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***  dark2light A nrbl 1 cutoff 3  ***

CA distance fluctuations for 22022217490245406

---  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
PRO 80 0.00 PRO 80 -1.64 GLU 117
LEU 119 0.83 GLU 81 -0.16 GLY 269
GLY 247 0.43 ASP 82 -0.36 GLY 269
GLU 81 0.77 LEU 83 -0.38 GLY 269
GLU 81 0.66 GLY 84 -0.64 PRO 80
GLY 247 0.44 THR 85 -0.35 PRO 80
GLY 247 0.50 GLY 86 -0.32 GLY 269
GLY 247 0.60 LEU 87 -0.39 PRO 80
GLY 247 0.53 LEU 88 -0.47 PRO 80
GLY 247 0.47 GLU 89 -0.31 ASP 201
GLY 247 0.55 ALA 90 -0.33 ASP 201
GLY 247 0.58 LEU 91 -0.38 ASP 201
GLY 247 0.48 LEU 92 -0.35 ASP 201
GLY 247 0.47 ARG 93 -0.33 ASP 201
GLY 247 0.54 GLY 94 -0.37 ASP 201
GLY 247 0.57 ASP 95 -0.36 ASP 201
GLY 247 0.66 LEU 96 -0.41 ASP 201
GLY 247 0.66 ALA 97 -0.38 ASP 201
GLY 247 0.62 GLY 98 -0.36 LYS 268
GLY 247 0.68 ALA 99 -0.38 LYS 268
GLY 247 0.76 GLU 100 -0.44 LYS 268
GLY 247 0.69 ALA 101 -0.43 LYS 268
GLY 247 0.67 LEU 102 -0.41 LYS 268
GLY 247 0.79 PHE 103 -0.49 LYS 268
GLY 247 0.79 ARG 104 -0.53 LYS 268
GLY 247 0.68 ARG 105 -0.46 LYS 268
GLU 81 0.77 GLY 106 -0.50 LYS 268
GLY 247 0.83 LEU 107 -0.62 LYS 268
GLY 247 0.72 ARG 108 -0.56 GLU 272
GLY 247 0.63 PHE 109 -0.56 GLU 272
GLY 247 0.67 TRP 110 -0.64 PRO 80
GLY 247 0.79 GLY 111 -0.70 LYS 268
GLY 247 0.98 PRO 112 -0.91 LYS 268
GLY 247 0.97 GLU 113 -1.02 LYS 268
GLY 247 0.77 GLY 114 -1.11 PRO 80
GLY 247 0.85 VAL 115 -1.07 PRO 80
GLY 247 0.99 LEU 116 -1.27 PRO 80
GLY 247 0.74 GLU 117 -1.64 PRO 80
GLU 81 0.75 HIS 118 -1.57 PRO 80
GLU 81 0.83 LEU 119 -1.21 PRO 80
GLY 247 0.85 LEU 120 -1.17 PRO 80
GLY 247 0.71 LEU 121 -1.36 PRO 80
GLY 247 0.51 PRO 122 -1.18 PRO 80
GLU 81 0.58 VAL 123 -0.89 PRO 80
GLY 247 0.54 LEU 124 -0.92 PRO 80
GLU 81 0.36 ARG 125 -0.94 PRO 80
GLU 81 0.36 GLU 126 -0.73 PRO 80
GLU 81 0.37 VAL 127 -0.64 PRO 80
GLY 248 0.37 GLY 128 -0.69 PRO 80
ARG 230 0.31 GLU 129 -0.62 PRO 80
GLU 81 0.25 ALA 130 -0.47 PRO 80
GLY 248 0.34 TRP 131 -0.57 PRO 228
SER 226 0.31 HIS 132 -0.63 PRO 228
SER 226 0.26 ARG 133 -0.54 PRO 228
SER 226 0.27 GLY 134 -0.55 PRO 228
GLY 248 0.24 GLU 135 -0.48 PRO 228
GLY 248 0.33 ILE 136 -0.49 PRO 228
GLY 248 0.39 GLY 137 -0.55 PRO 228
GLY 248 0.49 VAL 138 -0.67 VAL 224
GLY 248 0.53 ALA 139 -0.65 VAL 224
GLY 248 0.51 GLU 140 -0.55 ASP 201
GLY 248 0.58 GLU 141 -0.58 ASP 201
GLY 248 0.70 HIS 142 -0.76 VAL 224
GLY 248 0.65 LEU 143 -0.61 ASP 201
GLY 247 0.67 ALA 144 -0.53 ASP 201
GLY 248 0.84 SER 145 -0.69 PRO 80
GLY 248 0.87 THR 146 -0.68 VAL 224
GLY 247 0.88 PHE 147 -0.51 ASP 201
GLY 247 1.01 LEU 148 -0.70 PRO 80
GLY 247 1.07 ARG 149 -0.74 PRO 80
GLY 247 1.10 ALA 150 -0.57 PRO 80
GLY 247 1.23 ARG 151 -0.60 PRO 80
GLY 247 1.46 LEU 152 -0.78 PRO 80
GLY 247 1.35 GLN 153 -0.66 PRO 80
GLY 247 1.32 GLU 154 -0.53 PRO 80
GLY 247 1.51 LEU 155 -0.63 PRO 80
GLY 247 1.55 LEU 156 -0.69 LYS 268
GLY 247 1.29 ASP 157 -0.57 LYS 268
GLY 247 1.27 LEU 158 -0.54 LYS 268
GLY 247 1.31 ALA 159 -0.64 LYS 268
GLY 247 1.06 GLY 160 -0.64 LYS 268
GLY 247 0.88 PHE 161 -0.74 LYS 268
GLY 247 0.83 PRO 162 -0.80 ALA 241
GLY 247 0.64 PRO 163 -0.96 ALA 241
GLY 247 0.55 GLY 164 -1.14 ALA 241
LEU 274 0.76 PRO 165 -1.50 ALA 241
LEU 274 0.81 PRO 166 -1.58 ALA 241
LEU 274 0.92 VAL 167 -1.26 LEU 240
ALA 195 0.88 LEU 168 -1.72 LEU 237
VAL 220 1.02 VAL 169 -1.39 VAL 219
GLY 248 0.85 THR 170 -0.91 ALA 236
SER 222 1.48 THR 171 -1.27 LEU 204
PRO 228 0.98 PRO 172 -1.57 PRO 203
PRO 228 1.57 PRO 173 -0.99 PRO 203
GLU 227 1.35 GLY 174 -0.95 PRO 203
ALA 223 1.26 GLU 175 -1.22 VAL 224
ALA 223 1.49 ARG 176 -1.70 VAL 224
GLY 248 1.53 HIS 177 -1.11 VAL 224
GLY 248 1.63 GLU 178 -0.96 VAL 224
GLY 248 1.31 ILE 179 -1.03 PRO 80
GLY 248 1.07 GLY 180 -1.05 PRO 80
GLY 248 1.08 ALA 181 -0.92 PRO 80
GLY 247 1.36 MET 182 -0.94 PRO 80
GLY 247 1.56 LEU 183 -1.19 LEU 267
GLY 247 1.24 ALA 184 -0.94 PRO 80
GLY 247 1.34 ALA 185 -0.92 LYS 268
GLY 247 1.66 TYR 186 -1.22 LYS 268
GLY 247 1.37 HIS 187 -1.74 LYS 268
GLY 247 1.13 LEU 188 -0.94 LYS 268
GLY 247 1.20 ARG 189 -0.88 LYS 268
GLY 247 1.20 ARG 190 -0.94 LYS 268
GLY 247 0.97 LYS 191 -0.74 GLU 272
GLY 247 0.91 GLY 192 -0.61 ALA 241
GLY 247 0.93 VAL 193 -0.77 ARG 243
GLY 247 1.00 PRO 194 -1.08 ALA 241
GLY 247 1.17 ALA 195 -1.39 GLY 217
GLY 247 1.06 LEU 196 -1.41 GLY 217
GLY 247 1.09 TYR 197 -0.99 GLY 217
GLY 248 0.90 LEU 198 -0.79 ALA 236
GLY 248 1.06 GLY 199 -0.75 PRO 80
ALA 223 1.25 PRO 200 -0.97 VAL 224
ALA 223 0.88 ASP 201 -1.30 VAL 224
ALA 273 0.62 THR 202 -1.18 VAL 224
ALA 273 0.45 PRO 203 -1.57 PRO 172
ALA 241 0.51 LEU 204 -1.28 PRO 172
ALA 273 0.33 PRO 205 -1.32 LEU 232
ALA 273 0.47 ASP 206 -1.38 ALA 236
ALA 273 0.59 LEU 207 -1.46 ALA 236
ALA 273 0.42 ARG 208 -1.64 ALA 236
ALA 273 0.43 ALA 209 -1.60 ALA 236
ALA 273 0.61 LEU 210 -1.45 ALA 236
ALA 273 0.64 ALA 211 -1.47 LEU 237
ALA 273 0.43 ARG 212 -1.44 GLY 235
LEU 274 0.49 ARG 213 -1.28 GLY 235
LEU 274 0.73 LEU 214 -1.23 LEU 240
LEU 274 0.55 GLY 215 -1.55 LEU 240
LEU 274 0.80 ALA 216 -1.57 LEU 240
ALA 273 0.72 GLY 217 -1.41 LEU 196
LEU 274 1.55 ALA 218 -1.65 LEU 237
ALA 273 1.57 VAL 219 -1.39 VAL 169
VAL 169 1.02 VAL 220 -1.31 ALA 256
ALA 273 0.87 LEU 221 -1.07 GLY 250
THR 171 1.48 SER 222 -1.16 GLY 250
ARG 176 1.49 ALA 223 -1.14 GLU 265
GLY 252 1.29 VAL 224 -1.70 ARG 176
ARG 176 0.89 LEU 225 -0.84 PRO 80
GLY 174 0.68 SER 226 -1.26 GLY 252
GLY 174 1.35 GLU 227 -0.80 PRO 80
PRO 173 1.57 PRO 228 -0.66 PRO 80
ALA 251 1.01 LEU 229 -1.22 PRO 205
ALA 251 1.14 ARG 230 -1.15 PRO 205
GLU 255 0.72 ALA 231 -1.19 PRO 205
ALA 256 0.76 LEU 232 -1.32 PRO 205
LEU 237 0.48 PRO 233 -1.24 PRO 205
ALA 231 0.18 ASP 234 -1.34 ALA 209
PRO 228 0.27 GLY 235 -1.58 ALA 209
PRO 228 0.28 ALA 236 -1.64 ARG 208
PRO 228 0.67 LEU 237 -1.72 LEU 168
PRO 228 0.56 LYS 238 -1.55 ALA 218
PRO 228 0.66 ASP 239 -1.47 GLY 215
PRO 228 0.89 LEU 240 -1.57 ALA 216
PRO 228 0.84 ALA 241 -1.58 PRO 166
PRO 228 0.73 PRO 242 -1.18 PRO 165
PRO 228 0.78 ARG 243 -1.05 VAL 167
PRO 228 0.94 VAL 244 -1.24 VAL 167
ALA 273 0.90 PHE 245 -1.04 MET 264
ALA 184 0.78 LEU 246 -1.36 ALA 256
TYR 186 1.66 GLY 247 -1.04 GLU 254
GLU 178 1.63 GLY 248 -0.83 PRO 80
TYR 263 0.88 GLN 249 -1.00 PRO 80
ARG 230 1.11 GLY 250 -1.16 SER 222
ARG 230 1.14 ALA 251 -1.10 VAL 220
VAL 224 1.29 GLY 252 -1.26 SER 226
VAL 224 0.95 PRO 253 -1.11 LEU 246
VAL 224 0.69 GLU 254 -1.04 LEU 246
ARG 230 0.74 GLU 255 -1.20 LEU 246
LEU 229 0.91 ALA 256 -1.36 LEU 246
LEU 232 0.50 ARG 257 -0.98 LEU 246
ALA 231 0.42 ARG 258 -1.17 PRO 205
LEU 232 0.73 LEU 259 -1.38 ARG 208
PRO 228 0.52 GLY 260 -1.18 ARG 212
PRO 228 0.84 ALA 261 -1.05 VAL 220
LEU 229 0.89 GLU 262 -0.66 PRO 80
PRO 172 0.98 TYR 263 -0.63 PRO 80
LYS 268 0.71 MET 264 -1.04 PHE 245
VAL 224 0.59 GLU 265 -1.14 ALA 223
VAL 224 0.69 ASP 266 -0.98 PRO 80
MET 264 0.67 LEU 267 -1.19 LEU 183
MET 264 0.71 LYS 268 -1.74 HIS 187
ALA 218 0.77 GLY 269 -1.12 PRO 80
ALA 218 0.66 LEU 270 -0.97 ASP 266
ALA 218 0.55 ALA 271 -0.83 PRO 80
ALA 218 1.03 GLU 272 -0.93 PRO 80
VAL 219 1.57 ALA 273 -0.82 PRO 80
ALA 218 1.55 LEU 274 -0.69 PRO 80

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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: October 18th, 2018.