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CA distance fluctuations for 2404111610033706944

---  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 0.64 VAL 97 -0.35 GLY 112
THR 284 0.58 PRO 98 -0.50 HIS 214
LEU 289 0.78 SER 99 -0.46 HIS 214
LEU 130 0.79 GLN 100 -0.55 GLY 112
LEU 130 1.23 LYS 101 -0.33 ASP 228
LEU 130 1.68 THR 102 -0.36 ASP 228
ALA 129 1.64 TYR 103 -0.44 LEU 206
ALA 129 1.71 GLN 104 -0.30 LEU 206
ALA 129 1.48 GLY 105 -0.38 LEU 206
ALA 129 1.29 SER 106 -0.34 LEU 206
ALA 129 1.19 TYR 107 -0.32 GLY 226
ALA 129 1.35 GLY 108 -0.35 GLY 226
ALA 129 1.24 PHE 109 -0.26 VAL 147
PRO 128 1.32 ARG 110 -0.52 TRP 146
PRO 128 0.90 LEU 111 -0.52 TRP 146
ASP 148 0.61 GLY 112 -1.41 PHE 270
ARG 110 0.59 PHE 113 -0.89 PHE 270
ARG 110 0.45 LEU 114 -0.52 GLU 271
ARG 110 0.50 HIS 115 -0.53 THR 231
ARG 110 0.33 SER 116 -0.70 PRO 219
THR 102 0.43 SER 121 -0.63 PRO 219
THR 102 0.48 VAL 122 -0.59 PRO 219
THR 102 0.38 THR 123 -0.60 PRO 219
THR 102 0.45 CYS 124 -0.50 PRO 219
THR 102 0.66 THR 125 -0.35 PRO 219
THR 102 0.84 TYR 126 -0.34 ASP 228
THR 102 1.16 SER 127 -0.51 ARG 248
GLN 104 1.42 PRO 128 -0.55 ARG 248
GLN 104 1.71 ALA 129 -0.74 ARG 248
THR 102 1.68 LEU 130 -0.89 ARG 248
THR 102 1.40 ASN 131 -0.65 PRO 250
THR 102 1.00 LYS 132 -0.56 PRO 250
ASN 268 0.79 MET 133 -0.53 ARG 273
THR 102 0.70 PHE 134 -0.32 GLU 285
THR 102 0.47 CYS 135 -0.37 PRO 219
GLY 226 0.44 GLN 136 -0.42 PRO 219
GLY 226 0.54 LEU 137 -0.49 ASP 186
GLY 226 0.66 ALA 138 -0.43 PRO 219
GLY 226 0.60 LYS 139 -0.58 PRO 219
GLY 226 0.58 THR 140 -0.69 PRO 219
GLY 226 0.42 CYS 141 -0.59 PRO 219
GLY 226 0.38 PRO 142 -0.64 PRO 219
LEU 111 0.55 VAL 143 -0.57 GLU 271
ASN 200 0.62 GLN 144 -0.67 PHE 270
ASN 200 0.75 LEU 145 -0.44 GLN 144
ASN 210 0.72 TRP 146 -0.52 LEU 111
ALA 129 0.89 VAL 147 -0.29 GLN 165
ALA 129 0.94 ASP 148 -0.43 VAL 225
ASN 210 1.04 SER 149 -0.41 VAL 225
ASN 210 1.13 THR 150 -0.29 VAL 225
ASN 210 1.30 PRO 151 -0.22 HIS 233
ASN 210 1.52 PRO 152 -0.31 HIS 233
ARG 209 1.38 PRO 153 -0.42 HIS 233
ARG 209 1.61 GLY 154 -0.53 GLY 199
ARG 209 1.43 THR 155 -0.50 HIS 233
ASP 208 1.35 ARG 156 -0.72 HIS 233
ASP 208 1.32 VAL 157 -0.77 HIS 233
ASP 208 1.45 ARG 158 -0.73 HIS 233
ASP 208 0.77 ALA 159 -0.38 GLY 112
ASP 208 0.59 MET 160 -0.49 GLY 112
ILE 232 0.43 ALA 161 -0.60 GLY 112
ILE 232 0.36 ILE 162 -0.64 GLY 112
ASP 281 0.37 TYR 163 -0.70 GLY 112
VAL 97 0.64 LYS 164 -0.85 GLY 112
VAL 97 0.55 GLN 165 -0.81 GLY 112
GLN 165 0.38 GLU 171 -0.46 GLY 112
GLU 224 0.41 VAL 172 -0.45 GLY 112
GLU 224 0.40 VAL 173 -0.50 GLY 112
GLU 224 0.51 ARG 174 -0.71 PHE 212
VAL 225 0.57 ARG 175 -0.86 PHE 212
GLY 226 0.57 CYS 176 -0.86 PHE 212
GLY 226 0.68 PRO 177 -1.02 PHE 212
GLY 226 0.75 HIS 178 -0.89 PHE 212
GLY 226 0.76 HIS 179 -0.88 PHE 212
VAL 225 0.81 GLU 180 -1.13 PHE 212
GLY 226 0.95 ARG 181 -0.98 PHE 212
VAL 225 1.11 SER 185 -0.66 PHE 212
VAL 225 1.21 ASP 186 -0.56 SER 261
VAL 225 1.23 GLY 187 -0.58 PHE 212
GLU 224 1.27 LEU 188 -0.62 SER 261
GLU 224 1.03 ALA 189 -0.59 PHE 212
GLU 224 0.94 PRO 190 -0.87 PHE 212
VAL 225 0.86 PRO 191 -1.15 PHE 212
GLU 224 0.72 GLN 192 -1.32 PHE 212
GLU 224 0.70 HIS 193 -0.75 PHE 212
GLU 224 0.57 LEU 194 -0.56 PHE 212
GLU 224 0.59 ILE 195 -0.32 PHE 212
GLU 224 0.76 ARG 196 -0.44 SER 261
THR 231 0.87 VAL 197 -0.50 SER 261
GLU 224 0.84 GLU 198 -0.70 PRO 219
SER 227 1.09 GLY 199 -0.71 PRO 219
THR 230 1.42 ASN 200 -0.62 SER 261
PRO 223 1.45 LEU 201 -0.76 SER 261
GLU 224 1.20 ARG 202 -0.91 SER 261
GLU 224 1.07 VAL 203 -0.81 GLY 262
GLU 224 0.97 GLU 204 -0.92 GLY 262
GLU 224 0.90 TYR 205 -0.66 GLY 262
GLU 224 0.78 LEU 206 -0.65 LEU 264
GLU 224 0.67 ASP 207 -0.41 PRO 190
ARG 158 1.45 ASP 208 -0.56 GLN 192
SER 260 1.76 ARG 209 -0.94 ARG 181
PRO 152 1.52 ASN 210 -0.74 ARG 181
ARG 158 0.82 THR 211 -0.63 GLN 192
ARG 156 0.77 PHE 212 -1.32 GLN 192
GLU 224 0.54 ARG 213 -0.46 GLN 192
GLU 224 0.60 HIS 214 -0.50 PRO 98
ILE 232 0.64 SER 215 -0.45 LEU 264
GLU 224 0.72 VAL 216 -0.50 GLY 262
ASP 208 1.11 VAL 217 -0.56 GLY 262
ASP 208 1.07 VAL 218 -0.71 HIS 233
ASP 208 1.16 PRO 219 -0.88 HIS 233
ASP 208 1.12 TYR 220 -0.61 HIS 233
ASP 208 1.02 GLU 221 -0.57 SER 116
LEU 201 0.98 PRO 222 -0.44 SER 116
LEU 201 1.45 PRO 223 -0.36 HIS 115
LEU 201 1.37 GLU 224 -0.29 ASP 148
GLY 187 1.23 VAL 225 -0.43 ASP 148
ASP 186 1.11 GLY 226 -0.43 ASP 148
LEU 201 1.20 SER 227 -0.28 GLN 165
LEU 201 1.03 ASP 228 -0.59 PHE 270
LEU 201 1.03 CYS 229 -0.49 PHE 270
ASN 200 1.42 THR 230 -0.44 LEU 114
ASN 200 1.30 THR 231 -0.56 SER 116
ASP 208 0.83 ILE 232 -0.80 PRO 219
GLY 226 0.52 HIS 233 -0.88 PRO 219
GLY 226 0.49 TYR 234 -0.64 ARG 158
GLY 226 0.58 ASN 235 -0.48 ARG 158
GLY 226 0.51 TYR 236 -0.38 PHE 212
GLY 226 0.63 MET 237 -0.58 PHE 212
GLY 226 0.54 CYS 238 -0.59 PHE 212
GLY 226 0.44 ASN 239 -0.49 GLU 285
GLY 226 0.30 SER 240 -0.67 LEU 130
GLY 226 0.34 SER 241 -0.75 LEU 130
GLY 226 0.45 CYS 242 -0.58 LEU 130
GLY 226 0.43 MET 243 -0.60 LEU 289
GLY 226 0.45 GLY 244 -0.64 PHE 212
VAL 225 0.43 GLY 245 -0.58 PHE 212
VAL 225 0.30 MET 246 -0.58 LEU 130
GLY 226 0.29 ASN 247 -0.70 LEU 130
ALA 276 0.22 ARG 248 -0.89 LEU 130
VAL 97 0.25 ARG 249 -0.78 LEU 130
ASP 281 0.38 PRO 250 -0.75 GLY 112
ASP 281 0.40 ILE 251 -0.76 GLY 112
VAL 97 0.51 LEU 252 -0.94 GLY 112
ASP 208 0.52 THR 253 -0.90 GLY 112
ASP 208 0.67 ILE 254 -0.74 GLY 112
ASP 208 0.72 ILE 255 -0.47 GLY 112
ASN 210 0.81 THR 256 -0.40 LEU 206
ASN 210 1.02 LEU 257 -0.34 HIS 233
ASN 210 1.19 GLU 258 -0.52 GLU 204
ASN 210 1.47 ASP 259 -0.56 GLU 204
ARG 209 1.76 SER 260 -0.79 ARG 202
ASN 210 1.30 SER 261 -0.91 ARG 202
ARG 209 1.18 GLY 262 -0.92 GLU 204
ASN 210 1.23 ASN 263 -0.76 GLU 204
ASN 210 1.11 LEU 264 -0.66 GLU 204
ASN 210 1.19 LEU 265 -0.46 LEU 206
ALA 129 1.26 GLY 266 -0.44 LEU 206
ALA 129 1.17 ARG 267 -0.41 LEU 206
ASN 131 1.35 ASN 268 -0.42 TRP 146
ASN 131 0.78 SER 269 -0.96 GLY 112
ASP 208 0.57 PHE 270 -1.41 GLY 112
ASP 281 0.69 GLU 271 -1.03 GLY 112
ASP 281 0.54 VAL 272 -0.68 GLY 112
VAL 272 0.51 ARG 273 -0.58 LEU 130
THR 102 0.37 VAL 274 -0.41 LEU 130
THR 102 0.44 CYS 275 -0.54 GLU 285
THR 102 0.42 ALA 276 -0.51 ASP 186
THR 102 0.59 CYS 277 -0.41 ASP 186
THR 102 0.66 PRO 278 -0.35 GLU 285
THR 102 0.74 GLY 279 -0.33 PRO 219
THR 102 0.78 ARG 280 -0.30 ASP 186
THR 102 0.90 ASP 281 -0.40 GLU 285
THR 102 0.98 ARG 282 -0.27 ASP 228
THR 102 0.98 ARG 283 -0.24 ASP 228
THR 102 1.02 THR 284 -0.32 SER 241
THR 102 1.06 GLU 285 -0.61 SER 241
THR 102 1.25 GLU 286 -0.51 SER 241
TYR 103 1.10 GLU 287 -0.45 SER 241
TYR 103 1.07 ASN 288 -0.60 SER 241
TYR 103 1.27 LEU 289 -0.66 SER 241
TYR 103 1.25 ARG 290 -0.54 SER 241

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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.