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 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 increase ref largest decrease
ARG 25 0.44 VAL 1 -0.09 TYR 73

ARG 25 0.38 ILE 2 -0.08 ASP 272

ARG 25 0.36 LEU 3 -0.09 ASP 272

ARG 25 0.31 THR 4 -0.11 ASP 272

ARG 25 0.28 GLY 5 -0.10 ASP 272

ARG 25 0.24 ASN 6 -0.13 ASP 272

ARG 25 0.24 SER 7 -0.16 ASP 272

ARG 25 0.18 SER 8 -0.21 ASP 272

ARG 25 0.16 LEU 9 -0.14 TYR 271

ARG 25 0.16 CYS 10 -0.12 TYR 88

THR 203 0.10 PRO 11 -0.13 GLY 30

VAL 67 0.10 ILE 12 -0.15 GLY 30

VAL 67 0.11 SER 13 -0.17 GLY 30

VAL 67 0.10 GLY 14 -0.19 GLY 30

VAL 67 0.09 TRP 15 -0.20 GLY 30

THR 331 0.12 ALA 16 -0.24 GLY 30

THR 331 0.16 ILE 17 -0.25 GLY 30

ARG 25 0.30 TYR 18 -0.25 GLU 83

ARG 25 0.36 SER 19 -0.28 GLU 83

ARG 25 0.32 LYS 20 -0.30 GLY 30

GLY 23 0.47 ASP 21 -0.33 GLY 30

GLY 23 0.54 ASN 22 -0.37 GLY 30

GLU 83 0.72 GLY 23 -0.35 SER 374

GLU 83 0.45 ILE 24 -0.53 PRO 376

GLU 83 0.75 ARG 25 -0.51 THR 315

ASN 89 0.69 ILE 26 -0.30 GLY 27

ASN 89 0.40 GLY 27 -0.30 ILE 26

ASN 89 0.22 SER 28 -0.21 ARG 25

ARG 91 0.12 LYS 29 -0.22 ASN 22

TYR 88 0.23 GLY 30 -0.37 ASN 22

ILE 26 0.34 ASP 31 -0.29 ASP 21

ILE 26 0.42 VAL 32 -0.30 ASP 21

ILE 26 0.37 PHE 33 -0.16 LYS 20

ILE 26 0.23 VAL 34 -0.12 LYS 20

ILE 26 0.27 ILE 35 -0.08 ILE 361

ASN 262 0.25 ARG 36 -0.13 SER 98

ASN 262 0.19 GLU 37 -0.15 TRP 355

ILE 26 0.26 PRO 38 -0.09 ASP 117

ILE 26 0.24 PHE 39 -0.06 ASP 117

ARG 25 0.33 ILE 40 -0.08 SER 368

ARG 25 0.37 SER 41 -0.07 ASN 367

ARG 25 0.43 CYS 42 -0.09 ASN 89

ARG 25 0.47 SER 43 -0.10 GLU 93

ARG 25 0.49 HIS 44 -0.09 GLU 93

ARG 25 0.58 LEU 45 -0.12 TYR 88

ARG 25 0.60 GLU 46 -0.13 TYR 88

ARG 25 0.53 CYS 47 -0.14 ASN 367

ARG 25 0.52 ARG 48 -0.12 SER 368

ARG 25 0.44 THR 49 -0.12 SER 368

ILE 26 0.36 PHE 50 -0.09 SER 368

ILE 26 0.32 PHE 51 -0.08 SER 368

ILE 26 0.27 LEU 52 -0.11 ILE 354

ILE 26 0.27 THR 53 -0.10 ASN 64

ASN 262 0.30 GLN 54 -0.13 PHE 92

ILE 26 0.26 GLY 55 -0.14 SER 90

ASN 262 0.24 ALA 56 -0.12 LYS 20

ILE 26 0.19 LEU 57 -0.17 ASP 21

ASN 262 0.14 LEU 58 -0.16 ASP 21

ASN 262 0.12 ASN 59 -0.18 ASP 21

ASN 262 0.17 ASP 60 -0.15 ASP 21

ASN 262 0.20 LYS 61 -0.16 ARG 25

ASN 262 0.26 HIS 62 -0.11 ARG 25

ASN 262 0.31 SER 63 -0.13 ARG 25

ASN 262 0.34 ASN 64 -0.20 ASP 69

ASN 262 0.47 GLY 65 -0.23 ASN 352

ASN 262 0.59 THR 66 -0.27 PRO 116

ASN 262 0.61 VAL 67 -0.24 PRO 116

ASN 262 0.49 LYS 68 -0.15 ASN 352

ASN 262 0.48 ASP 69 -0.24 ILE 354

SER 165 0.38 ARG 70 -0.25 THR 66

SER 165 0.34 SER 71 -0.17 THR 66

SER 165 0.27 PRO 72 -0.21 ILE 130

ASN 262 0.29 TYR 73 -0.19 GLY 128

ASN 262 0.28 ARG 74 -0.21 THR 75

ILE 26 0.30 THR 75 -0.21 ARG 74

ILE 26 0.33 LEU 76 -0.10 ILE 354

ILE 26 0.40 MET 77 -0.11 GLY 55

ILE 26 0.46 SER 78 -0.12 SER 368

ARG 25 0.58 CYS 79 -0.16 SER 368

ARG 25 0.69 PRO 80 -0.20 SER 368

ARG 25 0.58 VAL 81 -0.19 PRO 85

ARG 25 0.65 GLY 82 -0.26 GLU 83

ARG 25 0.75 GLU 83 -0.28 SER 19

ILE 26 0.68 ALA 84 -0.24 LYS 20

ILE 26 0.63 PRO 85 -0.20 SER 19

ILE 26 0.63 SER 86 -0.19 SER 19

ILE 26 0.46 PRO 87 -0.17 ASP 369

ILE 26 0.55 TYR 88 -0.22 ASP 369

ILE 26 0.69 ASN 89 -0.20 SER 368

ILE 26 0.56 SER 90 -0.15 SER 368

ARG 25 0.51 ARG 91 -0.12 GLY 55

ILE 26 0.42 PHE 92 -0.15 TYR 73

ILE 26 0.38 GLU 93 -0.14 TYR 73

ILE 26 0.32 SER 94 -0.16 TYR 73

ILE 26 0.29 VAL 95 -0.18 GLY 128

ILE 26 0.24 ALA 96 -0.16 ILE 354

SER 165 0.26 TRP 97 -0.20 ILE 354

SER 165 0.20 SER 98 -0.20 TRP 355

ILE 26 0.23 ALA 99 -0.15 TRP 355

ILE 26 0.24 SER 100 -0.11 PRO 349

ARG 25 0.31 ALA 101 -0.09 VAL 95

ARG 25 0.34 CYS 102 -0.08 VAL 95

ARG 25 0.40 HIS 103 -0.10 VAL 95

ARG 25 0.37 ASP 104 -0.09 VAL 95

ARG 25 0.43 GLY 105 -0.09 VAL 95

ARG 25 0.44 MET 106 -0.11 PRO 72

ARG 25 0.44 GLY 107 -0.12 PRO 72

ARG 25 0.43 TRP 108 -0.13 VAL 95

ARG 25 0.36 LEU 109 -0.12 VAL 95

ARG 25 0.32 THR 110 -0.14 VAL 95

ILE 26 0.26 ILE 111 -0.12 PRO 349

ILE 26 0.25 GLY 112 -0.15 ILE 354

ILE 26 0.21 ILE 113 -0.18 PRO 349

ILE 26 0.20 SER 114 -0.20 ILE 354

ILE 26 0.18 GLY 115 -0.21 THR 66

PRO 72 0.16 PRO 116 -0.27 PRO 349

PRO 164 0.18 ASP 117 -0.32 PRO 349

PRO 87 0.11 ASN 118 -0.31 PRO 349

PRO 87 0.13 GLY 119 -0.26 PRO 349

ILE 26 0.15 ALA 120 -0.24 PRO 349

ILE 26 0.19 VAL 121 -0.20 PRO 349

ILE 26 0.21 ALA 122 -0.17 PRO 349

ILE 26 0.25 VAL 123 -0.18 PRO 72

ARG 25 0.28 LEU 124 -0.15 PRO 72

ARG 25 0.34 LYS 125 -0.18 PRO 72

ARG 25 0.38 TYR 126 -0.15 PRO 72

ARG 25 0.45 ASN 127 -0.15 PRO 72

ARG 25 0.43 GLY 128 -0.19 PRO 72

ARG 25 0.39 ILE 129 -0.20 PRO 72

ARG 25 0.32 ILE 130 -0.21 PRO 72

ARG 25 0.31 THR 131 -0.17 PRO 72

ARG 25 0.26 ASP 132 -0.15 PRO 72

ILE 26 0.22 THR 133 -0.15 PRO 349

ILE 26 0.19 ILE 134 -0.17 PRO 349

ILE 26 0.17 LYS 135 -0.20 PRO 349

ILE 26 0.13 SER 136 -0.23 PRO 349

ILE 26 0.12 TRP 137 -0.22 PRO 349

PRO 87 0.10 ARG 138 -0.25 PRO 349

PRO 87 0.11 ASN 139 -0.27 PRO 349

PRO 72 0.11 ASN 140 -0.31 PRO 349

PRO 72 0.16 ILE 141 -0.32 PRO 349

ILE 26 0.12 LEU 142 -0.26 PRO 349

ILE 26 0.13 ARG 143 -0.24 PRO 349

ILE 26 0.16 THR 144 -0.18 PRO 349

ILE 26 0.15 GLN 145 -0.14 PRO 349

ILE 26 0.18 GLU 146 -0.14 PRO 349

ILE 26 0.19 SER 147 -0.09 PRO 349

ARG 25 0.25 GLU 148 -0.06 TRP 355

ARG 25 0.24 CYS 149 -0.08 PRO 349

ARG 25 0.25 ALA 150 -0.05 PRO 349

ARG 25 0.29 CYS 151 -0.06 VAL 95

ARG 25 0.27 VAL 152 -0.07 ASP 272

ARG 25 0.30 ASN 153 -0.08 ASP 272

ARG 25 0.33 GLY 154 -0.08 PRO 72

ARG 25 0.29 SER 155 -0.07 PRO 72

ARG 25 0.27 CYS 156 -0.07 PRO 349

ARG 25 0.22 PHE 157 -0.09 PRO 349

ARG 25 0.19 THR 158 -0.11 PRO 349

ILE 26 0.15 ILE 159 -0.13 PRO 349

ILE 26 0.14 MET 160 -0.17 PRO 349

ASP 69 0.14 THR 161 -0.21 PRO 349

SER 71 0.11 ASP 162 -0.24 PRO 349

SER 71 0.17 GLY 163 -0.27 PRO 349

LYS 68 0.28 PRO 164 -0.30 PRO 349

ASP 69 0.40 SER 165 -0.28 PRO 349

VAL 67 0.45 ASN 166 -0.25 PRO 349

VAL 67 0.34 GLY 167 -0.22 PRO 349

VAL 67 0.26 GLN 168 -0.20 PRO 349

LYS 68 0.19 ALA 169 -0.22 PRO 349

ASP 69 0.13 SER 170 -0.20 PRO 349

ASP 69 0.13 TYR 171 -0.17 PRO 349

ILE 26 0.13 LYS 172 -0.15 PRO 349

ILE 26 0.14 ILE 173 -0.12 PRO 349

ARG 25 0.18 LEU 174 -0.12 PRO 349

ARG 25 0.22 LYS 175 -0.10 PRO 349

ARG 25 0.26 ILE 176 -0.09 PRO 349

ARG 25 0.30 GLU 177 -0.09 PRO 72

ARG 25 0.34 LYS 178 -0.11 PRO 72

ARG 25 0.32 GLY 179 -0.12 PRO 72

ARG 25 0.27 LYS 180 -0.11 PRO 72

ARG 25 0.23 VAL 181 -0.11 PRO 349

ARG 25 0.23 THR 182 -0.10 PRO 349

ARG 25 0.19 LYS 183 -0.11 PRO 349

ARG 25 0.16 SER 184 -0.13 PRO 349

ILE 26 0.13 ILE 185 -0.13 PRO 349

ILE 26 0.11 GLU 186 -0.15 PRO 349

VAL 67 0.11 LEU 187 -0.13 PRO 349

VAL 67 0.13 ASN 188 -0.13 PRO 349

VAL 67 0.18 ALA 189 -0.12 PRO 349

VAL 67 0.21 PRO 190 -0.13 PRO 349

VAL 67 0.26 ASN 191 -0.12 PRO 349

VAL 67 0.26 TYR 192 -0.12 PRO 349

VAL 67 0.29 HIS 193 -0.15 PRO 349

VAL 67 0.25 TYR 194 -0.14 PRO 349

ASP 69 0.28 GLU 195 -0.16 PRO 349

ASP 69 0.24 GLU 196 -0.14 PRO 349

VAL 67 0.19 CYS 197 -0.10 PRO 349

VAL 67 0.16 SER 198 -0.08 ASP 377

ARG 25 0.15 CYS 199 -0.05 PRO 349

ARG 25 0.18 TYR 200 -0.05 ASN 89

ARG 25 0.20 PRO 201 -0.07 ASP 272

ARG 25 0.18 ASP 202 -0.12 ASP 272

ARG 25 0.18 THR 203 -0.15 ASP 272

ARG 25 0.20 GLY 204 -0.10 THR 299

ARG 25 0.17 LYS 205 -0.07 CYS 253

ARG 25 0.17 VAL 206 -0.07 MET 207

VAL 67 0.13 MET 207 -0.07 VAL 206

VAL 67 0.15 CYS 208 -0.06 ASP 377

VAL 67 0.20 VAL 209 -0.08 ASP 377

VAL 67 0.25 CYS 210 -0.10 ASP 377

VAL 67 0.33 ARG 211 -0.12 ASP 377

VAL 67 0.37 ASP 212 -0.13 ILE 24

VAL 67 0.46 ASN 213 -0.18 SER 285

VAL 67 0.43 TRP 214 -0.16 PRO 349

VAL 67 0.41 HIS 215 -0.14 ILE 24

VAL 67 0.43 GLY 216 -0.16 ILE 24

VAL 67 0.39 SER 217 -0.18 ILE 24

VAL 67 0.34 ASN 218 -0.15 ILE 24

VAL 67 0.29 ARG 219 -0.13 ILE 24

VAL 67 0.26 PRO 220 -0.10 ILE 24

VAL 67 0.21 TRP 221 -0.07 ASP 377

VAL 67 0.17 VAL 222 -0.07 PRO 349

VAL 67 0.13 SER 223 -0.09 GLY 233

ARG 25 0.13 PHE 224 -0.09 ASP 225

ARG 25 0.17 ASP 225 -0.09 PHE 224

ARG 25 0.20 GLN 226 -0.06 GLY 233

ARG 25 0.18 ASN 227 -0.07 PRO 349

ARG 25 0.15 LEU 228 -0.09 PRO 349

ARG 25 0.13 ASP 229 -0.07 PRO 349

VAL 67 0.10 TYR 230 -0.08 GLY 233

VAL 67 0.14 GLN 231 -0.08 ASP 225

VAL 67 0.18 ILE 232 -0.08 PRO 255

VAL 67 0.22 GLY 233 -0.09 SER 223

VAL 67 0.25 TYR 234 -0.11 ILE 24

VAL 67 0.25 ILE 235 -0.12 ILE 24

VAL 67 0.25 CYS 236 -0.13 ILE 24

VAL 67 0.25 SER 237 -0.16 ILE 24

VAL 67 0.27 GLY 238 -0.18 ILE 24

VAL 67 0.26 VAL 239 -0.20 ILE 24

VAL 67 0.30 PHE 240 -0.20 ILE 24

VAL 67 0.29 GLY 241 -0.19 ILE 24

VAL 67 0.35 ASP 242 -0.19 ILE 24

THR 66 0.40 ASN 243 -0.21 ILE 24

VAL 67 0.44 PRO 244 -0.22 ILE 24

VAL 67 0.40 ARG 245 -0.22 ILE 24

VAL 67 0.37 PRO 246 -0.23 ILE 24

VAL 67 0.32 ASN 247 -0.25 ILE 24

VAL 67 0.29 ASP 248 -0.23 ILE 24

VAL 67 0.29 GLY 249 -0.21 ILE 24

VAL 67 0.29 THR 250 -0.18 ILE 24

VAL 67 0.29 GLY 251 -0.16 ILE 24

VAL 67 0.29 SER 252 -0.14 ILE 24

VAL 67 0.26 CYS 253 -0.12 ILE 24

VAL 67 0.29 GLY 254 -0.12 ILE 24

VAL 67 0.33 PRO 255 -0.13 ILE 24

VAL 67 0.36 VAL 256 -0.16 ILE 24

VAL 67 0.42 SER 257 -0.16 ILE 24

VAL 67 0.42 SER 258 -0.18 ILE 24

VAL 67 0.47 ASN 259 -0.19 ILE 24

VAL 67 0.48 GLY 260 -0.17 ILE 24

VAL 67 0.57 ALA 261 -0.18 SER 285

VAL 67 0.61 ASN 262 -0.23 SER 285

VAL 67 0.47 GLY 263 -0.17 ASN 213

THR 66 0.40 ILE 264 -0.17 ILE 24

VAL 67 0.30 LYS 265 -0.14 ASP 377

VAL 67 0.24 GLY 266 -0.13 ILE 24

VAL 67 0.21 PHE 267 -0.10 ILE 24

VAL 67 0.19 SER 268 -0.11 ILE 24

VAL 67 0.16 PHE 269 -0.08 GLY 30

VAL 67 0.16 ARG 270 -0.11 SER 8

VAL 67 0.14 TYR 271 -0.17 SER 8

VAL 67 0.14 ASP 272 -0.21 SER 8

VAL 67 0.17 ASN 273 -0.16 SER 8

VAL 67 0.17 GLY 274 -0.14 SER 8

VAL 67 0.18 VAL 275 -0.13 ILE 24

VAL 67 0.17 TRP 276 -0.14 ILE 24

VAL 67 0.21 ILE 277 -0.17 ILE 24

VAL 67 0.20 GLY 278 -0.19 ILE 24

THR 66 0.24 ARG 279 -0.23 ILE 24

THR 66 0.25 THR 280 -0.29 ILE 24

THR 66 0.22 LYS 281 -0.34 ILE 24

THR 66 0.26 SER 282 -0.34 ILE 24

THR 66 0.33 THR 283 -0.28 ILE 24

THR 66 0.39 SER 284 -0.27 ILE 24

ILE 354 0.33 SER 285 -0.29 ILE 24

ILE 354 0.27 ARG 286 -0.29 ILE 24

GLN 348 0.21 SER 287 -0.37 ILE 24

THR 66 0.16 GLY 288 -0.41 ILE 24

THR 66 0.18 PHE 289 -0.32 ILE 24

THR 66 0.17 GLU 290 -0.30 ILE 24

VAL 67 0.17 MET 291 -0.23 ILE 24

VAL 67 0.18 ILE 292 -0.21 ILE 24

VAL 67 0.17 TRP 293 -0.18 ILE 24

VAL 67 0.19 ASP 294 -0.17 ILE 24

VAL 67 0.17 PRO 295 -0.14 ILE 24

VAL 67 0.19 ASN 296 -0.14 ILE 24

VAL 67 0.21 GLY 297 -0.14 ILE 24

VAL 67 0.20 TRP 298 -0.12 SER 8

VAL 67 0.21 THR 299 -0.13 SER 8

VAL 67 0.22 GLU 300 -0.14 ILE 24

VAL 67 0.25 THR 301 -0.15 ILE 24

VAL 67 0.24 ASP 302 -0.17 ILE 24

VAL 67 0.25 SER 303 -0.20 ILE 24

VAL 67 0.22 SER 304 -0.20 ILE 24

VAL 67 0.20 PHE 305 -0.20 ILE 24

VAL 67 0.17 SER 306 -0.20 ILE 24

VAL 67 0.15 VAL 307 -0.22 ILE 24

VAL 67 0.16 ARG 308 -0.26 ILE 24

VAL 67 0.13 GLN 309 -0.28 ILE 24

PRO 349 0.14 ASP 310 -0.35 ILE 24

TRP 317 0.11 ILE 311 -0.34 ILE 24

TRP 317 0.17 VAL 312 -0.43 ILE 24

PRO 349 0.17 ALA 313 -0.53 ILE 24

PRO 349 0.21 ILE 314 -0.46 ILE 24

PRO 349 0.21 THR 315 -0.52 ILE 24

PRO 349 0.18 ASP 316 -0.53 ILE 24

VAL 312 0.17 TRP 317 -0.37 ILE 24

THR 66 0.16 SER 318 -0.30 ILE 24

THR 66 0.25 GLY 319 -0.22 ILE 24

THR 66 0.23 TYR 320 -0.16 ASP 377

THR 66 0.19 SER 321 -0.14 ASP 377

VAL 67 0.16 GLY 322 -0.09 ASP 377

ARG 25 0.15 SER 323 -0.07 GLY 30

ARG 25 0.23 PHE 324 -0.08 PRO 80

ARG 25 0.27 VAL 325 -0.10 PRO 80

ARG 25 0.34 GLN 326 -0.14 CYS 47

ARG 25 0.35 HIS 327 -0.10 ASP 272

ARG 25 0.36 PRO 328 -0.11 ASP 272

ARG 25 0.42 GLU 329 -0.10 ASP 272

ARG 25 0.47 LEU 330 -0.13 TYR 88

ARG 25 0.41 THR 331 -0.15 TYR 88

ARG 25 0.39 GLY 332 -0.14 TYR 88

ARG 25 0.32 LEU 333 -0.13 TYR 88

ARG 25 0.28 ASP 334 -0.13 ASP 272

ARG 25 0.24 CYS 335 -0.14 ASP 272

ARG 25 0.25 MET 336 -0.12 ASP 272

ARG 25 0.23 ARG 337 -0.14 PRO 80

ARG 25 0.18 PRO 338 -0.13 PRO 80

ARG 25 0.18 CYS 339 -0.14 PRO 80

ARG 25 0.13 PHE 340 -0.12 GLY 30

ARG 25 0.13 TRP 341 -0.13 GLY 30

THR 66 0.13 VAL 342 -0.14 ASP 377

GLY 23 0.11 GLU 343 -0.14 ASP 377

THR 66 0.08 LEU 344 -0.26 ASP 377

ALA 84 0.09 ILE 345 -0.20 ILE 24

SER 284 0.09 ARG 346 -0.26 ARG 25

SER 284 0.19 GLY 347 -0.27 ARG 25

SER 285 0.24 GLN 348 -0.31 ASP 117

THR 315 0.21 PRO 349 -0.32 ASP 117

PRO 376 0.13 LYS 350 -0.38 ARG 25

SER 284 0.14 GLU 351 -0.36 ARG 25

SER 284 0.21 ASN 352 -0.30 ARG 25

SER 284 0.27 THR 353 -0.25 ARG 25

SER 284 0.36 ILE 354 -0.30 ASP 117

SER 284 0.26 TRP 355 -0.27 ASP 117

SER 284 0.20 THR 356 -0.20 ASP 117

ILE 26 0.15 SER 357 -0.15 ASP 117

GLY 23 0.13 GLY 358 -0.14 ALA 379

GLY 23 0.24 SER 359 -0.18 GLY 30

GLY 23 0.21 SER 360 -0.18 GLY 30

ARG 25 0.14 ILE 361 -0.21 GLY 30

ARG 25 0.19 SER 362 -0.19 GLY 30

ARG 25 0.14 PHE 363 -0.19 GLY 30

ARG 25 0.17 CYS 364 -0.18 GLU 83

ARG 25 0.11 GLY 365 -0.17 GLU 83

CYS 10 0.10 VAL 366 -0.20 GLU 83

THR 203 0.09 ASN 367 -0.20 GLY 30

THR 315 0.08 SER 368 -0.23 GLY 30

THR 315 0.09 ASP 369 -0.26 GLY 30

THR 315 0.10 THR 370 -0.26 GLY 30

PRO 349 0.11 VAL 371 -0.28 ILE 24

THR 315 0.14 GLY 372 -0.33 ILE 24

PRO 349 0.13 TRP 373 -0.42 ILE 24

PRO 349 0.14 SER 374 -0.51 ILE 24

PRO 349 0.12 TRP 375 -0.43 ILE 24

LYS 350 0.13 PRO 376 -0.53 ILE 24

GLU 46 0.12 ASP 377 -0.31 ILE 24

GLY 82 0.27 GLY 378 -0.44 ILE 24

GLU 83 0.24 ALA 379 -0.39 GLY 378

GLU 83 0.22 GLU 380 -0.41 ARG 25

ASN 89 0.14 LEU 381 -0.31 ARG 25

ASN 89 0.09 PRO 382 -0.35 ARG 25

SER 284 0.12 PHE 383 -0.27 ARG 25

SER 284 0.15 SER 384 -0.26 ARG 25

SER 284 0.21 ILE 385 -0.23 ARG 25

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 8 ---

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

* EXP_3CYE_unrelaxed_rank_001_alphafold2_ptm_model_5_seed_000 *