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 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
LEU 218 0.52 SER 1 -0.13 VAL 7
LEU 218 0.63 ARG 2 -0.26 VAL 7
LEU 218 0.64 PRO 3 -0.37 VAL 7
LYS 88 0.53 GLY 4 -0.26 GLY 29
ALA 89 0.50 LEU 5 -0.23 GLY 29
ALA 89 0.52 PRO 6 -0.27 GLY 29
ALA 89 0.53 VAL 7 -0.37 PRO 3
ALA 89 0.56 GLU 8 -0.36 PRO 3
ALA 89 0.63 TYR 9 -0.28 PRO 3
ALA 89 0.57 LEU 10 -0.24 PRO 3
ALA 89 0.55 GLN 11 -0.25 PRO 224
ALA 89 0.44 VAL 12 -0.26 PRO 224
GLY 90 0.32 PRO 13 -0.27 PRO 224
TRP 107 0.30 SER 14 -0.28 PRO 224
TRP 107 0.25 PRO 15 -0.26 PRO 224
GLN 106 0.21 SER 16 -0.28 PRO 224
SER 83 0.26 MET 17 -0.30 PRO 224
SER 83 0.26 GLY 18 -0.27 PRO 224
GLY 90 0.33 ARG 19 -0.29 PRO 224
GLY 90 0.37 ASP 20 -0.32 PRO 224
ALA 89 0.51 ILE 21 -0.31 PRO 224
ALA 89 0.65 LYS 22 -0.30 PRO 224
ALA 89 0.58 VAL 23 -0.30 PRO 224
ALA 89 0.57 GLN 24 -0.29 PRO 224
ALA 89 0.52 PHE 25 -0.26 PRO 224
ALA 89 0.46 GLN 26 -0.24 PRO 224
ALA 89 0.42 SER 27 -0.27 PRO 6
ALA 89 0.37 GLY 28 -0.23 PRO 6
ALA 89 0.36 GLY 29 -0.27 PRO 6
ALA 89 0.35 ASN 30 -0.30 ASN 203
ALA 89 0.32 ASN 31 -0.34 ASN 203
GLY 284 0.32 SER 32 -0.29 ASN 203
ALA 89 0.29 PRO 33 -0.29 ASN 250
ALA 89 0.33 ALA 34 -0.27 PRO 224
ALA 89 0.31 VAL 35 -0.31 PRO 224
ALA 89 0.32 TYR 36 -0.34 PRO 224
LYS 88 0.34 LEU 37 -0.40 PRO 224
LYS 88 0.33 LEU 38 -0.44 PRO 224
LYS 88 0.37 ASP 39 -0.55 PRO 224
LYS 88 0.31 GLY 40 -0.66 PRO 224
LYS 88 0.24 LEU 41 -0.64 PRO 224
TRP 263 0.39 ARG 42 -0.54 PRO 224
LYS 88 0.54 ALA 43 -0.51 PRO 224
LYS 88 0.83 GLN 44 -0.41 PRO 224
ALA 89 1.01 ASP 45 -0.33 PRO 224
ALA 89 0.90 ASP 46 -0.29 PRO 224
ALA 89 0.73 TYR 47 -0.33 PRO 224
ALA 89 0.59 ASN 48 -0.41 PRO 224
LYS 88 0.57 GLY 49 -0.49 PRO 224
LYS 88 0.47 TRP 50 -0.42 PRO 224
LYS 88 0.53 ASP 51 -0.33 PRO 224
LYS 88 0.58 ILE 52 -0.34 PRO 224
LYS 88 0.52 ASN 53 -0.37 PRO 224
LYS 88 0.45 THR 54 -0.30 PRO 224
LYS 88 0.43 PRO 55 -0.23 PRO 224
LYS 88 0.41 ALA 56 -0.28 PRO 224
ALA 89 0.43 PHE 57 -0.25 PRO 224
LYS 88 0.40 GLU 58 -0.20 PRO 224
LYS 88 0.35 TRP 59 -0.25 PRO 224
ALA 89 0.36 TYR 60 -0.25 PRO 224
ALA 89 0.40 TYR 61 -0.20 PRO 224
ALA 89 0.38 GLN 62 -0.22 SER 63
ALA 89 0.33 SER 63 -0.23 PRO 224
ALA 89 0.33 GLY 64 -0.23 PRO 224
ALA 89 0.34 LEU 65 -0.25 PRO 224
ALA 89 0.38 SER 66 -0.26 PRO 224
ALA 89 0.40 ILE 67 -0.29 PRO 224
ALA 89 0.43 VAL 68 -0.31 PRO 224
ALA 89 0.46 MET 69 -0.36 PRO 224
ALA 89 0.48 PRO 70 -0.37 PRO 224
ALA 89 0.63 VAL 71 -0.38 PRO 224
ALA 89 0.64 GLY 72 -0.39 PRO 224
LYS 88 0.34 GLY 73 -0.43 PRO 224
GLY 49 0.34 GLN 74 -0.43 PRO 224
GLY 49 0.23 SER 75 -0.45 PRO 224
LEU 38 0.19 SER 76 -0.41 PRO 224
ALA 186 0.20 PHE 77 -0.42 PRO 224
ALA 186 0.21 TYR 78 -0.40 PRO 224
ALA 186 0.23 SER 79 -0.34 PRO 224
ASP 184 0.22 ASP 80 -0.29 PRO 224
LYS 95 0.27 TRP 81 -0.30 ARG 189
LYS 95 0.21 TYR 82 -0.32 ARG 189
THR 93 0.28 SER 83 -0.29 ARG 189
ILE 21 0.30 PRO 84 -0.24 ARG 189
GLY 72 0.36 ALA 85 -0.24 PRO 224
ASP 45 0.46 CYS 86 -0.21 ASP 177
ASP 45 0.62 GLY 87 -0.25 ASP 177
ASP 45 0.90 LYS 88 -0.23 ALA 176
ASP 45 1.01 ALA 89 -0.17 ILE 223
ASP 45 0.72 GLY 90 -0.17 ASP 177
ASP 45 0.43 CYS 91 -0.19 PRO 224
ILE 21 0.44 GLN 92 -0.25 PRO 224
ILE 21 0.29 THR 93 -0.26 PRO 224
ILE 21 0.24 TYR 94 -0.31 PRO 224
TRP 81 0.27 LYS 95 -0.31 PRO 224
PRO 116 0.22 TRP 96 -0.35 PRO 224
ALA 186 0.22 GLU 97 -0.32 PRO 224
PRO 116 0.24 THR 98 -0.29 PRO 224
PRO 116 0.23 PHE 99 -0.31 PRO 224
PRO 116 0.25 LEU 100 -0.33 PRO 224
PRO 116 0.30 THR 101 -0.31 HIS 138
PRO 116 0.33 SER 102 -0.33 GLU 103
GLN 106 0.27 GLU 103 -0.33 SER 102
ALA 89 0.30 LEU 104 -0.28 PRO 224
LYS 115 0.27 PRO 105 -0.38 GLN 140
ALA 89 0.28 GLN 106 -0.44 GLN 140
ALA 89 0.35 TRP 107 -0.37 GLN 140
ALA 89 0.37 LEU 108 -0.34 GLN 140
ALA 89 0.31 SER 109 -0.42 GLN 140
ALA 89 0.33 ALA 110 -0.37 GLN 140
ALA 89 0.39 ASN 111 -0.32 GLN 140
ALA 89 0.40 ARG 112 -0.28 GLN 140
ALA 89 0.36 ALA 113 -0.31 ASN 203
ALA 89 0.35 VAL 114 -0.32 ASN 203
ALA 89 0.29 LYS 115 -0.37 ASN 203
SER 102 0.33 PRO 116 -0.42 GLN 140
THR 101 0.27 THR 117 -0.42 ASN 203
ALA 89 0.21 GLY 118 -0.44 ASN 203
ALA 89 0.23 SER 119 -0.26 ASN 203
ALA 89 0.22 ALA 120 -0.29 PRO 224
LYS 88 0.22 ALA 121 -0.32 PRO 224
LYS 88 0.24 ILE 122 -0.36 PRO 224
LYS 88 0.24 GLY 123 -0.40 PRO 224
LYS 88 0.25 LEU 124 -0.49 PRO 224
ALA 170 0.23 SER 125 -0.51 PRO 224
LEU 41 0.18 MET 126 -0.50 PRO 224
LYS 88 0.19 ALA 127 -0.45 PRO 224
LYS 88 0.15 GLY 128 -0.36 PRO 224
LEU 41 0.15 SER 129 -0.29 PRO 224
ALA 186 0.15 SER 130 -0.33 PRO 224
ALA 186 0.13 ALA 131 -0.32 PRO 224
LEU 41 0.10 MET 132 -0.24 PRO 224
ALA 283 0.11 ILE 133 -0.24 PRO 224
ALA 186 0.19 LEU 134 -0.27 LEU 100
TYR 144 0.14 ALA 135 -0.29 PRO 105
SER 280 0.12 ALA 136 -0.29 THR 101
PRO 185 0.16 TYR 137 -0.29 LYS 198
LEU 281 0.17 HIS 138 -0.35 GLN 106
ILE 143 0.27 PRO 139 -0.39 GLN 106
SER 280 0.21 GLN 140 -0.44 GLN 106
GLY 118 0.20 GLN 141 -0.36 GLN 106
LEU 281 0.17 PHE 142 -0.35 THR 204
PRO 139 0.27 ILE 143 -0.37 GLY 118
PRO 139 0.16 TYR 144 -0.23 GLY 118
LYS 88 0.16 ALA 145 -0.25 PRO 224
LYS 88 0.19 GLY 146 -0.28 PRO 224
ARG 42 0.17 SER 147 -0.26 PRO 224
LYS 88 0.21 LEU 148 -0.31 PRO 224
ARG 42 0.21 SER 149 -0.23 PRO 224
SER 125 0.21 ALA 150 -0.24 PRO 224
SER 125 0.18 LEU 151 -0.22 ARG 233
SER 125 0.16 LEU 152 -0.19 TRP 81
LEU 41 0.15 ASP 153 -0.32 SER 234
LEU 41 0.16 PRO 154 -0.35 SER 234
LEU 41 0.14 SER 155 -0.39 SER 234
GLY 159 0.14 GLN 156 -0.52 SER 234
PRO 3 0.11 GLY 157 -0.62 SER 234
PRO 3 0.15 MET 158 -0.44 SER 234
PRO 3 0.14 GLY 159 -0.47 SER 234
PRO 3 0.15 PRO 160 -0.36 SER 234
PRO 3 0.17 SER 161 -0.30 ASN 230
PRO 3 0.19 LEU 162 -0.34 ASN 230
PRO 3 0.18 ILE 163 -0.37 PHE 227
GLY 4 0.18 GLY 164 -0.31 PHE 227
PRO 3 0.20 LEU 165 -0.37 PHE 227
PRO 3 0.21 ALA 166 -0.38 PHE 227
GLN 44 0.24 MET 167 -0.35 PRO 224
GLN 44 0.30 GLY 168 -0.28 ILE 223
SER 262 0.29 ASP 169 -0.28 ILE 223
TRP 263 0.35 ALA 170 -0.33 PRO 224
GLN 44 0.60 GLY 171 -0.23 ILE 223
GLN 44 0.44 GLY 172 -0.23 ILE 223
ASP 45 0.34 TYR 173 -0.26 PRO 224
GLY 72 0.26 LYS 174 -0.26 ALA 175
GLY 72 0.21 ALA 175 -0.26 PHE 227
GLY 72 0.20 ALA 176 -0.25 SER 234
GLY 72 0.24 ASP 177 -0.25 GLY 87
GLY 72 0.21 MET 178 -0.26 PRO 224
ASP 80 0.22 TRP 179 -0.27 SER 234
PRO 181 0.21 GLY 180 -0.28 SER 234
GLY 180 0.21 PRO 181 -0.31 SER 234
ASP 80 0.16 SER 182 -0.37 SER 234
THR 98 0.17 SER 183 -0.39 SER 234
ASP 80 0.22 ASP 184 -0.32 SER 234
GLU 97 0.18 PRO 185 -0.30 SER 234
SER 79 0.23 ALA 186 -0.26 SER 234
PHE 77 0.14 TRP 187 -0.29 SER 234
ARG 189 0.15 GLU 188 -0.28 SER 234
GLU 188 0.15 ARG 189 -0.32 TYR 82
SER 130 0.15 ASN 190 -0.27 TRP 81
LEU 41 0.14 ASP 191 -0.23 TRP 81
LEU 41 0.14 PRO 192 -0.21 TRP 81
LEU 41 0.12 THR 193 -0.21 TYR 82
LEU 41 0.12 GLN 194 -0.25 PRO 185
GLY 40 0.11 GLN 195 -0.26 TYR 82
SER 125 0.12 ILE 196 -0.25 GLN 106
ALA 272 0.12 PRO 197 -0.28 GLN 106
ALA 272 0.13 LYS 198 -0.33 GLN 106
ALA 272 0.13 LEU 199 -0.33 GLN 106
ALA 272 0.15 VAL 200 -0.33 GLN 106
ALA 272 0.14 ALA 201 -0.35 GLN 106
ARG 205 0.16 ASN 202 -0.40 GLN 106
ALA 272 0.14 ASN 203 -0.44 GLY 118
ARG 205 0.21 THR 204 -0.40 GLY 118
THR 204 0.21 ARG 205 -0.37 GLY 118
ALA 272 0.17 LEU 206 -0.25 GLY 118
LYS 88 0.17 TRP 207 -0.20 GLY 118
ARG 2 0.19 VAL 208 -0.17 GLY 118
ARG 2 0.25 TYR 209 -0.17 GLU 217
ARG 2 0.26 CYS 210 -0.24 GLY 157
ARG 2 0.32 GLY 211 -0.29 GLY 157
PRO 3 0.29 ASN 212 -0.40 GLY 157
PRO 3 0.28 GLY 213 -0.31 GLY 157
PRO 3 0.35 THR 214 -0.31 GLY 157
PRO 3 0.41 PRO 215 -0.22 GLY 157
PRO 3 0.52 ASN 216 -0.23 GLY 157
PRO 3 0.63 GLU 217 -0.34 ALA 272
PRO 3 0.64 LEU 218 -0.42 ALA 272
PRO 3 0.52 GLY 219 -0.35 ALA 272
LYS 88 0.39 GLY 220 -0.30 ALA 272
PRO 3 0.32 ALA 221 -0.24 ALA 272
PRO 3 0.18 ASN 222 -0.36 TRP 263
SER 234 0.25 ILE 223 -0.47 LEU 41
SER 234 0.20 PRO 224 -0.66 GLY 40
PRO 3 0.18 ALA 225 -0.36 GLY 40
PRO 3 0.22 GLU 226 -0.25 ILE 163
SER 234 0.30 PHE 227 -0.38 ALA 166
SER 234 0.21 LEU 228 -0.40 MET 126
PRO 3 0.23 GLU 229 -0.27 GLY 159
ARG 233 0.27 ASN 230 -0.57 PHE 231
LYS 238 0.25 PHE 231 -0.57 ASN 230
LYS 238 0.21 VAL 232 -0.35 GLY 159
ASN 230 0.27 ARG 233 -0.45 GLY 157
PHE 227 0.30 SER 234 -0.62 GLY 157
VAL 232 0.20 SER 235 -0.40 GLY 157
ARG 2 0.19 ASN 236 -0.28 GLY 157
SER 234 0.27 LEU 237 -0.34 GLY 157
PHE 227 0.25 LYS 238 -0.34 GLN 156
PHE 231 0.17 PHE 239 -0.24 PRO 185
ASN 230 0.20 GLN 240 -0.21 GLY 118
ASN 230 0.24 ASP 241 -0.25 PRO 185
PHE 227 0.20 ALA 242 -0.28 PRO 185
ASN 230 0.15 TYR 243 -0.25 GLY 118
ASN 230 0.20 ASN 244 -0.25 GLY 118
PHE 227 0.20 ALA 245 -0.25 PRO 185
ASN 230 0.16 ALA 246 -0.27 GLN 106
ASN 230 0.16 GLY 247 -0.30 GLY 118
ALA 272 0.15 GLY 248 -0.33 GLY 118
ALA 272 0.20 HIS 249 -0.34 GLY 118
ALA 251 0.20 ASN 250 -0.39 GLY 118
ASN 250 0.20 ALA 251 -0.29 GLY 118
ALA 272 0.26 VAL 252 -0.26 SER 280
ARG 2 0.22 PHE 253 -0.21 SER 280
ARG 2 0.28 ASN 254 -0.25 GLU 217
ARG 2 0.30 PHE 255 -0.30 GLY 157
ARG 2 0.36 PRO 256 -0.32 GLU 217
ARG 2 0.41 PRO 257 -0.41 GLY 157
ARG 2 0.43 ASN 258 -0.33 GLY 157
ARG 2 0.39 GLY 259 -0.24 GLY 157
PRO 3 0.32 THR 260 -0.18 MET 273
LYS 88 0.27 HIS 261 -0.32 PRO 224
LYS 88 0.39 SER 262 -0.41 PRO 224
LYS 88 0.44 TRP 263 -0.44 PRO 224
PRO 3 0.45 GLU 264 -0.36 ALA 268
ARG 2 0.42 TYR 265 -0.28 ALA 272
LYS 88 0.34 TRP 266 -0.33 PRO 224
LYS 88 0.37 GLY 267 -0.32 PRO 224
ARG 2 0.38 ALA 268 -0.36 GLU 264
ARG 2 0.31 GLN 269 -0.27 PRO 224
LYS 88 0.30 LEU 270 -0.31 PRO 224
LYS 88 0.29 ASN 271 -0.29 GLU 264
VAL 252 0.26 ALA 272 -0.42 LEU 218
LYS 88 0.24 MET 273 -0.32 LEU 218
ALA 89 0.27 LYS 274 -0.26 PRO 224
ALA 89 0.25 GLY 275 -0.32 LEU 218
ALA 89 0.22 ASP 276 -0.30 LEU 218
ALA 89 0.24 LEU 277 -0.25 PRO 224
ALA 89 0.26 GLN 278 -0.23 PRO 224
ALA 89 0.22 SER 279 -0.26 GLU 217
PRO 139 0.22 SER 280 -0.27 ASN 250
ALA 89 0.23 LEU 281 -0.31 ASN 250
ALA 89 0.24 GLY 282 -0.28 ASN 250
ALA 89 0.30 ALA 283 -0.20 PRO 224
SER 32 0.32 GLY 284 -0.26 GLY 275

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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.