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

* 7avq *

CA strain for 230125035839121270

--- normal mode 9 ---

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 -0.0002

PRO 472 VAL 473 0.0285

VAL 473 PRO 474 -0.0002

PRO 474 PHE 475 0.0307

PHE 475 SER 476 0.0001

SER 476 HIS 477 -0.0490

HIS 477 CYS 478 -0.0003

CYS 478 LEU 479 -0.0657

LEU 479 PRO 480 -0.0002

PRO 480 THR 481 -0.0417

THR 481 GLU 482 0.0000

GLU 482 LYS 483 -0.0286

LYS 483 LEU 484 0.0001

LEU 484 GLN 485 -0.0336

GLN 485 ARG 486 -0.0002

ARG 486 CYS 487 -0.0007

CYS 487 GLU 488 0.0002

GLU 488 LYS 489 0.0463

LYS 489 ILE 490 0.0002

ILE 490 GLY 491 0.0133

GLY 491 GLU 492 0.0001

GLU 492 GLY 493 -0.0448

GLY 493 VAL 494 -0.0002

VAL 494 PHE 495 0.0267

PHE 495 GLY 496 0.0001

GLY 496 GLU 497 -0.0023

GLU 497 VAL 498 0.0002

VAL 498 PHE 499 -0.0517

PHE 499 GLN 500 0.0001

GLN 500 THR 501 0.0684

THR 501 ILE 502 -0.0001

ILE 502 ILE 502 0.0416

ILE 502 ALA 503 -0.0438

ALA 503 ASP 504 -0.0002

ASP 504 HIS 505 -0.0176

HIS 505 THR 506 -0.0001

THR 506 PRO 507 0.0601

PRO 507 VAL 508 0.0002

VAL 508 ALA 509 -0.0508

ALA 509 ILE 510 0.0002

ILE 510 ILE 510 -0.0036

ILE 510 LYS 511 -0.0279

LYS 511 ILE 512 0.0001

ILE 512 ILE 513 0.0426

ILE 513 ALA 514 -0.0004

ALA 514 ILE 515 0.0408

ILE 515 GLU 516 0.0001

GLU 516 GLY 517 -0.0415

GLY 517 PRO 518 -0.0001

PRO 518 ASP 519 -0.0012

ASP 519 LEU 520 0.0001

LEU 520 VAL 521 0.0068

VAL 521 ASN 522 -0.0002

ASN 522 GLY 523 -0.0061

GLY 523 SER 524 -0.0002

SER 524 HIS 525 -0.0223

HIS 525 GLN 526 0.0001

GLN 526 LYS 527 -0.0357

LYS 527 THR 528 -0.0001

THR 528 PHE 529 0.0183

PHE 529 GLU 530 0.0001

GLU 530 GLU 531 -0.0031

GLU 531 ILE 532 0.0002

ILE 532 ILE 532 0.0034

ILE 532 LEU 533 0.0092

LEU 533 PRO 534 0.0002

PRO 534 GLU 535 -0.0353

GLU 535 ILE 536 -0.0003

ILE 536 ILE 537 -0.1187

ILE 537 ILE 538 0.0000

ILE 538 SER 539 -0.0658

SER 539 LYS 540 0.0003

LYS 540 GLU 541 -0.0896

GLU 541 LEU 542 -0.0002

LEU 542 SER 543 -0.0137

SER 543 LEU 544 -0.0001

LEU 544 LEU 545 -0.0277

LEU 545 SER 546 -0.0002

SER 546 GLY 547 0.0023

GLY 547 GLU 548 -0.0002

GLU 548 VAL 549 -0.0232

VAL 549 CYS 550 -0.0001

CYS 550 ASN 551 0.0193

ASN 551 ARG 552 0.0001

ARG 552 ARG 552 -0.0173

ARG 552 THR 553 0.0134

THR 553 GLU 554 0.0001

GLU 554 GLY 555 -0.0195

GLY 555 PHE 556 0.0002

PHE 556 ILE 557 0.0430

ILE 557 GLY 558 -0.0004

GLY 558 LEU 559 0.0568

LEU 559 ASN 560 -0.0002

ASN 560 SER 561 0.0956

SER 561 VAL 562 -0.0003

VAL 562 HIS 563 -0.0530

HIS 563 CYS 564 -0.0003

CYS 564 VAL 565 -0.0538

VAL 565 GLN 566 -0.0003

GLN 566 GLY 567 0.0057

GLY 567 SER 568 0.0002

SER 568 TYR 569 0.0703

TYR 569 PRO 570 0.0002

PRO 570 PRO 571 -0.0280

PRO 571 LEU 572 -0.0001

LEU 572 LEU 573 -0.0037

LEU 573 LEU 574 -0.0001

LEU 574 LYS 575 -0.0262

LYS 575 ALA 576 -0.0001

ALA 576 TRP 577 -0.0208

TRP 577 ASP 578 0.0002

ASP 578 HIS 579 0.0054

HIS 579 TYR 580 0.0000

TYR 580 ASN 581 -0.0343

ASN 581 SER 582 0.0004

SER 582 THR 583 0.0934

THR 583 LYS 584 -0.0000

LYS 584 GLY 585 0.0101

GLY 585 SER 586 -0.0000

SER 586 ALA 587 0.0018

ALA 587 ASN 588 0.0002

ASN 588 ASP 589 -0.0071

ASP 589 ARG 590 0.0001

ARG 590 PRO 591 -0.0050

PRO 591 ASP 592 0.0001

ASP 592 PHE 593 0.0323

PHE 593 PHE 594 -0.0003

PHE 594 LYS 595 0.0154

LYS 595 ASP 596 0.0001

ASP 596 ASP 597 -0.0053

ASP 597 GLN 598 0.0002

GLN 598 LEU 599 -0.0126

LEU 599 PHE 600 0.0003

PHE 600 ILE 601 -0.0555

ILE 601 VAL 602 0.0003

VAL 602 LEU 603 0.0215

LEU 603 GLU 604 -0.0002

GLU 604 PHE 605 0.1328

PHE 605 GLU 606 -0.0001

GLU 606 PHE 607 0.0478

PHE 607 GLY 608 -0.0001

GLY 608 GLY 609 0.0571

GLY 609 ILE 610 -0.0001

ILE 610 ASP 611 0.0291

ASP 611 LEU 612 0.0000

LEU 612 GLU 613 -0.0057

GLU 613 GLN 614 -0.0001

GLN 614 GLN 614 0.0322

GLN 614 MET 615 0.2326

MET 615 ARG 616 0.0002

ARG 616 THR 617 -0.0316

THR 617 LYS 618 -0.0005

LYS 618 LEU 619 -0.0410

LEU 619 SER 620 -0.0001

SER 620 SER 621 0.0479

SER 621 LEU 622 0.0002

LEU 622 ALA 623 -0.0161

ALA 623 THR 624 -0.0000

THR 624 ALA 625 -0.0264

ALA 625 LYS 626 0.0002

LYS 626 SER 627 0.0480

SER 627 ILE 628 -0.0005

ILE 628 LEU 629 0.0638

LEU 629 HIS 630 -0.0003

HIS 630 GLN 631 0.0659

GLN 631 LEU 632 -0.0000

LEU 632 THR 633 0.0653

THR 633 ALA 634 -0.0001

ALA 634 SER 635 0.0081

SER 635 LEU 636 0.0001

LEU 636 ALA 637 0.0052

ALA 637 VAL 638 0.0000

VAL 638 ALA 639 -0.0205

ALA 639 GLU 640 0.0002

GLU 640 ALA 641 0.0282

ALA 641 SER 642 -0.0003

SER 642 SER 642 -0.0068

SER 642 LEU 643 0.0104

LEU 643 ARG 644 0.0001

ARG 644 PHE 645 0.0184

PHE 645 GLU 646 0.0002

GLU 646 HIS 647 0.0272

HIS 647 ARG 648 -0.0002

ARG 648 ASP 649 0.0305

ASP 649 LEU 650 -0.0001

LEU 650 HIS 651 -0.0045

HIS 651 TRP 652 -0.0006

TRP 652 GLY 653 0.0592

GLY 653 ASN 654 -0.0000

ASN 654 VAL 655 -0.0220

VAL 655 LEU 656 0.0001

LEU 656 LEU 657 -0.0458

LEU 657 LYS 658 0.0001

LYS 658 LYS 659 0.0743

LYS 659 THR 660 0.0000

THR 660 SER 661 0.0381

SER 661 LEU 662 -0.0000

LEU 662 LYS 663 -0.0034

LYS 663 LYS 664 -0.0000

LYS 664 LEU 665 0.0152

LEU 665 HIS 666 0.0001

HIS 666 TYR 667 0.0161

TYR 667 THR 668 -0.0002

THR 668 LEU 669 0.0121

LEU 669 ASN 670 0.0005

ASN 670 GLY 671 0.0024

GLY 671 LYS 672 0.0005

LYS 672 SER 673 -0.0014

SER 673 SER 674 -0.0002

SER 674 THR 675 -0.0188

THR 675 ILE 676 -0.0004

ILE 676 PRO 677 -0.0089

PRO 677 SER 678 0.0000

SER 678 CYS 679 -0.0235

CYS 679 GLY 680 -0.0002

GLY 680 LEU 681 -0.0457

LEU 681 GLN 682 -0.0001

GLN 682 GLN 682 0.0331

GLN 682 VAL 683 -0.0302

VAL 683 SER 684 0.0000

SER 684 ILE 685 0.0096

ILE 685 ILE 686 -0.0003

ILE 686 ASP 687 -0.0196

ASP 687 TYR 688 -0.0002

TYR 688 THR 689 -0.0612

THR 689 LEU 690 -0.0000

LEU 690 SER 691 -0.0047

SER 691 ARG 692 -0.0005

ARG 692 LEU 693 0.0555

LEU 693 GLU 694 0.0001

GLU 694 ARG 695 0.0282

ARG 695 ASP 696 -0.0005

ASP 696 GLY 697 -0.0226

GLY 697 ILE 698 -0.0002

ILE 698 VAL 699 0.0097

VAL 699 VAL 700 0.0001

VAL 700 PHE 701 0.0657

PHE 701 CYS 702 -0.0000

CYS 702 ASP 703 -0.0783

ASP 703 VAL 704 0.0000

VAL 704 SER 705 -0.0413

SER 705 MET 706 -0.0004

MET 706 ASP 707 -0.0015

ASP 707 GLU 708 -0.0002

GLU 708 ASP 709 0.0003

ASP 709 LEU 710 -0.0000

LEU 710 PHE 711 0.0064

PHE 711 THR 712 -0.0000

THR 712 GLY 713 -0.0098

GLY 713 ASP 714 0.0002

ASP 714 ASP 714 -0.0255

ASP 714 GLY 715 -0.0089

GLY 715 ASP 716 -0.0003

ASP 716 TYR 717 0.0157

TYR 717 GLN 718 -0.0001

GLN 718 PHE 719 -0.0371

PHE 719 ASP 720 -0.0006

ASP 720 ILE 721 0.0210

ILE 721 TYR 722 -0.0001

TYR 722 ARG 723 -0.0126

ARG 723 LEU 724 0.0002

LEU 724 MET 725 -0.0160

MET 725 LYS 726 -0.0002

LYS 726 LYS 727 0.0037

LYS 727 GLU 728 0.0001

GLU 728 ASN 729 -0.0398

ASN 729 ASN 730 -0.0002

ASN 730 ASN 731 -0.0037

ASN 731 ARG 732 0.0003

ARG 732 TRP 733 -0.0611

TRP 733 GLY 734 0.0000

GLY 734 GLU 735 -0.0435

GLU 735 TYR 736 0.0001

TYR 736 HIS 737 -0.0445

HIS 737 PRO 738 -0.0002

PRO 738 TYR 739 -0.0351

TYR 739 SER 740 -0.0002

SER 740 ASN 741 0.0196

ASN 741 VAL 742 0.0002

VAL 742 LEU 743 0.0216

LEU 743 TRP 744 -0.0002

TRP 744 LEU 745 -0.0223

LEU 745 HIS 746 0.0005

HIS 746 TYR 747 0.0286

TYR 747 LEU 748 0.0000

LEU 748 THR 749 0.0267

THR 749 ASP 750 0.0003

ASP 750 LYS 751 0.0432

LYS 751 MET 752 -0.0003

MET 752 MET 752 0.0009

MET 752 LEU 753 0.0357

LEU 753 LYS 754 -0.0001

LYS 754 GLN 755 0.0617

GLN 755 MET 756 -0.0001

MET 756 THR 757 -0.0527

THR 757 THR 757 -0.0164

THR 757 PHE 758 0.0003

PHE 758 LYS 759 -0.0857

LYS 759 THR 760 -0.0002

THR 760 LYS 761 0.0271

LYS 761 CYS 762 0.0004

CYS 762 CYS 762 -0.0333

CYS 762 ASN 763 -0.0010

ASN 763 THR 764 0.0000

THR 764 PRO 765 0.0242

PRO 765 ALA 766 -0.0002

ALA 766 MET 767 0.0495

MET 767 LYS 768 0.0001

LYS 768 GLN 769 -0.0200

GLN 769 ILE 770 -0.0001

ILE 770 LYS 771 0.0008

LYS 771 ARG 772 0.0003

ARG 772 LYS 773 -0.0546

LYS 773 ILE 774 0.0002

ILE 774 GLN 775 0.0245

GLN 775 GLU 776 0.0004

GLU 776 PHE 777 -0.0172

PHE 777 HIS 778 0.0003

HIS 778 ARG 779 0.0501

ARG 779 THR 780 -0.0000

THR 780 MET 781 -0.0329

MET 781 LEU 782 0.0001

LEU 782 ASN 783 0.0560

ASN 783 PHE 784 -0.0003

PHE 784 SER 785 -0.0804

SER 785 SER 785 0.0130

SER 785 SER 786 -0.0003

SER 786 ALA 787 0.0344

ALA 787 THR 788 -0.0004

THR 788 ASP 789 -0.0293

ASP 789 LEU 790 0.0000

LEU 790 LEU 791 0.0347

LEU 791 CYS 792 0.0002

CYS 792 GLN 793 -0.0001

GLN 793 HIS 794 0.0001

HIS 794 SER 795 -0.0428

SER 795 LEU 796 -0.0000

LEU 796 PHE 797 -0.0128

PHE 797 LYS 798 -0.0002

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 9 ---

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

* 7avq *