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

* 5WGD_A *

CA distance fluctuations for 2404102226553446872

--- 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
ARG 352 0.17 LEU 308 -0.31 LEU 497

GLU 330 0.17 SER 309 -0.25 LEU 497

PRO 365 0.18 LEU 310 -0.17 HIS 501

ALA 493 0.13 THR 311 -0.14 ASN 439

LYS 492 0.18 ALA 312 -0.16 GLN 441

LYS 492 0.38 ASP 313 -0.18 GLU 443

ALA 493 0.33 GLN 314 -0.09 GLU 443

ALA 493 0.31 MET 315 -0.08 HIS 501

ALA 493 0.46 VAL 316 -0.12 GLU 443

ALA 493 0.51 SER 317 -0.05 VAL 446

ALA 493 0.41 ALA 318 -0.03 HIS 501

ALA 493 0.40 LEU 319 -0.07 ASP 321

ALA 493 0.51 LEU 320 -0.06 SER 450

ALA 493 0.46 ASP 321 -0.07 SER 450

ALA 493 0.38 ALA 322 -0.07 GLU 542

ALA 493 0.37 GLU 323 -0.07 GLU 542

LEU 372 0.32 PRO 324 -0.09 VAL 355

LEU 372 0.32 PRO 325 -0.12 GLU 353

LEU 372 0.33 ILE 326 -0.08 ASP 351

LEU 372 0.40 LEU 327 -0.09 ASP 351

LEU 372 0.41 TYR 328 -0.09 ASN 348

LEU 372 0.42 SER 329 -0.08 VAL 534

LEU 372 0.51 GLU 330 -0.17 LEU 408

LEU 372 0.41 TYR 331 -0.28 LEU 408

LEU 372 0.51 ASP 332 -0.26 LEU 410

LEU 372 0.38 PRO 333 -0.53 LEU 410

LEU 372 0.49 THR 334 -0.46 ASP 411

LEU 372 0.48 ARG 335 -0.45 ASN 413

LEU 372 0.34 PRO 336 -0.48 ASN 413

LEU 372 0.30 PHE 337 -0.32 GLN 414

LEU 372 0.27 SER 338 -0.14 HIS 513

LEU 372 0.24 GLU 339 -0.15 HIS 513

LEU 372 0.31 ALA 340 -0.11 ALA 505

LEU 372 0.36 SER 341 -0.11 GLU 330

LEU 372 0.31 MET 342 -0.14 HIS 513

LEU 372 0.31 MET 343 -0.12 ALA 505

LEU 372 0.39 GLY 344 -0.10 VAL 534

LEU 372 0.40 LEU 345 -0.10 HIS 513

LEU 372 0.34 LEU 346 -0.11 ALA 505

LEU 372 0.40 THR 347 -0.09 ALA 505

LEU 372 0.50 ASN 348 -0.10 PRO 535

LEU 372 0.45 LEU 349 -0.08 TYR 328

LEU 372 0.43 ALA 350 -0.08 HIS 501

LEU 372 0.55 ASP 351 -0.10 ARG 352

LEU 372 0.59 ARG 352 -0.10 ASP 351

LEU 372 0.50 GLU 353 -0.12 PRO 325

LEU 372 0.54 LEU 354 -0.10 PRO 325

LEU 372 0.67 VAL 355 -0.14 HIS 356

LEU 372 0.51 HIS 356 -0.14 VAL 355

LEU 372 0.42 MET 357 -0.10 GLU 542

LEU 372 0.58 ILE 358 -0.16 TRP 383

LEU 372 0.48 ASN 359 -0.13 ALA 546

ASP 332 0.30 TRP 360 -0.11 ASN 359

ASP 332 0.27 ALA 361 -0.12 HIS 501

ASP 332 0.32 LYS 362 -0.14 GLU 380

ALA 493 0.29 ARG 363 -0.10 GLU 380

ALA 493 0.25 VAL 364 -0.14 HIS 501

ASP 332 0.20 PRO 365 -0.19 HIS 501

ASP 332 0.21 GLY 366 -0.29 HIS 501

ARG 352 0.26 PHE 367 -0.25 HIS 501

VAL 355 0.35 VAL 368 -0.23 HIS 501

ASP 332 0.30 ASP 369 -0.29 HIS 501

VAL 355 0.36 LEU 370 -0.35 HIS 501

VAL 355 0.47 THR 371 -0.33 HIS 501

VAL 355 0.67 LEU 372 -0.25 HIS 501

LEU 539 0.66 HIS 373 -0.31 HIS 501

LEU 539 0.47 ASP 374 -0.36 HIS 501

VAL 355 0.46 GLN 375 -0.25 HIS 501

LEU 539 0.61 VAL 376 -0.20 HIS 501

LEU 539 0.43 HIS 377 -0.25 HIS 501

LEU 539 0.25 LEU 378 -0.25 HIS 501

ASP 351 0.28 LEU 379 -0.17 HIS 501

LEU 539 0.25 GLU 380 -0.18 HIS 501

GLY 457 0.18 CYS 381 -0.20 HIS 501

GLY 457 0.18 CYS 381 -0.20 HIS 501

ASP 332 0.13 ALA 382 -0.18 HIS 501

VAL 376 0.22 TRP 383 -0.16 ILE 358

VAL 376 0.16 LEU 384 -0.13 HIS 501

VAL 376 0.08 GLU 385 -0.16 HIS 501

LEU 372 0.15 ILE 386 -0.13 HIS 501

LEU 372 0.21 LEU 387 -0.12 PRO 325

LEU 372 0.14 MET 388 -0.16 PRO 333

LEU 372 0.11 ILE 389 -0.16 PRO 333

LEU 372 0.19 GLY 390 -0.13 PRO 333

LEU 372 0.19 LEU 391 -0.19 PRO 333

LEU 372 0.13 VAL 392 -0.25 PRO 333

LEU 372 0.14 TRP 393 -0.21 PRO 333

LEU 372 0.19 ARG 394 -0.23 PRO 333

LEU 372 0.16 SER 395 -0.33 PRO 333

LEU 372 0.12 MET 396 -0.32 PRO 333

GLN 499 0.15 GLU 397 -0.35 PRO 333

LEU 372 0.15 HIS 398 -0.44 PRO 333

LEU 429 0.12 PRO 399 -0.45 PRO 333

LEU 372 0.12 GLY 400 -0.46 PRO 333

LEU 372 0.16 LYS 401 -0.49 PRO 333

LEU 372 0.18 LEU 402 -0.39 PRO 333

LEU 372 0.23 LEU 403 -0.34 PRO 333

LEU 372 0.27 PHE 404 -0.21 PRO 333

LEU 372 0.31 ALA 405 -0.15 PRO 333

LEU 372 0.28 PRO 406 -0.18 PRO 333

LEU 372 0.31 ASN 407 -0.21 PRO 333

LEU 372 0.29 LEU 408 -0.33 PRO 333

LEU 372 0.24 LEU 409 -0.49 PRO 333

LEU 372 0.22 LEU 410 -0.53 PRO 333

LEU 372 0.17 ASP 411 -0.52 PRO 333

LEU 372 0.14 ARG 412 -0.42 PRO 333

LEU 372 0.16 ASN 413 -0.48 PRO 336

LEU 372 0.20 GLN 414 -0.44 PRO 333

LEU 372 0.18 GLY 415 -0.32 PRO 333

LEU 372 0.16 LYS 416 -0.33 PRO 336

LEU 372 0.19 CYS 417 -0.30 PRO 336

LEU 372 0.19 VAL 418 -0.17 HIS 513

LEU 372 0.13 GLU 419 -0.19 HIS 516

SER 527 0.09 GLY 420 -0.24 HIS 516

LEU 372 0.12 MET 421 -0.22 HIS 516

LEU 372 0.11 VAL 422 -0.28 PRO 336

HIS 524 0.13 GLU 423 -0.29 HIS 513

GLU 523 0.10 ILE 424 -0.27 HIS 513

LEU 372 0.11 PHE 425 -0.30 PRO 333

PRO 399 0.10 ASP 426 -0.32 PRO 333

PRO 399 0.10 MET 427 -0.34 HIS 513

LYS 520 0.09 LEU 428 -0.29 PRO 333

PRO 399 0.12 LEU 429 -0.36 PRO 333

LYS 520 0.10 ALA 430 -0.33 PRO 333

MET 517 0.10 THR 431 -0.30 PRO 333

LYS 520 0.09 SER 432 -0.32 PRO 333

LYS 520 0.08 SER 433 -0.36 PRO 333

HIS 513 0.08 ARG 434 -0.32 PRO 333

HIS 513 0.07 PHE 435 -0.27 PRO 333

GLN 499 0.12 ARG 436 -0.30 PRO 333

GLN 498 0.09 MET 437 -0.29 PRO 333

GLN 499 0.15 MET 438 -0.27 ALA 493

GLN 499 0.25 ASN 439 -0.24 LEU 489

GLN 499 0.23 LEU 440 -0.21 PRO 333

LEU 495 0.32 GLN 441 -0.17 ASP 313

ALA 493 0.37 GLY 442 -0.14 ASP 313

ALA 493 0.47 GLU 443 -0.18 ASP 313

ALA 493 0.24 GLU 444 -0.15 ILE 482

ALA 493 0.21 PHE 445 -0.13 PRO 333

ALA 493 0.29 VAL 446 -0.07 PRO 333

ALA 493 0.21 CYS 447 -0.11 GLY 366

ALA 493 0.12 LEU 448 -0.15 HIS 501

ALA 493 0.16 LYS 449 -0.13 HIS 501

ALA 493 0.17 SER 450 -0.17 HIS 501

ALA 493 0.17 SER 450 -0.17 HIS 501

GLU 353 0.08 ILE 451 -0.28 HIS 501

GLU 353 0.08 ILE 452 -0.25 HIS 501

GLU 353 0.16 LEU 453 -0.22 HIS 501

ARG 352 0.17 LEU 454 -0.33 HIS 501

LEU 539 0.14 ASN 455 -0.40 HIS 501

ALA 546 0.13 SER 456 -0.32 HIS 501

LEU 539 0.21 GLY 457 -0.32 HIS 501

LEU 539 0.22 VAL 458 -0.40 HIS 501

ALA 546 0.22 TYR 459 -0.45 HIS 501

GLU 542 0.27 THR 460 -0.37 HIS 501

LEU 539 0.22 ASP 473 -0.52 GLN 498

LEU 539 0.22 HIS 474 -0.45 HIS 501

LEU 539 0.22 ILE 475 -0.46 HIS 501

LEU 539 0.18 HIS 476 -0.58 HIS 501

LEU 539 0.16 ARG 477 -0.52 HIS 501

ARG 352 0.16 VAL 478 -0.41 HIS 501

ARG 352 0.12 LEU 479 -0.49 HIS 501

LYS 481 0.12 ASP 480 -0.59 HIS 501

ASP 480 0.12 LYS 481 -0.35 HIS 501

ARG 352 0.09 ILE 482 -0.29 HIS 501

ARG 352 0.07 THR 483 -0.42 HIS 501

ARG 352 0.07 ASP 484 -0.32 LEU 497

ALA 493 0.09 THR 485 -0.16 ASN 439

LEU 319 0.07 LEU 486 -0.19 ASN 439

LEU 320 0.08 ILE 487 -0.30 ASP 480

VAL 316 0.11 HIS 488 -0.20 ASN 439

VAL 316 0.35 LEU 489 -0.24 ASN 439

GLU 443 0.26 MET 490 -0.23 MET 438

SER 317 0.26 ALA 491 -0.24 ASP 480

SER 317 0.43 LYS 492 -0.22 MET 438

SER 317 0.51 ALA 493 -0.27 MET 438

LEU 320 0.38 GLY 494 -0.20 ASP 480

GLU 443 0.34 LEU 495 -0.29 ASP 480

GLU 443 0.34 LEU 495 -0.29 ASP 480

GLN 441 0.24 THR 496 -0.39 ASP 480

GLN 441 0.18 LEU 497 -0.51 ASP 480

GLN 441 0.21 GLN 498 -0.52 HIS 476

GLN 441 0.30 GLN 499 -0.40 HIS 476

GLU 443 0.18 GLN 500 -0.47 ASP 480

ARG 503 0.11 HIS 501 -0.59 ASP 480

ARG 503 0.27 GLN 502 -0.47 HIS 476

GLN 502 0.27 ARG 503 -0.33 HIS 476

GLU 443 0.08 LEU 504 -0.41 ASP 480

GLU 443 0.08 ALA 505 -0.41 HIS 476

GLN 441 0.08 GLN 506 -0.29 HIS 476

GLY 442 0.07 LEU 507 -0.25 HIS 476

LEU 509 0.06 LEU 508 -0.32 ASN 455

GLY 442 0.06 LEU 509 -0.30 TYR 459

LEU 440 0.06 ILE 510 -0.31 MET 427

LEU 448 0.05 LEU 511 -0.25 MET 427

GLY 442 0.04 SER 512 -0.30 TYR 459

GLY 442 0.04 SER 512 -0.30 TYR 459

ARG 434 0.08 HIS 513 -0.34 MET 427

PHE 435 0.07 ILE 514 -0.21 MET 427

GLU 385 0.06 ARG 515 -0.23 THR 460

ARG 434 0.08 HIS 516 -0.26 GLU 423

THR 431 0.10 MET 517 -0.21 ILE 424

THR 431 0.07 SER 518 -0.17 HIS 501

THR 431 0.07 ASN 519 -0.21 THR 460

ALA 430 0.10 LYS 520 -0.21 GLY 420

ASP 426 0.10 GLY 521 -0.15 HIS 501

ASP 426 0.07 MET 522 -0.15 HIS 501

GLU 423 0.10 GLU 523 -0.15 HIS 501

GLU 423 0.13 HIS 524 -0.15 LYS 520

LEU 372 0.16 LEU 525 -0.13 HIS 501

ARG 335 0.14 TYR 526 -0.13 HIS 501

GLU 423 0.11 SER 527 -0.13 HIS 501

GLU 423 0.12 SER 527 -0.13 HIS 501

LEU 372 0.19 MET 528 -0.12 HIS 501

ARG 335 0.22 LYS 529 -0.11 HIS 501

ARG 335 0.18 CYS 530 -0.11 HIS 501

ARG 335 0.18 LYS 531 -0.11 HIS 501

ARG 335 0.26 ASN 532 -0.10 HIS 501

LEU 372 0.26 VAL 533 -0.10 HIS 501

ARG 335 0.34 VAL 534 -0.10 GLY 344

ARG 335 0.44 PRO 535 -0.10 ASN 348

HIS 373 0.42 LEU 536 -0.09 HIS 501

HIS 373 0.53 SER 537 -0.09 ARG 352

HIS 373 0.61 ASP 538 -0.09 ARG 352

HIS 373 0.66 LEU 539 -0.10 PRO 325

VAL 376 0.46 LEU 540 -0.10 HIS 501

HIS 373 0.39 LEU 541 -0.11 HIS 501

HIS 373 0.44 GLU 542 -0.13 ILE 358

VAL 376 0.32 MET 543 -0.15 ILE 358

ARG 335 0.21 LEU 544 -0.13 HIS 501

ARG 335 0.22 ASP 545 -0.13 ILE 358

THR 460 0.25 ALA 546 -0.15 ILE 358

ARG 335 0.14 HIS 547 -0.14 HIS 501

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.

*** 5WGD_A ***

CA distance fluctuations for 2404102226553446872

--- normal mode 10 ---

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

* 5WGD_A *