CNRS Nantes University US2B US2B
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CA distance fluctuations for 2605130610242337669

---  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 increasereflargest decrease
LYS 327 0.26 GLN 6 -0.01 ASP 355
LYS 327 0.29 GLY 7 -0.01 ASP 355
LYS 327 0.34 ILE 8 -0.01 ASP 355
LYS 327 0.35 GLY 9 -0.01 ASP 355
LYS 327 0.41 VAL 10 -0.01 ASP 355
ARG 331 0.41 ILE 11 -0.01 ASP 355
ARG 331 0.47 SER 12 -0.01 ASP 355
ARG 331 0.52 THR 13 -0.01 ASP 355
ARG 331 0.58 ALA 14 -0.01 ASP 355
ARG 331 0.55 TYR 15 -0.01 ASP 355
ARG 331 0.54 PHE 16 -0.01 ASP 355
ARG 331 0.46 THR 17 -0.01 ASP 355
LEU 330 0.41 MET 18 -0.01 ASP 355
LEU 330 0.37 LYS 19 -0.01 LEU 356
LEU 330 0.26 ASP 20 -0.01 LEU 356
LEU 330 0.25 LYS 21 -0.01 LEU 356
LEU 330 0.20 HIS 22 -0.01 LEU 356
LYS 327 0.22 SER 23 -0.01 LEU 356
LEU 330 0.27 ILE 24 -0.01 LEU 356
ARG 331 0.23 LYS 25 -0.01 LEU 356
ARG 331 0.25 THR 26 -0.01 LEU 356
ARG 331 0.20 VAL 27 -0.01 LEU 356
ARG 331 0.21 LYS 28 -0.01 LEU 356
ARG 331 0.26 LYS 29 -0.01 ASP 355
ARG 331 0.25 TYR 30 -0.01 ASP 355
ARG 331 0.28 TRP 31 -0.01 ASP 355
ARG 331 0.28 TRP 32 -0.01 ASP 355
ARG 331 0.29 LYS 33 -0.01 ASP 355
ARG 331 0.35 ASN 34 -0.01 ASP 355
ARG 331 0.36 CYS 35 -0.01 ASP 355
ARG 331 0.37 VAL 36 -0.01 ASP 355
ARG 331 0.33 ILE 37 -0.01 ASP 355
ARG 331 0.31 GLN 38 -0.01 ASP 355
ARG 331 0.28 HIS 39 -0.01 ASP 355
ARG 331 0.29 VAL 40 -0.01 ASP 355
LYS 327 0.25 LYS 41 -0.01 LEU 356
LYS 327 0.30 TYR 42 -0.01 ASP 355
LYS 327 0.27 HIS 43 -0.01 LEU 356
LYS 327 0.24 GLY 44 -0.01 LEU 356
LYS 327 0.27 LYS 45 -0.01 ASP 355
LYS 327 0.27 THR 46 -0.01 ASP 355
LYS 327 0.32 PHE 47 -0.01 ASP 355
ARG 331 0.32 ILE 48 -0.01 ASP 355
ARG 331 0.38 ILE 49 -0.01 ASP 355
ARG 331 0.39 ALA 50 -0.01 ASP 355
ARG 331 0.45 THR 51 -0.01 ASP 355
ARG 331 0.44 VAL 52 -0.01 ASP 355
ARG 331 0.45 GLY 53 -0.01 ASP 355
ARG 331 0.47 TYR 54 -0.01 ASP 355
ARG 331 0.43 GLY 55 -0.00 LYS 353
ARG 331 0.39 LYS 56 -0.00 LYS 353
ARG 331 0.36 ALA 57 -0.00 LYS 353
ARG 331 0.38 ASN 58 -0.01 ASP 355
ARG 331 0.39 ALA 59 -0.00 ASP 355
ARG 331 0.35 ALA 60 -0.00 ASP 355
ARG 331 0.33 MET 61 -0.00 ASP 355
ARG 331 0.34 THR 62 -0.01 ASP 355
ARG 331 0.34 ILE 63 -0.00 ASP 355
ARG 331 0.30 THR 64 -0.00 ASP 355
ARG 331 0.28 TYR 65 -0.01 ASP 355
ARG 331 0.30 LEU 66 -0.01 ASP 355
ARG 331 0.28 LEU 67 -0.00 ASP 355
ARG 331 0.25 GLU 68 -0.00 ASP 355
ARG 331 0.24 LYS 69 -0.01 ASP 355
ARG 331 0.25 TYR 70 -0.01 ASP 355
ARG 331 0.24 PRO 71 -0.00 ASP 355
LYS 327 0.25 GLY 72 -0.00 ASP 355
LYS 327 0.29 LEU 73 -0.00 ASP 355
LYS 327 0.31 GLN 74 -0.00 ASP 355
LYS 327 0.35 THR 75 -0.00 ASP 355
LYS 327 0.38 ILE 76 -0.00 ASP 355
LYS 327 0.44 LEU 77 -0.00 ASP 355
LYS 327 0.48 ASN 78 -0.00 ASP 355
LYS 327 0.54 VAL 79 -0.01 ASP 355
LYS 327 0.60 ASP 80 -0.01 ASP 355
LYS 327 0.69 LEU 81 -0.01 ASP 355
LYS 327 0.66 ALA 82 -0.00 LYS 353
ASN 324 0.68 LEU 83 -0.00 LYS 353
ASN 324 0.67 SER 84 -0.00 SER 383
ASN 324 0.63 THR 85 -0.00 SER 383
ASN 324 0.63 ASN 86 -0.00 SER 383
ASN 324 0.68 ASP 87 -0.00 SER 383
ASN 324 0.68 LYS 88 -0.00 SER 383
ASN 324 0.72 HIS 89 -0.00 ASP 381
ASN 324 0.81 ASP 90 -0.00 ASP 381
ASN 324 0.89 THR 91 -0.00 LYS 353
ASN 324 0.83 GLY 92 -0.00 ASP 355
ASN 324 0.74 ASP 93 -0.00 LYS 353
ASN 324 0.66 THR 94 -0.00 ASP 355
ASN 324 0.60 THR 95 -0.00 LYS 353
ASN 324 0.53 ILE 96 -0.00 ASP 355
ASN 324 0.50 SER 97 -0.00 ASN 388
ASN 324 0.45 THR 98 -0.00 ASN 388
ASN 324 0.44 LYS 99 -0.00 ASN 388
ASN 324 0.44 PHE 100 -0.00 ASN 388
ASN 324 0.43 ILE 101 -0.00 GLY 389
ASN 324 0.41 TYR 102 -0.00 GLY 389
ASN 324 0.44 ARG 103 -0.00 GLY 389
ASN 324 0.39 ASP 104 -0.00 LYS 353
ASN 324 0.36 ALA 105 -0.00 GLY 389
ASN 324 0.35 ASP 106 -0.00 GLY 389
ASN 324 0.32 LEU 107 -0.00 GLY 389
ASN 324 0.33 THR 108 -0.00 GLY 389
ASN 324 0.30 VAL 109 -0.00 GLY 389
ASN 324 0.29 PHE 110 -0.00 GLY 389
ASN 324 0.29 LYS 111 -0.00 GLY 389
ASN 324 0.31 ASP 112 -0.00 GLY 389
ASN 324 0.33 ILE 113 -0.00 GLY 389
ASN 324 0.36 LYS 114 -0.00 GLY 389
ASN 324 0.38 TYR 115 -0.00 GLY 389
ASN 324 0.38 GLY 116 -0.00 GLY 389
ASN 324 0.35 GLN 117 -0.00 GLY 389
LYS 327 0.32 ILE 118 -0.00 GLY 389
LYS 327 0.30 VAL 119 -0.00 GLY 389
LYS 327 0.29 ASN 120 -0.00 GLY 389
LYS 327 0.31 GLU 121 -0.00 GLY 389
ASN 324 0.34 PRO 122 -0.00 GLY 389
ASN 324 0.37 GLU 123 -0.00 GLY 389
ASN 324 0.39 SER 124 -0.00 GLY 389
ASN 324 0.38 PHE 125 -0.00 ASN 388
ASN 324 0.40 GLN 126 -0.00 ASN 388
ASN 324 0.39 PHE 127 -0.00 ASN 388
ASN 324 0.40 ASP 128 -0.00 ASN 388
ASN 324 0.37 GLY 129 -0.00 ASN 388
ASN 324 0.37 GLU 130 -0.00 ASN 388
ASN 324 0.38 PHE 131 -0.00 ASN 388
ASN 324 0.42 ALA 132 -0.00 ASN 388
ASN 324 0.42 LYS 133 -0.00 ASN 388
ASN 324 0.40 VAL 134 -0.00 ASN 388
ASN 324 0.44 VAL 135 -0.00 ASP 355
ASN 324 0.47 LYS 136 -0.00 PHE 279
ASN 324 0.44 ASP 137 -0.00 PHE 279
ASN 324 0.45 PHE 138 -0.00 ASP 355
ASN 324 0.50 LYS 139 -0.00 ASP 355
ASN 324 0.54 LEU 140 -0.00 ASP 355
ASN 324 0.59 GLY 141 -0.00 SER 243
ASN 324 0.58 LEU 142 -0.00 SER 243
ASN 324 0.59 THR 143 -0.00 SER 383
ASN 324 0.55 GLU 144 -0.00 SER 383
ASN 324 0.55 GLY 145 -0.00 SER 383
ASN 324 0.51 VAL 146 -0.00 GLY 389
ASN 324 0.51 THR 147 -0.00 ASN 388
ASN 324 0.49 GLY 148 -0.00 GLY 389
LYS 327 0.46 THR 149 -0.00 LYS 353
LYS 327 0.44 ALA 150 -0.00 LYS 353
ARG 331 0.44 ASP 151 -0.00 LYS 353
LYS 327 0.46 MET 152 -0.00 LYS 353
LYS 327 0.53 LEU 153 -0.00 LYS 353
ASN 324 0.56 ILE 154 -0.00 LYS 353
ASN 324 0.59 TYR 155 -0.00 LYS 353
ASN 324 0.55 ASN 156 -0.00 SER 383
ASN 324 0.55 SER 157 -0.00 SER 383
ASN 324 0.49 LYS 158 -0.00 SER 383
ASN 324 0.49 GLN 159 -0.00 GLY 389
ASN 324 0.53 PHE 160 -0.00 SER 383
ASN 324 0.49 LYS 161 -0.00 SER 383
ASN 324 0.46 GLU 162 -0.00 SER 383
ASN 324 0.48 MET 163 -0.00 GLY 389
ASN 324 0.49 VAL 164 -0.00 SER 383
ASN 324 0.44 ASP 165 -0.00 SER 383
ASN 324 0.43 LYS 166 -0.00 GLY 389
ASN 324 0.45 TYR 167 -0.00 GLY 389
ASN 324 0.47 GLY 168 -0.00 SER 383
ASN 324 0.51 HIS 169 -0.00 SER 383
ASN 324 0.50 THR 170 -0.00 GLY 389
ASN 324 0.52 ILE 171 -0.00 GLY 389
ASN 324 0.57 ASP 172 -0.00 SER 383
ASN 324 0.59 VAL 173 -0.00 LYS 353
ASN 324 0.57 ILE 174 -0.00 LYS 353
LYS 327 0.54 ASP 175 -0.00 LYS 353
LYS 327 0.48 THR 176 -0.00 LYS 353
LYS 327 0.45 GLU 177 -0.00 ASP 355
LYS 327 0.46 ALA 178 -0.00 ASP 355
LYS 327 0.42 GLY 179 -0.00 LYS 353
LYS 327 0.38 ALA 180 -0.00 ASP 355
LYS 327 0.38 ILE 181 -0.00 ASP 355
LYS 327 0.39 ALA 182 -0.00 ASP 355
LYS 327 0.35 GLN 183 -0.00 ASP 355
LYS 327 0.33 VAL 184 -0.00 ASP 355
LYS 327 0.34 ALA 185 -0.00 ASP 355
LYS 327 0.33 LYS 186 -0.00 ASP 355
LYS 327 0.30 LYS 187 -0.00 ASP 355
LYS 327 0.29 SER 188 -0.00 ASP 355
LYS 327 0.31 SER 189 -0.00 ASP 355
LYS 327 0.32 ILE 190 -0.00 ASP 355
LYS 327 0.36 ASN 191 -0.00 ASP 355
LYS 327 0.40 TYR 192 -0.00 ASP 355
LYS 327 0.44 ILE 193 -0.00 ASP 355
LYS 327 0.49 ALA 194 -0.00 ASP 355
LYS 327 0.55 LEU 195 -0.00 ASP 355
LYS 327 0.61 LYS 196 -0.00 ASP 355
LYS 327 0.69 ILE 197 -0.00 ASP 355
ASN 324 0.74 ILE 198 -0.00 LYS 353
ASN 324 0.83 TYR 199 -0.00 LYS 353
ASN 324 0.83 ASN 200 -0.00 LYS 353
ASN 324 0.75 ASN 201 -0.00 SER 383
ASN 324 0.68 ALA 202 -0.00 LYS 353
ASN 324 0.68 LEU 203 -0.00 SER 383
ASN 324 0.78 SER 204 -0.00 SER 383
ASN 324 0.79 PRO 205 -0.00 LYS 353
ASN 324 0.81 TRP 206 -0.00 LYS 353
ASN 324 0.74 ASP 207 -0.00 LYS 353
ASN 324 0.83 ASN 208 -0.00 LYS 353
ASN 324 1.01 ASP 209 -0.00 LYS 353
ASN 324 1.19 PRO 210 -0.01 LYS 353
ASN 324 1.36 ILE 211 -0.01 LYS 353
ASN 324 1.18 HIS 212 -0.01 LYS 353
LYS 327 1.37 LYS 213 -0.01 ASP 355
ASN 324 1.34 PHE 214 -0.01 ASP 355
ASN 324 1.12 LYS 215 -0.01 ASP 355
LYS 327 1.09 MET 216 -0.01 ASP 355
LYS 327 1.17 TYR 217 -0.01 ASP 355
LYS 327 0.99 GLU 218 -0.01 ASP 355
LYS 327 0.90 THR 219 -0.01 ASP 355
LYS 327 0.88 VAL 220 -0.01 ASP 355
LYS 327 0.84 ASN 221 -0.01 ASP 355
LYS 327 0.76 THR 222 -0.01 ASP 355
LYS 327 0.71 LEU 223 -0.01 ASP 355
LYS 327 0.66 LYS 224 -0.01 ASP 355
LYS 327 0.63 TYR 225 -0.01 ASP 355
LYS 327 0.59 LEU 226 -0.01 ASP 355
LYS 327 0.54 LEU 227 -0.01 ASP 355
LYS 327 0.50 ARG 228 -0.01 ASP 355
LYS 327 0.49 ARG 229 -0.01 ASP 355
LYS 327 0.47 LEU 230 -0.01 ASP 355
LYS 327 0.42 PHE 231 -0.01 ASP 355
LYS 327 0.40 ASN 232 -0.01 ASP 355
LYS 327 0.40 LEU 233 -0.01 ASP 355
LYS 327 0.38 LEU 234 -0.01 ASP 355
LYS 327 0.34 SER 235 -0.01 ASP 355
LYS 327 0.33 SER 236 -0.00 ASP 355
LYS 327 0.30 ASN 237 -0.00 ASP 355
ASN 324 0.32 TYR 238 -0.00 ASP 355
ASN 324 0.34 ILE 239 -0.00 ASP 355
ASN 324 0.38 ILE 240 -0.00 ASP 355
ASN 324 0.40 ASP 241 -0.00 ASP 137
ASN 324 0.43 LEU 242 -0.00 PRO 446
ASN 324 0.45 SER 243 -0.00 ASP 381
ASN 324 0.45 GLN 244 -0.00 ASP 381
ASN 324 0.46 CYS 245 -0.00 LYS 378
ASN 324 0.49 SER 246 -0.00 LYS 378
ASN 324 0.53 GLN 247 -0.00 ALA 374
ASN 324 0.50 ASP 248 -0.00 ALA 352
ASN 324 0.46 ASP 249 -0.00 ILE 299
ASN 324 0.48 LEU 250 -0.00 ASP 355
ASN 324 0.50 ASP 251 -0.00 ASP 355
PRO 326 0.44 SER 252 -0.00 ASP 355
ASN 324 0.42 ILE 253 -0.00 ASP 355
PRO 326 0.45 ASN 254 -0.01 ASP 355
PRO 326 0.44 GLU 255 -0.01 ASP 355
PRO 326 0.38 LEU 256 -0.01 ASP 355
PRO 326 0.38 PHE 257 -0.01 ASP 355
PRO 326 0.39 GLU 258 -0.01 ASP 355
PRO 326 0.35 ILE 259 -0.01 LEU 356
PRO 326 0.31 LYS 260 -0.01 LEU 356
PRO 326 0.32 HIS 261 -0.01 ASP 355
ASN 324 0.29 ASP 262 -0.00 ASP 355
PRO 326 0.27 GLN 263 -0.00 LEU 356
PRO 326 0.30 TRP 264 -0.00 LEU 356
ASN 324 0.30 ILE 265 -0.00 ASP 355
ASN 324 0.27 LYS 266 -0.00 LEU 356
ASN 324 0.26 LEU 267 -0.00 LEU 356
ASN 324 0.28 PHE 268 -0.00 PRO 469
ASN 324 0.27 LYS 269 -0.00 ASP 355
ASN 324 0.25 PRO 270 -0.00 LEU 356
ASN 324 0.25 ASN 271 -0.00 ASP 355
ASN 324 0.28 THR 272 -0.00 ASP 355
ASN 324 0.29 HIS 273 -0.00 ASP 355
ASN 324 0.32 LYS 274 -0.00 GLU 130
ASN 324 0.35 VAL 275 -0.00 GLU 130
ASN 324 0.37 LEU 276 -0.00 ASP 137
ASN 324 0.40 SER 277 -0.00 PRO 446
ASN 324 0.40 GLY 278 -0.00 PRO 446
ASN 324 0.37 PHE 279 -0.00 PRO 446
ASN 324 0.36 GLY 280 -0.00 PRO 446
ASN 324 0.36 PRO 281 -0.00 PRO 446
ASN 324 0.39 SER 282 -0.00 PRO 446
ASN 324 0.37 LEU 283 -0.00 GLN 448
ASN 324 0.34 MET 284 -0.00 GLN 448
ASN 324 0.32 LEU 285 -0.00 GLY 473
ASN 324 0.30 VAL 286 -0.00 GLU 130
ASN 324 0.28 ASP 287 -0.00 GLU 130
ASN 324 0.27 LYS 288 -0.00 GLU 130
ASN 324 0.26 GLN 289 -0.00 GLU 130
ASN 324 0.28 GLU 290 -0.00 GLU 130
ASN 324 0.26 LYS 291 -0.00 GLY 473
ASN 324 0.27 THR 292 -0.00 GLY 473
ASN 324 0.29 PRO 293 -0.00 GLY 473
ASN 324 0.30 VAL 294 -0.00 GLN 448
ASN 324 0.32 ALA 295 -0.01 GLN 448
ASN 324 0.33 LEU 296 -0.00 GLN 449
ASN 324 0.36 ASP 297 -0.00 ILE 450
ASN 324 0.38 ILE 298 -0.00 ILE 450
ASN 324 0.39 ILE 299 -0.00 SER 246
ASN 324 0.42 GLN 300 -0.00 GLU 370
ASN 324 0.40 VAL 301 -0.00 GLU 370
ASN 324 0.42 ILE 302 -0.00 GLU 255
ASN 324 0.47 ARG 303 -0.00 GLU 255
ASN 324 0.50 SER 304 -0.00 ALA 352
ASN 324 0.57 LYS 305 -0.00 ALA 352
ILE 211 1.36 ASN 324 -0.00 SER 414
PHE 214 1.09 ALA 325 -0.02 SER 414
PHE 214 1.15 PRO 326 -0.00 LYS 327
LYS 213 1.37 LYS 327 -0.03 SER 414
LYS 213 1.10 LYS 328 -0.07 SER 414
LYS 213 0.86 TRP 329 -0.06 SER 414
TYR 217 0.97 LEU 330 -0.05 SER 414
LYS 213 0.94 ARG 331 -0.10 SER 414
LYS 213 0.72 LYS 332 -0.13 SER 414
TYR 217 0.64 LEU 333 -0.10 SER 414
TYR 217 0.52 LEU 334 -0.16 SER 414
LYS 213 0.47 PHE 335 -0.19 SER 414
TYR 217 0.43 LEU 336 -0.12 SER 414
TYR 217 0.36 GLU 337 -0.09 SER 414
TYR 217 0.23 GLN 338 -0.17 GLU 416
TYR 217 0.19 VAL 339 -0.16 GLU 416
TYR 217 0.10 ARG 340 -0.08 PHE 417
LEU 336 0.07 VAL 341 -0.06 VAL 511
PRO 326 0.16 ASN 342 -0.06 VAL 341
TRP 329 0.22 ASP 343 -0.01 GLU 416
ALA 325 0.31 ASP 344 -0.01 VAL 341
ALA 325 0.20 GLU 345 -0.03 VAL 341
ALA 325 0.12 LEU 346 -0.02 VAL 341
ALA 325 0.10 LEU 347 -0.02 VAL 339
ALA 325 0.14 TRP 348 -0.01 ASP 344
ALA 325 0.27 ASN 349 -0.01 TYR 461
ALA 325 0.23 LYS 350 -0.01 VAL 341
ALA 325 0.25 SER 351 -0.01 TYR 461
ALA 325 0.28 ALA 352 -0.01 TYR 461
ALA 325 0.33 LYS 353 -0.01 TYR 217
ALA 325 0.39 TYR 354 -0.01 TYR 461
ALA 325 0.43 ASP 355 -0.01 TYR 461
ALA 325 0.49 LEU 356 -0.01 TYR 461
ALA 325 0.41 ASN 357 -0.01 TYR 461
ALA 325 0.44 ASN 358 -0.01 LYS 350
PRO 326 0.45 GLU 359 -0.01 ARG 462
ASN 324 0.42 LYS 360 -0.00 LYS 350
PRO 326 0.37 LEU 361 -0.00 VAL 341
ASN 324 0.33 TYR 362 -0.01 VAL 341
PRO 326 0.28 LYS 363 -0.02 VAL 339
PRO 326 0.27 ILE 364 -0.02 VAL 339
ASN 324 0.26 GLU 365 -0.02 VAL 339
ASN 324 0.30 THR 366 -0.01 VAL 341
ASN 324 0.32 VAL 367 -0.01 VAL 341
ASN 324 0.29 ALA 368 -0.01 VAL 341
ASN 324 0.29 ASN 369 -0.01 VAL 341
ASN 324 0.33 GLU 370 -0.00 VAL 341
ASN 324 0.33 ILE 371 -0.00 VAL 301
ASN 324 0.30 ALA 372 -0.00 VAL 341
ASN 324 0.32 ALA 373 -0.00 SER 246
ASN 324 0.34 ALA 374 -0.00 SER 246
ASN 324 0.32 ILE 375 -0.00 SER 246
ASN 324 0.30 ALA 376 -0.00 SER 246
ASN 324 0.33 GLU 377 -0.00 SER 246
ASN 324 0.33 LYS 378 -0.00 SER 246
ASN 324 0.30 CYS 379 -0.00 GLN 244
ASN 324 0.31 GLN 380 -0.00 GLN 244
ASN 324 0.31 ASP 381 -0.00 GLN 244
ASN 324 0.30 LYS 382 -0.00 GLY 280
ASN 324 0.30 SER 383 -0.00 GLY 280
ASN 324 0.30 SER 384 -0.01 PRO 446
ASN 324 0.32 TYR 385 -0.01 PRO 446
ASN 324 0.31 THR 386 -0.00 ALA 474
ASN 324 0.31 TYR 387 -0.00 GLY 473
ASN 324 0.31 ASN 388 -0.00 GLY 129
ASN 324 0.30 GLY 389 -0.00 GLY 129
ASN 324 0.29 ALA 390 -0.00 GLY 473
ASN 324 0.29 THR 391 -0.00 GLY 473
ASN 324 0.29 VAL 392 -0.01 GLY 473
ASN 324 0.27 PRO 393 -0.01 GLY 473
PRO 326 0.42 ASP 402 -0.00 ASP 355
PRO 326 0.38 ALA 403 -0.00 LYS 350
PRO 326 0.40 ARG 404 -0.00 GLU 359
PRO 326 0.34 ILE 405 -0.01 VAL 341
PRO 326 0.29 SER 406 -0.02 VAL 339
PRO 326 0.23 PHE 407 -0.05 VAL 339
PRO 326 0.17 TYR 408 -0.09 VAL 339
PRO 326 0.14 ILE 409 -0.10 VAL 339
PRO 326 0.09 THR 410 -0.12 PHE 335
PRO 326 0.07 HIS 411 -0.14 PHE 335
PRO 326 0.07 ASN 412 -0.13 PHE 335
PRO 326 0.03 GLN 413 -0.16 PHE 335
LYS 213 0.01 SER 414 -0.19 PHE 335
PRO 326 0.03 HIS 415 -0.18 PHE 335
PRO 326 0.02 GLU 416 -0.19 PHE 335
PRO 326 0.06 PHE 417 -0.16 PHE 335
PRO 326 0.09 VAL 418 -0.13 GLN 338
PRO 326 0.11 GLU 419 -0.13 GLN 338
PRO 326 0.12 ASP 420 -0.10 GLN 338
PRO 326 0.18 LYS 421 -0.05 GLN 338
PRO 326 0.17 ASN 422 -0.05 GLN 338
PRO 326 0.14 PHE 423 -0.07 GLN 338
PRO 326 0.17 GLY 424 -0.07 GLN 338
PRO 326 0.22 THR 425 -0.03 VAL 339
PRO 326 0.19 GLN 426 -0.04 GLN 338
PRO 326 0.18 LEU 427 -0.06 GLN 338
PRO 326 0.22 VAL 428 -0.04 VAL 339
PRO 326 0.23 SER 429 -0.03 VAL 339
PRO 326 0.20 ASN 430 -0.04 VAL 339
PRO 326 0.21 GLU 431 -0.04 VAL 339
PRO 326 0.24 PHE 432 -0.02 VAL 339
PRO 326 0.22 VAL 433 -0.03 VAL 339
ASN 324 0.20 LYS 434 -0.03 VAL 339
ASN 324 0.23 TYR 435 -0.03 VAL 339
ASN 324 0.25 LEU 436 -0.02 VAL 339
ASN 324 0.22 ASN 437 -0.02 VAL 339
ASN 324 0.22 GLU 438 -0.02 VAL 339
ASN 324 0.25 ALA 439 -0.01 VAL 339
ASN 324 0.25 LEU 440 -0.01 VAL 339
ASN 324 0.23 LYS 441 -0.02 VAL 339
ASN 324 0.24 ASP 442 -0.01 VAL 339
ASN 324 0.26 VAL 443 -0.00 VAL 341
ASN 324 0.26 ASP 444 -0.00 SER 384
ASN 324 0.27 SER 445 -0.00 SER 384
ASN 324 0.28 PRO 446 -0.01 SER 384
ASN 324 0.28 TYR 447 -0.00 PRO 281
ASN 324 0.26 GLN 448 -0.01 ALA 295
ASN 324 0.26 GLN 449 -0.00 ALA 295
ASN 324 0.28 ILE 450 -0.00 LEU 296
ASN 324 0.29 VAL 451 -0.00 LEU 296
PRO 326 0.31 ILE 452 -0.00 LYS 350
PRO 326 0.34 TYR 453 -0.00 LEU 356
PRO 326 0.35 MET 454 -0.00 LEU 356
PRO 326 0.37 THR 455 -0.00 LEU 356
PRO 326 0.34 ILE 456 -0.00 LEU 356
PRO 326 0.36 PRO 457 -0.01 LEU 356
PRO 326 0.31 ALA 458 -0.01 LEU 356
PRO 326 0.28 LEU 459 -0.01 LEU 356
PRO 326 0.35 ASP 460 -0.01 LEU 356
PRO 326 0.47 TYR 461 -0.01 LEU 356
PRO 326 0.43 ARG 462 -0.01 LEU 356
PRO 326 0.39 LYS 463 -0.01 LEU 356
PRO 326 0.32 ILE 464 -0.01 LEU 356
PRO 326 0.33 SER 465 -0.01 LEU 356
PRO 326 0.29 VAL 466 -0.00 LEU 356
PRO 326 0.28 PHE 467 -0.00 LEU 356
PRO 326 0.26 ILE 468 -0.01 VAL 341
PRO 326 0.25 PRO 469 -0.00 VAL 341
ASN 324 0.24 SER 470 -0.01 VAL 341
ASN 324 0.22 ASN 471 -0.01 VAL 339
ASN 324 0.23 LYS 472 -0.00 VAL 294
ASN 324 0.23 GLY 473 -0.01 PRO 393
ASN 324 0.24 ALA 474 -0.01 SER 384
ASN 324 0.23 ASN 475 -0.01 VAL 339
ASN 324 0.23 ARG 476 -0.01 VAL 339
ASN 324 0.23 GLY 477 -0.01 VAL 339
ASN 324 0.25 VAL 478 -0.01 VAL 339
ASN 324 0.22 LYS 479 -0.02 VAL 339
ASN 324 0.23 PHE 480 -0.01 VAL 339
ASN 324 0.20 VAL 481 -0.02 VAL 339
PRO 326 0.18 ALA 482 -0.03 VAL 339
PRO 326 0.17 LEU 483 -0.04 GLN 338
PRO 326 0.14 ASN 484 -0.06 GLN 338
PRO 326 0.13 GLN 485 -0.06 PHE 335
PRO 326 0.11 LYS 486 -0.09 PHE 335
PRO 326 0.12 LEU 487 -0.08 PHE 335
PRO 326 0.13 GLN 488 -0.07 GLN 338
PRO 326 0.11 ARG 489 -0.09 PHE 335
PRO 326 0.09 ASP 490 -0.11 PHE 335
PRO 326 0.11 TYR 491 -0.10 PHE 335
PRO 326 0.13 THR 492 -0.08 VAL 339
PRO 326 0.17 VAL 493 -0.07 VAL 339
PRO 326 0.17 VAL 494 -0.07 VAL 339
PRO 326 0.21 ASP 495 -0.05 VAL 339
PRO 326 0.21 ILE 496 -0.05 VAL 339
PRO 326 0.25 THR 497 -0.03 VAL 339
ASN 324 0.22 ARG 498 -0.04 VAL 339
ASN 324 0.19 ASN 499 -0.05 VAL 339
ASN 324 0.17 ASP 500 -0.06 VAL 339
ASN 324 0.14 TYR 501 -0.07 VAL 339
PRO 326 0.10 ASP 502 -0.08 VAL 339
PRO 326 0.08 PRO 503 -0.10 PHE 335
PRO 326 0.05 ILE 504 -0.12 PHE 335
PRO 326 0.07 LYS 505 -0.12 PHE 335
PRO 326 0.09 VAL 506 -0.11 PHE 335
PRO 326 0.07 GLY 507 -0.12 PHE 335
PRO 326 0.08 SER 508 -0.11 VAL 339
PRO 326 0.06 PHE 509 -0.13 VAL 339
PRO 326 0.12 LYS 510 -0.09 VAL 339
PRO 326 0.11 VAL 511 -0.11 VAL 339
PRO 326 0.17 THR 512 -0.08 VAL 339
PRO 326 0.15 ILE 513 -0.11 VAL 339
PRO 326 0.21 ARG 514 -0.06 VAL 339
PRO 326 0.20 LEU 515 -0.06 VAL 339
PRO 326 0.18 LYS 516 -0.05 GLN 338
PRO 326 0.25 SER 517 -0.01 LEU 356
PRO 326 0.21 GLU 518 -0.01 LEU 356

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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.