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 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
ASN 300 0.11 SER 1 -0.02 GLU 234

ASN 300 0.11 THR 2 -0.02 GLN 148

ASN 300 0.14 ALA 3 -0.02 GLU 234

ASN 300 0.14 GLY 4 -0.02 ALA 213

ASN 300 0.13 LYS 5 -0.01 ALA 214

ASN 300 0.12 VAL 6 -0.01 ALA 214

ASN 300 0.10 ILE 7 -0.01 ILE 269

ASN 300 0.08 LYS 8 -0.02 ILE 269

ASN 300 0.07 CYS 9 -0.02 ILE 269

ASN 300 0.05 LYS 10 -0.03 ILE 269

ASN 300 0.05 ALA 11 -0.03 ILE 318

LYS 231 0.05 ALA 12 -0.04 TRP 314

ASP 227 0.05 VAL 13 -0.04 TRP 314

ASP 227 0.07 LEU 14 -0.05 TRP 314

ASP 227 0.07 TRP 15 -0.05 TRP 314

ASP 227 0.09 GLU 16 -0.06 LEU 308

ASN 225 0.11 GLU 17 -0.10 GLN 299

ASP 227 0.12 LYS 18 -0.17 GLN 299

ASP 227 0.10 LYS 19 -0.14 GLN 299

ASP 227 0.09 PRO 20 -0.13 GLN 299

ASP 227 0.07 PHE 21 -0.08 GLN 299

ALA 230 0.06 SER 22 -0.06 GLN 299

LYS 231 0.05 ILE 23 -0.04 GLN 299

ALA 230 0.04 GLU 24 -0.03 TRP 314

ASN 300 0.04 GLU 25 -0.03 TRP 314

ASN 300 0.07 VAL 26 -0.02 TRP 314

ASN 300 0.09 GLU 27 -0.02 GLY 321

ASN 300 0.12 VAL 28 -0.02 GLY 321

ASN 300 0.14 ALA 29 -0.02 ALA 214

ASN 300 0.16 PRO 30 -0.02 ALA 214

ASN 300 0.19 PRO 31 -0.02 ALA 214

ASN 300 0.21 LYS 32 -0.03 ALA 214

ASN 300 0.23 ALA 33 -0.03 ALA 213

ASN 300 0.25 HIS 34 -0.04 ALA 213

ASN 300 0.23 GLU 35 -0.03 ALA 213

ASN 300 0.20 VAL 36 -0.03 ALA 213

ASN 300 0.17 ARG 37 -0.02 ALA 213

ASN 300 0.16 ILE 38 -0.02 VAL 235

ASN 300 0.13 LYS 39 -0.03 ILE 269

ASN 300 0.11 MET 40 -0.03 ILE 269

ASN 300 0.10 VAL 41 -0.04 ILE 269

ASN 300 0.09 ALA 42 -0.05 ILE 269

ASN 300 0.09 THR 43 -0.05 ILE 269

ASN 300 0.08 GLY 44 -0.07 ILE 269

LYS 231 0.06 ILE 45 -0.09 ILE 269

GLY 202 0.10 CYS 46 -0.08 ILE 269

GLY 201 0.15 ARG 47 -0.12 GLY 293

GLY 201 0.13 SER 48 -0.10 ILE 318

GLY 201 0.09 ASP 49 -0.08 ILE 318

ASP 227 0.11 ASP 50 -0.09 GLN 299

ASN 225 0.13 HIS 51 -0.10 ASP 297

ASN 225 0.10 VAL 52 -0.07 TRP 314

ASN 225 0.11 VAL 53 -0.09 GLN 299

ASN 225 0.14 SER 54 -0.18 GLN 299

ASN 225 0.13 GLY 55 -0.09 TRP 314

ILE 224 0.14 THR 56 -0.10 TRP 314

ILE 224 0.11 LEU 57 -0.11 TRP 314

GLN 299 0.14 VAL 58 -0.10 TRP 314

GLN 299 0.16 THR 59 -0.09 ILE 318

ASN 300 0.12 PRO 60 -0.07 ILE 318

GLN 244 0.08 LEU 61 -0.06 TRP 314

ASN 225 0.07 PRO 62 -0.05 TRP 314

ASN 300 0.09 VAL 63 -0.05 ILE 318

ASN 300 0.10 ILE 64 -0.04 ILE 318

ASN 300 0.10 ALA 65 -0.05 ILE 318

ASN 300 0.12 GLY 66 -0.05 ILE 318

ASN 300 0.18 HIS 67 -0.04 ILE 318

ASN 300 0.16 GLU 68 -0.04 ILE 269

ASN 300 0.15 ALA 69 -0.04 ILE 269

ASN 300 0.15 ALA 70 -0.04 ILE 269

ASN 300 0.14 GLY 71 -0.03 ILE 269

ASN 300 0.15 ILE 72 -0.03 GLU 234

ASN 300 0.16 VAL 73 -0.03 GLU 234

ASN 300 0.15 GLU 74 -0.03 GLU 234

ASN 300 0.16 SER 75 -0.03 GLU 234

ASN 300 0.19 ILE 76 -0.03 ALA 213

ASN 300 0.20 GLY 77 -0.03 ALA 213

ASN 300 0.21 GLU 78 -0.03 ALA 213

ASN 300 0.23 GLY 79 -0.04 ALA 213

ASN 300 0.23 VAL 80 -0.04 ALA 213

ASN 300 0.23 THR 81 -0.05 ALA 213

ASN 300 0.24 THR 82 -0.05 ALA 213

ASN 300 0.21 VAL 83 -0.05 GLU 234

ASN 300 0.19 ARG 84 -0.05 GLU 234

ASN 300 0.16 PRO 85 -0.04 GLU 234

ASN 300 0.15 GLY 86 -0.05 GLU 234

ASN 300 0.17 ASP 87 -0.05 GLU 234

ASN 300 0.16 LYS 88 -0.05 GLU 234

ASN 300 0.19 VAL 89 -0.04 GLU 234

ASN 300 0.20 ILE 90 -0.03 VAL 235

ASN 300 0.22 PRO 91 -0.02 ALA 213

ASN 300 0.27 LEU 92 -0.04 ALA 214

ASN 300 0.30 PHE 93 -0.05 GLY 321

ASN 300 0.37 THR 94 -0.06 GLY 321

ASN 300 0.36 PRO 95 -0.06 ALA 214

ASN 300 0.36 GLN 96 -0.07 ALA 214

ASN 300 0.36 CYS 97 -0.07 ALA 214

ASN 300 0.36 GLY 98 -0.09 ALA 213

ASN 300 0.39 LYS 99 -0.08 ALA 214

ASN 300 0.44 CYS 100 -0.08 ALA 214

ASN 300 0.48 ARG 101 -0.08 ALA 214

ASN 300 0.49 VAL 102 -0.09 LYS 185

ASN 300 0.42 CYS 103 -0.10 ALA 214

ASN 300 0.41 LYS 104 -0.11 ALA 214

ASN 300 0.45 HIS 105 -0.12 ALA 214

ASN 300 0.40 PRO 106 -0.15 ALA 214

ASN 300 0.43 GLU 107 -0.17 LYS 185

ASN 300 0.49 GLY 108 -0.12 LYS 185

ASN 300 0.44 ASN 109 -0.11 LYS 185

ASN 300 0.50 PHE 110 -0.08 SER 117

ASN 300 0.46 CYS 111 -0.07 LYS 185

ASN 300 0.49 LEU 112 -0.06 LYS 185

ASN 300 0.42 LYS 113 -0.05 ALA 214

ASN 300 0.42 ASN 114 -0.06 LYS 185

ASN 300 0.37 ASP 115 -0.06 GLY 321

ASN 300 0.40 LEU 116 -0.08 GLY 321

ASN 300 0.51 SER 117 -0.08 PHE 110

GLN 299 0.42 MET 118 -0.06 VAL 186

ASN 300 0.31 PRO 119 -0.06 GLY 321

ASN 300 0.27 ARG 120 -0.05 GLY 321

ASN 300 0.22 GLY 121 -0.05 GLY 321

ASN 300 0.23 THR 122 -0.04 GLY 321

ASN 300 0.25 MET 123 -0.03 ALA 214

ASN 300 0.29 GLN 124 -0.04 ALA 214

ASN 300 0.26 ASP 125 -0.04 ALA 214

ASN 300 0.25 GLY 126 -0.03 LYS 185

ASN 300 0.20 THR 127 -0.03 GLY 321

ASN 300 0.17 SER 128 -0.03 GLY 321

ASN 300 0.16 ARG 129 -0.02 GLY 321

ASN 300 0.12 PHE 130 -0.02 GLY 321

ASN 300 0.09 THR 131 -0.02 GLY 321

ASN 300 0.06 CYS 132 -0.03 TRP 314

ASN 300 0.05 ARG 133 -0.03 TRP 314

ASN 300 0.07 GLY 134 -0.03 TRP 314

ASN 300 0.07 LYS 135 -0.03 TRP 314

ASN 300 0.10 PRO 136 -0.03 GLY 321

ASN 300 0.10 ILE 137 -0.03 ILE 318

ASN 300 0.14 HIS 138 -0.04 GLY 321

ASN 300 0.18 HIS 139 -0.04 GLY 321

ASN 300 0.19 PHE 140 -0.05 ILE 318

ASN 300 0.27 LEU 141 -0.05 GLY 321

ASN 300 0.26 GLY 142 -0.04 GLY 321

ASN 300 0.21 THR 143 -0.03 GLY 321

ASN 300 0.16 SER 144 -0.03 GLY 321

ASN 300 0.13 THR 145 -0.03 ILE 318

ASN 300 0.08 PHE 146 -0.03 ILE 318

ASN 300 0.09 SER 147 -0.03 ILE 269

ASN 300 0.09 GLN 148 -0.03 ILE 269

ASN 300 0.12 TYR 149 -0.02 ILE 269

ASN 300 0.15 THR 150 -0.02 GLY 321

ASN 300 0.18 VAL 151 -0.02 ALA 214

ASN 300 0.22 VAL 152 -0.03 ALA 214

ASN 300 0.26 ASP 153 -0.04 ALA 214

ASN 300 0.26 GLU 154 -0.05 ALA 213

ASN 300 0.30 ILE 155 -0.05 ALA 213

ASN 300 0.29 SER 156 -0.04 ALA 213

ASN 300 0.25 VAL 157 -0.04 ALA 213

ASN 300 0.24 ALA 158 -0.05 ALA 213

ASN 300 0.21 LYS 159 -0.06 GLU 234

ASN 300 0.19 ILE 160 -0.07 GLU 234

ASN 300 0.17 ASP 161 -0.08 GLU 234

ASN 300 0.15 ALA 162 -0.08 GLU 234

ASN 300 0.13 ALA 163 -0.09 GLU 234

ASN 300 0.13 SER 164 -0.09 GLU 234

ASN 300 0.11 PRO 165 -0.07 LYS 228

ASN 300 0.12 LEU 166 -0.05 LYS 228

ASN 300 0.09 GLU 167 -0.06 ILE 269

ASN 300 0.10 LYS 168 -0.08 LYS 228

ASN 300 0.14 VAL 169 -0.06 LYS 228

ASN 300 0.14 CYS 170 -0.05 ILE 269

ASN 300 0.14 LEU 171 -0.06 ILE 269

ASN 300 0.19 ILE 172 -0.04 VAL 235

ASN 300 0.21 GLY 173 -0.03 ILE 269

ASN 300 0.22 CYS 174 -0.03 SER 177

ASN 300 0.17 GLY 175 -0.06 ILE 269

ASN 300 0.18 PHE 176 -0.06 SER 327

ASN 300 0.23 SER 177 -0.07 PHE 322

ASN 300 0.26 THR 178 -0.05 CYS 46

ASN 300 0.22 GLY 179 -0.05 PHE 322

ASN 300 0.21 TYR 180 -0.09 PHE 322

ASN 300 0.26 GLY 181 -0.09 PHE 322

ASN 300 0.28 SER 182 -0.05 ARG 363

ASN 300 0.23 ALA 183 -0.07 PRO 106

ASN 300 0.23 VAL 184 -0.14 GLU 107

ASN 300 0.27 LYS 185 -0.17 GLU 107

ASN 300 0.31 VAL 186 -0.08 VAL 58

ASN 300 0.26 ALA 187 -0.07 VAL 58

ASN 300 0.24 LYS 188 -0.13 GLU 107

ASN 300 0.20 VAL 189 -0.11 PRO 106

ASN 300 0.18 THR 190 -0.13 PRO 106

ASN 300 0.15 GLN 191 -0.13 PRO 106

ASN 300 0.12 GLY 192 -0.10 PRO 106

ASN 300 0.13 SER 193 -0.09 PRO 106

ASN 300 0.11 THR 194 -0.07 PRO 106

ASN 300 0.12 CYS 195 -0.05 PRO 106

ASN 300 0.10 ALA 196 -0.03 PHE 340

ASN 300 0.11 VAL 197 -0.05 THR 274

ILE 269 0.09 PHE 198 -0.10 THR 274

THR 56 0.09 GLY 199 -0.11 THR 274

THR 56 0.10 LEU 200 -0.09 PRO 344

ARG 47 0.15 GLY 201 -0.10 THR 274

ARG 47 0.13 GLY 202 -0.08 LEU 345

ASN 300 0.15 VAL 203 -0.06 ILE 269

ASN 300 0.12 GLY 204 -0.06 PHE 340

ASN 300 0.11 LEU 205 -0.11 PHE 340

ASN 300 0.15 SER 206 -0.08 LEU 331

ASN 300 0.18 VAL 207 -0.06 SER 327

ASN 300 0.14 ILE 208 -0.08 PHE 340

ASN 300 0.14 MET 209 -0.10 LEU 331

ASN 300 0.18 GLY 210 -0.10 PRO 106

ASN 300 0.17 CYS 211 -0.09 PRO 106

ASN 300 0.14 LYS 212 -0.11 PRO 106

ASN 300 0.16 ALA 213 -0.13 PRO 106

ASN 300 0.17 ALA 214 -0.15 PRO 106

ASN 300 0.14 GLY 215 -0.13 PRO 106

ASN 300 0.13 ALA 216 -0.10 PRO 106

ASN 300 0.10 ALA 217 -0.09 PRO 106

ASN 300 0.09 ARG 218 -0.07 PRO 106

ASN 300 0.09 ILE 219 -0.06 LYS 339

ASN 300 0.06 ILE 220 -0.07 PHE 340

THR 56 0.07 GLY 221 -0.08 PHE 340

THR 56 0.08 VAL 222 -0.07 THR 277

THR 56 0.12 ASP 223 -0.09 ASP 273

THR 56 0.14 ILE 224 -0.10 ASP 273

THR 56 0.14 ASN 225 -0.11 PRO 344

SER 54 0.12 LYS 226 -0.11 PRO 344

GLY 365 0.19 ASP 227 -0.14 PRO 344

GLY 365 0.13 LYS 228 -0.16 PRO 344

GLY 365 0.12 PHE 229 -0.11 PHE 340

GLU 366 0.18 ALA 230 -0.13 PHE 340

GLU 366 0.20 LYS 231 -0.16 PHE 340

GLU 366 0.11 ALA 232 -0.14 PHE 340

GLU 366 0.12 LYS 233 -0.15 PHE 340

GLU 366 0.14 GLU 234 -0.20 PHE 340

GLU 366 0.11 VAL 235 -0.23 PHE 340

ASN 300 0.09 GLY 236 -0.16 PHE 340

ASN 300 0.08 ALA 237 -0.12 PHE 340

GLU 366 0.07 THR 238 -0.11 LYS 339

SER 54 0.06 GLU 239 -0.09 LYS 339

SER 54 0.08 CYS 240 -0.09 PHE 340

THR 56 0.09 VAL 241 -0.08 PHE 340

THR 56 0.11 ASN 242 -0.07 PHE 340

THR 56 0.11 PRO 243 -0.09 SER 302

THR 56 0.14 GLN 244 -0.09 SER 302

THR 56 0.12 ASP 245 -0.08 SER 302

THR 56 0.11 TYR 246 -0.08 SER 302

THR 56 0.11 LYS 247 -0.08 SER 302

THR 56 0.10 LYS 248 -0.09 ASN 304

SER 117 0.10 PRO 249 -0.12 ASN 304

ILE 269 0.09 ILE 250 -0.09 ASN 304

SER 117 0.07 GLN 251 -0.10 ASN 304

SER 117 0.06 GLU 252 -0.10 ASN 304

ILE 269 0.06 VAL 253 -0.08 ASN 304

ILE 269 0.06 LEU 254 -0.06 ASN 304

ILE 269 0.04 THR 255 -0.07 ASN 304

ILE 269 0.04 GLU 256 -0.07 ASN 304

ILE 269 0.05 MET 257 -0.05 ASN 304

ASN 300 0.06 SER 258 -0.04 ASN 304

ASN 300 0.04 ASN 259 -0.05 ASN 304

ASN 300 0.05 GLY 260 -0.05 ASN 304

ASN 300 0.07 GLY 261 -0.04 ASN 304

ASN 300 0.10 VAL 262 -0.03 PRO 106

ASN 300 0.14 ASP 263 -0.05 PRO 106

ASN 300 0.17 PHE 264 -0.04 ARG 363

ASN 300 0.16 SER 265 -0.06 GLY 365

ASN 300 0.19 PHE 266 -0.07 GLY 365

ASN 300 0.17 GLU 267 -0.11 GLY 365

ASN 300 0.17 VAL 268 -0.11 GLY 365

PRO 243 0.10 ILE 269 -0.19 GLY 365

SER 117 0.14 GLY 270 -0.19 GLY 365

SER 117 0.15 ARG 271 -0.24 GLY 365

SER 117 0.17 LEU 272 -0.21 SER 364

SER 117 0.15 ASP 273 -0.21 GLY 365

SER 117 0.11 THR 274 -0.19 GLY 365

ASN 300 0.14 MET 275 -0.15 GLY 365

ARG 101 0.13 VAL 276 -0.15 GLY 365

ARG 101 0.09 THR 277 -0.13 GLY 365

ASN 300 0.11 ALA 278 -0.11 GLY 365

ASN 300 0.15 LEU 279 -0.11 GLY 365

ARG 101 0.07 SER 280 -0.10 GLY 365

ASN 300 0.07 CYS 281 -0.07 GLY 365

ASN 300 0.11 CYS 282 -0.06 SER 364

ASN 300 0.10 GLN 283 -0.05 SER 364

ASN 300 0.09 GLU 284 -0.07 SER 364

ASN 300 0.10 ALA 285 -0.07 PRO 296

ASN 300 0.14 TYR 286 -0.07 PRO 296

ASN 300 0.15 GLY 287 -0.06 PRO 296

ASN 300 0.21 VAL 288 -0.07 PRO 296

ASN 300 0.24 SER 289 -0.08 SER 364

ASN 300 0.31 VAL 290 -0.08 ARG 363

ASN 300 0.36 ILE 291 -0.11 ARG 363

ASN 300 0.32 VAL 292 -0.10 ARG 363

ASN 300 0.31 GLY 293 -0.13 ARG 363

ASN 300 0.30 VAL 294 -0.14 ARG 363

SER 117 0.18 PRO 295 -0.14 ARG 363

SER 117 0.26 PRO 296 -0.12 TRP 314

SER 117 0.26 ASP 297 -0.17 ARG 363

SER 117 0.28 SER 298 -0.15 SER 364

SER 117 0.50 GLN 299 -0.30 SER 364

GLY 316 0.52 ASN 300 -0.22 SER 364

GLY 316 0.30 LEU 301 -0.19 SER 364

ARG 101 0.27 SER 302 -0.18 SER 364

ARG 101 0.23 MET 303 -0.15 SER 364

ARG 101 0.21 ASN 304 -0.13 SER 364

HIS 105 0.20 PRO 305 -0.14 SER 364

HIS 105 0.15 MET 306 -0.11 SER 364

HIS 105 0.14 LEU 307 -0.11 SER 364

PRO 106 0.15 LEU 308 -0.11 SER 364

PRO 106 0.13 LEU 309 -0.10 SER 364

ASN 300 0.09 SER 310 -0.08 SER 364

ASN 300 0.13 GLY 311 -0.09 PRO 296

ASN 300 0.16 ARG 312 -0.09 PRO 296

ASN 300 0.24 THR 313 -0.10 PRO 296

ASN 300 0.33 TRP 314 -0.12 PRO 296

ASN 300 0.42 LYS 315 -0.10 LEU 57

ASN 300 0.52 GLY 316 -0.10 LEU 57

ASN 300 0.47 ALA 317 -0.10 LEU 57

ASN 300 0.43 ILE 318 -0.10 SER 48

ASN 300 0.33 PHE 319 -0.07 SER 48

ASN 300 0.31 GLY 320 -0.06 VAL 58

ASN 300 0.38 GLY 321 -0.08 ASN 109

ASN 300 0.33 PHE 322 -0.09 GLY 181

ASN 300 0.35 LYS 323 -0.10 ALA 214

ASN 300 0.32 SER 324 -0.08 ALA 213

ASN 300 0.30 LYS 325 -0.08 ALA 213

ASN 300 0.29 ASP 326 -0.11 ALA 213

ASN 300 0.27 SER 327 -0.12 ALA 213

ASN 300 0.25 VAL 328 -0.08 ALA 213

ASN 300 0.23 PRO 329 -0.08 VAL 235

ASN 300 0.23 LYS 330 -0.10 ALA 213

ASN 300 0.21 LEU 331 -0.11 VAL 235

ASN 300 0.18 VAL 332 -0.10 VAL 235

ASN 300 0.19 ALA 333 -0.10 GLU 234

ASN 300 0.18 ASP 334 -0.13 VAL 235

ASN 300 0.16 PHE 335 -0.13 VAL 235

ASN 300 0.15 MET 336 -0.12 GLU 234

ASN 300 0.15 ALA 337 -0.14 GLU 234

ASN 300 0.13 LYS 338 -0.17 GLU 234

ASN 300 0.14 LYS 339 -0.18 VAL 235

ASN 300 0.14 PHE 340 -0.23 VAL 235

ALA 213 0.14 ALA 341 -0.14 LYS 231

ASN 300 0.10 LEU 342 -0.10 LYS 231

ALA 213 0.10 ASP 343 -0.11 LYS 228

MET 209 0.11 PRO 344 -0.16 LYS 228

MET 209 0.11 LEU 345 -0.09 LYS 228

MET 209 0.08 ILE 346 -0.08 ILE 269

GLU 234 0.10 THR 347 -0.11 ILE 269

GLU 234 0.08 HIS 348 -0.10 ARG 271

ALA 213 0.06 VAL 349 -0.09 ARG 271

GLU 234 0.05 LEU 350 -0.09 ARG 271

LYS 338 0.04 PRO 351 -0.07 ARG 271

GLU 234 0.03 PHE 352 -0.07 ARG 271

LYS 231 0.04 GLU 353 -0.07 ARG 271

LYS 231 0.05 LYS 354 -0.10 GLN 299

LYS 231 0.06 ILE 355 -0.09 GLN 299

LYS 231 0.07 ASN 356 -0.14 GLN 299

LYS 231 0.08 GLU 357 -0.15 GLN 299

LYS 231 0.08 GLY 358 -0.13 GLN 299

LYS 231 0.09 PHE 359 -0.16 GLN 299

LYS 231 0.10 ASP 360 -0.21 GLN 299

LYS 231 0.12 LEU 361 -0.19 GLN 299

LYS 231 0.12 LEU 362 -0.18 GLN 299

ASP 227 0.14 ARG 363 -0.26 GLN 299

ASP 227 0.17 SER 364 -0.30 GLN 299

ASP 227 0.19 GLY 365 -0.25 GLN 299

LYS 231 0.20 GLU 366 -0.19 ARG 271

LYS 231 0.15 SER 367 -0.15 ARG 271

LYS 231 0.15 ILE 368 -0.14 ILE 269

LYS 231 0.09 ARG 369 -0.13 ILE 269

LYS 231 0.07 THR 370 -0.11 ILE 269

ALA 213 0.04 ILE 371 -0.08 ILE 269

LYS 338 0.04 LEU 372 -0.07 ILE 269

ASN 300 0.05 THR 373 -0.06 ILE 269

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 7 ---

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

* *