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CA distance fluctuations for 240415023434287799

---  normal mode 8  ---

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
ARG 213 0.63 SER 96 -0.54 GLY 105
SER 215 0.36 VAL 97 -0.56 TYR 103
SER 215 0.41 PRO 98 -0.74 TYR 103
ARG 158 0.72 SER 99 -0.50 ASN 210
ARG 158 0.32 GLN 100 -0.51 ASP 208
LEU 264 0.49 LYS 101 -0.57 ASN 210
LEU 289 0.50 THR 102 -0.76 ASN 210
ALA 129 0.66 TYR 103 -1.16 ASP 208
ALA 129 0.77 GLN 104 -1.20 ASN 210
ALA 129 0.63 GLY 105 -1.48 ARG 209
ALA 129 0.59 SER 106 -1.65 ARG 209
ALA 129 0.59 TYR 107 -1.39 ARG 209
PRO 128 0.75 GLY 108 -1.25 ARG 209
PRO 128 0.71 PHE 109 -1.07 ARG 209
PRO 128 0.82 ARG 110 -0.83 ARG 209
ASN 131 0.72 LEU 111 -0.65 ASP 208
TRP 146 0.62 GLY 112 -0.55 ASP 208
SER 227 0.96 PHE 113 -0.54 SER 269
SER 227 1.23 LEU 114 -0.37 ARG 158
VAL 225 1.16 SER 121 -0.29 SER 261
SER 227 1.16 VAL 122 -0.30 ARG 158
SER 227 1.28 THR 123 -0.37 ARG 158
SER 227 1.25 CYS 124 -0.37 ARG 158
SER 227 1.06 THR 125 -0.30 ARG 158
SER 227 0.86 TYR 126 -0.30 LEU 114
SER 227 0.71 SER 127 -0.24 ASP 208
ARG 110 0.82 PRO 128 -0.35 LEU 114
GLN 104 0.77 ALA 129 -0.22 ASN 210
ARG 110 0.69 LEU 130 -0.20 ASP 208
ARG 110 0.77 ASN 131 -0.29 ASP 208
SER 227 0.70 LYS 132 -0.25 ASP 208
SER 227 0.84 MET 133 -0.28 ARG 158
SER 227 0.95 PHE 134 -0.27 ARG 158
SER 227 1.08 CYS 135 -0.36 ARG 158
VAL 225 1.09 GLN 136 -0.44 SER 261
VAL 225 1.10 LEU 137 -0.55 SER 261
VAL 225 1.10 ALA 138 -0.57 SER 261
SER 227 1.20 LYS 139 -0.50 ARG 158
SER 227 1.32 THR 140 -0.51 ARG 158
SER 227 1.25 CYS 141 -0.58 ARG 158
SER 227 1.25 PRO 142 -0.53 ARG 158
SER 227 0.77 VAL 143 -0.47 ARG 158
SER 227 0.54 GLN 144 -0.42 ARG 209
PRO 151 0.37 LEU 145 -0.62 ASP 208
PHE 113 0.63 TRP 146 -0.86 ARG 209
PRO 128 0.62 VAL 147 -1.07 ARG 209
PRO 128 0.67 ASP 148 -1.15 ARG 209
PRO 128 0.54 SER 149 -1.23 ARG 209
PRO 128 0.49 THR 150 -1.14 ARG 209
PRO 128 0.46 PRO 151 -1.20 ARG 209
ALA 129 0.37 PRO 152 -1.12 ARG 209
ALA 129 0.28 PRO 153 -0.90 ARG 209
LYS 101 0.26 GLY 154 -0.85 ASP 208
THR 230 0.34 THR 155 -1.02 ASP 208
SER 99 0.35 ARG 156 -0.83 ASP 208
SER 99 0.44 VAL 157 -0.69 ASP 208
SER 99 0.72 ARG 158 -0.74 TYR 234
THR 231 0.59 ALA 159 -0.49 ASP 208
THR 231 0.52 MET 160 -0.61 GLY 262
SER 227 0.51 ALA 161 -0.54 GLY 262
SER 227 0.44 ILE 162 -0.47 ASN 263
SER 227 0.46 TYR 163 -0.41 SER 261
LEU 289 0.45 LYS 164 -0.29 SER 99
LEU 289 0.46 GLN 165 -0.30 SER 99
LEU 289 0.43 SER 166 -0.28 SER 96
GLY 226 0.45 GLN 167 -0.32 SER 261
GLY 226 0.47 HIS 168 -0.42 SER 261
GLY 226 0.39 MET 169 -0.39 ASN 263
GLY 226 0.39 THR 170 -0.56 ASN 263
GLY 226 0.48 GLU 171 -0.69 ASN 263
GLY 226 0.48 VAL 172 -0.83 ASN 263
VAL 225 0.54 VAL 173 -0.74 GLY 262
VAL 225 0.63 ARG 174 -0.83 SER 261
VAL 225 0.77 ARG 175 -0.79 SER 261
VAL 225 0.82 CYS 176 -0.73 SER 261
VAL 225 0.86 PRO 177 -0.78 SER 261
VAL 225 1.00 HIS 178 -0.71 SER 261
VAL 225 1.01 HIS 179 -0.73 SER 261
VAL 225 0.90 GLU 180 -0.84 SER 261
VAL 225 1.00 ARG 181 -0.80 SER 261
VAL 225 1.14 CYS 182 -0.71 SER 261
VAL 225 1.00 SER 185 -0.72 SER 261
GLU 224 0.98 ASP 186 -0.70 SER 261
GLU 224 0.85 GLY 187 -0.82 SER 261
GLU 224 0.85 LEU 188 -0.88 SER 261
GLU 224 0.81 ALA 189 -0.93 SER 261
GLU 224 0.68 PRO 190 -1.13 SER 261
VAL 225 0.79 PRO 191 -0.98 SER 261
VAL 225 0.69 GLN 192 -1.00 SER 261
GLU 224 0.66 HIS 193 -0.95 SER 261
VAL 225 0.71 LEU 194 -0.76 SER 261
GLU 224 0.72 ILE 195 -0.69 SER 261
GLU 224 0.87 ARG 196 -0.68 SER 261
GLU 224 0.97 VAL 197 -0.54 SER 261
GLU 224 1.24 GLU 198 -0.50 SER 261
GLU 224 1.46 GLY 199 -0.37 SER 261
GLU 224 1.10 ASN 200 -0.36 SER 261
GLU 224 0.95 LEU 201 -0.43 SER 261
GLU 224 0.71 ARG 202 -0.50 SER 261
GLU 224 0.76 VAL 203 -0.67 SER 261
GLU 224 0.58 GLU 204 -0.96 SER 260
GLU 224 0.61 TYR 205 -1.17 SER 261
SER 96 0.61 LEU 206 -1.57 GLY 262
SER 96 0.52 ASP 207 -1.54 GLY 262
GLN 192 0.34 ASP 208 -1.75 LEU 264
PRO 177 0.55 ARG 209 -1.65 SER 106
PRO 177 0.51 ASN 210 -1.58 SER 106
GLY 226 0.33 THR 211 -1.22 LEU 264
GLN 192 0.69 PHE 212 -1.31 ASN 263
SER 96 0.63 ARG 213 -1.13 ASN 263
SER 96 0.56 HIS 214 -1.17 GLY 262
SER 96 0.58 SER 215 -0.99 GLY 262
THR 231 0.60 VAL 216 -0.86 GLY 262
SER 99 0.55 VAL 217 -0.55 SER 261
GLU 224 0.46 VAL 218 -0.47 HIS 233
SER 99 0.36 PRO 219 -0.50 ASP 208
THR 230 0.39 TYR 220 -0.67 ASP 208
ASN 200 0.47 GLU 221 -0.60 ARG 209
GLY 199 0.38 PRO 222 -0.78 ARG 209
GLY 199 0.61 PRO 223 -0.65 ARG 209
GLY 199 1.46 GLU 224 -0.81 SER 227
SER 121 1.16 VAL 225 -0.45 SER 149
HIS 178 0.89 GLY 226 -0.21 SER 149
THR 140 1.32 SER 227 -0.81 GLU 224
LEU 114 0.76 ASP 228 -0.72 ASN 210
PHE 113 0.56 CYS 229 -0.54 ARG 209
ASN 200 0.58 THR 230 -0.40 ARG 209
ILE 232 0.91 THR 231 -0.21 ASN 210
THR 231 0.91 ILE 232 -0.19 PRO 219
GLU 224 1.06 HIS 233 -0.67 ARG 158
SER 227 0.88 TYR 234 -0.74 ARG 158
SER 227 0.99 ASN 235 -0.63 ARG 158
SER 227 0.90 TYR 236 -0.60 SER 261
VAL 225 0.93 MET 237 -0.68 SER 261
VAL 225 0.92 CYS 238 -0.63 SER 261
VAL 225 0.92 ASN 239 -0.54 SER 261
VAL 225 0.80 SER 240 -0.47 SER 261
VAL 225 0.84 SER 241 -0.48 SER 261
VAL 225 0.86 CYS 242 -0.56 SER 261
VAL 225 0.73 GLY 245 -0.67 SER 261
VAL 225 0.68 MET 246 -0.57 SER 261
VAL 225 0.73 ASN 247 -0.51 SER 261
VAL 225 0.71 ARG 248 -0.42 SER 261
VAL 225 0.61 ARG 249 -0.41 SER 261
SER 227 0.58 PRO 250 -0.33 SER 261
SER 227 0.58 ILE 251 -0.37 SER 261
SER 227 0.52 LEU 252 -0.29 ASP 208
SER 227 0.54 THR 253 -0.37 ASP 208
ILE 232 0.48 ILE 254 -0.60 ASP 208
THR 231 0.49 ILE 255 -0.72 ASP 208
LYS 101 0.44 THR 256 -1.08 ASP 208
THR 230 0.38 LEU 257 -1.23 ASP 208
LYS 101 0.44 GLU 258 -1.35 ASP 208
LYS 101 0.35 ASP 259 -1.23 ASP 208
LYS 101 0.33 SER 260 -1.17 LEU 206
LYS 101 0.32 SER 261 -1.32 LEU 206
LYS 101 0.44 GLY 262 -1.57 LEU 206
LYS 101 0.44 ASN 263 -1.51 ASP 207
LYS 101 0.49 LEU 264 -1.75 ASP 208
ALA 129 0.44 LEU 265 -1.70 ASP 208
ALA 129 0.50 GLY 266 -1.47 ASP 208
ALA 129 0.43 ARG 267 -1.14 ASP 208
ASN 131 0.48 ASN 268 -0.78 ASP 208
LEU 289 0.38 SER 269 -0.54 PHE 113
SER 227 0.48 PHE 270 -0.52 PHE 113
SER 227 0.60 GLU 271 -0.27 ASP 208
SER 227 0.76 VAL 272 -0.29 SER 261
SER 227 0.80 ARG 273 -0.33 SER 261
SER 227 0.89 VAL 274 -0.43 SER 261
VAL 225 0.97 CYS 275 -0.41 SER 261
VAL 225 1.08 ALA 276 -0.42 SER 261
VAL 225 1.02 CYS 277 -0.32 SER 261
SER 227 0.95 PRO 278 -0.28 SER 261
SER 227 0.92 GLY 279 -0.23 ARG 158
VAL 225 0.86 ARG 280 -0.20 SER 261
VAL 225 0.80 ASP 281 -0.21 SER 261
SER 227 0.77 TRP 282 -0.15 ARG 158
SER 227 0.70 ARG 283 -0.15 GLY 279
VAL 225 0.68 THR 284 -0.16 GLU 287
SER 227 0.62 GLU 285 -0.13 ALA 129
SER 227 0.59 GLU 286 -0.15 LEU 289
GLY 108 0.61 GLU 287 -0.18 ARG 280
SER 227 0.53 ASN 288 -0.10 THR 284
GLN 104 0.58 LEU 289 -0.15 GLU 286

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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.