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

* STRUCTURAL PROTEIN 28-FEB-12 4DXT *

CA distance fluctuations for 2403152111393385834

--- normal mode 8 ---

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
PHE 577 0.13 GLY 520 -0.59 ALA 681

PRO 580 0.17 PRO 521 -0.55 ALA 681

PRO 580 0.20 GLY 522 -0.52 ALA 681

PRO 580 0.20 VAL 523 -0.46 ALA 681

TRP 582 0.23 THR 524 -0.38 ALA 681

TRP 582 0.28 GLU 525 -0.31 ALA 681

TRP 582 0.24 GLU 526 -0.28 ALA 681

TRP 582 0.20 GLN 527 -0.34 ALA 681

TRP 582 0.24 VAL 528 -0.33 ALA 681

TRP 582 0.26 HIS 529 -0.24 ALA 681

TRP 582 0.19 HIS 530 -0.25 ALA 681

TRP 582 0.19 HIS 530 -0.25 ALA 681

TRP 582 0.18 ILE 531 -0.32 ALA 681

TRP 582 0.23 VAL 532 -0.25 GLN 680

TRP 582 0.21 LYS 533 -0.17 GLN 680

TRP 582 0.15 GLN 534 -0.20 HIS 678

HIS 597 0.17 ALA 535 -0.24 HIS 678

ASP 595 0.24 LEU 536 -0.15 HIS 678

ASP 595 0.16 GLN 537 -0.10 HIS 678

ASP 595 0.13 ARG 538 -0.14 HIS 678

ASP 595 0.19 TYR 539 -0.12 ILE 544

PRO 594 0.23 SER 540 -0.07 GLU 672

SER 553 0.11 GLU 541 -0.12 GLY 520

SER 540 0.16 ASP 542 -0.10 GLY 520

ASP 595 0.09 ARG 543 -0.11 GLY 520

TRP 582 0.04 ILE 544 -0.20 GLY 520

ILE 544 0.04 GLY 545 -0.22 GLY 520

GLU 541 0.04 LEU 546 -0.28 GLY 520

GLU 541 0.09 ALA 547 -0.25 GLY 520

SER 540 0.11 ASP 548 -0.22 GLY 520

SER 540 0.10 TYR 549 -0.24 GLY 520

SER 540 0.12 ALA 550 -0.20 GLY 520

SER 540 0.17 LEU 551 -0.14 GLY 520

SER 540 0.17 GLU 552 -0.11 GLY 520

SER 540 0.21 SER 553 -0.07 GLY 520

SER 540 0.18 GLY 554 -0.13 GLY 520

SER 540 0.15 GLY 555 -0.14 GLY 520

SER 540 0.13 ALA 556 -0.17 GLY 520

SER 540 0.12 SER 557 -0.15 GLY 520

SER 540 0.11 VAL 558 -0.15 GLY 520

SER 540 0.09 ILE 559 -0.17 GLY 520

SER 540 0.09 SER 560 -0.13 GLY 520

SER 540 0.08 THR 561 -0.15 GLY 520

SER 540 0.07 ARG 562 -0.18 GLY 520

SER 540 0.07 CYS 563 -0.16 GLY 520

SER 540 0.07 SER 564 -0.15 GLY 520

SER 540 0.07 GLU 565 -0.11 GLY 520

SER 540 0.08 THR 566 -0.08 GLY 520

HIS 529 0.08 TYR 567 -0.06 GLY 520

HIS 529 0.11 GLU 568 -0.02 ILE 579

GLU 525 0.11 THR 569 -0.00 THR 561

GLU 525 0.15 LYS 570 -0.01 THR 561

GLU 525 0.14 THR 571 -0.01 GLU 565

GLU 525 0.14 ALA 572 -0.01 THR 561

GLU 525 0.19 LEU 573 -0.01 THR 561

GLU 525 0.19 LEU 574 -0.02 GLU 565

GLU 525 0.17 SER 575 -0.02 GLU 565

GLU 525 0.18 LEU 576 -0.01 GLU 565

GLU 525 0.22 PHE 577 -0.02 THR 561

GLU 525 0.22 GLY 578 -0.02 THR 561

GLU 525 0.22 ILE 579 -0.03 GLU 565

GLU 525 0.26 PRO 580 -0.02 THR 561

GLU 525 0.27 LEU 581 -0.03 THR 561

GLU 525 0.28 TRP 582 -0.02 THR 561

GLU 525 0.24 TYR 583 -0.02 THR 561

GLU 525 0.19 HIS 584 -0.02 SER 560

GLU 525 0.19 HIS 584 -0.02 SER 560

HIS 529 0.15 SER 585 -0.01 SER 560

HIS 529 0.14 GLN 586 -0.01 GLY 520

HIS 529 0.11 SER 587 -0.05 GLY 520

SER 540 0.11 PRO 588 -0.10 GLY 520

SER 540 0.13 ARG 589 -0.09 GLY 520

SER 540 0.14 VAL 590 -0.06 GLY 520

SER 540 0.12 ILE 591 -0.11 GLY 520

SER 540 0.15 LEU 592 -0.11 GLY 520

SER 540 0.19 GLN 593 -0.05 GLY 520

SER 540 0.23 PRO 594 -0.03 GLY 520

LEU 536 0.24 ASP 595 -0.01 ARG 708

LEU 536 0.18 VAL 596 -0.01 ARG 708

VAL 532 0.22 HIS 597 -0.00 PRO 635

GLU 525 0.18 PRO 598 -0.00 PRO 635

GLU 525 0.16 GLY 599 -0.00 PRO 635

HIS 529 0.16 ASN 600 -0.01 VAL 590

LEU 536 0.11 CYS 601 -0.03 GLY 520

SER 540 0.10 TRP 602 -0.06 GLY 520

SER 540 0.08 ALA 603 -0.07 GLY 520

SER 540 0.07 PHE 604 -0.10 GLY 520

SER 540 0.05 GLN 605 -0.10 GLY 520

SER 540 0.04 GLY 606 -0.12 GLY 520

SER 540 0.03 PRO 607 -0.16 GLY 520

SER 540 0.04 GLN 608 -0.19 GLY 520

SER 540 0.05 GLY 609 -0.18 GLY 520

SER 540 0.06 PHE 610 -0.20 GLY 520

SER 540 0.07 ALA 611 -0.19 GLY 520

SER 540 0.07 VAL 612 -0.21 GLY 520

SER 540 0.09 VAL 613 -0.21 GLY 520

SER 540 0.09 ARG 614 -0.22 GLY 520

SER 540 0.10 LEU 615 -0.23 GLY 520

SER 540 0.11 SER 616 -0.21 GLY 520

SER 540 0.08 ALA 617 -0.26 GLY 520

SER 540 0.06 ARG 618 -0.31 GLY 520

SER 540 0.04 ILE 619 -0.36 GLY 520

SER 540 0.02 ARG 620 -0.42 GLY 520

ASP 542 0.02 PRO 621 -0.41 GLY 520

TRP 582 0.01 THR 622 -0.46 GLY 520

TRP 582 0.01 ALA 623 -0.40 GLY 520

ASP 542 0.02 VAL 624 -0.32 GLY 520

ASP 542 0.02 THR 625 -0.26 GLY 520

SER 540 0.03 LEU 626 -0.20 GLY 520

SER 540 0.03 GLU 627 -0.13 GLY 520

SER 540 0.04 HIS 628 -0.08 GLY 520

VAL 532 0.08 VAL 629 -0.00 PRO 594

GLY 522 0.07 PRO 630 -0.01 ASP 542

GLY 522 0.07 LYS 631 -0.01 SER 540

GLY 522 0.17 ALA 632 -0.01 SER 540

GLY 522 0.19 LEU 633 -0.01 ASP 595

GLY 522 0.14 SER 634 -0.00 ASP 595

GLY 522 0.14 SER 634 -0.00 ASP 595

GLY 522 0.15 PRO 635 -0.00 PRO 598

GLY 522 0.13 ASN 636 -0.00 ASP 595

GLY 522 0.10 SER 637 -0.00 ASP 542

GLY 522 0.03 THR 638 -0.00 ASP 595

PRO 580 0.03 ILE 639 -0.03 GLY 520

LEU 573 0.02 SER 640 -0.07 GLY 520

SER 540 0.03 SER 641 -0.08 GLY 520

SER 540 0.03 ALA 642 -0.11 GLY 520

SER 540 0.02 PRO 643 -0.17 GLY 520

PRO 580 0.01 LYS 644 -0.22 GLY 520

LEU 573 0.01 ASP 645 -0.27 GLY 520

SER 540 0.01 PHE 646 -0.28 GLY 520

SER 540 0.02 ALA 647 -0.32 GLY 520

SER 540 0.02 ILE 648 -0.33 GLY 520

SER 540 0.03 PHE 649 -0.33 GLY 520

SER 540 0.04 GLY 650 -0.34 GLY 520

SER 540 0.04 PHE 651 -0.32 GLY 520

SER 540 0.04 ASP 652 -0.34 GLY 520

SER 540 0.05 GLU 653 -0.30 GLY 520

SER 540 0.06 ASP 654 -0.26 GLY 520

SER 540 0.06 LEU 655 -0.25 GLY 520

SER 540 0.05 GLN 656 -0.27 GLY 520

SER 540 0.04 GLN 657 -0.27 GLY 520

SER 540 0.04 GLU 658 -0.31 GLY 520

SER 540 0.03 GLY 659 -0.33 GLY 520

SER 540 0.02 THR 660 -0.37 GLY 520

SER 540 0.01 LEU 661 -0.38 GLY 520

ASP 542 0.01 LEU 662 -0.41 GLY 520

ASP 542 0.01 GLY 663 -0.41 GLY 520

ASP 542 0.01 LYS 664 -0.38 GLY 520

TRP 582 0.01 PHE 665 -0.36 GLY 520

PRO 580 0.01 THR 666 -0.30 GLY 520

PRO 580 0.01 TYR 667 -0.24 GLY 520

PRO 580 0.02 ASP 668 -0.22 GLY 520

PRO 580 0.02 GLN 669 -0.14 GLY 520

PRO 580 0.02 ASP 670 -0.16 GLU 525

PRO 580 0.02 GLY 671 -0.19 VAL 528

PRO 580 0.03 GLU 672 -0.15 VAL 532

PRO 580 0.03 PRO 673 -0.08 GLY 520

TRP 582 0.03 ILE 674 -0.15 GLY 520

TRP 582 0.02 GLN 675 -0.24 GLY 520

TRP 582 0.02 THR 676 -0.32 GLY 520

TRP 582 0.01 PHE 677 -0.39 GLY 520

TRP 582 0.01 HIS 678 -0.47 GLY 520

TRP 582 0.01 PHE 679 -0.48 GLY 520

TRP 582 0.01 GLN 680 -0.55 GLY 520

TRP 582 0.01 GLN 680 -0.55 GLY 520

TRP 582 0.01 ALA 681 -0.59 GLY 520

HIS 717 0.01 PRO 682 -0.52 GLY 520

HIS 717 0.01 THR 683 -0.52 GLY 520

HIS 717 0.01 MET 684 -0.50 GLY 520

SER 540 0.01 ALA 685 -0.44 GLY 520

SER 540 0.03 THR 686 -0.40 GLY 520

SER 540 0.04 TYR 687 -0.35 GLY 520

SER 540 0.06 GLN 688 -0.29 GLY 520

SER 540 0.06 VAL 689 -0.27 GLY 520

SER 540 0.06 VAL 690 -0.29 GLY 520

SER 540 0.05 GLU 691 -0.26 GLY 520

SER 540 0.05 LEU 692 -0.25 GLY 520

SER 540 0.04 ARG 693 -0.25 GLY 520

SER 540 0.03 ILE 694 -0.22 GLY 520

SER 540 0.02 LEU 695 -0.24 GLY 520

SER 540 0.02 THR 696 -0.21 GLY 520

SER 540 0.02 ASN 697 -0.16 GLY 520

LEU 573 0.01 TRP 698 -0.14 GLY 520

SER 540 0.01 GLY 699 -0.12 GLY 520

SER 540 0.03 HIS 700 -0.08 GLY 520

SER 540 0.03 PRO 701 -0.08 GLY 520

SER 540 0.04 GLU 702 -0.07 GLY 520

SER 540 0.05 TYR 703 -0.08 GLY 520

SER 540 0.05 THR 704 -0.10 GLY 520

SER 540 0.06 CYS 705 -0.08 GLY 520

SER 540 0.06 CYS 705 -0.08 GLY 520

SER 540 0.07 ILE 706 -0.11 GLY 520

SER 540 0.10 TYR 707 -0.07 GLY 520

SER 540 0.10 ARG 708 -0.11 GLY 520

SER 540 0.08 PHE 709 -0.18 GLY 520

SER 540 0.08 ARG 710 -0.22 GLY 520

SER 540 0.06 VAL 711 -0.28 GLY 520

GLU 541 0.04 HIS 712 -0.33 GLY 520

GLU 541 0.02 GLY 713 -0.39 GLY 520

GLU 541 0.01 GLU 714 -0.42 GLY 520

SER 540 0.04 PRO 715 -0.37 GLY 520

SER 540 0.03 ALA 716 -0.37 GLY 520

SER 540 0.02 HIS 717 -0.39 GLY 520

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 2403152111393385834

--- normal mode 8 ---

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

* STRUCTURAL PROTEIN 28-FEB-12 4DXT *