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

* *

CA strain for 2504102047043794046

--- 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 348 ARG 349 0.0001

ARG 349 ALA 350 0.0008

ALA 350 SER 351 0.0001

SER 351 LEU 352 -0.0028

LEU 352 ARG 353 -0.0001

ARG 353 ARG 354 0.0079

ARG 354 HIS 355 -0.0001

HIS 355 TYR 356 -0.0055

TYR 356 SER 357 0.0004

SER 357 VAL 358 0.0051

VAL 358 ARG 359 -0.0000

ARG 359 HIS 360 -0.0029

HIS 360 LEU 361 -0.0004

LEU 361 ALA 362 -0.0018

ALA 362 ALA 363 -0.0004

ALA 363 ARG 364 0.0015

ARG 364 GLU 365 0.0002

GLU 365 LEU 366 -0.0059

LEU 366 LEU 367 -0.0002

LEU 367 ASP 368 -0.0047

ASP 368 THR 369 -0.0001

THR 369 GLU 370 -0.0035

GLU 370 LYS 371 0.0001

LYS 371 SER 372 0.0242

SER 372 PHE 373 -0.0002

PHE 373 VAL 374 -0.0086

VAL 374 GLU 375 -0.0001

GLU 375 GLY 376 0.0214

GLY 376 LEU 377 0.0001

LEU 377 GLU 378 -0.0012

GLU 378 PHE 379 -0.0001

PHE 379 LEU 380 0.0093

LEU 380 VAL 381 0.0006

VAL 381 THR 382 -0.0110

THR 382 LYS 383 -0.0002

LYS 383 TYR 384 0.0046

TYR 384 MET 385 0.0001

MET 385 ARG 386 -0.0040

ARG 386 PRO 387 0.0003

PRO 387 LEU 388 0.0022

LEU 388 ARG 389 0.0000

ARG 389 GLN 390 -0.0007

GLN 390 PRO 391 0.0000

PRO 391 LEU 392 -0.0006

LEU 392 GLU 393 0.0003

GLU 393 CYS 394 0.0014

CYS 394 THR 395 0.0001

THR 395 LEU 396 -0.0029

LEU 396 ILE 397 0.0002

ILE 397 GLU 398 0.0003

GLU 398 ALA 399 -0.0002

ALA 399 SER 400 -0.0026

SER 400 LEU 401 0.0005

LEU 401 VAL 402 0.0031

VAL 402 ASP 403 0.0002

ASP 403 LYS 404 0.0027

LYS 404 ILE 405 -0.0002

ILE 405 PHE 406 0.0050

PHE 406 TYR 407 0.0001

TYR 407 ARG 408 0.0111

ARG 408 ILE 409 -0.0002

ILE 409 PRO 410 0.0015

PRO 410 GLU 411 -0.0002

GLU 411 ILE 412 0.0009

ILE 412 LEU 413 0.0001

LEU 413 ALA 414 -0.0000

ALA 414 HIS 415 -0.0004

HIS 415 HIS 416 -0.0113

HIS 416 GLN 417 0.0002

GLN 417 VAL 418 0.0095

VAL 418 LEU 419 0.0000

LEU 419 LEU 420 -0.0012

LEU 420 THR 421 -0.0001

THR 421 THR 422 0.0065

THR 422 LEU 423 -0.0002

LEU 423 SER 424 -0.0057

SER 424 GLN 425 0.0001

GLN 425 ARG 426 0.0172

ARG 426 ILE 427 -0.0005

ILE 427 ASP 428 -0.0129

ASP 428 GLN 429 0.0002

GLN 429 TRP 430 0.0008

TRP 430 HIS 431 -0.0002

HIS 431 LYS 432 -0.0042

LYS 432 ASP 433 -0.0000

ASP 433 ALA 434 -0.0099

ALA 434 ILE 435 -0.0002

ILE 435 LEU 436 -0.0105

LEU 436 GLY 437 -0.0001

GLY 437 ASP 438 -0.0086

ASP 438 VAL 439 -0.0001

VAL 439 LEU 440 0.0153

LEU 440 LEU 441 0.0003

LEU 441 ALA 442 0.0052

ALA 442 HIS 443 -0.0001

HIS 443 PHE 444 -0.0144

PHE 444 SER 445 -0.0006

SER 445 LYS 446 -0.0302

LYS 446 GLN 447 -0.0004

GLN 447 SER 448 0.0145

SER 448 MET 449 0.0003

MET 449 ILE 450 0.0109

ILE 450 GLU 451 0.0001

GLU 451 THR 452 0.0034

THR 452 TYR 453 -0.0003

TYR 453 ILE 454 -0.0215

ILE 454 SER 455 0.0001

SER 455 PHE 456 -0.0356

PHE 456 VAL 457 0.0004

VAL 457 ASP 458 0.0424

ASP 458 ASN 459 -0.0001

ASN 459 PHE 460 0.0242

PHE 460 LYS 461 0.0001

LYS 461 PHE 462 0.0105

PHE 462 ALA 463 0.0002

ALA 463 LYS 464 0.0005

LYS 464 ALA 465 0.0001

ALA 465 SER 466 0.0042

SER 466 ILE 467 0.0002

ILE 467 ILE 468 -0.0013

ILE 468 GLN 469 0.0003

GLN 469 ALA 470 0.0106

ALA 470 ARG 471 0.0001

ARG 471 GLN 472 -0.0129

GLN 472 LYS 473 0.0004

LYS 473 HIS 474 0.0020

HIS 474 ALA 475 -0.0001

ALA 475 PHE 476 -0.0046

PHE 476 GLU 477 -0.0002

GLU 477 LYS 478 0.0137

LYS 478 TYR 479 0.0000

TYR 479 TYR 480 -0.0041

TYR 480 ASN 481 -0.0001

ASN 481 ARG 482 0.0081

ARG 482 CYS 483 -0.0003

CYS 483 CYS 484 -0.0019

CYS 484 ARG 485 0.0003

ARG 485 ASP 486 -0.0004

ASP 486 HIS 487 -0.0001

HIS 487 PRO 488 -0.0014

PRO 488 ASN 489 -0.0000

ASN 489 LYS 490 -0.0070

LYS 490 LEU 491 0.0001

LEU 491 ASP 492 0.0084

ASP 492 LEU 493 -0.0004

LEU 493 ASP 494 0.0042

ASP 494 SER 495 -0.0001

SER 495 LEU 496 -0.0002

LEU 496 LEU 497 -0.0003

LEU 497 ILE 498 -0.0026

ILE 498 SER 499 -0.0002

SER 499 PRO 500 -0.0150

PRO 500 ILE 501 0.0003

ILE 501 GLN 502 0.0501

GLN 502 ARG 503 0.0002

ARG 503 VAL 504 -0.0318

VAL 504 PRO 505 -0.0002

PRO 505 ARG 506 0.0264

ARG 506 TYR 507 -0.0000

TYR 507 GLU 508 -0.0012

GLU 508 LEU 509 0.0001

LEU 509 ILE 510 0.0052

ILE 510 VAL 511 -0.0002

VAL 511 LYS 512 0.0030

LYS 512 GLN 513 0.0001

GLN 513 MET 514 0.0019

MET 514 LEU 515 0.0001

LEU 515 LYS 516 -0.0021

LYS 516 HIS 517 0.0002

HIS 517 THR 518 0.0045

THR 518 PRO 519 0.0001

PRO 519 VAL 520 -0.0062

VAL 520 GLU 521 -0.0002

GLU 521 HIS 522 0.0110

HIS 522 GLU 523 -0.0002

GLU 523 ASP 524 -0.0053

ASP 524 ARG 525 0.0002

ARG 525 GLU 526 0.0011

GLU 526 ARG 527 -0.0004

ARG 527 LEU 528 -0.0005

LEU 528 LEU 529 -0.0001

LEU 529 ARG 530 -0.0075

ARG 530 ALA 531 0.0001

ALA 531 GLN 532 0.0091

GLN 532 ARG 533 0.0001

ARG 533 HIS 534 0.0055

HIS 534 ILE 535 0.0000

ILE 535 HIS 536 0.0074

HIS 536 CYS 537 0.0001

CYS 537 LEU 538 0.0115

LEU 538 ALA 539 0.0002

ALA 539 VAL 540 0.0182

VAL 540 ALA 541 -0.0004

ALA 541 ILE 542 -0.0114

ILE 542 ASN 543 0.0001

ASN 543 GLN 544 -0.0212

GLN 544 HIS 545 -0.0001

HIS 545 LYS 546 -0.0042

LYS 546 ASP 547 -0.0003

ASP 547 GLY 548 -0.0491

GLY 548 SER 549 -0.0001

SER 549 GLU 550 0.0220

GLU 550 GLN 551 0.0003

GLN 551 MET 552 -0.0406

MET 552 GLU 553 0.0000

GLU 553 GLN 554 0.0455

GLN 554 ARG 555 -0.0002

ARG 555 LEU 556 -0.0312

LEU 556 ARG 557 -0.0004

ARG 557 GLU 558 0.0452

GLU 558 ILE 559 -0.0002

ILE 559 GLU 560 -0.0297

GLU 560 ALA 561 0.0002

ALA 561 ILE 562 0.0506

ILE 562 VAL 563 0.0003

VAL 563 ASP 564 0.0045

ASP 564 GLY 565 -0.0002

GLY 565 LEU 566 -0.0172

LEU 566 ASP 567 0.0000

ASP 567 ASP 568 -0.0307

ASP 568 LEU 569 0.0000

LEU 569 VAL 570 0.0047

VAL 570 THR 571 0.0002

THR 571 LYS 572 0.0079

LYS 572 ASP 573 -0.0001

ASP 573 ARG 574 -0.0704

ARG 574 THR 575 0.0001

THR 575 LEU 576 0.0146

LEU 576 LEU 577 -0.0001

LEU 577 ARG 578 -0.0223

ARG 578 HIS 579 0.0002

HIS 579 ASP 580 0.0054

ASP 580 ILE 581 0.0003

ILE 581 ILE 582 0.0289

ILE 582 THR 583 0.0001

THR 583 LEU 584 0.0063

LEU 584 LYS 585 -0.0003

LYS 585 GLY 586 -0.0120

GLY 586 THR 587 0.0003

THR 587 ASP 588 0.0127

ASP 588 ARG 589 0.0002

ARG 589 GLU 590 0.0279

GLU 590 ARG 591 0.0000

ARG 591 CYS 592 0.0277

CYS 592 ILE 593 -0.0003

ILE 593 PHE 594 -0.0076

PHE 594 MET 595 0.0005

MET 595 LEU 596 0.0199

LEU 596 SER 597 0.0001

SER 597 ASP 598 -0.0135

ASP 598 LEU 599 -0.0004

LEU 599 LEU 600 0.0006

LEU 600 LEU 601 -0.0001

LEU 601 VAL 602 -0.0275

VAL 602 THR 603 0.0000

THR 603 SER 604 0.0142

SER 604 VAL 605 -0.0001

VAL 605 LYS 606 0.0049

LYS 606 LYS 607 -0.0002

LYS 607 LYS 608 0.0232

LYS 608 PRO 609 -0.0002

PRO 609 LYS 610 -0.0121

LYS 610 VAL 611 0.0002

VAL 611 LEU 612 0.0222

LEU 612 TYR 613 -0.0002

TYR 613 SER 614 0.0551

SER 614 LYS 615 0.0000

LYS 615 MET 616 0.0730

MET 616 SER 617 0.0000

SER 617 SER 618 0.0359

SER 618 GLN 619 -0.0003

GLN 619 SER 620 0.0082

SER 620 MET 621 -0.0001

MET 621 GLY 622 0.0091

GLY 622 PHE 623 -0.0005

PHE 623 LEU 624 0.0034

LEU 624 GLU 625 -0.0001

GLU 625 GLY 626 -0.0002

GLY 626 ASN 627 -0.0002

ASN 627 ARG 628 0.0007

ARG 628 PHE 629 0.0003

PHE 629 LYS 630 0.0019

LYS 630 LEU 631 -0.0004

LEU 631 LEU 632 -0.0033

LEU 632 PHE 633 -0.0003

PHE 633 LYS 634 0.0013

LYS 634 VAL 635 -0.0001

VAL 635 ALA 636 0.0254

ALA 636 LEU 637 0.0001

LEU 637 GLU 638 0.0005

GLU 638 ASP 639 0.0002

ASP 639 VAL 640 -0.0103

VAL 640 GLN 641 -0.0002

GLN 641 ILE 642 0.0027

ILE 642 SER 643 -0.0005

SER 643 LYS 644 0.0063

LYS 644 ASP 645 -0.0002

ASP 645 THR 646 0.0022

THR 646 LEU 647 0.0002

LEU 647 SER 648 0.0016

SER 648 GLN 649 0.0002

GLN 649 LEU 650 0.0068

LEU 650 GLU 651 -0.0002

GLU 651 GLU 652 -0.0062

GLU 652 VAL 653 0.0002

VAL 653 GLU 654 0.0039

GLU 654 ARG 655 0.0005

ARG 655 LYS 656 -0.0059

LYS 656 LEU 657 -0.0004

LEU 657 GLU 658 -0.0025

GLU 658 SER 659 0.0001

SER 659 SER 660 -0.0027

SER 660 ARG 661 -0.0001

ARG 661 GLU 662 -0.0052

GLU 662 ASP 663 -0.0001

ASP 663 ASP 664 0.0016

ASP 664 ARG 665 0.0000

ARG 665 VAL 666 0.0207

VAL 666 LEU 667 -0.0001

LEU 667 LYS 668 0.0010

LYS 668 LYS 669 0.0002

LYS 669 MET 670 0.0051

MET 670 SER 671 0.0003

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 9 ---

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

* *