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CA distance fluctuations for 240415000348227985

---  normal mode 14  ---

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
ASN 288 1.30 VAL 97 -1.15 ARG 213
GLU 285 1.23 PRO 98 -0.37 THR 150
LEU 257 1.75 SER 99 -1.47 GLN 167
GLU 285 1.56 GLN 100 -0.57 ILE 162
GLU 285 1.79 LYS 101 -0.44 SER 166
GLU 285 1.83 THR 102 -0.34 SER 166
GLU 285 1.65 TYR 103 -0.38 LEU 206
LEU 130 1.74 GLN 104 -0.31 LEU 206
LEU 130 1.72 GLY 105 -0.43 LEU 206
LEU 130 1.57 SER 106 -0.47 PRO 151
ALA 129 1.64 TYR 107 -0.38 LEU 206
ALA 129 1.72 GLY 108 -0.28 LEU 206
ASN 131 1.57 PHE 109 -0.21 THR 256
ASN 131 1.78 ARG 110 -0.20 SER 166
ASN 131 1.38 LEU 111 -0.31 CYS 229
PRO 151 1.27 GLY 112 -0.55 ILE 255
PRO 151 1.29 PHE 113 -1.20 PHE 270
PRO 151 1.10 LEU 114 -0.79 PHE 270
PRO 151 0.94 HIS 115 -0.66 GLY 226
PRO 151 0.82 SER 116 -0.73 GLY 226
ALA 276 0.88 SER 121 -0.90 GLY 226
PRO 151 0.72 VAL 122 -0.64 GLY 226
PRO 151 0.68 THR 123 -0.58 GLY 226
PRO 151 0.82 CYS 124 -0.49 GLY 226
PRO 151 1.01 THR 125 -0.41 GLY 226
PRO 151 1.11 TYR 126 -0.30 GLY 226
ARG 110 1.31 SER 127 -0.39 ARG 248
TRP 146 1.87 PRO 128 -0.59 ASN 247
ASP 148 1.81 ALA 129 -0.77 ASN 247
GLN 104 1.74 LEU 130 -0.80 ASN 247
ARG 110 1.78 ASN 131 -0.74 ASN 247
ARG 282 1.06 LYS 132 -0.40 PRO 250
PRO 151 0.90 MET 133 -0.39 LEU 114
PRO 151 0.88 PHE 134 -0.46 LEU 130
PRO 151 0.73 CYS 135 -0.39 GLY 262
PRO 151 0.61 GLN 136 -0.51 GLY 262
PRO 151 0.53 LEU 137 -0.60 GLY 262
PRO 151 0.50 ALA 138 -0.71 GLY 262
PRO 151 0.60 LYS 139 -0.65 GLY 262
PRO 151 0.68 THR 140 -0.68 ARG 158
PRO 151 0.80 CYS 141 -0.69 ARG 158
PRO 151 0.94 PRO 142 -0.80 ILE 255
PRO 151 1.03 VAL 143 -1.08 ILE 255
PRO 151 1.28 GLN 144 -0.79 ILE 255
PRO 128 1.46 LEU 145 -0.62 THR 256
PRO 128 1.87 TRP 146 -0.39 THR 256
ALA 129 1.67 VAL 147 -0.57 LEU 257
ALA 129 1.81 ASP 148 -0.48 ARG 156
ALA 129 1.61 SER 149 -0.64 THR 155
ALA 129 1.31 THR 150 -1.12 GLU 258
PRO 128 1.70 PRO 151 -0.47 SER 106
ALA 129 1.56 PRO 152 -0.28 LEU 206
LEU 289 1.40 PRO 153 -0.58 ASP 186
LEU 289 1.35 GLY 154 -0.74 GLU 204
LEU 289 1.38 THR 155 -1.06 THR 150
SER 99 1.23 ARG 156 -0.86 THR 150
SER 99 1.36 VAL 157 -1.10 ILE 232
SER 99 1.14 ARG 158 -1.00 ILE 232
GLU 285 0.98 ALA 159 -0.89 TYR 234
GLU 285 0.93 MET 160 -0.58 GLY 262
GLU 285 0.85 ALA 161 -0.57 PHE 113
GLU 285 0.84 ILE 162 -0.57 PHE 113
THR 284 0.81 TYR 163 -0.73 SER 99
THR 284 1.01 LYS 164 -0.70 SER 99
THR 284 0.94 GLN 165 -1.07 SER 99
THR 284 0.96 SER 166 -1.46 SER 99
THR 284 0.76 GLN 167 -1.47 SER 99
THR 284 0.71 HIS 168 -1.23 SER 99
THR 284 0.84 MET 169 -1.21 SER 99
ASN 288 0.84 THR 170 -0.86 SER 99
ASN 288 0.64 GLU 171 -0.76 SER 99
ASN 288 0.62 VAL 172 -0.78 VAL 97
GLU 285 0.58 VAL 173 -0.57 GLY 262
GLU 285 0.47 ARG 174 -0.67 GLY 262
GLU 285 0.34 ARG 175 -0.67 GLY 262
SER 121 0.27 CYS 176 -0.59 GLY 262
SER 121 0.25 PRO 177 -0.62 SER 261
SER 121 0.29 HIS 178 -0.61 SER 261
PRO 151 0.30 HIS 179 -0.66 SER 261
ASP 186 0.29 GLU 180 -0.73 SER 261
ASP 186 0.36 ARG 181 -0.72 SER 261
LEU 289 0.38 ASP 186 -1.12 LEU 201
LEU 289 0.43 GLY 187 -0.96 SER 261
LEU 289 0.55 LEU 188 -1.14 SER 261
LEU 289 0.53 ALA 189 -1.07 GLY 262
LEU 289 0.49 PRO 190 -1.02 SER 261
LEU 289 0.39 PRO 191 -0.88 SER 261
GLU 285 0.42 GLN 192 -0.83 GLY 262
GLU 285 0.54 HIS 193 -0.91 GLY 262
GLU 285 0.54 LEU 194 -0.77 GLY 262
GLU 285 0.68 ILE 195 -0.82 GLY 262
GLU 285 0.60 ARG 196 -0.89 GLY 262
GLU 285 0.61 VAL 197 -0.88 GLY 262
PRO 151 0.54 GLU 198 -0.78 GLY 262
PRO 128 0.59 GLY 199 -0.76 PRO 219
PRO 128 0.92 ASN 200 -0.64 ASP 186
GLU 224 1.07 LEU 201 -1.12 ASP 186
LEU 289 0.85 ARG 202 -0.87 SER 261
LEU 289 0.82 VAL 203 -1.05 GLY 262
LEU 289 0.79 GLU 204 -1.55 GLY 262
LEU 289 0.71 TYR 205 -1.47 GLY 262
LEU 289 0.73 LEU 206 -1.38 GLY 262
LEU 289 0.74 ASP 207 -0.92 GLY 262
ARG 158 0.95 ASP 208 -0.74 VAL 97
LEU 289 1.00 ARG 209 -0.56 PRO 191
ASN 288 1.15 ASN 210 -0.48 PRO 177
ASN 288 1.02 THR 211 -0.67 VAL 97
ASN 288 0.79 PHE 212 -0.79 VAL 97
ASN 288 0.74 ARG 213 -1.15 VAL 97
GLU 285 0.69 HIS 214 -0.91 GLY 262
GLU 285 0.79 SER 215 -1.00 GLY 262
GLU 285 0.80 VAL 216 -1.17 GLY 262
LEU 289 0.93 VAL 217 -0.89 GLY 262
SER 99 0.99 VAL 218 -0.73 GLU 198
LEU 289 1.05 PRO 219 -0.76 GLY 199
SER 99 1.18 TYR 220 -0.56 THR 150
LEU 289 1.05 GLU 221 -0.42 SER 121
PRO 128 1.08 PRO 222 -0.40 SER 121
PRO 128 1.03 PRO 223 -0.47 SER 121
LEU 201 1.07 GLU 224 -0.67 SER 121
LEU 201 0.81 VAL 225 -0.81 SER 121
PRO 151 0.78 GLY 226 -0.90 SER 121
PRO 151 0.97 SER 227 -0.66 SER 121
PRO 151 1.20 ASP 228 -0.41 SER 121
PRO 151 1.33 CYS 229 -0.40 ILE 255
PRO 128 1.14 THR 230 -0.48 VAL 157
PRO 151 1.04 THR 231 -0.77 VAL 157
PRO 128 0.86 ILE 232 -1.10 VAL 157
PRO 151 0.73 HIS 233 -0.95 ARG 158
PRO 151 0.64 TYR 234 -0.96 ARG 158
PRO 151 0.55 ASN 235 -0.74 GLY 262
PRO 151 0.51 TYR 236 -0.67 GLY 262
PRO 151 0.43 MET 237 -0.70 GLY 262
PRO 151 0.40 CYS 238 -0.60 GLY 262
PRO 151 0.40 CYS 238 -0.60 GLY 262
PRO 151 0.45 ASN 239 -0.55 LEU 130
PRO 151 0.42 SER 240 -0.61 LEU 130
SER 121 0.51 SER 241 -0.79 LEU 130
SER 121 0.41 CYS 242 -0.63 LEU 130
THR 284 0.35 MET 243 -0.52 LEU 130
THR 284 0.44 GLY 244 -0.62 LEU 130
SER 121 0.41 GLY 245 -0.68 LEU 130
SER 121 0.52 MET 246 -0.78 LEU 130
ARG 280 0.57 ASN 247 -0.80 LEU 130
ARG 280 0.58 ARG 248 -0.79 LEU 130
THR 284 0.68 ARG 249 -0.71 SER 99
THR 284 0.78 PRO 250 -0.53 ASN 131
THR 284 0.78 ILE 251 -0.59 PHE 113
GLU 285 0.98 LEU 252 -0.80 PHE 113
GLU 285 1.01 THR 253 -0.85 PHE 113
GLU 285 1.20 ILE 254 -0.91 VAL 143
GLU 285 1.22 ILE 255 -1.08 VAL 143
SER 99 1.62 THR 256 -0.76 VAL 143
SER 99 1.75 LEU 257 -0.86 THR 150
LEU 289 1.48 GLU 258 -1.12 THR 150
LEU 289 1.57 ASP 259 -1.07 THR 150
LEU 289 1.40 SER 260 -1.17 GLU 204
LEU 289 1.41 SER 261 -1.29 GLU 204
LEU 289 1.44 GLY 262 -1.55 GLU 204
LEU 289 1.72 ASN 263 -1.29 LEU 206
LEU 289 1.75 LEU 264 -1.01 LEU 206
LEU 289 1.64 LEU 265 -0.84 THR 150
LEU 289 1.47 GLY 266 -0.55 THR 150
GLU 285 1.60 ARG 267 -0.44 VAL 143
GLU 285 1.55 ASN 268 -0.50 PHE 113
GLU 285 1.37 SER 269 -0.86 PHE 113
GLU 285 1.14 PHE 270 -1.20 PHE 113
GLU 285 0.98 GLU 271 -0.84 PHE 113
ASP 281 0.74 VAL 272 -0.61 PHE 113
PRO 151 0.63 ARG 273 -0.49 LEU 130
PRO 151 0.58 VAL 274 -0.48 LEU 130
PRO 151 0.60 CYS 275 -0.64 LEU 130
SER 121 0.88 ALA 276 -0.61 LEU 130
PRO 151 0.66 CYS 277 -0.48 LEU 130
PRO 151 0.77 PRO 278 -0.51 LEU 130
PRO 151 0.81 GLY 279 -0.49 GLY 226
PRO 151 0.72 ARG 280 -0.46 GLY 226
GLU 271 0.93 ASP 281 -0.60 LEU 130
LYS 132 1.06 ARG 282 -0.67 LEU 130
THR 102 0.97 ARG 283 -0.37 GLY 226
LYS 101 1.36 THR 284 -0.18 GLY 226
THR 102 1.83 GLU 285 -0.25 GLU 286
THR 102 1.65 GLU 286 -0.25 GLU 285
LYS 101 1.43 GLU 287 -0.18 SER 121
LEU 264 1.42 ASN 288 -0.08 ARG 280
LEU 264 1.75 LEU 289 -0.05 MET 246
ASN 263 1.41 ARG 290 -0.09 SER 121

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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.