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

* TEST *

CA distance fluctuations for 2502031613291658206

--- normal mode 11 ---

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
GLU 524 0.33 ASP 513 -0.10 ASN 604

ASN 525 0.21 ASN 514 -0.08 PRO 558

GLU 596 0.19 LEU 515 -0.04 ARG 546

ASP 513 0.17 VAL 516 -0.09 ARG 546

ASP 513 0.18 LEU 517 -0.14 ARG 12

ASP 513 0.18 ILE 518 -0.19 ARG 12

ASP 513 0.20 ARG 519 -0.26 ARG 12

ASP 513 0.21 MET 520 -0.29 ARG 12

ASP 513 0.23 LYS 521 -0.33 ARG 12

ASP 513 0.25 PRO 522 -0.33 ARG 12

ASP 513 0.21 ASP 523 -0.42 GLN 581

ASP 513 0.21 GLU 524 -0.62 PHE 585

ASP 513 0.26 ASN 525 -0.66 GLN 581

ASP 513 0.28 GLY 526 -0.51 LEU 584

ASP 513 0.26 ARG 527 -0.34 GLN 581

ASP 513 0.23 PHE 528 -0.27 THR 11

ASP 513 0.21 GLY 529 -0.23 GLU 10

ASP 513 0.21 PHE 530 -0.18 GLU 10

GLY 571 0.25 ASN 531 -0.14 GLU 10

GLY 571 0.27 VAL 532 -0.11 GLY 535

ARG 572 0.28 LYS 533 -0.09 GLY 535

LEU 584 0.31 GLY 534 -0.17 GLY 535

ASN 525 0.39 GLY 535 -0.17 GLY 534

ASP 580 0.49 TYR 536 -0.12 GLY 534

ASP 580 0.58 ASP 537 -0.10 GLY 8

ASP 580 0.44 GLN 538 -0.13 GLY 8

ASP 580 0.44 LYS 539 -0.10 GLY 8

ASN 525 0.35 MET 540 -0.08 SER 545

ASN 525 0.35 MET 540 -0.09 SER 545

ASN 525 0.36 PRO 541 -0.05 TYR 536

ASN 525 0.33 VAL 542 -0.08 ALA 575

ASN 525 0.25 ILE 543 -0.08 MET 540

GLY 571 0.22 VAL 544 -0.06 GLU 10

GLY 571 0.22 SER 545 -0.09 MET 540

ASP 513 0.19 ARG 546 -0.11 GLU 10

ASP 513 0.19 VAL 547 -0.15 GLU 10

ASP 513 0.18 ALA 548 -0.18 GLU 10

ASP 513 0.16 PRO 549 -0.19 GLU 10

ASP 513 0.16 GLY 550 -0.23 GLU 591

ASP 513 0.19 THR 551 -0.24 GLU 10

ASP 513 0.19 PRO 552 -0.26 ARG 12

ASP 513 0.19 ALA 553 -0.21 ARG 12

ASP 513 0.17 ASP 554 -0.19 ARG 12

ASP 513 0.16 LEU 555 -0.24 GLU 591

ASP 513 0.17 CYS 556 -0.23 ARG 12

ASP 513 0.16 VAL 557 -0.21 ARG 12

ASP 513 0.16 PRO 558 -0.16 ARG 12

ASP 513 0.16 ARG 559 -0.15 ARG 12

ASP 513 0.18 LEU 560 -0.14 GLU 10

ASP 513 0.17 ASN 561 -0.09 GLU 10

ASP 513 0.18 GLU 562 -0.06 GLU 10

GLY 571 0.19 GLY 563 -0.06 ASP 513

GLY 571 0.19 ASP 564 -0.05 MET 540

ASN 525 0.26 GLN 565 -0.06 VAL 601

ASN 525 0.30 VAL 566 -0.10 ALA 575

ASN 525 0.38 VAL 567 -0.13 ALA 575

ASN 525 0.41 LEU 568 -0.13 ALA 575

GLU 596 0.33 ILE 569 -0.17 GLU 10

GLY 595 0.39 ASN 570 -0.25 ARG 12

GLU 524 0.49 GLY 571 -0.13 ARG 546

ASN 525 0.67 ARG 572 -0.12 GLU 10

ASN 525 0.61 ASP 573 -0.09 GLY 571

ASN 525 0.57 ILE 574 -0.09 HIS 577

ASN 525 0.53 ALA 575 -0.13 LEU 568

ASN 525 0.61 GLU 576 -0.09 GLY 534

ASN 525 0.56 HIS 577 -0.09 HIS 579

ASP 580 0.54 THR 578 -0.15 HIS 579

LEU 584 0.40 HIS 579 -0.15 THR 578

LEU 584 0.53 ASP 580 -0.13 ASN 525

LEU 584 0.61 GLN 581 -0.10 GLY 9

LEU 584 0.38 VAL 582 -0.13 GLU 10

GLY 571 0.34 VAL 583 -0.26 GLU 10

ALA 588 0.41 LEU 584 -0.33 GLU 10

GLU 596 0.41 PHE 585 -0.30 GLU 10

GLU 596 0.30 ILE 586 -0.30 THR 11

ALA 588 0.35 LYS 587 -0.39 THR 11

PHE 585 0.40 ALA 588 -0.48 ARG 12

GLU 596 0.35 SER 589 -0.39 ARG 12

GLU 596 0.47 CYS 590 -0.40 GLY 526

GLY 595 0.54 GLU 591 -0.43 ARG 12

GLY 595 0.46 ARG 592 -0.36 ARG 12

GLY 595 0.42 HIS 593 -0.50 ASN 525

SER 594 0.29 SER 594 -0.63 GLU 524

ASP 513 0.28 GLY 595 -0.49 GLY 526

ASP 513 0.25 GLU 596 -0.32 ARG 12

GLY 595 0.23 LEU 597 -0.32 ARG 12

GLY 595 0.25 MET 598 -0.24 ARG 12

GLY 595 0.24 LEU 599 -0.16 GLU 10

GLU 596 0.24 LEU 600 -0.10 ALA 575

GLU 596 0.22 VAL 601 -0.06 ALA 575

ASN 525 0.23 ARG 602 -0.04 ILE 518

ASP 513 0.17 PRO 603 -0.07 ASP 513

ASN 525 0.19 ASN 604 -0.10 ASP 513

GLY 571 0.44 HIS 512 -0.41 PRO 541

GLY 571 0.45 ASP 513 -0.34 LYS 539

SER 594 0.30 ASN 514 -0.24 PRO 541

GLU 591 0.34 LEU 515 -0.25 PRO 541

SER 594 0.28 VAL 516 -0.17 PRO 541

SER 594 0.37 LEU 517 -0.17 PRO 541

GLU 576 0.34 ILE 518 -0.22 GLY 571

GLU 576 0.38 ARG 519 -0.33 GLY 571

GLU 576 0.40 MET 520 -0.26 GLY 571

GLU 576 0.44 LYS 521 -0.24 GLU 524

GLU 576 0.48 PRO 522 -0.29 GLU 524

GLU 576 0.51 ASP 523 -0.41 SER 594

ARG 572 0.58 GLU 524 -0.63 SER 594

ARG 572 0.67 ASN 525 -0.52 SER 594

GLU 576 0.54 GLY 526 -0.50 SER 594

GLU 576 0.56 ARG 527 -0.37 SER 594

GLU 576 0.48 PHE 528 -0.32 GLU 524

GLU 576 0.44 GLY 529 -0.29 GLU 524

GLU 576 0.35 PHE 530 -0.32 GLU 524

GLU 576 0.31 ASN 531 -0.37 GLU 524

ASP 537 0.33 VAL 532 -0.38 GLU 524

ASP 537 0.30 LYS 533 -0.37 GLU 524

ASP 537 0.34 GLY 534 -0.38 ASN 525

ASP 537 0.41 GLY 535 -0.43 GLU 524

ASP 537 0.42 TYR 536 -0.44 ASN 525

ASP 537 0.45 ASP 537 -0.48 ASN 525

ASP 537 0.37 GLN 538 -0.44 ASN 525

ASP 537 0.34 LYS 539 -0.41 HIS 512

ASP 537 0.30 MET 540 -0.41 HIS 512

ASP 537 0.31 PRO 541 -0.41 HIS 512

ASP 537 0.32 VAL 542 -0.33 GLU 524

ASP 537 0.26 ILE 543 -0.29 GLU 524

ASP 537 0.26 VAL 544 -0.28 GLU 524

MET 540 0.20 SER 545 -0.30 GLU 524

ASP 537 0.20 ARG 546 -0.30 GLU 524

GLU 576 0.25 VAL 547 -0.27 GLU 524

GLU 576 0.29 ALA 548 -0.30 SER 594

GLU 576 0.27 PRO 549 -0.28 SER 594

GLU 576 0.35 GLY 550 -0.27 SER 594

GLU 576 0.41 THR 551 -0.30 SER 594

GLU 576 0.42 PRO 552 -0.23 GLU 524

GLU 576 0.38 ALA 553 -0.23 GLU 524

GLU 576 0.33 ASP 554 -0.20 GLU 524

GLU 576 0.35 LEU 555 -0.17 GLY 571

GLU 576 0.36 CYS 556 -0.20 GLY 571

GLU 576 0.32 VAL 557 -0.18 GLY 571

GLU 576 0.30 PRO 558 -0.13 GLY 571

GLU 576 0.30 ARG 559 -0.14 PRO 603

GLU 576 0.30 ARG 559 -0.14 PRO 603

GLU 576 0.30 LEU 560 -0.17 PRO 603

ASP 537 0.22 ASN 561 -0.22 PRO 603

ASP 537 0.18 GLU 562 -0.22 GLU 524

ALA 575 0.17 GLY 563 -0.20 GLU 524

ASP 537 0.22 ASP 564 -0.18 GLU 524

ASP 537 0.26 GLN 565 -0.22 HIS 512

ASP 537 0.32 VAL 566 -0.22 GLU 524

ASP 537 0.33 VAL 567 -0.25 LYS 539

ASP 537 0.35 LEU 568 -0.21 LYS 539

GLN 581 0.40 ILE 569 -0.27 GLU 524

GLN 581 0.40 ASN 570 -0.33 LEU 597

ASP 513 0.45 GLY 571 -0.34 MET 598

GLU 3 0.48 ARG 572 -0.25 GLU 524

GLU 3 0.40 ASP 573 -0.25 GLU 524

ASP 537 0.39 ILE 574 -0.39 GLU 524

ASP 537 0.36 ALA 575 -0.35 GLU 524

ASP 537 0.40 GLU 576 -0.45 GLU 524

ASP 537 0.45 HIS 577 -0.52 GLU 524

ASP 537 0.50 THR 578 -0.53 ASN 525

ASP 537 0.49 HIS 579 -0.51 ASN 525

ASP 537 0.58 ASP 580 -0.56 ASN 525

ASP 537 0.50 GLN 581 -0.66 ASN 525

ASP 537 0.46 VAL 582 -0.52 GLU 524

THR 578 0.51 VAL 583 -0.52 ASN 525

GLN 581 0.61 LEU 584 -0.60 ASN 525

GLN 581 0.45 PHE 585 -0.62 GLU 524

GLN 581 0.46 ILE 586 -0.48 GLU 524

GLN 581 0.54 LYS 587 -0.49 GLU 524

GLN 581 0.45 ALA 588 -0.55 GLU 524

MET 598 0.43 SER 589 -0.45 GLU 524

MET 598 0.38 CYS 590 -0.33 GLU 524

ASP 513 0.39 GLU 591 -0.49 GLU 524

GLU 591 0.39 SER 594 -0.33 GLU 524

GLU 591 0.54 GLY 595 -0.24 GLU 524

GLU 591 0.49 GLU 596 -0.27 ASN 570

GLN 581 0.41 LEU 597 -0.33 ASN 570

SER 589 0.43 MET 598 -0.34 GLY 571

THR 578 0.36 LEU 599 -0.21 LEU 568

THR 578 0.35 LEU 600 -0.20 PRO 541

ASP 537 0.28 VAL 601 -0.21 PRO 541

LEU 568 0.25 ARG 602 -0.22 PRO 541

ASN 604 0.25 PRO 603 -0.22 ASN 561

PRO 603 0.25 ASN 604 -0.17 ASP 513

ARG 572 0.41 SER 1 -0.31 GLY 9

ARG 572 0.45 TRP 2 -0.38 ASN 525

ARG 572 0.48 GLU 3 -0.49 ASN 525

ARG 572 0.43 SER 4 -0.29 GLY 9

ARG 572 0.43 SER 4 -0.29 GLY 9

ARG 572 0.38 HIS 5 -0.25 GLY 9

ARG 572 0.37 LYS 6 -0.17 GLY 9

ARG 572 0.33 SER 7 -0.10 GLY 9

ARG 572 0.31 GLY 8 -0.13 GLN 538

ARG 572 0.34 GLY 9 -0.11 GLN 538

ARG 572 0.31 GLU 10 -0.10 GLY 535

ARG 572 0.33 THR 11 -0.16 GLY 9

GLY 571 0.30 ARG 12 -0.21 GLY 9

GLY 571 0.30 LEU 13 -0.25 GLY 9

ASP 537 0.32 GLY 9 -0.44 ASN 525

ASP 537 0.30 GLU 10 -0.43 ASN 525

ASP 537 0.40 THR 11 -0.45 ALA 588

GLU 576 0.42 ARG 12 -0.48 ALA 588

GLU 576 0.51 LEU 13 -0.40 GLU 524

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.

*** TEST ***

CA distance fluctuations for 2502031613291658206

--- normal mode 11 ---

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

* TEST *