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CA distance fluctuations for 240414224652190601

---  normal mode 9  ---

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
LYS 164 0.48 VAL 97 -0.76 SER 215
THR 211 0.61 PRO 98 -0.71 ARG 158
ASP 208 0.67 SER 99 -0.72 ARG 158
ASP 208 0.82 GLN 100 -0.90 SER 166
ASP 208 1.00 LYS 101 -1.11 SER 166
ASP 208 1.31 THR 102 -0.91 SER 166
ASP 208 1.63 TYR 103 -0.75 SER 166
ASP 208 1.79 GLN 104 -0.65 SER 166
ASP 208 1.79 GLY 105 -0.60 SER 166
ASP 208 1.55 SER 106 -0.51 SER 166
ASP 208 1.55 SER 106 -0.51 SER 166
ASP 208 1.55 TYR 107 -0.49 ALA 129
ASP 208 1.60 GLY 108 -0.64 ALA 129
ASP 208 1.60 PHE 109 -0.59 ASN 131
ASP 208 1.38 ARG 110 -0.76 ASN 131
ASP 208 1.38 ARG 110 -0.77 ASN 131
ASP 208 1.12 LEU 111 -0.51 ASN 131
ASP 208 1.01 GLY 112 -0.41 TRP 146
ASP 208 0.83 PHE 113 -0.32 TRP 146
ASP 208 0.72 LEU 114 -0.25 THR 150
GLY 226 0.93 VAL 122 -0.25 ARG 110
GLY 226 0.93 THR 123 -0.26 LEU 111
VAL 225 0.79 CYS 124 -0.31 LEU 111
VAL 225 0.79 CYS 124 -0.31 LEU 111
GLY 226 0.65 THR 125 -0.37 ARG 110
ASP 208 0.54 TYR 126 -0.50 ARG 110
ASP 208 0.53 SER 127 -0.58 ARG 110
ASP 208 0.65 PRO 128 -0.68 ARG 110
ASP 208 0.57 ALA 129 -0.64 GLY 108
ASP 208 0.52 LEU 130 -0.62 ARG 110
ASP 208 0.63 ASN 131 -0.77 ARG 110
ASP 208 0.51 LYS 132 -0.60 ARG 110
GLY 226 0.55 MET 133 -0.49 LEU 111
GLY 226 0.55 MET 133 -0.49 LEU 111
GLY 226 0.70 PHE 134 -0.38 ARG 110
GLY 226 0.81 CYS 135 -0.32 LEU 111
GLY 226 0.81 CYS 135 -0.32 LEU 111
GLY 226 0.96 GLN 136 -0.30 PHE 212
GLY 226 0.98 LEU 137 -0.41 PHE 212
GLY 226 0.99 ALA 138 -0.42 PHE 212
VAL 225 1.00 LYS 139 -0.29 PHE 212
VAL 225 1.03 THR 140 -0.25 LEU 111
VAL 225 0.79 CYS 141 -0.33 LEU 111
VAL 225 0.79 CYS 141 -0.33 LEU 111
SER 227 0.75 PRO 142 -0.22 LEU 111
ASP 208 0.80 VAL 143 -0.36 LEU 111
ASP 208 0.97 GLN 144 -0.26 THR 150
ASP 208 1.11 LEU 145 -0.33 SER 166
ASP 208 1.22 TRP 146 -0.45 ASN 131
ASP 208 1.37 VAL 147 -0.58 ASP 228
ASP 208 1.35 ASP 148 -0.63 ASP 228
ASP 208 1.31 SER 149 -0.64 ASP 228
ASP 208 1.31 SER 149 -0.64 ASP 228
ASP 208 1.18 THR 150 -0.77 ASP 228
ASP 208 1.23 PRO 151 -0.59 VAL 225
ASP 208 1.12 PRO 152 -0.84 VAL 225
ASP 208 0.95 PRO 153 -0.82 VAL 225
ASP 207 0.87 GLY 154 -0.51 VAL 225
ASP 208 1.03 THR 155 -0.53 PRO 222
ASP 208 0.91 ARG 156 -0.37 SER 99
ASP 208 0.92 VAL 157 -0.43 SER 99
THR 231 0.93 ARG 158 -0.72 SER 99
THR 231 0.68 ALA 159 -0.52 SER 99
GLY 262 0.52 MET 160 -0.79 MET 160
GLY 262 0.52 MET 160 -0.79 MET 160
GLY 262 0.48 ALA 161 -0.35 ILE 162
GLY 226 0.41 ILE 162 -0.35 ALA 161
GLY 226 0.45 TYR 163 -0.39 THR 102
VAL 97 0.48 LYS 164 -0.52 THR 102
GLY 226 0.37 GLN 165 -0.64 THR 102
ASN 247 0.50 SER 166 -1.11 LYS 101
ASN 247 0.50 SER 166 -1.11 LYS 101
ASN 247 0.78 GLN 167 -0.78 LYS 101
ASN 247 0.78 GLN 167 -0.78 LYS 101
ASN 247 0.63 HIS 168 -0.58 LYS 101
ASN 247 0.35 MET 169 -0.68 GLN 100
SER 261 0.38 THR 170 -0.37 LYS 101
SER 261 0.62 GLU 171 -0.34 SER 249
GLY 262 0.80 VAL 172 -0.32 SER 249
SER 261 0.71 VAL 173 -0.33 SER 249
SER 261 0.84 ARG 174 -0.50 PHE 212
GLY 226 0.76 ARG 175 -0.76 PHE 212
GLY 226 0.76 ARG 175 -0.76 PHE 212
GLY 226 0.81 CYS 176 -0.86 PHE 212
GLY 226 0.83 PRO 177 -1.09 PHE 212
GLY 226 0.94 HIS 178 -0.96 PHE 212
GLY 226 0.94 HIS 179 -0.89 PHE 212
GLY 226 0.85 GLU 180 -1.10 PHE 212
GLY 226 0.91 ARG 181 -1.17 PHE 212
SER 261 0.76 LEU 188 -0.51 ASP 207
SER 261 0.82 ALA 189 -0.61 ASP 207
SER 261 1.12 PRO 190 -0.58 ASP 207
SER 261 0.91 PRO 191 -0.87 PHE 212
SER 261 0.92 GLN 192 -0.90 PHE 212
SER 261 0.88 HIS 193 -0.51 PHE 212
GLY 226 0.71 LEU 194 -0.43 PHE 212
GLY 226 0.66 ILE 195 -0.34 ARG 196
GLY 226 0.70 ARG 196 -0.42 THR 253
VAL 225 0.77 VAL 197 -0.37 THR 253
VAL 225 1.02 GLU 198 -0.38 LEU 188
GLU 224 1.20 GLY 199 -0.39 LEU 188
GLU 224 1.11 ASN 200 -0.32 VAL 97
GLU 224 0.86 LEU 201 -0.34 VAL 97
GLU 224 0.77 ARG 202 -0.40 PRO 98
GLU 224 0.75 VAL 203 -0.45 PRO 98
SER 261 0.76 GLU 204 -0.51 PRO 98
SER 261 0.99 TYR 205 -0.47 VAL 97
GLY 262 1.28 LEU 206 -0.57 VAL 97
GLY 262 1.66 ASP 207 -0.70 GLN 192
GLN 104 1.79 ASP 208 -0.59 ARG 181
SER 106 1.16 ARG 209 -0.64 ARG 181
ASP 148 0.93 ASN 210 -0.44 ARG 181
LEU 264 1.16 THR 211 -0.49 GLN 192
LEU 264 1.45 PHE 212 -1.17 ARG 181
GLY 262 1.08 ARG 213 -0.30 VAL 97
GLY 262 1.10 HIS 214 -0.47 VAL 97
GLY 262 0.74 SER 215 -0.76 VAL 97
GLY 262 0.63 VAL 216 -0.51 VAL 97
GLU 224 0.71 VAL 217 -0.58 PRO 98
GLU 224 0.76 VAL 218 -0.45 SER 99
ASP 208 0.70 PRO 219 -0.38 SER 99
ASP 208 0.92 TYR 220 -0.38 SER 166
ASP 208 0.87 GLU 221 -0.31 SER 166
ASP 208 0.88 PRO 222 -0.57 PRO 153
ASP 208 0.88 PRO 222 -0.57 PRO 153
ASP 208 0.86 PRO 223 -0.53 PRO 153
GLY 199 1.20 GLU 224 -0.91 SER 227
GLY 199 1.12 VAL 225 -0.84 PRO 152
ALA 276 1.05 GLY 226 -0.46 PRO 152
ASP 208 0.83 SER 227 -0.91 GLU 224
ASP 208 0.87 ASP 228 -0.77 THR 150
ASP 208 1.03 CYS 229 -0.37 THR 150
ASP 208 1.00 THR 230 -0.19 CYS 229
ARG 158 0.93 THR 231 -0.12 THR 150
GLU 224 0.78 ILE 232 -0.27 LEU 111
VAL 225 0.83 HIS 233 -0.27 LEU 111
VAL 225 0.77 TYR 234 -0.40 LEU 111
VAL 225 0.82 ASN 235 -0.30 LEU 111
GLY 226 0.79 TYR 236 -0.30 PHE 212
GLY 226 0.88 MET 237 -0.50 PHE 212
GLY 226 0.87 CYS 238 -0.54 PHE 212
GLY 226 0.88 CYS 238 -0.54 PHE 212
GLY 226 0.89 ASN 239 -0.45 PHE 212
GLY 226 0.89 ASN 239 -0.45 PHE 212
GLY 226 0.79 SER 240 -0.38 GLU 285
GLY 226 0.86 SER 241 -0.43 PHE 212
GLY 226 0.88 CYS 242 -0.57 PHE 212
GLY 226 0.83 MET 243 -0.61 PHE 212
GLY 226 0.77 GLY 244 -0.72 PHE 212
GLY 226 0.74 GLY 245 -0.62 PHE 212
GLY 226 0.70 MET 246 -0.40 PHE 212
GLN 167 0.78 ASN 247 -0.42 PHE 212
GLY 226 0.73 ARG 248 -0.43 GLU 285
GLY 226 0.63 SER 249 -0.34 GLU 171
GLY 226 0.56 PRO 250 -0.35 THR 102
GLY 226 0.56 PRO 250 -0.35 THR 102
GLY 226 0.51 ILE 251 -0.31 THR 102
ASP 208 0.49 LEU 252 -0.40 SER 269
ASP 208 0.58 THR 253 -0.42 ARG 196
ASP 208 0.80 ILE 254 -0.45 SER 166
ASP 208 0.80 ILE 254 -0.45 SER 166
ASP 208 0.99 ILE 255 -0.43 SER 166
ASP 208 1.16 THR 256 -0.53 SER 166
ASP 208 1.17 THR 256 -0.52 SER 166
ASP 208 1.31 LEU 257 -0.47 SER 166
ASP 207 1.20 GLU 258 -0.41 SER 166
ASP 207 1.25 ASP 259 -0.46 VAL 225
ASP 207 1.19 SER 260 -0.44 VAL 225
ASP 207 1.30 SER 261 -0.44 VAL 225
ASP 207 1.30 SER 261 -0.44 VAL 225
ASP 207 1.66 GLY 262 -0.25 VAL 225
ASP 207 1.62 ASN 263 -0.36 VAL 225
PHE 212 1.45 LEU 264 -0.48 SER 166
ASP 208 1.48 LEU 265 -0.50 SER 166
ASP 208 1.68 GLY 266 -0.56 SER 166
ASP 208 1.43 ARG 267 -0.63 SER 166
ASP 208 1.43 ARG 267 -0.63 SER 166
ASP 208 1.21 ASN 268 -0.63 SER 166
ASP 208 0.88 SER 269 -0.60 SER 166
ASP 208 0.70 PHE 270 -0.49 ARG 110
ASP 208 0.51 GLU 271 -0.45 ARG 110
GLY 226 0.57 VAL 272 -0.36 ARG 110
GLY 226 0.56 VAL 272 -0.37 ARG 110
GLY 226 0.69 ARG 273 -0.37 GLU 285
GLY 226 0.81 VAL 274 -0.30 GLU 285
GLY 226 0.92 CYS 275 -0.31 PHE 212
GLY 226 1.05 ALA 276 -0.35 PHE 212
GLY 226 0.99 CYS 277 -0.26 ARG 110
GLY 226 0.99 CYS 277 -0.26 ARG 110
GLY 226 0.85 PRO 278 -0.31 ARG 110
GLY 226 0.82 GLY 279 -0.33 ARG 110
GLY 226 0.86 ARG 280 -0.32 ARG 110
GLY 226 0.78 ASP 281 -0.32 ARG 110
GLY 226 0.66 ARG 282 -0.40 ARG 110
GLY 226 0.66 ARG 282 -0.40 ARG 110
GLY 226 0.69 ARG 283 -0.37 ARG 110
GLY 226 0.69 THR 284 -0.36 ARG 110
GLY 226 0.57 GLU 285 -0.43 ARG 248
GLY 226 0.52 GLU 286 -0.45 GLY 108
GLY 226 0.56 GLU 287 -0.43 GLN 104

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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.