CNRS Nantes University US2B US2B
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***  1F0N_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000  ***

CA distance fluctuations for 240220091526165245

---  normal mode 12  ---

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
VAL 7 0.13 SER 1 -0.50 LEU 218
VAL 7 0.27 ARG 2 -0.61 LEU 218
VAL 7 0.35 PRO 3 -0.63 GLU 217
GLY 29 0.26 GLY 4 -0.53 ALA 89
GLY 29 0.22 LEU 5 -0.50 ALA 89
SER 27 0.26 PRO 6 -0.51 ALA 89
PRO 3 0.35 VAL 7 -0.53 ALA 89
PRO 3 0.34 GLU 8 -0.55 ALA 89
PRO 3 0.25 TYR 9 -0.62 ALA 89
PRO 224 0.25 LEU 10 -0.57 ALA 89
PRO 224 0.26 GLN 11 -0.54 ALA 89
PRO 224 0.27 VAL 12 -0.44 ALA 89
PRO 224 0.28 PRO 13 -0.32 GLY 90
PRO 224 0.30 SER 14 -0.30 TRP 107
PRO 224 0.28 PRO 15 -0.26 TRP 107
PRO 224 0.29 SER 16 -0.21 GLN 106
PRO 224 0.31 MET 17 -0.27 SER 83
PRO 224 0.28 GLY 18 -0.27 SER 83
PRO 224 0.30 ARG 19 -0.34 GLN 92
PRO 224 0.33 ASP 20 -0.38 GLY 90
PRO 224 0.32 ILE 21 -0.50 ALA 89
PRO 224 0.30 LYS 22 -0.64 ALA 89
PRO 224 0.30 VAL 23 -0.57 ALA 89
PRO 224 0.29 GLN 24 -0.57 ALA 89
PRO 224 0.26 PHE 25 -0.51 ALA 89
PRO 224 0.24 GLN 26 -0.46 ALA 89
PRO 6 0.26 SER 27 -0.42 ALA 89
PRO 224 0.23 GLY 28 -0.37 ALA 89
GLY 4 0.26 GLY 29 -0.36 ALA 89
ASN 203 0.32 ASN 30 -0.35 ALA 89
ASN 203 0.36 ASN 31 -0.32 ALA 89
ASN 250 0.31 SER 32 -0.31 ALA 89
ASN 250 0.31 PRO 33 -0.29 ALA 89
PRO 224 0.27 ALA 34 -0.32 ALA 89
PRO 224 0.32 VAL 35 -0.30 ALA 89
PRO 224 0.35 TYR 36 -0.32 ALA 89
PRO 224 0.41 LEU 37 -0.33 ALA 89
PRO 224 0.46 LEU 38 -0.32 LYS 88
PRO 224 0.57 ASP 39 -0.36 LYS 88
PRO 224 0.69 GLY 40 -0.29 LYS 88
PRO 224 0.69 LEU 41 -0.23 LYS 88
PRO 224 0.57 ARG 42 -0.38 TRP 263
PRO 224 0.53 ALA 43 -0.52 LYS 88
PRO 224 0.41 GLN 44 -0.81 LYS 88
PRO 224 0.34 ASP 45 -1.00 ALA 89
PRO 224 0.30 ASP 46 -0.90 ALA 89
PRO 224 0.33 TYR 47 -0.73 ALA 89
PRO 224 0.41 ASN 48 -0.59 ALA 89
PRO 224 0.48 GLY 49 -0.56 LYS 88
PRO 224 0.42 TRP 50 -0.46 LYS 88
PRO 224 0.33 ASP 51 -0.52 LYS 88
PRO 224 0.33 ILE 52 -0.57 LYS 88
PRO 224 0.36 ASN 53 -0.50 LYS 88
PRO 224 0.29 THR 54 -0.44 LYS 88
PRO 224 0.22 PRO 55 -0.42 LYS 88
PRO 224 0.28 ALA 56 -0.40 LYS 88
PRO 224 0.25 PHE 57 -0.43 ALA 89
PRO 224 0.20 GLU 58 -0.40 ALA 89
PRO 224 0.24 TRP 59 -0.35 ALA 89
PRO 224 0.25 TYR 60 -0.35 ALA 89
PRO 224 0.20 TYR 61 -0.39 ALA 89
SER 63 0.23 GLN 62 -0.37 ALA 89
GLN 62 0.23 SER 63 -0.33 ALA 89
PRO 224 0.23 GLY 64 -0.33 ALA 89
PRO 224 0.26 LEU 65 -0.33 ALA 89
PRO 224 0.26 SER 66 -0.38 ALA 89
PRO 224 0.30 ILE 67 -0.39 ALA 89
PRO 224 0.32 VAL 68 -0.42 ALA 89
PRO 224 0.36 MET 69 -0.46 ALA 89
PRO 224 0.38 PRO 70 -0.48 ALA 89
PRO 224 0.39 VAL 71 -0.62 ALA 89
PRO 224 0.40 GLY 72 -0.63 ALA 89
PRO 224 0.45 GLY 73 -0.33 LYS 88
PRO 224 0.46 GLN 74 -0.34 GLY 72
PRO 224 0.49 SER 75 -0.22 GLY 49
PRO 224 0.44 SER 76 -0.19 VAL 68
PRO 224 0.46 PHE 77 -0.19 ALA 186
PRO 224 0.42 TYR 78 -0.21 ALA 186
PRO 224 0.37 SER 79 -0.23 ALA 186
PRO 224 0.32 ASP 80 -0.23 ASP 184
PRO 224 0.30 TRP 81 -0.28 LYS 95
ARG 189 0.31 TYR 82 -0.22 MET 17
TYR 82 0.28 SER 83 -0.29 THR 93
PRO 224 0.23 PRO 84 -0.30 ILE 21
PRO 224 0.27 ALA 85 -0.36 GLY 72
ILE 223 0.21 CYS 86 -0.46 ASP 45
ASP 177 0.24 GLY 87 -0.61 ASP 45
ALA 176 0.23 LYS 88 -0.88 ASP 45
ILE 223 0.20 ALA 89 -1.00 ASP 45
ILE 223 0.18 GLY 90 -0.72 ASP 45
PRO 224 0.22 CYS 91 -0.42 ASP 45
PRO 224 0.27 GLN 92 -0.45 ILE 21
PRO 224 0.28 THR 93 -0.29 ILE 21
PRO 224 0.34 TYR 94 -0.25 ILE 21
PRO 224 0.33 LYS 95 -0.28 TRP 81
PRO 224 0.37 TRP 96 -0.22 PRO 116
PRO 224 0.34 GLU 97 -0.23 ALA 186
PRO 224 0.31 THR 98 -0.24 PRO 116
PRO 224 0.33 PHE 99 -0.23 PRO 116
PRO 224 0.35 LEU 100 -0.25 PRO 116
HIS 138 0.31 THR 101 -0.30 PRO 116
GLU 103 0.32 SER 102 -0.33 PRO 116
SER 102 0.32 GLU 103 -0.27 GLN 106
PRO 224 0.29 LEU 104 -0.29 ALA 89
GLN 140 0.38 PRO 105 -0.27 LYS 115
GLN 140 0.45 GLN 106 -0.27 GLU 103
GLN 140 0.37 TRP 107 -0.34 ALA 89
GLN 140 0.34 LEU 108 -0.36 ALA 89
GLN 140 0.42 SER 109 -0.31 ALA 89
GLN 140 0.38 ALA 110 -0.33 ALA 89
GLN 140 0.32 ASN 111 -0.38 ALA 89
ASN 203 0.29 ARG 112 -0.40 ALA 89
ASN 203 0.32 ALA 113 -0.36 ALA 89
ASN 203 0.34 VAL 114 -0.34 ALA 89
ASN 203 0.39 LYS 115 -0.29 ALA 89
GLN 140 0.42 PRO 116 -0.33 SER 102
ASN 203 0.44 THR 117 -0.27 THR 101
ASN 203 0.46 GLY 118 -0.21 GLN 141
ASN 203 0.28 SER 119 -0.22 ALA 283
PRO 224 0.30 ALA 120 -0.22 ALA 89
PRO 224 0.33 ALA 121 -0.21 ALA 89
PRO 224 0.37 ILE 122 -0.24 LYS 88
PRO 224 0.42 GLY 123 -0.23 LYS 88
PRO 224 0.51 LEU 124 -0.25 LYS 88
PRO 224 0.55 SER 125 -0.23 ALA 170
PRO 224 0.54 MET 126 -0.19 LEU 41
PRO 224 0.48 ALA 127 -0.18 LYS 88
PRO 224 0.38 GLY 128 -0.15 LEU 41
PRO 224 0.32 SER 129 -0.15 LEU 41
PRO 224 0.35 SER 130 -0.15 ALA 186
PRO 224 0.34 ALA 131 -0.13 ALA 186
PRO 224 0.26 MET 132 -0.10 LEU 41
PRO 224 0.26 ILE 133 -0.11 ALA 283
PRO 224 0.29 LEU 134 -0.18 ALA 186
PRO 105 0.29 ALA 135 -0.15 SER 280
THR 101 0.28 ALA 136 -0.12 SER 280
LYS 198 0.28 TYR 137 -0.16 PRO 185
GLN 106 0.35 HIS 138 -0.17 SER 280
GLN 106 0.39 PRO 139 -0.28 ILE 143
GLN 106 0.45 GLN 140 -0.22 SER 280
GLN 106 0.36 GLN 141 -0.21 GLY 118
THR 204 0.36 PHE 142 -0.17 LEU 281
GLY 118 0.39 ILE 143 -0.28 PRO 139
GLY 118 0.24 TYR 144 -0.17 PRO 139
PRO 224 0.26 ALA 145 -0.15 LYS 88
PRO 224 0.29 GLY 146 -0.18 LYS 88
PRO 224 0.28 SER 147 -0.18 ARG 42
PRO 224 0.33 LEU 148 -0.21 ARG 42
PRO 224 0.26 SER 149 -0.22 ARG 42
PRO 224 0.27 ALA 150 -0.22 SER 125
ARG 233 0.21 LEU 151 -0.19 SER 125
TRP 81 0.17 LEU 152 -0.16 SER 125
SER 234 0.29 ASP 153 -0.16 LEU 41
SER 234 0.31 PRO 154 -0.17 LEU 41
SER 234 0.35 SER 155 -0.15 LEU 41
SER 234 0.46 GLN 156 -0.14 LEU 41
SER 234 0.53 GLY 157 -0.12 PRO 3
SER 234 0.38 MET 158 -0.16 PRO 3
SER 234 0.41 GLY 159 -0.15 PRO 3
ASN 230 0.33 PRO 160 -0.15 PRO 3
ASN 230 0.30 SER 161 -0.18 PRO 3
ASN 230 0.35 LEU 162 -0.20 PRO 3
PHE 227 0.39 ILE 163 -0.18 PRO 3
PHE 227 0.34 GLY 164 -0.19 PRO 3
PHE 227 0.39 LEU 165 -0.21 PRO 3
PRO 224 0.43 ALA 166 -0.22 PRO 3
PRO 224 0.40 MET 167 -0.24 GLN 44
ILE 223 0.32 GLY 168 -0.30 GLN 44
ILE 223 0.33 ASP 169 -0.29 PRO 3
PRO 224 0.37 ALA 170 -0.34 SER 262
ILE 223 0.27 GLY 171 -0.58 GLN 44
ILE 223 0.26 GLY 172 -0.43 GLN 44
ILE 223 0.29 TYR 173 -0.34 ASP 45
ILE 223 0.27 LYS 174 -0.26 GLY 72
PRO 224 0.28 ALA 175 -0.21 GLY 72
PHE 227 0.24 ALA 176 -0.20 GLY 72
GLY 87 0.24 ASP 177 -0.24 GLY 72
PRO 224 0.29 MET 178 -0.21 GLY 72
PRO 224 0.26 TRP 179 -0.22 ASP 80
SER 234 0.25 GLY 180 -0.21 PRO 181
SER 234 0.28 PRO 181 -0.21 GLY 180
SER 234 0.34 SER 182 -0.16 ASP 80
SER 234 0.36 SER 183 -0.17 THR 98
SER 234 0.30 ASP 184 -0.23 THR 98
SER 234 0.28 PRO 185 -0.19 THR 98
SER 234 0.24 ALA 186 -0.23 SER 79
SER 234 0.26 TRP 187 -0.14 PHE 77
SER 234 0.26 GLU 188 -0.15 ARG 189
TYR 82 0.31 ARG 189 -0.15 GLU 188
TRP 81 0.25 ASN 190 -0.13 SER 130
TRP 81 0.21 ASP 191 -0.14 LEU 41
TRP 81 0.19 PRO 192 -0.14 LEU 41
TYR 82 0.20 THR 193 -0.12 LEU 41
PRO 185 0.23 GLN 194 -0.12 LEU 41
TYR 82 0.24 GLN 195 -0.11 GLY 40
GLN 106 0.25 ILE 196 -0.12 LEU 41
GLN 106 0.27 PRO 197 -0.12 ALA 272
GLN 106 0.32 LYS 198 -0.13 ALA 272
GLN 106 0.33 LEU 199 -0.13 ALA 272
GLN 106 0.33 VAL 200 -0.15 ALA 272
GLN 106 0.35 ALA 201 -0.15 ALA 272
GLN 106 0.40 ASN 202 -0.16 ARG 205
GLY 118 0.46 ASN 203 -0.15 ALA 272
GLY 118 0.42 THR 204 -0.22 ARG 205
GLY 118 0.39 ARG 205 -0.22 THR 204
GLY 118 0.27 LEU 206 -0.17 ALA 272
PRO 33 0.22 TRP 207 -0.17 LYS 88
GLU 217 0.19 VAL 208 -0.18 ARG 2
GLU 217 0.20 TYR 209 -0.24 ARG 2
GLY 157 0.21 CYS 210 -0.25 ARG 2
GLY 157 0.25 GLY 211 -0.31 PRO 3
PHE 231 0.38 ASN 212 -0.28 PRO 3
PHE 231 0.30 GLY 213 -0.28 PRO 3
GLY 157 0.27 THR 214 -0.34 PRO 3
GLY 157 0.20 PRO 215 -0.40 PRO 3
PRO 256 0.24 ASN 216 -0.50 PRO 3
PRO 256 0.40 GLU 217 -0.63 PRO 3
ALA 272 0.40 LEU 218 -0.62 PRO 3
ALA 272 0.32 GLY 219 -0.51 PRO 3
ALA 272 0.29 GLY 220 -0.37 LYS 88
ALA 272 0.23 ALA 221 -0.30 PRO 3
TRP 263 0.37 ASN 222 -0.17 PRO 3
LEU 41 0.51 ILE 223 -0.26 SER 234
LEU 41 0.69 PRO 224 -0.20 SER 234
GLY 40 0.38 ALA 225 -0.18 PRO 3
ILE 163 0.27 GLU 226 -0.22 PRO 3
ALA 166 0.40 PHE 227 -0.32 SER 234
MET 126 0.40 LEU 228 -0.22 SER 234
GLY 159 0.28 GLU 229 -0.23 PRO 3
PHE 231 0.61 ASN 230 -0.30 SER 234
ASN 230 0.61 PHE 231 -0.24 LYS 238
GLY 159 0.31 VAL 232 -0.20 PRO 3
GLY 157 0.39 ARG 233 -0.27 ASN 230
GLY 157 0.53 SER 234 -0.32 PHE 227
GLN 156 0.34 SER 235 -0.19 PHE 231
GLY 157 0.23 ASN 236 -0.18 ARG 2
GLY 157 0.27 LEU 237 -0.29 ASN 230
GLN 156 0.28 LYS 238 -0.26 PHE 227
PRO 185 0.22 PHE 239 -0.17 PHE 231
GLY 118 0.22 GLN 240 -0.21 ASN 230
PRO 185 0.23 ASP 241 -0.25 ASN 230
PRO 185 0.25 ALA 242 -0.20 ASN 230
GLY 118 0.26 TYR 243 -0.17 ASN 230
GLY 118 0.27 ASN 244 -0.21 ASN 230
GLY 118 0.25 ALA 245 -0.21 ASN 230
GLN 106 0.27 ALA 246 -0.17 ASN 230
GLY 118 0.31 GLY 247 -0.17 ASN 230
GLY 118 0.35 GLY 248 -0.15 ASN 230
GLY 118 0.36 HIS 249 -0.21 PHE 253
GLY 118 0.41 ASN 250 -0.23 ALA 251
GLY 118 0.30 ALA 251 -0.23 ASN 250
SER 280 0.28 VAL 252 -0.24 ALA 272
GLU 217 0.24 PHE 253 -0.21 HIS 249
GLU 217 0.29 ASN 254 -0.26 ARG 2
GLU 217 0.29 PHE 255 -0.28 ARG 2
GLU 217 0.40 PRO 256 -0.33 ARG 2
GLY 157 0.37 PRO 257 -0.38 ARG 2
GLY 157 0.29 ASN 258 -0.40 ARG 2
GLY 157 0.21 GLY 259 -0.38 PRO 3
MET 273 0.17 THR 260 -0.32 PRO 3
PRO 224 0.33 HIS 261 -0.27 LYS 88
PRO 224 0.40 SER 262 -0.38 LYS 88
PRO 224 0.43 TRP 263 -0.43 LYS 88
ALA 268 0.32 GLU 264 -0.44 PRO 3
ALA 272 0.28 TYR 265 -0.40 ARG 2
PRO 224 0.33 TRP 266 -0.33 LYS 88
PRO 224 0.32 GLY 267 -0.35 LYS 88
GLU 264 0.32 ALA 268 -0.37 ARG 2
PRO 224 0.27 GLN 269 -0.29 ARG 2
PRO 224 0.31 LEU 270 -0.29 LYS 88
PRO 224 0.27 ASN 271 -0.28 LYS 88
LEU 218 0.40 ALA 272 -0.24 VAL 252
GLU 217 0.28 MET 273 -0.24 ALA 89
PRO 224 0.25 LYS 274 -0.27 ALA 89
GLU 217 0.32 GLY 275 -0.24 ALA 89
GLU 217 0.31 ASP 276 -0.21 ALA 89
PRO 224 0.26 LEU 277 -0.24 ALA 89
GLU 217 0.24 GLN 278 -0.26 ALA 89
GLU 217 0.27 SER 279 -0.22 ALA 89
ASN 250 0.30 SER 280 -0.23 PRO 139
ASN 250 0.34 LEU 281 -0.23 ALA 89
ASN 250 0.31 GLY 282 -0.23 ALA 89
PRO 224 0.21 ALA 283 -0.29 ALA 89
GLU 217 0.24 GLY 284 -0.29 ALA 89

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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.