CNRS Nantes University US2B US2B
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CA distance fluctuations for 2402161603593066233

---  normal mode 16  ---

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
PRO 177 0.92 SER 96 -1.19 ASP 208
THR 284 0.72 VAL 97 -1.29 ASP 208
THR 284 0.61 PRO 98 -1.61 ASN 263
THR 284 0.59 SER 99 -1.66 ASN 263
ILE 232 0.51 GLN 100 -1.07 ASN 263
ASN 210 0.46 LYS 101 -0.95 ASP 208
ASN 210 0.65 THR 102 -0.71 PHE 270
ASN 210 0.77 TYR 103 -0.74 PRO 128
ASN 210 0.70 GLN 104 -0.77 PRO 128
ASN 210 0.62 GLY 105 -0.81 ARG 209
SER 261 0.61 SER 106 -0.88 ARG 209
ASN 210 0.57 TYR 107 -0.80 ARG 209
ASN 210 0.61 GLY 108 -0.66 ARG 209
ASN 210 0.73 PHE 109 -0.67 TYR 126
ASN 210 0.65 ARG 110 -0.82 TYR 126
ASN 210 0.58 LEU 111 -0.82 THR 256
PHE 270 1.00 GLY 112 -0.72 VAL 122
PHE 270 0.75 PHE 113 -0.76 LEU 111
GLY 187 0.84 LEU 114 -1.00 VAL 122
ASP 186 1.23 VAL 122 -1.00 LEU 114
LEU 188 1.10 THR 123 -0.87 HIS 179
LEU 188 0.95 CYS 124 -0.86 ARG 158
GLY 187 0.96 THR 125 -0.81 LEU 111
GLY 187 0.86 TYR 126 -0.86 ASN 268
ASP 186 0.83 SER 127 -0.64 ASN 268
GLU 286 0.79 PRO 128 -0.77 GLN 104
ASP 186 0.73 ALA 129 -0.65 ASN 247
ASP 186 0.74 LEU 130 -0.69 ASN 247
ILE 232 0.66 ASN 131 -0.63 THR 102
ASP 186 0.72 LYS 132 -0.56 ASN 247
ASP 186 0.76 MET 133 -0.84 ASN 268
ASP 186 0.76 MET 133 -0.84 ASN 268
ASP 186 0.90 PHE 134 -0.62 ILE 255
LEU 188 0.89 CYS 135 -0.72 ILE 255
LEU 188 1.01 GLN 136 -0.79 HIS 179
ALA 189 1.06 LEU 137 -0.81 SER 261
ALA 189 1.40 ALA 138 -1.08 HIS 179
LEU 188 1.18 LYS 139 -1.16 HIS 179
LEU 188 1.01 THR 140 -1.04 HIS 179
LEU 188 0.83 CYS 141 -1.10 ARG 158
LEU 188 0.84 CYS 141 -1.10 ARG 158
PHE 270 0.76 PRO 142 -0.96 ARG 158
PHE 270 1.25 VAL 143 -0.89 ARG 158
PHE 270 0.98 GLN 144 -0.67 VAL 122
ASN 210 0.69 LEU 145 -0.63 VAL 122
ASN 210 0.67 TRP 146 -0.63 VAL 122
ASN 210 0.61 VAL 147 -0.60 ARG 209
ASN 210 0.53 ASP 148 -0.67 ARG 209
ASN 210 0.47 SER 149 -0.79 ARG 209
ASN 200 0.48 THR 150 -0.86 ARG 209
ASN 210 0.48 PRO 151 -0.95 ARG 209
SER 261 0.42 PRO 152 -1.18 ARG 209
ASN 200 0.34 PRO 153 -1.16 ARG 209
ASN 210 0.34 GLY 154 -1.01 ARG 209
ASN 210 0.51 THR 155 -0.91 ARG 209
ASN 210 0.78 ARG 156 -0.68 SER 185
ASN 210 0.98 VAL 157 -0.80 CYS 141
ASN 210 1.31 ARG 158 -1.10 CYS 141
ASN 210 0.82 ALA 159 -0.90 GLY 262
ASN 210 0.76 MET 160 -1.13 GLY 262
ILE 232 0.69 ALA 161 -0.98 SER 261
THR 284 0.61 ILE 162 -1.06 SER 261
THR 284 0.87 TYR 163 -0.91 SER 261
THR 284 1.00 LYS 164 -0.78 ASN 263
THR 284 1.47 GLN 165 -0.81 ASN 263
THR 284 1.27 SER 166 -1.06 ASN 263
THR 284 1.27 SER 166 -1.06 ASN 263
THR 284 1.31 GLN 167 -0.88 ASN 263
THR 284 1.02 HIS 168 -0.91 SER 261
THR 284 0.98 MET 169 -1.08 ASN 263
ASN 247 0.88 THR 170 -1.11 SER 261
GLY 245 0.94 GLU 171 -1.08 SER 261
GLY 245 0.86 VAL 172 -1.21 SER 261
GLY 245 0.64 VAL 173 -1.06 SER 261
ASP 207 0.70 ARG 174 -1.00 SER 261
ASP 207 1.07 ARG 175 -0.89 SER 261
GLY 245 1.43 CYS 176 -0.72 SER 261
ARG 209 1.19 PRO 177 -0.60 LYS 139
ARG 209 1.54 HIS 178 -0.77 LYS 139
ARG 209 1.37 HIS 179 -1.16 LYS 139
ARG 209 1.29 GLU 180 -0.78 ALA 138
ARG 209 1.42 ARG 181 -0.74 LYS 139
CYS 238 1.21 SER 185 -1.58 LEU 201
ARG 280 1.29 ASP 186 -0.68 SER 261
VAL 122 1.10 GLY 187 -0.59 SER 261
LYS 139 1.18 LEU 188 -1.04 SER 261
ALA 138 1.40 ALA 189 -1.51 SER 261
ALA 138 0.81 PRO 190 -1.40 SER 261
ASP 207 1.18 PRO 191 -1.07 SER 261
ASP 207 1.49 GLN 192 -0.90 SER 261
GLY 245 0.59 HIS 193 -1.35 SER 261
ARG 273 0.70 LEU 194 -1.20 SER 261
VAL 272 0.99 ILE 195 -1.24 SER 261
VAL 272 1.03 ARG 196 -1.09 SER 261
THR 231 0.86 VAL 197 -0.90 SER 261
THR 231 0.60 GLU 198 -0.90 HIS 179
PRO 223 0.89 GLY 199 -1.01 SER 185
GLU 221 1.00 ASN 200 -1.24 SER 185
GLU 221 0.80 LEU 201 -1.58 SER 185
PRO 190 0.48 ARG 202 -1.13 SER 185
PRO 190 0.52 VAL 203 -1.05 SER 185
GLN 192 0.81 GLU 204 -1.39 SER 260
GLN 192 0.84 TYR 205 -1.53 SER 261
GLN 192 1.38 LEU 206 -1.38 SER 261
GLN 192 1.49 ASP 207 -1.41 SER 261
GLU 180 1.23 ASP 208 -1.60 SER 99
HIS 178 1.54 ARG 209 -1.18 PRO 152
ARG 158 1.31 ASN 210 -0.75 LEU 188
PRO 177 0.82 THR 211 -1.01 SER 261
GLY 245 1.11 PHE 212 -1.44 SER 261
THR 211 0.76 ARG 213 -1.49 SER 261
GLN 192 0.92 HIS 214 -1.61 SER 261
GLN 192 0.86 SER 215 -1.40 GLY 262
GLN 192 0.65 VAL 216 -1.23 SER 261
ASN 210 0.82 VAL 217 -0.78 TYR 234
ASN 210 0.73 VAL 218 -0.78 HIS 233
ASN 210 0.72 PRO 219 -0.71 SER 185
ASN 210 0.69 TYR 220 -0.57 ARG 209
ASN 200 1.00 GLU 221 -0.52 ARG 209
ASN 200 0.94 PRO 222 -0.53 ARG 209
GLY 199 0.89 PRO 223 -0.44 VAL 122
GLY 199 0.85 GLU 224 -0.42 SER 185
GLY 199 0.52 VAL 225 -0.46 HIS 179
GLY 199 0.77 GLY 226 -0.38 ARG 181
GLY 199 0.69 SER 227 -0.47 VAL 122
GLY 199 0.62 ASP 228 -0.54 VAL 122
GLY 199 0.69 CYS 229 -0.60 VAL 122
ASN 200 0.85 THR 230 -0.55 VAL 122
VAL 197 0.86 THR 231 -0.63 VAL 122
PHE 270 1.16 ILE 232 -0.52 VAL 122
PHE 270 0.71 HIS 233 -0.93 ARG 158
VAL 272 1.04 TYR 234 -1.00 ARG 158
ALA 189 1.05 ASN 235 -0.94 SER 261
ALA 189 1.06 TYR 236 -0.99 SER 261
ALA 189 0.81 MET 237 -1.00 SER 261
SER 185 1.21 CYS 238 -0.94 SER 261
SER 185 1.20 CYS 238 -0.95 SER 261
SER 185 1.18 ASN 239 -0.82 SER 261
SER 185 0.87 SER 240 -0.73 SER 261
SER 185 1.01 SER 241 -0.71 SER 261
SER 185 1.03 CYS 242 -0.78 SER 261
SER 185 0.78 MET 243 -0.78 SER 261
SER 185 0.80 GLY 244 -0.67 SER 261
CYS 176 1.43 GLY 245 -0.74 GLU 286
ARG 209 1.06 MET 246 -1.11 GLU 287
HIS 168 0.90 ASN 247 -1.35 GLU 286
GLN 167 0.97 ARG 248 -0.86 GLU 286
ASP 281 1.05 SER 249 -0.72 SER 261
ASP 281 1.05 PRO 250 -0.74 SER 261
ILE 232 0.66 ILE 251 -0.77 SER 261
ILE 232 0.83 LEU 252 -0.71 CYS 238
ILE 232 1.02 THR 253 -0.93 CYS 238
ASN 210 0.81 ILE 254 -0.82 TYR 236
ASN 210 0.81 ILE 254 -0.82 TYR 236
ASN 210 0.96 ILE 255 -0.86 TYR 236
ASN 210 1.27 THR 256 -0.87 CYS 141
ASN 210 1.26 THR 256 -0.87 CYS 141
ASN 210 0.91 LEU 257 -0.63 ARG 209
ASN 210 0.72 GLU 258 -0.94 SER 99
SER 106 0.42 ASP 259 -1.12 ASP 208
SER 106 0.30 SER 260 -1.39 GLU 204
SER 106 0.61 SER 261 -1.61 HIS 214
SER 106 0.35 GLY 262 -1.46 PRO 98
SER 106 0.55 ASN 263 -1.66 SER 99
ASN 210 0.59 LEU 264 -1.26 SER 99
ASN 210 0.64 LEU 265 -0.93 ASP 208
ASN 210 0.81 GLY 266 -0.71 ARG 209
ASN 210 0.94 ARG 267 -0.77 TYR 126
ASN 210 0.81 ASN 268 -0.86 TYR 126
ILE 232 0.88 SER 269 -0.63 CYS 238
VAL 143 1.25 PHE 270 -0.71 THR 102
ILE 232 0.93 GLU 271 -0.65 ARG 248
TYR 234 1.04 VAL 272 -0.63 ARG 248
TYR 234 1.04 VAL 272 -0.63 ARG 248
ILE 195 0.82 ARG 273 -0.59 GLU 285
ASP 186 0.82 VAL 274 -0.70 SER 261
ASP 186 0.98 CYS 275 -0.77 GLU 285
ASP 186 1.13 ALA 276 -0.69 GLU 285
ASP 186 1.25 CYS 277 -0.66 HIS 178
ASP 186 1.25 CYS 277 -0.67 HIS 178
ASP 186 1.14 PRO 278 -0.58 SER 261
ASP 186 1.28 GLY 279 -0.64 LEU 114
ASP 186 1.29 ARG 280 -0.57 LEU 114
GLN 167 1.13 ASP 281 -0.44 SER 261
ASP 186 1.09 ARG 282 -0.45 SER 261
ASP 186 1.26 ARG 283 -0.52 ALA 129
GLN 165 1.47 THR 284 -0.39 CYS 277
GLN 165 1.08 GLU 285 -0.91 MET 246
ASP 186 0.99 GLU 286 -1.35 ASN 247
ASP 186 1.03 GLU 287 -1.15 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.