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CA distance fluctuations for 2402182157513347386

---  normal mode 14  ---

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
GLU 204 0.12 SER 96 -0.27 ASN 288
ASN 210 0.14 VAL 97 -0.29 ASN 288
ASN 210 0.19 PRO 98 -0.27 ASN 288
PRO 128 0.17 SER 99 -0.30 ASN 288
PRO 128 0.19 GLN 100 -0.33 ASN 288
PRO 128 0.28 LYS 101 -0.31 ASN 288
PRO 128 0.36 THR 102 -0.27 ASN 288
HIS 115 0.41 TYR 103 -0.21 PRO 98
HIS 115 0.50 GLN 104 -0.18 ASN 288
HIS 115 0.44 GLY 105 -0.19 PRO 98
GLY 226 0.55 SER 106 -0.17 ARG 213
GLY 226 0.55 TYR 107 -0.14 ASN 288
HIS 115 0.54 GLY 108 -0.18 PRO 222
HIS 115 0.49 PHE 109 -0.17 ASN 288
HIS 115 0.58 ARG 110 -0.20 ASN 288
PHE 113 0.50 LEU 111 -0.29 SER 227
LEU 114 0.59 GLY 112 -0.45 SER 227
GLY 112 0.54 PHE 113 -0.63 GLY 226
GLY 112 0.59 LEU 114 -0.71 GLY 226
ARG 110 0.58 HIS 115 -0.65 GLY 226
GLY 112 0.54 SER 116 -0.50 GLY 226
ASP 148 0.49 GLY 117 -0.42 GLY 226
ASP 148 0.41 THR 118 -0.31 GLY 226
ASP 148 0.47 ALA 119 -0.29 ARG 248
PRO 223 0.43 LYS 120 -0.37 ARG 248
PRO 223 0.54 SER 121 -0.40 SER 241
GLN 144 0.50 VAL 122 -0.27 GLY 226
PRO 142 0.40 THR 123 -0.37 GLY 226
GLN 144 0.34 CYS 124 -0.45 GLY 226
PHE 113 0.40 THR 125 -0.46 GLY 226
ARG 110 0.32 TYR 126 -0.52 GLY 226
GLN 104 0.26 SER 127 -0.50 GLY 226
THR 102 0.36 PRO 128 -0.57 GLY 226
LEU 130 0.19 ALA 129 -0.53 GLY 226
ARG 248 0.22 LEU 130 -0.46 GLY 226
THR 102 0.19 ASN 131 -0.45 GLY 226
SER 241 0.16 LYS 132 -0.44 GLY 226
GLN 104 0.17 MET 133 -0.44 GLY 226
GLN 104 0.17 MET 133 -0.44 GLY 226
ASP 148 0.16 PHE 134 -0.41 GLY 226
PRO 223 0.19 CYS 135 -0.41 GLY 226
PRO 223 0.23 GLN 136 -0.37 GLY 226
PRO 223 0.19 LEU 137 -0.36 GLY 226
PRO 223 0.21 ALA 138 -0.38 GLY 226
PRO 223 0.27 LYS 139 -0.44 GLY 226
PRO 223 0.31 THR 140 -0.51 GLY 226
VAL 122 0.29 CYS 141 -0.51 GLY 226
VAL 122 0.29 CYS 141 -0.51 GLY 226
VAL 122 0.48 PRO 142 -0.58 GLY 226
VAL 122 0.43 VAL 143 -0.55 SER 227
VAL 122 0.50 GLN 144 -0.55 SER 227
VAL 122 0.44 LEU 145 -0.21 SER 227
SER 116 0.50 TRP 146 -0.20 CYS 229
HIS 115 0.50 VAL 147 -0.27 PRO 222
SER 227 0.58 ASP 148 -0.26 PRO 222
SER 227 0.81 SER 149 -0.16 PRO 222
SER 227 0.83 THR 150 -0.10 GLU 221
GLY 226 0.69 PRO 151 -0.11 ASN 288
VAL 225 0.78 PRO 152 -0.12 TYR 205
VAL 225 0.96 PRO 153 -0.09 PRO 190
VAL 225 0.75 GLY 154 -0.15 LEU 188
VAL 225 0.60 THR 155 -0.15 TYR 205
VAL 225 0.43 ARG 156 -0.13 LEU 188
VAL 225 0.27 PHE 157 -0.14 ASN 288
ASN 210 0.24 ARG 158 -0.15 VAL 216
ASN 210 0.19 ALA 159 -0.22 SER 227
ASN 210 0.12 MET 160 -0.19 ASN 263
ILE 162 0.06 ALA 161 -0.23 SER 227
PRO 128 0.06 ILE 162 -0.28 THR 284
ARG 175 0.07 TYR 163 -0.37 THR 284
ASN 247 0.07 LYS 164 -0.45 GLU 285
CYS 176 0.08 GLN 165 -0.55 THR 284
SER 96 0.08 SER 166 -0.50 ASN 288
GLU 171 0.12 GLN 167 -0.51 THR 284
ARG 174 0.11 HIS 168 -0.44 THR 284
HIS 214 0.09 MET 169 -0.38 THR 284
ARG 213 0.12 THR 170 -0.34 THR 284
PRO 190 0.12 GLU 171 -0.32 THR 284
PRO 190 0.11 VAL 172 -0.28 THR 284
HIS 168 0.10 VAL 173 -0.25 CYS 275
HIS 168 0.11 ARG 174 -0.34 ARG 209
HIS 168 0.10 ARG 175 -0.34 ARG 209
GLY 245 0.15 CYS 176 -0.41 ARG 209
LEU 289 0.13 PRO 177 -0.50 ARG 209
LEU 289 0.17 HIS 178 -0.40 ARG 209
LEU 289 0.14 HIS 179 -0.34 ARG 209
PRO 223 0.12 GLU 180 -0.42 ARG 209
PRO 223 0.13 ARG 181 -0.43 ARG 209
PRO 223 0.16 CYS 182 -0.33 ARG 209
ALA 138 0.20 SER 183 -0.33 ARG 209
PRO 223 0.21 ASP 184 -0.25 GLY 226
PRO 223 0.18 SER 185 -0.25 SER 261
PRO 223 0.21 ASP 186 -0.25 GLY 226
VAL 225 0.20 GLY 187 -0.28 SER 261
VAL 225 0.23 LEU 188 -0.29 SER 261
VAL 225 0.19 ALA 189 -0.29 SER 261
VAL 225 0.18 PRO 190 -0.33 SER 261
VAL 225 0.13 PRO 191 -0.33 ARG 209
VAL 225 0.11 GLN 192 -0.40 ARG 209
GLU 171 0.12 HIS 193 -0.26 GLY 262
PRO 223 0.11 LEU 194 -0.25 SER 227
PRO 223 0.13 ILE 195 -0.28 SER 227
PRO 223 0.17 ARG 196 -0.29 SER 227
PRO 223 0.23 VAL 197 -0.32 SER 227
PRO 223 0.29 GLU 198 -0.38 GLY 226
PRO 223 0.33 GLY 199 -0.39 GLY 226
PRO 223 0.30 ASN 200 -0.30 SER 227
VAL 225 0.33 LEU 201 -0.23 SER 227
VAL 225 0.38 ARG 202 -0.19 SER 227
VAL 225 0.31 VAL 203 -0.20 SER 227
VAL 225 0.32 GLU 204 -0.28 SER 261
LEU 206 0.27 TYR 205 -0.38 GLY 262
GLU 204 0.28 LEU 206 -0.46 GLY 262
VAL 225 0.23 ASP 207 -0.39 ASN 263
GLU 204 0.30 ASP 208 -0.29 ASN 263
VAL 225 0.36 ARG 209 -0.50 PRO 177
VAL 225 0.32 ASN 210 -0.35 PRO 177
VAL 225 0.20 THR 211 -0.23 ASN 263
GLU 204 0.20 PHE 212 -0.33 ARG 209
VAL 225 0.14 ARG 213 -0.33 ASN 263
VAL 225 0.15 HIS 214 -0.35 ASN 263
ASP 208 0.20 SER 215 -0.32 ASN 263
ASP 208 0.25 VAL 216 -0.25 GLY 262
ARG 209 0.31 VAL 217 -0.19 GLY 262
VAL 225 0.34 VAL 218 -0.16 SER 227
VAL 225 0.47 PRO 219 -0.11 ASN 288
VAL 225 0.48 TYR 220 -0.11 ASN 288
VAL 225 0.56 GLU 221 -0.18 VAL 147
VAL 225 0.55 PRO 222 -0.27 VAL 147
SER 121 0.54 PRO 223 -0.30 GLU 224
SER 121 0.52 GLU 224 -0.30 PRO 223
PRO 153 0.96 VAL 225 -0.46 ALA 129
THR 150 0.83 GLY 226 -0.71 LEU 114
THR 150 0.83 SER 227 -0.68 THR 231
THR 150 0.78 ASP 228 -0.43 ALA 129
SER 121 0.53 CYS 229 -0.30 ALA 129
SER 121 0.50 THR 230 -0.40 SER 227
SER 121 0.50 THR 231 -0.68 SER 227
VAL 122 0.37 ILE 232 -0.51 SER 227
VAL 122 0.32 HIS 233 -0.48 SER 227
VAL 122 0.21 TYR 234 -0.39 SER 227
PRO 223 0.20 ASN 235 -0.38 GLY 226
PRO 223 0.15 TYR 236 -0.34 GLY 226
PRO 223 0.16 MET 237 -0.30 GLY 226
LEU 289 0.13 CYS 238 -0.29 GLY 226
LEU 289 0.19 ASN 239 -0.31 GLY 226
LEU 289 0.22 SER 240 -0.43 CYS 275
LEU 289 0.28 SER 241 -0.52 ALA 276
LEU 289 0.22 CYS 242 -0.36 ALA 276
LEU 289 0.22 MET 243 -0.34 ARG 209
LEU 289 0.17 GLY 244 -0.42 ARG 209
CYS 176 0.15 GLY 245 -0.37 ARG 209
LEU 289 0.13 MET 246 -0.34 CYS 277
LEU 289 0.20 ASN 247 -0.40 CYS 277
LEU 289 0.25 ARG 248 -0.50 CYS 277
ASN 247 0.14 ARG 249 -0.50 ASP 281
ARG 248 0.19 PRO 250 -0.50 ASP 281
ARG 248 0.11 ILE 251 -0.33 ARG 273
ARG 248 0.10 LEU 252 -0.29 SER 227
ASN 210 0.09 THR 253 -0.29 SER 227
ASN 210 0.14 ILE 254 -0.23 ASN 288
VAL 122 0.21 ILE 255 -0.19 ASN 288
VAL 122 0.21 THR 256 -0.19 ASN 288
VAL 122 0.27 LEU 257 -0.16 ASN 288
VAL 225 0.37 GLU 258 -0.21 LEU 206
VAL 225 0.53 ASP 259 -0.24 LEU 206
VAL 225 0.59 SER 260 -0.26 TYR 205
VAL 225 0.52 SER 261 -0.42 LEU 206
VAL 225 0.42 GLY 262 -0.46 LEU 206
VAL 225 0.40 ASN 263 -0.42 LEU 206
VAL 225 0.31 LEU 264 -0.32 LEU 206
GLY 226 0.38 LEU 265 -0.22 LEU 206
HIS 115 0.36 GLY 266 -0.18 ARG 213
HIS 115 0.31 ARG 267 -0.21 ASN 288
HIS 115 0.32 ASN 268 -0.24 ASN 288
THR 125 0.18 SER 269 -0.28 ASN 288
THR 102 0.13 PHE 270 -0.37 SER 227
ARG 248 0.20 GLU 271 -0.36 SER 227
SER 240 0.16 VAL 272 -0.37 GLY 226
SER 241 0.18 ARG 273 -0.37 GLY 226
LEU 289 0.14 VAL 274 -0.35 GLY 226
GLU 285 0.17 CYS 275 -0.43 SER 240
PRO 223 0.24 ALA 276 -0.52 SER 241
PRO 223 0.27 CYS 277 -0.50 ARG 248
PRO 223 0.28 CYS 277 -0.50 ARG 248
ASP 148 0.24 PRO 278 -0.35 ARG 249
ASP 148 0.32 GLY 279 -0.33 ARG 249
ASP 148 0.25 ARG 280 -0.46 ARG 249
ASP 148 0.15 ASP 281 -0.50 PRO 250
ASP 148 0.17 ARG 282 -0.36 GLY 226
ASP 148 0.23 ARG 283 -0.37 GLN 165
SER 183 0.14 THR 284 -0.55 GLN 165
CYS 275 0.17 GLU 285 -0.54 GLN 165
SER 183 0.11 GLU 286 -0.39 GLY 226
SER 183 0.12 GLU 287 -0.45 GLN 165
SER 241 0.20 ASN 288 -0.50 SER 166
SER 241 0.28 LEU 289 -0.45 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.