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

* STRUCTURAL PROTEIN 28-FEB-12 4DXT *

CA distance fluctuations for 2403150145323283196

--- 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 increase ref largest decrease
GLU 525 0.17 GLY 520 -1.12 HIS 678

GLU 525 0.20 PRO 521 -0.78 GLU 672

GLU 525 0.04 GLY 522 -0.55 ALA 632

THR 524 0.09 VAL 523 -0.40 ARG 543

PRO 521 0.17 THR 524 -0.22 ASP 595

PRO 521 0.20 GLU 525 -0.15 SER 553

LYS 533 0.16 GLU 526 -0.14 SER 553

ALA 681 0.09 GLN 527 -0.22 ASP 595

GLN 680 0.15 VAL 528 -0.25 ASP 595

GLY 671 0.23 HIS 529 -0.18 SER 553

GLN 680 0.18 HIS 530 -0.21 SER 553

GLN 680 0.18 HIS 530 -0.21 SER 553

GLN 680 0.20 ILE 531 -0.31 ALA 535

GLY 671 0.29 VAL 532 -0.26 GLY 522

GLY 671 0.26 LYS 533 -0.25 SER 553

GLN 680 0.22 GLN 534 -0.37 GLY 520

GLY 671 0.27 ALA 535 -0.49 GLY 520

GLU 672 0.29 LEU 536 -0.38 GLY 520

GLU 672 0.21 GLN 537 -0.41 GLY 520

HIS 678 0.21 ARG 538 -0.62 GLY 520

GLU 672 0.24 TYR 539 -0.61 GLY 520

GLU 672 0.17 SER 540 -0.50 GLY 520

GLU 672 0.11 GLU 541 -0.63 GLY 520

PRO 580 0.15 ASP 542 -0.72 GLY 520

PRO 580 0.18 ARG 543 -0.78 GLY 520

PRO 580 0.16 ILE 544 -0.92 GLY 520

PRO 580 0.13 GLY 545 -0.84 GLY 520

PRO 580 0.12 LEU 546 -0.90 GLY 520

PRO 580 0.10 ALA 547 -0.81 GLY 520

PRO 580 0.08 ASP 548 -0.80 GLY 520

PRO 580 0.03 TYR 549 -0.77 GLY 520

HIS 717 0.03 ALA 550 -0.76 GLY 520

TRP 582 0.05 LEU 551 -0.71 GLY 520

HIS 717 0.04 GLU 552 -0.65 GLY 520

HIS 717 0.05 SER 553 -0.61 GLY 520

HIS 717 0.06 GLY 554 -0.64 GLY 520

HIS 717 0.06 GLY 555 -0.62 GLY 520

HIS 717 0.04 ALA 556 -0.67 GLY 520

HIS 717 0.03 SER 557 -0.65 GLY 520

PRO 635 0.03 VAL 558 -0.67 GLY 520

PRO 635 0.03 ILE 559 -0.65 GLY 520

PRO 635 0.03 SER 560 -0.62 GLY 520

PRO 635 0.03 THR 561 -0.61 GLY 520

PRO 635 0.02 ARG 562 -0.66 GLY 520

PRO 635 0.03 CYS 563 -0.67 GLY 520

PRO 635 0.03 SER 564 -0.67 GLY 520

PRO 635 0.04 GLU 565 -0.63 GLY 520

PRO 635 0.06 THR 566 -0.62 GLY 520

PRO 635 0.06 TYR 567 -0.61 GLY 520

PRO 635 0.11 GLU 568 -0.58 GLY 520

PRO 635 0.13 THR 569 -0.58 GLY 520

PRO 635 0.29 LYS 570 -0.51 GLY 520

PRO 635 0.21 THR 571 -0.51 GLY 520

ASN 636 0.27 ALA 572 -0.47 GLY 520

PRO 635 0.54 LEU 573 -0.41 GLY 520

PRO 635 0.42 LEU 574 -0.42 GLY 520

PRO 635 0.34 SER 575 -0.41 GLY 520

PRO 635 0.44 LEU 576 -0.37 GLY 520

PRO 635 0.60 PHE 577 -0.31 GLY 520

PRO 635 0.53 GLY 578 -0.32 GLY 520

PRO 635 0.46 ILE 579 -0.35 GLY 520

PRO 635 0.58 PRO 580 -0.28 GLY 520

PRO 635 0.47 LEU 581 -0.36 THR 561

HIS 597 0.51 TRP 582 -0.30 GLY 520

GLY 599 0.43 TYR 583 -0.39 GLY 520

PRO 635 0.21 HIS 584 -0.50 GLY 520

PRO 635 0.21 HIS 584 -0.50 GLY 520

PRO 635 0.13 SER 585 -0.55 GLY 520

PRO 635 0.08 GLN 586 -0.60 GLY 520

PRO 635 0.06 SER 587 -0.62 GLY 520

PRO 635 0.04 PRO 588 -0.66 GLY 520

PRO 635 0.04 ARG 589 -0.65 GLY 520

TRP 582 0.09 VAL 590 -0.66 GLY 520

TRP 582 0.09 ILE 591 -0.72 GLY 520

TRP 582 0.06 LEU 592 -0.71 GLY 520

TRP 582 0.15 GLN 593 -0.67 GLY 520

TRP 582 0.23 PRO 594 -0.68 GLY 520

TRP 582 0.36 ASP 595 -0.64 GLY 520

TRP 582 0.38 VAL 596 -0.68 GLY 520

TRP 582 0.51 HIS 597 -0.63 GLY 520

PRO 580 0.55 PRO 598 -0.63 GLY 520

PRO 580 0.48 GLY 599 -0.61 GLY 520

TRP 582 0.39 ASN 600 -0.63 GLY 520

TRP 582 0.23 CYS 601 -0.68 GLY 520

TRP 582 0.10 TRP 602 -0.67 GLY 520

LEU 573 0.08 ALA 603 -0.67 GLY 520

ALA 572 0.06 PHE 604 -0.67 GLY 520

ALA 572 0.09 GLN 605 -0.65 GLY 520

ALA 572 0.12 GLY 606 -0.68 GLY 520

LEU 573 0.13 PRO 607 -0.74 GLY 520

ALA 572 0.08 GLN 608 -0.74 GLY 520

ALA 572 0.06 GLY 609 -0.73 GLY 520

ALA 572 0.04 PHE 610 -0.75 GLY 520

PRO 635 0.03 ALA 611 -0.73 GLY 520

PRO 635 0.02 VAL 612 -0.72 GLY 520

PRO 635 0.02 VAL 613 -0.72 GLY 520

HIS 717 0.03 ARG 614 -0.70 GLY 520

HIS 717 0.03 LEU 615 -0.72 GLY 520

HIS 717 0.05 SER 616 -0.68 GLY 520

HIS 717 0.06 ALA 617 -0.69 GLY 520

HIS 717 0.02 ARG 618 -0.72 GLY 520

ILE 544 0.02 ILE 619 -0.78 GLY 520

ALA 535 0.08 ARG 620 -0.84 GLY 520

ALA 535 0.10 PRO 621 -0.90 GLY 520

ALA 535 0.17 THR 622 -0.99 GLY 520

ALA 535 0.17 ALA 623 -1.02 GLY 520

ALA 535 0.12 VAL 624 -0.97 GLY 520

PRO 580 0.14 THR 625 -0.96 GLY 520

PRO 580 0.17 LEU 626 -0.91 GLY 520

PRO 580 0.23 GLU 627 -0.88 GLY 520

PRO 580 0.29 HIS 628 -0.82 GLY 520

PRO 580 0.39 VAL 629 -0.75 GLY 520

PRO 580 0.40 PRO 630 -0.78 GLY 520

PRO 580 0.42 LYS 631 -0.76 GLY 520

PRO 580 0.48 ALA 632 -0.69 GLY 520

PRO 580 0.55 LEU 633 -0.65 GLY 520

PRO 580 0.54 SER 634 -0.66 GLY 520

PRO 580 0.54 SER 634 -0.66 GLY 520

PHE 577 0.60 PRO 635 -0.61 GLY 520

PHE 577 0.56 ASN 636 -0.64 GLY 520

PHE 577 0.46 SER 637 -0.70 GLY 520

PHE 577 0.41 THR 638 -0.73 GLY 520

PRO 580 0.35 ILE 639 -0.75 GLY 520

LEU 573 0.31 SER 640 -0.75 GLY 520

LEU 573 0.27 SER 641 -0.74 GLY 520

PRO 580 0.23 ALA 642 -0.80 GLY 520

LEU 573 0.17 PRO 643 -0.83 GLY 520

LEU 573 0.17 LYS 644 -0.88 GLY 520

VAL 532 0.15 ASP 645 -0.90 GLY 520

ALA 535 0.12 PHE 646 -0.89 GLY 520

ALA 535 0.12 ALA 647 -0.89 GLY 520

ALA 535 0.10 ILE 648 -0.87 GLY 520

ALA 535 0.08 PHE 649 -0.82 GLY 520

ALA 535 0.06 GLY 650 -0.80 GLY 520

ALA 535 0.03 PHE 651 -0.74 GLY 520

ALA 535 0.03 ASP 652 -0.72 GLY 520

PRO 635 0.01 GLU 653 -0.67 GLY 520

PRO 635 0.02 ASP 654 -0.65 GLY 520

PRO 635 0.01 LEU 655 -0.63 GLY 520

PRO 635 0.02 GLN 656 -0.67 GLY 520

ALA 535 0.02 GLN 657 -0.67 GLY 520

ALA 535 0.05 GLU 658 -0.70 GLY 520

ALA 535 0.06 GLY 659 -0.75 GLY 520

ALA 535 0.09 THR 660 -0.80 GLY 520

ALA 535 0.12 LEU 661 -0.85 GLY 520

ALA 535 0.14 LEU 662 -0.90 GLY 520

ALA 535 0.17 GLY 663 -0.95 GLY 520

ALA 535 0.18 LYS 664 -0.96 GLY 520

ALA 535 0.20 PHE 665 -1.00 GLY 520

VAL 532 0.20 THR 666 -0.99 GLY 520

ALA 535 0.18 TYR 667 -0.97 GLY 520

VAL 532 0.23 ASP 668 -0.99 GLY 520

PRO 580 0.26 GLN 669 -0.91 GLY 520

PRO 580 0.28 ASP 670 -0.95 GLY 520

VAL 532 0.29 GLY 671 -1.03 GLY 520

LEU 536 0.29 GLU 672 -1.00 GLY 520

PRO 580 0.30 PRO 673 -0.91 GLY 520

PRO 580 0.25 ILE 674 -0.95 GLY 520

ALA 535 0.22 GLN 675 -1.05 GLY 520

ALA 535 0.24 THR 676 -1.09 GLY 520

ALA 535 0.25 PHE 677 -1.10 GLY 520

ALA 535 0.27 HIS 678 -1.12 GLY 520

ALA 535 0.22 PHE 679 -1.05 GLY 520

ALA 535 0.26 GLN 680 -1.08 GLY 520

ALA 535 0.26 GLN 680 -1.08 GLY 520

ALA 535 0.24 ALA 681 -1.02 GLY 520

ALA 535 0.18 PRO 682 -0.95 GLY 520

ALA 535 0.15 THR 683 -0.88 GLY 520

ALA 535 0.12 MET 684 -0.84 GLY 520

ALA 535 0.09 ALA 685 -0.80 GLY 520

ALA 535 0.05 THR 686 -0.78 GLY 520

ALA 535 0.03 TYR 687 -0.76 GLY 520

PRO 635 0.01 GLN 688 -0.73 GLY 520

PRO 635 0.02 VAL 689 -0.73 GLY 520

ALA 535 0.02 VAL 690 -0.78 GLY 520

ALA 535 0.03 GLU 691 -0.78 GLY 520

ALA 535 0.05 LEU 692 -0.81 GLY 520

ALA 535 0.06 ARG 693 -0.80 GLY 520

LEU 573 0.09 ILE 694 -0.81 GLY 520

VAL 532 0.10 LEU 695 -0.81 GLY 520

LEU 573 0.14 THR 696 -0.81 GLY 520

LEU 573 0.18 ASN 697 -0.80 GLY 520

LEU 573 0.23 TRP 698 -0.80 GLY 520

LEU 573 0.24 GLY 699 -0.74 GLY 520

LEU 573 0.27 HIS 700 -0.70 GLY 520

LEU 573 0.23 PRO 701 -0.67 GLY 520

ALA 572 0.20 GLU 702 -0.64 GLY 520

LEU 573 0.17 TYR 703 -0.67 GLY 520

LEU 573 0.17 THR 704 -0.72 GLY 520

PRO 580 0.17 CYS 705 -0.72 GLY 520

PRO 580 0.18 CYS 705 -0.72 GLY 520

PRO 580 0.16 ILE 706 -0.76 GLY 520

PRO 580 0.23 TYR 707 -0.75 GLY 520

TRP 582 0.17 ARG 708 -0.78 GLY 520

PRO 580 0.11 PHE 709 -0.83 GLY 520

PRO 580 0.10 ARG 710 -0.85 GLY 520

PRO 580 0.06 VAL 711 -0.87 GLY 520

PRO 580 0.08 HIS 712 -0.91 GLY 520

ALA 535 0.08 GLY 713 -0.90 GLY 520

ALA 535 0.06 GLU 714 -0.84 GLY 520

PRO 594 0.02 PRO 715 -0.76 GLY 520

HIS 717 0.02 ALA 716 -0.70 GLY 520

GLY 554 0.06 HIS 717 -0.68 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 2403150145323283196

--- normal mode 11 ---

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

* STRUCTURAL PROTEIN 28-FEB-12 4DXT *