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CA distance fluctuations for 2402161531523054209

---  normal mode 7  ---

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 181 0.23 SER 96 -1.15 PRO 128
GLN 167 0.15 VAL 97 -1.04 GLY 187
GLN 167 0.52 PRO 98 -1.22 LEU 201
SER 166 0.58 SER 99 -1.62 VAL 217
THR 256 0.16 GLN 100 -0.95 ASP 208
ALA 129 0.22 LYS 101 -1.31 ASP 208
ALA 129 0.18 THR 102 -1.35 THR 211
ALA 129 0.13 TYR 103 -1.58 ASP 208
ALA 129 0.13 GLN 104 -1.45 ASP 208
ALA 129 0.10 GLY 105 -1.59 ASP 208
ALA 129 0.10 SER 106 -1.40 ASP 208
LEU 201 0.12 TYR 107 -1.28 ASP 208
PRO 128 0.13 GLY 108 -1.25 ASP 208
LEU 201 0.15 PHE 109 -1.24 ASP 208
PRO 128 0.16 ARG 110 -1.08 ASP 208
ASN 200 0.17 LEU 111 -0.97 SER 96
PRO 128 0.18 GLY 112 -1.03 SER 96
ASN 200 0.17 PHE 113 -0.98 SER 96
ASN 200 0.16 LEU 114 -0.99 SER 96
ASP 207 0.21 VAL 122 -0.71 SER 96
ASP 207 0.26 THR 123 -0.63 SER 96
TYR 205 0.21 CYS 124 -0.71 SER 96
TYR 205 0.19 THR 125 -0.83 SER 96
TYR 205 0.17 TYR 126 -0.93 SER 96
TYR 205 0.15 SER 127 -1.01 SER 96
LYS 101 0.19 PRO 128 -1.15 SER 96
LYS 101 0.22 ALA 129 -1.15 SER 96
LYS 101 0.20 LEU 130 -0.99 SER 96
LYS 101 0.19 ASN 131 -0.98 SER 96
TYR 205 0.15 LYS 132 -0.84 SER 96
TYR 205 0.19 MET 133 -0.78 SER 96
TYR 205 0.19 MET 133 -0.77 SER 96
TYR 205 0.19 PHE 134 -0.69 SER 96
ASP 207 0.24 CYS 135 -0.60 SER 96
ASP 207 0.35 GLN 136 -0.59 VAL 97
PHE 212 0.49 LEU 137 -0.64 VAL 97
ASP 207 0.55 ALA 138 -0.74 VAL 97
ASP 207 0.41 LYS 139 -0.73 VAL 97
TYR 205 0.32 THR 140 -0.73 VAL 97
TYR 205 0.27 CYS 141 -0.70 SER 99
TYR 205 0.27 CYS 141 -0.70 SER 99
TYR 205 0.23 PRO 142 -0.76 SER 99
ASN 200 0.21 VAL 143 -0.79 SER 99
ASN 200 0.23 GLN 144 -0.87 SER 96
ASN 200 0.21 LEU 145 -0.87 ASP 208
LEU 201 0.18 TRP 146 -0.98 SER 96
LEU 201 0.16 VAL 147 -1.06 ASP 208
PRO 128 0.13 ASP 148 -1.06 ASN 210
LEU 201 0.11 SER 149 -1.05 ASP 208
LEU 201 0.11 THR 150 -1.01 ASP 208
PRO 222 0.25 PRO 151 -1.09 ASP 208
GLU 221 0.15 PRO 152 -0.98 SER 99
GLU 221 0.13 PRO 153 -1.09 SER 99
GLU 221 0.10 GLY 154 -1.28 SER 99
LEU 201 0.09 THR 155 -1.34 SER 99
GLN 100 0.08 ARG 156 -1.61 SER 99
PHE 270 0.09 VAL 157 -1.47 SER 99
GLN 100 0.07 ARG 158 -1.38 SER 99
HIS 214 0.18 ALA 159 -1.04 SER 99
HIS 214 0.16 MET 160 -0.79 SER 99
VAL 172 0.15 ALA 161 -0.48 SER 99
VAL 172 0.07 ILE 162 -0.62 ARG 213
MET 169 0.15 TYR 163 -0.50 ARG 213
SER 99 0.22 LYS 164 -0.53 THR 211
SER 99 0.43 GLN 165 -0.50 THR 211
SER 99 0.58 SER 166 -0.63 THR 211
SER 99 0.58 SER 166 -0.63 THR 211
PRO 98 0.52 GLN 167 -0.51 ARG 213
GLY 245 0.45 HIS 168 -0.53 ARG 213
GLY 245 0.35 MET 169 -0.85 ARG 213
PRO 98 0.30 THR 170 -0.79 ARG 213
GLY 245 0.22 GLU 171 -0.42 ARG 213
ALA 161 0.15 VAL 172 -0.33 HIS 214
PHE 212 0.18 VAL 173 -0.31 SER 99
PHE 212 0.51 ARG 174 -0.44 SER 99
PHE 212 0.76 ARG 175 -0.51 VAL 97
PHE 212 0.88 CYS 176 -0.48 VAL 97
PHE 212 1.13 PRO 177 -0.53 VAL 97
PHE 212 1.12 HIS 178 -0.61 VAL 97
PHE 212 1.06 HIS 179 -0.67 VAL 97
PHE 212 1.24 GLU 180 -0.68 VAL 97
PHE 212 1.47 ARG 181 -0.75 VAL 97
PHE 212 1.00 SER 185 -0.95 VAL 97
PHE 212 0.74 ASP 186 -1.03 SER 99
ASP 207 0.85 GLY 187 -1.04 VAL 97
ASP 207 0.73 LEU 188 -1.16 SER 99
ASP 207 0.88 ALA 189 -1.12 SER 99
ASP 207 1.44 PRO 190 -0.91 SER 99
ASP 207 1.46 PRO 191 -0.76 VAL 97
ASP 207 1.13 GLN 192 -0.64 SER 99
ASP 207 0.83 HIS 193 -0.80 SER 99
ASP 207 0.57 LEU 194 -0.66 SER 99
ASP 207 0.39 ILE 195 -0.83 SER 99
TYR 205 0.64 ARG 196 -0.97 SER 99
TYR 205 0.59 VAL 197 -1.11 SER 99
TYR 205 0.53 GLU 198 -0.99 SER 99
TYR 205 0.37 GLY 199 -1.10 PRO 98
ILE 232 0.37 ASN 200 -1.16 SER 99
GLU 224 0.31 LEU 201 -1.22 PRO 98
THR 231 0.16 ARG 202 -1.34 SER 99
ILE 232 0.19 VAL 203 -1.39 SER 99
GLU 198 0.22 GLU 204 -1.47 SER 99
ARG 196 0.64 TYR 205 -1.28 SER 99
PRO 190 0.45 LEU 206 -1.27 SER 99
PRO 191 1.46 ASP 207 -1.27 ASN 263
ARG 181 0.82 ASP 208 -1.59 GLY 105
ARG 181 0.85 ARG 209 -1.28 SER 106
ARG 181 0.69 ASN 210 -1.26 SER 106
ARG 181 0.81 THR 211 -1.47 TYR 103
ARG 181 1.47 PHE 212 -1.13 LEU 264
GLN 192 0.70 ARG 213 -0.85 MET 169
ILE 195 0.30 HIS 214 -0.86 SER 99
HIS 214 0.28 SER 215 -1.11 SER 99
ALA 159 0.15 VAL 216 -1.32 SER 99
HIS 214 0.05 VAL 217 -1.62 SER 99
PHE 270 0.12 VAL 218 -1.60 SER 99
LEU 201 0.12 PRO 219 -1.52 SER 99
LEU 201 0.18 TYR 220 -1.33 SER 99
LEU 201 0.27 GLU 221 -1.16 SER 99
LEU 201 0.27 PRO 222 -1.06 PRO 98
LEU 201 0.28 PRO 223 -1.03 PRO 98
LEU 201 0.31 GLU 224 -1.14 PRO 98
LEU 201 0.26 VAL 225 -1.14 PRO 98
LEU 201 0.23 GLY 226 -1.02 PRO 98
LEU 201 0.24 SER 227 -0.95 PRO 98
LEU 201 0.21 ASP 228 -1.00 SER 96
LEU 201 0.23 CYS 229 -0.93 SER 96
LEU 201 0.28 THR 230 -0.94 SER 99
ASN 200 0.32 THR 231 -0.92 SER 99
ASN 200 0.37 ILE 232 -1.04 SER 99
TYR 205 0.34 HIS 233 -0.93 SER 99
TYR 205 0.37 TYR 234 -0.91 SER 99
ASP 207 0.41 ASN 235 -0.78 SER 99
ASP 207 0.44 TYR 236 -0.65 SER 99
ASP 207 0.66 MET 237 -0.65 VAL 97
PHE 212 0.61 CYS 238 -0.55 VAL 97
PHE 212 0.61 CYS 238 -0.55 VAL 97
PHE 212 0.49 ASN 239 -0.47 VAL 97
PHE 212 0.33 SER 240 -0.35 VAL 97
PHE 212 0.44 SER 241 -0.34 VAL 97
PHE 212 0.60 CYS 242 -0.39 VAL 97
PHE 212 0.42 MET 243 -0.31 VAL 97
HIS 168 0.44 GLY 244 -0.19 VAL 97
HIS 168 0.45 GLY 245 -0.16 VAL 97
GLN 167 0.46 MET 246 -0.15 GLN 100
GLN 167 0.49 ASN 247 -0.27 SER 96
GLN 167 0.37 ARG 248 -0.31 SER 96
HIS 168 0.39 ARG 249 -0.32 SER 96
HIS 168 0.23 PRO 250 -0.44 SER 96
ILE 195 0.14 ILE 251 -0.43 SER 96
ILE 195 0.15 LEU 252 -0.53 SER 96
ILE 195 0.18 THR 253 -0.54 ASP 208
ILE 254 0.08 ILE 254 -0.79 ASP 208
ILE 254 0.08 ILE 254 -0.79 ASP 208
VAL 216 0.11 ILE 255 -0.87 ASP 208
GLN 100 0.16 THR 256 -1.11 ASP 208
GLN 100 0.16 THR 256 -1.11 ASP 208
GLN 100 0.13 LEU 257 -1.17 ASP 208
GLN 100 0.11 GLU 258 -1.24 SER 99
GLN 100 0.09 ASP 259 -1.20 SER 99
GLN 100 0.07 SER 260 -1.28 SER 99
GLN 100 0.06 SER 261 -1.12 SER 99
GLN 100 0.07 GLY 262 -1.23 ASP 207
GLN 100 0.09 ASN 263 -1.27 ASP 207
GLN 100 0.13 LEU 264 -1.47 ASP 208
GLN 100 0.12 LEU 265 -1.54 ASP 208
GLN 100 0.12 GLY 266 -1.55 ASP 208
GLN 100 0.14 ARG 267 -1.38 ASP 208
ASN 200 0.12 ASN 268 -1.13 ASP 208
ILE 195 0.12 SER 269 -0.88 ASP 208
ILE 195 0.19 PHE 270 -0.79 SER 96
ILE 195 0.19 GLU 271 -0.70 SER 96
ILE 195 0.23 VAL 272 -0.61 SER 96
ILE 195 0.23 VAL 272 -0.61 SER 96
ASP 207 0.18 ARG 273 -0.54 SER 96
ASP 207 0.29 VAL 274 -0.45 SER 96
PHE 212 0.33 CYS 275 -0.46 SER 96
PHE 212 0.39 ALA 276 -0.52 VAL 97
PHE 212 0.29 CYS 277 -0.56 SER 96
PHE 212 0.29 CYS 277 -0.56 SER 96
ASP 207 0.20 PRO 278 -0.66 SER 96
ASP 207 0.16 GLY 279 -0.75 SER 96
GLN 167 0.17 ARG 280 -0.70 SER 96
GLN 167 0.20 ASP 281 -0.68 SER 96
GLN 167 0.16 ARG 282 -0.81 SER 96
GLN 167 0.17 ARG 283 -0.84 SER 96
GLN 167 0.23 THR 284 -0.75 SER 96
GLN 167 0.23 GLU 285 -0.78 SER 96
GLN 167 0.18 GLU 286 -0.93 SER 96
GLN 167 0.21 GLU 287 -0.89 SER 96

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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.