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

* 1Z7H_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000 *

CA distance fluctuations for 240220091409163486

--- normal mode 15 ---

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
LYS 345 0.17 PRO 1 -0.35 ASN 315

ARG 176 0.17 ILE 2 -0.34 ASN 315

ASN 179 0.19 THR 3 -0.32 ASN 315

ASN 179 0.22 ILE 4 -0.28 ASN 315

ASN 179 0.27 ASN 5 -0.27 ASN 315

ASN 179 0.28 ASN 6 -0.22 ASN 315

ASN 179 0.33 PHE 7 -0.20 ASN 315

ASN 179 0.35 ARG 8 -0.16 ASN 315

ASN 179 0.40 TYR 9 -0.13 ASN 315

ASN 179 0.41 SER 10 -0.12 PRO 314

ASN 179 0.40 ASP 11 -0.15 PRO 314

ASN 179 0.44 PRO 12 -0.14 PRO 314

ASN 179 0.48 VAL 13 -0.15 PRO 314

ASN 179 0.45 ASN 14 -0.20 PRO 314

ASN 179 0.49 ASN 15 -0.21 PRO 314

ASN 179 0.43 ASP 16 -0.27 PRO 314

ASN 179 0.39 THR 17 -0.27 ASN 315

ASN 179 0.44 ILE 18 -0.19 ASN 315

ASN 179 0.51 ILE 19 -0.16 PRO 314

ASN 179 0.59 MET 20 -0.11 PRO 314

ASN 179 0.62 MET 21 -0.09 PRO 314

ASN 179 0.73 GLU 22 -0.07 LEU 123

ASN 179 0.65 PRO 23 -0.06 LEU 123

ARG 176 0.75 PRO 24 -0.06 LEU 123

ARG 176 0.77 TYR 25 -0.05 ALA 68

ASN 179 0.88 CYS 26 -0.06 THR 147

ASN 179 1.01 LYS 27 -0.08 THR 147

ASN 179 1.19 GLY 28 -0.10 ALA 146

ASN 179 1.08 LEU 29 -0.09 ALA 146

ASN 179 0.94 ASP 30 -0.11 THR 147

ASN 179 0.82 ILE 31 -0.07 ALA 146

ASN 179 0.71 TYR 32 -0.05 LEU 123

ASN 179 0.60 TYR 33 -0.08 GLY 52

ASN 179 0.53 LYS 34 -0.10 PRO 314

ASN 179 0.47 ALA 35 -0.14 ASN 315

ASN 179 0.40 PHE 36 -0.20 ASN 315

ASN 179 0.35 LYS 37 -0.26 ASN 315

ASN 179 0.29 ILE 38 -0.26 ASN 315

ASN 179 0.25 THR 39 -0.32 ASN 315

ARG 176 0.26 ASP 40 -0.37 ASN 315

ARG 176 0.30 ARG 41 -0.32 ASN 315

ARG 176 0.30 ILE 42 -0.25 ASN 315

ASN 179 0.36 TRP 43 -0.21 ASN 315

ASN 179 0.36 ILE 44 -0.17 ASN 315

ASN 179 0.43 VAL 45 -0.13 ASN 315

ASN 179 0.41 PRO 46 -0.12 ASN 315

ASN 179 0.46 GLU 47 -0.08 ASN 315

ASN 179 0.43 ARG 48 -0.06 ASN 315

ASN 179 0.42 TYR 49 -0.06 ASN 315

ASN 179 0.51 GLU 50 -0.06 SER 63

ASN 179 0.64 PHE 51 -0.05 SER 63

ASN 179 0.76 GLY 52 -0.08 GLY 145

ASN 179 0.64 THR 53 -0.07 PRO 12

ASN 179 0.57 LYS 54 -0.09 LYS 83

ASN 179 0.47 PRO 55 -0.08 ARG 85

ASN 179 0.45 GLU 56 -0.09 THR 79

ASN 179 0.49 ASP 57 -0.07 THR 79

ASN 179 0.43 PHE 58 -0.07 PRO 385

TYR 264 0.37 ASN 59 -0.06 PRO 385

TYR 264 0.39 PRO 60 -0.07 PRO 385

TYR 264 0.48 PRO 61 -0.08 ASP 426

TYR 264 0.52 SER 62 -0.09 ASP 426

TYR 264 0.56 SER 63 -0.09 ASP 426

HIS 262 0.41 LEU 64 -0.12 ASP 426

HIS 262 0.39 ILE 65 -0.14 ASP 426

HIS 262 0.38 GLU 66 -0.13 ILE 212

GLN 256 0.30 GLY 67 -0.16 ILE 212

HIS 262 0.38 ALA 68 -0.15 SER 248

HIS 262 0.28 SER 69 -0.15 SER 247

HIS 262 0.39 GLU 70 -0.10 ASP 426

HIS 262 0.29 TYR 71 -0.08 ASP 426

TYR 264 0.30 TYR 72 -0.08 PRO 385

ASN 179 0.27 ASP 73 -0.10 PRO 385

ASN 179 0.35 PRO 74 -0.09 PRO 385

ASN 179 0.36 ASN 75 -0.10 PRO 385

ASN 179 0.33 TYR 76 -0.09 PRO 385

ASN 179 0.38 LEU 77 -0.08 ARG 85

ASN 179 0.43 ARG 78 -0.09 GLU 56

ASN 179 0.42 THR 79 -0.09 GLU 56

ASN 179 0.42 ASP 80 -0.09 LYS 54

ASN 179 0.36 SER 81 -0.09 ASN 315

ASN 179 0.35 ASP 82 -0.09 ASN 315

ASN 179 0.38 LYS 83 -0.10 ASN 315

ASN 179 0.35 ASP 84 -0.13 ASN 315

ASN 179 0.29 ARG 85 -0.12 ASN 315

ASN 179 0.29 PHE 86 -0.13 ASN 315

ASN 179 0.31 LEU 87 -0.15 ASN 315

ASN 179 0.27 GLN 88 -0.17 ASN 315

ASN 179 0.23 THR 89 -0.16 ASN 315

ASN 179 0.23 MET 90 -0.17 ASN 315

ASN 179 0.23 VAL 91 -0.20 ASN 315

ASN 179 0.19 LYS 92 -0.19 ASN 315

ARG 176 0.17 LEU 93 -0.19 ASN 315

ARG 176 0.18 PHE 94 -0.22 ASN 315

ARG 176 0.16 ASN 95 -0.23 ASN 315

ASN 211 0.17 ARG 96 -0.21 ASN 315

ASN 211 0.16 ILE 97 -0.22 ASN 315

ASN 211 0.15 LYS 98 -0.25 ASN 315

ASN 211 0.17 ASN 99 -0.24 ASN 315

ASN 211 0.19 ASN 100 -0.23 ASN 315

THR 213 0.18 VAL 101 -0.24 ASN 315

ASN 211 0.17 ALA 102 -0.23 ASN 315

ASN 211 0.15 GLY 103 -0.23 ASN 315

ILE 348 0.17 GLU 104 -0.27 ASN 315

ILE 348 0.21 ALA 105 -0.25 ASN 315

ILE 348 0.17 LEU 106 -0.23 ASN 315

LEU 175 0.18 LEU 107 -0.26 ASN 315

LYS 345 0.19 ASP 108 -0.29 ASN 315

LYS 345 0.19 LYS 109 -0.25 ASN 315

LEU 175 0.21 ILE 110 -0.24 ASN 315

LEU 175 0.22 ILE 111 -0.31 ASN 315

LEU 175 0.22 ASN 112 -0.29 ASN 315

LEU 175 0.24 ALA 113 -0.22 ASN 315

LEU 175 0.28 ILE 114 -0.22 ASN 315

LEU 175 0.32 PRO 115 -0.12 ASN 315

LEU 175 0.26 TYR 116 -0.11 TYR 121

LEU 175 0.32 LEU 117 -0.10 ILE 114

ASP 178 0.21 GLY 118 -0.11 VAL 134

LEU 175 0.14 ASN 119 -0.17 ILE 301

ASN 312 0.12 SER 120 -0.38 ALA 300

ASN 312 0.22 TYR 121 -0.42 ALA 300

ASN 312 0.22 SER 122 -0.14 ALA 300

ASP 178 0.14 LEU 123 -0.16 SER 131

SER 248 0.11 LEU 124 -0.17 TYR 121

ASP 178 0.11 ASP 125 -0.09 SER 150

ASP 178 0.27 LYS 126 -0.12 ASP 128

ASP 178 0.33 PHE 127 -0.11 LYS 126

ASP 178 0.49 ASP 128 -0.12 LEU 123

ASP 178 0.55 THR 129 -0.16 THR 154

ASP 178 0.72 ASN 130 -0.14 LEU 123

ARG 176 0.65 SER 131 -0.16 LEU 123

ARG 176 0.75 ASN 132 -0.13 LEU 123

LEU 175 0.67 SER 133 -0.10 LEU 123

LEU 175 0.45 VAL 134 -0.11 GLY 118

ARG 176 0.52 SER 135 -0.11 LEU 123

ASN 179 0.62 PHE 136 -0.09 LEU 123

ASN 179 0.72 ASN 137 -0.10 LEU 123

ASN 179 0.65 LEU 138 -0.12 ASN 312

ASN 179 0.66 LEU 139 -0.11 ASN 312

ASN 179 0.59 GLU 140 -0.14 ASN 312

ASN 179 0.56 GLN 141 -0.13 ASN 312

ASN 179 0.52 ASP 142 -0.13 ASN 312

ASN 179 0.48 PRO 143 -0.12 ASN 312

ASN 179 0.47 SER 144 -0.13 ASN 312

ASN 179 0.52 GLY 145 -0.10 ASN 312

ASN 179 0.55 ALA 146 -0.12 ASN 312

ASN 179 0.61 THR 147 -0.12 ASN 312

ASN 179 0.65 THR 148 -0.14 ASN 312

ASN 179 0.71 LYS 149 -0.13 ASN 312

ASP 178 0.65 SER 150 -0.18 ASN 312

ASP 178 0.63 ALA 151 -0.18 ASN 312

ASN 179 0.51 MET 152 -0.22 ASP 313

ASP 178 0.42 LEU 153 -0.21 ASP 313

ARG 176 0.37 THR 154 -0.24 ASN 315

LEU 175 0.34 ASN 155 -0.21 ASN 315

LEU 175 0.33 LEU 156 -0.18 ASN 315

ARG 176 0.37 ILE 157 -0.16 ASN 315

ARG 176 0.31 ILE 158 -0.15 ASN 315

ASN 179 0.36 PHE 159 -0.11 ASN 315

ASN 179 0.33 GLY 160 -0.11 ASN 315

ASN 179 0.27 PRO 161 -0.09 ASN 315

TYR 264 0.32 GLY 162 -0.06 ASN 315

TYR 264 0.35 PRO 163 -0.06 PRO 385

TYR 264 0.37 VAL 164 -0.07 ASN 315

TYR 264 0.29 LEU 165 -0.08 ASN 315

TYR 264 0.27 ASN 166 -0.09 ASN 315

TYR 264 0.35 LYS 167 -0.09 ASN 315

TYR 264 0.28 ASN 168 -0.11 ASN 315

TYR 264 0.27 GLU 169 -0.10 ALA 68

TYR 264 0.21 VAL 170 -0.10 ASN 315

LEU 175 0.22 ARG 171 -0.09 ALA 68

LEU 175 0.27 GLY 172 -0.16 PHE 183

LEU 175 0.47 ILE 173 -0.12 PHE 183

LEU 175 0.33 VAL 174 -0.10 LYS 293

SER 133 0.67 LEU 175 -0.13 LYS 293

LYS 27 0.87 ARG 176 -0.32 LYS 293

GLY 28 0.71 VAL 177 -0.45 LYS 293

GLY 28 1.04 ASP 178 -0.60 LYS 293

GLY 28 1.19 ASN 179 -0.60 ASP 289

GLY 28 0.76 LYS 180 -0.77 LYS 293

TYR 25 0.41 ASN 181 -0.37 LYS 293

LYS 27 0.25 TYR 182 -0.34 LYS 293

GLY 52 0.13 PHE 183 -0.30 PRO 184

LEU 175 0.16 PRO 184 -0.30 PHE 183

LEU 175 0.22 CYS 185 -0.25 LYS 180

SER 247 0.14 ARG 186 -0.47 LYS 180

SER 248 0.12 ASP 187 -0.52 LYS 180

SER 248 0.09 GLY 188 -0.39 LYS 180

LEU 175 0.17 PHE 189 -0.23 LYS 180

LEU 175 0.25 GLY 190 -0.17 LYS 180

LEU 175 0.43 SER 191 -0.13 PHE 183

LEU 175 0.45 ILE 192 -0.10 ASN 315

LEU 175 0.34 MET 193 -0.12 ASN 315

LEU 175 0.32 GLN 194 -0.11 ASN 315

ARG 176 0.25 MET 195 -0.12 ASN 315

ARG 176 0.25 ALA 196 -0.11 ASN 315

TYR 264 0.22 PHE 197 -0.12 ASN 315

TYR 264 0.21 CYS 198 -0.12 ASN 315

ASN 179 0.17 PRO 199 -0.14 ASN 315

ASN 179 0.17 GLU 200 -0.12 ASN 315

TYR 264 0.18 TYR 201 -0.11 ASN 315

TYR 264 0.14 VAL 202 -0.11 ASN 315

ASN 378 0.14 PRO 203 -0.11 ASN 315

GLU 70 0.12 THR 204 -0.11 ASN 315

GLU 70 0.16 PHE 205 -0.13 ILE 212

SER 63 0.15 ASP 206 -0.15 ILE 212

ASN 211 0.19 ASN 207 -0.13 LYS 180

LEU 215 0.17 VAL 208 -0.16 ILE 212

LEU 215 0.29 ILE 209 -0.15 GLU 257

LEU 215 0.57 GLU 210 -0.29 GLU 257

GLU 409 0.45 ASN 211 -0.50 ILE 258

GLU 409 0.32 ILE 212 -0.93 ILE 258

GLU 409 0.39 THR 213 -0.65 ILE 258

GLU 409 0.28 SER 214 -0.35 ILE 258

GLU 210 0.57 LEU 215 -0.29 ILE 258

GLU 210 0.17 THR 216 -0.14 HIS 262

SER 63 0.10 ILE 217 -0.22 ILE 212

ASN 211 0.17 GLY 218 -0.12 LYS 180

SER 63 0.11 LYS 219 -0.12 LYS 180

ASN 211 0.17 SER 220 -0.10 ASN 315

ASN 211 0.12 LYS 221 -0.11 ASN 315

ASN 211 0.17 TYR 222 -0.12 ASN 315

ASN 211 0.14 PHE 223 -0.12 ASN 315

ASN 211 0.15 GLN 224 -0.13 ASN 315

ASN 211 0.18 ASP 225 -0.15 ASN 315

ASN 211 0.15 PRO 226 -0.15 ASN 315

ASN 211 0.16 ALA 227 -0.17 ASN 315

ASN 211 0.17 LEU 228 -0.17 ASN 315

TYR 264 0.13 LEU 229 -0.15 ASN 315

LEU 175 0.15 LEU 230 -0.17 ASN 315

LEU 175 0.14 MET 231 -0.18 ASN 315

LEU 175 0.12 HIS 232 -0.15 ASN 315

LEU 175 0.15 GLU 233 -0.14 ASN 315

LEU 175 0.17 LEU 234 -0.18 ASN 315

LEU 175 0.14 ILE 235 -0.18 LYS 180

LEU 175 0.15 HIS 236 -0.19 LYS 180

LEU 175 0.21 VAL 237 -0.15 ASN 315

LEU 175 0.19 LEU 238 -0.17 LYS 180

LEU 175 0.14 HIS 239 -0.27 LYS 180

LEU 175 0.21 GLY 240 -0.22 LYS 180

LEU 175 0.26 LEU 241 -0.15 LYS 180

LEU 175 0.17 TYR 242 -0.26 LYS 180

LEU 175 0.13 GLY 243 -0.35 LYS 180

LEU 175 0.07 MET 244 -0.43 LYS 180

GLY 172 0.10 GLN 245 -0.40 LYS 180

ASN 59 0.07 VAL 246 -0.50 LYS 180

ARG 186 0.14 SER 247 -0.47 LYS 180

ARG 186 0.12 SER 248 -0.63 LYS 180

ILE 282 0.13 HIS 249 -0.55 LYS 180

SER 62 0.21 GLU 250 -0.38 LYS 180

SER 62 0.25 ILE 251 -0.35 LYS 180

SER 62 0.34 ILE 252 -0.35 ILE 212

SER 63 0.34 PRO 253 -0.41 ILE 212

SER 63 0.38 SER 254 -0.48 ILE 212

SER 63 0.42 LYS 255 -0.65 ILE 212

SER 63 0.40 GLN 256 -0.72 ILE 212

SER 63 0.32 GLU 257 -0.84 ILE 212

SER 63 0.26 ILE 258 -0.93 ILE 212

SER 63 0.27 TYR 259 -0.62 ILE 212

SER 63 0.33 MET 260 -0.56 ILE 212

SER 63 0.40 GLN 261 -0.48 ILE 212

SER 63 0.54 HIS 262 -0.50 ILE 212

SER 63 0.52 THR 263 -0.50 ILE 212

SER 63 0.56 TYR 264 -0.39 ILE 212

SER 62 0.38 PRO 265 -0.33 ILE 212

SER 62 0.27 ILE 266 -0.26 LYS 180

PRO 61 0.17 SER 267 -0.33 LYS 180

SER 62 0.13 ALA 268 -0.41 LYS 180

PRO 61 0.10 GLU 269 -0.36 LYS 180

GLU 169 0.13 GLU 270 -0.27 LYS 180

SER 62 0.14 LEU 271 -0.29 LYS 180

SER 62 0.10 PHE 272 -0.33 LYS 180

ILE 209 0.09 THR 273 -0.26 LYS 180

SER 62 0.12 PHE 274 -0.23 LYS 180

LEU 215 0.17 GLY 275 -0.26 LYS 180

LEU 215 0.24 GLY 276 -0.24 LYS 180

LEU 215 0.26 GLN 277 -0.25 LYS 180

SER 63 0.19 ASP 278 -0.27 LYS 180

LEU 215 0.16 ALA 279 -0.32 LYS 180

LEU 215 0.20 ASN 280 -0.33 LYS 180

SER 62 0.20 LEU 281 -0.35 SER 254

SER 62 0.16 ILE 282 -0.40 LYS 180

SER 62 0.12 SER 283 -0.45 LYS 180

LEU 215 0.11 ILE 284 -0.50 LYS 180

GLU 361 0.07 ASP 285 -0.58 LYS 180

LEU 124 0.07 ILE 286 -0.58 LYS 180

GLU 361 0.09 LYS 287 -0.55 LYS 180

TYR 355 0.12 ASN 288 -0.61 LYS 180

TYR 355 0.08 ASP 289 -0.73 LYS 180

TYR 355 0.07 LEU 290 -0.67 LYS 180

ALA 105 0.10 TYR 291 -0.60 LYS 180

ALA 105 0.09 GLU 292 -0.69 LYS 180

LEU 124 0.08 LYS 293 -0.77 LYS 180

ALA 105 0.07 THR 294 -0.61 LYS 180

ALA 105 0.09 LEU 295 -0.58 LYS 180

LEU 124 0.08 ASN 296 -0.67 LYS 180

LEU 124 0.09 ASP 297 -0.61 LYS 180

ASN 112 0.06 TYR 298 -0.47 LYS 180

ASN 303 0.06 LYS 299 -0.49 LYS 180

LYS 304 0.09 ALA 300 -0.49 LYS 180

LYS 304 0.06 ILE 301 -0.35 TYR 121

ASN 112 0.05 ALA 302 -0.31 LYS 180

SER 306 0.06 ASN 303 -0.35 TYR 121

ALA 300 0.09 LYS 304 -0.33 TYR 121

LEU 175 0.08 LEU 305 -0.20 TYR 121

ASN 303 0.06 SER 306 -0.19 TYR 121

ALA 300 0.07 GLN 307 -0.17 TYR 121

ASP 178 0.10 VAL 308 -0.09 PRO 1

ASP 178 0.19 THR 309 -0.11 PRO 1

ASP 178 0.33 SER 310 -0.15 PRO 1

ASP 178 0.44 CYS 311 -0.17 PRO 1

ASP 178 0.62 ASN 312 -0.19 MET 152

ASP 178 0.61 ASP 313 -0.25 ASP 40

ASP 178 0.55 PRO 314 -0.28 PRO 1

ASP 178 0.50 ASN 315 -0.37 ASP 40

ASP 178 0.43 ILE 316 -0.26 PRO 1

ASP 178 0.33 ASP 317 -0.24 PRO 1

ASP 178 0.27 ILE 318 -0.17 PRO 1

ASP 178 0.19 ASP 319 -0.15 PRO 1

ASP 178 0.21 SER 320 -0.19 PRO 1

LEU 175 0.23 TYR 321 -0.16 LYS 109

LEU 175 0.18 LYS 322 -0.11 ASN 280

LEU 175 0.17 GLN 323 -0.15 SER 352

LEU 175 0.21 ILE 324 -0.17 SER 352

LEU 175 0.18 TYR 325 -0.13 ASN 280

LEU 175 0.13 GLN 326 -0.17 LYS 180

ASN 112 0.19 GLN 327 -0.19 SER 352

ASN 112 0.21 LYS 328 -0.17 LYS 180

ASN 112 0.14 TYR 329 -0.27 LYS 180

ASN 112 0.16 GLN 330 -0.26 LYS 180

ASN 112 0.13 PHE 331 -0.27 LYS 180

ASN 112 0.12 ASP 332 -0.26 LYS 180

ASP 334 0.14 LYS 333 -0.24 LYS 180

LYS 333 0.14 ASP 334 -0.29 LYS 180

ASP 319 0.16 SER 335 -0.26 LYS 180

GLY 337 0.31 ASN 336 -0.24 LYS 180

ASN 336 0.31 GLY 337 -0.18 LYS 180

ASP 319 0.09 GLN 338 -0.23 LYS 180

PRO 143 0.07 TYR 339 -0.26 LYS 180

ASN 112 0.08 ILE 340 -0.35 LYS 180

ASN 112 0.09 VAL 341 -0.39 LYS 180

ASP 108 0.13 ASN 342 -0.37 LYS 180

ALA 105 0.14 GLU 343 -0.43 LYS 180

ALA 105 0.17 ASP 344 -0.38 LYS 180

ASP 108 0.19 LYS 345 -0.33 LYS 180

LYS 109 0.15 PHE 346 -0.38 LYS 180

ALA 105 0.16 GLN 347 -0.41 LYS 180

ALA 105 0.21 ILE 348 -0.33 LYS 180

LYS 109 0.18 LEU 349 -0.31 LYS 180

ALA 105 0.13 TYR 350 -0.39 LYS 180

SER 352 0.20 ASN 351 -0.36 LYS 180

ASN 351 0.20 SER 352 -0.29 LYS 180

LEU 106 0.11 ILE 353 -0.29 LYS 180

ASN 288 0.09 MET 354 -0.35 LYS 180

ASN 288 0.12 TYR 355 -0.31 LYS 180

LEU 215 0.12 GLY 356 -0.26 LYS 180

LEU 215 0.12 PHE 357 -0.22 LYS 180

LEU 215 0.14 THR 358 -0.22 LYS 180

ASN 211 0.15 GLU 359 -0.18 LYS 180

ASN 211 0.19 VAL 360 -0.19 LYS 180

ASN 211 0.20 GLU 361 -0.18 LYS 180

ASN 211 0.20 LEU 362 -0.19 ASN 315

ASN 211 0.24 GLY 363 -0.17 ASN 315

ASN 211 0.28 LYS 364 -0.17 ASN 315

ASN 211 0.25 LYS 365 -0.19 ASN 315

ASN 211 0.25 PHE 366 -0.19 ASN 315

ASN 211 0.31 ASN 367 -0.17 ASN 315

ASN 211 0.27 ILE 368 -0.16 ASN 315

ASN 211 0.29 LYS 369 -0.14 ASN 315

ASN 211 0.23 THR 370 -0.13 ASN 315

ILE 209 0.18 ARG 371 -0.14 LYS 180

LEU 215 0.21 LEU 372 -0.17 LYS 180

SER 63 0.22 SER 373 -0.19 LYS 180

SER 63 0.23 TYR 374 -0.19 LYS 180

SER 63 0.31 PHE 375 -0.34 ILE 212

SER 63 0.26 SER 376 -0.31 ILE 212

SER 63 0.27 MET 377 -0.34 ILE 212

GLU 70 0.28 ASN 378 -0.23 ILE 212

GLU 70 0.16 HIS 379 -0.19 ILE 212

GLN 256 0.14 ASP 380 -0.15 ILE 212

HIS 262 0.14 PRO 381 -0.11 SER 247

HIS 262 0.12 VAL 382 -0.10 ASN 315

ASN 179 0.12 LYS 383 -0.10 ASN 315

ASN 179 0.13 ILE 384 -0.11 ASN 315

ASN 179 0.17 PRO 385 -0.11 ASN 315

ASN 179 0.17 ASN 386 -0.12 ASN 315

ASN 179 0.16 LEU 387 -0.14 ASN 315

ASN 179 0.19 LEU 388 -0.14 ASN 315

ASN 179 0.17 ASP 389 -0.14 ASN 315

ASN 211 0.16 ASP 390 -0.15 ASN 315

ASN 211 0.17 THR 391 -0.14 ASN 315

ASN 211 0.17 ILE 392 -0.14 ASN 315

ASN 211 0.18 TYR 393 -0.15 ASN 315

ASN 211 0.19 ASN 394 -0.17 ASN 315

ASN 211 0.18 ASP 395 -0.19 ASN 315

ASN 211 0.21 THR 396 -0.19 ASN 315

ASN 211 0.23 GLU 397 -0.18 ASN 315

ASN 211 0.21 GLY 398 -0.17 ASN 315

ASN 211 0.22 PHE 399 -0.15 ASN 315

ASN 211 0.27 ASN 400 -0.15 ASN 315

ASN 211 0.24 ILE 401 -0.15 ASN 315

THR 213 0.28 GLU 402 -0.15 ASN 315

THR 213 0.25 SER 403 -0.15 ASN 315

THR 213 0.24 LYS 404 -0.14 ASN 315

THR 213 0.29 ASP 405 -0.14 ASN 315

ASN 211 0.28 LEU 406 -0.14 ASN 315

ASN 211 0.32 LYS 407 -0.15 ASN 315

ASN 211 0.39 SER 408 -0.14 ASN 315

ASN 211 0.45 GLU 409 -0.13 ASN 315

ASN 211 0.35 TYR 410 -0.14 ASN 315

ASN 211 0.30 LYS 411 -0.13 ASN 315

ASN 211 0.25 GLY 412 -0.13 ASN 315

ASN 211 0.23 GLN 413 -0.13 ASN 315

ASN 211 0.22 ASN 414 -0.12 ASN 315

ASN 211 0.15 MET 415 -0.11 ASN 315

ASN 211 0.16 ARG 416 -0.11 ASN 315

ASN 211 0.20 VAL 417 -0.11 ASN 315

ASN 211 0.18 ASN 418 -0.12 ASN 315

ASN 211 0.13 THR 419 -0.11 ASN 315

ASN 211 0.13 ASN 420 -0.11 ASN 315

ASN 211 0.14 ALA 421 -0.12 ASN 315

ASN 211 0.11 PHE 422 -0.11 ASN 315

ASN 179 0.10 ARG 423 -0.09 ASN 315

SER 81 0.09 ASN 424 -0.10 LEU 215

HIS 262 0.11 VAL 425 -0.11 ILE 212

SER 81 0.12 ASP 426 -0.14 ILE 65

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.

*** 1Z7H_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000 ***

CA distance fluctuations for 240220091409163486

--- normal mode 15 ---

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

* 1Z7H_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000 *