CNRS Nantes University US2B US2B
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CA distance fluctuations for 2404210115201599106

---  normal mode 13  ---

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
PHE 212 0.92 VAL 97 -0.45 LYS 164
ARG 209 0.99 PRO 98 -0.40 LEU 252
ARG 209 1.01 SER 99 -0.48 PHE 113
SER 166 1.04 GLN 100 -0.59 PHE 113
SER 166 1.59 LYS 101 -0.53 PHE 113
SER 166 1.34 THR 102 -0.44 PHE 113
SER 166 1.15 TYR 103 -0.44 CYS 182
LEU 130 1.30 GLN 104 -0.49 CYS 182
LEU 130 1.12 GLY 105 -0.57 CYS 182
ASN 210 1.18 SER 106 -0.67 CYS 182
ASN 210 1.18 SER 106 -0.67 CYS 182
ALA 129 1.27 TYR 107 -0.74 CYS 182
ALA 129 1.45 GLY 108 -0.59 CYS 182
LEU 130 1.47 PHE 109 -0.63 CYS 182
LEU 130 1.56 ARG 110 -0.49 CYS 182
LYS 132 1.50 LEU 111 -0.44 CYS 182
ASN 131 1.15 GLY 112 -0.45 CYS 182
GLY 226 1.14 PHE 113 -0.96 SER 269
GLY 226 1.12 LEU 114 -0.61 SER 269
GLY 226 1.29 HIS 115 -0.44 SER 269
GLY 226 1.01 SER 116 -0.50 VAL 225
GLY 226 0.97 VAL 122 -0.65 VAL 225
GLY 226 0.83 THR 123 -0.68 VAL 225
GLY 226 0.95 CYS 124 -0.49 VAL 225
GLY 226 1.17 THR 125 -0.37 CYS 182
GLY 226 1.17 THR 125 -0.37 CYS 182
GLY 226 1.14 TYR 126 -0.34 CYS 182
ASP 228 1.32 SER 127 -0.27 CYS 182
ASP 228 1.51 PRO 128 -0.29 CYS 182
VAL 147 1.56 ALA 129 -0.43 GLU 285
ARG 110 1.56 LEU 130 -0.32 ASP 281
TRP 146 1.61 ASN 131 -0.25 VAL 97
TRP 146 1.62 ASN 131 -0.25 VAL 97
LEU 111 1.50 LYS 132 -0.25 GLN 165
LEU 111 0.98 MET 133 -0.31 CYS 182
GLY 226 0.92 PHE 134 -0.36 VAL 225
GLY 226 0.80 CYS 135 -0.54 VAL 225
GLY 226 0.67 GLN 136 -0.72 VAL 225
GLY 226 0.50 LEU 137 -0.83 VAL 225
PRO 191 0.47 ALA 138 -0.90 VAL 225
GLY 226 0.50 LYS 139 -0.84 VAL 225
GLY 226 0.50 LYS 139 -0.84 VAL 225
GLY 226 0.51 THR 140 -0.71 VAL 225
GLY 226 0.65 CYS 141 -0.73 ARG 158
GLY 226 0.65 CYS 141 -0.73 ARG 158
GLY 226 0.66 PRO 142 -0.67 ARG 158
LYS 132 0.62 VAL 143 -0.57 CYS 182
ASN 131 0.96 GLN 144 -0.57 CYS 182
ASN 131 1.23 LEU 145 -0.70 CYS 182
ASN 131 1.62 TRP 146 -0.64 CYS 182
ALA 129 1.56 VAL 147 -0.75 CYS 182
ALA 129 1.51 ASP 148 -0.68 CYS 182
ALA 129 1.28 SER 149 -0.80 CYS 182
ALA 129 1.19 THR 150 -0.89 CYS 182
ASN 210 1.15 PRO 151 -0.91 CYS 182
ASN 210 1.26 PRO 152 -1.01 CYS 182
ASN 210 1.25 PRO 152 -1.04 CYS 182
ASN 210 1.17 PRO 153 -1.15 CYS 182
ASN 210 1.09 PRO 153 -1.21 CYS 182
ASN 210 1.06 GLY 154 -1.25 CYS 182
ASN 210 1.03 GLY 154 -1.27 CYS 182
ASN 210 1.01 THR 155 -1.10 CYS 182
ARG 209 0.88 ARG 156 -1.13 CYS 182
ARG 209 0.93 VAL 157 -0.94 CYS 182
ASP 208 1.19 ARG 158 -1.02 TYR 234
ASP 208 0.82 ALA 159 -0.62 CYS 182
ASP 208 0.75 MET 160 -0.70 GLY 262
GLU 285 0.74 ALA 161 -0.62 GLY 262
GLU 285 0.83 ILE 162 -0.52 SER 261
GLU 285 0.95 TYR 163 -0.45 SER 261
GLU 285 1.18 LYS 164 -0.45 VAL 97
LYS 101 1.13 GLN 165 -0.26 ARG 273
LYS 101 1.59 SER 166 -0.27 ARG 248
LYS 101 1.17 GLN 167 -0.62 ARG 248
LYS 101 1.18 GLN 167 -0.61 ARG 248
LYS 101 0.93 HIS 168 -0.44 SER 261
LYS 101 1.10 MET 169 -0.28 SER 261
LYS 101 0.71 THR 170 -0.43 SER 261
GLU 285 0.69 GLU 171 -0.67 SER 261
GLU 285 0.63 VAL 172 -0.82 SER 261
GLU 285 0.69 VAL 173 -0.84 SER 261
GLU 285 0.62 ARG 174 -1.06 SER 261
GLU 285 0.64 ARG 175 -1.18 SER 261
GLU 285 0.64 ARG 175 -1.18 SER 261
GLU 285 0.67 CYS 176 -1.09 SER 261
GLU 285 0.56 PRO 177 -1.11 SER 261
GLU 285 0.46 HIS 178 -1.10 VAL 225
GLU 285 0.44 HIS 179 -1.18 SER 261
GLU 285 0.47 GLU 180 -1.36 SER 261
GLU 285 0.31 ARG 181 -1.33 LEU 201
HIS 178 0.14 CYS 182 -1.83 LEU 201
HIS 178 0.14 CYS 182 -1.82 LEU 201
LEU 206 0.42 GLY 187 -1.44 CYS 182
LEU 206 0.59 LEU 188 -1.27 CYS 182
LEU 206 0.44 ALA 189 -1.32 SER 261
GLU 285 0.48 PRO 190 -1.67 SER 261
GLU 285 0.47 PRO 191 -1.81 SER 261
GLU 285 0.51 GLN 192 -1.53 SER 261
GLU 285 0.53 HIS 193 -1.32 SER 261
GLU 285 0.60 LEU 194 -1.08 SER 261
GLU 285 0.57 ILE 195 -0.95 SER 261
GLU 285 0.47 ARG 196 -0.95 SER 261
ASP 208 0.49 VAL 197 -1.06 CYS 182
ASP 208 0.38 GLU 198 -1.16 CYS 182
ASP 208 0.40 GLY 199 -1.31 GLU 224
THR 231 0.55 ASN 200 -1.57 CYS 182
THR 231 0.56 LEU 201 -1.83 CYS 182
THR 231 0.49 ARG 202 -1.53 CYS 182
ASP 208 0.54 VAL 203 -1.26 CYS 182
VAL 203 0.50 GLU 204 -1.48 SER 260
GLU 285 0.48 TYR 205 -1.54 GLY 262
LEU 188 0.59 LEU 206 -1.77 GLY 262
GLU 285 0.50 ASP 207 -1.42 GLY 262
ARG 158 1.19 ASP 208 -0.82 SER 261
ARG 158 1.07 ARG 209 -0.79 GLY 244
PRO 152 1.26 ASN 210 -0.57 GLY 244
PHE 212 1.10 THR 211 -0.74 SER 261
THR 211 1.10 PHE 212 -0.94 SER 261
GLU 285 0.58 ARG 213 -0.96 GLY 262
GLU 285 0.56 HIS 214 -1.27 GLY 262
GLU 285 0.58 SER 215 -1.30 GLY 262
GLU 285 0.58 SER 215 -1.31 GLY 262
ASP 208 0.63 VAL 216 -1.22 GLY 262
ASP 208 0.87 VAL 217 -1.02 CYS 182
ASP 208 0.69 VAL 218 -1.23 CYS 182
ARG 209 0.74 PRO 219 -1.29 CYS 182
ASN 210 0.83 TYR 220 -1.15 CYS 182
ASN 210 0.81 GLU 221 -1.20 CYS 182
ASN 131 0.91 PRO 222 -1.09 CYS 182
ALA 129 0.93 PRO 223 -1.09 CYS 182
ASN 210 0.71 GLU 224 -1.45 CYS 182
ASN 210 0.69 VAL 225 -1.30 CYS 182
HIS 115 1.29 GLY 226 -0.53 CYS 182
PRO 128 1.14 SER 227 -0.83 CYS 182
PRO 128 1.51 ASP 228 -0.73 CYS 182
ASN 131 1.22 CYS 229 -0.76 CYS 182
ASN 131 0.91 THR 230 -0.92 CYS 182
ASN 131 0.62 THR 231 -0.80 CYS 182
ASP 208 0.64 ILE 232 -0.87 CYS 182
ASP 208 0.40 HIS 233 -0.85 CYS 182
GLU 285 0.42 TYR 234 -1.02 ARG 158
GLU 285 0.38 ASN 235 -0.82 ARG 158
GLU 285 0.49 TYR 236 -0.81 SER 261
GLU 285 0.51 MET 237 -1.00 SER 261
GLU 285 0.57 CYS 238 -0.95 SER 261
GLU 285 0.57 CYS 238 -0.94 SER 261
GLU 285 0.61 ASN 239 -0.79 SER 261
GLU 285 0.86 SER 240 -0.68 SER 261
GLU 285 0.76 SER 241 -0.69 SER 261
GLU 285 0.70 CYS 242 -0.83 SER 261
GLU 285 0.72 MET 243 -0.81 SER 261
GLU 285 0.78 GLY 244 -0.87 SER 261
GLU 285 0.85 GLY 245 -0.92 SER 261
GLU 285 0.98 MET 246 -0.76 SER 261
GLU 285 0.91 ASN 247 -0.73 SER 261
GLU 285 1.02 ARG 248 -0.62 GLN 167
GLU 285 1.18 ARG 249 -0.55 GLN 167
GLU 285 1.48 PRO 250 -0.46 SER 261
GLU 285 1.13 ILE 251 -0.48 SER 261
GLU 285 1.00 LEU 252 -0.41 LEU 252
GLU 285 1.00 LEU 252 -0.41 LEU 252
GLU 285 0.74 THR 253 -0.42 PHE 113
ASP 208 0.78 ILE 254 -0.55 PHE 113
ASP 208 0.78 ILE 254 -0.55 PHE 113
ARG 209 0.79 ILE 255 -0.58 CYS 182
ARG 209 0.97 THR 256 -1.11 THR 256
ARG 209 0.95 THR 256 -1.11 THR 256
ARG 209 0.90 LEU 257 -0.81 CYS 182
ARG 209 1.02 GLU 258 -0.94 LEU 206
ARG 209 1.01 GLU 258 -0.93 LEU 206
ASN 210 1.15 ASP 259 -1.19 GLU 204
ASN 210 1.04 SER 260 -1.52 PRO 190
ASN 210 1.10 SER 261 -1.81 PRO 191
ASN 210 0.93 GLY 262 -1.77 LEU 206
ASN 210 1.16 ASN 263 -1.49 LEU 206
ASN 210 1.06 LEU 264 -1.01 LEU 206
ASN 210 1.12 LEU 265 -0.78 LEU 206
ASN 210 0.97 GLY 266 -0.63 CYS 182
GLU 286 0.89 ARG 267 -0.52 CYS 182
GLU 285 0.97 ASN 268 -0.55 PHE 113
GLU 285 0.85 SER 269 -0.96 PHE 113
LEU 111 1.00 PHE 270 -0.65 PHE 113
GLU 285 1.04 GLU 271 -0.33 VAL 97
GLU 285 1.04 GLU 271 -0.33 VAL 97
GLU 285 0.87 VAL 272 -0.39 SER 261
GLU 285 0.82 ARG 273 -0.45 SER 261
GLY 226 0.66 VAL 274 -0.59 SER 261
GLY 226 0.70 CYS 275 -0.62 VAL 225
GLY 226 0.70 ALA 276 -0.74 VAL 225
GLY 226 0.83 CYS 277 -0.64 VAL 225
GLY 226 0.93 PRO 278 -0.50 VAL 225
GLY 226 1.04 GLY 279 -0.45 ARG 283
GLY 226 0.95 ARG 280 -0.43 VAL 225
GLY 226 0.89 ASP 281 -0.36 VAL 225
GLY 226 0.99 ARG 282 -0.24 ASP 281
GLY 108 0.91 ARG 283 -0.45 GLY 279
ARG 110 0.96 THR 284 -0.21 VAL 225
PRO 250 1.48 GLU 285 -0.43 ALA 129
GLN 104 1.24 GLU 286 -0.27 HIS 115

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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.