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.


***  1AOL_unrelaxed_rank_001_alphafold2_ptm_model_4_seed_000  ***

CA distance fluctuations for 240220085659142820

---  normal mode 8  ---

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
PRO 225 0.24 GLN 1 -0.15 THR 191
PRO 225 0.33 VAL 2 -0.11 THR 195
VAL 169 0.16 TYR 3 -0.12 THR 195
VAL 169 0.19 ASN 4 -0.09 THR 195
PRO 228 0.18 ILE 5 -0.07 HIS 117
PRO 228 0.19 THR 6 -0.08 GLN 221
PRO 228 0.21 TRP 7 -0.08 GLN 221
PRO 228 0.17 GLU 8 -0.10 GLN 221
PRO 228 0.18 VAL 9 -0.08 GLN 221
PRO 228 0.12 THR 10 -0.12 GLY 224
PRO 228 0.11 ASN 11 -0.12 GLY 224
PRO 228 0.06 GLY 12 -0.15 GLY 224
SER 116 0.04 ASP 13 -0.18 GLY 224
GLU 15 0.03 ARG 14 -0.20 GLY 224
PRO 228 0.05 GLU 15 -0.16 GLY 224
PRO 228 0.11 THR 16 -0.11 GLY 224
PRO 228 0.20 VAL 17 -0.04 GLN 221
PRO 228 0.27 TRP 18 -0.04 VAL 32
PRO 228 0.28 ALA 19 -0.04 VAL 32
PRO 228 0.35 ILE 20 -0.05 TRP 30
PRO 228 0.33 SER 21 -0.07 THR 6
PRO 228 0.39 GLY 22 -0.05 ILE 5
ARG 226 0.37 ASN 23 -0.06 PRO 25
PRO 225 0.36 HIS 24 -0.07 PRO 25
PRO 225 0.25 PRO 25 -0.08 ARG 120
PRO 228 0.10 LEU 26 -0.11 THR 191
PRO 228 0.13 TRP 27 -0.10 LEU 26
PRO 228 0.25 THR 28 -0.04 HIS 117
PRO 228 0.33 TRP 29 -0.03 HIS 117
PRO 228 0.32 TRP 30 -0.05 ILE 20
PRO 228 0.42 PRO 31 -0.04 ALA 19
PRO 228 0.42 VAL 32 -0.04 TRP 18
PRO 228 0.38 LEU 33 -0.04 VAL 32
PRO 228 0.42 THR 34 -0.04 ILE 181
PRO 228 0.36 PRO 35 -0.05 TYR 56
PRO 228 0.36 ASP 36 -0.03 TYR 56
PRO 228 0.31 LEU 37 -0.02 ASN 160
PRO 228 0.29 CYS 38 -0.02 ASN 160
PRO 228 0.27 MET 39 -0.02 ASN 160
PRO 228 0.21 LEU 40 -0.06 GLN 221
PRO 228 0.19 ALA 41 -0.06 GLN 221
PRO 228 0.18 LEU 42 -0.05 GLY 224
PRO 228 0.10 SER 43 -0.10 GLY 224
PRO 228 0.11 GLY 44 -0.11 GLY 224
PRO 228 0.10 PRO 45 -0.11 GLY 224
PRO 228 0.12 PRO 46 -0.09 GLY 224
PRO 228 0.16 HIS 47 -0.08 SER 69
PRO 228 0.20 TRP 48 -0.05 SER 69
PRO 228 0.20 GLY 49 -0.07 SER 69
PRO 228 0.19 LEU 50 -0.04 SER 69
PRO 228 0.12 GLU 51 -0.08 GLY 224
PRO 228 0.12 TYR 52 -0.07 GLY 224
PRO 228 0.17 GLN 53 -0.04 GLY 224
PRO 228 0.14 ALA 54 -0.06 GLY 224
PRO 228 0.17 PRO 55 -0.04 GLY 224
PRO 228 0.26 TYR 56 -0.05 PRO 35
PRO 228 0.27 SER 57 -0.03 PRO 35
PRO 228 0.35 SER 58 -0.03 PRO 178
PRO 228 0.36 PRO 59 -0.01 LEU 161
PRO 228 0.32 PRO 60 -0.01 TYR 52
PRO 228 0.35 GLY 61 -0.01 TYR 52
PRO 228 0.41 PRO 62 -0.01 LYS 105
PRO 228 0.44 PRO 63 -0.02 LEU 83
PRO 228 0.41 CYS 64 -0.02 GLY 207
PRO 228 0.38 CYS 65 -0.02 SER 72
PRO 228 0.33 SER 66 -0.07 SER 69
PRO 228 0.34 GLY 67 -0.11 ARG 77
PRO 228 0.39 SER 68 -0.06 ARG 77
PRO 228 0.38 SER 69 -0.11 ARG 77
PRO 228 0.40 GLY 70 -0.08 ALA 73
PRO 228 0.36 SER 71 -0.04 ARG 77
PRO 228 0.35 SER 72 -0.03 PRO 46
PRO 228 0.30 ALA 73 -0.08 SER 69
PRO 228 0.30 GLY 74 -0.06 SER 69
PRO 228 0.33 CYS 75 -0.03 PRO 46
PRO 228 0.32 SER 76 -0.04 SER 69
PRO 228 0.29 ARG 77 -0.11 SER 69
PRO 228 0.30 ASP 78 -0.10 GLY 67
PRO 228 0.34 CYS 79 -0.04 GLY 67
PRO 228 0.34 ASP 80 -0.05 GLY 67
PRO 228 0.30 GLU 81 -0.08 GLY 67
PRO 228 0.30 PRO 82 -0.06 GLY 67
PRO 228 0.27 LEU 83 -0.06 GLY 67
PRO 228 0.22 THR 84 -0.07 GLY 67
PRO 228 0.18 SER 85 -0.07 SER 69
PRO 228 0.17 LEU 86 -0.09 SER 69
PRO 228 0.22 THR 87 -0.08 SER 69
PRO 228 0.24 PRO 88 -0.05 GLY 67
PRO 228 0.25 ARG 89 -0.04 GLY 67
PRO 228 0.29 CYS 90 -0.02 GLY 67
PRO 228 0.28 ASN 91 -0.02 SER 69
PRO 228 0.34 THR 92 -0.02 ASN 173
PRO 228 0.40 ALA 93 -0.02 LYS 105
PRO 228 0.39 TRP 94 -0.02 SER 107
PRO 228 0.34 ASN 95 -0.02 GLY 12
PRO 228 0.37 ARG 96 -0.02 LEU 99
PRO 228 0.42 LEU 97 -0.02 LYS 105
PRO 228 0.37 LYS 98 -0.02 GLU 108
PRO 228 0.34 LEU 99 -0.02 TYR 198
PRO 228 0.40 ASP 100 -0.02 GLY 109
PRO 228 0.40 GLN 101 -0.03 VAL 167
PRO 228 0.35 VAL 102 -0.03 GLY 109
PRO 228 0.35 THR 103 -0.03 TYR 198
PRO 228 0.40 HIS 104 -0.03 THR 163
PRO 228 0.38 LYS 105 -0.04 VAL 167
PRO 228 0.35 SER 106 -0.03 VAL 167
PRO 228 0.32 SER 107 -0.03 VAL 167
PRO 228 0.31 GLU 108 -0.03 GLY 67
PRO 228 0.31 GLY 109 -0.03 TYR 198
PRO 228 0.27 PHE 110 -0.04 TYR 198
PRO 228 0.23 TYR 111 -0.05 GLN 221
PRO 228 0.19 VAL 112 -0.07 GLN 221
PRO 228 0.13 CYS 113 -0.10 GLY 224
PRO 228 0.09 PRO 114 -0.14 GLY 224
GLY 12 0.04 GLY 115 -0.19 GLY 224
ASP 13 0.04 SER 116 -0.23 GLY 224
ASP 13 0.03 HIS 117 -0.22 GLY 224
ASP 153 0.02 ARG 118 -0.19 GLY 224
ASP 13 0.02 PRO 119 -0.19 GLY 224
ASP 13 0.02 ARG 120 -0.22 GLY 224
SER 150 0.03 GLU 121 -0.18 GLY 224
SER 150 0.03 ALA 122 -0.17 GLY 224
SER 150 0.02 LYS 123 -0.20 GLY 224
SER 150 0.02 SER 124 -0.17 GLY 224
THR 156 0.03 CYS 125 -0.16 GLY 224
GLY 44 0.02 GLY 126 -0.19 GLY 224
SER 43 0.03 GLY 127 -0.21 GLY 224
GLY 44 0.03 PRO 128 -0.19 GLY 224
GLY 44 0.03 ASP 129 -0.18 GLY 224
PRO 228 0.05 SER 130 -0.15 GLY 224
PRO 228 0.08 PHE 131 -0.14 GLY 224
PRO 228 0.05 TYR 132 -0.16 GLY 224
PRO 228 0.09 CYS 133 -0.12 GLY 224
PRO 228 0.06 ALA 134 -0.14 GLY 224
PRO 228 0.07 SER 135 -0.12 GLY 224
PRO 228 0.11 TRP 136 -0.10 GLY 224
PRO 228 0.12 GLY 137 -0.10 GLY 224
PRO 228 0.10 CYS 138 -0.11 GLY 224
PRO 228 0.16 GLU 139 -0.08 ASN 222
PRO 228 0.18 THR 140 -0.07 ASN 222
PRO 228 0.24 THR 141 -0.05 GLN 221
PRO 228 0.28 GLY 142 -0.03 GLN 221
PRO 228 0.33 ARG 143 -0.03 SER 149
PRO 228 0.30 VAL 144 -0.03 THR 163
PRO 228 0.30 TYR 145 -0.02 THR 163
PRO 228 0.26 TRP 146 -0.03 SER 192
PRO 228 0.28 LYS 147 -0.03 THR 163
PRO 228 0.23 PRO 148 -0.04 ASN 222
PRO 228 0.23 SER 149 -0.04 ASN 222
PRO 228 0.18 SER 150 -0.07 ASN 222
PRO 228 0.17 SER 151 -0.07 ASN 222
PRO 228 0.11 TRP 152 -0.11 ASN 222
PRO 228 0.13 ASP 153 -0.10 ASN 222
PRO 228 0.15 TYR 154 -0.10 ASN 222
PRO 228 0.22 ILE 155 -0.06 GLN 221
PRO 228 0.28 THR 156 -0.04 GLN 221
PRO 228 0.31 VAL 157 -0.03 THR 156
PRO 228 0.38 ASP 158 -0.03 ASP 153
PRO 228 0.43 ASN 159 -0.02 ASP 153
PRO 228 0.50 ASN 160 -0.03 LEU 179
PRO 228 0.54 LEU 161 -0.02 SER 58
PRO 228 0.55 THR 162 -0.03 SER 149
PRO 228 0.51 THR 163 -0.03 LYS 105
PRO 228 0.57 SER 164 -0.03 LYS 105
PRO 228 0.60 GLN 165 -0.02 LYS 105
PRO 228 0.53 ALA 166 -0.02 LYS 105
PRO 228 0.53 VAL 167 -0.04 LYS 105
PRO 228 0.59 GLN 168 -0.03 LYS 105
PRO 228 0.57 VAL 169 -0.02 LYS 105
PRO 228 0.49 CYS 170 -0.02 GLN 101
PRO 228 0.52 LYS 171 -0.03 GLN 101
PRO 228 0.55 ASP 172 -0.02 LYS 105
PRO 228 0.47 ASN 173 -0.02 LYS 105
PRO 228 0.49 LYS 174 -0.02 LYS 105
PRO 228 0.44 TRP 175 -0.02 LEU 161
PRO 228 0.47 CYS 176 -0.02 THR 162
PRO 228 0.42 ASN 177 -0.02 SER 58
PRO 228 0.44 PRO 178 -0.03 SER 57
PRO 228 0.39 LEU 179 -0.03 TYR 56
PRO 228 0.41 ALA 180 -0.03 TYR 56
PRO 228 0.33 ILE 181 -0.04 THR 34
PRO 228 0.34 GLN 182 -0.03 THR 34
PRO 228 0.27 PHE 183 -0.04 GLN 221
PRO 228 0.24 THR 184 -0.05 ASN 222
PRO 228 0.21 ASN 185 -0.05 ASN 222
PRO 228 0.13 ALA 186 -0.09 ASN 222
PRO 228 0.14 GLY 187 -0.10 ASN 222
PRO 228 0.16 LYS 188 -0.08 ASN 222
PRO 228 0.08 GLN 189 -0.11 ASN 222
SER 192 0.04 VAL 190 -0.17 GLY 224
ARG 217 0.05 THR 191 -0.23 GLY 224
ARG 217 0.05 SER 192 -0.27 GLY 224
ARG 217 0.06 TRP 193 -0.21 GLY 224
LYS 174 0.06 THR 194 -0.29 GLY 224
ARG 217 0.07 THR 195 -0.32 GLY 224
THR 16 0.05 GLY 196 -0.24 GLY 224
GLU 15 0.03 HIS 197 -0.20 GLY 224
PRO 228 0.06 TYR 198 -0.17 GLY 224
PRO 228 0.10 TRP 199 -0.13 GLY 224
PRO 228 0.12 GLY 200 -0.11 GLY 224
PRO 228 0.18 LEU 201 -0.07 GLN 221
PRO 228 0.19 ARG 202 -0.06 GLN 221
PRO 228 0.23 LEU 203 -0.04 GLN 221
PRO 228 0.24 TYR 204 -0.04 GLY 67
PRO 228 0.24 VAL 205 -0.05 GLY 67
PRO 228 0.22 SER 206 -0.06 GLY 67
PRO 228 0.17 GLY 207 -0.07 GLY 67
PRO 228 0.15 ARG 208 -0.07 GLY 224
PRO 228 0.17 ASP 209 -0.07 GLY 224
PRO 228 0.16 PRO 210 -0.07 GLY 224
PRO 228 0.16 GLY 211 -0.08 GLY 224
PRO 228 0.14 LEU 212 -0.10 GLY 224
PRO 228 0.10 THR 213 -0.13 GLY 224
PRO 228 0.12 PHE 214 -0.12 GLY 224
PRO 228 0.09 GLY 215 -0.14 GLY 224
PRO 228 0.12 ILE 216 -0.13 GLN 221
PRO 228 0.07 ARG 217 -0.17 GLY 224
PRO 228 0.07 LEU 218 -0.18 GLN 221
VAL 169 0.09 ARG 219 -0.22 GLN 221
VAL 169 0.11 TYR 220 -0.28 GLN 221
ASP 172 0.11 GLN 221 -0.28 TYR 220
ASP 172 0.14 ASN 222 -0.29 THR 195
VAL 169 0.21 LEU 223 -0.23 THR 195
GLN 168 0.19 GLY 224 -0.32 THR 195
HIS 24 0.36 PRO 225 -0.24 THR 195
GLN 165 0.41 ARG 226 -0.21 GLY 224
GLN 165 0.39 VAL 227 -0.23 THR 195
GLN 165 0.60 PRO 228 -0.11 PRO 225

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.