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CA distance fluctuations for 24041412272582721

---  normal mode 10  ---

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
GLN 165 0.34 SER 96 -1.25 LEU 206
LYS 164 0.49 VAL 97 -0.91 SER 215
SER 99 0.58 PRO 98 -1.05 ARG 158
THR 211 0.81 SER 99 -0.91 ARG 158
THR 211 0.70 GLN 100 -0.91 SER 166
ASP 208 0.82 LYS 101 -1.16 SER 166
ASP 208 1.23 THR 102 -1.12 ASN 288
ASP 208 1.61 TYR 103 -1.12 LEU 130
ASP 208 1.73 GLN 104 -1.27 ALA 129
ASP 208 1.65 GLY 105 -1.03 ALA 129
ASP 208 1.48 SER 106 -0.95 ALA 129
ASP 208 1.58 TYR 107 -0.97 ALA 129
ASP 208 1.61 GLY 108 -1.20 ALA 129
ASP 208 1.69 PHE 109 -1.13 ALA 129
ASP 208 1.37 ARG 110 -1.23 ASN 131
ASP 208 1.07 LEU 111 -0.92 ASN 131
ASP 208 0.95 GLY 112 -0.68 TRP 146
ASP 208 0.78 PHE 113 -0.49 TRP 146
ASP 208 0.67 LEU 114 -0.28 ASP 148
ASP 208 0.60 HIS 115 -0.42 ASP 148
GLY 226 0.74 SER 116 -0.34 ARG 110
GLY 226 0.64 GLY 117 -0.47 ARG 110
GLY 226 0.60 THR 118 -0.47 ARG 110
GLY 226 0.72 ALA 119 -0.35 ARG 110
GLY 226 0.68 LYS 120 -0.33 ARG 110
GLY 226 0.80 SER 121 -0.34 ALA 276
GLY 226 0.80 VAL 122 -0.28 ARG 110
GLY 226 0.66 THR 123 -0.32 LEU 111
GLY 226 0.59 CYS 124 -0.39 LEU 111
GLY 226 0.51 THR 125 -0.55 ARG 110
ASP 208 0.45 TYR 126 -0.77 ARG 110
ASP 208 0.39 SER 127 -1.05 ARG 110
ASP 208 0.50 PRO 128 -1.20 ARG 110
ASP 208 0.37 ALA 129 -1.27 GLN 104
ARG 249 0.45 LEU 130 -1.20 GLN 104
ASP 208 0.45 ASN 131 -1.23 ARG 110
ASP 208 0.41 LYS 132 -0.79 ARG 110
ASP 208 0.38 MET 133 -0.72 LEU 111
GLY 226 0.36 PHE 134 -0.57 ARG 110
ARG 158 0.45 CYS 135 -0.46 LEU 111
GLY 226 0.46 GLN 136 -0.37 LEU 111
SER 261 0.51 LEU 137 -0.46 PHE 212
SER 261 0.56 ALA 138 -0.47 PHE 212
ARG 158 0.54 LYS 139 -0.43 CYS 182
ARG 158 0.63 THR 140 -0.41 SER 183
ARG 158 0.74 CYS 141 -0.43 LEU 111
ARG 158 0.82 PRO 142 -0.30 LEU 111
ARG 158 0.82 VAL 143 -0.45 LEU 111
ASP 208 0.93 GLN 144 -0.36 ALA 129
ASP 208 1.07 LEU 145 -0.58 ASN 131
ASP 208 1.29 TRP 146 -0.79 PRO 128
ASP 208 1.44 VAL 147 -0.94 ALA 129
ASP 208 1.39 ASP 148 -1.00 ALA 129
ASP 208 1.36 SER 149 -0.86 ALA 129
ASP 208 1.23 THR 150 -0.94 VAL 225
ASP 208 1.26 PRO 151 -0.91 VAL 225
ASP 208 1.06 PRO 152 -1.00 VAL 225
ASP 208 0.89 PRO 153 -0.84 VAL 225
ASP 208 0.80 GLY 154 -0.59 VAL 225
ASP 208 1.00 THR 155 -0.54 VAL 225
ASP 208 0.85 ARG 156 -0.57 PRO 98
ASP 208 0.87 VAL 157 -0.60 PRO 98
HIS 233 0.86 ARG 158 -1.05 PRO 98
ASP 208 0.56 ALA 159 -0.63 PRO 98
THR 256 0.50 MET 160 -0.48 SER 96
SER 261 0.36 ALA 161 -0.49 ASN 288
PHE 113 0.33 ILE 162 -0.55 ASN 288
GLY 245 0.36 TYR 163 -0.64 ASN 288
VAL 97 0.49 LYS 164 -0.79 ASN 288
GLY 244 0.40 GLN 165 -0.80 ASN 288
GLY 244 0.59 SER 166 -1.16 LYS 101
GLY 244 0.90 GLN 167 -0.82 LYS 101
GLY 244 0.81 HIS 168 -0.67 ASN 288
GLY 244 0.47 MET 169 -0.70 GLN 100
GLY 244 0.23 THR 170 -0.52 ASN 288
SER 261 0.49 GLU 171 -0.65 ARG 249
ASN 263 0.68 VAL 172 -0.62 ARG 249
GLY 262 0.62 VAL 173 -0.56 ARG 249
SER 261 0.71 ARG 174 -0.58 PHE 212
SER 261 0.73 ARG 175 -0.76 PHE 212
SER 261 0.69 CYS 176 -0.92 PHE 212
SER 261 0.76 PRO 177 -1.15 PHE 212
SER 261 0.74 HIS 178 -1.01 PHE 212
SER 261 0.76 HIS 179 -0.89 PHE 212
SER 261 0.87 GLU 180 -1.03 PHE 212
SER 261 0.90 ARG 181 -1.07 PHE 212
SER 261 0.82 CYS 182 -0.87 PHE 212
SER 261 0.84 SER 183 -0.79 PHE 212
SER 261 0.75 ASP 184 -0.70 PHE 212
SER 261 0.87 SER 185 -0.66 PHE 212
SER 261 0.81 ASP 186 -0.53 SER 96
SER 261 0.96 GLY 187 -0.62 SER 96
SER 261 0.99 LEU 188 -0.73 SER 96
SER 261 0.96 ALA 189 -0.72 SER 96
SER 261 1.16 PRO 190 -0.74 ASP 207
SER 261 1.03 PRO 191 -0.84 PHE 212
SER 261 0.96 GLN 192 -0.82 PHE 212
GLY 262 0.88 HIS 193 -0.56 SER 96
SER 261 0.67 LEU 194 -0.44 SER 96
GLY 262 0.60 ILE 195 -0.48 SER 96
SER 261 0.64 ARG 196 -0.58 SER 96
SER 261 0.53 VAL 197 -0.57 SER 96
SER 261 0.54 GLU 198 -0.50 SER 96
SER 121 0.54 GLY 199 -0.53 SER 96
SER 261 0.45 ASN 200 -0.62 SER 96
SER 261 0.59 LEU 201 -0.68 SER 96
SER 260 0.62 ARG 202 -0.75 SER 96
SER 261 0.71 VAL 203 -0.78 SER 96
SER 260 0.98 GLU 204 -0.92 SER 96
GLY 262 1.19 TYR 205 -0.97 SER 96
GLY 262 1.33 LEU 206 -1.25 SER 96
LEU 264 1.32 ASP 207 -0.74 PRO 190
GLN 104 1.73 ASP 208 -0.53 THR 211
SER 106 1.29 ARG 209 -0.61 PRO 177
ASP 148 1.01 ASN 210 -0.41 PRO 177
TYR 103 1.47 THR 211 -0.60 PRO 177
GLY 105 1.33 PHE 212 -1.15 PRO 177
LEU 264 0.99 ARG 213 -0.70 SER 96
GLY 262 0.90 HIS 214 -0.81 SER 96
GLY 262 0.72 SER 215 -1.00 SER 96
GLY 262 0.75 VAL 216 -0.81 SER 96
HIS 233 0.54 VAL 217 -0.92 PRO 98
HIS 233 0.51 VAL 218 -0.73 PRO 98
ASP 208 0.60 PRO 219 -0.63 PRO 98
ASP 208 0.86 TYR 220 -0.45 PRO 98
ASP 208 0.78 GLU 221 -0.40 SER 96
ASP 208 0.88 PRO 222 -0.45 ALA 129
ASP 208 0.86 PRO 223 -0.36 ALA 129
ASP 208 0.67 GLU 224 -0.61 PRO 152
ASN 210 0.63 VAL 225 -1.00 PRO 152
SER 121 0.80 GLY 226 -0.70 THR 150
ASP 208 0.81 SER 227 -0.39 THR 150
ASP 208 0.97 ASP 228 -0.44 ALA 129
ASP 208 1.00 CYS 229 -0.41 ALA 129
ASP 208 0.92 THR 230 -0.33 ALA 129
ASP 208 0.71 THR 231 -0.41 ASN 200
GLU 224 0.60 ILE 232 -0.43 ILE 255
ARG 158 0.86 HIS 233 -0.33 ASP 184
ARG 158 0.83 TYR 234 -0.39 LEU 111
ARG 158 0.68 ASN 235 -0.33 SER 96
SER 261 0.53 TYR 236 -0.34 PHE 212
SER 261 0.64 MET 237 -0.53 PHE 212
SER 261 0.59 CYS 238 -0.60 PHE 212
SER 261 0.48 ASN 239 -0.54 PHE 212
GLN 167 0.46 SER 240 -0.45 PHE 212
GLN 167 0.59 SER 241 -0.53 PHE 212
GLN 167 0.66 CYS 242 -0.67 PHE 212
GLN 167 0.86 MET 243 -0.75 PHE 212
GLN 167 0.90 GLY 244 -0.87 PHE 212
HIS 168 0.75 GLY 245 -0.74 PHE 212
HIS 168 0.66 MET 246 -0.50 VAL 172
GLN 167 0.85 ASN 247 -0.56 PHE 212
GLN 167 0.68 ARG 248 -0.45 VAL 172
GLN 167 0.54 ARG 249 -0.65 GLU 171
LEU 130 0.41 PRO 250 -0.53 ASN 288
PHE 113 0.32 ILE 251 -0.60 ASN 288
PHE 113 0.41 LEU 252 -0.64 ASN 288
ASP 208 0.51 THR 253 -0.54 ASN 288
ASP 208 0.74 ILE 254 -0.60 ASN 288
ASP 208 0.97 ILE 255 -0.59 ASN 288
ASP 208 1.19 THR 256 -0.66 ASN 288
ASP 208 1.35 LEU 257 -0.68 ASN 288
ASP 208 1.14 GLU 258 -0.64 ASN 288
ASP 208 0.99 ASP 259 -0.60 VAL 225
GLU 204 0.98 SER 260 -0.48 VAL 225
PRO 190 1.16 SER 261 -0.46 VAL 225
LEU 206 1.33 GLY 262 -0.51 LYS 101
ASP 207 1.26 ASN 263 -0.65 ASN 288
ASP 207 1.32 LEU 264 -0.78 ASN 288
ASP 208 1.44 LEU 265 -0.80 ASN 288
ASP 208 1.66 GLY 266 -0.85 ALA 129
ASP 208 1.44 ARG 267 -0.87 ASN 288
ASP 208 1.18 ASN 268 -0.88 ASN 288
GLY 112 0.80 SER 269 -0.75 ASN 288
PHE 113 0.72 PHE 270 -0.67 ASN 288
PHE 113 0.46 GLU 271 -0.69 ASN 288
PHE 113 0.33 VAL 272 -0.52 GLU 285
LEU 130 0.33 ARG 273 -0.42 ARG 110
GLY 226 0.35 VAL 274 -0.38 LEU 111
GLY 226 0.38 CYS 275 -0.40 PHE 212
GLY 226 0.43 ALA 276 -0.41 PHE 212
GLY 226 0.53 CYS 277 -0.38 ARG 110
GLY 226 0.48 PRO 278 -0.47 ARG 110
GLY 226 0.55 GLY 279 -0.48 ARG 110
GLY 226 0.47 ARG 280 -0.48 ARG 110
GLY 226 0.37 ASP 281 -0.54 ARG 110
GLY 226 0.34 ARG 282 -0.65 ARG 110
GLY 226 0.36 ARG 283 -0.65 GLN 104
GLY 226 0.28 THR 284 -0.70 GLN 104
LEU 289 0.26 GLU 285 -0.85 THR 102
GLU 285 0.22 GLU 286 -0.90 GLN 104
GLY 226 0.22 GLU 287 -0.81 TYR 103
LYS 120 0.12 ASN 288 -1.12 THR 102
GLU 285 0.26 LEU 289 -1.01 GLN 104

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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.