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***  EXP_1F0N_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000  ***

CA distance fluctuations for 24021912142413056

---  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
ALA 89 0.42 SER 1 -0.40 ASN 222
ALA 89 0.45 ARG 2 -0.39 ASN 222
ASP 46 0.56 PRO 3 -0.35 ASN 222
ALA 89 0.41 GLY 4 -0.32 ASN 222
ALA 89 0.31 LEU 5 -0.32 ASN 222
ALA 89 0.25 PRO 6 -0.31 ASN 222
ALA 89 0.26 VAL 7 -0.36 PRO 224
PRO 3 0.26 GLU 8 -0.36 PRO 224
PRO 3 0.36 TYR 9 -0.40 PRO 224
PRO 3 0.27 LEU 10 -0.36 PRO 224
PRO 3 0.26 GLN 11 -0.35 PRO 224
PRO 3 0.21 VAL 12 -0.30 PRO 224
PRO 3 0.19 PRO 13 -0.27 PRO 224
PRO 3 0.19 SER 14 -0.23 PRO 224
PRO 3 0.17 PRO 15 -0.18 PRO 224
PRO 3 0.19 SER 16 -0.16 GLN 92
PRO 3 0.23 MET 17 -0.19 PRO 224
PRO 3 0.23 GLY 18 -0.21 PRO 224
PRO 3 0.26 ARG 19 -0.28 PRO 224
PRO 3 0.26 ASP 20 -0.33 PRO 224
PRO 3 0.28 ILE 21 -0.34 PRO 224
PRO 3 0.34 LYS 22 -0.39 PRO 224
PRO 3 0.30 VAL 23 -0.36 PRO 224
PRO 3 0.34 GLN 24 -0.39 PRO 224
ALA 89 0.21 PHE 25 -0.33 PRO 224
ALA 89 0.21 GLN 26 -0.29 PRO 224
ALA 89 0.16 SER 27 -0.25 PRO 224
ALA 89 0.14 GLY 28 -0.21 PRO 224
ALA 89 0.12 GLY 29 -0.19 PRO 224
ASN 250 0.13 ASN 30 -0.17 PRO 224
ASN 250 0.16 ASN 31 -0.15 PRO 224
ASN 250 0.14 SER 32 -0.16 PRO 224
ASN 250 0.14 PRO 33 -0.14 PRO 224
ALA 89 0.11 ALA 34 -0.18 PRO 224
ALA 89 0.14 VAL 35 -0.19 PRO 224
PRO 3 0.14 TYR 36 -0.22 PRO 224
ARG 42 0.18 LEU 37 -0.28 PRO 224
LEU 41 0.19 LEU 38 -0.28 PRO 224
LEU 41 0.24 ASP 39 -0.41 PRO 224
LEU 41 0.38 GLY 40 -0.41 LEU 228
GLY 49 0.40 LEU 41 -0.41 PHE 231
GLY 49 0.57 ARG 42 -0.50 PRO 224
GLY 49 0.46 ALA 43 -0.54 PRO 224
ALA 89 0.52 GLN 44 -0.62 PRO 224
ALA 89 0.47 ASP 45 -0.53 PRO 224
PRO 3 0.56 ASP 46 -0.59 PRO 224
PRO 3 0.52 TYR 47 -0.57 PRO 224
PRO 3 0.37 ASN 48 -0.52 PRO 224
ARG 42 0.57 GLY 49 -0.57 PRO 224
ARG 42 0.41 TRP 50 -0.43 PRO 224
ARG 42 0.39 ASP 51 -0.46 PRO 224
ARG 42 0.46 ILE 52 -0.57 PRO 224
ARG 42 0.52 ASN 53 -0.51 ASN 222
ARG 42 0.40 THR 54 -0.40 ASN 222
LYS 88 0.35 PRO 55 -0.41 GLU 264
ARG 42 0.30 ALA 56 -0.32 GLU 264
ALA 89 0.29 PHE 57 -0.31 ASN 222
LYS 88 0.30 GLU 58 -0.30 ASN 222
LYS 88 0.27 TRP 59 -0.25 LEU 218
LYS 88 0.24 TYR 60 -0.21 PRO 224
ALA 89 0.25 TYR 61 -0.22 ASN 222
ALA 89 0.20 GLN 62 -0.18 ASN 222
ALA 89 0.19 SER 63 -0.16 PRO 224
ALA 89 0.15 GLY 64 -0.15 PRO 224
ALA 89 0.15 LEU 65 -0.18 PRO 224
ALA 89 0.15 SER 66 -0.22 PRO 224
ALA 89 0.19 ILE 67 -0.26 PRO 224
PRO 3 0.18 VAL 68 -0.29 PRO 224
PRO 3 0.25 MET 69 -0.35 PRO 224
PRO 3 0.28 PRO 70 -0.35 PRO 224
PRO 3 0.38 VAL 71 -0.45 PRO 224
PRO 3 0.36 GLY 72 -0.42 PRO 224
PRO 3 0.33 GLY 73 -0.30 PRO 224
GLY 49 0.40 GLN 74 -0.30 PRO 224
GLY 49 0.33 SER 75 -0.24 PHE 231
PRO 3 0.27 SER 76 -0.16 PHE 231
PRO 3 0.21 PHE 77 -0.12 PHE 231
PRO 3 0.21 TYR 78 -0.12 PRO 224
PRO 3 0.19 SER 79 -0.11 THR 117
PRO 3 0.20 ASP 80 -0.19 TRP 81
PRO 3 0.23 TRP 81 -0.19 ASP 80
PRO 3 0.22 TYR 82 -0.16 TYR 137
PRO 3 0.26 SER 83 -0.15 SER 102
PRO 3 0.30 PRO 84 -0.15 SER 16
PRO 3 0.34 ALA 85 -0.12 SER 16
PRO 3 0.38 CYS 86 -0.12 SER 16
PRO 3 0.43 GLY 87 -0.16 PHE 231
PRO 3 0.50 LYS 88 -0.19 PHE 231
PRO 3 0.53 ALA 89 -0.20 PHE 231
PRO 3 0.47 GLY 90 -0.15 PHE 231
PRO 3 0.39 CYS 91 -0.16 GLY 18
PRO 3 0.36 GLN 92 -0.17 GLY 18
PRO 3 0.29 THR 93 -0.16 GLN 92
PRO 3 0.28 TYR 94 -0.11 PHE 231
PRO 3 0.22 LYS 95 -0.13 PRO 116
PRO 3 0.22 TRP 96 -0.15 PRO 224
PRO 3 0.17 GLU 97 -0.13 PRO 116
PRO 3 0.16 THR 98 -0.17 PRO 116
PRO 3 0.18 PHE 99 -0.18 PRO 224
PRO 3 0.16 LEU 100 -0.17 PRO 224
HIS 138 0.14 THR 101 -0.19 PRO 116
LYS 198 0.15 SER 102 -0.19 PRO 116
SER 102 0.15 GLU 103 -0.18 PRO 224
PRO 3 0.15 LEU 104 -0.22 PRO 224
PRO 139 0.18 PRO 105 -0.18 PRO 224
GLN 140 0.20 GLN 106 -0.17 PRO 224
GLN 140 0.16 TRP 107 -0.22 PRO 224
ASN 203 0.15 LEU 108 -0.22 PRO 224
ASN 203 0.18 SER 109 -0.18 PRO 224
ASN 203 0.17 ALA 110 -0.20 PRO 224
ASN 203 0.14 ASN 111 -0.23 PRO 224
ASN 203 0.13 ARG 112 -0.23 PRO 224
ASN 203 0.14 ALA 113 -0.19 PRO 224
ASN 203 0.14 VAL 114 -0.19 PRO 224
ASN 203 0.17 LYS 115 -0.15 PRO 224
ASN 203 0.20 PRO 116 -0.19 SER 102
ASN 203 0.22 THR 117 -0.16 TYR 82
ASN 250 0.23 GLY 118 -0.15 GLN 141
ARG 205 0.14 SER 119 -0.12 PRO 224
ARG 205 0.10 ALA 120 -0.12 PRO 224
ALA 166 0.11 ALA 121 -0.14 PRO 224
ALA 166 0.16 ILE 122 -0.16 PRO 224
ALA 166 0.20 GLY 123 -0.18 PRO 224
ALA 166 0.30 LEU 124 -0.21 LEU 228
ILE 163 0.37 SER 125 -0.31 GLY 40
ILE 163 0.29 MET 126 -0.24 VAL 232
ALA 166 0.16 ALA 127 -0.15 PHE 231
ILE 163 0.15 GLY 128 -0.11 ALA 43
GLY 220 0.09 SER 129 -0.11 ALA 43
PRO 3 0.13 SER 130 -0.07 ALA 43
PRO 3 0.10 ALA 131 -0.08 PRO 224
PRO 3 0.07 MET 132 -0.08 ARG 189
PRO 3 0.10 ILE 133 -0.09 ALA 186
PRO 3 0.11 LEU 134 -0.11 TYR 82
PRO 105 0.12 ALA 135 -0.13 ILE 143
THR 101 0.13 ALA 136 -0.17 PRO 185
LYS 198 0.14 TYR 137 -0.18 PRO 185
LEU 199 0.16 HIS 138 -0.16 TYR 82
GLN 106 0.19 PRO 139 -0.20 ILE 143
ASN 203 0.22 GLN 140 -0.16 GLY 282
ASN 203 0.19 GLN 141 -0.15 GLY 118
THR 204 0.19 PHE 142 -0.13 LEU 281
GLY 118 0.20 ILE 143 -0.20 PRO 139
GLY 118 0.13 TYR 144 -0.11 ALA 135
ALA 166 0.09 ALA 145 -0.08 GLY 267
ALA 166 0.13 GLY 146 -0.09 PRO 224
ALA 166 0.14 SER 147 -0.08 GLN 44
ALA 166 0.23 LEU 148 -0.12 ASN 48
ILE 163 0.25 SER 149 -0.20 GLN 44
LEU 151 0.28 ALA 150 -0.23 ALA 43
ALA 150 0.28 LEU 151 -0.27 LEU 41
VAL 232 0.15 LEU 152 -0.18 LEU 41
LEU 228 0.25 ASP 153 -0.18 PHE 239
LEU 228 0.35 PRO 154 -0.16 ILE 163
LEU 228 0.34 SER 155 -0.19 ALA 246
LEU 228 0.41 GLN 156 -0.25 ALA 242
PRO 224 0.50 GLY 157 -0.30 ALA 242
PRO 224 0.57 MET 158 -0.28 LYS 238
LEU 228 0.55 GLY 159 -0.18 ALA 242
PRO 224 0.46 PRO 160 -0.16 ALA 242
PRO 224 0.56 SER 161 -0.19 LYS 238
PRO 224 0.65 LEU 162 -0.22 ALA 166
SER 262 0.49 ILE 163 -0.16 PRO 154
SER 262 0.46 GLY 164 -0.13 ALA 242
ALA 225 0.56 LEU 165 -0.16 GLY 168
SER 262 0.61 ALA 166 -0.22 LEU 162
SER 262 0.44 MET 167 -0.18 PHE 231
SER 262 0.43 GLY 168 -0.17 SER 234
SER 262 0.50 ASP 169 -0.27 PHE 231
ASN 53 0.49 ALA 170 -0.31 PHE 231
ASN 53 0.46 GLY 171 -0.24 PHE 231
ASN 53 0.39 GLY 172 -0.19 PHE 231
PRO 3 0.35 TYR 173 -0.14 SER 234
SER 262 0.32 LYS 174 -0.12 ALA 175
SER 262 0.34 ALA 175 -0.12 LYS 174
GLY 220 0.29 ALA 176 -0.13 ALA 246
PRO 3 0.27 ASP 177 -0.11 TYR 137
PRO 3 0.24 MET 178 -0.12 TYR 137
GLY 220 0.22 TRP 179 -0.14 TYR 137
PRO 224 0.27 GLY 180 -0.14 LYS 198
PRO 224 0.36 PRO 181 -0.16 ALA 246
PRO 224 0.41 SER 182 -0.18 ALA 246
PRO 224 0.38 SER 183 -0.19 ALA 246
PRO 224 0.30 ASP 184 -0.19 LYS 198
PRO 224 0.24 PRO 185 -0.23 LYS 198
PRO 224 0.19 ALA 186 -0.19 ARG 189
PRO 224 0.25 TRP 187 -0.16 ALA 246
LEU 228 0.23 GLU 188 -0.23 GLN 195
LEU 228 0.15 ARG 189 -0.19 ALA 186
LEU 228 0.13 ASN 190 -0.10 LYS 174
LEU 228 0.17 ASP 191 -0.11 MET 167
VAL 232 0.13 PRO 192 -0.10 TYR 243
SER 235 0.18 THR 193 -0.16 TYR 243
PHE 231 0.18 GLN 194 -0.21 ALA 246
PHE 231 0.13 GLN 195 -0.23 GLU 188
TYR 137 0.14 ILE 196 -0.17 GLU 188
ALA 242 0.15 PRO 197 -0.22 PRO 185
HIS 138 0.16 LYS 198 -0.23 PRO 185
PRO 139 0.16 LEU 199 -0.18 PRO 185
GLN 140 0.18 VAL 200 -0.18 PRO 185
ALA 246 0.20 ALA 201 -0.22 PRO 185
GLN 140 0.21 ASN 202 -0.19 PRO 185
GLN 140 0.22 ASN 203 -0.17 PRO 185
GLY 118 0.20 THR 204 -0.18 ARG 205
GLY 118 0.22 ARG 205 -0.18 THR 204
GLY 118 0.15 LEU 206 -0.10 ILE 196
GLY 118 0.11 TRP 207 -0.11 ILE 196
ALA 166 0.10 VAL 208 -0.10 GLY 267
ALA 166 0.15 TYR 209 -0.10 GLN 44
LEU 162 0.16 CYS 210 -0.17 GLN 44
LEU 162 0.20 GLY 211 -0.19 GLN 44
GLY 159 0.17 ASN 212 -0.23 GLN 44
LEU 162 0.29 GLY 213 -0.28 GLN 44
LEU 162 0.26 THR 214 -0.26 ILE 52
LEU 165 0.36 PRO 215 -0.29 ARG 2
LEU 165 0.33 ASN 216 -0.28 ARG 2
LEU 165 0.37 GLU 217 -0.34 ARG 2
ALA 166 0.41 LEU 218 -0.36 ARG 2
LEU 165 0.48 GLY 219 -0.39 ARG 2
LEU 165 0.56 GLY 220 -0.45 ASN 53
LEU 165 0.48 ALA 221 -0.43 ILE 52
LEU 165 0.54 ASN 222 -0.54 ILE 52
LEU 162 0.48 ILE 223 -0.52 ASP 46
LEU 162 0.65 PRO 224 -0.62 GLN 44
LEU 162 0.62 ALA 225 -0.49 GLY 49
LEU 162 0.44 GLU 226 -0.38 GLN 44
GLY 157 0.44 PHE 227 -0.46 GLN 44
GLY 159 0.55 LEU 228 -0.49 ARG 42
GLY 159 0.38 GLU 229 -0.34 GLN 44
GLN 156 0.26 ASN 230 -0.33 GLN 44
GLN 156 0.35 PHE 231 -0.43 ARG 42
GLN 156 0.28 VAL 232 -0.35 LEU 41
ASN 230 0.14 ARG 233 -0.26 ALA 43
LEU 237 0.14 SER 234 -0.27 LEU 41
THR 193 0.18 SER 235 -0.25 LEU 41
ASN 230 0.11 ASN 236 -0.18 ALA 43
SER 234 0.14 LEU 237 -0.18 MET 158
PHE 231 0.15 LYS 238 -0.29 GLY 157
PHE 231 0.13 PHE 239 -0.23 GLY 157
GLY 118 0.14 GLN 240 -0.19 GLY 157
GLY 118 0.12 ASP 241 -0.26 GLY 157
PRO 197 0.15 ALA 242 -0.30 GLY 157
GLN 140 0.14 TYR 243 -0.22 GLY 157
GLY 118 0.15 ASN 244 -0.21 GLY 157
ALA 201 0.14 ALA 245 -0.27 GLY 157
ALA 201 0.20 ALA 246 -0.25 GLY 157
GLN 140 0.18 GLY 247 -0.21 GLY 157
GLY 118 0.19 GLY 248 -0.17 GLY 157
GLY 118 0.19 HIS 249 -0.14 GLN 194
GLY 118 0.23 ASN 250 -0.14 ILE 196
GLY 118 0.18 ALA 251 -0.14 ILE 196
SER 280 0.16 VAL 252 -0.13 ALA 272
SER 280 0.14 PHE 253 -0.11 ALA 268
ASP 276 0.13 ASN 254 -0.12 ARG 2
ASP 276 0.13 PHE 255 -0.12 GLN 44
ASP 276 0.14 PRO 256 -0.14 ARG 2
ASP 276 0.14 PRO 257 -0.14 ARG 2
LEU 165 0.21 ASN 258 -0.19 ARG 2
LEU 165 0.30 GLY 259 -0.21 ARG 2
LEU 162 0.41 THR 260 -0.30 ILE 52
LEU 162 0.51 HIS 261 -0.35 GLY 49
ALA 166 0.61 SER 262 -0.54 TRP 263
ALA 166 0.53 TRP 263 -0.54 SER 262
ALA 166 0.49 GLU 264 -0.41 PRO 55
ALA 166 0.39 TYR 265 -0.26 PRO 55
ALA 166 0.39 TRP 266 -0.21 ALA 56
ALA 166 0.37 GLY 267 -0.25 ALA 56
ALA 166 0.32 ALA 268 -0.19 ARG 2
ALA 166 0.27 GLN 269 -0.14 ALA 268
ALA 166 0.27 LEU 270 -0.16 PRO 224
ALA 166 0.27 ASN 271 -0.19 LEU 218
ALA 166 0.23 ALA 272 -0.14 LEU 218
ALA 166 0.20 MET 273 -0.12 ASN 250
ALA 166 0.19 LYS 274 -0.13 LEU 218
ALA 166 0.17 GLY 275 -0.11 ASN 202
ALA 166 0.14 ASP 276 -0.14 THR 204
ALA 166 0.14 LEU 277 -0.12 PRO 139
ARG 42 0.13 GLN 278 -0.13 PRO 139
PRO 257 0.14 SER 279 -0.14 ASN 202
VAL 252 0.16 SER 280 -0.17 PRO 139
ASN 250 0.14 LEU 281 -0.16 PRO 139
VAL 252 0.13 GLY 282 -0.16 GLN 140
ALA 89 0.11 ALA 283 -0.14 GLN 140
ARG 42 0.12 GLY 284 -0.13 GLN 140

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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.