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 2404250734012549507

---  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
SER 166 0.73 SER 96 -1.08 ASN 263
THR 211 1.21 VAL 97 -1.07 ASN 288
THR 211 1.34 PRO 98 -1.19 ASN 288
ASN 210 1.35 SER 99 -1.33 ASN 288
ASN 210 1.06 GLN 100 -1.58 ASN 288
ASN 210 1.01 LYS 101 -1.43 ASN 288
ASN 210 0.78 THR 102 -1.48 LEU 289
ASN 210 0.66 TYR 103 -1.29 LEU 289
PRO 152 0.60 GLN 104 -1.18 LEU 289
PRO 152 0.52 GLY 105 -1.03 LEU 289
PRO 152 0.46 SER 106 -0.90 LEU 206
PRO 152 0.46 SER 106 -0.90 LEU 206
PRO 152 0.81 TYR 107 -0.98 LEU 206
PRO 152 0.65 GLY 108 -0.94 LEU 289
PRO 152 0.89 PHE 109 -1.20 LEU 289
PRO 151 0.70 ARG 110 -1.23 LEU 289
PRO 151 0.86 LEU 111 -1.26 LEU 289
PRO 151 0.98 GLY 112 -1.24 VAL 157
PRO 151 0.95 PHE 113 -1.07 ARG 158
PRO 151 0.94 LEU 114 -1.01 VAL 218
PRO 151 0.84 HIS 115 -0.85 ASP 186
PRO 151 0.85 SER 116 -0.92 GLY 262
PRO 151 0.69 VAL 122 -1.01 GLY 262
PRO 151 0.69 THR 123 -1.11 GLY 262
PRO 151 0.71 CYS 124 -1.06 GLY 262
PRO 151 0.71 THR 125 -0.92 GLY 262
PRO 151 0.72 TYR 126 -0.87 SER 185
PRO 151 0.52 SER 127 -0.98 SER 227
ASN 210 0.40 PRO 128 -1.39 CYS 229
ARG 248 0.55 ALA 129 -1.61 ASP 228
ARG 248 0.82 LEU 130 -1.28 ASP 228
ASN 210 0.49 ASN 131 -1.14 CYS 229
PRO 151 0.52 LYS 132 -1.47 GLU 286
PRO 151 0.59 MET 133 -1.10 GLU 285
LEU 130 0.67 PHE 134 -1.13 GLY 262
PRO 151 0.57 CYS 135 -1.24 GLY 262
PRO 151 0.54 GLN 136 -1.35 GLY 262
PRO 151 0.47 LEU 137 -1.56 GLY 262
VAL 225 0.52 ALA 138 -1.50 GLY 262
PRO 151 0.63 LYS 139 -1.29 GLY 262
PRO 151 0.63 LYS 139 -1.29 GLY 262
PRO 151 0.74 THR 140 -1.13 ASP 186
PRO 151 0.74 CYS 141 -1.21 ASP 186
PRO 151 0.92 PRO 142 -1.13 VAL 218
PRO 151 0.96 VAL 143 -1.48 ARG 158
PRO 151 1.31 GLN 144 -1.60 ARG 158
PRO 151 1.16 LEU 145 -1.60 VAL 157
PRO 151 1.25 TRP 146 -1.25 VAL 157
PRO 152 0.65 VAL 147 -1.27 TYR 220
PRO 152 0.44 ASP 148 -1.31 TYR 220
PRO 152 0.53 SER 149 -0.97 TYR 220
CYS 229 0.74 THR 150 -1.03 LEU 206
GLN 144 1.31 PRO 151 -0.61 LEU 206
CYS 229 1.14 PRO 152 -0.81 LEU 206
CYS 229 1.18 PRO 152 -0.81 LEU 206
ASP 228 1.01 PRO 153 -1.03 LEU 206
ASP 228 1.10 PRO 153 -1.07 GLU 204
ASP 228 0.73 GLY 154 -1.50 TYR 205
ASP 228 0.75 GLY 154 -1.47 TYR 205
PRO 222 0.74 THR 155 -1.31 GLU 204
ASN 210 0.62 ARG 156 -1.43 LEU 145
ARG 209 0.88 VAL 157 -1.60 LEU 145
ARG 209 1.09 ARG 158 -1.60 GLN 144
ASP 208 0.90 ALA 159 -1.15 LEU 289
ASP 208 0.88 MET 160 -1.10 LEU 289
THR 211 0.68 ALA 161 -1.12 SER 185
THR 211 0.86 ILE 162 -1.25 ASN 288
THR 211 0.71 TYR 163 -1.22 ASN 288
THR 211 0.78 LYS 164 -1.42 ASN 288
THR 211 0.68 GLN 165 -1.23 ASN 288
THR 211 0.76 SER 166 -1.20 ASN 288
THR 211 0.60 GLN 167 -1.01 ASN 288
THR 211 0.58 HIS 168 -1.03 ASN 288
THR 211 0.91 MET 169 -1.22 ASN 288
THR 211 0.97 THR 170 -1.06 ASN 288
ARG 213 0.49 GLU 171 -1.11 ASN 263
ARG 213 0.50 GLU 171 -1.11 ASN 263
GLU 224 0.33 VAL 172 -1.31 ASN 263
GLU 224 0.35 VAL 173 -1.34 ASN 263
GLU 224 0.41 ARG 174 -1.53 ASN 263
VAL 225 0.46 ARG 175 -1.56 GLY 262
VAL 225 0.43 CYS 176 -1.51 GLY 262
VAL 225 0.50 PRO 177 -1.53 SER 261
VAL 225 0.51 HIS 178 -1.73 SER 261
VAL 225 0.54 HIS 179 -1.68 SER 261
VAL 225 0.61 GLU 180 -1.61 ASN 263
VAL 225 0.66 ARG 181 -1.70 SER 261
VAL 225 0.65 CYS 182 -1.80 SER 261
VAL 225 0.79 SER 185 -1.61 GLY 262
VAL 225 0.96 ASP 186 -1.72 ASN 235
VAL 225 1.03 GLY 187 -1.44 GLY 262
VAL 225 1.02 LEU 188 -1.50 SER 260
VAL 225 0.86 ALA 189 -1.85 SER 260
VAL 225 0.76 PRO 190 -1.81 SER 260
VAL 225 0.74 PRO 191 -1.66 ASN 263
VAL 225 0.61 GLN 192 -1.94 ASN 263
VAL 225 0.61 GLN 192 -1.94 ASN 263
GLU 224 0.59 HIS 193 -1.57 ASN 263
GLU 221 0.51 LEU 194 -1.52 GLY 262
GLU 221 0.60 ILE 195 -1.49 SER 185
GLU 221 0.77 ARG 196 -1.35 ASP 186
GLU 221 0.90 VAL 197 -1.13 ASP 186
GLU 221 1.01 GLU 198 -1.03 GLY 262
GLU 221 1.17 GLY 199 -0.80 GLY 262
GLU 221 1.41 ASN 200 -0.63 GLY 262
GLU 221 1.82 LEU 201 -0.65 SER 260
GLU 221 1.14 ARG 202 -0.72 GLY 154
GLU 221 1.07 VAL 203 -0.93 GLY 154
GLU 224 0.65 GLU 204 -1.42 GLY 154
GLU 224 0.63 TYR 205 -1.50 GLY 154
VAL 225 0.46 LEU 206 -1.56 ASP 259
THR 170 0.48 ASP 207 -1.69 ASP 259
ARG 158 0.97 ASP 208 -1.26 ASN 263
ARG 158 1.09 ARG 209 -1.17 PRO 191
SER 99 1.35 ASN 210 -1.00 ARG 181
PRO 98 1.34 THR 211 -1.27 ASN 263
THR 170 0.91 PHE 212 -1.77 ASN 263
THR 170 0.56 ARG 213 -1.43 LEU 264
GLU 224 0.45 HIS 214 -1.38 LEU 264
ASP 208 0.70 SER 215 -1.17 LEU 264
GLU 221 0.62 VAL 216 -1.04 SER 260
ASP 208 0.84 VAL 217 -1.33 ILE 232
ASP 208 0.71 VAL 218 -1.58 ILE 232
ARG 209 0.63 PRO 219 -1.37 THR 231
ASN 200 1.13 TYR 220 -1.31 ASP 148
LEU 201 1.81 GLU 221 -1.23 ASP 148
LEU 201 1.82 GLU 221 -1.23 ASP 148
ASN 200 1.10 PRO 222 -0.86 LEU 289
GLY 199 0.94 PRO 223 -1.02 PRO 128
LEU 201 1.54 GLU 224 -0.73 ALA 129
LEU 201 1.06 VAL 225 -0.73 ALA 129
PRO 153 0.76 GLY 226 -1.23 ALA 129
PRO 151 0.89 SER 227 -1.48 ALA 129
PRO 153 1.10 ASP 228 -1.61 ALA 129
PRO 151 1.27 CYS 229 -1.39 PRO 128
PRO 151 1.03 THR 230 -1.06 PRO 219
PRO 151 1.11 THR 231 -1.53 VAL 218
PRO 151 0.82 ILE 232 -1.58 VAL 218
PRO 151 0.77 HIS 233 -1.06 VAL 218
PRO 151 0.59 TYR 234 -1.38 ASP 186
GLU 221 0.57 ASN 235 -1.72 ASP 186
GLU 221 0.48 TYR 236 -1.64 ASP 186
GLU 221 0.52 MET 237 -1.79 GLY 262
LEU 130 0.50 CYS 238 -1.87 GLY 262
LEU 130 0.50 CYS 238 -1.87 GLY 262
LEU 130 0.62 ASN 239 -1.64 GLY 262
LEU 130 0.76 SER 240 -1.46 GLY 262
LEU 130 0.80 SER 241 -1.42 GLY 262
LEU 130 0.61 CYS 242 -1.52 GLY 262
LEU 130 0.56 MET 243 -1.37 GLY 262
LEU 130 0.41 GLY 244 -1.31 GLY 262
LEU 130 0.39 GLY 245 -1.39 GLY 262
LEU 130 0.48 MET 246 -1.34 GLY 262
LEU 130 0.62 ASN 247 -1.31 GLY 262
LEU 130 0.82 ARG 248 -1.23 GLY 262
LEU 130 0.62 ARG 249 -1.09 GLY 262
LEU 130 0.58 PRO 250 -1.09 THR 284
THR 211 0.57 ILE 251 -1.17 ASN 288
THR 211 0.71 LEU 252 -1.34 ASN 288
ASN 210 0.63 THR 253 -1.23 LEU 289
ASN 210 0.80 ILE 254 -1.39 LEU 289
ASN 210 0.89 ILE 255 -1.41 LEU 289
ASN 210 0.92 THR 256 -1.30 LEU 289
ASN 210 0.61 LEU 257 -1.17 LEU 289
ASN 210 0.51 GLU 258 -1.21 LEU 206
ASP 228 0.49 ASP 259 -1.69 ASP 207
PRO 222 0.36 SER 260 -1.85 ALA 189
SER 106 0.27 SER 261 -1.80 CYS 182
SER 106 0.14 GLY 262 -1.87 CYS 238
SER 106 0.40 ASN 263 -1.94 GLN 192
GLY 105 0.37 LEU 264 -1.43 ARG 213
THR 230 0.63 LEU 265 -1.12 LEU 206
THR 230 0.61 GLY 266 -1.20 LEU 289
ASN 210 0.66 ARG 267 -1.39 LEU 289
ASN 210 0.71 ASN 268 -1.68 LEU 289
ASN 210 0.70 ASN 268 -1.67 LEU 289
ASN 210 0.73 SER 269 -1.70 LEU 289
ASN 210 0.63 PHE 270 -1.40 GLU 285
ASN 210 0.60 GLU 271 -1.83 GLU 285
ASN 210 0.59 GLU 271 -1.83 GLU 285
PRO 151 0.46 VAL 272 -1.38 GLU 285
LEU 130 0.79 ARG 273 -1.22 GLY 262
LEU 130 0.67 VAL 274 -1.43 GLY 262
LEU 130 0.74 CYS 275 -1.37 GLY 262
LEU 130 0.61 ALA 276 -1.29 GLY 262
LEU 130 0.54 CYS 277 -1.16 GLY 262
LEU 130 0.61 PRO 278 -1.12 GLY 262
PRO 151 0.62 GLY 279 -0.97 GLY 262
PRO 151 0.53 ARG 280 -1.01 GLY 262
LEU 130 0.64 ASP 281 -1.10 GLY 262
LEU 130 0.68 ARG 282 -0.98 GLY 262
PRO 151 0.49 ARG 283 -0.90 GLY 262
ARG 280 0.27 THR 284 -1.09 PRO 250
GLU 286 0.19 GLU 285 -1.83 GLU 271
GLU 285 0.19 GLU 286 -1.47 LYS 132
ARG 280 0.21 GLU 287 -1.14 GLU 271
ARG 280 0.11 ASN 288 -1.58 GLN 100
THR 284 0.05 LEU 289 -1.70 SER 269

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.