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CA distance fluctuations for 2402101815042310756

---  normal mode 11  ---

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
SER 261 0.89 SER 96 -0.41 ARG 290
ASN 263 0.82 VAL 97 -0.43 ARG 290
ASN 263 0.83 PRO 98 -0.37 ARG 290
ASN 263 0.50 SER 99 -0.35 ARG 290
ASN 263 0.35 GLN 100 -0.39 ARG 290
ASN 263 0.16 LYS 101 -0.35 ARG 290
PHE 113 0.10 THR 102 -0.37 ARG 290
ASN 210 0.11 TYR 103 -0.34 ARG 290
ASN 210 0.18 GLN 104 -0.35 ARG 290
ASN 210 0.26 GLY 105 -0.31 ARG 290
ASN 210 0.32 SER 106 -0.29 ARG 290
ASN 210 0.34 TYR 107 -0.30 ARG 290
ASN 210 0.24 GLY 108 -0.35 ARG 290
ASN 210 0.24 PHE 109 -0.33 ARG 290
ASN 210 0.15 ARG 110 -0.36 ARG 290
ASN 210 0.12 LEU 111 -0.31 ARG 290
GLY 199 0.11 GLY 112 -0.36 PRO 128
THR 102 0.10 PHE 113 -0.32 CYS 229
ASP 186 0.12 LEU 114 -0.40 SER 227
ASP 186 0.15 HIS 115 -0.50 SER 227
ASP 186 0.17 SER 116 -0.37 SER 227
ARG 290 0.22 GLY 117 -0.39 SER 227
ARG 290 0.25 THR 118 -0.33 SER 227
ARG 290 0.28 ALA 119 -0.29 GLY 226
ARG 290 0.23 LYS 120 -0.23 SER 227
ASP 184 0.25 SER 121 -0.19 SER 227
ASP 186 0.22 VAL 122 -0.21 SER 227
ASP 186 0.22 THR 123 -0.18 PRO 222
ASP 186 0.17 CYS 124 -0.19 PRO 222
ASP 186 0.14 THR 125 -0.27 SER 227
ASP 186 0.10 TYR 126 -0.29 GLY 112
ASP 186 0.08 SER 127 -0.34 ASP 228
ASP 186 0.06 PRO 128 -0.43 ASP 228
SER 127 0.07 ALA 129 -0.39 ASP 228
ALA 129 0.05 LEU 130 -0.42 ARG 290
LYS 132 0.07 ASN 131 -0.37 ARG 290
ASN 263 0.10 LYS 132 -0.27 ARG 290
ASN 263 0.09 LEU 133 -0.24 GLY 112
ASP 184 0.11 PHE 134 -0.20 GLY 112
ASP 184 0.14 CYS 135 -0.15 GLY 112
ASP 184 0.20 GLN 136 -0.12 PRO 222
ASP 184 0.19 LEU 137 -0.10 GLY 199
VAL 225 0.24 ALA 138 -0.12 GLY 199
ASP 186 0.25 LYS 139 -0.13 TYR 220
VAL 225 0.22 THR 140 -0.18 TYR 220
GLU 224 0.14 CYS 141 -0.19 TYR 220
GLY 187 0.12 PRO 142 -0.25 TYR 220
ASN 210 0.13 VAL 143 -0.24 TYR 220
ASN 210 0.17 GLN 144 -0.26 TYR 220
ASN 210 0.24 LEU 145 -0.27 PRO 128
ASN 210 0.23 TRP 146 -0.36 PRO 128
ASN 210 0.28 VAL 147 -0.33 ARG 290
ASN 210 0.27 ASP 148 -0.45 VAL 225
ASN 210 0.35 SER 149 -0.46 VAL 225
ASN 210 0.42 THR 150 -0.34 VAL 225
ASN 210 0.49 PRO 151 -0.26 ARG 290
ASN 210 0.59 PRO 152 -0.23 ARG 290
ASN 210 0.65 PRO 153 -0.27 THR 231
ASN 210 0.75 GLY 154 -0.21 ILE 232
ASN 210 0.66 THR 155 -0.22 ARG 290
ASN 210 0.59 ARG 156 -0.21 ARG 290
ASN 210 0.42 VAL 157 -0.22 ARG 290
GLU 224 0.36 ARG 158 -0.21 ARG 290
GLU 224 0.32 ALA 159 -0.22 ARG 290
GLY 262 0.34 MET 160 -0.25 ARG 290
GLY 262 0.37 ALA 161 -0.31 LEU 289
GLY 262 0.46 ILE 162 -0.39 LEU 289
GLY 262 0.43 TYR 163 -0.47 LEU 289
ASN 263 0.37 LYS 164 -0.57 LEU 289
ASN 263 0.41 GLN 165 -0.65 LEU 289
ASN 263 0.50 SER 166 -0.61 LEU 289
ASN 263 0.47 GLN 167 -0.56 LEU 289
SER 261 0.48 HIS 168 -0.50 LEU 289
ASN 263 0.55 MET 169 -0.49 LEU 289
SER 261 0.63 THR 170 -0.43 LEU 289
SER 261 0.55 GLU 171 -0.39 LEU 289
SER 261 0.55 VAL 172 -0.36 LEU 289
GLY 262 0.42 VAL 173 -0.33 LEU 289
SER 261 0.36 ARG 174 -0.27 LEU 289
SER 261 0.27 ARG 175 -0.21 LEU 289
SER 261 0.27 CYS 176 -0.20 LEU 289
SER 261 0.25 PRO 177 -0.21 ARG 209
VAL 225 0.24 HIS 178 -0.18 ARG 209
VAL 225 0.26 HIS 179 -0.16 ARG 209
VAL 225 0.31 GLU 180 -0.21 ARG 209
VAL 225 0.32 ARG 181 -0.22 ARG 209
VAL 225 0.32 CYS 182 -0.17 ARG 209
VAL 225 0.39 SER 183 -0.18 ARG 209
VAL 225 0.39 ASP 184 -0.13 ARG 209
VAL 225 0.47 SER 185 -0.12 ARG 209
VAL 225 0.55 ASP 186 -0.17 LEU 201
VAL 225 0.62 GLY 187 -0.11 SER 99
VAL 225 0.62 LEU 188 -0.13 SER 99
VAL 225 0.51 ALA 189 -0.13 SER 99
VAL 225 0.46 PRO 190 -0.15 LEU 289
VAL 225 0.40 PRO 191 -0.19 ARG 209
GLU 224 0.35 GLN 192 -0.22 ARG 209
GLU 224 0.35 HIS 193 -0.20 LEU 289
GLU 224 0.29 LEU 194 -0.20 LEU 289
GLU 224 0.33 ILE 195 -0.18 LEU 289
GLU 224 0.42 ARG 196 -0.13 LEU 289
GLU 224 0.51 VAL 197 -0.12 PRO 219
VAL 225 0.54 GLU 198 -0.17 PRO 219
VAL 225 0.76 GLY 199 -0.15 GLY 154
GLU 224 0.90 ASN 200 -0.14 GLU 198
GLU 224 0.90 LEU 201 -0.18 SER 260
GLU 224 0.79 ARG 202 -0.23 SER 260
GLU 224 0.70 ALA 203 -0.15 GLY 262
GLU 224 0.59 GLU 204 -0.16 LEU 264
GLU 224 0.52 TYR 205 -0.19 SER 99
GLU 224 0.49 LEU 206 -0.25 SER 99
SER 261 0.47 ASP 207 -0.24 SER 99
SER 261 0.83 ASP 208 -0.24 ARG 290
SER 261 1.01 ARG 209 -0.27 PHE 212
SER 261 1.22 ASN 210 -0.28 ARG 290
SER 261 0.97 THR 211 -0.32 ARG 290
SER 261 0.76 PHE 212 -0.31 LEU 289
SER 261 0.63 ARG 213 -0.30 LEU 289
SER 261 0.42 HIS 214 -0.26 LEU 289
GLU 224 0.39 SER 215 -0.23 SER 99
GLU 224 0.47 VAL 216 -0.18 LEU 289
GLU 224 0.50 VAL 217 -0.19 ARG 290
GLU 224 0.59 VAL 218 -0.17 ARG 290
ARG 209 0.54 PRO 219 -0.28 ILE 232
ASN 210 0.50 TYR 220 -0.33 ILE 232
ASN 210 0.45 GLU 221 -0.29 THR 231
ASN 210 0.42 PRO 222 -0.31 LEU 114
ASN 200 0.48 PRO 223 -0.36 HIS 115
ASN 200 0.90 GLU 224 -0.36 SER 149
LEU 201 0.89 VAL 225 -0.46 SER 149
LEU 201 0.70 GLY 226 -0.45 HIS 115
ASN 200 0.60 SER 227 -0.50 HIS 115
ASN 200 0.45 ASP 228 -0.43 PRO 128
ASN 200 0.36 CYS 229 -0.40 HIS 115
ASN 200 0.39 THR 230 -0.37 LEU 114
ASN 200 0.28 THR 231 -0.30 TYR 220
GLU 224 0.37 ILE 232 -0.33 TYR 220
GLU 224 0.34 HIS 233 -0.26 TYR 220
GLU 224 0.31 TYR 234 -0.16 PRO 219
GLU 224 0.28 ASN 235 -0.11 PRO 219
GLU 224 0.22 TYR 236 -0.13 LEU 289
VAL 225 0.25 MET 237 -0.11 GLY 199
GLU 224 0.19 CYS 238 -0.14 LEU 289
GLY 262 0.18 TYR 239 -0.14 LEU 289
GLY 262 0.22 SER 240 -0.22 LEU 289
GLY 262 0.22 SER 241 -0.19 LEU 289
SER 261 0.23 CYS 242 -0.17 LEU 289
SER 261 0.26 MET 243 -0.20 LEU 289
SER 261 0.31 GLY 244 -0.24 LEU 289
SER 261 0.31 GLY 245 -0.26 LEU 289
SER 261 0.31 MET 246 -0.31 LEU 289
SER 261 0.29 ASN 247 -0.29 LEU 289
GLY 262 0.27 ARG 248 -0.32 LEU 289
GLY 262 0.31 ARG 249 -0.44 LEU 289
ASN 263 0.28 PRO 250 -0.48 LEU 289
GLY 262 0.30 ILE 251 -0.41 LEU 289
ASN 263 0.27 LEU 252 -0.39 LEU 289
GLY 262 0.24 THR 253 -0.28 ARG 290
GLY 262 0.25 ILE 254 -0.30 ARG 290
PRO 98 0.20 ILE 255 -0.26 ARG 290
PRO 98 0.38 THR 256 -0.26 ARG 290
ASN 210 0.43 LEU 257 -0.25 ARG 290
ASN 210 0.63 GLU 258 -0.22 ARG 290
ASN 210 0.79 ASP 259 -0.21 ARG 290
ASN 210 0.98 SER 260 -0.23 ARG 202
ASN 210 1.22 SER 261 -0.21 ARG 202
ASN 210 0.99 GLY 262 -0.21 ARG 202
SER 96 0.88 ASN 263 -0.16 ARG 202
PRO 98 0.64 LEU 264 -0.22 ARG 290
PRO 98 0.46 LEU 265 -0.25 ARG 290
PRO 98 0.32 GLY 266 -0.29 ARG 290
PRO 98 0.21 ARG 267 -0.30 ARG 290
ASN 263 0.09 ASP 268 -0.34 ARG 290
ASN 263 0.14 SER 269 -0.34 ARG 290
ASN 263 0.14 PHE 270 -0.34 ARG 290
ASN 263 0.18 GLU 271 -0.37 LEU 289
GLY 262 0.17 VAL 272 -0.27 LEU 289
GLY 262 0.17 HIS 273 -0.22 LEU 289
GLY 262 0.15 VAL 274 -0.14 LEU 289
ASP 184 0.14 CYS 275 -0.13 ARG 248
ASP 184 0.21 ALA 276 -0.13 GLY 112
ASP 184 0.22 CYS 277 -0.15 CYS 229
ASP 184 0.17 PRO 278 -0.19 SER 227
GLU 287 0.18 GLY 279 -0.25 SER 227
GLU 287 0.25 ARG 280 -0.24 SER 227
THR 284 0.16 ASP 281 -0.21 SER 227
ASP 184 0.12 ARG 282 -0.26 SER 227
GLU 287 0.24 ARG 283 -0.31 GLY 226
GLU 287 0.22 THR 284 -0.27 GLY 226
ASP 184 0.07 GLU 285 -0.30 GLN 165
LEU 289 0.16 GLU 286 -0.35 GLN 165
ARG 280 0.25 GLU 287 -0.36 GLN 165
ARG 283 0.10 ASN 288 -0.43 GLN 165
GLU 286 0.16 LEU 289 -0.65 GLN 165
ALA 119 0.28 ARG 290 -0.59 SER 166

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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.