CNRS Nantes University US2B US2B
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CA distance fluctuations for 2402161450163041169

---  normal mode 8  ---

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
TYR 103 0.33 SER 96 -0.39 THR 231
TYR 103 0.33 VAL 97 -0.41 THR 231
TYR 103 0.41 PRO 98 -0.44 THR 231
ASN 210 0.38 SER 99 -0.44 THR 231
ASP 228 0.34 GLN 100 -0.40 THR 231
ASP 228 0.44 LYS 101 -0.42 LEU 264
ASP 228 0.53 THR 102 -0.33 ALA 129
ASN 210 0.60 TYR 103 -0.41 ALA 129
ASP 228 0.56 GLN 104 -0.40 PRO 128
ASN 210 0.63 GLY 105 -0.35 ALA 129
ASN 210 0.58 SER 106 -0.31 ALA 129
ASN 210 0.48 TYR 107 -0.28 PRO 128
ASP 228 0.66 GLY 108 -0.36 PRO 128
ASP 228 0.56 PHE 109 -0.36 THR 231
TRP 146 0.64 ARG 110 -0.37 LEU 111
ASP 228 0.41 LEU 111 -0.37 ARG 110
ARG 158 0.27 GLY 112 -0.33 SER 227
ARG 158 0.23 PHE 113 -0.55 SER 227
THR 231 0.33 LEU 114 -0.67 SER 227
PRO 219 0.23 VAL 122 -0.94 SER 227
PRO 219 0.25 THR 123 -1.09 SER 227
PRO 219 0.25 CYS 124 -0.99 SER 227
PRO 219 0.20 THR 125 -0.78 SER 227
ARG 158 0.17 TYR 126 -0.60 SER 227
ASP 228 0.12 SER 127 -0.46 SER 227
ASP 228 0.27 PRO 128 -0.40 GLN 104
ASP 228 0.26 ALA 129 -0.41 TYR 103
ASP 228 0.23 LEU 130 -0.34 SER 227
ASP 228 0.27 ASN 131 -0.34 SER 227
ASP 228 0.14 LYS 132 -0.49 SER 227
ARG 158 0.20 MET 133 -0.64 SER 227
ARG 158 0.20 MET 133 -0.65 SER 227
ARG 158 0.18 PHE 134 -0.76 SER 227
ARG 158 0.23 CYS 135 -0.94 SER 227
SER 261 0.26 GLN 136 -1.02 SER 227
SER 261 0.32 LEU 137 -1.03 SER 227
SER 261 0.36 ALA 138 -1.18 SER 227
SER 261 0.32 LYS 139 -1.31 SER 227
PRO 219 0.32 THR 140 -1.40 SER 227
PRO 219 0.34 CYS 141 -1.09 SER 227
PRO 219 0.34 CYS 141 -1.09 SER 227
PRO 219 0.36 PRO 142 -0.97 SER 227
PRO 219 0.35 VAL 143 -0.62 SER 227
TYR 220 0.27 GLN 144 -0.43 SER 227
LEU 111 0.29 LEU 145 -0.34 ASN 200
ARG 110 0.64 TRP 146 -0.28 GLY 199
ASP 228 0.50 VAL 147 -0.32 ASN 200
ASP 228 0.78 ASP 148 -0.25 ASN 200
PRO 223 0.57 SER 149 -0.24 ASN 200
PRO 223 0.43 THR 150 -0.29 ASN 200
ASN 210 0.41 PRO 151 -0.27 THR 230
ARG 209 0.42 PRO 152 -0.15 ALA 129
ARG 209 0.32 PRO 153 -0.14 LYS 101
ARG 202 0.35 GLY 154 -0.16 LYS 101
PRO 222 0.39 THR 155 -0.22 THR 231
TYR 234 0.41 ARG 156 -0.28 THR 231
TYR 234 0.43 VAL 157 -0.50 THR 231
TYR 234 0.47 ARG 158 -0.53 THR 231
ASN 235 0.31 ALA 159 -0.83 THR 231
GLY 262 0.27 MET 160 -0.67 THR 231
SER 261 0.21 ALA 161 -0.58 GLU 224
TRP 146 0.20 ILE 162 -0.48 GLU 224
TRP 146 0.18 TYR 163 -0.43 GLU 224
ASP 228 0.20 LYS 164 -0.36 SER 227
ASP 228 0.21 GLN 165 -0.32 SER 227
LYS 101 0.26 SER 166 -0.26 THR 231
LYS 101 0.26 SER 166 -0.26 THR 231
LYS 101 0.21 GLN 167 -0.30 GLU 224
TRP 146 0.18 HIS 168 -0.38 GLU 224
TYR 103 0.23 MET 169 -0.36 GLU 224
TYR 103 0.25 THR 170 -0.40 GLU 224
TYR 103 0.21 GLU 171 -0.48 GLU 224
ASN 263 0.29 VAL 172 -0.56 GLU 224
SER 261 0.28 VAL 173 -0.63 GLU 224
SER 261 0.35 ARG 174 -0.73 GLU 224
SER 261 0.35 ARG 175 -0.80 GLU 224
SER 261 0.31 CYS 176 -0.76 VAL 225
SER 261 0.33 PRO 177 -0.83 VAL 225
SER 261 0.32 HIS 178 -0.95 VAL 225
SER 261 0.34 HIS 179 -0.94 VAL 225
SER 261 0.38 GLU 180 -0.93 GLU 224
SER 261 0.37 ARG 181 -0.98 VAL 225
SER 261 0.42 SER 185 -1.30 GLU 224
SER 261 0.43 ASP 186 -1.49 GLU 224
SER 261 0.47 GLY 187 -1.41 GLU 224
SER 261 0.54 LEU 188 -1.37 GLU 224
SER 261 0.54 ALA 189 -1.24 GLU 224
SER 261 0.55 PRO 190 -1.08 GLU 224
SER 261 0.46 PRO 191 -1.06 GLU 224
SER 261 0.45 GLN 192 -0.91 GLU 224
SER 261 0.46 HIS 193 -0.93 GLU 224
SER 261 0.38 LEU 194 -0.87 GLU 224
SER 261 0.40 ILE 195 -0.91 GLU 224
SER 261 0.43 ARG 196 -1.11 GLU 224
SER 261 0.41 VAL 197 -1.16 GLU 224
SER 261 0.40 GLU 198 -1.41 GLU 224
SER 261 0.32 GLY 199 -1.37 GLU 224
SER 261 0.34 ASN 200 -1.19 GLU 224
SER 261 0.42 LEU 201 -1.23 GLU 224
SER 261 0.56 ARG 202 -1.01 GLU 224
SER 261 0.61 VAL 203 -1.08 GLU 224
SER 261 0.80 GLU 204 -0.94 GLU 224
SER 261 0.72 TYR 205 -0.95 GLU 224
GLY 262 0.80 LEU 206 -0.77 GLU 224
GLY 262 0.69 ASP 207 -0.70 GLU 224
ASN 263 0.82 ASP 208 -0.52 GLU 224
ASN 263 0.91 ARG 209 -0.45 GLU 224
LEU 264 0.79 ASN 210 -0.35 GLU 224
LEU 264 0.45 THR 211 -0.48 GLU 224
ASN 263 0.56 PHE 212 -0.57 GLU 224
ASN 263 0.45 ARG 213 -0.60 GLU 224
GLY 262 0.50 HIS 214 -0.72 GLU 224
GLY 262 0.55 SER 215 -0.71 GLU 224
GLY 262 0.57 VAL 216 -0.84 GLU 224
SER 261 0.50 VAL 217 -0.70 THR 231
TYR 234 0.46 VAL 218 -0.65 GLU 224
HIS 233 0.51 PRO 219 -0.39 GLU 224
PRO 222 0.37 TYR 220 -0.29 THR 230
ILE 232 0.26 GLU 221 -0.55 LEU 201
THR 155 0.39 PRO 222 -0.59 LEU 201
ASP 148 0.60 PRO 223 -1.02 GLY 199
SER 227 1.11 GLU 224 -1.49 ASP 186
SER 149 0.45 VAL 225 -0.98 ARG 181
SER 106 0.24 GLY 226 -0.72 HIS 178
GLU 224 1.11 SER 227 -1.40 THR 140
ASP 148 0.78 ASP 228 -0.91 GLY 199
THR 230 0.22 CYS 229 -0.67 ASN 200
CYS 229 0.22 THR 230 -0.83 ASN 200
LEU 114 0.33 THR 231 -1.16 ILE 232
PRO 219 0.29 ILE 232 -1.16 THR 231
PRO 219 0.51 HIS 233 -1.09 SER 227
ARG 158 0.47 TYR 234 -0.97 SER 227
ARG 158 0.44 ASN 235 -1.11 SER 227
SER 261 0.35 TYR 236 -0.96 SER 227
SER 261 0.37 MET 237 -0.97 SER 227
SER 261 0.31 CYS 238 -0.86 SER 227
SER 261 0.31 CYS 238 -0.86 SER 227
SER 261 0.26 ASN 239 -0.82 SER 227
SER 261 0.20 SER 240 -0.71 SER 227
SER 261 0.20 SER 241 -0.72 VAL 225
SER 261 0.24 CYS 242 -0.74 VAL 225
SER 261 0.22 MET 243 -0.64 SER 227
SER 261 0.17 GLY 244 -0.56 VAL 225
SER 261 0.17 GLY 245 -0.60 VAL 225
SER 261 0.14 MET 246 -0.57 VAL 225
LEU 130 0.10 ASN 247 -0.50 VAL 225
LEU 130 0.12 ARG 248 -0.54 VAL 225
SER 261 0.12 SER 249 -0.49 SER 227
TRP 146 0.12 PRO 250 -0.51 SER 227
TRP 146 0.14 ILE 251 -0.52 SER 227
TRP 146 0.18 LEU 252 -0.46 SER 227
TRP 146 0.19 THR 253 -0.60 THR 231
TRP 146 0.29 ILE 254 -0.61 THR 231
TRP 146 0.29 ILE 254 -0.61 THR 231
TRP 146 0.36 ILE 255 -0.72 THR 231
TRP 146 0.41 THR 256 -0.57 THR 231
TRP 146 0.42 THR 256 -0.57 THR 231
TRP 146 0.42 LEU 257 -0.48 THR 231
ARG 209 0.53 GLU 258 -0.36 THR 231
ARG 209 0.58 ASP 259 -0.24 LYS 101
GLU 204 0.61 SER 260 -0.22 LYS 101
GLU 204 0.80 SER 261 -0.26 LYS 101
LEU 206 0.80 GLY 262 -0.32 LYS 101
ARG 209 0.91 ASN 263 -0.36 LYS 101
ARG 209 0.82 LEU 264 -0.42 LYS 101
ASN 210 0.65 LEU 265 -0.34 THR 231
ASN 210 0.60 GLY 266 -0.45 THR 231
ASN 210 0.50 ARG 267 -0.48 THR 231
TRP 146 0.43 ASN 268 -0.46 THR 231
TRP 146 0.31 SER 269 -0.47 THR 231
GLY 112 0.25 PHE 270 -0.39 SER 227
GLY 112 0.16 GLU 271 -0.47 SER 227
ARG 158 0.15 VAL 272 -0.64 SER 227
ARG 158 0.15 VAL 272 -0.64 SER 227
SER 261 0.15 ARG 273 -0.70 SER 227
SER 261 0.22 VAL 274 -0.83 SER 227
SER 261 0.20 CYS 275 -0.82 SER 227
SER 261 0.22 ALA 276 -0.87 SER 227
PRO 219 0.17 CYS 277 -0.81 SER 227
PRO 219 0.18 CYS 277 -0.81 SER 227
PRO 219 0.18 PRO 278 -0.79 SER 227
PRO 219 0.17 GLY 279 -0.71 SER 227
PRO 219 0.14 ARG 280 -0.65 SER 227
PRO 219 0.12 ASP 281 -0.63 SER 227
PRO 219 0.12 ARG 282 -0.57 SER 227
PRO 219 0.11 ARG 283 -0.51 SER 227
ASP 186 0.09 THR 284 -0.49 SER 227
SER 241 0.11 GLU 285 -0.46 SER 227
ASP 228 0.10 GLU 286 -0.41 SER 227
SER 241 0.08 GLU 287 -0.38 SER 227

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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.