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 7 ---

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
GLN 123 0.07 ASP 20 -0.30 ALA 407

GLN 123 0.06 PRO 21 -0.34 ALA 407

GLY 125 0.07 GLU 22 -0.32 ALA 407

GLN 123 0.08 LEU 23 -0.30 ALA 407

GLN 123 0.08 LEU 24 -0.32 ALA 407

GLY 125 0.07 ALA 25 -0.35 ALA 407

GLY 125 0.08 SER 26 -0.31 ALA 407

GLY 125 0.10 VAL 27 -0.30 ALA 406

GLY 125 0.08 THR 28 -0.33 ALA 406

GLY 125 0.07 PRO 29 -0.36 ALA 406

GLY 125 0.06 PHE 30 -0.39 ALA 407

GLY 125 0.06 THR 31 -0.39 ALA 407

GLY 125 0.06 VAL 32 -0.38 ALA 407

GLY 125 0.05 GLU 33 -0.42 ALA 407

GLY 125 0.04 GLU 34 -0.45 ALA 407

GLY 125 0.05 VAL 35 -0.40 ALA 407

GLY 125 0.04 GLU 36 -0.41 ALA 407

ASN 199 0.05 ALA 37 -0.47 ALA 407

ASN 199 0.04 LEU 38 -0.44 ALA 407

ARG 200 0.04 TYR 39 -0.39 ALA 407

ARG 200 0.06 GLU 40 -0.41 ALA 407

ARG 200 0.06 LEU 41 -0.43 ALA 407

ARG 200 0.04 PHE 42 -0.37 ALA 407

ARG 200 0.05 LYS 43 -0.34 ALA 407

THR 201 0.06 LYS 44 -0.35 ALA 407

THR 201 0.04 LEU 45 -0.33 ALA 407

ARG 200 0.04 SER 46 -0.28 ALA 407

ARG 200 0.04 SER 47 -0.26 ALA 407

THR 201 0.04 SER 48 -0.23 ALA 407

VAL 146 0.05 ILE 49 -0.18 ALA 407

VAL 146 0.05 ILE 50 -0.19 ALA 407

VAL 146 0.04 ASP 51 -0.22 ALA 407

VAL 146 0.05 ASP 52 -0.22 ALA 407

ARG 200 0.04 GLY 53 -0.26 ALA 407

VAL 146 0.05 LEU 54 -0.25 ALA 407

HIS 141 0.05 ILE 55 -0.25 ALA 407

VAL 146 0.07 HIS 56 -0.20 ALA 407

VAL 146 0.09 LYS 57 -0.18 ALA 407

VAL 146 0.08 GLU 58 -0.17 ALA 407

VAL 146 0.05 GLU 59 -0.22 ALA 407

HIS 141 0.04 PHE 60 -0.24 ALA 407

HIS 141 0.05 GLN 61 -0.19 ALA 407

SER 185 0.03 LEU 62 -0.20 ALA 407

LEU 327 0.03 ALA 63 -0.29 ALA 407

SER 185 0.04 LEU 64 -0.28 ALA 406

SER 185 0.05 PHE 65 -0.18 ALA 407

SER 185 0.05 ARG 66 -0.17 ALA 407

LYS 418 0.08 ASN 67 -0.11 ALA 407

SER 422 0.08 ARG 68 -0.13 ALA 407

SER 422 0.13 ASN 69 -0.09 ALA 407

SER 422 0.11 ARG 70 -0.09 ALA 406

GLU 144 0.13 ARG 71 -0.11 ALA 406

HIS 141 0.13 ASN 72 -0.13 ALA 406

HIS 141 0.12 LEU 73 -0.13 ALA 406

HIS 141 0.07 PHE 74 -0.18 ALA 406

HIS 141 0.07 ALA 75 -0.20 ALA 406

HIS 141 0.10 ASP 76 -0.18 ALA 406

HIS 141 0.08 ARG 77 -0.19 ALA 406

HIS 141 0.05 ILE 78 -0.24 ALA 406

HIS 141 0.07 PHE 79 -0.23 ALA 406

VAL 146 0.08 ASP 80 -0.20 ALA 406

ARG 97 0.06 VAL 81 -0.23 ALA 406

HIS 141 0.05 PHE 82 -0.26 ALA 406

VAL 146 0.07 ASP 83 -0.23 ALA 406

ARG 122 0.08 VAL 84 -0.23 ALA 406

ARG 122 0.08 LYS 85 -0.21 ALA 406

VAL 146 0.09 ARG 86 -0.19 ALA 406

VAL 146 0.10 ASN 87 -0.18 ALA 407

VAL 146 0.10 GLY 88 -0.18 ALA 407

VAL 146 0.08 VAL 89 -0.21 ALA 407

HIS 141 0.05 ILE 90 -0.26 ALA 407

HIS 141 0.04 GLU 91 -0.27 ALA 407

GLN 123 0.04 PHE 92 -0.31 ALA 407

GLN 123 0.06 GLY 93 -0.29 ALA 407

GLN 123 0.06 GLU 94 -0.28 ALA 406

GLN 123 0.04 PHE 95 -0.32 ALA 406

GLN 123 0.06 VAL 96 -0.35 ALA 406

GLN 123 0.08 ARG 97 -0.31 ALA 406

GLN 123 0.07 SER 98 -0.32 ALA 406

GLY 125 0.05 LEU 99 -0.38 ALA 406

GLY 125 0.06 GLY 100 -0.36 ALA 406

GLY 125 0.06 VAL 101 -0.34 ALA 406

GLY 125 0.04 PHE 102 -0.40 ALA 406

GLY 125 0.05 HIS 103 -0.43 ALA 406

VAL 108 0.05 PRO 104 -0.43 ALA 406

GLY 125 0.05 SER 105 -0.40 ARG 368

GLY 125 0.06 ALA 106 -0.34 ARG 368

GLY 125 0.05 PRO 107 -0.32 ARG 368

PRO 193 0.05 VAL 108 -0.30 ARG 368

GLY 125 0.04 HIS 109 -0.26 ARG 368

GLY 125 0.07 GLU 110 -0.25 ARG 368

GLY 125 0.04 LYS 111 -0.27 ARG 368

SER 325 0.04 VAL 112 -0.23 ARG 368

GLY 125 0.05 LYS 113 -0.20 ARG 368

VAL 101 0.05 PHE 114 -0.23 ALA 406

LEU 132 0.03 ALA 115 -0.21 ALA 406

VAL 27 0.05 PHE 116 -0.17 ALA 406

VAL 27 0.06 LYS 117 -0.18 ALA 406

VAL 146 0.05 LEU 118 -0.19 ALA 406

LEU 132 0.06 TYR 119 -0.16 ALA 406

GLU 149 0.07 ASP 120 -0.14 ALA 406

LEU 147 0.09 LEU 121 -0.14 ALA 406

GLU 149 0.09 ARG 122 -0.13 ALA 406

VAL 27 0.10 GLN 123 -0.14 ALA 406

VAL 27 0.09 THR 124 -0.12 ALA 406

VAL 27 0.10 GLY 125 -0.13 ALA 406

VAL 27 0.07 PHE 126 -0.12 ALA 406

GLU 149 0.06 ILE 127 -0.12 ALA 406

GLU 149 0.08 GLU 128 -0.10 ALA 406

GLU 149 0.09 ARG 129 -0.08 ALA 406

GLU 149 0.14 GLU 130 -0.08 ALA 406

GLU 149 0.10 GLU 131 -0.10 ALA 406

LEU 147 0.07 LEU 132 -0.09 ALA 406

LEU 147 0.10 LYS 133 -0.07 ALA 406

LEU 147 0.14 GLU 134 -0.08 ALA 406

LEU 147 0.09 MET 135 -0.10 ALA 406

LEU 147 0.07 VAL 136 -0.07 ALA 406

LEU 147 0.14 VAL 137 -0.06 ALA 406

VAL 146 0.11 ALA 138 -0.08 ALA 406

SER 422 0.06 LEU 139 -0.08 ALA 406

ALA 138 0.08 LEU 140 -0.08 PRO 193

ASN 72 0.13 HIS 141 -0.06 ALA 406

ASN 72 0.12 GLU 142 -0.08 ALA 406

ARG 71 0.08 SER 143 -0.11 SER 325

ARG 71 0.13 GLU 144 -0.09 PRO 193

ILE 428 0.11 LEU 145 -0.11 PRO 193

VAL 137 0.13 VAL 146 -0.09 PRO 193

VAL 137 0.14 LEU 147 -0.09 PRO 193

GLU 130 0.11 SER 148 -0.08 PRO 193

GLU 130 0.14 GLU 149 -0.07 PRO 193

GLU 130 0.11 ASP 150 -0.07 PRO 193

GLU 130 0.11 MET 151 -0.09 PRO 193

GLU 130 0.10 ILE 152 -0.08 PRO 193

GLU 130 0.10 GLU 153 -0.06 PRO 193

SER 397 0.10 VAL 154 -0.07 PRO 193

SER 397 0.07 MET 155 -0.08 PRO 193

SER 397 0.07 VAL 156 -0.05 PRO 193

SER 397 0.08 ASP 157 -0.05 PRO 193

SER 397 0.05 LYS 158 -0.06 PRO 193

ASP 333 0.03 ALA 159 -0.06 ARG 368

SER 397 0.04 PHE 160 -0.06 ARG 368

SER 397 0.04 VAL 161 -0.05 ARG 368

ASP 333 0.03 GLN 162 -0.07 ARG 368

ASP 333 0.03 ALA 163 -0.10 ARG 368

GLU 149 0.03 ASP 164 -0.08 ARG 368

ASP 333 0.03 ARG 165 -0.09 ARG 368

GLU 149 0.03 LYS 166 -0.08 ARG 368

SER 397 0.04 ASN 167 -0.06 ARG 368

ASP 150 0.06 ASP 168 -0.06 ALA 406

ASP 150 0.07 GLY 169 -0.06 ALA 406

GLU 149 0.07 LYS 170 -0.08 ALA 406

GLU 149 0.05 ILE 171 -0.10 ARG 368

VAL 27 0.05 ASP 172 -0.12 ARG 368

GLU 110 0.05 ILE 173 -0.15 ARG 368

PRO 107 0.04 ASP 174 -0.15 ARG 368

ASP 333 0.03 GLU 175 -0.14 ARG 368

LEU 132 0.03 TRP 176 -0.16 ARG 368

ASP 333 0.04 LYS 177 -0.19 ARG 368

ASP 333 0.04 ASP 178 -0.18 ARG 368

ASP 333 0.04 PHE 179 -0.17 ARG 368

ASP 333 0.05 VAL 180 -0.22 ARG 368

ASP 333 0.05 SER 181 -0.24 ARG 368

ASP 333 0.06 LEU 182 -0.22 ASN 369

ASP 333 0.07 ASN 183 -0.28 LEU 308

ASP 333 0.07 PRO 184 -0.31 ASN 369

ASP 333 0.08 SER 185 -0.34 ASN 369

ASP 333 0.06 LEU 186 -0.26 LEU 308

ASP 333 0.06 ILE 187 -0.28 LYS 371

ASP 333 0.07 LYS 188 -0.37 LYS 371

ASP 333 0.06 ASN 189 -0.34 ALA 406

SER 325 0.05 MET 190 -0.34 ALA 406

VAL 108 0.05 THR 191 -0.42 ALA 406

VAL 108 0.05 LEU 192 -0.54 ALA 406

VAL 108 0.05 PRO 193 -0.59 ALA 406

VAL 108 0.04 TYR 194 -0.65 ALA 406

GLY 125 0.03 LEU 195 -0.54 ALA 406

GLY 125 0.04 LYS 196 -0.53 ALA 406

LEU 41 0.04 ASP 197 -0.61 ALA 407

LEU 41 0.05 ILE 198 -0.58 ALA 407

GLU 40 0.06 ASN 199 -0.54 ALA 407

GLU 40 0.06 ARG 200 -0.61 ALA 407

LYS 44 0.06 THR 201 -0.66 ALA 407

PRO 396 0.07 GLU 305 -0.26 PRO 193

PRO 396 0.07 GLY 306 -0.25 PRO 193

PRO 396 0.04 PRO 307 -0.27 PRO 193

PHE 334 0.04 LEU 308 -0.33 SER 185

LYS 336 0.05 MET 309 -0.19 SER 185

LYS 336 0.06 MET 310 -0.17 LEU 186

ASP 333 0.04 ASN 311 -0.09 PRO 193

ASP 333 0.03 ALA 312 -0.08 PRO 193

ASP 333 0.04 PHE 313 -0.11 LYS 371

ASP 333 0.05 GLU 314 -0.16 LYS 371

LYS 336 0.05 MET 315 -0.11 GLU 390

ASP 333 0.04 ILE 316 -0.12 ALA 406

ASP 333 0.06 THR 317 -0.17 GLU 390

LYS 336 0.07 LEU 318 -0.16 ARG 404

THR 317 0.06 SER 319 -0.17 ARG 404

SER 185 0.06 GLN 320 -0.23 ALA 406

SER 185 0.04 GLY 321 -0.22 ALA 406

LEU 186 0.05 LEU 322 -0.26 ALA 406

ASP 333 0.05 ASN 323 -0.38 ALA 406

ASN 189 0.03 LEU 324 -0.43 ALA 406

MET 190 0.05 SER 325 -0.59 ALA 406

ARG 331 0.05 ALA 326 -0.49 ALA 406

ALA 63 0.03 LEU 327 -0.45 ALA 407

VAL 108 0.03 PHE 328 -0.58 ALA 407

LYS 188 0.04 ASP 329 -0.62 ALA 407

PRO 193 0.04 ARG 330 -0.57 GLY 408

LYS 188 0.06 ARG 331 -0.51 GLU 409

ASP 333 0.08 GLN 332 -0.38 GLU 409

GLN 332 0.08 ASP 333 -0.13 GLU 409

SER 185 0.07 PHE 334 -0.08 LYS 44

LEU 318 0.06 VAL 335 -0.06 ALA 37

LEU 318 0.07 LYS 336 -0.13 ARG 337

ASN 69 0.10 ARG 337 -0.14 ALA 326

ASN 69 0.08 GLN 338 -0.16 SER 325

ASN 69 0.06 THR 339 -0.22 SER 325

ASN 69 0.06 ARG 340 -0.19 PRO 193

LEU 145 0.08 PHE 341 -0.18 PRO 193

VAL 137 0.09 VAL 342 -0.17 PRO 193

VAL 137 0.09 SER 343 -0.18 PRO 193

ARG 345 0.11 ARG 344 -0.17 PRO 193

ARG 344 0.11 ARG 345 -0.19 PRO 193

ASP 150 0.08 GLU 346 -0.22 PRO 193

ASP 150 0.05 PRO 347 -0.25 PRO 193

THR 367 0.06 SER 348 -0.27 PRO 193

ASP 150 0.06 GLU 349 -0.25 PRO 193

SER 148 0.06 ILE 350 -0.26 PRO 193

ILE 350 0.06 ILE 351 -0.31 PRO 193

TRP 429 0.06 ALA 352 -0.30 PRO 193

TRP 429 0.07 ASN 353 -0.27 PRO 193

TRP 429 0.06 ILE 354 -0.31 TYR 194

TRP 429 0.05 GLU 355 -0.34 TYR 194

TRP 429 0.06 ALA 356 -0.31 ASP 197

ARG 430 0.07 VAL 357 -0.30 ASP 197

TRP 429 0.05 ALA 358 -0.35 ASP 197

TRP 429 0.05 ASN 359 -0.36 ARG 200

ARG 430 0.06 SER 360 -0.33 ARG 200

SER 379 0.06 MET 361 -0.35 ARG 200

SER 379 0.06 GLY 362 -0.40 ARG 200

TRP 429 0.04 PHE 363 -0.43 ARG 200

TRP 429 0.04 LYS 364 -0.46 ASP 197

ALA 352 0.04 SER 365 -0.45 ASP 197

ALA 352 0.05 HIS 366 -0.47 TYR 194

SER 348 0.06 THR 367 -0.45 PRO 193

SER 348 0.06 ARG 368 -0.46 PRO 193

SER 348 0.03 ASN 369 -0.41 PRO 193

PRO 396 0.04 PHE 370 -0.37 PRO 193

SER 348 0.04 LYS 371 -0.46 PRO 193

SER 348 0.04 THR 372 -0.46 PRO 193

SER 348 0.04 ARG 373 -0.52 PRO 193

ALA 352 0.03 LEU 374 -0.48 TYR 194

ILE 427 0.03 GLU 375 -0.52 ASP 197

TRP 429 0.03 GLY 376 -0.49 ARG 200

GLY 362 0.03 LEU 377 -0.49 ARG 200

MET 361 0.06 SER 378 -0.48 ARG 200

MET 361 0.06 SER 379 -0.53 ARG 200

LYS 419 0.05 ILE 380 -0.51 ARG 200

LYS 419 0.03 LYS 381 -0.57 ARG 200

LYS 415 0.03 ALA 382 -0.49 THR 201

PHE 416 0.05 GLY 383 -0.47 THR 201

LYS 419 0.02 GLN 384 -0.56 ARG 200

PHE 416 0.02 LEU 385 -0.52 THR 201

SER 348 0.02 ALA 386 -0.55 TYR 194

SER 348 0.02 VAL 387 -0.50 TYR 194

SER 348 0.03 VAL 388 -0.51 PRO 193

LYS 405 0.02 ILE 389 -0.42 PRO 193

PHE 334 0.03 GLU 390 -0.39 PRO 193

ARG 340 0.03 ILE 391 -0.30 PRO 193

PHE 334 0.04 TYR 392 -0.25 LYS 188

VAL 137 0.04 GLU 393 -0.18 PRO 193

ALA 138 0.04 VAL 394 -0.14 PRO 193

ASP 157 0.06 ALA 395 -0.12 PRO 193

GLY 306 0.07 PRO 396 -0.13 PRO 193

VAL 154 0.10 SER 397 -0.14 PRO 193

VAL 154 0.08 LEU 398 -0.15 PRO 193

VAL 137 0.06 PHE 399 -0.19 PRO 193

VAL 137 0.05 MET 400 -0.20 PRO 193

ASN 69 0.04 VAL 401 -0.26 PRO 193

ARG 340 0.05 ASP 402 -0.29 PRO 193

PRO 307 0.02 VAL 403 -0.33 PRO 193

THR 410 0.04 ARG 404 -0.45 SER 325

LEU 411 0.03 LYS 405 -0.51 SER 325

ASN 369 0.03 ALA 406 -0.65 TYR 194

ASN 369 0.03 ALA 407 -0.66 THR 201

ASN 369 0.02 GLY 408 -0.59 THR 201

LEU 411 0.03 GLU 409 -0.51 ARG 331

ARG 404 0.04 THR 410 -0.40 ASP 329

ASN 69 0.05 LEU 411 -0.28 ARG 331

ASN 69 0.05 GLU 412 -0.34 THR 201

ASN 69 0.03 TYR 413 -0.35 ASP 329

ASN 69 0.08 HIS 414 -0.25 THR 201

ASN 69 0.10 LYS 415 -0.26 THR 201

ASN 69 0.07 PHE 416 -0.30 THR 201

ASN 69 0.08 TYR 417 -0.26 THR 201

ASN 69 0.13 LYS 418 -0.21 THR 201

ASN 69 0.11 LYS 419 -0.24 ARG 200

ASN 69 0.09 LEU 420 -0.26 ARG 200

ASN 69 0.11 CYS 421 -0.21 TYR 194

ASN 69 0.13 SER 422 -0.20 ARG 200

ASN 69 0.10 LYS 423 -0.23 ARG 200

ASN 69 0.09 LEU 424 -0.22 TYR 194

ARG 430 0.11 GLU 425 -0.18 TYR 194

ARG 430 0.11 ASN 426 -0.18 TYR 194

TRP 429 0.10 ILE 427 -0.19 PRO 193

TRP 429 0.11 ILE 428 -0.17 PRO 193

ILE 428 0.11 TRP 429 -0.15 PRO 193

GLU 425 0.11 ARG 430 -0.12 PRO 193

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 7 ---

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 *