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

* Xilanase_model1_428-522 *

CA distance fluctuations for 2404070544032760801

--- normal mode 9 ---

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
GLY 522 0.45 LYS 228 -0.92 GLY 293

GLY 231 0.20 LYS 229 -0.41 THR 257

ASP 393 0.18 ILE 230 -0.14 GLY 521

LYS 228 0.26 GLY 231 -0.08 GLY 522

ASP 393 0.20 PHE 232 -0.05 SER 391

ASP 393 0.15 PRO 233 -0.21 LYS 228

ASP 393 0.14 PHE 234 -0.29 LYS 228

ASP 393 0.08 GLY 235 -0.38 LYS 228

ASP 393 0.04 CYS 236 -0.37 LYS 228

PHE 352 0.02 ALA 237 -0.34 LYS 228

PHE 352 0.02 ILE 238 -0.38 LYS 228

ASN 263 0.03 ASN 239 -0.35 LYS 228

PRO 306 0.03 ARG 240 -0.36 LYS 228

LYS 307 0.03 ASN 241 -0.35 LYS 228

PRO 306 0.03 ILE 242 -0.37 LYS 228

PRO 306 0.03 LEU 243 -0.43 LYS 228

LYS 307 0.03 ASN 244 -0.42 LYS 228

LYS 307 0.03 ASN 245 -0.42 LYS 228

LYS 307 0.03 ASN 246 -0.46 LYS 228

PHE 352 0.03 ALA 247 -0.44 LYS 228

PHE 352 0.02 TYR 248 -0.47 LYS 228

SER 250 0.02 GLN 249 -0.56 LYS 228

ASP 393 0.04 SER 250 -0.55 LYS 228

ASP 393 0.06 TRP 251 -0.51 LYS 228

ASP 393 0.05 PHE 252 -0.61 LYS 228

ASP 393 0.07 SER 253 -0.75 LYS 228

ASP 393 0.09 SER 254 -0.61 LYS 228

ASP 393 0.11 ARG 255 -0.51 LYS 228

ASP 393 0.09 PHE 256 -0.57 LYS 228

ASP 393 0.09 THR 257 -0.65 LYS 228

ASP 393 0.06 VAL 258 -0.51 LYS 228

ASP 393 0.02 THR 259 -0.47 LYS 228

PRO 477 0.01 THR 260 -0.36 LYS 228

PHE 354 0.01 PHE 261 -0.35 LYS 228

ASN 491 0.02 GLU 262 -0.29 LYS 228

ASN 491 0.03 ASN 263 -0.31 ARG 392

LYS 266 0.02 GLU 264 -0.30 LYS 228

LYS 266 0.01 MET 265 -0.30 ARG 392

ASN 491 0.03 LYS 266 -0.37 ARG 392

ASN 491 0.02 TRP 267 -0.41 ARG 392

ASN 491 0.02 ALA 268 -0.43 ARG 392

ARG 240 0.02 SER 269 -0.37 ARG 392

ASN 244 0.02 THR 270 -0.35 ARG 392

ASN 502 0.02 GLU 271 -0.39 ARG 392

ASN 244 0.02 PRO 272 -0.38 ARG 392

ASN 502 0.02 SER 273 -0.42 ARG 392

ASN 502 0.01 GLN 274 -0.42 ARG 392

PRO 412 0.01 GLY 275 -0.38 ARG 392

ASN 502 0.01 HIS 276 -0.35 ARG 392

PRO 477 0.01 GLU 277 -0.33 ARG 392

ALA 284 0.01 ASP 278 -0.30 ARG 392

PRO 477 0.01 TYR 279 -0.29 LYS 228

ALA 284 0.01 SER 280 -0.32 LYS 228

SER 269 0.02 THR 281 -0.34 LYS 228

SER 269 0.01 ALA 282 -0.35 LYS 228

PRO 477 0.02 ASP 283 -0.37 LYS 228

SER 269 0.02 ALA 284 -0.40 LYS 228

PRO 477 0.01 MET 285 -0.44 LYS 228

PRO 477 0.02 VAL 286 -0.46 LYS 228

PRO 477 0.02 GLN 287 -0.48 LYS 228

PRO 477 0.02 PHE 288 -0.54 LYS 228

PRO 477 0.02 ALA 289 -0.60 LYS 228

PRO 477 0.02 LYS 290 -0.62 LYS 228

PRO 477 0.02 LYS 291 -0.64 LYS 228

ASP 393 0.03 ASN 292 -0.77 LYS 228

ASP 393 0.05 GLY 293 -0.92 LYS 228

ASP 393 0.05 ILE 294 -0.76 LYS 228

ASP 393 0.05 ALA 295 -0.57 LYS 228

PRO 477 0.03 ILE 296 -0.46 LYS 228

PRO 477 0.02 ARG 297 -0.34 LYS 228

PRO 477 0.02 GLY 298 -0.30 LYS 228

ASN 491 0.02 HIS 299 -0.26 ARG 392

ASN 491 0.03 ASN 300 -0.35 ARG 392

ASN 491 0.03 VAL 301 -0.38 ARG 392

ASN 491 0.03 PHE 302 -0.46 ARG 392

ASN 491 0.04 TRP 303 -0.49 ARG 392

ASN 491 0.05 ASP 304 -0.60 ARG 392

ASN 491 0.06 ASP 305 -0.61 ARG 392

ASN 491 0.05 PRO 306 -0.54 ARG 392

ASN 491 0.06 LYS 307 -0.61 ARG 392

ASN 491 0.05 TYR 308 -0.70 ARG 392

ASN 491 0.04 GLN 309 -0.63 ARG 392

ASN 491 0.04 SER 310 -0.56 ARG 392

ASN 491 0.03 GLY 311 -0.55 ARG 392

ASN 491 0.03 TRP 312 -0.53 ARG 392

ASN 491 0.03 VAL 313 -0.59 ARG 392

ASN 491 0.04 SER 314 -0.64 ARG 392

ASN 491 0.03 SER 315 -0.59 ARG 392

ASN 491 0.03 LEU 316 -0.57 ARG 392

ASN 491 0.03 SER 317 -0.58 ARG 392

ASN 491 0.03 PRO 318 -0.58 ARG 392

ASN 491 0.03 ASN 319 -0.50 ARG 392

ASN 491 0.02 ASP 320 -0.50 ARG 392

ASN 491 0.03 LEU 321 -0.53 ARG 392

ASN 491 0.03 ASN 322 -0.48 ARG 392

ASN 491 0.02 ALA 323 -0.43 ARG 392

ASN 491 0.02 ALA 324 -0.44 ARG 392

ASN 491 0.02 ALA 325 -0.43 ARG 392

ASN 491 0.02 THR 326 -0.38 ARG 392

ASN 491 0.01 LYS 327 -0.37 ARG 392

ASN 491 0.02 ARG 328 -0.37 ARG 392

GLY 446 0.02 ILE 329 -0.33 ARG 392

PRO 477 0.02 ASN 330 -0.30 ARG 392

PRO 477 0.02 SER 331 -0.30 ARG 392

PRO 477 0.02 VAL 332 -0.28 ARG 392

PRO 477 0.02 MET 333 -0.25 ARG 392

PRO 477 0.03 ASN 334 -0.24 ARG 392

PRO 477 0.02 ARG 335 -0.28 LYS 228

PRO 477 0.03 TYR 336 -0.32 LYS 228

PRO 477 0.03 LYS 337 -0.27 LYS 228

PRO 477 0.04 GLY 338 -0.31 LYS 228

PRO 477 0.03 GLN 339 -0.40 LYS 228

PRO 477 0.03 VAL 340 -0.35 LYS 228

PRO 477 0.04 ILE 341 -0.32 LYS 228

PRO 477 0.03 GLY 342 -0.24 LYS 228

PRO 477 0.02 TRP 343 -0.22 ARG 392

ASN 491 0.03 ASP 344 -0.26 ARG 392

ASN 491 0.03 VAL 345 -0.34 ARG 392

CYS 493 0.04 VAL 346 -0.42 ARG 392

CYS 493 0.05 ASN 347 -0.39 ARG 392

CYS 493 0.06 GLU 348 -0.50 ARG 392

CYS 493 0.05 ASN 349 -0.53 ARG 392

CYS 493 0.06 LEU 350 -0.61 ARG 392

CYS 493 0.07 HIS 351 -0.76 ARG 392

CYS 493 0.08 PHE 352 -0.97 ARG 392

CYS 493 0.06 SER 353 -0.83 ARG 392

ASN 491 0.06 PHE 354 -0.85 ARG 392

ASN 491 0.05 PHE 355 -0.77 ARG 392

ASN 491 0.05 GLU 356 -0.75 ARG 392

ASN 491 0.04 SER 357 -0.66 ARG 392

ASN 491 0.04 LYS 358 -0.60 ARG 392

ASN 491 0.04 LEU 359 -0.60 ARG 392

ASN 491 0.04 GLY 360 -0.57 ARG 392

CYS 493 0.04 ALA 361 -0.47 ARG 392

ASN 491 0.03 ASN 362 -0.46 ARG 392

ASN 491 0.03 ALA 363 -0.47 ARG 392

ASN 491 0.03 SER 364 -0.41 ARG 392

ASN 491 0.03 ALA 365 -0.36 ARG 392

ASN 491 0.02 VAL 366 -0.38 ARG 392

ASN 491 0.02 PHE 367 -0.36 ARG 392

GLY 446 0.02 TYR 368 -0.30 ARG 392

GLY 446 0.02 GLY 369 -0.29 ARG 392

GLY 446 0.02 GLU 370 -0.30 ARG 392

GLY 446 0.03 ALA 371 -0.26 ARG 392

GLY 446 0.03 HIS 372 -0.23 ARG 392

GLY 446 0.03 LYS 373 -0.24 ARG 392

PRO 477 0.03 THR 374 -0.24 ARG 392

PRO 477 0.03 ASP 375 -0.20 ARG 392

PRO 477 0.04 PRO 376 -0.18 ARG 392

PRO 477 0.05 SER 377 -0.14 ARG 392

PRO 477 0.04 THR 378 -0.17 LYS 228

ASP 393 0.05 THR 379 -0.14 ARG 392

GLY 394 0.03 LEU 380 -0.20 ARG 392

GLY 394 0.04 PHE 381 -0.20 ARG 392

CYS 493 0.03 MET 382 -0.27 ARG 392

CYS 493 0.04 ASN 383 -0.28 ARG 392

CYS 493 0.04 GLU 384 -0.32 SER 391

TYR 494 0.05 TYR 385 -0.37 SER 391

SER 426 0.08 ASN 386 -0.39 SER 391

ASP 393 0.12 THR 387 -0.22 SER 391

ASP 393 0.24 VAL 388 -0.11 TYR 434

ASP 393 0.09 GLU 389 -0.20 SER 391

ASN 431 0.20 ASP 390 -0.25 HIS 351

SER 428 0.23 SER 391 -0.60 HIS 351

ASN 431 0.60 ARG 392 -0.97 PHE 352

PRO 433 0.68 ASP 393 -0.50 PHE 352

TYR 434 0.39 GLY 394 -0.24 PHE 352

SER 428 0.08 GLN 395 -0.19 HIS 351

SER 426 0.09 ALA 396 -0.33 SER 391

GLY 394 0.22 THR 397 -0.13 SER 391

ASP 393 0.29 PRO 398 -0.14 SER 391

ASP 393 0.26 ALA 399 -0.11 SER 391

GLY 394 0.11 LYS 400 -0.28 ARG 392

GLY 394 0.11 TYR 401 -0.25 ARG 392

ASP 393 0.17 LEU 402 -0.17 SER 391

GLY 394 0.11 GLU 403 -0.24 ARG 392

GLY 394 0.05 LYS 404 -0.34 ARG 392

GLY 394 0.08 LEU 405 -0.24 ARG 392

GLY 394 0.10 ARG 406 -0.20 ARG 392

GLY 394 0.06 SER 407 -0.29 ARG 392

GLY 394 0.04 ILE 408 -0.30 ARG 392

GLY 394 0.07 GLN 409 -0.22 ARG 392

GLY 394 0.07 SER 410 -0.22 ARG 392

GLY 394 0.04 LEU 411 -0.28 ARG 392

GLY 394 0.03 PRO 412 -0.25 ARG 392

GLY 394 0.04 GLY 413 -0.24 ARG 392

GLY 394 0.05 ASN 414 -0.23 ARG 392

GLY 394 0.07 GLY 415 -0.17 ARG 392

ASP 393 0.08 ASN 416 -0.14 ARG 392

ASP 393 0.07 MET 417 -0.16 ARG 392

ASP 393 0.11 GLY 418 -0.15 SER 391

ASP 393 0.11 ILE 419 -0.18 SER 391

ASP 393 0.08 GLY 420 -0.19 SER 391

ASP 393 0.10 LEU 421 -0.19 SER 391

TYR 401 0.03 GLU 422 -0.20 SER 391

ASP 393 0.10 SER 423 -0.11 SER 391

ASN 386 0.05 HIS 424 -0.11 LYS 228

ARG 392 0.23 PHE 425 -0.09 LYS 228

ARG 392 0.29 SER 426 -0.09 LYS 228

ARG 392 0.38 SER 427 -0.09 LYS 228

ARG 392 0.58 SER 428 -0.05 LYS 228

ARG 392 0.59 PRO 429 -0.04 LYS 307

ARG 392 0.51 PRO 430 -0.06 LYS 307

ARG 392 0.60 ASN 431 -0.08 LYS 307

ASP 393 0.53 ILE 432 -0.05 LYS 307

ASP 393 0.68 PRO 433 -0.08 THR 397

ASP 393 0.64 TYR 434 -0.11 VAL 388

ASP 393 0.45 MET 435 -0.07 THR 387

ASP 393 0.51 ARG 436 -0.06 THR 397

ASP 393 0.58 SER 437 -0.09 THR 397

ASP 393 0.43 ALA 438 -0.07 THR 397

ASP 393 0.38 ILE 439 -0.05 SER 391

ASP 393 0.44 ASP 440 -0.05 THR 397

ASP 393 0.41 THR 441 -0.05 THR 397

ASP 393 0.30 LEU 442 -0.09 SER 391

ASP 393 0.33 ALA 443 -0.06 SER 391

ASP 393 0.35 ALA 444 -0.05 SER 391

ASP 393 0.27 THR 445 -0.08 SER 391

ASP 393 0.24 GLY 446 -0.08 SER 391

ASP 393 0.20 LEU 447 -0.11 SER 391

ASP 393 0.19 PRO 448 -0.11 SER 391

ASP 393 0.20 VAL 449 -0.11 SER 391

ASP 393 0.15 TRP 450 -0.12 SER 391

ASP 393 0.16 LEU 451 -0.11 SER 391

ASP 393 0.07 THR 452 -0.17 LYS 228

ASP 393 0.03 GLU 453 -0.18 LYS 228

ASP 393 0.11 VAL 454 -0.15 LYS 228

ARG 392 0.09 ASP 455 -0.16 LYS 228

ARG 392 0.24 VAL 456 -0.12 LYS 228

ARG 392 0.20 GLN 457 -0.14 LYS 228

ARG 392 0.24 SER 458 -0.15 LYS 228

ARG 392 0.34 GLY 459 -0.11 LYS 228

ARG 392 0.38 GLY 460 -0.10 LYS 228

ARG 392 0.43 ASN 461 -0.07 LYS 228

ARG 392 0.33 GLN 462 -0.10 LYS 228

ARG 392 0.32 ALA 463 -0.09 LYS 228

ARG 392 0.40 GLN 464 -0.03 LYS 228

ARG 392 0.40 SER 465 -0.04 LYS 228

ARG 392 0.29 LEU 466 -0.07 LYS 228

ARG 392 0.32 GLU 467 -0.03 SER 475

ARG 392 0.38 GLN 468 -0.03 GLU 472

ASP 393 0.33 ILE 469 -0.03 GLU 472

ASP 393 0.29 LEU 470 -0.03 PRO 477

ASP 393 0.35 ARG 471 -0.05 SER 475

ASP 393 0.39 GLU 472 -0.03 ILE 469

ASP 393 0.32 ALA 473 -0.03 ARG 471

ASP 393 0.31 HIS 474 -0.05 PRO 477

ASP 393 0.37 SER 475 -0.05 ARG 471

ASP 393 0.35 HIS 476 -0.04 ARG 471

ASP 393 0.30 PRO 477 -0.05 HIS 474

ASP 393 0.27 LYS 478 -0.06 SER 391

ASP 393 0.26 VAL 479 -0.07 SER 391

ASP 393 0.20 ARG 480 -0.08 SER 391

ASP 393 0.17 GLY 481 -0.08 SER 391

ASP 393 0.16 ILE 482 -0.14 LYS 228

ASP 393 0.09 VAL 483 -0.24 LYS 228

ASP 393 0.07 ILE 484 -0.25 LYS 228

PHE 352 0.03 TRP 485 -0.27 LYS 228

PHE 352 0.04 SER 486 -0.30 LYS 228

PHE 352 0.04 ALA 487 -0.32 LYS 228

PHE 352 0.04 TRP 488 -0.32 LYS 228

PHE 352 0.05 SER 489 -0.27 LYS 228

PHE 352 0.06 PRO 490 -0.25 LYS 228

PHE 352 0.07 ASN 491 -0.25 LYS 228

PHE 352 0.07 GLY 492 -0.22 LYS 228

PHE 352 0.08 CYS 493 -0.23 LYS 228

PHE 352 0.07 TYR 494 -0.20 LYS 228

PHE 352 0.06 ARG 495 -0.21 LYS 228

ARG 392 0.12 MET 496 -0.20 LYS 228

ARG 392 0.07 CYS 497 -0.26 LYS 228

ARG 392 0.11 LEU 498 -0.27 LYS 228

ARG 392 0.09 THR 499 -0.30 LYS 228

ARG 392 0.09 ASP 500 -0.27 LYS 228

PHE 352 0.05 ASN 501 -0.29 LYS 228

ARG 392 0.06 ASN 502 -0.30 LYS 228

ARG 392 0.06 PHE 503 -0.33 LYS 228

ARG 392 0.12 HIS 504 -0.29 LYS 228

ARG 392 0.14 ASN 505 -0.27 LYS 228

ARG 392 0.18 LEU 506 -0.21 LYS 228

ARG 392 0.25 PRO 507 -0.16 LYS 228

ARG 392 0.23 THR 508 -0.17 LYS 228

ARG 392 0.17 GLY 509 -0.24 LYS 228

ARG 392 0.21 ASP 510 -0.18 LYS 228

ARG 392 0.24 VAL 511 -0.11 LYS 228

ARG 392 0.19 VAL 512 -0.17 LYS 228

ASP 393 0.17 ASP 513 -0.22 LYS 228

ARG 392 0.21 LYS 514 -0.09 LYS 228

ASP 393 0.23 LEU 515 -0.03 PRO 477

ASP 393 0.19 LEU 516 -0.12 LYS 228

ASP 393 0.19 ARG 517 -0.07 LYS 228

ASP 393 0.24 GLU 518 -0.03 ARG 480

ASP 393 0.23 TRP 519 -0.04 ARG 480

ASP 393 0.20 GLY 520 -0.05 SER 254

LYS 228 0.36 GLY 521 -0.14 ILE 230

LYS 228 0.45 GLY 522 -0.08 GLY 231

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.

*** Xilanase_model1_428-522 ***

CA distance fluctuations for 2404070544032760801

--- normal mode 9 ---

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

* Xilanase_model1_428-522 *