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

* 7avq *

CA strain for 230125035839121270

--- normal mode 11 ---

This graph displays the distance variation between successive pairs of CA atoms in the two extreme conformations that were computed for this mode (DQMIN/DQMAX). Large distance variations can be an indicator for residue pairs that support the important strain in that particular normal mode movement. Note that residue pairs between chain breaks or at flexible ends of the protein may also exhibit large CA-CA distance variations. If more than one residues ae grouped together into a rigid block (NRBL>1), CA-CA distance variations between CA atoms in the same block will be very low.

This feature is still experimental and will be further developped in the future.

CA i CA i+1 vari
GLY 471 PRO 472 -0.0001

PRO 472 VAL 473 0.0568

VAL 473 PRO 474 -0.0002

PRO 474 PHE 475 0.0039

PHE 475 SER 476 0.0000

SER 476 HIS 477 -0.0625

HIS 477 CYS 478 0.0001

CYS 478 LEU 479 -0.0304

LEU 479 PRO 480 0.0002

PRO 480 THR 481 -0.0590

THR 481 GLU 482 -0.0002

GLU 482 LYS 483 0.0142

LYS 483 LEU 484 0.0002

LEU 484 GLN 485 -0.0627

GLN 485 ARG 486 -0.0001

ARG 486 CYS 487 -0.1444

CYS 487 GLU 488 -0.0003

GLU 488 LYS 489 -0.1999

LYS 489 ILE 490 -0.0002

ILE 490 GLY 491 -0.0915

GLY 491 GLU 492 0.0002

GLU 492 GLY 493 -0.0494

GLY 493 VAL 494 -0.0004

VAL 494 PHE 495 0.0712

PHE 495 GLY 496 0.0001

GLY 496 GLU 497 -0.0558

GLU 497 VAL 498 -0.0001

VAL 498 PHE 499 -0.0750

PHE 499 GLN 500 0.0001

GLN 500 THR 501 -0.0944

THR 501 ILE 502 0.0003

ILE 502 ILE 502 0.0237

ILE 502 ALA 503 -0.0083

ALA 503 ASP 504 0.0001

ASP 504 HIS 505 0.0788

HIS 505 THR 506 0.0005

THR 506 PRO 507 -0.1556

PRO 507 VAL 508 0.0003

VAL 508 ALA 509 0.0622

ALA 509 ILE 510 0.0002

ILE 510 ILE 510 -0.0071

ILE 510 LYS 511 -0.0040

LYS 511 ILE 512 0.0003

ILE 512 ILE 513 -0.0237

ILE 513 ALA 514 -0.0002

ALA 514 ILE 515 -0.0108

ILE 515 GLU 516 0.0003

GLU 516 GLY 517 -0.1115

GLY 517 PRO 518 0.0001

PRO 518 ASP 519 -0.0435

ASP 519 LEU 520 -0.0000

LEU 520 VAL 521 0.0246

VAL 521 ASN 522 -0.0000

ASN 522 GLY 523 0.0116

GLY 523 SER 524 -0.0002

SER 524 HIS 525 -0.0076

HIS 525 GLN 526 0.0001

GLN 526 LYS 527 0.0849

LYS 527 THR 528 -0.0002

THR 528 PHE 529 -0.0238

PHE 529 GLU 530 -0.0001

GLU 530 GLU 531 -0.0066

GLU 531 ILE 532 -0.0002

ILE 532 ILE 532 -0.0273

ILE 532 LEU 533 0.1153

LEU 533 PRO 534 -0.0001

PRO 534 GLU 535 0.0421

GLU 535 ILE 536 -0.0001

ILE 536 ILE 537 0.0156

ILE 537 ILE 538 0.0000

ILE 538 SER 539 0.0478

SER 539 LYS 540 -0.0002

LYS 540 GLU 541 0.0796

GLU 541 LEU 542 0.0001

LEU 542 SER 543 0.0508

SER 543 LEU 544 0.0001

LEU 544 LEU 545 0.0905

LEU 545 SER 546 -0.0002

SER 546 GLY 547 -0.0125

GLY 547 GLU 548 -0.0002

GLU 548 VAL 549 0.0620

VAL 549 CYS 550 -0.0000

CYS 550 ASN 551 -0.0417

ASN 551 ARG 552 -0.0002

ARG 552 ARG 552 0.0154

ARG 552 THR 553 0.0741

THR 553 GLU 554 -0.0002

GLU 554 GLY 555 0.0144

GLY 555 PHE 556 0.0001

PHE 556 ILE 557 0.1881

ILE 557 GLY 558 -0.0002

GLY 558 LEU 559 -0.1875

LEU 559 ASN 560 -0.0000

ASN 560 SER 561 -0.1824

SER 561 VAL 562 -0.0003

VAL 562 HIS 563 -0.2751

HIS 563 CYS 564 0.0003

CYS 564 VAL 565 -0.0963

VAL 565 GLN 566 0.0002

GLN 566 GLY 567 -0.0616

GLY 567 SER 568 -0.0001

SER 568 TYR 569 0.0708

TYR 569 PRO 570 0.0000

PRO 570 PRO 571 -0.0438

PRO 571 LEU 572 0.0001

LEU 572 LEU 573 0.0355

LEU 573 LEU 574 -0.0003

LEU 574 LYS 575 -0.0592

LYS 575 ALA 576 -0.0002

ALA 576 TRP 577 -0.0323

TRP 577 ASP 578 0.0004

ASP 578 HIS 579 0.0034

HIS 579 TYR 580 -0.0000

TYR 580 ASN 581 -0.0191

ASN 581 SER 582 0.0002

SER 582 THR 583 0.1944

THR 583 LYS 584 0.0003

LYS 584 GLY 585 0.1059

GLY 585 SER 586 0.0002

SER 586 ALA 587 -0.0485

ALA 587 ASN 588 0.0003

ASN 588 ASP 589 0.0487

ASP 589 ARG 590 0.0002

ARG 590 PRO 591 -0.0099

PRO 591 ASP 592 -0.0002

ASP 592 PHE 593 0.0200

PHE 593 PHE 594 0.0004

PHE 594 LYS 595 0.0404

LYS 595 ASP 596 0.0000

ASP 596 ASP 597 0.0027

ASP 597 GLN 598 -0.0001

GLN 598 LEU 599 -0.0433

LEU 599 PHE 600 -0.0003

PHE 600 ILE 601 -0.0624

ILE 601 VAL 602 -0.0000

VAL 602 LEU 603 -0.0256

LEU 603 GLU 604 -0.0001

GLU 604 PHE 605 -0.1297

PHE 605 GLU 606 -0.0001

GLU 606 PHE 607 -0.1512

PHE 607 GLY 608 -0.0004

GLY 608 GLY 609 -0.3728

GLY 609 ILE 610 0.0002

ILE 610 ASP 611 -0.0995

ASP 611 LEU 612 -0.0002

LEU 612 GLU 613 -0.0006

GLU 613 GLN 614 -0.0004

GLN 614 GLN 614 -0.0053

GLN 614 MET 615 0.2180

MET 615 ARG 616 0.0002

ARG 616 THR 617 0.0061

THR 617 LYS 618 -0.0003

LYS 618 LEU 619 0.0579

LEU 619 SER 620 -0.0002

SER 620 SER 621 0.0082

SER 621 LEU 622 -0.0002

LEU 622 ALA 623 0.0068

ALA 623 THR 624 -0.0000

THR 624 ALA 625 0.0214

ALA 625 LYS 626 -0.0004

LYS 626 SER 627 0.0348

SER 627 ILE 628 0.0002

ILE 628 LEU 629 -0.0383

LEU 629 HIS 630 0.0004

HIS 630 GLN 631 0.0480

GLN 631 LEU 632 -0.0003

LEU 632 THR 633 0.0249

THR 633 ALA 634 -0.0001

ALA 634 SER 635 0.0610

SER 635 LEU 636 -0.0003

LEU 636 ALA 637 0.0409

ALA 637 VAL 638 0.0001

VAL 638 ALA 639 -0.0229

ALA 639 GLU 640 -0.0001

GLU 640 ALA 641 -0.0556

ALA 641 SER 642 -0.0001

SER 642 SER 642 -0.0043

SER 642 LEU 643 -0.1004

LEU 643 ARG 644 -0.0004

ARG 644 PHE 645 0.0231

PHE 645 GLU 646 -0.0001

GLU 646 HIS 647 0.0249

HIS 647 ARG 648 -0.0001

ARG 648 ASP 649 0.0321

ASP 649 LEU 650 0.0004

LEU 650 HIS 651 0.0044

HIS 651 TRP 652 0.0002

TRP 652 GLY 653 -0.1006

GLY 653 ASN 654 0.0002

ASN 654 VAL 655 0.0782

VAL 655 LEU 656 -0.0002

LEU 656 LEU 657 0.0239

LEU 657 LYS 658 0.0000

LYS 658 LYS 659 0.1839

LYS 659 THR 660 0.0000

THR 660 SER 661 0.0969

SER 661 LEU 662 0.0003

LEU 662 LYS 663 0.0197

LYS 663 LYS 664 -0.0000

LYS 664 LEU 665 -0.0068

LEU 665 HIS 666 0.0001

HIS 666 TYR 667 -0.1295

TYR 667 THR 668 0.0004

THR 668 LEU 669 -0.0276

LEU 669 ASN 670 -0.0002

ASN 670 GLY 671 0.0229

GLY 671 LYS 672 -0.0001

LYS 672 SER 673 0.0189

SER 673 SER 674 0.0002

SER 674 THR 675 0.0787

THR 675 ILE 676 0.0004

ILE 676 PRO 677 0.0271

PRO 677 SER 678 0.0000

SER 678 CYS 679 0.0398

CYS 679 GLY 680 -0.0002

GLY 680 LEU 681 0.0261

LEU 681 GLN 682 -0.0001

GLN 682 GLN 682 0.0217

GLN 682 VAL 683 -0.0151

VAL 683 SER 684 0.0001

SER 684 ILE 685 0.0633

ILE 685 ILE 686 0.0001

ILE 686 ASP 687 0.1259

ASP 687 TYR 688 0.0003

TYR 688 THR 689 0.1061

THR 689 LEU 690 0.0001

LEU 690 SER 691 0.0831

SER 691 ARG 692 -0.0002

ARG 692 LEU 693 0.0045

LEU 693 GLU 694 0.0002

GLU 694 ARG 695 0.0240

ARG 695 ASP 696 -0.0001

ASP 696 GLY 697 -0.0001

GLY 697 ILE 698 0.0002

ILE 698 VAL 699 -0.0305

VAL 699 VAL 700 0.0002

VAL 700 PHE 701 -0.0373

PHE 701 CYS 702 0.0004

CYS 702 ASP 703 0.0400

ASP 703 VAL 704 -0.0000

VAL 704 SER 705 0.0414

SER 705 MET 706 -0.0001

MET 706 ASP 707 -0.0098

ASP 707 GLU 708 0.0001

GLU 708 ASP 709 0.0093

ASP 709 LEU 710 0.0001

LEU 710 PHE 711 -0.0295

PHE 711 THR 712 -0.0003

THR 712 GLY 713 0.0358

GLY 713 ASP 714 -0.0001

ASP 714 ASP 714 0.0255

ASP 714 GLY 715 0.0097

GLY 715 ASP 716 0.0003

ASP 716 TYR 717 -0.0051

TYR 717 GLN 718 0.0000

GLN 718 PHE 719 0.0356

PHE 719 ASP 720 0.0002

ASP 720 ILE 721 -0.0380

ILE 721 TYR 722 -0.0000

TYR 722 ARG 723 0.0320

ARG 723 LEU 724 0.0000

LEU 724 MET 725 0.0142

MET 725 LYS 726 -0.0002

LYS 726 LYS 727 -0.0308

LYS 727 GLU 728 -0.0000

GLU 728 ASN 729 -0.0030

ASN 729 ASN 730 -0.0002

ASN 730 ASN 731 -0.0211

ASN 731 ARG 732 0.0000

ARG 732 TRP 733 0.0597

TRP 733 GLY 734 -0.0000

GLY 734 GLU 735 -0.0389

GLU 735 TYR 736 0.0001

TYR 736 HIS 737 0.0440

HIS 737 PRO 738 -0.0001

PRO 738 TYR 739 0.0708

TYR 739 SER 740 0.0001

SER 740 ASN 741 -0.0369

ASN 741 VAL 742 0.0002

VAL 742 LEU 743 -0.0614

LEU 743 TRP 744 0.0001

TRP 744 LEU 745 -0.0206

LEU 745 HIS 746 -0.0001

HIS 746 TYR 747 -0.0171

TYR 747 LEU 748 -0.0002

LEU 748 THR 749 -0.0528

THR 749 ASP 750 -0.0002

ASP 750 LYS 751 0.0011

LYS 751 MET 752 0.0003

MET 752 MET 752 0.0036

MET 752 LEU 753 -0.0451

LEU 753 LYS 754 0.0003

LYS 754 GLN 755 -0.0719

GLN 755 MET 756 -0.0002

MET 756 THR 757 0.0086

THR 757 THR 757 0.0127

THR 757 PHE 758 0.0002

PHE 758 LYS 759 0.0401

LYS 759 THR 760 0.0002

THR 760 LYS 761 0.0350

LYS 761 CYS 762 -0.0002

CYS 762 CYS 762 0.0283

CYS 762 ASN 763 -0.0112

ASN 763 THR 764 -0.0000

THR 764 PRO 765 -0.0262

PRO 765 ALA 766 0.0000

ALA 766 MET 767 -0.0267

MET 767 LYS 768 0.0001

LYS 768 GLN 769 0.0711

GLN 769 ILE 770 0.0002

ILE 770 LYS 771 0.0113

LYS 771 ARG 772 0.0001

ARG 772 LYS 773 0.1270

LYS 773 ILE 774 -0.0000

ILE 774 GLN 775 0.0560

GLN 775 GLU 776 -0.0004

GLU 776 PHE 777 0.0009

PHE 777 HIS 778 -0.0001

HIS 778 ARG 779 0.0046

ARG 779 THR 780 -0.0001

THR 780 MET 781 0.0210

MET 781 LEU 782 -0.0003

LEU 782 ASN 783 -0.0086

ASN 783 PHE 784 -0.0002

PHE 784 SER 785 0.0641

SER 785 SER 785 -0.0613

SER 785 SER 786 0.0005

SER 786 ALA 787 -0.0321

ALA 787 THR 788 -0.0000

THR 788 ASP 789 0.0910

ASP 789 LEU 790 0.0001

LEU 790 LEU 791 -0.0484

LEU 791 CYS 792 0.0004

CYS 792 GLN 793 0.0655

GLN 793 HIS 794 0.0005

HIS 794 SER 795 0.0620

SER 795 LEU 796 0.0003

LEU 796 PHE 797 0.0476

PHE 797 LYS 798 -0.0000

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: October 18th, 2018.

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

*** 7avq ***

CA strain for 230125035839121270

--- normal mode 11 ---

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

* 7avq *