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

* STRUCTURAL PROTEIN 28-FEB-12 4DXT *

CA distance fluctuations for 2403150145323283196

--- 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
GLN 680 0.70 GLY 520 -0.16 THR 524

HIS 678 0.49 PRO 521 -0.13 THR 524

PRO 580 0.48 GLY 522 -0.02 THR 524

LEU 581 0.42 VAL 523 -0.04 THR 524

LEU 581 0.34 THR 524 -0.16 GLY 520

LEU 581 0.33 GLU 525 -0.21 ALA 632

LEU 581 0.29 GLU 526 -0.19 ALA 632

LEU 581 0.34 GLN 527 -0.09 ALA 632

LEU 581 0.39 VAL 528 -0.14 ALA 632

LEU 581 0.34 HIS 529 -0.26 ALA 632

TRP 582 0.34 HIS 530 -0.17 ALA 632

TRP 582 0.34 HIS 530 -0.17 ALA 632

TRP 582 0.40 ILE 531 -0.09 ALA 632

TRP 582 0.42 VAL 532 -0.23 ALA 632

TRP 582 0.38 LYS 533 -0.23 ALA 632

TRP 582 0.38 GLN 534 -0.14 ALA 632

TRP 582 0.43 ALA 535 -0.16 GLU 672

TRP 582 0.46 LEU 536 -0.21 GLU 672

TRP 582 0.42 GLN 537 -0.15 ALA 632

TRP 582 0.40 ARG 538 -0.12 GLU 672

TRP 582 0.46 TYR 539 -0.16 GLU 672

TRP 582 0.47 SER 540 -0.12 ALA 632

TRP 582 0.40 GLU 541 -0.08 ALA 632

TRP 582 0.41 ASP 542 -0.06 ALA 632

GLY 520 0.45 ARG 543 -0.10 GLU 672

GLY 520 0.54 ILE 544 -0.05 GLU 672

GLY 520 0.48 GLY 545 -0.04 ALA 632

GLY 520 0.51 LEU 546 -0.03 ALA 632

GLY 520 0.45 ALA 547 -0.03 ALA 632

GLY 520 0.44 ASP 548 -0.02 ALA 632

GLY 520 0.43 TYR 549 -0.07 HIS 584

GLY 520 0.42 ALA 550 -0.08 HIS 584

GLY 520 0.38 LEU 551 -0.05 HIS 584

GLY 520 0.34 GLU 552 -0.09 HIS 584

GLY 520 0.30 SER 553 -0.04 HIS 584

GLY 520 0.32 GLY 554 -0.06 HIS 584

GLY 520 0.32 GLY 555 -0.12 HIS 584

GLY 520 0.35 ALA 556 -0.14 HIS 584

GLY 520 0.35 SER 557 -0.21 HIS 584

GLY 520 0.36 VAL 558 -0.25 HIS 584

GLY 520 0.36 ILE 559 -0.32 LEU 581

GLY 520 0.34 SER 560 -0.40 LEU 581

GLY 520 0.34 THR 561 -0.47 LEU 581

GLY 520 0.37 ARG 562 -0.35 LEU 581

GLY 520 0.38 CYS 563 -0.30 ILE 579

GLY 520 0.38 SER 564 -0.30 ILE 579

GLY 520 0.35 GLU 565 -0.39 ILE 579

GLY 520 0.34 THR 566 -0.31 ILE 579

GLY 520 0.34 TYR 567 -0.25 ILE 579

GLY 520 0.32 GLU 568 -0.17 ILE 579

GLY 520 0.34 THR 569 -0.08 HIS 529

PRO 635 0.35 LYS 570 -0.09 SER 585

GLY 520 0.31 THR 571 -0.11 GLU 565

PRO 635 0.31 ALA 572 -0.06 THR 561

PRO 635 0.69 LEU 573 -0.14 SER 585

PRO 635 0.51 LEU 574 -0.25 GLU 565

PRO 635 0.41 SER 575 -0.27 GLU 565

PRO 635 0.54 LEU 576 -0.17 THR 561

PRO 635 0.74 PHE 577 -0.22 THR 561

PRO 635 0.63 GLY 578 -0.32 THR 561

PRO 635 0.54 ILE 579 -0.42 THR 561

LEU 633 0.73 PRO 580 -0.35 THR 561

LEU 633 0.61 LEU 581 -0.47 THR 561

HIS 597 0.73 TRP 582 -0.37 THR 561

PRO 598 0.61 TYR 583 -0.33 THR 561

GLY 520 0.31 HIS 584 -0.38 SER 560

GLY 520 0.31 HIS 584 -0.37 SER 560

GLY 520 0.30 SER 585 -0.21 SER 560

GLY 520 0.32 GLN 586 -0.09 HIS 584

GLY 520 0.32 SER 587 -0.30 HIS 584

GLY 520 0.35 PRO 588 -0.24 HIS 584

GLY 520 0.34 ARG 589 -0.21 HIS 584

GLY 520 0.35 VAL 590 -0.06 HIS 584

GLY 520 0.39 ILE 591 -0.05 HIS 584

GLY 520 0.38 LEU 592 -0.06 HIS 584

GLY 520 0.35 GLN 593 -0.03 HIS 529

TRP 582 0.42 PRO 594 -0.04 HIS 529

TRP 582 0.57 ASP 595 -0.06 HIS 529

TRP 582 0.56 VAL 596 -0.09 HIS 529

TRP 582 0.73 HIS 597 -0.11 HIS 529

PRO 580 0.71 PRO 598 -0.12 HIS 529

TYR 583 0.58 GLY 599 -0.09 HIS 529

TRP 582 0.51 ASN 600 -0.07 HIS 529

GLY 520 0.37 CYS 601 -0.08 HIS 529

GLY 520 0.37 TRP 602 -0.06 HIS 529

GLY 520 0.37 ALA 603 -0.07 HIS 529

GLY 520 0.38 PHE 604 -0.17 ILE 579

GLY 520 0.37 GLN 605 -0.19 ILE 579

GLY 520 0.39 GLY 606 -0.14 SER 575

GLY 520 0.43 PRO 607 -0.09 HIS 529

GLY 520 0.44 GLN 608 -0.13 ILE 579

GLY 520 0.42 GLY 609 -0.17 ILE 579

GLY 520 0.43 PHE 610 -0.17 ILE 579

GLY 520 0.41 ALA 611 -0.19 HIS 584

GLY 520 0.41 VAL 612 -0.20 HIS 584

GLY 520 0.41 VAL 613 -0.18 HIS 584

GLY 520 0.39 ARG 614 -0.18 HIS 584

GLY 520 0.40 LEU 615 -0.13 HIS 584

GLY 520 0.37 SER 616 -0.12 HIS 584

GLY 520 0.39 ALA 617 -0.11 HIS 584

GLY 520 0.42 ARG 618 -0.11 HIS 584

GLY 520 0.46 ILE 619 -0.09 HIS 584

GLY 520 0.51 ARG 620 -0.08 HIS 584

GLY 520 0.54 PRO 621 -0.07 HIS 584

GLY 520 0.61 THR 622 -0.04 HIS 584

GLY 520 0.62 ALA 623 -0.03 HIS 584

GLY 520 0.57 VAL 624 -0.03 VAL 532

GLY 520 0.56 THR 625 -0.05 VAL 532

GLY 520 0.53 LEU 626 -0.07 VAL 532

GLY 520 0.51 GLU 627 -0.10 HIS 529

GLY 520 0.47 HIS 628 -0.12 HIS 529

PRO 580 0.53 VAL 629 -0.15 HIS 529

PRO 580 0.55 PRO 630 -0.20 HIS 529

PRO 580 0.56 LYS 631 -0.22 HIS 529

PRO 580 0.65 ALA 632 -0.26 HIS 529

PRO 580 0.73 LEU 633 -0.22 HIS 529

PRO 580 0.68 SER 634 -0.20 HIS 529

PRO 580 0.68 SER 634 -0.20 HIS 529

PHE 577 0.74 PRO 635 -0.20 HIS 529

PHE 577 0.67 ASN 636 -0.22 HIS 529

PRO 580 0.57 SER 637 -0.23 HIS 529

PHE 577 0.49 THR 638 -0.19 HIS 529

GLY 520 0.43 ILE 639 -0.16 HIS 529

GLY 520 0.44 SER 640 -0.15 HIS 529

GLY 520 0.42 SER 641 -0.12 HIS 529

GLY 520 0.46 ALA 642 -0.12 HIS 529

GLY 520 0.49 PRO 643 -0.10 VAL 532

GLY 520 0.53 LYS 644 -0.11 VAL 532

GLY 520 0.55 ASP 645 -0.10 VAL 532

GLY 520 0.54 PHE 646 -0.07 VAL 532

GLY 520 0.54 ALA 647 -0.08 HIS 584

GLY 520 0.53 ILE 648 -0.09 HIS 584

GLY 520 0.50 PHE 649 -0.12 HIS 584

GLY 520 0.48 GLY 650 -0.13 ILE 579

GLY 520 0.44 PHE 651 -0.19 LEU 581

GLY 520 0.43 ASP 652 -0.18 LEU 581

GLY 520 0.40 GLU 653 -0.24 LEU 581

GLY 520 0.37 ASP 654 -0.29 LEU 581

GLY 520 0.37 LEU 655 -0.34 LEU 581

GLY 520 0.39 GLN 656 -0.29 LEU 581

GLY 520 0.40 GLN 657 -0.30 LEU 581

GLY 520 0.43 GLU 658 -0.24 LEU 581

GLY 520 0.46 GLY 659 -0.19 LEU 581

GLY 520 0.50 THR 660 -0.14 ILE 579

GLY 520 0.53 LEU 661 -0.10 ILE 579

GLY 520 0.56 LEU 662 -0.08 HIS 584

GLY 520 0.60 GLY 663 -0.06 HIS 584

GLY 520 0.60 LYS 664 -0.07 VAL 532

GLY 520 0.62 PHE 665 -0.09 VAL 532

GLY 520 0.61 THR 666 -0.11 VAL 532

GLY 520 0.59 TYR 667 -0.12 VAL 532

GLY 520 0.61 ASP 668 -0.16 VAL 532

GLY 520 0.55 GLN 669 -0.17 VAL 532

GLY 520 0.59 ASP 670 -0.21 VAL 532

GLY 520 0.64 GLY 671 -0.21 VAL 532

GLY 520 0.61 GLU 672 -0.22 VAL 532

GLY 520 0.53 PRO 673 -0.17 LEU 536

GLY 520 0.56 ILE 674 -0.13 LEU 536

GLY 520 0.63 GLN 675 -0.12 LEU 536

GLY 520 0.65 THR 676 -0.08 LEU 536

GLY 520 0.67 PHE 677 -0.07 VAL 532

GLY 520 0.70 HIS 678 -0.05 VAL 532

GLY 520 0.66 PHE 679 -0.04 HIS 584

GLY 520 0.70 GLN 680 -0.04 VAL 532

GLY 520 0.70 GLN 680 -0.04 VAL 532

GLY 520 0.68 ALA 681 -0.04 HIS 584

GLY 520 0.62 PRO 682 -0.06 HIS 584

GLY 520 0.57 THR 683 -0.07 HIS 584

GLY 520 0.54 MET 684 -0.07 HIS 584

GLY 520 0.50 ALA 685 -0.09 HIS 584

GLY 520 0.47 THR 686 -0.10 HIS 584

GLY 520 0.45 TYR 687 -0.12 HIS 584

GLY 520 0.42 GLN 688 -0.14 HIS 584

GLY 520 0.42 VAL 689 -0.17 LEU 581

GLY 520 0.46 VAL 690 -0.14 HIS 584

GLY 520 0.46 GLU 691 -0.15 HIS 584

GLY 520 0.47 LEU 692 -0.11 HIS 584

GLY 520 0.48 ARG 693 -0.11 ILE 579

GLY 520 0.48 ILE 694 -0.08 HIS 584

GLY 520 0.49 LEU 695 -0.08 VAL 532

GLY 520 0.49 THR 696 -0.09 VAL 532

GLY 520 0.48 ASN 697 -0.10 VAL 532

GLY 520 0.48 TRP 698 -0.13 VAL 532

GLY 520 0.45 GLY 699 -0.12 HIS 529

GLY 520 0.41 HIS 700 -0.13 HIS 529

GLY 520 0.39 PRO 701 -0.11 HIS 529

GLY 520 0.37 GLU 702 -0.10 HIS 529

GLY 520 0.38 TYR 703 -0.10 HIS 529

GLY 520 0.41 THR 704 -0.09 HIS 529

GLY 520 0.41 CYS 705 -0.09 HIS 529

GLY 520 0.41 CYS 705 -0.09 HIS 529

GLY 520 0.43 ILE 706 -0.08 HIS 529

GLY 520 0.42 TYR 707 -0.08 HIS 529

GLY 520 0.43 ARG 708 -0.06 HIS 529

GLY 520 0.47 PHE 709 -0.04 HIS 529

GLY 520 0.48 ARG 710 -0.02 SER 587

GLY 520 0.50 VAL 711 -0.05 HIS 584

GLY 520 0.53 HIS 712 -0.03 HIS 584

GLY 520 0.54 GLY 713 -0.05 HIS 584

GLY 520 0.51 GLU 714 -0.05 HIS 584

GLY 520 0.44 PRO 715 -0.07 HIS 584

GLY 520 0.41 ALA 716 -0.08 HIS 584

GLY 520 0.41 HIS 717 -0.07 HIS 584

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.

*** STRUCTURAL PROTEIN 28-FEB-12 4DXT ***

CA distance fluctuations for 2403150145323283196

--- normal mode 10 ---

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

* STRUCTURAL PROTEIN 28-FEB-12 4DXT *