CNRS Nantes University US2B US2B
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***  EXP_1F0N_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000  ***

CA distance fluctuations for 24021912142413056

---  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
ALA 89 0.51 SER 1 -0.18 TRP 59
ALA 89 0.59 ARG 2 -0.31 TRP 59
ASP 46 0.95 PRO 3 -0.21 GLY 275
ASP 46 0.61 GLY 4 -0.31 GLY 275
ALA 89 0.37 LEU 5 -0.23 GLY 275
GLY 90 0.29 PRO 6 -0.16 GLY 275
PRO 3 0.39 VAL 7 -0.10 PRO 256
PRO 3 0.50 GLU 8 -0.10 PRO 55
PRO 3 0.72 TYR 9 -0.09 ILE 52
PRO 3 0.56 LEU 10 -0.09 ASP 46
PRO 3 0.58 GLN 11 -0.19 ASP 45
PRO 3 0.47 VAL 12 -0.17 ASP 45
PRO 3 0.44 PRO 13 -0.18 GLY 171
PRO 3 0.44 SER 14 -0.20 ALA 89
PRO 3 0.41 PRO 15 -0.25 ALA 89
PRO 3 0.41 SER 16 -0.29 GLN 92
PRO 3 0.49 MET 17 -0.28 GLN 92
PRO 3 0.49 GLY 18 -0.34 ALA 89
PRO 3 0.55 ARG 19 -0.27 ALA 89
PRO 3 0.56 ASP 20 -0.24 ASP 45
PRO 3 0.58 ILE 21 -0.22 ASP 45
PRO 3 0.68 LYS 22 -0.16 ASP 45
PRO 3 0.57 VAL 23 -0.08 ASP 46
PRO 3 0.61 GLN 24 -0.07 PRO 256
PRO 3 0.39 PHE 25 -0.09 ASN 250
PRO 224 0.25 GLN 26 -0.13 ASN 250
PRO 224 0.22 SER 27 -0.15 ASN 250
PRO 224 0.21 GLY 28 -0.18 ASN 250
PRO 224 0.19 GLY 29 -0.16 ASN 250
PRO 224 0.17 ASN 30 -0.14 ASN 250
LEU 218 0.17 ASN 31 -0.14 ASN 250
LEU 218 0.20 SER 32 -0.17 ASN 250
LEU 218 0.20 PRO 33 -0.17 ASN 250
PRO 224 0.17 ALA 34 -0.13 ASN 250
PRO 224 0.18 VAL 35 -0.13 ASN 250
PRO 3 0.25 TYR 36 -0.07 ASN 250
PRO 3 0.29 LEU 37 -0.09 LEU 162
PRO 3 0.35 LEU 38 -0.10 LEU 162
PRO 3 0.43 ASP 39 -0.14 LEU 162
PRO 3 0.39 GLY 40 -0.19 LEU 162
PRO 3 0.41 LEU 41 -0.19 LEU 162
LEU 228 0.56 ARG 42 -0.18 ASP 20
PRO 3 0.58 ALA 43 -0.16 ASP 20
PRO 3 0.69 GLN 44 -0.17 ASP 20
PRO 3 0.77 ASP 45 -0.24 ASP 20
PRO 3 0.95 ASP 46 -0.17 GLN 11
PRO 3 0.86 TYR 47 -0.13 LEU 218
PRO 3 0.64 ASN 48 -0.10 LEU 218
PRO 3 0.50 GLY 49 -0.13 LEU 218
PRO 224 0.39 TRP 50 -0.11 LEU 162
PRO 3 0.48 ASP 51 -0.09 PRO 256
PRO 3 0.55 ILE 52 -0.18 LEU 218
PRO 224 0.56 ASN 53 -0.20 LEU 218
PRO 224 0.45 THR 54 -0.16 ALA 268
PRO 224 0.42 PRO 55 -0.17 PRO 256
PRO 224 0.35 ALA 56 -0.16 LEU 270
PRO 224 0.33 PHE 57 -0.18 GLY 275
PRO 224 0.34 GLU 58 -0.49 TRP 59
ASN 222 0.33 TRP 59 -0.49 GLU 58
ASN 222 0.27 TYR 60 -0.27 GLU 58
ASN 222 0.30 TYR 61 -0.30 GLY 275
ASN 222 0.26 GLN 62 -0.34 SER 63
LEU 218 0.29 SER 63 -0.34 GLN 62
LEU 218 0.25 GLY 64 -0.24 ASN 250
LEU 218 0.23 LEU 65 -0.21 ASN 250
PRO 224 0.21 SER 66 -0.15 ASN 250
PRO 224 0.23 ILE 67 -0.13 ASN 250
PRO 3 0.32 VAL 68 -0.08 ASN 250
PRO 3 0.45 MET 69 -0.06 LEU 162
PRO 3 0.52 PRO 70 -0.11 VAL 71
PRO 3 0.68 VAL 71 -0.11 PRO 70
PRO 3 0.63 GLY 72 -0.19 ASP 20
PRO 3 0.56 GLY 73 -0.16 ASP 20
PRO 3 0.55 GLN 74 -0.18 ASP 20
PRO 3 0.45 SER 75 -0.11 ALA 166
PRO 3 0.45 SER 76 -0.08 HIS 138
PRO 3 0.35 PHE 77 -0.12 GLY 220
PRO 3 0.38 TYR 78 -0.08 ILE 143
PRO 3 0.36 SER 79 -0.17 LEU 134
PRO 3 0.39 ASP 80 -0.23 PRO 84
PRO 3 0.43 TRP 81 -0.26 TYR 137
PRO 3 0.41 TYR 82 -0.27 TYR 137
PRO 3 0.47 SER 83 -0.25 TYR 137
PRO 3 0.54 PRO 84 -0.23 ASP 80
PRO 3 0.57 ALA 85 -0.19 ASP 80
PRO 3 0.61 CYS 86 -0.16 SER 16
PRO 3 0.62 GLY 87 -0.23 GLY 18
PRO 3 0.68 LYS 88 -0.26 GLY 18
PRO 3 0.79 ALA 89 -0.34 GLY 18
PRO 3 0.77 GLY 90 -0.27 GLY 18
PRO 3 0.68 CYS 91 -0.24 SER 16
PRO 3 0.66 GLN 92 -0.37 THR 93
PRO 3 0.56 THR 93 -0.37 GLN 92
PRO 3 0.52 TYR 94 -0.25 LYS 95
PRO 3 0.43 LYS 95 -0.25 TYR 94
PRO 3 0.43 TRP 96 -0.13 GLN 140
PRO 3 0.34 GLU 97 -0.18 PRO 84
PRO 3 0.35 THR 98 -0.22 PRO 84
PRO 3 0.38 PHE 99 -0.18 GLN 92
PRO 3 0.34 LEU 100 -0.12 THR 117
PRO 3 0.28 THR 101 -0.19 THR 117
PRO 3 0.28 SER 102 -0.19 PRO 116
PRO 3 0.33 GLU 103 -0.17 PRO 116
PRO 3 0.34 LEU 104 -0.11 PRO 105
PRO 3 0.25 PRO 105 -0.14 GLU 103
PRO 3 0.24 GLN 106 -0.18 PRO 15
PRO 3 0.28 TRP 107 -0.12 PRO 15
PRO 3 0.25 LEU 108 -0.08 ASP 45
PRO 3 0.19 SER 109 -0.12 PRO 15
PRO 3 0.19 ALA 110 -0.11 PRO 15
PRO 3 0.22 ASN 111 -0.08 ASP 45
PRO 3 0.19 ARG 112 -0.09 ASN 250
PRO 224 0.15 ALA 113 -0.09 ASN 250
PRO 224 0.15 VAL 114 -0.10 ASN 250
GLU 217 0.15 LYS 115 -0.13 SER 16
PRO 3 0.17 PRO 116 -0.19 SER 102
GLU 217 0.15 THR 117 -0.19 THR 101
GLU 217 0.20 GLY 118 -0.16 ASN 203
LEU 218 0.17 SER 119 -0.13 THR 98
LEU 218 0.18 ALA 120 -0.12 GLU 58
PRO 3 0.17 ALA 121 -0.11 SER 79
PRO 3 0.17 ILE 122 -0.10 GLY 159
PRO 3 0.23 GLY 123 -0.14 GLY 159
ALA 170 0.24 LEU 124 -0.20 GLY 159
ALA 170 0.32 SER 125 -0.29 GLY 159
PRO 3 0.31 MET 126 -0.22 LEU 162
PRO 3 0.30 ALA 127 -0.14 LEU 162
PRO 3 0.21 GLY 128 -0.15 GLY 159
PRO 3 0.21 SER 129 -0.12 GLY 220
PRO 3 0.26 SER 130 -0.10 TRP 81
PRO 3 0.21 ALA 131 -0.11 TRP 81
PRO 3 0.16 MET 132 -0.14 TYR 82
PRO 3 0.20 ILE 133 -0.17 TYR 82
PRO 3 0.22 LEU 134 -0.20 TRP 81
PRO 3 0.15 ALA 135 -0.19 TYR 82
PRO 3 0.15 ALA 136 -0.22 TYR 82
PRO 3 0.19 TYR 137 -0.27 TYR 82
PRO 3 0.18 HIS 138 -0.24 TYR 82
GLU 217 0.14 PRO 139 -0.21 TYR 82
GLU 217 0.16 GLN 140 -0.22 TYR 82
PRO 3 0.15 GLN 141 -0.18 SER 83
GLU 217 0.15 PHE 142 -0.16 TYR 82
GLU 217 0.18 ILE 143 -0.17 TYR 82
GLU 217 0.21 TYR 144 -0.17 GLN 62
GLU 217 0.16 ALA 145 -0.15 GLU 58
LEU 218 0.17 GLY 146 -0.16 GLU 58
ALA 170 0.22 SER 147 -0.14 LEU 151
ALA 170 0.27 LEU 148 -0.17 LEU 151
ALA 170 0.37 SER 149 -0.21 GLY 159
ALA 170 0.39 ALA 150 -0.33 LEU 151
ALA 166 0.49 LEU 151 -0.33 ALA 150
ALA 166 0.35 LEU 152 -0.20 LEU 228
ALA 166 0.31 ASP 153 -0.31 LEU 228
ILE 163 0.28 PRO 154 -0.39 LEU 228
PRO 3 0.20 SER 155 -0.38 PRO 224
ALA 242 0.24 GLN 156 -0.49 LEU 228
ALA 242 0.28 GLY 157 -0.65 PRO 224
LYS 238 0.33 MET 158 -0.69 PRO 224
LYS 238 0.28 GLY 159 -0.57 PRO 224
PRO 3 0.22 PRO 160 -0.44 PRO 224
LYS 238 0.24 SER 161 -0.52 PRO 224
SER 234 0.38 LEU 162 -0.59 PRO 224
SER 235 0.38 ILE 163 -0.31 ASN 222
PRO 3 0.32 GLY 164 -0.24 GLY 220
PHE 231 0.50 LEU 165 -0.22 ASN 222
PHE 231 0.72 ALA 166 -0.19 GLY 220
PHE 231 0.53 MET 167 -0.11 ASP 20
PHE 231 0.55 GLY 168 -0.14 PRO 181
PHE 231 0.75 ASP 169 -0.17 ARG 19
LEU 228 0.71 ALA 170 -0.20 ASP 20
LEU 228 0.58 GLY 171 -0.25 GLY 18
PRO 3 0.52 GLY 172 -0.18 GLY 18
PRO 3 0.49 TYR 173 -0.11 ASP 169
PRO 3 0.43 LYS 174 -0.12 PRO 181
PRO 3 0.36 ALA 175 -0.17 GLY 220
PRO 3 0.36 ALA 176 -0.15 GLY 220
PRO 3 0.43 ASP 177 -0.17 TYR 137
PRO 3 0.40 MET 178 -0.18 TYR 137
PRO 3 0.34 TRP 179 -0.16 GLY 220
PRO 3 0.34 GLY 180 -0.17 ASN 222
PRO 3 0.29 PRO 181 -0.28 PRO 224
PRO 3 0.24 SER 182 -0.37 PRO 224
PRO 3 0.23 SER 183 -0.36 PRO 224
SER 16 0.27 ASP 184 -0.27 PRO 224
SER 16 0.29 PRO 185 -0.24 PRO 224
SER 16 0.30 ALA 186 -0.18 PRO 224
PRO 3 0.25 TRP 187 -0.25 PRO 224
PRO 3 0.21 GLU 188 -0.26 LEU 228
PRO 3 0.22 ARG 189 -0.19 TYR 82
PRO 3 0.24 ASN 190 -0.16 ALA 225
PRO 3 0.20 ASP 191 -0.21 LEU 228
ALA 166 0.19 PRO 192 -0.15 LEU 228
ALA 166 0.24 THR 193 -0.21 VAL 232
ALA 166 0.16 GLN 194 -0.21 PHE 231
PRO 3 0.14 GLN 195 -0.14 PHE 231
ALA 166 0.17 ILE 196 -0.15 SER 280
GLY 157 0.13 PRO 197 -0.15 TYR 82
PRO 3 0.10 LYS 198 -0.19 TYR 82
GLU 217 0.14 LEU 199 -0.16 TYR 82
GLU 217 0.16 VAL 200 -0.20 SER 280
GLU 217 0.15 ALA 201 -0.18 GLY 282
GLU 217 0.17 ASN 202 -0.19 TYR 82
GLU 217 0.21 ASN 203 -0.27 GLY 282
GLU 217 0.20 THR 204 -0.23 LEU 281
GLU 217 0.24 ARG 205 -0.23 SER 280
GLU 217 0.22 LEU 206 -0.19 GLN 62
GLU 217 0.24 TRP 207 -0.22 MET 273
ALA 170 0.23 VAL 208 -0.18 ASN 236
ALA 170 0.27 TYR 209 -0.20 ALA 272
ASP 169 0.35 CYS 210 -0.15 GLY 157
ASP 169 0.35 GLY 211 -0.18 GLY 157
ASP 169 0.43 ASN 212 -0.20 GLY 157
ASP 169 0.42 GLY 213 -0.34 GLY 157
ASP 169 0.32 THR 214 -0.28 GLY 157
ALA 89 0.23 PRO 215 -0.30 GLY 157
ALA 272 0.29 ASN 216 -0.21 GLY 157
ALA 272 0.47 GLU 217 -0.23 LEU 162
ALA 272 0.55 LEU 218 -0.25 LEU 162
ALA 272 0.41 GLY 219 -0.33 LEU 162
ALA 268 0.33 GLY 220 -0.42 LEU 162
PRO 55 0.30 ALA 221 -0.40 MET 158
ASN 53 0.44 ASN 222 -0.51 MET 158
ASN 53 0.48 ILE 223 -0.56 GLY 157
ASN 53 0.56 PRO 224 -0.69 MET 158
ASN 53 0.44 ALA 225 -0.54 MET 158
ASP 169 0.45 GLU 226 -0.48 GLY 157
ASP 169 0.70 PHE 227 -0.59 GLY 157
ASP 169 0.73 LEU 228 -0.62 GLY 157
ASP 169 0.54 GLU 229 -0.41 GLY 157
ASP 169 0.61 ASN 230 -0.37 GLY 157
ASP 169 0.75 PHE 231 -0.53 GLY 157
ALA 166 0.65 VAL 232 -0.35 GLN 156
ASP 169 0.52 ARG 233 -0.17 GLN 156
ALA 166 0.56 SER 234 -0.14 PHE 227
ALA 166 0.53 SER 235 -0.20 THR 193
ALA 166 0.41 ASN 236 -0.18 VAL 208
ALA 166 0.41 LEU 237 -0.18 ALA 272
ALA 166 0.41 LYS 238 -0.16 MET 273
ALA 166 0.35 PHE 239 -0.16 MET 273
ALA 166 0.31 GLN 240 -0.20 MET 273
ALA 166 0.32 ASP 241 -0.19 SER 279
ALA 166 0.30 ALA 242 -0.18 SER 279
ALA 166 0.25 TYR 243 -0.19 SER 280
ALA 166 0.25 ASN 244 -0.23 SER 279
GLY 157 0.26 ALA 245 -0.22 SER 279
GLY 157 0.22 ALA 246 -0.20 SER 279
ALA 166 0.19 GLY 247 -0.24 SER 279
GLU 217 0.20 GLY 248 -0.27 SER 280
GLU 217 0.27 HIS 249 -0.31 SER 279
GLU 217 0.27 ASN 250 -0.38 SER 280
GLU 217 0.26 ALA 251 -0.26 LEU 277
GLU 217 0.32 VAL 252 -0.27 MET 273
GLU 217 0.26 PHE 253 -0.28 ALA 272
GLU 217 0.31 ASN 254 -0.29 ALA 272
ASP 169 0.31 PHE 255 -0.26 ALA 272
ASP 169 0.27 PRO 256 -0.24 ALA 268
ASP 169 0.30 PRO 257 -0.24 ALA 268
ASP 169 0.27 ASN 258 -0.16 GLY 157
ASP 169 0.26 GLY 259 -0.22 GLY 157
ALA 170 0.29 THR 260 -0.33 GLY 157
ALA 170 0.35 HIS 261 -0.38 GLY 159
TRP 263 0.45 SER 262 -0.36 LEU 162
SER 262 0.45 TRP 263 -0.25 LEU 162
ASN 271 0.38 GLU 264 -0.24 LEU 162
GLN 269 0.33 TYR 265 -0.20 GLY 159
LEU 270 0.27 TRP 266 -0.19 GLY 159
GLU 264 0.35 GLY 267 -0.17 PRO 256
LEU 218 0.41 ALA 268 -0.24 PRO 256
LEU 218 0.36 GLN 269 -0.20 PRO 256
LEU 218 0.29 LEU 270 -0.21 GLU 58
LEU 218 0.42 ASN 271 -0.26 GLU 58
LEU 218 0.55 ALA 272 -0.29 ASN 254
LEU 218 0.42 MET 273 -0.28 PHE 253
LEU 218 0.39 LYS 274 -0.28 GLU 58
LEU 218 0.44 GLY 275 -0.33 GLN 62
LEU 218 0.40 ASP 276 -0.28 GLN 62
LEU 218 0.34 LEU 277 -0.28 ASN 250
LEU 218 0.34 GLN 278 -0.30 ASN 250
GLU 217 0.36 SER 279 -0.34 ASN 250
GLU 217 0.31 SER 280 -0.38 ASN 250
LEU 218 0.27 LEU 281 -0.29 ASN 250
GLU 217 0.29 GLY 282 -0.30 ASN 250
LEU 218 0.30 ALA 283 -0.27 ASN 250
LEU 218 0.34 GLY 284 -0.25 ASN 250

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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.