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***  1yci  ***

CA distance fluctuations for 210514004643109143

---  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
ARG 40 0.40 GLY 14 -0.33 ARG 44
GLU 18 0.32 GLU 15 -0.20 ARG 44
PRO 41 0.27 PRO 16 -0.11 GLY 287
PRO 41 0.44 ARG 17 -0.23 GLY 288
PRO 43 0.51 GLU 18 -0.39 GLY 288
LEU 45 0.72 GLU 19 -0.55 GLY 288
LEU 45 0.90 ALA 20 -0.57 GLN 137
ASP 49 0.80 GLY 21 -0.70 GLN 137
ASP 49 0.61 ALA 22 -0.58 GLN 137
SER 46 0.60 LEU 23 -0.69 GLY 139
SER 46 0.40 GLY 24 -0.50 ASN 286
ARG 44 0.27 PRO 25 -0.37 GLY 287
PRO 309 0.21 ALA 26 -0.43 GLY 287
PRO 309 0.16 TRP 27 -0.29 GLY 287
PRO 309 0.14 ASP 28 -0.22 LEU 23
SER 30 0.17 GLU 29 -0.17 LEU 23
GLU 29 0.17 SER 30 -0.31 LEU 23
GLY 212 0.10 GLN 31 -0.34 LEU 23
GLU 15 0.12 LEU 32 -0.23 LEU 23
GLU 15 0.14 ARG 33 -0.23 LEU 23
GLU 15 0.18 SER 34 -0.17 LEU 23
GLU 15 0.19 TYR 35 -0.14 GLY 346
GLY 14 0.21 SER 36 -0.15 GLY 346
GLY 14 0.25 PHE 37 -0.14 ASN 349
GLY 14 0.35 PRO 38 -0.12 ASN 349
GLY 14 0.39 THR 39 -0.11 ASN 349
ALA 20 0.47 ARG 40 -0.09 ASN 349
ALA 20 0.53 PRO 41 -0.09 ASN 349
ALA 20 0.57 ILE 42 -0.11 ASN 349
ALA 20 0.73 PRO 43 -0.17 GLY 14
ALA 20 0.78 ARG 44 -0.33 GLY 14
ALA 20 0.90 LEU 45 -0.26 GLY 14
ALA 20 0.88 SER 46 -0.23 GLY 14
ALA 20 0.70 GLN 47 -0.18 GLY 14
ALA 20 0.78 SER 48 -0.17 GLY 14
ALA 20 0.88 ASP 49 -0.18 GLY 14
ALA 20 0.79 PRO 50 -0.14 GLY 14
ALA 20 0.80 ARG 51 -0.13 GLY 14
ALA 20 0.73 ALA 52 -0.14 GLY 14
ALA 20 0.65 GLU 53 -0.11 GLY 14
ALA 20 0.65 GLU 54 -0.11 PRO 303
ALA 20 0.62 LEU 55 -0.11 ASN 349
ALA 20 0.53 ILE 56 -0.12 ASN 349
ALA 20 0.52 GLU 57 -0.13 PRO 303
PRO 309 0.55 ASN 58 -0.13 ASN 349
ALA 20 0.47 GLU 59 -0.15 ASN 349
ALA 20 0.51 GLU 60 -0.14 ASN 349
ALA 20 0.50 PRO 61 -0.14 ASN 349
ALA 20 0.58 VAL 62 -0.12 ASN 349
ALA 20 0.57 VAL 63 -0.19 GLY 14
ALA 20 0.62 LEU 64 -0.21 GLY 14
ALA 20 0.63 THR 65 -0.25 GLY 14
ALA 20 0.59 ASP 66 -0.21 GLY 14
ALA 20 0.46 THR 67 -0.17 GLY 14
LEU 23 0.40 ASN 68 -0.16 GLY 14
LEU 23 0.29 LEU 69 -0.13 GLY 14
LEU 23 0.21 VAL 70 -0.13 GLY 14
LEU 23 0.27 TYR 71 -0.13 GLY 14
LEU 23 0.17 PRO 72 -0.15 GLU 18
PRO 309 0.11 ALA 73 -0.17 GLU 18
PRO 309 0.13 LEU 74 -0.23 GLU 18
PRO 309 0.11 LYS 75 -0.38 ALA 20
PRO 309 0.09 TRP 76 -0.36 ALA 20
GLY 287 0.09 ASP 77 -0.46 ALA 20
GLY 287 0.07 LEU 78 -0.48 GLY 21
ASN 286 0.07 GLU 79 -0.53 GLY 21
GLY 287 0.07 TYR 80 -0.45 ALA 20
GLY 287 0.06 LEU 81 -0.36 ALA 20
ASN 286 0.05 GLN 82 -0.40 GLY 21
SER 30 0.05 GLU 83 -0.39 GLY 21
GLY 287 0.05 ASN 84 -0.31 ALA 20
GLY 287 0.04 ILE 85 -0.26 ALA 20
GLY 287 0.03 GLY 86 -0.25 GLY 21
HIS 98 0.03 ASN 87 -0.27 GLY 21
ARG 143 0.03 GLY 88 -0.22 GLY 21
LYS 304 0.05 ASP 89 -0.22 GLY 21
LYS 304 0.06 PHE 90 -0.22 GLY 21
LYS 304 0.10 SER 91 -0.21 GLY 21
LYS 304 0.11 VAL 92 -0.26 GLY 21
LYS 304 0.14 TYR 93 -0.27 LEU 23
LYS 304 0.14 SER 94 -0.34 LEU 23
LYS 304 0.15 ALA 95 -0.35 LEU 23
LYS 304 0.16 SER 96 -0.39 LEU 23
LYS 304 0.15 THR 97 -0.38 LEU 23
LYS 304 0.13 HIS 98 -0.35 LEU 23
LYS 304 0.15 LYS 99 -0.27 LEU 23
LYS 304 0.17 PHE 100 -0.25 LEU 23
LYS 304 0.21 LEU 101 -0.21 LEU 23
LYS 304 0.23 TYR 102 -0.17 ASN 349
LYS 304 0.28 TYR 103 -0.18 ASN 349
LYS 304 0.33 ASP 104 -0.17 ASN 349
LYS 304 0.33 GLU 105 -0.16 ASN 349
LYS 304 0.40 LYS 106 -0.16 GLU 122
LYS 304 0.42 LYS 107 -0.16 ASN 349
LYS 304 0.38 MET 108 -0.14 ASN 349
LYS 304 0.41 ALA 109 -0.13 ASN 349
LYS 304 0.44 ASN 110 -0.13 GLY 337
LYS 304 0.39 PHE 111 -0.15 GLY 337
LYS 304 0.37 GLN 112 -0.17 LEU 23
LYS 304 0.33 ASN 113 -0.19 LEU 23
LYS 304 0.32 PHE 114 -0.19 LEU 23
LYS 304 0.28 LYS 115 -0.24 LEU 23
LYS 304 0.26 PRO 116 -0.23 LEU 23
LYS 304 0.22 ARG 117 -0.28 LEU 23
LYS 304 0.20 SER 118 -0.28 LEU 23
LYS 304 0.19 ASN 119 -0.28 LEU 23
LYS 304 0.16 ARG 120 -0.24 LEU 23
LYS 304 0.13 GLU 121 -0.26 GLY 21
LYS 304 0.09 GLU 122 -0.24 GLY 21
LYS 304 0.07 MET 123 -0.30 GLY 21
LYS 304 0.04 LYS 124 -0.32 GLY 21
HIS 98 0.04 PHE 125 -0.35 GLY 21
ASN 246 0.04 HIS 126 -0.42 GLY 21
LYS 304 0.05 GLU 127 -0.41 GLY 21
LYS 304 0.06 PHE 128 -0.40 GLY 21
ASN 246 0.06 VAL 129 -0.48 GLY 21
ASN 246 0.06 GLU 130 -0.51 GLY 21
LYS 304 0.07 LYS 131 -0.47 GLY 21
ASN 246 0.07 LEU 132 -0.51 GLY 21
ASN 246 0.07 GLN 133 -0.61 GLY 21
ASN 246 0.07 ASP 134 -0.58 GLY 21
ASN 246 0.09 ILE 135 -0.57 LEU 23
ASN 246 0.09 GLN 136 -0.67 LEU 23
ASN 246 0.09 GLN 137 -0.70 GLY 21
ASN 246 0.09 ARG 138 -0.64 LEU 23
ASN 246 0.11 GLY 139 -0.69 LEU 23
ASN 246 0.11 GLY 140 -0.60 LEU 23
ASN 246 0.12 GLU 141 -0.56 LEU 23
LYS 304 0.12 GLU 142 -0.48 LEU 23
LYS 304 0.11 ARG 143 -0.44 LEU 23
LYS 304 0.11 LEU 144 -0.37 LEU 23
LYS 304 0.10 TYR 145 -0.29 LEU 23
LYS 304 0.08 LEU 146 -0.24 GLY 21
LYS 304 0.09 GLN 147 -0.16 ASN 349
LYS 304 0.06 GLN 148 -0.17 ASN 349
GLU 105 0.06 THR 149 -0.17 ASN 349
GLU 105 0.05 LEU 150 -0.16 ASN 349
GLU 105 0.05 ASN 151 -0.16 ASN 349
LEU 163 0.04 ASP 152 -0.15 ASN 349
LEU 163 0.03 THR 153 -0.15 ASN 349
GLY 287 0.03 VAL 154 -0.16 ALA 20
GLY 287 0.04 GLY 155 -0.20 ALA 20
PRO 309 0.04 ARG 156 -0.18 ALA 20
PRO 309 0.06 LYS 157 -0.21 ALA 20
PRO 309 0.06 ILE 158 -0.18 ALA 20
PRO 309 0.05 VAL 159 -0.13 ASN 349
LEU 23 0.09 MET 160 -0.12 ASN 349
LEU 23 0.10 ASP 161 -0.12 GLU 18
LEU 23 0.10 PHE 162 -0.12 ASN 349
LEU 23 0.15 LEU 163 -0.12 ASN 349
LEU 23 0.20 GLY 164 -0.11 ASN 349
LEU 23 0.22 PHE 165 -0.12 ASN 349
LEU 23 0.29 ASN 166 -0.12 GLY 14
LEU 23 0.26 TRP 167 -0.11 ASN 349
GLY 21 0.33 ASN 168 -0.14 LYS 304
GLY 21 0.39 TRP 169 -0.12 LYS 304
GLY 21 0.33 ILE 170 -0.12 ASN 349
GLY 21 0.31 ASN 171 -0.15 LYS 304
GLY 21 0.39 LYS 172 -0.17 LYS 304
ALA 20 0.41 GLN 173 -0.14 LYS 304
ALA 20 0.33 GLN 174 -0.14 LYS 304
ALA 20 0.35 GLY 175 -0.22 LYS 304
ALA 20 0.42 LYS 176 -0.23 LYS 304
ALA 20 0.40 ARG 177 -0.18 LYS 304
ALA 20 0.34 GLY 178 -0.24 LYS 304
ALA 20 0.30 TRP 179 -0.13 ASN 349
LYS 106 0.25 GLY 180 -0.14 ASN 349
LYS 106 0.24 GLN 181 -0.14 ASN 349
LYS 106 0.21 LEU 182 -0.14 ASN 349
LYS 106 0.25 THR 183 -0.15 ASN 349
LYS 106 0.18 SER 184 -0.16 ASN 349
GLU 105 0.12 ASN 185 -0.15 ASN 349
GLU 105 0.08 LEU 186 -0.16 ASN 349
PRO 309 0.05 LEU 187 -0.15 ASN 349
THR 302 0.07 LEU 188 -0.15 ASN 349
THR 302 0.06 ILE 189 -0.26 GLY 21
LYS 304 0.08 GLY 190 -0.31 LEU 23
LYS 304 0.08 MET 191 -0.44 LEU 23
LYS 304 0.07 GLU 192 -0.47 LEU 23
LYS 304 0.09 GLY 193 -0.41 LEU 23
LYS 304 0.10 ASN 194 -0.33 LEU 23
LYS 304 0.12 VAL 195 -0.24 LEU 23
LYS 304 0.14 THR 196 -0.17 ASN 349
LYS 304 0.17 PRO 197 -0.18 ASN 349
LYS 304 0.17 ALA 198 -0.20 ASN 349
LYS 304 0.21 HIS 199 -0.21 ASN 349
LYS 304 0.22 TYR 200 -0.21 ASN 349
THR 302 0.23 ASP 201 -0.20 ASN 349
THR 302 0.30 GLU 202 -0.20 ASN 349
ALA 20 0.24 GLN 203 -0.19 ASN 349
ALA 20 0.29 GLN 204 -0.17 ASN 349
ALA 20 0.26 ASN 205 -0.16 ASN 349
ALA 20 0.27 PHE 206 -0.14 ASN 349
ALA 20 0.20 PHE 207 -0.14 ASN 349
PRO 309 0.15 ALA 208 -0.13 ASN 349
PRO 309 0.15 GLN 209 -0.13 GLY 14
PRO 309 0.13 ILE 210 -0.17 GLU 18
PRO 309 0.12 LYS 211 -0.30 GLU 19
PRO 309 0.11 GLY 212 -0.30 GLU 19
PRO 309 0.13 TYR 213 -0.14 GLU 18
PRO 309 0.12 LYS 214 -0.13 ASN 349
PRO 309 0.13 ARG 215 -0.13 ASN 349
ALA 20 0.20 CYS 216 -0.14 ASN 349
ALA 20 0.25 ILE 217 -0.15 ASN 349
ALA 20 0.31 LEU 218 -0.17 ASN 349
ALA 20 0.32 PHE 219 -0.18 ASN 349
ALA 20 0.38 PRO 220 -0.20 ASN 349
ALA 20 0.33 PRO 221 -0.23 ASN 349
ALA 20 0.35 ASP 222 -0.24 ASN 349
ALA 20 0.30 GLN 223 -0.24 ASN 349
ALA 20 0.26 PHE 224 -0.30 ASN 349
ALA 20 0.24 GLU 225 -0.34 ASN 349
ALA 20 0.23 CYS 226 -0.27 ASN 349
LYS 304 0.20 LEU 227 -0.27 ASN 349
LYS 304 0.25 TYR 228 -0.32 ASN 349
LYS 304 0.29 PRO 229 -0.28 ASN 349
LYS 304 0.33 TYR 230 -0.25 ASN 349
LYS 304 0.40 PRO 231 -0.25 ASN 349
LYS 304 0.48 VAL 232 -0.22 ASN 349
LYS 304 0.49 HIS 233 -0.18 ASN 349
LYS 304 0.41 HIS 234 -0.20 ASN 349
LYS 304 0.37 PRO 235 -0.18 ASN 349
LYS 304 0.32 CYS 236 -0.20 ASN 349
LYS 304 0.37 ASP 237 -0.22 ASN 349
LYS 304 0.32 ARG 238 -0.23 ASN 349
LYS 304 0.26 GLN 239 -0.23 ASN 349
LYS 304 0.23 SER 240 -0.24 ASN 349
LYS 304 0.24 GLN 241 -0.25 ASN 349
LYS 304 0.19 VAL 242 -0.23 ASN 349
LYS 304 0.17 ASP 243 -0.20 ASN 349
LYS 304 0.15 PHE 244 -0.18 ASN 349
LYS 304 0.13 ASP 245 -0.19 LEU 23
LYS 304 0.14 ASN 246 -0.18 GLY 346
LYS 304 0.15 PRO 247 -0.20 GLY 346
LYS 304 0.17 ASP 248 -0.23 GLY 346
LYS 304 0.15 TYR 249 -0.23 GLY 346
LYS 304 0.17 GLU 250 -0.28 GLY 346
LYS 304 0.19 ARG 251 -0.30 GLY 346
LYS 304 0.19 PHE 252 -0.28 ASN 349
ALA 20 0.16 PRO 253 -0.25 GLY 346
ALA 20 0.21 ASN 254 -0.25 ASN 349
ALA 20 0.19 PHE 255 -0.22 ASN 349
ALA 20 0.21 GLN 256 -0.18 GLY 346
ALA 20 0.26 ASN 257 -0.17 ASN 349
ALA 20 0.27 VAL 258 -0.18 ASN 349
ALA 20 0.33 VAL 259 -0.15 ASN 349
ALA 20 0.34 GLY 260 -0.14 ASN 349
ALA 20 0.41 TYR 261 -0.13 ASN 349
ALA 20 0.34 GLU 262 -0.11 ASN 349
ALA 20 0.36 THR 263 -0.10 ASN 349
ALA 20 0.21 VAL 264 -0.18 GLY 14
ALA 20 0.20 VAL 265 -0.19 GLY 14
PRO 309 0.17 GLY 266 -0.19 GLY 14
PRO 309 0.16 PRO 267 -0.20 ARG 17
LEU 23 0.32 GLY 268 -0.18 GLY 14
LEU 23 0.32 ASP 269 -0.20 GLY 14
ALA 20 0.35 VAL 270 -0.16 GLY 14
ALA 20 0.37 LEU 271 -0.13 ASN 349
ALA 20 0.41 TYR 272 -0.14 ASN 349
ALA 20 0.34 ILE 273 -0.16 ASN 349
ALA 20 0.37 PRO 274 -0.17 ASN 349
ALA 20 0.30 MET 275 -0.19 ASN 349
ALA 20 0.28 TYR 276 -0.21 ASN 349
ALA 20 0.31 TRP 277 -0.20 ASN 349
ALA 20 0.25 TRP 278 -0.21 ASN 349
ALA 20 0.21 HIS 279 -0.18 ASN 349
ALA 20 0.13 HIS 280 -0.17 ASN 349
LYS 304 0.10 ILE 281 -0.16 ASN 349
LYS 304 0.09 GLU 282 -0.18 LEU 23
PRO 309 0.09 SER 283 -0.27 LEU 23
PRO 309 0.10 LEU 284 -0.32 LEU 23
PRO 309 0.08 LEU 285 -0.46 LEU 23
GLY 288 0.09 ASN 286 -0.64 LEU 23
PRO 309 0.10 GLY 287 -0.57 LEU 23
ASN 286 0.09 GLY 288 -0.61 LEU 23
PRO 309 0.08 ILE 289 -0.45 LEU 23
PRO 309 0.09 THR 290 -0.29 GLU 19
PRO 309 0.09 ILE 291 -0.21 GLU 19
PRO 309 0.10 THR 292 -0.14 ASN 349
PRO 309 0.10 VAL 293 -0.14 ASN 349
ALA 20 0.10 ASN 294 -0.15 ASN 349
ALA 20 0.16 PHE 295 -0.15 ASN 349
LYS 106 0.19 TRP 296 -0.16 ASN 349
ALA 20 0.22 TYR 297 -0.16 ASN 349
LYS 106 0.27 LYS 298 -0.16 ASN 349
ALA 20 0.29 GLY 299 -0.16 ASN 349
ALA 20 0.31 ALA 300 -0.14 ASN 349
LYS 324 0.31 PRO 301 -0.11 ASN 349
ASN 321 0.52 THR 302 -0.17 ILE 306
ASN 321 0.48 PRO 303 -0.15 LYS 176
ASN 321 0.78 LYS 304 -0.24 GLY 178
ASN 321 0.55 ARG 305 -0.08 LYS 176
ILE 318 0.38 ILE 306 -0.17 THR 302
ALA 20 0.43 GLU 307 -0.22 ASN 349
ALA 20 0.50 TYR 308 -0.34 ASN 349
ALA 20 0.55 PRO 309 -0.45 ASN 349
ALA 20 0.46 LEU 310 -0.31 ASN 349
ALA 20 0.47 LYS 311 -0.32 ASN 349
ALA 20 0.41 ALA 312 -0.32 ASN 349
ALA 20 0.35 HIS 313 -0.26 ASN 349
ALA 20 0.35 GLN 314 -0.25 ASN 349
LYS 304 0.39 LYS 315 -0.29 ASN 349
LYS 304 0.41 VAL 316 -0.28 ASN 349
LYS 304 0.57 ALA 317 -0.23 ASN 349
LYS 304 0.65 ILE 318 -0.23 ASN 349
LYS 304 0.55 MET 319 -0.27 ASN 349
LYS 304 0.59 ARG 320 -0.23 ASN 349
LYS 304 0.78 ASN 321 -0.19 ASN 349
LYS 304 0.69 ILE 322 -0.18 ASN 349
LYS 304 0.61 GLU 323 -0.20 ASN 349
LYS 304 0.69 LYS 324 -0.16 ASN 349
LYS 304 0.77 MET 325 -0.15 GLU 122
LYS 304 0.66 LEU 326 -0.13 GLU 122
LYS 304 0.61 GLY 327 -0.15 GLU 122
LYS 304 0.67 GLU 328 -0.16 GLU 122
LYS 304 0.64 ALA 329 -0.14 GLU 122
LYS 304 0.56 LEU 330 -0.13 GLU 122
LYS 304 0.56 GLY 331 -0.14 GLU 122
LYS 304 0.53 ASN 332 -0.13 GLU 122
LYS 304 0.52 PRO 333 -0.13 GLU 122
LYS 304 0.47 GLN 334 -0.12 ALA 109
LYS 304 0.48 GLU 335 -0.10 GLU 122
LYS 304 0.51 VAL 336 -0.12 LYS 107
LYS 304 0.45 GLY 337 -0.15 HIS 234
LYS 304 0.43 PRO 338 -0.13 PRO 309
LYS 304 0.48 LEU 339 -0.14 PRO 309
LYS 304 0.45 LEU 340 -0.17 PRO 309
LYS 304 0.38 ASN 341 -0.19 PRO 309
LYS 304 0.41 THR 342 -0.18 PRO 309
LYS 304 0.42 MET 343 -0.21 PRO 309
LYS 304 0.32 ILE 344 -0.29 PRO 309
LYS 304 0.28 LYS 345 -0.29 PRO 309
LYS 304 0.23 GLY 346 -0.33 PRO 309
LYS 304 0.25 ARG 347 -0.35 PRO 309
LYS 304 0.19 TYR 348 -0.43 PRO 309
LYS 304 0.13 ASN 349 -0.45 PRO 309

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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: October 18th, 2018.