Should you encounter any unexpected behaviour,
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elNémo has been relocated.
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CA distance fluctuations for 2608052227103017248

--- normal mode 8 ---

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 339 0.73 PHE 239 -0.29 THR 247

ALA 339 0.56 SER 240 -0.36 THR 247

ALA 339 0.44 PHE 241 -0.39 ALA 244

ALA 339 0.45 ILE 242 -0.26 ALA 244

ALA 339 0.48 LYS 243 -0.29 ALA 244

ALA 339 0.38 ALA 244 -0.35 SER 240

ALA 339 0.33 LEU 245 -0.26 SER 240

ALA 339 0.36 GLN 246 -0.25 SER 240

ALA 339 0.34 THR 247 -0.34 SER 240

ALA 339 0.28 ALA 248 -0.32 SER 240

ALA 339 0.28 GLN 249 -0.21 THR 344

ALA 339 0.25 GLN 250 -0.20 LEU 336

ALA 339 0.22 ASN 251 -0.19 ASP 375

ALA 339 0.22 PHE 252 -0.14 LEU 336

ALA 339 0.19 VAL 253 -0.15 PHE 239

ASP 338 0.20 VAL 254 -0.22 PHE 239

ASP 375 0.12 THR 255 -0.23 PHE 239

ASP 375 0.24 ASP 256 -0.24 PHE 239

ASP 375 0.32 PRO 257 -0.18 ALA 248

ASP 375 0.44 SER 258 -0.21 ALA 248

ASP 375 0.42 LEU 259 -0.19 ALA 248

ASP 375 0.44 PRO 260 -0.15 ALA 248

ASP 375 0.29 ASP 261 -0.14 ASN 342

ASP 375 0.24 ASN 262 -0.15 PHE 239

ASP 375 0.17 PRO 263 -0.17 PHE 239

ASP 375 0.10 ILE 264 -0.19 PHE 239

THR 344 0.15 VAL 265 -0.25 PHE 239

ASP 338 0.23 TYR 266 -0.21 PHE 239

ALA 339 0.23 ALA 267 -0.13 PHE 239

ALA 339 0.27 SER 268 -0.14 LEU 336

ALA 339 0.25 GLN 269 -0.14 ASP 338

ALA 339 0.23 GLY 270 -0.16 ASP 338

ALA 339 0.19 PHE 271 -0.15 ASP 375

ALA 339 0.18 LEU 272 -0.12 ASP 375

ALA 339 0.18 ASN 273 -0.17 ASP 375

ALA 339 0.16 LEU 274 -0.23 ASP 375

ALA 339 0.13 THR 275 -0.21 ASP 375

ALA 339 0.13 GLY 276 -0.17 ASP 375

ALA 339 0.13 TYR 277 -0.11 ASP 375

ALA 339 0.15 SER 278 -0.09 ASP 338

ALA 339 0.16 LEU 279 -0.11 PHE 239

ALA 339 0.13 ASP 280 -0.12 PHE 239

ALA 339 0.10 GLN 281 -0.11 PHE 239

ALA 339 0.10 ILE 282 -0.13 PHE 239

ALA 339 0.11 LEU 283 -0.16 PHE 239

ASP 375 0.17 GLY 284 -0.17 PHE 239

PRO 297 0.11 ARG 285 -0.14 PHE 239

PRO 297 0.13 ASN 286 -0.13 PHE 239

PRO 297 0.11 CYS 287 -0.11 ALA 371

PRO 297 0.14 ARG 288 -0.20 ALA 371

PRO 297 0.09 PHE 289 -0.18 ALA 371

SER 240 0.11 LEU 290 -0.24 ASP 375

SER 240 0.13 GLN 291 -0.32 ASP 375

SER 240 0.14 GLY 292 -0.36 ASP 375

SER 240 0.14 PRO 293 -0.43 ASP 375

SER 240 0.18 GLU 294 -0.52 ASP 375

SER 240 0.17 THR 295 -0.51 ASP 375

SER 240 0.16 ASP 296 -0.64 ASP 375

ASP 261 0.15 PRO 297 -0.60 ASP 375

SER 258 0.14 LYS 298 -0.76 ASP 375

SER 240 0.14 ALA 299 -0.64 ASP 375

ASP 261 0.14 VAL 300 -0.46 ALA 371

ASP 261 0.15 GLU 301 -0.56 ALA 371

LYS 305 0.18 ARG 302 -0.59 ALA 371

LYS 305 0.16 ILE 303 -0.36 ALA 371

LYS 305 0.20 ARG 304 -0.29 ALA 371

LYS 305 0.27 LYS 305 -0.37 ALA 371

LYS 305 0.23 ALA 306 -0.25 GLN 309

LYS 305 0.18 ILE 307 -0.21 ASN 342

LYS 305 0.20 GLU 308 -0.29 ASN 342

SER 258 0.20 GLN 309 -0.28 ALA 372

PRO 257 0.15 GLY 310 -0.21 ASN 342

ARG 302 0.13 ASN 311 -0.22 ALA 372

LYS 305 0.11 ASP 312 -0.25 ALA 372

ALA 306 0.11 MET 313 -0.41 ALA 372

SER 240 0.14 SER 314 -0.45 ALA 372

SER 240 0.19 VAL 315 -0.56 ASP 375

SER 240 0.25 CYS 316 -0.57 ASP 375

SER 240 0.22 LEU 317 -0.55 ASP 375

SER 240 0.22 LEU 318 -0.50 ASP 375

SER 240 0.19 ASN 319 -0.39 ASP 375

SER 240 0.16 TYR 320 -0.32 ASP 375

SER 240 0.14 ARG 321 -0.26 ASP 375

SER 240 0.10 VAL 322 -0.19 ASP 375

SER 240 0.13 ASP 323 -0.23 ASP 375

SER 240 0.15 GLY 324 -0.29 ASP 375

SER 240 0.18 THR 325 -0.33 ASP 375

SER 240 0.21 THR 326 -0.39 ASP 375

SER 240 0.26 PHE 327 -0.41 ASP 375

SER 240 0.29 TRP 328 -0.48 ASP 375

SER 240 0.27 ASN 329 -0.43 ASP 375

SER 240 0.30 GLN 330 -0.45 ASP 375

SER 240 0.18 PHE 331 -0.37 ASP 375

SER 240 0.12 PHE 332 -0.31 ASP 375

ALA 339 0.08 ILE 333 -0.22 ALA 372

ALA 339 0.10 ALA 334 -0.14 ALA 372

ILE 242 0.11 ALA 335 -0.17 ALA 248

ARG 337 0.30 LEU 336 -0.24 ALA 248

PHE 239 0.46 ARG 337 -0.18 ALA 372

PHE 239 0.57 ASP 338 -0.17 ALA 372

PHE 239 0.73 ALA 339 -0.19 ALA 372

PHE 239 0.52 GLY 340 -0.24 ALA 372

PHE 239 0.49 GLY 341 -0.26 ALA 372

PHE 239 0.34 ASN 342 -0.29 GLU 308

ALA 371 0.23 VAL 343 -0.17 ALA 372

ALA 371 0.22 THR 344 -0.23 ALA 248

ALA 371 0.16 ASN 345 -0.24 ALA 248

ARG 337 0.10 PHE 346 -0.18 ALA 248

ARG 337 0.18 VAL 347 -0.14 ALA 248

ALA 339 0.13 GLY 348 -0.16 ALA 372

ALA 339 0.18 VAL 349 -0.21 ASP 375

SER 240 0.17 GLN 350 -0.28 ASP 375

SER 240 0.33 CYS 351 -0.34 ASP 375

SER 240 0.35 LYS 352 -0.38 ASP 375

SER 240 0.43 VAL 353 -0.44 ASP 375

SER 240 0.40 SER 354 -0.48 ASP 375

SER 240 0.33 ASP 355 -0.55 ASP 375

SER 240 0.33 GLN 356 -0.57 ASP 375

SER 240 0.36 TYR 357 -0.56 ASP 375

SER 240 0.31 ALA 358 -0.61 ASP 375

SER 240 0.26 ALA 359 -0.68 ASP 375

SER 240 0.25 THR 360 -0.70 ASP 375

SER 240 0.25 VAL 361 -0.71 ASP 375

SER 240 0.21 THR 362 -0.77 ASP 375

SER 240 0.20 LYS 363 -0.86 ASP 375

SER 258 0.19 GLN 364 -0.88 ASP 375

SER 258 0.18 GLN 365 -0.92 ASP 375

SER 258 0.18 GLU 366 -1.04 ASP 375

SER 258 0.24 GLU 367 -1.13 ASP 375

SER 258 0.24 GLU 368 -1.15 ASP 375

SER 258 0.21 GLU 369 -1.29 ASP 375

SER 258 0.21 GLU 370 -1.44 ASP 375

SER 258 0.26 ALA 371 -1.50 ASP 375

SER 258 0.21 ALA 372 -1.59 ASP 375

ALA 339 0.43 SER 240 -0.35 ALA 244

VAL 353 0.31 PHE 241 -0.32 ALA 244

ALA 339 0.34 ILE 242 -0.28 ALA 244

ALA 339 0.38 LYS 243 -0.34 ALA 244

VAL 353 0.28 ALA 244 -0.39 PHE 241

ALA 339 0.25 LEU 245 -0.30 PHE 241

ALA 339 0.29 GLN 246 -0.26 PHE 241

ALA 339 0.28 THR 247 -0.36 SER 240

ALA 248 0.26 ALA 248 -0.28 SER 240

ALA 339 0.23 GLN 249 -0.22 LEU 336

ALA 339 0.20 GLN 250 -0.24 LEU 336

ALA 339 0.17 ASN 251 -0.19 LEU 336

ASP 338 0.18 PHE 252 -0.21 ASP 375

ASP 338 0.18 VAL 253 -0.25 ASP 375

ASP 338 0.18 VAL 254 -0.28 ASP 375

ASP 338 0.09 THR 255 -0.32 ASP 375

ALA 371 0.14 ASP 256 -0.35 ASP 375

ALA 371 0.19 PRO 257 -0.40 ASP 375

ALA 371 0.26 SER 258 -0.38 ASP 375

ALA 371 0.23 LEU 259 -0.34 ASP 375

ALA 371 0.22 PRO 260 -0.33 ASP 375

LYS 305 0.15 ASP 261 -0.34 ASP 375

LYS 305 0.12 ASN 262 -0.35 ASP 375

LYS 305 0.09 PRO 263 -0.30 ASP 375

ASP 338 0.11 ILE 264 -0.28 ASP 375

ASP 338 0.16 VAL 265 -0.27 ASP 375

ASP 338 0.23 TYR 266 -0.24 ASP 375

ASP 338 0.20 ALA 267 -0.22 ASP 375

ALA 339 0.23 SER 268 -0.19 ASP 375

ALA 339 0.21 GLN 269 -0.16 LEU 336

ALA 339 0.19 GLY 270 -0.18 LEU 336

ALA 339 0.16 PHE 271 -0.17 ASP 375

ALA 339 0.16 LEU 272 -0.16 ASP 375

ALA 339 0.15 ASN 273 -0.15 THR 344

ALA 339 0.14 LEU 274 -0.14 ASP 338

ALA 339 0.11 THR 275 -0.14 ALA 373

ALA 339 0.12 GLY 276 -0.13 ALA 373

ALA 339 0.12 TYR 277 -0.15 ASP 375

ALA 339 0.14 SER 278 -0.16 ASP 375

ASP 338 0.15 LEU 279 -0.19 ASP 375

ASP 338 0.13 ASP 280 -0.18 ASP 375

ASP 338 0.10 GLN 281 -0.18 ASP 375

ASP 338 0.10 ILE 282 -0.21 ASP 375

ASP 338 0.12 LEU 283 -0.23 ASP 375

ALA 371 0.09 GLY 284 -0.26 ASP 375

LYS 305 0.08 ARG 285 -0.26 ASP 375

LYS 305 0.09 ASN 286 -0.28 ASP 375

LYS 305 0.07 CYS 287 -0.26 ASP 375

PHE 239 0.10 ARG 288 -0.26 ASP 375

PHE 239 0.09 PHE 289 -0.21 ASP 375

PHE 239 0.12 LEU 290 -0.19 ALA 373

PHE 239 0.15 GLN 291 -0.19 ALA 373

PHE 239 0.16 GLY 292 -0.21 ALA 372

PHE 239 0.17 PRO 293 -0.24 ALA 372

PHE 239 0.21 GLU 294 -0.27 ALA 372

PHE 239 0.21 THR 295 -0.28 ALA 372

PHE 239 0.20 ASP 296 -0.35 ALA 372

PHE 239 0.17 PRO 297 -0.36 ALA 372

PHE 239 0.17 LYS 298 -0.46 ALA 372

PHE 239 0.18 ALA 299 -0.38 ALA 372

PHE 239 0.15 VAL 300 -0.35 ALA 373

LYS 305 0.17 GLU 301 -0.49 ALA 373

LYS 305 0.19 ARG 302 -0.50 ALA 373

LYS 305 0.17 ILE 303 -0.41 ALA 373

LYS 305 0.20 ARG 304 -0.47 ASP 375

LYS 305 0.27 LYS 305 -0.60 ASP 375

LYS 305 0.22 ALA 306 -0.55 ASP 375

LYS 305 0.17 ILE 307 -0.50 ASP 375

LYS 305 0.19 GLU 308 -0.61 ASP 375

ARG 302 0.16 GLN 309 -0.70 ASP 375

PRO 257 0.15 GLY 310 -0.59 ASP 375

ARG 302 0.13 ASN 311 -0.55 ASP 375

LYS 305 0.10 ASP 312 -0.43 ALA 372

ALA 306 0.12 MET 313 -0.41 ALA 372

PHE 239 0.18 SER 314 -0.29 ALA 372

PHE 239 0.24 VAL 315 -0.30 ALA 372

PHE 239 0.31 CYS 316 -0.31 ALA 372

PHE 239 0.26 LEU 317 -0.30 ALA 372

PHE 239 0.25 LEU 318 -0.26 ALA 372

PHE 239 0.20 ASN 319 -0.21 ALA 372

PHE 239 0.16 TYR 320 -0.17 ALA 372

SER 240 0.14 ARG 321 -0.14 ALA 372

SER 240 0.10 VAL 322 -0.13 ASP 375

SER 240 0.12 ASP 323 -0.13 ALA 372

PHE 239 0.14 GLY 324 -0.16 ALA 372

SER 240 0.18 THR 325 -0.17 ALA 372

PHE 239 0.21 THR 326 -0.20 ALA 372

SER 240 0.26 PHE 327 -0.21 ALA 372

PHE 239 0.32 TRP 328 -0.25 ALA 372

PHE 239 0.29 ASN 329 -0.22 ALA 372

PHE 239 0.34 GLN 330 -0.22 ALA 372

PHE 239 0.21 PHE 331 -0.22 ALA 372

SER 240 0.13 PHE 332 -0.26 ALA 372

LYS 305 0.06 ILE 333 -0.32 ALA 372

VAL 315 0.07 ALA 334 -0.36 ASP 375

ILE 242 0.09 ALA 335 -0.44 ASP 375

ILE 242 0.24 LEU 336 -0.42 ASP 375

ILE 242 0.24 ARG 337 -0.47 ASP 375

LYS 243 0.33 ASP 338 -0.46 ASP 375

SER 240 0.43 ALA 339 -0.47 ASP 375

SER 240 0.32 GLY 340 -0.54 ASP 375

SER 240 0.30 GLY 341 -0.57 ASP 375

LYS 243 0.20 ASN 342 -0.57 ASP 375

GLN 364 0.14 VAL 343 -0.52 ASP 375

GLU 367 0.15 THR 344 -0.43 ASP 375

TYR 266 0.14 ASN 345 -0.39 ASP 375

LEU 336 0.11 PHE 346 -0.37 ASP 375

LEU 336 0.16 VAL 347 -0.30 ASP 375

LEU 336 0.11 GLY 348 -0.27 ASP 375

ALA 339 0.13 VAL 349 -0.22 ALA 372

SER 240 0.18 GLN 350 -0.19 ALA 372

SER 240 0.32 CYS 351 -0.18 ARG 337

SER 240 0.36 LYS 352 -0.18 ALA 372

PHE 239 0.46 VAL 353 -0.21 ALA 372

PHE 239 0.48 SER 354 -0.23 ALA 372

PHE 239 0.40 ASP 355 -0.27 ALA 372

PHE 239 0.44 GLN 356 -0.28 ALA 372

PHE 239 0.51 TYR 357 -0.27 ALA 372

PHE 239 0.41 ALA 358 -0.31 ALA 372

PHE 239 0.37 ALA 359 -0.34 ALA 372

PHE 239 0.37 THR 360 -0.34 ALA 372

PHE 239 0.36 VAL 361 -0.35 ALA 372

PHE 239 0.32 THR 362 -0.41 ALA 372

PHE 239 0.29 LYS 363 -0.45 ALA 372

PHE 239 0.26 GLN 364 -0.45 ALA 372

PHE 239 0.23 GLN 365 -0.51 ALA 372

PHE 239 0.23 GLU 366 -0.60 ALA 372

ALA 371 0.31 GLU 367 -0.66 ALA 372

SER 258 0.30 GLU 368 -0.72 ALA 372

SER 258 0.24 GLU 369 -0.82 ALA 372

SER 258 0.27 GLU 370 -0.95 ALA 372

SER 258 0.38 ALA 371 -1.12 ALA 372

SER 258 0.34 ALA 372 -1.42 ALA 372

SER 258 0.30 ALA 373 -1.39 ALA 372

SER 258 0.39 ASN 374 -1.35 ALA 372

SER 258 0.44 ASP 375 -1.59 ALA 372

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 ***

CA distance fluctuations for 2608052227103017248

--- normal mode 8 ---

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 *