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CA distance fluctuations for 24041412150577045

---  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
TYR 103 0.48 SER 96 -1.06 LEU 206
LYS 164 0.48 VAL 97 -0.91 SER 215
GLN 100 0.57 PRO 98 -0.98 SER 215
THR 211 0.47 SER 99 -1.30 ARG 158
GLY 112 0.58 GLN 100 -0.80 SER 166
ASP 208 0.67 LYS 101 -1.02 SER 166
ASP 208 1.12 THR 102 -1.02 ASN 288
ASP 208 1.53 TYR 103 -1.03 ASN 288
ASP 208 1.70 GLN 104 -1.18 ALA 129
ASP 208 1.70 GLY 105 -0.96 ALA 129
ASP 208 1.54 SER 106 -0.88 ALA 129
ASP 208 1.64 TYR 107 -0.90 ALA 129
ASP 208 1.65 GLY 108 -1.11 ALA 129
ASP 208 1.68 PHE 109 -1.05 ALA 129
ASP 208 1.33 ARG 110 -1.19 ASN 131
ASP 208 1.04 LEU 111 -0.90 ASN 131
ASP 208 0.92 GLY 112 -0.71 TRP 146
ASP 208 0.75 PHE 113 -0.54 TRP 146
ASP 208 0.64 LEU 114 -0.38 ASP 228
ASP 208 0.57 HIS 115 -0.46 ASP 148
GLY 226 0.55 SER 116 -0.36 ASP 148
GLY 226 0.46 GLY 117 -0.46 GLY 108
GLY 226 0.44 THR 118 -0.46 ARG 110
GLY 226 0.55 ALA 119 -0.36 GLY 108
GLY 226 0.54 LYS 120 -0.33 ARG 110
GLY 226 0.65 SER 121 -0.27 ARG 110
GLY 226 0.64 VAL 122 -0.30 ARG 110
GLY 226 0.56 THR 123 -0.33 LEU 111
ARG 158 0.53 CYS 124 -0.39 LEU 111
ARG 158 0.43 THR 125 -0.53 ARG 110
ASP 208 0.43 TYR 126 -0.73 ARG 110
ASP 208 0.38 SER 127 -0.97 ARG 110
ASP 208 0.49 PRO 128 -1.09 ARG 110
ASP 208 0.36 ALA 129 -1.18 GLN 104
PRO 98 0.34 LEU 130 -1.09 GLN 104
PRO 98 0.47 ASN 131 -1.19 ARG 110
PRO 98 0.38 LYS 132 -0.80 ARG 110
ASP 208 0.36 MET 133 -0.70 LEU 111
ASP 208 0.36 MET 133 -0.70 LEU 111
ARG 158 0.32 PHE 134 -0.55 ARG 110
ARG 158 0.46 CYS 135 -0.44 LEU 111
ARG 158 0.46 GLN 136 -0.36 PHE 212
SER 261 0.52 LEU 137 -0.48 PHE 212
SER 261 0.55 ALA 138 -0.48 CYS 182
ARG 158 0.54 LYS 139 -0.44 CYS 182
ARG 158 0.61 THR 140 -0.41 CYS 182
ARG 158 0.74 CYS 141 -0.39 LEU 111
ARG 158 0.74 CYS 141 -0.39 LEU 111
ARG 158 0.81 PRO 142 -0.28 LEU 111
ARG 158 0.81 VAL 143 -0.41 LEU 111
ASP 208 0.90 GLN 144 -0.37 ASN 288
ASP 208 1.07 LEU 145 -0.57 ASN 131
ASP 208 1.29 TRP 146 -0.77 ALA 129
ASP 208 1.50 VAL 147 -0.89 ALA 129
ASP 208 1.42 ASP 148 -0.94 ALA 129
ASP 208 1.41 SER 149 -0.80 VAL 225
ASP 208 1.29 THR 150 -0.96 VAL 225
ASP 208 1.33 PRO 151 -0.90 VAL 225
ASP 208 1.14 PRO 152 -0.96 VAL 225
ASP 208 0.97 PRO 153 -0.84 VAL 225
ASP 208 0.87 GLY 154 -0.55 VAL 225
ASP 208 1.07 THR 155 -0.53 SER 99
ASP 208 0.91 ARG 156 -0.74 SER 99
ASP 208 0.93 PHE 157 -0.79 SER 99
HIS 233 0.84 ARG 158 -1.30 SER 99
VAL 143 0.54 ALA 159 -0.81 SER 99
THR 256 0.53 MET 160 -0.56 SER 99
GLY 262 0.44 ALA 161 -0.50 ASN 288
SER 261 0.33 ILE 162 -0.55 ASN 288
MET 246 0.45 TYR 163 -0.66 ASN 288
PRO 98 0.52 LYS 164 -0.81 ASN 288
ASN 247 0.44 GLN 165 -0.82 ASN 288
GLY 244 0.62 SER 166 -1.02 LYS 101
GLY 244 0.94 GLN 167 -0.74 LYS 101
GLY 244 0.87 HIS 168 -0.69 ASN 288
GLY 244 0.51 MET 169 -0.67 LYS 101
SER 261 0.33 THR 170 -0.53 ASN 288
SER 261 0.64 GLU 171 -0.70 ARG 249
ASN 263 0.87 VAL 172 -0.68 ARG 249
GLY 262 0.77 VAL 173 -0.64 ARG 249
GLY 262 0.84 ARG 174 -0.62 PHE 212
SER 261 0.82 ARG 175 -0.79 PHE 212
SER 261 0.79 CYS 176 -0.96 PHE 212
SER 261 0.88 PRO 177 -1.15 PHE 212
SER 261 0.82 HIS 178 -0.97 PHE 212
SER 261 0.83 HIS 179 -0.87 PHE 212
SER 261 0.96 GLU 180 -1.01 PHE 212
SER 261 0.97 ARG 181 -1.01 PHE 212
SER 261 0.85 CYS 182 -0.83 PHE 212
SER 261 0.86 SER 183 -0.76 PHE 212
SER 261 0.75 ASP 184 -0.66 PHE 212
SER 261 0.87 SER 185 -0.63 PHE 212
SER 261 0.78 ASP 186 -0.48 PHE 212
SER 261 0.91 GLY 187 -0.54 ASP 207
SER 261 0.95 LEU 188 -0.59 SER 96
SER 261 0.96 ALA 189 -0.66 ASP 207
SER 261 1.21 PRO 190 -0.75 ASP 207
SER 261 1.09 PRO 191 -0.81 PHE 212
SER 261 1.08 GLN 192 -0.82 PHE 212
GLY 262 0.98 HIS 193 -0.49 PHE 212
GLY 262 0.73 LEU 194 -0.46 PHE 212
GLY 262 0.65 ILE 195 -0.37 SER 99
SER 261 0.64 ARG 196 -0.51 SER 99
SER 261 0.52 VAL 197 -0.55 SER 99
GLY 226 0.52 GLU 198 -0.39 SER 99
GLY 226 0.61 GLY 199 -0.43 SER 99
GLU 224 0.45 ASN 200 -0.58 SER 99
SER 261 0.51 LEU 201 -0.61 SER 99
SER 261 0.51 ARG 202 -0.71 SER 99
SER 261 0.64 VAL 203 -0.76 SER 99
SER 260 0.90 GLU 204 -0.83 SER 99
GLY 262 1.16 TYR 205 -0.83 PRO 98
GLY 262 1.40 LEU 206 -1.06 SER 96
LEU 264 1.42 ASP 207 -0.75 PRO 190
GLN 104 1.70 ASP 208 -0.52 THR 211
SER 106 1.26 ARG 209 -0.62 ARG 181
ASP 148 0.96 ASN 210 -0.40 PRO 177
TYR 103 1.51 THR 211 -0.57 PRO 177
GLY 105 1.36 PHE 212 -1.15 PRO 177
LEU 264 1.16 ARG 213 -0.54 GLN 192
GLY 262 1.07 HIS 214 -0.66 SER 96
GLY 262 0.81 SER 215 -0.98 PRO 98
GLY 262 0.77 VAL 216 -0.82 SER 99
VAL 216 0.56 VAL 217 -1.02 SER 99
ASP 208 0.54 VAL 218 -0.83 SER 99
ASP 208 0.67 PRO 219 -0.73 SER 99
ASP 208 0.91 TYR 220 -0.56 SER 99
ASP 208 0.85 GLU 221 -0.44 SER 99
ASP 208 0.96 PRO 222 -0.46 ALA 129
ASP 208 0.91 PRO 223 -0.36 ALA 129
ASP 208 0.74 GLU 224 -0.58 THR 150
ASP 208 0.64 VAL 225 -0.96 PRO 152
ASP 208 0.67 GLY 226 -0.82 THR 150
ASP 208 0.84 SER 227 -0.45 THR 150
ASP 208 0.98 ASP 228 -0.51 PHE 113
ASP 208 1.01 CYS 229 -0.42 ALA 129
ASP 208 0.94 THR 230 -0.32 ALA 129
ASP 208 0.74 THR 231 -0.29 ASN 200
GLU 224 0.68 ILE 232 -0.37 LEU 111
ARG 158 0.84 HIS 233 -0.30 ASP 184
ARG 158 0.82 TYR 234 -0.39 LEU 111
ARG 158 0.66 ASN 235 -0.31 LEU 111
SER 261 0.55 TYR 236 -0.35 PHE 212
SER 261 0.67 MET 237 -0.54 PHE 212
SER 261 0.63 CYS 238 -0.61 PHE 212
SER 261 0.52 ASN 239 -0.54 PHE 212
GLN 167 0.47 SER 240 -0.48 VAL 173
GLN 167 0.61 SER 241 -0.55 PHE 212
GLN 167 0.68 CYS 242 -0.69 PHE 212
GLN 167 0.89 MET 243 -0.78 PHE 212
GLN 167 0.94 GLY 244 -0.91 PHE 212
HIS 168 0.78 GLY 245 -0.79 PHE 212
HIS 168 0.67 MET 246 -0.54 VAL 172
GLN 167 0.90 ASN 247 -0.62 PHE 212
GLN 167 0.72 ARG 248 -0.50 VAL 172
GLN 167 0.56 ARG 249 -0.70 GLU 171
LEU 130 0.31 PRO 250 -0.56 ASN 288
SER 261 0.30 ILE 251 -0.62 ASN 288
PRO 98 0.43 LEU 252 -0.65 ASN 288
ASP 208 0.46 THR 253 -0.53 ASN 288
ASP 208 0.69 ILE 254 -0.59 ASN 288
ASP 208 0.92 ILE 255 -0.57 ASN 288
ASP 208 1.13 THR 256 -0.62 ASN 288
ASP 208 1.34 LEU 257 -0.64 ASN 288
ASP 208 1.18 GLU 258 -0.60 SER 99
ASP 207 1.08 ASP 259 -0.58 VAL 225
LEU 206 1.09 SER 260 -0.53 SER 99
PRO 190 1.21 SER 261 -0.43 VAL 225
LEU 206 1.40 GLY 262 -0.55 SER 99
ASP 207 1.41 ASN 263 -0.57 ASN 288
ASP 207 1.42 LEU 264 -0.70 ASN 288
ASP 208 1.47 LEU 265 -0.74 ASN 288
ASP 208 1.62 GLY 266 -0.79 ASN 288
ASP 208 1.35 ARG 267 -0.82 ASN 288
ASP 208 1.11 ASN 268 -0.85 ASN 288
PHE 113 0.73 SER 269 -0.74 ASN 288
PHE 113 0.64 PHE 270 -0.68 ASN 288
PRO 98 0.46 GLU 271 -0.69 ASN 288
ARG 158 0.30 VAL 272 -0.51 ASN 288
SER 261 0.27 ARG 273 -0.43 ARG 110
SER 261 0.37 VAL 274 -0.38 LEU 111
SER 261 0.36 CYS 275 -0.41 PHE 212
SER 261 0.38 ALA 276 -0.44 PHE 212
GLY 226 0.42 CYS 277 -0.38 ARG 110
GLY 226 0.42 CYS 277 -0.38 ARG 110
GLY 226 0.39 PRO 278 -0.45 ARG 110
GLY 226 0.41 GLY 279 -0.46 ARG 110
GLY 226 0.36 ARG 280 -0.46 ARG 110
GLY 226 0.28 ASP 281 -0.51 ARG 110
GLY 226 0.23 ARG 282 -0.62 ARG 110
GLY 226 0.24 ARG 283 -0.60 GLN 104
GLY 226 0.18 THR 284 -0.65 GLN 104
GLU 286 0.25 GLU 285 -0.76 GLN 104
GLU 285 0.25 GLU 286 -0.83 GLN 104
ALA 119 0.22 GLU 287 -0.75 GLN 104
LYS 120 0.13 ASN 288 -1.03 TYR 103

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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.