CNRS Nantes University US2B US2B
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CA distance fluctuations for 2404260424312878936

---  normal mode 12  ---

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
LEU 264 1.39 VAL 97 -0.59 GLU 171
LEU 264 1.11 PRO 98 -1.05 ARG 213
LEU 130 0.93 SER 99 -0.99 LEU 206
ASN 131 1.06 GLN 100 -0.67 LEU 206
LEU 130 0.92 LYS 101 -0.57 LEU 206
PHE 113 0.72 THR 102 -0.34 ARG 213
PRO 98 0.53 TYR 103 -0.30 LEU 206
ASN 200 0.56 GLN 104 -0.18 ALA 129
PRO 98 0.63 GLY 105 -0.36 THR 230
ASN 210 0.59 SER 106 -0.45 THR 230
VAL 218 0.71 TYR 107 -0.59 PRO 128
LEU 201 0.80 GLY 108 -0.59 ALA 129
ASN 200 0.82 PHE 109 -0.63 PRO 128
ASN 200 0.79 ARG 110 -0.67 PRO 128
ASN 200 0.70 LEU 111 -0.97 PHE 270
ASN 200 0.60 GLY 112 -1.02 PRO 128
SER 269 0.74 PHE 113 -1.14 TYR 220
THR 102 0.60 LEU 114 -1.47 TYR 220
LYS 101 0.53 HIS 115 -1.41 TYR 220
SER 121 0.44 SER 116 -1.51 TYR 220
SER 116 0.44 SER 121 -0.96 TYR 220
LYS 101 0.39 VAL 122 -1.16 TYR 220
SER 185 0.48 THR 123 -1.18 TYR 220
SER 185 0.46 CYS 124 -1.25 TYR 220
LYS 101 0.52 THR 125 -1.20 TYR 220
LYS 101 0.67 TYR 126 -1.16 SER 227
GLN 100 0.70 SER 127 -1.27 SER 227
LYS 101 0.84 PRO 128 -1.24 ASP 228
LYS 101 0.84 ALA 129 -1.12 ASP 228
GLN 100 1.06 LEU 130 -0.94 SER 227
GLN 100 1.06 ASN 131 -0.96 GLY 112
GLN 100 0.75 LYS 132 -0.89 SER 227
GLN 100 0.55 MET 133 -0.92 TYR 220
SER 185 0.46 PHE 134 -0.91 TYR 220
SER 185 0.53 CYS 135 -0.99 TYR 220
SER 185 0.59 GLN 136 -0.93 TYR 220
SER 185 0.72 LEU 137 -0.80 TYR 220
SER 185 0.99 ALA 138 -0.84 TYR 220
SER 185 0.75 LYS 139 -1.07 TYR 220
SER 185 0.65 THR 140 -1.27 TYR 220
SER 185 0.54 CYS 141 -1.27 TYR 220
ASP 186 0.50 PRO 142 -1.39 TYR 220
ASN 200 0.65 VAL 143 -1.04 VAL 157
ASN 200 0.69 GLN 144 -1.15 LEU 257
ASN 200 1.02 LEU 145 -1.09 LEU 257
LEU 201 0.91 TRP 146 -0.92 PRO 128
LEU 201 1.18 VAL 147 -0.89 PRO 128
LEU 201 1.08 ASP 148 -0.89 ALA 129
LEU 201 1.04 SER 149 -0.71 ALA 129
PRO 219 1.60 THR 150 -0.60 PRO 128
ASN 210 0.97 PRO 151 -1.53 GLU 224
ASN 210 0.99 PRO 152 -1.27 GLU 224
ASN 210 0.89 PRO 153 -1.17 VAL 225
ASN 210 1.11 GLY 154 -1.06 GLU 224
ASN 210 1.25 THR 155 -1.24 GLU 224
ARG 209 1.37 ARG 156 -1.37 THR 231
THR 150 0.85 VAL 157 -1.86 ILE 232
GLU 221 1.06 ARG 158 -0.83 ILE 232
GLU 221 1.08 ALA 159 -0.44 GLN 144
GLU 221 0.90 MET 160 -0.43 SER 99
GLU 221 0.74 ALA 161 -0.36 GLN 144
GLY 262 0.88 ILE 162 -0.38 LEU 111
GLY 262 0.94 TYR 163 -0.38 LEU 111
GLY 262 0.89 LYS 164 -0.46 LEU 111
GLY 262 1.01 GLN 165 -0.40 SER 227
GLY 262 1.17 GLU 171 -0.59 VAL 97
GLY 262 0.99 VAL 172 -0.61 PRO 98
GLY 262 0.78 VAL 173 -0.38 PRO 98
GLU 221 0.64 ARG 174 -0.43 PRO 98
GLU 221 0.58 ARG 175 -0.33 PRO 98
ASN 288 0.57 CYS 176 -0.30 SER 227
ASN 288 0.53 PRO 177 -0.34 PRO 98
ASN 288 0.50 HIS 178 -0.34 TYR 220
GLU 221 0.47 HIS 179 -0.40 TYR 220
GLU 221 0.53 GLU 180 -0.38 LEU 201
GLU 221 0.46 ARG 181 -0.44 LEU 201
ALA 138 0.99 SER 185 -0.66 LEU 201
GLU 198 0.95 ASP 186 -0.87 LEU 201
GLU 221 0.65 GLY 187 -0.70 LEU 201
GLU 221 0.78 LEU 188 -0.70 LEU 201
GLU 221 0.82 ALA 189 -0.54 LEU 201
GLU 221 0.74 PRO 190 -0.56 SER 99
GLU 221 0.65 PRO 191 -0.46 PRO 98
GLU 221 0.68 GLN 192 -0.53 PRO 98
GLU 221 0.76 HIS 193 -0.46 PRO 98
GLU 221 0.70 LEU 194 -0.36 TYR 220
GLU 221 0.79 ILE 195 -0.45 VAL 218
GLU 221 0.82 ARG 196 -0.66 VAL 218
GLU 221 0.82 VAL 197 -1.13 VAL 218
ASP 186 0.95 GLU 198 -1.04 VAL 218
THR 230 0.59 GLY 199 -1.02 PRO 219
PRO 222 1.11 ASN 200 -0.47 PRO 219
PRO 223 1.43 LEU 201 -0.87 ASP 186
PRO 222 1.38 ARG 202 -0.53 GLY 262
GLU 221 1.40 VAL 203 -0.42 SER 99
GLU 221 1.13 GLU 204 -0.68 SER 99
GLU 221 1.03 TYR 205 -0.72 SER 99
GLU 221 0.92 LEU 206 -0.99 SER 99
THR 150 0.93 ASP 207 -0.87 PRO 98
ARG 156 1.17 ASP 208 -1.02 PRO 98
ARG 156 1.37 ARG 209 -0.67 PRO 98
ASP 259 1.52 ASN 210 -0.56 PRO 98
GLY 262 1.29 THR 211 -0.89 PRO 98
SER 260 1.04 PHE 212 -0.86 PRO 98
GLY 262 0.85 ARG 213 -1.05 PRO 98
GLU 221 0.87 HIS 214 -0.75 PRO 98
GLU 221 1.01 SER 215 -0.74 SER 99
GLU 221 1.23 VAL 216 -0.60 SER 99
GLU 221 1.40 VAL 217 -0.55 ILE 232
GLU 221 1.28 VAL 218 -1.13 VAL 197
THR 150 1.60 PRO 219 -1.26 HIS 233
THR 150 1.22 TYR 220 -1.51 SER 116
VAL 217 1.40 GLU 221 -1.47 ASP 259
LEU 201 1.39 PRO 222 -1.08 PRO 152
LEU 201 1.43 PRO 223 -1.49 PRO 151
LEU 201 1.17 GLU 224 -1.53 PRO 151
ASP 148 0.94 VAL 225 -1.17 PRO 153
ASP 148 0.74 GLY 226 -1.22 ARG 283
LEU 201 0.74 SER 227 -1.32 LEU 114
LEU 201 0.85 ASP 228 -1.24 PRO 128
LEU 201 0.96 CYS 229 -1.03 PRO 151
ASN 200 1.05 THR 230 -1.23 LEU 257
ASN 200 0.72 THR 231 -1.37 ARG 156
ASN 200 0.88 ILE 232 -1.86 VAL 157
ASP 186 0.65 HIS 233 -1.26 PRO 219
ASP 186 0.62 TYR 234 -0.90 VAL 157
SER 185 0.81 ASN 235 -0.85 TYR 220
SER 185 0.70 TYR 236 -0.69 TYR 220
SER 185 0.71 MET 237 -0.58 TYR 220
GLU 221 0.49 CYS 238 -0.52 TYR 220
GLU 285 0.59 ASN 239 -0.57 TYR 220
GLU 285 0.78 SER 240 -0.53 SER 227
GLU 285 0.83 SER 241 -0.50 SER 227
ASN 288 0.68 CYS 242 -0.43 SER 227
ASN 288 0.76 MET 243 -0.38 SER 227
ASN 288 0.70 GLY 244 -0.32 SER 227
ASN 288 0.67 GLY 245 -0.34 SER 227
LEU 289 0.75 MET 246 -0.40 SER 227
ASN 288 0.86 ASN 247 -0.42 SER 227
GLU 285 0.99 ARG 248 -0.49 SER 227
LEU 289 0.98 ARG 249 -0.47 SER 227
LEU 289 0.86 PRO 250 -0.53 SER 227
GLY 262 0.69 ILE 251 -0.48 SER 227
GLY 262 0.63 LEU 252 -0.52 LEU 111
GLU 221 0.68 THR 253 -0.52 LEU 111
GLU 221 0.72 ILE 254 -0.48 GLN 144
GLU 221 0.90 ILE 255 -0.65 GLN 144
VAL 97 0.67 THR 256 -0.74 THR 231
ASN 210 0.94 LEU 257 -1.34 THR 231
ASN 210 1.40 GLU 258 -1.11 THR 231
ASN 210 1.52 ASP 259 -1.47 GLU 221
ASN 210 1.34 SER 260 -1.24 GLU 221
ASN 210 1.13 SER 261 -0.80 GLU 221
THR 211 1.29 GLY 262 -0.59 THR 231
VAL 97 1.32 ASN 263 -0.64 THR 230
VAL 97 1.39 LEU 264 -0.74 THR 231
VAL 97 0.96 LEU 265 -1.00 THR 230
PRO 98 0.84 GLY 266 -0.68 LEU 145
PRO 98 0.73 ARG 267 -0.38 LEU 145
GLU 221 0.67 ASN 268 -0.25 GLN 165
PHE 113 0.74 SER 269 -0.42 LYS 164
GLN 100 0.74 PHE 270 -0.97 LEU 111
GLN 100 0.63 GLU 271 -0.72 GLY 112
GLU 285 0.47 VAL 272 -0.68 SER 227
GLU 285 0.64 ARG 273 -0.69 SER 227
GLU 285 0.52 VAL 274 -0.73 TYR 220
SER 185 0.50 CYS 275 -0.74 TYR 220
SER 185 0.46 ALA 276 -0.79 TYR 220
SER 185 0.41 CYS 277 -0.86 TYR 220
SER 185 0.43 PRO 278 -0.94 TYR 220
LYS 101 0.47 GLY 279 -1.06 GLY 226
LYS 101 0.42 ARG 280 -1.00 GLY 226
SER 185 0.42 ASP 281 -0.93 GLY 226
GLN 100 0.55 ARG 282 -1.05 GLY 226
GLN 100 0.57 ARG 283 -1.22 GLY 226
ARG 248 0.66 THR 284 -1.05 GLY 226
ARG 248 0.99 GLU 285 -0.96 GLY 226
SER 99 0.73 GLU 286 -1.20 GLY 226
SER 99 0.68 GLU 287 -1.19 GLY 226
ARG 248 0.94 ASN 288 -0.96 GLY 226
ARG 249 0.98 LEU 289 -0.98 GLY 226
SER 99 0.76 ARG 290 -1.12 GLY 226
GLN 165 0.74 LYS 291 -0.96 GLY 226

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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.