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

* 1ERR monomer *

CA distance fluctuations for 2404102156053369258

--- 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
ALA 318 0.24 ALA 307 -0.45 ASP 369

ALA 318 0.22 LEU 308 -0.37 LEU 497

ARG 477 0.14 SER 309 -0.42 ASP 369

ARG 477 0.14 LEU 310 -0.41 VAL 368

LYS 481 0.16 THR 311 -0.35 VAL 368

ILE 482 0.16 ALA 312 -0.35 LEU 497

ILE 482 0.16 ASP 313 -0.34 ARG 363

ARG 477 0.12 GLN 314 -0.44 ARG 363

ARG 477 0.14 MET 315 -0.42 ARG 363

CYS 447 0.16 VAL 316 -0.35 ARG 363

LEU 308 0.14 SER 317 -0.39 LYS 492

ALA 307 0.24 ALA 318 -0.42 ARG 363

ALA 307 0.16 LEU 319 -0.30 ARG 363

ALA 307 0.13 LEU 320 -0.33 LYS 492

ALA 307 0.23 ASP 321 -0.34 LYS 492

ALA 307 0.15 ALA 322 -0.30 PRO 325

ALA 307 0.08 GLU 323 -0.30 ARG 394

TRP 383 0.04 PRO 324 -0.30 ILE 326

LEU 387 0.13 PRO 325 -0.31 ASP 321

GLY 390 0.13 ILE 326 -0.30 PRO 324

GLN 506 0.08 LEU 327 -0.29 PRO 324

ARG 434 0.11 TYR 328 -0.21 ASP 321

GLN 506 0.11 SER 329 -0.19 PRO 324

GLN 506 0.09 GLU 330 -0.19 PRO 333

LEU 408 0.24 TYR 331 -0.26 ALA 546

LEU 408 0.28 ASP 332 -0.21 ASP 321

LEU 409 0.16 PRO 333 -0.19 GLU 330

LEU 410 0.20 THR 334 -0.17 ASP 321

ASN 413 0.26 ARG 335 -0.21 ASN 407

ASN 413 0.37 PRO 336 -0.15 ASN 407

PRO 535 0.22 PHE 337 -0.15 ASN 407

PRO 535 0.31 SER 338 -0.11 ASN 407

PRO 535 0.43 GLU 339 -0.10 ASN 407

PRO 535 0.38 ALA 340 -0.13 TYR 526

PRO 535 0.21 SER 341 -0.15 TYR 526

PRO 535 0.25 MET 342 -0.13 TYR 526

PRO 535 0.35 MET 343 -0.19 TYR 526

LEU 539 0.18 GLY 344 -0.24 TYR 526

GLN 502 0.13 LEU 345 -0.20 TYR 526

LEU 539 0.17 LEU 346 -0.22 TYR 526

MET 543 0.23 THR 347 -0.27 TYR 526

GLN 502 0.09 ASN 348 -0.22 TYR 526

GLN 506 0.10 LEU 349 -0.17 TYR 526

MET 343 0.12 ALA 350 -0.16 GLY 457

HIS 547 0.16 ASP 351 -0.25 LEU 536

PRO 325 0.10 ARG 352 -0.32 LEU 536

MET 528 0.11 GLU 353 -0.18 TYR 331

MET 528 0.22 LEU 354 -0.21 ARG 352

MET 528 0.21 VAL 355 -0.34 LEU 540

MET 528 0.15 HIS 356 -0.26 LEU 327

MET 528 0.17 MET 357 -0.20 LEU 327

MET 528 0.27 ILE 358 -0.24 GLN 314

MET 528 0.20 ASN 359 -0.30 ALA 318

MET 528 0.15 TRP 360 -0.26 ALA 318

MET 528 0.20 ALA 361 -0.23 GLN 314

MET 528 0.23 LYS 362 -0.41 GLN 314

MET 528 0.15 ARG 363 -0.44 GLN 314

ALA 322 0.14 VAL 364 -0.28 THR 485

ASP 321 0.18 PRO 365 -0.34 THR 485

MET 528 0.16 GLY 366 -0.27 LEU 497

MET 528 0.22 PHE 367 -0.28 LEU 310

MET 528 0.24 VAL 368 -0.41 LEU 310

TYR 526 0.24 ASP 369 -0.45 ALA 307

TYR 526 0.28 LEU 370 -0.30 ALA 307

TYR 526 0.37 THR 371 -0.31 SER 309

TYR 526 0.43 LEU 372 -0.29 SER 309

TYR 526 0.49 HIS 373 -0.23 SER 309

ASN 519 0.43 ASP 374 -0.20 ALA 307

ASN 519 0.39 GLN 375 -0.21 ALA 307

TYR 526 0.49 VAL 376 -0.21 VAL 355

ASN 519 0.58 HIS 377 -0.20 ARG 352

ASN 519 0.45 LEU 378 -0.17 ARG 352

ASN 519 0.41 LEU 379 -0.20 ARG 352

ASN 519 0.65 GLU 380 -0.25 ARG 352

SER 518 0.33 ALA 382 -0.32 GLY 457

MET 421 0.23 TRP 383 -0.23 GLY 457

GLU 380 0.28 LEU 384 -0.12 ASP 351

GLU 380 0.29 GLU 385 -0.09 ASP 351

GLN 506 0.15 ILE 386 -0.12 GLY 457

GLN 506 0.15 LEU 387 -0.12 SER 518

GLU 380 0.21 MET 388 -0.14 SER 518

GLN 506 0.18 ILE 389 -0.10 SER 518

PRO 325 0.13 GLY 390 -0.12 GLU 323

GLN 506 0.17 LEU 391 -0.15 PRO 324

GLN 499 0.21 VAL 392 -0.15 MET 517

GLN 499 0.16 TRP 393 -0.16 GLU 323

PRO 406 0.16 ARG 394 -0.30 GLU 323

GLN 499 0.18 SER 395 -0.22 ASP 321

GLN 499 0.19 MET 396 -0.20 ASP 321

ASP 332 0.19 GLU 397 -0.27 ASP 321

ASP 332 0.22 HIS 398 -0.26 ASP 321

GLN 499 0.25 PRO 399 -0.21 ASP 321

GLN 502 0.29 GLY 400 -0.18 ASP 321

GLN 502 0.24 LYS 401 -0.20 ASP 321

GLN 502 0.22 LEU 402 -0.19 ASP 321

ASP 332 0.18 LEU 403 -0.25 PRO 324

GLN 506 0.16 PHE 404 -0.20 PRO 324

ARG 434 0.13 ALA 405 -0.28 PRO 324

GLU 397 0.18 PRO 406 -0.28 ASP 321

TYR 331 0.19 ASN 407 -0.24 ASP 321

ASP 332 0.28 LEU 408 -0.23 ASP 321

ASP 332 0.26 LEU 409 -0.24 ASP 321

PRO 336 0.22 LEU 410 -0.19 ASP 321

PRO 336 0.28 ASP 411 -0.18 ASP 321

PRO 535 0.30 ARG 412 -0.14 ASP 321

PRO 336 0.37 ASN 413 -0.14 ASP 321

PRO 336 0.37 GLN 414 -0.14 ASP 321

PRO 535 0.38 GLY 415 -0.10 ASP 321

PRO 535 0.44 LYS 416 -0.10 ASN 407

PRO 535 0.42 CYS 417 -0.11 ASN 407

PRO 535 0.52 VAL 418 -0.08 ASN 407

PRO 535 0.63 GLU 419 -0.10 MET 528

PRO 535 0.60 GLY 420 -0.12 MET 528

PRO 535 0.54 MET 421 -0.10 MET 528

PRO 535 0.46 VAL 422 -0.11 PRO 399

PRO 535 0.48 GLU 423 -0.12 MET 528

PRO 535 0.45 ILE 424 -0.11 SER 527

PRO 535 0.37 PHE 425 -0.11 SER 395

GLN 502 0.34 ASP 426 -0.11 MET 396

GLN 502 0.39 MET 427 -0.10 SER 527

GLN 502 0.32 LEU 428 -0.11 VAL 392

GLN 502 0.33 LEU 429 -0.12 MET 396

GLN 502 0.39 ALA 430 -0.09 SER 527

GLN 502 0.35 THR 431 -0.10 LYS 520

GLN 499 0.27 SER 432 -0.12 ASP 321

ARG 434 0.35 SER 433 -0.12 ASP 321

GLN 499 0.35 ARG 434 -0.09 HIS 513

GLN 499 0.29 PHE 435 -0.11 ASP 321

GLN 499 0.27 ARG 436 -0.15 ASP 321

GLN 499 0.40 MET 437 -0.11 ASP 321

GLN 499 0.36 MET 438 -0.10 LEU 509

GLN 499 0.20 ASN 439 -0.12 ASP 321

GLN 499 0.14 LEU 440 -0.11 ARG 363

ASP 313 0.11 GLN 441 -0.15 ARG 363

ASP 313 0.11 GLY 442 -0.23 GLU 397

ASP 313 0.15 GLU 443 -0.25 MET 490

ASP 313 0.15 GLU 444 -0.18 ARG 363

ALA 382 0.11 PHE 445 -0.14 ARG 363

SER 317 0.10 VAL 446 -0.17 ARG 363

VAL 316 0.16 CYS 447 -0.20 VAL 364

ILE 452 0.14 LEU 448 -0.09 VAL 364

ALA 382 0.12 LYS 449 -0.09 ARG 394

LEU 319 0.13 SER 450 -0.12 LEU 497

SER 456 0.15 ILE 451 -0.09 HIS 476

LEU 507 0.18 ILE 452 -0.09 ASP 351

ASN 519 0.17 LEU 453 -0.11 ARG 352

ASN 519 0.17 LEU 454 -0.11 ARG 352

THR 483 0.24 ASN 455 -0.13 ALA 382

LEU 508 0.33 SER 456 -0.26 ALA 382

ASN 519 0.31 GLY 457 -0.32 ALA 382

HIS 516 0.25 VAL 458 -0.17 ALA 382

HIS 516 0.33 TYR 459 -0.19 ASP 351

ASP 369 0.19 GLU 470 -0.16 GLN 498

ASP 369 0.20 GLU 471 -0.14 LEU 497

LEU 370 0.15 LYS 472 -0.13 TYR 459

GLY 420 0.12 ASP 473 -0.17 GLN 498

GLY 420 0.12 ASP 473 -0.16 GLN 498

TYR 526 0.14 HIS 474 -0.21 LEU 497

ASN 519 0.15 ILE 475 -0.15 LEU 497

GLU 423 0.12 HIS 476 -0.16 GLN 498

ALA 318 0.15 ARG 477 -0.26 GLN 498

ALA 318 0.17 VAL 478 -0.25 LEU 497

ASN 455 0.15 LEU 479 -0.18 GLN 498

TYR 459 0.20 ASP 480 -0.27 HIS 501

THR 311 0.16 LYS 481 -0.32 LEU 497

ASP 313 0.16 ILE 482 -0.31 PRO 365

ASN 455 0.24 THR 483 -0.30 HIS 501

TYR 459 0.18 ASP 484 -0.38 LEU 497

SER 456 0.15 THR 485 -0.34 PRO 365

SER 456 0.16 LEU 486 -0.28 ARG 363

TYR 459 0.20 ILE 487 -0.28 PRO 365

TYR 459 0.16 HIS 488 -0.35 LEU 497

SER 456 0.13 LEU 489 -0.31 ARG 363

TYR 459 0.16 MET 490 -0.26 ARG 363

TYR 459 0.16 ALA 491 -0.31 SER 317

TYR 459 0.13 LYS 492 -0.39 SER 317

MET 438 0.13 ALA 493 -0.28 ASP 321

MET 437 0.21 GLY 494 -0.25 SER 317

MET 437 0.30 LEU 495 -0.21 ARG 363

MET 437 0.35 THR 496 -0.28 LEU 308

MET 437 0.27 LEU 497 -0.38 ASP 484

ALA 430 0.34 GLN 498 -0.34 ASP 484

MET 437 0.40 GLN 499 -0.22 ASP 484

MET 427 0.26 GLN 500 -0.27 ASP 484

MET 427 0.31 HIS 501 -0.34 ASP 484

MET 427 0.39 GLN 502 -0.21 ASP 484

MET 427 0.31 ARG 503 -0.14 PRO 365

TYR 459 0.25 LEU 504 -0.16 PRO 365

LEU 509 0.37 ALA 505 -0.13 ASP 480

ILE 510 0.38 GLN 506 -0.10 ASP 480

SER 456 0.27 LEU 507 -0.07 PRO 365

SER 456 0.33 LEU 508 -0.08 LEU 440

ALA 505 0.37 LEU 509 -0.10 LEU 440

GLN 506 0.38 ILE 510 -0.05 LEU 440

SER 456 0.31 LEU 511 -0.10 SER 512

ALA 505 0.36 SER 512 -0.10 LEU 511

GLN 502 0.35 HIS 513 -0.09 ARG 434

GLU 380 0.34 ILE 514 -0.09 SER 512

GLU 380 0.42 ARG 515 -0.08 GLY 390

GLU 380 0.46 HIS 516 -0.12 VAL 392

GLU 380 0.46 MET 517 -0.15 VAL 392

GLU 380 0.56 SER 518 -0.14 MET 388

GLU 380 0.65 ASN 519 -0.11 THR 347

PRO 535 0.60 LYS 520 -0.14 VAL 392

PRO 535 0.62 GLY 521 -0.14 THR 347

LEU 536 0.78 MET 522 -0.20 THR 347

PRO 535 0.84 GLU 523 -0.17 THR 347

PRO 535 0.82 HIS 524 -0.13 SER 527

PRO 535 0.93 LEU 525 -0.21 THR 347

PRO 535 1.16 TYR 526 -0.27 THR 347

PRO 535 0.97 SER 527 -0.15 GLU 523

PRO 535 0.98 MET 528 -0.12 GLY 420

TYR 526 1.16 PRO 535 -0.28 ARG 352

TYR 526 0.93 LEU 536 -0.32 ARG 352

TYR 526 0.85 TYR 537 -0.26 ARG 352

TYR 526 0.81 ASP 538 -0.26 VAL 355

TYR 526 0.73 LEU 539 -0.32 VAL 355

TYR 526 0.59 LEU 540 -0.34 VAL 355

TYR 526 0.61 LEU 541 -0.24 GLN 314

MET 528 0.59 GLU 542 -0.27 GLN 314

MET 528 0.51 MET 543 -0.27 GLN 314

MET 528 0.44 LEU 544 -0.32 GLN 314

MET 528 0.47 ASP 545 -0.35 GLN 314

MET 528 0.45 ALA 546 -0.36 GLN 314

MET 528 0.38 HIS 547 -0.40 GLN 314

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 11 ---

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

* 1ERR monomer *