Should you encounter any unexpected behaviour,
please let us know.
elNémo has been hacked on november 27th.
It has been moved away and runs again.
Still some additional cleaning from time to time
Sorry for the inconvenience.

* PROTEIN BINDING 10-JUN-10 3NFL *

CA distance fluctuations for 2602021513101103345

--- normal mode 9 ---

This matrix displays the maximum distance fluctuations between all pairs of CA atoms and between the two extreme conformations that were computed for this mode (DQMIN/DQMAX). Distance increases are plotted in blue and decreases in red for the strongest 10% of the residue pair distance changes. Every pixel corresponds to a single residue. Grey lines are drawn every 10 residues, yellow lines every 100 residues (counting from the upper left corner).

The following table indicates for every residue the two corresponding residues with the strongest CA distance fluctuations.

[HELP on distance fluctuations]

GD ok

largest increase ref largest decrease
ILE 12 0.11 HIS 512 -0.00 ASP 513

ILE 12 0.13 ASP 513 -0.00 HIS 512

ILE 12 0.12 ASN 514 -0.00 ARG 602

ILE 12 0.12 LEU 515 -0.00 LEU 600

ILE 12 0.10 VAL 516 -0.00 LEU 515

ILE 12 0.10 LEU 517 -0.00 PRO 558

MET 540 0.08 ILE 518 -0.00 ARG 519

GLY 563 0.09 ARG 519 -0.00 ILE 518

GLY 563 0.08 MET 520 -0.00 GLY 595

GLY 563 0.08 LYS 521 -0.00 ASP 523

GLY 563 0.07 PRO 522 -0.00 ASP 523

GLY 563 0.06 ASP 523 -0.00 PRO 522

PRO 603 0.06 GLU 524 -0.00 ARG 527

GLY 563 0.06 ASN 525 -0.00 GLY 595

GLY 563 0.07 GLY 526 -0.00 GLY 595

GLY 563 0.06 ARG 527 -0.00 GLU 524

GLY 563 0.06 PHE 528 -0.00 PHE 530

GLY 563 0.05 GLY 529 -0.00 PHE 530

MET 540 0.04 PHE 530 -0.00 ASP 15

MET 540 0.04 ASN 531 -0.00 VAL 16

ILE 12 0.04 VAL 532 -0.00 ASN 531

ILE 12 0.04 LYS 533 -0.00 MET 540

ILE 12 0.04 GLY 534 -0.00 TYR 536

ILE 12 0.05 GLY 535 -0.00 TYR 536

ILE 12 0.05 TYR 536 -0.00 GLY 535

ILE 12 0.05 ASP 537 -0.00 GLN 538

ILE 12 0.04 GLN 538 -0.00 ASP 537

ILE 12 0.05 LYS 539 -0.00 MET 540

ILE 12 0.04 MET 540 -0.01 MET 540

ILE 12 0.04 MET 540 -0.01 MET 540

ILE 12 0.05 PRO 541 -0.00 VAL 567

ILE 12 0.05 VAL 542 -0.00 VAL 567

GLN 538 0.05 ILE 543 -0.00 PRO 541

LYS 539 0.04 VAL 544 -0.00 LEU 599

LYS 539 0.04 SER 545 -0.00 VAL 532

MET 540 0.03 ARG 546 -0.00 VAL 532

MET 540 0.04 VAL 547 -0.00 LEU 560

PRO 603 0.04 ALA 548 -0.00 HIS 512

ASP 513 0.04 PRO 549 -0.01 HIS 512

ASP 513 0.04 GLY 550 -0.01 HIS 512

PRO 603 0.05 THR 551 -0.00 ALA 548

GLY 563 0.06 PRO 552 -0.00 GLY 550

MET 540 0.05 ALA 553 -0.00 ASP 15

MET 540 0.05 ASP 554 -0.00 VAL 547

MET 540 0.05 LEU 555 -0.00 VAL 557

MET 540 0.07 CYS 556 -0.00 VAL 557

MET 540 0.08 VAL 557 -0.00 LEU 555

MET 540 0.08 PRO 558 -0.00 LEU 517

MET 540 0.06 ARG 559 -0.00 CYS 556

MET 540 0.06 LEU 560 -0.00 VAL 547

LYS 539 0.05 ASN 561 -0.00 ASP 564

LYS 539 0.04 GLU 562 -0.00 ASP 564

LYS 539 0.04 GLY 563 -0.00 PRO 541

GLN 538 0.05 ASP 564 -0.00 GLU 562

ILE 12 0.06 GLN 565 -0.00 VAL 566

ILE 12 0.07 VAL 566 -0.00 GLN 565

ILE 12 0.09 VAL 567 -0.00 GLN 565

ILE 12 0.09 LEU 568 -0.00 VAL 601

SER 545 0.08 ILE 569 -0.00 ILE 586

SER 545 0.10 ASN 570 -0.00 ARG 519

SER 545 0.11 GLY 571 -0.00 ARG 519

ARG 546 0.09 ARG 572 -0.00 ARG 519

ILE 12 0.09 ASP 573 -0.00 ILE 574

ILE 12 0.08 ILE 574 -0.00 ASP 573

ILE 12 0.07 ALA 575 -0.00 HIS 577

ILE 12 0.07 GLU 576 -0.00 HIS 577

ILE 12 0.06 HIS 577 -0.00 GLU 576

ILE 12 0.06 THR 578 -0.00 ASP 580

ILE 12 0.05 HIS 579 -0.00 GLY 534

SER 545 0.05 ASP 580 -0.00 THR 578

ARG 546 0.06 GLN 581 -0.00 GLN 581

ILE 12 0.06 VAL 582 -0.00 ASP 573

SER 545 0.06 VAL 583 -0.00 LEU 584

ARG 546 0.06 LEU 584 -0.00 VAL 583

SER 545 0.07 PHE 585 -0.00 ILE 586

SER 545 0.07 ILE 586 -0.00 PHE 585

GLY 563 0.07 LYS 587 -0.00 SER 589

GLU 562 0.08 ALA 588 -0.00 CYS 590

GLY 563 0.08 SER 589 -0.00 LYS 587

GLU 562 0.09 CYS 590 -0.00 LYS 587

GLU 562 0.09 GLU 591 -0.00 ALA 588

GLY 563 0.10 ARG 592 -0.00 GLU 596

GLY 563 0.11 HIS 593 -0.00 ARG 592

GLY 563 0.11 SER 594 -0.00 ARG 592

GLY 563 0.10 GLY 595 -0.00 GLU 596

GLY 563 0.09 GLU 596 -0.00 ARG 592

GLY 563 0.09 LEU 597 -0.00 ALA 588

SER 545 0.09 MET 598 -0.00 ARG 519

ILE 12 0.08 LEU 599 -0.00 LEU 568

ILE 12 0.10 LEU 600 -0.00 LEU 568

ILE 12 0.08 VAL 601 -0.00 LEU 568

ILE 12 0.08 ARG 602 -0.00 PRO 603

GLN 538 0.06 PRO 603 -0.00 ARG 602

SER 594 0.06 HIS 512 -0.00 GLY 571

SER 594 0.07 ASP 513 -0.00 PRO 603

GLU 524 0.08 ASN 514 -0.00 LEU 515

GLU 524 0.08 LEU 515 -0.00 VAL 516

GLU 524 0.08 VAL 516 -0.00 LEU 515

GLU 524 0.08 LEU 517 -0.00 MET 598

GLU 524 0.08 ILE 518 -0.00 LEU 560

GLU 524 0.08 ARG 519 -0.00 PRO 558

GLY 550 0.08 MET 520 -0.00 LYS 521

GLY 550 0.08 LYS 521 -0.00 PRO 522

PRO 549 0.08 PRO 522 -0.00 LYS 521

PRO 549 0.08 ASP 523 -0.00 GLY 529

PRO 549 0.08 GLU 524 -0.00 GLY 529

PRO 549 0.08 ASN 525 -0.00 GLU 596

PRO 549 0.07 GLY 526 -0.00 GLY 529

PRO 549 0.08 ARG 527 -0.00 GLY 529

ASN 525 0.08 PHE 528 -0.00 THR 551

ASN 525 0.09 GLY 529 -0.00 THR 551

ASN 525 0.09 PHE 530 -0.00 ASN 531

GLY 571 0.09 ASN 531 -0.00 PHE 530

GLY 571 0.09 VAL 532 -0.00 VAL 542

LEU 517 0.10 LYS 533 -0.00 VAL 542

LEU 517 0.09 GLY 534 -0.00 PRO 541

LEU 517 0.08 GLY 535 -0.00 TYR 536

ASN 514 0.07 TYR 536 -0.00 GLY 535

ASN 514 0.09 ASP 537 -0.00 GLN 538

ASN 514 0.10 GLN 538 -0.00 ASP 537

VAL 516 0.09 LYS 539 -0.00 ASP 537

LEU 517 0.09 MET 540 -0.00 PRO 541

LEU 517 0.08 PRO 541 -0.00 MET 540

LEU 517 0.08 VAL 542 -0.00 VAL 532

HIS 593 0.09 ILE 543 -0.00 GLY 563

HIS 593 0.10 VAL 544 -0.00 GLU 562

HIS 593 0.11 SER 545 -0.00 ARG 546

ASN 525 0.11 ARG 546 -0.00 SER 545

ASN 525 0.10 VAL 547 -0.00 ALA 548

ASN 525 0.10 ALA 548 -0.00 VAL 547

PRO 549 0.11 PRO 549 -0.00 GLY 550

PRO 549 0.10 GLY 550 -0.00 PRO 549

PRO 549 0.09 THR 551 -0.00 GLY 529

GLY 550 0.09 PRO 552 -0.00 ASP 523

ASN 525 0.09 ALA 553 -0.00 PRO 549

ASN 525 0.10 ASP 554 -0.00 LEU 555

GLY 550 0.10 LEU 555 -0.00 ASP 554

GLY 550 0.09 CYS 556 -0.00 ASP 554

GLY 550 0.09 VAL 557 -0.00 PRO 558

GLU 524 0.09 PRO 558 -0.00 VAL 557

GLU 524 0.10 ARG 559 -0.00 ILE 518

GLU 524 0.10 LEU 560 -0.00 ILE 518

GLU 524 0.11 ASN 561 -0.00 ARG 602

ASN 525 0.11 GLU 562 -0.00 VAL 544

SER 594 0.11 GLY 563 -0.00 VAL 544

SER 594 0.10 ASP 564 -0.00 ILE 543

SER 594 0.09 GLN 565 -0.00 ARG 602

SER 594 0.08 VAL 566 -0.00 ASN 570

SER 594 0.07 VAL 567 -0.00 GLY 571

SER 594 0.06 LEU 568 -0.00 GLY 571

SER 594 0.06 ILE 569 -0.00 ASN 570

GLU 524 0.06 ASN 570 -0.00 ILE 569

SER 594 0.06 GLY 571 -0.00 ARG 572

SER 594 0.05 ARG 572 -0.00 GLY 571

SER 594 0.05 ARG 572 -0.00 GLY 571

SER 594 0.05 ASP 573 -0.00 GLY 571

LEU 517 0.06 ILE 574 -0.00 HIS 577

LEU 517 0.06 ALA 575 -0.00 GLU 576

VAL 516 0.06 GLU 576 -0.00 ALA 575

ASN 514 0.07 HIS 577 -0.00 ILE 574

ASN 514 0.08 THR 578 -0.00 PRO 541

ASP 513 0.09 HIS 579 -0.00 GLU 13

ASP 513 0.09 ASP 580 -0.00 GLU 13

ASP 513 0.07 GLN 581 -0.00 GLU 13

ASP 513 0.07 VAL 582 -0.00 ILE 569

ASP 513 0.08 VAL 583 -0.00 LEU 584

ASP 513 0.07 LEU 584 -0.00 VAL 583

GLY 571 0.06 PHE 585 -0.00 ALA 588

GLY 571 0.07 ILE 586 -0.00 LEU 584

GLY 571 0.07 LYS 587 -0.00 SER 589

GLY 571 0.06 ALA 588 -0.00 ALA 588

ASN 525 0.06 SER 589 -0.00 CYS 590

ASN 525 0.05 CYS 590 -0.00 SER 589

GLY 550 0.06 SER 594 -0.00 GLU 596

GLY 550 0.06 GLY 595 -0.00 GLU 596

GLY 550 0.07 GLU 596 -0.00 GLY 595

ASN 525 0.07 LEU 597 -0.00 GLY 595

GLU 524 0.07 MET 598 -0.00 LEU 599

GLU 524 0.07 LEU 599 -0.00 MET 598

GLU 524 0.07 LEU 600 -0.00 GLY 571

SER 594 0.08 VAL 601 -0.00 MET 598

SER 594 0.09 ARG 602 -0.00 GLN 565

SER 594 0.10 PRO 603 -0.00 LEU 515

ASP 513 0.07 PRO 511 -0.01 PRO 549

ASP 513 0.07 HIS 512 -0.01 PRO 549

ASP 513 0.06 ASP 513 -0.01 PRO 549

ASP 513 0.06 ASN 514 -0.01 PRO 549

ASP 513 0.06 LEU 515 -0.00 PRO 549

ASP 513 0.06 VAL 516 -0.00 PRO 549

ASP 513 0.06 LEU 517 -0.00 PRO 549

ASP 513 0.06 ILE 518 -0.00 PRO 558

ASP 513 0.06 ARG 519 -0.00 PRO 558

PRO 549 0.05 MET 520 -0.00 ILE 518

PRO 549 0.06 LYS 521 -0.00 CYS 556

PRO 549 0.05 PRO 522 -0.00 THR 551

PRO 549 0.05 ASP 523 -0.00 ASN 525

PRO 549 0.05 GLU 524 -0.00 ASP 523

PRO 549 0.05 ASN 525 -0.00 ASP 523

PRO 549 0.05 GLY 526 -0.00 CYS 590

PRO 549 0.05 ARG 527 -0.00 VAL 16

ASP 513 0.05 PHE 528 -0.00 VAL 16

ASP 513 0.05 GLY 529 -0.00 ALA 548

ASP 513 0.05 PHE 530 -0.00 SER 545

ASP 513 0.05 ASN 531 -0.00 SER 545

ASP 513 0.06 VAL 532 -0.00 VAL 542

ASP 513 0.06 LYS 533 -0.00 HIS 579

ASP 513 0.06 GLY 534 -0.00 VAL 542

ASP 513 0.07 GLY 535 -0.00 GLN 538

ASP 513 0.07 TYR 536 -0.00 GLY 550

ASP 513 0.07 ASP 537 -0.00 GLY 550

ASP 513 0.06 GLN 538 -0.00 GLY 550

ASP 513 0.07 LYS 539 -0.01 GLY 550

ASP 513 0.06 MET 540 -0.00 GLY 550

ASP 513 0.06 PRO 541 -0.00 GLY 550

ASP 513 0.06 VAL 542 -0.00 GLY 534

ASP 513 0.06 ILE 543 -0.00 GLN 565

ASP 513 0.06 VAL 544 -0.00 GLN 565

ASP 513 0.05 SER 545 -0.00 PHE 530

ASP 513 0.05 ARG 546 -0.00 SER 545

ASP 513 0.05 VAL 547 -0.00 ALA 548

ASP 513 0.04 ALA 548 -0.00 VAL 547

ASP 513 0.04 PRO 549 -0.00 VAL 547

PRO 549 0.04 GLY 550 -0.00 CYS 556

PRO 549 0.05 THR 551 -0.00 PRO 522

PRO 549 0.05 PRO 552 -0.00 CYS 556

ASP 513 0.05 ALA 553 -0.00 CYS 556

ASP 513 0.05 ASP 554 -0.00 CYS 556

PRO 549 0.05 LEU 555 -0.00 CYS 556

PRO 549 0.05 CYS 556 -0.00 LEU 555

PRO 549 0.05 VAL 557 -0.00 LEU 600

ASP 513 0.05 PRO 558 -0.00 LEU 560

ASP 513 0.05 ARG 559 -0.00 LEU 560

ASP 513 0.05 LEU 560 -0.00 ARG 559

ASP 513 0.05 ASN 561 -0.00 GLU 562

ASP 513 0.05 GLU 562 -0.00 ASN 561

ASP 513 0.05 GLY 563 -0.00 PRO 549

ASP 513 0.06 ASP 564 -0.00 PRO 549

ASP 513 0.06 GLN 565 -0.00 PRO 549

ASP 513 0.06 VAL 566 -0.00 PRO 549

ASP 513 0.07 VAL 567 -0.00 PRO 549

ASP 513 0.07 LEU 568 -0.00 PRO 549

ASP 513 0.07 ILE 569 -0.00 PHE 528

ASP 513 0.07 ASN 570 -0.00 GLY 571

ASP 513 0.07 GLY 571 -0.00 ILE 574

ASP 513 0.08 ARG 572 -0.00 ILE 574

ASP 513 0.08 ASP 573 -0.00 PRO 549

ASP 513 0.08 ILE 574 -0.00 PRO 549

ASP 513 0.08 ALA 575 -0.00 PRO 549

ASP 513 0.08 GLU 576 -0.00 PRO 549

ASP 513 0.08 HIS 577 -0.00 ALA 575

ASP 513 0.07 THR 578 -0.00 ASP 580

ASP 513 0.07 HIS 579 -0.00 LYS 533

ASP 513 0.07 ASP 580 -0.00 THR 578

ASP 513 0.07 GLN 581 -0.00 VAL 582

ASP 513 0.07 VAL 582 -0.00 GLN 581

ASP 513 0.06 VAL 583 -0.00 LYS 587

ASP 513 0.07 LEU 584 -0.00 PHE 585

ASP 513 0.07 PHE 585 -0.00 LEU 584

ASP 513 0.06 ILE 586 -0.00 ILE 569

ASP 513 0.06 LYS 587 -0.00 PHE 585

ASP 513 0.06 ALA 588 -0.00 ALA 588

ASP 513 0.06 SER 589 -0.00 ALA 588

PRO 549 0.06 CYS 590 -0.00 CYS 590

PRO 549 0.06 GLU 596 -0.00 CYS 590

ASP 513 0.06 LEU 597 -0.00 ALA 588

ASP 513 0.06 MET 598 -0.06 MET 598

ASP 513 0.06 MET 598 -0.06 MET 598

ASP 513 0.06 LEU 599 -0.00 LEU 600

ASP 513 0.06 LEU 600 -0.00 PRO 549

ASP 513 0.06 VAL 601 -0.00 PRO 549

ASP 513 0.06 ARG 602 -0.00 PRO 549

ASP 513 0.06 PRO 603 -0.00 PRO 549

ASP 513 0.06 ASN 604 -0.00 PRO 549

PRO 549 0.06 ASP 513 -0.00 VAL 542

PRO 549 0.06 ASN 514 -0.00 LEU 517

PRO 549 0.07 LEU 515 -0.00 LEU 517

PRO 549 0.07 VAL 516 -0.00 LEU 517

PRO 549 0.07 LEU 517 -0.00 ILE 518

PRO 549 0.07 ILE 518 -0.00 LEU 517

PRO 549 0.08 ARG 519 -0.00 MET 598

PRO 549 0.08 MET 520 -0.00 PHE 528

GLU 562 0.09 LYS 521 -0.00 CYS 556

GLU 562 0.09 PRO 522 -0.00 ASN 525

GLU 562 0.10 ASP 523 -0.00 THR 551

GLU 562 0.11 GLU 524 -0.00 THR 551

GLU 562 0.11 ASN 525 -0.00 ARG 527

GLU 562 0.10 GLY 526 -0.00 ASN 525

GLU 562 0.10 ARG 527 -0.00 ASN 525

PRO 549 0.09 PHE 528 -0.00 ALA 553

PRO 549 0.10 GLY 529 -0.00 ALA 553

PRO 549 0.09 PHE 530 -0.00 VAL 547

PRO 549 0.09 ASN 531 -0.00 ARG 546

PRO 549 0.08 VAL 532 -0.00 LYS 533

PRO 549 0.08 LYS 533 -0.00 VAL 544

PRO 549 0.07 GLY 534 -0.00 GLY 535

PRO 549 0.07 GLY 535 -0.00 HIS 579

PRO 549 0.06 TYR 536 -0.00 HIS 577

PRO 549 0.06 ASP 537 -0.00 GLN 538

PRO 549 0.07 GLN 538 -0.00 ASP 537

PRO 549 0.06 LYS 539 -0.00 ASP 537

PRO 549 0.07 MET 540 -0.00 LYS 539

PRO 549 0.07 PRO 541 -0.00 VAL 542

PRO 549 0.07 VAL 542 -0.00 VAL 566

PRO 549 0.08 ILE 543 -0.00 VAL 544

PRO 549 0.08 VAL 544 -0.00 ILE 543

PRO 549 0.09 SER 545 -0.00 LYS 533

PRO 549 0.10 ARG 546 -0.00 ASN 531

PRO 549 0.10 VAL 547 -0.00 PHE 530

PRO 549 0.11 ALA 548 -0.00 PHE 530

PRO 549 0.11 PRO 549 -0.00 LYS 533

PRO 549 0.11 GLY 550 -0.00 ASP 554

PRO 549 0.10 THR 551 -0.00 ASP 523

PRO 549 0.09 PRO 552 -0.00 CYS 556

PRO 549 0.09 ALA 553 -0.00 PHE 528

PRO 549 0.10 ASP 554 -0.00 GLY 550

PRO 549 0.09 LEU 555 -0.00 PRO 552

PRO 549 0.09 CYS 556 -0.00 PRO 552

PRO 549 0.08 VAL 557 -0.00 ASN 561

PRO 549 0.08 PRO 558 -0.00 ASN 561

PRO 549 0.09 ARG 559 -0.00 ASN 561

PRO 549 0.08 LEU 560 -0.00 ASN 561

PRO 549 0.09 ASN 561 -0.00 ARG 559

PRO 549 0.09 GLU 562 -0.00 ASP 564

PRO 549 0.08 GLY 563 -0.00 ASP 564

PRO 549 0.08 ASP 564 -0.00 GLY 563

PRO 549 0.07 GLN 565 -0.00 GLY 563

PRO 549 0.07 VAL 566 -0.00 VAL 542

PRO 549 0.07 VAL 567 -0.00 HIS 577

PRO 549 0.06 LEU 568 -0.00 GLY 563

PRO 549 0.07 ILE 569 -0.00 ASP 573

GLU 562 0.07 ASN 570 -0.00 LEU 597

GLU 562 0.06 GLY 571 -0.00 PHE 585

PRO 549 0.06 ARG 572 -0.00 ASP 573

PRO 549 0.06 ASP 573 -0.00 ARG 572

PRO 549 0.06 ILE 574 -0.00 HIS 577

PRO 549 0.06 ALA 575 -0.00 GLU 576

PRO 549 0.05 GLU 576 -0.00 ALA 575

PRO 549 0.06 HIS 577 -0.00 ILE 574

PRO 549 0.06 THR 578 -0.00 VAL 582

PRO 549 0.07 HIS 579 -0.00 GLY 535

PRO 549 0.07 ASP 580 -0.00 VAL 583

PRO 549 0.06 GLN 581 -0.00 GLN 581

PRO 549 0.07 VAL 582 -0.00 GLY 535

PRO 549 0.08 VAL 583 -0.00 ASP 580

ARG 546 0.07 LEU 584 -0.00 ALA 588

GLU 562 0.07 PHE 585 -0.00 ASP 573

PRO 549 0.08 ILE 586 -0.00 ASN 570

GLU 562 0.08 LYS 587 -0.00 CYS 590

GLU 562 0.07 ALA 588 -0.00 LYS 587

GLU 562 0.08 SER 589 -0.00 LYS 587

GLU 562 0.08 CYS 590 -0.00 GLU 591

GLY 563 0.08 GLU 591 -0.00 GLY 595

GLU 562 0.08 GLY 595 -0.00 GLU 591

GLU 562 0.08 GLU 596 -0.00 MET 520

GLU 562 0.08 LEU 597 -0.00 ASN 570

PRO 549 0.07 MET 598 -0.00 LEU 599

PRO 549 0.07 LEU 599 -0.00 MET 598

PRO 549 0.07 LEU 600 -0.00 ILE 518

PRO 549 0.07 VAL 601 -0.00 PRO 603

PRO 549 0.07 ARG 602 -0.00 PRO 603

PRO 549 0.07 PRO 603 -0.00 ARG 602

PRO 549 0.07 ASN 604 -0.00 LEU 517

ILE 12 0.03 ILE 12 -0.00 GLU 13

MET 540 0.03 GLU 13 -0.00 HIS 579

GLY 563 0.04 SER 14 -0.00 VAL 16

GLY 563 0.04 ASP 15 -0.00 VAL 16

GLY 563 0.05 VAL 16 -0.00 ASP 15

ASP 513 0.13 ILE 12 -0.00 GLU 13

ASP 513 0.11 GLU 13 -0.00 ILE 12

ASP 513 0.10 SER 14 -0.00 LEU 584

GLY 571 0.09 ASP 15 -0.00 SER 545

GLY 571 0.08 VAL 16 -0.00 SER 14

ASP 513 0.05 ILE 12 -0.00 GLU 13

ASP 513 0.05 GLU 13 -0.00 ILE 12

ASP 513 0.05 SER 14 -0.00 ASN 531

ASP 513 0.05 ASP 15 -0.00 SER 14

ASP 513 0.05 VAL 16 -0.00 PHE 528

PRO 549 0.08 ILE 12 -0.00 LYS 539

PRO 549 0.09 GLU 13 -0.00 GLY 535

PRO 549 0.09 SER 14 -0.00 GLU 13

PRO 549 0.10 ASP 15 -0.00 VAL 16

PRO 549 0.09 VAL 16 -0.00 ASP 15

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).
Between 2015 and 2025, it was hosted by US2B (Nantes).
Last modification: december 26th, 2025.

Should you encounter any unexpected behaviour, please let us know. elNémo has been hacked on november 27th. It has been moved away and runs again. **Still some additional cleaning from time to time** Sorry for the inconvenience.

*** PROTEIN BINDING 10-JUN-10 3NFL ***

CA distance fluctuations for 2602021513101103345

--- normal mode 9 ---

Should you encounter any unexpected behaviour,
please let us know.
elNémo has been hacked on november 27th.
It has been moved away and runs again.
Still some additional cleaning from time to time
Sorry for the inconvenience.

* PROTEIN BINDING 10-JUN-10 3NFL *