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***  HEBERTH  ***

CA distance fluctuations for 22040801552493864

---  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
SER 238 0.25 ASP 113 -0.36 ARG 162
SER 238 0.30 LEU 114 -0.29 ARG 162
SER 238 0.24 LYS 115 -0.25 ARG 162
SER 238 0.18 TRP 116 -0.23 ASP 163
SER 238 0.18 HIS 117 -0.21 ASP 163
SER 238 0.14 HIS 118 -0.14 PRO 254
SER 238 0.13 HIS 119 -0.18 PRO 254
SER 161 0.12 ASN 120 -0.20 GLY 253
SER 238 0.11 ILE 121 -0.18 GLY 253
VAL 151 0.12 THR 122 -0.21 GLY 176
TRP 124 0.19 TYR 123 -0.29 GLY 176
TYR 123 0.19 TRP 124 -0.50 GLY 176
ARG 162 0.18 ILE 125 -0.54 GLY 176
TYR 128 0.25 GLN 126 -0.76 GLY 176
TYR 128 0.21 ASN 127 -0.68 GLY 176
GLN 126 0.25 TYR 128 -0.51 GLY 176
ASN 127 0.21 SER 129 -0.36 HIS 175
ARG 162 0.21 GLU 130 -0.33 GLY 176
GLN 126 0.17 ASP 131 -0.22 GLY 176
VAL 216 0.24 LEU 132 -0.26 GLY 176
VAL 216 0.24 PRO 133 -0.32 GLY 176
ARG 162 0.23 ARG 134 -0.39 GLY 176
GLY 215 0.26 ALA 135 -0.34 GLY 176
GLY 215 0.29 VAL 136 -0.33 GLY 253
GLY 215 0.22 ILE 137 -0.29 GLY 176
GLY 215 0.23 ASP 138 -0.33 GLY 176
GLY 215 0.26 ASP 139 -0.35 GLY 253
LYS 258 0.25 ALA 140 -0.35 GLY 253
LYS 258 0.23 PHE 141 -0.27 GLY 253
LYS 258 0.27 ALA 142 -0.32 GLY 253
LYS 258 0.32 ARG 143 -0.43 GLY 253
LYS 258 0.28 ALA 144 -0.31 GLY 253
LYS 258 0.25 PHE 145 -0.28 GLY 253
LYS 258 0.28 ALA 146 -0.38 GLY 253
LYS 258 0.36 LEU 147 -0.35 PRO 254
LYS 258 0.24 TRP 148 -0.26 PRO 254
ARG 158 0.28 SER 149 -0.30 PRO 254
ARG 158 0.29 ALA 150 -0.36 PRO 254
ARG 158 0.26 VAL 151 -0.21 PRO 254
ARG 158 0.22 THR 152 -0.19 PRO 254
THR 157 0.21 PRO 153 -0.21 PRO 254
THR 157 0.20 LEU 154 -0.22 PRO 254
THR 157 0.24 THR 155 -0.26 GLY 253
ARG 158 0.29 PHE 156 -0.24 GLY 253
PHE 156 0.25 THR 157 -0.25 GLY 176
PHE 156 0.29 ARG 158 -0.37 GLY 176
SER 161 0.24 VAL 159 -0.46 GLY 176
ALA 135 0.24 TYR 160 -0.66 GLY 176
VAL 159 0.24 SER 161 -0.65 GLY 176
ARG 134 0.23 ARG 162 -0.76 GLY 197
TYR 128 0.18 ASP 163 -0.61 PRO 196
TYR 128 0.13 ALA 164 -0.43 CA 305
TYR 128 0.09 ASP 165 -0.26 ARG 162
TYR 128 0.08 ILE 166 -0.24 ARG 162
TYR 128 0.09 VAL 167 -0.34 ASP 177
LYS 258 0.09 ILE 168 -0.35 GLY 176
GLY 197 0.13 GLN 169 -0.42 GLY 176
GLY 197 0.11 PHE 170 -0.41 HIS 175
ILE 198 0.18 GLY 171 -0.38 TYR 128
ILE 198 0.15 VAL 172 -0.29 TYR 128
CA 304 0.15 ALA 173 -0.29 TYR 128
HIS 236 0.24 GLU 174 -0.46 ASN 127
HIS 236 0.18 HIS 175 -0.55 ASN 127
HIS 236 0.24 GLY 176 -0.76 GLN 126
HIS 236 0.31 ASP 177 -0.72 ARG 162
HIS 236 0.43 GLY 178 -0.64 ARG 162
HIS 236 0.42 TYR 179 -0.50 ARG 162
PRO 246 0.30 PRO 180 -0.40 ARG 162
CA 304 0.23 PHE 181 -0.26 ARG 162
CA 304 0.17 ASP 182 -0.22 ARG 162
THR 251 0.11 GLY 183 -0.14 VAL 216
THR 251 0.10 LYS 184 -0.30 CA 304
THR 251 0.17 ASP 185 -0.27 PRO 246
ARG 249 0.25 GLY 186 -0.17 SER 238
ARG 249 0.26 LEU 187 -0.21 ARG 162
PHE 181 0.18 LEU 188 -0.17 VAL 216
TYR 179 0.16 ALA 189 -0.19 ARG 162
GLU 227 0.20 HIS 190 -0.27 ARG 162
GLY 178 0.19 ALA 191 -0.30 ARG 162
ASP 177 0.18 PHE 192 -0.38 ARG 162
GLY 178 0.21 PRO 193 -0.35 ARG 162
SER 238 0.19 PRO 194 -0.37 ARG 162
SER 238 0.17 GLY 195 -0.45 ARG 162
SER 238 0.14 PRO 196 -0.61 ASP 163
CA 305 0.18 GLY 197 -0.76 ARG 162
GLY 171 0.18 ILE 198 -0.75 ARG 162
GLY 176 0.15 GLN 199 -0.54 ARG 162
SER 238 0.12 GLY 200 -0.39 ARG 162
GLY 171 0.12 ASP 201 -0.38 ARG 162
GLY 171 0.10 ALA 202 -0.23 ARG 162
GLY 171 0.14 HIS 203 -0.20 ARG 162
LYS 258 0.08 PHE 204 -0.11 GLY 176
LYS 258 0.07 ASP 205 -0.13 TYR 128
ASP 207 0.12 ASP 206 -0.18 VAL 172
ASP 206 0.12 ASP 207 -0.20 VAL 216
ASN 127 0.08 GLU 208 -0.19 VAL 216
ASP 185 0.10 LEU 209 -0.19 MET 247
GLN 126 0.11 TRP 210 -0.15 PRO 240
ILE 137 0.19 SER 211 -0.19 GLU 252
GLY 215 0.28 LEU 212 -0.31 GLU 252
LYS 258 0.17 GLY 213 -0.22 PRO 240
ASP 139 0.25 LYS 214 -0.42 ARG 249
VAL 136 0.29 GLY 215 -0.39 ARG 249
VAL 136 0.25 VAL 216 -0.39 MET 247
VAL 136 0.10 GLY 217 -0.29 MET 247
SER 219 0.14 TYR 218 -0.24 MET 247
LYS 258 0.17 SER 219 -0.17 PRO 240
LYS 258 0.17 LEU 220 -0.19 GLY 253
LYS 258 0.24 PHE 221 -0.27 GLY 253
LYS 258 0.22 LEU 222 -0.13 PHE 250
TYR 179 0.16 VAL 223 -0.09 VAL 216
LYS 258 0.17 ALA 224 -0.12 GLY 253
LYS 258 0.22 ALA 225 -0.13 PHE 250
TYR 179 0.22 HIS 226 -0.12 PHE 250
HIS 190 0.20 GLU 227 -0.16 ARG 162
TYR 179 0.13 PHE 228 -0.13 ARG 162
TYR 179 0.19 GLY 229 -0.14 ARG 162
GLY 178 0.24 HIS 230 -0.21 ARG 162
PHE 192 0.17 ALA 231 -0.25 ARG 162
SER 238 0.19 LEU 232 -0.21 ARG 162
SER 238 0.25 GLY 233 -0.24 ARG 162
SER 238 0.29 LEU 234 -0.26 ASN 262
GLY 178 0.38 ASP 235 -0.34 ASN 262
GLY 178 0.43 HIS 236 -0.33 ASP 259
GLY 178 0.35 SER 237 -0.27 ASP 259
GLY 178 0.38 SER 238 -0.31 VAL 216
GLY 178 0.31 VAL 239 -0.30 VAL 216
GLY 178 0.33 PRO 240 -0.38 PHE 250
GLY 253 0.44 GLU 241 -0.30 PHE 250
GLY 253 0.35 ALA 242 -0.25 PHE 250
TYR 179 0.26 LEU 243 -0.23 PHE 250
TYR 179 0.29 MET 244 -0.19 PHE 250
GLY 178 0.35 TYR 245 -0.28 VAL 216
TYR 179 0.40 PRO 246 -0.30 VAL 216
TYR 179 0.34 MET 247 -0.39 VAL 216
GLY 253 0.28 TYR 248 -0.34 MET 247
GLY 253 0.30 ARG 249 -0.42 LYS 214
GLY 186 0.24 PHE 250 -0.38 PRO 240
GLY 186 0.25 THR 251 -0.16 LEU 212
LYS 258 0.41 GLU 252 -0.31 LEU 212
LYS 258 0.53 GLY 253 -0.43 ARG 143
LYS 258 0.59 PRO 254 -0.36 ALA 150
LYS 258 0.42 PRO 255 -0.18 ALA 150
LYS 258 0.52 LEU 256 -0.18 GLU 241
PRO 254 0.46 HIS 257 -0.14 VAL 151
PRO 254 0.59 LYS 258 -0.16 HIS 236
GLY 253 0.32 ASP 259 -0.33 HIS 236
GLY 253 0.20 ASP 260 -0.16 HIS 236
LEU 147 0.21 VAL 261 -0.16 HIS 236
GLY 253 0.24 ASN 262 -0.40 GLY 263
SER 238 0.22 GLY 263 -0.40 ASN 262
SER 238 0.19 ILE 264 -0.16 ASN 262
ARG 158 0.14 ARG 265 -0.12 LEU 267
SER 238 0.22 HIS 266 -0.15 ARG 162
SER 238 0.24 LEU 267 -0.18 ASN 262
SER 238 0.18 TYR 268 -0.11 ARG 162
ARG 158 0.14 GLY 269 -0.09 LYS 258
PHE 181 0.23 CA 304 -0.30 LYS 184
GLY 197 0.18 CA 305 -0.68 ARG 162

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: October 18th, 2018.