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 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
PRO 423 0.06 GLY 41 -0.14 ASP 419

PRO 423 0.05 VAL 42 -0.12 ASP 419

PRO 423 0.06 PRO 43 -0.14 ASP 419

PRO 423 0.02 GLY 44 -0.17 ASP 419

VAL 42 0.00 GLN 45 -0.16 ASP 419

GLN 45 0.00 VAL 46 -0.15 ASP 419

PHE 48 0.00 ASP 47 -0.20 ASP 419

ASP 47 0.00 PHE 48 -0.21 ASP 419

PHE 48 0.00 TYR 49 -0.20 TRP 420

ARG 51 0.00 ALA 50 -0.21 TRP 420

ALA 50 0.00 ARG 51 -0.27 TRP 420

PRO 54 0.00 PHE 52 -0.28 TRP 420

VAL 402 0.00 SER 53 -0.30 TRP 420

VAL 85 0.00 PRO 54 -0.29 PRO 423

VAL 85 0.00 SER 55 -0.34 PRO 423

SER 55 0.00 PRO 56 -0.39 PRO 423

SER 58 0.00 LEU 57 -0.41 PRO 423

GLU 398 0.00 SER 58 -0.47 PRO 423

GLU 398 0.00 MET 59 -0.46 PRO 423

GLU 398 0.00 LYS 60 -0.46 PRO 423

PHE 65 0.00 GLN 61 -0.42 PRO 423

HIS 198 0.00 PHE 62 -0.38 PRO 423

GLN 61 0.00 LEU 63 -0.40 PRO 423

CYS 71 0.00 ASP 64 -0.39 PRO 423

GLN 61 0.00 PHE 65 -0.34 PRO 423

ILE 219 0.00 GLY 66 -0.33 PRO 423

CYS 71 0.00 SER 67 -0.34 PRO 423

SER 75 0.00 CYS 71 -0.27 PRO 423

LEU 201 0.00 GLU 72 -0.24 PRO 423

THR 74 0.00 LYS 73 -0.23 PRO 423

LYS 73 0.00 THR 74 -0.27 PRO 423

THR 74 0.00 SER 75 -0.26 PRO 423

ILE 135 0.00 PHE 76 -0.21 PRO 423

ARG 80 0.00 MET 77 -0.23 PRO 423

LEU 79 0.00 PHE 78 -0.26 PRO 423

PHE 78 0.00 LEU 79 -0.22 PRO 423

PHE 78 0.00 ARG 80 -0.18 PRO 423

PHE 78 0.00 GLN 81 -0.20 TRP 420

PHE 78 0.00 GLU 82 -0.23 PRO 423

PRO 84 0.00 LEU 83 -0.18 PRO 423

LEU 83 0.00 PRO 84 -0.15 TRP 420

PRO 54 0.00 VAL 85 -0.19 TRP 420

ILE 90 0.00 ARG 86 -0.19 PRO 423

ASN 89 0.00 LEU 87 -0.12 TRP 420

LEU 83 0.00 ALA 88 -0.14 TRP 420

ILE 90 0.00 ASN 89 -0.17 TRP 420

MET 91 0.00 ILE 90 -0.11 TRP 420

ILE 90 0.00 MET 91 -0.08 ASP 419

MET 91 0.00 LYS 92 -0.13 ASP 419

MET 91 0.00 GLU 93 -0.08 ASP 419

PRO 423 0.06 ILE 94 -0.03 ASP 419

PRO 423 0.12 SER 95 -0.07 ASP 419

PRO 423 0.13 LEU 96 -0.07 ASP 419

PRO 423 0.18 LEU 97 -0.00 SER 95

PRO 423 0.30 PRO 98 -0.00 ASP 99

PRO 423 0.34 ASP 99 -0.00 PRO 98

PRO 423 0.40 ASN 100 -0.00 THR 104

PRO 423 0.30 LEU 101 -0.00 TYR 163

PRO 423 0.24 LEU 102 -0.00 SER 95

PRO 423 0.31 ARG 103 -0.00 ASN 100

PRO 423 0.30 THR 104 -0.00 LEU 101

PRO 423 0.26 PRO 105 -0.00 GLU 162

PRO 423 0.19 SER 106 -0.00 PRO 154

PRO 423 0.17 VAL 107 -0.00 PRO 154

PRO 423 0.19 GLN 108 -0.00 VAL 110

PRO 423 0.14 LEU 109 -0.00 VAL 110

PRO 423 0.08 VAL 110 -0.00 LEU 109

PRO 423 0.08 GLN 111 -0.00 ASP 419

PRO 423 0.09 SER 112 -0.01 ASP 419

PRO 423 0.04 TRP 113 -0.00 ASP 419

SER 117 0.00 TYR 114 -0.03 ASP 419

PRO 423 0.03 ILE 115 -0.05 ASP 419

PRO 423 0.02 GLN 116 -0.04 ASP 419

GLN 116 0.00 SER 117 -0.05 TRP 420

ILE 145 0.00 LEU 118 -0.09 TRP 420

GLU 120 0.00 GLN 119 -0.08 ASP 419

GLN 119 0.00 GLU 120 -0.08 TRP 420

ILE 143 0.00 LEU 121 -0.11 TRP 420

GLN 116 0.00 LEU 122 -0.13 TRP 420

LEU 122 0.00 ASP 123 -0.11 TRP 420

LYS 127 0.00 PHE 124 -0.13 TRP 420

ASP 126 0.00 LYS 125 -0.16 TRP 420

PHE 124 0.00 ASP 126 -0.17 TRP 420

PHE 124 0.00 LYS 127 -0.15 TRP 420

ASP 131 0.00 SER 128 -0.16 TRP 420

SER 128 0.00 ALA 129 -0.18 PRO 423

SER 128 0.00 GLU 130 -0.18 PRO 423

SER 128 0.00 ASP 131 -0.15 PRO 423

LYS 133 0.00 ALA 132 -0.16 PRO 423

ALA 134 0.00 LYS 133 -0.12 PRO 423

LYS 133 0.00 ALA 134 -0.13 PRO 423

PHE 76 0.00 ILE 135 -0.16 PRO 423

ASP 137 0.00 TYR 136 -0.14 PRO 423

PHE 138 0.00 ASP 137 -0.11 PRO 423

ILE 143 0.00 PHE 138 -0.13 PRO 423

ILE 143 0.00 THR 139 -0.16 PRO 423

ILE 143 0.00 ASP 140 -0.11 PRO 423

ILE 143 0.00 THR 141 -0.10 PRO 423

ILE 143 0.00 VAL 142 -0.13 PRO 423

VAL 142 0.00 ILE 143 -0.13 PRO 423

ASN 147 0.00 ARG 144 -0.08 PRO 423

ARG 188 0.00 ILE 145 -0.08 PRO 423

ASP 419 0.01 ARG 146 -0.12 PRO 423

ASP 419 0.03 ASN 147 -0.09 PRO 423

ASP 419 0.03 ARG 148 -0.04 PRO 423

ASP 419 0.04 HIS 149 -0.03 PRO 423

ASP 419 0.07 ASN 150 -0.06 PRO 423

ASP 419 0.09 ASP 151 -0.01 PRO 423

ASP 419 0.07 VAL 152 -0.01 PRO 423

ASP 419 0.11 ILE 153 -0.03 PRO 423

TRP 420 0.14 PRO 154 -0.00 THR 155

TRP 420 0.13 THR 155 -0.00 PRO 154

TRP 420 0.13 MET 156 -0.00 THR 155

TRP 420 0.19 ALA 157 -0.00 TYR 334

TRP 420 0.21 GLN 158 -0.00 VAL 160

PRO 423 0.21 GLY 159 -0.00 VAL 160

TRP 420 0.24 VAL 160 -0.00 GLY 159

TRP 420 0.28 ILE 161 -0.00 GLN 158

PRO 423 0.34 GLU 162 -0.00 THR 104

PRO 423 0.37 TYR 163 -0.00 LEU 101

PRO 423 0.43 LYS 164 -0.00 PHE 167

PRO 423 0.47 GLU 165 -0.00 LYS 164

PRO 423 0.53 SER 166 -0.00 PHE 167

PRO 423 0.57 PHE 167 -0.00 LYS 164

PRO 423 0.55 ASP 170 -0.00 SER 174

ALA 417 0.54 PRO 171 -0.00 VAL 172

VAL 422 0.42 VAL 172 -0.00 PRO 171

VAL 422 0.32 THR 173 -0.00 SER 174

ALA 417 0.36 SER 174 -0.00 THR 173

ALA 417 0.31 GLN 175 -0.00 THR 173

ALA 417 0.14 ASN 176 -0.00 TYR 411

ALA 417 0.19 VAL 177 -0.00 GLN 178

ALA 417 0.20 GLN 178 -0.02 PRO 423

ASP 419 0.08 TYR 179 -0.11 PRO 423

ASP 419 0.04 PHE 180 -0.05 PRO 423

ASP 419 0.10 LEU 181 -0.07 PRO 423

ASP 419 0.09 ASP 182 -0.20 PRO 423

ASP 419 0.01 ARG 183 -0.20 PRO 423

ASP 419 0.02 PHE 184 -0.12 PRO 423

ASP 419 0.06 TYR 185 -0.16 PRO 423

ASP 419 0.03 MET 186 -0.26 PRO 423

ARG 399 0.00 SER 187 -0.22 PRO 423

ASP 419 0.01 ARG 188 -0.17 PRO 423

ASP 419 0.03 ILE 189 -0.25 PRO 423

ILE 189 0.00 SER 190 -0.28 PRO 423

MET 193 0.00 ILE 191 -0.21 PRO 423

ASP 419 0.00 ARG 192 -0.20 PRO 423

ILE 191 0.00 MET 193 -0.27 PRO 423

LEU 195 0.00 LEU 194 -0.25 PRO 423

LEU 194 0.00 LEU 195 -0.20 PRO 423

ASP 419 0.00 ASN 196 -0.22 PRO 423

HIS 198 0.00 GLN 197 -0.27 PRO 423

LEU 201 0.00 HIS 198 -0.23 PRO 423

LEU 201 0.00 SER 199 -0.19 PRO 423

SER 218 0.00 LEU 200 -0.23 PRO 423

HIS 198 0.00 LEU 201 -0.25 PRO 423

LEU 201 0.00 PHE 202 -0.21 PRO 423

ASP 137 0.00 GLY 203 -0.18 PRO 423

ASP 419 0.02 HIS 215 -0.33 PRO 423

ASN 222 0.00 ILE 216 -0.33 PRO 423

SER 218 0.00 GLY 217 -0.29 PRO 423

ASP 419 0.02 SER 218 -0.30 PRO 423

ASP 419 0.02 ILE 219 -0.36 PRO 423

ASP 419 0.03 ASN 220 -0.38 PRO 423

ASP 419 0.01 PRO 221 -0.43 PRO 423

ASP 419 0.04 ASN 222 -0.44 PRO 423

ASP 419 0.06 CYS 223 -0.43 PRO 423

ASP 419 0.09 ASN 224 -0.43 PRO 423

ASP 419 0.11 VAL 225 -0.46 PRO 423

ASP 419 0.14 LEU 226 -0.45 PRO 423

ASP 419 0.13 GLU 227 -0.38 PRO 423

ASP 419 0.13 VAL 228 -0.37 PRO 423

ASP 419 0.16 ILE 229 -0.39 PRO 423

ASP 419 0.17 LYS 230 -0.35 PRO 423

ASP 419 0.15 ASP 231 -0.30 PRO 423

ASP 419 0.18 GLY 232 -0.30 PRO 423

ASP 419 0.20 TYR 233 -0.30 PRO 423

ASP 419 0.19 GLU 234 -0.25 PRO 423

ASP 419 0.19 ASN 235 -0.20 PRO 423

ASP 419 0.22 ALA 236 -0.20 PRO 423

ASP 419 0.22 ARG 237 -0.20 PRO 423

ASP 419 0.21 ARG 238 -0.14 PRO 423

ASP 419 0.22 LEU 239 -0.10 PRO 423

ASP 419 0.25 CYS 240 -0.12 PRO 423

ASP 419 0.24 ASP 241 -0.10 PRO 423

ASP 419 0.23 LEU 242 -0.04 PRO 423

TRP 420 0.26 TYR 243 -0.01 PRO 423

ASP 419 0.27 TYR 244 -0.04 PRO 423

ASP 419 0.25 ILE 245 -0.05 PRO 423

ASP 419 0.26 ASN 246 -0.12 PRO 423

ASP 419 0.26 SER 247 -0.18 PRO 423

ASP 419 0.27 PRO 248 -0.25 PRO 423

ASP 419 0.24 GLU 249 -0.30 PRO 423

ASP 419 0.23 LEU 250 -0.36 PRO 423

ASP 419 0.22 GLU 251 -0.43 PRO 423

ASP 419 0.20 LEU 252 -0.47 PRO 423

ASP 419 0.18 GLU 253 -0.54 PRO 423

ASP 419 0.15 GLU 254 -0.57 PRO 423

ASP 419 0.13 LEU 255 -0.63 PRO 423

ASP 419 0.10 ASN 256 -0.63 PRO 423

ASP 419 0.09 ALA 257 -0.70 PRO 423

ASP 419 0.06 LYS 258 -0.67 PRO 423

ASP 419 0.06 SER 259 -0.62 PRO 423

ASP 419 0.09 PRO 260 -0.62 PRO 423

ASP 419 0.10 GLY 261 -0.56 PRO 423

ASP 419 0.08 GLN 262 -0.54 PRO 423

ASP 419 0.09 PRO 263 -0.51 PRO 423

ASP 419 0.09 ILE 264 -0.54 PRO 423

ASP 419 0.07 GLN 265 -0.51 PRO 423

ASP 419 0.05 VAL 266 -0.52 PRO 423

ASP 419 0.02 VAL 267 -0.48 PRO 423

ASP 419 0.04 TYR 268 -0.44 PRO 423

ASP 419 0.05 VAL 269 -0.38 PRO 423

ASP 419 0.08 PRO 270 -0.36 PRO 423

ASP 419 0.09 SER 271 -0.30 PRO 423

ASP 419 0.10 HIS 272 -0.34 PRO 423

ASP 419 0.12 LEU 273 -0.40 PRO 423

ASP 419 0.14 TYR 274 -0.33 PRO 423

ASP 419 0.15 HIS 275 -0.28 PRO 423

ASP 419 0.15 HIS 275 -0.29 PRO 423

ASP 419 0.17 MET 276 -0.36 PRO 423

ASP 419 0.19 VAL 277 -0.37 PRO 423

ASP 419 0.20 PHE 278 -0.28 PRO 423

ASP 419 0.22 GLU 279 -0.25 PRO 423

ASP 419 0.25 LEU 280 -0.34 PRO 423

ASP 419 0.25 PHE 281 -0.30 PRO 423

ASP 419 0.26 LYS 282 -0.21 PRO 423

ASP 419 0.30 ASN 283 -0.23 PRO 423

ASP 419 0.31 ALA 284 -0.30 PRO 423

ASP 419 0.29 MET 285 -0.22 PRO 423

ASP 419 0.32 ARG 286 -0.13 PRO 423

ASP 419 0.36 ALA 287 -0.18 PRO 423

ASP 419 0.34 THR 288 -0.22 PRO 423

ASP 419 0.32 MET 289 -0.13 PRO 423

TRP 420 0.36 GLU 290 -0.06 PRO 423

ASP 419 0.38 HIS 291 -0.12 PRO 423

ASP 419 0.35 HIS 292 -0.14 PRO 423

TRP 420 0.34 ALA 293 -0.05 PRO 423

TRP 420 0.35 ASN 294 -0.03 PRO 423

ASP 419 0.33 ARG 295 -0.11 PRO 423

ASP 419 0.30 GLY 296 -0.11 PRO 423

ASP 419 0.30 VAL 297 -0.19 PRO 423

ASP 419 0.30 TYR 298 -0.23 PRO 423

ASP 419 0.30 PRO 299 -0.31 PRO 423

ASP 419 0.27 PRO 300 -0.35 PRO 423

ASP 419 0.27 ILE 301 -0.39 PRO 423

ASP 419 0.25 GLN 302 -0.47 PRO 423

ASP 419 0.22 VAL 303 -0.51 PRO 423

ASP 419 0.20 HIS 304 -0.59 PRO 423

ASP 419 0.16 VAL 305 -0.60 PRO 423

ASP 419 0.14 THR 306 -0.66 PRO 423

ASP 419 0.09 LEU 307 -0.66 PRO 423

ASP 419 0.08 GLY 308 -0.74 PRO 423

ASP 419 0.03 ASN 309 -0.74 PRO 423

ASP 419 0.02 GLU 310 -0.74 PRO 423

ASP 419 0.07 ASP 311 -0.73 PRO 423

ASP 419 0.10 LEU 312 -0.65 PRO 423

ASP 419 0.15 THR 313 -0.67 PRO 423

ASP 419 0.18 VAL 314 -0.59 PRO 423

ASP 419 0.23 LYS 315 -0.61 PRO 423

ASP 419 0.26 MET 316 -0.51 PRO 423

ASP 419 0.30 SER 317 -0.51 PRO 423

ASP 419 0.33 ASP 318 -0.41 PRO 423

ASP 419 0.35 ARG 319 -0.37 PRO 423

ASP 419 0.37 GLY 320 -0.28 PRO 423

ASP 419 0.42 GLY 321 -0.28 PRO 423

ASP 419 0.45 GLY 322 -0.34 PRO 423

ASP 419 0.51 VAL 323 -0.28 PRO 423

ASP 419 0.60 PRO 324 -0.33 PRO 423

ASP 419 0.64 LEU 325 -0.47 PRO 423

ASP 419 0.72 ARG 326 -0.26 PRO 423

ASP 419 0.60 LYS 327 -0.16 PRO 423

ASP 419 0.51 ILE 328 -0.32 PRO 423

ASP 419 0.47 ASP 329 -0.31 PRO 423

ASP 419 0.46 ARG 330 -0.10 PRO 423

ASP 419 0.38 LEU 331 -0.17 PRO 423

ASP 419 0.32 PHE 332 -0.22 PRO 423

ASP 419 0.34 ASN 333 -0.07 PRO 423

ALA 417 0.28 TYR 334 -0.00 ALA 157

ALA 417 0.36 MET 335 -0.00 PHE 167

TRP 420 0.42 TYR 336 -0.00 ILE 328

TRP 420 0.34 SER 337 -0.00 THR 338

TRP 420 0.32 THR 338 -0.00 SER 337

TRP 420 0.34 ALA 339 -0.00 PRO 340

TRP 420 0.32 PRO 340 -0.00 ALA 339

TRP 420 0.26 ARG 341 -0.00 ARG 348

TRP 420 0.26 PRO 342 -0.00 ARG 348

TRP 420 0.25 ARG 343 -0.00 HIS 149

TRP 420 0.22 VAL 344 -0.00 VAL 350

TRP 420 0.23 GLU 345 -0.00 ARG 348

TRP 420 0.24 THR 346 -0.00 SER 347

TRP 420 0.23 SER 347 -0.00 THR 346

TRP 420 0.26 ARG 348 -0.00 ALA 349

TRP 420 0.25 ALA 349 -0.00 ARG 348

TRP 420 0.25 VAL 350 -0.00 ARG 348

TRP 420 0.28 PRO 351 -0.00 PRO 342

ASP 419 0.27 LEU 352 -0.06 PRO 423

ASP 419 0.30 ALA 353 -0.03 PRO 423

TRP 420 0.30 GLY 354 -0.00 GLY 358

TRP 420 0.26 PHE 355 -0.00 MET 156

ASP 419 0.21 GLY 356 -0.01 PRO 423

ASP 419 0.22 TYR 357 -0.07 PRO 423

ASP 419 0.22 GLY 358 -0.16 PRO 423

ASP 419 0.25 LEU 359 -0.25 PRO 423

ASP 419 0.23 PRO 360 -0.24 PRO 423

ASP 419 0.17 ILE 361 -0.24 PRO 423

ASP 419 0.18 SER 362 -0.33 PRO 423

ASP 419 0.18 ARG 363 -0.41 PRO 423

ASP 419 0.11 LEU 364 -0.36 PRO 423

ASP 419 0.10 TYR 365 -0.38 PRO 423

ASP 419 0.11 ALA 366 -0.49 PRO 423

ASP 419 0.06 GLN 367 -0.51 PRO 423

ASP 419 0.02 TYR 368 -0.44 PRO 423

ASP 419 0.00 PHE 369 -0.50 PRO 423

GLY 371 0.00 GLN 370 -0.59 PRO 423

ASP 419 0.07 GLY 371 -0.61 PRO 423

ASP 419 0.13 ASP 372 -0.62 PRO 423

ASP 419 0.21 LEU 373 -0.57 PRO 423

ASP 419 0.28 LYS 374 -0.64 PRO 423

ASP 419 0.35 LEU 375 -0.58 PRO 423

ASP 419 0.41 TYR 376 -0.66 PRO 423

ASP 419 0.40 TYR 376 -0.67 PRO 423

ASP 419 0.45 SER 377 -0.55 PRO 423

ASP 419 0.47 LEU 378 -0.56 PRO 423

ASP 419 0.52 GLU 379 -0.39 PRO 423

ASP 419 0.47 GLY 380 -0.32 PRO 423

ASP 419 0.42 TYR 381 -0.41 PRO 423

ASP 419 0.40 GLY 382 -0.43 PRO 423

ASP 419 0.38 THR 383 -0.49 PRO 423

ASP 419 0.33 ASP 384 -0.59 PRO 423

ASP 419 0.29 ALA 385 -0.55 PRO 423

ASP 419 0.24 VAL 386 -0.63 PRO 423

ASP 419 0.18 ILE 387 -0.59 PRO 423

ASP 419 0.13 TYR 388 -0.66 PRO 423

ASP 419 0.08 ILE 389 -0.61 PRO 423

ASP 419 0.03 LYS 390 -0.64 PRO 423

ASP 419 0.03 ALA 391 -0.63 PRO 423

GLU 310 0.00 LEU 392 -0.61 PRO 423

VAL 267 0.00 SER 393 -0.54 PRO 423

VAL 267 0.00 THR 394 -0.56 PRO 423

ILE 389 0.00 ASP 395 -0.62 PRO 423

PHE 369 0.00 SER 396 -0.55 PRO 423

SER 396 0.00 ILE 397 -0.51 PRO 423

SER 58 0.00 GLU 398 -0.44 PRO 423

PRO 401 0.00 ARG 399 -0.45 PRO 423

PRO 401 0.00 LEU 400 -0.36 PRO 423

ARG 399 0.00 PRO 401 -0.29 PRO 423

ARG 86 0.00 VAL 402 -0.27 TRP 420

LYS 405 0.00 TYR 403 -0.25 ALA 417

LYS 405 0.00 ASN 404 -0.32 ALA 417

TYR 403 0.00 LYS 405 -0.39 ALA 417

LYS 405 0.00 ALA 406 -0.45 ALA 417

MET 91 0.00 ALA 407 -0.29 ALA 417

TYR 411 0.00 TRP 408 -0.25 ALA 417

HIS 410 0.00 LYS 409 -0.34 ALA 417

LYS 409 0.00 HIS 410 -0.25 ALA 417

PRO 423 0.05 TYR 411 -0.10 ASP 419

PRO 423 0.11 ASN 412 -0.18 ASP 419

PRO 423 0.06 THR 413 -0.21 ASP 419

VAL 422 0.11 ASN 414 -0.08 ASP 419

ARG 326 0.60 ALA 417 -0.45 ALA 406

ARG 326 0.29 ASP 418 -0.22 ALA 406

ARG 326 0.72 ASP 419 -0.36 LYS 405

ARG 326 0.65 TRP 420 -0.38 ALA 406

ASP 170 0.46 CYS 421 -0.39 GLU 310

ASP 170 0.55 VAL 422 -0.56 GLU 310

PHE 167 0.57 PRO 423 -0.74 GLU 310

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 7 ---

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 *