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

* *

CA strain for 2504102047043794046

--- normal mode 10 ---

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
SER 348 ARG 349 -0.0002

ARG 349 ALA 350 -0.0064

ALA 350 SER 351 -0.0002

SER 351 LEU 352 0.0079

LEU 352 ARG 353 -0.0001

ARG 353 ARG 354 -0.0032

ARG 354 HIS 355 0.0000

HIS 355 TYR 356 0.0122

TYR 356 SER 357 0.0001

SER 357 VAL 358 0.0199

VAL 358 ARG 359 -0.0001

ARG 359 HIS 360 -0.0062

HIS 360 LEU 361 -0.0000

LEU 361 ALA 362 0.0146

ALA 362 ALA 363 -0.0002

ALA 363 ARG 364 -0.0067

ARG 364 GLU 365 0.0000

GLU 365 LEU 366 0.0077

LEU 366 LEU 367 0.0003

LEU 367 ASP 368 0.0069

ASP 368 THR 369 -0.0001

THR 369 GLU 370 -0.0251

GLU 370 LYS 371 0.0004

LYS 371 SER 372 0.0134

SER 372 PHE 373 0.0000

PHE 373 VAL 374 0.0117

VAL 374 GLU 375 -0.0002

GLU 375 GLY 376 0.0260

GLY 376 LEU 377 -0.0001

LEU 377 GLU 378 -0.0052

GLU 378 PHE 379 -0.0002

PHE 379 LEU 380 -0.0039

LEU 380 VAL 381 -0.0001

VAL 381 THR 382 0.0207

THR 382 LYS 383 -0.0002

LYS 383 TYR 384 -0.0034

TYR 384 MET 385 0.0002

MET 385 ARG 386 0.0052

ARG 386 PRO 387 -0.0001

PRO 387 LEU 388 -0.0089

LEU 388 ARG 389 -0.0001

ARG 389 GLN 390 0.0046

GLN 390 PRO 391 0.0000

PRO 391 LEU 392 0.0012

LEU 392 GLU 393 0.0003

GLU 393 CYS 394 0.0036

CYS 394 THR 395 0.0002

THR 395 LEU 396 -0.0198

LEU 396 ILE 397 -0.0003

ILE 397 GLU 398 0.0087

GLU 398 ALA 399 -0.0003

ALA 399 SER 400 0.0325

SER 400 LEU 401 -0.0002

LEU 401 VAL 402 0.0245

VAL 402 ASP 403 -0.0001

ASP 403 LYS 404 0.0020

LYS 404 ILE 405 -0.0000

ILE 405 PHE 406 0.0166

PHE 406 TYR 407 -0.0001

TYR 407 ARG 408 0.0769

ARG 408 ILE 409 0.0000

ILE 409 PRO 410 -0.0195

PRO 410 GLU 411 0.0002

GLU 411 ILE 412 -0.0168

ILE 412 LEU 413 0.0002

LEU 413 ALA 414 0.0033

ALA 414 HIS 415 -0.0001

HIS 415 HIS 416 -0.0279

HIS 416 GLN 417 -0.0001

GLN 417 VAL 418 0.0023

VAL 418 LEU 419 0.0002

LEU 419 LEU 420 -0.0356

LEU 420 THR 421 -0.0002

THR 421 THR 422 -0.0119

THR 422 LEU 423 -0.0003

LEU 423 SER 424 -0.0143

SER 424 GLN 425 0.0002

GLN 425 ARG 426 -0.0179

ARG 426 ILE 427 -0.0003

ILE 427 ASP 428 0.0029

ASP 428 GLN 429 0.0003

GLN 429 TRP 430 0.0110

TRP 430 HIS 431 -0.0000

HIS 431 LYS 432 0.0289

LYS 432 ASP 433 0.0004

ASP 433 ALA 434 -0.0222

ALA 434 ILE 435 -0.0001

ILE 435 LEU 436 0.0447

LEU 436 GLY 437 -0.0002

GLY 437 ASP 438 -0.0109

ASP 438 VAL 439 -0.0001

VAL 439 LEU 440 0.0683

LEU 440 LEU 441 -0.0000

LEU 441 ALA 442 -0.0095

ALA 442 HIS 443 -0.0002

HIS 443 PHE 444 0.0887

PHE 444 SER 445 0.0001

SER 445 LYS 446 0.0780

LYS 446 GLN 447 0.0001

GLN 447 SER 448 -0.0435

SER 448 MET 449 0.0001

MET 449 ILE 450 0.0537

ILE 450 GLU 451 0.0004

GLU 451 THR 452 -0.0300

THR 452 TYR 453 -0.0001

TYR 453 ILE 454 -0.0084

ILE 454 SER 455 0.0003

SER 455 PHE 456 -0.0040

PHE 456 VAL 457 -0.0002

VAL 457 ASP 458 0.0160

ASP 458 ASN 459 -0.0001

ASN 459 PHE 460 -0.0262

PHE 460 LYS 461 -0.0001

LYS 461 PHE 462 0.0591

PHE 462 ALA 463 0.0005

ALA 463 LYS 464 -0.0122

LYS 464 ALA 465 -0.0001

ALA 465 SER 466 -0.0910

SER 466 ILE 467 0.0001

ILE 467 ILE 468 0.0471

ILE 468 GLN 469 -0.0005

GLN 469 ALA 470 -0.0645

ALA 470 ARG 471 0.0001

ARG 471 GLN 472 0.0118

GLN 472 LYS 473 0.0002

LYS 473 HIS 474 -0.0090

HIS 474 ALA 475 -0.0002

ALA 475 PHE 476 -0.0024

PHE 476 GLU 477 -0.0002

GLU 477 LYS 478 0.0047

LYS 478 TYR 479 -0.0003

TYR 479 TYR 480 -0.0369

TYR 480 ASN 481 -0.0002

ASN 481 ARG 482 -0.0200

ARG 482 CYS 483 0.0002

CYS 483 CYS 484 -0.0170

CYS 484 ARG 485 -0.0002

ARG 485 ASP 486 0.0017

ASP 486 HIS 487 0.0001

HIS 487 PRO 488 -0.0111

PRO 488 ASN 489 0.0004

ASN 489 LYS 490 -0.0108

LYS 490 LEU 491 0.0004

LEU 491 ASP 492 0.0521

ASP 492 LEU 493 -0.0000

LEU 493 ASP 494 -0.0325

ASP 494 SER 495 -0.0004

SER 495 LEU 496 0.0288

LEU 496 LEU 497 0.0002

LEU 497 ILE 498 -0.0409

ILE 498 SER 499 0.0002

SER 499 PRO 500 -0.0342

PRO 500 ILE 501 0.0002

ILE 501 GLN 502 -0.0023

GLN 502 ARG 503 0.0000

ARG 503 VAL 504 -0.0146

VAL 504 PRO 505 0.0003

PRO 505 ARG 506 0.0235

ARG 506 TYR 507 0.0002

TYR 507 GLU 508 0.0136

GLU 508 LEU 509 0.0001

LEU 509 ILE 510 0.0179

ILE 510 VAL 511 -0.0000

VAL 511 LYS 512 0.0054

LYS 512 GLN 513 -0.0000

GLN 513 MET 514 -0.0160

MET 514 LEU 515 0.0001

LEU 515 LYS 516 0.0334

LYS 516 HIS 517 0.0002

HIS 517 THR 518 -0.0335

THR 518 PRO 519 -0.0003

PRO 519 VAL 520 0.0376

VAL 520 GLU 521 0.0002

GLU 521 HIS 522 -0.0191

HIS 522 GLU 523 0.0001

GLU 523 ASP 524 -0.0135

ASP 524 ARG 525 0.0003

ARG 525 GLU 526 0.0041

GLU 526 ARG 527 0.0001

ARG 527 LEU 528 0.0082

LEU 528 LEU 529 0.0000

LEU 529 ARG 530 0.0010

ARG 530 ALA 531 -0.0003

ALA 531 GLN 532 0.0123

GLN 532 ARG 533 -0.0006

ARG 533 HIS 534 -0.0274

HIS 534 ILE 535 0.0003

ILE 535 HIS 536 0.0231

HIS 536 CYS 537 0.0002

CYS 537 LEU 538 0.0007

LEU 538 ALA 539 0.0001

ALA 539 VAL 540 0.0165

VAL 540 ALA 541 -0.0002

ALA 541 ILE 542 -0.0197

ILE 542 ASN 543 0.0001

ASN 543 GLN 544 -0.0097

GLN 544 HIS 545 0.0000

HIS 545 LYS 546 -0.0191

LYS 546 ASP 547 0.0003

ASP 547 GLY 548 -0.0374

GLY 548 SER 549 -0.0003

SER 549 GLU 550 -0.0285

GLU 550 GLN 551 -0.0000

GLN 551 MET 552 0.0055

MET 552 GLU 553 0.0000

GLU 553 GLN 554 0.0044

GLN 554 ARG 555 0.0002

ARG 555 LEU 556 -0.0268

LEU 556 ARG 557 -0.0003

ARG 557 GLU 558 0.0728

GLU 558 ILE 559 -0.0003

ILE 559 GLU 560 -0.0383

GLU 560 ALA 561 -0.0003

ALA 561 ILE 562 -0.0289

ILE 562 VAL 563 -0.0002

VAL 563 ASP 564 0.0097

ASP 564 GLY 565 0.0002

GLY 565 LEU 566 -0.0162

LEU 566 ASP 567 0.0000

ASP 567 ASP 568 0.0133

ASP 568 LEU 569 -0.0002

LEU 569 VAL 570 -0.0255

VAL 570 THR 571 0.0001

THR 571 LYS 572 0.0151

LYS 572 ASP 573 0.0001

ASP 573 ARG 574 -0.0089

ARG 574 THR 575 -0.0003

THR 575 LEU 576 -0.0133

LEU 576 LEU 577 -0.0003

LEU 577 ARG 578 0.0027

ARG 578 HIS 579 0.0001

HIS 579 ASP 580 -0.0010

ASP 580 ILE 581 -0.0001

ILE 581 ILE 582 -0.0140

ILE 582 THR 583 -0.0002

THR 583 LEU 584 -0.0078

LEU 584 LYS 585 0.0002

LYS 585 GLY 586 0.0020

GLY 586 THR 587 -0.0000

THR 587 ASP 588 -0.0041

ASP 588 ARG 589 -0.0002

ARG 589 GLU 590 -0.0180

GLU 590 ARG 591 -0.0000

ARG 591 CYS 592 -0.0097

CYS 592 ILE 593 0.0005

ILE 593 PHE 594 0.0014

PHE 594 MET 595 0.0002

MET 595 LEU 596 0.0036

LEU 596 SER 597 -0.0001

SER 597 ASP 598 -0.0071

ASP 598 LEU 599 -0.0003

LEU 599 LEU 600 0.0133

LEU 600 LEU 601 -0.0001

LEU 601 VAL 602 0.0062

VAL 602 THR 603 0.0001

THR 603 SER 604 -0.0048

SER 604 VAL 605 0.0001

VAL 605 LYS 606 0.0062

LYS 606 LYS 607 0.0004

LYS 607 LYS 608 -0.0097

LYS 608 PRO 609 -0.0003

PRO 609 LYS 610 0.0085

LYS 610 VAL 611 -0.0000

VAL 611 LEU 612 -0.0005

LEU 612 TYR 613 -0.0003

TYR 613 SER 614 0.0040

SER 614 LYS 615 -0.0001

LYS 615 MET 616 0.0148

MET 616 SER 617 0.0002

SER 617 SER 618 -0.0046

SER 618 GLN 619 -0.0003

GLN 619 SER 620 0.0181

SER 620 MET 621 0.0005

MET 621 GLY 622 0.0139

GLY 622 PHE 623 0.0003

PHE 623 LEU 624 0.0115

LEU 624 GLU 625 0.0001

GLU 625 GLY 626 0.0069

GLY 626 ASN 627 -0.0001

ASN 627 ARG 628 -0.0017

ARG 628 PHE 629 -0.0002

PHE 629 LYS 630 0.0046

LYS 630 LEU 631 0.0003

LEU 631 LEU 632 -0.0009

LEU 632 PHE 633 -0.0002

PHE 633 LYS 634 -0.0053

LYS 634 VAL 635 -0.0002

VAL 635 ALA 636 0.0024

ALA 636 LEU 637 -0.0004

LEU 637 GLU 638 0.0037

GLU 638 ASP 639 0.0002

ASP 639 VAL 640 -0.0013

VAL 640 GLN 641 0.0002

GLN 641 ILE 642 -0.0016

ILE 642 SER 643 0.0001

SER 643 LYS 644 -0.0038

LYS 644 ASP 645 0.0002

ASP 645 THR 646 -0.0022

THR 646 LEU 647 0.0003

LEU 647 SER 648 0.0052

SER 648 GLN 649 -0.0001

GLN 649 LEU 650 0.0037

LEU 650 GLU 651 0.0001

GLU 651 GLU 652 0.0023

GLU 652 VAL 653 -0.0004

VAL 653 GLU 654 0.0020

GLU 654 ARG 655 0.0000

ARG 655 LYS 656 -0.0098

LYS 656 LEU 657 0.0001

LEU 657 GLU 658 -0.0169

GLU 658 SER 659 -0.0001

SER 659 SER 660 -0.0101

SER 660 ARG 661 -0.0005

ARG 661 GLU 662 -0.0035

GLU 662 ASP 663 0.0001

ASP 663 ASP 664 -0.0035

ASP 664 ARG 665 0.0004

ARG 665 VAL 666 0.0086

VAL 666 LEU 667 -0.0001

LEU 667 LYS 668 -0.0052

LYS 668 LYS 669 0.0003

LYS 669 MET 670 -0.0056

MET 670 SER 671 -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: April 8th, 2025.

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

*** ***

CA strain for 2504102047043794046

--- normal mode 10 ---

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

* *