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

* *

CA strain for 2504102031593723925

--- normal mode 10 ---

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 -0.0164

ALA 349 SER 350 -0.0003

SER 350 LEU 351 0.0092

LEU 351 ARG 352 0.0001

ARG 352 ARG 353 -0.0085

ARG 353 HIS 354 0.0000

HIS 354 TYR 355 -0.0007

TYR 355 SER 356 -0.0001

SER 356 VAL 357 0.0108

VAL 357 ARG 358 -0.0001

ARG 358 HIS 359 -0.0016

HIS 359 LEU 360 0.0002

LEU 360 ALA 361 0.0234

ALA 361 ALA 362 -0.0002

ALA 362 ARG 363 -0.0028

ARG 363 GLU 364 0.0002

GLU 364 LEU 365 -0.0066

LEU 365 LEU 366 0.0003

LEU 366 ASP 367 0.0020

ASP 367 THR 368 -0.0001

THR 368 GLU 369 -0.0059

GLU 369 LYS 370 -0.0002

LYS 370 SER 371 -0.0005

SER 371 PHE 372 -0.0003

PHE 372 VAL 373 0.0079

VAL 373 GLU 374 -0.0000

GLU 374 GLY 375 0.0021

GLY 375 LEU 376 -0.0000

LEU 376 GLU 377 0.0084

GLU 377 PHE 378 -0.0002

PHE 378 LEU 379 0.0054

LEU 379 VAL 380 -0.0001

VAL 380 THR 381 0.0003

THR 381 LYS 382 0.0001

LYS 382 TYR 383 -0.0056

TYR 383 MET 384 -0.0000

MET 384 ARG 385 -0.0165

ARG 385 PRO 386 0.0000

PRO 386 LEU 387 -0.0146

LEU 387 ARG 388 -0.0000

ARG 388 GLN 389 0.0009

GLN 389 PRO 390 -0.0001

PRO 390 LEU 391 0.0114

LEU 391 GLU 392 0.0001

GLU 392 CYS 393 -0.0070

CYS 393 THR 394 0.0002

THR 394 LEU 395 -0.0254

LEU 395 ILE 396 0.0004

ILE 396 GLU 397 0.0280

GLU 397 ALA 398 -0.0001

ALA 398 SER 399 0.0398

SER 399 LEU 400 -0.0001

LEU 400 VAL 401 0.0378

VAL 401 ASP 402 -0.0001

ASP 402 LYS 403 -0.0437

LYS 403 ILE 404 -0.0004

ILE 404 PHE 405 0.0316

PHE 405 TYR 406 -0.0001

TYR 406 ARG 407 0.0377

ARG 407 ILE 408 -0.0004

ILE 408 PRO 409 -0.0180

PRO 409 GLU 410 0.0001

GLU 410 ILE 411 -0.0260

ILE 411 LEU 412 -0.0001

LEU 412 ALA 413 0.0101

ALA 413 HIS 414 0.0005

HIS 414 HIS 415 -0.0108

HIS 415 GLN 416 0.0003

GLN 416 VAL 417 -0.0175

VAL 417 LEU 418 0.0001

LEU 418 LEU 419 -0.0218

LEU 419 THR 420 0.0000

THR 420 THR 421 -0.0167

THR 421 LEU 422 -0.0002

LEU 422 SER 423 -0.0037

SER 423 GLN 424 0.0000

GLN 424 ARG 425 -0.0134

ARG 425 ILE 426 0.0002

ILE 426 ASP 427 0.0095

ASP 427 GLN 428 0.0003

GLN 428 TRP 429 -0.0193

TRP 429 HIS 430 0.0001

HIS 430 LYS 431 0.0204

LYS 431 ASP 432 0.0000

ASP 432 ALA 433 -0.0171

ALA 433 ILE 434 0.0004

ILE 434 LEU 435 -0.0040

LEU 435 GLY 436 0.0005

GLY 436 ASP 437 -0.0119

ASP 437 VAL 438 -0.0001

VAL 438 LEU 439 -0.0103

LEU 439 LEU 440 -0.0001

LEU 440 ALA 441 -0.0140

ALA 441 HIS 442 -0.0004

HIS 442 PHE 443 -0.0367

PHE 443 SER 444 -0.0002

SER 444 LYS 445 0.0100

LYS 445 GLN 446 -0.0001

GLN 446 SER 447 0.0102

SER 447 MET 448 0.0002

MET 448 ILE 449 0.0034

ILE 449 GLU 450 0.0001

GLU 450 THR 451 0.0492

THR 451 TYR 452 0.0002

TYR 452 ILE 453 -0.0065

ILE 453 SER 454 -0.0002

SER 454 PHE 455 -0.0035

PHE 455 VAL 456 -0.0003

VAL 456 ASP 457 -0.0009

ASP 457 ASN 458 -0.0003

ASN 458 PHE 459 0.0201

PHE 459 LYS 460 -0.0001

LYS 460 PHE 461 -0.0297

PHE 461 ALA 462 0.0001

ALA 462 LYS 463 0.0179

LYS 463 ALA 464 -0.0002

ALA 464 SER 465 -0.0491

SER 465 ILE 466 0.0001

ILE 466 ILE 467 0.0228

ILE 467 GLN 468 -0.0000

GLN 468 ALA 469 -0.0078

ALA 469 ARG 470 -0.0002

ARG 470 GLN 471 0.0247

GLN 471 LYS 472 0.0003

LYS 472 HIS 473 0.0030

HIS 473 ALA 474 -0.0000

ALA 474 PHE 475 0.0049

PHE 475 GLU 476 -0.0003

GLU 476 LYS 477 -0.0014

LYS 477 TYR 478 0.0002

TYR 478 TYR 479 -0.0527

TYR 479 ASN 480 -0.0002

ASN 480 ARG 481 -0.0094

ARG 481 CYS 482 -0.0001

CYS 482 CYS 483 -0.0181

CYS 483 ARG 484 -0.0000

ARG 484 ASP 485 0.0116

ASP 485 HIS 486 -0.0000

HIS 486 PRO 487 -0.0089

PRO 487 ASN 488 0.0004

ASN 488 LYS 489 -0.0188

LYS 489 LEU 490 0.0002

LEU 490 ASP 491 0.0234

ASP 491 LEU 492 -0.0001

LEU 492 ASP 493 -0.0069

ASP 493 SER 494 0.0001

SER 494 LEU 495 0.0235

LEU 495 LEU 496 -0.0001

LEU 496 ILE 497 -0.0392

ILE 497 SER 498 -0.0002

SER 498 PRO 499 -0.0297

PRO 499 ILE 500 -0.0002

ILE 500 GLN 501 0.0252

GLN 501 ARG 502 -0.0002

ARG 502 VAL 503 -0.0091

VAL 503 PRO 504 -0.0003

PRO 504 ARG 505 0.0159

ARG 505 TYR 506 0.0002

TYR 506 GLU 507 0.0065

GLU 507 LEU 508 0.0000

LEU 508 ILE 509 0.0263

ILE 509 VAL 510 0.0001

VAL 510 LYS 511 0.0148

LYS 511 GLN 512 0.0002

GLN 512 MET 513 -0.0002

MET 513 LEU 514 -0.0003

LEU 514 LYS 515 0.0220

LYS 515 HIS 516 0.0003

HIS 516 THR 517 -0.0184

THR 517 PRO 518 0.0003

PRO 518 VAL 519 -0.0006

VAL 519 GLU 520 0.0002

GLU 520 HIS 521 -0.0158

HIS 521 GLU 522 0.0003

GLU 522 ASP 523 -0.0003

ASP 523 ARG 524 0.0000

ARG 524 GLU 525 -0.0055

GLU 525 ARG 526 0.0002

ARG 526 LEU 527 0.0231

LEU 527 LEU 528 -0.0001

LEU 528 ARG 529 0.0250

ARG 529 ALA 530 0.0005

ALA 530 GLN 531 0.0272

GLN 531 ARG 532 0.0000

ARG 532 HIS 533 -0.0154

HIS 533 ILE 534 -0.0001

ILE 534 HIS 535 0.0275

HIS 535 CYS 536 0.0003

CYS 536 LEU 537 -0.0061

LEU 537 ALA 538 -0.0002

ALA 538 VAL 539 0.0178

VAL 539 ALA 540 -0.0000

ALA 540 ILE 541 -0.0097

ILE 541 ASN 542 0.0001

ASN 542 GLN 543 0.0076

GLN 543 HIS 544 -0.0002

HIS 544 LYS 545 -0.0219

LYS 545 ASP 546 -0.0003

ASP 546 GLY 547 -0.0201

GLY 547 SER 548 0.0001

SER 548 GLU 549 -0.0170

GLU 549 GLN 550 -0.0000

GLN 550 MET 551 -0.0012

MET 551 GLU 552 -0.0000

GLU 552 GLN 553 0.0089

GLN 553 ARG 554 -0.0002

ARG 554 LEU 555 -0.0116

LEU 555 ARG 556 -0.0001

ARG 556 GLU 557 -0.0457

GLU 557 ILE 558 -0.0002

ILE 558 GLU 559 0.0164

GLU 559 ALA 560 0.0001

ALA 560 ILE 561 -0.0287

ILE 561 VAL 562 -0.0004

VAL 562 ASP 563 0.0073

ASP 563 GLY 564 0.0000

GLY 564 LEU 565 -0.0111

LEU 565 ASP 566 0.0002

ASP 566 ASP 567 -0.0085

ASP 567 LEU 568 -0.0001

LEU 568 VAL 569 -0.0174

VAL 569 THR 570 0.0003

THR 570 LYS 571 -0.0007

LYS 571 ASP 572 0.0002

ASP 572 ARG 573 0.0006

ARG 573 THR 574 0.0003

THR 574 LEU 575 -0.0117

LEU 575 LEU 576 -0.0001

LEU 576 ARG 577 0.0050

ARG 577 HIS 578 0.0001

HIS 578 ASP 579 -0.0029

ASP 579 ILE 580 -0.0003

ILE 580 ILE 581 -0.0163

ILE 581 THR 582 -0.0001

THR 582 LEU 583 -0.0068

LEU 583 LYS 584 0.0000

LYS 584 GLY 585 0.0020

GLY 585 THR 586 -0.0003

THR 586 ASP 587 -0.0032

ASP 587 ARG 588 -0.0000

ARG 588 GLU 589 -0.0145

GLU 589 ARG 590 -0.0002

ARG 590 CYS 591 -0.0117

CYS 591 ILE 592 0.0001

ILE 592 PHE 593 -0.0008

PHE 593 MET 594 0.0001

MET 594 LEU 595 0.0006

LEU 595 SER 596 0.0001

SER 596 ASP 597 -0.0078

ASP 597 LEU 598 0.0001

LEU 598 LEU 599 0.0063

LEU 599 LEU 600 -0.0002

LEU 600 VAL 601 0.0072

VAL 601 THR 602 -0.0002

THR 602 SER 603 -0.0017

SER 603 VAL 604 -0.0000

VAL 604 LYS 605 0.0035

LYS 605 LYS 606 0.0001

LYS 606 LYS 607 -0.0063

LYS 607 PRO 608 0.0001

PRO 608 LYS 609 0.0066

LYS 609 VAL 610 0.0001

VAL 610 LEU 611 -0.0020

LEU 611 TYR 612 0.0001

TYR 612 SER 613 -0.0026

SER 613 LYS 614 -0.0002

LYS 614 MET 615 0.0121

MET 615 SER 616 -0.0002

SER 616 SER 617 -0.0086

SER 617 GLN 618 0.0001

GLN 618 SER 619 0.0093

SER 619 MET 620 0.0001

MET 620 GLY 621 0.0190

GLY 621 PHE 622 0.0003

PHE 622 LEU 623 0.0118

LEU 623 GLU 624 -0.0004

GLU 624 GLY 625 0.0035

GLY 625 ASN 626 -0.0000

ASN 626 ARG 627 -0.0014

ARG 627 PHE 628 0.0001

PHE 628 LYS 629 0.0053

LYS 629 LEU 630 -0.0001

LEU 630 LEU 631 0.0006

LEU 631 PHE 632 0.0001

PHE 632 LYS 633 -0.0063

LYS 633 VAL 634 -0.0001

VAL 634 ALA 635 0.0032

ALA 635 LEU 636 -0.0002

LEU 636 GLU 637 -0.0006

GLU 637 ASP 638 0.0000

ASP 638 VAL 639 -0.0001

VAL 639 GLN 640 -0.0001

GLN 640 ILE 641 0.0001

ILE 641 SER 642 0.0000

SER 642 LYS 643 -0.0040

LYS 643 ASP 644 -0.0000

ASP 644 THR 645 -0.0032

THR 645 LEU 646 0.0001

LEU 646 SER 647 0.0041

SER 647 GLN 648 0.0000

GLN 648 LEU 649 0.0030

LEU 649 GLU 650 0.0002

GLU 650 GLU 651 0.0048

GLU 651 VAL 652 0.0003

VAL 652 GLU 653 -0.0016

GLU 653 ARG 654 0.0001

ARG 654 LYS 655 -0.0087

LYS 655 LEU 656 0.0000

LEU 656 GLU 657 -0.0142

GLU 657 SER 658 0.0002

SER 658 SER 659 -0.0077

SER 659 ARG 660 -0.0001

ARG 660 GLU 661 0.0001

GLU 661 ASP 662 0.0002

ASP 662 ASP 663 -0.0046

ASP 663 ARG 664 -0.0002

ARG 664 VAL 665 0.0038

VAL 665 LEU 666 -0.0001

LEU 666 LYS 667 -0.0013

LYS 667 LYS 668 -0.0001

LYS 668 MET 669 -0.0001

MET 669 SER 670 0.0002

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 2504102031593723925

--- normal mode 10 ---

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

* *