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

* secyeg-tasr *

CA distance fluctuations for 2605152131492949579

--- 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
ASP 254 0.07 MET 1 -0.24 LYS 425

ASP 254 0.06 ASN 2 -0.22 LYS 425

SER 253 0.07 VAL 3 -0.29 LYS 425

SER 253 0.07 GLY 4 -0.32 LYS 425

ASP 254 0.06 ALA 5 -0.24 LYS 425

SER 253 0.05 ARG 6 -0.27 LYS 425

SER 253 0.06 GLY 7 -0.36 LYS 425

SER 253 0.06 ASN 8 -0.33 LYS 425

SER 253 0.04 ALA 9 -0.28 LYS 425

GLU 102 0.04 GLY 10 -0.18 ALA 421

MET 335 0.04 LEU 11 -0.18 LYS 425

ASP 254 0.04 PHE 12 -0.21 LYS 425

MET 335 0.03 TRP 13 -0.16 LYS 425

MET 335 0.02 ARG 14 -0.11 LYS 425

ASP 254 0.03 PHE 15 -0.14 LYS 425

ASP 254 0.02 GLY 16 -0.16 VAL 432

MET 335 0.02 PHE 17 -0.10 VAL 432

MET 335 0.02 THR 18 -0.09 TRP 429

ASP 254 0.02 LEU 19 -0.13 VAL 432

SER 253 0.01 LEU 20 -0.12 VAL 432

THR 412 0.01 ALA 21 -0.07 VAL 432

THR 412 0.01 LEU 22 -0.09 VAL 432

SER 253 0.01 ILE 23 -0.11 VAL 432

THR 412 0.01 VAL 24 -0.08 VAL 432

SER 416 0.02 TYR 25 -0.06 VAL 432

SER 416 0.01 ARG 26 -0.08 VAL 432

THR 412 0.01 LEU 27 -0.09 VAL 432

SER 416 0.02 GLY 28 -0.06 VAL 432

SER 416 0.02 THR 29 -0.06 VAL 432

SER 416 0.01 TYR 30 -0.08 VAL 432

SER 416 0.01 ILE 31 -0.07 VAL 432

SER 416 0.02 PRO 32 -0.06 VAL 432

SER 420 0.02 ILE 33 -0.04 TRP 429

SER 416 0.02 PRO 34 -0.04 VAL 432

SER 420 0.02 GLY 35 -0.04 VAL 432

SER 420 0.02 VAL 36 -0.04 TRP 429

SER 416 0.02 ASN 37 -0.05 VAL 432

SER 416 0.02 PRO 38 -0.06 VAL 432

SER 416 0.01 SER 39 -0.07 VAL 432

SER 416 0.02 VAL 40 -0.06 VAL 432

SER 416 0.02 VAL 41 -0.05 TRP 429

SER 416 0.02 GLU 42 -0.06 VAL 432

SER 416 0.02 ASP 43 -0.07 VAL 432

SER 416 0.02 ILE 44 -0.05 TRP 429

SER 416 0.03 ILE 45 -0.05 TRP 429

SER 416 0.02 SER 46 -0.06 TRP 429

SER 416 0.02 SER 47 -0.05 TRP 429

SER 420 0.03 HIS 48 -0.04 TRP 429

SER 420 0.04 ALA 49 -0.03 TRP 429

SER 420 0.03 THR 50 -0.04 TRP 429

SER 420 0.03 GLY 51 -0.04 TRP 429

SER 420 0.05 VAL 52 -0.02 TRP 429

SER 420 0.05 LEU 53 -0.02 TRP 429

SER 420 0.04 GLY 54 -0.04 TRP 429

SER 420 0.05 ILE 55 -0.03 TRP 429

SER 420 0.05 PHE 56 -0.02 VAL 3

SER 420 0.04 ASN 57 -0.04 TRP 429

SER 416 0.04 VAL 58 -0.05 TRP 429

SER 420 0.05 PHE 59 -0.02 TRP 429

SER 420 0.05 SER 60 -0.03 TRP 429

SER 416 0.03 GLY 61 -0.05 TRP 429

SER 416 0.03 GLY 62 -0.06 TRP 429

SER 416 0.03 ALA 63 -0.05 TRP 429

SER 420 0.03 LEU 64 -0.04 TRP 429

SER 416 0.03 GLY 65 -0.05 TRP 429

SER 416 0.02 ARG 66 -0.06 VAL 432

SER 416 0.03 MET 67 -0.05 TRP 429

SER 416 0.03 THR 68 -0.04 TRP 429

SER 420 0.04 ILE 69 -0.02 TRP 429

SER 420 0.05 PHE 70 -0.02 VAL 3

SER 420 0.05 ALA 71 -0.02 VAL 3

SER 420 0.07 LEU 72 -0.02 VAL 3

SER 420 0.06 ASN 73 -0.02 VAL 3

SER 420 0.08 VAL 74 -0.01 ASN 2

SER 420 0.09 MET 75 -0.01 VAL 3

SER 420 0.10 PRO 76 -0.01 VAL 3

SER 420 0.11 TYR 77 -0.00 ASN 2

SER 420 0.12 ILE 78 -0.00 LEU 325

SER 420 0.12 VAL 79 -0.01 LYS 330

GLU 427 0.14 SER 80 -0.01 LYS 330

GLU 427 0.15 SER 81 -0.01 LEU 325

GLU 427 0.15 ILE 82 -0.01 LYS 330

GLU 427 0.16 ILE 83 -0.01 LYS 330

GLU 427 0.18 VAL 84 -0.01 GLU 331

GLU 427 0.19 GLN 85 -0.01 LYS 330

GLU 427 0.18 LEU 86 -0.01 LYS 330

LYS 431 0.20 LEU 87 -0.01 LYS 330

LYS 431 0.22 SER 88 -0.01 GLU 331

GLU 427 0.22 VAL 89 -0.01 LYS 330

LYS 431 0.21 ALA 90 -0.01 LYS 330

LYS 431 0.23 ILE 91 -0.01 GLU 334

LYS 431 0.26 PRO 92 -0.01 GLU 334

LYS 431 0.26 THR 93 -0.01 GLU 334

LYS 431 0.25 LEU 94 -0.01 GLU 331

LYS 431 0.27 ASN 95 -0.01 GLU 331

LYS 431 0.29 GLU 96 -0.01 GLU 334

LYS 431 0.28 MET 97 -0.01 GLU 331

LYS 431 0.28 ARG 98 -0.01 GLU 331

LYS 431 0.32 GLN 99 -0.02 GLU 331

LYS 431 0.34 ASP 100 -0.01 MET 335

LYS 431 0.35 GLY 101 -0.01 MET 335

LYS 431 0.33 GLU 102 -0.01 ASP 254

LYS 431 0.31 LEU 103 -0.01 ASP 254

LYS 431 0.29 GLY 104 -0.01 MET 335

GLU 427 0.27 ARG 105 -0.01 ASP 254

LYS 431 0.25 MET 106 -0.01 ASP 254

LYS 431 0.24 LYS 107 -0.01 ASP 254

LYS 431 0.23 MET 108 -0.01 GLU 331

GLU 427 0.20 SER 109 -0.01 ASP 254

LYS 431 0.19 ALA 110 -0.01 ASP 254

LYS 431 0.19 TYR 111 -0.01 GLU 331

GLU 427 0.17 THR 112 -0.01 GLU 331

GLU 427 0.15 ARG 113 -0.01 ILE 258

LYS 431 0.15 TYR 114 -0.01 GLU 331

GLU 427 0.14 LEU 115 -0.01 GLU 331

GLU 427 0.12 SER 116 -0.01 LYS 330

GLU 427 0.11 VAL 117 -0.00 LYS 330

GLU 427 0.12 ALA 118 -0.01 LYS 330

GLU 427 0.11 PHE 119 -0.01 LYS 330

GLU 427 0.09 CYS 120 -0.01 VAL 3

GLU 427 0.09 ILE 121 -0.01 VAL 3

GLU 427 0.09 ALA 122 -0.01 VAL 3

SER 420 0.08 GLN 123 -0.01 VAL 3

SER 420 0.07 GLY 124 -0.01 VAL 3

GLU 427 0.07 LEU 125 -0.01 VAL 3

GLU 427 0.07 VAL 126 -0.01 VAL 3

SER 420 0.06 ILE 127 -0.01 VAL 3

SER 420 0.05 LEU 128 -0.01 VAL 3

SER 420 0.06 LEU 129 -0.01 VAL 3

SER 420 0.06 GLY 130 -0.01 VAL 3

SER 420 0.05 LEU 131 -0.02 VAL 3

SER 420 0.04 GLU 132 -0.02 VAL 3

SER 420 0.05 ARG 133 -0.01 VAL 3

SER 420 0.05 MET 134 -0.01 VAL 3

SER 420 0.04 ASN 135 -0.02 VAL 3

SER 420 0.04 SER 136 -0.01 VAL 3

SER 420 0.03 ASP 137 -0.02 TRP 429

SER 420 0.03 GLU 138 -0.03 TRP 429

SER 420 0.03 VAL 139 -0.03 TRP 429

SER 420 0.03 MET 140 -0.03 TRP 429

SER 420 0.03 VAL 141 -0.03 TRP 429

SER 420 0.02 VAL 142 -0.03 TRP 429

SER 420 0.03 ILE 143 -0.02 TRP 429

SER 420 0.04 ASN 144 -0.01 VAL 3

SER 420 0.04 PRO 145 -0.01 VAL 3

SER 420 0.04 GLY 146 -0.01 VAL 3

GLU 427 0.05 ILE 147 -0.01 VAL 3

SER 420 0.05 MET 148 -0.01 VAL 3

SER 420 0.04 PHE 149 -0.01 VAL 3

SER 420 0.05 ARG 150 -0.01 VAL 3

GLU 427 0.06 VAL 151 -0.01 VAL 3

SER 420 0.05 VAL 152 -0.01 VAL 3

SER 420 0.05 GLY 153 -0.01 VAL 3

SER 420 0.06 ILE 154 -0.01 VAL 3

SER 420 0.06 SER 155 -0.01 VAL 3

SER 420 0.05 SER 156 -0.01 VAL 3

SER 420 0.06 LEU 157 -0.01 VAL 3

SER 420 0.07 LEU 158 -0.01 VAL 3

SER 420 0.06 ALA 159 -0.01 VAL 3

SER 420 0.05 GLY 160 -0.01 VAL 3

SER 420 0.07 THR 161 -0.01 VAL 3

SER 420 0.08 MET 162 -0.01 ASN 2

SER 420 0.06 PHE 163 -0.01 VAL 3

SER 420 0.06 LEU 164 -0.01 VAL 3

SER 420 0.09 LEU 165 -0.01 ASN 2

SER 420 0.08 TRP 166 -0.00 SER 181

SER 420 0.06 LEU 167 -0.01 ASN 2

SER 420 0.08 GLY 168 -0.01 LEU 182

SER 420 0.10 GLU 169 -0.01 GLY 179

SER 420 0.07 ARG 170 -0.01 ASP 405

SER 420 0.06 ILE 171 -0.01 PRO 193

SER 420 0.10 ASN 172 -0.01 ASP 405

SER 420 0.11 ALA 173 -0.01 ASP 405

SER 420 0.05 LYS 174 -0.01 PRO 193

SER 420 0.03 GLY 175 -0.03 TRP 429

SER 420 0.07 ILE 176 -0.01 THR 406

SER 416 0.07 GLY 177 -0.02 THR 406

SER 420 0.10 ASN 178 -0.01 ILE 403

SER 420 0.07 GLY 179 -0.01 GLU 169

SER 420 0.08 ILE 180 -0.01 ASN 2

SER 420 0.07 SER 181 -0.01 ASN 2

SER 416 0.05 LEU 182 -0.05 TRP 429

SER 416 0.04 ILE 183 -0.05 TRP 429

SER 416 0.05 ILE 184 -0.04 TRP 429

SER 416 0.03 PHE 185 -0.07 TRP 429

SER 416 0.02 VAL 186 -0.09 TRP 429

SER 416 0.02 GLY 187 -0.08 TRP 429

SER 416 0.02 ILE 188 -0.08 TRP 429

SER 253 0.01 ILE 189 -0.11 TRP 429

SER 253 0.01 SER 190 -0.12 TRP 429

SER 416 0.01 GLU 191 -0.10 TRP 429

SER 253 0.01 LEU 192 -0.13 TRP 429

SER 253 0.01 PRO 193 -0.15 VAL 432

SER 253 0.01 SER 194 -0.14 VAL 432

SER 253 0.01 SER 195 -0.13 VAL 432

SER 253 0.01 ILE 196 -0.15 VAL 432

SER 39 0.01 SER 197 -0.16 VAL 432

ASP 43 0.01 SER 198 -0.14 VAL 432

ASP 43 0.01 VAL 199 -0.14 VAL 432

ASP 43 0.01 PHE 200 -0.17 VAL 432

ASP 43 0.01 LEU 201 -0.16 VAL 432

ASP 43 0.01 LEU 202 -0.15 LYS 433

ASP 43 0.01 GLY 203 -0.16 LYS 433

ASP 43 0.01 LYS 204 -0.17 LYS 433

ASP 43 0.01 ASN 205 -0.16 LYS 433

ASP 43 0.01 GLY 206 -0.15 LYS 433

SER 46 0.01 GLU 207 -0.13 LYS 433

SER 46 0.01 VAL 208 -0.13 LYS 433

SER 46 0.01 SER 209 -0.15 LYS 433

SER 253 0.01 GLY 210 -0.16 LYS 433

SER 253 0.01 LEU 211 -0.15 LYS 433

SER 253 0.01 VAL 212 -0.13 LYS 433

SER 253 0.01 VAL 213 -0.15 LYS 433

SER 253 0.01 LEU 214 -0.16 LYS 433

SER 253 0.01 SER 215 -0.14 LYS 433

SER 253 0.01 MET 216 -0.13 TRP 429

SER 253 0.01 LEU 217 -0.15 TRP 429

SER 253 0.01 LEU 218 -0.15 TRP 429

SER 253 0.01 ALA 219 -0.12 TRP 429

SER 253 0.01 PHE 220 -0.12 TRP 429

SER 253 0.01 PHE 221 -0.14 TRP 429

SER 253 0.01 ALA 222 -0.12 TRP 429

SER 416 0.02 LEU 223 -0.09 TRP 429

SER 416 0.01 PHE 224 -0.11 TRP 429

SER 255 0.01 LEU 225 -0.12 TRP 429

SER 416 0.02 LEU 226 -0.08 TRP 429

SER 416 0.03 ILE 227 -0.06 TRP 429

SER 416 0.02 ILE 228 -0.08 TRP 429

SER 416 0.02 PHE 229 -0.07 TRP 429

SER 420 0.05 PHE 230 -0.03 TRP 429

SER 420 0.07 GLU 231 -0.02 LYS 425

SER 420 0.05 ARG 232 -0.03 LYS 425

SER 420 0.07 SER 233 -0.00 ILE 363

MET 423 0.11 TYR 234 -0.00 MET 106

MET 423 0.13 ARG 235 -0.01 GLU 102

MET 423 0.16 LYS 236 -0.01 GLU 102

MET 423 0.20 VAL 237 -0.01 GLY 101

GLU 427 0.20 PHE 238 -0.01 GLY 101

LYS 430 0.26 VAL 239 -0.01 GLY 101

LYS 430 0.28 GLN 240 -0.01 GLY 101

LYS 430 0.35 TYR 241 -0.01 GLN 99

LYS 430 0.41 PRO 242 -0.01 GLN 99

LYS 430 0.39 LYS 243 -0.01 GLN 99

LYS 430 0.46 ARG 244 -0.01 GLN 99

LYS 430 0.53 GLN 245 -0.01 ASP 100

LYS 430 0.59 THR 246 -0.01 ASP 100

LYS 430 0.59 GLY 247 -0.01 GLN 99

LYS 430 0.68 GLY 248 -0.01 ASP 100

LYS 430 0.62 ARG 249 -0.01 GLN 99

LYS 430 0.56 PHE 250 -0.01 GLN 99

LYS 430 0.57 TYR 251 -0.01 GLY 101

SER 426 0.50 ASN 252 -0.01 GLY 101

SER 426 0.50 SER 253 -0.01 GLY 101

MET 423 0.48 ASP 254 -0.01 GLY 101

MET 423 0.35 SER 255 -0.01 GLY 101

SER 426 0.28 SER 256 -0.01 GLY 101

MET 423 0.24 TYR 257 -0.01 GLY 101

MET 423 0.27 ILE 258 -0.01 GLY 101

MET 423 0.21 PRO 259 -0.01 GLU 102

MET 423 0.20 LEU 260 -0.01 GLU 102

SER 420 0.16 LYS 261 -0.01 MET 106

SER 420 0.14 ILE 262 -0.00 MET 106

SER 420 0.14 ASN 263 -0.01 SER 109

SER 420 0.18 THR 264 -0.01 SER 109

SER 420 0.14 ALA 265 -0.01 GLU 169

SER 420 0.14 GLY 266 -0.01 GLU 169

SER 420 0.11 VAL 267 -0.01 ILE 403

SER 420 0.13 ILE 268 -0.01 ILE 403

SER 420 0.14 PRO 269 -0.01 ILE 403

SER 420 0.11 PRO 270 -0.01 ILE 403

SER 420 0.10 ILE 271 -0.01 ASN 2

SER 420 0.12 PHE 272 -0.00 ILE 403

SER 420 0.11 ALA 273 -0.01 VAL 3

SER 420 0.09 ASN 274 -0.01 VAL 3

SER 420 0.10 ALA 275 -0.01 VAL 3

SER 420 0.11 LEU 276 -0.01 VAL 3

SER 420 0.09 LEU 277 -0.01 VAL 3

SER 420 0.08 LEU 278 -0.01 VAL 3

SER 420 0.09 SER 279 -0.01 VAL 3

SER 420 0.09 SER 280 -0.01 VAL 3

SER 420 0.07 ILE 281 -0.01 VAL 3

SER 420 0.07 SER 282 -0.01 VAL 3

SER 420 0.08 LEU 283 -0.01 VAL 3

SER 420 0.07 VAL 284 -0.01 VAL 3

SER 420 0.06 ARG 285 -0.02 VAL 3

SER 420 0.06 PHE 286 -0.01 VAL 3

SER 420 0.06 HIS 287 -0.01 VAL 3

SER 420 0.05 SER 288 -0.02 VAL 3

SER 420 0.05 GLY 289 -0.02 VAL 3

SER 420 0.05 SER 290 -0.01 VAL 3

SER 420 0.06 GLU 291 -0.01 VAL 3

SER 420 0.06 TRP 292 -0.01 VAL 3

SER 420 0.06 ALA 293 -0.01 VAL 3

SER 420 0.05 ASP 294 -0.02 VAL 3

SER 420 0.06 VAL 295 -0.02 VAL 3

SER 420 0.07 LEU 296 -0.01 VAL 3

SER 420 0.06 LEU 297 -0.02 VAL 3

SER 420 0.05 ARG 298 -0.02 VAL 3

SER 420 0.06 TYR 299 -0.02 VAL 3

SER 420 0.06 LEU 300 -0.02 VAL 3

SER 420 0.05 SER 301 -0.02 VAL 3

SER 420 0.05 SER 302 -0.02 TRP 429

SER 420 0.04 GLU 303 -0.03 TRP 429

SER 420 0.05 GLY 304 -0.02 VAL 3

SER 420 0.05 VAL 305 -0.02 VAL 3

SER 420 0.06 LEU 306 -0.01 VAL 3

SER 420 0.07 TYR 307 -0.02 VAL 3

SER 420 0.06 VAL 308 -0.02 VAL 3

SER 420 0.07 SER 309 -0.01 VAL 3

SER 420 0.08 VAL 310 -0.01 VAL 3

SER 420 0.08 TYR 311 -0.01 VAL 3

SER 420 0.08 ILE 312 -0.01 VAL 3

SER 420 0.10 ALA 313 -0.01 GLU 354

SER 420 0.11 LEU 314 -0.01 GLU 354

SER 420 0.11 ILE 315 -0.01 VAL 3

SER 420 0.11 MET 316 -0.01 GLU 354

SER 420 0.13 PHE 317 -0.01 GLU 354

SER 420 0.14 PHE 318 -0.01 ASP 357

SER 420 0.14 THR 319 -0.00 ASP 357

SER 420 0.16 PHE 320 -0.01 ASP 357

GLU 427 0.18 PHE 321 -0.01 LYS 330

SER 420 0.19 TYR 322 -0.01 SER 81

SER 420 0.19 THR 323 -0.01 ILE 258

GLU 427 0.22 SER 324 -0.01 THR 329

GLU 427 0.24 LEU 325 -0.01 GLN 85

SER 420 0.25 VAL 326 -0.01 ARG 105

MET 423 0.26 PHE 327 -0.01 ILE 258

GLU 427 0.32 ASP 328 -0.01 GLN 99

GLU 427 0.32 THR 329 -0.01 VAL 89

GLU 427 0.36 LYS 330 -0.01 VAL 89

GLU 427 0.40 GLU 331 -0.02 GLN 99

MET 423 0.38 THR 332 -0.01 GLN 99

GLU 427 0.39 SER 333 -0.01 GLN 99

GLU 427 0.45 GLU 334 -0.02 GLN 99

GLU 427 0.48 MET 335 -0.02 GLN 99

GLU 427 0.44 LEU 336 -0.01 GLN 99

GLU 427 0.46 LYS 337 -0.01 GLN 99

GLU 427 0.54 LYS 338 -0.01 GLN 99

GLU 427 0.54 ASN 339 -0.01 GLN 99

LYS 430 0.49 GLY 340 -0.01 GLN 99

LYS 430 0.42 GLY 341 -0.01 GLN 99

LYS 430 0.37 PHE 342 -0.01 GLN 99

LYS 430 0.31 VAL 343 -0.01 GLN 99

LYS 430 0.27 PRO 344 -0.01 GLN 99

LYS 430 0.26 GLY 345 -0.01 GLN 99

LYS 430 0.30 LYS 346 -0.01 VAL 89

LYS 430 0.32 ARG 347 -0.01 VAL 89

LYS 430 0.36 PRO 348 -0.01 PRO 92

GLU 427 0.36 GLY 349 -0.01 VAL 89

GLU 427 0.32 LYS 350 -0.01 VAL 89

LYS 430 0.29 ALA 351 -0.01 VAL 89

GLU 427 0.30 THR 352 -0.01 VAL 89

GLU 427 0.30 LYS 353 -0.01 VAL 89

GLU 427 0.27 GLU 354 -0.01 PHE 317

GLU 427 0.25 TYR 355 -0.01 VAL 89

GLU 427 0.25 PHE 356 -0.01 VAL 89

GLU 427 0.24 ASP 357 -0.01 PHE 317

GLU 427 0.21 GLN 358 -0.01 GLY 361

GLU 427 0.19 VAL 359 -0.00 VAL 365

GLU 427 0.20 ILE 360 -0.00 PHE 317

GLU 427 0.18 GLY 361 -0.01 GLN 358

GLU 427 0.15 ARG 362 -0.00 LEU 366

MET 423 0.14 ILE 363 -0.00 SER 233

MET 423 0.14 THR 364 -0.00 ASP 357

MET 423 0.13 VAL 365 -0.01 GLY 361

SER 420 0.11 LEU 366 -0.00 ARG 362

SER 420 0.11 GLY 367 -0.00 SER 109

SER 420 0.11 ALA 368 -0.00 GLU 354

SER 420 0.09 ILE 369 -0.01 GLN 358

SER 420 0.07 TYR 370 -0.01 VAL 3

SER 420 0.08 LEU 371 -0.01 VAL 3

SER 420 0.07 SER 372 -0.01 VAL 3

SER 420 0.06 VAL 373 -0.02 TRP 429

SER 420 0.05 VAL 374 -0.04 TRP 429

SER 420 0.05 CYS 375 -0.03 TRP 429

SER 420 0.05 VAL 376 -0.03 TRP 429

SER 416 0.03 VAL 377 -0.05 TRP 429

SER 416 0.03 PRO 378 -0.06 TRP 429

SER 420 0.03 GLU 379 -0.05 TRP 429

SER 416 0.03 ILE 380 -0.06 TRP 429

SER 416 0.02 VAL 381 -0.08 TRP 429

SER 416 0.02 ARG 382 -0.07 TRP 429

SER 416 0.02 HIS 383 -0.06 TRP 429

SER 416 0.02 TYR 384 -0.08 TRP 429

SER 416 0.01 CYS 385 -0.10 TRP 429

SER 416 0.01 ALA 386 -0.09 TRP 429

SER 416 0.01 VAL 387 -0.10 TRP 429

SER 416 0.01 SER 388 -0.10 TRP 429

SER 416 0.02 PHE 389 -0.08 TRP 429

SER 416 0.02 THR 390 -0.08 TRP 429

SER 416 0.02 LEU 391 -0.09 TRP 429

SER 416 0.03 GLY 392 -0.06 TRP 429

SER 416 0.04 GLY 393 -0.05 TRP 429

SER 420 0.05 THR 394 -0.03 TRP 429

SER 416 0.04 SER 395 -0.06 TRP 429

SER 416 0.03 PHE 396 -0.07 TRP 429

SER 416 0.05 LEU 397 -0.04 TRP 429

SER 416 0.05 ILE 398 -0.04 TRP 429

SER 416 0.03 ILE 399 -0.07 TRP 429

SER 416 0.04 VAL 400 -0.07 TRP 429

SER 416 0.06 ASN 401 -0.03 TRP 429

SER 416 0.06 VAL 402 -0.04 TRP 429

SER 416 0.03 ILE 403 -0.08 LYS 425

SER 416 0.05 ASN 404 -0.06 LYS 425

SER 416 0.08 ASP 405 -0.02 LYS 425

SER 416 0.05 THR 406 -0.06 LYS 425

SER 416 0.03 PHE 407 -0.09 LYS 425

SER 416 0.08 SER 408 -0.03 LYS 425

SER 416 0.09 GLN 409 -0.02 LYS 425

GLU 331 0.05 VAL 410 -0.08 LYS 425

MET 335 0.06 GLN 411 -0.07 LYS 425

SER 416 0.12 THR 412 -0.02 GLY 10

GLU 331 0.08 GLN 413 -0.04 ASN 8

MET 335 0.10 VAL 414 -0.10 ARG 418

MET 335 0.14 TYR 415 -0.06 GLY 4

GLU 331 0.20 SER 416 -0.12 ASN 8

MET 335 0.19 GLY 417 -0.23 ASN 8

ASP 254 0.26 ARG 418 -0.25 GLY 4

ASP 254 0.37 TYR 419 -0.18 ASN 8

MET 335 0.39 SER 420 -0.23 ASN 8

ASN 339 0.32 ALA 421 -0.33 ASN 8

SER 253 0.43 LEU 422 -0.28 GLY 7

ASN 339 0.50 MET 423 -0.24 GLY 7

LYS 338 0.45 LYS 424 -0.30 GLY 7

GLY 248 0.46 LYS 425 -0.36 GLY 7

GLY 248 0.57 SER 426 -0.29 GLY 7

GLY 248 0.61 GLU 427 -0.27 GLY 7

GLY 248 0.53 LEU 428 -0.33 GLY 7

GLY 248 0.58 TRP 429 -0.33 GLY 7

GLY 248 0.68 LYS 430 -0.28 GLY 7

GLY 248 0.63 LYS 431 -0.28 GLY 7

GLY 248 0.57 VAL 432 -0.31 GLY 7

GLY 248 0.63 LYS 433 -0.29 GLY 7

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.

*** secyeg-tasr ***

CA distance fluctuations for 2605152131492949579

--- 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.

* secyeg-tasr *