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 14  ---

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
GLN 24 0.20 SER 1 -0.38 ASN 222
TYR 9 0.43 ARG 2 -0.43 LEU 218
TYR 9 1.12 PRO 3 -0.40 GLU 217
GLU 8 0.66 GLY 4 -0.36 GLU 217
ARG 112 0.19 LEU 5 -0.34 ILE 223
PRO 3 0.32 PRO 6 -0.34 PRO 224
PRO 3 0.78 VAL 7 -0.34 PRO 224
PRO 3 0.99 GLU 8 -0.33 PRO 224
PRO 3 1.12 TYR 9 -0.32 PRO 224
PRO 3 0.87 LEU 10 -0.31 PRO 224
PRO 3 0.76 GLN 11 -0.27 PRO 224
PRO 3 0.65 VAL 12 -0.28 PRO 224
PRO 3 0.58 PRO 13 -0.24 PRO 224
PRO 3 0.52 SER 14 -0.26 ALA 186
PRO 3 0.46 PRO 15 -0.25 PRO 185
PRO 3 0.42 SER 16 -0.28 ASP 184
PRO 3 0.43 MET 17 -0.24 PRO 224
PRO 3 0.44 GLY 18 -0.20 PRO 224
PRO 3 0.51 ARG 19 -0.20 PRO 224
PRO 3 0.60 ASP 20 -0.21 PRO 224
PRO 3 0.63 ILE 21 -0.29 PRO 224
PRO 3 0.76 LYS 22 -0.33 PRO 224
PRO 3 0.75 VAL 23 -0.37 PRO 224
PRO 3 0.83 GLN 24 -0.39 PRO 224
PRO 3 0.69 PHE 25 -0.37 PRO 224
PRO 3 0.49 GLN 26 -0.35 PRO 224
PRO 3 0.36 SER 27 -0.31 PRO 224
PRO 3 0.19 GLY 28 -0.31 ASN 250
PRO 6 0.25 GLY 29 -0.32 ASN 250
PRO 6 0.28 ASN 30 -0.38 ASN 250
PRO 3 0.26 ASN 31 -0.42 ASN 203
PRO 3 0.21 SER 32 -0.41 ASN 250
PRO 3 0.19 PRO 33 -0.39 ASN 250
PRO 3 0.27 ALA 34 -0.33 PRO 224
PRO 3 0.23 VAL 35 -0.37 PRO 224
PRO 3 0.32 TYR 36 -0.41 PRO 224
PRO 3 0.31 LEU 37 -0.47 PRO 224
PRO 3 0.34 LEU 38 -0.50 PRO 224
PRO 3 0.37 ASP 39 -0.62 PRO 224
PRO 3 0.30 GLY 40 -0.72 PRO 224
PRO 3 0.34 LEU 41 -0.69 PRO 224
PRO 3 0.39 ARG 42 -0.71 PRO 224
PRO 3 0.43 ALA 43 -0.61 PRO 224
PRO 3 0.51 GLN 44 -0.51 PRO 224
PRO 3 0.59 ASP 45 -0.47 ALA 89
PRO 3 0.70 ASP 46 -0.42 ALA 89
PRO 3 0.72 TYR 47 -0.43 PRO 224
PRO 3 0.56 ASN 48 -0.50 PRO 224
PRO 3 0.40 GLY 49 -0.61 PRO 224
PRO 3 0.29 TRP 50 -0.53 PRO 224
PRO 3 0.40 ASP 51 -0.46 PRO 224
PRO 3 0.36 ILE 52 -0.50 ILE 223
ASP 169 0.20 ASN 53 -0.55 ASN 222
ALA 166 0.19 THR 54 -0.47 ASN 222
ALA 166 0.14 PRO 55 -0.44 ASN 222
ALA 166 0.16 ALA 56 -0.42 PRO 224
PRO 3 0.21 PHE 57 -0.39 PRO 224
ALA 166 0.12 GLU 58 -0.51 TRP 59
ALA 166 0.17 TRP 59 -0.51 GLU 58
ALA 166 0.16 TYR 60 -0.32 PRO 224
ALA 166 0.13 TYR 61 -0.30 PRO 224
ALA 166 0.13 GLN 62 -0.29 GLY 4
ALA 166 0.15 SER 63 -0.29 ASN 250
ALA 166 0.12 GLY 64 -0.33 ASN 250
ALA 166 0.13 LEU 65 -0.33 ASN 250
PRO 3 0.28 SER 66 -0.33 PRO 224
PRO 3 0.34 ILE 67 -0.38 PRO 224
PRO 3 0.47 VAL 68 -0.39 PRO 224
PRO 3 0.53 MET 69 -0.44 PRO 224
PRO 3 0.57 PRO 70 -0.42 PRO 224
PRO 3 0.62 VAL 71 -0.43 PRO 224
PRO 3 0.53 GLY 72 -0.44 PRO 224
PRO 3 0.42 GLY 73 -0.46 PRO 224
PRO 3 0.39 GLN 74 -0.49 PRO 224
PRO 3 0.33 SER 75 -0.43 PRO 224
PRO 3 0.33 SER 76 -0.40 PRO 224
PRO 3 0.29 PHE 77 -0.42 PRO 224
PRO 3 0.33 TYR 78 -0.40 PRO 224
ILE 133 0.32 SER 79 -0.36 ALA 186
PRO 3 0.30 ASP 80 -0.34 ALA 186
GLN 195 0.41 TRP 81 -0.27 LYS 95
ARG 189 0.43 TYR 82 -0.26 SER 16
GLN 195 0.40 SER 83 -0.21 LEU 165
GLN 195 0.33 PRO 84 -0.20 PRO 224
GLN 195 0.33 ALA 85 -0.22 ASP 45
ALA 246 0.33 CYS 86 -0.25 ASP 45
SER 161 0.35 GLY 87 -0.24 ASP 45
SER 161 0.31 LYS 88 -0.32 ASP 45
SER 161 0.23 ALA 89 -0.47 ASP 45
SER 161 0.28 GLY 90 -0.44 ASP 45
ALA 246 0.28 CYS 91 -0.31 ASP 45
PRO 3 0.29 GLN 92 -0.27 ASP 45
PRO 3 0.32 THR 93 -0.24 PRO 224
PRO 3 0.33 TYR 94 -0.29 PRO 224
PRO 3 0.36 LYS 95 -0.29 PRO 224
PRO 3 0.38 TRP 96 -0.35 PRO 224
PRO 3 0.35 GLU 97 -0.42 ALA 186
PRO 3 0.37 THR 98 -0.40 ALA 186
PRO 3 0.44 PHE 99 -0.34 ALA 186
PRO 3 0.41 LEU 100 -0.36 PRO 224
PRO 3 0.36 THR 101 -0.35 ALA 186
PRO 3 0.40 SER 102 -0.36 ALA 186
PRO 3 0.47 GLU 103 -0.32 ALA 186
PRO 3 0.51 LEU 104 -0.32 PRO 224
PRO 3 0.44 PRO 105 -0.32 PRO 224
PRO 3 0.46 GLN 106 -0.30 HIS 138
PRO 3 0.52 TRP 107 -0.29 PRO 224
PRO 3 0.52 LEU 108 -0.31 PRO 224
PRO 3 0.44 SER 109 -0.35 ASN 203
PRO 3 0.47 ALA 110 -0.30 ASN 203
PRO 3 0.53 ASN 111 -0.28 ASN 203
PRO 3 0.51 ARG 112 -0.31 ASN 203
PRO 3 0.40 ALA 113 -0.34 ASN 203
PRO 3 0.37 VAL 114 -0.36 ASN 203
PRO 3 0.31 LYS 115 -0.39 ASN 203
PRO 3 0.34 PRO 116 -0.36 ASN 203
PRO 3 0.25 THR 117 -0.41 ASN 203
THR 101 0.18 GLY 118 -0.49 ASN 203
LEU 281 0.20 SER 119 -0.32 THR 204
ALA 166 0.17 ALA 120 -0.34 PRO 224
PRO 3 0.21 ALA 121 -0.37 PRO 224
ALA 166 0.25 ILE 122 -0.42 PRO 224
ALA 166 0.31 GLY 123 -0.46 PRO 224
ALA 166 0.40 LEU 124 -0.56 PRO 224
ALA 166 0.56 SER 125 -0.58 PRO 224
ALA 166 0.45 MET 126 -0.54 PRO 224
ALA 166 0.31 ALA 127 -0.49 PRO 224
ALA 166 0.37 GLY 128 -0.43 PRO 224
ALA 166 0.32 SER 129 -0.36 PRO 224
MET 132 0.25 SER 130 -0.37 PRO 224
ALA 166 0.23 ALA 131 -0.37 PRO 224
TRP 81 0.29 MET 132 -0.30 PRO 224
TRP 81 0.34 ILE 133 -0.29 PRO 224
SER 79 0.31 LEU 134 -0.31 PRO 224
SER 79 0.27 ALA 135 -0.29 PRO 224
TRP 81 0.33 ALA 136 -0.24 PRO 224
TRP 81 0.33 TYR 137 -0.24 PRO 224
TRP 81 0.24 HIS 138 -0.30 PRO 105
TRP 81 0.20 PRO 139 -0.31 LEU 199
ASP 80 0.20 GLN 140 -0.39 ASN 202
PRO 3 0.22 GLN 141 -0.34 PRO 116
SER 79 0.19 PHE 142 -0.30 PRO 224
SER 79 0.21 ILE 143 -0.41 GLY 118
ALA 166 0.22 TYR 144 -0.31 PRO 33
ALA 166 0.27 ALA 145 -0.30 PRO 224
ALA 166 0.30 GLY 146 -0.34 PRO 224
ALA 166 0.41 SER 147 -0.31 PRO 224
ALA 166 0.45 LEU 148 -0.37 PRO 224
ALA 166 0.59 SER 149 -0.30 PRO 224
ALA 166 0.62 ALA 150 -0.31 PRO 224
ALA 166 0.59 LEU 151 -0.22 PRO 224
ALA 166 0.44 LEU 152 -0.17 PRO 224
PHE 239 0.53 ASP 153 -0.22 ILE 133
LYS 174 0.50 PRO 154 -0.20 THR 101
ALA 242 0.53 SER 155 -0.27 ASN 190
ALA 242 0.61 GLN 156 -0.22 THR 101
ALA 245 0.52 GLY 157 -0.20 THR 101
ALA 245 0.42 MET 158 -0.21 LEU 41
ALA 242 0.46 GLY 159 -0.26 PHE 77
LYS 174 0.47 PRO 160 -0.22 GLU 97
LYS 174 0.47 SER 161 -0.14 GLU 97
SER 235 0.45 LEU 162 -0.24 LEU 41
LEU 151 0.57 ILE 163 -0.20 LEU 162
VAL 232 0.40 GLY 164 -0.33 ALA 175
LEU 228 0.68 LEU 165 -0.39 ALA 175
ALA 150 0.62 ALA 166 -0.18 ALA 175
ALA 150 0.47 MET 167 -0.16 ILE 223
VAL 232 0.42 GLY 168 -0.22 LYS 174
HIS 261 0.49 ASP 169 -0.17 LYS 174
PRO 3 0.35 ALA 170 -0.33 ILE 223
PRO 3 0.32 GLY 171 -0.31 ILE 223
GLY 164 0.39 GLY 172 -0.14 ILE 223
LEU 151 0.38 TYR 173 -0.15 PRO 84
ALA 175 0.60 LYS 174 -0.22 GLY 168
LYS 174 0.60 ALA 175 -0.39 LEU 165
ALA 245 0.44 ALA 176 -0.35 LEU 165
ALA 246 0.40 ASP 177 -0.28 LEU 165
ASP 191 0.43 MET 178 -0.25 LEU 165
ALA 246 0.44 TRP 179 -0.31 ASP 80
ALA 246 0.46 GLY 180 -0.32 LEU 165
ALA 245 0.47 PRO 181 -0.31 LEU 165
ALA 245 0.52 SER 182 -0.25 GLU 97
ALA 245 0.58 SER 183 -0.27 THR 98
ALA 246 0.54 ASP 184 -0.33 THR 98
ALA 246 0.59 PRO 185 -0.36 THR 98
ALA 246 0.49 ALA 186 -0.42 GLU 97
ALA 246 0.49 TRP 187 -0.30 GLU 97
ALA 246 0.60 GLU 188 -0.33 ARG 189
GLN 195 0.45 ARG 189 -0.33 GLU 188
MET 178 0.40 ASN 190 -0.27 SER 155
LYS 174 0.44 ASP 191 -0.26 ILE 133
LYS 174 0.37 PRO 192 -0.20 PRO 105
TYR 243 0.52 THR 193 -0.18 SER 109
ALA 246 0.57 GLN 194 -0.22 TYR 137
GLU 188 0.49 GLN 195 -0.23 ALA 136
GLU 188 0.43 ILE 196 -0.26 PRO 139
PRO 185 0.46 PRO 197 -0.30 ALA 242
TYR 82 0.39 LYS 198 -0.30 PRO 139
TYR 82 0.34 LEU 199 -0.34 GLY 118
GLU 188 0.37 VAL 200 -0.38 GLY 118
TYR 82 0.35 ALA 201 -0.31 GLY 118
TYR 82 0.30 ASN 202 -0.41 GLY 118
TYR 82 0.29 ASN 203 -0.49 GLY 118
TRP 81 0.26 THR 204 -0.46 GLY 118
ALA 166 0.27 ARG 205 -0.37 LEU 281
ALA 166 0.32 LEU 206 -0.28 SER 32
ALA 166 0.35 TRP 207 -0.24 SER 32
ALA 166 0.40 VAL 208 -0.21 TYR 209
ALA 166 0.44 TYR 209 -0.21 VAL 208
ALA 166 0.47 CYS 210 -0.17 GLU 58
LEU 165 0.43 GLY 211 -0.18 GLU 58
LEU 165 0.42 ASN 212 -0.18 ARG 2
LEU 165 0.44 GLY 213 -0.20 GLU 58
LEU 165 0.36 THR 214 -0.25 ARG 2
LEU 165 0.38 PRO 215 -0.31 ARG 2
LEU 165 0.34 ASN 216 -0.34 ARG 2
LEU 165 0.35 GLU 217 -0.41 ARG 2
LEU 165 0.36 LEU 218 -0.43 ARG 2
LEU 165 0.38 GLY 219 -0.38 ARG 2
LEU 165 0.44 GLY 220 -0.39 PRO 55
LEU 165 0.33 ALA 221 -0.42 ASN 53
LEU 165 0.31 ASN 222 -0.55 ASN 53
THR 214 0.26 ILE 223 -0.60 ARG 42
LEU 165 0.32 PRO 224 -0.72 GLY 40
LEU 165 0.50 ALA 225 -0.43 GLY 40
LEU 165 0.45 GLU 226 -0.26 PRO 55
LEU 165 0.49 PHE 227 -0.31 GLY 40
LEU 165 0.68 LEU 228 -0.37 SER 125
LEU 165 0.58 GLU 229 -0.20 ILE 122
LEU 165 0.51 ASN 230 -0.16 GLU 58
LEU 165 0.57 PHE 231 -0.15 GLY 128
LEU 165 0.60 VAL 232 -0.15 ILE 122
LEU 165 0.50 ARG 233 -0.16 SER 32
LEU 165 0.47 SER 234 -0.16 SER 32
LEU 165 0.49 SER 235 -0.17 ALA 135
ALA 166 0.45 ASN 236 -0.19 GLY 118
LEU 165 0.42 LEU 237 -0.20 GLY 118
GLN 156 0.51 LYS 238 -0.24 PHE 239
ASP 153 0.53 PHE 239 -0.24 LYS 238
ALA 166 0.37 GLN 240 -0.25 GLY 118
GLN 156 0.50 ASP 241 -0.27 GLY 118
GLN 156 0.61 ALA 242 -0.30 PRO 197
THR 193 0.52 TYR 243 -0.31 GLY 118
GLN 156 0.44 ASN 244 -0.31 ALA 245
GLN 156 0.59 ALA 245 -0.31 SER 280
GLU 188 0.60 ALA 246 -0.33 GLY 118
GLU 188 0.50 GLY 247 -0.36 ASN 31
GLU 188 0.46 GLY 248 -0.40 SER 280
GLU 188 0.40 HIS 249 -0.42 SER 280
GLU 188 0.32 ASN 250 -0.54 SER 280
ALA 166 0.34 ALA 251 -0.34 SER 280
ALA 166 0.34 VAL 252 -0.24 SER 32
ALA 166 0.37 PHE 253 -0.22 SER 32
ALA 166 0.38 ASN 254 -0.19 ARG 2
ALA 166 0.38 PHE 255 -0.17 ARG 2
LEU 165 0.35 PRO 256 -0.20 ARG 2
LEU 165 0.34 PRO 257 -0.20 ARG 2
LEU 165 0.37 ASN 258 -0.23 ARG 2
LEU 165 0.42 GLY 259 -0.23 ARG 2
LEU 165 0.48 THR 260 -0.24 PRO 55
ALA 166 0.58 HIS 261 -0.39 PRO 224
ALA 166 0.48 SER 262 -0.46 PRO 224
ALA 166 0.38 TRP 263 -0.53 PRO 224
ALA 166 0.36 GLU 264 -0.38 PRO 55
ALA 166 0.38 TYR 265 -0.29 GLU 58
ALA 166 0.39 TRP 266 -0.37 PRO 224
ALA 166 0.30 GLY 267 -0.38 PRO 224
ALA 166 0.30 ALA 268 -0.38 LEU 218
ALA 166 0.34 GLN 269 -0.29 PRO 224
ALA 166 0.30 LEU 270 -0.34 PRO 224
ALA 166 0.27 ASN 271 -0.40 LEU 218
ALA 166 0.29 ALA 272 -0.37 LEU 218
ALA 166 0.28 MET 273 -0.30 LEU 218
ALA 166 0.25 LYS 274 -0.31 LEU 218
ALA 166 0.24 GLY 275 -0.29 GLY 4
ALA 166 0.26 ASP 276 -0.31 ASN 250
ALA 166 0.23 LEU 277 -0.37 ASN 250
ALA 166 0.21 GLN 278 -0.37 ASN 250
ALA 166 0.22 SER 279 -0.43 ASN 250
ALA 166 0.22 SER 280 -0.54 ASN 250
SER 119 0.20 LEU 281 -0.49 ASN 250
ALA 166 0.17 GLY 282 -0.45 ASN 250
ALA 166 0.17 ALA 283 -0.36 ASN 250
ALA 166 0.15 GLY 284 -0.31 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.