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

* open_cutoff10 *

CA distance fluctuations for 2604261322202455018

--- normal mode 16 ---

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 32 0.19 ALA 1 -0.16 THR 103

ALA 32 0.19 SER 2 -0.12 THR 103

ALA 32 0.21 SER 3 -0.08 SER 424

ALA 32 0.22 THR 4 -0.08 SER 424

ALA 32 0.22 ASN 5 -0.09 SER 424

ALA 32 0.25 LEU 6 -0.10 SER 424

ALA 32 0.24 LYS 7 -0.10 SER 424

ALA 32 0.22 ASP 8 -0.09 SER 424

ALA 32 0.24 VAL 9 -0.09 SER 424

ALA 32 0.26 LEU 10 -0.10 SER 424

ALA 32 0.23 ALA 11 -0.10 SER 424

ALA 32 0.25 LEU 13 -0.10 ALA 321

ALA 32 0.26 ILE 14 -0.11 SER 424

ALA 32 0.21 PRO 15 -0.17 PRO 422

ALA 32 0.20 LYS 16 -0.16 PRO 422

ALA 32 0.26 GLU 17 -0.16 PRO 422

ALA 32 0.27 GLN 18 -0.23 PRO 422

ALA 32 0.17 ALA 19 -0.29 PRO 422

ALA 32 0.19 ARG 20 -0.25 PRO 422

ALA 32 0.29 ILE 21 -0.30 PRO 422

ALA 32 0.14 LYS 22 -0.47 PRO 422

GLN 100 0.14 THR 23 -0.41 PRO 422

ALA 32 0.15 PHE 24 -0.36 PRO 422

LYS 22 0.13 ARG 25 -0.53 PRO 422

THR 23 0.10 GLN 26 -0.68 PRO 422

GLY 68 0.16 GLN 27 -0.50 PRO 422

LYS 423 0.23 HIS 28 -0.33 PRO 422

LYS 423 0.12 GLY 29 -0.61 GLY 34

LYS 423 0.45 THR 31 -0.19 GLN 35

GLY 50 0.75 ALA 32 -0.07 THR 427

LYS 423 0.67 GLY 34 -0.61 GLY 29

LYS 423 0.79 GLN 35 -0.46 GLY 29

LYS 423 0.90 ILE 36 -0.40 GLY 29

LYS 423 0.73 THR 37 -0.34 GLY 29

LYS 423 0.60 VAL 38 -0.29 GLY 29

LYS 423 0.55 ASP 39 -0.27 GLY 29

LYS 423 0.70 MET 40 -0.29 GLY 29

LYS 423 0.71 SER 41 -0.27 GLN 26

PRO 422 0.52 TYR 42 -0.24 GLN 26

PRO 422 0.54 GLY 43 -0.24 GLY 29

PRO 422 0.74 GLY 44 -0.24 GLY 312

LYS 423 0.72 MET 45 -0.27 GLY 29

LYS 423 0.59 ARG 46 -0.29 GLY 29

LYS 423 0.60 GLY 47 -0.34 GLY 29

LYS 423 0.75 MET 48 -0.38 GLY 29

ALA 32 0.65 LYS 49 -0.44 GLY 29

ALA 32 0.75 GLY 50 -0.37 ARG 25

ALA 32 0.65 LEU 51 -0.36 ARG 25

ALA 32 0.54 TYR 53 -0.22 ARG 25

ALA 32 0.50 GLU 54 -0.15 GLU 17

ALA 32 0.43 THR 55 -0.10 ARG 25

ALA 32 0.44 SER 56 -0.12 ARG 25

ALA 32 0.45 VAL 57 -0.15 ARG 25

ALA 32 0.39 LEU 58 -0.16 ARG 25

LYS 423 0.39 ASP 59 -0.13 ARG 25

LYS 423 0.40 PRO 60 -0.14 ARG 25

LYS 423 0.36 ASP 61 -0.09 ARG 25

LYS 423 0.32 GLU 62 -0.08 ARG 25

LYS 423 0.32 GLY 63 -0.11 ARG 25

ALA 32 0.34 ILE 64 -0.11 ARG 25

ALA 32 0.37 ARG 65 -0.09 ALA 321

ALA 32 0.37 PHE 66 -0.08 ALA 321

ALA 32 0.39 ARG 67 -0.08 ALA 321

ALA 32 0.37 GLY 68 -0.08 LEU 13

ALA 32 0.33 PHE 69 -0.07 ALA 1

ALA 32 0.32 SER 70 -0.06 ALA 1

ALA 32 0.29 ILE 71 -0.06 ALA 1

ALA 32 0.26 PRO 72 -0.08 ALA 1

ALA 32 0.27 GLU 73 -0.08 ALA 1

ALA 32 0.28 CYS 74 -0.08 ALA 1

ALA 32 0.26 GLN 75 -0.09 ALA 1

ALA 32 0.24 LYS 76 -0.11 ALA 1

ALA 32 0.26 LEU 77 -0.11 ALA 1

ALA 32 0.27 LEU 78 -0.11 ALA 1

ALA 32 0.24 PRO 79 -0.14 ALA 1

ALA 32 0.23 LYS 80 -0.13 ALA 1

ALA 32 0.21 GLY 82 -0.16 ALA 1

ALA 32 0.20 GLY 84 -0.11 ALA 1

ALA 32 0.22 GLU 86 -0.09 ALA 1

ALA 32 0.24 PRO 87 -0.09 ALA 1

ALA 32 0.25 LEU 88 -0.08 SER 424

ALA 32 0.27 PRO 89 -0.09 SER 424

ALA 32 0.27 GLU 90 -0.09 SER 424

ALA 32 0.27 GLY 91 -0.08 SER 424

ALA 32 0.30 LEU 92 -0.08 SER 424

ALA 32 0.30 PHE 93 -0.10 SER 424

ALA 32 0.30 TRP 94 -0.09 SER 424

ALA 32 0.32 LEU 95 -0.08 SER 424

ALA 32 0.35 LEU 96 -0.09 SER 424

ALA 32 0.34 VAL 97 -0.10 SER 424

ALA 32 0.33 THR 98 -0.08 SER 424

ALA 32 0.35 GLY 99 -0.07 ALA 321

ALA 32 0.31 GLN 100 -0.07 SER 2

ALA 32 0.28 ILE 101 -0.08 ALA 1

ALA 32 0.27 PRO 102 -0.09 ALA 1

ALA 32 0.24 THR 103 -0.16 ALA 1

ALA 32 0.24 GLN 106 -0.09 ALA 1

ALA 32 0.24 VAL 107 -0.10 ALA 1

ALA 32 0.22 SER 108 -0.14 ALA 1

ALA 32 0.22 TRP 109 -0.09 SER 424

ALA 32 0.23 SER 111 -0.09 SER 424

ALA 32 0.22 LYS 112 -0.08 SER 424

ALA 32 0.24 GLU 113 -0.09 SER 424

ALA 32 0.24 TRP 114 -0.10 SER 424

ALA 32 0.22 ALA 115 -0.09 SER 424

ALA 32 0.22 LYS 116 -0.09 SER 424

ALA 32 0.23 ARG 117 -0.10 SER 424

ALA 32 0.22 ALA 118 -0.11 SER 424

ALA 32 0.21 ALA 119 -0.11 SER 424

ALA 32 0.20 LEU 120 -0.11 SER 424

ALA 32 0.19 PRO 121 -0.11 SER 424

ALA 32 0.18 SER 122 -0.11 LYS 423

ALA 32 0.18 HIS 123 -0.14 LYS 423

ALA 32 0.19 VAL 124 -0.12 SER 424

ALA 32 0.18 VAL 125 -0.11 SER 424

ALA 32 0.17 THR 126 -0.11 LYS 423

ALA 32 0.17 MET 127 -0.12 LYS 423

ALA 32 0.18 LEU 128 -0.12 SER 424

ALA 32 0.17 ASP 129 -0.11 SER 424

PRO 422 0.16 ASN 130 -0.11 SER 424

PRO 422 0.19 PHE 131 -0.12 SER 424

PRO 422 0.19 PRO 132 -0.11 SER 424

PRO 422 0.20 THR 133 -0.11 SER 424

PRO 422 0.22 ASN 134 -0.11 SER 424

PRO 422 0.23 LEU 135 -0.13 SER 424

PRO 422 0.25 HIS 136 -0.13 SER 424

PRO 422 0.25 PRO 137 -0.13 SER 424

PRO 422 0.28 MET 138 -0.15 SER 424

PRO 422 0.27 SER 139 -0.15 SER 424

PRO 422 0.23 GLN 140 -0.14 SER 424

PRO 422 0.24 LEU 141 -0.14 SER 424

PRO 422 0.26 SER 142 -0.16 SER 424

PRO 422 0.22 ALA 143 -0.16 SER 424

ALA 32 0.21 ALA 144 -0.14 SER 424

ALA 32 0.23 ILE 145 -0.15 SER 424

ALA 32 0.22 THR 146 -0.16 SER 424

ALA 32 0.20 ALA 147 -0.16 LYS 423

ALA 32 0.22 LEU 148 -0.14 SER 424

ALA 32 0.23 ASN 149 -0.15 LYS 423

ALA 32 0.21 SER 150 -0.18 LYS 423

ALA 32 0.22 GLU 151 -0.14 LYS 423

ALA 32 0.23 SER 152 -0.14 LYS 423

ALA 32 0.23 ASN 153 -0.13 LYS 423

ALA 32 0.25 PHE 154 -0.15 LYS 423

ALA 32 0.23 ALA 155 -0.20 LYS 423

ALA 32 0.21 ARG 156 -0.20 LYS 423

ALA 32 0.22 ALA 157 -0.18 LYS 423

ALA 32 0.22 TYR 158 -0.23 LYS 423

ALA 32 0.20 ALA 159 -0.25 LYS 423

ALA 32 0.19 GLU 160 -0.22 LYS 423

ALA 32 0.20 GLY 161 -0.22 LYS 423

ALA 32 0.22 ILE 162 -0.17 LYS 423

ALA 32 0.26 ARG 164 -0.17 PRO 422

ALA 32 0.26 THR 165 -0.15 PRO 422

ALA 32 0.25 LYS 166 -0.10 PRO 422

ALA 32 0.28 TYR 167 -0.13 GLN 26

ALA 32 0.30 TRP 168 -0.11 SER 424

ALA 32 0.27 GLU 169 -0.10 SER 424

ALA 32 0.29 VAL 171 -0.13 SER 424

ALA 32 0.29 TYR 172 -0.11 SER 424

ALA 32 0.26 GLU 173 -0.11 SER 424

ALA 32 0.28 ALA 175 -0.13 SER 424

ALA 32 0.27 MET 176 -0.11 SER 424

ALA 32 0.24 ASP 177 -0.12 SER 424

ALA 32 0.26 LEU 178 -0.13 SER 424

ALA 32 0.26 ILE 179 -0.12 SER 424

ALA 32 0.24 ALA 180 -0.11 SER 424

ALA 32 0.23 LYS 181 -0.12 SER 424

ALA 32 0.24 LEU 182 -0.12 SER 424

ALA 32 0.23 PRO 183 -0.11 SER 424

ALA 32 0.21 CYS 184 -0.11 SER 424

ALA 32 0.21 VAL 185 -0.12 SER 424

ALA 32 0.21 ALA 186 -0.12 SER 424

ALA 32 0.20 ALA 187 -0.11 SER 424

ALA 32 0.19 LYS 188 -0.11 SER 424

PRO 422 0.20 ILE 189 -0.12 SER 424

PRO 422 0.20 TYR 190 -0.11 SER 424

PRO 422 0.18 ARG 191 -0.10 SER 424

PRO 422 0.18 ASN 192 -0.10 SER 424

PRO 422 0.20 LEU 193 -0.11 SER 424

PRO 422 0.19 TYR 194 -0.10 SER 424

PRO 422 0.17 ARG 195 -0.09 SER 424

PRO 422 0.17 ALA 196 -0.09 SER 424

PRO 422 0.16 GLY 197 -0.10 SER 424

ALA 32 0.16 SER 198 -0.09 SER 424

ALA 32 0.17 SER 199 -0.09 SER 424

ALA 32 0.18 ILE 200 -0.10 SER 424

ALA 32 0.18 GLY 201 -0.09 SER 424

ALA 32 0.19 ALA 202 -0.09 SER 424

ALA 32 0.20 ILE 203 -0.09 SER 424

ALA 32 0.19 ASP 204 -0.08 SER 424

ALA 32 0.20 SER 205 -0.08 SER 424

ALA 32 0.19 LYS 206 -0.08 SER 424

ALA 32 0.20 LEU 207 -0.08 SER 424

ALA 32 0.22 ASP 208 -0.08 SER 424

ALA 32 0.23 TRP 209 -0.09 SER 424

ALA 32 0.23 SER 210 -0.09 SER 424

ALA 32 0.21 HIS 211 -0.08 SER 424

ALA 32 0.21 ASN 212 -0.09 SER 424

ALA 32 0.21 PHE 213 -0.10 SER 424

ALA 32 0.20 THR 214 -0.09 SER 424

ALA 32 0.19 ASN 215 -0.09 SER 424

ALA 32 0.19 MET 216 -0.09 SER 424

ALA 32 0.19 LEU 217 -0.10 SER 424

ALA 32 0.18 GLY 218 -0.09 SER 424

ALA 32 0.18 TYR 219 -0.09 SER 424

ALA 32 0.18 THR 220 -0.08 SER 424

ALA 32 0.17 ASP 221 -0.08 SER 424

ALA 32 0.18 GLN 223 -0.07 SER 424

ALA 32 0.19 PHE 224 -0.08 SER 424

ALA 32 0.20 THR 225 -0.08 SER 424

ALA 32 0.21 GLU 226 -0.08 SER 424

ALA 32 0.21 LEU 227 -0.08 SER 424

ALA 32 0.22 MET 228 -0.09 SER 424

ALA 32 0.23 ARG 229 -0.08 SER 424

ALA 32 0.24 LEU 230 -0.08 SER 424

ALA 32 0.24 TYR 231 -0.09 SER 424

ALA 32 0.26 LEU 232 -0.10 SER 424

ALA 32 0.28 THR 233 -0.09 SER 424

ALA 32 0.28 ILE 234 -0.08 SER 424

ALA 32 0.28 HIS 235 -0.10 SER 424

ALA 32 0.31 SER 236 -0.11 SER 424

ALA 32 0.35 ASP 237 -0.12 ARG 25

ALA 32 0.36 HIS 238 -0.15 ARG 25

ALA 32 0.43 GLU 239 -0.19 ARG 25

ALA 32 0.45 GLY 240 -0.22 ARG 25

PRO 422 0.47 GLY 241 -0.24 ARG 25

PRO 422 0.47 ASN 242 -0.20 ARG 25

PRO 422 0.52 VAL 243 -0.20 GLN 26

PRO 422 0.41 SER 244 -0.18 SER 424

PRO 422 0.38 ALA 245 -0.19 GLN 26

PRO 422 0.50 HIS 246 -0.24 GLN 26

PRO 422 0.47 THR 247 -0.24 SER 424

ALA 32 0.33 SER 248 -0.21 GLN 26

ALA 32 0.38 HIS 249 -0.25 GLN 26

PRO 422 0.38 LEU 250 -0.28 GLN 26

ALA 32 0.30 VAL 251 -0.25 SER 424

ALA 32 0.33 GLY 252 -0.23 GLN 26

ALA 32 0.36 SER 253 -0.28 GLN 26

ALA 32 0.30 ALA 254 -0.28 LYS 423

ALA 32 0.30 LEU 255 -0.22 GLN 26

ALA 32 0.28 SER 256 -0.21 LYS 423

ALA 32 0.27 ASP 257 -0.16 GLN 26

ALA 32 0.29 PRO 258 -0.16 SER 424

ALA 32 0.26 TYR 259 -0.16 SER 424

ALA 32 0.26 LEU 260 -0.18 SER 424

ALA 32 0.29 SER 261 -0.20 SER 424

ALA 32 0.28 PHE 262 -0.18 SER 424

PRO 422 0.27 ALA 263 -0.18 SER 424

PRO 422 0.34 ALA 264 -0.21 SER 424

PRO 422 0.36 ALA 265 -0.20 SER 424

PRO 422 0.34 MET 266 -0.18 SER 424

PRO 422 0.37 ASN 267 -0.20 SER 424

PRO 422 0.44 GLY 268 -0.21 SER 424

PRO 422 0.39 LEU 269 -0.17 SER 424

PRO 422 0.36 ALA 270 -0.17 SER 424

PRO 422 0.41 GLY 271 -0.18 ARG 313

PRO 422 0.38 PRO 272 -0.21 ARG 313

PRO 422 0.42 LEU 273 -0.25 ARG 313

PRO 422 0.41 HIS 274 -0.19 ARG 313

PRO 422 0.35 GLY 275 -0.15 ARG 313

PRO 422 0.32 LEU 276 -0.14 ARG 313

PRO 422 0.30 ALA 277 -0.14 ARG 25

PRO 422 0.27 ASN 278 -0.12 ARG 25

PRO 422 0.26 GLN 279 -0.12 ARG 25

PRO 422 0.26 GLU 280 -0.15 TYR 304

PRO 422 0.24 VAL 281 -0.13 ILE 305

PRO 422 0.23 LEU 282 -0.11 GLY 29

PRO 422 0.21 TRP 284 -0.18 TYR 304

PRO 422 0.20 LEU 285 -0.13 LEU 301

PRO 422 0.18 GLN 287 -0.12 GLY 29

PRO 422 0.19 LEU 288 -0.11 LEU 301

PRO 422 0.17 GLN 289 -0.10 GLY 29

PRO 422 0.16 LYS 290 -0.10 GLY 29

PRO 422 0.13 ASP 298 -0.10 TRP 284

PRO 422 0.13 LEU 301 -0.15 TRP 284

PRO 422 0.12 ARG 302 -0.14 TRP 284

PRO 422 0.10 ASP 303 -0.15 TRP 284

PRO 422 0.11 TYR 304 -0.18 TRP 284

PRO 422 0.12 ILE 305 -0.16 GLY 29

PRO 422 0.11 TRP 306 -0.16 GLY 29

PRO 422 0.10 ASN 307 -0.17 GLY 29

LEU 288 0.13 THR 308 -0.20 LEU 273

PRO 422 0.11 LEU 309 -0.20 GLY 29

PRO 422 0.09 ASN 310 -0.20 GLY 29

LEU 288 0.11 SER 311 -0.21 GLY 44

LEU 288 0.13 GLY 312 -0.24 GLY 44

LEU 288 0.19 ARG 313 -0.25 LEU 273

LEU 288 0.17 VAL 314 -0.23 LEU 273

PRO 422 0.17 VAL 315 -0.21 PRO 316

PRO 422 0.23 PRO 316 -0.21 VAL 315

PRO 422 0.23 GLY 317 -0.16 GLY 29

PRO 422 0.21 TYR 318 -0.16 GLY 29

LYS 423 0.25 GLY 319 -0.19 GLY 29

LYS 423 0.30 HIS 320 -0.20 GLY 29

LYS 423 0.35 ALA 321 -0.24 GLY 29

LYS 423 0.41 VAL 322 -0.20 GLY 29

LYS 423 0.35 LEU 323 -0.16 ARG 25

LYS 423 0.35 ARG 324 -0.13 ARG 25

LYS 423 0.30 LYS 325 -0.10 GLY 29

LYS 423 0.27 THR 326 -0.10 ARG 25

LYS 423 0.27 ASP 327 -0.11 ARG 25

ALA 32 0.25 PRO 328 -0.08 ARG 25

ALA 32 0.25 ARG 329 -0.09 ARG 25

PRO 422 0.22 TYR 330 -0.09 ARG 25

ALA 32 0.21 THR 331 -0.07 ARG 25

ALA 32 0.23 CYS 332 -0.06 ARG 25

ALA 32 0.21 GLN 333 -0.07 SER 424

ALA 32 0.19 ARG 334 -0.06 GLY 29

ALA 32 0.20 GLU 335 -0.05 SER 424

ALA 32 0.20 PHE 336 -0.06 SER 424

ALA 32 0.18 ALA 337 -0.06 SER 424

ALA 32 0.17 LEU 338 -0.06 SER 424

ALA 32 0.18 LYS 339 -0.05 SER 424

ALA 32 0.18 HIS 340 -0.06 SER 424

PRO 422 0.17 LEU 341 -0.06 SER 424

PRO 422 0.16 PRO 342 -0.06 SER 424

PRO 422 0.17 ASP 344 -0.07 SER 424

PRO 422 0.16 PRO 345 -0.07 SER 424

PRO 422 0.18 MET 346 -0.08 GLY 29

PRO 422 0.18 PHE 347 -0.08 GLY 29

PRO 422 0.17 LYS 348 -0.08 GLY 29

PRO 422 0.18 LEU 349 -0.09 GLY 29

PRO 422 0.19 VAL 350 -0.10 GLY 29

PRO 422 0.18 ALA 351 -0.08 GLY 29

PRO 422 0.17 GLN 352 -0.09 GLY 29

PRO 422 0.17 LEU 353 -0.11 GLY 29

LYS 423 0.19 TYR 354 -0.09 GLY 29

LYS 423 0.18 LYS 355 -0.08 GLY 29

LYS 423 0.16 ILE 356 -0.11 GLY 29

LYS 423 0.17 VAL 357 -0.13 GLY 29

LYS 423 0.21 PRO 358 -0.13 GLY 29

LYS 423 0.20 ASN 359 -0.12 GLY 29

LYS 423 0.17 VAL 360 -0.14 GLY 29

LYS 423 0.19 LEU 361 -0.17 GLY 29

LYS 423 0.22 LEU 362 -0.15 GLY 29

LYS 423 0.19 GLU 363 -0.15 GLY 29

LYS 423 0.17 GLN 364 -0.18 GLY 29

LYS 423 0.20 GLY 365 -0.20 GLY 29

LYS 423 0.25 ALA 367 -0.19 GLY 29

LYS 423 0.30 ASN 369 -0.16 GLY 29

LYS 423 0.25 PRO 370 -0.15 GLY 29

LYS 423 0.25 TRP 371 -0.13 GLY 29

LYS 423 0.23 PRO 372 -0.13 GLY 29

PRO 422 0.25 ASN 373 -0.13 ARG 25

PRO 422 0.25 VAL 374 -0.11 ARG 25

PRO 422 0.26 ASP 375 -0.12 ARG 25

PRO 422 0.23 ALA 376 -0.12 GLY 29

PRO 422 0.22 HIS 377 -0.09 ARG 25

PRO 422 0.23 SER 378 -0.09 ARG 25

PRO 422 0.23 GLY 379 -0.09 ARG 25

PRO 422 0.21 VAL 380 -0.08 SER 424

PRO 422 0.20 LEU 381 -0.08 SER 424

PRO 422 0.21 LEU 382 -0.09 SER 424

PRO 422 0.20 GLN 383 -0.09 SER 424

PRO 422 0.19 TYR 384 -0.08 SER 424

PRO 422 0.18 TYR 385 -0.08 SER 424

PRO 422 0.19 GLY 386 -0.08 SER 424

PRO 422 0.20 MET 387 -0.09 SER 424

PRO 422 0.21 THR 388 -0.09 SER 424

PRO 422 0.22 GLU 389 -0.10 SER 424

PRO 422 0.24 MET 390 -0.10 SER 424

PRO 422 0.26 ASN 391 -0.12 SER 424

PRO 422 0.25 TYR 392 -0.12 SER 424

PRO 422 0.26 TYR 393 -0.11 SER 424

PRO 422 0.29 THR 394 -0.13 SER 424

PRO 422 0.26 VAL 395 -0.13 SER 424

PRO 422 0.24 LEU 396 -0.12 SER 424

PRO 422 0.27 PHE 397 -0.12 SER 424

PRO 422 0.28 GLY 398 -0.14 SER 424

ALA 32 0.26 VAL 399 -0.13 SER 424

ALA 32 0.27 SER 400 -0.12 SER 424

ALA 32 0.30 ARG 401 -0.13 SER 424

ALA 32 0.30 ALA 402 -0.13 SER 424

ALA 32 0.31 LEU 403 -0.12 SER 424

ALA 32 0.35 GLY 404 -0.12 SER 424

ALA 32 0.35 VAL 405 -0.15 SER 424

ALA 32 0.33 LEU 406 -0.14 SER 424

ALA 32 0.35 ALA 407 -0.12 SER 424

ALA 32 0.40 GLN 408 -0.13 GLN 26

ALA 32 0.37 LEU 409 -0.16 GLN 26

ALA 32 0.35 ILE 410 -0.13 SER 424

ALA 32 0.39 TRP 411 -0.12 SER 424

ALA 32 0.42 SER 412 -0.21 GLN 26

ALA 32 0.36 ARG 413 -0.18 GLN 26

ALA 32 0.35 ALA 414 -0.12 GLN 26

ALA 32 0.39 LEU 415 -0.16 GLN 26

ALA 32 0.37 GLY 416 -0.24 GLN 26

ALA 32 0.42 PHE 417 -0.36 GLN 26

ALA 32 0.40 PRO 418 -0.39 GLN 26

ALA 32 0.40 LEU 419 -0.34 GLN 26

ALA 32 0.40 GLU 420 -0.36 GLN 26

ALA 32 0.46 ARG 421 -0.35 GLN 26

GLY 44 0.74 PRO 422 -0.68 GLN 26

ILE 36 0.90 LYS 423 -0.28 ALA 254

ALA 32 0.20 SER 424 -0.32 GLN 26

ALA 32 0.05 MET 425 -0.36 GLN 26

TYR 42 0.09 SER 426 -0.34 GLN 26

LEU 273 0.13 THR 427 -0.34 GLN 26

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.

*** open_cutoff10 ***

CA distance fluctuations for 2604261322202455018

--- normal mode 16 ---

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

* open_cutoff10 *