CNRS Nantes University UFIP UFIP
home |  start a new run |  job status |  references&downloads |  examples |  help  

Should you encounter any unexpected behaviour,
please let us know.


***  dndD2_2  ***

CA distance fluctuations for 220505024451142116

---  normal mode 9  ---

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 329 1.03 MET 1 -0.02 SER 487
LYS 329 1.08 LEU 2 -0.02 SER 487
LYS 329 1.14 ILE 3 -0.01 SER 487
LYS 329 1.15 LYS 4 -0.02 SER 487
LYS 329 1.20 GLN 5 -0.01 SER 487
LYS 329 1.24 LEU 6 -0.01 SER 487
LYS 329 1.25 VAL 7 -0.01 SER 487
LYS 329 1.28 LEU 8 -0.01 SER 487
GLU 330 1.26 HIS 9 -0.00 SER 487
GLU 330 1.29 ASN 10 -0.00 SER 487
LYS 329 1.32 PHE 11 -0.00 LEU 80
GLU 330 1.39 ARG 12 -0.00 SER 487
GLU 330 1.46 VAL 13 -0.00 SER 487
GLU 330 1.41 PHE 14 -0.00 SER 487
GLU 330 1.37 ASN 15 -0.00 SER 487
GLU 330 1.31 GLY 16 -0.00 SER 487
GLU 330 1.28 THR 17 -0.01 SER 487
LYS 329 1.34 HIS 18 -0.01 SER 487
LYS 329 1.30 THR 19 -0.01 SER 487
LYS 329 1.32 ILE 20 -0.01 SER 487
LYS 329 1.28 ASP 21 -0.01 SER 487
LYS 329 1.24 LEU 22 -0.01 SER 487
LYS 329 1.19 ALA 23 -0.02 SER 487
LYS 329 1.18 PRO 24 -0.02 SER 487
LYS 329 1.19 ARG 25 -0.02 SER 487
LYS 329 1.16 LYS 26 -0.02 SER 487
LYS 329 1.19 ARG 27 -0.02 SER 487
LYS 329 1.17 PRO 28 -0.03 SER 487
LYS 329 1.11 HIS 29 -0.03 SER 487
LYS 329 1.09 ASP 30 -0.02 SER 487
LYS 329 1.04 LEU 31 -0.03 SER 487
LYS 329 1.06 ASN 32 -0.02 SER 487
LYS 329 1.08 PRO 33 -0.02 SER 487
LYS 329 1.15 ARG 34 -0.02 SER 487
LYS 329 1.15 PRO 35 -0.02 SER 487
LYS 329 1.22 ILE 36 -0.01 SER 487
LYS 329 1.29 VAL 37 -0.01 SER 487
LYS 329 1.35 LEU 38 -0.01 SER 487
LYS 329 1.42 PHE 39 -0.01 SER 487
LYS 329 1.48 GLY 40 -0.01 SER 487
LYS 329 1.54 GLY 41 -0.00 SER 487
GLU 330 1.57 LEU 42 -0.00 SER 487
GLU 330 1.56 ASN 43 -0.00 SER 487
GLU 330 1.58 GLY 44 -0.00 SER 487
GLU 330 1.57 ALA 45 -0.00 SER 487
LYS 329 1.50 GLY 46 -0.00 SER 487
LYS 329 1.46 LYS 47 -0.00 SER 487
LYS 329 1.43 THR 48 -0.00 SER 487
LYS 329 1.41 SER 49 -0.00 SER 487
LYS 329 1.36 ILE 50 -0.00 SER 487
LYS 329 1.32 LEU 51 -0.00 SER 487
LYS 329 1.31 SER 52 -0.00 SER 487
LYS 329 1.28 ALA 53 -0.00 SER 487
LYS 329 1.23 ILE 54 -0.01 SER 487
LYS 329 1.21 ARG 55 -0.00 SER 487
LYS 329 1.20 ILE 56 -0.00 SER 487
LYS 329 1.16 ALA 57 -0.00 SER 487
LYS 329 1.11 LEU 58 -0.01 SER 487
LYS 329 1.12 TYR 59 -0.00 SER 487
LYS 329 1.14 GLY 60 -0.00 ARG 61
LYS 329 1.14 ARG 61 -0.00 GLY 60
LYS 329 1.13 LEU 62 -0.00 LEU 58
LYS 329 1.20 ALA 63 -0.00 LEU 98
LYS 329 1.24 PHE 64 -0.00 ILE 54
LYS 329 1.20 GLY 65 -0.00 LYS 4
LYS 329 1.13 LEU 66 -0.00 LEU 58
LYS 329 1.16 ALA 67 -0.00 ALA 261
LYS 329 1.19 THR 68 -0.00 ALA 261
LYS 329 1.15 GLN 69 -0.01 ALA 261
LYS 329 1.11 GLN 70 -0.01 ALA 261
GLU 330 1.15 GLN 71 -0.01 ALA 261
LYS 329 1.21 GLU 72 -0.01 ALA 261
LYS 329 1.19 TYR 73 -0.00 ALA 261
GLU 330 1.17 ILE 74 -0.01 ALA 261
GLU 330 1.23 GLU 75 -0.01 ALA 261
LYS 329 1.27 GLN 76 -0.00 LEU 8
LYS 329 1.23 LEU 77 -0.00 GLU 72
GLU 330 1.24 SER 78 -0.00 ALA 261
GLU 330 1.32 ALA 79 -0.00 ALA 261
GLU 330 1.32 LEU 80 -0.00 PHE 11
GLU 330 1.29 ILE 81 -0.00 ASN 10
GLU 330 1.35 HIS 82 -0.00 SER 487
GLN 333 1.37 ASN 83 -0.00 GLY 44
GLN 333 1.41 GLY 84 -0.00 SER 487
PHE 334 1.44 ALA 85 -0.00 SER 487
GLN 337 1.40 TYR 86 -0.00 ALA 261
GLN 337 1.38 TYR 87 -0.00 SER 487
GLN 337 1.35 ILE 88 -0.00 SER 487
GLN 337 1.27 GLU 89 -0.00 SER 487
GLN 333 1.28 GLN 90 -0.00 ALA 261
GLN 333 1.24 PRO 91 -0.00 SER 487
GLN 333 1.18 GLU 92 -0.00 ALA 261
GLN 333 1.17 GLU 93 -0.00 SER 487
GLU 330 1.21 ALA 94 -0.00 SER 487
LYS 329 1.19 SER 95 -0.00 SER 487
LYS 329 1.20 VAL 96 -0.00 SER 487
LYS 329 1.16 GLU 97 -0.01 SER 487
LYS 329 1.15 LEU 98 -0.01 SER 487
LYS 329 1.12 THR 99 -0.01 SER 487
LYS 329 1.08 PHE 100 -0.02 SER 487
LYS 329 1.03 THR 101 -0.02 ALA 488
LYS 329 0.98 TYR 102 -0.03 ALA 488
LYS 329 0.93 ASN 103 -0.04 ALA 488
LYS 329 0.89 LYS 104 -0.14 LYS 192
LYS 329 0.84 GLY 105 -1.07 LEU 193
LYS 329 0.86 GLY 106 -0.43 ASN 195
LYS 329 0.88 HIS 107 -0.15 ASP 196
LYS 329 0.94 GLU 108 -0.04 ALA 488
LYS 329 0.95 ALA 109 -0.03 ALA 488
LYS 329 1.01 GLU 110 -0.02 ALA 488
LYS 329 1.02 PHE 111 -0.02 ALA 488
LYS 329 1.06 THR 112 -0.01 SER 487
LYS 329 1.07 VAL 113 -0.01 SER 487
LYS 329 1.09 THR 114 -0.01 SER 487
LYS 329 1.11 ARG 115 -0.00 SER 487
GLU 330 1.12 THR 116 -0.00 SER 487
GLU 330 1.13 TRP 117 -0.00 GLU 163
GLU 330 1.13 LYS 118 -0.00 ALA 261
GLN 333 1.17 LYS 119 -0.01 ALA 261
GLN 333 1.14 GLY 120 -0.01 ALA 261
GLU 330 1.10 LYS 121 -0.01 ALA 261
GLU 330 1.09 ARG 122 -0.00 ALA 261
LYS 329 1.09 ASP 123 -0.00 THR 116
GLU 330 1.04 ARG 124 -0.00 SER 487
LYS 329 1.04 LEU 125 -0.00 SER 487
LYS 329 1.01 SER 126 -0.01 SER 487
LYS 329 1.00 LEU 127 -0.01 SER 487
LYS 329 0.98 GLN 128 -0.01 SER 487
LYS 329 0.96 GLN 129 -0.02 ALA 488
LYS 329 0.97 ASP 130 -0.03 ALA 488
LYS 329 0.98 GLY 131 -0.02 ALA 488
LYS 329 0.94 GLN 132 -0.02 ALA 488
LYS 329 0.94 PRO 133 -0.01 SER 487
LYS 329 0.91 LEU 134 -0.01 ALA 488
GLU 330 0.89 SER 135 -0.01 SER 487
GLU 330 0.86 GLU 136 -0.01 SER 487
LYS 329 0.89 LEU 137 -0.01 SER 487
LYS 329 0.91 ASP 138 -0.00 SER 487
LYS 329 0.96 TYR 139 -0.00 SER 487
LYS 329 0.95 ASP 140 -0.00 GLN 128
LYS 329 0.92 GLN 141 -0.00 SER 487
LYS 329 0.96 CYS 142 -0.01 SER 487
LYS 329 1.00 GLN 143 -0.00 SER 487
LYS 329 0.95 GLY 144 -0.00 SER 487
LYS 329 0.95 PHE 145 -0.01 ALA 488
LYS 329 1.01 LEU 146 -0.01 SER 487
LYS 329 1.00 ASN 147 -0.01 SER 487
LYS 329 0.95 GLU 148 -0.01 ALA 488
LYS 329 0.98 LEU 149 -0.02 ALA 488
LYS 329 1.02 ILE 150 -0.01 SER 487
LYS 329 1.02 PRO 151 -0.01 SER 487
LYS 329 1.07 HIS 152 -0.00 SER 487
LYS 329 1.06 GLY 153 -0.00 SER 487
LYS 329 1.05 ILE 154 -0.01 SER 487
LYS 329 1.11 ALA 155 -0.01 SER 487
LYS 329 1.15 ASP 156 -0.00 SER 487
LYS 329 1.12 LEU 157 -0.01 ILE 176
LYS 329 1.13 PHE 158 -0.01 SER 487
LYS 329 1.20 PHE 159 -0.01 SER 487
LYS 329 1.24 PHE 160 -0.00 SER 487
LYS 329 1.32 ASP 161 -0.00 SER 487
LYS 329 1.32 GLY 162 -0.00 SER 487
LYS 329 1.35 GLU 163 -0.00 ASN 491
LYS 329 1.28 LYS 164 -0.00 ASN 491
LYS 329 1.23 ILE 165 -0.00 SER 487
LYS 329 1.26 ALA 166 -0.00 ASN 491
LYS 329 1.26 GLU 167 -0.00 PHE 160
LYS 329 1.18 LEU 168 -0.00 ASP 171
LYS 329 1.16 ALA 169 -0.00 ASN 491
LYS 329 1.19 GLU 170 -0.00 LYS 512
LYS 329 1.16 ASP 171 -0.00 LEU 168
LYS 329 1.12 GLU 172 -0.00 ILE 569
LYS 329 1.10 SER 173 -0.01 PRO 608
LYS 329 1.07 GLY 174 -0.02 ASP 30
LYS 329 1.08 ASN 175 -0.01 SER 611
LYS 329 1.11 ILE 176 -0.01 LYS 26
LYS 329 1.07 LEU 177 -0.01 PRO 33
LYS 329 1.01 ARG 178 -0.01 LEU 31
LYS 329 1.04 THR 179 -0.00 HIS 612
LYS 329 1.04 ALA 180 -0.01 HIS 612
LYS 329 0.98 VAL 181 -0.00 ASN 491
LYS 329 0.96 ARG 182 -0.01 ARG 581
LYS 329 0.98 ARG 183 -0.01 ARG 581
LYS 329 0.97 LEU 184 -0.01 ARG 581
LYS 329 0.91 LEU 185 -0.01 ASN 491
LYS 329 0.91 GLY 186 -0.01 ASN 491
LYS 329 0.89 LEU 187 -0.00 ASN 491
LYS 329 0.92 ASP 188 -0.00 ASN 491
LYS 329 0.88 LEU 189 -0.03 GLY 106
LYS 329 0.85 ILE 190 -0.10 GLY 106
LYS 329 0.86 SER 191 -0.07 GLY 106
LYS 329 0.87 LYS 192 -0.29 GLY 106
LYS 329 0.83 LEU 193 -1.07 GLY 105
LYS 329 0.81 ARG 194 -0.22 GLY 105
LYS 329 0.83 ASN 195 -0.64 GLY 105
LYS 329 0.82 ASP 196 -0.38 GLY 105
LYS 329 0.79 LEU 197 -0.19 GLY 105
LYS 329 0.78 MET 198 -0.16 GLY 105
LYS 329 0.79 ILE 199 -0.22 GLY 105
LYS 329 0.77 PHE 200 -0.13 GLY 105
LYS 329 0.75 VAL 201 -0.10 GLY 105
LYS 329 0.75 LYS 202 -0.10 GLY 105
LYS 329 0.75 ARG 203 -0.10 GLY 105
GLU 330 0.73 GLN 204 -0.08 GLY 105
GLU 330 0.72 GLN 205 -0.34 ASN 491
GLU 330 0.72 SER 206 -0.18 ASN 491
GLU 330 0.72 SER 207 -0.53 ALA 488
GLU 330 0.69 GLN 208 -0.24 SER 487
GLU 330 0.69 LEU 209 -0.17 LYS 490
GLU 330 0.68 ALA 210 -0.12 SER 484
GLU 330 0.70 SER 211 -0.22 LYS 490
GLU 330 0.69 SER 212 -0.09 LYS 490
GLU 330 0.69 GLN 213 -0.05 LYS 490
LYS 329 0.71 GLN 214 -0.12 LYS 490
LYS 329 0.72 GLN 215 -0.05 GLY 105
LYS 329 0.71 GLN 216 -0.03 GLY 105
LYS 329 0.72 ILE 217 -0.04 GLY 105
LYS 329 0.74 ALA 218 -0.03 GLY 105
LEU 498 1.43 GLU 219 -0.01 LYS 436
LYS 329 0.73 LEU 220 -0.01 LYS 436
LYS 329 0.76 GLU 221 -0.01 LYS 436
LYS 329 0.77 LYS 222 -0.01 LYS 436
LYS 329 0.75 GLN 223 -0.01 GLU 226
LYS 329 0.75 SER 224 -0.00 LYS 436
LYS 329 0.78 LYS 225 -0.01 LYS 436
LYS 329 0.77 GLU 226 -0.01 LYS 436
LYS 329 0.75 LEU 227 -0.01 ALA 233
LYS 329 0.77 ALA 228 -0.00 LYS 436
LYS 329 0.78 CYS 229 -0.01 LYS 436
LYS 329 0.75 GLN 230 -0.01 ALA 233
LYS 329 0.74 THR 231 -0.00 ALA 233
LYS 329 0.76 GLU 232 -0.01 LYS 436
LYS 329 0.73 ALA 233 -0.01 GLN 230
LYS 329 0.69 LEU 234 -0.01 SER 237
LYS 329 0.70 LEU 235 -0.00 GLN 230
LYS 329 0.70 GLU 236 -0.01 HIS 254
LYS 329 0.65 SER 237 -0.01 GLN 230
LYS 329 0.63 ALA 238 -0.01 ALA 241
LYS 329 0.64 ASP 239 -0.00 LYS 436
LYS 329 0.60 PHE 240 -0.01 SER 243
LYS 329 0.55 ALA 241 -0.05 LYS 270
LYS 329 0.55 LYS 242 -0.01 LYS 270
LYS 329 0.53 SER 243 -0.03 LYS 270
GLU 330 0.47 ARG 244 -0.20 LYS 270
GLU 330 0.46 ILE 245 -0.24 LYS 270
GLU 330 0.45 GLU 246 -0.21 LYS 270
GLN 333 0.41 PHE 247 -0.36 LYS 270
GLN 337 0.38 LEU 248 -0.55 LYS 270
GLN 337 0.38 SER 249 -0.50 LYS 270
THR 405 0.42 LYS 250 -0.57 LYS 270
GLU 409 0.60 ASP 251 -0.85 LYS 270
SER 408 0.73 ILE 252 -0.92 LYS 270
GLU 409 0.37 THR 253 -0.85 LYS 270
GLU 409 0.31 HIS 254 -1.06 ALA 267
GLN 413 0.38 TYR 255 -1.37 LYS 270
GLN 337 0.26 GLU 256 -1.27 LYS 270
GLN 337 0.25 GLY 257 -1.36 ALA 265
GLN 337 0.23 LEU 258 -1.60 ALA 265
GLN 337 0.22 LEU 259 -1.72 ALA 267
GLN 337 0.22 ASN 260 -1.71 ALA 265
GLN 337 0.20 ALA 261 -1.89 ALA 265
LEU 311 1.07 GLN 262 -1.71 GLY 264
HIS 310 1.09 GLY 263 -1.67 GLY 264
GLN 337 0.21 GLY 264 -1.88 ALA 265
HIS 310 1.01 ALA 265 -1.89 ALA 261
LEU 311 0.99 PHE 266 -1.70 GLY 264
ARG 423 1.50 ALA 267 -1.77 THR 269
GLN 337 0.23 GLN 268 -1.65 ALA 267
GLN 337 0.22 THR 269 -1.77 ALA 267
ALA 419 1.36 LYS 270 -1.81 GLN 416
GLN 337 0.23 ALA 271 -1.68 LYS 270
GLN 413 0.25 GLN 272 -1.47 LYS 270
GLN 337 0.23 GLU 273 -1.65 LYS 270
PHE 434 0.32 LYS 274 -1.57 ALA 418
LEU 437 0.48 GLN 275 -1.23 ALA 418
LEU 437 0.36 LYS 276 -1.23 LYS 270
LYS 436 0.49 VAL 277 -1.35 ALA 418
ARG 438 0.28 GLU 278 -1.09 ALA 418
LEU 440 0.28 THR 279 -0.86 ALA 418
LEU 440 0.32 LEU 280 -0.98 ALA 418
ASP 439 0.33 LEU 281 -0.98 ALA 418
THR 367 0.29 LYS 282 -0.68 ALA 418
THR 367 0.28 ASP 283 -0.59 ALA 418
LEU 440 0.32 LYS 284 -0.78 ALA 418
THR 367 0.30 GLU 285 -0.61 ALA 418
THR 367 0.31 HIS 286 -0.35 ALA 418
ASP 363 0.29 LEU 287 -0.41 LYS 270
THR 367 0.29 GLU 288 -0.55 ALA 418
PRO 369 0.32 LYS 289 -0.29 ALA 418
ASP 363 0.31 ALA 290 -0.11 LYS 270
ASP 363 0.29 LEU 291 -0.27 LYS 270
THR 367 0.31 ARG 292 -0.26 LYS 270
TYR 364 0.32 GLN 293 -0.08 LYS 351
GLU 426 0.41 GLU 294 -0.09 LYS 351
ASP 363 0.29 CYS 295 -0.09 LYS 270
GLU 428 0.35 ASP 296 -0.08 LYS 351
GLU 428 0.59 GLY 297 -0.12 LYS 351
GLU 426 0.73 SER 298 -0.14 LYS 351
GLU 426 0.56 LEU 299 -0.12 LYS 351
GLU 426 0.46 PRO 300 -0.11 ALA 354
PRO 425 0.72 TYR 301 -0.15 ALA 354
PRO 425 0.64 ALA 302 -0.16 ILE 357
PRO 425 0.38 LEU 303 -0.14 ALA 354
PRO 425 0.55 ALA 304 -0.17 ILE 357
PRO 425 0.72 PRO 305 -0.21 ILE 357
GLY 263 0.74 THR 306 -0.24 ILE 357
GLY 263 0.83 ILE 307 -0.22 ILE 357
GLY 263 0.97 LEU 308 -0.25 GLY 371
GLY 263 1.07 SER 309 -0.45 GLY 371
GLY 263 1.09 HIS 310 -0.51 GLY 371
GLY 263 1.09 LEU 311 -0.49 GLY 371
GLY 263 1.07 LEU 312 -0.71 GLY 371
GLY 263 1.04 GLN 313 -0.94 GLY 371
GLY 263 1.03 GLN 314 -0.97 GLY 371
PRO 425 0.95 ILE 315 -0.99 GLY 371
GLY 263 0.90 ALA 316 -1.41 GLY 371
GLY 263 0.87 ASP 317 -1.63 GLY 371
PRO 425 0.85 GLU 318 -1.43 GLY 371
PRO 425 0.79 THR 319 -1.47 ILE 321
ASP 432 1.19 GLN 320 -1.44 THR 319
ASP 432 1.17 ILE 321 -1.47 THR 319
ASP 432 1.07 LYS 322 -1.42 THR 319
ASP 432 1.04 GLN 323 -1.15 THR 319
ASP 432 1.04 ALA 324 -0.98 THR 319
ASP 432 0.99 LYS 325 -0.99 LYS 329
GLU 428 0.90 SER 326 -1.36 LYS 329
GLU 428 0.91 PHE 327 -1.43 LYS 329
GLU 428 0.91 GLU 328 -1.34 LYS 329
VAL 643 1.58 LYS 329 -1.43 PHE 327
PHE 644 1.60 GLU 330 -1.17 PHE 327
ALA 646 1.62 LEU 331 -1.19 GLU 328
GLN 333 1.83 SER 332 -1.10 GLU 328
SER 332 1.83 GLN 333 -0.79 PHE 327
ALA 646 1.64 PHE 334 -0.69 GLU 328
THR 336 1.99 LEU 335 -0.83 THR 358
LEU 335 1.99 THR 336 -0.54 GLU 328
LEU 338 1.68 GLN 337 -0.37 PHE 327
GLN 337 1.68 LEU 338 -1.02 ALA 354
ASN 340 1.58 ARG 339 -1.09 ALA 354
ARG 339 1.58 ASN 340 -0.71 ALA 354
HIS 647 1.46 ASP 341 -0.69 ALA 354
LYS 351 1.97 ILE 342 -0.94 ALA 354
LYS 351 1.77 ALA 343 -0.83 ALA 354
GLY 350 1.73 PHE 344 -0.55 ALA 354
THR 349 1.96 ARG 345 -0.65 ALA 354
GLY 348 1.87 SER 346 -0.82 ALA 354
THR 349 1.65 ALA 347 -0.88 ALA 354
SER 346 1.87 GLY 348 -1.07 ALA 353
ARG 345 1.96 THR 349 -1.27 ILE 352
PHE 344 1.73 GLY 350 -1.30 ALA 354
ILE 342 1.97 LYS 351 -1.51 ALA 354
THR 358 0.99 ILE 352 -1.35 LYS 351
THR 358 1.08 ALA 353 -1.48 LYS 351
THR 358 1.20 ALA 354 -1.51 LYS 351
THR 358 1.43 GLU 355 -1.15 LYS 351
ASP 359 1.37 ALA 356 -0.75 LYS 351
THR 358 1.69 ILE 357 -0.93 LYS 351
ILE 357 1.69 THR 358 -0.83 LEU 335
ILE 357 1.39 ASP 359 -0.25 LEU 331
ALA 356 1.24 ASN 360 -0.19 THR 319
ILE 357 1.16 LEU 361 -0.53 LEU 331
GLU 625 1.07 LYS 362 -0.36 THR 319
THR 621 1.18 ASP 363 -0.31 ASP 317
THR 621 1.15 TYR 364 -0.37 ASP 317
GLU 625 1.10 MET 365 -0.54 THR 319
GLU 625 1.21 ALA 366 -0.54 ASP 317
TRP 659 1.28 THR 367 -0.57 ASP 317
GLU 625 1.17 LYS 368 -0.78 ASP 317
ASP 432 1.15 PRO 369 -1.09 ASP 317
ASP 432 1.17 LYS 370 -1.19 ASP 317
ASP 432 1.25 GLY 371 -1.63 ASP 317
PRO 425 0.85 ASP 372 -1.41 GLY 371
PRO 425 0.87 LEU 373 -1.07 GLY 371
PRO 425 0.97 LEU 374 -0.72 GLY 371
ASP 427 0.93 PHE 375 -0.53 GLY 371
ASP 427 0.83 ASP 376 -0.81 LYS 322
GLU 426 0.82 ILE 377 -0.67 LYS 322
GLU 426 0.75 SER 378 -0.84 LYS 322
ASP 427 0.77 GLU 379 -1.12 LYS 322
GLU 426 0.75 ARG 380 -0.77 LYS 322
GLU 428 0.81 GLU 381 -0.50 LYS 322
ASP 427 0.89 ALA 382 -0.69 LYS 322
ASP 427 0.88 GLY 383 -0.74 LYS 322
GLU 426 0.87 MET 384 -0.39 LYS 322
ASP 427 0.96 LEU 385 -0.33 GLY 371
PRO 425 1.01 GLN 386 -0.56 GLY 371
ASP 427 0.98 GLN 387 -0.44 GLY 371
ASP 427 0.94 SER 388 -0.23 LYS 351
PRO 425 1.00 ILE 389 -0.23 GLY 371
PRO 425 1.03 GLU 390 -0.39 GLY 371
PRO 425 1.01 ILE 391 -0.32 GLY 371
ASP 427 0.92 ASP 392 -0.20 LYS 351
PRO 425 0.84 SER 393 -0.16 ALA 354
PRO 425 0.85 LYS 394 -0.19 ILE 357
PRO 425 0.84 ARG 395 -0.16 ALA 354
GLU 426 0.66 ALA 396 -0.13 LYS 351
PRO 425 0.54 TRP 397 -0.14 ALA 354
PRO 425 0.58 GLN 398 -0.15 ALA 354
GLU 426 0.51 ARG 399 -0.12 ALA 354
GLU 426 0.29 PHE 400 -0.10 ALA 354
LYS 250 0.31 GLU 401 -0.17 LYS 270
GLN 337 0.27 LEU 402 -0.12 ALA 354
GLN 337 0.26 TYR 403 -0.29 LYS 270
ASP 251 0.39 ARG 404 -0.80 GLN 406
ASP 251 0.46 THR 405 -0.59 LYS 270
ASP 251 0.38 GLN 406 -0.80 ARG 404
ILE 252 0.36 LEU 407 -0.80 LYS 270
ILE 252 0.73 SER 408 -1.05 LYS 270
ILE 252 0.62 GLU 409 -1.01 LYS 270
ILE 252 0.41 ILE 410 -1.04 LYS 270
LEU 437 0.70 GLU 411 -1.30 LYS 270
GLN 337 0.25 GLN 412 -1.46 LYS 270
TYR 255 0.38 GLN 413 -1.41 LYS 270
LEU 437 0.28 LEU 414 -1.49 ALA 418
GLN 337 0.22 GLU 415 -1.77 LYS 270
GLN 337 0.23 GLN 416 -1.81 LYS 270
GLN 337 0.22 ALA 417 -1.80 LYS 270
GLY 371 1.19 ALA 418 -1.84 LEU 433
LYS 270 1.36 ALA 419 -1.58 LEU 433
ARG 423 1.17 ASN 420 -1.67 GLN 416
ALA 422 1.39 ILE 421 -1.67 LEU 433
ILE 421 1.39 ALA 422 -1.40 LEU 433
ALA 267 1.50 ARG 423 -1.27 GLN 416
ALA 267 1.29 ALA 424 -1.35 GLN 416
ALA 267 1.17 PRO 425 -1.17 LEU 433
GLN 429 1.72 GLU 426 -1.20 LEU 433
LEU 430 1.26 ASP 427 -1.21 LEU 433
GLY 371 1.21 GLU 428 -1.24 LEU 433
GLU 426 1.72 GLN 429 -1.40 LEU 433
GLU 426 1.33 LEU 430 -1.59 LEU 433
GLY 371 1.23 MET 431 -1.60 LEU 433
GLY 371 1.25 ASP 432 -1.61 LEU 433
GLN 337 0.22 LEU 433 -1.84 ALA 418
LYS 274 0.32 PHE 434 -1.68 ALA 418
ASN 360 0.24 GLU 435 -1.53 ASP 432
VAL 277 0.49 LYS 436 -1.40 ALA 418
GLU 411 0.70 LEU 437 -1.23 ALA 418
LEU 281 0.29 ARG 438 -1.09 ALA 418
LEU 281 0.33 ASP 439 -0.99 ASP 432
LEU 280 0.32 LEU 440 -0.85 ALA 418
PRO 369 0.35 ASP 441 -0.72 ALA 418
GLY 371 0.39 ARG 442 -0.64 ASP 432
GLY 371 0.40 GLN 443 -0.55 ALA 418
GLY 371 0.42 ARG 444 -0.44 LYS 270
GLY 371 0.46 GLU 445 -0.38 LYS 270
GLY 371 0.49 ALA 446 -0.32 LYS 270
GLY 371 0.51 GLN 447 -0.23 LYS 270
GLY 371 0.52 LEU 448 -0.18 LYS 270
GLY 371 0.55 GLN 449 -0.17 LYS 270
GLY 371 0.57 LYS 450 -0.11 LYS 270
GLY 371 0.57 TYR 451 -0.04 LYS 270
GLY 371 0.59 ARG 452 -0.04 LYS 270
GLY 371 0.60 SER 453 -0.04 LYS 270
LYS 329 0.62 LEU 454 -0.00 ALA 241
LYS 329 0.64 LEU 455 -0.00 ALA 241
LYS 329 0.63 GLU 456 -0.00 ALA 241
LYS 329 0.65 ASP 457 -0.00 ALA 241
LYS 329 0.69 ALA 458 -0.00 SER 237
LYS 329 0.68 LYS 459 -0.00 ALA 233
LYS 329 0.67 ARG 460 -0.00 GLN 216
LYS 329 0.70 LYS 461 -0.00 GLN 216
LYS 329 0.72 LYS 462 -0.00 LEU 227
LYS 329 0.70 GLN 463 -0.00 ALA 233
LYS 329 0.70 GLN 464 -0.00 LEU 466
LYS 329 0.73 GLN 465 -0.00 ALA 233
LYS 329 0.72 LEU 466 -0.00 GLN 464
LYS 329 0.70 ASP 467 -0.00 GLN 464
LYS 329 0.72 CYS 468 -0.01 ARG 470
LYS 329 0.73 VAL 469 -0.00 GLU 221
LYS 329 0.70 ARG 470 -0.01 CYS 468
LYS 329 0.69 GLN 471 -0.01 GLY 105
LYS 329 0.71 ILE 472 -0.04 GLN 473
LYS 329 0.71 GLN 473 -0.04 ILE 472
LYS 329 0.68 LYS 474 -0.03 GLY 105
LYS 329 0.69 ALA 475 -0.04 GLY 105
LYS 329 0.70 HIS 476 -0.06 GLU 494
LYS 329 0.68 ASP 477 -0.04 GLY 106
GLU 330 0.66 ALA 478 -0.04 GLY 106
GLU 330 0.67 ALA 479 -0.05 SER 212
GLU 330 0.67 ARG 480 -0.07 SER 212
GLU 330 0.65 TYR 481 -0.04 GLY 106
GLU 330 0.65 GLN 482 -0.04 GLY 106
GLU 330 0.66 HIS 483 -0.09 ALA 210
GLU 330 0.66 SER 484 -0.12 ALA 210
GLU 330 0.66 TYR 485 -0.10 ALA 210
GLU 330 0.69 SER 486 -0.15 GLN 208
GLU 330 0.69 SER 487 -0.24 GLN 208
GLU 330 0.72 ALA 488 -0.53 SER 207
GLU 330 0.71 PHE 489 -0.14 SER 206
GLU 330 0.70 LYS 490 -0.22 SER 211
LYS 329 0.72 ASN 491 -0.34 GLN 205
LYS 329 0.74 ALA 492 -0.10 GLY 105
LYS 329 0.73 GLN 493 -0.07 GLY 105
LYS 329 0.72 GLU 494 -0.06 HIS 476
LYS 329 0.75 THR 495 -0.09 GLY 105
LYS 329 0.76 ILE 496 -0.08 GLY 106
GLU 219 1.17 ASN 497 -0.05 GLY 106
GLU 219 1.43 LEU 498 -0.05 GLY 106
LYS 329 0.78 LEU 499 -0.06 GLY 106
LYS 329 0.78 ASP 500 -0.03 GLY 106
LYS 329 0.75 ARG 501 -0.02 GLY 106
LYS 329 0.77 TYR 502 -0.02 GLY 106
LYS 329 0.81 SER 503 -0.01 GLY 106
LYS 329 0.79 ASP 504 -0.01 GLY 106
LYS 329 0.77 VAL 505 -0.01 ALA 509
LYS 329 0.81 LEU 506 -0.01 ASN 491
LYS 329 0.84 THR 507 -0.01 ASN 491
LYS 329 0.81 GLN 508 -0.01 THR 513
LYS 329 0.80 ALA 509 -0.01 ASN 491
LYS 329 0.85 ARG 510 -0.01 ASN 491
LYS 329 0.86 VAL 511 -0.01 ASN 491
LYS 329 0.82 LYS 512 -0.01 ASN 491
LYS 329 0.84 THR 513 -0.01 ASN 491
LYS 329 0.89 LEU 514 -0.01 ASN 491
LYS 329 0.87 SER 515 -0.01 SER 487
LYS 329 0.85 THR 516 -0.01 SER 487
LYS 329 0.90 ASN 517 -0.01 SER 487
LYS 329 0.93 PHE 518 -0.01 SER 487
LYS 329 0.88 GLU 519 -0.01 SER 487
LYS 329 0.89 LEU 520 -0.01 SER 487
LYS 329 0.96 ALA 521 -0.01 SER 487
LYS 329 0.95 TYR 522 -0.01 SER 487
LYS 329 0.91 ARG 523 -0.01 SER 487
LYS 329 0.95 LYS 524 -0.01 SER 487
LYS 329 1.00 LEU 525 -0.01 SER 487
THR 367 0.97 ALA 526 -0.01 SER 487
PRO 369 0.98 ARG 527 -0.01 SER 487
PRO 369 0.94 LYS 528 -0.01 SER 487
PRO 369 0.94 GLU 529 -0.00 SER 487
PRO 369 0.95 ASP 530 -0.00 SER 487
PRO 369 0.91 LEU 531 -0.01 SER 487
PRO 369 0.88 GLN 532 -0.00 SER 487
PRO 369 0.88 LEU 533 -0.00 SER 487
LYS 329 0.86 SER 534 -0.00 SER 487
LYS 329 0.89 ALA 535 -0.00 SER 487
LYS 329 0.87 HIS 536 -0.00 ASN 491
LYS 329 0.89 ILE 537 -0.00 ASN 491
LYS 329 0.87 ASN 538 -0.00 LEU 31
LYS 329 0.85 PRO 539 -0.00 LEU 31
LYS 329 0.86 GLN 540 -0.01 THR 578
LYS 329 0.92 THR 541 -0.01 THR 578
LYS 329 0.93 PHE 542 -0.01 LEU 31
LYS 329 0.96 ASP 543 -0.01 ALA 574
LYS 329 0.95 VAL 544 -0.00 LEU 31
LYS 329 0.92 GLU 545 -0.00 GLN 508
LYS 329 0.91 LEU 546 -0.00 ASN 491
PRO 369 0.85 ILE 547 -0.00 ASN 491
PRO 369 0.86 ASP 548 -0.00 SER 487
PRO 369 0.82 GLU 549 -0.00 SER 487
PRO 369 0.81 ASN 550 -0.00 SER 487
PRO 369 0.80 GLY 551 -0.00 ASN 491
PRO 369 0.84 SER 552 -0.00 GLN 508
PRO 369 0.87 VAL 553 -0.00 GLN 508
PRO 369 0.91 ILE 554 -0.00 GLN 508
LYS 329 0.96 ASN 555 -0.00 GLN 508
LYS 329 1.02 ARG 556 -0.00 GLN 508
LYS 329 1.06 LYS 557 -0.00 GLN 508
THR 367 1.03 LEU 558 -0.00 GLN 508
THR 367 1.04 LEU 559 -0.00 ASN 491
THR 367 1.09 SER 560 -0.00 ASN 491
LYS 329 1.16 ALA 561 -0.00 ASN 491
LYS 329 1.13 GLY 562 -0.00 SER 487
LYS 329 1.06 GLU 563 -0.00 SER 487
LYS 329 1.10 LYS 564 -0.00 ASN 491
LYS 329 1.15 GLN 565 -0.00 SER 487
LYS 329 1.08 ILE 566 -0.00 SER 487
LYS 329 1.04 TYR 567 -0.00 SER 487
LYS 329 1.09 ALA 568 -0.01 ILE 569
LYS 329 1.10 ILE 569 -0.01 ALA 568
LYS 329 1.03 ALA 570 -0.01 SER 487
LYS 329 1.02 ILE 571 -0.01 SER 487
LYS 329 1.06 LEU 572 -0.01 GLY 174
LYS 329 1.03 GLU 573 -0.01 ASN 32
LYS 329 0.97 ALA 574 -0.01 ASP 543
LYS 329 0.98 LEU 575 -0.01 SER 487
LYS 329 1.00 ALA 576 -0.01 SER 487
LYS 329 0.95 LYS 577 -0.01 SER 487
LYS 329 0.91 THR 578 -0.01 ASN 491
LYS 329 0.93 SER 579 -0.01 ASN 491
LYS 329 0.91 GLY 580 -0.02 ASN 491
LYS 329 0.96 ARG 581 -0.02 ASN 491
LYS 329 0.99 ASP 582 -0.02 ASN 491
LYS 329 1.05 LEU 583 -0.02 SER 487
LYS 329 1.11 PRO 584 -0.01 SER 487
LYS 329 1.15 VAL 585 -0.01 SER 487
LYS 329 1.23 ILE 586 -0.01 SER 487
LYS 329 1.27 ILE 587 -0.01 SER 487
LYS 329 1.35 ASP 588 -0.00 SER 487
LYS 329 1.37 THR 589 -0.00 SER 487
LYS 329 1.29 PRO 590 -0.00 SER 487
LYS 329 1.28 LEU 591 -0.00 SER 487
LYS 329 1.33 GLY 592 -0.00 SER 487
LYS 329 1.26 ARG 593 -0.00 SER 487
LYS 329 1.19 LEU 594 -0.00 SER 487
THR 367 1.17 ASP 595 -0.00 SER 487
THR 367 1.16 SER 596 -0.00 SER 487
THR 367 1.10 GLN 597 -0.01 SER 487
THR 367 1.09 HIS 598 -0.01 SER 487
LYS 329 1.15 ARG 599 -0.01 SER 487
LYS 329 1.10 ASP 600 -0.01 SER 487
LYS 329 1.06 LYS 601 -0.01 SER 487
LYS 329 1.11 LEU 602 -0.01 SER 487
LYS 329 1.15 ILE 603 -0.01 SER 487
LYS 329 1.08 ASN 604 -0.01 SER 487
LYS 329 1.04 HIS 605 -0.01 SER 487
LYS 329 1.08 TYR 606 -0.01 SER 487
LYS 329 1.14 PHE 607 -0.01 SER 487
LYS 329 1.10 PRO 608 -0.01 SER 487
LYS 329 1.04 GLU 609 -0.01 SER 487
LYS 329 1.07 ALA 610 -0.01 ASP 30
LYS 329 1.07 SER 611 -0.01 SER 487
LYS 329 1.06 HIS 612 -0.02 SER 487
LYS 329 1.13 GLN 613 -0.02 SER 487
LYS 329 1.18 VAL 614 -0.01 SER 487
LYS 329 1.26 VAL 615 -0.01 SER 487
LYS 329 1.30 LEU 616 -0.01 SER 487
LYS 329 1.38 LEU 617 -0.01 SER 487
LYS 329 1.41 SER 618 -0.01 SER 487
LYS 329 1.46 THR 619 -0.00 SER 487
LYS 329 1.45 ASP 620 -0.00 SER 487
GLU 330 1.38 THR 621 -0.00 SER 487
LYS 329 1.34 GLU 622 -0.00 SER 487
LYS 329 1.33 VAL 623 -0.01 SER 487
LYS 329 1.33 ASP 624 -0.01 SER 487
LYS 329 1.32 GLU 625 -0.01 SER 487
LYS 329 1.23 ARG 626 -0.01 SER 487
LYS 329 1.23 TYR 627 -0.01 SER 487
LYS 329 1.30 PHE 628 -0.01 SER 487
LYS 329 1.27 VAL 629 -0.01 SER 487
LYS 329 1.18 ASP 630 -0.01 SER 487
LYS 329 1.16 GLN 631 -0.01 SER 487
LYS 329 1.21 LEU 632 -0.01 SER 487
LYS 329 1.23 ARG 633 -0.01 SER 487
LYS 329 1.17 ASP 634 -0.01 SER 487
LYS 329 1.17 ASP 635 -0.01 SER 487
LYS 329 1.25 ILE 636 -0.01 SER 487
LYS 329 1.25 SER 637 -0.01 SER 487
LYS 329 1.33 HIS 638 -0.01 SER 487
LYS 329 1.40 ALA 639 -0.01 SER 487
LYS 329 1.46 TYR 640 -0.01 SER 487
LYS 329 1.53 GLU 641 -0.01 SER 487
LYS 329 1.54 ILE 642 -0.01 SER 487
GLU 330 1.60 VAL 643 -0.00 SER 487
GLU 330 1.60 PHE 644 -0.00 SER 487
GLN 333 1.62 ASN 645 -0.00 SER 487
GLN 333 1.64 ALA 646 -0.00 SER 487
PHE 334 1.60 HIS 647 -0.00 SER 487
GLN 333 1.52 THR 648 -0.00 SER 487
GLN 333 1.54 LYS 649 -0.00 SER 487
GLN 333 1.50 SER 650 -0.00 SER 487
GLU 330 1.52 SER 651 -0.00 SER 487
GLU 330 1.51 THR 652 -0.01 SER 487
LYS 329 1.49 LEU 653 -0.01 SER 487
LYS 329 1.53 LYS 654 -0.01 SER 487
LYS 329 1.49 PRO 655 -0.01 SER 487
LYS 329 1.50 GLY 656 -0.01 SER 487
LYS 329 1.49 TYR 657 -0.01 SER 487
LYS 329 1.51 PHE 658 -0.01 SER 487
LYS 329 1.46 TRP 659 -0.01 SER 487
LYS 329 1.47 GLU 660 -0.01 SER 487
LYS 329 1.40 LEU 661 -0.01 SER 487
LYS 329 1.38 THR 662 -0.01 SER 487
LYS 329 1.43 LYS 663 -0.01 SER 487
LYS 329 1.34 GLU 664 -0.01 SER 487
LYS 329 1.33 ALA 665 -0.01 SER 487
LYS 329 1.37 ILE 666 -0.02 SER 487

If you find results from this site helpful for your research, please cite one of our papers:

elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.