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CA distance fluctuations for 2604261910212506628

---  normal mode 12  ---

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
ALA 215 0.07 LYS 1 -0.05 ASN 124
LYS 142 0.07 ILE 2 -0.06 ASN 124
LYS 142 0.08 GLU 3 -0.07 ASN 124
LYS 142 0.08 GLU 4 -0.07 ASN 124
LYS 142 0.08 GLY 5 -0.08 ASN 124
LYS 142 0.09 LYS 6 -0.09 ASN 124
LYS 142 0.09 LEU 7 -0.09 ASN 124
LYS 142 0.09 VAL 8 -0.08 ASN 124
LYS 142 0.10 ILE 9 -0.09 ASN 124
LYS 142 0.10 TRP 10 -0.08 ASN 124
LYS 142 0.11 ILE 11 -0.09 ASN 124
ALA 215 0.12 ASN 12 -0.09 ASP 236
LYS 142 0.12 GLY 13 -0.14 SER 233
LYS 142 0.13 ASP 14 -0.16 TRP 232
LYS 142 0.14 LYS 15 -0.12 ASN 124
LYS 142 0.14 GLY 16 -0.13 ASN 124
LYS 142 0.13 TYR 17 -0.12 ASN 124
LYS 142 0.13 ASN 18 -0.12 ASN 124
LYS 142 0.14 GLY 19 -0.14 ASN 124
LYS 142 0.13 LEU 20 -0.12 ASN 124
LYS 142 0.12 ALA 21 -0.12 ASN 124
PRO 81 0.13 GLU 22 -0.13 PRO 123
PRO 81 0.16 VAL 23 -0.13 ASN 124
PRO 81 0.14 GLY 24 -0.11 ASN 124
PRO 81 0.13 LYS 25 -0.12 PRO 123
PRO 81 0.16 LYS 26 -0.13 PRO 123
PRO 81 0.17 PHE 27 -0.11 PRO 123
PRO 81 0.14 GLU 28 -0.11 PRO 123
PRO 81 0.15 LYS 29 -0.12 PRO 123
PRO 81 0.17 ASP 30 -0.11 PRO 123
PRO 81 0.15 THR 31 -0.10 PRO 123
PRO 81 0.12 GLY 32 -0.10 PRO 123
PRO 81 0.11 ILE 33 -0.10 ASN 124
LYS 142 0.10 LYS 34 -0.09 ASN 124
PRO 81 0.10 VAL 35 -0.10 ASN 124
LYS 142 0.10 THR 36 -0.09 ASN 124
LYS 142 0.11 VAL 37 -0.09 ASN 124
LYS 142 0.10 GLU 38 -0.08 ASN 124
LYS 142 0.10 HIS 39 -0.10 ASP 236
ALA 215 0.10 PRO 40 -0.12 SER 233
ALA 215 0.12 ASP 41 -0.15 SER 233
ALA 215 0.13 LYS 42 -0.15 SER 233
ALA 215 0.12 LEU 43 -0.10 SER 233
ALA 215 0.13 GLU 44 -0.11 TYR 70
ALA 215 0.13 GLU 45 -0.10 SER 233
ALA 215 0.11 LYS 46 -0.09 SER 233
ALA 215 0.11 PHE 47 -0.07 LEU 75
ARG 66 0.12 PRO 48 -0.09 SER 73
ALA 215 0.11 GLN 49 -0.07 SER 233
ALA 215 0.10 VAL 50 -0.06 SER 233
ALA 215 0.10 ALA 51 -0.05 ALA 268
TYR 70 0.12 ALA 52 -0.04 SER 233
ALA 215 0.09 THR 53 -0.05 SER 233
ALA 215 0.08 GLY 54 -0.04 ASP 236
ALA 215 0.09 ASP 55 -0.05 ASP 236
ALA 215 0.09 GLY 56 -0.06 ASP 236
LYS 142 0.09 PRO 57 -0.07 ASN 124
LYS 142 0.09 ASP 58 -0.07 ASN 124
LYS 142 0.09 ILE 59 -0.08 ASN 124
LYS 142 0.10 ILE 60 -0.07 ASN 124
LYS 142 0.11 PHE 61 -0.08 ASN 124
ALA 215 0.11 TRP 62 -0.09 TRP 230
ALA 215 0.11 ALA 63 -0.12 TRP 230
GLU 214 0.09 HIS 64 -0.11 TRP 340
GLU 214 0.10 ASP 65 -0.13 SER 337
PRO 48 0.12 ARG 66 -0.12 SER 337
PRO 48 0.09 PHE 67 -0.10 SER 337
GLU 214 0.08 GLY 68 -0.11 SER 337
ALA 52 0.11 GLY 69 -0.11 SER 337
ALA 52 0.12 TYR 70 -0.11 GLU 44
ALA 215 0.07 ALA 71 -0.08 SER 337
ASP 177 0.09 GLN 72 -0.09 SER 337
ASP 177 0.09 SER 73 -0.09 GLU 44
GLY 54 0.07 GLY 74 -0.08 GLU 44
ALA 215 0.08 LEU 75 -0.08 GLU 44
ALA 215 0.08 LEU 76 -0.07 GLU 44
LYS 277 0.10 ALA 77 -0.07 SER 337
GLU 281 0.12 GLU 78 -0.08 SER 337
GLU 281 0.18 ILE 79 -0.07 PRO 81
GLU 281 0.25 THR 80 -0.07 LYS 102
GLU 281 0.41 PRO 81 -0.19 LEU 103
ASN 282 0.28 ASP 82 -0.17 ASN 173
ASN 282 0.18 LYS 83 -0.16 ASN 173
THR 286 0.19 ALA 84 -0.12 GLU 172
THR 286 0.24 PHE 85 -0.11 GLU 172
THR 286 0.17 GLN 86 -0.13 GLU 172
SER 233 0.14 ASP 87 -0.10 GLU 172
SER 233 0.17 LYS 88 -0.12 GLU 281
SER 233 0.17 LEU 89 -0.10 ASN 124
SER 233 0.15 TYR 90 -0.10 ASN 124
SER 233 0.12 PRO 91 -0.12 GLU 172
LYS 142 0.11 PHE 92 -0.11 TYR 171
LYS 142 0.12 THR 93 -0.08 TRP 340
LYS 142 0.11 TRP 94 -0.12 GLN 86
LYS 142 0.09 ASP 95 -0.11 PRO 81
LYS 142 0.09 ALA 96 -0.09 SER 337
LYS 142 0.09 VAL 97 -0.10 PRO 81
GLU 214 0.08 ARG 98 -0.14 PRO 81
GLU 214 0.07 TYR 99 -0.14 ILE 333
GLU 214 0.07 ASN 100 -0.13 ILE 333
GLU 214 0.07 GLY 101 -0.15 PRO 81
LYS 142 0.07 LYS 102 -0.17 PRO 81
LYS 142 0.08 LEU 103 -0.19 PRO 81
LYS 142 0.08 ILE 104 -0.09 PRO 81
LYS 142 0.10 ALA 105 -0.08 PHE 85
LYS 142 0.11 TYR 106 -0.08 ASN 124
LYS 142 0.12 PRO 107 -0.09 ASN 124
LYS 142 0.14 ILE 108 -0.10 ASN 124
LYS 142 0.15 ALA 109 -0.12 ASN 124
LYS 142 0.15 VAL 110 -0.12 ASN 124
LYS 142 0.15 GLU 111 -0.13 ASN 124
LYS 142 0.13 ALA 112 -0.12 ASN 124
LYS 142 0.14 LEU 113 -0.14 ASN 124
LYS 142 0.18 SER 114 -0.18 ASN 124
GLU 138 0.21 LEU 115 -0.18 ASN 124
LYS 142 0.28 ILE 116 -0.21 ASN 124
LEU 139 0.42 TYR 117 -0.12 PRO 123
LYS 142 0.58 ASN 118 -0.11 GLU 214
LYS 142 0.70 LYS 119 -0.12 LYS 295
LYS 142 0.94 ASP 120 -0.10 LYS 295
LEU 139 1.06 LEU 121 -0.08 GLY 220
GLU 138 0.93 LEU 122 -0.13 THR 245
GLU 138 0.92 PRO 123 -0.24 PRO 315
GLU 138 0.74 ASN 124 -0.33 THR 245
GLU 138 0.53 PRO 125 -0.19 THR 245
LEU 135 0.48 PRO 126 -0.11 THR 245
LEU 135 0.29 LYS 127 -0.08 ALA 318
LEU 198 0.30 THR 128 -0.06 GLU 309
LEU 198 0.38 TRP 129 -0.20 PRO 133
ASP 197 0.52 GLU 130 -0.18 ALA 134
LEU 198 0.41 GLU 131 -0.09 ALA 223
LEU 198 0.40 ILE 132 -0.07 ALA 223
PRO 123 0.27 PRO 133 -0.32 PHE 194
PRO 123 0.52 ALA 134 -0.23 PHE 194
LEU 122 0.64 LEU 135 -0.08 ASP 358
LEU 122 0.49 ASP 136 -0.19 PHE 194
LEU 122 0.60 LYS 137 -0.34 ASN 201
LEU 122 0.93 GLU 138 -0.23 LYS 202
LEU 121 1.06 LEU 139 -0.26 LYS 202
LEU 121 0.73 LYS 140 -0.53 LYS 202
LEU 121 0.82 ALA 141 -0.52 LYS 202
LEU 121 0.99 LYS 142 -0.37 LYS 202
LEU 121 0.65 GLY 143 -0.45 LYS 202
LEU 121 0.51 LYS 144 -0.18 LYS 202
LEU 121 0.34 SER 145 -0.15 GLY 143
LEU 122 0.31 ALA 146 -0.10 PHE 194
LEU 121 0.14 LEU 147 -0.15 PRO 133
THR 208 0.11 MET 148 -0.21 ASN 234
TRP 129 0.13 PHE 149 -0.29 ASN 234
TRP 129 0.13 ASN 150 -0.36 ASN 234
GLU 130 0.18 LEU 151 -0.29 ASN 234
GLU 130 0.15 GLN 152 -0.33 ASN 234
GLU 130 0.12 GLU 153 -0.28 ASN 234
GLU 130 0.13 PRO 154 -0.22 ASN 234
MET 336 0.12 TYR 155 -0.23 TRP 230
TRP 129 0.10 PHE 156 -0.22 ASN 234
GLU 130 0.14 THR 157 -0.20 ASN 234
GLU 130 0.10 TRP 158 -0.17 PRO 133
GLU 130 0.09 PRO 159 -0.18 PRO 133
GLU 130 0.13 LEU 160 -0.24 PRO 133
GLU 130 0.13 ILE 161 -0.21 PRO 133
ALA 351 0.08 ALA 162 -0.18 PRO 133
ALA 351 0.09 ALA 163 -0.20 PRO 133
ALA 351 0.08 ASP 164 -0.21 PRO 133
ALA 351 0.07 GLY 165 -0.18 PRO 133
ALA 351 0.06 GLY 166 -0.17 PRO 133
ALA 52 0.06 TYR 167 -0.14 PRO 133
ALA 52 0.06 ALA 168 -0.12 PRO 133
ALA 52 0.07 PHE 169 -0.11 PRO 133
ALA 52 0.06 LYS 170 -0.11 LYS 83
GLU 214 0.06 TYR 171 -0.13 LYS 83
GLU 214 0.05 GLU 172 -0.16 LYS 83
GLU 214 0.07 ASN 173 -0.17 ASP 82
GLU 214 0.08 GLY 174 -0.16 PRO 81
GLU 214 0.07 LYS 175 -0.13 PRO 81
ALA 52 0.08 TYR 176 -0.11 ASP 82
GLN 72 0.09 ASP 177 -0.11 ASP 82
ALA 52 0.09 ILE 178 -0.09 PRO 133
ALA 52 0.09 LYS 179 -0.11 PRO 133
ALA 52 0.07 ASP 180 -0.12 PRO 133
ALA 52 0.06 VAL 181 -0.12 PRO 133
ALA 52 0.05 GLY 182 -0.14 PRO 133
GLU 130 0.08 VAL 183 -0.15 PRO 133
GLU 130 0.07 ASP 184 -0.16 ALA 141
VAL 357 0.06 ASN 185 -0.17 PRO 133
VAL 357 0.08 ALA 186 -0.19 PRO 133
ALA 350 0.08 GLY 187 -0.20 PRO 133
GLU 130 0.10 ALA 188 -0.20 PRO 133
GLU 130 0.12 LYS 189 -0.20 PRO 133
GLU 130 0.13 ALA 190 -0.26 PRO 133
GLU 130 0.19 GLY 191 -0.26 PRO 133
GLU 130 0.23 LEU 192 -0.22 PRO 133
GLU 130 0.29 THR 193 -0.24 LYS 137
GLU 130 0.45 PHE 194 -0.32 PRO 133
GLU 130 0.41 LEU 195 -0.25 LYS 140
GLU 130 0.37 VAL 196 -0.27 ALA 141
GLU 130 0.52 ASP 197 -0.30 ALA 141
GLU 130 0.50 LEU 198 -0.32 LYS 140
GLU 130 0.36 ILE 199 -0.33 ALA 141
GLU 130 0.36 LYS 200 -0.39 ALA 141
GLU 131 0.37 ASN 201 -0.47 ALA 141
GLU 130 0.26 LYS 202 -0.53 LYS 140
ILE 132 0.31 HIS 203 -0.39 LYS 140
ILE 132 0.30 MET 204 -0.29 LYS 140
GLU 130 0.25 ASN 205 -0.32 GLY 143
GLU 130 0.26 ALA 206 -0.26 ASN 234
GLU 130 0.20 ASP 207 -0.33 ASN 234
GLU 130 0.16 THR 208 -0.37 ASN 234
GLU 130 0.13 ASP 209 -0.44 ASN 234
MET 336 0.10 TYR 210 -0.59 ASN 234
MET 336 0.09 SER 211 -0.66 ASN 234
THR 222 0.11 ILE 212 -0.44 ASN 234
ILE 212 0.09 ALA 213 -0.36 ASN 234
ASN 227 0.19 GLU 214 -0.50 ASN 234
TRP 230 0.21 ALA 215 -0.31 SER 238
ALA 231 0.17 ALA 216 -0.18 LYS 202
ALA 231 0.27 PHE 217 -0.12 LYS 202
ALA 231 0.36 ASN 218 -0.18 ALA 215
ALA 231 0.26 LYS 219 -0.13 LYS 202
LYS 142 0.32 GLY 220 -0.08 LEU 121
ALA 231 0.18 GLU 221 -0.11 LYS 202
ALA 231 0.15 THR 222 -0.09 PHE 194
LEU 139 0.40 ALA 223 -0.09 GLU 131
LEU 139 0.26 MET 224 -0.07 ASN 124
LEU 139 0.17 THR 225 -0.17 ASN 234
GLU 214 0.12 ILE 226 -0.14 PRO 133
GLU 214 0.19 ASN 227 -0.14 ASN 124
GLU 214 0.16 GLY 228 -0.16 ASN 124
LYS 142 0.19 PRO 229 -0.15 ASN 124
ASN 218 0.27 TRP 230 -0.23 TYR 155
ASN 218 0.36 ALA 231 -0.37 TYR 210
ARG 316 0.49 TRP 232 -0.32 TYR 210
ASP 314 0.59 SER 233 -0.49 SER 211
ASP 314 0.40 ASN 234 -0.66 SER 211
ASP 314 0.31 ILE 235 -0.41 SER 211
ASP 314 0.45 ASP 236 -0.38 SER 211
ASP 314 0.36 THR 237 -0.44 SER 211
LYS 142 0.30 SER 238 -0.36 SER 211
LYS 142 0.47 LYS 239 -0.26 SER 211
LYS 142 0.55 VAL 240 -0.22 GLU 214
LYS 142 0.60 ASN 241 -0.20 GLU 214
LYS 142 0.50 TYR 242 -0.17 TYR 210
LYS 142 0.42 GLY 243 -0.22 PRO 123
LYS 142 0.33 VAL 244 -0.24 ASN 124
LYS 142 0.26 THR 245 -0.33 ASN 124
GLU 138 0.22 VAL 246 -0.23 ASN 124
GLU 138 0.19 LEU 247 -0.13 ASN 124
LEU 135 0.18 PRO 248 -0.10 PRO 133
ASP 197 0.17 THR 249 -0.13 PRO 133
PHE 194 0.22 PHE 250 -0.20 PRO 133
PHE 194 0.21 LYS 251 -0.17 PRO 133
PHE 194 0.16 GLY 252 -0.11 PRO 133
PHE 194 0.13 GLN 253 -0.13 PRO 133
ASP 197 0.10 PRO 254 -0.12 PRO 133
ALA 351 0.09 SER 255 -0.16 PRO 133
GLU 138 0.07 LYS 256 -0.14 PRO 133
GLU 214 0.10 PRO 257 -0.13 PRO 133
GLU 214 0.10 PHE 258 -0.12 TRP 230
GLU 214 0.10 VAL 259 -0.11 TRP 230
GLU 214 0.11 GLY 260 -0.14 TRP 230
LYS 142 0.12 VAL 261 -0.09 ASN 124
LYS 142 0.12 LEU 262 -0.09 ASN 124
LYS 142 0.11 SER 263 -0.08 ASN 124
LYS 142 0.11 ALA 264 -0.08 ASN 124
LYS 142 0.09 GLY 265 -0.07 SER 337
LYS 142 0.09 ILE 266 -0.07 ASN 124
LYS 142 0.08 ASN 267 -0.06 GLU 44
LYS 277 0.07 ALA 268 -0.06 GLU 44
ALA 215 0.07 ALA 269 -0.05 ASN 124
LYS 142 0.08 SER 270 -0.06 ASN 124
LYS 142 0.07 PRO 271 -0.07 ASN 124
LYS 142 0.08 ASN 272 -0.08 ASN 124
LYS 142 0.08 LYS 273 -0.08 LYS 88
THR 31 0.09 GLU 274 -0.09 LYS 88
THR 31 0.11 LEU 275 -0.09 ASN 124
PRO 81 0.11 ALA 276 -0.09 ASN 124
PRO 81 0.19 LYS 277 -0.11 LYS 88
PRO 81 0.24 GLU 278 -0.10 ASN 124
PRO 81 0.21 PHE 279 -0.10 ASN 124
PRO 81 0.25 LEU 280 -0.11 ASN 124
PRO 81 0.41 GLU 281 -0.12 LYS 88
PRO 81 0.33 ASN 282 -0.11 ASN 124
PRO 81 0.24 TYR 283 -0.12 ASN 124
PRO 81 0.22 LEU 284 -0.12 ASN 124
PRO 81 0.26 LEU 285 -0.13 ASN 124
PRO 81 0.24 THR 286 -0.13 ASN 124
PHE 85 0.20 ASP 287 -0.15 ASN 124
PRO 81 0.18 GLU 288 -0.15 ASN 124
PRO 81 0.19 GLY 289 -0.14 ASN 124
SER 233 0.17 LEU 290 -0.16 ASN 124
SER 233 0.20 GLU 291 -0.17 ASN 124
ASN 234 0.15 ALA 292 -0.16 PRO 123
ASN 234 0.15 VAL 293 -0.15 ASN 124
SER 233 0.21 ASN 294 -0.17 ASN 124
SER 233 0.21 LYS 295 -0.17 PRO 123
ASN 234 0.18 ASP 296 -0.15 PRO 123
ASN 234 0.20 LYS 297 -0.15 ASN 124
SER 233 0.28 PRO 298 -0.17 ASN 124
SER 233 0.21 LEU 299 -0.16 ASN 124
SER 233 0.31 GLY 300 -0.18 ASN 124
SER 233 0.29 ALA 301 -0.15 ASN 124
SER 233 0.23 VAL 302 -0.13 ASN 124
SER 233 0.18 ALA 303 -0.12 ASN 124
SER 233 0.21 LEU 304 -0.11 ASN 124
SER 233 0.24 LYS 305 -0.11 ASN 124
SER 233 0.26 SER 306 -0.12 ASN 124
SER 233 0.29 TYR 307 -0.14 ASN 124
SER 233 0.32 GLU 308 -0.15 ASN 124
SER 233 0.34 GLU 309 -0.15 ASN 124
SER 233 0.40 GLU 310 -0.16 ASN 124
SER 233 0.46 LEU 311 -0.17 ASN 124
SER 233 0.43 ALA 312 -0.20 ASN 124
SER 233 0.49 LYS 313 -0.21 ASN 124
SER 233 0.59 ASP 314 -0.22 ASN 124
SER 233 0.46 PRO 315 -0.28 ASN 124
TRP 232 0.49 ARG 316 -0.24 ASN 124
SER 233 0.43 ILE 317 -0.21 ASN 124
SER 233 0.34 ALA 318 -0.22 ASN 124
SER 233 0.26 ALA 319 -0.24 ASN 124
SER 233 0.21 THR 320 -0.19 ASN 124
SER 233 0.21 MET 321 -0.16 ASN 124
LYS 142 0.18 GLU 322 -0.16 ASN 124
LYS 142 0.16 ASN 323 -0.14 ASN 124
LYS 142 0.14 ALA 324 -0.12 ASN 124
LYS 142 0.13 GLN 325 -0.11 ASN 124
LYS 142 0.12 LYS 326 -0.10 PRO 133
LYS 142 0.09 GLY 327 -0.11 PRO 133
GLU 214 0.08 GLU 328 -0.11 PRO 133
GLU 214 0.08 ILE 329 -0.09 TRP 230
GLU 214 0.10 MET 330 -0.13 TRP 340
GLU 214 0.09 PRO 331 -0.10 TRP 340
GLU 214 0.09 ASN 332 -0.13 SER 337
GLU 214 0.10 ILE 333 -0.14 TYR 99
GLU 214 0.10 PRO 334 -0.11 ASN 100
GLU 214 0.09 GLN 335 -0.10 ASN 100
TYR 155 0.12 MET 336 -0.09 ALA 338
TYR 210 0.10 SER 337 -0.13 SER 233
GLU 130 0.08 ALA 338 -0.13 SER 233
GLU 130 0.09 PHE 339 -0.13 TRP 230
GLU 130 0.10 TRP 340 -0.17 SER 233
GLU 130 0.10 TYR 341 -0.19 SER 233
GLU 130 0.10 ALA 342 -0.17 ASN 234
GLU 130 0.12 VAL 343 -0.18 ASN 234
GLU 130 0.13 ARG 344 -0.22 ASN 234
GLU 130 0.14 THR 345 -0.22 ASN 234
GLU 130 0.16 ALA 346 -0.19 ASN 234
GLU 130 0.19 VAL 347 -0.22 ASN 234
GLU 130 0.20 ILE 348 -0.25 ASN 234
GLU 130 0.21 ASN 349 -0.22 ASN 234
GLU 130 0.25 ALA 350 -0.24 ALA 141
GLU 130 0.30 ALA 351 -0.26 ALA 141
GLU 130 0.27 SER 352 -0.26 ALA 141
GLU 130 0.27 GLY 353 -0.28 ALA 141
GLU 130 0.22 ARG 354 -0.24 ALA 141
GLU 130 0.19 GLN 355 -0.25 ALA 141
GLU 130 0.19 THR 356 -0.28 ALA 141
GLU 130 0.17 VAL 357 -0.27 ALA 141
GLU 130 0.10 ASP 358 -0.25 ALA 141
GLU 130 0.12 GLU 359 -0.23 ALA 141
GLU 130 0.15 ALA 360 -0.21 ALA 141
GLU 130 0.11 LEU 361 -0.19 ALA 141
GLU 130 0.08 LYS 362 -0.19 ALA 141
GLU 130 0.09 ASP 363 -0.18 ALA 141
GLU 130 0.10 ALA 364 -0.16 ALA 141
GLU 130 0.08 GLN 365 -0.14 ALA 141
GLU 130 0.07 THR 366 -0.15 ALA 141
GLU 130 0.08 ARG 367 -0.13 ALA 141
GLU 130 0.07 ILE 368 -0.11 ASN 234
GLU 130 0.06 THR 369 -0.11 ALA 141

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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).
Between 2015 and 2025, it was hosted by US2B (Nantes).
Last modification: april 24th, 2026.