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

* 1F0N_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000 *

CA distance fluctuations for 240220091526165245

--- normal mode 9 ---

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
TRP 59 0.18 SER 1 -0.62 PRO 224

TRP 59 0.31 ARG 2 -0.60 ALA 89

GLY 275 0.22 PRO 3 -0.99 ASP 46

GLY 275 0.32 GLY 4 -0.64 ASP 46

GLY 275 0.23 LEU 5 -0.44 PRO 224

GLY 275 0.17 PRO 6 -0.39 PRO 224

ASN 250 0.12 VAL 7 -0.40 PRO 224

ASN 250 0.10 GLU 8 -0.47 PRO 3

ASN 250 0.08 TYR 9 -0.69 PRO 3

ASN 250 0.07 LEU 10 -0.54 PRO 3

ASP 45 0.14 GLN 11 -0.56 PRO 3

ASP 45 0.13 VAL 12 -0.46 PRO 3

ASP 45 0.14 PRO 13 -0.43 PRO 3

GLY 171 0.14 SER 14 -0.43 PRO 3

GLN 92 0.20 PRO 15 -0.39 PRO 3

GLN 92 0.25 SER 16 -0.40 PRO 3

GLN 92 0.25 MET 17 -0.48 PRO 3

ALA 89 0.27 GLY 18 -0.48 PRO 3

ALA 89 0.20 ARG 19 -0.54 PRO 3

ASP 45 0.22 ASP 20 -0.54 PRO 3

ASP 45 0.19 ILE 21 -0.57 PRO 3

ASP 46 0.12 LYS 22 -0.67 PRO 3

ASP 46 0.06 VAL 23 -0.56 PRO 3

ASN 250 0.08 GLN 24 -0.60 PRO 3

ASN 250 0.11 PHE 25 -0.38 PRO 3

ASN 250 0.15 GLN 26 -0.36 PRO 224

ASN 250 0.17 SER 27 -0.31 PRO 224

ASN 250 0.21 GLY 28 -0.29 PRO 224

ASN 250 0.18 GLY 29 -0.27 PRO 224

ASN 203 0.17 ASN 30 -0.24 PRO 224

ASN 203 0.18 ASN 31 -0.22 PRO 224

ASN 203 0.20 SER 32 -0.24 PRO 224

ASN 203 0.21 PRO 33 -0.22 PRO 224

ASN 250 0.14 ALA 34 -0.26 PRO 224

ASN 250 0.14 VAL 35 -0.27 PRO 224

TYR 144 0.08 TYR 36 -0.29 PRO 224

LEU 162 0.08 LEU 37 -0.34 PRO 224

LEU 162 0.09 LEU 38 -0.37 PRO 3

LEU 162 0.11 ASP 39 -0.46 PRO 3

LEU 162 0.15 GLY 40 -0.46 PRO 224

LEU 162 0.12 LEU 41 -0.56 LEU 228

ASP 20 0.15 ARG 42 -0.78 PRO 224

ASP 20 0.13 ALA 43 -0.62 PRO 3

ASP 20 0.15 GLN 44 -0.74 PRO 3

ASP 20 0.22 ASP 45 -0.81 PRO 3

ASP 20 0.15 ASP 46 -0.99 PRO 3

LEU 218 0.10 TYR 47 -0.90 PRO 3

LEU 218 0.08 ASN 48 -0.68 PRO 3

LEU 218 0.11 GLY 49 -0.67 PRO 224

LEU 162 0.07 TRP 50 -0.55 PRO 224

LEU 270 0.09 ASP 51 -0.58 PRO 224

LEU 218 0.14 ILE 52 -0.69 PRO 224

GLY 267 0.18 ASN 53 -0.72 PRO 224

ALA 268 0.16 THR 54 -0.57 PRO 224

ASN 271 0.14 PRO 55 -0.53 PRO 224

LEU 270 0.14 ALA 56 -0.46 PRO 224

GLY 275 0.18 PHE 57 -0.44 PRO 224

TRP 59 0.48 GLU 58 -0.43 PRO 224

GLU 58 0.48 TRP 59 -0.39 ASN 222

GLU 58 0.29 TYR 60 -0.35 PRO 224

GLY 275 0.31 TYR 61 -0.38 PRO 224

SER 63 0.39 GLN 62 -0.32 ASN 222

GLN 62 0.39 SER 63 -0.29 ASN 222

GLN 62 0.27 GLY 64 -0.26 PRO 224

ASN 250 0.23 LEU 65 -0.28 PRO 224

ASN 250 0.17 SER 66 -0.30 PRO 224

ASN 250 0.15 ILE 67 -0.34 PRO 224

ASN 250 0.10 VAL 68 -0.34 PRO 224

TYR 144 0.07 MET 69 -0.45 PRO 3

VAL 71 0.11 PRO 70 -0.52 PRO 3

PRO 70 0.11 VAL 71 -0.69 PRO 3

ASP 20 0.16 GLY 72 -0.65 PRO 3

ASP 20 0.12 GLY 73 -0.58 PRO 3

ASP 20 0.14 GLN 74 -0.59 PRO 3

ALA 166 0.08 SER 75 -0.49 PRO 3

HIS 138 0.07 SER 76 -0.47 PRO 3

GLY 220 0.08 PHE 77 -0.38 PRO 3

ILE 143 0.08 TYR 78 -0.39 PRO 3

LEU 134 0.16 SER 79 -0.36 PRO 3

TRP 81 0.22 ASP 80 -0.38 PRO 3

TYR 137 0.23 TRP 81 -0.44 PRO 3

TYR 137 0.25 TYR 82 -0.41 PRO 3

TYR 137 0.22 SER 83 -0.47 PRO 3

ASP 80 0.21 PRO 84 -0.55 PRO 3

ASP 80 0.18 ALA 85 -0.58 PRO 3

SER 16 0.14 CYS 86 -0.63 PRO 3

GLY 18 0.19 GLY 87 -0.66 PRO 3

GLY 18 0.21 LYS 88 -0.73 PRO 3

GLY 18 0.27 ALA 89 -0.84 PRO 3

GLY 18 0.22 GLY 90 -0.80 PRO 3

SER 16 0.22 CYS 91 -0.70 PRO 3

THR 93 0.33 GLN 92 -0.66 PRO 3

GLN 92 0.33 THR 93 -0.55 PRO 3

LYS 95 0.22 TYR 94 -0.52 PRO 3

TYR 94 0.22 LYS 95 -0.43 PRO 3

THR 117 0.12 TRP 96 -0.42 PRO 3

PRO 84 0.17 GLU 97 -0.34 PRO 3

PRO 84 0.21 THR 98 -0.34 PRO 3

GLN 92 0.15 PHE 99 -0.37 PRO 3

TRP 96 0.10 LEU 100 -0.33 PRO 3

PRO 84 0.16 THR 101 -0.27 PRO 3

PRO 84 0.18 SER 102 -0.27 PRO 3

PRO 116 0.14 GLU 103 -0.32 PRO 3

PRO 116 0.09 LEU 104 -0.32 PRO 3

GLU 103 0.12 PRO 105 -0.24 PRO 3

SER 16 0.16 GLN 106 -0.23 PRO 3

PRO 15 0.11 TRP 107 -0.27 PRO 3

ASN 250 0.07 LEU 108 -0.25 PRO 224

PRO 15 0.10 SER 109 -0.22 PRO 224

PRO 15 0.10 ALA 110 -0.22 PRO 224

ASN 250 0.07 ASN 111 -0.24 PRO 224

ASN 250 0.10 ARG 112 -0.26 PRO 224

ASN 203 0.12 ALA 113 -0.24 PRO 224

ASN 203 0.13 VAL 114 -0.24 PRO 224

ASN 203 0.14 LYS 115 -0.20 PRO 224

SER 102 0.17 PRO 116 -0.19 PRO 224

TYR 82 0.16 THR 117 -0.16 PRO 224

ASN 203 0.21 GLY 118 -0.19 GLU 217

ASN 203 0.15 SER 119 -0.19 PRO 224

GLN 62 0.14 ALA 120 -0.20 PRO 224

SER 79 0.12 ALA 121 -0.20 PRO 224

GLU 58 0.10 ILE 122 -0.24 PRO 224

LEU 162 0.14 GLY 123 -0.25 PRO 3

LEU 162 0.17 LEU 124 -0.29 PRO 224

LEU 162 0.26 SER 125 -0.32 PRO 3

LEU 162 0.21 MET 126 -0.35 PRO 3

LEU 162 0.15 ALA 127 -0.33 PRO 3

GLY 159 0.13 GLY 128 -0.23 PRO 3

PRO 160 0.11 SER 129 -0.23 PRO 3

PRO 160 0.10 SER 130 -0.27 PRO 3

TRP 81 0.11 ALA 131 -0.22 PRO 3

TYR 82 0.13 MET 132 -0.16 PRO 3

TYR 82 0.16 ILE 133 -0.20 PRO 3

TRP 81 0.19 LEU 134 -0.22 PRO 3

TYR 82 0.18 ALA 135 -0.14 PRO 3

TYR 82 0.20 ALA 136 -0.15 PRO 3

TYR 82 0.25 TYR 137 -0.18 PRO 3

TYR 82 0.23 HIS 138 -0.17 PRO 3

TYR 82 0.21 PRO 139 -0.14 GLU 217

TYR 82 0.21 GLN 140 -0.15 GLU 217

TYR 82 0.18 GLN 141 -0.14 PRO 224

TYR 82 0.16 PHE 142 -0.14 GLU 217

GLN 62 0.19 ILE 143 -0.17 GLU 217

GLN 62 0.20 TYR 144 -0.19 GLU 217

GLU 58 0.16 ALA 145 -0.15 GLU 217

GLU 58 0.16 GLY 146 -0.16 GLU 217

LEU 151 0.12 SER 147 -0.17 ALA 170

LEU 151 0.14 LEU 148 -0.23 ALA 170

LEU 151 0.16 SER 149 -0.33 ALA 170

LEU 151 0.27 ALA 150 -0.33 ALA 170

ALA 150 0.27 LEU 151 -0.40 ALA 166

VAL 232 0.15 LEU 152 -0.28 ALA 166

PHE 231 0.21 ASP 153 -0.26 ALA 166

LEU 228 0.24 PRO 154 -0.24 PRO 3

LEU 228 0.24 SER 155 -0.23 PRO 3

LEU 228 0.35 GLN 156 -0.22 ALA 242

PRO 224 0.48 GLY 157 -0.28 LYS 238

PRO 224 0.51 MET 158 -0.30 LYS 238

PRO 224 0.38 GLY 159 -0.26 LYS 238

PRO 224 0.26 PRO 160 -0.27 PRO 3

PRO 224 0.35 SER 161 -0.27 PRO 3

PRO 224 0.37 LEU 162 -0.35 SER 234

GLY 220 0.24 ILE 163 -0.36 SER 234

GLY 220 0.18 GLY 164 -0.37 PRO 3

GLY 220 0.18 LEU 165 -0.51 PHE 231

GLY 220 0.15 ALA 166 -0.71 PHE 231

ASP 20 0.08 MET 167 -0.53 PHE 231

PRO 181 0.11 GLY 168 -0.55 PHE 227

ARG 19 0.14 ASP 169 -0.82 PHE 227

ARG 19 0.16 ALA 170 -0.79 LEU 228

GLY 18 0.21 GLY 171 -0.72 PRO 224

GLY 18 0.15 GLY 172 -0.57 PRO 3

GLY 172 0.10 TYR 173 -0.53 PRO 3

TYR 137 0.11 LYS 174 -0.46 PRO 3

GLY 220 0.12 ALA 175 -0.40 PRO 3

TYR 137 0.14 ALA 176 -0.39 PRO 3

TYR 137 0.17 ASP 177 -0.45 PRO 3

TYR 137 0.17 MET 178 -0.42 PRO 3

TYR 137 0.16 TRP 179 -0.35 PRO 3

TYR 137 0.14 GLY 180 -0.35 PRO 3

GLY 220 0.17 PRO 181 -0.31 PRO 3

PRO 224 0.22 SER 182 -0.27 PRO 3

PRO 224 0.22 SER 183 -0.25 PRO 3

GLY 220 0.15 ASP 184 -0.28 PRO 3

GLY 220 0.14 PRO 185 -0.26 PRO 3

ARG 189 0.18 ALA 186 -0.30 PRO 3

GLY 220 0.16 TRP 187 -0.27 PRO 3

PHE 231 0.17 GLU 188 -0.22 PRO 3

ALA 186 0.18 ARG 189 -0.23 PRO 3

MET 132 0.12 ASN 190 -0.25 PRO 3

PHE 231 0.13 ASP 191 -0.21 PRO 3

LEU 206 0.14 PRO 192 -0.17 PRO 3

PHE 231 0.18 THR 193 -0.19 ALA 166

PHE 231 0.18 GLN 194 -0.16 PRO 3

SER 280 0.14 GLN 195 -0.14 PRO 3

SER 280 0.18 ILE 196 -0.14 ALA 166

GLY 282 0.17 PRO 197 -0.10 ALA 166

GLY 282 0.17 LYS 198 -0.10 GLU 217

LEU 281 0.20 LEU 199 -0.13 GLU 217

GLY 282 0.24 VAL 200 -0.15 GLU 217

GLY 282 0.22 ALA 201 -0.15 GLU 217

GLY 282 0.24 ASN 202 -0.16 GLU 217

GLY 282 0.32 ASN 203 -0.19 GLU 217

LEU 281 0.28 THR 204 -0.19 GLU 217

SER 280 0.27 ARG 205 -0.22 GLU 217

GLN 62 0.21 LEU 206 -0.21 GLU 217

MET 273 0.21 TRP 207 -0.23 GLU 217

ASN 236 0.17 VAL 208 -0.19 ALA 170

ALA 272 0.19 TYR 209 -0.24 ALA 170

ALA 272 0.11 CYS 210 -0.32 ALA 170

ALA 268 0.09 GLY 211 -0.34 ASP 169

ILE 223 0.10 ASN 212 -0.44 ASP 169

GLY 157 0.20 GLY 213 -0.47 ASP 169

GLY 157 0.15 THR 214 -0.37 ASP 169

GLY 157 0.19 PRO 215 -0.25 ALA 89

LEU 162 0.12 ASN 216 -0.23 ALA 272

GLY 219 0.24 GLU 217 -0.44 ALA 272

LEU 162 0.21 LEU 218 -0.51 ALA 272

LEU 162 0.28 GLY 219 -0.37 ALA 272

LEU 162 0.35 GLY 220 -0.42 PRO 55

MET 158 0.29 ALA 221 -0.43 ASN 53

MET 158 0.39 ASN 222 -0.64 ASN 53

GLY 157 0.42 ILE 223 -0.64 ASN 53

MET 158 0.51 PRO 224 -0.78 ARG 42

MET 158 0.41 ALA 225 -0.57 ASN 53

GLY 157 0.33 GLU 226 -0.56 ASP 169

GLY 157 0.42 PHE 227 -0.82 ASP 169

GLY 157 0.44 LEU 228 -0.79 ALA 170

GLY 157 0.26 GLU 229 -0.56 ALA 170

GLY 157 0.22 ASN 230 -0.64 ASP 169

GLY 157 0.35 PHE 231 -0.71 ALA 166

GLN 156 0.24 VAL 232 -0.58 ALA 166

ASN 230 0.19 ARG 233 -0.48 ASP 169

PHE 227 0.19 SER 234 -0.51 ALA 166

PHE 231 0.19 SER 235 -0.46 ALA 166

VAL 208 0.17 ASN 236 -0.35 ALA 166

ALA 272 0.17 LEU 237 -0.36 ALA 166

PHE 227 0.16 LYS 238 -0.36 ALA 166

SER 280 0.16 PHE 239 -0.29 ALA 166

SER 280 0.20 GLN 240 -0.26 ALA 166

SER 279 0.21 ASP 241 -0.28 ALA 166

SER 280 0.19 ALA 242 -0.26 GLY 157

SER 280 0.22 TYR 243 -0.21 ALA 166

SER 279 0.25 ASN 244 -0.21 ALA 166

SER 279 0.23 ALA 245 -0.25 GLY 157

SER 280 0.22 ALA 246 -0.20 GLY 157

SER 279 0.27 GLY 247 -0.18 GLU 217

SER 280 0.31 GLY 248 -0.19 GLU 217

SER 279 0.34 HIS 249 -0.25 GLU 217

SER 280 0.42 ASN 250 -0.25 GLU 217

LEU 277 0.28 ALA 251 -0.25 GLU 217

MET 273 0.27 VAL 252 -0.30 GLU 217

ALA 272 0.28 PHE 253 -0.25 GLU 217

ALA 272 0.29 ASN 254 -0.30 GLU 217

ALA 272 0.25 PHE 255 -0.29 ASP 169

ALA 272 0.23 PRO 256 -0.27 ASP 169

ALA 272 0.22 PRO 257 -0.32 ASP 169

ALA 268 0.14 ASN 258 -0.28 ASP 169

GLY 159 0.12 GLY 259 -0.26 ASP 169

GLY 159 0.22 THR 260 -0.31 ALA 170

LEU 162 0.29 HIS 261 -0.35 ALA 170

LEU 162 0.31 SER 262 -0.61 TRP 263

LEU 162 0.20 TRP 263 -0.61 SER 262

LEU 162 0.21 GLU 264 -0.39 ASN 271

LEU 162 0.16 TYR 265 -0.30 GLN 269

LEU 162 0.16 TRP 266 -0.30 LEU 270

ASN 53 0.18 GLY 267 -0.36 PRO 224

PRO 257 0.22 ALA 268 -0.40 LEU 218

PRO 257 0.18 GLN 269 -0.34 LEU 218

GLU 58 0.19 LEU 270 -0.30 TRP 266

GLU 58 0.25 ASN 271 -0.41 LEU 218

ASN 254 0.29 ALA 272 -0.51 LEU 218

VAL 252 0.27 MET 273 -0.38 LEU 218

GLU 58 0.29 LYS 274 -0.38 LEU 218

GLN 62 0.36 GLY 275 -0.41 LEU 218

GLN 62 0.30 ASP 276 -0.37 LEU 218

ASN 250 0.31 LEU 277 -0.32 LEU 218

ASN 250 0.33 GLN 278 -0.33 LEU 218

ASN 250 0.38 SER 279 -0.34 GLU 217

ASN 250 0.42 SER 280 -0.29 GLU 217

ASN 250 0.33 LEU 281 -0.26 GLU 217

ASN 250 0.33 GLY 282 -0.28 GLU 217

ASN 250 0.30 ALA 283 -0.29 LEU 218

ASN 250 0.28 GLY 284 -0.34 LEU 218

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.

*** 1F0N_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000 ***

CA distance fluctuations for 240220091526165245

--- normal mode 9 ---

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

* 1F0N_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000 *