CNRS Nantes University US2B US2B
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CA distance fluctuations for 240415022434281025

---  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
ASN 263 1.57 SER 96 -0.81 ARG 213
LEU 264 1.49 VAL 97 -1.27 ARG 213
LEU 264 1.17 PRO 98 -0.72 LEU 206
ARG 267 0.92 SER 99 -0.45 LEU 206
ASN 131 0.83 GLN 100 -0.51 LEU 206
ASN 131 0.81 LYS 101 -0.46 LEU 206
PHE 113 0.67 THR 102 -0.25 LEU 206
ASN 210 0.77 TYR 103 -0.17 LEU 206
ASN 210 0.89 GLN 104 -0.28 ALA 129
ASN 210 1.13 GLY 105 -0.38 THR 230
ASN 210 1.29 SER 106 -0.44 THR 230
ARG 209 1.22 TYR 107 -0.62 PRO 128
ASN 210 0.95 GLY 108 -0.67 ALA 129
ASN 210 0.93 PHE 109 -0.67 PRO 128
ASN 200 0.75 ARG 110 -0.78 ASN 131
ASN 200 0.69 LEU 111 -0.94 PHE 270
ASN 200 0.63 GLY 112 -1.12 ASN 131
SER 269 0.73 PHE 113 -1.32 SER 227
THR 102 0.54 LEU 114 -1.58 SER 227
SER 185 0.33 SER 121 -1.31 GLY 226
LYS 101 0.33 VAL 122 -1.34 GLY 226
SER 185 0.40 THR 123 -1.26 TYR 220
SER 185 0.39 CYS 124 -1.33 TYR 220
LYS 101 0.46 THR 125 -1.35 GLY 226
LYS 101 0.62 TYR 126 -1.28 SER 227
LYS 101 0.61 SER 127 -1.29 SER 227
LYS 101 0.73 PRO 128 -1.23 ASP 228
LYS 101 0.69 ALA 129 -1.08 ASP 228
LYS 101 0.73 LEU 130 -0.98 SER 227
GLN 100 0.83 ASN 131 -1.12 GLY 112
GLN 100 0.64 LYS 132 -0.99 SER 227
GLN 100 0.50 MET 133 -1.04 SER 227
GLN 100 0.40 PHE 134 -1.06 GLY 226
SER 185 0.42 CYS 135 -1.08 TYR 220
SER 185 0.47 GLN 136 -1.00 TYR 220
SER 185 0.57 LEU 137 -0.87 TYR 220
SER 185 0.78 ALA 138 -0.89 TYR 220
SER 185 0.60 LYS 139 -1.12 TYR 220
SER 185 0.55 THR 140 -1.31 TYR 220
SER 269 0.45 CYS 141 -1.34 TYR 220
SER 269 0.44 PRO 142 -1.47 TYR 220
ASN 200 0.67 VAL 143 -1.05 TYR 220
ASN 200 0.77 GLN 144 -1.12 LEU 257
ASN 200 1.06 LEU 145 -1.11 LEU 257
ASN 200 0.91 TRP 146 -0.96 PRO 128
VAL 218 1.12 VAL 147 -0.91 PRO 128
LEU 201 1.04 ASP 148 -0.93 ALA 129
ARG 209 1.13 SER 149 -0.72 ALA 129
PRO 219 1.69 THR 150 -0.58 ARG 290
ARG 209 1.32 PRO 151 -1.25 GLU 224
ARG 209 1.20 PRO 152 -1.15 GLU 224
ARG 209 1.03 PRO 153 -1.15 VAL 225
ARG 209 1.16 GLY 154 -1.10 GLU 224
ARG 209 1.47 THR 155 -1.46 GLU 224
ASP 208 1.49 ARG 156 -1.43 THR 231
ASP 208 1.33 VAL 157 -1.63 ILE 232
GLU 221 1.25 ARG 158 -0.52 ILE 232
GLU 221 1.17 ALA 159 -0.34 VAL 97
GLU 221 0.99 MET 160 -0.52 VAL 97
GLU 221 0.79 ALA 161 -0.53 VAL 97
GLY 262 0.87 ILE 162 -0.49 VAL 97
GLY 262 0.98 TYR 163 -0.45 GLY 226
GLY 262 0.93 LYS 164 -0.49 GLY 226
GLY 262 1.08 GLN 165 -0.50 GLY 226
GLY 262 1.32 SER 166 -0.36 GLY 226
GLY 262 1.45 GLN 167 -0.39 GLY 226
GLY 262 1.42 HIS 168 -0.44 ARG 249
GLY 262 1.41 MET 169 -0.29 GLY 226
GLY 262 1.58 THR 170 -0.32 GLY 245
GLY 262 1.41 GLU 171 -0.48 VAL 97
GLY 262 1.05 VAL 172 -1.14 VAL 97
GLY 262 0.83 VAL 173 -0.83 VAL 97
GLU 221 0.67 ARG 174 -0.83 VAL 97
GLU 221 0.61 ARG 175 -0.68 VAL 97
GLY 262 0.56 CYS 176 -0.62 PHE 212
SER 261 0.54 PRO 177 -0.74 PHE 212
GLU 221 0.45 HIS 178 -0.61 PHE 212
GLU 221 0.49 HIS 179 -0.58 PHE 212
GLU 221 0.55 GLU 180 -0.73 PHE 212
GLU 221 0.49 ARG 181 -0.70 PHE 212
GLU 221 0.45 CYS 182 -0.56 PHE 212
ALA 138 0.78 SER 185 -0.68 LEU 201
GLU 198 0.85 ASP 186 -0.91 LEU 201
GLU 221 0.63 GLY 187 -0.82 LEU 201
GLU 221 0.75 LEU 188 -0.82 LEU 201
GLU 221 0.82 ALA 189 -0.58 LEU 201
GLU 221 0.76 PRO 190 -0.75 ASP 207
GLU 221 0.66 PRO 191 -0.74 PHE 212
GLU 221 0.70 GLN 192 -0.84 PHE 212
GLU 221 0.78 HIS 193 -0.74 VAL 97
GLU 221 0.71 LEU 194 -0.61 VAL 97
GLU 221 0.80 ILE 195 -0.51 VAL 97
GLU 221 0.80 ARG 196 -0.73 VAL 218
GLU 221 0.78 VAL 197 -1.19 VAL 218
ASP 186 0.85 GLU 198 -1.01 PRO 219
THR 230 0.58 GLY 199 -0.99 PRO 219
THR 230 1.20 ASN 200 -0.46 PRO 219
PRO 223 1.45 LEU 201 -0.91 ASP 186
PRO 222 1.44 ARG 202 -0.48 GLY 262
GLU 221 1.31 VAL 203 -0.41 LEU 188
GLU 221 1.15 GLU 204 -0.44 VAL 97
GLU 221 1.06 TYR 205 -0.58 VAL 97
GLU 221 1.02 LEU 206 -0.72 PRO 98
THR 150 1.16 ASP 207 -0.75 PRO 190
LEU 257 1.51 ASP 208 -0.46 PRO 190
THR 155 1.47 ARG 209 -0.62 ARG 181
LEU 265 1.59 ASN 210 -0.55 ARG 181
GLU 258 1.83 THR 211 -0.47 PRO 177
GLU 258 1.41 PHE 212 -0.84 GLN 192
GLU 221 0.92 ARG 213 -1.27 VAL 97
GLU 221 0.94 HIS 214 -0.95 VAL 97
GLU 221 1.11 SER 215 -0.64 VAL 97
GLU 221 1.30 VAL 216 -0.48 VAL 97
GLU 221 1.58 VAL 217 -0.37 LEU 264
GLU 221 1.31 VAL 218 -1.19 VAL 197
THR 150 1.69 PRO 219 -1.33 PRO 142
ARG 209 1.17 TYR 220 -1.49 LEU 114
VAL 217 1.58 GLU 221 -1.58 ASP 259
ARG 202 1.44 PRO 222 -1.15 ASP 259
LEU 201 1.45 PRO 223 -1.32 THR 155
LEU 201 1.27 GLU 224 -1.46 THR 155
LEU 201 0.84 VAL 225 -1.24 LEU 114
LEU 201 0.52 GLY 226 -1.35 THR 125
LEU 201 0.71 SER 227 -1.58 LEU 114
LEU 201 0.85 ASP 228 -1.23 PRO 128
LEU 201 0.98 CYS 229 -1.01 PRO 151
ASN 200 1.20 THR 230 -1.27 LEU 257
ASN 200 0.86 THR 231 -1.43 ARG 156
ASN 200 0.97 ILE 232 -1.63 VAL 157
ASP 186 0.56 HIS 233 -1.32 PRO 219
GLU 221 0.60 TYR 234 -0.93 TYR 220
SER 185 0.70 ASN 235 -0.90 TYR 220
SER 185 0.59 TYR 236 -0.75 TYR 220
SER 185 0.62 MET 237 -0.63 TYR 220
GLU 221 0.50 CYS 238 -0.60 GLY 226
GLU 221 0.42 ASN 239 -0.70 GLY 226
GLY 262 0.53 SER 240 -0.69 GLY 226
GLY 262 0.55 SER 241 -0.68 GLY 226
GLY 262 0.55 CYS 242 -0.60 GLY 226
GLY 262 0.70 GLY 245 -0.58 VAL 97
GLY 262 0.73 MET 246 -0.53 GLY 226
GLY 262 0.70 ASN 247 -0.57 GLY 226
GLY 262 0.67 ARG 248 -0.65 GLY 226
GLY 262 0.79 ARG 249 -0.60 GLY 226
GLY 262 0.72 PRO 250 -0.65 GLY 226
GLY 262 0.70 ILE 251 -0.57 GLY 226
GLY 262 0.62 LEU 252 -0.53 SER 227
GLU 221 0.70 THR 253 -0.45 SER 227
GLU 221 0.77 ILE 254 -0.30 SER 227
GLU 221 0.96 ILE 255 -0.37 GLN 144
ASP 208 1.07 THR 256 -0.64 THR 231
ASP 208 1.51 LEU 257 -1.27 THR 231
THR 211 1.83 GLU 258 -1.12 THR 230
PHE 212 1.39 ASP 259 -1.58 GLU 221
PHE 212 1.28 SER 260 -1.25 GLU 221
THR 170 1.25 SER 261 -0.82 GLU 221
THR 170 1.58 GLY 262 -0.63 GLU 221
SER 96 1.57 ASN 263 -0.67 THR 230
SER 96 1.51 LEU 264 -0.76 THR 230
ASN 210 1.59 LEU 265 -1.04 THR 230
THR 211 1.15 GLY 266 -0.67 THR 230
SER 99 0.92 ARG 267 -0.33 THR 231
GLU 221 0.66 ASN 268 -0.17 LYS 164
PHE 113 0.73 SER 269 -0.33 LYS 164
GLN 100 0.79 PHE 270 -0.94 LEU 111
GLN 100 0.64 GLU 271 -0.73 SER 227
GLN 100 0.42 VAL 272 -0.78 GLY 226
GLY 262 0.39 ARG 273 -0.85 GLY 226
SER 185 0.40 VAL 274 -0.83 GLY 226
SER 185 0.39 CYS 275 -0.91 GLY 226
SER 185 0.37 ALA 276 -0.95 GLY 226
SER 185 0.34 CYS 277 -1.08 GLY 226
SER 185 0.35 PRO 278 -1.17 GLY 226
LYS 101 0.40 GLY 279 -1.34 GLY 226
LYS 101 0.36 ARG 280 -1.21 GLY 226
LYS 101 0.34 ASP 281 -1.11 GLY 226
LYS 101 0.44 ARG 282 -1.22 GLY 226
LYS 101 0.45 ARG 283 -1.28 GLY 226
GLN 100 0.39 THR 284 -1.11 GLY 226
GLN 100 0.47 GLU 285 -1.04 GLY 226
LYS 101 0.52 GLU 286 -1.15 GLY 226
LYS 101 0.46 GLU 287 -1.12 GLY 226
GLN 100 0.45 ASN 288 -0.98 GLY 226
GLN 100 0.53 LEU 289 -0.97 GLY 226
LYS 101 0.49 ARG 290 -1.02 GLY 226

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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.