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

* closed_cutoff10 *

CA distance fluctuations for 2604261326212470324

--- normal mode 12 ---

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
SER 424 0.05 ALA 1 -0.28 LYS 423

SER 424 0.05 SER 2 -0.25 LYS 423

SER 424 0.05 SER 3 -0.20 LYS 423

SER 424 0.06 THR 4 -0.17 LYS 423

SER 424 0.06 ASN 5 -0.14 LYS 423

SER 424 0.07 LEU 6 -0.17 LYS 423

SER 424 0.07 LYS 7 -0.10 LYS 423

SER 424 0.07 ASP 8 -0.10 LYS 423

SER 424 0.06 VAL 9 -0.17 LYS 423

SER 424 0.07 LEU 10 -0.17 LYS 423

MET 425 0.07 ALA 11 -0.10 LYS 423

MET 425 0.07 LEU 13 -0.21 LYS 423

MET 425 0.08 ILE 14 -0.17 LYS 423

MET 425 0.08 PRO 15 -0.14 LYS 423

MET 425 0.08 LYS 16 -0.22 LYS 423

MET 425 0.08 GLU 17 -0.26 LYS 423

MET 425 0.09 GLN 18 -0.19 LYS 423

PRO 422 0.11 ALA 19 -0.20 LYS 423

MET 425 0.08 ARG 20 -0.31 LYS 423

MET 425 0.09 ILE 21 -0.33 LYS 423

PRO 422 0.17 LYS 22 -0.23 LYS 423

PRO 422 0.15 THR 23 -0.28 LYS 423

MET 425 0.08 PHE 24 -0.40 LYS 423

PRO 422 0.16 ARG 25 -0.36 LYS 423

PRO 422 0.23 GLN 26 -0.27 LYS 423

PRO 422 0.17 GLN 27 -0.37 LYS 423

PRO 422 0.12 HIS 28 -0.49 LYS 423

PRO 422 0.21 GLY 29 -0.43 LYS 423

THR 427 0.10 THR 31 -0.63 LYS 423

THR 427 0.09 ALA 32 -0.81 LYS 423

THR 427 0.04 GLY 34 -1.24 LYS 423

THR 427 0.05 GLN 35 -1.34 LYS 423

GLY 50 0.06 ILE 36 -1.32 LYS 423

GLU 420 0.05 THR 37 -1.24 LYS 423

GLU 420 0.08 VAL 38 -0.99 LYS 423

GLU 420 0.06 ASP 39 -1.15 LYS 423

GLU 420 0.05 MET 40 -1.39 LYS 423

GLU 420 0.11 SER 41 -1.00 LYS 423

GLU 420 0.10 TYR 42 -0.84 LYS 423

GLU 420 0.04 GLY 43 -1.05 LYS 423

THR 247 0.06 GLY 44 -1.18 PRO 422

HIS 246 0.05 MET 45 -1.24 LYS 423

VAL 243 0.04 ARG 46 -1.39 LYS 423

GLY 271 0.03 GLY 47 -1.60 LYS 423

ALA 32 0.03 MET 48 -1.58 LYS 423

GLY 241 0.04 LYS 49 -1.27 LYS 423

MET 425 0.09 GLY 50 -0.98 LYS 423

SER 424 0.13 LEU 51 -0.74 LYS 423

SER 424 0.09 TYR 53 -0.58 LYS 423

SER 424 0.08 GLU 54 -0.53 LYS 423

SER 424 0.08 THR 55 -0.50 LYS 423

SER 424 0.07 SER 56 -0.63 LYS 423

SER 424 0.05 VAL 57 -0.77 LYS 423

SER 424 0.04 LEU 58 -0.86 LYS 423

GLY 34 0.03 ASP 59 -0.92 LYS 423

GLY 34 0.03 PRO 60 -0.99 LYS 423

GLY 34 0.03 ASP 61 -0.91 LYS 423

GLY 34 0.03 GLU 62 -0.81 LYS 423

SER 424 0.03 GLY 63 -0.79 LYS 423

SER 424 0.04 ILE 64 -0.73 LYS 423

SER 424 0.04 ARG 65 -0.68 LYS 423

SER 424 0.05 PHE 66 -0.57 LYS 423

SER 424 0.06 ARG 67 -0.54 LYS 423

SER 424 0.05 GLY 68 -0.60 LYS 423

SER 424 0.04 PHE 69 -0.58 LYS 423

SER 424 0.04 SER 70 -0.61 LYS 423

SER 424 0.04 ILE 71 -0.57 LYS 423

SER 424 0.03 PRO 72 -0.54 LYS 423

SER 424 0.03 GLU 73 -0.53 LYS 423

SER 424 0.04 CYS 74 -0.48 LYS 423

SER 424 0.04 GLN 75 -0.47 LYS 423

SER 424 0.04 LYS 76 -0.45 LYS 423

SER 424 0.04 LEU 77 -0.42 LYS 423

SER 424 0.05 LEU 78 -0.39 LYS 423

SER 424 0.05 PRO 79 -0.34 LYS 423

SER 424 0.04 LYS 80 -0.33 LYS 423

SER 424 0.04 GLY 82 -0.27 LYS 423

LYS 339 0.04 GLY 84 -0.32 LYS 423

SER 424 0.04 GLU 86 -0.38 LYS 423

SER 424 0.05 PRO 87 -0.38 LYS 423

SER 424 0.05 LEU 88 -0.33 LYS 423

SER 424 0.06 PRO 89 -0.33 LYS 423

SER 424 0.06 GLU 90 -0.28 LYS 423

SER 424 0.06 GLY 91 -0.32 LYS 423

SER 424 0.06 LEU 92 -0.38 LYS 423

SER 424 0.07 PHE 93 -0.32 LYS 423

SER 424 0.07 TRP 94 -0.30 LYS 423

SER 424 0.06 LEU 95 -0.38 LYS 423

SER 424 0.07 LEU 96 -0.40 LYS 423

SER 424 0.08 VAL 97 -0.31 LYS 423

SER 424 0.07 THR 98 -0.32 LYS 423

SER 424 0.06 GLY 99 -0.41 LYS 423

SER 424 0.06 GLN 100 -0.38 LYS 423

SER 424 0.05 ILE 101 -0.38 LYS 423

SER 424 0.05 PRO 102 -0.32 LYS 423

SER 424 0.05 THR 103 -0.29 LYS 423

SER 424 0.06 GLN 106 -0.23 LYS 423

SER 424 0.06 VAL 107 -0.25 LYS 423

SER 424 0.06 SER 108 -0.20 LYS 423

SER 424 0.06 TRP 109 -0.17 LYS 423

SER 424 0.06 SER 111 -0.21 PRO 422

SER 424 0.06 LYS 112 -0.17 PRO 422

SER 424 0.07 GLU 113 -0.16 PRO 422

SER 424 0.07 TRP 114 -0.20 PRO 422

SER 424 0.06 ALA 115 -0.19 PRO 422

SER 424 0.07 LYS 116 -0.15 PRO 422

SER 424 0.07 ARG 117 -0.15 PRO 422

SER 424 0.07 ALA 118 -0.18 PRO 422

SER 424 0.07 ALA 119 -0.16 PRO 422

SER 424 0.07 LEU 120 -0.17 PRO 422

LYS 423 0.10 PRO 121 -0.14 PRO 422

LYS 423 0.11 SER 122 -0.13 PRO 422

LYS 423 0.15 HIS 123 -0.14 PRO 422

LYS 423 0.10 VAL 124 -0.18 PRO 422

SER 424 0.07 VAL 125 -0.19 PRO 422

LYS 423 0.10 THR 126 -0.17 PRO 422

LYS 423 0.11 MET 127 -0.19 PRO 422

SER 424 0.07 LEU 128 -0.23 PRO 422

SER 424 0.06 ASP 129 -0.21 PRO 422

LYS 423 0.08 ASN 130 -0.21 PRO 422

SER 424 0.06 PHE 131 -0.25 PRO 422

SER 424 0.06 PRO 132 -0.26 PRO 422

SER 424 0.05 THR 133 -0.29 PRO 422

SER 424 0.05 ASN 134 -0.32 PRO 422

SER 424 0.06 LEU 135 -0.33 PRO 422

SER 424 0.06 HIS 136 -0.38 PRO 422

SER 424 0.06 PRO 137 -0.38 PRO 422

SER 424 0.07 MET 138 -0.43 PRO 422

SER 424 0.08 SER 139 -0.38 PRO 422

SER 424 0.08 GLN 140 -0.33 PRO 422

SER 424 0.08 LEU 141 -0.35 PRO 422

SER 424 0.09 SER 142 -0.36 PRO 422

SER 424 0.09 ALA 143 -0.29 PRO 422

SER 424 0.09 ALA 144 -0.26 PRO 422

SER 424 0.10 ILE 145 -0.27 PRO 422

LYS 423 0.12 THR 146 -0.23 PRO 422

LYS 423 0.16 ALA 147 -0.17 PRO 422

LYS 423 0.11 LEU 148 -0.17 PRO 422

LYS 423 0.17 ASN 149 -0.13 PRO 422

LYS 423 0.22 SER 150 -0.07 PRO 422

LYS 423 0.16 GLU 151 -0.08 PRO 422

LYS 423 0.16 SER 152 -0.07 PRO 422

LYS 423 0.16 ASN 153 -0.04 GLU 420

LYS 423 0.17 PHE 154 -0.05 GLU 420

LYS 423 0.26 ALA 155 -0.04 GLY 312

LYS 423 0.28 ARG 156 -0.03 GLY 312

LYS 423 0.26 ALA 157 -0.03 GLU 420

LYS 423 0.32 TYR 158 -0.04 GLY 312

LYS 423 0.40 ALA 159 -0.04 GLY 312

LYS 423 0.36 GLU 160 -0.03 GLY 312

LYS 423 0.38 GLY 161 -0.04 GLY 312

LYS 423 0.29 ILE 162 -0.03 GLU 420

PRO 422 0.23 ARG 164 -0.05 GLU 420

PRO 422 0.17 THR 165 -0.05 GLU 420

LYS 423 0.11 LYS 166 -0.05 GLU 420

LYS 423 0.12 TYR 167 -0.06 GLU 420

SER 424 0.09 TRP 168 -0.07 GLU 420

SER 424 0.09 GLU 169 -0.06 GLU 420

SER 424 0.10 VAL 171 -0.08 PRO 422

SER 424 0.09 TYR 172 -0.11 PRO 422

SER 424 0.08 GLU 173 -0.10 PRO 422

SER 424 0.09 ALA 175 -0.20 PRO 422

SER 424 0.08 MET 176 -0.18 PRO 422

SER 424 0.08 ASP 177 -0.17 PRO 422

SER 424 0.09 LEU 178 -0.23 PRO 422

SER 424 0.08 ILE 179 -0.27 PRO 422

SER 424 0.07 ALA 180 -0.23 PRO 422

SER 424 0.08 LYS 181 -0.23 PRO 422

SER 424 0.08 LEU 182 -0.29 PRO 422

SER 424 0.07 PRO 183 -0.29 PRO 422

SER 424 0.07 CYS 184 -0.25 PRO 422

SER 424 0.07 VAL 185 -0.27 PRO 422

SER 424 0.07 ALA 186 -0.32 PRO 422

SER 424 0.06 ALA 187 -0.29 PRO 422

SER 424 0.06 LYS 188 -0.26 PRO 422

SER 424 0.06 ILE 189 -0.30 PRO 422

SER 424 0.05 TYR 190 -0.31 PRO 422

SER 424 0.05 ARG 191 -0.27 PRO 422

SER 424 0.06 ASN 192 -0.26 PRO 422

SER 424 0.05 LEU 193 -0.30 PRO 422

SER 424 0.05 TYR 194 -0.30 PRO 422

SER 424 0.05 ARG 195 -0.27 PRO 422

SER 424 0.05 ALA 196 -0.25 PRO 422

SER 424 0.05 GLY 197 -0.23 PRO 422

SER 424 0.05 SER 198 -0.23 PRO 422

SER 424 0.05 SER 199 -0.21 PRO 422

SER 424 0.06 ILE 200 -0.23 PRO 422

SER 424 0.06 GLY 201 -0.20 PRO 422

SER 424 0.06 ALA 202 -0.19 PRO 422

SER 424 0.06 ILE 203 -0.20 PRO 422

SER 424 0.05 ASP 204 -0.19 PRO 422

SER 424 0.06 SER 205 -0.17 PRO 422

SER 424 0.05 LYS 206 -0.18 PRO 422

SER 424 0.05 LEU 207 -0.21 PRO 422

SER 424 0.05 ASP 208 -0.24 PRO 422

SER 424 0.06 TRP 209 -0.26 PRO 422

SER 424 0.06 SER 210 -0.29 PRO 422

SER 424 0.05 HIS 211 -0.27 PRO 422

SER 424 0.06 ASN 212 -0.25 PRO 422

SER 424 0.06 PHE 213 -0.28 PRO 422

SER 424 0.05 THR 214 -0.29 PRO 422

SER 424 0.05 ASN 215 -0.26 PRO 422

SER 424 0.05 MET 216 -0.26 PRO 422

SER 424 0.05 LEU 217 -0.29 PRO 422

SER 424 0.05 GLY 218 -0.27 PRO 422

SER 424 0.04 TYR 219 -0.29 PRO 422

SER 424 0.04 THR 220 -0.27 PRO 422

SER 424 0.04 ASP 221 -0.28 PRO 422

SER 424 0.03 GLN 223 -0.31 LYS 423

SER 424 0.04 PHE 224 -0.32 PRO 422

SER 424 0.04 THR 225 -0.30 PRO 422

SER 424 0.04 GLU 226 -0.33 LYS 423

SER 424 0.04 LEU 227 -0.36 LYS 423

SER 424 0.05 MET 228 -0.35 PRO 422

SER 424 0.05 ARG 229 -0.34 LYS 423

SER 424 0.04 LEU 230 -0.40 LYS 423

SER 424 0.05 TYR 231 -0.41 PRO 422

SER 424 0.06 LEU 232 -0.39 PRO 422

SER 424 0.05 THR 233 -0.41 LYS 423

SER 424 0.05 ILE 234 -0.49 LYS 423

SER 424 0.06 HIS 235 -0.49 PRO 422

SER 424 0.07 SER 236 -0.46 PRO 422

SER 424 0.07 ASP 237 -0.52 LYS 423

SER 424 0.07 HIS 238 -0.65 LYS 423

SER 424 0.07 GLU 239 -0.71 LYS 423

SER 424 0.10 GLY 240 -0.69 PRO 422

SER 424 0.08 GLY 241 -0.94 PRO 422

SER 424 0.08 ASN 242 -0.89 PRO 422

SER 424 0.10 VAL 243 -0.92 PRO 422

SER 424 0.11 SER 244 -0.72 PRO 422

SER 424 0.11 ALA 245 -0.67 PRO 422

SER 424 0.14 HIS 246 -0.82 PRO 422

SER 424 0.16 THR 247 -0.71 PRO 422

SER 424 0.15 SER 248 -0.50 PRO 422

SER 424 0.16 HIS 249 -0.46 PRO 422

SER 424 0.20 LEU 250 -0.47 PRO 422

SER 424 0.17 VAL 251 -0.31 PRO 422

SER 424 0.15 GLY 252 -0.20 PRO 422

SER 424 0.15 SER 253 -0.20 GLU 420

ARG 421 0.29 ALA 254 -0.09 GLU 420

LYS 423 0.23 LEU 255 -0.09 GLU 420

LYS 423 0.23 SER 256 -0.07 PRO 422

LYS 423 0.14 ASP 257 -0.11 PRO 422

SER 424 0.11 PRO 258 -0.21 PRO 422

SER 424 0.11 TYR 259 -0.22 PRO 422

SER 424 0.12 LEU 260 -0.23 PRO 422

SER 424 0.13 SER 261 -0.32 PRO 422

SER 424 0.12 PHE 262 -0.38 PRO 422

SER 424 0.11 ALA 263 -0.37 PRO 422

SER 424 0.13 ALA 264 -0.45 PRO 422

SER 424 0.12 ALA 265 -0.56 PRO 422

SER 424 0.10 MET 266 -0.51 PRO 422

SER 424 0.10 ASN 267 -0.55 PRO 422

SER 424 0.10 GLY 268 -0.70 PRO 422

SER 424 0.08 LEU 269 -0.64 PRO 422

SER 424 0.07 ALA 270 -0.58 PRO 422

SER 424 0.06 GLY 271 -0.67 PRO 422

SER 424 0.03 PRO 272 -0.64 PRO 422

ALA 321 0.03 LEU 273 -0.75 PRO 422

SER 424 0.05 HIS 274 -0.74 PRO 422

SER 424 0.05 GLY 275 -0.63 PRO 422

SER 424 0.05 LEU 276 -0.58 PRO 422

SER 424 0.03 ALA 277 -0.60 PRO 422

SER 424 0.03 ASN 278 -0.54 PRO 422

SER 424 0.03 GLN 279 -0.50 PRO 422

SER 424 0.02 GLU 280 -0.52 PRO 422

VAL 314 0.01 VAL 281 -0.51 PRO 422

SER 424 0.02 LEU 282 -0.46 PRO 422

VAL 314 0.02 TRP 284 -0.47 PRO 422

VAL 314 0.02 LEU 285 -0.45 PRO 422

ARG 313 0.03 GLN 287 -0.41 PRO 422

THR 308 0.05 LEU 288 -0.42 PRO 422

THR 308 0.04 GLN 289 -0.39 PRO 422

SER 311 0.03 LYS 290 -0.37 PRO 422

PRO 342 0.02 ASP 298 -0.50 LYS 423

LYS 348 0.02 LEU 301 -0.49 LYS 423

THR 331 0.02 ARG 302 -0.53 LYS 423

THR 331 0.02 ASP 303 -0.50 LYS 423

GLN 289 0.03 TYR 304 -0.48 LYS 423

GLN 289 0.02 ILE 305 -0.54 LYS 423

GLN 289 0.02 TRP 306 -0.54 LYS 423

GLN 289 0.03 ASN 307 -0.48 LYS 423

LEU 288 0.05 THR 308 -0.50 LYS 423

LEU 288 0.03 LEU 309 -0.56 LYS 423

LEU 288 0.03 ASN 310 -0.51 LYS 423

LEU 288 0.04 SER 311 -0.49 PRO 422

LEU 288 0.04 GLY 312 -0.54 PRO 422

LEU 288 0.04 ARG 313 -0.57 PRO 422

LEU 288 0.04 VAL 314 -0.61 PRO 422

LEU 288 0.04 VAL 315 -0.59 LYS 423

VAL 314 0.02 PRO 316 -0.58 PRO 422

ALA 32 0.01 GLY 317 -0.60 LYS 423

LEU 288 0.01 TYR 318 -0.69 LYS 423

ASN 369 0.01 GLY 319 -0.80 LYS 423

ARG 324 0.01 HIS 320 -0.87 LYS 423

LEU 273 0.03 ALA 321 -1.01 LYS 423

ALA 32 0.02 VAL 322 -1.06 LYS 423

ALA 32 0.02 LEU 323 -0.95 LYS 423

GLY 34 0.02 ARG 324 -0.96 LYS 423

GLY 34 0.02 LYS 325 -0.84 LYS 423

TRP 371 0.02 THR 326 -0.75 LYS 423

ALA 32 0.02 ASP 327 -0.72 LYS 423

LYS 355 0.03 PRO 328 -0.67 LYS 423

SER 424 0.03 ARG 329 -0.60 LYS 423

TYR 354 0.03 TYR 330 -0.60 LYS 423

TYR 354 0.04 THR 331 -0.60 LYS 423

LYS 355 0.03 CYS 332 -0.55 LYS 423

TYR 354 0.03 GLN 333 -0.51 LYS 423

ALA 351 0.03 ARG 334 -0.52 LYS 423

GLU 86 0.03 GLU 335 -0.50 LYS 423

GLU 86 0.03 PHE 336 -0.45 LYS 423

GLU 86 0.03 ALA 337 -0.44 LYS 423

GLY 84 0.03 LEU 338 -0.46 LYS 423

GLY 84 0.04 LYS 339 -0.42 LYS 423

GLY 84 0.03 HIS 340 -0.39 LYS 423

GLY 84 0.03 LEU 341 -0.39 LYS 423

ASP 298 0.02 PRO 342 -0.42 LYS 423

GLY 84 0.02 ASP 344 -0.38 LYS 423

THR 308 0.02 PRO 345 -0.39 LYS 423

THR 308 0.02 MET 346 -0.40 LYS 423

GLY 84 0.02 PHE 347 -0.44 LYS 423

ASP 298 0.02 LYS 348 -0.45 LYS 423

THR 308 0.03 LEU 349 -0.46 LYS 423

THR 308 0.02 VAL 350 -0.50 LYS 423

THR 331 0.03 ALA 351 -0.52 LYS 423

THR 331 0.02 GLN 352 -0.52 LYS 423

THR 331 0.03 LEU 353 -0.55 LYS 423

THR 331 0.04 TYR 354 -0.59 LYS 423

THR 331 0.04 LYS 355 -0.60 LYS 423

THR 331 0.03 ILE 356 -0.59 LYS 423

THR 331 0.02 VAL 357 -0.63 LYS 423

THR 331 0.02 PRO 358 -0.70 LYS 423

THR 331 0.02 ASN 359 -0.68 LYS 423

THR 331 0.02 VAL 360 -0.66 LYS 423

THR 331 0.02 LEU 361 -0.72 LYS 423

PRO 72 0.01 LEU 362 -0.76 LYS 423

PRO 72 0.01 GLU 363 -0.71 LYS 423

GLN 289 0.01 GLN 364 -0.71 LYS 423

GLN 289 0.01 GLY 365 -0.80 LYS 423

LEU 288 0.02 ALA 367 -0.88 LYS 423

LEU 288 0.01 ASN 369 -0.91 LYS 423

LEU 288 0.01 PRO 370 -0.80 LYS 423

THR 326 0.02 TRP 371 -0.76 LYS 423

TRP 371 0.01 PRO 372 -0.69 LYS 423

ALA 32 0.02 ASN 373 -0.68 LYS 423

SER 424 0.03 VAL 374 -0.60 LYS 423

SER 424 0.03 ASP 375 -0.56 PRO 422

SER 424 0.01 ALA 376 -0.55 LYS 423

SER 424 0.02 HIS 377 -0.51 LYS 423

SER 424 0.03 SER 378 -0.47 PRO 422

SER 424 0.03 GLY 379 -0.45 PRO 422

SER 424 0.02 VAL 380 -0.42 PRO 422

SER 424 0.03 LEU 381 -0.40 PRO 422

SER 424 0.03 LEU 382 -0.39 PRO 422

SER 424 0.03 GLN 383 -0.38 PRO 422

SER 424 0.03 TYR 384 -0.36 PRO 422

SER 424 0.03 TYR 385 -0.34 PRO 422

SER 424 0.03 GLY 386 -0.33 PRO 422

SER 424 0.04 MET 387 -0.35 PRO 422

SER 424 0.03 THR 388 -0.37 PRO 422

SER 424 0.04 GLU 389 -0.38 PRO 422

SER 424 0.04 MET 390 -0.42 PRO 422

SER 424 0.04 ASN 391 -0.42 PRO 422

SER 424 0.05 TYR 392 -0.41 PRO 422

SER 424 0.05 TYR 393 -0.45 PRO 422

SER 424 0.06 THR 394 -0.49 PRO 422

SER 424 0.07 VAL 395 -0.43 PRO 422

SER 424 0.06 LEU 396 -0.42 PRO 422

SER 424 0.06 PHE 397 -0.49 PRO 422

SER 424 0.08 GLY 398 -0.47 PRO 422

SER 424 0.07 VAL 399 -0.40 PRO 422

SER 424 0.07 SER 400 -0.42 PRO 422

SER 424 0.08 ARG 401 -0.48 PRO 422

SER 424 0.09 ALA 402 -0.40 PRO 422

SER 424 0.08 LEU 403 -0.37 PRO 422

SER 424 0.08 GLY 404 -0.43 PRO 422

SER 424 0.10 VAL 405 -0.44 PRO 422

SER 424 0.10 LEU 406 -0.31 PRO 422

SER 424 0.09 ALA 407 -0.29 PRO 422

SER 424 0.10 GLN 408 -0.32 LYS 423

SER 424 0.11 LEU 409 -0.25 PRO 422

SER 424 0.10 ILE 410 -0.15 PRO 422

SER 424 0.10 TRP 411 -0.23 LYS 423

SER 424 0.11 SER 412 -0.19 LYS 423

SER 424 0.11 ARG 413 -0.11 GLU 420

SER 424 0.09 ALA 414 -0.09 GLU 420

MET 425 0.10 LEU 415 -0.15 LYS 423

PRO 422 0.14 GLY 416 -0.10 GLU 420

MET 425 0.14 PHE 417 -0.13 GLU 420

PRO 422 0.25 PRO 418 -0.16 GLU 420

PRO 422 0.17 LEU 419 -0.38 GLU 420

SER 424 0.33 GLU 420 -0.38 LEU 419

ALA 254 0.29 ARG 421 -0.61 GLY 50

PRO 418 0.25 PRO 422 -1.18 MET 45

ALA 159 0.40 LYS 423 -1.60 GLY 47

GLU 420 0.33 SER 424 -0.08 GLY 312

GLU 420 0.27 MET 425 -0.14 GLY 312

GLU 420 0.21 SER 426 -0.19 GLY 312

GLU 420 0.18 THR 427 -0.22 GLY 312

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.

*** closed_cutoff10 ***

CA distance fluctuations for 2604261326212470324

--- normal mode 12 ---

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

* closed_cutoff10 *