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CA distance fluctuations for 2402161052242961240

---  normal mode 14  ---

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 256 0.90 SER 96 -0.71 GLN 192
ILE 254 0.88 VAL 97 -1.03 VAL 172
ILE 254 1.39 PRO 98 -0.97 VAL 172
THR 256 1.47 SER 99 -1.16 VAL 172
ASN 131 0.90 GLN 100 -0.93 VAL 172
LEU 130 1.00 LYS 101 -0.85 VAL 172
LEU 130 1.38 THR 102 -0.58 VAL 172
ALA 129 1.46 TYR 103 -0.56 LEU 206
ALA 129 1.60 GLN 104 -0.46 LEU 206
ALA 129 1.34 GLY 105 -0.58 LEU 206
ALA 129 1.20 SER 106 -0.54 LEU 206
PRO 128 1.20 TYR 107 -0.46 LEU 206
PRO 152 1.50 GLY 108 -0.39 LEU 206
PRO 128 1.49 PHE 109 -0.37 SER 166
PRO 128 1.45 ARG 110 -0.42 CYS 229
TYR 126 1.06 LEU 111 -0.70 CYS 229
PRO 152 1.11 GLY 112 -0.98 PHE 270
PRO 151 1.12 PHE 113 -1.60 PHE 270
PRO 151 1.26 LEU 114 -1.28 PHE 270
PRO 151 1.00 VAL 122 -0.85 GLY 226
PRO 151 0.95 THR 123 -0.69 GLY 226
PRO 151 0.94 CYS 124 -0.74 GLY 226
PRO 152 0.96 THR 125 -0.82 GLY 226
ARG 110 1.14 TYR 126 -0.82 GLY 226
PRO 152 1.31 SER 127 -0.70 GLY 226
GLN 104 1.51 PRO 128 -0.61 GLY 226
GLN 104 1.60 ALA 129 -0.79 ASN 247
THR 102 1.38 LEU 130 -0.88 ASN 247
ASN 268 1.35 ASN 131 -0.69 SER 227
PRO 152 0.91 LYS 132 -0.77 SER 227
PRO 152 0.86 MET 133 -0.75 SER 227
PRO 152 0.86 MET 133 -0.75 SER 227
PRO 152 0.79 PHE 134 -0.72 SER 185
PRO 151 0.79 CYS 135 -0.77 ASP 186
PRO 151 0.78 GLN 136 -0.94 ASP 186
PRO 151 0.69 LEU 137 -1.22 ASP 186
PRO 191 0.76 ALA 138 -1.14 ASP 186
PRO 151 0.85 LYS 139 -0.80 ASP 186
PRO 151 0.91 THR 140 -0.80 VAL 218
PRO 151 0.91 CYS 141 -0.79 ALA 159
PRO 151 0.91 CYS 141 -0.79 ALA 159
PRO 151 1.00 PRO 142 -1.12 PHE 270
PRO 151 0.91 VAL 143 -1.39 ILE 254
PRO 151 0.91 GLN 144 -1.29 ILE 255
PRO 152 0.91 LEU 145 -1.17 ILE 255
PRO 152 1.11 TRP 146 -0.73 THR 256
PRO 152 1.41 VAL 147 -0.98 LEU 257
PRO 152 1.51 ASP 148 -0.72 THR 155
ALA 129 0.96 SER 149 -1.12 THR 155
ALA 129 0.56 THR 150 -1.36 LEU 264
LEU 114 1.26 PRO 151 -0.27 ASN 263
ALA 129 1.56 PRO 152 -0.28 LEU 206
PRO 128 0.88 PRO 153 -0.78 GLU 204
SER 99 0.74 GLY 154 -1.12 GLU 204
SER 99 1.03 THR 155 -1.12 SER 149
SER 99 1.01 ARG 156 -0.88 SER 149
SER 99 0.99 VAL 157 -1.22 ILE 232
ASN 210 0.96 ARG 158 -1.25 ILE 232
PRO 98 0.85 ALA 159 -1.06 TYR 234
THR 170 0.77 MET 160 -0.85 VAL 143
THR 170 0.50 ALA 161 -0.90 SER 185
THR 170 0.55 ILE 162 -0.87 GLN 100
THR 211 0.37 TYR 163 -0.81 PHE 113
THR 211 0.44 LYS 164 -1.00 PHE 113
THR 211 0.47 GLN 165 -0.88 PHE 113
THR 211 0.56 SER 166 -0.79 PHE 113
THR 211 0.56 SER 166 -0.79 PHE 113
THR 211 0.55 GLN 167 -0.70 PHE 113
ARG 213 0.57 HIS 168 -0.78 SER 99
THR 211 0.71 MET 169 -0.99 SER 99
THR 211 1.31 THR 170 -0.80 SER 99
ARG 213 0.71 GLU 171 -0.93 SER 99
HIS 214 0.59 VAL 172 -1.16 SER 99
TYR 205 0.28 VAL 173 -0.93 SER 185
TYR 205 0.32 ARG 174 -1.04 SER 185
PRO 151 0.29 ARG 175 -1.36 SER 185
PRO 151 0.28 CYS 176 -1.14 SER 185
ALA 138 0.28 PRO 177 -0.84 VAL 97
PRO 151 0.37 HIS 178 -0.79 SER 185
ALA 138 0.46 HIS 179 -1.02 GLY 187
ALA 138 0.55 GLU 180 -1.05 PHE 212
ALA 138 0.48 ARG 181 -0.99 ARG 209
PRO 151 0.35 SER 185 -1.60 CYS 238
PRO 151 0.46 ASP 186 -1.76 MET 237
GLU 224 0.69 GLY 187 -1.02 HIS 179
GLY 199 0.76 LEU 188 -1.13 SER 261
GLU 198 0.62 ALA 189 -1.36 GLY 262
GLU 198 0.47 PRO 190 -1.23 GLY 262
ALA 138 0.76 PRO 191 -1.30 ARG 209
ALA 138 0.40 GLN 192 -1.59 PHE 212
TYR 205 0.50 HIS 193 -1.04 GLY 262
PRO 151 0.37 LEU 194 -1.36 SER 185
PRO 151 0.43 ILE 195 -1.07 ASP 186
PRO 151 0.52 ARG 196 -1.05 GLY 262
PRO 151 0.55 VAL 197 -0.98 GLY 262
PRO 151 0.70 GLU 198 -0.84 GLY 262
LEU 188 0.76 GLY 199 -0.73 VAL 218
GLU 221 0.87 ASN 200 -0.61 GLY 262
PRO 223 1.11 LEU 201 -0.77 SER 261
GLU 221 1.01 ARG 202 -0.98 GLY 154
GLU 221 0.70 VAL 203 -1.15 GLY 262
THR 170 0.60 GLU 204 -1.47 GLY 262
THR 170 0.61 TYR 205 -1.83 GLY 262
THR 170 0.65 LEU 206 -1.51 ASN 263
THR 170 0.87 ASP 207 -1.17 THR 150
THR 170 0.98 ASP 208 -1.11 THR 150
THR 170 0.83 ARG 209 -1.30 PRO 191
ARG 158 0.96 ASN 210 -1.07 PRO 191
THR 170 1.31 THR 211 -1.09 GLN 192
THR 170 1.17 PHE 212 -1.59 GLN 192
THR 170 1.16 ARG 213 -1.03 THR 150
THR 170 0.79 HIS 214 -1.08 THR 150
THR 170 0.80 SER 215 -1.08 GLY 262
THR 170 0.66 VAL 216 -1.20 GLY 262
ASP 208 0.78 VAL 217 -0.86 GLY 262
ASP 208 0.73 VAL 218 -1.01 HIS 233
SER 99 0.84 PRO 219 -0.72 HIS 233
SER 99 0.91 TYR 220 -0.67 SER 149
LEU 201 1.09 GLU 221 -0.56 ASP 148
LEU 201 1.09 PRO 222 -0.47 ASP 148
LEU 201 1.11 PRO 223 -0.57 PHE 270
LEU 201 1.08 GLU 224 -0.55 PHE 270
LEU 201 0.76 VAL 225 -0.63 VAL 122
PRO 151 0.63 GLY 226 -0.85 VAL 122
PRO 151 0.74 SER 227 -0.92 PHE 270
PRO 151 0.76 ASP 228 -0.92 PHE 270
PRO 151 0.82 CYS 229 -0.94 PHE 270
LEU 201 0.88 THR 230 -0.74 PHE 270
PRO 151 0.85 THR 231 -0.99 ILE 255
PRO 151 0.73 ILE 232 -1.25 ARG 158
PRO 151 0.80 HIS 233 -1.05 ARG 158
PRO 151 0.69 TYR 234 -1.06 ALA 159
PRO 151 0.68 ASN 235 -0.90 ASP 186
PRO 151 0.60 TYR 236 -1.29 ASP 186
PRO 191 0.57 MET 237 -1.76 ASP 186
PRO 151 0.51 CYS 238 -1.59 SER 185
PRO 151 0.51 CYS 238 -1.60 SER 185
PRO 151 0.54 ASN 239 -1.28 SER 185
PRO 151 0.45 SER 240 -1.18 SER 185
PRO 151 0.45 SER 241 -1.07 SER 185
PRO 151 0.39 CYS 242 -1.20 SER 185
PRO 151 0.30 MET 243 -1.17 SER 185
PRO 152 0.28 GLY 244 -0.97 SER 185
PRO 151 0.24 GLY 245 -0.87 SER 185
PRO 152 0.27 MET 246 -0.89 GLU 286
PRO 152 0.34 ASN 247 -0.96 GLU 286
PRO 152 0.37 ARG 248 -0.86 SER 185
PRO 152 0.35 SER 249 -0.85 SER 185
PRO 152 0.42 PRO 250 -0.85 SER 185
PRO 152 0.42 ILE 251 -0.93 SER 185
PRO 98 0.60 LEU 252 -1.05 PHE 113
PRO 98 0.80 THR 253 -1.27 VAL 143
PRO 98 1.39 ILE 254 -1.39 VAL 143
PRO 98 1.39 ILE 254 -1.39 VAL 143
PRO 98 1.27 ILE 255 -1.31 VAL 143
SER 99 1.46 THR 256 -1.04 LEU 145
SER 99 1.47 THR 256 -1.04 LEU 145
SER 99 1.45 LEU 257 -0.98 VAL 147
SER 99 1.24 GLU 258 -1.03 SER 149
SER 99 0.92 ASP 259 -1.15 GLU 204
SER 99 0.64 SER 260 -1.39 GLU 204
PRO 128 0.45 SER 261 -1.35 TYR 205
SER 99 0.50 GLY 262 -1.83 TYR 205
ALA 129 0.66 ASN 263 -1.51 LEU 206
SER 99 0.90 LEU 264 -1.37 LEU 206
PRO 128 1.07 LEU 265 -1.04 THR 150
PRO 128 1.32 GLY 266 -0.72 THR 150
PRO 128 1.19 ARG 267 -0.67 LEU 145
ASN 131 1.35 ASN 268 -0.70 LEU 145
ASN 131 1.03 SER 269 -0.93 PHE 113
PRO 98 0.94 PHE 270 -1.60 PHE 113
PRO 152 0.60 GLU 271 -1.21 PHE 113
PRO 152 0.60 VAL 272 -0.87 SER 185
PRO 152 0.59 VAL 272 -0.88 SER 185
PRO 152 0.60 ARG 273 -0.94 SER 185
PRO 151 0.61 VAL 274 -1.06 SER 185
PRO 151 0.68 CYS 275 -0.95 SER 185
PRO 151 0.77 ALA 276 -0.90 ASP 186
PRO 151 0.79 CYS 277 -0.75 ASP 186
PRO 151 0.79 CYS 277 -0.76 ASP 186
PRO 151 0.84 PRO 278 -0.71 ASP 186
PRO 151 0.92 GLY 279 -0.76 GLY 226
PRO 152 0.84 ARG 280 -0.67 GLY 226
PRO 152 0.89 ASP 281 -0.70 SER 185
PRO 152 1.04 ARG 282 -0.66 SER 185
PRO 152 1.04 ARG 283 -0.65 GLY 226
PRO 152 1.01 THR 284 -0.61 SER 185
PRO 152 1.20 GLU 285 -0.70 MET 246
PRO 152 1.29 GLU 286 -0.96 ASN 247
PRO 152 1.16 GLU 287 -0.65 ASN 247

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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.