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CA distance fluctuations for 240414154245135808

---  normal mode 12  ---

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
ALA 129 0.69 SER 94 -0.54 GLU 204
LEU 289 0.56 SER 95 -0.88 ARG 202
LYS 164 0.56 SER 96 -0.87 LEU 206
LYS 164 0.76 VAL 97 -1.08 ARG 158
LEU 130 0.74 PRO 98 -1.29 ARG 158
LEU 130 0.77 SER 99 -1.43 ARG 158
ASN 131 0.73 GLN 100 -1.57 MET 169
ASP 208 0.90 LYS 101 -1.65 MET 169
ASP 208 1.29 THR 102 -1.25 GLN 165
ASP 208 1.85 TYR 103 -1.12 SER 166
ASP 208 1.56 GLN 104 -1.02 SER 166
ASP 208 1.51 GLY 105 -1.10 SER 166
ARG 209 1.37 SER 106 -1.01 SER 166
ASP 208 1.23 TYR 107 -0.99 SER 166
ASP 208 1.30 GLY 108 -0.91 SER 166
ASP 208 1.32 PHE 109 -0.93 SER 166
ASP 208 1.19 ARG 110 -1.02 ASN 131
ASP 208 0.99 LEU 111 -0.80 ASN 131
ASP 208 0.87 GLY 112 -0.45 TRP 146
ARG 158 0.73 PHE 113 -0.41 ASP 148
ARG 158 0.67 LEU 114 -0.33 ASP 148
ARG 158 0.57 HIS 115 -0.43 ASP 148
ARG 158 0.52 SER 116 -0.39 ASP 148
ARG 290 0.51 GLY 117 -0.41 ASP 148
ARG 290 0.42 THR 118 -0.39 ASP 148
ARG 158 0.40 ALA 119 -0.34 ASP 186
GLN 167 0.47 LYS 120 -0.37 ASP 186
GLN 167 0.42 SER 121 -0.43 ASP 186
ARG 158 0.47 VAL 122 -0.42 ASP 186
ARG 158 0.51 THR 123 -0.48 ASP 186
ARG 158 0.58 CYS 124 -0.40 ASP 186
ARG 158 0.53 THR 125 -0.41 ARG 110
ARG 158 0.51 TYR 126 -0.55 ARG 110
SER 99 0.55 SER 127 -0.67 ARG 110
GLN 100 0.66 PRO 128 -0.77 ARG 110
SER 99 0.72 ALA 129 -0.73 ARG 110
SER 99 0.77 LEU 130 -0.78 ARG 110
GLN 100 0.73 ASN 131 -1.02 ARG 110
PRO 98 0.58 LYS 132 -0.77 ARG 110
ARG 158 0.47 MET 133 -0.60 LEU 111
ARG 158 0.48 PHE 134 -0.45 ARG 110
ARG 158 0.53 CYS 135 -0.38 ASP 186
SER 261 0.57 GLN 136 -0.45 ASP 186
SER 261 0.69 LEU 137 -0.48 ASP 186
SER 261 0.75 ALA 138 -0.62 ASP 186
SER 261 0.61 LYS 139 -0.66 ASP 186
ARG 158 0.65 THR 140 -0.58 LEU 188
ARG 158 0.81 CYS 141 -0.39 LEU 188
ARG 158 0.90 PRO 142 -0.34 LEU 188
ARG 158 1.06 VAL 143 -0.35 SER 166
ARG 158 0.83 GLN 144 -0.49 SER 166
ASP 208 0.83 LEU 145 -0.69 SER 166
ASP 208 1.00 TRP 146 -0.72 SER 166
ASP 208 1.09 VAL 147 -0.85 SER 166
ARG 209 1.15 ASP 148 -0.81 SER 166
ARG 209 1.15 SER 149 -0.86 SER 166
ARG 209 1.01 THR 150 -0.92 SER 166
ARG 209 0.97 PRO 151 -1.01 SER 166
ARG 209 0.89 PRO 152 -0.99 SER 166
GLY 187 0.82 PRO 153 -0.94 SER 166
GLU 204 1.07 GLY 154 -0.93 SER 166
GLU 204 0.96 THR 155 -1.03 SER 166
GLU 204 0.86 ARG 156 -0.97 SER 99
ASP 208 0.66 VAL 157 -0.94 SER 99
VAL 143 1.06 ARG 158 -1.43 SER 99
VAL 143 0.69 ALA 159 -0.73 SER 99
GLY 262 0.52 MET 160 -0.54 MET 169
SER 261 0.47 ALA 161 -0.63 ILE 162
ASP 281 0.30 ILE 162 -0.63 ALA 161
ASP 281 0.40 TYR 163 -0.90 LYS 101
VAL 97 0.76 LYS 164 -1.04 THR 102
ASP 281 0.57 GLN 165 -1.25 THR 102
ARG 248 0.52 SER 166 -1.51 LEU 264
MET 243 0.77 GLN 167 -0.93 LEU 264
ASN 247 0.98 HIS 168 -1.21 LYS 101
ASN 247 0.55 MET 169 -1.65 LYS 101
ASN 247 0.44 THR 170 -1.06 LYS 101
SER 261 0.48 GLU 171 -0.77 LYS 101
SER 261 0.70 VAL 172 -0.38 LYS 101
SER 261 0.74 VAL 173 -0.39 LYS 101
SER 261 1.01 ARG 174 -0.39 PHE 212
SER 261 1.06 ARG 175 -0.56 PHE 212
SER 261 1.03 CYS 176 -0.60 PHE 212
SER 261 1.15 PRO 177 -0.73 PHE 212
SER 261 1.11 HIS 178 -0.62 PHE 212
SER 261 1.15 HIS 179 -0.61 PHE 212
SER 261 1.33 GLU 180 -0.77 PHE 212
SER 261 1.35 ARG 181 -0.74 PHE 212
SER 261 1.25 CYS 182 -0.61 PHE 212
SER 261 1.37 SER 183 -0.64 PHE 212
SER 261 1.28 ASP 184 -0.55 PHE 212
SER 261 1.43 SER 185 -0.54 PHE 212
SER 261 1.33 ASP 186 -0.66 LYS 139
SER 261 1.49 GLY 187 -0.53 LYS 139
SER 261 1.56 LEU 188 -0.65 GLU 198
SER 261 1.44 ALA 189 -0.52 ASP 207
SER 261 1.62 PRO 190 -0.58 PHE 212
SER 261 1.53 PRO 191 -0.73 PHE 212
SER 261 1.37 GLN 192 -0.77 PHE 212
GLY 262 1.23 HIS 193 -0.47 PHE 212
SER 261 0.95 LEU 194 -0.36 PHE 212
GLY 262 0.83 ILE 195 -0.43 ARG 196
SER 261 0.88 ARG 196 -0.54 THR 253
SER 261 0.70 VAL 197 -0.58 PRO 98
SER 261 0.62 GLU 198 -0.65 LEU 188
VAL 225 0.55 GLY 199 -0.54 SER 95
SER 261 0.49 ASN 200 -0.72 PRO 98
ASP 186 0.75 LEU 201 -0.78 PRO 98
ASP 186 0.77 ARG 202 -0.94 PRO 98
SER 260 0.86 VAL 203 -0.93 PRO 98
SER 260 1.28 GLU 204 -0.95 PRO 98
GLY 262 1.56 TYR 205 -0.73 PRO 98
GLY 262 1.42 LEU 206 -0.87 SER 96
LEU 264 1.45 ASP 207 -0.57 PRO 190
TYR 103 1.85 ASP 208 -0.47 ARG 181
SER 106 1.37 ARG 209 -0.63 ARG 181
GLY 105 1.30 ASN 210 -0.55 ARG 181
TYR 103 1.18 THR 211 -0.50 PRO 191
LEU 264 1.25 PHE 212 -0.77 GLU 180
LEU 264 1.00 ARG 213 -0.48 GLN 192
GLY 262 1.07 HIS 214 -0.53 SER 96
GLY 262 0.92 SER 215 -0.82 VAL 97
GLY 262 0.94 VAL 216 -0.82 PRO 98
TYR 234 0.59 VAL 217 -1.21 PRO 98
ASP 186 0.54 VAL 218 -1.03 PRO 98
ASP 186 0.58 PRO 219 -0.99 PRO 98
ASP 208 0.61 TYR 220 -0.88 SER 166
ARG 209 0.55 GLU 221 -0.81 SER 166
ARG 209 0.64 PRO 222 -0.79 SER 166
ASN 210 0.63 PRO 223 -0.66 SER 166
ASN 210 0.53 GLU 224 -0.56 SER 166
GLY 199 0.55 VAL 225 -0.59 SER 166
GLY 199 0.54 GLY 226 -0.46 SER 166
ASN 210 0.60 SER 227 -0.48 SER 166
ASN 210 0.72 ASP 228 -0.57 SER 166
ASP 208 0.75 CYS 229 -0.59 SER 166
ARG 158 0.70 THR 230 -0.59 SER 166
ARG 158 0.85 THR 231 -0.46 SER 166
ARG 158 0.69 ILE 232 -0.54 THR 253
ARG 158 0.86 HIS 233 -0.42 LEU 188
ARG 158 0.87 TYR 234 -0.57 THR 253
SER 261 0.69 ASN 235 -0.48 LEU 188
SER 261 0.75 TYR 236 -0.36 LEU 252
SER 261 0.92 MET 237 -0.41 PHE 212
SER 261 0.86 CYS 238 -0.48 ASN 288
SER 261 0.71 ASN 239 -0.57 ASN 288
SER 261 0.62 SER 240 -0.63 ASN 288
GLN 167 0.71 SER 241 -0.71 ASN 288
SER 261 0.78 CYS 242 -0.60 LYS 291
HIS 168 0.79 MET 243 -0.62 LYS 291
SER 261 0.87 GLY 244 -0.52 LYS 291
SER 261 0.86 GLY 245 -0.48 LYS 291
SER 261 0.68 MET 246 -0.51 LYS 291
HIS 168 0.98 ASN 247 -0.63 LYS 291
HIS 168 0.83 ARG 248 -0.72 LYS 291
CYS 275 0.48 ARG 249 -0.62 THR 102
ASP 281 0.52 PRO 250 -0.68 THR 102
PRO 98 0.44 ILE 251 -0.55 THR 102
PRO 98 0.60 LEU 252 -0.61 SER 269
ASP 208 0.58 THR 253 -0.57 TYR 234
ASP 208 0.81 ILE 254 -0.65 MET 169
ASP 208 0.89 ILE 255 -0.75 SER 166
ASP 208 1.11 THR 256 -1.02 SER 166
ASP 208 1.12 LEU 257 -1.10 SER 166
LEU 206 1.23 GLU 258 -1.24 SER 166
LEU 206 1.20 ASP 259 -1.15 SER 166
LEU 188 1.42 SER 260 -0.99 SER 166
PRO 190 1.62 SER 261 -0.80 SER 166
TYR 205 1.56 GLY 262 -1.14 SER 166
LEU 206 1.36 ASN 263 -1.31 SER 166
ASP 207 1.45 LEU 264 -1.51 SER 166
ASP 208 1.27 LEU 265 -1.27 SER 166
ASP 208 1.55 GLY 266 -1.16 SER 166
ASP 208 1.50 ARG 267 -1.06 SER 166
ASP 208 1.20 ASN 268 -0.89 SER 166
ASP 208 0.87 SER 269 -0.90 LYS 164
ASP 208 0.70 PHE 270 -0.61 GLU 271
PRO 98 0.64 GLU 271 -0.63 ARG 110
PRO 98 0.42 VAL 272 -0.49 ARG 110
SER 261 0.47 ARG 273 -0.58 ASN 288
SER 261 0.57 VAL 274 -0.50 ASN 288
GLN 167 0.55 CYS 275 -0.51 ASN 288
GLN 167 0.60 ALA 276 -0.49 CYS 182
GLN 167 0.57 CYS 277 -0.42 CYS 182
GLN 167 0.44 PRO 278 -0.37 ARG 110
GLN 167 0.42 GLY 279 -0.35 ARG 110
GLN 167 0.53 ARG 280 -0.35 ARG 110
GLN 165 0.57 ASP 281 -0.37 ARG 110
PRO 98 0.54 ARG 282 -0.47 ARG 110
PRO 98 0.51 ARG 283 -0.44 ASP 148
PRO 98 0.58 THR 284 -0.41 ARG 110
PRO 98 0.61 GLU 285 -0.52 ARG 110
SER 99 0.61 GLU 286 -0.52 GLY 108
SER 94 0.53 GLU 287 -0.47 GLY 108
SER 94 0.52 ASN 288 -0.71 SER 241
SER 94 0.62 LEU 289 -0.59 GLN 104
SER 94 0.61 ARG 290 -0.50 ARG 248
SER 94 0.50 LYS 291 -0.72 ARG 248

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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.