CNRS Nantes University US2B US2B
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***  FLT3_jst  ***

CA distance fluctuations for 2403190929353871101

---  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
PRO 851 0.23 TYR 572 -0.85 ASN 847
PRO 851 0.17 GLU 573 -1.19 ASN 847
ARG 595 0.19 SER 574 -1.02 ASN 847
ARG 595 0.15 GLN 575 -1.06 ALA 848
LYS 634 0.12 LEU 576 -0.92 ASN 847
ASP 593 0.11 GLN 577 -1.04 ASN 847
GLY 669 0.08 MET 578 -0.94 ASN 847
PHE 590 0.09 VAL 579 -0.92 ASN 847
SER 806 0.22 GLN 580 -0.88 GLY 846
SER 806 0.31 VAL 581 -0.85 GLY 846
PHE 804 0.31 THR 582 -0.88 GLY 846
PHE 804 0.35 GLY 583 -0.79 GLY 846
PHE 804 0.40 SER 584 -0.68 GLY 846
SER 935 0.28 SER 585 -0.72 GLY 846
ILE 867 0.19 ASP 586 -0.74 GLY 846
PHE 804 0.15 ASN 587 -0.90 GLY 846
PHE 804 0.24 GLU 588 -0.94 GLY 846
PHE 804 0.21 TYR 589 -1.00 GLY 846
SER 806 0.13 PHE 590 -1.13 GLY 846
VAL 579 0.08 TYR 591 -1.14 ASN 847
GLY 669 0.06 VAL 592 -1.01 ASN 847
GLN 575 0.12 ASP 593 -1.01 ASN 847
SER 574 0.15 PHE 594 -0.84 ASN 847
SER 574 0.19 ARG 595 -0.76 ASN 847
SER 574 0.14 GLU 596 -0.68 GLY 846
ASN 701 0.12 TYR 597 -0.66 ASN 847
ASN 701 0.13 GLU 598 -0.57 ASN 847
SER 705 0.15 TYR 599 -0.59 ASN 847
SER 705 0.13 ASP 600 -0.54 ASN 847
SER 705 0.15 LEU 601 -0.51 LYS 634
SER 705 0.14 LYS 602 -0.65 LYS 634
SER 705 0.16 TRP 603 -0.52 ASN 847
SER 705 0.20 GLU 604 -0.48 ASN 847
SER 705 0.22 PHE 605 -0.44 LYS 634
SER 705 0.24 PRO 606 -0.42 LYS 634
SER 705 0.27 ARG 607 -0.37 ASN 847
SER 705 0.28 GLU 608 -0.32 ASN 847
SER 705 0.28 ASN 609 -0.34 ASN 847
SER 705 0.31 LEU 610 -0.35 ASN 847
SER 705 0.34 GLU 611 -0.29 ASN 847
SER 705 0.39 PHE 612 -0.29 ASN 847
SER 705 0.46 GLY 613 -0.25 ASN 847
SER 705 0.55 LYS 614 -0.23 ASN 847
SER 705 0.52 VAL 615 -0.24 ASN 847
ASN 701 0.57 LEU 616 -0.28 ASN 847
ASN 701 0.54 GLY 617 -0.26 ASN 847
ASN 701 0.37 SER 618 -0.26 ASN 847
ARG 704 0.28 GLY 619 -0.24 ASN 847
VAL 886 0.24 ALA 620 -0.18 ASN 847
SER 705 0.22 PHE 621 -0.39 ASN 847
SER 705 0.28 GLY 622 -0.40 ASN 847
ASN 701 0.34 LYS 623 -0.38 ASN 847
ASN 701 0.38 VAL 624 -0.42 ASN 847
SER 705 0.41 MET 625 -0.35 ASN 847
SER 705 0.44 ASN 626 -0.33 ASN 847
SER 705 0.38 ALA 627 -0.33 ASN 847
SER 705 0.34 THR 628 -0.33 ASN 847
SER 705 0.29 ALA 629 -0.37 ASN 847
SER 705 0.27 TYR 630 -0.35 ASN 847
CYS 695 0.26 GLY 631 -0.38 ASN 847
CYS 695 0.27 ILE 632 -0.43 ASN 847
CYS 695 0.40 SER 633 -0.40 ASN 847
HIS 821 0.77 LYS 634 -0.65 LYS 602
HIS 821 0.44 THR 635 -0.35 ASN 847
CYS 695 0.28 GLY 636 -0.34 ASN 847
CYS 695 0.27 VAL 637 -0.34 ASN 847
CYS 695 0.29 SER 638 -0.34 ASN 847
LYS 634 0.42 ILE 639 -0.35 ASN 847
LYS 634 0.46 GLN 640 -0.35 ASN 847
LYS 634 0.38 VAL 641 -0.41 ASN 847
SER 705 0.33 ALA 642 -0.44 ASN 847
SER 705 0.32 VAL 643 -0.46 ASN 847
ASN 701 0.30 LYS 644 -0.53 ASN 847
SER 705 0.28 MET 645 -0.50 ASN 847
SER 705 0.26 LEU 646 -0.46 ASN 847
SER 705 0.26 LYS 647 -0.30 ASN 847
SER 705 0.29 GLU 648 -0.28 ASN 847
SER 705 0.20 ARG 655 -0.63 ASN 847
ASN 701 0.17 GLU 656 -0.73 ASN 847
ASN 701 0.17 ALA 657 -0.96 ASN 847
ASN 701 0.20 LEU 658 -0.81 ASN 847
ASN 701 0.18 MET 659 -0.74 ASN 847
ASN 701 0.15 SER 660 -0.90 ASN 847
ASN 701 0.16 GLU 661 -0.92 ASN 847
ASN 701 0.17 LEU 662 -0.76 ASN 847
ASN 701 0.15 LYS 663 -0.75 ASN 847
ASN 701 0.12 MET 664 -0.83 ASN 847
ASN 701 0.13 MET 665 -0.75 ASN 847
SER 705 0.12 THR 666 -0.67 ASN 847
ASP 698 0.11 GLN 667 -0.69 ASN 847
SER 584 0.13 LEU 668 -0.69 ASN 847
SER 584 0.17 GLY 669 -0.60 ASN 847
LYS 634 0.20 SER 670 -0.56 ASN 847
LYS 634 0.29 HIS 671 -0.53 ASN 847
LYS 634 0.46 GLU 672 -0.47 ASN 847
LYS 634 0.41 ASN 673 -0.48 ASN 847
LYS 634 0.36 ILE 674 -0.56 ASN 847
LYS 634 0.40 VAL 675 -0.55 ASN 847
LYS 634 0.34 ASN 676 -0.58 ASN 847
LYS 634 0.17 LEU 677 -0.60 ASN 847
SER 705 0.18 LEU 678 -0.53 ASN 847
SER 705 0.20 GLY 679 -0.53 ASN 847
SER 705 0.22 ALA 680 -0.54 ASN 847
SER 705 0.24 CYS 681 -0.48 ASN 847
SER 705 0.22 THR 682 -0.50 ASN 847
SER 705 0.21 LEU 683 -0.43 ASN 847
SER 705 0.23 SER 684 -0.36 ASN 847
SER 705 0.25 GLY 685 -0.36 ASN 847
SER 705 0.26 PRO 686 -0.40 ASN 847
SER 705 0.24 ILE 687 -0.51 ASN 847
SER 705 0.27 TYR 688 -0.51 ASN 847
SER 705 0.24 LEU 689 -0.59 ASN 847
SER 705 0.25 ILE 690 -0.52 ASN 847
LYS 634 0.29 PHE 691 -0.53 ASN 847
LYS 634 0.54 GLU 692 -0.48 ASN 847
LYS 634 0.58 TYR 693 -0.42 ASN 847
LYS 634 0.60 CYS 694 -0.38 ASN 847
LYS 634 0.68 CYS 695 -0.33 ASN 847
LYS 634 0.58 TYR 696 -0.30 ALA 848
LYS 634 0.51 GLY 697 -0.32 ALA 848
LYS 634 0.45 ASP 698 -0.33 ALA 848
LYS 634 0.43 LEU 699 -0.30 ALA 848
GLY 617 0.41 LEU 700 -0.23 ALA 848
LEU 616 0.57 ASN 701 -0.18 ALA 848
LYS 634 0.47 TYR 702 -0.20 ALA 848
LYS 634 0.42 LEU 703 -0.17 ALA 848
LEU 616 0.47 ARG 704 -0.10 ALA 848
LYS 614 0.55 SER 705 -0.10 PRO 893
LYS 634 0.45 LYS 706 -0.12 ALA 848
LYS 614 0.41 ARG 707 -0.08 PRO 890
LYS 614 0.47 GLU 708 -0.09 GLY 891
LYS 634 0.45 LYS 709 -0.09 ALA 848
LYS 634 0.41 PHE 710 -0.11 ALA 848
LYS 634 0.45 LEU 783 -0.17 ALA 848
LYS 634 0.40 THR 784 -0.17 ALA 848
LYS 634 0.35 PHE 785 -0.18 ALA 848
LYS 634 0.36 GLU 786 -0.21 ALA 848
LYS 634 0.41 ASP 787 -0.24 ALA 848
LYS 634 0.37 LEU 788 -0.23 ALA 848
LYS 634 0.33 LEU 789 -0.25 ALA 848
LYS 634 0.37 CYS 790 -0.29 ASN 847
LYS 634 0.39 PHE 791 -0.32 ALA 848
LYS 634 0.32 ALA 792 -0.32 ALA 848
LYS 634 0.30 TYR 793 -0.35 ASN 847
LYS 634 0.35 GLN 794 -0.40 ASN 847
LYS 634 0.31 VAL 795 -0.43 ASN 847
SER 584 0.28 ALA 796 -0.44 ASN 847
SER 584 0.30 LYS 797 -0.46 ASN 847
LYS 634 0.27 GLY 798 -0.53 ASN 847
SER 584 0.29 MET 799 -0.56 ASN 847
SER 584 0.36 GLU 800 -0.54 ASN 847
SER 584 0.31 PHE 801 -0.58 ASN 847
SER 584 0.30 LEU 802 -0.67 ASN 847
SER 584 0.38 GLU 803 -0.64 ASN 847
SER 584 0.40 PHE 804 -0.61 ASN 847
SER 584 0.25 LYS 805 -0.69 ASN 847
VAL 581 0.31 SER 806 -0.73 ASN 847
SER 584 0.20 CYS 807 -0.82 ASN 847
SER 584 0.19 VAL 808 -0.81 ASN 847
SER 584 0.16 HIS 809 -0.82 ALA 848
LYS 634 0.13 ARG 810 -0.98 ALA 848
LYS 634 0.16 ASP 811 -0.77 ALA 848
LYS 634 0.21 LEU 812 -0.60 ALA 848
LYS 634 0.26 ALA 813 -0.44 ALA 848
LYS 634 0.32 ALA 814 -0.35 ALA 848
LYS 634 0.31 ARG 815 -0.36 ALA 848
LYS 634 0.30 ASN 816 -0.50 ALA 848
LYS 634 0.37 VAL 817 -0.45 ALA 848
LYS 634 0.46 LEU 818 -0.40 ALA 848
LYS 634 0.56 VAL 819 -0.35 ALA 848
LYS 634 0.69 THR 820 -0.35 ASN 847
LYS 634 0.77 HIS 821 -0.32 ASN 847
LYS 634 0.67 GLY 822 -0.31 ASN 847
LYS 634 0.58 LYS 823 -0.30 ASN 847
LYS 634 0.57 VAL 824 -0.36 ASN 847
LYS 634 0.50 VAL 825 -0.39 ASN 847
LYS 634 0.45 LYS 826 -0.47 ASN 847
LYS 634 0.33 ILE 827 -0.54 ASN 847
LYS 634 0.28 CYS 828 -0.61 ASN 847
LYS 634 0.20 ASP 829 -0.67 ASN 847
LYS 634 0.24 PHE 830 -0.53 ASN 847
ASN 701 0.20 GLY 831 -0.55 ASN 847
ASN 701 0.26 LEU 832 -0.53 ASN 847
ASN 701 0.35 ALA 833 -0.39 ASN 847
ASN 701 0.31 ARG 834 -0.28 ASN 847
VAL 886 0.28 ASP 835 -0.18 ALA 848
VAL 886 0.24 ILE 836 -0.20 ALA 848
GLY 891 0.27 MET 837 -0.27 GLY 863
VAL 886 0.36 SER 838 -0.20 GLY 863
VAL 886 0.33 ASP 839 -0.16 GLY 863
VAL 844 0.39 SER 840 -0.19 GLY 863
VAL 843 0.33 ASN 841 -0.16 LEU 850
VAL 843 0.31 TYR 842 -0.21 GLY 863
VAL 894 0.40 VAL 843 -0.41 GLY 863
PRO 893 0.50 VAL 844 -0.70 GLY 863
ASP 895 0.77 ARG 845 -0.98 GLY 863
ASP 895 0.62 GLY 846 -1.13 PHE 590
ASP 895 0.52 ASN 847 -1.19 GLU 573
ASP 895 0.46 ALA 848 -1.06 GLN 575
ASP 895 0.26 ARG 849 -0.47 ARG 810
TYR 572 0.17 LEU 850 -0.34 ASP 811
TYR 572 0.23 PRO 851 -0.27 LEU 850
TYR 572 0.17 VAL 852 -0.12 GLY 863
VAL 843 0.26 LYS 853 -0.08 ALA 848
LYS 634 0.19 TRP 854 -0.30 ALA 848
LYS 634 0.15 MET 855 -0.33 ALA 848
LYS 634 0.14 ALA 856 -0.33 ALA 848
LYS 634 0.12 PRO 857 -0.27 GLY 846
LYS 634 0.10 GLU 858 -0.48 GLY 846
LYS 634 0.10 SER 859 -0.56 ARG 845
LYS 634 0.11 LEU 860 -0.36 ARG 845
LYS 634 0.09 PHE 861 -0.44 ARG 845
GLY 863 0.07 GLU 862 -0.73 ARG 845
GLU 862 0.07 GLY 863 -0.98 ARG 845
LYS 634 0.07 ILE 864 -0.84 GLY 846
LYS 634 0.09 TYR 865 -0.78 GLY 846
SER 584 0.16 THR 866 -0.71 GLY 846
SER 584 0.32 ILE 867 -0.64 ASN 847
SER 584 0.25 LYS 868 -0.52 GLY 846
SER 584 0.14 SER 869 -0.53 ALA 848
SER 584 0.19 ASP 870 -0.57 ALA 848
SER 584 0.21 VAL 871 -0.44 ALA 848
LYS 634 0.17 TRP 872 -0.37 ALA 848
LYS 634 0.19 SER 873 -0.43 ALA 848
LYS 634 0.22 TYR 874 -0.41 ALA 848
LYS 634 0.21 GLY 875 -0.30 ALA 848
LYS 634 0.23 ILE 876 -0.26 ALA 848
LYS 634 0.27 LEU 877 -0.31 ALA 848
LYS 634 0.27 LEU 878 -0.27 ALA 848
LYS 634 0.26 TRP 879 -0.19 ALA 848
LYS 634 0.30 GLU 880 -0.19 ALA 848
LYS 634 0.34 ILE 881 -0.21 ALA 848
LYS 634 0.31 PHE 882 -0.16 ALA 848
LYS 634 0.31 SER 883 -0.10 ALA 848
LYS 634 0.35 LEU 884 -0.13 ALA 848
GLY 617 0.38 GLY 885 -0.12 ALA 848
SER 838 0.36 VAL 886 -0.08 PRO 890
SER 840 0.35 ASN 887 -0.10 PRO 893
VAL 843 0.29 PRO 888 -0.07 GLY 863
VAL 843 0.33 TYR 889 -0.08 GLU 708
ARG 845 0.39 PRO 890 -0.09 SER 705
ARG 845 0.50 GLY 891 -0.10 SER 705
ARG 845 0.52 ILE 892 -0.09 SER 705
ARG 845 0.65 PRO 893 -0.11 ASN 701
ARG 845 0.66 VAL 894 -0.11 GLY 863
ARG 845 0.77 ASP 895 -0.10 SER 585
ARG 845 0.55 ALA 896 -0.11 SER 585
ARG 845 0.47 ASN 897 -0.09 SER 585
ARG 845 0.41 PHE 898 -0.08 SER 585
ARG 845 0.22 TYR 899 -0.11 SER 585
ASN 847 0.22 LYS 900 -0.10 SER 585
ARG 845 0.23 LEU 901 -0.08 SER 585
LYS 634 0.14 ILE 902 -0.07 SER 585
LYS 634 0.12 GLN 903 -0.11 SER 585
LYS 634 0.12 ASN 904 -0.09 SER 585
LYS 634 0.14 GLY 905 -0.07 VAL 581
LYS 634 0.15 PHE 906 -0.08 GLU 708
VAL 843 0.18 LYS 907 -0.07 GLU 708
VAL 843 0.22 MET 908 -0.08 GLU 708
SER 840 0.22 ASP 909 -0.08 GLU 708
LYS 634 0.23 GLN 910 -0.08 ALA 848
LYS 634 0.26 PRO 911 -0.08 ALA 848
LYS 634 0.28 PHE 912 -0.07 GLU 708
LYS 634 0.30 TYR 913 -0.12 ALA 848
LYS 634 0.27 ALA 914 -0.14 ALA 848
LYS 634 0.24 THR 915 -0.14 ALA 848
LYS 634 0.21 GLU 916 -0.13 ALA 848
LYS 634 0.19 GLU 917 -0.18 ALA 848
LYS 634 0.22 ILE 918 -0.20 ALA 848
LYS 634 0.21 TYR 919 -0.16 ALA 848
LYS 634 0.18 ILE 920 -0.18 ALA 848
LYS 634 0.18 ILE 921 -0.24 ALA 848
LYS 634 0.20 MET 922 -0.23 ALA 848
LYS 634 0.18 GLN 923 -0.18 ALA 848
LYS 634 0.15 SER 924 -0.23 ALA 848
LYS 634 0.16 CYS 925 -0.29 ALA 848
LYS 634 0.16 TRP 926 -0.22 ALA 848
LYS 634 0.13 ALA 927 -0.22 ALA 848
LYS 634 0.12 PHE 928 -0.22 GLY 846
LYS 634 0.10 ASP 929 -0.32 GLY 846
LYS 634 0.10 SER 930 -0.42 GLY 846
ASN 938 0.11 ARG 931 -0.43 GLY 846
LYS 634 0.10 LYS 932 -0.33 GLY 846
SER 584 0.16 ARG 933 -0.33 ASN 847
SER 584 0.24 PRO 934 -0.36 ASN 847
SER 584 0.38 SER 935 -0.43 ASN 847
SER 584 0.36 PHE 936 -0.46 ASN 847
SER 584 0.38 PRO 937 -0.44 ASN 847
SER 584 0.34 ASN 938 -0.38 ASN 847
SER 584 0.28 LEU 939 -0.36 ASN 847
SER 584 0.29 THR 940 -0.39 ASN 847
SER 584 0.28 SER 941 -0.35 ASN 847
SER 584 0.24 PHE 942 -0.29 ASN 847
SER 584 0.23 LEU 943 -0.30 ASN 847
SER 584 0.24 GLY 944 -0.32 ASN 847
SER 584 0.22 CYS 945 -0.28 ASN 847
LYS 634 0.23 GLN 946 -0.24 ASN 847
LYS 634 0.27 LEU 947 -0.25 ASN 847

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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.