CNRS Nantes University US2B US2B
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CA distance fluctuations for 240322152211123579

---  normal mode 8  ---

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
ASP 156 0.10 GLU 26 -0.18 GLY 196
ASP 156 0.10 MET 27 -0.18 GLY 196
LYS 182 0.10 THR 28 -0.15 GLY 196
LYS 182 0.11 ARG 29 -0.13 GLY 196
LYS 182 0.12 ILE 30 -0.14 GLY 196
LYS 182 0.14 GLY 31 -0.12 GLY 196
LYS 182 0.15 VAL 32 -0.13 GLY 196
LYS 182 0.18 VAL 33 -0.10 GLY 196
LYS 182 0.20 ARG 34 -0.11 ALA 192
LYS 182 0.25 ASN 35 -0.09 LYS 157
LYS 182 0.25 PRO 36 -0.10 PHE 185
LYS 182 0.34 LYS 37 -0.13 LYS 157
LYS 182 0.29 SER 38 -0.14 GLU 310
LYS 182 0.23 HIS 39 -0.23 ALA 192
PHE 244 0.18 GLY 40 -0.29 ALA 192
LYS 182 0.18 ASN 41 -0.21 ALA 192
LYS 182 0.18 ARG 42 -0.22 PHE 185
PHE 244 0.19 ILE 43 -0.32 PHE 185
PHE 244 0.13 ARG 44 -0.28 ALA 192
LYS 182 0.14 PRO 45 -0.21 ALA 192
LYS 182 0.13 PRO 46 -0.21 ALA 192
LYS 182 0.11 GLY 47 -0.19 ALA 192
LYS 182 0.12 PRO 48 -0.15 ALA 192
LYS 182 0.12 ALA 49 -0.15 ALA 192
LYS 182 0.11 PRO 50 -0.16 ALA 192
LYS 182 0.11 GLU 51 -0.13 GLY 196
LYS 182 0.11 ASP 52 -0.14 GLY 196
LYS 182 0.12 VAL 53 -0.14 GLY 196
LYS 182 0.14 ARG 54 -0.10 GLY 196
LYS 182 0.16 LEU 55 -0.10 ALA 192
LYS 182 0.18 VAL 56 -0.06 ALA 192
LYS 182 0.22 GLU 57 -0.05 PHE 185
LYS 182 0.23 PRO 58 -0.05 GLU 57
LYS 182 0.28 ILE 59 -0.07 LYS 157
ARG 179 0.28 GLY 60 -0.08 LYS 157
ARG 179 0.23 ARG 61 -0.08 LYS 37
ARG 179 0.22 GLU 62 -0.06 HIS 97
ARG 179 0.22 ALA 63 -0.04 PRO 323
LYS 182 0.19 LEU 64 -0.05 LYS 37
ARG 179 0.17 LYS 65 -0.06 PRO 323
ARG 179 0.17 ALA 66 -0.05 PRO 323
LYS 182 0.17 ALA 67 -0.04 GLY 255
LYS 182 0.15 LEU 68 -0.06 GLY 255
LYS 182 0.14 ASP 69 -0.07 GLY 255
LYS 182 0.14 ASP 70 -0.06 ARG 253
LYS 182 0.14 PHE 71 -0.08 ARG 253
ASP 156 0.13 ALA 72 -0.10 ARG 253
ASP 156 0.13 ARG 73 -0.09 ARG 253
LYS 182 0.12 THR 74 -0.09 ARG 253
ASP 156 0.13 GLY 75 -0.11 ARG 253
LYS 182 0.12 LEU 76 -0.11 GLY 196
ASP 156 0.11 ASP 77 -0.14 GLY 196
LYS 182 0.11 LEU 78 -0.16 GLY 196
LYS 182 0.13 LEU 79 -0.15 GLY 196
LYS 182 0.14 VAL 80 -0.18 GLY 196
LYS 182 0.16 ILE 81 -0.17 GLY 196
LYS 182 0.17 ASP 82 -0.18 GLY 196
LYS 182 0.21 GLY 83 -0.17 ALA 192
LYS 182 0.22 GLY 84 -0.20 GLY 196
LYS 182 0.20 ASP 85 -0.19 GLY 196
LYS 182 0.21 GLY 86 -0.10 GLY 196
LYS 182 0.21 THR 87 -0.10 GLY 196
LYS 182 0.17 VAL 88 -0.14 GLY 196
LYS 182 0.14 ARG 89 -0.10 GLY 196
LYS 182 0.16 ASP 90 -0.08 SER 38
LYS 182 0.15 VAL 91 -0.08 GLY 196
LYS 182 0.12 ILE 92 -0.10 GLY 196
LYS 182 0.11 SER 93 -0.06 SER 38
TYR 312 0.13 LEU 94 -0.07 PRO 323
ASP 156 0.12 LEU 95 -0.10 GLY 255
ASP 156 0.17 PRO 96 -0.13 PRO 323
LYS 157 0.18 HIS 97 -0.10 GLY 255
ASP 156 0.15 THR 98 -0.09 GLY 255
ASP 156 0.16 PHE 99 -0.12 ARG 253
ASP 156 0.21 GLY 100 -0.13 GLY 255
ASP 156 0.20 GLU 101 -0.15 ARG 253
ASP 156 0.17 ALA 102 -0.15 ARG 253
ASP 156 0.14 THR 103 -0.13 ARG 253
ASP 156 0.12 PRO 104 -0.13 GLY 196
LYS 182 0.11 LEU 105 -0.17 GLY 196
LYS 182 0.12 LEU 106 -0.19 GLY 196
LYS 182 0.12 ALA 107 -0.23 GLY 196
LYS 182 0.13 VAL 108 -0.24 GLY 196
LYS 182 0.13 LEU 109 -0.27 GLY 196
LYS 182 0.13 PRO 110 -0.32 GLY 196
LYS 182 0.16 SER 111 -0.28 ALA 192
LYS 182 0.22 GLY 112 -0.26 ALA 192
PHE 244 0.28 LYS 113 -0.35 ALA 192
LEU 246 0.22 THR 114 -0.41 GLY 196
LYS 182 0.16 ASN 115 -0.35 GLY 196
LYS 182 0.17 VAL 116 -0.36 GLY 196
LYS 182 0.14 LEU 117 -0.29 GLY 196
LYS 182 0.13 ALA 118 -0.34 GLY 196
GLY 184 0.13 ILE 119 -0.40 GLY 196
GLY 184 0.13 ASP 120 -0.34 GLY 196
LYS 182 0.11 LEU 121 -0.32 GLY 196
GLU 254 0.10 GLY 122 -0.39 GLY 196
LYS 182 0.09 THR 123 -0.38 GLY 196
GLU 254 0.08 SER 124 -0.44 GLY 196
PRO 252 0.08 GLU 125 -0.46 GLY 196
LYS 182 0.06 GLY 126 -0.41 GLY 196
LYS 182 0.08 TRP 127 -0.36 GLY 196
LYS 182 0.09 ARG 128 -0.30 GLY 196
LYS 182 0.10 LEU 129 -0.25 GLY 196
LYS 182 0.08 GLU 130 -0.26 GLY 196
LYS 182 0.07 ASP 131 -0.30 GLY 196
LYS 182 0.09 ALA 132 -0.27 GLY 196
LYS 182 0.09 LEU 133 -0.24 GLY 196
LYS 182 0.07 ARG 134 -0.27 GLY 196
LYS 182 0.07 ALA 135 -0.28 GLY 196
LYS 182 0.09 ALA 136 -0.23 GLY 196
ASP 156 0.08 ARG 137 -0.23 GLY 196
ALA 102 0.09 ARG 138 -0.26 GLY 196
ALA 102 0.11 GLU 139 -0.24 GLY 196
PRO 323 0.11 ASN 140 -0.26 GLY 196
PRO 323 0.10 PRO 141 -0.26 GLY 196
PRO 323 0.08 THR 142 -0.29 GLY 196
PRO 323 0.10 ILE 143 -0.25 GLY 196
LYS 182 0.10 LYS 144 -0.25 GLY 196
LEU 321 0.11 SER 145 -0.21 GLY 196
LYS 182 0.10 ARG 146 -0.20 GLY 196
LEU 321 0.13 PRO 147 -0.15 GLY 196
LYS 182 0.10 PRO 148 -0.14 GLY 196
LYS 182 0.08 LEU 149 -0.11 GLY 196
ALA 324 0.09 ARG 150 -0.08 GLY 196
VAL 215 0.07 VAL 151 -0.07 SER 38
GLU 101 0.13 SER 152 -0.08 LYS 37
GLU 101 0.13 TRP 153 -0.10 LYS 37
GLU 101 0.15 ALA 154 -0.09 LYS 37
GLY 100 0.17 ASP 155 -0.11 LYS 37
GLY 100 0.21 ASP 156 -0.11 LYS 37
GLY 100 0.18 LYS 157 -0.13 LYS 37
HIS 97 0.17 PRO 158 -0.10 LYS 37
PRO 96 0.13 CYS 159 -0.09 LYS 37
PRO 96 0.08 LEU 160 -0.09 SER 38
LYS 182 0.08 GLN 161 -0.08 GLY 196
LYS 182 0.11 GLY 162 -0.12 GLY 196
LYS 182 0.12 PHE 163 -0.17 GLY 196
LYS 182 0.13 PHE 164 -0.16 GLY 196
LEU 276 0.10 PHE 165 -0.11 GLY 196
LEU 272 0.13 GLY 166 -0.14 VAL 116
LEU 272 0.12 ILE 167 -0.14 THR 114
GLY 60 0.12 GLY 168 -0.17 PRO 243
LEU 272 0.17 ALA 169 -0.25 PRO 243
LEU 272 0.21 PRO 170 -0.22 THR 114
LEU 272 0.17 VAL 171 -0.22 THR 114
GLY 60 0.18 LYS 172 -0.26 THR 114
LEU 272 0.25 ALA 173 -0.36 THR 114
PRO 273 0.24 THR 174 -0.30 THR 114
GLY 60 0.25 ASN 175 -0.22 LYS 113
GLY 60 0.22 LEU 176 -0.25 THR 114
PRO 273 0.34 ALA 177 -0.34 LYS 113
PRO 273 0.28 GLN 178 -0.14 LYS 113
GLY 60 0.28 ARG 179 -0.21 GLU 210
PRO 273 0.32 VAL 180 -0.15 GLU 210
PRO 273 0.36 HIS 181 -0.12 GLU 210
LYS 37 0.34 LYS 182 -0.17 GLU 210
PRO 273 0.28 VAL 183 -0.20 GLU 210
PRO 273 0.40 GLY 184 -0.11 GLU 210
PRO 273 0.46 PHE 185 -0.32 ILE 43
PRO 273 0.47 PHE 186 -0.26 ILE 43
PRO 273 0.34 HIS 187 -0.13 GLU 210
PRO 273 0.23 ASN 188 -0.19 GLU 125
HIS 269 0.18 PHE 189 -0.35 GLU 125
GLY 60 0.20 ALA 190 -0.29 GLU 125
GLY 60 0.19 VAL 191 -0.28 GLU 125
GLY 196 0.24 ALA 192 -0.43 GLU 125
GLY 60 0.14 LEU 193 -0.42 GLU 125
GLY 60 0.20 THR 194 -0.34 GLU 125
ALA 199 0.19 ILE 195 -0.40 GLU 125
ALA 192 0.24 GLY 196 -0.49 PHE 244
GLY 60 0.14 THR 197 -0.42 PHE 244
GLY 60 0.15 ALA 198 -0.38 PHE 244
PHE 185 0.23 ALA 199 -0.48 PHE 244
PHE 185 0.20 LEU 200 -0.45 PHE 244
GLY 60 0.12 GLY 201 -0.36 PHE 244
PHE 185 0.16 ALA 202 -0.35 PHE 244
PHE 185 0.26 LEU 203 -0.34 PHE 244
PHE 185 0.18 PHE 204 -0.30 PHE 244
GLY 60 0.11 GLY 205 -0.28 PHE 244
GLU 62 0.11 GLY 206 -0.23 PHE 244
GLU 62 0.11 SER 207 -0.20 PHE 244
GLY 302 0.13 ARG 208 -0.20 PHE 244
GLU 62 0.13 ASP 209 -0.24 PHE 244
ALA 303 0.16 GLU 210 -0.23 PRO 243
GLU 62 0.14 TRP 211 -0.26 PRO 243
GLY 60 0.12 ARG 212 -0.23 PRO 243
ALA 303 0.13 GLU 213 -0.19 PRO 243
GLU 62 0.11 GLY 214 -0.18 PRO 243
ALA 303 0.14 VAL 215 -0.15 ARG 179
ARG 208 0.11 PRO 216 -0.14 ARG 179
ARG 208 0.08 ALA 217 -0.10 ARG 179
ARG 208 0.08 ARG 218 -0.08 ARG 179
PHE 186 0.06 LEU 219 -0.05 PRO 243
GLY 255 0.06 VAL 220 -0.06 PRO 282
PHE 186 0.08 LEU 221 -0.07 PRO 282
GLY 255 0.09 ASP 222 -0.08 PRO 282
ASN 140 0.08 GLY 223 -0.07 PRO 282
GLY 255 0.08 GLU 224 -0.08 PRO 282
PHE 186 0.06 ALA 225 -0.06 PRO 282
PHE 186 0.08 GLN 226 -0.05 PRO 282
PHE 186 0.08 GLY 227 -0.05 PRO 243
ARG 208 0.07 GLU 228 -0.08 ARG 179
ARG 208 0.09 GLY 229 -0.10 PRO 243
GLU 62 0.08 HIS 230 -0.12 PRO 243
GLY 60 0.08 ARG 231 -0.14 PRO 243
GLY 60 0.11 PHE 232 -0.18 PRO 243
PHE 186 0.13 ALA 233 -0.17 PRO 243
PHE 186 0.12 VAL 234 -0.11 PRO 243
PHE 186 0.14 ILE 235 -0.12 ALA 199
PHE 186 0.13 ALA 236 -0.12 ALA 199
GLY 184 0.14 THR 237 -0.16 ALA 199
GLY 184 0.12 ALA 238 -0.17 GLY 196
GLY 184 0.15 LEU 239 -0.23 GLY 196
GLY 184 0.16 LYS 240 -0.24 GLY 196
GLY 184 0.19 ARG 241 -0.30 GLY 196
GLY 184 0.22 LEU 242 -0.36 ALA 199
GLY 184 0.26 PRO 243 -0.47 GLY 196
GLY 184 0.32 PHE 244 -0.49 GLY 196
PHE 186 0.29 GLY 245 -0.37 GLY 196
PHE 186 0.35 LEU 246 -0.33 LEU 200
PHE 186 0.30 LYS 247 -0.24 LEU 200
PHE 186 0.29 PRO 248 -0.21 LEU 200
PHE 186 0.24 PHE 249 -0.16 LEU 200
PHE 186 0.26 GLY 250 -0.16 LEU 200
PHE 186 0.25 ALA 251 -0.17 LEU 200
PHE 186 0.21 PRO 252 -0.20 LEU 200
PHE 186 0.17 ARG 253 -0.20 GLU 254
GLY 184 0.14 GLU 254 -0.20 ARG 253
ARG 295 0.14 GLY 255 -0.17 PRO 323
PHE 186 0.12 LEU 256 -0.12 GLY 196
PHE 186 0.15 LYS 257 -0.13 ALA 199
PHE 186 0.15 LEU 258 -0.11 ALA 199
PHE 186 0.18 LEU 259 -0.11 LEU 200
PHE 186 0.15 ASP 260 -0.09 PRO 243
PHE 186 0.16 VAL 261 -0.12 PRO 243
PHE 186 0.13 ASP 262 -0.12 PRO 243
PHE 186 0.10 ALA 263 -0.15 PRO 243
PHE 185 0.10 PRO 264 -0.17 PRO 243
PHE 185 0.17 PRO 265 -0.17 PHE 244
PHE 186 0.21 ARG 266 -0.13 PHE 244
PHE 186 0.27 ARG 267 -0.13 PHE 244
PHE 185 0.29 LEU 268 -0.18 PHE 244
PHE 185 0.37 HIS 269 -0.21 PHE 244
PHE 186 0.38 LYS 270 -0.13 ASN 140
PHE 186 0.35 ALA 271 -0.12 ASN 140
PHE 185 0.40 LEU 272 -0.17 LEU 246
PHE 186 0.47 PRO 273 -0.16 ASN 140
PHE 186 0.40 LEU 274 -0.15 ASN 140
PHE 186 0.35 MET 275 -0.13 LEU 200
PHE 186 0.40 LEU 276 -0.22 LEU 200
PHE 186 0.41 SER 277 -0.18 ASN 140
PHE 186 0.34 GLY 278 -0.16 ASN 140
PHE 186 0.34 LYS 279 -0.16 ASN 140
PHE 186 0.29 VAL 280 -0.13 ASN 140
PHE 186 0.30 VAL 281 -0.12 ASN 140
PHE 186 0.26 PRO 282 -0.09 ASN 140
PHE 186 0.26 ALA 283 -0.09 ASN 140
PHE 186 0.26 LEU 284 -0.09 ASN 140
PHE 186 0.22 GLU 285 -0.06 ASN 140
PHE 186 0.20 GLY 286 -0.06 ASN 140
PHE 186 0.21 LEU 287 -0.08 THR 142
PHE 186 0.18 GLY 288 -0.07 PRO 243
PHE 186 0.22 TYR 289 -0.08 THR 142
PHE 186 0.19 ARG 290 -0.07 LEU 200
PHE 186 0.20 ARG 291 -0.09 LEU 200
PHE 186 0.16 ARG 292 -0.09 VAL 280
PHE 186 0.14 ASP 293 -0.10 VAL 280
GLY 255 0.12 PRO 294 -0.09 VAL 280
GLY 255 0.14 ARG 295 -0.08 VAL 280
SER 145 0.09 SER 296 -0.07 VAL 280
PHE 186 0.07 VAL 297 -0.05 GLY 196
ALA 324 0.07 LYS 298 -0.05 LYS 113
VAL 215 0.08 LEU 299 -0.07 LYS 113
ARG 208 0.09 SER 300 -0.09 LYS 113
ARG 208 0.12 GLY 301 -0.12 ARG 179
GLY 315 0.16 GLY 302 -0.13 LYS 182
GLU 210 0.16 ALA 303 -0.14 LYS 113
GLU 210 0.13 PRO 304 -0.16 LYS 113
LEU 272 0.13 PHE 305 -0.15 LYS 113
ARG 61 0.15 VAL 306 -0.16 THR 114
ARG 61 0.13 LEU 307 -0.13 LYS 113
LEU 276 0.14 ASP 308 -0.15 ASN 115
PRO 273 0.18 GLY 309 -0.24 LYS 113
ARG 61 0.21 GLU 310 -0.25 LYS 113
ARG 61 0.20 VAL 311 -0.21 LYS 113
GLU 62 0.16 TYR 312 -0.18 LYS 113
GLU 62 0.15 GLU 313 -0.16 LYS 113
GLU 210 0.14 GLY 314 -0.14 LYS 113
GLY 302 0.16 GLY 315 -0.12 LYS 113
VAL 215 0.11 ASP 316 -0.10 LYS 113
GLU 101 0.10 LEU 317 -0.08 LYS 113
GLY 322 0.09 THR 318 -0.06 SER 38
ALA 324 0.07 ILE 319 -0.06 GLY 196
SER 145 0.08 GLN 320 -0.08 GLY 196
PRO 147 0.13 LEU 321 -0.10 GLY 196
SER 152 0.10 GLY 322 -0.13 GLY 255
ALA 324 0.12 PRO 323 -0.17 GLY 255
PRO 323 0.12 ALA 324 -0.18 ARG 253
ARG 326 0.13 LEU 325 -0.16 GLY 196
LEU 325 0.13 ARG 326 -0.19 GLY 196
LYS 182 0.11 PHE 327 -0.23 GLY 196
LYS 182 0.10 LEU 328 -0.25 GLY 196
LYS 182 0.09 VAL 329 -0.30 GLY 196
LYS 182 0.07 GLY 330 -0.34 GLY 196

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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).
Last modification: April 25th, 2023.