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***  EXP_1DQZ_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000  ***

CA distance fluctuations for 24021912402138273

---  normal mode 9  ---

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
ILE 49 1.47 ARG 1 -0.23 GLY 3
ASP 43 1.40 PRO 2 -0.28 GLN 59
ASN 219 0.74 GLY 3 -0.48 GLN 59
ASN 219 0.57 LEU 4 -0.32 GLY 27
ASN 219 0.43 PRO 5 -0.19 GLY 27
ASN 219 0.42 VAL 6 -0.07 GLU 56
PRO 2 0.41 GLU 7 -0.06 PRO 52
PRO 2 0.66 TYR 8 -0.08 PRO 52
PRO 2 0.59 LEU 9 -0.05 ASN 200
PRO 2 0.66 GLN 10 -0.07 ASP 42
PRO 2 0.57 VAL 11 -0.06 ASP 42
PRO 2 0.57 PRO 12 -0.08 GLY 168
PRO 2 0.60 SER 13 -0.08 GLY 168
PRO 2 0.55 ALA 14 -0.10 ALA 103
PRO 2 0.59 SER 15 -0.11 ASN 88
PRO 2 0.69 MET 16 -0.09 GLN 87
PRO 2 0.68 GLY 17 -0.08 ALA 103
PRO 2 0.74 ARG 18 -0.10 GLY 168
PRO 2 0.73 ASP 19 -0.09 GLY 168
PRO 2 0.78 ILE 20 -0.08 GLY 168
PRO 2 0.84 LYS 21 -0.07 ASP 42
PRO 2 0.70 VAL 22 -0.05 ILE 65
PRO 2 0.67 GLN 23 -0.07 PRO 52
PRO 2 0.41 PHE 24 -0.07 TYR 8
ASN 219 0.36 GLN 25 -0.11 PRO 5
ASN 219 0.31 GLY 26 -0.20 GLY 3
ASN 219 0.30 GLY 27 -0.38 GLY 3
ASN 219 0.25 GLY 28 -0.35 GLY 3
ASN 219 0.22 PRO 29 -0.27 GLY 3
ASN 219 0.21 HIS 30 -0.21 GLY 3
ASN 219 0.23 ALA 31 -0.16 TYR 58
ARG 1 0.30 VAL 32 -0.10 TYR 58
ARG 1 0.45 TYR 33 -0.08 GLU 56
ARG 1 0.60 LEU 34 -0.07 LEU 159
ARG 1 0.71 LEU 35 -0.09 LEU 159
ARG 1 0.88 ASP 36 -0.10 LEU 159
ARG 1 0.87 GLY 37 -0.14 LEU 159
ARG 1 0.86 LEU 38 -0.14 LEU 159
ARG 1 1.01 ARG 39 -0.10 ALA 163
ARG 1 1.07 ALA 40 -0.08 LEU 159
PRO 2 1.20 GLN 41 -0.06 ILE 20
PRO 2 1.23 ASP 42 -0.08 ILE 20
PRO 2 1.40 ASP 43 -0.06 LYS 21
ARG 1 1.31 TYR 44 -0.06 GLU 265
ARG 1 1.14 ASN 45 -0.06 LEU 159
ARG 1 1.20 GLY 46 -0.09 LEU 159
ARG 1 0.95 TRP 47 -0.09 ILE 49
ARG 1 1.09 ASP 48 -0.09 PRO 52
ARG 1 1.47 ILE 49 -0.11 GLU 265
ARG 1 1.14 ASN 50 -0.15 GLU 265
ARG 1 0.78 THR 51 -0.10 VAL 268
ASN 219 0.55 PRO 52 -0.12 ALA 53
ASN 219 0.47 ALA 53 -0.12 PRO 52
ASN 219 0.45 PHE 54 -0.09 GLU 56
ASN 219 0.50 GLU 55 -0.12 ALA 272
ASN 219 0.41 GLU 56 -0.19 LYS 271
ASN 219 0.37 TYR 57 -0.21 ILE 274
ASN 219 0.43 TYR 58 -0.29 GLY 61
ASN 219 0.35 GLN 59 -0.48 GLY 3
ASN 219 0.29 SER 60 -0.34 GLN 275
ASN 219 0.26 GLY 61 -0.41 GLY 3
ASN 219 0.26 LEU 62 -0.26 GLY 3
ASN 219 0.28 SER 63 -0.17 TYR 58
ASN 219 0.32 VAL 64 -0.09 GLU 56
ARG 1 0.46 ILE 65 -0.07 GLU 56
ARG 1 0.69 MET 66 -0.06 TYR 44
ARG 1 0.75 PRO 67 -0.06 TYR 33
PRO 2 0.94 VAL 68 -0.05 ASP 42
PRO 2 0.99 GLY 69 -0.07 ILE 20
PRO 2 0.88 GLY 70 -0.07 GLN 71
PRO 2 0.94 GLN 71 -0.07 GLY 70
PRO 2 0.81 SER 72 -0.06 LEU 162
PRO 2 0.75 SER 73 -0.05 LEU 162
ARG 1 0.66 PHE 74 -0.07 SER 259
ARG 1 0.64 TYR 75 -0.05 ILE 160
PRO 2 0.58 THR 76 -0.08 LEU 131
PRO 2 0.59 ASP 77 -0.12 TYR 134
PRO 2 0.64 TRP 78 -0.11 TYR 134
PRO 2 0.61 TYR 79 -0.13 TYR 134
PRO 2 0.67 GLN 80 -0.12 TYR 134
PRO 2 0.76 PRO 81 -0.10 TYR 134
PRO 2 0.80 SER 82 -0.07 TYR 134
PRO 2 0.77 GLN 83 -0.07 TYR 134
PRO 2 0.82 SER 84 -0.05 PRO 178
PRO 2 0.92 ASN 85 -0.07 MET 16
PRO 2 0.94 GLY 86 -0.08 MET 16
PRO 2 0.93 GLN 87 -0.09 MET 16
PRO 2 0.88 ASN 88 -0.11 SER 15
PRO 2 0.81 TYR 89 -0.10 SER 15
PRO 2 0.74 THR 90 -0.10 TYR 134
PRO 2 0.74 TYR 91 -0.07 TYR 135
PRO 2 0.64 LYS 92 -0.12 THR 95
PRO 2 0.64 TRP 93 -0.06 GLY 168
PRO 2 0.53 GLU 94 -0.09 LYS 92
PRO 2 0.50 THR 95 -0.12 LYS 92
PRO 2 0.54 PHE 96 -0.06 GLY 168
PRO 2 0.49 LEU 97 -0.06 PHE 96
ARG 1 0.39 THR 98 -0.09 LYS 92
PRO 2 0.38 ARG 99 -0.09 PRO 113
PRO 2 0.44 GLU 100 -0.08 PRO 113
PRO 2 0.43 MET 101 -0.06 ALA 14
PRO 2 0.31 PRO 102 -0.08 ASN 200
PRO 2 0.28 ALA 103 -0.10 ALA 14
PRO 2 0.32 TRP 104 -0.07 ALA 14
PRO 2 0.26 LEU 105 -0.08 ASN 200
ASN 219 0.21 GLN 106 -0.10 GLY 3
PRO 221 0.21 ALA 107 -0.08 GLY 3
PRO 221 0.24 ASN 108 -0.08 PRO 5
ASN 219 0.25 LYS 109 -0.13 GLY 3
ASN 219 0.23 GLY 110 -0.21 GLY 3
ASN 219 0.22 VAL 111 -0.16 GLY 3
ASN 219 0.19 SER 112 -0.16 GLY 3
ARG 1 0.21 PRO 113 -0.10 ASN 200
ARG 1 0.18 THR 114 -0.14 ASN 200
ARG 1 0.14 GLY 115 -0.18 ASN 200
ARG 1 0.21 ASN 116 -0.15 TYR 58
ARG 1 0.27 ALA 117 -0.14 SER 60
ARG 1 0.40 ALA 118 -0.09 SER 60
ARG 1 0.47 VAL 119 -0.08 LEU 159
ARG 1 0.59 GLY 120 -0.10 LEU 159
ARG 1 0.68 LEU 121 -0.15 LEU 159
ARG 1 0.71 SER 122 -0.19 LEU 159
ARG 1 0.70 MET 123 -0.17 ILE 160
ARG 1 0.66 SER 124 -0.11 ILE 160
ARG 1 0.57 GLY 125 -0.09 PRO 151
ARG 1 0.52 GLY 126 -0.08 PRO 151
ARG 1 0.54 SER 127 -0.07 ILE 160
ARG 1 0.48 ALA 128 -0.07 SER 60
ARG 1 0.41 LEU 129 -0.10 SER 60
ARG 1 0.42 ILE 130 -0.09 TYR 79
ARG 1 0.41 LEU 131 -0.10 ASP 77
ARG 1 0.33 ALA 132 -0.11 SER 60
ARG 1 0.32 ALA 133 -0.11 SER 60
ARG 1 0.33 TYR 134 -0.13 TYR 79
ARG 1 0.30 TYR 135 -0.11 ASP 77
ARG 1 0.24 PRO 136 -0.13 ALA 198
ARG 1 0.20 GLN 137 -0.19 ASN 199
ARG 1 0.24 GLN 138 -0.12 ASN 199
ARG 1 0.26 PHE 139 -0.13 SER 60
ARG 1 0.19 PRO 140 -0.17 SER 60
ARG 1 0.21 TYR 141 -0.19 SER 60
ARG 1 0.32 ALA 142 -0.13 SER 60
ARG 1 0.37 ALA 143 -0.11 SER 60
ARG 1 0.47 SER 144 -0.10 GLY 147
ARG 1 0.53 LEU 145 -0.14 GLY 147
ARG 1 0.59 SER 146 -0.15 GLY 147
ARG 1 0.57 GLY 147 -0.15 SER 146
ARG 1 0.57 PHE 148 -0.16 PRO 151
ARG 1 0.49 LEU 149 -0.17 THR 229
ARG 1 0.47 ASN 150 -0.24 LEU 225
ARG 1 0.50 PRO 151 -0.25 LEU 225
PRO 2 0.46 SER 152 -0.26 PRO 221
ARG 1 0.44 GLU 153 -0.37 PRO 221
PRO 2 0.43 SER 154 -0.50 PRO 221
PRO 2 0.47 TRP 155 -0.55 PRO 221
PRO 2 0.50 TRP 156 -0.42 PRO 221
PRO 2 0.53 PRO 157 -0.29 PRO 221
PRO 2 0.54 THR 158 -0.35 PRO 221
PRO 2 0.56 LEU 159 -0.39 PRO 221
PRO 2 0.61 ILE 160 -0.23 GLY 217
PRO 2 0.65 GLY 161 -0.17 GLY 216
PRO 2 0.66 LEU 162 -0.19 GLY 216
PRO 2 0.70 ALA 163 -0.16 GLY 216
PRO 2 0.76 MET 164 -0.09 GLY 216
PRO 2 0.79 ASN 165 -0.08 PRO 178
PRO 2 0.81 ASP 166 -0.07 ARG 18
PRO 2 0.88 SER 167 -0.08 ASP 19
PRO 2 0.95 GLY 168 -0.10 ARG 18
PRO 2 0.87 GLY 169 -0.06 ARG 18
PRO 2 0.82 TYR 170 -0.05 TYR 91
PRO 2 0.73 ASN 171 -0.07 GLY 216
PRO 2 0.66 ALA 172 -0.11 GLY 216
PRO 2 0.62 ASN 173 -0.10 GLY 216
PRO 2 0.67 SER 174 -0.07 TYR 134
PRO 2 0.65 MET 175 -0.07 GLY 216
PRO 2 0.57 TRP 176 -0.10 GLY 216
PRO 2 0.57 GLY 177 -0.11 GLY 216
PRO 2 0.53 PRO 178 -0.15 GLY 217
PRO 2 0.49 SER 179 -0.24 PRO 221
PRO 2 0.46 SER 180 -0.24 PRO 221
PRO 2 0.48 ASP 181 -0.15 PRO 221
PRO 2 0.44 PRO 182 -0.15 PHE 224
PRO 2 0.48 ALA 183 -0.10 GLY 216
PRO 2 0.48 TRP 184 -0.15 LEU 225
PRO 2 0.42 LYS 185 -0.18 PHE 224
ARG 1 0.42 ARG 186 -0.12 LEU 228
ARG 1 0.47 ASN 187 -0.09 GLY 216
ARG 1 0.45 ASP 188 -0.15 LEU 228
ARG 1 0.42 PRO 189 -0.14 LEU 228
ARG 1 0.39 MET 190 -0.21 LEU 228
ARG 1 0.37 VAL 191 -0.20 LEU 228
ARG 1 0.35 GLN 192 -0.15 LEU 228
ARG 1 0.31 ILE 193 -0.14 LEU 228
ARG 1 0.27 PRO 194 -0.13 LEU 228
ARG 1 0.27 ARG 195 -0.12 SER 60
ARG 1 0.26 LEU 196 -0.14 SER 60
ARG 1 0.21 VAL 197 -0.18 GLY 280
ARG 1 0.19 ALA 198 -0.17 GLN 137
ARG 1 0.19 ASN 199 -0.19 GLN 137
ARG 1 0.15 ASN 200 -0.23 GLY 280
ARG 1 0.19 THR 201 -0.19 SER 60
ARG 1 0.17 ARG 202 -0.21 SER 60
ARG 1 0.24 ILE 203 -0.19 SER 60
ARG 1 0.27 TRP 204 -0.15 SER 60
ARG 1 0.35 VAL 205 -0.13 TRP 204
ARG 1 0.40 TYR 206 -0.16 CYS 207
ARG 1 0.47 CYS 207 -0.16 TYR 206
ARG 1 0.49 GLY 208 -0.12 SER 154
ARG 1 0.51 ASN 209 -0.20 PHE 252
ARG 1 0.64 GLY 210 -0.24 SER 154
ARG 1 0.57 THR 211 -0.20 SER 154
ARG 1 0.60 PRO 212 -0.22 SER 154
ARG 1 0.43 SER 213 -0.18 TRP 155
ARG 1 0.39 ASP 214 -0.20 LEU 159
ARG 1 0.48 LEU 215 -0.22 LEU 159
ARG 1 0.66 GLY 216 -0.29 LEU 159
ARG 1 0.87 GLY 217 -0.34 TRP 155
ARG 1 0.85 ASP 218 -0.33 TRP 155
ARG 1 1.07 ASN 219 -0.42 TRP 155
ARG 1 1.03 ILE 220 -0.45 TRP 155
ARG 1 1.10 PRO 221 -0.55 TRP 155
ARG 1 0.98 ALA 222 -0.45 TRP 155
ARG 1 0.82 LYS 223 -0.37 SER 154
ARG 1 0.84 PHE 224 -0.46 SER 154
ARG 1 0.82 LEU 225 -0.45 SER 154
ARG 1 0.69 GLU 226 -0.29 SER 154
ARG 1 0.63 GLY 227 -0.26 SER 154
ARG 1 0.65 LEU 228 -0.35 SER 154
ARG 1 0.58 THR 229 -0.20 SER 154
ARG 1 0.50 LEU 230 -0.20 GLY 227
ARG 1 0.47 ARG 231 -0.24 PHE 224
ARG 1 0.47 THR 232 -0.28 LEU 228
ARG 1 0.44 ASN 233 -0.17 LEU 228
ARG 1 0.36 GLN 234 -0.18 PHE 224
ARG 1 0.38 THR 235 -0.21 LEU 228
ARG 1 0.37 PHE 236 -0.17 LEU 228
ARG 1 0.30 ARG 237 -0.16 HIS 276
ARG 1 0.28 ASP 238 -0.16 GLY 280
ARG 1 0.30 THR 239 -0.16 LEU 228
ARG 1 0.27 TYR 240 -0.17 GLY 280
ARG 1 0.21 ALA 241 -0.21 GLY 280
ARG 1 0.22 ALA 242 -0.19 GLY 280
ARG 1 0.22 ASP 243 -0.18 GLY 280
GLU 153 0.17 GLY 244 -0.23 GLY 280
ARG 1 0.18 GLY 245 -0.24 GLY 280
ARG 1 0.13 ARG 246 -0.28 GLY 280
ARG 1 0.13 ASN 247 -0.26 GLY 280
ARG 1 0.19 GLY 248 -0.21 HIS 276
ARG 1 0.18 VAL 249 -0.21 HIS 276
ARG 1 0.25 PHE 250 -0.15 ALA 272
ARG 1 0.26 ASN 251 -0.16 ALA 272
ARG 1 0.33 PHE 252 -0.20 ASN 209
ARG 1 0.27 PRO 253 -0.17 ALA 269
ARG 1 0.31 PRO 254 -0.12 ALA 272
ARG 1 0.40 ASN 255 -0.12 SER 154
ARG 1 0.52 GLY 256 -0.16 SER 154
ARG 1 0.69 THR 257 -0.25 TRP 155
ARG 1 0.80 HIS 258 -0.28 TRP 155
ARG 1 0.80 SER 259 -0.27 LEU 159
ARG 1 0.85 TRP 260 -0.20 LEU 159
ARG 1 0.65 PRO 261 -0.20 LEU 159
ARG 1 0.55 TYR 262 -0.17 LEU 159
ARG 1 0.58 TRP 263 -0.15 LEU 159
ARG 1 0.50 ASN 264 -0.15 ASN 50
ARG 1 0.30 GLU 265 -0.15 ASN 50
ARG 1 0.31 GLN 266 -0.12 PRO 253
ARG 1 0.32 LEU 267 -0.10 PRO 253
GLY 217 0.26 VAL 268 -0.13 GLU 56
ASP 214 0.23 ALA 269 -0.17 GLU 56
ASP 214 0.17 MET 270 -0.19 GLU 56
GLY 217 0.22 LYS 271 -0.19 GLU 56
ASP 214 0.22 ALA 272 -0.26 GLY 3
ASP 214 0.18 ASP 273 -0.27 SER 60
ASP 214 0.17 ILE 274 -0.29 SER 60
ASP 214 0.18 GLN 275 -0.34 SER 60
ASP 214 0.18 HIS 276 -0.28 GLY 3
ASP 214 0.14 VAL 277 -0.26 ASN 247
ASP 214 0.15 LEU 278 -0.25 SER 60
ASP 214 0.17 ASN 279 -0.31 GLY 3
ASP 214 0.16 GLY 280 -0.31 GLY 3

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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.