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

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CA strain for 2504102034353735962

--- 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
SER 347 ARG 348 -0.0000

ARG 348 ALA 349 -0.0007

ALA 349 SER 350 0.0000

SER 350 LEU 351 -0.0012

LEU 351 ARG 352 0.0001

ARG 352 ARG 353 -0.0053

ARG 353 HIS 354 0.0005

HIS 354 TYR 355 -0.0066

TYR 355 SER 356 -0.0002

SER 356 VAL 357 0.0035

VAL 357 ARG 358 0.0001

ARG 358 HIS 359 -0.0038

HIS 359 LEU 360 0.0001

LEU 360 ALA 361 0.0024

ALA 361 ALA 362 -0.0001

ALA 362 ARG 363 -0.0039

ARG 363 GLU 364 0.0000

GLU 364 LEU 365 -0.0023

LEU 365 LEU 366 -0.0003

LEU 366 ASP 367 0.0038

ASP 367 THR 368 -0.0002

THR 368 GLU 369 0.0028

GLU 369 LYS 370 -0.0002

LYS 370 SER 371 -0.0189

SER 371 PHE 372 0.0001

PHE 372 VAL 373 0.0082

VAL 373 GLU 374 -0.0002

GLU 374 GLY 375 -0.0106

GLY 375 LEU 376 -0.0000

LEU 376 GLU 377 0.0052

GLU 377 PHE 378 0.0001

PHE 378 LEU 379 -0.0087

LEU 379 VAL 380 0.0005

VAL 380 THR 381 0.0065

THR 381 LYS 382 -0.0002

LYS 382 TYR 383 -0.0047

TYR 383 MET 384 -0.0001

MET 384 ARG 385 0.0033

ARG 385 PRO 386 0.0001

PRO 386 LEU 387 -0.0013

LEU 387 ARG 388 0.0001

ARG 388 GLN 389 -0.0001

GLN 389 PRO 390 -0.0001

PRO 390 LEU 391 -0.0007

LEU 391 GLU 392 0.0004

GLU 392 CYS 393 -0.0048

CYS 393 THR 394 -0.0001

THR 394 LEU 395 0.0040

LEU 395 ILE 396 0.0000

ILE 396 GLU 397 -0.0033

GLU 397 ALA 398 0.0000

ALA 398 SER 399 -0.0003

SER 399 LEU 400 -0.0004

LEU 400 VAL 401 -0.0077

VAL 401 ASP 402 -0.0003

ASP 402 LYS 403 0.0004

LYS 403 ILE 404 0.0001

ILE 404 PHE 405 -0.0155

PHE 405 TYR 406 -0.0003

TYR 406 ARG 407 -0.0163

ARG 407 ILE 408 -0.0000

ILE 408 PRO 409 -0.0021

PRO 409 GLU 410 0.0001

GLU 410 ILE 411 0.0005

ILE 411 LEU 412 0.0000

LEU 412 ALA 413 -0.0005

ALA 413 HIS 414 0.0001

HIS 414 HIS 415 0.0042

HIS 415 GLN 416 -0.0000

GLN 416 VAL 417 0.0023

VAL 417 LEU 418 -0.0002

LEU 418 LEU 419 0.0072

LEU 419 THR 420 0.0003

THR 420 THR 421 0.0050

THR 421 LEU 422 0.0001

LEU 422 SER 423 0.0040

SER 423 GLN 424 -0.0001

GLN 424 ARG 425 -0.0044

ARG 425 ILE 426 -0.0000

ILE 426 ASP 427 0.0109

ASP 427 GLN 428 0.0003

GLN 428 TRP 429 -0.0018

TRP 429 HIS 430 -0.0003

HIS 430 LYS 431 -0.0011

LYS 431 ASP 432 -0.0001

ASP 432 ALA 433 -0.0074

ALA 433 ILE 434 -0.0003

ILE 434 LEU 435 -0.0063

LEU 435 GLY 436 -0.0001

GLY 436 ASP 437 -0.0034

ASP 437 VAL 438 -0.0002

VAL 438 LEU 439 0.0292

LEU 439 LEU 440 -0.0002

LEU 440 ALA 441 -0.0243

ALA 441 HIS 442 0.0001

HIS 442 PHE 443 0.0534

PHE 443 SER 444 0.0003

SER 444 LYS 445 -0.0019

LYS 445 GLN 446 -0.0002

GLN 446 SER 447 0.0060

SER 447 MET 448 -0.0002

MET 448 ILE 449 -0.0151

ILE 449 GLU 450 -0.0003

GLU 450 THR 451 -0.0042

THR 451 TYR 452 0.0000

TYR 452 ILE 453 -0.0176

ILE 453 SER 454 -0.0000

SER 454 PHE 455 0.0002

PHE 455 VAL 456 -0.0002

VAL 456 ASP 457 -0.0544

ASP 457 ASN 458 -0.0002

ASN 458 PHE 459 -0.0490

PHE 459 LYS 460 0.0003

LYS 460 PHE 461 0.0101

PHE 461 ALA 462 0.0001

ALA 462 LYS 463 -0.0067

LYS 463 ALA 464 0.0003

ALA 464 SER 465 0.0236

SER 465 ILE 466 -0.0004

ILE 466 ILE 467 -0.0012

ILE 467 GLN 468 0.0002

GLN 468 ALA 469 0.0010

ALA 469 ARG 470 -0.0002

ARG 470 GLN 471 0.0100

GLN 471 LYS 472 -0.0003

LYS 472 HIS 473 0.0040

HIS 473 ALA 474 -0.0001

ALA 474 PHE 475 0.0116

PHE 475 GLU 476 -0.0003

GLU 476 LYS 477 0.0149

LYS 477 TYR 478 -0.0001

TYR 478 TYR 479 0.0003

TYR 479 ASN 480 0.0003

ASN 480 ARG 481 0.0056

ARG 481 CYS 482 -0.0002

CYS 482 CYS 483 0.0000

CYS 483 ARG 484 0.0000

ARG 484 ASP 485 0.0032

ASP 485 HIS 486 -0.0000

HIS 486 PRO 487 0.0014

PRO 487 ASN 488 0.0001

ASN 488 LYS 489 -0.0018

LYS 489 LEU 490 -0.0001

LEU 490 ASP 491 -0.0110

ASP 491 LEU 492 -0.0002

LEU 492 ASP 493 0.0017

ASP 493 SER 494 0.0005

SER 494 LEU 495 -0.0151

LEU 495 LEU 496 0.0002

LEU 496 ILE 497 -0.0162

ILE 497 SER 498 -0.0001

SER 498 PRO 499 -0.0205

PRO 499 ILE 500 0.0005

ILE 500 GLN 501 -0.0183

GLN 501 ARG 502 0.0000

ARG 502 VAL 503 -0.0059

VAL 503 PRO 504 -0.0001

PRO 504 ARG 505 0.0028

ARG 505 TYR 506 -0.0001

TYR 506 GLU 507 -0.0048

GLU 507 LEU 508 -0.0001

LEU 508 ILE 509 0.0037

ILE 509 VAL 510 -0.0001

VAL 510 LYS 511 0.0063

LYS 511 GLN 512 -0.0000

GLN 512 MET 513 0.0031

MET 513 LEU 514 0.0002

LEU 514 LYS 515 0.0063

LYS 515 HIS 516 -0.0001

HIS 516 THR 517 -0.0093

THR 517 PRO 518 0.0000

PRO 518 VAL 519 0.0048

VAL 519 GLU 520 0.0000

GLU 520 HIS 521 -0.0035

HIS 521 GLU 522 0.0000

GLU 522 ASP 523 -0.0008

ASP 523 ARG 524 0.0000

ARG 524 GLU 525 -0.0005

GLU 525 ARG 526 0.0000

ARG 526 LEU 527 0.0160

LEU 527 LEU 528 -0.0002

LEU 528 ARG 529 0.0168

ARG 529 ALA 530 -0.0001

ALA 530 GLN 531 -0.0047

GLN 531 ARG 532 0.0001

ARG 532 HIS 533 0.0074

HIS 533 ILE 534 -0.0002

ILE 534 HIS 535 0.0073

HIS 535 CYS 536 0.0002

CYS 536 LEU 537 -0.0219

LEU 537 ALA 538 -0.0001

ALA 538 VAL 539 0.0052

VAL 539 ALA 540 0.0001

ALA 540 ILE 541 -0.0060

ILE 541 ASN 542 -0.0002

ASN 542 GLN 543 -0.0067

GLN 543 HIS 544 0.0002

HIS 544 LYS 545 0.0025

LYS 545 ASP 546 0.0000

ASP 546 GLY 547 -0.0124

GLY 547 SER 548 0.0002

SER 548 GLU 549 0.0159

GLU 549 GLN 550 0.0000

GLN 550 MET 551 0.0254

MET 551 GLU 552 0.0000

GLU 552 GLN 553 0.0677

GLN 553 ARG 554 -0.0002

ARG 554 LEU 555 0.0485

LEU 555 ARG 556 0.0000

ARG 556 GLU 557 -0.0160

GLU 557 ILE 558 -0.0004

ILE 558 GLU 559 0.0236

GLU 559 ALA 560 0.0001

ALA 560 ILE 561 -0.0235

ILE 561 VAL 562 -0.0002

VAL 562 ASP 563 -0.0041

ASP 563 GLY 564 -0.0001

GLY 564 LEU 565 -0.1303

LEU 565 ASP 566 -0.0001

ASP 566 ASP 567 0.0331

ASP 567 LEU 568 0.0003

LEU 568 VAL 569 -0.0555

VAL 569 THR 570 -0.0003

THR 570 LYS 571 -0.0383

LYS 571 ASP 572 -0.0002

ASP 572 ARG 573 -0.0027

ARG 573 THR 574 -0.0003

THR 574 LEU 575 0.0119

LEU 575 LEU 576 -0.0003

LEU 576 ARG 577 -0.0019

ARG 577 HIS 578 -0.0000

HIS 578 ASP 579 0.0009

ASP 579 ILE 580 0.0002

ILE 580 ILE 581 0.0258

ILE 581 THR 582 0.0002

THR 582 LEU 583 0.0002

LEU 583 LYS 584 -0.0001

LYS 584 GLY 585 0.0321

GLY 585 THR 586 -0.0002

THR 586 ASP 587 0.0097

ASP 587 ARG 588 -0.0001

ARG 588 GLU 589 -0.0123

GLU 589 ARG 590 0.0001

ARG 590 CYS 591 -0.0006

CYS 591 ILE 592 0.0003

ILE 592 PHE 593 -0.0221

PHE 593 MET 594 -0.0002

MET 594 LEU 595 -0.0027

LEU 595 SER 596 0.0000

SER 596 ASP 597 -0.0293

ASP 597 LEU 598 -0.0000

LEU 598 LEU 599 -0.0185

LEU 599 LEU 600 -0.0001

LEU 600 VAL 601 0.0123

VAL 601 THR 602 0.0001

THR 602 SER 603 -0.0220

SER 603 VAL 604 -0.0001

VAL 604 LYS 605 -0.0017

LYS 605 LYS 606 0.0002

LYS 606 LYS 607 0.0040

LYS 607 PRO 608 0.0000

PRO 608 LYS 609 0.0058

LYS 609 VAL 610 -0.0003

VAL 610 LEU 611 -0.0168

LEU 611 TYR 612 -0.0000

TYR 612 SER 613 -0.0086

SER 613 LYS 614 0.0001

LYS 614 MET 615 0.0281

MET 615 SER 616 0.0003

SER 616 SER 617 -0.0714

SER 617 GLN 618 0.0003

GLN 618 SER 619 -0.0300

SER 619 MET 620 0.0001

MET 620 GLY 621 -0.0975

GLY 621 PHE 622 0.0004

PHE 622 LEU 623 -0.0512

LEU 623 GLU 624 -0.0003

GLU 624 GLY 625 -0.0230

GLY 625 ASN 626 0.0004

ASN 626 ARG 627 0.0041

ARG 627 PHE 628 -0.0005

PHE 628 LYS 629 -0.0004

LYS 629 LEU 630 0.0002

LEU 630 LEU 631 0.0025

LEU 631 PHE 632 0.0004

PHE 632 LYS 633 0.0033

LYS 633 VAL 634 -0.0003

VAL 634 ALA 635 0.0087

ALA 635 LEU 636 0.0001

LEU 636 GLU 637 0.0033

GLU 637 ASP 638 -0.0001

ASP 638 VAL 639 0.0070

VAL 639 GLN 640 0.0001

GLN 640 ILE 641 0.0095

ILE 641 SER 642 -0.0001

SER 642 LYS 643 -0.0008

LYS 643 ASP 644 0.0001

ASP 644 THR 645 -0.0026

THR 645 LEU 646 0.0000

LEU 646 SER 647 0.0050

SER 647 GLN 648 0.0003

GLN 648 LEU 649 -0.0089

LEU 649 GLU 650 -0.0004

GLU 650 GLU 651 0.0041

GLU 651 VAL 652 0.0001

VAL 652 GLU 653 0.0024

GLU 653 ARG 654 0.0002

ARG 654 LYS 655 0.0049

LYS 655 LEU 656 0.0002

LEU 656 GLU 657 0.0014

GLU 657 SER 658 0.0000

SER 658 SER 659 -0.0120

SER 659 ARG 660 0.0000

ARG 660 GLU 661 0.0083

GLU 661 ASP 662 0.0003

ASP 662 ASP 663 -0.0001

ASP 663 ARG 664 -0.0001

ARG 664 VAL 665 0.0038

VAL 665 LEU 666 0.0001

LEU 666 LYS 667 -0.0008

LYS 667 LYS 668 0.0002

LYS 668 MET 669 0.0148

MET 669 SER 670 -0.0002

SER 670 GLN 671 0.0060

GLN 671 LEU 672 0.0002

LEU 672 CYS 673 0.0259

CYS 673 SER 674 -0.0001

SER 674 LEU 675 0.0008

LEU 675 LEU 676 -0.0002

LEU 676 LYS 677 -0.0013

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.

*** iva ***

CA strain for 2504102034353735962

--- normal mode 9 ---

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

* iva *