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

* *

CA strain for 2504102032463731627

--- normal mode 8 ---

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 0.0003

ARG 348 ALA 349 -0.0026

ALA 349 SER 350 0.0003

SER 350 LEU 351 0.0063

LEU 351 ARG 352 -0.0003

ARG 352 ARG 353 -0.0072

ARG 353 HIS 354 -0.0000

HIS 354 TYR 355 -0.0008

TYR 355 SER 356 -0.0001

SER 356 VAL 357 -0.0159

VAL 357 ARG 358 0.0000

ARG 358 HIS 359 -0.0028

HIS 359 LEU 360 -0.0001

LEU 360 ALA 361 -0.0054

ALA 361 ALA 362 -0.0003

ALA 362 ARG 363 -0.0061

ARG 363 GLU 364 0.0001

GLU 364 LEU 365 -0.0021

LEU 365 LEU 366 0.0000

LEU 366 ASP 367 -0.0036

ASP 367 THR 368 -0.0000

THR 368 GLU 369 0.0062

GLU 369 LYS 370 -0.0003

LYS 370 SER 371 -0.0038

SER 371 PHE 372 0.0002

PHE 372 VAL 373 -0.0075

VAL 373 GLU 374 -0.0001

GLU 374 GLY 375 0.0007

GLY 375 LEU 376 0.0001

LEU 376 GLU 377 -0.0074

GLU 377 PHE 378 0.0002

PHE 378 LEU 379 0.0010

LEU 379 VAL 380 0.0002

VAL 380 THR 381 0.0037

THR 381 LYS 382 0.0001

LYS 382 TYR 383 0.0010

TYR 383 MET 384 -0.0000

MET 384 ARG 385 0.0015

ARG 385 PRO 386 -0.0001

PRO 386 LEU 387 0.0030

LEU 387 ARG 388 -0.0002

ARG 388 GLN 389 0.0059

GLN 389 PRO 390 -0.0000

PRO 390 LEU 391 -0.0061

LEU 391 GLU 392 0.0001

GLU 392 CYS 393 0.0088

CYS 393 THR 394 0.0001

THR 394 LEU 395 -0.0004

LEU 395 ILE 396 0.0000

ILE 396 GLU 397 -0.0025

GLU 397 ALA 398 0.0001

ALA 398 SER 399 -0.0015

SER 399 LEU 400 0.0002

LEU 400 VAL 401 -0.0067

VAL 401 ASP 402 0.0000

ASP 402 LYS 403 0.0043

LYS 403 ILE 404 -0.0001

ILE 404 PHE 405 -0.0071

PHE 405 TYR 406 -0.0001

TYR 406 ARG 407 -0.0209

ARG 407 ILE 408 0.0001

ILE 408 PRO 409 0.0053

PRO 409 GLU 410 0.0004

GLU 410 ILE 411 -0.0090

ILE 411 LEU 412 0.0001

LEU 412 ALA 413 -0.0014

ALA 413 HIS 414 0.0003

HIS 414 HIS 415 0.0076

HIS 415 GLN 416 0.0001

GLN 416 VAL 417 -0.0090

VAL 417 LEU 418 0.0003

LEU 418 LEU 419 -0.0024

LEU 419 THR 420 0.0000

THR 420 THR 421 -0.0047

THR 421 LEU 422 -0.0000

LEU 422 SER 423 0.0018

SER 423 GLN 424 0.0002

GLN 424 ARG 425 -0.0001

ARG 425 ILE 426 0.0000

ILE 426 ASP 427 -0.0011

ASP 427 GLN 428 -0.0002

GLN 428 TRP 429 -0.0004

TRP 429 HIS 430 0.0002

HIS 430 LYS 431 -0.0047

LYS 431 ASP 432 -0.0002

ASP 432 ALA 433 0.0004

ALA 433 ILE 434 -0.0000

ILE 434 LEU 435 -0.0021

LEU 435 GLY 436 0.0000

GLY 436 ASP 437 -0.0040

ASP 437 VAL 438 -0.0002

VAL 438 LEU 439 0.0019

LEU 439 LEU 440 0.0003

LEU 440 ALA 441 -0.0009

ALA 441 HIS 442 -0.0001

HIS 442 PHE 443 0.0010

PHE 443 SER 444 -0.0000

SER 444 LYS 445 -0.0062

LYS 445 GLN 446 -0.0002

GLN 446 SER 447 0.0116

SER 447 MET 448 0.0002

MET 448 ILE 449 0.0211

ILE 449 GLU 450 -0.0002

GLU 450 THR 451 0.0362

THR 451 TYR 452 0.0002

TYR 452 ILE 453 0.0189

ILE 453 SER 454 0.0003

SER 454 PHE 455 0.0347

PHE 455 VAL 456 0.0000

VAL 456 ASP 457 0.0156

ASP 457 ASN 458 -0.0002

ASN 458 PHE 459 0.0073

PHE 459 LYS 460 -0.0004

LYS 460 PHE 461 0.0067

PHE 461 ALA 462 0.0005

ALA 462 LYS 463 -0.0032

LYS 463 ALA 464 0.0001

ALA 464 SER 465 0.0016

SER 465 ILE 466 -0.0002

ILE 466 ILE 467 0.0040

ILE 467 GLN 468 -0.0001

GLN 468 ALA 469 0.0003

ALA 469 ARG 470 0.0002

ARG 470 GLN 471 0.0009

GLN 471 LYS 472 0.0001

LYS 472 HIS 473 0.0012

HIS 473 ALA 474 -0.0001

ALA 474 PHE 475 -0.0014

PHE 475 GLU 476 -0.0002

GLU 476 LYS 477 -0.0019

LYS 477 TYR 478 -0.0000

TYR 478 TYR 479 0.0028

TYR 479 ASN 480 -0.0002

ASN 480 ARG 481 -0.0017

ARG 481 CYS 482 0.0003

CYS 482 CYS 483 0.0006

CYS 483 ARG 484 -0.0002

ARG 484 ASP 485 0.0009

ASP 485 HIS 486 0.0001

HIS 486 PRO 487 -0.0002

PRO 487 ASN 488 0.0003

ASN 488 LYS 489 0.0004

LYS 489 LEU 490 0.0001

LEU 490 ASP 491 0.0010

ASP 491 LEU 492 0.0004

LEU 492 ASP 493 -0.0053

ASP 493 SER 494 0.0002

SER 494 LEU 495 0.0021

LEU 495 LEU 496 -0.0000

LEU 496 ILE 497 0.0003

ILE 497 SER 498 0.0002

SER 498 PRO 499 -0.0013

PRO 499 ILE 500 0.0002

ILE 500 GLN 501 -0.0117

GLN 501 ARG 502 -0.0003

ARG 502 VAL 503 -0.0253

VAL 503 PRO 504 -0.0003

PRO 504 ARG 505 -0.0413

ARG 505 TYR 506 -0.0001

TYR 506 GLU 507 -0.0065

GLU 507 LEU 508 -0.0005

LEU 508 ILE 509 -0.0200

ILE 509 VAL 510 -0.0004

VAL 510 LYS 511 0.0072

LYS 511 GLN 512 0.0000

GLN 512 MET 513 -0.0042

MET 513 LEU 514 0.0000

LEU 514 LYS 515 -0.0014

LYS 515 HIS 516 -0.0002

HIS 516 THR 517 0.0049

THR 517 PRO 518 -0.0002

PRO 518 VAL 519 -0.0129

VAL 519 GLU 520 -0.0003

GLU 520 HIS 521 -0.0050

HIS 521 GLU 522 0.0001

GLU 522 ASP 523 0.0014

ASP 523 ARG 524 0.0001

ARG 524 GLU 525 0.0002

GLU 525 ARG 526 -0.0002

ARG 526 LEU 527 0.0089

LEU 527 LEU 528 -0.0000

LEU 528 ARG 529 -0.0063

ARG 529 ALA 530 0.0001

ALA 530 GLN 531 -0.0030

GLN 531 ARG 532 0.0002

ARG 532 HIS 533 0.0056

HIS 533 ILE 534 -0.0002

ILE 534 HIS 535 -0.0055

HIS 535 CYS 536 -0.0001

CYS 536 LEU 537 0.0024

LEU 537 ALA 538 0.0000

ALA 538 VAL 539 -0.0015

VAL 539 ALA 540 0.0000

ALA 540 ILE 541 -0.0097

ILE 541 ASN 542 -0.0001

ASN 542 GLN 543 -0.0033

GLN 543 HIS 544 0.0001

HIS 544 LYS 545 -0.1277

LYS 545 ASP 546 -0.0001

ASP 546 GLY 547 -0.0100

GLY 547 SER 548 -0.0001

SER 548 GLU 549 -0.0319

GLU 549 GLN 550 -0.0002

GLN 550 MET 551 0.0146

MET 551 GLU 552 0.0001

GLU 552 GLN 553 -0.0020

GLN 553 ARG 554 0.0001

ARG 554 LEU 555 0.0186

LEU 555 ARG 556 -0.0001

ARG 556 GLU 557 0.0040

GLU 557 ILE 558 -0.0002

ILE 558 GLU 559 0.0155

GLU 559 ALA 560 0.0001

ALA 560 ILE 561 0.0291

ILE 561 VAL 562 -0.0001

VAL 562 ASP 563 -0.0154

ASP 563 GLY 564 0.0001

GLY 564 LEU 565 -0.0204

LEU 565 ASP 566 -0.0003

ASP 566 ASP 567 -0.0016

ASP 567 LEU 568 -0.0000

LEU 568 VAL 569 -0.0063

VAL 569 THR 570 -0.0003

THR 570 LYS 571 -0.0005

LYS 571 ASP 572 0.0002

ASP 572 ARG 573 0.0065

ARG 573 THR 574 0.0001

THR 574 LEU 575 -0.0243

LEU 575 LEU 576 0.0002

LEU 576 ARG 577 0.0021

ARG 577 HIS 578 0.0002

HIS 578 ASP 579 -0.0653

ASP 579 ILE 580 0.0003

ILE 580 ILE 581 -0.0280

ILE 581 THR 582 0.0001

THR 582 LEU 583 -0.0057

LEU 583 LYS 584 -0.0000

LYS 584 GLY 585 0.0031

GLY 585 THR 586 0.0001

THR 586 ASP 587 -0.0052

ASP 587 ARG 588 -0.0000

ARG 588 GLU 589 -0.0096

GLU 589 ARG 590 0.0002

ARG 590 CYS 591 -0.0212

CYS 591 ILE 592 -0.0002

ILE 592 PHE 593 0.0096

PHE 593 MET 594 0.0001

MET 594 LEU 595 -0.0024

LEU 595 SER 596 0.0000

SER 596 ASP 597 -0.0047

ASP 597 LEU 598 -0.0001

LEU 598 LEU 599 0.0071

LEU 599 LEU 600 -0.0002

LEU 600 VAL 601 0.0140

VAL 601 THR 602 0.0000

THR 602 SER 603 -0.0070

SER 603 VAL 604 -0.0002

VAL 604 LYS 605 0.0026

LYS 605 LYS 606 0.0000

LYS 606 LYS 607 -0.0056

LYS 607 PRO 608 0.0002

PRO 608 LYS 609 0.0035

LYS 609 VAL 610 -0.0004

VAL 610 LEU 611 -0.0131

LEU 611 TYR 612 0.0003

TYR 612 SER 613 -0.0027

SER 613 LYS 614 -0.0004

LYS 614 MET 615 0.0199

MET 615 SER 616 -0.0002

SER 616 SER 617 -0.0081

SER 617 GLN 618 -0.0001

GLN 618 SER 619 0.0074

SER 619 MET 620 -0.0001

MET 620 GLY 621 0.0078

GLY 621 PHE 622 0.0002

PHE 622 LEU 623 0.0056

LEU 623 GLU 624 -0.0003

GLU 624 GLY 625 0.0044

GLY 625 ASN 626 0.0002

ASN 626 ARG 627 -0.0036

ARG 627 PHE 628 0.0002

PHE 628 LYS 629 0.0045

LYS 629 LEU 630 -0.0000

LEU 630 LEU 631 -0.0012

LEU 631 PHE 632 0.0000

PHE 632 LYS 633 -0.0119

LYS 633 VAL 634 -0.0002

VAL 634 ALA 635 -0.0028

ALA 635 LEU 636 -0.0004

LEU 636 GLU 637 0.0002

GLU 637 ASP 638 0.0002

ASP 638 VAL 639 -0.0023

VAL 639 GLN 640 0.0001

GLN 640 ILE 641 -0.0002

ILE 641 SER 642 0.0001

SER 642 LYS 643 -0.0058

LYS 643 ASP 644 -0.0003

ASP 644 THR 645 -0.0069

THR 645 LEU 646 0.0002

LEU 646 SER 647 0.0018

SER 647 GLN 648 -0.0001

GLN 648 LEU 649 0.0027

LEU 649 GLU 650 -0.0003

GLU 650 GLU 651 0.0031

GLU 651 VAL 652 -0.0002

VAL 652 GLU 653 -0.0018

GLU 653 ARG 654 0.0001

ARG 654 LYS 655 -0.0074

LYS 655 LEU 656 0.0002

LEU 656 GLU 657 -0.0158

GLU 657 SER 658 -0.0000

SER 658 SER 659 -0.0122

SER 659 ARG 660 0.0002

ARG 660 GLU 661 -0.0046

GLU 661 ASP 662 -0.0002

ASP 662 ASP 663 -0.0044

ASP 663 ARG 664 0.0002

ARG 664 VAL 665 0.0010

VAL 665 LEU 666 0.0000

LEU 666 LYS 667 0.0003

LYS 667 LYS 668 0.0003

LYS 668 MET 669 0.0011

MET 669 SER 670 -0.0001

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 2504102032463731627

--- normal mode 8 ---

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

* *