CNRS Nantes University US2B US2B
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CA distance fluctuations for 2404131447413989959

---  normal mode 13  ---

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
THR 284 1.00 SER 96 -0.74 GLN 167
THR 284 1.11 VAL 97 -0.87 PHE 212
THR 284 0.95 PRO 98 -0.89 ARG 158
ASN 288 1.04 SER 99 -0.83 ARG 158
ASN 288 0.87 GLN 100 -0.83 SER 166
ASN 288 0.83 LYS 101 -0.96 SER 166
ASN 288 0.57 THR 102 -0.80 SER 166
LEU 206 0.56 TYR 103 -0.73 ASN 210
LEU 206 0.54 GLN 104 -0.74 ASN 210
LEU 206 0.75 GLY 105 -0.83 ASN 210
LEU 206 0.77 SER 106 -0.84 ASN 210
LEU 206 0.69 TYR 107 -0.82 ASN 210
LEU 206 0.57 GLY 108 -0.77 GLU 287
LEU 206 0.53 PHE 109 -0.73 ASN 210
ARG 158 0.42 ARG 110 -0.80 SER 127
ARG 158 0.57 LEU 111 -0.66 SER 127
ARG 158 0.67 GLY 112 -0.73 TRP 146
ARG 158 0.85 PHE 113 -0.88 TRP 146
ARG 158 0.68 LEU 114 -1.00 ASP 228
GLN 167 0.64 SER 121 -1.11 SER 227
GLN 167 0.55 VAL 122 -1.17 SER 227
SER 261 0.46 THR 123 -0.87 SER 227
GLY 226 0.49 CYS 124 -0.81 SER 227
ARG 158 0.47 THR 125 -0.88 ASP 228
ARG 158 0.57 TYR 126 -0.71 TRP 146
VAL 122 0.39 SER 127 -0.80 ARG 110
LEU 114 0.65 PRO 128 -0.72 GLY 108
LEU 114 0.57 ALA 129 -0.94 ARG 248
ARG 158 0.43 LEU 130 -1.12 ARG 248
PHE 113 0.63 ASN 131 -0.83 PRO 250
ARG 158 0.54 LYS 132 -0.63 CYS 238
ARG 158 0.64 MET 133 -0.56 LEU 111
ARG 158 0.67 PHE 134 -0.58 GLU 286
SER 261 0.65 CYS 135 -0.56 SER 227
SER 261 0.75 GLN 136 -0.67 GLU 285
SER 261 0.89 LEU 137 -0.81 LEU 289
SER 261 0.87 ALA 138 -0.69 LEU 289
GLY 226 0.89 LYS 139 -0.72 ASP 186
GLY 226 0.99 THR 140 -0.59 VAL 122
GLY 226 0.87 CYS 141 -0.54 THR 123
ARG 158 0.87 PRO 142 -0.71 VAL 122
ARG 158 0.94 VAL 143 -0.62 CYS 124
ARG 158 0.62 GLN 144 -0.60 ASP 208
ARG 158 0.63 LEU 145 -0.69 ASN 210
ARG 158 0.55 TRP 146 -0.88 PHE 113
LEU 206 0.53 VAL 147 -0.79 GLU 287
LEU 206 0.49 ASP 148 -0.90 GLU 287
LEU 206 0.56 SER 149 -0.78 GLU 287
GLU 204 0.54 THR 150 -0.82 ASN 210
LEU 206 0.70 PRO 151 -0.89 ASN 210
GLU 204 0.85 PRO 152 -0.95 ASN 210
GLU 204 0.94 PRO 153 -0.96 ASN 210
GLU 204 1.29 GLY 154 -1.06 ASN 210
GLU 204 1.18 THR 155 -1.00 ASN 210
GLU 204 0.99 ARG 156 -1.19 ARG 209
GLY 226 0.57 VAL 157 -1.10 ASP 208
VAL 143 0.94 ARG 158 -1.45 ASP 208
ARG 273 0.71 ALA 159 -1.08 ASP 208
GLY 262 0.83 MET 160 -0.73 ASP 208
ARG 273 0.87 ALA 161 -0.44 ILE 162
ASP 281 0.97 ILE 162 -0.44 ALA 161
ASP 281 1.24 TYR 163 -0.54 LEU 289
ASP 281 1.28 LYS 164 -0.63 THR 102
ASP 281 1.66 GLN 165 -0.73 THR 102
THR 284 1.72 SER 166 -0.96 LYS 101
THR 284 1.68 GLN 167 -0.75 LYS 101
THR 284 1.42 HIS 168 -0.61 LEU 289
THR 284 1.35 MET 169 -0.62 GLN 100
THR 284 1.27 THR 170 -0.44 ARG 158
THR 284 1.20 GLU 171 -0.49 LEU 289
GLY 262 0.98 VAL 172 -0.52 LEU 289
ARG 273 1.03 VAL 173 -0.63 LEU 289
GLY 262 1.41 ARG 174 -0.86 LEU 289
SER 261 1.47 ARG 175 -1.12 LEU 289
SER 261 1.55 CYS 176 -1.35 LEU 289
SER 261 1.80 PRO 177 -1.30 LEU 289
SER 261 1.63 HIS 178 -1.37 LEU 289
SER 261 1.56 HIS 179 -1.25 LEU 289
SER 261 1.74 GLU 180 -1.09 LEU 289
SER 261 1.61 ARG 181 -1.11 LEU 289
SER 261 1.48 CYS 182 -1.17 LEU 289
SER 261 1.23 SER 185 -0.76 LEU 289
SER 260 1.16 ASP 186 -0.72 LYS 139
SER 260 1.28 GLY 187 -0.66 LEU 289
SER 260 1.41 LEU 188 -0.64 LYS 139
SER 260 1.42 ALA 189 -0.59 LEU 289
SER 260 1.72 PRO 190 -0.67 LEU 289
SER 261 1.54 PRO 191 -0.84 LEU 289
GLY 262 1.68 GLN 192 -0.84 LEU 289
GLY 262 1.57 HIS 193 -0.70 LEU 289
GLY 262 1.25 LEU 194 -0.78 LEU 289
GLY 262 1.07 ILE 195 -0.57 LEU 289
GLY 262 0.96 ARG 196 -0.53 LEU 252
GLY 226 0.83 VAL 197 -0.65 ASP 208
GLY 226 1.02 GLU 198 -0.55 ASP 208
GLY 226 1.07 GLY 199 -0.64 VAL 122
GLY 226 0.80 ASN 200 -0.71 ASP 208
ASP 186 0.81 LEU 201 -0.72 ASP 208
ASP 186 0.97 ARG 202 -0.83 ASP 208
SER 260 0.90 VAL 203 -0.85 ASP 208
GLY 154 1.29 GLU 204 -0.75 ASP 208
SER 260 1.51 TYR 205 -0.52 LEU 206
ASN 263 1.56 LEU 206 -0.52 TYR 205
ASN 263 1.73 ASP 207 -0.36 LEU 289
SER 261 0.83 ASP 208 -1.45 ARG 158
PRO 177 1.02 ARG 209 -1.19 ARG 156
PRO 177 0.73 ASN 210 -1.63 GLY 262
THR 284 0.94 THR 211 -1.55 PHE 212
GLY 245 1.28 PHE 212 -1.55 THR 211
GLY 262 1.16 ARG 213 -0.38 LEU 289
GLY 262 1.41 HIS 214 -0.43 LEU 289
GLY 262 1.24 SER 215 -0.56 ASP 208
GLY 262 1.07 VAL 216 -0.85 ASP 208
ARG 156 0.95 VAL 217 -1.42 ASP 208
GLY 226 0.70 VAL 218 -1.15 ASP 208
ASP 186 0.68 PRO 219 -1.02 ARG 209
PRO 219 0.53 TYR 220 -0.89 ARG 209
PRO 219 0.43 GLU 221 -0.79 ASN 210
ASP 148 0.38 PRO 222 -0.78 ASN 210
ARG 158 0.39 PRO 223 -0.84 VAL 122
PRO 219 0.39 GLU 224 -1.00 SER 121
ARG 158 0.34 VAL 225 -1.00 SER 121
ILE 232 1.11 GLY 226 -0.68 SER 149
ASP 228 0.48 SER 227 -1.17 VAL 122
SER 227 0.48 ASP 228 -1.00 LEU 114
ARG 158 0.52 CYS 229 -0.85 LEU 114
ARG 158 0.56 THR 230 -0.72 VAL 122
GLY 226 0.85 THR 231 -0.72 VAL 122
GLY 226 1.11 ILE 232 -0.80 ASP 208
GLY 226 1.08 HIS 233 -0.60 VAL 122
ARG 158 0.93 TYR 234 -0.52 ASP 208
GLY 226 0.86 ASN 235 -0.53 LEU 289
SER 261 0.92 TYR 236 -0.74 LEU 289
SER 261 1.14 MET 237 -0.95 LEU 289
SER 261 1.19 CYS 238 -1.17 LEU 289
SER 261 1.09 ASN 239 -1.24 LEU 289
SER 261 1.05 SER 240 -1.30 LEU 289
SER 261 1.05 SER 241 -1.55 LEU 289
SER 261 1.23 CYS 242 -1.67 LEU 289
SER 261 1.32 GLY 245 -1.38 LEU 289
PHE 212 1.09 MET 246 -1.28 LEU 289
SER 261 1.10 ASN 247 -1.62 LEU 289
CYS 277 0.93 ARG 248 -1.38 LEU 289
ASP 281 1.11 ARG 249 -1.11 LEU 289
ASP 281 1.35 PRO 250 -0.83 ASN 131
ASP 281 1.06 ILE 251 -0.65 CYS 238
ASP 281 0.77 LEU 252 -0.64 MET 237
ASP 281 0.62 THR 253 -0.63 ILE 232
ASN 288 0.56 ILE 254 -0.64 ASP 208
ASN 288 0.46 ILE 255 -0.81 ASP 208
SER 215 0.60 THR 256 -0.89 ARG 209
LEU 206 0.79 LEU 257 -0.91 ARG 209
LEU 206 1.28 GLU 258 -1.08 ARG 209
LEU 206 1.49 ASP 259 -1.20 ASN 210
PRO 190 1.72 SER 260 -1.41 ASN 210
PRO 177 1.80 SER 261 -0.89 ASN 210
GLN 192 1.68 GLY 262 -1.63 ASN 210
ASP 207 1.73 ASN 263 -1.33 ASN 210
LEU 206 1.51 LEU 264 -1.05 ASN 210
LEU 206 1.14 LEU 265 -0.96 ASN 210
LEU 206 0.82 GLY 266 -0.83 ASN 210
LEU 206 0.53 ARG 267 -0.72 ASN 210
ASN 288 0.46 ASN 268 -0.62 ARG 209
ASN 288 0.53 SER 269 -0.61 LYS 164
ARG 158 0.50 PHE 270 -0.66 PRO 250
ARG 282 0.69 GLU 271 -0.70 CYS 238
PHE 134 0.63 VAL 272 -0.75 CYS 238
VAL 173 1.03 ARG 273 -1.06 LEU 130
SER 261 0.93 VAL 274 -0.92 LEU 289
SER 261 0.90 CYS 275 -0.97 GLU 285
SER 261 0.80 ALA 276 -1.04 GLU 285
PRO 250 1.07 CYS 277 -0.75 GLU 285
PRO 250 1.02 PRO 278 -0.75 SER 227
GLN 165 0.98 GLY 279 -0.96 SER 227
GLN 167 1.33 ARG 280 -0.85 SER 227
GLN 165 1.66 ASP 281 -0.66 GLU 285
GLN 165 1.23 ARG 282 -0.74 SER 227
GLN 167 1.17 ARG 283 -0.92 SER 227
SER 166 1.72 THR 284 -0.54 SER 227
SER 166 1.10 GLU 285 -1.04 ALA 276
GLN 165 0.52 GLU 286 -0.82 ARG 273
GLN 167 0.82 GLU 287 -0.90 ASP 148
SER 99 1.04 ASN 288 -0.76 CYS 182
GLY 226 0.29 LEU 289 -1.67 CYS 242

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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.