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.

* WP_011044792.1 *

CA distance fluctuations for 260407192227468946

--- normal mode 11 ---

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 480 0.28 MET 1 -0.07 GLU 470

ASP 480 0.29 SER 2 -0.07 GLU 470

ASP 480 0.29 ILE 3 -0.06 GLU 470

ASP 480 0.30 ILE 4 -0.05 GLU 470

ASP 480 0.30 ILE 5 -0.04 GLU 470

ASP 480 0.30 ARG 6 -0.04 GLU 470

ASP 480 0.30 GLY 7 -0.03 ASP 463

ASP 480 0.31 GLY 8 -0.03 ASP 463

ASP 480 0.32 THR 9 -0.03 ASP 463

ASP 480 0.34 VAL 10 -0.03 ASP 463

ASP 480 0.34 VAL 11 -0.03 ASP 463

ASP 480 0.36 THR 12 -0.03 ASP 463

ASP 480 0.37 ALA 13 -0.03 ASP 463

ASP 480 0.39 ASP 14 -0.03 ASP 463

ASP 480 0.38 MET 15 -0.03 ASP 463

ASP 480 0.35 THR 16 -0.03 ASP 463

ASP 480 0.35 PHE 17 -0.03 ASP 463

ASP 480 0.33 ALA 18 -0.03 ASP 463

ASP 480 0.34 ALA 19 -0.04 GLU 470

ASP 480 0.32 ASP 20 -0.05 GLU 470

ASP 480 0.33 VAL 21 -0.05 GLU 470

ASP 480 0.32 TYR 22 -0.07 GLU 470

ASP 480 0.32 CYS 23 -0.07 GLU 470

ASP 480 0.31 ASP 24 -0.09 GLU 470

ASP 480 0.31 GLU 25 -0.10 GLU 470

ASP 480 0.31 GLY 26 -0.09 GLU 470

ASP 480 0.33 LYS 27 -0.09 GLU 470

ASP 480 0.34 ILE 28 -0.08 GLU 470

ASP 480 0.35 VAL 29 -0.09 GLU 470

ASP 480 0.35 ALA 30 -0.08 GLU 470

ASP 480 0.35 ILE 31 -0.07 GLU 470

ASP 480 0.35 GLY 32 -0.06 GLU 470

ASP 480 0.34 ASP 33 -0.05 GLU 470

ASP 480 0.32 ASN 34 -0.06 GLU 470

ASP 480 0.33 LEU 35 -0.07 GLU 470

ASP 480 0.32 ASP 36 -0.08 GLU 470

ASP 480 0.31 VAL 37 -0.08 GLU 470

ASP 480 0.29 PRO 38 -0.08 GLU 470

ASP 480 0.28 GLU 39 -0.07 GLU 470

ASP 480 0.27 ASN 40 -0.07 GLU 470

ASP 480 0.28 ALA 41 -0.06 GLU 470

ASP 480 0.28 GLU 42 -0.05 GLU 470

ASP 480 0.28 CYS 43 -0.04 GLU 470

ASP 480 0.28 ILE 44 -0.03 GLU 470

ASP 480 0.28 ASP 45 -0.02 ASP 463

ASP 480 0.29 ALA 46 -0.02 ASP 463

ASP 480 0.28 THR 47 -0.02 ASP 463

ASP 480 0.28 GLY 48 -0.02 ASP 463

ASP 480 0.29 GLN 49 -0.02 ASP 463

ASP 480 0.30 TYR 50 -0.02 ASP 463

ASP 480 0.32 ILE 51 -0.03 ASP 463

ASP 480 0.32 ILE 52 -0.03 ASP 463

ASP 480 0.33 PRO 53 -0.03 ASP 463

ASP 480 0.31 GLY 54 -0.03 ASP 463

ASN 478 0.30 GLY 55 -0.03 ASP 463

ASN 478 0.33 ILE 56 -0.03 ASP 463

ASN 478 0.34 ASP 57 -0.02 ASP 463

ASN 478 0.36 PRO 58 -0.03 PRO 460

ASN 478 0.36 HIS 59 -0.02 PRO 460

ASN 478 0.35 THR 60 -0.02 PRO 460

ASN 478 0.34 HIS 61 -0.01 PRO 460

ASN 478 0.32 MET 62 -0.01 THR 466

ASN 478 0.31 GLN 63 -0.01 THR 466

ASN 478 0.33 LEU 64 -0.01 PRO 460

ALA 476 0.34 PRO 65 -0.01 PRO 460

ALA 476 0.37 PHE 66 -0.01 PRO 460

THR 475 0.40 MET 67 -0.01 PRO 460

ALA 476 0.36 GLY 68 -0.01 PRO 460

ALA 476 0.34 THR 69 -0.01 PRO 460

ALA 476 0.32 VAL 70 -0.01 PRO 460

THR 475 0.32 ALA 71 -0.01 PRO 460

ASN 478 0.29 SER 72 -0.01 PRO 460

ASN 478 0.29 ASP 73 -0.01 ASP 463

ASN 478 0.30 ASP 74 -0.02 THR 466

ASN 478 0.30 PHE 75 -0.03 THR 466

ASN 478 0.28 TYR 76 -0.03 THR 466

ASN 478 0.28 THR 77 -0.02 THR 466

ASN 478 0.29 GLY 78 -0.02 ASP 463

ASN 478 0.29 THR 79 -0.02 THR 466

ASN 478 0.28 ALA 80 -0.02 THR 466

ASN 478 0.28 ALA 81 -0.02 ASP 463

ASN 478 0.29 GLY 82 -0.02 ASP 463

ASN 478 0.28 LEU 83 -0.02 ASP 463

ASN 478 0.27 ALA 84 -0.02 ASP 463

ASN 478 0.28 GLY 85 -0.02 ASP 463

ASN 478 0.28 GLY 86 -0.02 ASP 463

ASN 478 0.30 THR 87 -0.03 ASP 463

ASN 478 0.29 THR 88 -0.03 THR 466

ASN 478 0.31 THR 89 -0.03 THR 466

ASN 478 0.33 ILE 90 -0.03 THR 466

ASN 478 0.36 ILE 91 -0.03 THR 466

ASN 478 0.36 ASP 92 -0.02 THR 466

ASN 478 0.38 PHE 93 -0.02 THR 466

ASN 478 0.37 VAL 94 -0.02 THR 466

ASN 478 0.38 ILE 95 -0.01 THR 466

ASN 478 0.38 PRO 96 -0.01 THR 466

ALA 476 0.39 ALA 97 -0.01 MET 67

ALA 476 0.43 PRO 98 -0.00 MET 67

ALA 476 0.39 GLY 99 -0.01 HIS 468

ASN 478 0.37 GLN 100 -0.02 THR 466

ASN 478 0.38 SER 101 -0.03 THR 466

ASN 478 0.39 LEU 102 -0.03 THR 466

ASN 478 0.37 ILE 103 -0.06 GLU 470

ASN 478 0.35 GLU 104 -0.04 GLU 470

ASN 478 0.36 ALA 105 -0.03 THR 466

ASN 478 0.36 PHE 106 -0.04 GLU 470

ASN 478 0.33 HIS 107 -0.06 GLU 470

ASN 478 0.32 GLN 108 -0.03 GLU 470

ASN 478 0.33 TRP 109 -0.03 THR 466

ASN 478 0.32 GLN 110 -0.05 GLU 470

ASN 478 0.30 ASP 111 -0.05 GLU 470

ASN 478 0.30 TRP 112 -0.03 THR 466

ASN 478 0.31 ALA 113 -0.04 THR 466

ASN 478 0.29 SER 114 -0.05 GLU 470

ASN 478 0.28 LYS 115 -0.04 GLU 470

ASN 478 0.29 SER 116 -0.04 THR 466

ASN 478 0.28 ALA 117 -0.03 THR 466

ASN 478 0.29 ALA 118 -0.04 THR 466

ASN 478 0.30 ASP 119 -0.05 GLU 470

ASN 478 0.32 TYR 120 -0.04 THR 466

ASN 478 0.35 SER 121 -0.05 THR 466

ASN 478 0.37 PHE 122 -0.04 THR 466

ASN 478 0.40 HIS 123 -0.03 THR 466

ASN 478 0.41 VAL 124 -0.03 THR 466

ASN 478 0.42 ALA 125 -0.01 PRO 460

ALA 476 0.45 ILE 126 -0.01 ASN 459

ALA 476 0.47 THR 127 -0.01 PRO 460

ALA 476 0.49 TRP 128 -0.00 GLU 255

ALA 476 0.50 TRP 129 -0.02 HIS 468

ASN 478 0.46 ASP 130 -0.04 HIS 468

ASN 478 0.46 ASP 131 -0.06 HIS 468

ASN 478 0.43 SER 132 -0.05 ALA 469

ASN 478 0.45 VAL 133 -0.04 HIS 468

ASN 478 0.49 TYR 134 -0.06 HIS 468

ASN 478 0.45 GLU 135 -0.09 ALA 469

ASN 478 0.42 ASP 136 -0.07 GLU 470

ASN 478 0.45 MET 137 -0.06 GLU 470

ASN 478 0.45 GLY 138 -0.12 GLU 470

ASN 478 0.40 THR 139 -0.12 GLU 470

ASN 478 0.40 LEU 140 -0.09 GLU 470

ASN 478 0.42 VAL 141 -0.12 GLU 470

ASN 478 0.40 ASN 142 -0.17 GLU 470

ASN 478 0.36 GLU 143 -0.15 GLU 470

ASN 478 0.36 TYR 144 -0.11 GLU 470

ASN 478 0.38 GLY 145 -0.12 GLU 470

ASN 478 0.40 VAL 146 -0.07 GLU 470

ASN 478 0.43 ASN 147 -0.07 THR 466

ASN 478 0.45 SER 148 -0.03 THR 466

ASN 478 0.46 PHE 149 -0.01 THR 466

ASN 478 0.45 LYS 150 -0.01 PRO 460

THR 475 0.52 HIS 151 -0.01 PRO 460

THR 475 0.55 PHE 152 -0.01 PRO 460

THR 475 0.64 MET 153 -0.01 PRO 460

THR 475 0.60 ALA 154 -0.01 PRO 460

THR 475 0.54 TYR 155 -0.01 PRO 460

THR 475 0.57 LYS 156 -0.01 PRO 460

THR 475 0.51 ASN 157 -0.00 PRO 460

ALA 476 0.48 ALA 158 -0.01 PRO 460

ALA 476 0.49 ILE 159 -0.01 PRO 460

THR 475 0.56 MET 160 -0.01 PRO 460

ALA 476 0.59 ALA 161 -0.01 GLY 261

THR 475 0.68 ASP 162 -0.01 VAL 237

THR 475 0.78 ASP 163 -0.01 GLY 256

ALA 476 0.75 GLU 164 -0.01 GLY 256

ALA 476 0.64 THR 165 -0.01 GLY 256

ALA 476 0.66 LEU 166 -0.01 PRO 180

ALA 476 0.73 VAL 167 -0.01 GLY 256

ALA 476 0.62 LYS 168 -0.03 HIS 468

ASN 478 0.55 SER 169 -0.01 HIS 468

ASN 478 0.59 PHE 170 -0.01 GLN 257

ASN 478 0.64 ARG 171 -0.05 HIS 468

ASN 478 0.58 ARG 172 -0.07 HIS 468

ASN 478 0.55 SER 173 -0.03 HIS 468

ASN 478 0.59 MET 174 -0.06 HIS 468

ASN 478 0.59 ASP 175 -0.17 ALA 469

ASN 478 0.51 LEU 176 -0.13 GLU 470

ASN 478 0.50 GLY 177 -0.14 THR 466

ASN 478 0.49 ALA 178 -0.07 THR 466

ASN 478 0.49 ILE 179 -0.02 PRO 460

ASN 478 0.50 PRO 180 -0.01 ARG 226

PRO 474 0.49 THR 181 -0.02 PRO 460

PRO 474 0.58 VAL 182 -0.01 PRO 460

PRO 474 0.57 HIS 183 -0.01 PRO 460

PRO 474 0.67 ALA 184 -0.01 PRO 460

PRO 474 0.67 GLU 185 -0.01 PRO 460

THR 475 0.72 ASN 186 -0.01 PRO 460

THR 475 0.65 GLY 187 -0.01 PRO 460

THR 475 0.69 GLU 188 -0.00 VAL 216

THR 475 0.70 LEU 189 -0.01 LYS 295

THR 475 0.63 VAL 190 -0.01 PRO 460

THR 475 0.60 PHE 191 -0.01 PRO 460

THR 475 0.63 GLN 192 -0.01 SER 294

THR 475 0.62 LEU 193 -0.01 SER 294

THR 475 0.56 GLN 194 -0.01 PRO 460

THR 475 0.56 GLN 195 -0.00 PRO 460

THR 475 0.57 GLU 196 -0.00 THR 356

THR 475 0.55 MET 197 -0.01 THR 356

THR 475 0.51 LEU 198 -0.01 PRO 460

THR 475 0.52 SER 199 -0.00 THR 356

THR 475 0.52 GLN 200 -0.01 THR 356

THR 475 0.49 GLY 201 -0.01 PRO 460

THR 475 0.49 ILE 202 -0.01 PRO 460

THR 475 0.47 THR 203 -0.01 PRO 460

THR 475 0.45 GLY 204 -0.01 PRO 460

THR 475 0.46 PRO 205 -0.01 PRO 460

THR 475 0.49 GLU 206 -0.01 PRO 460

THR 475 0.51 GLY 207 -0.01 PRO 460

THR 475 0.52 HIS 208 -0.01 PRO 460

THR 475 0.54 PRO 209 -0.01 PRO 460

THR 475 0.57 LEU 210 -0.01 PRO 460

THR 475 0.59 SER 211 -0.01 PRO 460

THR 475 0.61 ARG 212 -0.01 PRO 460

THR 475 0.63 PRO 213 -0.01 PRO 460

PRO 474 0.67 PRO 214 -0.01 PRO 460

PRO 474 0.74 ALA 215 -0.01 PRO 460

PRO 474 0.72 VAL 216 -0.01 PRO 460

PRO 474 0.71 GLU 217 -0.01 PRO 460

PRO 474 0.79 GLY 218 -0.01 PRO 460

PRO 474 0.86 GLU 219 -0.01 PRO 460

PRO 474 0.80 ALA 220 -0.01 PRO 460

PRO 474 0.80 ALA 221 -0.01 PRO 460

PRO 474 0.94 ASN 222 -0.01 PRO 460

PRO 474 0.97 ARG 223 -0.01 PRO 180

PRO 474 0.84 ALA 224 -0.01 PRO 180

PRO 474 0.90 ILE 225 -0.01 PRO 180

PRO 474 1.11 ARG 226 -0.02 GLN 257

PRO 474 0.97 ILE 227 -0.02 GLN 257

PRO 474 0.82 ALA 228 -0.02 GLN 257

ALA 473 1.03 GLU 229 -0.05 PRO 234

ALA 473 1.17 VAL 230 -0.03 PRO 234

ALA 473 0.82 MET 231 -0.03 VAL 233

ALA 473 0.77 ASN 232 -0.05 ASP 175

ASN 478 0.60 VAL 233 -0.03 MET 231

ASN 478 0.52 PRO 234 -0.05 MET 461

PRO 474 0.59 ILE 235 -0.02 PRO 460

PRO 474 0.54 TYR 236 -0.03 PRO 460

PRO 474 0.60 VAL 237 -0.02 PRO 460

PRO 474 0.52 VAL 238 -0.02 PRO 460

PRO 474 0.52 HIS 239 -0.02 PRO 460

PRO 474 0.58 VAL 240 -0.02 PRO 460

PRO 474 0.57 SER 241 -0.01 PRO 460

PRO 474 0.63 CYS 242 -0.01 PRO 460

PRO 474 0.67 LYS 243 -0.01 PRO 460

PRO 474 0.75 GLU 244 -0.01 PRO 460

PRO 474 0.74 SER 245 -0.01 PRO 460

PRO 474 0.69 LEU 246 -0.02 PRO 460

PRO 474 0.77 GLU 247 -0.02 PRO 460

PRO 474 0.86 ALA 248 -0.01 PRO 460

PRO 474 0.76 ILE 249 -0.02 PRO 460

PRO 474 0.73 THR 250 -0.02 PRO 460

PRO 474 0.86 ARG 251 -0.02 PRO 460

PRO 474 0.88 ALA 252 -0.02 PRO 460

PRO 474 0.71 ARG 253 -0.02 PRO 460

PRO 474 0.73 ASN 254 -0.02 PRO 460

PRO 474 0.84 GLU 255 -0.03 PRO 234

ASN 472 0.74 GLY 256 -0.03 PRO 234

ALA 473 0.74 GLN 257 -0.04 PRO 234

PRO 474 0.57 LEU 258 -0.05 PRO 234

PRO 474 0.64 VAL 259 -0.03 PRO 460

PRO 474 0.54 TYR 260 -0.03 PRO 460

PRO 474 0.56 GLY 261 -0.03 PRO 460

PRO 474 0.49 GLU 262 -0.02 PRO 460

PRO 474 0.49 VAL 263 -0.02 PRO 460

PRO 474 0.45 LEU 264 -0.02 PRO 460

PRO 474 0.41 ALA 265 -0.02 PRO 460

PRO 474 0.43 GLY 266 -0.02 PRO 460

PRO 474 0.48 HIS 267 -0.02 PRO 460

PRO 474 0.46 LEU 268 -0.02 PRO 460

PRO 474 0.43 LEU 269 -0.01 PRO 460

PRO 474 0.44 VAL 270 -0.01 PRO 460

PRO 474 0.48 ASP 271 -0.01 PRO 460

PRO 474 0.49 ASP 272 -0.01 PRO 460

PRO 474 0.46 SER 273 -0.01 PRO 460

PRO 474 0.44 VAL 274 -0.01 PRO 460

THR 475 0.46 TYR 275 -0.01 PRO 460

THR 475 0.45 ARG 276 -0.01 PRO 460

THR 475 0.42 HIS 277 -0.01 PRO 460

THR 475 0.40 PRO 278 -0.01 PRO 460

THR 475 0.38 ASN 279 -0.01 PRO 460

THR 475 0.40 SER 280 -0.01 PRO 460

THR 475 0.38 GLU 281 -0.01 PRO 460

THR 475 0.38 PHE 282 -0.01 PRO 460

THR 475 0.42 ALA 283 -0.01 PRO 460

THR 475 0.41 ALA 284 -0.01 PRO 460

THR 475 0.39 ALA 285 -0.01 PRO 460

THR 475 0.42 HIS 286 -0.01 PRO 460

THR 475 0.45 VAL 287 -0.01 PRO 460

THR 475 0.46 MET 288 -0.01 PRO 460

THR 475 0.51 SER 289 -0.01 PRO 460

PRO 474 0.55 PRO 290 -0.01 PRO 460

PRO 474 0.52 PRO 291 -0.01 PRO 460

PRO 474 0.50 PHE 292 -0.01 PRO 460

PRO 474 0.54 ARG 293 -0.01 PRO 460

PRO 474 0.53 SER 294 -0.01 PRO 460

PRO 474 0.51 LYS 295 -0.01 PRO 460

PRO 474 0.55 ASP 296 -0.01 PRO 460

PRO 474 0.57 HIS 297 -0.01 PRO 460

PRO 474 0.52 GLN 298 -0.01 PRO 460

PRO 474 0.52 ALA 299 -0.01 PRO 460

PRO 474 0.57 ALA 300 -0.01 PRO 460

PRO 474 0.54 LEU 301 -0.02 PRO 460

PRO 474 0.49 TRP 302 -0.02 PRO 460

PRO 474 0.52 LYS 303 -0.02 PRO 460

PRO 474 0.55 GLY 304 -0.02 PRO 460

PRO 474 0.47 LEU 305 -0.02 PRO 460

PRO 474 0.45 GLN 306 -0.02 PRO 460

PRO 474 0.49 SER 307 -0.02 PRO 460

PRO 474 0.47 GLY 308 -0.02 PRO 460

PRO 474 0.57 ASN 309 -0.02 PRO 460

PRO 474 0.52 LEU 310 -0.02 PRO 460

PRO 474 0.44 GLN 311 -0.03 PRO 460

PRO 474 0.41 THR 312 -0.03 PRO 460

PRO 474 0.40 THR 313 -0.02 PRO 460

PRO 474 0.39 ALA 314 -0.02 PRO 460

PRO 474 0.38 THR 315 -0.02 PRO 460

PRO 474 0.40 ASP 316 -0.02 PRO 460

PRO 474 0.35 HIS 317 -0.02 PRO 460

THR 475 0.36 CYS 318 -0.01 PRO 460

THR 475 0.34 CYS 319 -0.01 PRO 460

THR 475 0.34 PHE 320 -0.01 PRO 460

THR 475 0.33 CYS 321 -0.01 PRO 460

THR 475 0.34 ALA 322 -0.01 PRO 460

THR 475 0.33 ASP 323 -0.01 PRO 460

THR 475 0.34 GLN 324 -0.01 PRO 460

THR 475 0.38 LYS 325 -0.01 PRO 460

THR 475 0.37 ALA 326 -0.01 PRO 460

THR 475 0.38 ALA 327 -0.01 PRO 460

THR 475 0.41 GLY 328 -0.01 PRO 460

THR 475 0.40 LYS 329 -0.01 PRO 460

THR 475 0.42 ASP 330 -0.01 PRO 460

THR 475 0.45 ASP 331 -0.01 PRO 460

THR 475 0.46 PHE 332 -0.01 PRO 460

THR 475 0.48 THR 333 -0.01 PRO 460

THR 475 0.43 LYS 334 -0.01 PRO 460

THR 475 0.42 ILE 335 -0.01 PRO 460

THR 475 0.41 PRO 336 -0.01 PRO 460

THR 475 0.43 ASN 337 -0.01 PRO 460

THR 475 0.41 GLY 338 -0.01 PRO 460

PRO 474 0.38 THR 339 -0.01 PRO 460

PRO 474 0.35 ALA 340 -0.01 PRO 460

PRO 474 0.34 GLY 341 -0.02 PRO 460

PRO 474 0.31 VAL 342 -0.02 ASP 463

ASN 478 0.29 GLU 343 -0.02 ASP 463

PRO 474 0.31 ASP 344 -0.02 ASP 463

PRO 474 0.33 ARG 345 -0.02 PRO 460

PRO 474 0.31 LEU 346 -0.02 ASP 463

PRO 474 0.30 ALA 347 -0.02 ASP 463

PRO 474 0.34 VAL 348 -0.01 PRO 460

PRO 474 0.36 LEU 349 -0.02 PRO 460

PRO 474 0.32 TRP 350 -0.02 ASP 463

PRO 474 0.33 ASP 351 -0.01 ASP 463

PRO 474 0.37 ALA 352 -0.01 PRO 460

PRO 474 0.37 GLY 353 -0.01 PRO 460

PRO 474 0.33 VAL 354 -0.02 ASP 463

PRO 474 0.32 ASN 355 -0.01 ASP 463

PRO 474 0.35 THR 356 -0.01 ASP 463

PRO 474 0.35 GLY 357 -0.01 ASP 463

PRO 474 0.39 ARG 358 -0.01 PRO 460

PRO 474 0.36 LEU 359 -0.01 ASP 463

ASP 480 0.32 THR 360 -0.02 ASP 463

ASP 480 0.32 ILE 361 -0.02 ASP 463

ASP 480 0.35 ASN 362 -0.02 ASP 463

ASP 480 0.34 GLU 363 -0.02 ASP 463

ASP 480 0.32 PHE 364 -0.02 ASP 463

ASP 480 0.33 VAL 365 -0.03 ASP 463

ASP 480 0.35 ALA 366 -0.03 ASP 463

PRO 474 0.35 ALA 367 -0.02 ASP 463

ASN 478 0.32 THR 368 -0.03 ASP 463

ASP 480 0.33 SER 369 -0.03 ASP 463

ASP 480 0.36 THR 370 -0.04 ASP 463

ASP 480 0.37 ASN 371 -0.04 ASP 463

ASN 478 0.37 ALA 372 -0.04 PRO 460

ASP 480 0.37 ALA 373 -0.04 ASP 463

ASP 480 0.40 LYS 374 -0.05 ASP 463

ASN 478 0.40 ILE 375 -0.05 PRO 460

ASN 478 0.40 PHE 376 -0.04 THR 466

ASP 480 0.40 ASN 377 -0.08 THR 466

ASP 480 0.38 LEU 378 -0.07 GLU 470

ASP 480 0.40 TYR 379 -0.07 GLU 470

ASP 480 0.40 PRO 380 -0.09 GLU 470

ASP 480 0.37 ARG 381 -0.09 GLU 470

ASP 480 0.35 LYS 382 -0.06 GLU 470

ASP 480 0.35 GLY 383 -0.04 ASP 463

ASP 480 0.37 SER 384 -0.05 GLU 470

ASP 480 0.36 VAL 385 -0.05 GLU 470

ASP 480 0.38 SER 386 -0.07 GLU 470

ASP 480 0.38 VAL 387 -0.10 GLU 470

ASP 480 0.38 GLY 388 -0.11 GLU 470

ASP 480 0.37 ALA 389 -0.09 GLU 470

ASP 480 0.34 ASP 390 -0.08 GLU 470

ASP 480 0.32 ALA 391 -0.07 GLU 470

ASP 480 0.31 ASP 392 -0.05 GLU 470

ASP 480 0.31 LEU 393 -0.03 ASP 463

ASP 480 0.29 VAL 394 -0.03 ASP 463

ASP 480 0.29 VAL 395 -0.03 ASP 463

ASP 480 0.28 TRP 396 -0.02 ASP 463

ASP 480 0.27 ASP 397 -0.02 ASP 463

ASP 480 0.27 PRO 398 -0.02 ASP 463

ASP 480 0.25 LYS 399 -0.02 ASP 463

ASP 480 0.25 GLY 400 -0.02 ASP 463

PRO 474 0.26 THR 401 -0.02 ASP 463

PRO 474 0.27 ARG 402 -0.01 ASP 463

PRO 474 0.29 THR 403 -0.01 ASP 463

PRO 474 0.30 ILE 404 -0.01 ASP 463

PRO 474 0.30 SER 405 -0.01 ASP 463

PRO 474 0.29 ALA 406 -0.01 PRO 460

PRO 474 0.27 LYS 407 -0.01 ASP 463

PRO 474 0.25 THR 408 -0.01 ASP 463

PRO 474 0.26 HIS 409 -0.01 ASP 463

ASN 478 0.26 HIS 410 -0.02 ASP 463

ASN 478 0.28 GLN 411 -0.01 ASP 463

ASN 478 0.28 ASN 412 -0.01 ASP 463

THR 475 0.30 ILE 413 -0.01 PRO 460

THR 475 0.30 ASP 414 -0.01 PRO 460

THR 475 0.33 PHE 415 -0.01 PRO 460

PRO 474 0.34 ASN 416 -0.01 PRO 460

PRO 474 0.37 ILE 417 -0.01 PRO 460

PRO 474 0.36 PHE 418 -0.01 PRO 460

PRO 474 0.33 GLU 419 -0.01 PRO 460

PRO 474 0.32 GLY 420 -0.01 PRO 460

PRO 474 0.33 ARG 421 -0.01 PRO 460

PRO 474 0.31 THR 422 -0.01 ASP 463

PRO 474 0.31 VAL 423 -0.01 ASP 463

PRO 474 0.28 THR 424 -0.01 ASP 463

PRO 474 0.27 GLY 425 -0.02 ASP 463

ASP 480 0.26 ILE 426 -0.02 ASP 463

ASP 480 0.26 PRO 427 -0.02 ASP 463

ASP 480 0.26 SER 428 -0.02 ASP 463

ASP 480 0.27 HIS 429 -0.02 ASP 463

ASP 480 0.27 THR 430 -0.03 ASP 463

ASP 480 0.29 ILE 431 -0.04 GLU 470

ASP 480 0.29 SER 432 -0.05 GLU 470

ASP 480 0.30 ARG 433 -0.07 GLU 470

ASP 480 0.30 GLY 434 -0.07 GLU 470

ASP 480 0.28 LYS 435 -0.05 GLU 470

ASP 480 0.27 LEU 436 -0.04 GLU 470

ASP 480 0.26 VAL 437 -0.03 GLU 470

ASP 480 0.25 TRP 438 -0.02 ASP 463

ASP 480 0.25 ALA 439 -0.02 ASP 463

ASP 480 0.24 ASN 440 -0.02 ASP 463

ASN 478 0.24 GLY 441 -0.02 ASP 463

ASN 478 0.23 VAL 442 -0.02 ASP 463

ASN 478 0.25 LEU 443 -0.02 THR 466

ASN 478 0.24 ASN 444 -0.03 THR 466

ASN 478 0.25 ALA 445 -0.03 THR 466

ASN 478 0.25 VAL 446 -0.04 GLU 470

ASN 478 0.26 ARG 447 -0.04 GLU 470

ASN 478 0.27 GLY 448 -0.05 GLU 470

ASN 478 0.27 ALA 449 -0.06 GLU 470

ASN 478 0.28 GLY 450 -0.05 GLU 470

ASN 478 0.29 GLN 451 -0.07 GLU 470

ASN 478 0.32 TYR 452 -0.07 GLU 470

ASN 478 0.33 VAL 453 -0.08 GLU 470

ASN 478 0.35 GLU 454 -0.10 GLU 470

ASN 478 0.37 ARG 455 -0.10 GLU 470

ASP 480 0.40 PRO 456 -0.15 GLU 470

ASN 478 0.43 PRO 457 -0.14 GLU 470

ASP 480 0.47 PHE 458 -0.18 THR 466

ASP 480 0.47 ASN 459 -0.12 THR 466

ASP 480 0.52 PRO 460 -0.10 GLU 470

ASP 480 0.51 MET 461 -0.06 ASP 463

ASP 480 0.53 PHE 462 -0.11 THR 466

ASP 480 0.62 ASP 463 -0.16 GLU 470

ASP 480 0.59 ALA 464 -0.07 VAL 471

ASN 478 0.56 LEU 465 -0.05 ASP 175

ASN 478 0.66 THR 466 -0.18 PHE 458

ASP 480 0.72 LYS 467 -0.19 VAL 471

ASP 480 0.56 HIS 468 -0.13 ASP 175

ASN 478 0.63 ALA 469 -0.17 ASP 175

ASN 478 0.83 GLU 470 -0.17 ASN 142

ASP 480 0.72 VAL 471 -0.19 LYS 467

GLU 255 0.83 ASN 472 -0.25 VAL 477

VAL 230 1.17 ALA 473 -0.17 VAL 471

ARG 226 1.11 PRO 474 -0.30 VAL 477

VAL 230 0.98 THR 475 -0.02 ASP 36

VAL 230 0.87 ALA 476 -0.26 PRO 474

GLU 164 0.52 VAL 477 -0.30 PRO 474

GLU 470 0.83 ASN 478 -0.01 VAL 477

GLU 470 0.48 SER 479 -0.17 PRO 474

GLU 470 0.76 ASP 480 -0.06 ALA 476

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.

*** WP_011044792.1 ***

CA distance fluctuations for 260407192227468946

--- normal mode 11 ---

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.

* WP_011044792.1 *