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 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
ARG 330 0.21 ASP 20 -0.23 LYS 85

ARG 330 0.24 PRO 21 -0.19 GLY 125

ARG 330 0.22 GLU 22 -0.22 GLY 125

ARG 330 0.17 LEU 23 -0.27 GLY 125

ARG 330 0.17 LEU 24 -0.24 GLY 125

ARG 330 0.19 ALA 25 -0.23 GLY 125

ARG 330 0.15 SER 26 -0.29 GLY 125

ARG 330 0.11 VAL 27 -0.34 GLY 125

ARG 330 0.11 THR 28 -0.26 GLY 125

ARG 337 0.15 PRO 29 -0.22 GLU 110

ARG 337 0.19 PHE 30 -0.19 GLY 125

THR 410 0.22 THR 31 -0.18 GLY 125

ARG 330 0.25 VAL 32 -0.18 GLY 125

ARG 330 0.32 GLU 33 -0.14 GLY 125

ARG 330 0.28 GLU 34 -0.12 GLY 125

ARG 330 0.27 VAL 35 -0.14 GLY 125

ARG 330 0.34 GLU 36 -0.12 GLY 93

ARG 330 0.44 ALA 37 -0.20 ASN 199

ARG 330 0.30 LEU 38 -0.18 LYS 381

ARG 330 0.28 TYR 39 -0.20 LYS 381

ARG 330 0.36 GLU 40 -0.28 ARG 200

ARG 330 0.31 LEU 41 -0.28 LYS 381

ARG 330 0.18 PHE 42 -0.29 ALA 407

ARG 331 0.17 LYS 43 -0.30 LYS 381

LYS 43 0.14 LYS 44 -0.39 ALA 407

PHE 60 0.08 LEU 45 -0.41 ALA 407

ARG 122 0.08 SER 46 -0.37 ALA 407

ARG 122 0.09 SER 47 -0.39 ALA 407

ARG 122 0.10 SER 48 -0.45 ALA 407

ARG 122 0.14 ILE 49 -0.43 ALA 407

ARG 122 0.14 ILE 50 -0.38 ALA 407

ARG 122 0.10 ASP 51 -0.36 LYS 381

ARG 122 0.09 ASP 52 -0.31 LYS 381

ARG 330 0.07 GLY 53 -0.29 ALA 407

ASP 80 0.08 LEU 54 -0.31 ALA 407

ASP 80 0.10 ILE 55 -0.36 ALA 407

ARG 122 0.16 HIS 56 -0.36 ALA 407

ARG 122 0.19 LYS 57 -0.38 ALA 407

ARG 122 0.17 GLU 58 -0.41 ALA 407

ARG 122 0.13 GLU 59 -0.44 ALA 407

ARG 122 0.10 PHE 60 -0.43 ALA 407

ARG 122 0.12 GLN 61 -0.46 ALA 407

LEU 41 0.12 LEU 62 -0.51 ALA 407

LEU 41 0.18 ALA 63 -0.53 ALA 407

ALA 37 0.19 LEU 64 -0.55 ALA 406

THR 201 0.19 PHE 65 -0.55 ALA 407

ALA 37 0.17 ARG 66 -0.57 ALA 407

ALA 37 0.13 ASN 67 -0.49 ALA 407

ARG 122 0.14 ARG 68 -0.45 ALA 407

ARG 122 0.16 ASN 69 -0.40 ALA 407

GLU 134 0.13 ARG 70 -0.39 ALA 407

GLU 134 0.17 ARG 71 -0.35 ALA 406

ARG 71 0.14 ASN 72 -0.35 ALA 406

GLU 131 0.13 LEU 73 -0.31 ALA 406

LEU 192 0.12 PHE 74 -0.35 ALA 406

THR 201 0.10 ALA 75 -0.39 ALA 406

LYS 57 0.14 ASP 76 -0.33 ALA 406

LYS 57 0.12 ARG 77 -0.32 ALA 406

LEU 192 0.06 ILE 78 -0.35 ALA 406

ASP 80 0.10 PHE 79 -0.35 ALA 406

HIS 56 0.15 ASP 80 -0.30 ALA 406

PHE 114 0.12 VAL 81 -0.28 ALA 406

GLU 110 0.12 PHE 82 -0.28 ALA 406

GLU 110 0.14 ASP 83 -0.28 ALA 407

GLU 110 0.21 VAL 84 -0.22 ALA 407

GLU 110 0.18 LYS 85 -0.23 ASP 20

LYS 113 0.16 ARG 86 -0.25 ALA 407

GLU 110 0.12 ASN 87 -0.27 ALA 407

GLN 123 0.16 GLY 88 -0.31 ALA 407

ASP 80 0.11 VAL 89 -0.31 ALA 407

GLU 110 0.09 ILE 90 -0.30 ALA 407

PRO 107 0.08 GLU 91 -0.26 ALA 407

ARG 330 0.13 PHE 92 -0.23 ALA 407

ARG 330 0.11 GLY 93 -0.20 LYS 381

PRO 107 0.11 GLU 94 -0.23 ALA 407

ARG 330 0.08 PHE 95 -0.25 ALA 407

ARG 330 0.12 VAL 96 -0.19 LYS 381

PRO 107 0.09 ARG 97 -0.22 GLN 123

PRO 107 0.10 SER 98 -0.23 ALA 406

ARG 337 0.11 LEU 99 -0.23 ALA 407

ARG 337 0.11 GLY 100 -0.18 LYS 381

VAL 84 0.12 VAL 101 -0.20 ALA 406

ARG 337 0.14 PHE 102 -0.21 ALA 406

ARG 337 0.18 HIS 103 -0.18 SER 379

GLN 338 0.19 PRO 104 -0.18 SER 379

ARG 337 0.16 SER 105 -0.16 SER 379

VAL 84 0.12 ALA 106 -0.17 SER 379

VAL 84 0.17 PRO 107 -0.18 ARG 368

VAL 84 0.17 VAL 108 -0.24 ARG 368

VAL 84 0.19 HIS 109 -0.22 ARG 368

VAL 84 0.21 GLU 110 -0.22 PRO 29

VAL 84 0.17 LYS 111 -0.23 ALA 406

VAL 84 0.14 VAL 112 -0.24 ARG 368

VAL 84 0.18 LYS 113 -0.25 VAL 27

VAL 84 0.17 PHE 114 -0.26 ALA 406

VAL 84 0.10 ALA 115 -0.29 ALA 406

GLY 88 0.10 PHE 116 -0.26 ALA 406

GLY 88 0.14 LYS 117 -0.27 VAL 27

LYS 57 0.09 LEU 118 -0.29 ALA 406

LYS 57 0.09 TYR 119 -0.27 ALA 406

LYS 57 0.12 ASP 120 -0.24 ALA 406

LYS 57 0.15 LEU 121 -0.24 ALA 406

LYS 57 0.19 ARG 122 -0.25 VAL 27

GLY 88 0.16 GLN 123 -0.32 VAL 27

LYS 57 0.14 THR 124 -0.31 VAL 27

GLY 88 0.15 GLY 125 -0.34 VAL 27

GLY 88 0.12 PHE 126 -0.27 VAL 27

LYS 57 0.11 ILE 127 -0.22 VAL 27

ARG 71 0.12 GLU 128 -0.21 VAL 27

ARG 71 0.12 ARG 129 -0.17 ALA 406

ARG 71 0.15 GLU 130 -0.17 ALA 406

ARG 71 0.15 GLU 131 -0.20 ALA 406

ARG 71 0.12 LEU 132 -0.20 ALA 406

ARG 71 0.13 LYS 133 -0.18 ALA 406

ARG 71 0.17 GLU 134 -0.20 ALA 406

ARG 71 0.13 MET 135 -0.24 ALA 406

PRO 193 0.15 VAL 136 -0.20 ALA 406

TYR 194 0.15 VAL 137 -0.18 ALA 406

TYR 194 0.16 ALA 138 -0.23 ALA 406

PRO 193 0.19 LEU 139 -0.25 ALA 406

TYR 194 0.21 LEU 140 -0.18 ALA 406

THR 201 0.20 HIS 141 -0.18 ALA 406

THR 201 0.22 GLU 142 -0.25 ALA 406

TYR 194 0.26 SER 143 -0.20 ARG 404

THR 201 0.25 GLU 144 -0.12 ALA 406

ARG 200 0.23 LEU 145 -0.10 ALA 406

THR 201 0.20 VAL 146 -0.09 ALA 406

ARG 200 0.18 LEU 147 -0.08 ALA 406

GLU 425 0.16 SER 148 -0.08 ALA 406

THR 201 0.13 GLU 149 -0.10 ALA 406

ASN 426 0.13 ASP 150 -0.08 ALA 406

ARG 200 0.14 MET 151 -0.08 ALA 406

PRO 193 0.14 ILE 152 -0.12 ALA 406

PRO 193 0.11 GLU 153 -0.11 ALA 406

PRO 193 0.12 VAL 154 -0.09 ALA 406

PRO 193 0.13 MET 155 -0.12 LYS 371

PRO 193 0.11 VAL 156 -0.15 ALA 406

PRO 193 0.08 ASP 157 -0.13 ALA 406

PRO 193 0.09 LYS 158 -0.14 ARG 368

PRO 193 0.09 ALA 159 -0.19 ARG 368

ARG 71 0.08 PHE 160 -0.18 ARG 368

ARG 71 0.07 VAL 161 -0.17 ARG 368

ARG 71 0.05 GLN 162 -0.21 ARG 368

GLY 88 0.06 ALA 163 -0.23 ARG 368

ARG 71 0.07 ASP 164 -0.20 ARG 368

GLY 88 0.08 ARG 165 -0.21 ARG 368

GLY 88 0.09 LYS 166 -0.19 ARG 368

ARG 71 0.08 ASN 167 -0.17 ARG 368

ASN 69 0.09 ASP 168 -0.19 VAL 27

ARG 71 0.10 GLY 169 -0.19 VAL 27

ARG 71 0.10 LYS 170 -0.21 VAL 27

GLY 88 0.09 ILE 171 -0.21 VAL 27

GLY 88 0.13 ASP 172 -0.24 VAL 27

ARG 86 0.15 ILE 173 -0.26 VAL 27

ARG 86 0.14 ASP 174 -0.23 ARG 368

ARG 86 0.11 GLU 175 -0.23 ARG 368

ARG 86 0.11 TRP 176 -0.25 ARG 368

ARG 86 0.13 LYS 177 -0.26 ARG 368

ARG 86 0.11 ASP 178 -0.27 ARG 368

VAL 84 0.08 PHE 179 -0.28 ARG 368

VAL 84 0.10 VAL 180 -0.31 ARG 368

VAL 84 0.11 SER 181 -0.33 ARG 368

VAL 84 0.09 LEU 182 -0.34 ARG 368

VAL 84 0.08 ASN 183 -0.38 ARG 368

HIS 109 0.11 PRO 184 -0.38 ARG 368

SER 105 0.15 SER 185 -0.40 ARG 368

PRO 104 0.08 LEU 186 -0.33 ARG 368

VAL 84 0.09 ILE 187 -0.30 ARG 368

PRO 104 0.16 LYS 188 -0.34 ALA 406

THR 191 0.19 ASN 189 -0.38 ALA 406

LEU 318 0.11 MET 190 -0.30 ALA 406

ASN 189 0.19 THR 191 -0.24 ALA 406

LEU 318 0.25 LEU 192 -0.23 LYS 381

GLN 338 0.29 PRO 193 -0.20 SER 379

ARG 337 0.33 TYR 194 -0.19 SER 379

ARG 337 0.26 LEU 195 -0.18 SER 379

ARG 337 0.28 LYS 196 -0.14 GLU 40

THR 410 0.37 ASP 197 -0.19 GLU 40

THR 410 0.34 ILE 198 -0.22 GLU 40

THR 410 0.36 ASN 199 -0.24 GLU 40

THR 410 0.46 ARG 200 -0.28 GLU 40

THR 410 0.43 THR 201 -0.20 GLU 40

ARG 200 0.09 GLU 305 -0.20 LEU 182

ARG 200 0.13 GLY 306 -0.15 LEU 182

ARG 200 0.15 PRO 307 -0.17 ASN 183

ASP 197 0.16 LEU 308 -0.22 ASN 183

PRO 193 0.18 MET 309 -0.18 ASN 369

PRO 193 0.21 MET 310 -0.29 ASN 311

PRO 193 0.15 ASN 311 -0.29 MET 310

PRO 193 0.15 ALA 312 -0.19 LYS 371

PRO 193 0.13 PHE 313 -0.24 LYS 371

PRO 193 0.17 GLU 314 -0.30 LYS 371

PRO 193 0.22 MET 315 -0.25 LYS 371

PRO 193 0.19 ILE 316 -0.29 ALA 406

PRO 193 0.21 THR 317 -0.36 ALA 406

PRO 193 0.29 LEU 318 -0.37 ALA 406

PRO 193 0.23 SER 319 -0.42 ALA 406

SER 325 0.22 GLN 320 -0.54 ALA 406

TYR 194 0.15 GLY 321 -0.45 ALA 406

LEU 192 0.17 LEU 322 -0.43 ALA 406

LEU 192 0.23 ASN 323 -0.50 ALA 406

ILE 198 0.17 LEU 324 -0.47 ALA 406

ARG 337 0.30 SER 325 -0.49 ALA 406

LYS 336 0.30 ALA 326 -0.60 ALA 406

ALA 37 0.22 LEU 327 -0.48 ALA 407

ALA 37 0.31 PHE 328 -0.42 ALA 407

THR 201 0.41 ASP 329 -0.64 ALA 407

ALA 37 0.44 ARG 330 -0.61 ALA 407

ALA 37 0.39 ARG 331 -0.79 ALA 407

THR 201 0.32 GLN 332 -0.81 ALA 407

THR 201 0.26 ASP 333 -0.62 GLY 408

THR 201 0.34 PHE 334 -0.46 GLY 408

THR 201 0.32 VAL 335 -0.50 THR 410

THR 201 0.38 LYS 336 -0.55 LYS 405

THR 201 0.39 ARG 337 -0.23 ASN 69

THR 201 0.33 GLN 338 -0.20 LYS 405

ARG 200 0.34 THR 339 -0.17 ASN 69

ARG 200 0.29 ARG 340 -0.11 ASN 69

ARG 200 0.26 PHE 341 -0.07 ASN 87

ARG 200 0.22 VAL 342 -0.06 ASN 87

ARG 200 0.20 SER 343 -0.05 ASN 87

ARG 200 0.18 ARG 344 -0.04 ASN 87

ARG 344 0.16 ARG 345 -0.06 ARG 331

ARG 200 0.14 GLU 346 -0.09 ARG 331

ARG 200 0.15 PRO 347 -0.12 ASN 183

ARG 200 0.13 SER 348 -0.15 ASN 183

ARG 200 0.14 GLU 349 -0.13 ARG 331

ARG 200 0.16 ILE 350 -0.12 ARG 331

ARG 200 0.14 ILE 351 -0.18 ARG 331

ARG 200 0.12 ALA 352 -0.18 ARG 331

ARG 200 0.15 ASN 353 -0.15 ARG 331

ARG 200 0.16 ILE 354 -0.18 ARG 331

ARG 200 0.11 GLU 355 -0.24 ARG 331

SER 379 0.12 ALA 356 -0.21 ARG 331

SER 379 0.16 VAL 357 -0.19 ARG 331

SER 378 0.15 ALA 358 -0.25 ARG 331

SER 379 0.15 ASN 359 -0.28 ARG 331

SER 379 0.21 SER 360 -0.23 ARG 331

SER 379 0.25 MET 361 -0.24 ARG 331

SER 379 0.25 GLY 362 -0.33 ARG 331

SER 378 0.11 PHE 363 -0.36 ARG 331

ILE 427 0.07 LYS 364 -0.39 ARG 331

ARG 200 0.07 SER 365 -0.36 ARG 331

ALA 352 0.09 HIS 366 -0.37 ARG 331

SER 348 0.11 THR 367 -0.34 SER 185

SER 348 0.11 ARG 368 -0.40 SER 185

ARG 200 0.09 ASN 369 -0.35 ASN 183

ARG 200 0.13 PHE 370 -0.25 ASN 183

ARG 200 0.13 LYS 371 -0.36 SER 185

ARG 200 0.12 THR 372 -0.31 SER 185

ARG 200 0.10 ARG 373 -0.40 ARG 331

ARG 200 0.12 LEU 374 -0.40 ARG 331

ARG 200 0.08 GLU 375 -0.48 ARG 331

ARG 200 0.10 GLY 376 -0.46 ARG 331

GLY 362 0.13 LEU 377 -0.45 ARG 331

GLY 362 0.24 SER 378 -0.44 ARG 331

MET 361 0.25 SER 379 -0.51 ARG 331

LYS 419 0.22 ILE 380 -0.52 ARG 331

LYS 419 0.12 LYS 381 -0.69 ARG 331

ARG 200 0.18 ALA 382 -0.52 ARG 331

PHE 416 0.19 GLY 383 -0.45 ARG 331

LYS 419 0.09 GLN 384 -0.60 ARG 331

ARG 200 0.19 LEU 385 -0.53 ARG 331

ARG 200 0.16 ALA 386 -0.56 ARG 331

ARG 200 0.21 VAL 387 -0.43 GLN 332

ARG 200 0.19 VAL 388 -0.38 GLN 320

ARG 200 0.21 ILE 389 -0.27 GLN 320

ARG 200 0.20 GLU 390 -0.27 LEU 318

ARG 200 0.20 ILE 391 -0.15 GLU 314

ASP 197 0.20 TYR 392 -0.16 ASN 311

PRO 193 0.18 GLU 393 -0.09 GLN 162

PRO 193 0.20 VAL 394 -0.11 MET 155

PRO 193 0.17 ALA 395 -0.06 MET 151

ASP 197 0.15 PRO 396 -0.04 ARG 331

ARG 200 0.16 SER 397 -0.04 ARG 331

ARG 200 0.18 LEU 398 -0.04 ASN 87

ASP 197 0.19 PHE 399 -0.06 ARG 331

ASP 197 0.22 MET 400 -0.07 ASN 87

ARG 200 0.24 VAL 401 -0.09 PHE 65

ASP 197 0.28 ASP 402 -0.19 SER 319

ARG 200 0.29 VAL 403 -0.25 GLN 320

ARG 200 0.32 ARG 404 -0.44 GLN 320

ARG 200 0.33 LYS 405 -0.55 LYS 336

ARG 200 0.23 ALA 406 -0.64 GLN 332

ARG 200 0.22 ALA 407 -0.81 GLN 332

ARG 200 0.26 GLY 408 -0.78 GLN 332

ARG 200 0.39 GLU 409 -0.56 GLN 332

ARG 200 0.46 THR 410 -0.50 VAL 335

ARG 200 0.41 LEU 411 -0.29 ASN 67

ARG 200 0.33 GLU 412 -0.25 ASN 67

ARG 200 0.36 TYR 413 -0.31 LYS 336

ARG 200 0.37 HIS 414 -0.21 ASN 69

ARG 200 0.32 LYS 415 -0.16 ASN 69

ARG 200 0.28 PHE 416 -0.17 LYS 336

ARG 200 0.30 TYR 417 -0.15 ASN 69

ARG 200 0.30 LYS 418 -0.08 ASN 69

ARG 200 0.26 LYS 419 -0.08 ILE 49

ARG 200 0.24 LEU 420 -0.10 ILE 49

ARG 200 0.25 CYS 421 -0.06 ASN 87

ARG 200 0.24 SER 422 -0.05 ASN 353

ARG 200 0.20 LYS 423 -0.07 ASN 353

ARG 200 0.20 LEU 424 -0.06 ASN 183

ARG 430 0.23 GLU 425 -0.04 ASN 87

ARG 430 0.21 ASN 426 -0.04 ASN 87

ARG 200 0.19 ILE 427 -0.05 ASN 87

ARG 200 0.22 ILE 428 -0.05 ASN 87

ARG 200 0.21 TRP 429 -0.05 ASN 87

GLU 425 0.23 ARG 430 -0.06 ARG 340

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 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.

* EHB *