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

* 1ERR monomer *

CA distance fluctuations for 2404102156053369258

--- normal mode 7 ---

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
ASN 519 0.15 ALA 307 -0.22 PRO 325

ASN 519 0.17 LEU 308 -0.19 PRO 325

ASN 519 0.15 SER 309 -0.19 PRO 325

ASP 369 0.14 LEU 310 -0.22 PRO 406

SER 512 0.12 THR 311 -0.22 PRO 406

SER 512 0.12 ALA 312 -0.22 PRO 406

LYS 492 0.16 ASP 313 -0.28 PRO 406

VAL 368 0.18 GLN 314 -0.28 PRO 406

ALA 493 0.14 MET 315 -0.24 PRO 406

ALA 493 0.22 VAL 316 -0.28 PRO 406

ALA 493 0.28 SER 317 -0.35 PRO 406

ARG 363 0.22 ALA 318 -0.28 PRO 406

ALA 493 0.20 LEU 319 -0.26 ILE 326

ALA 493 0.27 LEU 320 -0.36 PRO 406

ALA 493 0.27 ASP 321 -0.38 PRO 325

ALA 493 0.22 ALA 322 -0.34 PRO 325

GLY 442 0.20 GLU 323 -0.32 ILE 326

GLY 442 0.18 PRO 324 -0.29 LEU 327

ASN 439 0.18 PRO 325 -0.38 ASP 321

PRO 535 0.16 ILE 326 -0.36 ASP 321

PRO 535 0.23 LEU 327 -0.32 ASP 321

PRO 535 0.30 TYR 328 -0.30 ASP 321

PRO 535 0.36 SER 329 -0.25 ASP 321

PRO 535 0.44 GLU 330 -0.23 ASP 321

PRO 535 0.39 TYR 331 -0.28 ASP 321

PRO 535 0.38 ASP 332 -0.26 ASP 321

PRO 535 0.45 PRO 333 -0.21 ASP 321

PRO 535 0.41 THR 334 -0.20 ASP 321

PRO 535 0.35 ARG 335 -0.19 SER 317

PRO 535 0.33 PRO 336 -0.17 SER 317

PRO 535 0.38 PHE 337 -0.15 ASP 321

PRO 535 0.39 SER 338 -0.12 ASP 321

PRO 535 0.36 GLU 339 -0.10 ASP 321

PRO 535 0.48 ALA 340 -0.09 ASP 321

PRO 535 0.50 SER 341 -0.12 ASP 321

PRO 535 0.42 MET 342 -0.13 ASP 321

PRO 535 0.45 MET 343 -0.09 ASP 321

PRO 535 0.59 GLY 344 -0.10 ASP 321

PRO 535 0.48 LEU 345 -0.15 ASP 321

PRO 535 0.41 LEU 346 -0.17 MET 528

LEU 536 0.57 THR 347 -0.28 MET 528

PRO 535 0.57 ASN 348 -0.21 MET 528

PRO 535 0.39 LEU 349 -0.21 MET 528

LEU 536 0.39 ALA 350 -0.29 LEU 525

LEU 536 0.54 ASP 351 -0.28 LEU 525

LEU 536 0.38 ARG 352 -0.22 MET 528

LEU 536 0.22 GLU 353 -0.22 LEU 525

LEU 536 0.23 LEU 354 -0.21 LEU 525

LEU 539 0.21 VAL 355 -0.20 LEU 525

ALA 493 0.14 HIS 356 -0.16 LEU 525

GLY 442 0.13 MET 357 -0.12 LEU 384

ALA 493 0.13 ILE 358 -0.11 TRP 383

ALA 493 0.16 ASN 359 -0.12 LYS 362

ALA 493 0.17 TRP 360 -0.19 PRO 325

ALA 318 0.12 ALA 361 -0.13 PRO 325

ALA 318 0.20 LYS 362 -0.15 PRO 325

ALA 318 0.22 ARG 363 -0.24 PRO 325

GLN 314 0.13 VAL 364 -0.20 PRO 325

GLN 314 0.15 PRO 365 -0.21 PRO 325

GLU 523 0.16 GLY 366 -0.16 PRO 325

GLN 314 0.14 PHE 367 -0.15 HIS 501

GLN 314 0.18 VAL 368 -0.14 PRO 325

GLN 314 0.15 ASP 369 -0.14 PRO 325

GLU 523 0.18 LEU 370 -0.18 HIS 501

THR 347 0.19 THR 371 -0.19 HIS 501

THR 347 0.20 LEU 372 -0.17 ALA 505

THR 347 0.27 HIS 373 -0.21 ALA 505

THR 347 0.27 ASP 374 -0.24 HIS 501

THR 347 0.24 GLN 375 -0.20 ALA 505

THR 347 0.31 VAL 376 -0.21 ALA 505

THR 347 0.35 HIS 377 -0.25 ALA 505

THR 347 0.31 LEU 378 -0.26 ALA 505

THR 347 0.32 LEU 379 -0.21 LEU 508

THR 347 0.44 GLU 380 -0.26 ARG 515

GLY 457 0.28 ALA 382 -0.21 LEU 511

THR 347 0.33 TRP 383 -0.14 LEU 508

MET 343 0.26 LEU 384 -0.15 LEU 354

MET 343 0.20 GLU 385 -0.12 LEU 511

THR 347 0.17 ILE 386 -0.11 LEU 508

THR 347 0.17 LEU 387 -0.11 PRO 324

LYS 472 0.14 MET 388 -0.10 LEU 320

LYS 472 0.09 ILE 389 -0.09 LEU 320

PRO 325 0.09 GLY 390 -0.17 LEU 320

PRO 535 0.09 LEU 391 -0.17 LEU 320

PRO 325 0.10 VAL 392 -0.12 GLY 442

PRO 325 0.17 TRP 393 -0.18 GLY 442

PRO 325 0.16 ARG 394 -0.29 GLY 442

PRO 325 0.11 SER 395 -0.24 GLY 442

PRO 325 0.17 MET 396 -0.23 GLY 442

PRO 325 0.17 GLU 397 -0.27 GLY 442

PRO 535 0.11 HIS 398 -0.24 GLY 442

PRO 325 0.09 PRO 399 -0.19 GLY 442

LYS 472 0.08 GLY 400 -0.17 GLY 442

PRO 535 0.12 LYS 401 -0.18 GLY 442

PRO 535 0.13 LEU 402 -0.19 LEU 320

PRO 535 0.17 LEU 403 -0.25 LEU 320

PRO 535 0.21 PHE 404 -0.22 LEU 320

PRO 535 0.24 ALA 405 -0.29 LEU 320

PRO 535 0.22 PRO 406 -0.36 LEU 320

PRO 535 0.27 ASN 407 -0.30 LEU 320

PRO 535 0.28 LEU 408 -0.25 LEU 320

PRO 535 0.21 LEU 409 -0.24 LEU 320

PRO 535 0.20 LEU 410 -0.19 LEU 320

PRO 535 0.15 ASP 411 -0.16 SER 317

TYR 459 0.15 ARG 412 -0.13 GLY 442

TYR 459 0.17 ASN 413 -0.13 LEU 320

PRO 535 0.20 GLN 414 -0.14 LEU 320

TYR 459 0.23 GLY 415 -0.12 LEU 320

TYR 459 0.24 LYS 416 -0.10 LEU 320

TYR 459 0.27 CYS 417 -0.11 LEU 320

TYR 459 0.31 VAL 418 -0.11 THR 347

TYR 459 0.34 GLU 419 -0.15 THR 347

TYR 459 0.32 GLY 420 -0.12 ALA 350

TYR 459 0.29 MET 421 -0.13 ALA 350

TYR 459 0.22 VAL 422 -0.10 ALA 350

LYS 472 0.23 GLU 423 -0.11 HIS 524

LYS 472 0.22 ILE 424 -0.12 ALA 350

TYR 459 0.18 PHE 425 -0.10 LEU 320

LYS 472 0.16 ASP 426 -0.09 GLY 442

LYS 472 0.17 MET 427 -0.09 GLU 523

LYS 472 0.15 LEU 428 -0.09 HIS 524

LYS 472 0.11 LEU 429 -0.12 GLY 442

LEU 509 0.11 ALA 430 -0.08 GLU 523

ASP 480 0.09 THR 431 -0.07 LYS 520

PRO 325 0.11 SER 432 -0.13 GLY 442

ARG 434 0.13 SER 433 -0.11 ALA 493

SER 433 0.13 ARG 434 -0.10 ALA 493

PRO 325 0.13 PHE 435 -0.10 ALA 493

PRO 325 0.16 ARG 436 -0.16 ALA 493

PRO 325 0.14 MET 437 -0.15 ALA 493

PRO 325 0.14 MET 438 -0.16 ALA 493

PRO 325 0.18 ASN 439 -0.19 ALA 493

PRO 325 0.16 LEU 440 -0.14 LEU 489

PRO 324 0.17 GLN 441 -0.19 GLU 397

GLU 323 0.20 GLY 442 -0.29 ARG 394

ALA 493 0.21 GLU 443 -0.23 PRO 406

GLU 443 0.14 GLU 444 -0.14 PRO 406

TRP 360 0.09 PHE 445 -0.15 ARG 394

ALA 493 0.13 VAL 446 -0.20 PRO 406

SER 512 0.10 CYS 447 -0.15 PRO 406

ILE 514 0.11 LEU 448 -0.13 ASN 455

THR 347 0.10 LYS 449 -0.11 ALA 505

ASN 519 0.13 SER 450 -0.13 HIS 501

ASN 519 0.21 ILE 451 -0.21 HIS 501

ASN 519 0.20 ILE 452 -0.25 LEU 508

THR 347 0.19 LEU 453 -0.20 ALA 505

ASN 519 0.25 LEU 454 -0.25 HIS 501

ASN 519 0.35 ASN 455 -0.35 ALA 505

MET 522 0.40 SER 456 -0.37 LEU 508

MET 522 0.45 GLY 457 -0.33 ALA 505

GLU 523 0.44 VAL 458 -0.36 HIS 501

GLU 523 0.53 TYR 459 -0.40 ALA 505

GLU 523 0.35 GLU 470 -0.23 LEU 497

GLU 523 0.34 GLU 471 -0.21 HIS 501

GLU 523 0.40 LYS 472 -0.26 HIS 501

GLU 523 0.35 ASP 473 -0.27 LEU 497

GLU 523 0.35 ASP 473 -0.27 LEU 497

GLU 523 0.28 HIS 474 -0.22 HIS 501

GLU 523 0.29 ILE 475 -0.25 HIS 501

ASN 519 0.34 HIS 476 -0.30 HIS 501

ASN 519 0.27 ARG 477 -0.25 LEU 497

ASN 519 0.23 VAL 478 -0.19 HIS 501

ASN 519 0.27 LEU 479 -0.26 HIS 501

SER 512 0.28 ASP 480 -0.28 LEU 497

SER 512 0.22 LYS 481 -0.17 LEU 497

SER 512 0.19 ILE 482 -0.14 HIS 501

SER 512 0.24 THR 483 -0.21 HIS 501

SER 512 0.21 ASP 484 -0.16 LEU 497

SER 512 0.16 THR 485 -0.17 PRO 406

LEU 508 0.14 LEU 486 -0.16 TYR 459

LEU 508 0.13 ILE 487 -0.20 TYR 459

LEU 508 0.13 HIS 488 -0.15 PRO 406

SER 317 0.18 LEU 489 -0.19 GLU 397

SER 317 0.18 MET 490 -0.17 TYR 459

SER 317 0.17 ALA 491 -0.18 TYR 459

SER 317 0.24 LYS 492 -0.19 GLU 397

SER 317 0.28 ALA 493 -0.19 ASN 439

ASP 321 0.22 GLY 494 -0.16 TYR 459

LEU 320 0.17 LEU 495 -0.22 TYR 459

LEU 320 0.13 THR 496 -0.27 TYR 459

SER 317 0.09 LEU 497 -0.32 TYR 459

MET 437 0.10 GLN 498 -0.36 TYR 459

GLU 443 0.11 GLN 499 -0.30 TYR 459

SER 317 0.09 GLN 500 -0.30 TYR 459

GLU 423 0.08 HIS 501 -0.40 TYR 459

MET 437 0.09 GLN 502 -0.37 TYR 459

MET 437 0.07 ARG 503 -0.30 TYR 459

HIS 488 0.11 LEU 504 -0.33 TYR 459

GLU 423 0.11 ALA 505 -0.40 TYR 459

ALA 505 0.10 GLN 506 -0.29 TYR 459

ASP 484 0.10 LEU 507 -0.25 SER 456

THR 483 0.21 LEU 508 -0.37 SER 456

ASP 484 0.16 LEU 509 -0.32 SER 456

ASP 480 0.15 ILE 510 -0.18 SER 456

ASP 480 0.23 LEU 511 -0.24 SER 456

ASP 480 0.28 SER 512 -0.26 GLU 380

ASP 480 0.21 HIS 513 -0.18 GLU 380

ASP 480 0.20 ILE 514 -0.17 GLU 380

HIS 476 0.26 ARG 515 -0.26 GLU 380

HIS 476 0.29 HIS 516 -0.22 PRO 535

LYS 472 0.24 MET 517 -0.14 LEU 536

SER 456 0.31 SER 518 -0.17 LEU 536

TYR 459 0.42 ASN 519 -0.27 PRO 535

TYR 459 0.37 LYS 520 -0.18 PRO 535

TYR 459 0.37 GLY 521 -0.17 ALA 350

TYR 459 0.50 MET 522 -0.20 LEU 539

TYR 459 0.53 GLU 523 -0.19 LEU 539

TYR 459 0.44 HIS 524 -0.21 ALA 350

TYR 459 0.44 LEU 525 -0.29 ALA 350

TYR 459 0.52 TYR 526 -0.24 ASP 351

TYR 459 0.49 SER 527 -0.23 ASP 351

TYR 459 0.42 MET 528 -0.28 THR 347

GLY 344 0.59 PRO 535 -0.27 ASN 519

THR 347 0.57 LEU 536 -0.27 ASN 519

THR 347 0.44 TYR 537 -0.23 SER 512

ASN 348 0.38 ASP 538 -0.19 SER 512

ASP 351 0.39 LEU 539 -0.23 ASN 519

ASP 351 0.35 LEU 540 -0.18 ARG 515

ASP 351 0.26 LEU 541 -0.16 ALA 505

ASN 348 0.21 GLU 542 -0.15 ASN 519

ARG 352 0.14 MET 543 -0.17 TYR 526

ASP 351 0.14 LEU 544 -0.12 ALA 505

ALA 318 0.14 ASP 545 -0.12 ALA 505

ALA 318 0.14 ALA 546 -0.14 TYR 526

ALA 318 0.16 HIS 547 -0.13 MET 528

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 7 ---

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

* 1ERR monomer *