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

* *

CA strain for 2504102047043794046

--- 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 348 ARG 349 -0.0002

ARG 349 ALA 350 0.0189

ALA 350 SER 351 -0.0003

SER 351 LEU 352 -0.0248

LEU 352 ARG 353 0.0001

ARG 353 ARG 354 -0.0278

ARG 354 HIS 355 -0.0001

HIS 355 TYR 356 0.0097

TYR 356 SER 357 0.0001

SER 357 VAL 358 -0.0095

VAL 358 ARG 359 0.0002

ARG 359 HIS 360 0.0105

HIS 360 LEU 361 0.0001

LEU 361 ALA 362 0.0000

ALA 362 ALA 363 -0.0000

ALA 363 ARG 364 -0.0091

ARG 364 GLU 365 -0.0005

GLU 365 LEU 366 0.0290

LEU 366 LEU 367 0.0002

LEU 367 ASP 368 0.0150

ASP 368 THR 369 -0.0003

THR 369 GLU 370 0.0101

GLU 370 LYS 371 0.0001

LYS 371 SER 372 -0.0599

SER 372 PHE 373 -0.0003

PHE 373 VAL 374 0.0556

VAL 374 GLU 375 0.0001

GLU 375 GLY 376 -0.0367

GLY 376 LEU 377 0.0002

LEU 377 GLU 378 0.0319

GLU 378 PHE 379 -0.0002

PHE 379 LEU 380 -0.0064

LEU 380 VAL 381 -0.0001

VAL 381 THR 382 0.0435

THR 382 LYS 383 0.0000

LYS 383 TYR 384 0.0099

TYR 384 MET 385 0.0003

MET 385 ARG 386 0.0387

ARG 386 PRO 387 -0.0002

PRO 387 LEU 388 0.0241

LEU 388 ARG 389 0.0002

ARG 389 GLN 390 0.0320

GLN 390 PRO 391 0.0003

PRO 391 LEU 392 -0.0190

LEU 392 GLU 393 -0.0001

GLU 393 CYS 394 0.0560

CYS 394 THR 395 -0.0000

THR 395 LEU 396 -0.0073

LEU 396 ILE 397 -0.0003

ILE 397 GLU 398 -0.0241

GLU 398 ALA 399 -0.0001

ALA 399 SER 400 0.0116

SER 400 LEU 401 -0.0002

LEU 401 VAL 402 -0.0443

VAL 402 ASP 403 -0.0002

ASP 403 LYS 404 0.0165

LYS 404 ILE 405 0.0003

ILE 405 PHE 406 -0.0269

PHE 406 TYR 407 -0.0003

TYR 407 ARG 408 -0.0262

ARG 408 ILE 409 -0.0003

ILE 409 PRO 410 0.0205

PRO 410 GLU 411 0.0001

GLU 411 ILE 412 -0.0022

ILE 412 LEU 413 -0.0003

LEU 413 ALA 414 0.0055

ALA 414 HIS 415 0.0001

HIS 415 HIS 416 0.0114

HIS 416 GLN 417 -0.0002

GLN 417 VAL 418 0.0065

VAL 418 LEU 419 0.0002

LEU 419 LEU 420 0.0287

LEU 420 THR 421 0.0000

THR 421 THR 422 0.0115

THR 422 LEU 423 -0.0000

LEU 423 SER 424 0.0405

SER 424 GLN 425 -0.0002

GLN 425 ARG 426 -0.0087

ARG 426 ILE 427 -0.0001

ILE 427 ASP 428 0.0545

ASP 428 GLN 429 -0.0002

GLN 429 TRP 430 0.0170

TRP 430 HIS 431 0.0000

HIS 431 LYS 432 -0.0589

LYS 432 ASP 433 -0.0001

ASP 433 ALA 434 0.0962

ALA 434 ILE 435 0.0005

ILE 435 LEU 436 -0.0038

LEU 436 GLY 437 0.0001

GLY 437 ASP 438 0.0289

ASP 438 VAL 439 -0.0001

VAL 439 LEU 440 -0.0683

LEU 440 LEU 441 -0.0002

LEU 441 ALA 442 -0.0076

ALA 442 HIS 443 -0.0000

HIS 443 PHE 444 0.0238

PHE 444 SER 445 -0.0000

SER 445 LYS 446 0.0398

LYS 446 GLN 447 0.0000

GLN 447 SER 448 -0.0157

SER 448 MET 449 -0.0001

MET 449 ILE 450 0.0228

ILE 450 GLU 451 0.0001

GLU 451 THR 452 0.0093

THR 452 TYR 453 -0.0001

TYR 453 ILE 454 -0.0389

ILE 454 SER 455 0.0001

SER 455 PHE 456 -0.0184

PHE 456 VAL 457 0.0001

VAL 457 ASP 458 0.0077

ASP 458 ASN 459 -0.0000

ASN 459 PHE 460 -0.0024

PHE 460 LYS 461 -0.0003

LYS 461 PHE 462 -0.0095

PHE 462 ALA 463 -0.0003

ALA 463 LYS 464 -0.0111

LYS 464 ALA 465 0.0000

ALA 465 SER 466 0.0703

SER 466 ILE 467 -0.0000

ILE 467 ILE 468 -0.0347

ILE 468 GLN 469 0.0001

GLN 469 ALA 470 0.0382

ALA 470 ARG 471 -0.0001

ARG 471 GLN 472 -0.0289

GLN 472 LYS 473 0.0000

LYS 473 HIS 474 0.0046

HIS 474 ALA 475 -0.0002

ALA 475 PHE 476 -0.0309

PHE 476 GLU 477 -0.0001

GLU 477 LYS 478 0.0263

LYS 478 TYR 479 -0.0002

TYR 479 TYR 480 -0.0089

TYR 480 ASN 481 -0.0002

ASN 481 ARG 482 0.0146

ARG 482 CYS 483 -0.0000

CYS 483 CYS 484 0.0032

CYS 484 ARG 485 -0.0000

ARG 485 ASP 486 0.0005

ASP 486 HIS 487 0.0003

HIS 487 PRO 488 0.0263

PRO 488 ASN 489 -0.0001

ASN 489 LYS 490 0.0244

LYS 490 LEU 491 -0.0001

LEU 491 ASP 492 0.0068

ASP 492 LEU 493 -0.0002

LEU 493 ASP 494 0.0127

ASP 494 SER 495 -0.0001

SER 495 LEU 496 0.0028

LEU 496 LEU 497 -0.0001

LEU 497 ILE 498 0.0180

ILE 498 SER 499 -0.0000

SER 499 PRO 500 -0.0007

PRO 500 ILE 501 0.0002

ILE 501 GLN 502 0.0087

GLN 502 ARG 503 0.0003

ARG 503 VAL 504 -0.0245

VAL 504 PRO 505 0.0004

PRO 505 ARG 506 -0.0276

ARG 506 TYR 507 -0.0003

TYR 507 GLU 508 -0.0241

GLU 508 LEU 509 0.0003

LEU 509 ILE 510 0.0048

ILE 510 VAL 511 -0.0002

VAL 511 LYS 512 -0.0316

LYS 512 GLN 513 -0.0001

GLN 513 MET 514 0.0293

MET 514 LEU 515 -0.0001

LEU 515 LYS 516 0.0204

LYS 516 HIS 517 0.0003

HIS 517 THR 518 -0.0080

THR 518 PRO 519 0.0000

PRO 519 VAL 520 0.0571

VAL 520 GLU 521 -0.0003

GLU 521 HIS 522 -0.0669

HIS 522 GLU 523 -0.0003

GLU 523 ASP 524 0.0431

ASP 524 ARG 525 -0.0002

ARG 525 GLU 526 -0.0108

GLU 526 ARG 527 0.0004

ARG 527 LEU 528 -0.0071

LEU 528 LEU 529 0.0002

LEU 529 ARG 530 0.0436

ARG 530 ALA 531 0.0005

ALA 531 GLN 532 -0.0351

GLN 532 ARG 533 0.0002

ARG 533 HIS 534 -0.0128

HIS 534 ILE 535 0.0002

ILE 535 HIS 536 -0.0255

HIS 536 CYS 537 -0.0001

CYS 537 LEU 538 -0.0337

LEU 538 ALA 539 0.0003

ALA 539 VAL 540 -0.0134

VAL 540 ALA 541 -0.0001

ALA 541 ILE 542 -0.0549

ILE 542 ASN 543 0.0000

ASN 543 GLN 544 -0.0071

GLN 544 HIS 545 0.0002

HIS 545 LYS 546 -0.1345

LYS 546 ASP 547 0.0004

ASP 547 GLY 548 -0.0338

GLY 548 SER 549 -0.0002

SER 549 GLU 550 -0.0271

GLU 550 GLN 551 -0.0002

GLN 551 MET 552 0.0077

MET 552 GLU 553 -0.0001

GLU 553 GLN 554 -0.0177

GLN 554 ARG 555 0.0003

ARG 555 LEU 556 -0.0081

LEU 556 ARG 557 0.0001

ARG 557 GLU 558 0.0159

GLU 558 ILE 559 -0.0000

ILE 559 GLU 560 0.0600

GLU 560 ALA 561 -0.0001

ALA 561 ILE 562 0.0536

ILE 562 VAL 563 -0.0000

VAL 563 ASP 564 -0.0031

ASP 564 GLY 565 0.0003

GLY 565 LEU 566 -0.0569

LEU 566 ASP 567 0.0001

ASP 567 ASP 568 0.0318

ASP 568 LEU 569 0.0002

LEU 569 VAL 570 -0.0100

VAL 570 THR 571 0.0002

THR 571 LYS 572 0.0027

LYS 572 ASP 573 0.0005

ASP 573 ARG 574 0.0147

ARG 574 THR 575 -0.0002

THR 575 LEU 576 -0.0558

LEU 576 LEU 577 0.0002

LEU 577 ARG 578 0.0091

ARG 578 HIS 579 -0.0001

HIS 579 ASP 580 -0.0020

ASP 580 ILE 581 0.0002

ILE 581 ILE 582 -0.0101

ILE 582 THR 583 0.0006

THR 583 LEU 584 -0.0029

LEU 584 LYS 585 0.0000

LYS 585 GLY 586 0.0021

GLY 586 THR 587 0.0001

THR 587 ASP 588 0.0085

ASP 588 ARG 589 0.0002

ARG 589 GLU 590 0.0187

GLU 590 ARG 591 -0.0000

ARG 591 CYS 592 0.0111

CYS 592 ILE 593 -0.0001

ILE 593 PHE 594 0.0043

PHE 594 MET 595 -0.0002

MET 595 LEU 596 0.0021

LEU 596 SER 597 0.0002

SER 597 ASP 598 -0.0092

ASP 598 LEU 599 -0.0002

LEU 599 LEU 600 0.0061

LEU 600 LEU 601 0.0005

LEU 601 VAL 602 -0.0049

VAL 602 THR 603 0.0000

THR 603 SER 604 -0.0035

SER 604 VAL 605 0.0005

VAL 605 LYS 606 0.0203

LYS 606 LYS 607 -0.0001

LYS 607 LYS 608 0.0293

LYS 608 PRO 609 -0.0000

PRO 609 LYS 610 -0.0170

LYS 610 VAL 611 -0.0002

VAL 611 LEU 612 0.0011

LEU 612 TYR 613 -0.0002

TYR 613 SER 614 0.0379

SER 614 LYS 615 -0.0001

LYS 615 MET 616 0.0607

MET 616 SER 617 -0.0003

SER 617 SER 618 0.0109

SER 618 GLN 619 -0.0001

GLN 619 SER 620 0.0246

SER 620 MET 621 0.0004

MET 621 GLY 622 0.0236

GLY 622 PHE 623 -0.0001

PHE 623 LEU 624 0.0169

LEU 624 GLU 625 -0.0003

GLU 625 GLY 626 0.0075

GLY 626 ASN 627 -0.0000

ASN 627 ARG 628 -0.0061

ARG 628 PHE 629 -0.0000

PHE 629 LYS 630 0.0071

LYS 630 LEU 631 -0.0001

LEU 631 LEU 632 -0.0164

LEU 632 PHE 633 -0.0001

PHE 633 LYS 634 -0.0070

LYS 634 VAL 635 -0.0002

VAL 635 ALA 636 0.0192

ALA 636 LEU 637 0.0002

LEU 637 GLU 638 0.0048

GLU 638 ASP 639 0.0004

ASP 639 VAL 640 -0.0192

VAL 640 GLN 641 -0.0000

GLN 641 ILE 642 -0.0049

ILE 642 SER 643 0.0001

SER 643 LYS 644 -0.0078

LYS 644 ASP 645 -0.0000

ASP 645 THR 646 -0.0077

THR 646 LEU 647 -0.0001

LEU 647 SER 648 0.0090

SER 648 GLN 649 -0.0003

GLN 649 LEU 650 0.0012

LEU 650 GLU 651 0.0001

GLU 651 GLU 652 0.0032

GLU 652 VAL 653 -0.0001

VAL 653 GLU 654 -0.0010

GLU 654 ARG 655 0.0000

ARG 655 LYS 656 -0.0226

LYS 656 LEU 657 -0.0002

LEU 657 GLU 658 -0.0575

GLU 658 SER 659 0.0002

SER 659 SER 660 -0.0128

SER 660 ARG 661 -0.0000

ARG 661 GLU 662 -0.0329

GLU 662 ASP 663 -0.0001

ASP 663 ASP 664 0.0001

ASP 664 ARG 665 -0.0000

ARG 665 VAL 666 0.0140

VAL 666 LEU 667 0.0000

LEU 667 LYS 668 -0.0111

LYS 668 LYS 669 0.0001

LYS 669 MET 670 -0.0034

MET 670 SER 671 -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 2504102047043794046

--- normal mode 11 ---

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

* *