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CA distance fluctuations for 2404260424312878936

---  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
GLU 171 1.07 VAL 97 -0.73 ASN 288
ARG 213 0.79 PRO 98 -1.04 ILE 254
ARG 213 0.64 SER 99 -1.07 GLU 285
HIS 214 0.56 GLN 100 -1.16 GLU 285
ARG 213 0.46 LYS 101 -1.41 GLU 285
LEU 206 0.34 THR 102 -1.62 GLU 285
LEU 206 0.41 TYR 103 -1.64 GLU 285
LEU 206 0.31 GLN 104 -1.66 LEU 130
LEU 206 0.43 GLY 105 -1.55 LEU 289
PRO 151 0.54 SER 106 -1.75 LEU 289
LEU 206 0.36 TYR 107 -1.60 LEU 289
LEU 206 0.25 GLY 108 -1.78 LEU 130
LEU 206 0.17 PHE 109 -1.49 LEU 130
THR 256 0.10 ARG 110 -1.74 ASN 131
ILE 254 0.26 LEU 111 -1.46 SER 127
ILE 254 0.51 GLY 112 -1.51 SER 127
PHE 270 1.64 PHE 113 -1.02 PRO 151
PHE 270 0.99 LEU 114 -0.80 PRO 151
PHE 270 0.57 HIS 115 -0.72 PRO 151
GLY 226 0.67 SER 116 -0.58 SER 121
ARG 280 0.99 SER 121 -0.60 PRO 151
VAL 225 0.61 VAL 122 -0.54 PRO 151
VAL 225 0.58 THR 123 -0.49 PRO 151
GLY 226 0.43 CYS 124 -0.63 PRO 151
MET 133 0.24 THR 125 -0.88 PRO 151
PRO 250 0.29 TYR 126 -1.15 LEU 111
ARG 248 0.57 SER 127 -1.51 GLY 112
ARG 248 0.46 PRO 128 -1.77 PRO 151
ARG 248 0.68 ALA 129 -1.74 VAL 147
ARG 248 0.95 LEU 130 -1.78 GLY 108
PRO 250 0.57 ASN 131 -1.74 ARG 110
PHE 113 0.60 LYS 132 -0.88 ARG 282
LEU 114 0.55 MET 133 -0.80 PRO 151
LEU 130 0.34 PHE 134 -0.76 PRO 151
GLY 226 0.33 CYS 135 -0.58 PRO 151
GLY 262 0.46 GLN 136 -0.44 PRO 151
GLY 262 0.55 LEU 137 -0.37 PRO 151
GLY 262 0.68 ALA 138 -0.32 PRO 151
GLY 262 0.60 LYS 139 -0.39 PRO 151
ARG 158 0.65 THR 140 -0.44 PRO 151
ILE 254 0.65 CYS 141 -0.58 TYR 126
ILE 255 0.78 PRO 142 -0.66 PRO 151
ILE 255 1.00 VAL 143 -1.07 TYR 126
ILE 255 0.59 GLN 144 -1.18 PRO 128
ILE 255 0.48 LEU 145 -1.51 PRO 128
THR 256 0.24 TRP 146 -1.74 PRO 128
LEU 257 0.37 VAL 147 -1.74 ALA 129
ARG 156 0.38 ASP 148 -1.72 ALA 129
THR 155 0.57 SER 149 -1.60 LEU 289
THR 155 1.17 THR 150 -1.42 LEU 289
SER 106 0.54 PRO 151 -1.77 PRO 128
LEU 188 0.24 PRO 152 -1.53 LEU 289
THR 150 0.54 PRO 153 -1.22 LEU 289
THR 150 0.68 GLY 154 -1.09 LEU 289
THR 150 1.17 THR 155 -1.11 LEU 289
THR 150 0.97 ARG 156 -1.02 ASN 210
ILE 232 1.02 VAL 157 -0.98 ASN 210
TYR 234 0.93 ARG 158 -1.19 ASP 208
TYR 234 0.85 ALA 159 -0.81 ASP 208
PHE 113 0.57 MET 160 -0.66 ASP 208
PHE 113 0.71 ALA 161 -0.52 THR 211
PHE 113 0.76 ILE 162 -0.53 THR 211
PHE 113 0.75 TYR 163 -0.46 THR 284
PHE 113 0.84 LYS 164 -0.63 THR 284
PHE 113 0.73 GLN 165 -0.57 THR 284
VAL 97 1.07 GLU 171 -0.30 THR 284
VAL 97 0.79 VAL 172 -0.27 THR 284
PHE 113 0.53 VAL 173 -0.26 THR 284
PHE 212 0.59 ARG 174 -0.16 PHE 270
GLY 262 0.59 ARG 175 -0.17 PRO 151
PHE 212 0.59 CYS 176 -0.16 PRO 151
PHE 212 0.66 PRO 177 -0.13 ALA 138
SER 261 0.56 HIS 178 -0.20 ALA 138
SER 261 0.61 HIS 179 -0.23 ALA 138
SER 261 0.69 GLU 180 -0.20 TYR 126
SER 261 0.69 ARG 181 -0.23 THR 140
SER 261 0.80 SER 185 -0.37 GLU 198
LEU 201 0.99 ASP 186 -0.41 PRO 128
LEU 201 1.05 GLY 187 -0.41 PRO 128
SER 261 1.09 LEU 188 -0.49 PRO 128
GLY 262 1.04 ALA 189 -0.46 PRO 128
GLY 262 0.94 PRO 190 -0.38 PRO 128
SER 261 0.82 PRO 191 -0.29 TYR 126
PHE 212 0.83 GLN 192 -0.23 TYR 126
GLY 262 0.81 HIS 193 -0.32 PRO 128
GLY 262 0.67 LEU 194 -0.31 TYR 126
GLY 262 0.73 ILE 195 -0.52 TYR 126
GLY 262 0.84 ARG 196 -0.53 PRO 128
ARG 158 0.87 VAL 197 -0.63 PRO 128
PRO 219 0.81 GLU 198 -0.57 PRO 128
PRO 219 0.88 GLY 199 -0.66 PRO 128
SER 261 0.70 ASN 200 -1.12 PRO 128
GLY 187 1.05 LEU 201 -1.03 PRO 128
SER 261 0.94 ARG 202 -1.00 PRO 128
GLY 262 1.06 VAL 203 -0.92 PRO 128
GLY 262 1.56 GLU 204 -0.75 PRO 128
GLY 262 1.32 TYR 205 -0.62 PRO 128
ASN 263 1.15 LEU 206 -0.51 PRO 128
ASN 263 0.70 ASP 207 -0.43 PRO 128
GLN 192 0.43 ASP 208 -1.19 ARG 158
PRO 191 0.61 ARG 209 -0.97 ARG 156
PRO 177 0.56 ASN 210 -1.02 ARG 156
PRO 177 0.45 THR 211 -0.94 ARG 158
GLN 192 0.83 PHE 212 -0.52 ARG 158
PRO 98 0.79 ARG 213 -0.41 ASN 288
GLY 262 0.74 HIS 214 -0.37 ASN 288
GLY 262 0.84 SER 215 -0.53 PRO 128
GLY 262 1.07 VAL 216 -0.72 PRO 128
GLY 262 0.91 VAL 217 -0.89 ASP 208
VAL 197 0.77 VAL 218 -0.98 PRO 128
GLY 199 0.88 PRO 219 -0.92 PRO 128
GLY 199 0.64 TYR 220 -1.16 PRO 128
GLY 199 0.49 GLU 221 -1.26 PRO 128
GLY 199 0.34 PRO 222 -1.41 PRO 128
SER 116 0.38 PRO 223 -1.39 PRO 128
SER 116 0.64 GLU 224 -1.00 PRO 128
SER 116 0.62 VAL 225 -0.87 PRO 128
SER 116 0.67 GLY 226 -0.83 PRO 151
SER 116 0.59 SER 227 -1.00 PRO 128
ILE 255 0.24 ASP 228 -1.35 PRO 128
ILE 255 0.35 CYS 229 -1.47 PRO 128
VAL 157 0.51 THR 230 -1.36 PRO 128
VAL 157 0.67 THR 231 -1.08 PRO 128
VAL 157 1.02 ILE 232 -0.99 ASN 200
VAL 157 0.88 HIS 233 -0.68 PRO 128
ARG 158 0.93 TYR 234 -0.63 TYR 126
GLY 262 0.68 ASN 235 -0.41 TYR 126
GLY 262 0.60 TYR 236 -0.37 PRO 151
GLY 262 0.63 MET 237 -0.31 PRO 151
GLY 262 0.53 CYS 238 -0.30 PRO 151
LEU 130 0.51 ASN 239 -0.35 PRO 151
LEU 130 0.65 SER 240 -0.34 PRO 151
LEU 130 0.83 SER 241 -0.30 PRO 151
LEU 130 0.67 CYS 242 -0.25 PRO 151
LEU 130 0.71 MET 243 -0.20 PRO 151
LEU 130 0.58 GLY 244 -0.15 PRO 151
LEU 130 0.53 GLY 245 -0.18 PRO 151
LEU 130 0.60 MET 246 -0.22 PRO 151
LEU 130 0.79 ASN 247 -0.23 PRO 151
LEU 130 0.95 ARG 248 -0.28 CYS 277
LEU 130 0.80 ARG 249 -0.34 ARG 280
PHE 113 0.74 PRO 250 -0.49 ASP 281
PHE 113 0.82 ILE 251 -0.49 ASP 281
PHE 113 1.04 LEU 252 -0.63 THR 284
PHE 113 1.01 THR 253 -0.62 GLU 285
PHE 113 0.96 ILE 254 -1.04 PRO 98
VAL 143 1.00 ILE 255 -0.86 GLU 285
ILE 232 0.75 THR 256 -0.96 ASN 210
THR 150 0.90 LEU 257 -1.07 LEU 289
THR 150 1.12 GLU 258 -1.08 LEU 289
THR 150 0.98 ASP 259 -1.17 LEU 289
GLU 204 1.06 SER 260 -1.01 LEU 289
GLU 204 1.28 SER 261 -0.97 LEU 289
GLU 204 1.56 GLY 262 -0.93 LEU 289
LEU 206 1.15 ASN 263 -1.14 LEU 289
LEU 206 0.97 LEU 264 -1.23 ASN 288
THR 150 0.68 LEU 265 -1.37 LEU 289
THR 150 0.51 GLY 266 -1.31 GLU 285
VAL 143 0.45 ARG 267 -1.29 GLU 285
PHE 113 0.55 ASN 268 -1.25 ASN 131
PHE 113 0.97 SER 269 -1.00 GLU 285
PHE 113 1.64 PHE 270 -0.80 GLU 285
PHE 113 1.19 GLU 271 -0.89 ASP 281
PHE 113 0.86 VAL 272 -0.63 ASP 281
PHE 113 0.52 ARG 273 -0.52 PRO 151
LEU 130 0.41 VAL 274 -0.47 PRO 151
LEU 130 0.46 CYS 275 -0.48 PRO 151
GLY 262 0.37 ALA 276 -0.46 PRO 151
SER 121 0.98 CYS 277 -0.55 PRO 151
SER 121 0.65 PRO 278 -0.66 PRO 151
SER 121 0.84 GLY 279 -0.73 PRO 151
SER 121 0.99 ARG 280 -0.75 THR 102
SER 121 0.67 ASP 281 -0.99 THR 102
SER 241 0.45 ARG 282 -1.05 ARG 110
SER 121 0.50 ARG 283 -0.94 THR 102
SER 121 0.50 THR 284 -1.31 THR 102
MET 243 0.37 GLU 285 -1.65 GLN 104
ARG 248 0.56 GLU 286 -1.47 ASP 148
SER 121 0.34 GLU 287 -1.30 TYR 103
SER 121 0.23 ASN 288 -1.47 GLY 105
MET 243 0.33 LEU 289 -1.75 SER 106
MET 243 0.32 ARG 290 -1.61 SER 106
SER 121 0.19 LYS 291 -1.32 SER 106

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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.