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CA distance fluctuations for 2404131437433984339

---  normal mode 16  ---

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
GLY 245 1.12 SER 96 -0.87 LEU 206
CYS 182 1.87 VAL 97 -0.53 ASN 288
ASN 210 0.43 PRO 98 -1.14 GLU 171
GLN 165 0.55 SER 99 -1.58 PRO 153
ASN 210 0.50 GLN 100 -1.37 MET 169
ASN 210 0.66 LYS 101 -1.37 SER 166
ASN 210 0.76 THR 102 -1.33 LEU 289
ASN 210 0.98 TYR 103 -1.35 LEU 289
ASN 210 1.02 GLN 104 -1.40 LEU 289
ASN 210 1.17 GLY 105 -1.25 LEU 289
ASN 210 1.19 SER 106 -1.16 LEU 289
ASN 210 1.10 TYR 107 -1.13 LEU 289
ASN 210 1.00 GLY 108 -1.24 LEU 289
ASN 210 1.00 PHE 109 -1.26 LEU 289
ASN 210 0.84 ARG 110 -1.31 LEU 289
ASN 210 0.74 LEU 111 -1.43 ASN 131
PRO 151 0.85 GLY 112 -1.61 PRO 128
PRO 151 0.70 PHE 113 -1.21 PRO 128
PRO 151 0.80 LEU 114 -0.77 GLY 226
PRO 151 0.97 SER 121 -0.99 CYS 182
PRO 151 0.79 VAL 122 -0.70 PRO 191
PRO 151 0.71 THR 123 -0.87 PRO 191
PRO 151 0.72 CYS 124 -0.83 PRO 191
PRO 151 0.57 THR 125 -0.75 PRO 191
PRO 151 0.42 TYR 126 -0.87 VAL 143
ARG 248 0.51 SER 127 -1.21 GLY 112
GLN 165 0.52 PRO 128 -1.61 GLY 112
GLN 165 0.69 ALA 129 -1.20 GLY 112
ARG 248 0.93 LEU 130 -1.08 ARG 110
GLN 165 0.66 ASN 131 -1.43 LEU 111
PRO 250 0.53 LYS 132 -1.03 GLU 285
PRO 151 0.42 MET 133 -0.64 PRO 191
VAL 97 0.52 PHE 134 -0.65 PRO 191
VAL 97 0.69 CYS 135 -0.74 PRO 191
VAL 97 0.82 GLN 136 -0.79 CYS 182
VAL 97 0.99 LEU 137 -0.85 CYS 182
VAL 97 1.05 ALA 138 -1.12 PRO 191
VAL 97 0.89 LYS 139 -1.19 PRO 191
TYR 205 0.83 THR 140 -1.25 PRO 191
PRO 151 0.77 CYS 141 -0.99 PRO 191
PRO 151 0.96 PRO 142 -0.89 PRO 191
PRO 151 0.90 VAL 143 -1.04 PRO 128
PRO 151 1.08 GLN 144 -1.32 PRO 128
PRO 151 0.96 LEU 145 -1.21 PRO 128
PRO 151 0.93 TRP 146 -1.26 PRO 128
ASN 210 0.88 VAL 147 -1.10 LEU 289
ASN 210 0.83 ASP 148 -0.94 LEU 289
ASN 210 0.78 SER 149 -1.11 SER 99
ASN 210 0.53 THR 150 -1.57 THR 155
SER 227 1.64 PRO 151 -0.97 SER 99
PRO 222 1.76 PRO 152 -1.33 SER 99
ASN 210 1.05 PRO 153 -1.58 SER 99
ASN 210 1.16 GLY 154 -1.50 SER 99
ASN 210 1.25 THR 155 -1.57 THR 150
ARG 209 1.29 ARG 156 -1.43 THR 150
ASP 208 1.21 VAL 157 -1.13 THR 150
ASP 208 1.22 ARG 158 -1.00 THR 170
ASP 208 0.84 ALA 159 -0.85 THR 170
ASP 208 0.60 MET 160 -0.87 PRO 98
VAL 97 0.59 ALA 161 -0.67 ASN 288
SER 96 0.73 ILE 162 -0.72 ASN 288
SER 96 0.91 TYR 163 -0.70 ASN 288
SER 96 0.81 LYS 164 -0.89 ASN 288
LEU 130 0.72 GLN 165 -0.64 ASN 288
ASN 247 0.80 SER 166 -1.37 LYS 101
SER 185 1.25 GLN 167 -0.78 LYS 101
ASN 247 1.50 HIS 168 -0.78 PRO 98
GLY 245 1.02 MET 169 -1.37 GLN 100
PRO 177 0.73 THR 170 -1.48 ASN 263
GLY 245 1.35 GLU 171 -1.14 PRO 98
SER 96 0.76 VAL 172 -0.66 MET 246
SER 96 0.84 VAL 173 -0.57 VAL 172
VAL 97 1.03 ARG 174 -0.58 LEU 201
VAL 97 1.23 ARG 175 -0.61 LEU 201
VAL 97 1.18 CYS 176 -0.70 SER 121
VAL 97 1.20 PRO 177 -0.79 LEU 201
VAL 97 1.36 HIS 178 -0.82 SER 121
VAL 97 1.61 HIS 179 -0.85 SER 121
VAL 97 1.52 GLU 180 -0.87 ALA 138
VAL 97 1.60 ARG 181 -0.83 ALA 138
VAL 97 1.87 CYS 182 -0.99 SER 121
GLN 167 1.25 SER 185 -0.79 ASN 200
HIS 178 0.94 ASP 186 -1.25 SER 99
VAL 97 1.06 GLY 187 -1.33 SER 99
VAL 97 1.16 LEU 188 -1.43 SER 99
VAL 97 1.66 ALA 189 -1.64 ARG 202
VAL 97 1.55 PRO 190 -1.34 LEU 201
VAL 97 1.26 PRO 191 -1.26 GLU 198
VAL 97 1.28 GLN 192 -1.00 LEU 201
VAL 97 1.33 HIS 193 -0.80 VAL 203
VAL 97 1.14 LEU 194 -0.59 THR 150
VAL 97 1.01 ILE 195 -0.66 THR 150
TYR 205 1.14 ARG 196 -0.77 PRO 191
TYR 205 1.29 VAL 197 -0.83 SER 99
TYR 205 1.17 GLU 198 -1.26 PRO 191
TYR 205 0.78 GLY 199 -1.08 PRO 191
PRO 151 1.04 ASN 200 -1.25 ALA 189
GLU 224 1.18 LEU 201 -1.34 PRO 190
GLU 224 0.81 ARG 202 -1.64 ALA 189
ILE 232 0.75 VAL 203 -1.29 ALA 189
GLU 198 0.77 GLU 204 -1.07 SER 261
VAL 197 1.29 TYR 205 -1.13 SER 261
VAL 97 0.95 LEU 206 -1.19 THR 170
VAL 97 0.84 ASP 207 -0.82 PRO 98
VAL 217 1.32 ASP 208 -0.76 GLU 171
GLY 262 1.60 ARG 209 -0.49 GLU 171
ASN 263 1.85 ASN 210 -0.44 PRO 177
GLU 258 1.30 THR 211 -0.56 HIS 168
GLU 258 0.70 PHE 212 -0.65 GLY 245
VAL 97 0.72 ARG 213 -1.08 GLU 171
VAL 97 0.89 HIS 214 -1.06 PRO 98
ASP 208 0.72 SER 215 -1.00 PRO 98
ASP 208 0.89 VAL 216 -0.79 THR 170
ASP 208 1.32 VAL 217 -0.92 ALA 189
ASP 208 1.09 VAL 218 -1.29 ALA 189
ASP 208 1.09 PRO 219 -1.24 SER 99
ARG 209 1.01 TYR 220 -1.22 SER 99
PRO 152 1.12 GLU 221 -1.14 SER 99
PRO 152 1.76 PRO 222 -1.12 SER 99
PRO 151 1.49 PRO 223 -0.99 PRO 128
PRO 151 1.45 GLU 224 -0.97 PRO 128
PRO 151 1.30 VAL 225 -0.96 PRO 128
PRO 151 1.32 GLY 226 -1.06 PRO 128
PRO 151 1.64 SER 227 -1.16 PRO 128
PRO 151 1.49 ASP 228 -1.12 PRO 128
PRO 151 1.53 CYS 229 -1.26 PRO 128
PRO 151 1.37 THR 230 -1.17 PRO 128
PRO 151 1.23 THR 231 -1.10 PRO 128
ASP 208 0.97 ILE 232 -0.88 PRO 128
PRO 151 0.83 HIS 233 -1.06 PRO 191
TYR 205 0.86 TYR 234 -0.99 PRO 191
VAL 97 0.94 ASN 235 -1.15 PRO 191
VAL 97 1.00 TYR 236 -0.77 PRO 191
VAL 97 1.21 MET 237 -0.71 PRO 191
VAL 97 1.15 CYS 238 -0.56 SER 121
VAL 97 0.96 ASN 239 -0.67 SER 121
HIS 168 0.91 SER 240 -0.63 SER 121
HIS 168 1.20 SER 241 -0.82 SER 121
HIS 168 1.33 CYS 242 -0.87 SER 121
GLU 171 1.35 GLY 245 -0.70 SER 121
HIS 168 1.07 MET 246 -0.66 VAL 172
HIS 168 1.50 ASN 247 -0.74 SER 121
HIS 168 1.09 ARG 248 -0.66 SER 121
LEU 130 0.86 ARG 249 -0.66 VAL 172
SER 96 0.76 PRO 250 -0.66 THR 284
SER 96 0.75 ILE 251 -0.71 THR 284
SER 96 0.53 LEU 252 -0.91 GLU 285
PHE 113 0.52 THR 253 -0.83 GLU 285
THR 211 0.70 ILE 254 -0.88 ASN 288
THR 211 0.86 ILE 255 -0.94 LEU 289
THR 211 1.14 THR 256 -1.10 THR 170
ASN 210 1.20 LEU 257 -1.16 THR 150
ASN 210 1.43 GLU 258 -1.31 THR 150
ASN 210 1.53 ASP 259 -1.20 THR 150
ARG 209 1.45 SER 260 -1.20 SER 99
ASN 210 1.50 SER 261 -1.24 THR 170
ASN 210 1.61 GLY 262 -1.36 THR 170
ASN 210 1.85 ASN 263 -1.48 THR 170
ASN 210 1.48 LEU 264 -1.39 THR 170
ASN 210 1.40 LEU 265 -1.18 THR 170
ASN 210 1.18 GLY 266 -1.15 LEU 289
ASN 210 0.97 ARG 267 -1.17 LEU 289
ASN 210 0.78 ASN 268 -1.23 LEU 289
PHE 113 0.68 SER 269 -1.11 GLU 285
PHE 113 0.60 PHE 270 -1.09 GLU 285
PHE 113 0.54 GLU 271 -1.13 GLU 285
PHE 113 0.58 VAL 272 -0.79 GLU 285
VAL 97 0.61 ARG 273 -0.64 ASP 281
VAL 97 0.78 VAL 274 -0.51 PRO 191
VAL 97 0.76 CYS 275 -0.59 SER 121
VAL 97 0.80 ALA 276 -0.71 SER 121
LEU 188 0.69 CYS 277 -0.48 CYS 182
VAL 97 0.58 PRO 278 -0.56 PRO 191
PRO 151 0.51 GLY 279 -0.54 PRO 191
ASP 186 0.61 ARG 280 -0.46 GLU 271
ASP 186 0.62 ASP 281 -0.73 GLU 271
SER 185 0.47 ARG 282 -0.70 LYS 132
ASP 186 0.49 ARG 283 -0.48 GLU 271
ASP 186 0.57 THR 284 -0.90 GLU 271
SER 185 0.54 GLU 285 -1.13 GLU 271
SER 185 0.47 GLU 286 -0.86 GLY 112
SER 185 0.47 GLU 287 -0.76 THR 102
SER 185 0.47 ASN 288 -1.27 THR 102
SER 185 0.38 LEU 289 -1.40 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.