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 13 ---

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 0.14 ALA 1 -0.11 GLU 160

ALA 32 0.16 SER 2 -0.09 SER 424

ALA 32 0.16 SER 3 -0.09 SER 424

ALA 32 0.18 THR 4 -0.10 SER 424

ALA 32 0.16 ASN 5 -0.09 SER 424

ALA 32 0.18 LEU 6 -0.11 SER 424

ALA 32 0.16 LYS 7 -0.10 SER 424

ALA 32 0.16 ASP 8 -0.09 SER 424

ALA 32 0.19 VAL 9 -0.10 SER 424

ALA 32 0.19 LEU 10 -0.11 SER 424

ALA 32 0.15 ALA 11 -0.10 SER 424

ALA 32 0.21 LEU 13 -0.10 SER 424

ALA 32 0.18 ILE 14 -0.10 SER 424

ALA 32 0.14 PRO 15 -0.14 PRO 422

ALA 32 0.20 LYS 16 -0.12 GLY 99

ALA 32 0.25 GLU 17 -0.15 GLY 99

ALA 32 0.15 GLN 18 -0.17 PRO 422

THR 165 0.18 ALA 19 -0.18 PRO 422

ALA 32 0.22 ARG 20 -0.25 ARG 67

ALA 32 0.21 ILE 21 -0.20 GLU 54

LYS 423 0.20 LYS 22 -0.21 PRO 422

LYS 423 0.22 THR 23 -0.25 GLY 68

LYS 423 0.24 PHE 24 -0.24 GLY 68

LYS 423 0.31 ARG 25 -0.25 PRO 422

LYS 423 0.30 GLN 26 -0.20 PRO 422

LYS 423 0.32 GLN 27 -0.23 GLY 68

LYS 423 0.30 HIS 28 -0.36 GLY 34

LYS 423 0.37 GLY 29 -0.30 PRO 422

LYS 423 0.38 THR 31 -0.31 PRO 422

ASP 59 0.46 ALA 32 -0.41 MET 425

LYS 423 0.70 GLY 34 -0.36 HIS 28

LYS 423 1.00 GLN 35 -0.23 MET 425

LYS 423 1.21 ILE 36 -0.28 MET 425

LYS 423 1.04 THR 37 -0.11 HIS 28

LYS 423 0.87 VAL 38 -0.14 ALA 32

LYS 423 0.77 ASP 39 -0.11 HIS 28

LYS 423 0.90 MET 40 -0.12 HIS 28

LYS 423 0.89 SER 41 -0.15 THR 427

PRO 422 0.75 TYR 42 -0.09 HIS 28

PRO 422 0.75 GLY 43 -0.12 HIS 28

PRO 422 0.94 GLY 44 -0.30 SER 424

PRO 422 0.87 MET 45 -0.36 SER 424

LYS 423 0.66 ARG 46 -0.24 SER 424

LYS 423 0.65 GLY 47 -0.26 HIS 28

LYS 423 0.78 MET 48 -0.34 MET 425

LYS 423 0.60 LYS 49 -0.37 SER 424

LYS 423 0.56 GLY 50 -0.42 SER 424

LYS 423 0.39 LEU 51 -0.34 SER 424

ALA 32 0.33 TYR 53 -0.25 SER 424

ALA 32 0.35 GLU 54 -0.24 ARG 20

ALA 32 0.33 THR 55 -0.21 ARG 20

ALA 32 0.37 SER 56 -0.21 SER 424

ALA 32 0.44 VAL 57 -0.22 PHE 24

ALA 32 0.44 LEU 58 -0.21 SER 424

ALA 32 0.46 ASP 59 -0.20 PHE 24

ALA 32 0.45 PRO 60 -0.18 HIS 28

ALA 32 0.40 ASP 61 -0.20 GLN 27

ALA 32 0.38 GLU 62 -0.19 GLN 27

ALA 32 0.37 GLY 63 -0.17 SER 424

ALA 32 0.37 ILE 64 -0.19 SER 424

ALA 32 0.38 ARG 65 -0.20 PHE 24

ALA 32 0.34 PHE 66 -0.20 ARG 20

ALA 32 0.37 ARG 67 -0.25 ARG 20

ALA 32 0.39 GLY 68 -0.25 THR 23

ALA 32 0.34 PHE 69 -0.21 THR 23

ALA 32 0.34 SER 70 -0.19 THR 23

ALA 32 0.31 ILE 71 -0.16 THR 23

ALA 32 0.29 PRO 72 -0.16 THR 23

ALA 32 0.30 GLU 73 -0.18 THR 23

ALA 32 0.28 CYS 74 -0.16 ARG 20

ALA 32 0.26 GLN 75 -0.14 THR 23

ALA 32 0.25 LYS 76 -0.15 THR 23

ALA 32 0.26 LEU 77 -0.15 THR 23

ALA 32 0.25 LEU 78 -0.14 ARG 20

ALA 32 0.22 PRO 79 -0.12 SER 424

ALA 32 0.21 LYS 80 -0.12 SER 424

ALA 32 0.18 GLY 82 -0.11 SER 424

ALA 32 0.19 GLY 84 -0.11 LYS 339

ALA 32 0.22 GLU 86 -0.13 SER 424

ALA 32 0.23 PRO 87 -0.13 SER 424

ALA 32 0.21 LEU 88 -0.13 SER 424

ALA 32 0.21 PRO 89 -0.15 SER 424

ALA 32 0.20 GLU 90 -0.14 SER 424

ALA 32 0.22 GLY 91 -0.14 SER 424

ALA 32 0.24 LEU 92 -0.15 SER 424

ALA 32 0.22 PHE 93 -0.15 SER 424

ALA 32 0.23 TRP 94 -0.14 SER 424

ALA 32 0.26 LEU 95 -0.17 ARG 20

ALA 32 0.27 LEU 96 -0.18 ARG 20

ALA 32 0.24 VAL 97 -0.16 ARG 20

ALA 32 0.25 THR 98 -0.18 ARG 20

ALA 32 0.29 GLY 99 -0.23 ARG 20

ALA 32 0.27 GLN 100 -0.19 ARG 20

ALA 32 0.26 ILE 101 -0.16 ARG 20

ALA 32 0.23 PRO 102 -0.13 ARG 20

ALA 32 0.21 THR 103 -0.11 THR 23

ALA 32 0.19 GLN 106 -0.11 SER 424

ALA 32 0.19 VAL 107 -0.12 SER 424

ALA 32 0.17 SER 108 -0.11 SER 424

ALA 32 0.17 TRP 109 -0.11 SER 424

ALA 32 0.17 SER 111 -0.11 SER 424

ALA 32 0.15 LYS 112 -0.10 SER 424

ALA 32 0.15 GLU 113 -0.10 SER 424

ALA 32 0.15 TRP 114 -0.11 SER 424

ALA 32 0.14 ALA 115 -0.10 SER 424

ALA 32 0.12 LYS 116 -0.10 SER 424

ALA 32 0.12 ARG 117 -0.10 SER 424

ALA 32 0.12 ALA 118 -0.11 SER 424

PRO 422 0.10 ALA 119 -0.10 SER 424

PRO 422 0.13 LEU 120 -0.10 SER 424

PRO 422 0.12 PRO 121 -0.10 LYS 423

PRO 422 0.12 SER 122 -0.11 LYS 423

PRO 422 0.13 HIS 123 -0.13 LYS 423

PRO 422 0.15 VAL 124 -0.11 LYS 423

PRO 422 0.15 VAL 125 -0.09 LYS 423

PRO 422 0.15 THR 126 -0.11 LYS 423

PRO 422 0.17 MET 127 -0.12 LYS 423

PRO 422 0.18 LEU 128 -0.10 SER 424

PRO 422 0.17 ASP 129 -0.09 SER 424

PRO 422 0.17 ASN 130 -0.10 LYS 423

PRO 422 0.20 PHE 131 -0.10 SER 424

PRO 422 0.21 PRO 132 -0.09 SER 424

PRO 422 0.22 THR 133 -0.10 SER 424

PRO 422 0.24 ASN 134 -0.10 SER 424

PRO 422 0.26 LEU 135 -0.12 SER 424

PRO 422 0.28 HIS 136 -0.13 SER 424

PRO 422 0.26 PRO 137 -0.14 SER 424

PRO 422 0.30 MET 138 -0.16 SER 424

PRO 422 0.29 SER 139 -0.15 SER 424

PRO 422 0.25 GLN 140 -0.13 SER 424

PRO 422 0.25 LEU 141 -0.14 SER 424

PRO 422 0.28 SER 142 -0.15 SER 424

PRO 422 0.24 ALA 143 -0.13 SER 424

PRO 422 0.20 ALA 144 -0.12 SER 424

PRO 422 0.20 ILE 145 -0.13 SER 424

PRO 422 0.20 THR 146 -0.15 LYS 423

PRO 422 0.17 ALA 147 -0.15 LYS 423

PRO 422 0.15 LEU 148 -0.12 LYS 423

PRO 422 0.13 ASN 149 -0.15 LYS 423

PRO 422 0.10 SER 150 -0.16 LYS 423

PRO 422 0.09 GLU 151 -0.13 LYS 423

SER 41 0.09 SER 152 -0.13 LYS 423

GLN 26 0.09 ASN 153 -0.12 LYS 423

GLN 26 0.10 PHE 154 -0.13 LYS 423

GLN 26 0.11 ALA 155 -0.18 LYS 423

GLN 26 0.11 ARG 156 -0.17 LYS 423

GLN 26 0.12 ALA 157 -0.15 LYS 423

GLN 26 0.14 TYR 158 -0.19 LYS 423

GLN 26 0.14 ALA 159 -0.21 LYS 423

GLN 26 0.14 GLU 160 -0.18 LYS 423

GLN 26 0.16 GLY 161 -0.18 LYS 423

GLN 26 0.15 ILE 162 -0.14 LYS 423

GLN 26 0.20 ARG 164 -0.17 PRO 422

LYS 22 0.18 THR 165 -0.15 PRO 422

GLN 26 0.13 LYS 166 -0.10 PRO 422

GLN 26 0.13 TYR 167 -0.08 SER 424

ALA 32 0.12 TRP 168 -0.10 SER 424

ALA 32 0.11 GLU 169 -0.09 SER 424

ALA 32 0.11 VAL 171 -0.11 SER 424

ALA 32 0.13 TYR 172 -0.12 SER 424

ALA 32 0.12 GLU 173 -0.10 SER 424

ALA 32 0.14 ALA 175 -0.13 SER 424

ALA 32 0.14 MET 176 -0.12 SER 424

ALA 32 0.12 ASP 177 -0.12 SER 424

PRO 422 0.14 LEU 178 -0.13 SER 424

PRO 422 0.15 ILE 179 -0.14 SER 424

ALA 32 0.14 ALA 180 -0.12 SER 424

PRO 422 0.15 LYS 181 -0.12 SER 424

PRO 422 0.18 LEU 182 -0.14 SER 424

PRO 422 0.18 PRO 183 -0.13 SER 424

PRO 422 0.16 CYS 184 -0.12 SER 424

PRO 422 0.19 VAL 185 -0.13 SER 424

PRO 422 0.21 ALA 186 -0.13 SER 424

PRO 422 0.19 ALA 187 -0.12 SER 424

PRO 422 0.18 LYS 188 -0.11 SER 424

PRO 422 0.21 ILE 189 -0.12 SER 424

PRO 422 0.21 TYR 190 -0.12 SER 424

PRO 422 0.19 ARG 191 -0.11 SER 424

PRO 422 0.19 ASN 192 -0.10 SER 424

PRO 422 0.21 LEU 193 -0.11 SER 424

PRO 422 0.21 TYR 194 -0.11 SER 424

PRO 422 0.18 ARG 195 -0.10 SER 424

PRO 422 0.18 ALA 196 -0.09 SER 424

PRO 422 0.17 GLY 197 -0.10 SER 424

PRO 422 0.16 SER 198 -0.09 SER 424

PRO 422 0.15 SER 199 -0.10 SER 424

PRO 422 0.15 ILE 200 -0.10 SER 424

PRO 422 0.13 GLY 201 -0.10 SER 424

PRO 422 0.12 ALA 202 -0.09 SER 424

ALA 32 0.12 ILE 203 -0.10 SER 424

ALA 32 0.13 ASP 204 -0.10 SER 424

ALA 32 0.14 SER 205 -0.10 SER 424

ALA 32 0.14 LYS 206 -0.10 SER 424

ALA 32 0.15 LEU 207 -0.10 SER 424

ALA 32 0.17 ASP 208 -0.11 SER 424

ALA 32 0.17 TRP 209 -0.12 SER 424

ALA 32 0.17 SER 210 -0.13 SER 424

ALA 32 0.16 HIS 211 -0.12 SER 424

ALA 32 0.15 ASN 212 -0.11 SER 424

PRO 422 0.17 PHE 213 -0.12 SER 424

PRO 422 0.17 THR 214 -0.12 SER 424

PRO 422 0.15 ASN 215 -0.11 SER 424

PRO 422 0.16 MET 216 -0.11 SER 424

PRO 422 0.18 LEU 217 -0.12 SER 424

PRO 422 0.17 GLY 218 -0.11 SER 424

PRO 422 0.17 TYR 219 -0.11 SER 424

PRO 422 0.15 THR 220 -0.10 SER 424

PRO 422 0.16 ASP 221 -0.10 SER 424

ALA 32 0.18 GLN 223 -0.12 HIS 340

PRO 422 0.17 PHE 224 -0.12 SER 424

ALA 32 0.17 THR 225 -0.12 SER 424

ALA 32 0.19 GLU 226 -0.12 SER 424

ALA 32 0.20 LEU 227 -0.13 SER 424

ALA 32 0.19 MET 228 -0.13 SER 424

ALA 32 0.20 ARG 229 -0.14 SER 424

ALA 32 0.22 LEU 230 -0.14 SER 424

ALA 32 0.21 TYR 231 -0.15 SER 424

ALA 32 0.21 LEU 232 -0.16 SER 424

ALA 32 0.23 THR 233 -0.16 SER 424

ALA 32 0.25 ILE 234 -0.17 SER 424

PRO 422 0.25 HIS 235 -0.18 SER 424

ALA 32 0.24 SER 236 -0.19 SER 424

ALA 32 0.27 ASP 237 -0.21 SER 424

ALA 32 0.30 HIS 238 -0.24 SER 424

ALA 32 0.34 GLU 239 -0.26 SER 424

PRO 422 0.31 GLY 240 -0.29 SER 424

PRO 422 0.43 GLY 241 -0.36 SER 424

PRO 422 0.46 ASN 242 -0.32 SER 424

PRO 422 0.53 VAL 243 -0.32 SER 424

PRO 422 0.42 SER 244 -0.27 SER 424

PRO 422 0.36 ALA 245 -0.28 SER 424

PRO 422 0.48 HIS 246 -0.34 SER 424

PRO 422 0.47 THR 247 -0.31 SER 424

PRO 422 0.32 SER 248 -0.25 SER 424

PRO 422 0.28 HIS 249 -0.27 SER 424

PRO 422 0.38 LEU 250 -0.29 SER 424

PRO 422 0.29 VAL 251 -0.21 SER 424

PRO 422 0.17 GLY 252 -0.18 SER 424

SER 41 0.16 SER 253 -0.16 SER 424

SER 41 0.17 ALA 254 -0.25 LYS 423

GLN 26 0.15 LEU 255 -0.19 LYS 423

SER 41 0.13 SER 256 -0.19 LYS 423

SER 41 0.11 ASP 257 -0.14 LYS 423

PRO 422 0.14 PRO 258 -0.14 SER 424

PRO 422 0.17 TYR 259 -0.14 SER 424

PRO 422 0.20 LEU 260 -0.15 LYS 423

PRO 422 0.25 SER 261 -0.18 SER 424

PRO 422 0.26 PHE 262 -0.19 SER 424

PRO 422 0.28 ALA 263 -0.17 SER 424

PRO 422 0.36 ALA 264 -0.21 SER 424

PRO 422 0.38 ALA 265 -0.23 SER 424

PRO 422 0.36 MET 266 -0.21 SER 424

PRO 422 0.40 ASN 267 -0.21 SER 424

PRO 422 0.48 GLY 268 -0.25 SER 424

PRO 422 0.41 LEU 269 -0.23 SER 424

PRO 422 0.40 ALA 270 -0.20 SER 424

PRO 422 0.46 GLY 271 -0.21 SER 424

PRO 422 0.43 PRO 272 -0.19 SER 424

PRO 422 0.47 LEU 273 -0.22 SER 424

PRO 422 0.45 HIS 274 -0.23 SER 424

PRO 422 0.39 GLY 275 -0.20 SER 424

PRO 422 0.36 LEU 276 -0.18 SER 424

PRO 422 0.36 ALA 277 -0.17 SER 424

PRO 422 0.31 ASN 278 -0.16 SER 424

PRO 422 0.31 GLN 279 -0.15 SER 424

PRO 422 0.33 GLU 280 -0.14 SER 424

PRO 422 0.31 VAL 281 -0.13 SER 424

PRO 422 0.28 LEU 282 -0.12 SER 424

PRO 422 0.30 TRP 284 -0.10 SER 424

PRO 422 0.27 LEU 285 -0.10 SER 424

PRO 422 0.27 GLN 287 -0.08 SER 424

PRO 422 0.25 LEU 288 -0.14 VAL 315

PRO 422 0.24 GLN 289 -0.09 ARG 313

PRO 422 0.24 LYS 290 -0.09 ARG 313

PRO 422 0.24 ASP 298 -0.09 PRO 342

PRO 422 0.27 LEU 301 -0.07 HIS 28

PRO 422 0.28 ARG 302 -0.06 HIS 28

PRO 422 0.28 ASP 303 -0.06 HIS 28

PRO 422 0.30 TYR 304 -0.06 HIS 28

PRO 422 0.32 ILE 305 -0.06 HIS 28

PRO 422 0.31 TRP 306 -0.06 HIS 28

PRO 422 0.32 ASN 307 -0.05 HIS 28

PRO 422 0.35 THR 308 -0.08 LEU 288

PRO 422 0.36 LEU 309 -0.07 LEU 288

PRO 422 0.35 ASN 310 -0.05 HIS 28

PRO 422 0.37 SER 311 -0.06 LEU 288

PRO 422 0.40 GLY 312 -0.08 LEU 288

PRO 422 0.41 ARG 313 -0.13 LEU 288

PRO 422 0.41 VAL 314 -0.13 LEU 288

PRO 422 0.37 VAL 315 -0.14 LEU 288

PRO 422 0.35 PRO 316 -0.11 SER 424

PRO 422 0.34 GLY 317 -0.11 SER 424

PRO 422 0.34 TYR 318 -0.09 SER 424

PRO 422 0.36 GLY 319 -0.09 HIS 28

PRO 422 0.37 HIS 320 -0.12 SER 424

LYS 423 0.44 ALA 321 -0.11 SER 424

ALA 32 0.43 VAL 322 -0.15 SER 424

ALA 32 0.39 LEU 323 -0.15 SER 424

ALA 32 0.38 ARG 324 -0.15 GLN 27

ALA 32 0.34 LYS 325 -0.15 GLN 27

ALA 32 0.31 THR 326 -0.13 GLN 27

ALA 32 0.31 ASP 327 -0.15 SER 424

ALA 32 0.30 PRO 328 -0.14 SER 424

ALA 32 0.28 ARG 329 -0.15 SER 424

ALA 32 0.26 TYR 330 -0.14 SER 424

ALA 32 0.27 THR 331 -0.13 SER 424

ALA 32 0.26 CYS 332 -0.14 SER 424

ALA 32 0.23 GLN 333 -0.13 SER 424

ALA 32 0.23 ARG 334 -0.12 SER 424

ALA 32 0.24 GLU 335 -0.12 SER 424

ALA 32 0.22 PHE 336 -0.12 SER 424

ALA 32 0.21 ALA 337 -0.11 SER 424

ALA 32 0.21 LEU 338 -0.10 SER 424

ALA 32 0.20 LYS 339 -0.11 GLY 84

ALA 32 0.19 HIS 340 -0.12 GLN 223

ALA 32 0.18 LEU 341 -0.10 SER 424

ALA 32 0.19 PRO 342 -0.10 SER 424

PRO 422 0.20 ASP 344 -0.10 SER 424

PRO 422 0.21 PRO 345 -0.09 SER 424

PRO 422 0.23 MET 346 -0.10 SER 424

PRO 422 0.22 PHE 347 -0.10 SER 424

PRO 422 0.21 LYS 348 -0.09 SER 424

PRO 422 0.23 LEU 349 -0.09 SER 424

PRO 422 0.25 VAL 350 -0.10 SER 424

PRO 422 0.22 ALA 351 -0.10 SER 424

PRO 422 0.24 GLN 352 -0.09 THR 23

PRO 422 0.26 LEU 353 -0.09 PHE 24

PRO 422 0.25 TYR 354 -0.10 ARG 334

ALA 32 0.24 LYS 355 -0.11 GLU 335

PRO 422 0.26 ILE 356 -0.09 THR 23

PRO 422 0.29 VAL 357 -0.08 HIS 28

LYS 423 0.28 PRO 358 -0.09 GLN 27

LYS 423 0.29 ASN 359 -0.09 GLN 27

LYS 423 0.29 VAL 360 -0.07 HIS 28

LYS 423 0.33 LEU 361 -0.07 HIS 28

LYS 423 0.34 LEU 362 -0.08 GLN 27

LYS 423 0.32 GLU 363 -0.07 GLN 27

LYS 423 0.34 GLN 364 -0.06 HIS 28

LYS 423 0.38 GLY 365 -0.06 HIS 28

LYS 423 0.38 ALA 367 -0.08 HIS 28

LYS 423 0.35 ASN 369 -0.11 HIS 28

LYS 423 0.33 PRO 370 -0.10 HIS 28

ALA 32 0.30 TRP 371 -0.11 HIS 28

PRO 422 0.29 PRO 372 -0.12 SER 424

PRO 422 0.30 ASN 373 -0.14 SER 424

PRO 422 0.28 VAL 374 -0.15 SER 424

PRO 422 0.31 ASP 375 -0.15 SER 424

PRO 422 0.29 ALA 376 -0.13 SER 424

PRO 422 0.26 HIS 377 -0.13 SER 424

PRO 422 0.25 SER 378 -0.14 SER 424

PRO 422 0.26 GLY 379 -0.14 SER 424

PRO 422 0.24 VAL 380 -0.12 SER 424

PRO 422 0.22 LEU 381 -0.13 SER 424

PRO 422 0.22 LEU 382 -0.13 SER 424

PRO 422 0.22 GLN 383 -0.12 SER 424

PRO 422 0.20 TYR 384 -0.12 SER 424

PRO 422 0.19 TYR 385 -0.12 SER 424

PRO 422 0.20 GLY 386 -0.12 SER 424

PRO 422 0.22 MET 387 -0.13 SER 424

PRO 422 0.23 THR 388 -0.12 SER 424

PRO 422 0.24 GLU 389 -0.13 SER 424

PRO 422 0.26 MET 390 -0.14 SER 424

PRO 422 0.28 ASN 391 -0.14 SER 424

PRO 422 0.26 TYR 392 -0.15 SER 424

PRO 422 0.27 TYR 393 -0.15 SER 424

PRO 422 0.31 THR 394 -0.17 SER 424

PRO 422 0.27 VAL 395 -0.16 SER 424

PRO 422 0.25 LEU 396 -0.16 SER 424

PRO 422 0.28 PHE 397 -0.18 SER 424

PRO 422 0.28 GLY 398 -0.18 SER 424

PRO 422 0.23 VAL 399 -0.17 SER 424

PRO 422 0.23 SER 400 -0.18 SER 424

PRO 422 0.26 ARG 401 -0.20 SER 424

PRO 422 0.22 ALA 402 -0.18 SER 424

ALA 32 0.20 LEU 403 -0.18 SER 424

ALA 32 0.23 GLY 404 -0.20 SER 424

PRO 422 0.22 VAL 405 -0.21 SER 424

ALA 32 0.18 LEU 406 -0.18 SER 424

ALA 32 0.21 ALA 407 -0.17 SER 424

ALA 32 0.22 GLN 408 -0.19 SER 424

ALA 32 0.17 LEU 409 -0.18 SER 424

ALA 32 0.16 ILE 410 -0.15 SER 424

ALA 32 0.20 TRP 411 -0.15 SER 424

ALA 32 0.17 SER 412 -0.17 SER 424

ALA 32 0.12 ARG 413 -0.13 SER 424

ALA 32 0.15 ALA 414 -0.12 SER 424

ALA 32 0.16 LEU 415 -0.13 PRO 422

GLN 26 0.17 GLY 416 -0.18 PRO 422

GLN 26 0.16 PHE 417 -0.19 PRO 422

GLN 26 0.21 PRO 418 -0.26 PRO 422

SER 41 0.24 LEU 419 -0.11 LYS 423

SER 41 0.22 GLU 420 -0.27 SER 424

SER 41 0.46 ARG 421 -0.17 ALA 254

GLY 44 0.94 PRO 422 -0.35 ALA 32

ILE 36 1.21 LYS 423 -0.25 ALA 254

VAL 38 0.21 SER 424 -0.42 GLY 50

SER 426 0.20 MET 425 -0.41 ALA 32

MET 425 0.20 SER 426 -0.33 ALA 32

GLY 312 0.24 THR 427 -0.35 ALA 32

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 13 ---

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 *