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CA distance fluctuations for 2404131452423995065

---  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 0.53 SER 96 -0.56 ARG 213
TYR 103 0.55 VAL 97 -0.31 SER 215
TYR 103 0.73 PRO 98 -0.34 SER 215
ASN 210 0.52 SER 99 -0.63 ARG 158
ASN 210 0.50 GLN 100 -0.30 ARG 158
ASN 210 0.56 LYS 101 -0.50 LEU 264
ASN 210 0.75 THR 102 -0.46 LEU 289
ASN 210 1.14 TYR 103 -0.65 ALA 129
ASN 210 1.16 GLN 104 -0.74 ALA 129
ASN 210 1.43 GLY 105 -0.61 ALA 129
ASN 210 1.50 SER 106 -0.58 ALA 129
ARG 209 1.27 TYR 107 -0.57 ALA 129
ASN 210 1.16 GLY 108 -0.70 PRO 128
ASN 210 1.00 PHE 109 -0.66 PRO 128
ASN 210 0.78 ARG 110 -0.77 PRO 128
ASN 210 0.58 LEU 111 -0.66 ASN 131
ASN 210 0.50 GLY 112 -0.60 TRP 146
SER 269 0.46 PHE 113 -0.78 SER 227
ARG 158 0.34 LEU 114 -1.00 SER 227
ASP 186 0.33 SER 121 -1.03 VAL 225
ARG 158 0.29 VAL 122 -0.97 VAL 225
ARG 158 0.36 THR 123 -1.03 VAL 225
ARG 158 0.36 CYS 124 -0.94 SER 227
ARG 158 0.29 THR 125 -0.79 SER 227
ARG 158 0.25 TYR 126 -0.63 SER 227
ASP 208 0.20 SER 127 -0.65 ARG 110
ASN 210 0.26 PRO 128 -0.77 ARG 110
ASN 210 0.21 ALA 129 -0.74 GLN 104
ASN 210 0.17 LEU 130 -0.64 ARG 110
ASN 210 0.26 ASN 131 -0.71 ARG 110
ASP 208 0.21 LYS 132 -0.54 LEU 111
ARG 158 0.26 MET 133 -0.62 SER 227
ARG 158 0.25 PHE 134 -0.74 VAL 225
ARG 158 0.34 CYS 135 -0.88 VAL 225
SER 261 0.41 GLN 136 -1.04 VAL 225
SER 261 0.52 LEU 137 -1.09 VAL 225
SER 261 0.55 ALA 138 -1.08 VAL 225
SER 261 0.48 LYS 139 -1.10 VAL 225
ARG 158 0.48 THR 140 -1.08 SER 227
ARG 158 0.56 CYS 141 -0.98 SER 227
ARG 158 0.50 PRO 142 -1.05 SER 227
ARG 158 0.42 VAL 143 -0.58 SER 227
ASN 210 0.35 GLN 144 -0.40 MET 133
ASN 210 0.56 LEU 145 -0.35 THR 230
ASN 210 0.80 TRP 146 -0.60 GLY 112
ARG 209 0.98 VAL 147 -0.57 PRO 128
ASN 210 1.05 ASP 148 -0.62 PRO 128
ARG 209 1.08 SER 149 -0.50 PRO 128
ARG 209 1.02 THR 150 -0.45 PRO 128
ARG 209 1.12 PRO 151 -0.43 ALA 129
ARG 209 1.07 PRO 152 -0.35 ALA 129
ARG 209 0.86 PRO 153 -0.26 ALA 129
ARG 209 0.81 GLY 154 -0.26 LYS 101
ASP 208 0.92 THR 155 -0.29 THR 230
ASP 208 0.75 ARG 156 -0.32 SER 99
ASP 208 0.62 VAL 157 -0.39 SER 99
TYR 234 0.70 ARG 158 -0.63 SER 99
ASP 208 0.46 ALA 159 -0.54 ILE 232
GLY 262 0.56 MET 160 -0.49 ILE 232
GLY 262 0.48 ALA 161 -0.45 VAL 225
ASN 263 0.42 ILE 162 -0.40 VAL 225
SER 261 0.36 TYR 163 -0.45 GLY 226
SER 99 0.25 LYS 164 -0.40 GLY 226
SER 99 0.28 GLN 165 -0.44 GLY 226
SER 99 0.26 SER 166 -0.39 GLY 226
SER 261 0.27 GLN 167 -0.46 GLY 226
ASN 263 0.36 HIS 168 -0.49 GLY 226
ASN 263 0.35 MET 169 -0.41 GLY 226
LEU 264 0.50 THR 170 -0.42 GLY 226
ASN 263 0.62 GLU 171 -0.51 GLY 226
ASN 263 0.74 VAL 172 -0.50 GLY 226
GLY 262 0.66 VAL 173 -0.57 VAL 225
SER 261 0.74 ARG 174 -0.66 VAL 225
SER 261 0.71 ARG 175 -0.81 VAL 225
SER 261 0.66 CYS 176 -0.86 VAL 225
SER 261 0.69 PRO 177 -0.91 VAL 225
SER 261 0.64 HIS 178 -1.06 VAL 225
SER 261 0.66 HIS 179 -1.05 VAL 225
SER 261 0.76 GLU 180 -0.96 VAL 225
SER 261 0.70 ARG 181 -1.11 VAL 225
SER 261 0.62 CYS 182 -1.21 VAL 225
SER 261 0.66 SER 185 -1.04 VAL 225
SER 261 0.66 ASP 186 -0.95 GLU 224
SER 261 0.78 GLY 187 -0.84 GLU 224
SER 261 0.85 LEU 188 -0.83 GLU 224
SER 261 0.88 ALA 189 -0.77 GLU 224
SER 261 1.04 PRO 190 -0.70 VAL 225
SER 261 0.89 PRO 191 -0.83 VAL 225
SER 261 0.90 GLN 192 -0.74 VAL 225
SER 261 0.87 HIS 193 -0.69 VAL 225
SER 261 0.70 LEU 194 -0.73 VAL 225
SER 261 0.66 ILE 195 -0.66 VAL 225
SER 261 0.65 ARG 196 -0.81 GLU 224
SER 261 0.55 VAL 197 -0.92 GLU 224
SER 261 0.51 GLU 198 -1.16 GLU 224
SER 261 0.38 GLY 199 -1.47 GLU 224
SER 261 0.38 ASN 200 -1.16 GLU 224
SER 261 0.46 LEU 201 -1.04 GLU 224
SER 261 0.54 ARG 202 -0.77 GLU 224
SER 261 0.70 VAL 203 -0.78 GLU 224
SER 261 0.99 GLU 204 -0.60 GLU 224
SER 261 1.15 TYR 205 -0.60 GLU 224
GLY 262 1.49 LEU 206 -0.52 SER 96
GLY 262 1.41 ASP 207 -0.44 SER 96
LEU 264 1.84 ASP 208 -0.32 SER 96
SER 106 1.50 ARG 209 -0.53 PRO 177
SER 106 1.50 ASN 210 -0.50 PRO 177
LEU 264 1.13 THR 211 -0.38 GLY 226
ASN 263 1.25 PHE 212 -0.64 GLN 192
ASN 263 1.03 ARG 213 -0.56 SER 96
GLY 262 1.06 HIS 214 -0.48 SER 96
GLY 262 0.94 SER 215 -0.50 SER 96
GLY 262 0.84 VAL 216 -0.57 GLU 224
SER 261 0.57 VAL 217 -0.48 SER 99
HIS 233 0.49 VAL 218 -0.48 GLU 224
HIS 233 0.47 PRO 219 -0.33 SER 99
ARG 209 0.60 TYR 220 -0.31 THR 230
ARG 209 0.52 GLU 221 -0.52 ASN 200
ARG 209 0.69 PRO 222 -0.43 ASN 200
ASN 210 0.57 PRO 223 -0.67 GLY 199
SER 227 1.01 GLU 224 -1.47 GLY 199
SER 149 0.44 VAL 225 -1.21 CYS 182
SER 149 0.19 GLY 226 -0.89 HIS 178
GLU 224 1.01 SER 227 -1.08 THR 140
ASN 210 0.66 ASP 228 -0.64 GLY 199
ASN 210 0.49 CYS 229 -0.49 ASN 200
ASN 210 0.35 THR 230 -0.62 ASN 200
ASN 210 0.22 THR 231 -0.73 VAL 197
PRO 219 0.25 ILE 232 -0.64 THR 231
ARG 158 0.65 HIS 233 -0.93 GLU 224
ARG 158 0.70 TYR 234 -0.75 GLU 224
ARG 158 0.59 ASN 235 -0.86 VAL 225
SER 261 0.56 TYR 236 -0.85 VAL 225
SER 261 0.63 MET 237 -0.95 VAL 225
SER 261 0.58 CYS 238 -0.93 VAL 225
SER 261 0.49 ASN 239 -0.93 VAL 225
SER 261 0.42 SER 240 -0.80 VAL 225
SER 261 0.42 SER 241 -0.85 VAL 225
SER 261 0.50 CYS 242 -0.89 VAL 225
SER 261 0.59 GLY 245 -0.76 VAL 225
SER 261 0.50 MET 246 -0.70 VAL 225
SER 261 0.45 ASN 247 -0.75 VAL 225
SER 261 0.36 ARG 248 -0.72 VAL 225
SER 261 0.34 ARG 249 -0.62 VAL 225
SER 261 0.29 PRO 250 -0.57 VAL 225
SER 261 0.33 ILE 251 -0.53 VAL 225
ASP 208 0.26 LEU 252 -0.42 VAL 225
ASP 208 0.33 THR 253 -0.50 ILE 232
ASP 208 0.55 ILE 254 -0.45 ILE 232
ASP 208 0.66 ILE 255 -0.43 ILE 232
ASP 208 1.02 THR 256 -0.42 LYS 101
ASP 208 1.11 LEU 257 -0.36 THR 230
ASP 208 1.29 GLU 258 -0.44 LYS 101
ASP 208 1.19 ASP 259 -0.36 LYS 101
LEU 206 1.05 SER 260 -0.34 LYS 101
LEU 206 1.30 SER 261 -0.34 LYS 101
LEU 206 1.49 GLY 262 -0.45 LYS 101
ASP 208 1.41 ASN 263 -0.46 LYS 101
ASP 208 1.84 LEU 264 -0.50 LYS 101
ASP 208 1.52 LEU 265 -0.43 ALA 129
ASP 208 1.32 GLY 266 -0.49 ALA 129
ASP 208 1.04 ARG 267 -0.43 ALA 129
ASP 208 0.71 ASN 268 -0.48 ASN 131
ASP 208 0.47 SER 269 -0.33 LEU 289
PHE 113 0.45 PHE 270 -0.33 VAL 225
ASP 208 0.24 GLU 271 -0.45 VAL 225
SER 261 0.26 VAL 272 -0.60 VAL 225
SER 261 0.29 ARG 273 -0.72 VAL 225
SER 261 0.39 VAL 274 -0.86 VAL 225
SER 261 0.37 CYS 275 -0.94 VAL 225
SER 261 0.38 ALA 276 -1.05 VAL 225
SER 261 0.30 CYS 277 -0.97 VAL 225
SER 261 0.26 PRO 278 -0.87 VAL 225
ARG 158 0.21 GLY 279 -0.81 VAL 225
ASP 186 0.19 ARG 280 -0.80 VAL 225
SER 261 0.19 ASP 281 -0.75 VAL 225
ARG 158 0.14 ARG 282 -0.66 VAL 225
ASP 186 0.13 ARG 283 -0.63 VAL 225
GLU 287 0.16 THR 284 -0.63 VAL 225
ALA 129 0.11 GLU 285 -0.56 VAL 225
LEU 289 0.15 GLU 286 -0.51 ARG 110
THR 284 0.16 GLU 287 -0.56 GLY 108
SER 241 0.13 ASN 288 -0.49 VAL 225
GLU 286 0.15 LEU 289 -0.55 GLN 104

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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.