CNRS Nantes University US2B US2B
home |  start a new run |  job status |  references&downloads |  examples |  help  

Should you encounter any unexpected behaviour,
please let us know.


***  1F0N_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000  ***

CA distance fluctuations for 240220091526165245

---  normal mode 10  ---

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
LEU 218 0.67 SER 1 -0.19 TYR 9
LEU 218 0.77 ARG 2 -0.31 TYR 9
LEU 218 0.70 PRO 3 -0.45 TYR 9
LEU 218 0.59 GLY 4 -0.27 GLU 8
LEU 218 0.50 LEU 5 -0.22 PRO 3
LEU 218 0.41 PRO 6 -0.27 PRO 3
ASN 222 0.39 VAL 7 -0.45 PRO 3
ASN 222 0.37 GLU 8 -0.45 PRO 3
ASN 222 0.37 TYR 9 -0.45 PRO 3
ASN 222 0.34 LEU 10 -0.38 PRO 3
ASN 222 0.33 GLN 11 -0.38 PRO 3
PRO 224 0.31 VAL 12 -0.32 PRO 3
PRO 224 0.29 PRO 13 -0.30 PRO 3
PRO 224 0.29 SER 14 -0.26 TYR 82
PRO 224 0.28 PRO 15 -0.28 TYR 82
PRO 224 0.29 SER 16 -0.36 TYR 82
PRO 224 0.31 MET 17 -0.25 TYR 82
PRO 224 0.29 GLY 18 -0.23 PRO 3
PRO 224 0.30 ARG 19 -0.25 PRO 3
PRO 224 0.32 ASP 20 -0.30 PRO 3
PRO 224 0.34 ILE 21 -0.26 PRO 3
ASN 222 0.35 LYS 22 -0.29 PRO 3
ASN 222 0.34 VAL 23 -0.26 PRO 3
ASN 222 0.36 GLN 24 -0.28 PRO 3
ASN 222 0.35 PHE 25 -0.26 PRO 3
ASN 222 0.33 GLN 26 -0.26 PRO 3
ASN 222 0.28 SER 27 -0.23 PRO 3
ASN 222 0.25 GLY 28 -0.21 HIS 138
ASN 222 0.24 GLY 29 -0.21 PRO 6
PRO 224 0.21 ASN 30 -0.23 HIS 138
PRO 224 0.20 ASN 31 -0.27 HIS 138
PRO 224 0.21 SER 32 -0.24 HIS 138
PRO 224 0.20 PRO 33 -0.26 HIS 138
PRO 224 0.24 ALA 34 -0.22 HIS 138
PRO 224 0.24 VAL 35 -0.15 ALA 186
PRO 224 0.29 TYR 36 -0.15 ALA 186
PRO 224 0.32 LEU 37 -0.08 ASP 51
PRO 224 0.36 LEU 38 -0.07 ASN 48
PRO 224 0.42 ASP 39 -0.10 GLN 44
PRO 224 0.53 GLY 40 -0.11 ALA 43
PRO 224 0.68 LEU 41 -0.15 MET 126
PRO 224 0.59 ARG 42 -0.13 VAL 232
PRO 224 0.49 ALA 43 -0.11 GLY 40
ASN 222 0.46 GLN 44 -0.10 ASP 39
ILE 223 0.40 ASP 45 -0.08 ASN 271
ASN 222 0.43 ASP 46 -0.09 ASN 271
ASN 222 0.47 TYR 47 -0.09 ASN 271
ASN 222 0.44 ASN 48 -0.10 ASN 271
ASN 222 0.49 GLY 49 -0.10 ASN 271
ASN 222 0.40 TRP 50 -0.13 ASN 271
ASN 222 0.46 ASP 51 -0.13 ASN 271
ASN 222 0.57 ILE 52 -0.14 ASN 271
ASN 222 0.57 ASN 53 -0.19 GLY 267
GLU 264 0.56 THR 54 -0.20 ASN 271
GLU 264 0.65 PRO 55 -0.10 ASP 51
GLU 264 0.44 ALA 56 -0.11 ASP 51
LEU 218 0.40 PHE 57 -0.10 GLN 24
LEU 218 0.49 GLU 58 -0.10 TYR 9
LEU 218 0.35 TRP 59 -0.09 ALA 56
LEU 218 0.25 TYR 60 -0.12 ASN 202
LEU 218 0.33 TYR 61 -0.13 HIS 138
LEU 218 0.24 GLN 62 -0.30 GLY 64
PRO 224 0.19 SER 63 -0.26 GLN 62
PRO 224 0.20 GLY 64 -0.30 GLN 62
PRO 224 0.22 LEU 65 -0.21 GLN 62
PRO 224 0.26 SER 66 -0.21 HIS 138
PRO 224 0.29 ILE 67 -0.16 PRO 3
PRO 224 0.31 VAL 68 -0.18 PRO 3
PRO 224 0.35 MET 69 -0.14 PRO 3
PRO 224 0.35 PRO 70 -0.16 PRO 3
PRO 224 0.39 VAL 71 -0.13 PRO 3
PRO 224 0.41 GLY 72 -0.08 PRO 3
PRO 224 0.42 GLY 73 -0.08 VAL 232
PRO 224 0.51 GLN 74 -0.10 VAL 232
PRO 224 0.58 SER 75 -0.11 LEU 151
PRO 224 0.48 SER 76 -0.08 SER 235
PRO 224 0.48 PHE 77 -0.08 SER 235
PRO 224 0.40 TYR 78 -0.10 PRO 70
PRO 224 0.38 SER 79 -0.20 GLU 97
PRO 224 0.35 ASP 80 -0.26 TRP 179
PRO 224 0.41 TRP 81 -0.32 LYS 95
PRO 224 0.39 TYR 82 -0.36 SER 16
PRO 224 0.39 SER 83 -0.28 SER 16
PRO 224 0.37 PRO 84 -0.17 SER 16
PRO 224 0.42 ALA 85 -0.09 SER 16
PRO 224 0.41 CYS 86 -0.09 LEU 165
ILE 223 0.45 GLY 87 -0.10 LEU 165
ILE 223 0.43 LYS 88 -0.14 PHE 231
ILE 223 0.34 ALA 89 -0.15 PHE 231
ILE 223 0.34 GLY 90 -0.10 PHE 231
ILE 223 0.34 CYS 91 -0.08 PRO 3
PRO 224 0.33 GLN 92 -0.13 PRO 3
PRO 224 0.33 THR 93 -0.15 PRO 3
PRO 224 0.37 TYR 94 -0.16 TRP 81
PRO 224 0.34 LYS 95 -0.32 TRP 81
PRO 224 0.35 TRP 96 -0.20 TRP 81
PRO 224 0.32 GLU 97 -0.31 ALA 186
PRO 224 0.29 THR 98 -0.34 ALA 186
PRO 224 0.30 PHE 99 -0.28 ALA 186
PRO 224 0.30 LEU 100 -0.26 ALA 186
PRO 224 0.26 THR 101 -0.35 ALA 186
PRO 224 0.25 SER 102 -0.39 PRO 185
PRO 224 0.27 GLU 103 -0.32 PRO 185
PRO 224 0.29 LEU 104 -0.26 ALA 186
PRO 224 0.26 PRO 105 -0.31 PRO 185
PRO 224 0.24 GLN 106 -0.35 PRO 185
PRO 224 0.26 TRP 107 -0.29 PRO 185
PRO 224 0.27 LEU 108 -0.26 PRO 185
PRO 224 0.24 SER 109 -0.30 PRO 185
PRO 224 0.24 ALA 110 -0.31 PRO 185
ASN 222 0.26 ASN 111 -0.27 PRO 3
ASN 222 0.27 ARG 112 -0.27 PRO 3
PRO 224 0.23 ALA 113 -0.26 PRO 185
PRO 224 0.24 VAL 114 -0.26 HIS 138
PRO 224 0.21 LYS 115 -0.29 HIS 138
PRO 224 0.21 PRO 116 -0.36 HIS 138
PRO 224 0.19 THR 117 -0.35 HIS 138
PRO 224 0.18 GLY 118 -0.28 GLN 140
PRO 224 0.19 SER 119 -0.21 HIS 138
PRO 224 0.20 ALA 120 -0.15 GLN 62
PRO 224 0.23 ALA 121 -0.13 ALA 186
PRO 224 0.25 ILE 122 -0.07 ASN 48
PRO 224 0.29 GLY 123 -0.10 GLN 44
PRO 224 0.33 LEU 124 -0.08 GLN 44
PRO 224 0.42 SER 125 -0.11 ARG 42
PRO 224 0.49 MET 126 -0.15 LEU 41
PRO 224 0.39 ALA 127 -0.08 LEU 41
PRO 224 0.30 GLY 128 -0.07 ASP 169
PRO 224 0.31 SER 129 -0.11 ASP 169
PRO 224 0.34 SER 130 -0.08 VAL 68
PRO 224 0.27 ALA 131 -0.09 ALA 186
PRO 224 0.22 MET 132 -0.10 PRO 33
PRO 224 0.27 ILE 133 -0.16 PRO 116
PRO 224 0.27 LEU 134 -0.20 ALA 186
PRO 224 0.20 ALA 135 -0.19 PRO 185
PRO 224 0.20 ALA 136 -0.21 PRO 185
PRO 224 0.24 TYR 137 -0.32 PRO 185
PRO 224 0.22 HIS 138 -0.36 PRO 116
PRO 224 0.17 PRO 139 -0.27 PRO 185
GLN 141 0.20 GLN 140 -0.28 GLY 118
GLN 140 0.20 GLN 141 -0.35 HIS 138
PRO 224 0.19 PHE 142 -0.21 PRO 185
PRO 224 0.14 ILE 143 -0.19 PRO 185
PRO 224 0.14 TYR 144 -0.15 GLN 62
PRO 224 0.17 ALA 145 -0.11 GLU 217
PRO 224 0.17 GLY 146 -0.11 GLU 217
PRO 224 0.18 SER 147 -0.11 TYR 209
PRO 55 0.19 LEU 148 -0.08 GLU 217
ARG 2 0.24 SER 149 -0.08 ALA 89
LEU 151 0.30 ALA 150 -0.15 ALA 170
PRO 224 0.32 LEU 151 -0.20 ASP 169
PRO 224 0.24 LEU 152 -0.16 ASP 169
PRO 224 0.27 ASP 153 -0.17 ALA 166
PRO 224 0.45 PRO 154 -0.17 ILE 163
PRO 224 0.42 SER 155 -0.18 SER 102
LEU 228 0.37 GLN 156 -0.15 SER 102
LEU 228 0.43 GLY 157 -0.15 GLN 194
PRO 224 0.50 MET 158 -0.14 LYS 238
LEU 228 0.61 GLY 159 -0.17 SER 161
PRO 224 0.63 PRO 160 -0.14 SER 102
PRO 224 0.67 SER 161 -0.17 GLY 159
PRO 224 0.82 LEU 162 -0.15 ASP 153
PRO 224 0.83 ILE 163 -0.17 PRO 154
PRO 224 0.77 GLY 164 -0.11 LYS 174
PRO 224 0.89 LEU 165 -0.15 GLY 168
PRO 224 1.03 ALA 166 -0.20 SER 235
PRO 224 0.77 MET 167 -0.16 LEU 151
PRO 224 0.68 GLY 168 -0.15 LEU 165
ILE 223 0.75 ASP 169 -0.22 PHE 231
PRO 224 0.69 ALA 170 -0.20 PHE 231
ILE 223 0.54 GLY 171 -0.16 PHE 231
ILE 223 0.55 GLY 172 -0.14 LEU 165
PRO 224 0.57 TYR 173 -0.11 LEU 165
PRO 224 0.57 LYS 174 -0.12 SER 16
PRO 224 0.62 ALA 175 -0.14 SER 102
PRO 224 0.53 ALA 176 -0.19 SER 102
PRO 224 0.47 ASP 177 -0.20 SER 16
PRO 224 0.48 MET 178 -0.20 SER 102
PRO 224 0.47 TRP 179 -0.29 SER 102
PRO 224 0.48 GLY 180 -0.28 SER 102
PRO 224 0.53 PRO 181 -0.27 SER 102
PRO 224 0.54 SER 182 -0.25 SER 102
PRO 224 0.49 SER 183 -0.29 SER 102
PRO 224 0.45 ASP 184 -0.36 SER 102
PRO 224 0.39 PRO 185 -0.39 SER 102
PRO 224 0.39 ALA 186 -0.39 SER 102
PRO 224 0.44 TRP 187 -0.25 SER 102
PRO 224 0.36 GLU 188 -0.28 ARG 189
PRO 224 0.31 ARG 189 -0.28 GLU 188
PRO 224 0.35 ASN 190 -0.21 SER 102
PRO 224 0.32 ASP 191 -0.17 PRO 116
PRO 224 0.24 PRO 192 -0.14 PRO 116
PRO 224 0.18 THR 193 -0.13 GLY 157
PRO 224 0.22 GLN 194 -0.19 PRO 139
PRO 224 0.21 GLN 195 -0.20 PRO 139
PRO 224 0.14 ILE 196 -0.14 THR 117
PRO 224 0.13 PRO 197 -0.16 ASN 31
PRO 224 0.16 LYS 198 -0.20 THR 117
PRO 224 0.14 LEU 199 -0.17 LEU 281
TRP 81 0.10 VAL 200 -0.19 PRO 257
LYS 95 0.12 ALA 201 -0.21 GLY 282
SER 16 0.13 ASN 202 -0.25 GLY 282
SER 16 0.12 ASN 203 -0.23 GLY 282
PRO 224 0.11 THR 204 -0.21 LEU 281
PRO 224 0.09 ARG 205 -0.20 GLU 217
PRO 224 0.09 LEU 206 -0.20 GLU 217
PRO 224 0.09 TRP 207 -0.20 GLU 217
ARG 2 0.13 VAL 208 -0.23 TYR 209
ARG 2 0.22 TYR 209 -0.23 VAL 208
ARG 2 0.26 CYS 210 -0.17 GLY 259
ARG 2 0.37 GLY 211 -0.20 ASN 254
ARG 2 0.38 ASN 212 -0.25 ILE 223
ARG 2 0.42 GLY 213 -0.25 ILE 223
ARG 2 0.49 THR 214 -0.28 ILE 223
ARG 2 0.57 PRO 215 -0.28 ASN 254
ARG 2 0.61 ASN 216 -0.35 ASN 254
ARG 2 0.73 GLU 217 -0.35 ASN 254
ARG 2 0.77 LEU 218 -0.29 ASN 254
ARG 2 0.72 GLY 219 -0.24 ASN 254
ARG 2 0.62 GLY 220 -0.18 ASN 254
ARG 2 0.62 ALA 221 -0.19 ASN 254
ALA 166 0.69 ASN 222 -0.20 THR 214
ALA 166 0.79 ILE 223 -0.28 THR 214
ALA 166 1.03 PRO 224 -0.13 THR 214
ALA 166 0.63 ALA 225 -0.08 ASN 254
LEU 162 0.54 GLU 226 -0.20 ASN 212
LEU 162 0.59 PHE 227 -0.16 SER 234
LEU 162 0.63 LEU 228 -0.05 LEU 237
GLY 159 0.41 GLU 229 -0.08 HIS 249
GLY 159 0.35 ASN 230 -0.20 LEU 237
GLY 159 0.34 PHE 231 -0.22 ASP 169
GLY 159 0.30 VAL 232 -0.20 ASP 169
ARG 2 0.24 ARG 233 -0.17 ASN 230
ARG 2 0.21 SER 234 -0.19 ASP 169
SER 183 0.18 SER 235 -0.20 ALA 166
ARG 2 0.18 ASN 236 -0.15 ASP 169
ARG 2 0.19 LEU 237 -0.20 ASN 212
ARG 2 0.15 LYS 238 -0.16 ASP 169
ARG 2 0.12 PHE 239 -0.14 PRO 257
ARG 2 0.13 GLN 240 -0.24 PRO 257
ARG 2 0.13 ASP 241 -0.25 PRO 257
ARG 2 0.10 ALA 242 -0.18 PRO 257
ARG 2 0.07 TYR 243 -0.22 PRO 257
ARG 2 0.08 ASN 244 -0.29 PRO 257
TYR 82 0.07 ALA 245 -0.25 PRO 257
TYR 82 0.09 ALA 246 -0.21 PRO 257
TYR 82 0.09 GLY 247 -0.26 PRO 257
TRP 81 0.08 GLY 248 -0.26 PRO 257
SER 16 0.08 HIS 249 -0.31 PRO 257
SER 16 0.08 ASN 250 -0.28 GLU 217
ASP 241 0.07 ALA 251 -0.27 GLU 217
GLN 240 0.11 VAL 252 -0.33 GLU 217
ALA 272 0.17 PHE 253 -0.29 GLU 217
ARG 2 0.21 ASN 254 -0.35 GLU 217
ARG 2 0.29 PHE 255 -0.29 PHE 253
ARG 2 0.36 PRO 256 -0.32 ASN 216
ARG 2 0.43 PRO 257 -0.31 HIS 249
ARG 2 0.49 ASN 258 -0.29 ASN 254
ARG 2 0.48 GLY 259 -0.32 ASN 254
ARG 2 0.46 THR 260 -0.19 ASN 254
LEU 162 0.40 HIS 261 -0.09 ASN 254
SER 1 0.47 SER 262 -0.08 ASN 254
SER 1 0.47 TRP 263 -0.18 TRP 266
PRO 55 0.65 GLU 264 -0.13 VAL 252
PRO 55 0.52 TYR 265 -0.17 VAL 252
PRO 55 0.38 TRP 266 -0.18 TRP 263
TRP 266 0.37 GLY 267 -0.19 ASN 53
ARG 2 0.34 ALA 268 -0.13 TRP 263
ARG 2 0.24 GLN 269 -0.14 TRP 263
GLU 58 0.20 LEU 270 -0.12 ASN 53
PRO 256 0.24 ASN 271 -0.20 THR 54
PHE 255 0.21 ALA 272 -0.18 GLU 217
PHE 253 0.13 MET 273 -0.15 GLU 217
PRO 224 0.14 LYS 274 -0.11 ASN 203
LEU 237 0.10 GLY 275 -0.14 GLU 217
PRO 224 0.08 ASP 276 -0.19 GLU 217
PRO 224 0.13 LEU 277 -0.14 ASN 202
PRO 224 0.13 GLN 278 -0.18 GLN 62
PRO 224 0.09 SER 279 -0.18 ASN 203
PRO 224 0.10 SER 280 -0.22 ASN 203
PRO 224 0.13 LEU 281 -0.25 ASN 202
PRO 224 0.13 GLY 282 -0.25 ASN 202
PRO 224 0.16 ALA 283 -0.22 GLN 62
PRO 224 0.15 GLY 284 -0.20 GLN 62

If you find results from this site helpful for your research, please cite one of our papers:

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.