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***  close cutoff 10 melek  ***

CA distance fluctuations for 260522120726406031

---  normal mode 15  ---

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
ILE 21 0.27 ALA 1 -0.30 LYS 423
ILE 21 0.24 SER 2 -0.26 SER 424
ILE 21 0.20 SER 3 -0.23 SER 424
GLY 29 0.20 THR 4 -0.21 SER 424
GLY 29 0.21 ASN 5 -0.23 VAL 33
GLY 29 0.25 LEU 6 -0.24 VAL 33
ASN 30 0.24 LYS 7 -0.26 VAL 33
GLY 29 0.20 ASP 8 -0.27 VAL 33
GLY 29 0.21 VAL 9 -0.29 VAL 33
GLY 29 0.26 LEU 10 -0.32 VAL 33
ASN 30 0.24 ALA 11 -0.31 VAL 33
GLY 29 0.17 SER 12 -0.35 VAL 33
ALA 1 0.20 LEU 13 -0.43 VAL 33
GLY 29 0.27 ILE 14 -0.43 PRO 422
ASN 30 0.26 PRO 15 -0.48 PRO 422
ALA 1 0.26 LYS 16 -0.59 PRO 422
THR 98 0.29 GLU 17 -0.67 PRO 422
ASN 30 0.37 GLN 18 -0.68 PRO 422
ASN 30 0.30 ALA 19 -0.70 PRO 422
GLY 99 0.28 ARG 20 -0.79 PRO 422
GLU 54 0.38 ILE 21 -1.00 PRO 422
ASN 30 0.45 LYS 22 -0.92 PRO 422
ASN 30 0.38 THR 23 -0.66 PRO 422
ILE 52 0.39 PHE 24 -0.68 PRO 422
ILE 52 0.53 ARG 25 -0.70 PRO 422
ASN 30 0.47 GLN 26 -0.52 PRO 422
GLY 50 0.50 GLN 27 -0.35 PRO 422
GLY 50 0.64 HIS 28 -0.42 LYS 423
GLY 50 0.77 GLY 29 -0.34 LYS 423
GLY 50 0.85 ASN 30 -0.07 LYS 423
ASN 30 0.76 THR 31 -0.34 LYS 423
VAL 33 0.97 ALA 32 -0.34 LYS 423
ALA 32 0.97 VAL 33 -1.13 LYS 423
ALA 32 0.70 GLY 34 -1.54 LYS 423
ALA 32 0.54 GLN 35 -1.45 LYS 423
ALA 32 0.59 ILE 36 -0.81 SER 424
LYS 432 0.39 THR 37 -0.39 LYS 423
ASP 39 0.54 VAL 38 -0.11 ILE 21
VAL 38 0.54 ASP 39 -0.11 ASP 291
PRO 422 0.46 MET 40 -0.17 ASP 291
PRO 422 0.78 SER 41 -0.25 ASP 291
PRO 422 0.82 TYR 42 -0.28 ASP 291
PRO 422 0.67 GLY 43 -0.24 ASP 291
PRO 422 0.81 GLY 44 -0.31 ASP 291
PRO 422 0.64 MET 45 -0.26 LEU 288
LYS 366 0.40 ARG 46 -0.21 LEU 288
LYS 366 0.36 GLY 47 -0.41 SER 424
ALA 32 0.53 MET 48 -0.68 SER 424
ASN 30 0.65 LYS 49 -0.85 SER 424
ASN 30 0.85 GLY 50 -1.08 SER 424
ASN 30 0.76 LEU 51 -0.85 SER 424
GLY 29 0.75 ILE 52 -0.76 SER 424
GLY 29 0.60 TYR 53 -0.57 SER 424
GLY 29 0.53 GLU 54 -0.52 SER 424
GLY 29 0.45 THR 55 -0.42 SER 424
GLY 29 0.44 SER 56 -0.42 SER 424
GLY 29 0.44 VAL 57 -0.48 SER 424
GLY 29 0.39 LEU 58 -0.41 SER 424
GLY 29 0.33 ASP 59 -0.41 LYS 423
GLY 29 0.31 PRO 60 -0.34 LYS 423
GLY 29 0.26 ASP 61 -0.34 LYS 423
GLY 29 0.27 GLU 62 -0.33 LYS 423
GLY 29 0.31 GLY 63 -0.30 SER 424
GLY 29 0.36 ILE 64 -0.33 SER 424
GLY 29 0.35 ARG 65 -0.36 SER 424
GLY 29 0.36 PHE 66 -0.35 SER 424
GLY 29 0.35 ARG 67 -0.39 SER 424
GLY 29 0.32 GLY 68 -0.42 LYS 423
GLY 29 0.30 PHE 69 -0.34 LYS 423
GLY 29 0.29 SER 70 -0.30 SER 424
GLY 29 0.28 ILE 71 -0.25 SER 424
GLY 29 0.25 PRO 72 -0.35 LYS 355
GLY 29 0.24 GLU 73 -0.30 ASN 359
GLY 29 0.27 CYS 74 -0.27 LYS 355
GLY 29 0.25 GLN 75 -0.32 LYS 355
GLY 29 0.23 LYS 76 -0.34 LYS 355
GLY 29 0.24 LEU 77 -0.29 LYS 355
GLY 29 0.25 LEU 78 -0.26 LYS 355
GLY 29 0.23 PRO 79 -0.25 LYS 355
GLY 29 0.22 LYS 80 -0.26 LYS 355
SER 311 0.25 ALA 81 -0.23 LYS 355
SER 311 0.23 GLY 82 -0.24 LYS 355
SER 311 0.24 GLY 84 -0.29 LYS 355
GLY 29 0.21 GLU 85 -0.34 LYS 355
SER 311 0.24 GLU 86 -0.29 LYS 355
GLY 29 0.25 PRO 87 -0.25 LYS 355
SER 311 0.27 LEU 88 -0.19 LYS 355
SER 311 0.30 PRO 89 -0.20 SER 426
GLY 29 0.28 GLU 90 -0.19 SER 426
GLY 29 0.27 GLY 91 -0.22 SER 424
GLY 29 0.31 LEU 92 -0.24 SER 424
GLY 29 0.33 PHE 93 -0.24 SER 424
GLY 29 0.31 TRP 94 -0.25 SER 424
GLY 29 0.32 LEU 95 -0.29 SER 424
GLY 29 0.37 LEU 96 -0.32 SER 424
GLY 29 0.37 VAL 97 -0.31 SER 424
ILE 21 0.33 THR 98 -0.33 SER 424
ILE 21 0.36 GLY 99 -0.36 SER 424
ILE 21 0.32 GLN 100 -0.32 SER 424
ILE 21 0.27 ILE 101 -0.29 SER 424
ILE 21 0.24 PRO 102 -0.25 SER 424
ILE 21 0.22 THR 103 -0.23 SER 424
GLY 29 0.21 PRO 104 -0.21 LYS 355
GLY 29 0.20 GLU 105 -0.19 SER 424
GLY 29 0.22 GLN 106 -0.21 SER 424
GLY 29 0.24 VAL 107 -0.19 SER 424
SER 311 0.25 SER 108 -0.16 SER 426
SER 311 0.24 TRP 109 -0.17 VAL 33
SER 311 0.27 VAL 110 -0.18 SER 426
SER 311 0.31 SER 111 -0.15 SER 426
SER 311 0.30 LYS 112 -0.15 SER 426
SER 311 0.31 GLU 113 -0.16 SER 426
SER 311 0.34 TRP 114 -0.15 SER 426
SER 311 0.35 ALA 115 -0.13 SER 426
SER 311 0.34 LYS 116 -0.14 SER 426
SER 311 0.35 ARG 117 -0.14 SER 426
SER 311 0.39 ALA 118 -0.13 SER 426
SER 311 0.41 ALA 119 -0.12 SER 426
SER 311 0.46 LEU 120 -0.13 GLY 201
SER 311 0.46 PRO 121 -0.11 GLY 201
SER 311 0.48 SER 122 -0.11 GLY 201
SER 311 0.51 HIS 123 -0.09 GLY 201
SER 311 0.53 VAL 124 -0.10 GLY 386
SER 311 0.53 VAL 125 -0.13 SER 199
SER 311 0.55 THR 126 -0.12 SER 199
SER 311 0.59 MET 127 -0.10 GLY 386
SER 311 0.60 LEU 128 -0.12 GLY 386
SER 311 0.60 ASP 129 -0.12 GLY 386
SER 311 0.64 ASN 130 -0.10 GLY 386
SER 311 0.68 PHE 131 -0.12 GLY 386
SER 311 0.74 PRO 132 -0.11 GLY 386
SER 311 0.77 THR 133 -0.14 GLY 386
SER 311 0.85 ASN 134 -0.11 GLY 386
SER 311 0.80 LEU 135 -0.12 GLY 386
SER 311 0.81 HIS 136 -0.12 GLY 386
SER 311 0.72 PRO 137 -0.17 MET 387
SER 311 0.69 MET 138 -0.14 ALA 428
GLY 312 0.71 SER 139 -0.12 GLY 386
SER 311 0.66 GLN 140 -0.14 GLY 386
SER 311 0.60 LEU 141 -0.14 GLY 386
GLY 312 0.60 SER 142 -0.14 ALA 428
GLY 312 0.60 ALA 143 -0.12 GLY 386
SER 311 0.56 ALA 144 -0.12 GLY 386
SER 311 0.52 ILE 145 -0.13 ALA 428
GLY 312 0.52 THR 146 -0.13 ALA 428
SER 311 0.51 ALA 147 -0.11 ALA 428
SER 311 0.47 LEU 148 -0.11 ALA 428
SER 311 0.45 ASN 149 -0.12 ALA 428
SER 311 0.43 SER 150 -0.11 ALA 428
SER 311 0.40 GLU 151 -0.11 ALA 428
ASN 30 0.39 SER 152 -0.13 SER 426
ASN 30 0.38 ASN 153 -0.13 SER 426
ASN 30 0.42 PHE 154 -0.16 SER 426
ASN 30 0.43 ALA 155 -0.12 ALA 428
ASN 30 0.40 ARG 156 -0.10 VAL 33
ASN 30 0.41 ALA 157 -0.11 VAL 33
ASN 30 0.45 TYR 158 -0.11 SER 426
ASN 30 0.45 ALA 159 -0.07 LYS 116
ASN 30 0.42 GLU 160 -0.11 LYS 116
ASN 30 0.45 GLY 161 -0.08 LYS 116
ASN 30 0.44 ILE 162 -0.11 VAL 33
ASN 30 0.46 ASN 163 -0.14 SER 426
ASN 30 0.51 ARG 164 -0.19 SER 426
ASN 30 0.44 THR 165 -0.22 SER 426
ASN 30 0.41 LYS 166 -0.20 VAL 33
ASN 30 0.46 TYR 167 -0.21 SER 426
ASN 30 0.43 TRP 168 -0.24 SER 426
ASN 30 0.37 GLU 169 -0.21 VAL 33
ASN 30 0.39 PHE 170 -0.18 SER 426
ASN 30 0.42 VAL 171 -0.21 SER 426
ASN 30 0.37 TYR 172 -0.22 SER 426
ASN 30 0.34 GLU 173 -0.18 VAL 33
ASN 30 0.37 ASP 174 -0.18 SER 426
ASN 30 0.37 ALA 175 -0.20 SER 426
ASN 30 0.33 MET 176 -0.19 SER 426
SER 311 0.36 ASP 177 -0.16 SER 426
SER 311 0.40 LEU 178 -0.17 SER 426
SER 311 0.38 ILE 179 -0.18 SER 426
SER 311 0.39 ALA 180 -0.15 SER 426
SER 311 0.43 LYS 181 -0.14 SER 426
SER 311 0.46 LEU 182 -0.15 SER 426
SER 311 0.46 PRO 183 -0.14 SER 426
SER 311 0.48 CYS 184 -0.12 SER 426
SER 311 0.52 VAL 185 -0.12 GLY 386
SER 311 0.54 ALA 186 -0.16 GLY 386
SER 311 0.54 ALA 187 -0.14 GLY 386
SER 311 0.56 LYS 188 -0.14 GLY 386
SER 311 0.61 ILE 189 -0.19 GLY 386
SER 311 0.62 TYR 190 -0.26 GLY 386
SER 311 0.59 ARG 191 -0.18 GLY 386
SER 311 0.62 ASN 192 -0.18 GLY 386
SER 311 0.68 LEU 193 -0.22 GLY 386
SER 311 0.66 TYR 194 -0.30 GLY 386
SER 311 0.61 ARG 195 -0.19 GLY 386
SER 311 0.61 ALA 196 -0.17 GLY 386
SER 311 0.59 GLY 197 -0.15 GLY 386
SER 311 0.55 SER 198 -0.10 LYS 339
SER 311 0.51 SER 199 -0.13 VAL 125
SER 311 0.50 ILE 200 -0.11 VAL 125
SER 311 0.46 GLY 201 -0.13 LEU 120
SER 311 0.42 ALA 202 -0.10 SER 426
SER 311 0.40 ILE 203 -0.11 SER 426
SER 311 0.37 ASP 204 -0.11 SER 426
SER 311 0.34 SER 205 -0.12 SER 426
SER 311 0.31 LYS 206 -0.12 SER 426
SER 311 0.33 LEU 207 -0.13 SER 426
SER 311 0.33 ASP 208 -0.14 SER 426
SER 311 0.37 TRP 209 -0.14 SER 426
SER 311 0.39 SER 210 -0.14 SER 426
SER 311 0.38 HIS 211 -0.12 SER 426
SER 311 0.41 ASN 212 -0.12 SER 426
SER 311 0.45 PHE 213 -0.12 SER 426
SER 311 0.47 THR 214 -0.11 SER 426
SER 311 0.45 ASN 215 -0.10 LYS 339
SER 311 0.48 MET 216 -0.10 SER 426
SER 311 0.52 LEU 217 -0.12 LYS 339
SER 311 0.51 GLY 218 -0.11 LYS 339
SER 311 0.48 TYR 219 -0.14 LYS 339
SER 311 0.43 THR 220 -0.16 LYS 339
SER 311 0.39 ASP 221 -0.23 LYS 339
SER 311 0.35 PRO 222 -0.23 LYS 339
SER 311 0.35 GLN 223 -0.24 LYS 339
SER 311 0.40 PHE 224 -0.17 LYS 339
SER 311 0.38 THR 225 -0.15 LYS 355
SER 311 0.33 GLU 226 -0.21 LYS 355
SER 311 0.38 LEU 227 -0.15 LYS 355
SER 311 0.41 MET 228 -0.15 SER 426
SER 311 0.34 ARG 229 -0.17 SER 426
SER 311 0.33 LEU 230 -0.18 LYS 355
SER 311 0.40 TYR 231 -0.17 SER 426
SER 311 0.39 LEU 232 -0.19 SER 426
SER 311 0.31 THR 233 -0.20 SER 426
SER 311 0.32 ILE 234 -0.20 SER 426
SER 311 0.38 HIS 235 -0.21 SER 426
GLY 29 0.35 SER 236 -0.24 SER 426
GLY 29 0.39 ASP 237 -0.28 SER 426
GLY 29 0.40 HIS 238 -0.31 SER 424
GLY 29 0.46 GLU 239 -0.42 SER 424
GLY 29 0.52 GLY 240 -0.42 SER 424
ASN 30 0.53 GLY 241 -0.45 SER 426
LYS 366 0.46 ASN 242 -0.38 SER 426
GLY 44 0.58 VAL 243 -0.35 SER 426
GLY 44 0.47 SER 244 -0.30 SER 426
ASN 30 0.47 ALA 245 -0.35 SER 426
GLY 44 0.58 HIS 246 -0.42 SER 426
GLY 44 0.60 THR 247 -0.34 SER 426
ASN 30 0.51 SER 248 -0.31 SER 426
ASN 30 0.58 HIS 249 -0.38 SER 426
ASN 30 0.61 LEU 250 -0.38 SER 426
ASN 30 0.56 VAL 251 -0.27 SER 426
ASN 30 0.56 GLY 252 -0.28 SER 426
ASN 30 0.65 SER 253 -0.32 SER 426
ASN 30 0.62 ALA 254 -0.25 SER 426
ASN 30 0.57 LEU 255 -0.20 SER 426
ASN 30 0.52 SER 256 -0.17 SER 426
ASN 30 0.47 ASP 257 -0.17 SER 426
ASN 30 0.44 PRO 258 -0.20 SER 426
SER 311 0.43 TYR 259 -0.16 SER 426
GLY 312 0.46 LEU 260 -0.16 ALA 428
ASN 30 0.48 SER 261 -0.22 SER 426
SER 311 0.45 PHE 262 -0.21 SER 426
GLY 312 0.52 ALA 263 -0.16 SER 426
GLY 312 0.54 ALA 264 -0.18 ALA 428
GLY 312 0.51 ALA 265 -0.24 SER 426
GLY 312 0.57 MET 266 -0.19 SER 426
GLY 312 0.65 ASN 267 -0.17 ALA 428
GLY 312 0.62 GLY 268 -0.21 SER 426
GLY 312 0.60 LEU 269 -0.21 SER 426
GLY 312 0.72 ALA 270 -0.17 ASN 391
GLY 312 0.78 GLY 271 -0.16 ALA 428
GLY 312 0.88 PRO 272 -0.16 ALA 428
GLY 312 0.75 LEU 273 -0.16 SER 426
GLY 312 0.64 HIS 274 -0.22 SER 426
GLY 312 0.61 GLY 275 -0.20 SER 426
GLY 312 0.74 LEU 276 -0.17 SER 426
SER 311 0.72 ALA 277 -0.16 SER 426
SER 311 0.67 ASN 278 -0.16 SER 426
SER 311 0.77 GLN 279 -0.14 SER 426
SER 311 0.87 GLU 280 -0.13 TRP 284
SER 311 0.77 VAL 281 -0.13 SER 426
SER 311 0.77 LEU 282 -0.11 SER 426
SER 311 0.89 LEU 283 -0.11 ALA 428
SER 311 0.92 TRP 284 -0.15 LEU 273
SER 311 0.76 LEU 285 -0.13 HIS 320
SER 311 0.70 SER 286 -0.13 VAL 315
SER 311 0.74 GLN 287 -0.31 VAL 315
SER 311 0.61 LEU 288 -0.77 VAL 315
SER 311 0.55 GLN 289 -0.41 VAL 315
SER 311 0.48 LYS 290 -0.32 VAL 315
SER 311 0.43 ASP 291 -0.46 VAL 315
SER 311 0.42 ASP 295 -0.18 VAL 315
SER 297 0.45 ALA 296 -0.26 VAL 315
ALA 296 0.45 SER 297 -0.16 GLU 335
SER 311 0.43 ASP 298 -0.21 GLU 335
TRP 284 0.44 GLU 299 -0.17 LYS 76
TRP 284 0.48 LYS 300 -0.13 ALA 367
TRP 284 0.49 LEU 301 -0.14 ALA 367
TRP 284 0.57 ARG 302 -0.14 PRO 72
TRP 284 0.61 ASP 303 -0.17 ALA 367
TRP 284 0.71 TYR 304 -0.29 ALA 367
TRP 284 0.72 ILE 305 -0.29 ALA 367
TRP 284 0.69 TRP 306 -0.27 LYS 366
TRP 284 0.81 ASN 307 -0.37 LYS 366
TRP 284 0.87 THR 308 -0.37 ALA 367
ASN 310 0.69 LEU 309 -0.59 LYS 366
TRP 284 0.80 ASN 310 -0.67 LYS 366
TRP 284 0.92 SER 311 -0.22 LYS 366
PRO 272 0.88 GLY 312 -0.46 LYS 366
PRO 272 0.88 ARG 313 -0.34 ALA 367
GLY 312 0.81 VAL 314 -0.51 LEU 288
PRO 316 0.78 VAL 315 -0.77 LEU 288
VAL 315 0.78 PRO 316 -0.32 LEU 288
GLN 364 0.59 GLY 317 -0.22 LEU 288
GLN 364 0.57 TYR 318 -0.39 LEU 288
LYS 366 0.56 GLY 319 -0.35 LEU 288
LYS 366 0.52 HIS 320 -0.32 LEU 288
LYS 366 0.52 ALA 321 -0.28 LEU 288
LYS 366 0.39 VAL 322 -0.26 SER 424
LYS 366 0.32 LEU 323 -0.24 SER 424
GLY 29 0.26 ARG 324 -0.22 LYS 423
GLY 29 0.25 LYS 325 -0.24 PRO 72
GLY 29 0.24 THR 326 -0.28 PRO 72
GLY 29 0.28 ASP 327 -0.19 SER 424
GLY 29 0.29 PRO 328 -0.27 THR 326
GLY 29 0.30 ARG 329 -0.18 TYR 354
SER 311 0.33 TYR 330 -0.19 TYR 354
GLY 29 0.27 THR 331 -0.38 TYR 354
GLY 29 0.28 CYS 332 -0.33 TYR 354
SER 311 0.33 GLN 333 -0.28 TYR 354
SER 311 0.32 ARG 334 -0.34 TYR 354
SER 311 0.26 GLU 335 -0.40 LYS 355
SER 311 0.31 PHE 336 -0.27 LYS 355
SER 311 0.35 ALA 337 -0.19 TYR 354
SER 311 0.30 LEU 338 -0.27 LYS 355
SER 311 0.28 LYS 339 -0.27 LYS 355
SER 311 0.33 HIS 340 -0.20 ASP 221
SER 311 0.37 LEU 341 -0.15 ALA 351
SER 311 0.33 PRO 342 -0.20 ALA 351
SER 311 0.37 SER 343 -0.12 TYR 194
SER 311 0.44 ASP 344 -0.11 TYR 194
SER 311 0.47 PRO 345 -0.09 VAL 315
SER 311 0.54 MET 346 -0.09 SER 426
SER 311 0.47 PHE 347 -0.09 SER 426
SER 311 0.43 LYS 348 -0.12 VAL 315
SER 311 0.49 LEU 349 -0.20 VAL 315
SER 311 0.48 VAL 350 -0.16 VAL 315
SER 311 0.41 ALA 351 -0.20 PRO 342
SER 311 0.43 GLN 352 -0.28 GLU 335
SER 311 0.46 LEU 353 -0.20 GLU 335
SER 311 0.42 TYR 354 -0.38 THR 331
SER 311 0.39 LYS 355 -0.40 GLU 335
PRO 316 0.46 ILE 356 -0.25 PRO 72
PRO 316 0.55 VAL 357 -0.21 PRO 72
ASN 359 0.46 PRO 358 -0.31 PRO 72
PRO 316 0.52 ASN 359 -0.32 PRO 72
PRO 316 0.66 VAL 360 -0.16 PRO 72
GLN 364 0.65 LEU 361 -0.19 PRO 72
PRO 370 0.52 LEU 362 -0.28 PRO 72
LEU 361 0.62 GLU 363 -0.19 GLU 73
VAL 314 0.71 GLN 364 -0.19 ASN 310
ALA 367 0.68 GLY 365 -0.28 ASN 310
ALA 367 0.77 LYS 366 -0.67 ASN 310
LYS 366 0.77 ALA 367 -0.54 LEU 309
GLY 365 0.55 LYS 368 -0.30 LEU 309
LYS 366 0.47 ASN 369 -0.28 LEU 288
LEU 362 0.52 PRO 370 -0.24 LEU 288
GLN 364 0.42 TRP 371 -0.25 PRO 72
GLN 364 0.42 PRO 372 -0.22 LEU 288
GLN 364 0.41 ASN 373 -0.19 LEU 288
SER 311 0.41 VAL 374 -0.16 SER 426
SER 311 0.53 ASP 375 -0.16 SER 426
SER 311 0.53 ALA 376 -0.13 SER 426
SER 311 0.48 HIS 377 -0.13 SER 426
SER 311 0.50 SER 378 -0.15 SER 426
SER 311 0.59 GLY 379 -0.14 SER 426
SER 311 0.55 VAL 380 -0.12 SER 426
SER 311 0.48 LEU 381 -0.13 SER 426
SER 311 0.54 LEU 382 -0.14 SER 426
SER 311 0.59 GLN 383 -0.12 SER 426
SER 311 0.51 TYR 384 -0.16 TYR 194
SER 311 0.49 TYR 385 -0.22 TYR 194
SER 311 0.55 GLY 386 -0.30 TYR 194
SER 311 0.59 MET 387 -0.22 TYR 190
SER 311 0.65 THR 388 -0.12 SER 426
SER 311 0.69 GLU 389 -0.13 ALA 428
SER 311 0.72 MET 390 -0.13 ALA 428
SER 311 0.75 ASN 391 -0.17 ALA 270
SER 311 0.68 TYR 392 -0.14 ALA 428
SER 311 0.63 TYR 393 -0.16 SER 426
SER 311 0.63 THR 394 -0.17 SER 426
SER 311 0.60 VAL 395 -0.17 MET 387
SER 311 0.53 LEU 396 -0.17 SER 426
SER 311 0.51 PHE 397 -0.19 SER 426
SER 311 0.51 GLY 398 -0.20 SER 426
SER 311 0.47 VAL 399 -0.19 SER 426
SER 311 0.41 SER 400 -0.21 SER 426
SER 311 0.41 ARG 401 -0.24 SER 426
SER 311 0.40 ALA 402 -0.23 SER 426
GLY 29 0.36 LEU 403 -0.24 SER 426
GLY 29 0.40 GLY 404 -0.28 SER 426
ASN 30 0.43 VAL 405 -0.30 SER 426
ASN 30 0.41 LEU 406 -0.27 SER 426
GLY 29 0.41 ALA 407 -0.29 SER 426
GLY 29 0.48 GLN 408 -0.34 SER 424
ASN 30 0.49 LEU 409 -0.31 SER 426
ASN 30 0.44 ILE 410 -0.29 SER 426
GLY 29 0.48 TRP 411 -0.37 SER 424
ASN 30 0.57 SER 412 -0.37 SER 424
ASN 30 0.54 ARG 413 -0.30 SER 426
ASN 30 0.47 ALA 414 -0.32 SER 424
ASN 30 0.54 LEU 415 -0.45 PRO 422
ASN 30 0.65 GLY 416 -0.33 SER 426
ASN 30 0.74 PHE 417 -0.40 SER 426
ASN 30 0.81 PRO 418 -0.32 SER 426
ASN 30 0.77 LEU 419 -0.32 SER 426
ASN 30 0.76 GLU 420 -0.42 SER 426
PRO 422 0.94 ARG 421 -0.42 SER 426
ARG 421 0.94 PRO 422 -1.00 ILE 21
ARG 421 0.74 LYS 423 -1.54 GLY 34
TYR 42 0.69 SER 424 -1.08 GLY 50
TYR 42 0.71 MET 425 -0.79 GLY 50
TYR 42 0.59 SER 426 -0.77 GLY 50
TYR 42 0.51 THR 427 -0.52 GLY 50
GLY 365 0.46 ALA 428 -0.39 GLY 50
TYR 42 0.49 GLY 429 -0.33 GLY 50
TYR 42 0.54 LEU 430 -0.26 ILE 21
GLY 365 0.50 GLU 431 -0.20 ILE 21
GLY 365 0.49 LYS 432 -0.14 ILE 21

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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.