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CA distance fluctuations for 240415002639235721

---  normal mode 9  ---

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
SER 215 0.75 VAL 97 -0.45 TYR 103
SER 215 0.86 PRO 98 -0.61 TYR 103
ARG 158 0.89 SER 99 -0.56 ASN 131
SER 166 0.67 GLN 100 -0.63 ASP 208
SER 166 0.78 LYS 101 -0.74 ASP 208
SER 166 0.76 THR 102 -1.11 ASP 208
SER 166 0.49 TYR 103 -1.37 ASP 208
SER 166 0.43 GLN 104 -1.64 ASP 208
SER 166 0.34 GLY 105 -1.68 ASP 208
GLY 226 0.46 SER 106 -1.72 ASP 208
VAL 225 0.46 TYR 107 -1.80 ASP 208
ASN 131 0.45 GLY 108 -1.84 ASP 208
ASN 131 0.48 PHE 109 -1.62 ASP 208
ASN 131 0.66 ARG 110 -1.36 ASP 208
ASN 131 0.59 LEU 111 -1.10 ASP 208
ASN 131 0.61 GLY 112 -0.97 ASP 208
ASP 228 0.42 PHE 113 -0.82 ASP 208
ASP 228 0.30 LEU 114 -0.70 ASP 208
ASP 228 0.24 HIS 115 -0.59 GLY 226
CYS 229 0.16 SER 116 -0.80 GLY 226
PHE 212 0.36 SER 121 -0.86 GLY 226
PHE 212 0.28 VAL 122 -0.83 GLY 226
PHE 212 0.31 THR 123 -0.93 GLY 226
PHE 212 0.19 CYS 124 -0.80 GLY 226
ASP 228 0.24 THR 125 -0.61 GLY 226
GLY 112 0.35 TYR 126 -0.57 ASP 208
GLY 112 0.45 SER 127 -0.54 ASP 208
GLY 112 0.51 PRO 128 -0.66 LYS 101
ASP 148 0.45 ALA 129 -0.60 LYS 101
ARG 110 0.50 LEU 130 -0.53 SER 99
ARG 110 0.66 ASN 131 -0.66 LYS 101
GLY 112 0.53 LYS 132 -0.49 ASP 208
GLY 112 0.38 MET 133 -0.52 GLY 226
GLY 112 0.27 PHE 134 -0.63 GLY 226
PHE 212 0.28 CYS 135 -0.80 GLY 226
PHE 212 0.44 GLN 136 -0.93 GLY 226
PHE 212 0.56 LEU 137 -0.99 GLY 226
PHE 212 0.54 ALA 138 -1.13 GLY 226
PHE 212 0.41 LYS 139 -1.16 GLY 226
PHE 212 0.26 THR 140 -1.15 GLY 226
LEU 111 0.12 CYS 141 -0.90 GLY 226
GLU 221 0.16 PRO 142 -0.78 GLY 226
LYS 132 0.27 VAL 143 -0.77 ASP 208
ASN 131 0.37 GLN 144 -0.94 ASP 208
ASN 131 0.40 LEU 145 -1.14 ASP 208
ASN 131 0.52 TRP 146 -1.33 ASP 208
ASN 131 0.47 VAL 147 -1.55 ASP 208
GLY 226 0.49 ASP 148 -1.58 ASP 208
VAL 225 0.69 SER 149 -1.55 ASP 208
VAL 225 0.69 THR 150 -1.41 ASP 208
VAL 225 0.56 PRO 151 -1.41 ASP 208
VAL 225 0.69 PRO 152 -1.23 ASP 208
VAL 225 0.51 PRO 153 -1.07 ASP 208
SER 99 0.34 GLY 154 -0.95 ASP 208
SER 99 0.36 THR 155 -1.10 ASP 208
SER 99 0.50 ARG 156 -0.96 ASP 208
SER 99 0.55 VAL 157 -0.94 ASP 208
SER 99 0.89 ARG 158 -0.68 ASP 208
SER 99 0.66 ALA 159 -0.61 GLY 226
SER 99 0.52 MET 160 -0.55 GLY 226
ARG 196 0.24 ALA 161 -0.54 GLY 226
LYS 101 0.24 ILE 162 -0.47 GLY 262
SER 269 0.35 TYR 163 -0.41 GLY 226
SER 269 0.44 LYS 164 -0.44 SER 99
THR 102 0.53 GLN 165 -0.33 SER 166
LYS 101 0.78 SER 166 -0.43 ASN 247
THR 102 0.53 GLN 167 -0.37 ASN 247
LYS 101 0.39 HIS 168 -0.40 SER 261
LYS 101 0.46 MET 169 -0.36 SER 261
LYS 101 0.26 THR 170 -0.60 ASN 263
ARG 249 0.50 GLU 171 -0.79 SER 261
MET 243 0.68 VAL 172 -1.00 GLY 262
SER 240 0.46 VAL 173 -0.74 GLY 262
PHE 212 0.56 ARG 174 -0.68 SER 261
PHE 212 0.78 ARG 175 -0.75 GLY 226
PHE 212 0.98 CYS 176 -0.74 GLY 226
PHE 212 1.28 PRO 177 -0.74 GLY 226
PHE 212 1.23 HIS 178 -0.81 GLY 226
PHE 212 1.04 HIS 179 -0.87 GLY 226
PHE 212 1.11 GLU 180 -0.84 GLY 226
PHE 212 1.24 ARG 181 -0.89 GLY 226
PHE 212 0.52 ASP 186 -1.12 GLY 226
ASP 207 0.58 GLY 187 -1.00 GLY 226
ASP 207 0.57 LEU 188 -0.98 GLY 226
ASP 207 0.68 ALA 189 -0.93 GLY 226
ASP 207 0.78 PRO 190 -0.81 GLY 226
PHE 212 0.82 PRO 191 -0.83 GLY 226
ASP 207 0.83 GLN 192 -0.77 GLY 226
ASP 207 0.55 HIS 193 -0.76 GLY 226
PHE 212 0.45 LEU 194 -0.80 GLY 226
SER 99 0.30 ILE 195 -0.84 GLY 226
SER 99 0.40 ARG 196 -0.99 GLY 226
SER 99 0.42 VAL 197 -1.05 GLY 226
SER 99 0.32 GLU 198 -1.28 GLY 226
SER 99 0.31 GLY 199 -1.33 GLY 226
SER 99 0.40 ASN 200 -1.11 VAL 225
SER 99 0.43 LEU 201 -1.04 VAL 225
SER 99 0.53 ARG 202 -0.81 VAL 225
SER 99 0.58 VAL 203 -0.86 GLY 226
SER 99 0.67 GLU 204 -0.74 GLY 226
SER 99 0.59 TYR 205 -0.74 GLY 226
PRO 98 0.75 LEU 206 -0.98 SER 261
GLN 192 0.83 ASP 207 -1.94 GLY 262
PRO 177 0.61 ASP 208 -1.84 GLY 108
ARG 181 0.56 ARG 209 -1.04 SER 106
HIS 178 0.37 ASN 210 -0.83 ASP 148
PRO 177 0.77 THR 211 -1.50 LEU 264
PRO 177 1.28 PHE 212 -1.24 LEU 265
GLN 192 0.49 ARG 213 -1.28 GLY 262
VAL 97 0.58 HIS 214 -1.03 GLY 262
PRO 98 0.86 SER 215 -0.73 GLY 226
SER 99 0.68 VAL 216 -0.74 GLY 226
SER 99 0.75 VAL 217 -0.67 GLY 226
SER 99 0.59 VAL 218 -0.62 GLY 226
SER 99 0.49 PRO 219 -0.80 ASP 208
SER 99 0.37 TYR 220 -1.03 ASP 208
SER 99 0.27 GLU 221 -1.01 ASP 208
PRO 152 0.34 PRO 222 -1.09 ASP 208
PRO 152 0.30 PRO 223 -1.03 ASP 208
SER 227 0.43 GLU 224 -0.91 ASP 208
SER 149 0.69 VAL 225 -1.25 GLY 199
SER 149 0.64 GLY 226 -1.33 GLY 199
GLU 224 0.43 SER 227 -0.95 ASP 208
PRO 128 0.48 ASP 228 -1.03 ASP 208
PHE 113 0.39 CYS 229 -1.12 ASP 208
ASN 131 0.28 THR 230 -1.04 ASP 208
ASN 131 0.20 THR 231 -0.89 ASP 208
ASN 131 0.20 ILE 232 -0.73 GLY 226
SER 99 0.18 HIS 233 -0.99 GLY 226
SER 99 0.24 TYR 234 -0.98 GLY 226
PHE 212 0.32 ASN 235 -1.05 GLY 226
PHE 212 0.39 TYR 236 -0.91 GLY 226
PHE 212 0.60 MET 237 -0.95 GLY 226
PHE 212 0.67 CYS 238 -0.85 GLY 226
PHE 212 0.67 CYS 238 -0.85 GLY 226
PHE 212 0.61 ASN 239 -0.79 GLY 226
VAL 172 0.48 SER 240 -0.66 GLY 226
PHE 212 0.58 SER 241 -0.66 GLY 226
PHE 212 0.73 CYS 242 -0.71 GLY 226
VAL 172 0.68 MET 243 -0.64 GLY 226
VAL 172 0.49 GLY 244 -0.55 GLY 226
GLU 171 0.49 GLY 245 -0.53 GLY 226
ASN 288 0.54 MET 246 -0.47 GLY 226
ASN 288 0.65 ASN 247 -0.43 SER 166
ASN 288 0.57 ARG 248 -0.47 GLY 226
GLU 171 0.50 ARG 249 -0.45 GLY 226
LEU 289 0.44 PRO 250 -0.44 GLY 226
LEU 289 0.33 ILE 251 -0.48 GLY 226
SER 269 0.35 LEU 252 -0.44 PRO 98
VAL 197 0.25 THR 253 -0.51 ASP 208
SER 166 0.35 ILE 254 -0.69 ASP 208
SER 99 0.33 ILE 255 -0.88 ASP 208
SER 99 0.52 THR 256 -1.03 ASP 208
SER 99 0.41 LEU 257 -1.23 ASP 208
SER 99 0.47 GLU 258 -1.19 ASP 207
SER 99 0.37 ASP 259 -1.25 ASP 207
SER 99 0.39 SER 260 -1.28 ASP 207
SER 99 0.33 SER 261 -1.49 ASP 207
SER 99 0.49 GLY 262 -1.94 ASP 207
LYS 101 0.36 ASN 263 -1.52 ASP 207
LYS 101 0.43 LEU 264 -1.50 THR 211
LYS 101 0.27 LEU 265 -1.37 ASP 208
SER 166 0.33 GLY 266 -1.44 ASP 208
SER 166 0.38 ARG 267 -1.20 ASP 208
SER 166 0.50 ASN 268 -1.08 ASP 208
SER 166 0.56 SER 269 -0.80 ASP 208
ARG 110 0.44 PHE 270 -0.64 ASP 208
LEU 111 0.42 GLU 271 -0.49 PRO 98
LEU 111 0.35 VAL 272 -0.52 GLY 226
VAL 173 0.29 ARG 273 -0.60 GLY 226
PHE 212 0.39 VAL 274 -0.75 GLY 226
PHE 212 0.47 CYS 275 -0.77 GLY 226
PHE 212 0.54 ALA 276 -0.83 GLY 226
PHE 212 0.43 CYS 277 -0.76 GLY 226
PHE 212 0.30 PRO 278 -0.70 GLY 226
PHE 212 0.25 GLY 279 -0.63 GLY 226
PHE 212 0.30 ARG 280 -0.59 GLY 226
PHE 212 0.29 ASP 281 -0.56 GLY 226
ASP 148 0.27 ARG 282 -0.48 GLY 226
ASP 148 0.28 ARG 283 -0.44 GLY 226
ASN 247 0.35 THR 284 -0.43 GLY 226
ARG 248 0.44 GLU 285 -0.36 GLY 226
ASN 247 0.39 GLU 286 -0.34 SER 99
ASN 247 0.47 GLU 287 -0.32 GLY 226
ASN 247 0.65 ASN 288 -0.28 GLY 226
ASN 247 0.60 LEU 289 -0.30 SER 99
ASN 247 0.58 ARG 290 -0.25 ASP 208

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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.