0.22 ARG 624

ASP 547 0.05 ILE 512 -0.22 ARG 624

ASP 547 0.07 ILE 513 -0.27 ARG 624

ASP 547 0.09 ALA 514 -0.25 ARG 624

ASP 547 0.07 TYR 515 -0.22 ARG 624

ASP 547 0.06 GLN 516 -0.19 ARG 624

ASP 547 0.05 PRO 517 -0.15 ARG 624

GLY 519 0.05 TYR 518 -0.14 ARG 624

TYR 518 0.05 GLY 519 -0.11 ARG 624

SER 654 0.05 LYS 520 -0.09 ASN 628

GLU 606 0.04 SER 521 -0.13 ARG 624

GLU 609 0.03 VAL 522 -0.16 ARG 624

GLY 658 0.03 ASP 523 -0.13 ARG 624

TRP 525 0.04 TRP 524 -0.13 ARG 624

TRP 524 0.04 TRP 525 -0.18 ARG 624

PRO 561 0.03 ALA 526 -0.20 ARG 624

GLY 658 0.02 PHE 527 -0.15 ARG 624

ILE 508 0.03 GLY 528 -0.19 ARG 624

PRO 561 0.03 VAL 529 -0.25 ARG 624

GLN 538 0.05 LEU 530 -0.22 ARG 624

LYS 468 0.03 LEU 531 -0.18 ARG 624

LYS 468 0.03 TYR 532 -0.26 ARG 624

GLN 538 0.06 GLU 533 -0.30 ARG 624

LEU 469 0.04 MET 534 -0.23 ARG 624

LYS 468 0.04 LEU 535 -0.23 ARG 624

GLU 533 0.05 ALA 536 -0.32 ARG 624

LEU 469 0.08 GLY 537 -0.39 ARG 624

LYS 468 0.08 GLN 538 -0.43 ARG 624

PRO 561 0.06 ALA 539 -0.44 ARG 624

PRO 561 0.06 PRO 540 -0.37 ARG 624

ALA 559 0.06 PHE 541 -0.41 ARG 624

ALA 559 0.06 GLU 542 -0.49 ARG 624

HSD 556 0.08 GLY 543 -0.56 ARG 624

HSD 556 0.08 GLU 544 -0.63 ARG 624

ALA 514 0.06 ASP 545 -0.54 ARG 624

LEU 549 0.05 GLU 546 -0.46 ARG 624

ALA 514 0.09 ASP 547 -0.42 ARG 624

GLN 551 0.09 GLU 548 -0.47 ARG 624

GLU 546 0.05 LEU 549 -0.44 ARG 624

PRO 510 0.05 PHE 550 -0.37 ARG 624

GLU 548 0.09 GLN 551 -0.38 ARG 624

GLY 543 0.08 SER 552 -0.40 ARG 624

MET 576 0.05 ILE 553 -0.34 ARG 624

GLN 551 0.09 MET 554 -0.31 ARG 624

GLU 544 0.07 GLU 555 -0.34 ARG 624

GLU 544 0.08 HSD 556 -0.36 ARG 624

ALA 570 0.07 ASN 557 -0.31 ARG 624

GLY 543 0.05 VAL 558 -0.32 ARG 624

GLY 543 0.07 ALA 559 -0.33 ARG 624

PRO 540 0.04 TYR 560 -0.29 ARG 624

ALA 539 0.06 PRO 561 -0.30 ARG 624

PRO 540 0.04 LYS 562 -0.26 ARG 624

LYS 468 0.03 SER 563 -0.24 ARG 624

LYS 468 0.03 MET 564 -0.22 ARG 624

ASN 557 0.03 SER 565 -0.16 ARG 624

ASN 557 0.05 LYS 566 -0.14 ARG 624

ASN 557 0.05 GLU 567 -0.11 ARG 624

ASN 557 0.04 ALA 568 -0.15 ARG 624

ASN 557 0.05 VAL 569 -0.19 ARG 624

ASN 557 0.07 ALA 570 -0.15 ARG 624

GLU 555 0.05 ILE 571 -0.14 ARG 624

ASN 557 0.04 CYS 572 -0.19 ARG 624

GLU 555 0.07 LYS 573 -0.20 ARG 624

THR 577 0.06 GLY 574 -0.16 ARG 624

GLU 555 0.04 LEU 575 -0.17 ARG 624

ILE 553 0.05 MET 576 -0.22 ARG 624

GLY 574 0.06 THR 577 -0.21 ARG 624

GLN 551 0.07 LYS 578 -0.24 ARG 624

GLN 551 0.07 HSD 579 -0.20 ARG 624

GLN 551 0.05 PRO 580 -0.17 ARG 624

GLN 551 0.05 GLY 581 -0.15 ARG 624

ASP 593 0.06 LYS 582 -0.15 ARG 624

THR 577 0.06 ARG 583 -0.15 ARG 624

ILE 594 0.06 LEU 584 -0.12 ARG 624

GLU 606 0.06 GLY 585 -0.09 ARG 624

GLU 606 0.06 CYS 586 -0.10 ARG 624

GLU 606 0.06 GLY 587 -0.08 ARG 624

GLU 606 0.07 PRO 588 -0.05 ASN 628

GLU 606 0.07 GLU 589 -0.07 PRO 669

GLU 606 0.06 GLY 590 -0.07 PRO 669

GLU 606 0.07 GLU 591 -0.08 PRO 669

GLU 606 0.08 ARG 592 -0.08 PRO 669

LYS 582 0.06 ASP 593 -0.08 PRO 669

LEU 584 0.06 ILE 594 -0.08 PRO 669

ASP 604 0.06 LYS 595 -0.10 PRO 669

ASP 604 0.07 GLU 596 -0.09 PRO 669

THR 577 0.05 HSD 597 -0.08 PRO 669

GLU 555 0.05 ALA 598 -0.08 PRO 669

ASN 557 0.04 PHE 599 -0.08 PRO 669

LYS 618 0.06 PHE 600 -0.09 PRO 669

LYS 618 0.06 ARG 601 -0.10 PRO 669

LYS 618 0.08 TYR 602 -0.10 PRO 669

GLY 623 0.09 ILE 603 -0.12 PRO 669

GLY 623 0.12 ASP 604 -0.15 PRO 669

GLY 623 0.12 TRP 605 -0.15 PRO 669

GLY 623 0.15 GLU 606 -0.17 PRO 669

GLY 623 0.18 LYS 607 -0.19 PRO 669

GLY 623 0.18 LEU 608 -0.19 PRO 669

GLY 623 0.18 GLU 609 -0.21 PRO 669

GLY 623 0.23 ARG 610 -0.26 PRO 669

GLY 623 0.25 LYS 611 -0.25 PRO 669

GLY 623 0.26 GLU 612 -0.22 PRO 669

GLY 623 0.22 ILE 613 -0.18 PRO 669

GLY 623 0.26 GLN 614 -0.15 PRO 669

GLY 623 0.23 PRO 615 -0.12 GLU 544

GLY 623 0.16 PRO 616 -0.13 GLU 544

GLY 623 0.21 TYR 617 -0.17 GLU 544

GLY 623 0.34 LYS 618 -0.18 GLU 544

GLY 623 0.45 PRO 619 -0.24 GLU 544

GLY 623 0.61 LYS 620 -0.28 GLU 544

PRO 669 0.61 ALA 621 -0.46 GLN 434

ASN 424 0.54 SER 622 -0.45 GLN 434

LYS 620 0.61 GLY 623 -0.51 GLU 544

PRO 669 0.42 ARG 624 -0.63 GLU 544

PRO 669 0.35 ASN 625 -0.57 GLU 544

ASN 424 0.48 ALA 626 -0.45 GLU 544

ASP 365 0.43 GLU 627 -0.52 GLU 544

ASP 365 0.27 ASN 628 -0.55 GLU 544

LEU 367 0.27 PHE 629 -0.39 GLU 544

LEU 367 0.37 ASP 630 -0.36 GLU 544

ASP 365 0.25 ARG 631 -0.40 GLU 544

LEU 367 0.17 PHE 632 -0.36 GLU 544

LEU 367 0.15 PHE 633 -0.26 GLU 544

ASP 365 0.16 THR 634 -0.27 GLU 544

MET 346 0.12 ARG 635 -0.25 GLU 544

MET 346 0.06 HSD 636 -0.26 GLU 646

GLY 351 0.06 PRO 637 -0.17 LYS 620

GLU 627 0.10 PRO 638 -0.17 LYS 620

GLY 351 0.08 VAL 639 -0.14 LYS 620

GLY 351 0.09 LEU 640 -0.14 ASP 644

SER 352 0.07 GLU 641 -0.24 HSD 636

VAL 377 0.09 PRO 642 -0.20 HSD 636

ASP 376 0.06 PRO 643 -0.19 HSD 636

THR 340 0.04 ASP 644 -0.25 HSD 636

THR 340 0.09 GLN 645 -0.20 HSD 636

MET 413 0.06 GLU 646 -0.26 HSD 636

ILE 651 0.07 VAL 647 -0.22 HSD 636

THR 412 0.08 ILE 648 -0.17 HSD 636

GLN 653 0.13 ARG 649 -0.16 HSD 636

GLN 653 0.10 ASN 650 -0.17 HSD 636

VAL 647 0.07 ILE 651 -0.13 ASN 628

ASN 650 0.08 ASP 652 -0.11 ASN 628

ARG 649 0.13 GLN 653 -0.09 HSD 636

ARG 649 0.11 SER 654 -0.08 HSD 636

ASN 491 0.09 GLU 655 -0.08 ASN 628

ALA 621 0.10 PHE 656 -0.07 GLU 544

ALA 621 0.12 GLU 657 -0.07 GLU 544

ALA 621 0.15 GLY 658 -0.06 GLU 544

ALA 621 0.15 PHE 659 -0.07 GLU 544

ALA 621 0.18 GLU 660 -0.07 GLU 544

ALA 621 0.21 PHE 661 -0.07 GLU 544

ALA 621 0.26 VAL 662 -0.08 GLU 544

ALA 621 0.29 ASN 663 -0.08 GLU 544

ALA 621 0.30 SER 664 -0.07 GLU 544

ALA 621 0.33 GLU 665 -0.07 GLU 544

ALA 621 0.37 PHE 666 -0.08 GLU 544

ALA 621 0.44 LEU 667 -0.12 ARG 610

ALA 621 0.52 LYS 668 -0.18 ARG 610

ALA 621 0.61 PRO 669 -0.26 ARG 610

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

K. Suhre & Y.H. Sanejouand, ElNemo: a normal mode web-server for protein movement analysis and the generation of templates for molecular replacement. Nucleic Acids Research, 32, W610-W614, 2004.
K. Suhre & Y.H. Sanejouand, On the potential of normal mode analysis for solving difficult molecular replacement problems. Acta Cryst. D vol.60, p796-799, 2004 © International Union of Crystallography.

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.

Should you encounter any unexpected behaviour, please let us know.

*** 3pfq_allatom ***

CA distance fluctuations for 240415112310379429

--- normal mode 10 ---

Should you encounter any unexpected behaviour,
please let us know.

* 3pfq_allatom *