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elNémo has been relocated.
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* shlomo *

CA distance fluctuations for 2605130610242337669

--- 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
LEU 334 0.15 GLN 6 -0.16 PRO 326

LEU 334 0.16 GLY 7 -0.17 PRO 326

LEU 334 0.18 ILE 8 -0.18 ASN 324

LEU 334 0.19 GLY 9 -0.18 TYR 354

LEU 334 0.21 VAL 10 -0.20 TYR 354

LEU 334 0.20 ILE 11 -0.22 TYR 354

LEU 334 0.22 SER 12 -0.24 TYR 354

LEU 334 0.22 THR 13 -0.27 TYR 354

LEU 334 0.25 ALA 14 -0.29 TYR 354

LEU 334 0.27 TYR 15 -0.29 TYR 354

LEU 334 0.30 PHE 16 -0.28 TYR 354

LEU 334 0.30 THR 17 -0.29 PRO 326

LEU 334 0.30 MET 18 -0.30 PRO 326

LEU 334 0.32 LYS 19 -0.33 PRO 326

LEU 334 0.27 ASP 20 -0.31 PRO 326

LEU 334 0.25 LYS 21 -0.30 PRO 326

LEU 334 0.20 HIS 22 -0.27 PRO 326

LEU 334 0.19 SER 23 -0.25 PRO 326

LEU 334 0.22 ILE 24 -0.26 PRO 326

LEU 334 0.21 LYS 25 -0.25 PRO 326

LEU 334 0.21 THR 26 -0.24 PRO 326

LEU 334 0.16 VAL 27 -0.21 PRO 326

LEU 334 0.15 LYS 28 -0.21 TYR 354

LEU 334 0.17 LYS 29 -0.23 TYR 354

LEU 334 0.14 TYR 30 -0.23 TYR 354

LEU 334 0.14 TRP 31 -0.24 TYR 354

LEU 334 0.13 TRP 32 -0.23 TYR 354

LEU 334 0.12 LYS 33 -0.24 TYR 354

LEU 334 0.14 ASN 34 -0.25 TYR 354

LEU 334 0.16 CYS 35 -0.24 TYR 354

LEU 334 0.18 VAL 36 -0.25 TYR 354

LEU 334 0.18 ILE 37 -0.23 TYR 354

LEU 334 0.19 GLN 38 -0.22 TYR 354

LEU 334 0.18 HIS 39 -0.20 PRO 326

LEU 334 0.20 VAL 40 -0.22 PRO 326

LEU 334 0.19 LYS 41 -0.22 PRO 326

LEU 334 0.21 TYR 42 -0.23 PRO 326

LEU 334 0.19 HIS 43 -0.23 PRO 326

LEU 334 0.17 GLY 44 -0.21 PRO 326

LEU 334 0.17 LYS 45 -0.20 PRO 326

LEU 334 0.18 THR 46 -0.19 PRO 326

LEU 334 0.20 PHE 47 -0.20 PRO 326

LEU 334 0.19 ILE 48 -0.19 TYR 354

LEU 334 0.21 ILE 49 -0.22 TYR 354

LEU 334 0.20 ALA 50 -0.23 TYR 354

LEU 334 0.21 THR 51 -0.25 TYR 354

LEU 334 0.18 VAL 52 -0.25 TYR 354

LEU 334 0.17 GLY 53 -0.26 LYS 353

LEU 334 0.17 TYR 54 -0.27 LYS 353

LEU 334 0.16 GLY 55 -0.25 LYS 353

LEU 334 0.15 LYS 56 -0.23 LYS 353

LEU 334 0.14 ALA 57 -0.23 LYS 353

LEU 334 0.15 ASN 58 -0.23 LYS 353

LEU 334 0.16 ALA 59 -0.22 LYS 353

LEU 334 0.14 ALA 60 -0.21 LYS 353

LEU 334 0.14 MET 61 -0.21 LYS 353

LEU 334 0.15 THR 62 -0.21 TYR 354

LEU 334 0.15 ILE 63 -0.20 TYR 354

LEU 334 0.13 THR 64 -0.19 TYR 354

LEU 334 0.13 TYR 65 -0.19 TYR 354

LEU 334 0.14 LEU 66 -0.19 TYR 354

LEU 334 0.14 LEU 67 -0.17 TYR 354

LEU 334 0.12 GLU 68 -0.17 TYR 354

LEU 334 0.12 LYS 69 -0.17 TYR 354

LEU 334 0.13 TYR 70 -0.17 TYR 354

LEU 334 0.13 PRO 71 -0.15 TYR 354

LEU 334 0.14 GLY 72 -0.15 TYR 354

LEU 334 0.15 LEU 73 -0.16 TYR 354

LEU 334 0.15 GLN 74 -0.15 ASN 324

LEU 334 0.17 THR 75 -0.17 ASN 324

LEU 334 0.18 ILE 76 -0.17 TYR 354

LEU 334 0.20 LEU 77 -0.19 TYR 354

LEU 334 0.21 ASN 78 -0.21 TYR 354

LEU 334 0.23 VAL 79 -0.23 TYR 354

LEU 334 0.24 ASP 80 -0.25 TYR 354

LEU 334 0.25 LEU 81 -0.28 LYS 353

LEU 334 0.23 ALA 82 -0.27 LYS 353

LEU 334 0.22 LEU 83 -0.28 LYS 353

LEU 334 0.20 SER 84 -0.25 LYS 353

LEU 334 0.19 THR 85 -0.23 LYS 353

LEU 334 0.19 ASN 86 -0.21 LYS 353

LEU 334 0.19 ASP 87 -0.21 LYS 353

LEU 334 0.20 LYS 88 -0.19 ASN 324

LEU 334 0.21 HIS 89 -0.22 LYS 353

LEU 334 0.23 ASP 90 -0.26 LYS 353

LEU 334 0.25 THR 91 -0.30 ASP 355

LEU 334 0.27 GLY 92 -0.31 ASN 324

LEU 334 0.24 ASP 93 -0.27 ASN 324

LEU 334 0.24 THR 94 -0.26 ASN 324

LEU 334 0.22 THR 95 -0.22 ASN 324

LEU 334 0.20 ILE 96 -0.21 ASN 324

LEU 334 0.19 SER 97 -0.18 ASN 324

LEU 334 0.18 THR 98 -0.16 ASN 324

LEU 334 0.17 LYS 99 -0.16 LYS 353

LEU 334 0.17 PHE 100 -0.18 LYS 353

LEU 334 0.16 ILE 101 -0.19 LYS 353

LEU 334 0.15 TYR 102 -0.20 LYS 353

LEU 334 0.15 ARG 103 -0.21 LYS 353

LEU 334 0.14 ASP 104 -0.22 LYS 353

LEU 334 0.13 ALA 105 -0.20 LYS 353

LEU 334 0.12 ASP 106 -0.19 LYS 353

LEU 334 0.12 LEU 107 -0.18 LYS 353

LEU 334 0.12 THR 108 -0.17 LYS 353

LEU 334 0.11 VAL 109 -0.17 LYS 353

LEU 334 0.10 PHE 110 -0.16 LYS 353

LEU 334 0.11 LYS 111 -0.15 LYS 353

LEU 334 0.11 ASP 112 -0.14 LYS 353

LEU 334 0.12 ILE 113 -0.16 LYS 353

LEU 334 0.13 LYS 114 -0.16 LYS 353

LEU 334 0.13 TYR 115 -0.18 LYS 353

LEU 334 0.14 GLY 116 -0.19 LYS 353

LEU 334 0.13 GLN 117 -0.17 LYS 353

LEU 334 0.12 ILE 118 -0.18 LYS 353

LEU 334 0.11 VAL 119 -0.17 LYS 353

LEU 334 0.11 ASN 120 -0.16 LYS 353

LEU 334 0.12 GLU 121 -0.16 LYS 353

LEU 334 0.13 PRO 122 -0.15 LYS 353

LEU 334 0.14 GLU 123 -0.16 LYS 353

LEU 334 0.15 SER 124 -0.16 LYS 353

LEU 334 0.15 PHE 125 -0.16 LYS 353

LEU 334 0.15 GLN 126 -0.15 LYS 353

LEU 334 0.16 PHE 127 -0.15 ASN 324

LEU 334 0.16 ASP 128 -0.15 ASN 324

LEU 334 0.16 GLY 129 -0.16 ASN 324

LEU 334 0.16 GLU 130 -0.17 ASN 324

LEU 334 0.17 PHE 131 -0.18 ASN 324

LEU 334 0.18 ALA 132 -0.18 ASN 324

LEU 334 0.17 LYS 133 -0.19 ASN 324

LEU 334 0.18 VAL 134 -0.20 ASN 324

LEU 334 0.19 VAL 135 -0.21 ASN 324

LEU 334 0.19 LYS 136 -0.21 ASN 324

LEU 334 0.19 ASP 137 -0.22 ASN 324

LEU 334 0.20 PHE 138 -0.24 ASN 324

LEU 334 0.20 LYS 139 -0.25 ASN 324

LEU 334 0.22 LEU 140 -0.27 ASN 324

LEU 334 0.22 GLY 141 -0.27 ASN 324

LEU 334 0.22 LEU 142 -0.24 ASN 324

LEU 334 0.21 THR 143 -0.22 ASN 324

LEU 334 0.19 GLU 144 -0.19 ASN 324

LEU 334 0.19 GLY 145 -0.17 ASN 324

LEU 334 0.18 VAL 146 -0.18 LYS 353

LEU 334 0.18 THR 147 -0.20 LYS 353

LEU 334 0.17 GLY 148 -0.21 LYS 353

LEU 334 0.17 THR 149 -0.22 LYS 353

LEU 334 0.16 ALA 150 -0.24 LYS 353

LEU 334 0.16 ASP 151 -0.25 LYS 353

LEU 334 0.16 MET 152 -0.27 LYS 353

LEU 334 0.18 LEU 153 -0.28 LYS 353

LEU 334 0.17 ILE 154 -0.27 LYS 353

LEU 334 0.17 TYR 155 -0.30 LYS 353

LEU 334 0.16 ASN 156 -0.28 LYS 353

LEU 334 0.16 SER 157 -0.26 LYS 353

LEU 334 0.14 LYS 158 -0.25 LYS 353

LEU 334 0.15 GLN 159 -0.25 LYS 353

LEU 334 0.16 PHE 160 -0.24 LYS 353

LEU 334 0.15 LYS 161 -0.22 LYS 353

LEU 334 0.14 GLU 162 -0.22 LYS 353

LEU 334 0.15 MET 163 -0.21 LYS 353

LEU 334 0.15 VAL 164 -0.20 LYS 353

LEU 334 0.14 ASP 165 -0.19 LYS 353

LEU 334 0.14 LYS 166 -0.18 LYS 353

LEU 334 0.15 TYR 167 -0.18 LYS 353

LEU 334 0.15 GLY 168 -0.17 LYS 353

LEU 334 0.16 HIS 169 -0.17 LYS 353

LEU 334 0.16 THR 170 -0.17 LYS 353

LEU 334 0.17 ILE 171 -0.19 LYS 353

LEU 334 0.18 ASP 172 -0.20 LYS 353

LEU 334 0.20 VAL 173 -0.22 LYS 353

LEU 334 0.19 ILE 174 -0.24 LYS 353

LEU 334 0.19 ASP 175 -0.25 LYS 353

LEU 334 0.18 THR 176 -0.25 LYS 353

LEU 334 0.18 GLU 177 -0.23 LYS 353

LEU 334 0.18 ALA 178 -0.22 LYS 353

LEU 334 0.16 GLY 179 -0.20 LYS 353

LEU 334 0.15 ALA 180 -0.20 LYS 353

LEU 334 0.16 ILE 181 -0.20 LYS 353

LEU 334 0.16 ALA 182 -0.18 LYS 353

LEU 334 0.14 GLN 183 -0.18 LYS 353

LEU 334 0.14 VAL 184 -0.18 LYS 353

LEU 334 0.15 ALA 185 -0.17 LYS 353

LEU 334 0.14 LYS 186 -0.16 LYS 353

LEU 334 0.13 LYS 187 -0.16 LYS 353

LEU 334 0.13 SER 188 -0.15 LYS 353

LEU 334 0.14 SER 189 -0.14 LYS 353

LEU 334 0.15 ILE 190 -0.15 TYR 354

LEU 334 0.16 ASN 191 -0.16 ASN 324

LEU 334 0.17 TYR 192 -0.16 LYS 353

LEU 334 0.19 ILE 193 -0.18 ASN 324

LEU 334 0.20 ALA 194 -0.19 LYS 353

LEU 334 0.22 LEU 195 -0.22 ASN 324

LEU 334 0.23 LYS 196 -0.23 LYS 353

LEU 334 0.25 ILE 197 -0.26 ASN 324

LEU 334 0.24 ILE 198 -0.27 LYS 353

LEU 334 0.25 TYR 199 -0.32 LYS 353

LEU 334 0.23 ASN 200 -0.31 LYS 353

LEU 334 0.21 ASN 201 -0.28 LYS 353

LEU 334 0.19 ALA 202 -0.29 LYS 353

LEU 334 0.18 LEU 203 -0.28 LYS 353

LEU 334 0.20 SER 204 -0.32 LYS 353

LEU 333 0.20 PRO 205 -0.35 LYS 353

LEU 334 0.22 TRP 206 -0.36 LYS 353

LEU 334 0.21 ASP 207 -0.38 LYS 353

LEU 333 0.22 ASN 208 -0.42 LYS 353

LEU 333 0.24 ASP 209 -0.43 LYS 353

GLU 337 0.27 PRO 210 -0.50 LYS 353

GLU 337 0.30 ILE 211 -0.49 LYS 353

LEU 333 0.29 HIS 212 -0.46 LYS 353

LEU 333 0.34 LYS 213 -0.50 TYR 354

GLU 337 0.34 PHE 214 -0.49 ASP 355

LEU 334 0.29 LYS 215 -0.41 ASP 355

LEU 334 0.32 MET 216 -0.41 TYR 354

LEU 334 0.36 TYR 217 -0.48 ASN 324

LEU 334 0.32 GLU 218 -0.42 ASN 324

LEU 334 0.30 THR 219 -0.36 ASN 324

LEU 334 0.34 VAL 220 -0.38 ASN 324

LEU 334 0.35 ASN 221 -0.42 ASN 324

LEU 334 0.30 THR 222 -0.36 ASN 324

LEU 334 0.30 LEU 223 -0.32 ASN 324

LEU 334 0.32 LYS 224 -0.35 ASN 324

LEU 334 0.30 TYR 225 -0.35 ASN 324

LEU 334 0.27 LEU 226 -0.30 ASN 324

LEU 334 0.27 LEU 227 -0.28 ASN 324

LEU 334 0.28 ARG 228 -0.30 ASN 324

LEU 334 0.25 ARG 229 -0.29 ASN 324

LEU 334 0.24 LEU 230 -0.26 ASN 324

LEU 334 0.23 PHE 231 -0.25 ASN 324

LEU 334 0.23 ASN 232 -0.26 ASN 324

LEU 334 0.21 LEU 233 -0.24 ASN 324

LEU 334 0.20 LEU 234 -0.22 ASN 324

LEU 334 0.20 SER 235 -0.21 ASN 324

LEU 334 0.18 SER 236 -0.22 ASN 324

LEU 334 0.17 ASN 237 -0.20 ASN 324

LEU 334 0.17 TYR 238 -0.20 ASN 324

LEU 334 0.17 ILE 239 -0.20 ASN 324

LEU 334 0.18 ILE 240 -0.22 ASN 324

LEU 334 0.17 ASP 241 -0.22 ASN 324

LEU 334 0.18 LEU 242 -0.24 ASN 324

LEU 334 0.18 SER 243 -0.23 ASN 324

LEU 334 0.17 GLN 244 -0.24 ASN 324

LEU 334 0.18 CYS 245 -0.26 ASN 324

LEU 334 0.18 SER 246 -0.28 ASN 324

LEU 334 0.19 GLN 247 -0.31 ASN 324

LEU 334 0.19 ASP 248 -0.33 ASN 324

LEU 334 0.18 ASP 249 -0.30 ASN 324

LEU 334 0.20 LEU 250 -0.30 ASN 324

LEU 334 0.21 ASP 251 -0.33 ASN 324

LEU 334 0.20 SER 252 -0.32 ASN 324

LEU 334 0.20 ILE 253 -0.29 ASN 324

LEU 334 0.22 ASN 254 -0.30 ASN 324

LEU 334 0.22 GLU 255 -0.33 ASN 324

LEU 334 0.20 LEU 256 -0.30 ASN 324

LEU 334 0.21 PHE 257 -0.28 ASN 324

LEU 334 0.24 GLU 258 -0.30 ASN 324

LEU 334 0.22 ILE 259 -0.30 ALA 325

LEU 334 0.19 LYS 260 -0.27 ALA 325

LEU 334 0.19 HIS 261 -0.25 ASN 324

LEU 334 0.17 ASP 262 -0.23 ASN 324

LEU 334 0.16 GLN 263 -0.23 ALA 325

LEU 334 0.16 TRP 264 -0.25 ASN 324

LEU 334 0.16 ILE 265 -0.23 ASN 324

LEU 334 0.14 LYS 266 -0.22 ASN 324

LEU 334 0.14 LEU 267 -0.23 ALA 325

LEU 334 0.13 PHE 268 -0.23 ASN 324

LEU 334 0.13 LYS 269 -0.21 ASN 324

LEU 334 0.13 PRO 270 -0.20 ASN 324

LEU 334 0.13 ASN 271 -0.19 ASN 324

LEU 334 0.14 THR 272 -0.20 ASN 324

LEU 334 0.15 HIS 273 -0.19 ASN 324

LEU 334 0.15 LYS 274 -0.20 ASN 324

LEU 334 0.16 VAL 275 -0.22 ASN 324

LEU 334 0.16 LEU 276 -0.22 ASN 324

LEU 334 0.16 SER 277 -0.23 ASN 324

LEU 334 0.15 GLY 278 -0.22 ASN 324

LEU 334 0.14 PHE 279 -0.21 ASN 324

LEU 334 0.13 GLY 280 -0.22 ASN 324

LEU 334 0.14 PRO 281 -0.24 ASN 324

LEU 334 0.15 SER 282 -0.25 ASN 324

LEU 334 0.15 LEU 283 -0.24 ASN 324

LEU 334 0.14 MET 284 -0.22 ASN 324

LEU 334 0.14 LEU 285 -0.21 ASN 324

LEU 334 0.14 VAL 286 -0.20 ASN 324

LEU 334 0.13 ASP 287 -0.18 ASN 324

LEU 334 0.13 LYS 288 -0.17 ASN 324

LEU 334 0.12 GLN 289 -0.16 ASN 324

LEU 334 0.12 GLU 290 -0.17 ASN 324

LEU 334 0.12 LYS 291 -0.17 ASN 324

LEU 334 0.12 THR 292 -0.18 ASN 324

LEU 334 0.12 PRO 293 -0.20 ASN 324

LEU 334 0.13 VAL 294 -0.21 ASN 324

LEU 334 0.13 ALA 295 -0.22 ASN 324

LEU 334 0.14 LEU 296 -0.24 ASN 324

LEU 334 0.14 ASP 297 -0.26 ASN 324

LEU 334 0.14 ILE 298 -0.28 ASN 324

LEU 334 0.14 ILE 299 -0.30 ASN 324

LEU 334 0.14 GLN 300 -0.33 ASN 324

GLN 338 0.13 VAL 301 -0.35 ASN 324

GLN 338 0.13 ILE 302 -0.39 ASN 324

GLN 338 0.16 ARG 303 -0.39 ASN 324

GLN 338 0.16 SER 304 -0.42 ASN 324

GLN 338 0.19 LYS 305 -0.45 ASN 324

ARG 331 0.01 ASN 324 -0.94 TYR 354

LYS 328 0.01 ALA 325 -0.95 TYR 354

PRO 210 0.14 PRO 326 -0.71 ASP 343

ASN 208 0.13 LYS 327 -0.63 TYR 354

ASN 208 0.06 LYS 328 -0.77 TRP 348

PRO 210 0.13 TRP 329 -0.76 ASP 343

LYS 213 0.28 LEU 330 -0.49 ASP 343

LYS 213 0.23 ARG 331 -0.52 TRP 348

LYS 213 0.21 LYS 332 -0.50 TRP 348

TYR 217 0.34 LEU 333 -0.31 ASP 343

TYR 217 0.36 LEU 334 -0.27 TRP 348

TYR 217 0.24 PHE 335 -0.35 TRP 348

LYS 213 0.22 LEU 336 -0.44 VAL 341

PHE 214 0.34 GLU 337 -0.10 GLU 416

ASP 460 0.33 GLN 338 -0.08 SER 414

PHE 214 0.23 VAL 339 -0.19 GLU 416

GLN 338 0.14 ARG 340 -0.41 LEU 336

LYS 305 0.07 VAL 341 -0.51 TRP 329

LYS 305 0.06 ASN 342 -0.64 ALA 325

LYS 360 0.07 ASP 343 -0.84 ALA 325

LYS 360 0.08 ASP 344 -0.87 ALA 325

ASN 499 0.06 GLU 345 -0.74 ALA 325

ASN 499 0.05 LEU 346 -0.76 ALA 325

ASN 499 0.06 LEU 347 -0.72 ALA 325

ASN 499 0.07 TRP 348 -0.85 ALA 325

ASN 499 0.08 ASN 349 -0.94 ALA 325

ASN 499 0.10 LYS 350 -0.80 ALA 325

ASN 499 0.12 SER 351 -0.82 ALA 325

ASN 499 0.15 ALA 352 -0.76 ALA 325

ASN 499 0.13 LYS 353 -0.85 ASN 324

ASN 499 0.10 TYR 354 -0.95 ALA 325

ASN 499 0.12 ASP 355 -0.86 ALA 325

ASN 499 0.08 LEU 356 -0.94 ALA 325

ASN 499 0.08 ASN 357 -0.82 ALA 325

GLN 338 0.08 ASN 358 -0.72 ALA 325

GLN 338 0.12 GLU 359 -0.63 ALA 325

GLN 338 0.13 LYS 360 -0.54 ALA 325

GLN 338 0.12 LEU 361 -0.51 ALA 325

GLN 338 0.10 TYR 362 -0.45 ALA 325

GLN 338 0.08 LYS 363 -0.42 ALA 325

GLN 338 0.08 ILE 364 -0.39 ALA 325

ALA 352 0.07 GLU 365 -0.36 ALA 325

GLN 338 0.08 THR 366 -0.38 ALA 325

GLN 338 0.10 VAL 367 -0.38 ALA 325

GLN 338 0.08 ALA 368 -0.34 ALA 325

GLN 338 0.08 ASN 369 -0.33 ALA 325

GLN 338 0.10 GLU 370 -0.34 ALA 325

LEU 334 0.10 ILE 371 -0.33 ALA 325

LEU 334 0.09 ALA 372 -0.31 ALA 325

GLN 338 0.09 ALA 373 -0.31 ASN 324

LEU 334 0.10 ALA 374 -0.31 ASN 324

LEU 334 0.10 ILE 375 -0.29 ASN 324

LEU 334 0.09 ALA 376 -0.28 ASN 324

LEU 334 0.09 GLU 377 -0.28 ASN 324

LEU 334 0.11 LYS 378 -0.27 ASN 324

LEU 334 0.10 CYS 379 -0.26 ASN 324

LEU 334 0.09 GLN 380 -0.25 ASN 324

LEU 334 0.10 ASP 381 -0.24 ASN 324

LEU 334 0.10 LYS 382 -0.23 ASN 324

LEU 334 0.10 SER 383 -0.22 ASN 324

LEU 334 0.11 SER 384 -0.21 ASN 324

LEU 334 0.12 TYR 385 -0.21 ASN 324

LEU 334 0.12 THR 386 -0.20 ASN 324

LEU 334 0.12 TYR 387 -0.19 ASN 324

LEU 334 0.12 ASN 388 -0.17 ASN 324

LEU 334 0.11 GLY 389 -0.17 ASN 324

LEU 334 0.11 ALA 390 -0.18 ASN 324

LEU 334 0.11 THR 391 -0.19 ASN 324

LEU 334 0.11 VAL 392 -0.20 ASN 324

LEU 334 0.11 PRO 393 -0.20 ASN 324

GLN 338 0.15 ASP 402 -0.40 ALA 325

GLN 338 0.14 ALA 403 -0.42 ALA 325

GLN 338 0.15 ARG 404 -0.47 ALA 325

GLN 338 0.12 ILE 405 -0.46 ALA 325

GLN 338 0.10 SER 406 -0.48 ALA 325

GLN 338 0.07 PHE 407 -0.43 ALA 325

ALA 352 0.04 TYR 408 -0.40 ALA 325

ALA 352 0.04 ILE 409 -0.34 ALA 325

ALA 352 0.05 THR 410 -0.32 ALA 325

ALA 352 0.05 HIS 411 -0.28 ALA 325

ALA 352 0.06 ASN 412 -0.28 ALA 325

ALA 352 0.06 GLN 413 -0.25 ALA 325

ALA 352 0.05 SER 414 -0.25 ALA 325

ALA 352 0.06 HIS 415 -0.29 ALA 325

ALA 352 0.04 GLU 416 -0.28 ALA 325

ALA 352 0.03 PHE 417 -0.31 ALA 325

LEU 334 0.04 VAL 418 -0.30 ALA 325

LEU 334 0.07 GLU 419 -0.32 ALA 325

LEU 334 0.12 ASP 420 -0.27 ALA 325

LEU 334 0.17 LYS 421 -0.29 ALA 325

LEU 334 0.17 ASN 422 -0.25 ALA 325

LEU 334 0.12 PHE 423 -0.26 ALA 325

LEU 334 0.10 GLY 424 -0.31 ALA 325

LEU 334 0.13 THR 425 -0.31 ALA 325

LEU 334 0.12 GLN 426 -0.28 ALA 325

LEU 334 0.08 LEU 427 -0.30 ALA 325

LEU 334 0.09 VAL 428 -0.33 ALA 325

LEU 334 0.10 SER 429 -0.31 ALA 325

LEU 334 0.08 ASN 430 -0.29 ALA 325

LEU 334 0.06 GLU 431 -0.32 ALA 325

LEU 334 0.08 PHE 432 -0.32 ALA 325

LEU 334 0.08 VAL 433 -0.29 ALA 325

LEU 334 0.06 LYS 434 -0.29 ALA 325

LEU 334 0.06 TYR 435 -0.31 ALA 325

LEU 334 0.08 LEU 436 -0.30 ALA 325

LEU 334 0.07 ASN 437 -0.28 ALA 325

ALA 352 0.06 GLU 438 -0.28 ALA 325

LEU 334 0.07 ALA 439 -0.29 ALA 325

LEU 334 0.08 LEU 440 -0.27 ALA 325

LEU 334 0.07 LYS 441 -0.26 ALA 325

LEU 334 0.07 ASP 442 -0.25 ALA 325

LEU 334 0.08 VAL 443 -0.25 ALA 325

LEU 334 0.08 ASP 444 -0.24 ALA 325

LEU 334 0.09 SER 445 -0.24 ALA 325

LEU 334 0.10 PRO 446 -0.23 ASN 324

LEU 334 0.11 TYR 447 -0.23 ASN 324

LEU 334 0.11 GLN 448 -0.22 ALA 325

LEU 334 0.12 GLN 449 -0.24 ALA 325

LEU 334 0.12 ILE 450 -0.26 ALA 325

LEU 334 0.13 VAL 451 -0.27 ALA 325

LEU 334 0.13 ILE 452 -0.30 ALA 325

LEU 334 0.15 TYR 453 -0.31 ALA 325

LEU 334 0.14 MET 454 -0.35 ALA 325

LEU 334 0.16 THR 455 -0.38 ALA 325

GLN 338 0.14 ILE 456 -0.41 ALA 325

GLN 338 0.16 PRO 457 -0.46 ALA 325

GLN 338 0.19 ALA 458 -0.44 ALA 325

GLN 338 0.23 LEU 459 -0.45 ALA 325

GLN 338 0.33 ASP 460 -0.52 PRO 326

GLN 338 0.27 TYR 461 -0.55 ALA 325

GLN 338 0.26 ARG 462 -0.45 ALA 325

GLN 338 0.20 LYS 463 -0.41 ALA 325

LEU 334 0.19 ILE 464 -0.35 ALA 325

LEU 334 0.18 SER 465 -0.34 ALA 325

LEU 334 0.15 VAL 466 -0.32 ALA 325

LEU 334 0.15 PHE 467 -0.29 ALA 325

LEU 334 0.12 ILE 468 -0.28 ALA 325

LEU 334 0.12 PRO 469 -0.26 ALA 325

LEU 334 0.11 SER 470 -0.25 ALA 325

LEU 334 0.10 ASN 471 -0.23 ALA 325

LEU 334 0.11 LYS 472 -0.22 ALA 325

LEU 334 0.10 GLY 473 -0.21 ALA 325

LEU 334 0.10 ALA 474 -0.22 ALA 325

LEU 334 0.09 ASN 475 -0.22 ALA 325

LEU 334 0.08 ARG 476 -0.23 ALA 325

LEU 334 0.08 GLY 477 -0.24 ALA 325

LEU 334 0.09 VAL 478 -0.25 ALA 325

LEU 334 0.08 LYS 479 -0.25 ALA 325

LEU 334 0.09 PHE 480 -0.26 ALA 325

LEU 334 0.09 VAL 481 -0.25 ALA 325

LEU 334 0.08 ALA 482 -0.24 ALA 325

LEU 334 0.08 LEU 483 -0.25 ALA 325

LEU 334 0.07 ASN 484 -0.24 ALA 325

LEU 334 0.05 GLN 485 -0.25 ALA 325

SER 23 0.05 LYS 486 -0.24 ALA 325

LEU 334 0.05 LEU 487 -0.26 ALA 325

ALA 352 0.05 GLN 488 -0.27 ALA 325

ALA 352 0.06 ARG 489 -0.26 ALA 325

ALA 352 0.05 ASP 490 -0.26 ALA 325

ALA 352 0.05 TYR 491 -0.28 ALA 325

ALA 352 0.06 THR 492 -0.32 ALA 325

ALA 352 0.06 VAL 493 -0.35 ALA 325

ALA 352 0.07 VAL 494 -0.37 ALA 325

ALA 352 0.08 ASP 495 -0.41 ALA 325

ALA 352 0.10 ILE 496 -0.45 ALA 325

ALA 352 0.11 THR 497 -0.45 ALA 325

ALA 352 0.13 ARG 498 -0.41 ALA 325

ALA 352 0.15 ASN 499 -0.41 ALA 325

ALA 352 0.14 ASP 500 -0.37 ALA 325

ALA 352 0.12 TYR 501 -0.36 ALA 325

ALA 352 0.12 ASP 502 -0.34 ALA 325

ALA 352 0.12 PRO 503 -0.35 ALA 325

ALA 352 0.10 ILE 504 -0.32 ALA 325

ALA 352 0.09 LYS 505 -0.32 ALA 325

ALA 352 0.09 VAL 506 -0.35 ALA 325

ALA 352 0.09 GLY 507 -0.36 ALA 325

ALA 352 0.11 SER 508 -0.41 ALA 325

ALA 352 0.08 PHE 509 -0.43 ALA 325

ALA 352 0.08 LYS 510 -0.49 ALA 325

ALA 352 0.05 VAL 511 -0.51 ALA 325

GLN 338 0.06 THR 512 -0.51 ALA 325

GLN 338 0.05 ILE 513 -0.45 ALA 325

GLN 338 0.11 ARG 514 -0.44 ALA 325

GLN 338 0.11 LEU 515 -0.37 ALA 325

LEU 334 0.17 LYS 516 -0.33 PRO 326

LEU 334 0.23 SER 517 -0.36 PRO 326

LEU 334 0.28 GLU 518 -0.29 PRO 326

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.

*** shlomo ***

CA distance fluctuations for 2605130610242337669

--- normal mode 11 ---

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

* shlomo *