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 15 ---

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 0.20 ALA 1 -0.04 GLU 160

ALA 32 0.21 SER 2 -0.04 GLU 160

ALA 32 0.23 SER 3 -0.05 GLU 173

ALA 32 0.24 THR 4 -0.05 GLN 100

ALA 32 0.24 ASN 5 -0.06 GLN 100

ALA 32 0.27 LEU 6 -0.05 LEU 51

ALA 32 0.26 LYS 7 -0.05 GLY 50

ALA 32 0.24 ASP 8 -0.06 GLY 34

ALA 32 0.26 VAL 9 -0.07 LYS 49

ALA 32 0.29 LEU 10 -0.08 LYS 49

ALA 32 0.24 ALA 11 -0.10 GLY 34

ALA 32 0.26 LEU 13 -0.13 LYS 49

ALA 32 0.27 ILE 14 -0.15 LYS 49

ALA 32 0.20 PRO 15 -0.17 GLY 34

ALA 32 0.20 LYS 16 -0.20 LYS 49

ALA 32 0.28 GLU 17 -0.22 LYS 49

ALA 32 0.24 GLN 18 -0.23 GLY 50

ALA 32 0.15 ALA 19 -0.26 GLY 34

ALA 32 0.19 ARG 20 -0.30 LYS 49

ALA 32 0.27 ILE 21 -0.34 LYS 49

PRO 422 0.18 LYS 22 -0.34 GLY 34

PRO 422 0.18 THR 23 -0.33 GLY 34

PRO 422 0.19 PHE 24 -0.39 GLY 34

PRO 422 0.27 ARG 25 -0.49 GLY 34

PRO 422 0.25 GLN 26 -0.39 GLY 34

PRO 422 0.29 GLN 27 -0.32 GLY 34

PRO 422 0.32 HIS 28 -0.37 GLY 34

PRO 422 0.36 GLY 29 -0.56 GLY 34

PRO 422 0.45 THR 31 -0.35 LYS 423

LEU 51 0.76 ALA 32 -0.34 LYS 423

ALA 32 0.19 GLY 34 -0.76 LYS 423

GLY 365 0.08 GLN 35 -0.82 LYS 423

GLY 365 0.10 ILE 36 -1.03 LYS 423

GLY 365 0.08 THR 37 -0.83 LYS 423

GLY 365 0.06 VAL 38 -0.68 LYS 423

GLY 365 0.07 ASP 39 -0.65 LYS 423

GLY 365 0.11 MET 40 -0.83 LYS 423

ALA 32 0.11 SER 41 -0.88 LYS 423

GLY 365 0.09 TYR 42 -0.59 LYS 423

ALA 32 0.14 GLY 43 -0.63 PRO 422

ALA 32 0.21 GLY 44 -0.86 PRO 422

ALA 32 0.26 MET 45 -0.88 LYS 423

ALA 32 0.26 ARG 46 -0.71 LYS 423

ALA 32 0.33 GLY 47 -0.70 LYS 423

ALA 32 0.41 MET 48 -0.86 LYS 423

ALA 32 0.71 LYS 49 -0.69 LYS 423

ALA 32 0.71 GLY 50 -0.61 LYS 423

ALA 32 0.76 LEU 51 -0.42 LYS 423

ALA 32 0.63 TYR 53 -0.26 LYS 423

ALA 32 0.59 GLU 54 -0.23 LYS 423

ALA 32 0.52 THR 55 -0.20 LYS 423

ALA 32 0.54 SER 56 -0.25 LYS 423

ALA 32 0.58 VAL 57 -0.31 LYS 423

ALA 32 0.52 LEU 58 -0.33 LYS 423

ALA 32 0.47 ASP 59 -0.32 LYS 423

ALA 32 0.42 PRO 60 -0.32 LYS 423

ALA 32 0.38 ASP 61 -0.29 LYS 423

ALA 32 0.38 GLU 62 -0.26 LYS 423

ALA 32 0.40 GLY 63 -0.27 LYS 423

ALA 32 0.45 ILE 64 -0.27 LYS 423

ALA 32 0.46 ARG 65 -0.24 LYS 423

ALA 32 0.45 PHE 66 -0.20 LYS 423

ALA 32 0.47 ARG 67 -0.21 LYS 423

ALA 32 0.45 GLY 68 -0.23 LYS 423

ALA 32 0.41 PHE 69 -0.20 LYS 423

ALA 32 0.40 SER 70 -0.22 LYS 423

ALA 32 0.37 ILE 71 -0.20 LYS 423

ALA 32 0.33 PRO 72 -0.19 LYS 423

ALA 32 0.34 GLU 73 -0.18 LYS 423

ALA 32 0.35 CYS 74 -0.16 LYS 423

ALA 32 0.32 GLN 75 -0.15 LYS 423

ALA 32 0.30 LYS 76 -0.14 LYS 423

ALA 32 0.31 LEU 77 -0.14 LYS 423

ALA 32 0.32 LEU 78 -0.12 LYS 423

ALA 32 0.29 PRO 79 -0.10 LYS 423

ALA 32 0.28 LYS 80 -0.11 PRO 422

ALA 32 0.25 GLY 82 -0.10 PRO 422

ALA 32 0.25 GLY 84 -0.13 PRO 422

ALA 32 0.28 GLU 86 -0.15 PRO 422

ALA 32 0.30 PRO 87 -0.14 PRO 422

ALA 32 0.30 LEU 88 -0.14 PRO 422

ALA 32 0.32 PRO 89 -0.16 PRO 422

ALA 32 0.31 GLU 90 -0.12 PRO 422

ALA 32 0.32 GLY 91 -0.10 PRO 422

ALA 32 0.35 LEU 92 -0.12 PRO 422

ALA 32 0.36 PHE 93 -0.12 PRO 422

ALA 32 0.34 TRP 94 -0.09 LYS 423

ALA 32 0.37 LEU 95 -0.12 LYS 423

ALA 32 0.41 LEU 96 -0.13 LYS 423

ALA 32 0.39 VAL 97 -0.10 LYS 423

ALA 32 0.37 THR 98 -0.11 LYS 423

ALA 32 0.40 GLY 99 -0.14 LYS 423

ALA 32 0.36 GLN 100 -0.12 LYS 423

ALA 32 0.33 ILE 101 -0.12 LYS 423

ALA 32 0.31 PRO 102 -0.09 LYS 423

ALA 32 0.28 THR 103 -0.09 LYS 423

ALA 32 0.27 GLN 106 -0.06 LYS 423

ALA 32 0.28 VAL 107 -0.08 PRO 422

ALA 32 0.26 SER 108 -0.08 PRO 422

ALA 32 0.25 TRP 109 -0.06 PRO 422

ALA 32 0.26 SER 111 -0.10 PRO 422

ALA 32 0.25 LYS 112 -0.08 PRO 422

ALA 32 0.26 GLU 113 -0.07 PRO 422

ALA 32 0.27 TRP 114 -0.10 PRO 422

ALA 32 0.25 ALA 115 -0.10 PRO 422

ALA 32 0.24 LYS 116 -0.09 PRO 422

ALA 32 0.25 ARG 117 -0.10 PRO 422

ALA 32 0.25 ALA 118 -0.12 PRO 422

ALA 32 0.23 ALA 119 -0.12 PRO 422

ALA 32 0.23 LEU 120 -0.15 PRO 422

ALA 32 0.21 PRO 121 -0.13 PRO 422

ALA 32 0.20 SER 122 -0.14 PRO 422

ALA 32 0.20 HIS 123 -0.15 PRO 422

ALA 32 0.22 VAL 124 -0.18 PRO 422

ALA 32 0.21 VAL 125 -0.18 PRO 422

ALA 32 0.20 THR 126 -0.18 PRO 422

ALA 32 0.20 MET 127 -0.20 PRO 422

ALA 32 0.21 LEU 128 -0.22 PRO 422

ALA 32 0.20 ASP 129 -0.21 PRO 422

ALA 32 0.19 ASN 130 -0.21 PRO 422

ALA 32 0.20 PHE 131 -0.25 PRO 422

ALA 32 0.19 PRO 132 -0.26 PRO 422

ALA 32 0.20 THR 133 -0.27 PRO 422

ALA 32 0.19 ASN 134 -0.29 PRO 422

ALA 32 0.21 LEU 135 -0.31 PRO 422

ALA 32 0.22 HIS 136 -0.33 PRO 422

ALA 32 0.24 PRO 137 -0.32 PRO 422

ALA 32 0.26 MET 138 -0.36 PRO 422

ALA 32 0.24 SER 139 -0.35 PRO 422

ALA 32 0.23 GLN 140 -0.30 PRO 422

ALA 32 0.26 LEU 141 -0.30 PRO 422

ALA 32 0.27 SER 142 -0.33 PRO 422

ALA 32 0.24 ALA 143 -0.28 PRO 422

ALA 32 0.24 ALA 144 -0.24 PRO 422

ALA 32 0.26 ILE 145 -0.24 PRO 422

ALA 32 0.25 THR 146 -0.24 PRO 422

ALA 32 0.23 ALA 147 -0.20 PRO 422

ALA 32 0.24 LEU 148 -0.17 PRO 422

ALA 32 0.25 ASN 149 -0.15 PRO 422

ALA 32 0.22 SER 150 -0.12 PRO 422

ALA 32 0.23 GLU 151 -0.10 PRO 422

ALA 32 0.25 SER 152 -0.08 PRO 422

ALA 32 0.24 ASN 153 -0.04 SER 3

ALA 32 0.25 PHE 154 -0.04 SER 3

ALA 32 0.23 ALA 155 -0.03 SER 3

LYS 423 0.22 ARG 156 -0.04 SER 3

ALA 32 0.21 ALA 157 -0.04 SER 3

LYS 423 0.26 TYR 158 -0.04 GLY 34

LYS 423 0.29 ALA 159 -0.04 SER 3

LYS 423 0.26 GLU 160 -0.04 SER 3

LYS 423 0.26 GLY 161 -0.04 GLY 34

LYS 423 0.21 ILE 162 -0.05 GLY 34

ALA 32 0.24 ARG 164 -0.08 GLY 34

ALA 32 0.24 THR 165 -0.09 GLY 34

ALA 32 0.23 LYS 166 -0.07 GLY 34

ALA 32 0.27 TYR 167 -0.06 GLY 34

ALA 32 0.30 TRP 168 -0.06 GLY 50

ALA 32 0.27 GLU 169 -0.06 GLY 34

ALA 32 0.30 VAL 171 -0.04 LEU 51

ALA 32 0.30 TYR 172 -0.04 LEU 51

ALA 32 0.27 GLU 173 -0.05 SER 3

ALA 32 0.31 ALA 175 -0.10 PRO 422

ALA 32 0.30 MET 176 -0.10 PRO 422

ALA 32 0.27 ASP 177 -0.11 PRO 422

ALA 32 0.29 LEU 178 -0.16 PRO 422

ALA 32 0.30 ILE 179 -0.17 PRO 422

ALA 32 0.28 ALA 180 -0.14 PRO 422

ALA 32 0.26 LYS 181 -0.17 PRO 422

ALA 32 0.28 LEU 182 -0.21 PRO 422

ALA 32 0.26 PRO 183 -0.20 PRO 422

ALA 32 0.25 CYS 184 -0.19 PRO 422

ALA 32 0.25 VAL 185 -0.22 PRO 422

ALA 32 0.25 ALA 186 -0.24 PRO 422

ALA 32 0.24 ALA 187 -0.22 PRO 422

ALA 32 0.23 LYS 188 -0.22 PRO 422

ALA 32 0.23 ILE 189 -0.25 PRO 422

ALA 32 0.23 TYR 190 -0.25 PRO 422

ALA 32 0.21 ARG 191 -0.22 PRO 422

ALA 32 0.21 ASN 192 -0.23 PRO 422

ALA 32 0.21 LEU 193 -0.25 PRO 422

ALA 32 0.20 TYR 194 -0.24 PRO 422

ALA 32 0.20 ARG 195 -0.22 PRO 422

ALA 32 0.19 ALA 196 -0.21 PRO 422

ALA 32 0.20 GLY 197 -0.21 PRO 422

ALA 32 0.19 SER 198 -0.19 PRO 422

ALA 32 0.20 SER 199 -0.18 PRO 422

ALA 32 0.22 ILE 200 -0.18 PRO 422

ALA 32 0.21 GLY 201 -0.16 PRO 422

ALA 32 0.22 ALA 202 -0.14 PRO 422

ALA 32 0.23 ILE 203 -0.13 PRO 422

ALA 32 0.22 ASP 204 -0.12 PRO 422

ALA 32 0.23 SER 205 -0.10 PRO 422

ALA 32 0.23 LYS 206 -0.10 PRO 422

ALA 32 0.24 LEU 207 -0.12 PRO 422

ALA 32 0.26 ASP 208 -0.12 PRO 422

ALA 32 0.27 TRP 209 -0.14 PRO 422

ALA 32 0.28 SER 210 -0.16 PRO 422

ALA 32 0.25 HIS 211 -0.15 PRO 422

ALA 32 0.25 ASN 212 -0.15 PRO 422

ALA 32 0.26 PHE 213 -0.18 PRO 422

ALA 32 0.25 THR 214 -0.19 PRO 422

ALA 32 0.23 ASN 215 -0.17 PRO 422

ALA 32 0.23 MET 216 -0.18 PRO 422

ALA 32 0.23 LEU 217 -0.20 PRO 422

ALA 32 0.22 GLY 218 -0.19 PRO 422

ALA 32 0.22 TYR 219 -0.19 PRO 422

ALA 32 0.22 THR 220 -0.17 PRO 422

ALA 32 0.22 ASP 221 -0.17 PRO 422

ALA 32 0.23 GLN 223 -0.17 PRO 422

ALA 32 0.24 PHE 224 -0.19 PRO 422

ALA 32 0.25 THR 225 -0.18 PRO 422

ALA 32 0.26 GLU 226 -0.17 PRO 422

ALA 32 0.27 LEU 227 -0.20 PRO 422

ALA 32 0.27 MET 228 -0.20 PRO 422

ALA 32 0.29 ARG 229 -0.18 PRO 422

ALA 32 0.30 LEU 230 -0.19 PRO 422

ALA 32 0.30 TYR 231 -0.22 PRO 422

ALA 32 0.32 LEU 232 -0.22 PRO 422

ALA 32 0.34 THR 233 -0.19 PRO 422

ALA 32 0.35 ILE 234 -0.22 PRO 422

ALA 32 0.36 HIS 235 -0.27 PRO 422

ALA 32 0.38 SER 236 -0.24 PRO 422

ALA 32 0.43 ASP 237 -0.25 PRO 422

ALA 32 0.46 HIS 238 -0.28 PRO 422

ALA 32 0.54 GLU 239 -0.30 LYS 423

ALA 32 0.55 GLY 240 -0.31 PRO 422

ALA 32 0.52 GLY 241 -0.49 PRO 422

ALA 32 0.44 ASN 242 -0.52 PRO 422

ALA 32 0.38 VAL 243 -0.61 PRO 422

ALA 32 0.38 SER 244 -0.47 PRO 422

ALA 32 0.44 ALA 245 -0.40 PRO 422

ALA 32 0.46 HIS 246 -0.52 PRO 422

ALA 32 0.39 THR 247 -0.53 PRO 422

ALA 32 0.39 SER 248 -0.35 PRO 422

ALA 32 0.43 HIS 249 -0.29 PRO 422

SER 424 0.43 LEU 250 -0.40 PRO 422

SER 424 0.39 VAL 251 -0.31 PRO 422

ALA 32 0.36 GLY 252 -0.18 PRO 422

ALA 32 0.36 SER 253 -0.08 LYS 22

SER 424 0.33 ALA 254 -0.06 GLN 26

ALA 32 0.29 LEU 255 -0.06 PHE 417

ALA 32 0.29 SER 256 -0.11 PRO 422

ALA 32 0.29 ASP 257 -0.10 PRO 422

ALA 32 0.32 PRO 258 -0.15 PRO 422

ALA 32 0.29 TYR 259 -0.19 PRO 422

ALA 32 0.29 LEU 260 -0.23 PRO 422

ALA 32 0.33 SER 261 -0.28 PRO 422

ALA 32 0.33 PHE 262 -0.30 PRO 422

ALA 32 0.29 ALA 263 -0.33 PRO 422

ALA 32 0.31 ALA 264 -0.42 PRO 422

ALA 32 0.34 ALA 265 -0.43 PRO 422

ALA 32 0.31 MET 266 -0.42 PRO 422

ALA 32 0.29 ASN 267 -0.47 PRO 422

ALA 32 0.32 GLY 268 -0.56 PRO 422

ALA 32 0.32 LEU 269 -0.48 PRO 422

ALA 32 0.28 ALA 270 -0.46 PRO 422

ALA 32 0.28 GLY 271 -0.53 PRO 422

ALA 32 0.26 PRO 272 -0.50 PRO 422

ALA 32 0.28 LEU 273 -0.55 PRO 422

ALA 32 0.31 HIS 274 -0.53 PRO 422

ALA 32 0.29 GLY 275 -0.45 PRO 422

ALA 32 0.25 LEU 276 -0.42 PRO 422

ALA 32 0.25 ALA 277 -0.40 PRO 422

ALA 32 0.25 ASN 278 -0.35 PRO 422

ALA 32 0.23 GLN 279 -0.36 PRO 422

ALA 32 0.20 GLU 280 -0.38 PRO 422

ALA 32 0.21 VAL 281 -0.34 PRO 422

ALA 32 0.21 LEU 282 -0.32 PRO 422

ALA 32 0.17 TRP 284 -0.33 PRO 422

ALA 32 0.18 LEU 285 -0.30 PRO 422

ALA 32 0.15 GLN 287 -0.30 PRO 422

ALA 32 0.15 LEU 288 -0.29 PRO 422

ALA 32 0.16 GLN 289 -0.26 PRO 422

ALA 32 0.14 LYS 290 -0.26 PRO 422

ALA 32 0.17 ASP 298 -0.18 PRO 422

ALA 32 0.16 LEU 301 -0.22 PRO 422

ALA 32 0.16 ARG 302 -0.20 PRO 422

ALA 32 0.14 ASP 303 -0.20 PRO 422

ALA 32 0.14 TYR 304 -0.23 PRO 422

ALA 32 0.16 ILE 305 -0.23 PRO 422

ALA 32 0.14 TRP 306 -0.21 PRO 422

TRP 284 0.13 ASN 307 -0.23 PRO 422

TRP 284 0.15 THR 308 -0.25 PRO 422

PRO 272 0.14 LEU 309 -0.25 PRO 422

PRO 272 0.14 ASN 310 -0.23 PRO 422

ASN 134 0.16 SER 311 -0.26 PRO 422

PRO 272 0.17 GLY 312 -0.28 PRO 422

PRO 272 0.17 ARG 313 -0.29 PRO 422

PRO 272 0.17 VAL 314 -0.29 PRO 422

PRO 316 0.21 VAL 315 -0.29 PRO 422

VAL 315 0.21 PRO 316 -0.35 PRO 422

ALA 32 0.24 GLY 317 -0.31 PRO 422

ALA 32 0.26 TYR 318 -0.27 PRO 422

ALA 32 0.27 GLY 319 -0.27 LYS 423

ALA 32 0.31 HIS 320 -0.30 LYS 423

ALA 32 0.33 ALA 321 -0.34 LYS 423

ALA 32 0.38 VAL 322 -0.35 LYS 423

ALA 32 0.36 LEU 323 -0.31 LYS 423

ALA 32 0.33 ARG 324 -0.29 LYS 423

ALA 32 0.31 LYS 325 -0.26 LYS 423

ALA 32 0.31 THR 326 -0.24 LYS 423

ALA 32 0.34 ASP 327 -0.24 LYS 423

ALA 32 0.33 PRO 328 -0.21 LYS 423

ALA 32 0.33 ARG 329 -0.22 PRO 422

ALA 32 0.30 TYR 330 -0.23 PRO 422

ALA 32 0.29 THR 331 -0.19 LYS 423

ALA 32 0.30 CYS 332 -0.19 PRO 422

ALA 32 0.28 GLN 333 -0.21 PRO 422

ALA 32 0.26 ARG 334 -0.20 PRO 422

ALA 32 0.27 GLU 335 -0.17 PRO 422

ALA 32 0.26 PHE 336 -0.18 PRO 422

ALA 32 0.24 ALA 337 -0.19 PRO 422

ALA 32 0.23 LEU 338 -0.17 PRO 422

ALA 32 0.24 LYS 339 -0.16 PRO 422

ALA 32 0.23 HIS 340 -0.17 PRO 422

ALA 32 0.22 LEU 341 -0.19 PRO 422

ALA 32 0.21 PRO 342 -0.18 PRO 422

ALA 32 0.20 ASP 344 -0.21 PRO 422

ALA 32 0.19 PRO 345 -0.22 PRO 422

ALA 32 0.20 MET 346 -0.24 PRO 422

ALA 32 0.21 PHE 347 -0.23 PRO 422

ALA 32 0.20 LYS 348 -0.21 PRO 422

ALA 32 0.19 LEU 349 -0.23 PRO 422

ALA 32 0.22 VAL 350 -0.24 PRO 422

ALA 32 0.22 ALA 351 -0.21 PRO 422

ALA 32 0.20 GLN 352 -0.21 PRO 422

ALA 32 0.21 LEU 353 -0.23 PRO 422

ALA 32 0.22 TYR 354 -0.21 PRO 422

ALA 32 0.21 LYS 355 -0.19 LYS 423

ALA 32 0.19 ILE 356 -0.19 PRO 422

ALA 32 0.20 VAL 357 -0.21 PRO 422

ALA 32 0.21 PRO 358 -0.22 LYS 423

ALA 32 0.19 ASN 359 -0.21 LYS 423

ALA 32 0.17 VAL 360 -0.20 LYS 423

ALA 32 0.19 LEU 361 -0.22 LYS 423

ALA 32 0.19 LEU 362 -0.22 LYS 423

ALA 32 0.16 GLU 363 -0.20 LYS 423

LEU 273 0.17 GLN 364 -0.20 LYS 423

LEU 273 0.17 GLY 365 -0.22 LYS 423

ALA 32 0.22 ALA 367 -0.26 LYS 423

ALA 32 0.27 ASN 369 -0.28 LYS 423

ALA 32 0.25 PRO 370 -0.25 LYS 423

ALA 32 0.27 TRP 371 -0.25 LYS 423

ALA 32 0.27 PRO 372 -0.25 PRO 422

ALA 32 0.30 ASN 373 -0.27 PRO 422

ALA 32 0.30 VAL 374 -0.28 PRO 422

ALA 32 0.28 ASP 375 -0.32 PRO 422

ALA 32 0.26 ALA 376 -0.29 PRO 422

ALA 32 0.26 HIS 377 -0.26 PRO 422

ALA 32 0.26 SER 378 -0.27 PRO 422

ALA 32 0.24 GLY 379 -0.29 PRO 422

ALA 32 0.23 VAL 380 -0.26 PRO 422

ALA 32 0.24 LEU 381 -0.24 PRO 422

ALA 32 0.24 LEU 382 -0.26 PRO 422

ALA 32 0.22 GLN 383 -0.26 PRO 422

ALA 32 0.21 TYR 384 -0.23 PRO 422

ALA 32 0.22 TYR 385 -0.22 PRO 422

ALA 32 0.21 GLY 386 -0.24 PRO 422

ALA 32 0.22 MET 387 -0.26 PRO 422

ALA 32 0.21 THR 388 -0.27 PRO 422

ALA 32 0.22 GLU 389 -0.29 PRO 422

ALA 32 0.22 MET 390 -0.32 PRO 422

ALA 32 0.22 ASN 391 -0.34 PRO 422

ALA 32 0.24 TYR 392 -0.32 PRO 422

ALA 32 0.26 TYR 393 -0.32 PRO 422

ALA 32 0.27 THR 394 -0.36 PRO 422

ALA 32 0.28 VAL 395 -0.31 PRO 422

ALA 32 0.29 LEU 396 -0.28 PRO 422

ALA 32 0.31 PHE 397 -0.32 PRO 422

ALA 32 0.32 GLY 398 -0.32 PRO 422

ALA 32 0.31 VAL 399 -0.26 PRO 422

ALA 32 0.34 SER 400 -0.25 PRO 422

ALA 32 0.37 ARG 401 -0.29 PRO 422

ALA 32 0.35 ALA 402 -0.24 PRO 422

ALA 32 0.37 LEU 403 -0.19 PRO 422

ALA 32 0.41 GLY 404 -0.20 PRO 422

ALA 32 0.41 VAL 405 -0.24 PRO 422

ALA 32 0.38 LEU 406 -0.17 PRO 422

ALA 32 0.40 ALA 407 -0.11 PRO 422

ALA 32 0.45 GLN 408 -0.10 LYS 423

ALA 32 0.41 LEU 409 -0.10 PRO 422

ALA 32 0.37 ILE 410 -0.06 LEU 51

ALA 32 0.41 TRP 411 -0.10 LEU 51

ALA 32 0.44 SER 412 -0.11 LEU 51

ALA 32 0.36 ARG 413 -0.08 GLY 50

ALA 32 0.34 ALA 414 -0.11 GLY 50

ALA 32 0.37 LEU 415 -0.16 GLY 50

ALA 32 0.35 GLY 416 -0.12 GLY 50

ALA 32 0.42 PHE 417 -0.14 GLY 50

ALA 32 0.34 PRO 418 -0.14 GLY 50

ALA 32 0.31 LEU 419 -0.25 GLU 420

ALA 32 0.41 GLU 420 -0.25 LEU 419

ALA 32 0.24 ARG 421 -0.36 MET 45

ALA 32 0.49 PRO 422 -0.86 GLY 44

ALA 254 0.32 LYS 423 -1.03 ILE 36

LEU 250 0.43 SER 424 -0.11 VAL 38

LEU 250 0.28 MET 425 -0.05 GLN 26

LYS 423 0.27 SER 426 -0.11 TYR 42

ALA 254 0.18 THR 427 -0.10 GLY 312

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 15 ---

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 *