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

* arojo@cua.uam.mx *

CA strain for 2504102030223723091

--- normal mode 7 ---

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 -0.0001

ARG 348 ALA 349 0.0018

ALA 349 SER 350 -0.0000

SER 350 LEU 351 -0.0028

LEU 351 ARG 352 0.0001

ARG 352 ARG 353 0.0044

ARG 353 HIS 354 0.0000

HIS 354 TYR 355 -0.0030

TYR 355 SER 356 0.0001

SER 356 VAL 357 0.0064

VAL 357 ARG 358 -0.0001

ARG 358 HIS 359 -0.0005

HIS 359 LEU 360 -0.0001

LEU 360 ALA 361 0.0042

ALA 361 ALA 362 -0.0000

ALA 362 ARG 363 -0.0000

ARG 363 GLU 364 -0.0002

GLU 364 LEU 365 0.0020

LEU 365 LEU 366 -0.0000

LEU 366 ASP 367 0.0012

ASP 367 THR 368 -0.0002

THR 368 GLU 369 -0.0036

GLU 369 LYS 370 -0.0004

LYS 370 SER 371 0.0146

SER 371 PHE 372 0.0000

PHE 372 VAL 373 -0.0007

VAL 373 GLU 374 -0.0001

GLU 374 GLY 375 0.0106

GLY 375 LEU 376 0.0000

LEU 376 GLU 377 0.0024

GLU 377 PHE 378 -0.0004

PHE 378 LEU 379 -0.0054

LEU 379 VAL 380 -0.0000

VAL 380 THR 381 0.0089

THR 381 LYS 382 0.0003

LYS 382 TYR 383 -0.0022

TYR 383 MET 384 -0.0004

MET 384 ARG 385 0.0049

ARG 385 PRO 386 -0.0002

PRO 386 LEU 387 -0.0053

LEU 387 ARG 388 -0.0002

ARG 388 GLN 389 -0.0010

GLN 389 PRO 390 0.0001

PRO 390 LEU 391 0.0002

LEU 391 GLU 392 0.0003

GLU 392 CYS 393 -0.0015

CYS 393 THR 394 0.0000

THR 394 LEU 395 -0.0016

LEU 395 ILE 396 0.0003

ILE 396 GLU 397 0.0017

GLU 397 ALA 398 -0.0001

ALA 398 SER 399 0.0051

SER 399 LEU 400 0.0001

LEU 400 VAL 401 -0.0015

VAL 401 ASP 402 0.0002

ASP 402 LYS 403 -0.0301

LYS 403 ILE 404 0.0001

ILE 404 PHE 405 -0.0074

PHE 405 TYR 406 0.0002

TYR 406 ARG 407 -0.0236

ARG 407 ILE 408 -0.0001

ILE 408 PRO 409 -0.0078

PRO 409 GLU 410 0.0001

GLU 410 ILE 411 -0.0041

ILE 411 LEU 412 -0.0002

LEU 412 ALA 413 0.0051

ALA 413 HIS 414 -0.0001

HIS 414 HIS 415 -0.0053

HIS 415 GLN 416 -0.0001

GLN 416 VAL 417 0.0175

VAL 417 LEU 418 -0.0001

LEU 418 LEU 419 0.0058

LEU 419 THR 420 -0.0000

THR 420 THR 421 0.0095

THR 421 LEU 422 -0.0001

LEU 422 SER 423 -0.0016

SER 423 GLN 424 0.0002

GLN 424 ARG 425 0.0056

ARG 425 ILE 426 -0.0003

ILE 426 ASP 427 -0.0029

ASP 427 GLN 428 -0.0000

GLN 428 TRP 429 -0.0086

TRP 429 HIS 430 -0.0000

HIS 430 LYS 431 -0.0110

LYS 431 ASP 432 0.0002

ASP 432 ALA 433 0.0013

ALA 433 ILE 434 0.0001

ILE 434 LEU 435 -0.0009

LEU 435 GLY 436 0.0003

GLY 436 ASP 437 0.0003

ASP 437 VAL 438 0.0001

VAL 438 LEU 439 0.0106

LEU 439 LEU 440 0.0002

LEU 440 ALA 441 0.0094

ALA 441 HIS 442 0.0002

HIS 442 PHE 443 0.0149

PHE 443 SER 444 -0.0002

SER 444 LYS 445 0.0073

LYS 445 GLN 446 0.0002

GLN 446 SER 447 -0.0360

SER 447 MET 448 -0.0001

MET 448 ILE 449 -0.0107

ILE 449 GLU 450 0.0003

GLU 450 THR 451 0.0393

THR 451 TYR 452 0.0001

TYR 452 ILE 453 0.0024

ILE 453 SER 454 0.0001

SER 454 PHE 455 0.0103

PHE 455 VAL 456 0.0001

VAL 456 ASP 457 0.0244

ASP 457 ASN 458 0.0000

ASN 458 PHE 459 0.0086

PHE 459 LYS 460 -0.0001

LYS 460 PHE 461 0.0039

PHE 461 ALA 462 0.0001

ALA 462 LYS 463 0.0027

LYS 463 ALA 464 -0.0003

ALA 464 SER 465 -0.0046

SER 465 ILE 466 -0.0003

ILE 466 ILE 467 0.0028

ILE 467 GLN 468 -0.0000

GLN 468 ALA 469 0.0015

ALA 469 ARG 470 0.0002

ARG 470 GLN 471 0.0031

GLN 471 LYS 472 -0.0000

LYS 472 HIS 473 -0.0019

HIS 473 ALA 474 0.0000

ALA 474 PHE 475 0.0026

PHE 475 GLU 476 0.0003

GLU 476 LYS 477 0.0009

LYS 477 TYR 478 -0.0003

TYR 478 TYR 479 -0.0026

TYR 479 ASN 480 -0.0003

ASN 480 ARG 481 -0.0038

ARG 481 CYS 482 0.0004

CYS 482 CYS 483 -0.0013

CYS 483 ARG 484 0.0002

ARG 484 ASP 485 0.0021

ASP 485 HIS 486 -0.0001

HIS 486 PRO 487 -0.0015

PRO 487 ASN 488 -0.0000

ASN 488 LYS 489 -0.0013

LYS 489 LEU 490 0.0003

LEU 490 ASP 491 0.0071

ASP 491 LEU 492 -0.0002

LEU 492 ASP 493 -0.0016

ASP 493 SER 494 -0.0003

SER 494 LEU 495 0.0065

LEU 495 LEU 496 0.0004

LEU 496 ILE 497 0.0038

ILE 497 SER 498 0.0003

SER 498 PRO 499 -0.0133

PRO 499 ILE 500 -0.0000

ILE 500 GLN 501 0.0360

GLN 501 ARG 502 0.0002

ARG 502 VAL 503 -0.0160

VAL 503 PRO 504 0.0002

PRO 504 ARG 505 0.0221

ARG 505 TYR 506 0.0000

TYR 506 GLU 507 -0.0018

GLU 507 LEU 508 0.0001

LEU 508 ILE 509 0.0055

ILE 509 VAL 510 -0.0003

VAL 510 LYS 511 -0.0066

LYS 511 GLN 512 0.0003

GLN 512 MET 513 0.0028

MET 513 LEU 514 0.0003

LEU 514 LYS 515 -0.0016

LYS 515 HIS 516 0.0003

HIS 516 THR 517 0.0001

THR 517 PRO 518 -0.0001

PRO 518 VAL 519 0.0038

VAL 519 GLU 520 -0.0000

GLU 520 HIS 521 -0.0002

HIS 521 GLU 522 0.0001

GLU 522 ASP 523 -0.0007

ASP 523 ARG 524 0.0002

ARG 524 GLU 525 -0.0103

GLU 525 ARG 526 -0.0002

ARG 526 LEU 527 0.0004

LEU 527 LEU 528 0.0000

LEU 528 ARG 529 0.0027

ARG 529 ALA 530 0.0003

ALA 530 GLN 531 -0.0015

GLN 531 ARG 532 -0.0005

ARG 532 HIS 533 0.0015

HIS 533 ILE 534 -0.0003

ILE 534 HIS 535 -0.0016

HIS 535 CYS 536 -0.0001

CYS 536 LEU 537 0.0053

LEU 537 ALA 538 0.0002

ALA 538 VAL 539 -0.0006

VAL 539 ALA 540 0.0001

ALA 540 ILE 541 0.0138

ILE 541 ASN 542 -0.0001

ASN 542 GLN 543 0.0176

GLN 543 HIS 544 -0.0000

HIS 544 LYS 545 0.0053

LYS 545 ASP 546 -0.0000

ASP 546 GLY 547 -0.0036

GLY 547 SER 548 -0.0002

SER 548 GLU 549 -0.0063

GLU 549 GLN 550 -0.0003

GLN 550 MET 551 -0.0228

MET 551 GLU 552 -0.0002

GLU 552 GLN 553 0.0215

GLN 553 ARG 554 -0.0003

ARG 554 LEU 555 -0.0029

LEU 555 ARG 556 -0.0001

ARG 556 GLU 557 -0.0437

GLU 557 ILE 558 0.0001

ILE 558 GLU 559 0.0371

GLU 559 ALA 560 -0.0002

ALA 560 ILE 561 -0.0623

ILE 561 VAL 562 0.0001

VAL 562 ASP 563 0.0186

ASP 563 GLY 564 0.0001

GLY 564 LEU 565 0.0043

LEU 565 ASP 566 0.0001

ASP 566 ASP 567 -0.0115

ASP 567 LEU 568 0.0001

LEU 568 VAL 569 -0.0053

VAL 569 THR 570 -0.0001

THR 570 LYS 571 -0.0052

LYS 571 ASP 572 0.0000

ASP 572 ARG 573 -0.0773

ARG 573 THR 574 0.0002

THR 574 LEU 575 0.0281

LEU 575 LEU 576 0.0001

LEU 576 ARG 577 -0.0007

ARG 577 HIS 578 0.0000

HIS 578 ASP 579 0.0383

ASP 579 ILE 580 0.0002

ILE 580 ILE 581 0.0235

ILE 581 THR 582 -0.0001

THR 582 LEU 583 0.0008

LEU 583 LYS 584 -0.0002

LYS 584 GLY 585 -0.0020

GLY 585 THR 586 0.0002

THR 586 ASP 587 0.0040

ASP 587 ARG 588 -0.0000

ARG 588 GLU 589 0.0008

GLU 589 ARG 590 -0.0001

ARG 590 CYS 591 0.0190

CYS 591 ILE 592 0.0003

ILE 592 PHE 593 -0.0002

PHE 593 MET 594 -0.0001

MET 594 LEU 595 0.0025

LEU 595 SER 596 -0.0002

SER 596 ASP 597 -0.0018

ASP 597 LEU 598 0.0000

LEU 598 LEU 599 -0.0008

LEU 599 LEU 600 -0.0002

LEU 600 VAL 601 -0.0088

VAL 601 THR 602 0.0000

THR 602 SER 603 0.0002

SER 603 VAL 604 0.0002

VAL 604 LYS 605 -0.0081

LYS 605 LYS 606 -0.0002

LYS 606 LYS 607 -0.0170

LYS 607 PRO 608 0.0001

PRO 608 LYS 609 -0.0033

LYS 609 VAL 610 0.0001

VAL 610 LEU 611 0.0112

LEU 611 TYR 612 -0.0000

TYR 612 SER 613 -0.0036

SER 613 LYS 614 0.0001

LYS 614 MET 615 0.0034

MET 615 SER 616 0.0001

SER 616 SER 617 0.0032

SER 617 GLN 618 -0.0002

GLN 618 SER 619 0.0048

SER 619 MET 620 -0.0000

MET 620 GLY 621 0.0062

GLY 621 PHE 622 0.0001

PHE 622 LEU 623 0.0051

LEU 623 GLU 624 0.0000

GLU 624 GLY 625 0.0025

GLY 625 ASN 626 -0.0003

ASN 626 ARG 627 0.0041

ARG 627 PHE 628 0.0001

PHE 628 LYS 629 -0.0013

LYS 629 LEU 630 0.0002

LEU 630 LEU 631 0.0017

LEU 631 PHE 632 -0.0003

PHE 632 LYS 633 0.0023

LYS 633 VAL 634 -0.0000

VAL 634 ALA 635 0.0056

ALA 635 LEU 636 0.0002

LEU 636 GLU 637 -0.0010

GLU 637 ASP 638 0.0001

ASP 638 VAL 639 0.0012

VAL 639 GLN 640 -0.0003

GLN 640 ILE 641 0.0002

ILE 641 SER 642 -0.0001

SER 642 LYS 643 0.0039

LYS 643 ASP 644 0.0003

ASP 644 THR 645 0.0008

THR 645 LEU 646 -0.0000

LEU 646 SER 647 -0.0005

SER 647 GLN 648 -0.0001

GLN 648 LEU 649 0.0022

LEU 649 GLU 650 0.0001

GLU 650 GLU 651 -0.0068

GLU 651 VAL 652 0.0002

VAL 652 GLU 653 0.0043

GLU 653 ARG 654 -0.0004

ARG 654 LYS 655 0.0028

LYS 655 LEU 656 0.0001

LEU 656 GLU 657 0.0159

GLU 657 SER 658 0.0003

SER 658 SER 659 0.0003

SER 659 ARG 660 0.0001

ARG 660 GLU 661 0.0056

GLU 661 ASP 662 -0.0004

ASP 662 ASP 663 -0.0063

ASP 663 ARG 664 0.0002

ARG 664 VAL 665 0.0078

VAL 665 LEU 666 0.0001

LEU 666 LYS 667 -0.0022

LYS 667 LYS 668 0.0002

LYS 668 MET 669 -0.0015

MET 669 SER 670 -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.

*** arojo@cua.uam.mx ***

CA strain for 2504102030223723091

--- normal mode 7 ---

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

* arojo@cua.uam.mx *