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

* EHB *

CA distance fluctuations for 260611084001679973

--- 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 125 0.18 ASP 20 -0.29 LYS 381

GLY 125 0.15 PRO 21 -0.31 LYS 381

GLU 110 0.17 GLU 22 -0.28 LYS 381

GLU 110 0.20 LEU 23 -0.25 LYS 381

GLU 110 0.19 LEU 24 -0.24 LYS 381

GLU 110 0.18 ALA 25 -0.24 LYS 381

GLU 110 0.24 SER 26 -0.21 LYS 381

GLU 110 0.30 VAL 27 -0.18 LYS 381

GLU 110 0.25 THR 28 -0.18 LYS 381

ARG 368 0.22 PRO 29 -0.17 LYS 381

ARG 368 0.16 PHE 30 -0.23 LYS 381

GLU 305 0.13 THR 31 -0.26 LYS 381

GLU 110 0.12 VAL 32 -0.31 LYS 381

GLU 110 0.09 GLU 33 -0.35 LYS 381

GLU 110 0.08 GLU 34 -0.33 LYS 381

GLU 110 0.11 VAL 35 -0.32 LYS 381

GLY 125 0.10 GLU 36 -0.38 LYS 381

ASN 199 0.09 ALA 37 -0.42 LYS 381

ASN 199 0.10 LEU 38 -0.36 LYS 381

ARG 200 0.10 TYR 39 -0.37 LYS 381

ARG 200 0.16 GLU 40 -0.43 LYS 381

THR 201 0.19 LEU 41 -0.40 LYS 381

THR 201 0.14 PHE 42 -0.34 LYS 381

THR 201 0.15 LYS 43 -0.39 ASP 333

THR 201 0.20 LYS 44 -0.45 ASP 333

THR 201 0.15 LEU 45 -0.39 ASP 333

THR 201 0.13 SER 46 -0.35 ASP 333

THR 201 0.15 SER 47 -0.41 ASP 333

THR 201 0.16 SER 48 -0.45 ASP 333

THR 201 0.13 ILE 49 -0.35 ASP 333

THR 201 0.12 ILE 50 -0.32 ASP 333

THR 201 0.12 ASP 51 -0.35 ASP 333

THR 201 0.10 ASP 52 -0.29 ASP 333

GLY 125 0.10 GLY 53 -0.30 ASP 333

GLY 125 0.11 LEU 54 -0.26 ASP 333

THR 201 0.10 ILE 55 -0.25 ASP 333

THR 201 0.09 HIS 56 -0.20 ASP 333

THR 201 0.08 LYS 57 -0.18 LYS 418

THR 201 0.09 GLU 58 -0.22 LYS 418

THR 201 0.11 GLU 59 -0.25 ASP 333

LEU 327 0.10 PHE 60 -0.20 LYS 418

ARG 330 0.08 GLN 61 -0.22 ARG 337

ARG 330 0.12 LEU 62 -0.28 VAL 335

LEU 327 0.14 ALA 63 -0.26 THR 410

ALA 326 0.09 LEU 64 -0.20 ARG 337

ARG 331 0.06 PHE 65 -0.29 ARG 337

ARG 331 0.12 ARG 66 -0.32 VAL 335

ARG 331 0.10 ASN 67 -0.30 LYS 418

ARG 330 0.12 ARG 68 -0.28 LYS 418

ARG 330 0.09 ASN 69 -0.27 SER 422

ARG 331 0.07 ARG 70 -0.25 GLU 425

ARG 331 0.05 ARG 71 -0.21 GLU 425

ARG 368 0.03 ASN 72 -0.17 GLU 425

ASN 369 0.06 LEU 73 -0.13 GLU 425

ASN 369 0.08 PHE 74 -0.10 GLU 425

ASN 369 0.07 ALA 75 -0.13 GLU 425

ASN 369 0.07 ASP 76 -0.12 GLU 425

ASN 369 0.11 ARG 77 -0.10 LYS 381

ASN 369 0.12 ILE 78 -0.12 LYS 381

ASN 369 0.09 PHE 79 -0.15 LYS 381

ASN 369 0.10 ASP 80 -0.12 LYS 381

ASN 369 0.14 VAL 81 -0.12 LYS 381

LYS 117 0.12 PHE 82 -0.16 LYS 381

GLY 125 0.15 ASP 83 -0.16 LYS 381

GLY 125 0.21 VAL 84 -0.16 LYS 381

GLY 125 0.20 LYS 85 -0.16 LYS 381

GLN 123 0.20 ARG 86 -0.15 LYS 381

THR 124 0.16 ASN 87 -0.16 LYS 381

ARG 122 0.16 GLY 88 -0.16 LYS 381

THR 124 0.12 VAL 89 -0.19 LYS 381

GLY 125 0.12 ILE 90 -0.21 LYS 381

GLY 125 0.13 GLU 91 -0.24 LYS 381

GLY 125 0.13 PHE 92 -0.28 LYS 381

GLY 125 0.17 GLY 93 -0.24 LYS 381

GLY 125 0.15 GLU 94 -0.21 LYS 381

GLY 125 0.11 PHE 95 -0.23 LYS 381

GLY 125 0.12 VAL 96 -0.24 LYS 381

LYS 113 0.19 ARG 97 -0.19 LYS 381

ASN 369 0.16 SER 98 -0.17 LYS 381

ARG 368 0.15 LEU 99 -0.19 LYS 381

ARG 368 0.19 GLY 100 -0.16 LYS 381

ASN 369 0.23 VAL 101 -0.13 LYS 381

ARG 368 0.22 PHE 102 -0.13 LYS 381

ARG 368 0.23 HIS 103 -0.14 LYS 381

ARG 368 0.30 PRO 104 -0.10 LYS 381

ARG 368 0.31 SER 105 -0.10 LYS 381

ARG 368 0.30 ALA 106 -0.10 LYS 381

ARG 368 0.33 PRO 107 -0.07 LYS 381

ASN 369 0.35 VAL 108 -0.09 PRO 104

GLU 305 0.32 HIS 109 -0.06 LYS 381

VAL 27 0.30 GLU 110 -0.08 LYS 381

ASN 369 0.28 LYS 111 -0.08 LYS 381

GLU 305 0.29 VAL 112 -0.08 PRO 193

VAL 27 0.26 LYS 113 -0.07 LYS 381

ASN 369 0.22 PHE 114 -0.09 LYS 381

LEU 308 0.23 ALA 115 -0.08 LYS 381

LEU 308 0.22 PHE 116 -0.07 LYS 381

VAL 27 0.18 LYS 117 -0.08 LYS 381

LEU 308 0.15 LEU 118 -0.09 LYS 381

LEU 308 0.16 TYR 119 -0.07 LYS 381

VAL 84 0.15 ASP 120 -0.07 VAL 146

ARG 86 0.14 LEU 121 -0.10 VAL 146

ARG 86 0.18 ARG 122 -0.10 VAL 146

ARG 86 0.20 GLN 123 -0.08 VAL 146

ARG 86 0.20 THR 124 -0.08 VAL 146

VAL 84 0.21 GLY 125 -0.06 LYS 381

VAL 27 0.18 PHE 126 -0.06 VAL 146

GLU 305 0.16 ILE 127 -0.06 PRO 193

VAL 27 0.13 GLU 128 -0.07 VAL 146

VAL 27 0.12 ARG 129 -0.07 VAL 146

ARG 86 0.10 GLU 130 -0.10 VAL 146

ARG 86 0.11 GLU 131 -0.10 VAL 146

VAL 27 0.10 LEU 132 -0.07 PRO 193

VAL 27 0.09 LYS 133 -0.09 VAL 146

VAL 27 0.08 GLU 134 -0.14 VAL 146

VAL 27 0.08 MET 135 -0.10 VAL 146

VAL 27 0.08 VAL 136 -0.07 VAL 146

VAL 27 0.06 VAL 137 -0.16 VAL 146

PHE 334 0.04 ALA 138 -0.15 VAL 146

PHE 334 0.05 LEU 139 -0.09 ILE 428

HIS 414 0.07 LEU 140 -0.11 ILE 428

LEU 411 0.06 HIS 141 -0.15 VAL 146

LYS 336 0.07 GLU 142 -0.16 GLU 425

LEU 318 0.08 SER 143 -0.20 PHE 341

HIS 414 0.10 GLU 144 -0.21 ILE 428

LYS 415 0.11 LEU 145 -0.18 ILE 428

LYS 415 0.14 VAL 146 -0.16 VAL 137

LYS 415 0.11 LEU 147 -0.13 VAL 137

LYS 415 0.10 SER 148 -0.08 GLU 305

LYS 415 0.09 GLU 149 -0.07 GLU 130

LYS 415 0.09 ASP 150 -0.08 GLU 305

LYS 415 0.08 MET 151 -0.08 THR 201

LYS 415 0.08 ILE 152 -0.07 THR 201

VAL 27 0.08 GLU 153 -0.06 THR 201

VAL 27 0.09 VAL 154 -0.08 THR 201

VAL 27 0.09 MET 155 -0.09 THR 201

VAL 27 0.10 VAL 156 -0.07 TYR 194

ALA 395 0.12 ASP 157 -0.08 TYR 194

ALA 395 0.20 LYS 158 -0.09 THR 201

ALA 395 0.18 ALA 159 -0.09 PRO 193

GLU 305 0.17 PHE 160 -0.09 PRO 193

PRO 396 0.19 VAL 161 -0.08 PRO 193

GLU 305 0.28 GLN 162 -0.09 PRO 193

GLU 305 0.27 ALA 163 -0.09 PRO 193

GLU 305 0.24 ASP 164 -0.08 PRO 193

GLU 305 0.29 ARG 165 -0.08 PRO 193

GLU 305 0.25 LYS 166 -0.07 PRO 193

GLU 305 0.21 ASN 167 -0.07 PRO 193

GLU 305 0.18 ASP 168 -0.06 PRO 193

GLU 305 0.15 GLY 169 -0.07 GLU 149

GLU 305 0.16 LYS 170 -0.06 PRO 193

GLU 305 0.21 ILE 171 -0.07 PRO 193

GLU 305 0.23 ASP 172 -0.06 PRO 193

GLU 305 0.25 ILE 173 -0.06 PRO 193

GLU 305 0.29 ASP 174 -0.07 PRO 193

GLU 305 0.30 GLU 175 -0.08 PRO 193

GLU 305 0.30 TRP 176 -0.09 PRO 193

GLU 305 0.34 LYS 177 -0.09 PRO 193

GLU 305 0.39 ASP 178 -0.10 PRO 193

GLU 305 0.38 PHE 179 -0.11 PRO 193

LEU 308 0.40 VAL 180 -0.13 PRO 193

GLU 305 0.45 SER 181 -0.13 PRO 193

GLU 305 0.52 LEU 182 -0.12 PRO 193

LEU 308 0.54 ASN 183 -0.13 PRO 193

LEU 308 0.45 PRO 184 -0.16 PRO 193

LEU 308 0.43 SER 185 -0.16 PRO 193

LEU 308 0.37 LEU 186 -0.13 PRO 193

ASN 369 0.31 ILE 187 -0.13 PRO 193

ASN 369 0.32 LYS 188 -0.15 PRO 193

ASN 369 0.23 ASN 189 -0.11 TYR 194

ASN 369 0.26 MET 190 -0.09 LYS 381

ARG 368 0.27 THR 191 -0.11 PRO 193

ARG 368 0.18 LEU 192 -0.15 LYS 381

ARG 368 0.21 PRO 193 -0.16 PRO 184

ARG 368 0.11 TYR 194 -0.21 LYS 381

ARG 368 0.13 LEU 195 -0.23 LYS 381

ARG 368 0.13 LYS 196 -0.22 LYS 381

LYS 44 0.11 ASP 197 -0.30 LYS 381

LEU 41 0.14 ILE 198 -0.37 LYS 381

GLU 40 0.14 ASN 199 -0.41 LYS 381

LEU 41 0.17 ARG 200 -0.47 LYS 381

LYS 44 0.20 THR 201 -0.51 LYS 381

LEU 182 0.52 GLU 305 -0.14 SER 397

LEU 182 0.44 GLY 306 -0.14 SER 397

ASN 183 0.42 PRO 307 -0.12 THR 201

ASN 183 0.54 LEU 308 -0.11 THR 201

ASN 183 0.39 MET 309 -0.13 THR 201

ASN 183 0.27 MET 310 -0.14 THR 201

MET 310 0.23 ASN 311 -0.11 THR 201

VAL 27 0.11 ALA 312 -0.10 THR 201

LEU 308 0.19 PHE 313 -0.10 TYR 194

TYR 392 0.22 GLU 314 -0.12 THR 201

TYR 392 0.13 MET 315 -0.12 THR 201

ASN 369 0.11 ILE 316 -0.09 THR 201

ASN 369 0.15 THR 317 -0.11 THR 201

GLN 338 0.10 LEU 318 -0.14 ALA 326

PHE 334 0.09 SER 319 -0.09 ALA 326

PHE 334 0.09 GLN 320 -0.13 GLU 425

ARG 368 0.07 GLY 321 -0.12 GLU 425

ASN 369 0.12 LEU 322 -0.10 LYS 381

ARG 368 0.11 ASN 323 -0.12 LYS 381

ARG 368 0.09 LEU 324 -0.17 LYS 381

LEU 192 0.09 SER 325 -0.21 LYS 381

ALA 63 0.13 ALA 326 -0.25 LYS 381

ALA 63 0.14 LEU 327 -0.29 LYS 381

ALA 63 0.11 PHE 328 -0.34 LYS 381

ALA 63 0.13 ASP 329 -0.41 GLU 409

ALA 63 0.12 ARG 330 -0.51 GLU 409

ARG 66 0.12 ARG 331 -0.61 GLU 409

PRO 193 0.08 GLN 332 -0.46 THR 410

PRO 193 0.10 ASP 333 -0.45 LYS 44

VAL 335 0.12 PHE 334 -0.39 SER 48

PHE 334 0.12 VAL 335 -0.32 ARG 66

PHE 334 0.10 LYS 336 -0.24 ARG 66

LEU 411 0.10 ARG 337 -0.30 ASN 67

SER 185 0.11 GLN 338 -0.21 GLU 425

SER 185 0.11 THR 339 -0.22 PHE 65

SER 185 0.14 ARG 340 -0.17 ASP 329

ASN 183 0.13 PHE 341 -0.20 SER 143

ASN 183 0.16 VAL 342 -0.15 SER 143

ASN 183 0.18 SER 343 -0.16 LEU 145

LEU 182 0.20 ARG 344 -0.13 ASN 69

LEU 182 0.24 ARG 345 -0.14 ASN 69

LEU 182 0.30 GLU 346 -0.12 ARG 331

LEU 182 0.32 PRO 347 -0.13 ARG 331

LEU 182 0.32 SER 348 -0.13 ARG 331

LEU 182 0.28 GLU 349 -0.14 ARG 331

LEU 182 0.26 ILE 350 -0.15 ARG 331

ASN 183 0.28 ILE 351 -0.16 ARG 331

LEU 182 0.26 ALA 352 -0.16 ARG 331

LEU 182 0.23 ASN 353 -0.17 ARG 331

ASN 183 0.22 ILE 354 -0.19 ARG 331

ASN 183 0.23 GLU 355 -0.18 ARG 331

LEU 182 0.21 ALA 356 -0.19 ARG 331

SER 379 0.20 VAL 357 -0.21 ARG 331

SER 378 0.19 ALA 358 -0.23 ARG 331

LEU 182 0.18 ASN 359 -0.22 ARG 331

SER 379 0.26 SER 360 -0.23 ARG 331

SER 378 0.30 MET 361 -0.26 ARG 331

SER 378 0.29 GLY 362 -0.27 ARG 331

SER 185 0.17 PHE 363 -0.24 ARG 331

SER 185 0.19 LYS 364 -0.20 ARG 331

SER 185 0.23 SER 365 -0.18 ARG 331

PRO 184 0.28 HIS 366 -0.14 ARG 331

PRO 184 0.32 THR 367 -0.12 ARG 331

PRO 184 0.39 ARG 368 -0.09 THR 201

ASN 183 0.44 ASN 369 -0.09 THR 201

ASN 183 0.38 PHE 370 -0.12 THR 201

SER 185 0.39 LYS 371 -0.13 THR 201

SER 185 0.30 THR 372 -0.15 THR 201

SER 185 0.25 ARG 373 -0.17 THR 201

SER 185 0.20 LEU 374 -0.22 ARG 331

SER 185 0.15 GLU 375 -0.24 ARG 331

SER 185 0.12 GLY 376 -0.29 ARG 331

GLY 362 0.15 LEU 377 -0.28 ARG 331

MET 361 0.30 SER 378 -0.34 ARG 331

MET 361 0.30 SER 379 -0.39 THR 201

LYS 419 0.29 ILE 380 -0.44 THR 201

LYS 419 0.18 LYS 381 -0.51 ARG 331

LYS 419 0.18 ALA 382 -0.52 ARG 331

LYS 419 0.26 GLY 383 -0.42 ARG 331

LYS 419 0.13 GLN 384 -0.39 ARG 331

SER 185 0.08 LEU 385 -0.37 ARG 331

SER 185 0.11 ALA 386 -0.29 ARG 331

SER 185 0.16 VAL 387 -0.25 ARG 331

SER 185 0.23 VAL 388 -0.20 THR 201

SER 185 0.27 ILE 389 -0.18 THR 201

SER 185 0.34 GLU 390 -0.15 THR 201

ASN 183 0.30 ILE 391 -0.15 THR 201

ASN 183 0.34 TYR 392 -0.13 THR 201

ASN 183 0.28 GLU 393 -0.13 THR 201

ASN 311 0.23 VAL 394 -0.12 THR 201

LYS 158 0.20 ALA 395 -0.11 THR 201

GLN 162 0.24 PRO 396 -0.11 THR 201

GLN 162 0.21 SER 397 -0.14 GLU 305

LEU 182 0.19 LEU 398 -0.12 THR 201

ASN 183 0.24 PHE 399 -0.12 THR 201

ASN 183 0.20 MET 400 -0.14 THR 201

SER 185 0.22 VAL 401 -0.15 THR 201

SER 185 0.21 ASP 402 -0.17 ASP 329

SER 185 0.18 VAL 403 -0.20 ASP 329

LYS 188 0.16 ARG 404 -0.24 ASP 329

LYS 188 0.11 LYS 405 -0.30 ARG 330

PRO 104 0.12 ALA 406 -0.30 THR 201

GLU 375 0.10 ALA 407 -0.40 ARG 330

LEU 385 0.07 GLY 408 -0.51 ARG 331

LEU 411 0.08 GLU 409 -0.61 ARG 331

LEU 411 0.10 THR 410 -0.49 ARG 331

VAL 146 0.10 LEU 411 -0.38 ARG 331

VAL 146 0.12 GLU 412 -0.39 ARG 331

VAL 146 0.10 TYR 413 -0.38 ARG 331

VAL 146 0.13 HIS 414 -0.31 ARG 331

ILE 380 0.19 LYS 415 -0.32 ARG 331

GLY 383 0.24 PHE 416 -0.29 ARG 331

GLY 383 0.17 TYR 417 -0.27 ARG 331

ILE 380 0.21 LYS 418 -0.30 ASN 67

ILE 380 0.29 LYS 419 -0.28 SER 48

ILE 380 0.22 LEU 420 -0.24 SER 48

ILE 380 0.20 CYS 421 -0.27 ASN 67

ILE 380 0.25 SER 422 -0.29 ASN 67

ILE 380 0.25 LYS 423 -0.24 ASN 67

ILE 380 0.19 LEU 424 -0.23 ASN 67

ILE 380 0.19 GLU 425 -0.27 ASN 69

ILE 380 0.17 ASN 426 -0.24 ASN 69

LEU 182 0.19 ILE 427 -0.20 ASN 69

LEU 182 0.15 ILE 428 -0.22 ASN 69

ILE 380 0.14 TRP 429 -0.18 ASN 69

ILE 380 0.16 ARG 430 -0.18 ASN 69

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.

*** EHB ***

CA distance fluctuations for 260611084001679973

--- normal mode 9 ---

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

* EHB *