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***  1Z7H_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000  ***

CA distance fluctuations for 240220091409163486

---  normal mode 13  ---

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
PRO 143 0.50 PRO 1 -0.09 ASN 315
PRO 143 0.51 ILE 2 -0.12 ASN 315
PRO 143 0.61 THR 3 -0.14 ASN 315
PRO 143 0.62 ILE 4 -0.16 ASN 315
PRO 143 0.73 ASN 5 -0.19 ASN 315
PRO 143 0.78 ASN 6 -0.17 ASN 315
PRO 143 0.78 PHE 7 -0.21 ASN 315
PRO 143 0.78 ARG 8 -0.18 ASN 315
PRO 143 0.67 TYR 9 -0.17 ASN 179
PRO 143 0.76 SER 10 -0.19 ASN 179
PRO 143 0.92 ASP 11 -0.21 ASN 315
PRO 143 0.99 PRO 12 -0.24 ASP 178
PRO 143 0.73 VAL 13 -0.29 ASP 178
PRO 143 0.79 ASN 14 -0.30 PRO 314
ASP 142 0.43 ASN 15 -0.32 PRO 314
PRO 143 0.51 ASP 16 -0.36 ASN 315
PRO 143 0.60 THR 17 -0.32 ASN 315
PRO 143 0.62 ILE 18 -0.24 ASN 315
PRO 143 0.39 ILE 19 -0.28 ASP 178
PRO 143 0.23 MET 20 -0.33 ASP 178
PRO 143 0.16 MET 21 -0.34 ASN 179
ASP 40 0.08 GLU 22 -0.41 ASN 179
PRO 143 0.08 PRO 23 -0.36 ASN 179
LEU 153 0.08 PRO 24 -0.43 ARG 176
ASN 132 0.09 TYR 25 -0.43 ARG 176
LEU 153 0.07 CYS 26 -0.51 ASN 179
LEU 153 0.09 LYS 27 -0.60 ASN 179
ALA 151 0.16 GLY 28 -0.75 ASN 179
ALA 151 0.09 LEU 29 -0.62 ASN 179
ASP 80 0.08 ASP 30 -0.55 ASN 179
ASP 80 0.08 ILE 31 -0.44 ASN 179
ASP 80 0.10 TYR 32 -0.39 ASN 179
PRO 143 0.19 TYR 33 -0.30 ASN 179
PRO 143 0.37 LYS 34 -0.26 ASN 179
PRO 143 0.41 ALA 35 -0.24 ASN 179
PRO 143 0.53 PHE 36 -0.21 ASN 315
PRO 143 0.52 LYS 37 -0.21 ASN 315
PRO 143 0.55 ILE 38 -0.19 ASN 315
PRO 143 0.50 THR 39 -0.20 ASN 315
PRO 143 0.42 ASP 40 -0.20 ASN 315
PRO 143 0.32 ARG 41 -0.19 ASN 315
PRO 143 0.37 ILE 42 -0.16 ASN 315
PRO 143 0.38 TRP 43 -0.17 ASN 315
PRO 143 0.40 ILE 44 -0.16 ASN 179
PRO 143 0.35 VAL 45 -0.20 ASN 179
PRO 143 0.37 PRO 46 -0.17 ASN 179
PRO 143 0.26 GLU 47 -0.19 ASN 179
PRO 143 0.20 ARG 48 -0.18 PRO 61
PRO 143 0.15 TYR 49 -0.25 SER 63
TYR 264 0.08 GLU 50 -0.31 SER 62
THR 53 0.08 PHE 51 -0.27 SER 62
TYR 25 0.08 GLY 52 -0.29 THR 147
TYR 264 0.09 THR 53 -0.23 THR 147
TYR 264 0.11 LYS 54 -0.18 ASN 179
TYR 264 0.14 PRO 55 -0.14 ASN 179
TYR 264 0.16 GLU 56 -0.12 THR 147
TYR 264 0.16 ASP 57 -0.18 THR 147
TYR 264 0.18 PHE 58 -0.18 THR 147
TYR 264 0.21 ASN 59 -0.20 THR 147
TYR 264 0.22 PRO 60 -0.17 LEU 29
TYR 264 0.28 PRO 61 -0.30 GLU 50
TYR 264 0.21 SER 62 -0.35 LEU 29
HIS 262 0.23 SER 63 -0.32 LEU 29
ASP 73 0.16 LEU 64 -0.22 LEU 29
ASP 426 0.26 ILE 65 -0.24 LEU 29
ASP 426 0.37 GLU 66 -0.25 TYR 25
ASP 426 0.26 GLY 67 -0.20 LEU 29
ASP 426 0.17 ALA 68 -0.21 TYR 25
PRO 143 0.18 SER 69 -0.15 LEU 29
TYR 264 0.22 GLU 70 -0.16 LEU 29
PRO 143 0.20 TYR 71 -0.12 LEU 29
TYR 264 0.19 TYR 72 -0.12 LEU 29
PRO 143 0.21 ASP 73 -0.10 ARG 423
PRO 143 0.17 PRO 74 -0.10 ASN 179
PRO 143 0.24 ASN 75 -0.10 ASN 179
PRO 143 0.28 TYR 76 -0.11 ASN 179
PRO 143 0.32 LEU 77 -0.13 ASN 179
PRO 143 0.28 ARG 78 -0.13 ASN 179
PRO 143 0.36 THR 79 -0.14 ASN 179
PRO 143 0.46 ASP 80 -0.15 ASN 179
PRO 143 0.49 SER 81 -0.13 ASN 179
PRO 143 0.43 ASP 82 -0.12 ASN 179
PRO 143 0.46 LYS 83 -0.15 ASN 179
PRO 143 0.57 ASP 84 -0.14 ASN 179
PRO 143 0.55 ARG 85 -0.12 ASN 179
PRO 143 0.48 PHE 86 -0.12 ASN 179
PRO 143 0.55 LEU 87 -0.13 ASN 179
PRO 143 0.62 GLN 88 -0.13 ASN 315
PRO 143 0.53 THR 89 -0.11 ASN 315
PRO 143 0.50 MET 90 -0.11 ASN 315
PRO 143 0.60 VAL 91 -0.11 ASN 315
PRO 143 0.59 LYS 92 -0.10 ASN 315
PRO 143 0.50 LEU 93 -0.10 ASN 315
PRO 143 0.51 PHE 94 -0.11 ASN 315
PRO 143 0.57 ASN 95 -0.10 ASN 315
PRO 143 0.52 ARG 96 -0.09 ASN 315
PRO 143 0.46 ILE 97 -0.09 ASN 315
PRO 143 0.50 LYS 98 -0.10 ASN 315
PRO 143 0.51 ASN 99 -0.09 ASN 211
PRO 143 0.45 ASN 100 -0.10 THR 213
PRO 143 0.41 VAL 101 -0.10 ILE 212
PRO 143 0.37 ALA 102 -0.10 ILE 212
PRO 143 0.40 GLY 103 -0.08 ASN 211
PRO 143 0.42 GLU 104 -0.09 ASN 315
PRO 143 0.36 ALA 105 -0.08 ASN 315
PRO 143 0.34 LEU 106 -0.08 ASN 315
PRO 143 0.38 LEU 107 -0.10 ASN 315
PRO 143 0.36 ASP 108 -0.10 ASN 315
PRO 143 0.29 LYS 109 -0.09 ASN 315
PRO 143 0.29 ILE 110 -0.10 ASN 315
PRO 143 0.32 ILE 111 -0.13 ASN 315
PRO 143 0.26 ASN 112 -0.10 ASN 315
PRO 143 0.20 ALA 113 -0.11 GLU 66
PRO 143 0.15 ILE 114 -0.11 SER 63
PRO 143 0.08 PRO 115 -0.15 SER 150
SER 120 0.04 TYR 116 -0.20 SER 150
PHE 183 0.04 LEU 117 -0.27 SER 150
PHE 127 0.05 GLY 118 -0.32 SER 150
GLY 190 0.05 ASN 119 -0.30 LYS 149
TYR 121 0.17 SER 120 -0.31 THR 147
SER 120 0.17 TYR 121 -0.41 LYS 149
LYS 293 0.05 SER 122 -0.41 LYS 149
SER 310 0.05 LEU 123 -0.38 ALA 146
ALA 300 0.06 LEU 124 -0.31 SER 144
SER 310 0.05 ASP 125 -0.32 SER 144
LEU 123 0.05 LYS 126 -0.33 SER 144
GLY 118 0.05 PHE 127 -0.30 SER 150
VAL 174 0.05 ASP 128 -0.41 SER 150
GLY 28 0.06 THR 129 -0.44 SER 150
ILE 316 0.08 ASN 130 -0.59 SER 150
TYR 25 0.06 SER 131 -0.43 SER 150
TYR 25 0.09 ASN 132 -0.36 SER 150
THR 53 0.05 SER 133 -0.26 SER 150
TYR 25 0.05 VAL 134 -0.25 SER 150
GLY 28 0.10 SER 135 -0.30 SER 150
GLY 28 0.14 PHE 136 -0.36 ARG 176
GLY 28 0.13 ASN 137 -0.46 ASP 178
ASP 40 0.11 LEU 138 -0.40 ASP 178
LYS 149 0.22 LEU 139 -0.46 ASP 178
ILE 19 0.29 GLU 140 -0.44 ASP 178
PRO 12 0.53 GLN 141 -0.42 ASP 178
PRO 12 0.78 ASP 142 -0.49 ASP 178
PRO 12 0.99 PRO 143 -0.41 ASP 178
PRO 12 0.76 SER 144 -0.55 ASP 178
PRO 12 0.72 GLY 145 -0.53 ASP 178
PRO 12 0.54 ALA 146 -0.65 ASP 178
PRO 12 0.42 THR 147 -0.67 ASP 178
PRO 12 0.29 THR 148 -0.60 ASP 178
LEU 139 0.22 LYS 149 -0.63 ASP 178
THR 3 0.11 SER 150 -0.59 ASN 130
GLY 28 0.16 ALA 151 -0.43 SER 150
GLY 28 0.13 MET 152 -0.27 ASP 178
GLY 28 0.12 LEU 153 -0.18 ASP 178
PRO 143 0.18 THR 154 -0.15 ASP 178
PRO 143 0.21 ASN 155 -0.14 SER 63
PRO 143 0.25 LEU 156 -0.14 SER 63
PRO 143 0.26 ILE 157 -0.17 ARG 176
PRO 143 0.30 ILE 158 -0.15 SER 63
PRO 143 0.28 PHE 159 -0.16 SER 63
PRO 143 0.29 GLY 160 -0.13 ASN 179
PRO 143 0.23 PRO 161 -0.15 SER 63
PRO 143 0.15 GLY 162 -0.23 SER 63
TYR 264 0.19 PRO 163 -0.23 PRO 61
TYR 264 0.22 VAL 164 -0.15 LEU 29
PRO 143 0.23 LEU 165 -0.10 LEU 29
PRO 143 0.24 ASN 166 -0.11 LEU 29
PRO 143 0.20 LYS 167 -0.15 ALA 68
PRO 143 0.23 ASN 168 -0.14 SER 63
PRO 143 0.19 GLU 169 -0.20 SER 63
PRO 143 0.18 VAL 170 -0.20 SER 63
PRO 143 0.12 ARG 171 -0.23 SER 63
PRO 143 0.09 GLY 172 -0.21 SER 63
THR 53 0.06 ILE 173 -0.25 THR 147
ASP 57 0.06 VAL 174 -0.30 THR 147
SER 122 0.02 LEU 175 -0.42 THR 147
ASN 181 0.10 ARG 176 -0.58 GLY 28
LYS 293 0.14 VAL 177 -0.56 THR 147
ASP 289 0.22 ASP 178 -0.69 GLY 28
SER 248 0.21 ASN 179 -0.75 GLY 28
SER 248 0.26 LYS 180 -0.54 GLY 28
LYS 180 0.12 ASN 181 -0.39 THR 147
LYS 180 0.17 TYR 182 -0.35 THR 147
LYS 180 0.12 PHE 183 -0.26 THR 147
LYS 180 0.11 PRO 184 -0.24 THR 147
LYS 180 0.11 CYS 185 -0.18 THR 147
LYS 180 0.20 ARG 186 -0.19 GLU 66
LYS 180 0.19 ASP 187 -0.21 THR 147
LYS 180 0.13 GLY 188 -0.18 LYS 149
LYS 180 0.09 PHE 189 -0.20 SER 150
LYS 180 0.08 GLY 190 -0.16 SER 150
PRO 143 0.06 SER 191 -0.19 SER 150
PRO 143 0.11 ILE 192 -0.17 SER 63
PRO 143 0.16 MET 193 -0.18 SER 63
PRO 143 0.18 GLN 194 -0.20 SER 63
PRO 143 0.23 MET 195 -0.18 SER 63
PRO 143 0.23 ALA 196 -0.18 SER 63
PRO 143 0.29 PHE 197 -0.12 SER 63
PRO 143 0.32 CYS 198 -0.09 ARG 176
PRO 143 0.39 PRO 199 -0.09 ARG 176
PRO 143 0.38 GLU 200 -0.08 ASN 179
PRO 143 0.32 TYR 201 -0.08 ARG 176
PRO 143 0.32 VAL 202 -0.10 GLU 169
PRO 143 0.27 PRO 203 -0.12 GLU 169
PRO 143 0.28 THR 204 -0.10 GLU 169
PRO 143 0.27 PHE 205 -0.09 TYR 25
PRO 143 0.26 ASP 206 -0.08 TYR 25
PRO 143 0.27 ASN 207 -0.08 ASN 211
PRO 143 0.24 VAL 208 -0.10 GLU 409
PRO 143 0.24 ILE 209 -0.20 GLU 409
PRO 143 0.22 GLU 210 -0.27 LEU 215
PRO 143 0.20 ASN 211 -0.34 GLU 409
ILE 258 0.42 ILE 212 -0.26 GLU 409
ILE 258 0.28 THR 213 -0.28 SER 408
PRO 143 0.20 SER 214 -0.20 GLU 409
PRO 143 0.21 LEU 215 -0.27 GLU 210
PRO 143 0.23 THR 216 -0.09 GLU 409
PRO 143 0.24 ILE 217 -0.08 GLU 409
PRO 143 0.26 GLY 218 -0.10 ASN 211
PRO 143 0.26 LYS 219 -0.08 TYR 259
PRO 143 0.29 SER 220 -0.11 ASN 211
PRO 143 0.29 LYS 221 -0.08 GLU 169
PRO 143 0.32 TYR 222 -0.09 ASN 211
PRO 143 0.33 PHE 223 -0.09 GLU 169
PRO 143 0.34 GLN 224 -0.10 GLU 169
PRO 143 0.38 ASP 225 -0.09 ASN 211
PRO 143 0.39 PRO 226 -0.08 ASN 315
PRO 143 0.41 ALA 227 -0.08 ASN 315
PRO 143 0.36 LEU 228 -0.08 ASN 211
PRO 143 0.33 LEU 229 -0.09 GLU 169
PRO 143 0.35 LEU 230 -0.09 LEU 175
PRO 143 0.34 MET 231 -0.08 ASN 315
PRO 143 0.29 HIS 232 -0.09 GLU 66
PRO 143 0.27 GLU 233 -0.11 GLU 66
PRO 143 0.29 LEU 234 -0.10 GLU 66
PRO 143 0.26 ILE 235 -0.11 GLU 66
PRO 143 0.21 HIS 236 -0.14 GLU 66
PRO 143 0.22 VAL 237 -0.13 GLU 66
PRO 143 0.22 LEU 238 -0.12 GLU 66
PRO 143 0.17 HIS 239 -0.14 GLU 66
PRO 143 0.13 GLY 240 -0.16 GLU 66
PRO 143 0.14 LEU 241 -0.14 GLU 66
PRO 143 0.12 TYR 242 -0.13 GLU 66
LYS 180 0.14 GLY 243 -0.16 GLU 66
LYS 180 0.16 MET 244 -0.16 GLU 66
LYS 180 0.16 GLN 245 -0.18 GLU 66
LYS 180 0.19 VAL 246 -0.19 GLU 66
LYS 180 0.20 SER 247 -0.23 GLU 66
LYS 180 0.26 SER 248 -0.23 GLU 66
LYS 180 0.22 HIS 249 -0.21 GLU 66
LYS 180 0.18 GLU 250 -0.20 GLU 66
PRO 61 0.16 ILE 251 -0.16 GLU 66
PRO 61 0.19 ILE 252 -0.13 GLU 66
ILE 212 0.20 PRO 253 -0.09 GLU 66
ILE 212 0.21 SER 254 -0.08 THR 147
ILE 212 0.27 LYS 255 -0.07 GLY 28
ILE 212 0.31 GLN 256 -0.07 GLY 28
ILE 212 0.38 GLU 257 -0.07 GLY 28
ILE 212 0.42 ILE 258 -0.08 GLU 409
ILE 212 0.32 TYR 259 -0.08 LYS 219
ILE 212 0.27 MET 260 -0.08 GLY 28
ILE 212 0.23 GLN 261 -0.09 GLY 28
SER 63 0.23 HIS 262 -0.09 GLY 28
PRO 61 0.24 THR 263 -0.11 GLU 66
PRO 61 0.28 TYR 264 -0.18 GLU 66
PRO 61 0.23 PRO 265 -0.20 GLU 66
PRO 61 0.17 ILE 266 -0.20 GLU 66
ASN 59 0.15 SER 267 -0.20 GLU 66
LYS 180 0.16 ALA 268 -0.17 GLU 66
PRO 143 0.15 GLU 269 -0.17 GLU 66
PRO 143 0.18 GLU 270 -0.16 GLU 66
PRO 143 0.18 LEU 271 -0.13 GLU 66
PRO 143 0.18 PHE 272 -0.12 GLU 66
PRO 143 0.22 THR 273 -0.11 GLU 66
PRO 143 0.23 PHE 274 -0.09 GLU 66
PRO 143 0.22 GLY 275 -0.08 GLU 66
PRO 143 0.23 GLY 276 -0.10 LEU 215
PRO 143 0.20 GLN 277 -0.10 LEU 215
PRO 143 0.19 ASP 278 -0.08 GLU 66
PRO 143 0.18 ALA 279 -0.09 GLU 66
PRO 143 0.16 ASN 280 -0.08 GLU 66
PRO 143 0.15 LEU 281 -0.09 GLU 66
LYS 180 0.16 ILE 282 -0.12 GLU 66
LYS 180 0.18 SER 283 -0.12 GLU 66
LYS 180 0.18 ILE 284 -0.11 GLU 66
LYS 180 0.21 ASP 285 -0.14 GLU 66
LYS 180 0.21 ILE 286 -0.15 GLU 66
LYS 180 0.18 LYS 287 -0.13 GLU 66
LYS 180 0.19 ASN 288 -0.13 GLU 66
LYS 180 0.22 ASP 289 -0.16 GLU 66
LYS 180 0.21 LEU 290 -0.16 GLU 66
LYS 180 0.18 TYR 291 -0.13 GLU 66
ASP 178 0.19 GLU 292 -0.15 GLU 66
LYS 180 0.22 LYS 293 -0.17 GLU 66
LYS 180 0.18 THR 294 -0.15 GLU 66
ASP 178 0.15 LEU 295 -0.14 LYS 149
ASP 178 0.19 ASN 296 -0.17 THR 147
ASP 178 0.17 ASP 297 -0.18 THR 147
LYS 180 0.12 TYR 298 -0.16 LYS 149
ASP 178 0.13 LYS 299 -0.16 LYS 149
ASP 178 0.14 ALA 300 -0.20 THR 147
LYS 180 0.09 ILE 301 -0.20 LYS 149
LYS 180 0.07 ALA 302 -0.16 LYS 149
ASP 178 0.08 ASN 303 -0.19 LYS 149
ASP 178 0.06 LYS 304 -0.23 LYS 149
LYS 180 0.04 LEU 305 -0.19 LYS 149
ALA 105 0.04 SER 306 -0.17 LYS 149
ALA 300 0.04 GLN 307 -0.24 SER 144
PRO 314 0.04 VAL 308 -0.24 SER 144
PRO 314 0.06 THR 309 -0.28 SER 144
PRO 314 0.06 SER 310 -0.33 SER 144
PRO 314 0.06 CYS 311 -0.33 SER 144
GLY 28 0.06 ASN 312 -0.45 SER 150
GLY 28 0.11 ASP 313 -0.37 SER 150
GLY 28 0.11 PRO 314 -0.36 ASP 142
GLY 28 0.13 ASN 315 -0.36 ASP 16
GLY 28 0.12 ILE 316 -0.22 ASP 16
GLY 28 0.09 ASP 317 -0.15 THR 17
GLY 28 0.06 ILE 318 -0.15 SER 144
GLY 28 0.06 ASP 319 -0.09 GLU 66
GLY 28 0.08 SER 320 -0.09 SER 63
GLY 28 0.06 TYR 321 -0.10 GLU 66
SER 120 0.04 LYS 322 -0.10 GLU 66
PRO 143 0.10 GLN 323 -0.09 GLU 66
PRO 143 0.14 ILE 324 -0.09 GLU 66
PRO 143 0.09 TYR 325 -0.10 GLU 66
PRO 143 0.10 GLN 326 -0.10 GLU 66
PRO 143 0.17 GLN 327 -0.08 GLU 66
PRO 143 0.16 LYS 328 -0.10 GLU 66
PRO 143 0.11 TYR 329 -0.11 GLU 66
PRO 143 0.13 GLN 330 -0.09 GLU 66
ALA 105 0.10 PHE 331 -0.10 GLU 66
ALA 105 0.10 ASP 332 -0.09 GLU 66
PRO 1 0.09 LYS 333 -0.09 GLU 66
VAL 101 0.09 ASP 334 -0.10 LYS 149
PRO 1 0.09 SER 335 -0.09 GLU 66
PRO 1 0.07 ASN 336 -0.12 SER 144
PRO 1 0.07 GLY 337 -0.10 LYS 149
VAL 101 0.06 GLN 338 -0.13 LYS 149
ALA 105 0.07 TYR 339 -0.13 LYS 149
ALA 105 0.08 ILE 340 -0.12 LYS 149
ASP 178 0.09 VAL 341 -0.11 LYS 149
ALA 105 0.10 ASN 342 -0.10 GLU 66
ASP 178 0.10 GLU 343 -0.10 GLU 66
PRO 143 0.12 ASP 344 -0.09 GLU 66
PRO 143 0.14 LYS 345 -0.08 GLU 66
PRO 143 0.12 PHE 346 -0.10 GLU 66
PRO 143 0.13 GLN 347 -0.09 GLU 66
PRO 143 0.17 ILE 348 -0.08 GLU 66
PRO 143 0.17 LEU 349 -0.09 GLU 66
PRO 143 0.15 TYR 350 -0.10 GLU 66
PRO 143 0.18 ASN 351 -0.09 GLU 66
PRO 143 0.21 SER 352 -0.08 GLU 66
PRO 143 0.20 ILE 353 -0.10 GLU 66
PRO 143 0.18 MET 354 -0.11 GLU 66
PRO 143 0.21 TYR 355 -0.09 GLU 66
PRO 143 0.24 GLY 356 -0.07 GLU 66
PRO 143 0.27 PHE 357 -0.07 GLU 66
PRO 143 0.26 THR 358 -0.08 GLU 66
PRO 143 0.28 GLU 359 -0.07 GLY 172
PRO 143 0.28 VAL 360 -0.09 LEU 215
PRO 143 0.29 GLU 361 -0.10 LEU 215
PRO 143 0.33 LEU 362 -0.09 ASN 211
PRO 143 0.34 GLY 363 -0.12 ASN 211
PRO 143 0.34 LYS 364 -0.15 ILE 212
PRO 143 0.36 LYS 365 -0.14 ILE 212
PRO 143 0.40 PHE 366 -0.14 ASN 211
PRO 143 0.39 ASN 367 -0.18 ASN 211
PRO 143 0.37 ILE 368 -0.15 ASN 211
PRO 143 0.33 LYS 369 -0.16 ASN 211
PRO 143 0.30 THR 370 -0.10 ASN 211
PRO 143 0.27 ARG 371 -0.07 TYR 25
PRO 143 0.24 LEU 372 -0.09 LEU 215
PRO 143 0.22 SER 373 -0.07 GLY 28
PRO 143 0.21 TYR 374 -0.09 GLU 66
PRO 143 0.20 PHE 375 -0.08 GLY 28
PRO 143 0.21 SER 376 -0.09 GLY 28
PRO 143 0.21 MET 377 -0.09 GLY 28
PRO 143 0.23 ASN 378 -0.10 TYR 25
PRO 143 0.23 HIS 379 -0.11 TYR 25
PRO 143 0.24 ASP 380 -0.11 LEU 29
PRO 143 0.27 PRO 381 -0.09 LEU 29
PRO 143 0.31 VAL 382 -0.08 ARG 176
PRO 143 0.35 LYS 383 -0.08 ARG 176
PRO 143 0.41 ILE 384 -0.08 ARG 176
PRO 143 0.44 PRO 385 -0.10 ASN 75
PRO 143 0.50 ASN 386 -0.09 ASN 75
PRO 143 0.51 LEU 387 -0.08 ASN 179
PRO 143 0.59 LEU 388 -0.08 ASN 315
PRO 143 0.58 ASP 389 -0.08 ASN 211
PRO 143 0.60 ASP 390 -0.11 ASN 211
PRO 143 0.55 THR 391 -0.12 ASN 211
PRO 143 0.51 ILE 392 -0.11 ASN 211
PRO 143 0.52 TYR 393 -0.11 ASN 211
PRO 143 0.56 ASN 394 -0.12 ASN 211
PRO 143 0.57 ASP 395 -0.11 ASN 211
PRO 143 0.53 THR 396 -0.13 ASN 211
PRO 143 0.49 GLU 397 -0.15 ASN 211
PRO 143 0.48 GLY 398 -0.13 ASN 211
PRO 143 0.45 PHE 399 -0.14 ASN 211
PRO 143 0.44 ASN 400 -0.19 ASN 211
PRO 143 0.49 ILE 401 -0.18 ASN 211
PRO 143 0.48 GLU 402 -0.21 ASN 211
PRO 143 0.50 SER 403 -0.19 THR 213
PRO 143 0.47 LYS 404 -0.19 ASN 211
PRO 143 0.44 ASP 405 -0.23 ASN 211
PRO 143 0.43 LEU 406 -0.22 ASN 211
PRO 143 0.42 LYS 407 -0.25 ASN 211
PRO 143 0.39 SER 408 -0.31 ASN 211
PRO 143 0.35 GLU 409 -0.34 ASN 211
PRO 143 0.37 TYR 410 -0.25 ASN 211
PRO 143 0.38 LYS 411 -0.23 ASN 211
PRO 143 0.41 GLY 412 -0.18 ASN 211
PRO 143 0.38 GLN 413 -0.15 ASN 211
PRO 143 0.35 ASN 414 -0.16 ASN 211
PRO 143 0.34 MET 415 -0.11 ASN 211
PRO 143 0.34 ARG 416 -0.13 ASN 211
PRO 143 0.37 VAL 417 -0.17 ASN 211
PRO 143 0.40 ASN 418 -0.14 ASN 211
PRO 143 0.38 THR 419 -0.10 ASN 211
PRO 143 0.42 ASN 420 -0.10 ASN 211
PRO 143 0.43 ALA 421 -0.10 ASN 211
PRO 143 0.39 PHE 422 -0.08 ASP 73
PRO 143 0.35 ARG 423 -0.10 ASP 73
PRO 143 0.31 ASN 424 -0.09 MET 415
PRO 143 0.29 VAL 425 -0.08 ASN 179
GLU 66 0.37 ASP 426 -0.09 ASN 179

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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.