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CA distance fluctuations for 2404140446434184336

---  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
ASN 210 0.52 VAL 97 -0.16 SER 215
ASN 210 0.66 PRO 98 -0.14 SER 215
ASN 210 0.67 SER 99 -0.11 SER 166
ASN 210 0.53 GLN 100 -0.16 SER 166
ASN 210 0.57 LYS 101 -0.19 SER 166
ASN 210 0.57 THR 102 -0.16 GLN 165
ARG 209 0.70 TYR 103 -0.12 SER 166
ARG 209 0.68 GLN 104 -0.11 GLN 165
ARG 209 0.80 GLY 105 -0.09 SER 166
ARG 209 0.80 SER 106 -0.08 SER 166
ARG 209 0.74 TYR 107 -0.08 GLN 165
ARG 209 0.66 GLY 108 -0.10 GLN 165
ARG 209 0.64 PHE 109 -0.10 GLN 165
ARG 209 0.53 ARG 110 -0.12 GLN 165
ARG 209 0.43 LEU 111 -0.10 ASN 247
ARG 209 0.35 GLY 112 -0.19 PRO 128
ARG 209 0.26 PHE 113 -0.22 GLY 226
ARG 209 0.20 LEU 114 -0.27 GLY 226
ASN 210 0.15 HIS 115 -0.29 GLY 226
ASP 208 0.11 SER 116 -0.23 GLY 226
LYS 101 0.08 SER 121 -0.16 GLY 226
LYS 101 0.08 VAL 122 -0.18 GLY 226
LYS 101 0.06 THR 123 -0.14 GLY 226
ASP 208 0.10 CYS 124 -0.16 GLY 226
ASN 210 0.13 THR 125 -0.22 GLY 226
ASN 210 0.20 TYR 126 -0.22 GLY 226
ASN 210 0.23 SER 127 -0.24 GLY 226
ASN 210 0.29 PRO 128 -0.25 GLY 226
ASN 210 0.30 ALA 129 -0.24 GLY 226
ASN 210 0.30 LEU 130 -0.18 GLY 226
ASN 210 0.32 ASN 131 -0.17 GLY 226
ASN 210 0.25 LYS 132 -0.16 GLY 226
ASN 210 0.19 MET 133 -0.15 GLY 226
ASP 208 0.12 PHE 134 -0.15 GLY 226
ASP 208 0.08 CYS 135 -0.12 GLY 226
MET 246 0.08 GLN 136 -0.15 PHE 212
MET 246 0.10 LEU 137 -0.19 PHE 212
MET 246 0.09 ALA 138 -0.18 PHE 212
MET 246 0.07 LYS 139 -0.14 PHE 212
ASP 208 0.06 THR 140 -0.11 ASP 186
ASP 208 0.13 CYS 141 -0.10 GLY 226
ARG 209 0.18 PRO 142 -0.12 GLY 226
ARG 209 0.27 VAL 143 -0.10 GLY 226
ARG 209 0.36 GLN 144 -0.13 PRO 128
ARG 209 0.47 LEU 145 -0.12 PRO 128
ARG 209 0.51 TRP 146 -0.15 PRO 128
ARG 209 0.60 VAL 147 -0.12 PRO 128
ARG 209 0.59 ASP 148 -0.12 PRO 128
ARG 209 0.65 SER 149 -0.10 PRO 128
ARG 209 0.67 THR 150 -0.10 PRO 128
ARG 209 0.77 PRO 151 -0.07 PRO 128
ARG 209 0.82 PRO 152 -0.07 THR 231
ARG 209 0.76 PRO 153 -0.09 THR 231
ARG 209 0.81 GLY 154 -0.08 THR 231
ARG 209 0.85 THR 155 -0.07 THR 231
ARG 209 0.76 ARG 156 -0.07 PRO 219
ARG 209 0.64 VAL 157 -0.07 SER 99
ARG 209 0.55 ARG 158 -0.12 PRO 98
ASP 208 0.42 ALA 159 -0.10 PRO 98
ASP 208 0.38 MET 160 -0.12 VAL 97
ASP 208 0.24 ALA 161 -0.07 VAL 172
LEU 289 0.30 ILE 162 -0.10 VAL 172
LEU 289 0.36 TYR 163 -0.10 VAL 172
LEU 289 0.45 LYS 164 -0.15 THR 102
LEU 289 0.50 GLN 165 -0.17 LYS 101
LEU 289 0.47 SER 166 -0.19 LYS 101
ARG 290 0.44 GLN 167 -0.14 LYS 101
ARG 290 0.37 HIS 168 -0.11 PHE 212
LEU 289 0.38 MET 169 -0.10 LYS 101
LEU 289 0.32 THR 170 -0.06 PHE 212
LEU 289 0.28 GLU 171 -0.23 PHE 212
LEU 289 0.20 VAL 172 -0.25 PHE 212
LEU 289 0.22 VAL 173 -0.31 PHE 212
LEU 289 0.18 ARG 174 -0.46 PHE 212
LEU 289 0.15 ARG 175 -0.43 ARG 209
MET 246 0.18 CYS 176 -0.51 ARG 209
MET 246 0.18 PRO 177 -0.64 ARG 209
MET 246 0.17 HIS 178 -0.54 ARG 209
MET 246 0.15 HIS 179 -0.47 ARG 209
MET 246 0.14 GLU 180 -0.56 ARG 209
GLY 187 0.17 ARG 181 -0.55 ARG 209
ARG 181 0.15 ASP 186 -0.22 ARG 209
ARG 181 0.17 GLY 187 -0.29 ARG 209
ARG 181 0.13 LEU 188 -0.19 ARG 209
GLU 204 0.11 ALA 189 -0.22 ARG 209
SER 261 0.15 PRO 190 -0.40 ARG 209
SER 261 0.14 PRO 191 -0.50 ARG 209
SER 261 0.15 GLN 192 -0.53 ARG 209
SER 261 0.14 HIS 193 -0.29 ARG 209
LEU 289 0.14 LEU 194 -0.26 PHE 212
LEU 289 0.12 ILE 195 -0.14 PHE 212
GLU 224 0.09 ARG 196 -0.11 PHE 212
ASP 208 0.10 VAL 197 -0.07 VAL 97
GLU 224 0.09 GLU 198 -0.08 LEU 188
GLU 224 0.14 GLY 199 -0.07 SER 116
GLU 224 0.19 ASN 200 -0.06 SER 116
VAL 225 0.21 LEU 201 -0.07 VAL 97
ARG 209 0.24 ARG 202 -0.08 VAL 97
ARG 209 0.20 VAL 203 -0.09 VAL 97
ARG 209 0.20 GLU 204 -0.12 VAL 97
SER 261 0.14 TYR 205 -0.11 VAL 97
SER 261 0.24 LEU 206 -0.14 VAL 97
GLY 262 0.46 ASP 207 -0.29 ASP 208
GLY 262 0.96 ASP 208 -0.30 GLN 192
ASN 263 1.44 ARG 209 -0.64 PRO 177
ASN 263 1.05 ASN 210 -0.45 PRO 177
ASN 263 0.52 THR 211 -0.23 PRO 177
GLY 262 0.57 PHE 212 -0.46 ARG 174
GLY 262 0.25 ARG 213 -0.08 GLN 192
GLY 262 0.21 HIS 214 -0.10 VAL 97
ASP 208 0.27 SER 215 -0.16 VAL 97
ASP 208 0.25 VAL 216 -0.12 VAL 97
ARG 209 0.43 VAL 217 -0.12 PRO 98
ARG 209 0.43 VAL 218 -0.08 PRO 98
ARG 209 0.56 PRO 219 -0.08 ILE 232
ARG 209 0.61 TYR 220 -0.11 THR 231
ARG 209 0.52 GLU 221 -0.12 THR 231
ARG 209 0.53 PRO 222 -0.11 PRO 128
ARG 209 0.45 PRO 223 -0.15 PRO 128
ARG 209 0.41 GLU 224 -0.17 HIS 115
ARG 209 0.40 VAL 225 -0.22 ARG 290
ARG 209 0.33 GLY 226 -0.29 ARG 290
ARG 209 0.35 SER 227 -0.25 ARG 290
ARG 209 0.40 ASP 228 -0.22 ARG 290
ARG 209 0.42 CYS 229 -0.18 PRO 128
ARG 209 0.43 THR 230 -0.14 PRO 128
ARG 209 0.32 THR 231 -0.12 GLU 221
ARG 209 0.28 ILE 232 -0.11 TYR 220
ASP 208 0.16 HIS 233 -0.07 THR 125
ASP 208 0.13 TYR 234 -0.06 THR 125
MET 246 0.06 ASN 235 -0.12 PHE 212
LEU 289 0.09 TYR 236 -0.17 PHE 212
MET 246 0.10 MET 237 -0.24 PHE 212
MET 246 0.12 CYS 238 -0.27 ARG 209
MET 246 0.12 CYS 238 -0.27 PHE 212
MET 246 0.12 ASN 239 -0.24 PHE 212
LEU 289 0.17 SER 240 -0.20 PHE 212
MET 246 0.16 SER 241 -0.23 ARG 209
MET 246 0.20 CYS 242 -0.33 ARG 209
LEU 289 0.20 MET 243 -0.29 PHE 212
LEU 289 0.23 GLY 244 -0.20 PHE 212
ARG 290 0.20 GLY 245 -0.25 ARG 209
ARG 290 0.20 MET 246 -0.22 ARG 209
ARG 290 0.27 ASN 247 -0.14 ARG 209
ASN 288 0.27 ARG 248 -0.13 PHE 212
LEU 289 0.35 ARG 249 -0.14 PHE 212
LEU 289 0.37 PRO 250 -0.10 ARG 110
LEU 289 0.31 ILE 251 -0.09 SER 269
LEU 289 0.29 LEU 252 -0.10 SER 269
ASP 208 0.31 THR 253 -0.07 LEU 252
ASP 208 0.45 ILE 254 -0.09 SER 166
ARG 209 0.52 ILE 255 -0.08 SER 166
ARG 209 0.73 THR 256 -0.08 SER 166
ARG 209 0.82 LEU 257 -0.07 SER 166
ARG 209 1.02 GLU 258 -0.05 SER 166
ARG 209 1.12 ASP 259 -0.05 THR 231
ARG 209 1.07 SER 260 -0.06 ARG 202
ARG 209 1.35 SER 261 -0.05 ARG 202
ARG 209 1.35 GLY 262 -0.06 ARG 202
ARG 209 1.44 ASN 263 -0.04 ARG 202
ARG 209 1.16 LEU 264 -0.05 SER 166
ARG 209 1.00 LEU 265 -0.06 SER 166
ARG 209 0.83 GLY 266 -0.09 SER 166
ARG 209 0.70 ARG 267 -0.10 SER 166
ARG 209 0.53 ASN 268 -0.13 LYS 164
ASN 210 0.44 SER 269 -0.13 LYS 164
ASN 210 0.34 PHE 270 -0.11 ASN 247
ASN 210 0.27 GLU 271 -0.11 ASN 247
LEU 289 0.18 VAL 272 -0.10 GLY 226
LEU 289 0.15 ARG 273 -0.10 GLY 226
LEU 289 0.10 VAL 274 -0.15 PHE 212
MET 246 0.08 CYS 275 -0.17 PHE 212
MET 246 0.09 ALA 276 -0.18 PHE 212
GLN 165 0.08 CYS 277 -0.14 PHE 212
GLN 165 0.08 PRO 278 -0.15 GLY 226
LYS 101 0.10 GLY 279 -0.20 GLY 226
GLN 165 0.12 ARG 280 -0.18 GLY 226
GLN 165 0.14 ASP 281 -0.16 GLY 226
GLN 165 0.15 ARG 282 -0.20 GLY 226
GLN 165 0.18 ARG 283 -0.23 GLY 226
GLN 165 0.21 THR 284 -0.19 GLY 226
GLN 165 0.27 GLU 285 -0.19 GLY 226
GLN 165 0.28 GLU 286 -0.24 GLY 226
GLN 165 0.32 GLU 287 -0.24 GLY 226
GLN 165 0.43 ASN 288 -0.20 GLY 226
GLN 165 0.50 LEU 289 -0.22 GLY 226
GLN 165 0.48 ARG 290 -0.29 GLY 226

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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.