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 2604262123532527858

--- normal mode 8 ---

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 0.12 SER 1 -0.05 ALA 214

ASN 300 0.13 THR 2 -0.05 LYS 185

ASN 300 0.15 ALA 3 -0.06 LYS 185

ASN 300 0.15 GLY 4 -0.06 LYS 185

ASN 300 0.13 LYS 5 -0.05 LYS 185

ASN 300 0.12 VAL 6 -0.05 LYS 185

ASN 300 0.11 ILE 7 -0.05 LYS 185

ASN 300 0.09 LYS 8 -0.04 LYS 185

GLN 244 0.09 CYS 9 -0.04 LYS 185

GLN 244 0.10 LYS 10 -0.04 LYS 185

GLN 244 0.10 ALA 11 -0.03 LYS 185

GLN 244 0.12 ALA 12 -0.03 LYS 185

GLN 244 0.12 VAL 13 -0.02 LYS 185

GLN 244 0.13 LEU 14 -0.02 PRO 60

LYS 247 0.13 TRP 15 -0.02 SER 177

LYS 247 0.14 GLU 16 -0.05 GLN 299

LYS 247 0.15 GLU 17 -0.08 GLN 299

LYS 247 0.17 LYS 18 -0.16 GLN 299

GLN 244 0.17 LYS 19 -0.12 GLN 299

GLN 244 0.17 PRO 20 -0.11 GLN 299

GLN 244 0.15 PHE 21 -0.06 GLN 299

GLN 244 0.13 SER 22 -0.05 GLN 299

GLN 244 0.12 ILE 23 -0.03 GLN 299

GLN 244 0.11 GLU 24 -0.03 LYS 185

GLN 244 0.10 GLU 25 -0.03 LYS 185

GLN 244 0.09 VAL 26 -0.04 LYS 185

ASN 300 0.10 GLU 27 -0.04 LYS 185

ASN 300 0.13 VAL 28 -0.05 LYS 185

ASN 300 0.14 ALA 29 -0.05 LYS 185

ASN 300 0.16 PRO 30 -0.06 LYS 185

ASN 300 0.19 PRO 31 -0.06 LYS 185

ASN 300 0.20 LYS 32 -0.06 LYS 185

ASN 300 0.23 ALA 33 -0.07 LYS 185

ASN 300 0.25 HIS 34 -0.08 LYS 185

ASN 300 0.23 GLU 35 -0.07 LYS 185

ASN 300 0.21 VAL 36 -0.07 LYS 185

ASN 300 0.18 ARG 37 -0.07 LYS 185

ASN 300 0.17 ILE 38 -0.07 LYS 185

ASN 300 0.14 LYS 39 -0.06 ALA 213

ASN 300 0.14 MET 40 -0.05 ALA 213

ASN 300 0.12 VAL 41 -0.06 ALA 213

ASN 300 0.11 ALA 42 -0.05 ALA 213

ASN 300 0.12 THR 43 -0.04 ALA 213

ASN 300 0.11 GLY 44 -0.05 ASP 297

ILE 224 0.13 ILE 45 -0.08 ASP 297

ILE 224 0.12 CYS 46 -0.09 ASP 297

ILE 269 0.16 ARG 47 -0.15 ASP 297

GLY 270 0.15 SER 48 -0.08 ASP 297

GLY 270 0.13 ASP 49 -0.05 THR 59

ARG 271 0.17 ASP 50 -0.11 ASP 297

ARG 271 0.18 HIS 51 -0.11 ASP 297

ARG 271 0.14 VAL 52 -0.06 THR 59

ARG 271 0.15 VAL 53 -0.08 GLN 299

ARG 271 0.19 SER 54 -0.16 GLN 299

ARG 271 0.15 GLY 55 -0.06 GLN 299

LEU 272 0.17 THR 56 -0.07 GLY 365

PRO 295 0.12 LEU 57 -0.05 GLY 365

ASP 297 0.16 VAL 58 -0.05 ILE 318

GLN 299 0.16 THR 59 -0.06 VAL 52

GLN 299 0.13 PRO 60 -0.05 VAL 52

LYS 247 0.11 LEU 61 -0.03 PHE 319

LYS 247 0.11 PRO 62 -0.03 ARG 120

LYS 247 0.10 VAL 63 -0.03 LYS 185

ASN 300 0.11 ILE 64 -0.03 LYS 185

ASN 300 0.12 ALA 65 -0.04 PRO 60

ASN 300 0.14 GLY 66 -0.04 LYS 185

ASN 300 0.21 HIS 67 -0.05 LYS 185

ASN 300 0.19 GLU 68 -0.06 SER 177

ASN 300 0.18 ALA 69 -0.06 LYS 185

ASN 300 0.18 ALA 70 -0.07 ALA 213

ASN 300 0.17 GLY 71 -0.07 ALA 213

ASN 300 0.17 ILE 72 -0.07 ALA 213

ASN 300 0.18 VAL 73 -0.07 ALA 214

ASN 300 0.16 GLU 74 -0.06 ALA 214

ASN 300 0.17 SER 75 -0.07 LYS 185

ASN 300 0.20 ILE 76 -0.08 LYS 185

ASN 300 0.20 GLY 77 -0.07 LYS 185

ASN 300 0.21 GLU 78 -0.07 LYS 185

ASN 300 0.23 GLY 79 -0.08 THR 190

ASN 300 0.24 VAL 80 -0.09 LYS 185

ASN 300 0.24 THR 81 -0.10 THR 190

ASN 300 0.25 THR 82 -0.11 LYS 185

ASN 300 0.22 VAL 83 -0.10 ALA 214

ASN 300 0.20 ARG 84 -0.09 ALA 214

ASN 300 0.18 PRO 85 -0.08 ALA 214

ASN 300 0.17 GLY 86 -0.08 ALA 214

ASN 300 0.19 ASP 87 -0.09 ALA 214

ASN 300 0.19 LYS 88 -0.09 ALA 213

ASN 300 0.21 VAL 89 -0.09 ALA 213

ASN 300 0.23 ILE 90 -0.09 LYS 185

ASN 300 0.25 PRO 91 -0.08 LYS 185

ASN 300 0.30 LEU 92 -0.09 LYS 185

ASN 300 0.32 PHE 93 -0.07 LYS 185

ASN 300 0.40 THR 94 -0.09 ASN 304

ASN 300 0.38 PRO 95 -0.09 ASN 304

ASN 300 0.39 GLN 96 -0.11 LYS 185

ASN 300 0.38 CYS 97 -0.10 ASN 304

ASN 300 0.38 GLY 98 -0.11 ASN 304

ASN 300 0.40 LYS 99 -0.12 ASN 304

ASN 300 0.45 CYS 100 -0.13 ASN 304

ASN 300 0.49 ARG 101 -0.15 ASN 304

ASN 300 0.52 VAL 102 -0.15 ASN 304

ASN 300 0.45 CYS 103 -0.13 ASN 304

ASN 300 0.44 LYS 104 -0.14 ASN 304

ASN 300 0.48 HIS 105 -0.17 THR 313

ASN 300 0.46 PRO 106 -0.18 THR 313

ASN 300 0.51 GLU 107 -0.20 THR 313

ASN 300 0.55 GLY 108 -0.16 THR 313

ASN 300 0.51 ASN 109 -0.13 ASN 304

ASN 300 0.55 PHE 110 -0.13 ASN 304

ASN 300 0.48 CYS 111 -0.12 ASN 304

ASN 300 0.49 LEU 112 -0.12 ASN 304

ASN 300 0.41 LYS 113 -0.10 ASN 304

ASN 300 0.42 ASN 114 -0.09 ASN 304

ASN 300 0.36 ASP 115 -0.08 ASN 304

ASN 300 0.40 LEU 116 -0.08 ASN 304

GLN 299 0.50 SER 117 -0.09 ASN 304

GLN 299 0.43 MET 118 -0.08 ASN 304

GLN 299 0.32 PRO 119 -0.06 ASN 304

GLN 299 0.27 ARG 120 -0.06 ASN 304

ASN 300 0.21 GLY 121 -0.05 ASN 304

ASN 300 0.22 THR 122 -0.05 ASN 304

ASN 300 0.24 MET 123 -0.06 ASN 304

ASN 300 0.28 GLN 124 -0.07 ASN 304

ASN 300 0.25 ASP 125 -0.07 ASN 304

ASN 300 0.23 GLY 126 -0.06 ASN 304

ASN 300 0.19 THR 127 -0.05 ASN 304

ASN 300 0.17 SER 128 -0.05 LYS 185

ASN 300 0.16 ARG 129 -0.05 LYS 185

ASN 300 0.13 PHE 130 -0.04 LYS 185

ASN 300 0.10 THR 131 -0.04 LYS 185

GLN 244 0.10 CYS 132 -0.03 LYS 185

LYS 247 0.10 ARG 133 -0.03 LYS 185

LYS 247 0.09 GLY 134 -0.03 LYS 185

LYS 247 0.09 LYS 135 -0.03 LYS 185

ASN 300 0.10 PRO 136 -0.04 LYS 185

ASN 300 0.10 ILE 137 -0.03 LYS 185

ASN 300 0.14 HIS 138 -0.04 LYS 185

ASN 300 0.18 HIS 139 -0.05 LYS 185

ASN 300 0.20 PHE 140 -0.04 LYS 185

ASN 300 0.28 LEU 141 -0.06 ASN 304

ASN 300 0.26 GLY 142 -0.06 LYS 185

ASN 300 0.23 THR 143 -0.06 LYS 185

ASN 300 0.17 SER 144 -0.05 LYS 185

ASN 300 0.15 THR 145 -0.05 LYS 185

ILE 224 0.10 PHE 146 -0.04 LYS 185

ASN 300 0.11 SER 147 -0.04 LYS 185

ASN 300 0.10 GLN 148 -0.05 LYS 185

ASN 300 0.13 TYR 149 -0.05 LYS 185

ASN 300 0.16 THR 150 -0.06 LYS 185

ASN 300 0.19 VAL 151 -0.06 LYS 185

ASN 300 0.23 VAL 152 -0.07 LYS 185

ASN 300 0.27 ASP 153 -0.08 LYS 185

ASN 300 0.27 GLU 154 -0.09 LYS 185

ASN 300 0.32 ILE 155 -0.10 LYS 185

ASN 300 0.30 SER 156 -0.09 LYS 185

ASN 300 0.27 VAL 157 -0.10 LYS 185

ASN 300 0.27 ALA 158 -0.11 LYS 185

ASN 300 0.24 LYS 159 -0.11 ALA 214

ASN 300 0.22 ILE 160 -0.12 ALA 213

ASN 300 0.20 ASP 161 -0.12 ALA 213

ASN 300 0.18 ALA 162 -0.10 ALA 213

ASN 300 0.16 ALA 163 -0.10 ALA 213

ASN 300 0.17 SER 164 -0.10 ALA 213

ASN 300 0.14 PRO 165 -0.09 ALA 213

ASN 300 0.15 LEU 166 -0.08 ALA 213

ASN 300 0.12 GLU 167 -0.06 ALA 213

ASN 300 0.13 LYS 168 -0.07 ALA 213

ASN 300 0.17 VAL 169 -0.09 ALA 213

ASN 300 0.17 CYS 170 -0.07 ALA 213

ASN 300 0.18 LEU 171 -0.06 ALA 213

ASN 300 0.23 ILE 172 -0.09 ALA 213

ASN 300 0.24 GLY 173 -0.07 LYS 185

ASN 300 0.26 CYS 174 -0.08 SER 177

ASN 300 0.21 GLY 175 -0.05 ASP 297

ASN 300 0.22 PHE 176 -0.05 PRO 305

ASN 300 0.29 SER 177 -0.08 CYS 174

ASN 300 0.32 THR 178 -0.07 ASN 304

ASN 300 0.28 GLY 179 -0.06 ASN 304

ASN 300 0.29 TYR 180 -0.08 LEU 331

ASN 300 0.38 GLY 181 -0.12 SER 327

ASN 300 0.42 SER 182 -0.08 SER 327

ASN 300 0.37 ALA 183 -0.11 SER 327

ASN 300 0.37 VAL 184 -0.17 SER 327

ASN 300 0.44 LYS 185 -0.20 SER 327

ASN 300 0.52 VAL 186 -0.14 PHE 322

ASN 300 0.48 ALA 187 -0.12 GLU 107

ASN 300 0.43 LYS 188 -0.16 SER 327

ASN 300 0.37 VAL 189 -0.15 LYS 330

ASN 300 0.34 THR 190 -0.16 LYS 330

ASN 300 0.28 GLN 191 -0.15 LYS 330

ASN 300 0.25 GLY 192 -0.13 LYS 330

ASN 300 0.27 SER 193 -0.12 LYS 330

ASN 300 0.23 THR 194 -0.10 LYS 330

ASN 300 0.24 CYS 195 -0.09 LYS 330

ASN 300 0.19 ALA 196 -0.07 LYS 330

ASN 300 0.18 VAL 197 -0.07 LYS 330

SER 364 0.15 PHE 198 -0.07 GLN 299

SER 364 0.17 GLY 199 -0.14 GLN 299

SER 364 0.14 LEU 200 -0.13 GLN 299

LEU 362 0.12 GLY 201 -0.14 GLN 299

ASN 300 0.09 GLY 202 -0.10 ASP 297

ASN 300 0.17 VAL 203 -0.08 ASP 297

ASN 300 0.14 GLY 204 -0.07 ASP 297

ASN 300 0.13 LEU 205 -0.07 ASP 297

ASN 300 0.20 SER 206 -0.06 LEU 331

ASN 300 0.25 VAL 207 -0.08 LEU 331

ASN 300 0.19 ILE 208 -0.09 LEU 331

ASN 300 0.20 MET 209 -0.11 LEU 331

ASN 300 0.27 GLY 210 -0.15 LEU 331

ASN 300 0.27 CYS 211 -0.13 LEU 331

ASN 300 0.22 LYS 212 -0.16 ASP 334

ASN 300 0.25 ALA 213 -0.23 ASP 334

ASN 300 0.29 ALA 214 -0.19 LYS 330

ASN 300 0.26 GLY 215 -0.17 ASP 334

ASN 300 0.25 ALA 216 -0.13 ASP 334

ASN 300 0.20 ALA 217 -0.12 ASP 334

ASN 300 0.18 ARG 218 -0.10 ASP 334

ASN 300 0.16 ILE 219 -0.09 ASP 334

SER 364 0.12 ILE 220 -0.07 ASP 334

SER 364 0.13 GLY 221 -0.07 GLN 299

SER 364 0.18 VAL 222 -0.13 GLN 299

SER 364 0.24 ASP 223 -0.21 GLN 299

SER 364 0.30 ILE 224 -0.29 GLN 299

GLY 365 0.31 ASN 225 -0.29 GLN 299

GLY 365 0.20 LYS 226 -0.23 GLN 299

GLU 366 0.17 ASP 227 -0.25 GLN 299

GLU 366 0.16 LYS 228 -0.22 GLN 299

GLU 366 0.14 PHE 229 -0.16 GLN 299

GLU 366 0.09 ALA 230 -0.14 GLN 299

THR 347 0.08 LYS 231 -0.11 GLN 299

SER 364 0.08 ALA 232 -0.09 GLN 299

SER 364 0.07 LYS 233 -0.07 GLN 299

ASN 300 0.06 GLU 234 -0.07 GLN 299

ASN 300 0.11 VAL 235 -0.06 PHE 340

ASN 300 0.13 GLY 236 -0.09 ASP 334

ASN 300 0.11 ALA 237 -0.08 ASP 334

ASN 300 0.10 THR 238 -0.09 ASP 334

SER 364 0.11 GLU 239 -0.07 ASP 334

SER 364 0.14 CYS 240 -0.10 GLN 299

SER 364 0.18 VAL 241 -0.13 GLN 299

SER 364 0.23 ASN 242 -0.19 GLN 299

SER 364 0.24 PRO 243 -0.19 GLN 299

SER 364 0.27 GLN 244 -0.25 GLN 299

SER 364 0.23 ASP 245 -0.20 GLN 299

SER 364 0.21 TYR 246 -0.16 GLN 299

SER 364 0.22 LYS 247 -0.14 GLN 299

SER 364 0.21 LYS 248 -0.11 GLN 299

SER 364 0.19 PRO 249 -0.11 GLN 299

SER 364 0.19 ILE 250 -0.09 GLN 299

SER 364 0.16 GLN 251 -0.07 GLU 107

SER 364 0.16 GLU 252 -0.08 PRO 106

SER 364 0.17 VAL 253 -0.07 PRO 106

SER 364 0.15 LEU 254 -0.08 GLU 107

SER 364 0.13 THR 255 -0.09 PRO 106

SER 364 0.14 GLU 256 -0.08 PRO 106

SER 364 0.14 MET 257 -0.08 PRO 106

ASN 300 0.16 SER 258 -0.09 PRO 106

ASN 300 0.15 ASN 259 -0.10 PRO 106

ASN 300 0.19 GLY 260 -0.11 PRO 106

ASN 300 0.21 GLY 261 -0.10 PRO 106

ASN 300 0.25 VAL 262 -0.10 GLU 107

ASN 300 0.32 ASP 263 -0.13 GLU 107

ASN 300 0.35 PHE 264 -0.12 GLU 107

ASN 300 0.31 SER 265 -0.09 GLU 107

ASN 300 0.31 PHE 266 -0.07 GLU 107

ASN 300 0.26 GLU 267 -0.05 PRO 305

ASN 300 0.20 VAL 268 -0.05 LYS 228

ARG 47 0.16 ILE 269 -0.13 GLN 299

HIS 51 0.17 GLY 270 -0.10 GLN 299

SER 54 0.19 ARG 271 -0.26 GLN 299

THR 56 0.17 LEU 272 -0.14 GLN 299

SER 54 0.17 ASP 273 -0.19 GLN 299

SER 54 0.16 THR 274 -0.11 GLN 299

ASN 300 0.24 MET 275 -0.07 ASN 225

ASN 300 0.20 VAL 276 -0.07 GLU 107

SER 364 0.14 THR 277 -0.07 GLU 107

ASN 300 0.23 ALA 278 -0.08 GLU 107

ASN 300 0.36 LEU 279 -0.10 GLU 107

ASN 300 0.23 SER 280 -0.10 GLU 107

ASN 300 0.19 CYS 281 -0.09 GLU 107

ASN 300 0.30 CYS 282 -0.11 GLU 107

ASN 300 0.29 GLN 283 -0.13 PRO 106

ASN 300 0.31 GLU 284 -0.14 PRO 106

ASN 300 0.35 ALA 285 -0.16 PRO 106

ASN 300 0.40 TYR 286 -0.17 PRO 106

ASN 300 0.40 GLY 287 -0.15 GLU 107

ASN 300 0.48 VAL 288 -0.16 GLU 107

ASN 300 0.49 SER 289 -0.12 GLU 107

ASN 300 0.52 VAL 290 -0.10 GLU 107

ASN 300 0.53 ILE 291 -0.10 ASN 304

ASN 300 0.41 VAL 292 -0.08 ASN 304

ASN 300 0.34 GLY 293 -0.10 MET 303

ASN 300 0.32 VAL 294 -0.08 MET 303

LEU 116 0.14 PRO 295 -0.13 GLY 365

LEU 116 0.24 PRO 296 -0.13 GLY 365

SER 117 0.25 ASP 297 -0.22 GLY 365

LEU 272 0.16 SER 298 -0.12 GLY 365

SER 117 0.50 GLN 299 -0.32 SER 364

LYS 315 0.75 ASN 300 -0.20 GLN 244

LEU 308 0.13 LEU 301 -0.08 ASN 225

LEU 308 0.09 SER 302 -0.11 ASN 300

GLN 299 0.13 MET 303 -0.12 GLU 107

ASN 300 0.14 ASN 304 -0.21 PRO 305

ASN 300 0.38 PRO 305 -0.21 ASN 304

ASN 300 0.29 MET 306 -0.15 HIS 105

ASN 300 0.35 LEU 307 -0.14 GLU 107

ASN 300 0.51 LEU 308 -0.17 GLU 107

ASN 300 0.43 LEU 309 -0.16 PRO 106

ASN 300 0.36 SER 310 -0.15 PRO 106

ASN 300 0.45 GLY 311 -0.18 PRO 106

ASN 300 0.49 ARG 312 -0.17 GLU 107

ASN 300 0.62 THR 313 -0.20 GLU 107

ASN 300 0.73 TRP 314 -0.15 GLU 107

ASN 300 0.75 LYS 315 -0.14 GLU 107

ASN 300 0.74 GLY 316 -0.13 ASN 304

ASN 300 0.62 ALA 317 -0.13 ASN 304

ASN 300 0.52 ILE 318 -0.10 ASN 304

ASN 300 0.41 PHE 319 -0.09 ASN 304

ASN 300 0.42 GLY 320 -0.09 ASN 304

ASN 300 0.48 GLY 321 -0.13 ASN 304

ASN 300 0.42 PHE 322 -0.18 LYS 185

ASN 300 0.42 LYS 323 -0.15 LYS 185

ASN 300 0.38 SER 324 -0.12 LYS 185

ASN 300 0.34 LYS 325 -0.14 LYS 185

ASN 300 0.34 ASP 326 -0.17 LYS 185

ASN 300 0.33 SER 327 -0.20 LYS 185

ASN 300 0.29 VAL 328 -0.15 LYS 185

ASN 300 0.26 PRO 329 -0.15 ALA 214

ASN 300 0.27 LYS 330 -0.19 ALA 214

ASN 300 0.26 LEU 331 -0.19 ALA 213

ASN 300 0.22 VAL 332 -0.15 ALA 213

ASN 300 0.22 ALA 333 -0.18 ALA 213

ASN 300 0.23 ASP 334 -0.23 ALA 213

ASN 300 0.20 PHE 335 -0.15 ALA 213

ASN 300 0.19 MET 336 -0.13 ALA 213

ASN 300 0.20 ALA 337 -0.11 ALA 213

ASN 300 0.18 LYS 338 -0.08 ALA 163

ASN 300 0.21 LYS 339 -0.10 ALA 213

ASN 300 0.20 PHE 340 -0.08 GLY 236

ASN 300 0.15 ALA 341 -0.07 PHE 340

ASN 300 0.14 LEU 342 -0.04 ASP 297

ASN 300 0.09 ASP 343 -0.07 ASP 297

ASN 300 0.07 PRO 344 -0.08 ASP 297

ASN 300 0.07 LEU 345 -0.09 ASP 297

ASN 225 0.09 ILE 346 -0.09 ASP 297

ASN 225 0.13 THR 347 -0.12 GLN 299

ASN 225 0.14 HIS 348 -0.12 GLN 299

ASN 225 0.12 VAL 349 -0.08 ASP 297

ASN 225 0.13 LEU 350 -0.08 GLN 299

ASN 225 0.12 PRO 351 -0.06 GLN 299

ASN 225 0.11 PHE 352 -0.05 ASP 297

ILE 224 0.12 GLU 353 -0.06 GLN 299

ASN 225 0.14 LYS 354 -0.09 GLN 299

ILE 224 0.14 ILE 355 -0.08 GLN 299

ILE 224 0.16 ASN 356 -0.13 GLN 299

ASN 225 0.17 GLU 357 -0.15 GLN 299

ASN 225 0.17 GLY 358 -0.13 GLN 299

ILE 224 0.18 PHE 359 -0.16 GLN 299

ILE 224 0.21 ASP 360 -0.21 GLN 299

ASN 225 0.22 LEU 361 -0.20 GLN 299

ILE 224 0.22 LEU 362 -0.20 GLN 299

ILE 224 0.25 ARG 363 -0.27 GLN 299

ILE 224 0.30 SER 364 -0.32 GLN 299

ASN 225 0.31 GLY 365 -0.31 GLN 299

ASN 225 0.27 GLU 366 -0.26 GLN 299

ASN 225 0.19 SER 367 -0.19 GLN 299

ASN 225 0.13 ILE 368 -0.15 GLN 299

ASN 225 0.13 ARG 369 -0.11 ASP 297

ASN 225 0.14 THR 370 -0.10 ASP 297

ASN 225 0.11 ILE 371 -0.07 ASP 297

ASN 225 0.11 LEU 372 -0.06 ASP 297

ASN 225 0.09 THR 373 -0.05 ALA 213

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 2604262123532527858

--- normal mode 8 ---

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

* *