CNRS Nantes University US2B US2B
home |  start a new run |  job status |  references&downloads |  examples |  help  

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


***    ***

CA distance fluctuations for 240322152211123579

---  normal mode 10  ---

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
ARG 295 0.20 GLU 26 -0.11 LYS 182
PHE 189 0.20 MET 27 -0.10 LYS 182
PHE 189 0.18 THR 28 -0.11 LYS 182
PHE 189 0.18 ARG 29 -0.09 ASN 175
PHE 189 0.20 ILE 30 -0.11 ASN 175
PHE 186 0.21 GLY 31 -0.13 GLU 310
PHE 186 0.24 VAL 32 -0.17 GLU 310
PHE 186 0.29 VAL 33 -0.21 GLU 310
PHE 186 0.31 ARG 34 -0.28 GLU 310
PHE 186 0.38 ASN 35 -0.38 GLU 310
PHE 186 0.36 PRO 36 -0.38 GLU 310
PHE 186 0.47 LYS 37 -0.49 GLU 310
PHE 186 0.44 SER 38 -0.48 GLU 310
PHE 186 0.47 HIS 39 -0.61 LYS 182
PHE 189 0.35 GLY 40 -0.54 LYS 182
PHE 186 0.31 ASN 41 -0.49 LYS 182
PHE 186 0.35 ARG 42 -0.64 LYS 182
PHE 189 0.28 ILE 43 -0.72 LYS 182
PHE 189 0.25 ARG 44 -0.58 LYS 182
PHE 189 0.21 PRO 45 -0.48 LYS 182
PHE 189 0.21 PRO 46 -0.40 LYS 182
PHE 189 0.17 GLY 47 -0.36 LYS 182
PHE 189 0.16 PRO 48 -0.30 LYS 182
PHE 189 0.17 ALA 49 -0.25 LYS 182
PHE 189 0.15 PRO 50 -0.24 LYS 182
PHE 189 0.13 GLU 51 -0.20 LYS 182
PHE 189 0.16 ASP 52 -0.16 LYS 182
PHE 189 0.18 VAL 53 -0.16 LYS 182
PHE 186 0.20 ARG 54 -0.15 GLU 310
PHE 186 0.23 LEU 55 -0.19 GLU 310
PHE 186 0.27 VAL 56 -0.22 TYR 312
PHE 186 0.31 GLU 57 -0.28 TYR 312
PHE 186 0.35 PRO 58 -0.29 TYR 312
PHE 186 0.41 ILE 59 -0.37 TYR 312
PHE 186 0.45 GLY 60 -0.35 GLU 313
PHE 185 0.42 ARG 61 -0.33 LYS 157
PHE 186 0.38 GLU 62 -0.33 LYS 157
PHE 186 0.37 ALA 63 -0.26 LYS 157
PHE 186 0.36 LEU 64 -0.23 LYS 157
PHE 186 0.33 LYS 65 -0.22 LYS 157
PHE 186 0.32 ALA 66 -0.20 LYS 157
PHE 186 0.30 ALA 67 -0.16 LYS 157
PHE 186 0.29 LEU 68 -0.12 LYS 157
PHE 186 0.28 ASP 69 -0.10 LYS 157
PHE 186 0.26 ASP 70 -0.11 LYS 157
PHE 186 0.24 PHE 71 -0.08 TYR 312
PHE 186 0.24 ALA 72 -0.03 TYR 312
PHE 186 0.23 ARG 73 -0.04 GLU 313
PHE 186 0.21 THR 74 -0.05 TYR 312
PHE 186 0.20 GLY 75 -0.03 ASN 175
PHE 189 0.20 LEU 76 -0.05 ASN 175
PHE 189 0.21 ASP 77 -0.05 ASN 175
PHE 189 0.23 LEU 78 -0.07 ASN 175
PHE 189 0.24 LEU 79 -0.10 GLU 310
PHE 189 0.26 VAL 80 -0.14 GLU 310
PHE 189 0.29 ILE 81 -0.18 GLU 310
PHE 189 0.29 ASP 82 -0.25 GLU 310
PHE 186 0.36 GLY 83 -0.33 GLU 310
PHE 185 0.41 GLY 84 -0.35 GLU 310
PHE 185 0.43 ASP 85 -0.23 GLU 310
PHE 185 0.48 GLY 86 -0.34 GLU 310
PHE 185 0.43 THR 87 -0.25 GLU 310
PHE 185 0.38 VAL 88 -0.14 ILE 81
PHE 185 0.37 ARG 89 -0.15 ASN 35
PHE 185 0.39 ASP 90 -0.16 GLU 57
PHE 185 0.35 VAL 91 -0.10 VAL 33
PHE 185 0.32 ILE 92 -0.05 PRO 147
PHE 185 0.32 SER 93 -0.09 GLU 57
PHE 185 0.32 LEU 94 -0.09 VAL 151
PHE 185 0.29 LEU 95 -0.05 LEU 325
PHE 185 0.27 PRO 96 -0.10 PRO 323
PHE 185 0.29 HIS 97 -0.08 PRO 323
PHE 185 0.28 THR 98 -0.04 SER 145
PHE 185 0.25 PHE 99 -0.05 SER 145
PHE 185 0.24 GLY 100 -0.07 LEU 325
ALA 192 0.22 GLU 101 -0.10 LEU 325
ALA 192 0.22 ALA 102 -0.06 SER 145
ALA 192 0.24 THR 103 -0.05 SER 145
PHE 189 0.24 PRO 104 -0.04 VAL 88
PHE 189 0.25 LEU 105 -0.06 VAL 88
PHE 189 0.27 LEU 106 -0.09 VAL 88
PHE 189 0.29 ALA 107 -0.12 GLU 310
PHE 189 0.32 VAL 108 -0.16 GLU 310
PHE 189 0.32 LEU 109 -0.23 GLN 178
PHE 189 0.38 PRO 110 -0.29 GLN 178
PHE 189 0.36 SER 111 -0.36 GLN 178
PHE 189 0.41 GLY 112 -0.39 GLN 178
PHE 189 0.52 LYS 113 -0.44 GLN 178
ALA 192 0.54 THR 114 -0.34 THR 174
PHE 189 0.45 ASN 115 -0.25 GLY 309
ALA 192 0.49 VAL 116 -0.12 THR 174
ALA 192 0.41 LEU 117 -0.09 GLY 309
PHE 189 0.40 ALA 118 -0.14 GLN 178
PHE 189 0.44 ILE 119 -0.13 GLN 178
ALA 192 0.41 ASP 120 -0.07 GLN 178
PHE 189 0.37 LEU 121 -0.08 LYS 182
PHE 189 0.37 GLY 122 -0.14 LYS 182
PHE 189 0.36 THR 123 -0.19 LYS 182
PHE 189 0.36 SER 124 -0.27 LYS 182
PHE 189 0.37 GLU 125 -0.35 LYS 182
PHE 189 0.31 GLY 126 -0.37 LYS 182
PHE 189 0.30 TRP 127 -0.30 LYS 182
PHE 189 0.26 ARG 128 -0.32 LYS 182
PHE 189 0.23 LEU 129 -0.28 LYS 182
PHE 189 0.20 GLU 130 -0.29 LYS 182
PHE 189 0.23 ASP 131 -0.27 LYS 182
PHE 189 0.24 ALA 132 -0.22 LYS 182
PHE 189 0.21 LEU 133 -0.21 LYS 182
PHE 189 0.20 ARG 134 -0.22 LYS 182
PHE 189 0.22 ALA 135 -0.19 LYS 182
PHE 189 0.22 ALA 136 -0.15 LYS 182
PHE 189 0.19 ARG 137 -0.16 LYS 182
GLU 254 0.21 ARG 138 -0.17 LYS 182
ARG 295 0.25 GLU 139 -0.13 LYS 182
ARG 295 0.27 ASN 140 -0.12 LYS 182
GLU 254 0.25 PRO 141 -0.13 LYS 182
GLU 254 0.27 THR 142 -0.12 LYS 182
GLU 254 0.28 ILE 143 -0.08 LYS 182
PHE 189 0.29 LYS 144 -0.08 GLU 101
ALA 192 0.29 SER 145 -0.10 GLU 101
ALA 192 0.31 ARG 146 -0.11 ALA 324
ALA 192 0.30 PRO 147 -0.09 PRO 323
ALA 192 0.31 PRO 148 -0.08 GLY 86
ALA 192 0.30 LEU 149 -0.11 LYS 37
ALA 192 0.25 ARG 150 -0.13 LYS 37
ALA 192 0.23 VAL 151 -0.19 LYS 37
HIS 181 0.19 SER 152 -0.22 ARG 61
HIS 181 0.18 TRP 153 -0.26 ARG 61
GLU 101 0.16 ALA 154 -0.23 GLY 60
HIS 181 0.18 ASP 155 -0.26 GLY 60
HIS 181 0.21 ASP 156 -0.27 GLU 62
HIS 181 0.24 LYS 157 -0.33 ARG 61
HIS 181 0.30 PRO 158 -0.25 GLU 62
HIS 181 0.27 CYS 159 -0.18 ARG 61
PHE 185 0.28 LEU 160 -0.19 ILE 59
ALA 192 0.29 GLN 161 -0.13 LYS 37
ALA 192 0.34 GLY 162 -0.16 GLY 86
ALA 192 0.37 PHE 163 -0.12 GLY 86
ALA 192 0.38 PHE 164 -0.16 LYS 37
ALA 192 0.31 PHE 165 -0.22 LYS 37
ALA 192 0.27 GLY 166 -0.26 LYS 37
GLY 196 0.18 ILE 167 -0.29 LYS 37
GLY 196 0.14 GLY 168 -0.29 LYS 37
GLY 196 0.22 ALA 169 -0.27 LYS 37
GLY 196 0.30 PRO 170 -0.29 LYS 37
ALA 192 0.19 VAL 171 -0.37 LYS 37
GLY 196 0.13 LYS 172 -0.35 LYS 37
ILE 195 0.32 ALA 173 -0.31 HIS 39
ALA 192 0.31 THR 174 -0.42 HIS 39
PRO 158 0.13 ASN 175 -0.47 HIS 39
THR 174 0.17 LEU 176 -0.34 HIS 39
GLY 309 0.36 ALA 177 -0.33 HIS 39
GLU 310 0.22 GLN 178 -0.61 HIS 39
PRO 158 0.15 ARG 179 -0.50 HIS 39
GLY 309 0.31 VAL 180 -0.29 ILE 43
GLY 60 0.41 HIS 181 -0.44 ILE 43
ARG 61 0.28 LYS 182 -0.72 ILE 43
ARG 61 0.23 VAL 183 -0.48 ILE 43
GLY 60 0.44 GLY 184 -0.25 ILE 43
LYS 113 0.49 PHE 185 -0.32 GLY 196
LYS 37 0.47 PHE 186 -0.31 GLY 196
GLY 60 0.33 HIS 187 -0.24 GLY 196
PHE 244 0.40 ASN 188 -0.17 ALA 192
PHE 244 0.63 PHE 189 -0.24 ARG 208
PHE 244 0.49 ALA 190 -0.26 GLU 210
PHE 244 0.42 VAL 191 -0.22 GLU 210
PHE 244 0.65 ALA 192 -0.22 HIS 187
PHE 244 0.61 LEU 193 -0.32 ASP 209
PHE 244 0.40 THR 194 -0.36 GLU 210
PHE 244 0.43 ILE 195 -0.23 ASP 209
PHE 244 0.53 GLY 196 -0.32 PHE 185
PHE 244 0.36 THR 197 -0.35 ASP 209
PHE 244 0.22 ALA 198 -0.24 ASP 209
LEU 276 0.26 ALA 199 -0.32 PHE 185
LEU 276 0.21 LEU 200 -0.29 PHE 185
PHE 244 0.12 GLY 201 -0.22 PHE 185
ALA 199 0.10 ALA 202 -0.21 PHE 185
GLY 196 0.14 LEU 203 -0.23 PHE 185
PHE 244 0.07 PHE 204 -0.23 PHE 185
PHE 244 0.07 GLY 205 -0.25 THR 197
HIS 269 0.07 GLY 206 -0.27 THR 197
SER 145 0.06 SER 207 -0.22 THR 197
PHE 244 0.05 ARG 208 -0.31 LEU 193
PHE 244 0.06 ASP 209 -0.35 THR 197
GLY 205 0.06 GLU 210 -0.36 THR 194
ALA 199 0.06 TRP 211 -0.25 LYS 37
ALA 199 0.06 ARG 212 -0.23 LYS 37
SER 145 0.06 GLU 213 -0.24 LYS 37
ALA 199 0.07 GLY 214 -0.26 LYS 37
ALA 199 0.07 VAL 215 -0.28 LYS 37
SER 145 0.08 PRO 216 -0.26 LYS 37
ASN 140 0.10 ALA 217 -0.24 LYS 37
ASN 140 0.12 ARG 218 -0.21 LYS 37
ASN 140 0.15 LEU 219 -0.19 LYS 37
ASN 140 0.18 VAL 220 -0.16 LYS 37
ASN 140 0.21 LEU 221 -0.13 LYS 37
ASN 140 0.24 ASP 222 -0.11 LYS 37
ASN 140 0.22 GLY 223 -0.13 ILE 59
ASN 140 0.22 GLU 224 -0.13 LYS 37
ASN 140 0.18 ALA 225 -0.15 LYS 37
ASN 140 0.17 GLN 226 -0.16 LYS 37
ASN 140 0.15 GLY 227 -0.17 LYS 37
ASN 140 0.13 GLU 228 -0.19 LYS 37
ASN 140 0.10 GLY 229 -0.21 LYS 37
ASN 140 0.08 HIS 230 -0.23 LYS 37
ALA 199 0.10 ARG 231 -0.23 LYS 37
ALA 199 0.14 PHE 232 -0.23 LYS 37
GLY 196 0.21 ALA 233 -0.23 LYS 37
GLY 196 0.21 VAL 234 -0.21 LYS 37
GLY 196 0.28 ILE 235 -0.19 LYS 37
ALA 192 0.29 ALA 236 -0.16 LYS 37
ALA 192 0.34 THR 237 -0.11 LYS 37
ALA 192 0.34 ALA 238 -0.08 GLY 86
ALA 192 0.39 LEU 239 -0.06 LYS 240
ALA 192 0.38 LYS 240 -0.08 PRO 323
ALA 192 0.43 ARG 241 -0.07 PHE 244
ALA 192 0.50 LEU 242 -0.04 PRO 323
ALA 192 0.58 PRO 243 -0.07 GLN 178
ALA 192 0.65 PHE 244 -0.09 GLY 122
ALA 192 0.54 GLY 245 -0.11 PRO 252
ALA 192 0.51 LEU 246 -0.04 PRO 252
ALA 192 0.42 LYS 247 -0.03 GLN 178
GLY 196 0.39 PRO 248 -0.08 LYS 37
ALA 192 0.33 PHE 249 -0.07 LYS 37
ALA 192 0.33 GLY 250 -0.05 ASP 293
ALA 192 0.33 ALA 251 -0.06 GLY 245
ALA 192 0.35 PRO 252 -0.11 GLY 245
ALA 192 0.32 ARG 253 -0.08 GLY 322
ALA 192 0.30 GLU 254 -0.10 GLY 322
ALA 192 0.29 GLY 255 -0.09 GLY 322
ALA 192 0.28 LEU 256 -0.08 GLN 320
ALA 192 0.29 LYS 257 -0.09 LYS 37
ALA 192 0.25 LEU 258 -0.13 LYS 37
GLY 196 0.27 LEU 259 -0.14 LYS 37
GLY 196 0.20 ASP 260 -0.17 LYS 37
GLY 196 0.18 VAL 261 -0.18 LYS 37
GLY 196 0.11 ASP 262 -0.19 LYS 37
ASN 140 0.08 ALA 263 -0.21 LYS 37
ASN 140 0.07 PRO 264 -0.20 LYS 37
GLY 196 0.10 PRO 265 -0.18 LYS 37
ASN 140 0.08 ARG 266 -0.16 LYS 37
GLY 196 0.09 ARG 267 -0.16 PHE 185
GLY 196 0.17 LEU 268 -0.16 LYS 37
GLY 196 0.21 HIS 269 -0.19 PHE 185
GLY 196 0.21 LYS 270 -0.15 HIS 181
GLY 196 0.25 ALA 271 -0.12 LYS 37
GLY 196 0.37 LEU 272 -0.13 HIS 181
GLY 196 0.41 PRO 273 -0.12 HIS 181
GLY 196 0.33 LEU 274 -0.09 HIS 181
GLY 196 0.35 MET 275 -0.09 LYS 37
GLY 196 0.45 LEU 276 -0.07 LYS 37
LEU 193 0.41 SER 277 -0.06 HIS 181
GLY 196 0.35 GLY 278 -0.04 ARG 292
LEU 193 0.31 LYS 279 -0.05 ARG 292
GLY 196 0.25 VAL 280 -0.06 ARG 292
GLY 196 0.22 VAL 281 -0.06 LYS 37
ASN 140 0.18 PRO 282 -0.07 LYS 37
GLY 196 0.15 ALA 283 -0.09 LYS 37
GLY 196 0.19 LEU 284 -0.10 LYS 37
GLY 196 0.16 GLU 285 -0.11 LYS 37
ASN 140 0.15 GLY 286 -0.12 LYS 37
ASN 140 0.12 LEU 287 -0.13 LYS 37
GLY 196 0.13 GLY 288 -0.15 LYS 37
GLY 196 0.20 TYR 289 -0.14 LYS 37
GLY 196 0.20 ARG 290 -0.13 LYS 37
GLY 196 0.24 ARG 291 -0.10 LYS 37
ALA 192 0.21 ARG 292 -0.10 LYS 37
ASN 140 0.24 ASP 293 -0.08 LYS 37
ASN 140 0.25 PRO 294 -0.10 LYS 37
SER 145 0.27 ARG 295 -0.08 GLU 62
ASN 140 0.22 SER 296 -0.12 LYS 37
ALA 192 0.18 VAL 297 -0.15 LYS 37
ASN 140 0.15 LYS 298 -0.18 LYS 37
ASN 140 0.12 LEU 299 -0.22 LYS 37
ASN 140 0.11 SER 300 -0.24 LYS 37
ALA 324 0.08 GLY 301 -0.27 LYS 37
HIS 181 0.10 GLY 302 -0.30 LYS 37
HIS 181 0.09 ALA 303 -0.32 LYS 37
HIS 181 0.14 PRO 304 -0.36 LYS 37
ALA 192 0.19 PHE 305 -0.34 LYS 37
ALA 192 0.27 VAL 306 -0.35 LYS 37
ALA 192 0.32 LEU 307 -0.30 GLY 86
ALA 192 0.41 ASP 308 -0.25 GLY 86
ALA 192 0.43 GLY 309 -0.37 SER 38
HIS 181 0.35 GLU 310 -0.49 LYS 37
HIS 181 0.26 VAL 311 -0.47 LYS 37
HIS 181 0.27 TYR 312 -0.42 LYS 37
HIS 181 0.22 GLU 313 -0.38 LYS 37
HIS 181 0.16 GLY 314 -0.33 LYS 37
HIS 181 0.14 GLY 315 -0.29 ILE 59
HIS 181 0.12 ASP 316 -0.25 ILE 59
ALA 192 0.14 LEU 317 -0.23 ILE 59
ALA 192 0.17 THR 318 -0.18 ILE 59
ALA 192 0.21 ILE 319 -0.16 LYS 37
ALA 192 0.23 GLN 320 -0.12 LYS 37
ALA 192 0.26 LEU 321 -0.08 LYS 37
ALA 192 0.26 GLY 322 -0.10 GLU 254
ALA 192 0.25 PRO 323 -0.10 PRO 96
ALA 192 0.27 ALA 324 -0.11 ARG 146
ALA 192 0.28 LEU 325 -0.10 GLU 101
ALA 192 0.27 ARG 326 -0.07 GLU 101
PHE 189 0.29 PHE 327 -0.08 VAL 88
PHE 189 0.28 LEU 328 -0.11 LYS 182
PHE 189 0.29 VAL 329 -0.15 LYS 182
PHE 189 0.28 GLY 330 -0.20 LYS 182

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: April 25th, 2023.