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

* *

CA strain for 2504102037223769681

--- normal mode 11 ---

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 -0.0004

ARG 348 ALA 349 -0.0335

ALA 349 SER 350 -0.0000

SER 350 LEU 351 0.0336

LEU 351 ARG 352 0.0001

ARG 352 ARG 353 -0.0216

ARG 353 HIS 354 0.0000

HIS 354 TYR 355 0.0172

TYR 355 SER 356 0.0002

SER 356 VAL 357 -0.0350

VAL 357 ARG 358 -0.0000

ARG 358 HIS 359 -0.0188

HIS 359 LEU 360 0.0001

LEU 360 ALA 361 -0.0072

ALA 361 ALA 362 0.0003

ALA 362 ARG 363 -0.0168

ARG 363 GLU 364 0.0003

GLU 364 LEU 365 0.0101

LEU 365 LEU 366 0.0003

LEU 366 ASP 367 -0.0148

ASP 367 THR 368 -0.0003

THR 368 GLU 369 0.0190

GLU 369 LYS 370 -0.0001

LYS 370 SER 371 -0.0823

SER 371 PHE 372 -0.0001

PHE 372 VAL 373 0.0505

VAL 373 GLU 374 0.0002

GLU 374 GLY 375 -0.0341

GLY 375 LEU 376 0.0001

LEU 376 GLU 377 0.0331

GLU 377 PHE 378 -0.0000

PHE 378 LEU 379 0.0175

LEU 379 VAL 380 -0.0000

VAL 380 THR 381 0.0193

THR 381 LYS 382 0.0002

LYS 382 TYR 383 -0.0105

TYR 383 MET 384 0.0001

MET 384 ARG 385 0.0032

ARG 385 PRO 386 -0.0004

PRO 386 LEU 387 0.0097

LEU 387 ARG 388 0.0002

ARG 388 GLN 389 0.0029

GLN 389 PRO 390 -0.0002

PRO 390 LEU 391 -0.0078

LEU 391 GLU 392 0.0001

GLU 392 CYS 393 0.0141

CYS 393 THR 394 -0.0001

THR 394 LEU 395 -0.0143

LEU 395 ILE 396 0.0000

ILE 396 GLU 397 -0.0047

GLU 397 ALA 398 -0.0002

ALA 398 SER 399 -0.0010

SER 399 LEU 400 0.0002

LEU 400 VAL 401 -0.0012

VAL 401 ASP 402 0.0001

ASP 402 LYS 403 0.0007

LYS 403 ILE 404 0.0001

ILE 404 PHE 405 -0.0004

PHE 405 TYR 406 -0.0000

TYR 406 ARG 407 0.0193

ARG 407 ILE 408 0.0001

ILE 408 PRO 409 0.0107

PRO 409 GLU 410 0.0002

GLU 410 ILE 411 0.0075

ILE 411 LEU 412 -0.0001

LEU 412 ALA 413 -0.0159

ALA 413 HIS 414 -0.0001

HIS 414 HIS 415 0.0021

HIS 415 GLN 416 -0.0001

GLN 416 VAL 417 -0.0378

VAL 417 LEU 418 0.0002

LEU 418 LEU 419 0.0260

LEU 419 THR 420 0.0002

THR 420 THR 421 -0.0032

THR 421 LEU 422 -0.0003

LEU 422 SER 423 0.0331

SER 423 GLN 424 0.0000

GLN 424 ARG 425 -0.0538

ARG 425 ILE 426 0.0001

ILE 426 ASP 427 0.0291

ASP 427 GLN 428 0.0002

GLN 428 TRP 429 0.0094

TRP 429 HIS 430 0.0003

HIS 430 LYS 431 0.0319

LYS 431 ASP 432 0.0002

ASP 432 ALA 433 -0.0427

ALA 433 ILE 434 0.0002

ILE 434 LEU 435 -0.0668

LEU 435 GLY 436 -0.0005

GLY 436 ASP 437 0.0068

ASP 437 VAL 438 -0.0004

VAL 438 LEU 439 0.0431

LEU 439 LEU 440 -0.0002

LEU 440 ALA 441 -0.0510

ALA 441 HIS 442 0.0002

HIS 442 PHE 443 0.0166

PHE 443 SER 444 -0.0003

SER 444 LYS 445 -0.0349

LYS 445 GLN 446 -0.0001

GLN 446 SER 447 0.0319

SER 447 MET 448 0.0001

MET 448 ILE 449 0.0066

ILE 449 GLU 450 0.0001

GLU 450 THR 451 0.0258

THR 451 TYR 452 -0.0000

TYR 452 ILE 453 0.0047

ILE 453 SER 454 0.0003

SER 454 PHE 455 0.0622

PHE 455 VAL 456 0.0002

VAL 456 ASP 457 -0.0074

ASP 457 ASN 458 0.0002

ASN 458 PHE 459 0.0654

PHE 459 LYS 460 -0.0000

LYS 460 PHE 461 -0.0146

PHE 461 ALA 462 0.0001

ALA 462 LYS 463 0.0083

LYS 463 ALA 464 -0.0001

ALA 464 SER 465 -0.0612

SER 465 ILE 466 0.0004

ILE 466 ILE 467 0.0176

ILE 467 GLN 468 -0.0002

GLN 468 ALA 469 -0.0121

ALA 469 ARG 470 0.0001

ARG 470 GLN 471 0.0020

GLN 471 LYS 472 -0.0001

LYS 472 HIS 473 -0.0048

HIS 473 ALA 474 -0.0001

ALA 474 PHE 475 0.0101

PHE 475 GLU 476 0.0001

GLU 476 LYS 477 0.0090

LYS 477 TYR 478 -0.0000

TYR 478 TYR 479 -0.0328

TYR 479 ASN 480 -0.0002

ASN 480 ARG 481 0.0230

ARG 481 CYS 482 0.0002

CYS 482 CYS 483 -0.0077

CYS 483 ARG 484 0.0001

ARG 484 ASP 485 0.0059

ASP 485 HIS 486 0.0002

HIS 486 PRO 487 0.0192

PRO 487 ASN 488 -0.0000

ASN 488 LYS 489 0.0114

LYS 489 LEU 490 -0.0003

LEU 490 ASP 491 -0.0074

ASP 491 LEU 492 0.0001

LEU 492 ASP 493 0.0103

ASP 493 SER 494 0.0000

SER 494 LEU 495 -0.0110

LEU 495 LEU 496 -0.0001

LEU 496 ILE 497 -0.0036

ILE 497 SER 498 -0.0002

SER 498 PRO 499 -0.0027

PRO 499 ILE 500 0.0001

ILE 500 GLN 501 -0.0448

GLN 501 ARG 502 0.0003

ARG 502 VAL 503 0.0070

VAL 503 PRO 504 0.0004

PRO 504 ARG 505 -0.0642

ARG 505 TYR 506 -0.0001

TYR 506 GLU 507 0.0007

GLU 507 LEU 508 -0.0000

LEU 508 ILE 509 -0.0132

ILE 509 VAL 510 0.0002

VAL 510 LYS 511 -0.0051

LYS 511 GLN 512 -0.0003

GLN 512 MET 513 0.0038

MET 513 LEU 514 -0.0001

LEU 514 LYS 515 -0.0284

LYS 515 HIS 516 -0.0001

HIS 516 THR 517 0.0516

THR 517 PRO 518 0.0002

PRO 518 VAL 519 0.1949

VAL 519 GLU 520 0.0000

GLU 520 HIS 521 -0.0963

HIS 521 GLU 522 0.0002

GLU 522 ASP 523 -0.1113

ASP 523 ARG 524 0.0001

ARG 524 GLU 525 0.1213

GLU 525 ARG 526 0.0002

ARG 526 LEU 527 0.0337

LEU 527 LEU 528 -0.0001

LEU 528 ARG 529 0.0037

ARG 529 ALA 530 -0.0002

ALA 530 GLN 531 -0.0425

GLN 531 ARG 532 -0.0000

ARG 532 HIS 533 0.0128

HIS 533 ILE 534 -0.0001

ILE 534 HIS 535 -0.0265

HIS 535 CYS 536 -0.0003

CYS 536 LEU 537 -0.0187

LEU 537 ALA 538 0.0001

ALA 538 VAL 539 -0.0224

VAL 539 ALA 540 -0.0003

ALA 540 ILE 541 -0.0217

ILE 541 ASN 542 0.0001

ASN 542 GLN 543 -0.0058

GLN 543 HIS 544 -0.0003

HIS 544 LYS 545 -0.1103

LYS 545 ASP 546 -0.0003

ASP 546 GLY 547 -0.0047

GLY 547 SER 548 -0.0001

SER 548 GLU 549 -0.0274

GLU 549 GLN 550 0.0001

GLN 550 MET 551 0.0017

MET 551 GLU 552 -0.0000

GLU 552 GLN 553 0.0008

GLN 553 ARG 554 -0.0005

ARG 554 LEU 555 -0.0134

LEU 555 ARG 556 0.0003

ARG 556 GLU 557 -0.0103

GLU 557 ILE 558 0.0003

ILE 558 GLU 559 0.0189

GLU 559 ALA 560 -0.0001

ALA 560 ILE 561 0.0409

ILE 561 VAL 562 -0.0002

VAL 562 ASP 563 -0.0032

ASP 563 GLY 564 -0.0000

GLY 564 LEU 565 -0.0073

LEU 565 ASP 566 0.0001

ASP 566 ASP 567 -0.0109

ASP 567 LEU 568 -0.0001

LEU 568 VAL 569 -0.0061

VAL 569 THR 570 -0.0002

THR 570 LYS 571 0.0031

LYS 571 ASP 572 0.0003

ASP 572 ARG 573 -0.0150

ARG 573 THR 574 -0.0002

THR 574 LEU 575 0.0023

LEU 575 LEU 576 0.0000

LEU 576 ARG 577 -0.0060

ARG 577 HIS 578 -0.0001

HIS 578 ASP 579 0.0156

ASP 579 ILE 580 0.0003

ILE 580 ILE 581 0.0207

ILE 581 THR 582 0.0004

THR 582 LEU 583 0.0084

LEU 583 LYS 584 0.0002

LYS 584 GLY 585 -0.0066

GLY 585 THR 586 0.0000

THR 586 ASP 587 0.0102

ASP 587 ARG 588 -0.0001

ARG 588 GLU 589 0.0220

GLU 589 ARG 590 -0.0003

ARG 590 CYS 591 0.0312

CYS 591 ILE 592 0.0002

ILE 592 PHE 593 0.0070

PHE 593 MET 594 -0.0002

MET 594 LEU 595 0.0090

LEU 595 SER 596 0.0003

SER 596 ASP 597 -0.0075

ASP 597 LEU 598 0.0001

LEU 598 LEU 599 -0.0010

LEU 599 LEU 600 0.0000

LEU 600 VAL 601 -0.0106

VAL 601 THR 602 0.0002

THR 602 SER 603 0.0022

SER 603 VAL 604 -0.0006

VAL 604 LYS 605 0.0018

LYS 605 LYS 606 -0.0001

LYS 606 LYS 607 0.0450

LYS 607 PRO 608 -0.0002

PRO 608 LYS 609 -0.0199

LYS 609 VAL 610 0.0004

VAL 610 LEU 611 0.0091

LEU 611 TYR 612 -0.0004

TYR 612 SER 613 0.0300

SER 613 LYS 614 0.0001

LYS 614 MET 615 0.0454

MET 615 SER 616 -0.0000

SER 616 SER 617 0.0099

SER 617 GLN 618 0.0003

GLN 618 SER 619 0.0178

SER 619 MET 620 0.0005

MET 620 GLY 621 0.0118

GLY 621 PHE 622 -0.0001

PHE 622 LEU 623 0.0046

LEU 623 GLU 624 0.0003

GLU 624 GLY 625 0.0002

GLY 625 ASN 626 -0.0004

ASN 626 ARG 627 -0.0011

ARG 627 PHE 628 0.0001

PHE 628 LYS 629 0.0018

LYS 629 LEU 630 -0.0001

LEU 630 LEU 631 -0.0063

LEU 631 PHE 632 0.0004

PHE 632 LYS 633 0.0051

LYS 633 VAL 634 0.0004

VAL 634 ALA 635 0.0227

ALA 635 LEU 636 -0.0001

LEU 636 GLU 637 0.0019

GLU 637 ASP 638 0.0001

ASP 638 VAL 639 -0.0109

VAL 639 GLN 640 0.0004

GLN 640 ILE 641 0.0010

ILE 641 SER 642 0.0001

SER 642 LYS 643 0.0097

LYS 643 ASP 644 -0.0001

ASP 644 THR 645 0.0051

THR 645 LEU 646 -0.0002

LEU 646 SER 647 0.0018

SER 647 GLN 648 -0.0002

GLN 648 LEU 649 0.0068

LEU 649 GLU 650 0.0003

GLU 650 GLU 651 -0.0069

GLU 651 VAL 652 -0.0003

VAL 652 GLU 653 -0.0028

GLU 653 ARG 654 -0.0003

ARG 654 LYS 655 -0.0063

LYS 655 LEU 656 -0.0003

LEU 656 GLU 657 -0.0071

GLU 657 SER 658 -0.0002

SER 658 SER 659 -0.0057

SER 659 ARG 660 0.0001

ARG 660 GLU 661 0.0004

GLU 661 ASP 662 0.0003

ASP 662 ASP 663 -0.0002

ASP 663 ARG 664 0.0003

ARG 664 VAL 665 0.0116

VAL 665 LEU 666 -0.0001

LEU 666 LYS 667 -0.0011

LYS 667 LYS 668 0.0001

LYS 668 MET 669 -0.0038

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 2504102037223769681

--- normal mode 11 ---

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

* *