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

* 3pfq_allatom *

CA strain for 240415112310379429

--- 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
LEU 339 THR 340 -0.0003

THR 340 ASP 341 -0.0153

ASP 341 PHE 342 -0.0001

PHE 342 ASN 343 0.0279

ASN 343 PHE 344 0.0001

PHE 344 LEU 345 -0.0286

LEU 345 MET 346 -0.0002

MET 346 VAL 347 0.0185

VAL 347 LEU 348 -0.0001

LEU 348 GLY 349 0.0617

GLY 349 LYS 350 -0.0000

LYS 350 GLY 351 0.0830

GLY 351 SER 352 0.0002

SER 352 PHE 353 -0.0319

PHE 353 GLY 354 -0.0004

GLY 354 LYS 355 -0.0034

LYS 355 VAL 356 0.0004

VAL 356 MET 357 -0.0033

MET 357 LEU 358 -0.0000

LEU 358 SER 359 -0.0055

SER 359 GLU 360 0.0004

GLU 360 ARG 361 -0.0051

ARG 361 LYS 362 -0.0000

LYS 362 GLY 363 -0.0075

GLY 363 THR 364 -0.0002

THR 364 ASP 365 -0.0218

ASP 365 GLU 366 -0.0003

GLU 366 LEU 367 -0.0235

LEU 367 TYR 368 -0.0002

TYR 368 ALA 369 -0.0029

ALA 369 VAL 370 0.0002

VAL 370 LYS 371 0.0273

LYS 371 ILE 372 0.0001

ILE 372 LEU 373 0.0306

LEU 373 LYS 374 0.0001

LYS 374 LYS 375 0.0529

LYS 375 ASP 376 0.0001

ASP 376 VAL 377 0.0283

VAL 377 VAL 378 0.0001

VAL 378 ILE 379 0.0206

ILE 379 GLN 380 0.0005

GLN 380 ASP 381 -0.0057

ASP 381 ASP 382 -0.0002

ASP 382 ASP 383 0.0079

ASP 383 VAL 384 -0.0000

VAL 384 GLU 385 -0.0638

GLU 385 CYS 386 -0.0001

CYS 386 THR 387 -0.0491

THR 387 MET 388 -0.0001

MET 388 VAL 389 -0.0063

VAL 389 GLU 390 0.0001

GLU 390 LYS 391 0.0161

LYS 391 ARG 392 0.0002

ARG 392 VAL 393 -0.0334

VAL 393 LEU 394 0.0000

LEU 394 ALA 395 0.0109

ALA 395 LEU 396 0.0002

LEU 396 PRO 397 0.0103

PRO 397 GLY 398 -0.0002

GLY 398 LYS 399 -0.0183

LYS 399 PRO 400 -0.0000

PRO 400 PRO 401 -0.0192

PRO 401 PHE 402 -0.0006

PHE 402 LEU 403 0.0061

LEU 403 THR 404 0.0002

THR 404 GLN 405 -0.0461

GLN 405 LEU 406 -0.0001

LEU 406 HSD 407 0.0252

HSD 407 SER 408 0.0000

SER 408 CYS 409 -0.0188

CYS 409 PHE 410 -0.0002

PHE 410 GLN 411 -0.0559

GLN 411 THR 412 -0.0001

THR 412 MET 413 -0.0572

MET 413 ASP 414 -0.0001

ASP 414 ARG 415 0.0078

ARG 415 LEU 416 -0.0005

LEU 416 TYR 417 0.0032

TYR 417 PHE 418 -0.0001

PHE 418 VAL 419 0.0190

VAL 419 MET 420 0.0000

MET 420 GLU 421 -0.0233

GLU 421 TYR 422 0.0002

TYR 422 VAL 423 -0.0649

VAL 423 ASN 424 -0.0004

ASN 424 GLY 425 -0.0233

GLY 425 GLY 426 0.0004

GLY 426 ASP 427 -0.0933

ASP 427 LEU 428 0.0001

LEU 428 MET 429 -0.0005

MET 429 TYR 430 0.0000

TYR 430 HSD 431 0.0147

HSD 431 ILE 432 -0.0001

ILE 432 GLN 433 -0.0283

GLN 433 GLN 434 0.0000

GLN 434 VAL 435 0.0088

VAL 435 GLY 436 -0.0002

GLY 436 ARG 437 -0.0101

ARG 437 PHE 438 -0.0000

PHE 438 LYS 439 0.0065

LYS 439 GLU 440 -0.0003

GLU 440 PRO 441 0.0207

PRO 441 HSD 442 -0.0002

HSD 442 ALA 443 0.0042

ALA 443 VAL 444 0.0001

VAL 444 PHE 445 0.0267

PHE 445 TYR 446 -0.0004

TYR 446 ALA 447 0.0138

ALA 447 ALA 448 0.0003

ALA 448 GLU 449 0.0102

GLU 449 ILE 450 0.0003

ILE 450 ALA 451 0.0042

ALA 451 ILE 452 0.0003

ILE 452 GLY 453 -0.0191

GLY 453 LEU 454 0.0004

LEU 454 PHE 455 -0.0019

PHE 455 PHE 456 -0.0001

PHE 456 LEU 457 -0.0187

LEU 457 GLN 458 -0.0003

GLN 458 SER 459 0.0402

SER 459 LYS 460 0.0004

LYS 460 GLY 461 0.0539

GLY 461 ILE 462 -0.0002

ILE 462 ILE 463 0.0316

ILE 463 TYR 464 0.0000

TYR 464 ARG 465 -0.0152

ARG 465 ASP 466 -0.0001

ASP 466 LEU 467 0.0375

LEU 467 LYS 468 -0.0001

LYS 468 LEU 469 -0.0102

LEU 469 ASP 470 -0.0001

ASP 470 ASN 471 0.0355

ASN 471 VAL 472 0.0002

VAL 472 MET 473 -0.0760

MET 473 LEU 474 -0.0001

LEU 474 ASP 475 -0.0453

ASP 475 SER 476 -0.0002

SER 476 GLU 477 0.0873

GLU 477 GLY 478 -0.0000

GLY 478 HSD 479 0.0109

HSD 479 ILE 480 -0.0000

ILE 480 LYS 481 0.0111

LYS 481 ILE 482 0.0003

ILE 482 ALA 483 0.0299

ALA 483 ASP 484 0.0000

ASP 484 PHE 485 0.0678

PHE 485 GLY 486 0.0002

GLY 486 MET 487 -0.1332

MET 487 CYS 488 0.0001

CYS 488 LYS 489 -0.0270

LYS 489 GLU 490 -0.0003

GLU 490 ASN 491 0.0003

ASN 491 ILE 492 0.0001

ILE 492 TRP 493 -0.0270

TRP 493 ASP 494 0.0001

ASP 494 GLY 495 0.0158

GLY 495 VAL 496 -0.0004

VAL 496 THR 497 0.0276

THR 497 THR 498 0.0000

THR 498 LYS 499 0.0400

LYS 499 GLU 500 -0.0001

GLU 500 PHE 501 0.0616

PHE 501 CYS 502 0.0003

CYS 502 GLY 503 -0.0076

GLY 503 THR 504 -0.0000

THR 504 PRO 505 -0.0197

PRO 505 ASP 506 -0.0003

ASP 506 TYR 507 -0.0160

TYR 507 ILE 508 -0.0000

ILE 508 ALA 509 -0.0208

ALA 509 PRO 510 -0.0001

PRO 510 GLU 511 -0.0030

GLU 511 ILE 512 -0.0001

ILE 512 ILE 513 0.0310

ILE 513 ALA 514 -0.0001

ALA 514 TYR 515 0.0101

TYR 515 GLN 516 0.0002

GLN 516 PRO 517 0.0263

PRO 517 TYR 518 -0.0001

TYR 518 GLY 519 0.0312

GLY 519 LYS 520 0.0000

LYS 520 SER 521 0.0051

SER 521 VAL 522 0.0001

VAL 522 ASP 523 -0.0062

ASP 523 TRP 524 -0.0002

TRP 524 TRP 525 0.0266

TRP 525 ALA 526 0.0001

ALA 526 PHE 527 -0.0015

PHE 527 GLY 528 0.0000

GLY 528 VAL 529 0.0014

VAL 529 LEU 530 0.0004

LEU 530 LEU 531 0.0090

LEU 531 TYR 532 -0.0003

TYR 532 GLU 533 -0.0350

GLU 533 MET 534 -0.0001

MET 534 LEU 535 0.0045

LEU 535 ALA 536 0.0002

ALA 536 GLY 537 -0.0327

GLY 537 GLN 538 0.0003

GLN 538 ALA 539 -0.0081

ALA 539 PRO 540 -0.0000

PRO 540 PHE 541 -0.0139

PHE 541 GLU 542 0.0001

GLU 542 GLY 543 -0.0404

GLY 543 GLU 544 -0.0000

GLU 544 ASP 545 -0.0077

ASP 545 GLU 546 -0.0003

GLU 546 ASP 547 -0.0078

ASP 547 GLU 548 -0.0004

GLU 548 LEU 549 -0.0166

LEU 549 PHE 550 0.0001

PHE 550 GLN 551 -0.0216

GLN 551 SER 552 -0.0001

SER 552 ILE 553 0.0084

ILE 553 MET 554 0.0000

MET 554 GLU 555 -0.0071

GLU 555 HSD 556 0.0003

HSD 556 ASN 557 0.0175

ASN 557 VAL 558 0.0003

VAL 558 ALA 559 0.0077

ALA 559 TYR 560 -0.0003

TYR 560 PRO 561 -0.0001

PRO 561 LYS 562 0.0001

LYS 562 SER 563 -0.0029

SER 563 MET 564 -0.0006

MET 564 SER 565 -0.0055

SER 565 LYS 566 0.0002

LYS 566 GLU 567 -0.0087

GLU 567 ALA 568 -0.0001

ALA 568 VAL 569 0.0110

VAL 569 ALA 570 0.0001

ALA 570 ILE 571 -0.0069

ILE 571 CYS 572 -0.0003

CYS 572 LYS 573 -0.0006

LYS 573 GLY 574 -0.0000

GLY 574 LEU 575 -0.0062

LEU 575 MET 576 -0.0001

MET 576 THR 577 -0.0169

THR 577 LYS 578 0.0002

LYS 578 HSD 579 -0.0036

HSD 579 PRO 580 -0.0001

PRO 580 GLY 581 -0.0160

GLY 581 LYS 582 0.0002

LYS 582 ARG 583 0.0060

ARG 583 LEU 584 -0.0002

LEU 584 GLY 585 -0.0072

GLY 585 CYS 586 0.0001

CYS 586 GLY 587 -0.0057

GLY 587 PRO 588 -0.0002

PRO 588 GLU 589 -0.0010

GLU 589 GLY 590 -0.0002

GLY 590 GLU 591 0.0254

GLU 591 ARG 592 -0.0000

ARG 592 ASP 593 -0.0012

ASP 593 ILE 594 -0.0003

ILE 594 LYS 595 0.0222

LYS 595 GLU 596 -0.0001

GLU 596 HSD 597 -0.0080

HSD 597 ALA 598 0.0000

ALA 598 PHE 599 -0.0006

PHE 599 PHE 600 -0.0001

PHE 600 ARG 601 -0.0145

ARG 601 TYR 602 0.0003

TYR 602 ILE 603 0.0063

ILE 603 ASP 604 -0.0001

ASP 604 TRP 605 -0.0029

TRP 605 GLU 606 0.0000

GLU 606 LYS 607 0.0194

LYS 607 LEU 608 0.0001

LEU 608 GLU 609 -0.0133

GLU 609 ARG 610 -0.0002

ARG 610 LYS 611 0.0186

LYS 611 GLU 612 0.0004

GLU 612 ILE 613 -0.0160

ILE 613 GLN 614 0.0003

GLN 614 PRO 615 0.0059

PRO 615 PRO 616 -0.0001

PRO 616 TYR 617 0.0594

TYR 617 LYS 618 -0.0002

LYS 618 PRO 619 0.0539

PRO 619 LYS 620 -0.0001

LYS 620 ALA 621 0.1340

ALA 621 SER 622 -0.0001

SER 622 GLY 623 -0.0094

GLY 623 ARG 624 0.0001

ARG 624 ASN 625 -0.0339

ASN 625 ALA 626 0.0000

ALA 626 GLU 627 0.0734

GLU 627 ASN 628 -0.0001

ASN 628 PHE 629 -0.0505

PHE 629 ASP 630 -0.0002

ASP 630 ARG 631 0.0087

ARG 631 PHE 632 -0.0001

PHE 632 PHE 633 -0.0254

PHE 633 THR 634 -0.0003

THR 634 ARG 635 -0.0707

ARG 635 HSD 636 -0.0000

HSD 636 PRO 637 0.0640

PRO 637 PRO 638 -0.0002

PRO 638 VAL 639 -0.0014

VAL 639 LEU 640 0.0002

LEU 640 GLU 641 0.0226

GLU 641 PRO 642 -0.0000

PRO 642 PRO 643 0.0155

PRO 643 ASP 644 -0.0005

ASP 644 GLN 645 0.0282

GLN 645 GLU 646 -0.0001

GLU 646 VAL 647 0.0081

VAL 647 ILE 648 0.0004

ILE 648 ARG 649 -0.0172

ARG 649 ASN 650 -0.0002

ASN 650 ILE 651 -0.0115

ILE 651 ASP 652 -0.0001

ASP 652 GLN 653 -0.0162

GLN 653 SER 654 -0.0002

SER 654 GLU 655 0.0228

GLU 655 PHE 656 0.0003

PHE 656 GLU 657 0.0068

GLU 657 GLY 658 -0.0005

GLY 658 PHE 659 -0.0003

PHE 659 GLU 660 0.0000

GLU 660 PHE 661 -0.0675

PHE 661 VAL 662 -0.0002

VAL 662 ASN 663 -0.0360

ASN 663 SER 664 -0.0003

SER 664 GLU 665 -0.0353

GLU 665 PHE 666 0.0003

PHE 666 LEU 667 0.0065

LEU 667 LYS 668 -0.0002

LYS 668 PRO 669 -0.0070

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 25th, 2023.

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

*** 3pfq_allatom ***

CA strain for 240415112310379429

--- normal mode 8 ---

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

* 3pfq_allatom *