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

* *

CA distance fluctuations for 2604262204102534339

--- normal mode 9 ---

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
ASN 300 0.08 SER 1 -0.06 ASN 225

ASN 300 0.08 THR 2 -0.07 ASN 225

ASN 300 0.10 ALA 3 -0.06 ASN 225

ASN 300 0.10 GLY 4 -0.06 ILE 224

ASN 300 0.08 LYS 5 -0.07 GLN 244

ASN 300 0.07 VAL 6 -0.08 GLN 244

ASN 300 0.07 ILE 7 -0.08 GLN 244

ASN 300 0.05 LYS 8 -0.09 GLN 244

ASN 300 0.05 CYS 9 -0.10 ILE 224

ASN 300 0.04 LYS 10 -0.11 ASN 225

ASN 300 0.04 ALA 11 -0.12 ILE 224

ILE 23 0.03 ALA 12 -0.14 ILE 224

PRO 60 0.03 VAL 13 -0.14 GLN 244

PRO 60 0.06 LEU 14 -0.16 GLN 244

PRO 60 0.04 TRP 15 -0.16 GLN 244

PRO 60 0.06 GLU 16 -0.18 GLN 244

PRO 60 0.09 GLU 17 -0.19 GLN 244

PRO 60 0.07 LYS 18 -0.22 GLN 244

PRO 60 0.07 LYS 19 -0.20 GLN 244

PRO 60 0.06 PRO 20 -0.19 GLN 244

PRO 60 0.04 PHE 21 -0.17 ILE 224

PRO 60 0.03 SER 22 -0.16 GLN 244

ALA 12 0.03 ILE 23 -0.14 GLN 244

ALA 213 0.02 GLU 24 -0.13 GLN 244

ALA 213 0.03 GLU 25 -0.12 GLN 244

ALA 213 0.03 VAL 26 -0.11 GLN 244

ASN 300 0.05 GLU 27 -0.10 GLN 244

ASN 300 0.07 VAL 28 -0.09 GLN 244

ASN 300 0.08 ALA 29 -0.08 GLN 244

ASN 300 0.10 PRO 30 -0.07 ILE 224

ASN 300 0.13 PRO 31 -0.06 ILE 224

ASN 300 0.13 LYS 32 -0.06 ILE 224

ASN 300 0.16 ALA 33 -0.05 ILE 269

ASN 300 0.18 HIS 34 -0.05 ILE 269

ASN 300 0.17 GLU 35 -0.06 ILE 269

ASN 300 0.16 VAL 36 -0.05 ILE 224

ASN 300 0.14 ARG 37 -0.06 ILE 224

ASN 300 0.14 ILE 38 -0.06 ASN 225

ASN 300 0.12 LYS 39 -0.07 ASN 225

ASN 300 0.12 MET 40 -0.08 ASN 225

ASN 300 0.12 VAL 41 -0.07 ASN 225

ASN 300 0.12 ALA 42 -0.09 ASN 225

ASN 300 0.13 THR 43 -0.10 ASN 225

ASN 300 0.13 GLY 44 -0.12 ASN 225

ASN 300 0.10 ILE 45 -0.15 ASN 225

ASN 300 0.14 CYS 46 -0.17 ILE 269

PRO 296 0.13 ARG 47 -0.25 ILE 269

ASN 300 0.14 SER 48 -0.24 ILE 269

ASN 300 0.09 ASP 49 -0.19 ILE 269

THR 59 0.06 ASP 50 -0.21 ILE 224

GLY 365 0.06 HIS 51 -0.22 ARG 271

THR 59 0.09 VAL 52 -0.17 ARG 271

PRO 60 0.10 VAL 53 -0.20 ILE 224

PRO 60 0.05 SER 54 -0.21 GLN 244

GLY 108 0.05 GLY 55 -0.18 LYS 247

GLY 365 0.08 THR 56 -0.19 ARG 271

ASN 300 0.09 LEU 57 -0.16 ARG 271

LEU 116 0.07 VAL 58 -0.16 ASP 297

VAL 52 0.09 THR 59 -0.12 LYS 247

VAL 53 0.10 PRO 60 -0.12 LYS 247

PRO 60 0.09 LEU 61 -0.14 LYS 247

ARG 120 0.04 PRO 62 -0.14 GLN 244

ASN 300 0.03 VAL 63 -0.13 GLN 244

ASN 300 0.06 ILE 64 -0.13 ILE 224

ASN 300 0.08 ALA 65 -0.14 ILE 224

ASN 300 0.12 GLY 66 -0.13 ILE 269

ASN 300 0.18 HIS 67 -0.11 ILE 269

ASN 300 0.19 GLU 68 -0.09 ILE 269

ASN 300 0.17 ALA 69 -0.08 ASN 225

ASN 300 0.17 ALA 70 -0.06 ASN 225

ASN 300 0.15 GLY 71 -0.06 ASN 225

ASN 300 0.15 ILE 72 -0.05 ASN 225

ASN 300 0.15 VAL 73 -0.05 ASN 225

ASN 300 0.13 GLU 74 -0.06 ASN 225

ASN 300 0.14 SER 75 -0.05 ASN 225

ASN 300 0.15 ILE 76 -0.04 ASN 225

ASN 300 0.15 GLY 77 -0.05 ILE 224

ASN 300 0.15 GLU 78 -0.04 ASP 297

ASN 300 0.18 GLY 79 -0.03 ASP 297

ASN 300 0.19 VAL 80 -0.03 ILE 269

ASN 300 0.20 THR 81 -0.03 LYS 99

ASN 300 0.21 THR 82 -0.04 GLY 98

ASN 300 0.19 VAL 83 -0.03 GLY 98

ASN 300 0.17 ARG 84 -0.03 ASN 225

ASN 300 0.15 PRO 85 -0.04 ASN 225

ASN 300 0.15 GLY 86 -0.04 ASN 225

ASN 300 0.17 ASP 87 -0.03 ASN 225

ASN 300 0.18 LYS 88 -0.03 ASN 225

ASN 300 0.19 VAL 89 -0.04 ASN 225

ASN 300 0.21 ILE 90 -0.04 ASN 225

ASN 300 0.21 PRO 91 -0.06 ILE 269

ASN 300 0.26 LEU 92 -0.07 PHE 340

ASN 300 0.27 PHE 93 -0.09 ILE 269

ASN 300 0.33 THR 94 -0.08 PHE 340

ASN 300 0.31 PRO 95 -0.07 PHE 340

ASN 300 0.32 GLN 96 -0.08 PHE 340

ASN 300 0.30 CYS 97 -0.07 PHE 340

ASN 300 0.33 GLY 98 -0.07 PHE 340

ASN 300 0.33 LYS 99 -0.07 PHE 340

ASN 300 0.36 CYS 100 -0.07 PHE 340

ASN 300 0.41 ARG 101 -0.08 PHE 340

ASN 300 0.45 VAL 102 -0.09 PHE 340

ASN 300 0.40 CYS 103 -0.09 PHE 340

ASN 300 0.39 LYS 104 -0.09 LYS 339

ASN 300 0.45 HIS 105 -0.10 LYS 339

ASN 300 0.44 PRO 106 -0.12 LYS 339

ASN 300 0.50 GLU 107 -0.12 LYS 339

ASN 300 0.51 GLY 108 -0.10 PHE 340

ASN 300 0.46 ASN 109 -0.10 PHE 340

ASN 300 0.47 PHE 110 -0.09 PHE 340

ASN 300 0.40 CYS 111 -0.08 PHE 340

ASN 300 0.38 LEU 112 -0.07 PHE 340

ASN 300 0.30 LYS 113 -0.07 VAL 294

ASN 300 0.31 ASN 114 -0.08 VAL 294

ASN 300 0.26 ASP 115 -0.09 ILE 269

ASN 300 0.30 LEU 116 -0.11 VAL 294

ASN 300 0.33 SER 117 -0.15 PRO 296

ASN 300 0.22 MET 118 -0.16 PRO 296

ASN 300 0.17 PRO 119 -0.15 PRO 296

ASN 300 0.13 ARG 120 -0.12 PRO 296

ASN 300 0.12 GLY 121 -0.11 ILE 269

ASN 300 0.13 THR 122 -0.09 ILE 269

ASN 300 0.16 MET 123 -0.08 ILE 269

ASN 300 0.19 GLN 124 -0.07 ILE 269

ASN 300 0.15 ASP 125 -0.07 ASP 297

ASN 300 0.13 GLY 126 -0.08 ASP 297

ASN 300 0.10 THR 127 -0.08 GLN 244

ASN 300 0.09 SER 128 -0.09 GLN 244

ASN 300 0.09 ARG 129 -0.09 GLN 244

ASN 300 0.06 PHE 130 -0.10 GLN 244

GLY 134 0.05 THR 131 -0.11 GLN 244

ALA 213 0.03 CYS 132 -0.12 GLN 244

GLU 27 0.02 ARG 133 -0.13 GLN 244

ALA 29 0.05 GLY 134 -0.12 LYS 247

THR 127 0.02 LYS 135 -0.13 GLN 244

ALA 213 0.03 PRO 136 -0.11 LYS 247

ASN 300 0.03 ILE 137 -0.12 GLN 244

ASN 300 0.06 HIS 138 -0.12 GLN 244

ASN 300 0.11 HIS 139 -0.11 ILE 269

ASN 300 0.13 PHE 140 -0.12 ILE 269

ASN 300 0.20 LEU 141 -0.11 ILE 269

ASN 300 0.19 GLY 142 -0.09 ILE 269

ASN 300 0.17 THR 143 -0.10 ILE 269

ASN 300 0.12 SER 144 -0.11 ILE 269

ASN 300 0.13 THR 145 -0.10 ILE 224

ASN 300 0.08 PHE 146 -0.12 ILE 224

ASN 300 0.08 SER 147 -0.11 ILE 224

ASN 300 0.08 GLN 148 -0.10 ASN 225

ASN 300 0.10 TYR 149 -0.08 ASN 225

ASN 300 0.12 THR 150 -0.08 ILE 224

ASN 300 0.14 VAL 151 -0.07 ILE 224

ASN 300 0.17 VAL 152 -0.07 ILE 269

ASN 300 0.20 ASP 153 -0.06 ILE 269

ASN 300 0.22 GLU 154 -0.05 ILE 269

ASN 300 0.26 ILE 155 -0.05 PHE 340

ASN 300 0.25 SER 156 -0.06 ILE 269

ASN 300 0.23 VAL 157 -0.05 ILE 269

ASN 300 0.24 ALA 158 -0.04 GLY 98

ASN 300 0.22 LYS 159 -0.04 LYS 104

ASN 300 0.22 ILE 160 -0.05 PRO 106

ASN 300 0.20 ASP 161 -0.05 PRO 106

ASN 300 0.17 ALA 162 -0.04 PRO 106

ASN 300 0.17 ALA 163 -0.04 PRO 106

ASN 300 0.17 SER 164 -0.04 PRO 106

ASN 300 0.15 PRO 165 -0.03 PRO 106

ASN 300 0.16 LEU 166 -0.05 ASN 225

ASN 300 0.14 GLU 167 -0.06 ASN 225

ASN 300 0.16 LYS 168 -0.04 ASN 225

ASN 300 0.19 VAL 169 -0.03 ASN 225

ASN 300 0.18 CYS 170 -0.06 ASN 225

ASN 300 0.20 LEU 171 -0.07 PHE 340

ASN 300 0.24 ILE 172 -0.11 PHE 340

ASN 300 0.25 GLY 173 -0.09 PHE 340

ASN 300 0.27 CYS 174 -0.09 PHE 340

ASN 300 0.24 GLY 175 -0.09 PHE 340

ASN 300 0.25 PHE 176 -0.13 PHE 340

ASN 300 0.31 SER 177 -0.19 PHE 340

ASN 300 0.35 THR 178 -0.13 PHE 340

ASN 300 0.31 GLY 179 -0.10 PHE 340

ASN 300 0.30 TYR 180 -0.17 PHE 340

ASN 300 0.35 GLY 181 -0.16 PHE 340

ASN 300 0.38 SER 182 -0.10 PHE 340

ASN 300 0.32 ALA 183 -0.08 PHE 340

ASN 300 0.31 VAL 184 -0.12 PHE 340

ASN 300 0.37 LYS 185 -0.13 PHE 340

ASN 300 0.43 VAL 186 -0.10 PHE 340

ASN 300 0.37 ALA 187 -0.07 GLY 316

ASN 300 0.33 LYS 188 -0.08 PHE 340

ASN 300 0.27 VAL 189 -0.05 SER 364

ASN 300 0.23 THR 190 -0.05 SER 364

ASN 300 0.20 GLN 191 -0.06 SER 364

ASN 300 0.17 GLY 192 -0.07 SER 364

ASN 300 0.18 SER 193 -0.07 SER 364

ASN 300 0.16 THR 194 -0.09 SER 364

ASN 300 0.18 CYS 195 -0.09 SER 364

ASN 300 0.16 ALA 196 -0.12 SER 364

ASN 300 0.18 VAL 197 -0.12 ARG 47

ASN 300 0.12 PHE 198 -0.16 ARG 47

ASN 300 0.11 GLY 199 -0.21 ARG 47

ASN 300 0.10 LEU 200 -0.18 ARG 363

ASN 300 0.12 GLY 201 -0.19 ARG 47

ASN 300 0.17 GLY 202 -0.12 CYS 46

ASN 300 0.24 VAL 203 -0.11 CYS 46

ASN 300 0.20 GLY 204 -0.13 ARG 47

ASN 300 0.18 LEU 205 -0.09 ARG 47

ASN 300 0.23 SER 206 -0.06 PHE 340

ASN 300 0.25 VAL 207 -0.07 ARG 47

ASN 300 0.20 ILE 208 -0.08 SER 364

ASN 300 0.21 MET 209 -0.05 SER 364

ASN 300 0.25 GLY 210 -0.06 PHE 340

ASN 300 0.23 CYS 211 -0.06 SER 364

ASP 334 0.24 LYS 212 -0.06 SER 364

ASP 334 0.31 ALA 213 -0.04 SER 364

LYS 330 0.24 ALA 214 -0.04 SER 364

ASP 334 0.23 GLY 215 -0.06 SER 364

ASN 300 0.19 ALA 216 -0.07 SER 364

ASP 334 0.17 ALA 217 -0.08 SER 364

ASP 334 0.15 ARG 218 -0.10 SER 364

ASP 334 0.14 ILE 219 -0.11 SER 364

ASP 334 0.12 ILE 220 -0.13 SER 364

ASP 334 0.10 GLY 221 -0.15 SER 364

ASP 334 0.08 VAL 222 -0.19 SER 364

ASP 334 0.05 ASP 223 -0.26 SER 364

GLU 107 0.04 ILE 224 -0.33 SER 364

ASP 334 0.04 ASN 225 -0.37 GLY 365

PHE 340 0.07 LYS 226 -0.30 GLY 365

PHE 340 0.05 ASP 227 -0.33 GLU 366

SER 298 0.06 LYS 228 -0.21 GLU 366

PHE 340 0.08 PHE 229 -0.20 GLY 365

PHE 340 0.11 ALA 230 -0.17 GLU 366

PHE 340 0.11 LYS 231 -0.16 ILE 368

ASN 300 0.11 ALA 232 -0.14 ILE 368

PHE 340 0.15 LYS 233 -0.12 GLY 365

PHE 340 0.19 GLU 234 -0.10 ILE 368

PHE 340 0.20 VAL 235 -0.08 ILE 368

PHE 340 0.19 GLY 236 -0.08 SER 364

ASP 334 0.14 ALA 237 -0.12 SER 364

ASP 334 0.15 THR 238 -0.12 SER 364

ASP 334 0.12 GLU 239 -0.15 SER 364

ASP 334 0.10 CYS 240 -0.18 SER 364

ASP 334 0.09 VAL 241 -0.21 SER 364

ASP 334 0.07 ASN 242 -0.26 SER 364

ASP 334 0.06 PRO 243 -0.25 SER 364

ASP 334 0.05 GLN 244 -0.29 SER 364

ASP 334 0.07 ASP 245 -0.26 SER 364

ASP 334 0.07 TYR 246 -0.22 SER 364

ASP 334 0.06 LYS 247 -0.27 GLN 299

PRO 106 0.07 LYS 248 -0.26 GLN 299

PRO 106 0.07 PRO 249 -0.25 GLN 299

PRO 106 0.08 ILE 250 -0.19 GLN 299

PRO 106 0.09 GLN 251 -0.18 SER 302

PRO 106 0.09 GLU 252 -0.18 SER 302

PRO 106 0.08 VAL 253 -0.17 SER 364

PRO 106 0.09 LEU 254 -0.16 SER 364

PRO 106 0.11 THR 255 -0.13 SER 364

PRO 106 0.10 GLU 256 -0.14 SER 364

ASP 334 0.10 MET 257 -0.16 SER 364

PRO 106 0.11 SER 258 -0.13 SER 364

PRO 106 0.12 ASN 259 -0.13 SER 364

PRO 106 0.13 GLY 260 -0.11 SER 364

PRO 106 0.13 GLY 261 -0.11 SER 364

ASN 300 0.15 VAL 262 -0.10 SER 364

ASN 300 0.21 ASP 263 -0.08 SER 364

ASN 300 0.26 PHE 264 -0.07 ARG 363

ASN 300 0.25 SER 265 -0.09 ARG 47

ASN 300 0.29 PHE 266 -0.10 ARG 47

ASN 300 0.27 GLU 267 -0.14 SER 48

ASN 300 0.26 VAL 268 -0.17 ARG 47

ASN 300 0.15 ILE 269 -0.25 ARG 47

ASN 300 0.22 GLY 270 -0.21 HIS 51

GLU 107 0.08 ARG 271 -0.22 HIS 51

GLU 107 0.11 LEU 272 -0.18 GLN 299

GLU 107 0.10 ASP 273 -0.24 GLN 299

GLU 107 0.08 THR 274 -0.16 HIS 51

ASN 300 0.22 MET 275 -0.17 PRO 295

GLU 107 0.12 VAL 276 -0.14 SER 54

GLU 107 0.09 THR 277 -0.15 SER 54

ASN 300 0.16 ALA 278 -0.12 HIS 51

ASN 300 0.23 LEU 279 -0.11 SER 54

PRO 106 0.11 SER 280 -0.11 SER 54

PRO 106 0.11 CYS 281 -0.12 SER 54

ASN 300 0.17 CYS 282 -0.09 SER 54

ASN 300 0.16 GLN 283 -0.08 SER 364

ASN 300 0.16 GLU 284 -0.08 SER 54

ASN 300 0.19 ALA 285 -0.06 SER 54

ASN 300 0.25 TYR 286 -0.06 SER 364

ASN 300 0.25 GLY 287 -0.06 SER 364

ASN 300 0.34 VAL 288 -0.05 SER 54

ASN 300 0.38 SER 289 -0.07 HIS 51

ASN 300 0.46 VAL 290 -0.07 VAL 294

ASN 300 0.52 ILE 291 -0.10 VAL 294

ASN 300 0.44 VAL 292 -0.09 SER 48

ASN 300 0.42 GLY 293 -0.12 SER 117

ASN 300 0.39 VAL 294 -0.14 SER 117

GLY 365 0.17 PRO 295 -0.17 MET 275

ASN 300 0.20 PRO 296 -0.16 MET 118

GLY 365 0.12 ASP 297 -0.16 VAL 58

VAL 294 0.18 SER 298 -0.11 MET 118

GLY 316 0.39 GLN 299 -0.27 LYS 247

GLY 316 0.69 ASN 300 -0.24 LYS 247

GLY 316 0.29 LEU 301 -0.20 PRO 249

GLU 107 0.21 SER 302 -0.25 PRO 249

GLU 107 0.17 MET 303 -0.13 LYS 248

GLU 107 0.15 ASN 304 -0.08 SER 54

ASN 300 0.19 PRO 305 -0.10 SER 298

PRO 106 0.14 MET 306 -0.08 SER 54

ASN 300 0.17 LEU 307 -0.08 SER 54

ASN 300 0.28 LEU 308 -0.09 PRO 295

ASN 300 0.21 LEU 309 -0.07 PRO 295

ASN 300 0.18 SER 310 -0.07 SER 54

ASN 300 0.25 GLY 311 -0.06 PRO 295

ASN 300 0.30 ARG 312 -0.07 PRO 295

ASN 300 0.41 THR 313 -0.07 VAL 294

ASN 300 0.53 TRP 314 -0.09 VAL 294

ASN 300 0.62 LYS 315 -0.06 VAL 294

ASN 300 0.69 GLY 316 -0.07 PHE 340

ASN 300 0.59 ALA 317 -0.09 PHE 340

ASN 300 0.50 ILE 318 -0.10 PHE 340

ASN 300 0.40 PHE 319 -0.12 PHE 340

ASN 300 0.41 GLY 320 -0.14 PHE 340

ASN 300 0.47 GLY 321 -0.13 PHE 340

ASN 300 0.39 PHE 322 -0.15 PHE 340

ASN 300 0.37 LYS 323 -0.13 PHE 340

ASN 300 0.32 SER 324 -0.12 PHE 340

ASN 300 0.29 LYS 325 -0.08 PHE 340

ASN 300 0.30 ASP 326 -0.09 PRO 106

ASN 300 0.31 SER 327 -0.11 PHE 340

ASN 300 0.28 VAL 328 -0.10 PHE 340

ASN 300 0.26 PRO 329 -0.06 PRO 106

ASN 300 0.27 LYS 330 -0.08 LYS 339

ASN 300 0.27 LEU 331 -0.11 LYS 339

ASN 300 0.23 VAL 332 -0.05 PRO 106

ALA 213 0.25 ALA 333 -0.06 PRO 106

ALA 213 0.31 ASP 334 -0.08 PRO 106

ASN 300 0.20 PHE 335 -0.07 PRO 106

ASN 300 0.19 MET 336 -0.05 PRO 106

ASN 300 0.18 ALA 337 -0.08 PRO 106

ASN 300 0.15 LYS 338 -0.09 PRO 106

ASN 300 0.17 LYS 339 -0.13 PHE 322

VAL 235 0.20 PHE 340 -0.19 SER 177

ASN 300 0.15 ALA 341 -0.09 SER 177

ASN 300 0.17 LEU 342 -0.05 SER 177

ASN 300 0.14 ASP 343 -0.05 LYS 338

ASN 300 0.13 PRO 344 -0.03 MET 209

ASN 300 0.15 LEU 345 -0.04 ASP 227

ASN 300 0.12 ILE 346 -0.07 ASP 227

ASN 300 0.10 THR 347 -0.11 ASP 227

PRO 295 0.08 HIS 348 -0.12 ASP 227

ASN 300 0.08 VAL 349 -0.11 ASN 225

ASN 300 0.06 LEU 350 -0.13 ASN 225

ASN 300 0.05 PRO 351 -0.11 ASN 225

ASN 300 0.06 PHE 352 -0.12 ASN 225

PHE 21 0.03 GLU 353 -0.13 ASN 225

PRO 295 0.04 LYS 354 -0.15 ASN 225

PRO 296 0.04 ILE 355 -0.16 ASN 225

PRO 296 0.04 ASN 356 -0.18 ASN 225

PRO 296 0.05 GLU 357 -0.19 ASN 225

PRO 295 0.06 GLY 358 -0.19 ASN 225

PRO 296 0.07 PHE 359 -0.21 ASN 225

PRO 296 0.07 ASP 360 -0.24 ASN 225

PRO 295 0.09 LEU 361 -0.25 ASN 225

PRO 295 0.11 LEU 362 -0.27 ASN 225

PRO 296 0.11 ARG 363 -0.30 ASN 225

PRO 295 0.12 SER 364 -0.36 ASN 225

PRO 295 0.17 GLY 365 -0.37 ASN 225

PRO 295 0.16 GLU 366 -0.33 ASP 227

PRO 295 0.12 SER 367 -0.21 ASP 227

PRO 295 0.14 ILE 368 -0.19 ASP 227

ASN 300 0.12 ARG 369 -0.14 ASN 225

ASN 300 0.09 THR 370 -0.15 ASN 225

ASN 300 0.11 ILE 371 -0.11 ASN 225

ASN 300 0.09 LEU 372 -0.11 ASN 225

ASN 300 0.09 THR 373 -0.09 ASN 225

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.

*** ***

CA distance fluctuations for 2604262204102534339

--- normal mode 9 ---

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

* *