Should you encounter any unexpected behaviour,
please let us know.

* EXP_3CYE_unrelaxed_rank_001_alphafold2_ptm_model_5_seed_000 *

CA distance fluctuations for 24021912342430053

--- normal mode 16 ---

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 increase ref largest decrease
ASP 272 0.23 VAL 1 -0.28 GLY 27

ASP 272 0.26 ILE 2 -0.27 GLY 27

ASP 272 0.29 LEU 3 -0.27 GLY 30

ASP 272 0.32 THR 4 -0.25 GLY 27

ASP 272 0.35 GLY 5 -0.25 GLY 30

ASP 272 0.40 ASN 6 -0.22 GLY 30

ASP 272 0.42 SER 7 -0.21 GLY 27

ASP 272 0.52 SER 8 -0.18 GLY 27

TYR 271 0.31 LEU 9 -0.16 GLY 27

PRO 295 0.29 CYS 10 -0.18 VAL 366

PRO 295 0.29 PRO 11 -0.13 GLY 27

SER 13 0.40 ILE 12 -0.13 ILE 24

PRO 295 0.50 SER 13 -0.21 VAL 371

SER 306 0.40 GLY 14 -0.18 GLY 372

SER 306 0.25 TRP 15 -0.17 ILE 24

TYR 88 0.24 ALA 16 -0.47 THR 370

TYR 88 0.28 ILE 17 -0.45 ASP 369

TYR 88 0.29 TYR 18 -0.45 ASP 369

TYR 88 0.33 SER 19 -0.39 ASP 369

TYR 88 0.34 LYS 20 -0.36 ASP 369

TYR 88 0.35 ASP 21 -0.34 GLY 82

TYR 88 0.33 ASN 22 -0.32 ASP 369

TYR 88 0.39 GLY 23 -0.43 ASP 369

TYR 88 0.33 ILE 24 -0.42 ASP 369

TYR 88 0.49 ARG 25 -0.45 PRO 382

ASP 31 0.53 ILE 26 -0.40 ASP 369

LYS 350 0.31 GLY 27 -0.50 GLU 83

LYS 350 0.39 SER 28 -0.39 ALA 84

GLU 351 0.43 LYS 29 -0.41 GLU 83

ILE 26 0.23 GLY 30 -0.70 ALA 84

ILE 26 0.53 ASP 31 -0.32 GLN 54

ILE 26 0.32 VAL 32 -0.52 GLY 30

HIS 62 0.15 PHE 33 -0.36 GLY 30

HIS 62 0.16 VAL 34 -0.36 ASP 69

SER 63 0.20 ILE 35 -0.32 GLY 30

SER 63 0.20 ARG 36 -0.32 SER 98

VAL 67 0.23 GLU 37 -0.28 ARG 143

PHE 51 0.19 PRO 38 -0.30 GLY 30

GLY 322 0.20 PHE 39 -0.32 GLY 30

PHE 340 0.21 ILE 40 -0.31 GLY 30

PHE 324 0.20 SER 41 -0.31 GLY 30

PRO 295 0.20 CYS 42 -0.31 GLY 30

ASP 272 0.22 SER 43 -0.31 GLY 30

ASP 272 0.23 HIS 44 -0.31 GLY 27

ASP 272 0.20 LEU 45 -0.34 GLY 27

PRO 295 0.21 GLU 46 -0.37 GLY 27

PRO 338 0.23 CYS 47 -0.35 GLY 30

CYS 339 0.20 ARG 48 -0.39 GLY 30

PHE 340 0.23 THR 49 -0.41 GLY 30

PHE 340 0.19 PHE 50 -0.37 GLY 30

SER 321 0.19 PHE 51 -0.35 GLY 30

SER 63 0.25 LEU 52 -0.34 TRP 97

SER 63 0.30 THR 53 -0.42 PRO 87

SER 63 0.50 GLN 54 -0.54 PRO 87

HIS 62 0.33 GLY 55 -0.53 GLN 54

HIS 62 0.31 ALA 56 -0.46 ASP 69

ILE 26 0.18 LEU 57 -0.40 ASP 69

ASN 352 0.18 LEU 58 -0.30 ASP 69

ASN 352 0.27 ASN 59 -0.25 SER 28

PRO 87 0.14 ASP 60 -0.24 ASP 69

GLN 54 0.26 LYS 61 -0.30 PRO 382

GLN 54 0.45 HIS 62 -0.26 VAL 67

GLN 54 0.50 SER 63 -0.25 VAL 67

GLN 54 0.33 ASN 64 -0.32 GLY 65

TYR 73 0.19 GLY 65 -0.32 ASN 64

ILE 264 0.33 THR 66 -0.42 ASP 117

ASN 262 0.42 VAL 67 -0.36 ALA 56

LYS 265 0.32 LYS 68 -0.44 ALA 56

GLU 196 0.34 ASP 69 -0.46 ALA 56

GLU 196 0.26 ARG 70 -0.37 PRO 87

GLU 196 0.23 SER 71 -0.39 PRO 87

SER 63 0.31 PRO 72 -0.41 PRO 87

SER 63 0.46 TYR 73 -0.52 PRO 87

SER 63 0.36 ARG 74 -0.51 PRO 87

SER 63 0.33 THR 75 -0.51 PRO 87

SER 63 0.25 LEU 76 -0.43 PRO 87

HIS 62 0.26 MET 77 -0.34 PRO 87

HIS 62 0.19 SER 78 -0.38 GLY 30

PHE 340 0.20 CYS 79 -0.44 GLY 30

VAL 81 0.24 PRO 80 -0.44 GLY 30

TYR 88 0.28 VAL 81 -0.39 GLY 30

TYR 88 0.34 GLY 82 -0.44 GLY 27

TYR 88 0.38 GLU 83 -0.56 GLY 30

TYR 88 0.34 ALA 84 -0.70 GLY 30

ILE 361 0.23 PRO 85 -0.60 GLY 30

ARG 25 0.29 SER 86 -0.44 GLY 30

ARG 25 0.36 PRO 87 -0.54 GLN 54

ARG 25 0.49 TYR 88 -0.43 PHE 92

ARG 25 0.24 ASN 89 -0.42 GLY 30

HIS 62 0.21 SER 90 -0.35 GLY 30

HIS 62 0.25 ARG 91 -0.38 TYR 88

HIS 62 0.29 PHE 92 -0.44 PRO 87

HIS 62 0.23 GLU 93 -0.37 PRO 87

SER 63 0.24 SER 94 -0.40 PRO 87

SER 63 0.27 VAL 95 -0.44 PRO 87

ALA 99 0.22 ALA 96 -0.41 PRO 87

SER 71 0.19 TRP 97 -0.41 PRO 87

GLU 146 0.29 SER 98 -0.33 PRO 87

ALA 96 0.22 ALA 99 -0.30 GLY 30

CYS 199 0.19 SER 100 -0.30 GLY 30

ASP 272 0.19 ALA 101 -0.31 GLY 30

ASP 272 0.24 CYS 102 -0.31 GLY 30

ASP 272 0.25 HIS 103 -0.31 GLY 30

ASP 272 0.27 ASP 104 -0.28 GLY 30

ASP 272 0.26 GLY 105 -0.29 GLY 30

ASP 272 0.23 MET 106 -0.28 GLY 30

ASP 272 0.23 GLY 107 -0.28 GLY 30

ASP 272 0.21 TRP 108 -0.31 GLY 30

ASP 272 0.22 LEU 109 -0.30 GLY 30

ASP 272 0.20 THR 110 -0.31 GLY 30

TYR 200 0.20 ILE 111 -0.31 PRO 87

ASP 272 0.17 GLY 112 -0.35 PRO 87

CYS 199 0.19 ILE 113 -0.35 PRO 87

GLY 115 0.16 SER 114 -0.37 PRO 87

VAL 123 0.18 GLY 115 -0.33 PRO 87

VAL 123 0.15 PRO 116 -0.37 THR 66

VAL 121 0.16 ASP 117 -0.42 THR 66

VAL 181 0.20 ASN 118 -0.35 ILE 354

VAL 181 0.23 GLY 119 -0.30 THR 66

VAL 121 0.28 ALA 120 -0.33 PRO 87

ALA 120 0.28 VAL 121 -0.33 PRO 87

TYR 200 0.19 ALA 122 -0.33 PRO 87

GLY 115 0.18 VAL 123 -0.33 PRO 87

ASP 272 0.19 LEU 124 -0.30 PRO 87

ASP 272 0.19 LYS 125 -0.29 PRO 87

ASP 272 0.20 TYR 126 -0.28 GLY 30

ASP 272 0.20 ASN 127 -0.27 GLY 30

ASP 272 0.19 GLY 128 -0.28 TYR 88

ASP 272 0.18 ILE 129 -0.27 TYR 88

ASP 272 0.18 ILE 130 -0.28 TYR 88

ASP 272 0.18 THR 131 -0.25 PRO 87

GLY 119 0.19 ASP 132 -0.27 PRO 87

LYS 180 0.20 THR 133 -0.29 PRO 87

LYS 135 0.38 ILE 134 -0.28 PRO 87

ILE 134 0.38 LYS 135 -0.30 PRO 87

VAL 181 0.25 SER 136 -0.30 PRO 87

SER 184 0.29 TRP 137 -0.29 PRO 87

SER 184 0.20 ARG 138 -0.29 ILE 354

SER 184 0.22 ASN 139 -0.31 ILE 354

SER 184 0.18 ASN 140 -0.36 ILE 354

LYS 175 0.13 ILE 141 -0.39 ILE 354

MET 160 0.16 LEU 142 -0.33 TRP 355

VAL 67 0.16 ARG 143 -0.32 TRP 355

CYS 208 0.20 THR 144 -0.29 GLY 30

VAL 67 0.26 GLN 145 -0.25 GLY 30

SER 98 0.29 GLU 146 -0.29 GLY 30

VAL 67 0.23 SER 147 -0.27 GLY 30

PHE 269 0.19 GLU 148 -0.28 GLY 30

ASP 272 0.21 CYS 149 -0.28 GLY 30

ASP 272 0.26 ALA 150 -0.27 GLY 30

ASP 272 0.29 CYS 151 -0.28 GLY 30

ASP 272 0.31 VAL 152 -0.25 GLY 30

ASP 272 0.29 ASN 153 -0.25 GLY 30

ASP 272 0.26 GLY 154 -0.26 GLY 30

ASP 272 0.26 SER 155 -0.26 GLY 30

ASP 272 0.26 CYS 156 -0.28 GLY 30

ASP 272 0.25 PHE 157 -0.28 GLY 30

LYS 135 0.22 THR 158 -0.28 GLY 30

CYS 208 0.25 ILE 159 -0.26 GLY 30

CYS 208 0.16 MET 160 -0.27 GLY 30

VAL 222 0.16 THR 161 -0.29 TRP 355

ILE 173 0.14 ASP 162 -0.31 TRP 355

VAL 67 0.11 GLY 163 -0.32 TRP 355

VAL 67 0.21 PRO 164 -0.35 GLN 348

VAL 67 0.36 SER 165 -0.36 GLN 348

VAL 67 0.37 ASN 166 -0.33 PRO 349

VAL 67 0.29 GLY 167 -0.28 PRO 349

VAL 67 0.21 GLN 168 -0.26 PRO 349

VAL 67 0.17 ALA 169 -0.28 PRO 349

VAL 222 0.11 SER 170 -0.25 PRO 349

VAL 222 0.18 TYR 171 -0.24 GLY 30

ILE 173 0.23 LYS 172 -0.26 GLY 30

LYS 172 0.23 ILE 173 -0.26 GLY 30

LYS 135 0.27 LEU 174 -0.27 GLY 30

LYS 135 0.30 LYS 175 -0.26 GLY 30

LYS 135 0.30 ILE 176 -0.28 GLY 30

LYS 135 0.26 GLU 177 -0.26 GLY 30

ASP 272 0.23 LYS 178 -0.27 GLY 30

LYS 135 0.22 GLY 179 -0.27 GLY 30

LYS 135 0.29 LYS 180 -0.25 GLY 30

LYS 135 0.36 VAL 181 -0.26 GLY 30

LYS 135 0.30 THR 182 -0.25 GLY 30

TRP 137 0.26 LYS 183 -0.25 GLY 30

TRP 137 0.29 SER 184 -0.25 GLY 30

TRP 137 0.19 ILE 185 -0.25 GLY 30

ASP 272 0.15 GLU 186 -0.24 GLY 30

THR 299 0.15 LEU 187 -0.23 GLY 30

THR 299 0.14 ASN 188 -0.20 PRO 349

VAL 67 0.17 ALA 189 -0.21 PRO 349

VAL 67 0.17 PRO 190 -0.20 PRO 349

VAL 67 0.22 ASN 191 -0.21 PRO 349

VAL 67 0.24 TYR 192 -0.22 PRO 349

VAL 67 0.29 HIS 193 -0.25 PRO 349

VAL 67 0.28 TYR 194 -0.25 PRO 349

VAL 67 0.35 GLU 195 -0.25 PRO 349

VAL 67 0.36 GLU 196 -0.22 PRO 349

VAL 67 0.30 CYS 197 -0.21 GLY 30

VAL 67 0.27 SER 198 -0.21 GLY 30

VAL 67 0.23 CYS 199 -0.21 GLY 30

ALA 150 0.23 TYR 200 -0.21 GLY 30

ASP 272 0.33 PRO 201 -0.21 GLY 30

ASP 272 0.46 ASP 202 -0.19 GLY 30

ASP 272 0.55 THR 203 -0.19 GLY 30

ASP 272 0.41 GLY 204 -0.21 GLY 30

ASP 272 0.40 LYS 205 -0.21 GLY 30

ASP 272 0.33 VAL 206 -0.22 GLY 30

ILE 159 0.23 MET 207 -0.18 GLY 30

ILE 159 0.25 CYS 208 -0.19 GLY 30

VAL 67 0.27 VAL 209 -0.20 PRO 349

VAL 67 0.31 CYS 210 -0.22 PRO 349

VAL 67 0.36 ARG 211 -0.25 PRO 349

VAL 67 0.35 ASP 212 -0.26 PRO 349

VAL 67 0.41 ASN 213 -0.31 PRO 349

VAL 67 0.34 TRP 214 -0.28 PRO 349

VAL 67 0.30 HIS 215 -0.26 PRO 349

VAL 67 0.31 GLY 216 -0.28 PRO 349

ASP 369 0.29 SER 217 -0.29 PRO 349

ASP 369 0.31 ASN 218 -0.25 PRO 349

VAL 67 0.29 ARG 219 -0.23 PRO 349

VAL 67 0.28 PRO 220 -0.21 PRO 349

VAL 67 0.25 TRP 221 -0.20 PRO 349

VAL 67 0.22 VAL 222 -0.19 PRO 349

THR 299 0.28 SER 223 -0.19 GLY 30

ASP 272 0.26 PHE 224 -0.21 GLY 30

ASP 272 0.30 ASP 225 -0.22 GLY 30

ASP 272 0.27 GLN 226 -0.24 GLY 30

ASP 272 0.24 ASN 227 -0.24 GLY 30

ASP 272 0.22 LEU 228 -0.24 GLY 30

THR 299 0.23 ASP 229 -0.22 GLY 30

THR 299 0.25 TYR 230 -0.21 GLY 30

THR 299 0.27 GLN 231 -0.18 GLY 30

THR 299 0.20 ILE 232 -0.18 PRO 349

ASP 369 0.26 GLY 233 -0.18 PRO 349

ASP 369 0.30 TYR 234 -0.20 PRO 349

ASP 369 0.37 ILE 235 -0.21 PRO 349

ASP 369 0.45 CYS 236 -0.22 PRO 349

ASP 369 0.54 SER 237 -0.23 PRO 349

ASP 369 0.57 GLY 238 -0.25 PRO 349

ASP 369 0.56 VAL 239 -0.25 PRO 349

ASP 369 0.42 PHE 240 -0.27 PRO 349

ASP 369 0.32 GLY 241 -0.24 PRO 349

VAL 67 0.32 ASP 242 -0.29 PRO 349

VAL 67 0.32 ASN 243 -0.34 PRO 349

VAL 67 0.29 PRO 244 -0.39 PRO 349

ASP 369 0.31 ARG 245 -0.35 PRO 349

ASP 369 0.38 PRO 246 -0.32 PRO 349

ASP 369 0.48 ASN 247 -0.31 PRO 349

ASP 369 0.56 ASP 248 -0.28 PRO 349

ASP 369 0.60 GLY 249 -0.26 PRO 349

ASP 369 0.57 THR 250 -0.25 PRO 349

ASP 369 0.51 GLY 251 -0.24 PRO 349

ASP 369 0.43 SER 252 -0.22 PRO 349

ASP 369 0.38 CYS 253 -0.20 PRO 349

ASP 369 0.33 GLY 254 -0.21 PRO 349

ASP 369 0.30 PRO 255 -0.23 PRO 349

ASP 369 0.33 VAL 256 -0.25 PRO 349

ASP 369 0.29 SER 257 -0.26 PRO 349

ASP 369 0.32 SER 258 -0.29 PRO 349

ASP 369 0.27 ASN 259 -0.34 PRO 349

VAL 67 0.30 GLY 260 -0.33 PRO 349

VAL 67 0.33 ALA 261 -0.37 PRO 349

VAL 67 0.42 ASN 262 -0.40 PRO 349

VAL 67 0.41 GLY 263 -0.32 PRO 349

VAL 67 0.42 ILE 264 -0.29 PRO 349

VAL 67 0.39 LYS 265 -0.24 PRO 349

VAL 67 0.33 GLY 266 -0.21 PRO 349

VAL 67 0.29 PHE 267 -0.18 PRO 349

VAL 67 0.26 SER 268 -0.18 PRO 349

SER 13 0.23 PHE 269 -0.16 PRO 349

ASP 369 0.29 ARG 270 -0.16 PRO 349

SER 8 0.43 TYR 271 -0.15 PRO 349

THR 203 0.55 ASP 272 -0.16 PRO 349

ASP 369 0.47 ASN 273 -0.17 PRO 349

ASP 369 0.53 GLY 274 -0.18 PRO 349

ASP 369 0.45 VAL 275 -0.18 PRO 349

ASP 369 0.40 TRP 276 -0.17 PRO 349

ASP 369 0.37 ILE 277 -0.19 PRO 349

VAL 67 0.25 GLY 278 -0.19 PRO 349

VAL 67 0.28 ARG 279 -0.22 PRO 349

VAL 67 0.25 THR 280 -0.27 PRO 349

ASP 369 0.24 LYS 281 -0.26 PRO 349

VAL 67 0.22 SER 282 -0.34 PRO 349

ASP 369 0.27 THR 283 -0.37 PRO 349

VAL 67 0.23 SER 284 -0.48 PRO 349

VAL 67 0.24 SER 285 -0.49 PRO 349

VAL 67 0.27 ARG 286 -0.35 PRO 349

VAL 67 0.20 SER 287 -0.29 PRO 349

VAL 67 0.19 GLY 288 -0.21 PRO 349

VAL 67 0.21 PHE 289 -0.20 PRO 349

ASP 369 0.25 GLU 290 -0.18 PRO 349

ASP 369 0.35 MET 291 -0.17 PRO 349

ASP 369 0.58 ILE 292 -0.19 PRO 349

ASP 369 0.71 TRP 293 -0.19 PRO 349

ASP 369 0.72 ASP 294 -0.20 PRO 349

ASP 369 0.75 PRO 295 -0.18 PRO 349

ASP 369 0.65 ASN 296 -0.20 PRO 349

ASP 369 0.57 GLY 297 -0.21 PRO 349

ASP 369 0.45 TRP 298 -0.20 PRO 349

ASP 369 0.48 THR 299 -0.19 PRO 349

ASP 369 0.57 GLU 300 -0.21 PRO 349

ASP 369 0.57 THR 301 -0.22 PRO 349

ASP 369 0.67 ASP 302 -0.23 PRO 349

ASP 369 0.71 SER 303 -0.24 PRO 349

ASP 369 0.85 SER 304 -0.23 PRO 349

ASP 369 0.92 PHE 305 -0.21 PRO 349

ASP 369 1.18 SER 306 -0.18 PRO 349

ASP 369 1.04 VAL 307 -0.16 PRO 349

ASP 369 0.74 ARG 308 -0.18 PRO 349

ASP 369 0.40 GLN 309 -0.13 PRO 349

ASP 369 0.21 ASP 310 -0.15 PRO 349

TYR 88 0.23 ILE 311 -0.16 ILE 24

TYR 88 0.21 VAL 312 -0.18 ILE 24

TYR 88 0.18 ALA 313 -0.17 SER 384

VAL 67 0.15 ILE 314 -0.21 PRO 349

TYR 88 0.14 THR 315 -0.21 GLU 351

TYR 88 0.16 ASP 316 -0.21 SER 384

VAL 67 0.15 TRP 317 -0.21 ILE 141

VAL 67 0.22 SER 318 -0.21 GLY 319

VAL 67 0.31 GLY 319 -0.21 SER 318

VAL 67 0.32 TYR 320 -0.21 GLU 196

VAL 67 0.29 SER 321 -0.20 SER 318

VAL 67 0.27 GLY 322 -0.20 SER 198

VAL 67 0.23 SER 323 -0.20 GLY 30

SER 41 0.20 PHE 324 -0.22 GLY 30

PRO 295 0.23 VAL 325 -0.23 GLY 30

PRO 295 0.23 GLN 326 -0.26 GLY 27

ASP 272 0.28 HIS 327 -0.27 GLY 27

ASP 272 0.27 PRO 328 -0.29 ASP 369

ASP 272 0.25 GLU 329 -0.30 ASP 369

ASP 272 0.23 LEU 330 -0.36 ASP 369

PRO 295 0.22 THR 331 -0.46 ASP 369

ASP 272 0.22 GLY 332 -0.46 ASP 369

ASP 272 0.25 LEU 333 -0.40 SER 368

ASP 272 0.29 ASP 334 -0.32 SER 368

ASP 272 0.33 CYS 335 -0.24 SER 368

ASP 272 0.29 MET 336 -0.29 ARG 337

PRO 295 0.24 ARG 337 -0.29 MET 336

CYS 47 0.23 PRO 338 -0.17 GLY 27

PRO 80 0.22 CYS 339 -0.18 TYR 200

THR 49 0.23 PHE 340 -0.17 GLY 30

TYR 88 0.20 TRP 341 -0.19 GLY 30

VAL 67 0.20 VAL 342 -0.20 ASP 377

VAL 67 0.18 GLU 343 -0.23 GLU 146

TYR 88 0.17 LEU 344 -0.22 ILE 141

THR 66 0.15 ILE 345 -0.27 ILE 141

LYS 29 0.18 ARG 346 -0.27 ILE 141

LYS 29 0.27 GLY 347 -0.32 ILE 141

LYS 29 0.30 GLN 348 -0.37 ASN 262

LYS 29 0.35 PRO 349 -0.49 SER 285

LYS 29 0.41 LYS 350 -0.36 SER 285

PRO 382 0.48 GLU 351 -0.30 SER 285

PRO 382 0.46 ASN 352 -0.31 ASP 117

LYS 29 0.28 THR 353 -0.32 ASP 117

LYS 29 0.19 ILE 354 -0.39 ASP 117

LYS 29 0.16 TRP 355 -0.38 ILE 141

ASN 64 0.13 THR 356 -0.33 ILE 141

PRO 85 0.12 SER 357 -0.29 ILE 141

VAL 32 0.15 GLY 358 -0.25 ILE 141

TYR 88 0.21 SER 359 -0.26 GLY 30

TYR 88 0.23 SER 360 -0.25 PHE 39

TYR 88 0.28 ILE 361 -0.24 ASP 369

TYR 88 0.27 SER 362 -0.24 ASP 369

TYR 88 0.26 PHE 363 -0.26 THR 370

TYR 88 0.24 CYS 364 -0.23 ASP 369

TYR 88 0.23 GLY 365 -0.15 GLY 27

SER 306 0.29 VAL 366 -0.24 SER 368

SER 306 0.36 ASN 367 -0.17 GLY 27

SER 306 0.65 SER 368 -0.40 LEU 333

SER 306 1.18 ASP 369 -0.46 THR 331

VAL 307 0.67 THR 370 -0.47 ALA 16

SER 306 0.26 VAL 371 -0.21 SER 13

TYR 88 0.22 GLY 372 -0.19 SER 13

TYR 88 0.22 TRP 373 -0.21 ILE 24

TYR 88 0.21 SER 374 -0.24 ILE 24

TYR 88 0.25 TRP 375 -0.26 THR 370

TYR 88 0.22 PRO 376 -0.25 ILE 24

TYR 88 0.22 ASP 377 -0.24 ASP 369

TYR 88 0.25 GLY 378 -0.34 ILE 24

ASP 31 0.25 ALA 379 -0.43 ARG 25

LYS 350 0.31 GLU 380 -0.41 ARG 25

LYS 350 0.40 LEU 381 -0.44 ARG 25

GLU 351 0.48 PRO 382 -0.45 ARG 25

LYS 29 0.39 PHE 383 -0.37 GLU 380

LYS 29 0.32 SER 384 -0.32 GLU 380

GLN 54 0.26 ILE 385 -0.25 GLU 380

If you find results from this site helpful for your research, please cite one of our papers:

K. Suhre & Y.H. Sanejouand, ElNemo: a normal mode web-server for protein movement analysis and the generation of templates for molecular replacement. Nucleic Acids Research, 32, W610-W614, 2004.
K. Suhre & Y.H. Sanejouand, On the potential of normal mode analysis for solving difficult molecular replacement problems. Acta Cryst. D vol.60, p796-799, 2004 © International Union of Crystallography.

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.

Should you encounter any unexpected behaviour, please let us know.

*** EXP_3CYE_unrelaxed_rank_001_alphafold2_ptm_model_5_seed_000 ***

CA distance fluctuations for 24021912342430053

--- normal mode 16 ---

Should you encounter any unexpected behaviour,
please let us know.

* EXP_3CYE_unrelaxed_rank_001_alphafold2_ptm_model_5_seed_000 *