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

* 1ERR monomer *

CA distance fluctuations for 2404102156053369258

--- normal mode 10 ---

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
ALA 318 0.24 ALA 307 -0.33 HIS 501

ALA 318 0.21 LEU 308 -0.43 LEU 497

GLU 470 0.24 SER 309 -0.35 LEU 497

GLU 470 0.19 LEU 310 -0.26 LEU 497

GLU 470 0.13 THR 311 -0.21 LEU 497

ALA 493 0.11 ALA 312 -0.16 LEU 497

ALA 493 0.30 ASP 313 -0.14 ASP 545

ALA 493 0.25 GLN 314 -0.17 ASP 545

ALA 493 0.20 MET 315 -0.16 ASP 545

ALA 493 0.32 VAL 316 -0.12 ASP 545

ALA 493 0.36 SER 317 -0.12 ASP 545

ALA 493 0.26 ALA 318 -0.16 HIS 547

ALA 493 0.26 LEU 319 -0.11 LYS 362

ALA 493 0.34 LEU 320 -0.08 MET 543

ALA 493 0.30 ASP 321 -0.11 MET 543

ALA 493 0.25 ALA 322 -0.12 MET 543

ALA 493 0.28 GLU 323 -0.05 LEU 536

ALA 493 0.24 PRO 324 -0.07 TRP 383

ALA 493 0.25 PRO 325 -0.16 LEU 387

ALA 546 0.25 ILE 326 -0.18 LEU 387

ALA 546 0.39 LEU 327 -0.16 TYR 526

ALA 546 0.42 TYR 328 -0.19 TYR 526

ALA 546 0.50 SER 329 -0.20 TYR 526

ALA 546 0.60 GLU 330 -0.21 TYR 526

ALA 546 0.55 TYR 331 -0.19 TYR 526

ALA 546 0.51 ASP 332 -0.17 LEU 408

ALA 546 0.59 PRO 333 -0.15 MET 528

ALA 546 0.52 THR 334 -0.17 LEU 410

ALA 546 0.47 ARG 335 -0.17 ASP 411

ALA 546 0.43 PRO 336 -0.27 GLN 414

ALA 546 0.46 PHE 337 -0.12 HIS 513

ALA 546 0.46 SER 338 -0.12 MET 528

LEU 539 0.45 GLU 339 -0.12 MET 528

LEU 539 0.53 ALA 340 -0.23 MET 528

ALA 546 0.54 SER 341 -0.20 MET 528

ALA 546 0.49 MET 342 -0.18 MET 528

LEU 539 0.53 MET 343 -0.22 MET 528

ALA 546 0.59 GLY 344 -0.27 TYR 526

ALA 546 0.56 LEU 345 -0.24 TYR 526

ALA 546 0.48 LEU 346 -0.27 LEU 525

MET 543 0.57 THR 347 -0.35 TYR 526

ALA 546 0.66 ASN 348 -0.29 TYR 526

ALA 546 0.52 LEU 349 -0.25 TYR 526

ALA 546 0.44 ALA 350 -0.23 TYR 526

MET 543 0.63 ASP 351 -0.23 TYR 526

ALA 546 0.64 ARG 352 -0.19 TYR 526

ALA 546 0.39 GLU 353 -0.14 TYR 526

ALA 546 0.36 LEU 354 -0.18 VAL 355

HIS 547 0.54 VAL 355 -0.18 LEU 354

HIS 547 0.33 HIS 356 -0.12 LEU 536

ARG 352 0.28 MET 357 -0.09 LEU 536

ARG 352 0.39 ILE 358 -0.18 ASN 359

ARG 352 0.36 ASN 359 -0.20 MET 543

ARG 352 0.25 TRP 360 -0.13 MET 543

ARG 352 0.27 ALA 361 -0.17 HIS 501

ARG 352 0.34 LYS 362 -0.21 HIS 501

GLU 470 0.27 ARG 363 -0.19 LYS 362

ARG 352 0.21 VAL 364 -0.23 HIS 501

GLU 470 0.22 PRO 365 -0.30 HIS 501

GLU 470 0.26 GLY 366 -0.39 HIS 501

ARG 352 0.26 PHE 367 -0.33 HIS 501

ARG 352 0.33 VAL 368 -0.30 HIS 501

GLU 470 0.37 ASP 369 -0.37 HIS 501

GLU 471 0.33 LEU 370 -0.36 HIS 501

ARG 352 0.30 THR 371 -0.33 HIS 501

ARG 352 0.35 LEU 372 -0.27 HIS 501

ASN 348 0.28 HIS 373 -0.26 HIS 501

ARG 352 0.23 ASP 374 -0.30 HIS 501

ARG 352 0.29 GLN 375 -0.27 HIS 501

ASN 348 0.28 VAL 376 -0.21 HIS 501

GLY 344 0.16 HIS 377 -0.23 HIS 501

ARG 352 0.14 LEU 378 -0.24 HIS 501

THR 347 0.18 LEU 379 -0.17 HIS 501

MET 343 0.17 GLU 380 -0.14 HIS 501

ALA 493 0.09 ALA 382 -0.14 HIS 501

MET 343 0.12 TRP 383 -0.12 VAL 355

LEU 536 0.14 LEU 384 -0.15 ALA 350

ALA 493 0.12 GLU 385 -0.13 ILE 326

ALA 493 0.14 ILE 386 -0.12 ILE 326

ALA 546 0.17 LEU 387 -0.18 ILE 326

ALA 546 0.14 MET 388 -0.15 ILE 326

GLY 494 0.16 ILE 389 -0.13 HIS 476

GLY 494 0.20 GLY 390 -0.14 ILE 326

ALA 546 0.21 LEU 391 -0.10 ILE 514

GLY 494 0.16 VAL 392 -0.16 HIS 476

GLY 494 0.21 TRP 393 -0.14 HIS 476

GLY 494 0.24 ARG 394 -0.10 PRO 406

GLY 494 0.20 SER 395 -0.12 HIS 476

GLY 494 0.21 MET 396 -0.16 HIS 476

GLY 494 0.24 GLU 397 -0.13 PRO 336

ALA 546 0.19 HIS 398 -0.16 PRO 336

ALA 546 0.17 PRO 399 -0.18 PRO 336

ALA 546 0.20 GLY 400 -0.19 PRO 336

ALA 546 0.24 LYS 401 -0.19 PRO 336

ALA 546 0.25 LEU 402 -0.15 PRO 336

ALA 546 0.28 LEU 403 -0.12 ASP 332

ALA 546 0.33 PHE 404 -0.14 LEU 525

ALA 546 0.35 ALA 405 -0.14 TYR 526

ALA 546 0.31 PRO 406 -0.12 TYR 526

ALA 546 0.36 ASN 407 -0.14 TYR 526

ALA 546 0.38 LEU 408 -0.17 ASP 332

ALA 546 0.32 LEU 409 -0.16 THR 334

ALA 546 0.32 LEU 410 -0.20 PRO 336

ALA 546 0.28 ASP 411 -0.23 PRO 336

ALA 546 0.26 ARG 412 -0.19 PRO 336

ALA 546 0.29 ASN 413 -0.22 PRO 336

ALA 546 0.34 GLN 414 -0.27 PRO 336

ALA 546 0.33 GLY 415 -0.18 PRO 336

LEU 539 0.33 LYS 416 -0.15 HIS 513

LEU 539 0.37 CYS 417 -0.13 PRO 336

LEU 539 0.41 VAL 418 -0.12 HIS 513

PRO 535 0.38 GLU 419 -0.13 LYS 520

PRO 535 0.31 GLY 420 -0.17 TYR 459

LEU 539 0.31 MET 421 -0.17 HIS 513

LEU 539 0.27 VAL 422 -0.18 LYS 472

PRO 535 0.23 GLU 423 -0.25 LYS 472

PRO 535 0.22 ILE 424 -0.22 LYS 472

LEU 539 0.23 PHE 425 -0.19 HIS 513

PRO 535 0.19 ASP 426 -0.23 LYS 472

PRO 535 0.16 MET 427 -0.29 HIS 513

LEU 539 0.16 LEU 428 -0.22 LYS 472

ALA 546 0.16 LEU 429 -0.22 HIS 476

PRO 535 0.14 ALA 430 -0.26 HIS 476

PRO 535 0.11 THR 431 -0.27 HIS 476

THR 496 0.14 SER 432 -0.21 HIS 476

THR 496 0.16 SER 433 -0.23 HIS 476

GLN 499 0.15 ARG 434 -0.27 HIS 476

GLN 499 0.19 PHE 435 -0.25 HIS 476

THR 496 0.24 ARG 436 -0.22 HIS 476

GLN 499 0.24 MET 437 -0.25 HIS 476

GLN 499 0.30 MET 438 -0.28 HIS 476

THR 496 0.33 ASN 439 -0.22 HIS 476

LEU 495 0.29 LEU 440 -0.22 HIS 476

GLY 494 0.37 GLN 441 -0.16 HIS 476

ALA 493 0.38 GLY 442 -0.09 HIS 476

ALA 493 0.42 GLU 443 -0.08 HIS 476

ALA 493 0.26 GLU 444 -0.17 HIS 476

ALA 493 0.23 PHE 445 -0.14 HIS 476

ALA 493 0.25 VAL 446 -0.06 LYS 362

ALA 493 0.17 CYS 447 -0.13 HIS 501

ALA 493 0.13 LEU 448 -0.19 HIS 476

ALA 493 0.15 LYS 449 -0.13 HIS 501

ALA 493 0.13 SER 450 -0.19 HIS 501

ASP 484 0.06 ILE 451 -0.28 HIS 501

ALA 493 0.07 ILE 452 -0.22 HIS 501

ARG 352 0.10 LEU 453 -0.22 HIS 501

ARG 352 0.12 LEU 454 -0.33 HIS 501

ASP 480 0.08 ASN 455 -0.39 SER 512

ASP 480 0.06 SER 456 -0.31 SER 512

GLU 380 0.10 GLY 457 -0.26 HIS 501

LEU 378 0.11 VAL 458 -0.40 SER 512

ASP 480 0.10 TYR 459 -0.37 SER 512

ASP 369 0.37 GLU 470 -0.55 GLN 498

ASP 369 0.36 GLU 471 -0.50 HIS 501

LEU 370 0.25 LYS 472 -0.58 HIS 501

GLY 366 0.19 ASP 473 -0.65 HIS 501

GLY 366 0.19 ASP 473 -0.65 HIS 501

GLY 366 0.24 HIS 474 -0.53 HIS 501

VAL 364 0.18 ILE 475 -0.53 HIS 501

ARG 352 0.11 HIS 476 -0.72 HIS 501

ARG 352 0.13 ARG 477 -0.67 HIS 501

ARG 352 0.14 VAL 478 -0.50 HIS 501

ASP 480 0.10 LEU 479 -0.60 HIS 501

LEU 479 0.10 ASP 480 -0.76 HIS 501

ARG 352 0.10 LYS 481 -0.51 HIS 501

ASP 484 0.07 ILE 482 -0.35 HIS 501

ASP 484 0.08 THR 483 -0.53 HIS 501

THR 483 0.08 ASP 484 -0.47 LEU 497

ARG 352 0.06 THR 485 -0.21 LEU 497

LEU 508 0.08 LEU 486 -0.20 HIS 476

LEU 504 0.08 ILE 487 -0.39 ASP 484

LEU 504 0.08 HIS 488 -0.17 ASP 480

MET 490 0.22 LEU 489 -0.13 ASP 480

GLU 443 0.26 MET 490 -0.27 ASP 480

GLU 443 0.19 ALA 491 -0.33 ASP 480

ASP 313 0.23 LYS 492 -0.17 ASP 480

GLU 443 0.42 ALA 493 -0.17 ASP 480

GLN 441 0.37 GLY 494 -0.28 ASP 480

GLN 441 0.36 LEU 495 -0.39 ASP 480

ASN 439 0.33 THR 496 -0.48 ASP 480

ASN 439 0.21 LEU 497 -0.65 ASP 480

ASN 439 0.23 GLN 498 -0.64 ASP 473

ASN 439 0.33 GLN 499 -0.50 ASP 480

GLN 441 0.18 GLN 500 -0.59 ASP 480

ASN 439 0.09 HIS 501 -0.76 ASP 480

MET 438 0.10 GLN 502 -0.59 HIS 476

GLN 499 0.16 ARG 503 -0.48 HIS 476

LEU 489 0.08 LEU 504 -0.55 HIS 476

LEU 489 0.06 ALA 505 -0.62 HIS 476

GLY 442 0.05 GLN 506 -0.47 HIS 476

GLN 499 0.07 LEU 507 -0.42 HIS 476

LEU 486 0.08 LEU 508 -0.52 HIS 476

LEU 507 0.07 LEU 509 -0.47 HIS 476

GLU 444 0.07 ILE 510 -0.35 HIS 476

ALA 493 0.06 LEU 511 -0.36 LYS 472

ILE 514 0.07 SER 512 -0.46 LYS 472

HIS 516 0.10 HIS 513 -0.36 LYS 472

GLY 494 0.09 ILE 514 -0.27 LYS 472

ALA 493 0.08 ARG 515 -0.29 LYS 472

ARG 434 0.11 HIS 516 -0.36 LYS 472

PRO 535 0.12 MET 517 -0.26 LYS 472

PRO 535 0.13 SER 518 -0.19 LYS 472

PRO 535 0.10 ASN 519 -0.25 TYR 459

PRO 535 0.15 LYS 520 -0.25 TYR 459

PRO 535 0.23 GLY 521 -0.20 THR 347

PRO 535 0.22 MET 522 -0.22 THR 347

PRO 535 0.21 GLU 523 -0.21 THR 347

PRO 535 0.32 HIS 524 -0.17 THR 347

PRO 535 0.47 LEU 525 -0.32 THR 347

PRO 535 0.40 TYR 526 -0.35 THR 347

PRO 535 0.35 SER 527 -0.25 THR 347

PRO 535 0.54 MET 528 -0.26 GLY 344

MET 528 0.54 PRO 535 -0.15 VAL 355

LEU 525 0.44 LEU 536 -0.17 VAL 355

ALA 340 0.34 TYR 537 -0.14 HIS 501

ALA 340 0.45 ASP 538 -0.13 HIS 501

THR 347 0.57 LEU 539 -0.18 ASN 359

THR 347 0.49 LEU 540 -0.16 ASN 359

ASN 348 0.45 LEU 541 -0.18 HIS 501

ASN 348 0.59 GLU 542 -0.15 HIS 501

ASN 348 0.63 MET 543 -0.20 ASN 359

ARG 352 0.51 LEU 544 -0.19 HIS 501

ASN 348 0.53 ASP 545 -0.20 HIS 501

ASN 348 0.66 ALA 546 -0.17 SER 309

ARG 352 0.62 HIS 547 -0.16 ALA 318

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.

*** 1ERR monomer ***

CA distance fluctuations for 2404102156053369258

--- normal mode 10 ---

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

* 1ERR monomer *