CNRS Nantes University US2B US2B
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CA distance fluctuations for 2404111520403683696

---  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
PRO 98 1.09 SER 94 -0.78 ARG 209
MET 243 0.61 SER 95 -1.37 THR 150
GLY 244 0.80 SER 96 -1.32 LEU 264
GLY 244 1.14 VAL 97 -0.94 GLY 105
SER 94 1.09 PRO 98 -1.84 ARG 158
SER 166 0.70 SER 99 -1.64 PRO 222
SER 94 0.87 GLN 100 -0.98 MET 169
SER 94 0.98 LYS 101 -0.88 SER 166
SER 94 0.86 THR 102 -0.66 THR 170
SER 94 0.62 TYR 103 -0.90 VAL 97
ALA 129 0.55 GLN 104 -0.79 SER 96
ALA 129 0.45 GLY 105 -1.00 SER 96
ALA 129 0.47 SER 106 -1.17 SER 95
PRO 128 0.58 TYR 107 -1.17 SER 95
ALA 129 0.69 GLY 108 -1.00 SER 95
PRO 128 0.74 PHE 109 -0.88 SER 99
PRO 128 0.97 ARG 110 -0.75 PRO 98
PRO 128 1.25 LEU 111 -0.80 PRO 98
PRO 128 1.66 GLY 112 -0.71 PRO 98
SER 127 1.08 PHE 113 -0.79 PRO 98
SER 227 0.91 LEU 114 -0.70 PRO 98
GLU 286 0.92 HIS 115 -0.57 PRO 98
GLU 224 0.86 SER 116 -0.61 VAL 122
GLU 224 0.92 GLY 117 -0.82 PRO 128
GLU 224 0.90 THR 118 -0.71 SER 127
GLU 224 0.89 ALA 119 -0.49 PRO 128
GLU 224 0.85 LYS 120 -0.32 PRO 98
GLU 224 0.92 SER 121 -0.47 SER 116
GLU 224 1.02 VAL 122 -0.61 SER 116
GLU 224 1.09 THR 123 -0.53 PRO 98
GLU 224 1.04 CYS 124 -0.61 PRO 98
GLU 224 0.94 THR 125 -0.53 PRO 98
GLU 224 0.80 TYR 126 -0.52 GLY 117
GLY 112 1.15 SER 127 -0.71 THR 118
GLY 112 1.66 PRO 128 -0.82 GLY 117
GLY 112 1.17 ALA 129 -0.54 GLY 117
GLY 112 0.77 LEU 130 -0.59 LYS 101
GLY 112 0.78 ASN 131 -0.54 GLY 117
GLU 224 0.67 LYS 132 -0.44 GLY 117
GLU 224 0.80 MET 133 -0.48 PRO 98
GLU 224 0.83 PHE 134 -0.45 PRO 98
GLU 224 0.98 CYS 135 -0.53 PRO 98
GLU 224 1.04 GLN 136 -0.50 PRO 98
GLU 224 1.10 LEU 137 -0.60 GLU 285
GLU 224 1.24 ALA 138 -0.62 PRO 98
GLU 224 1.30 LYS 139 -0.65 PRO 98
GLU 224 1.32 THR 140 -0.78 PRO 98
GLU 224 1.08 CYS 141 -0.84 PRO 98
GLU 224 0.93 PRO 142 -0.86 PRO 98
PRO 128 0.94 VAL 143 -0.94 PRO 98
PRO 128 1.10 GLN 144 -0.83 PRO 98
PRO 128 1.00 LEU 145 -0.99 PRO 98
PRO 128 0.99 TRP 146 -1.04 SER 99
PRO 128 0.84 VAL 147 -1.22 SER 99
ALA 129 0.75 ASP 148 -1.22 SER 99
PRO 128 0.63 SER 149 -1.37 SER 99
PRO 128 0.66 THR 150 -1.54 SER 99
PRO 128 0.59 PRO 151 -1.38 SER 99
PRO 128 0.50 PRO 152 -1.35 SER 99
PRO 128 0.46 PRO 153 -1.40 SER 99
PRO 128 0.40 GLY 154 -1.24 SER 99
PRO 128 0.46 THR 155 -1.20 SER 99
PRO 128 0.45 ARG 156 -1.31 PRO 98
PRO 128 0.49 VAL 157 -1.59 PRO 98
GLU 224 0.45 ARG 158 -1.84 PRO 98
GLU 224 0.57 ALA 159 -1.42 PRO 98
GLU 224 0.56 MET 160 -1.00 PRO 98
GLU 224 0.59 ALA 161 -0.59 GLU 285
SER 94 0.65 ILE 162 -0.69 GLU 285
SER 94 0.66 TYR 163 -0.78 LEU 289
SER 94 0.86 LYS 164 -0.74 GLU 286
SER 94 0.83 GLN 165 -0.84 LEU 289
SER 99 0.70 SER 166 -0.94 GLN 100
ARG 248 0.95 GLN 167 -0.75 ASN 263
ARG 248 1.24 HIS 168 -0.73 ASN 263
ASN 247 0.75 MET 169 -0.98 GLN 100
ASN 247 0.74 THR 170 -1.23 LEU 264
ASN 247 1.07 GLU 171 -0.80 ASN 263
VAL 97 1.09 VAL 172 -0.77 ASN 288
VAL 97 0.87 VAL 173 -0.77 ASN 288
VAL 97 0.97 ARG 174 -0.80 ASN 288
VAL 97 0.89 ARG 175 -0.84 GLU 285
VAL 97 0.98 CYS 176 -0.96 ASN 288
VAL 97 0.96 PRO 177 -0.95 ASN 288
GLU 224 0.89 HIS 178 -0.93 ASN 288
GLU 224 0.98 HIS 179 -0.80 GLU 285
GLU 224 0.94 GLU 180 -0.76 ASN 288
GLU 224 0.94 ARG 181 -0.76 ASN 288
GLU 224 1.04 CYS 182 -0.69 ASN 288
GLU 224 1.09 SER 183 -0.58 ASN 288
GLU 224 1.22 ASP 184 -0.49 GLU 285
GLU 224 1.19 SER 185 -0.55 PRO 98
GLU 224 1.30 ASP 186 -0.60 PRO 98
GLU 224 1.14 GLY 187 -0.59 PRO 98
GLU 224 1.03 LEU 188 -0.69 PRO 98
GLU 224 1.01 ALA 189 -0.72 PRO 98
GLU 224 0.92 PRO 190 -0.61 PRO 98
GLU 224 0.97 PRO 191 -0.60 ASN 288
GLU 224 0.87 GLN 192 -0.69 ASN 288
GLU 224 0.88 HIS 193 -0.63 PRO 98
GLU 224 0.90 LEU 194 -0.64 GLU 285
GLU 224 0.90 ILE 195 -0.84 PRO 98
GLU 224 1.03 ARG 196 -0.90 PRO 98
GLU 224 1.07 VAL 197 -1.02 PRO 98
GLU 224 1.27 GLU 198 -0.89 PRO 98
GLU 224 1.23 GLY 199 -0.86 PRO 98
GLU 224 0.97 ASN 200 -0.95 PRO 98
GLU 224 0.87 LEU 201 -0.91 SER 99
GLU 224 0.71 ARG 202 -0.97 PRO 98
GLU 224 0.80 VAL 203 -1.05 PRO 98
GLU 224 0.70 GLU 204 -1.02 PRO 98
GLU 224 0.73 TYR 205 -0.93 PRO 98
GLU 224 0.60 LEU 206 -0.83 PRO 98
GLU 224 0.60 ASP 207 -0.76 SER 261
GLU 224 0.38 ASP 208 -1.21 GLY 262
PRO 177 0.41 ARG 209 -1.26 SER 261
PRO 177 0.45 ASN 210 -1.17 ASN 263
PRO 177 0.53 THR 211 -1.18 ASN 263
GLN 192 0.63 PHE 212 -0.87 GLY 262
VAL 97 0.58 ARG 213 -0.72 GLY 262
GLU 224 0.64 HIS 214 -0.72 PRO 98
GLU 224 0.63 SER 215 -1.07 PRO 98
GLU 224 0.71 VAL 216 -1.23 PRO 98
GLU 224 0.58 VAL 217 -1.39 PRO 98
GLU 224 0.58 VAL 218 -1.28 PRO 98
PRO 128 0.47 PRO 219 -1.17 PRO 98
PRO 128 0.53 TYR 220 -1.28 SER 99
PRO 128 0.54 GLU 221 -1.46 SER 99
PRO 128 0.55 PRO 222 -1.64 SER 99
PRO 128 0.70 PRO 223 -1.43 SER 99
THR 140 1.32 GLU 224 -0.92 SER 99
GLY 187 0.89 VAL 225 -0.89 SER 95
GLY 199 0.99 GLY 226 -1.03 SER 99
LEU 114 0.91 SER 227 -1.22 SER 99
ARG 290 0.70 ASP 228 -1.17 SER 99
PRO 128 0.88 CYS 229 -1.12 SER 99
PRO 128 0.86 THR 230 -1.03 SER 99
PRO 128 0.81 THR 231 -0.91 PRO 98
GLU 224 0.82 ILE 232 -1.04 PRO 98
GLU 224 1.09 HIS 233 -0.96 PRO 98
GLU 224 1.05 TYR 234 -1.02 PRO 98
GLU 224 1.15 ASN 235 -0.84 PRO 98
GLU 224 1.03 TYR 236 -0.70 PRO 98
GLU 224 1.06 MET 237 -0.65 GLU 285
GLU 224 0.96 CYS 238 -0.87 GLU 285
GLU 224 0.91 ASN 239 -1.03 GLU 285
GLU 224 0.80 SER 240 -1.24 GLU 285
HIS 168 0.93 SER 241 -1.51 GLU 285
VAL 97 0.84 CYS 242 -1.25 GLU 285
VAL 97 0.97 MET 243 -1.23 ASN 288
VAL 97 1.14 GLY 244 -1.20 ASN 288
VAL 97 1.09 GLY 245 -1.07 GLU 285
GLU 171 0.95 MET 246 -1.16 GLU 285
HIS 168 1.19 ASN 247 -1.38 GLU 285
HIS 168 1.24 ARG 248 -1.61 GLU 285
HIS 168 1.07 ARG 249 -1.22 GLU 285
SER 94 0.65 PRO 250 -0.96 GLU 285
GLU 224 0.63 ILE 251 -0.78 GLU 285
SER 94 0.66 LEU 252 -0.50 GLU 285
GLU 224 0.57 THR 253 -0.68 PRO 98
SER 94 0.50 ILE 254 -0.84 PRO 98
PRO 128 0.43 ILE 255 -1.28 PRO 98
PRO 128 0.40 THR 256 -1.31 PRO 98
PRO 128 0.50 LEU 257 -1.25 PRO 98
PRO 128 0.38 GLU 258 -1.16 PRO 98
PRO 128 0.37 ASP 259 -0.99 PRO 98
PRO 128 0.31 SER 260 -0.99 PRO 98
PRO 128 0.22 SER 261 -1.26 ARG 209
PRO 128 0.20 GLY 262 -1.21 ASP 208
PRO 128 0.24 ASN 263 -1.23 SER 96
PRO 128 0.29 LEU 264 -1.32 SER 96
PRO 128 0.41 LEU 265 -1.18 SER 96
PRO 128 0.44 GLY 266 -1.00 SER 96
SER 94 0.45 ARG 267 -0.90 THR 170
SER 94 0.60 ASN 268 -0.72 PRO 98
SER 94 0.67 SER 269 -0.58 PRO 98
SER 94 0.62 PHE 270 -0.48 LYS 101
SER 94 0.66 GLU 271 -0.39 GLU 286
GLU 224 0.75 VAL 272 -0.56 GLU 285
GLU 224 0.80 ARG 273 -0.81 GLU 285
GLU 224 0.89 VAL 274 -0.78 GLU 285
GLU 224 0.89 CYS 275 -0.99 ASP 281
GLU 224 0.92 ALA 276 -0.85 ASP 281
GLU 224 0.81 CYS 277 -0.25 LYS 139
GLU 224 0.85 PRO 278 -0.34 PRO 98
GLU 224 0.86 GLY 279 -0.36 PRO 98
GLU 224 0.77 ARG 280 -0.36 CYS 275
GLU 224 0.71 ASP 281 -0.99 CYS 275
GLU 224 0.76 ARG 282 -0.73 ARG 273
GLU 224 0.77 ARG 283 -0.76 ARG 248
GLU 224 0.65 THR 284 -1.10 SER 241
GLU 224 0.57 GLU 285 -1.61 ARG 248
HIS 115 0.92 GLU 286 -1.16 ARG 248
SER 227 0.76 GLU 287 -1.06 ARG 248
SER 227 0.57 ASN 288 -1.24 ASN 247
SER 227 0.68 LEU 289 -1.12 ASN 247
SER 227 0.76 ARG 290 -0.84 ASN 247

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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.