Should you encounter any unexpected behaviour,
please let us know.
elNémo has been hacked on november 27th.
It has been moved away and runs again.
Still some additional cleaning from time to time
Sorry for the inconvenience.

* PDHK1 and DCA *

CA distance fluctuations for 2604162351172680512

--- 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
ASP 419 0.02 GLY 41 -0.56 PRO 423

THR 413 0.01 VAL 42 -0.59 PRO 423

ASP 419 0.02 PRO 43 -0.62 PRO 423

THR 413 0.01 GLY 44 -0.58 PRO 423

THR 413 0.01 GLN 45 -0.57 PRO 423

THR 413 0.01 VAL 46 -0.62 PRO 423

THR 413 0.01 ASP 47 -0.62 PRO 423

THR 413 0.01 PHE 48 -0.56 PRO 423

THR 413 0.01 TYR 49 -0.57 PRO 423

THR 413 0.01 ALA 50 -0.62 PRO 423

THR 413 0.01 ARG 51 -0.58 PRO 423

THR 413 0.00 PHE 52 -0.56 VAL 422

THR 413 0.00 SER 53 -0.59 VAL 422

THR 413 0.00 PRO 54 -0.57 VAL 422

THR 413 0.00 SER 55 -0.60 ALA 417

ILE 189 0.00 PRO 56 -0.62 ALA 417

ASP 151 0.00 LEU 57 -0.59 ALA 417

ASP 151 0.00 SER 58 -0.60 ALA 417

ASP 151 0.00 MET 59 -0.54 ALA 417

ASP 151 0.00 LYS 60 -0.54 ALA 417

ASP 151 0.00 GLN 61 -0.53 ALA 417

ASP 151 0.00 PHE 62 -0.48 ALA 417

LEU 392 0.00 LEU 63 -0.46 ALA 417

LEU 392 0.00 ASP 64 -0.47 ALA 417

THR 413 0.00 PHE 65 -0.44 ALA 417

SER 259 0.00 GLY 66 -0.41 ALA 417

SER 259 0.00 SER 67 -0.40 ALA 417

THR 413 0.00 CYS 71 -0.38 ALA 417

THR 413 0.00 GLU 72 -0.37 PRO 423

THR 413 0.00 LYS 73 -0.37 PRO 423

THR 413 0.00 THR 74 -0.41 ALA 417

THR 413 0.00 SER 75 -0.40 ALA 417

THR 413 0.00 PHE 76 -0.42 PRO 423

THR 413 0.00 MET 77 -0.41 PRO 423

THR 413 0.00 PHE 78 -0.44 ALA 417

THR 413 0.00 LEU 79 -0.46 PRO 423

THR 413 0.00 ARG 80 -0.47 PRO 423

THR 413 0.00 GLN 81 -0.48 PRO 423

THR 413 0.00 GLU 82 -0.50 PRO 423

THR 413 0.00 LEU 83 -0.53 PRO 423

THR 413 0.01 PRO 84 -0.55 PRO 423

THR 413 0.00 VAL 85 -0.56 PRO 423

THR 413 0.00 ARG 86 -0.59 PRO 423

THR 413 0.01 LEU 87 -0.61 PRO 423

THR 413 0.01 ALA 88 -0.63 PRO 423

THR 413 0.01 ASN 89 -0.66 PRO 423

THR 413 0.01 ILE 90 -0.71 PRO 423

THR 413 0.01 MET 91 -0.71 PRO 423

THR 413 0.01 LYS 92 -0.74 PRO 423

THR 413 0.01 GLU 93 -0.82 PRO 423

THR 413 0.01 ILE 94 -0.82 PRO 423

ASP 419 0.07 SER 95 -0.81 PRO 423

ASP 419 0.10 LEU 96 -0.90 PRO 423

ASP 419 0.12 LEU 97 -0.95 PRO 423

ASP 419 0.22 PRO 98 -1.00 PRO 423

ASP 419 0.24 ASP 99 -0.89 PRO 423

ASP 419 0.25 ASN 100 -0.89 PRO 423

ASP 419 0.16 LEU 101 -0.90 PRO 423

ASP 419 0.13 LEU 102 -0.84 PRO 423

ASP 419 0.17 ARG 103 -0.78 PRO 423

ASP 418 0.15 THR 104 -0.76 PRO 423

ASP 418 0.11 PRO 105 -0.69 PRO 423

ASP 418 0.06 SER 106 -0.70 PRO 423

ASP 419 0.04 VAL 107 -0.75 PRO 423

ASP 419 0.06 GLN 108 -0.70 PRO 423

ASP 419 0.02 LEU 109 -0.65 PRO 423

THR 413 0.01 VAL 110 -0.67 PRO 423

THR 413 0.01 GLN 111 -0.69 PRO 423

THR 413 0.01 SER 112 -0.63 PRO 423

THR 413 0.01 TRP 113 -0.61 PRO 423

THR 413 0.01 TYR 114 -0.62 PRO 423

THR 413 0.01 ILE 115 -0.61 PRO 423

THR 413 0.01 GLN 116 -0.56 PRO 423

THR 413 0.01 SER 117 -0.56 PRO 423

THR 413 0.01 LEU 118 -0.56 PRO 423

THR 413 0.01 GLN 119 -0.54 PRO 423

THR 413 0.01 GLU 120 -0.51 PRO 423

THR 413 0.00 LEU 121 -0.50 PRO 423

THR 413 0.01 LEU 122 -0.50 PRO 423

THR 413 0.00 ASP 123 -0.48 PRO 423

THR 413 0.00 PHE 124 -0.45 PRO 423

THR 413 0.00 LYS 125 -0.46 PRO 423

THR 413 0.00 ASP 126 -0.43 PRO 423

THR 413 0.00 LYS 127 -0.42 PRO 423

THR 413 0.00 SER 128 -0.39 PRO 423

THR 413 0.00 ALA 129 -0.38 PRO 423

THR 413 0.00 GLU 130 -0.36 PRO 423

THR 413 0.00 ASP 131 -0.37 PRO 423

THR 413 0.00 ALA 132 -0.36 PRO 423

THR 413 0.00 LYS 133 -0.38 PRO 423

THR 413 0.00 ALA 134 -0.40 PRO 423

THR 413 0.00 ILE 135 -0.40 PRO 423

THR 413 0.00 TYR 136 -0.39 PRO 423

THR 413 0.00 ASP 137 -0.42 PRO 423

THR 413 0.00 PHE 138 -0.43 PRO 423

THR 413 0.00 THR 139 -0.42 PRO 423

THR 413 0.00 ASP 140 -0.43 PRO 423

THR 413 0.00 THR 141 -0.46 PRO 423

THR 413 0.00 VAL 142 -0.47 PRO 423

THR 413 0.00 ILE 143 -0.45 PRO 423

THR 413 0.00 ARG 144 -0.47 PRO 423

THR 413 0.00 ILE 145 -0.50 PRO 423

THR 413 0.00 ARG 146 -0.49 PRO 423

THR 413 0.00 ASN 147 -0.47 PRO 423

THR 413 0.00 ARG 148 -0.50 PRO 423

THR 413 0.00 HIS 149 -0.55 PRO 423

THR 413 0.00 ASN 150 -0.53 PRO 423

THR 413 0.00 ASP 151 -0.57 PRO 423

THR 413 0.01 VAL 152 -0.63 PRO 423

THR 413 0.00 ILE 153 -0.65 PRO 423

THR 413 0.00 PRO 154 -0.63 PRO 423

THR 413 0.01 THR 155 -0.66 PRO 423

THR 413 0.01 MET 156 -0.73 PRO 423

ASP 418 0.02 ALA 157 -0.74 PRO 423

ASP 418 0.08 GLN 158 -0.71 PRO 423

ASP 418 0.09 GLY 159 -0.77 PRO 423

ASP 418 0.12 VAL 160 -0.85 PRO 423

ASP 418 0.18 ILE 161 -0.77 PRO 423

ASP 418 0.20 GLU 162 -0.76 PRO 423

ASP 418 0.24 TYR 163 -0.87 PRO 423

ASP 418 0.30 LYS 164 -0.88 PRO 423

ASP 418 0.32 GLU 165 -0.77 PRO 423

ASP 418 0.35 SER 166 -0.78 PRO 423

ASP 418 0.40 PHE 167 -0.88 PRO 423

ALA 417 0.48 ASP 170 -1.22 PRO 423

ALA 417 0.52 PRO 171 -1.48 PRO 423

ALA 417 0.43 VAL 172 -1.51 PRO 423

ASP 419 0.28 THR 173 -1.30 PRO 423

ALA 417 0.21 SER 174 -1.30 PRO 423

ASP 419 0.09 GLN 175 -1.36 PRO 423

ASP 419 0.08 ASN 176 -1.18 PRO 423

ASP 419 0.04 VAL 177 -1.09 PRO 423

THR 413 0.00 GLN 178 -1.06 PRO 423

THR 413 0.01 TYR 179 -1.01 PRO 423

THR 413 0.01 PHE 180 -0.93 PRO 423

THR 413 0.01 LEU 181 -0.87 PRO 423

THR 413 0.00 ASP 182 -0.81 PRO 423

THR 413 0.00 ARG 183 -0.78 PRO 423

THR 413 0.01 PHE 184 -0.76 PRO 423

THR 413 0.00 TYR 185 -0.70 PRO 423

THR 413 0.00 MET 186 -0.65 PRO 423

THR 413 0.00 SER 187 -0.65 PRO 423

THR 413 0.00 ARG 188 -0.62 PRO 423

THR 413 0.00 ILE 189 -0.57 PRO 423

THR 413 0.00 SER 190 -0.55 PRO 423

THR 413 0.00 ILE 191 -0.55 PRO 423

THR 413 0.00 ARG 192 -0.52 PRO 423

THR 413 0.00 MET 193 -0.48 PRO 423

THR 413 0.00 LEU 194 -0.47 PRO 423

THR 413 0.00 LEU 195 -0.48 PRO 423

THR 413 0.00 ASN 196 -0.45 PRO 423

THR 413 0.00 GLN 197 -0.42 PRO 423

THR 413 0.00 HIS 198 -0.42 PRO 423

THR 413 0.00 SER 199 -0.42 PRO 423

THR 413 0.00 LEU 200 -0.39 PRO 423

THR 413 0.00 LEU 201 -0.37 PRO 423

THR 413 0.00 PHE 202 -0.37 PRO 423

THR 413 0.00 GLY 203 -0.38 PRO 423

ASN 147 0.00 HIS 215 -0.37 TRP 420

LEU 201 0.00 ILE 216 -0.38 ALA 417

THR 413 0.00 GLY 217 -0.37 PRO 423

ASN 150 0.00 SER 218 -0.39 TRP 420

ASN 150 0.00 ILE 219 -0.41 TRP 420

ASN 150 0.00 ASN 220 -0.41 TRP 420

ASN 150 0.00 PRO 221 -0.44 ASP 419

ASN 150 0.00 ASN 222 -0.44 ASP 419

ASN 150 0.00 CYS 223 -0.44 TRP 420

ASN 150 0.00 ASN 224 -0.43 TRP 420

ASP 151 0.00 VAL 225 -0.46 TRP 420

ASP 151 0.00 LEU 226 -0.44 TRP 420

ASP 151 0.00 GLU 227 -0.41 TRP 420

ASP 151 0.00 VAL 228 -0.42 TRP 420

ASP 151 0.00 ILE 229 -0.44 TRP 420

ASP 151 0.00 LYS 230 -0.40 TRP 420

ASP 151 0.00 ASP 231 -0.38 TRP 420

PRO 154 0.00 GLY 232 -0.40 TRP 420

PRO 154 0.00 TYR 233 -0.39 TRP 420

ASP 170 0.00 GLU 234 -0.35 TRP 420

ASP 170 0.00 ASN 235 -0.34 TRP 420

ASP 170 0.00 ALA 236 -0.35 TRP 420

ASP 170 0.00 ARG 237 -0.33 TRP 420

ASP 170 0.00 ARG 238 -0.30 TRP 420

ASP 170 0.00 LEU 239 -0.32 PRO 423

ASP 170 0.00 CYS 240 -0.30 TRP 420

ASP 170 0.00 ASP 241 -0.27 TRP 420

ASP 418 0.01 LEU 242 -0.28 PRO 423

ASP 418 0.04 TYR 243 -0.30 PRO 423

ASP 418 0.04 TYR 244 -0.25 TRP 420

ASP 418 0.03 ILE 245 -0.24 TRP 420

ASP 170 0.00 ASN 246 -0.27 TRP 420

ASP 170 0.00 SER 247 -0.31 TRP 420

ASP 170 0.00 PRO 248 -0.34 TRP 420

ASP 170 0.00 GLU 249 -0.35 TRP 420

PRO 154 0.00 LEU 250 -0.39 TRP 420

ASP 151 0.00 GLU 251 -0.41 TRP 420

ASP 151 0.00 LEU 252 -0.43 TRP 420

ASP 151 0.00 GLU 253 -0.45 TRP 420

ASP 151 0.00 GLU 254 -0.49 ASP 419

ASP 151 0.00 LEU 255 -0.53 ASP 419

ASP 151 0.00 ASN 256 -0.55 ASP 419

PRO 221 0.00 ALA 257 -0.59 ASP 419

PRO 221 0.00 LYS 258 -0.59 ASP 419

ASN 222 0.00 SER 259 -0.54 ASP 419

ASP 151 0.00 PRO 260 -0.52 ASP 419

ASP 151 0.00 GLY 261 -0.48 ASP 419

ASN 150 0.00 GLN 262 -0.48 ASP 419

ASP 151 0.00 PRO 263 -0.46 ASP 419

ASP 151 0.00 ILE 264 -0.49 ASP 419

ASP 151 0.00 GLN 265 -0.48 ASP 419

ASP 151 0.00 VAL 266 -0.51 ASP 419

ASP 151 0.00 VAL 267 -0.48 ASP 419

ASP 151 0.00 TYR 268 -0.47 TRP 420

ASN 150 0.00 VAL 269 -0.44 TRP 420

ASN 150 0.00 PRO 270 -0.43 TRP 420

ASP 151 0.00 SER 271 -0.41 TRP 420

ASP 151 0.00 HIS 272 -0.45 TRP 420

ASP 151 0.00 LEU 273 -0.48 TRP 420

ASP 151 0.00 TYR 274 -0.43 TRP 420

HIS 275 0.02 HIS 275 -0.43 PRO 423

HIS 275 0.02 HIS 275 -0.43 PRO 423

PRO 154 0.00 MET 276 -0.48 TRP 420

PRO 154 0.00 VAL 277 -0.47 TRP 420

PRO 154 0.00 PHE 278 -0.41 TRP 420

PRO 154 0.00 GLU 279 -0.42 TRP 420

PRO 154 0.00 LEU 280 -0.47 TRP 420

ASP 170 0.00 PHE 281 -0.42 TRP 420

ASP 170 0.00 LYS 282 -0.38 TRP 420

ASP 170 0.00 ASN 283 -0.40 TRP 420

ASP 170 0.00 ALA 284 -0.42 TRP 420

ASP 170 0.00 MET 285 -0.36 TRP 420

ASP 170 0.00 ARG 286 -0.33 TRP 420

ALA 417 0.00 ALA 287 -0.35 TRP 420

ASP 170 0.00 THR 288 -0.34 TRP 420

ASP 418 0.02 MET 289 -0.29 TRP 420

ALA 417 0.08 GLU 290 -0.27 TRP 420

ALA 417 0.08 HIS 291 -0.28 TRP 420

ALA 417 0.06 HIS 292 -0.27 TRP 420

ALA 417 0.08 ALA 293 -0.23 TRP 420

ALA 417 0.11 ASN 294 -0.21 TRP 420

ALA 417 0.07 ARG 295 -0.23 TRP 420

ALA 417 0.04 GLY 296 -0.24 TRP 420

ALA 417 0.01 VAL 297 -0.27 TRP 420

ASP 170 0.00 TYR 298 -0.31 TRP 420

ASP 170 0.00 PRO 299 -0.34 TRP 420

ASP 170 0.00 PRO 300 -0.37 TRP 420

PRO 154 0.00 ILE 301 -0.41 TRP 420

ASP 151 0.00 GLN 302 -0.45 TRP 420

ASP 151 0.00 VAL 303 -0.48 TRP 420

VAL 305 0.00 HIS 304 -0.51 TRP 420

ASP 151 0.00 VAL 305 -0.52 TRP 420

ASP 151 0.00 THR 306 -0.57 ASP 419

ASP 151 0.00 LEU 307 -0.59 ASP 419

PRO 221 0.00 GLY 308 -0.66 ASP 419

LEU 63 0.00 ASN 309 -0.68 ASP 419

LEU 63 0.00 GLU 310 -0.71 ASP 419

ASP 151 0.00 ASP 311 -0.68 ASP 419

ASP 151 0.00 LEU 312 -0.60 ASP 419

ASP 151 0.00 THR 313 -0.60 TRP 420

ASP 151 0.00 VAL 314 -0.56 TRP 420

ASP 151 0.00 LYS 315 -0.57 TRP 420

PRO 154 0.00 MET 316 -0.52 TRP 420

PRO 154 0.00 SER 317 -0.49 TRP 420

ARG 319 0.00 ASP 318 -0.44 TRP 420

ASP 318 0.00 ARG 319 -0.39 TRP 420

ASP 170 0.00 GLY 320 -0.37 TRP 420

ALA 417 0.04 GLY 321 -0.36 TRP 420

ALA 417 0.01 GLY 322 -0.42 TRP 420

ALA 417 0.07 VAL 323 -0.41 TRP 420

ALA 417 0.11 PRO 324 -0.42 TRP 420

ALA 417 0.03 LEU 325 -0.55 TRP 420

ALA 417 0.19 ARG 326 -0.51 CYS 421

ALA 417 0.15 LYS 327 -0.48 PRO 423

PRO 401 0.00 ILE 328 -0.54 CYS 421

PRO 401 0.00 ASP 329 -0.64 PRO 423

ALA 417 0.06 ARG 330 -0.73 PRO 423

ALA 406 0.00 LEU 331 -0.62 PRO 423

PRO 401 0.00 PHE 332 -0.72 PRO 423

ALA 406 0.00 ASN 333 -0.88 PRO 423

ASP 418 0.01 TYR 334 -0.89 PRO 423

ASP 418 0.15 MET 335 -0.97 PRO 423

ALA 417 0.18 TYR 336 -0.86 PRO 423

ASP 418 0.08 SER 337 -0.74 PRO 423

ASP 418 0.12 THR 338 -0.76 PRO 423

ASP 418 0.14 ALA 339 -0.65 PRO 423

ASP 418 0.16 PRO 340 -0.60 PRO 423

ASP 418 0.10 ARG 341 -0.58 PRO 423

ASP 418 0.09 PRO 342 -0.50 PRO 423

ASP 418 0.12 ARG 343 -0.48 PRO 423

ASP 418 0.08 VAL 344 -0.45 PRO 423

ASP 418 0.11 GLU 345 -0.41 PRO 423

ASP 418 0.11 THR 346 -0.38 PRO 423

ASP 418 0.08 SER 347 -0.35 PRO 423

ASP 418 0.09 ARG 348 -0.35 PRO 423

ASP 418 0.06 ALA 349 -0.35 PRO 423

ASP 418 0.05 VAL 350 -0.40 PRO 423

ASP 418 0.06 PRO 351 -0.40 PRO 423

ASP 170 0.00 LEU 352 -0.40 PRO 423

ASP 418 0.02 ALA 353 -0.47 PRO 423

ASP 418 0.06 GLY 354 -0.55 PRO 423

ASP 418 0.05 PHE 355 -0.60 PRO 423

THR 413 0.00 GLY 356 -0.62 PRO 423

THR 413 0.00 TYR 357 -0.66 PRO 423

ASP 170 0.00 GLY 358 -0.56 PRO 423

GLY 358 0.00 LEU 359 -0.56 PRO 423

SER 53 0.00 PRO 360 -0.66 PRO 423

THR 413 0.00 ILE 361 -0.62 PRO 423

PRO 154 0.00 SER 362 -0.52 PRO 423

PRO 54 0.00 ARG 363 -0.58 TRP 420

PRO 54 0.00 LEU 364 -0.59 PRO 423

PRO 154 0.00 TYR 365 -0.52 TRP 420

LEU 373 0.00 ALA 366 -0.59 TRP 420

PRO 54 0.00 GLN 367 -0.63 TRP 420

PRO 54 0.00 TYR 368 -0.57 ALA 417

ASP 151 0.00 PHE 369 -0.60 ALA 417

TYR 376 0.00 GLN 370 -0.70 ALA 417

TYR 376 0.00 GLY 371 -0.66 TRP 420

LYS 374 0.00 ASP 372 -0.70 TRP 420

ALA 366 0.00 LEU 373 -0.67 TRP 420

PRO 54 0.00 LYS 374 -0.72 TRP 420

ARG 363 0.00 LEU 375 -0.66 TRP 420

TYR 376 0.00 TYR 376 -0.66 TRP 420

TYR 376 0.00 TYR 376 -0.66 TRP 420

SER 53 0.00 SER 377 -0.56 TRP 420

PRO 423 0.00 LEU 378 -0.50 TRP 420

ALA 417 0.05 GLU 379 -0.41 TRP 420

ALA 417 0.08 GLY 380 -0.34 TRP 420

PRO 423 0.03 TYR 381 -0.39 TRP 420

THR 383 0.00 GLY 382 -0.44 TRP 420

GLY 382 0.00 THR 383 -0.51 TRP 420

ALA 385 0.00 ASP 384 -0.57 TRP 420

ASP 384 0.00 ALA 385 -0.59 TRP 420

ASP 151 0.00 VAL 386 -0.63 TRP 420

ASP 151 0.00 ILE 387 -0.62 TRP 420

ILE 389 0.00 TYR 388 -0.66 TRP 420

TYR 388 0.00 ILE 389 -0.61 TRP 420

ASP 151 0.00 LYS 390 -0.64 ASP 419

ASP 151 0.00 ALA 391 -0.61 ASP 419

LEU 63 0.00 LEU 392 -0.61 ASP 419

LEU 392 0.00 SER 393 -0.56 ALA 417

LYS 60 0.00 THR 394 -0.62 ALA 417

ASP 151 0.00 ASP 395 -0.67 ALA 417

ASP 151 0.00 SER 396 -0.63 ALA 417

GLU 398 0.00 ILE 397 -0.66 ALA 417

ILE 397 0.00 GLU 398 -0.62 ALA 417

PRO 54 0.00 ARG 399 -0.68 ALA 417

PRO 54 0.00 LEU 400 -0.63 ALA 417

THR 413 0.00 PRO 401 -0.69 VAL 422

THR 413 0.00 VAL 402 -0.69 VAL 422

THR 413 0.01 TYR 403 -0.70 PRO 423

THR 413 0.01 ASN 404 -0.71 VAL 422

THR 413 0.01 LYS 405 -0.75 VAL 422

THR 413 0.01 ALA 406 -0.84 VAL 422

THR 413 0.01 ALA 407 -0.84 VAL 422

THR 413 0.02 TRP 408 -0.84 PRO 423

ASP 419 0.02 LYS 409 -0.91 VAL 422

THR 413 0.02 HIS 410 -1.02 VAL 422

ASP 419 0.10 TYR 411 -1.04 PRO 423

ASP 419 0.23 ASN 412 -1.01 PRO 423

ASP 419 0.24 THR 413 -1.05 VAL 422

ASP 419 0.34 ASN 414 -1.24 VAL 422

PRO 171 0.52 ALA 417 -0.70 GLN 370

ASP 170 0.48 ASP 418 -0.63 ASP 395

VAL 172 0.39 ASP 419 -0.71 GLU 310

ASP 170 0.03 TRP 420 -0.72 LYS 374

ASP 419 0.00 CYS 421 -0.64 ASP 329

GLY 380 0.04 VAL 422 -1.24 ASN 414

GLY 380 0.05 PRO 423 -1.51 VAL 172

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: december 26th, 2025.

Should you encounter any unexpected behaviour, please let us know. elNémo has been hacked on november 27th. It has been moved away and runs again. **Still some additional cleaning from time to time** Sorry for the inconvenience.

*** PDHK1 and DCA ***

CA distance fluctuations for 2604162351172680512

--- normal mode 10 ---

Should you encounter any unexpected behaviour,
please let us know.
elNémo has been hacked on november 27th.
It has been moved away and runs again.
Still some additional cleaning from time to time
Sorry for the inconvenience.

* PDHK1 and DCA *