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***  2cm5  ***

CA distance fluctuations for 21083121482279288

---  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
GLU 530 0.34 ALA 525 -1.20 GLY 635
ASN 573 0.54 LEU 526 -0.77 LYS 636
ASN 573 0.60 TYR 527 -1.00 LYS 636
LYS 601 0.56 GLU 528 -0.51 ILE 538
PRO 586 0.26 GLU 529 -0.42 ILE 538
ALA 525 0.34 GLU 530 -0.73 ILE 538
LYS 651 0.62 ILE 538 -0.73 GLU 530
LYS 651 0.73 GLU 539 -0.57 GLU 530
LYS 651 0.62 GLU 540 -0.47 GLU 530
LYS 651 0.56 ARG 541 -0.46 GLU 530
LYS 651 0.48 GLY 542 -0.37 GLU 530
LYS 651 0.41 LYS 543 -0.32 GLU 530
LYS 651 0.27 ILE 544 -0.27 GLU 530
LYS 651 0.16 LEU 545 -0.25 GLU 530
GLU 610 0.07 VAL 546 -0.21 GLU 530
GLU 670 0.13 SER 547 -0.24 GLN 553
LYS 668 0.11 LEU 548 -0.24 SER 547
ASN 677 0.14 TYR 550 -0.35 ASN 608
ASP 666 0.12 SER 551 -0.47 ASN 608
HIS 617 0.13 THR 552 -0.43 ASN 608
LYS 616 0.16 GLN 553 -0.56 ASN 608
ASP 587 0.12 GLN 554 -0.50 ASN 608
ASP 587 0.18 GLY 555 -0.36 ASN 608
ASN 677 0.17 GLY 556 -0.31 ASN 608
ASN 677 0.15 LEU 557 -0.29 ASN 608
LYS 668 0.15 ILE 558 -0.35 ASN 608
LYS 668 0.12 VAL 559 -0.19 ALA 525
GLU 610 0.11 GLY 560 -0.32 GLN 553
LYS 651 0.07 ILE 561 -0.31 GLN 553
LYS 651 0.10 ILE 562 -0.42 GLN 553
LYS 651 0.18 ARG 563 -0.37 GLN 553
LYS 651 0.28 CYS 564 -0.29 GLN 553
LYS 651 0.32 VAL 565 -0.29 GLN 553
LYS 651 0.39 HIS 566 -0.33 GLU 530
LYS 651 0.42 LEU 567 -0.39 GLU 530
LYS 651 0.44 ALA 568 -0.54 GLU 530
LYS 651 0.39 ALA 569 -0.41 GLU 530
LYS 651 0.30 ASP 571 -0.30 ILE 538
TYR 527 0.53 ALA 572 -0.32 ILE 538
TYR 527 0.60 ASN 573 -0.31 ILE 634
TYR 527 0.38 GLY 574 -0.21 GLN 553
LYS 651 0.34 TYR 575 -0.23 GLN 553
LYS 651 0.31 SER 576 -0.22 GLN 553
GLU 528 0.40 ASP 577 -0.25 GLN 553
LYS 651 0.25 PRO 578 -0.25 ALA 525
GLU 528 0.19 PHE 579 -0.26 ALA 525
TRP 583 0.17 VAL 580 -0.25 TYR 527
TRP 583 0.22 LYS 581 -0.27 TYR 527
ILE 634 0.17 LEU 582 -0.22 TYR 527
ILE 634 0.26 TRP 583 -0.17 TYR 527
ASN 677 0.30 LEU 584 -0.13 TYR 527
ASN 677 0.42 LYS 585 -0.17 SER 649
ASN 677 0.44 PRO 586 -0.21 SER 649
SER 637 0.33 ASP 587 -0.15 SER 649
ILE 634 0.21 LYS 591 -0.16 TYR 527
ILE 634 0.24 ALA 592 -0.15 TYR 527
ILE 634 0.24 LYS 593 -0.19 TYR 527
ILE 634 0.15 HIS 594 -0.22 TYR 527
GLU 528 0.13 LYS 595 -0.25 ALA 525
GLU 528 0.16 THR 596 -0.26 GLN 553
GLU 528 0.24 GLN 597 -0.32 GLN 553
GLU 528 0.32 ILE 598 -0.29 GLN 553
GLU 528 0.36 LYS 599 -0.35 GLN 553
GLU 528 0.55 LYS 600 -0.34 GLN 553
GLU 528 0.56 LYS 601 -0.31 GLN 553
GLU 528 0.35 THR 602 -0.33 GLN 553
LYS 651 0.34 LEU 603 -0.28 GLN 553
LYS 651 0.28 ASN 604 -0.34 GLN 553
LYS 651 0.23 PRO 605 -0.37 GLN 553
GLU 528 0.19 GLU 606 -0.46 GLN 553
GLU 528 0.17 PHE 607 -0.45 GLN 553
GLU 528 0.14 ASN 608 -0.56 GLN 553
GLU 528 0.11 GLU 609 -0.47 GLN 553
GLY 560 0.11 GLU 610 -0.41 GLN 554
LYS 668 0.09 PHE 611 -0.37 PHE 612
LYS 667 0.14 PHE 612 -0.37 PHE 611
ASN 677 0.15 TYR 613 -0.21 GLU 609
ALA 592 0.23 ASP 614 -0.23 ASN 608
ASN 677 0.26 ILE 615 -0.21 ASN 608
ASN 677 0.26 LYS 616 -0.23 ASN 608
ASN 677 0.26 HIS 617 -0.24 ASN 608
ASN 677 0.31 SER 618 -0.19 ASN 608
ASN 677 0.35 ASP 619 -0.17 ASN 608
ASN 677 0.35 LEU 620 -0.16 ASN 608
ASN 677 0.41 ALA 621 -0.13 ILE 558
ASN 677 0.47 LYS 622 -0.13 ILE 558
ASN 677 0.46 LYS 623 -0.15 VAL 559
ASN 677 0.48 SER 624 -0.15 GLY 647
ASN 677 0.32 LEU 625 -0.15 TYR 527
ASN 677 0.34 ASP 626 -0.17 TYR 527
SER 624 0.18 ILE 627 -0.23 TYR 527
ASP 626 0.33 SER 628 -0.30 TYR 527
SER 649 0.29 VAL 629 -0.29 TYR 527
PRO 586 0.31 TRP 630 -0.36 TYR 527
PRO 586 0.30 ASP 631 -0.30 TYR 527
PRO 586 0.31 TYR 632 -0.42 ALA 525
PRO 586 0.32 ASP 633 -0.58 ALA 525
PRO 586 0.33 ILE 634 -0.86 ALA 525
PRO 586 0.31 GLY 635 -1.20 ALA 525
PRO 586 0.34 LYS 636 -1.00 TYR 527
PRO 586 0.39 SER 637 -0.95 TYR 527
PRO 586 0.38 ASN 638 -0.67 TYR 527
PRO 586 0.34 ASP 639 -0.59 TYR 527
SER 649 0.40 TYR 640 -0.54 TYR 527
SER 649 0.41 ILE 641 -0.42 GLU 530
SER 649 0.48 GLY 642 -0.35 TYR 527
SER 649 0.44 GLY 643 -0.29 TYR 527
GLN 645 0.49 CYS 644 -0.22 TYR 527
CYS 644 0.49 GLN 645 -0.15 TYR 527
ASN 677 0.34 LEU 646 -0.14 TYR 527
ASN 677 0.45 GLY 647 -0.15 SER 624
ASN 677 0.55 ILE 648 -0.16 PRO 586
ASN 677 0.74 SER 649 -0.21 PRO 586
GLN 676 0.67 ALA 650 -0.16 PRO 586
GLN 676 0.76 LYS 651 -0.25 LEU 655
GLU 539 0.48 GLY 652 -0.11 PRO 586
GLU 539 0.27 GLU 653 -0.13 ARG 654
GLU 539 0.30 ARG 654 -0.13 GLU 653
GLN 676 0.40 LEU 655 -0.25 LYS 651
GLU 539 0.27 LYS 656 -0.21 LYS 651
GLU 539 0.18 HIS 657 -0.13 TYR 527
ASN 677 0.28 TRP 658 -0.13 LYS 651
ASN 677 0.28 TYR 659 -0.14 LYS 651
ASN 677 0.19 GLU 660 -0.13 GLU 670
ASN 677 0.18 CYS 661 -0.18 ASN 608
ASN 677 0.25 LEU 662 -0.19 ASN 608
ASN 677 0.21 LYS 663 -0.17 ASN 608
ASN 677 0.15 ASN 664 -0.21 ASN 608
ASN 677 0.14 LYS 665 -0.30 ASN 608
TYR 613 0.12 ASP 666 -0.39 ASN 608
PHE 612 0.14 LYS 667 -0.30 ASN 608
ILE 558 0.15 LYS 668 -0.30 ILE 562
PHE 612 0.08 ILE 669 -0.31 GLU 670
SER 547 0.13 GLU 670 -0.31 ILE 669
GLU 610 0.07 ARG 671 -0.23 GLU 530
LYS 651 0.20 TRP 672 -0.25 GLU 530
LYS 651 0.33 HIS 673 -0.24 GLU 530
LYS 651 0.58 GLN 674 -0.28 GLU 530
LYS 651 0.60 LEU 675 -0.31 GLU 530
LYS 651 0.76 GLN 676 -0.32 GLU 530
SER 649 0.74 ASN 677 -0.45 TYR 527

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: October 18th, 2018.