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 14 ---

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
ASN 222 0.44 SER 1 -0.16 VAL 7

LEU 218 0.50 ARG 2 -0.39 VAL 7

GLU 217 0.47 PRO 3 -0.81 GLU 8

LEU 218 0.42 GLY 4 -0.46 GLU 8

ASN 222 0.37 LEU 5 -0.31 GLY 29

PRO 224 0.34 PRO 6 -0.39 ASN 30

PRO 224 0.32 VAL 7 -0.77 PRO 3

PRO 224 0.30 GLU 8 -0.81 PRO 3

PRO 224 0.30 TYR 9 -0.73 PRO 3

PRO 224 0.28 LEU 10 -0.59 PRO 3

PRO 224 0.25 GLN 11 -0.48 PRO 3

PRO 224 0.26 VAL 12 -0.42 PRO 3

PRO 224 0.22 PRO 13 -0.37 PRO 3

PRO 224 0.23 SER 14 -0.31 PRO 3

ASP 184 0.21 PRO 15 -0.28 PRO 3

ASP 184 0.24 SER 16 -0.24 PRO 3

PRO 224 0.23 MET 17 -0.22 PRO 3

PRO 224 0.19 GLY 18 -0.24 PRO 3

PRO 224 0.20 ARG 19 -0.28 PRO 3

PRO 224 0.20 ASP 20 -0.34 PRO 3

PRO 224 0.27 ILE 21 -0.36 PRO 3

PRO 224 0.30 LYS 22 -0.43 PRO 3

PRO 224 0.34 VAL 23 -0.46 PRO 3

PRO 224 0.36 GLN 24 -0.52 PRO 3

PRO 224 0.34 PHE 25 -0.51 PRO 3

PRO 224 0.32 GLN 26 -0.43 PRO 3

ASN 250 0.29 SER 27 -0.36 PRO 3

ASN 250 0.35 GLY 28 -0.22 PRO 3

ASN 250 0.37 GLY 29 -0.35 PRO 6

ASN 250 0.43 ASN 30 -0.39 PRO 6

ASN 203 0.46 ASN 31 -0.29 PRO 3

ASN 250 0.45 SER 32 -0.22 PRO 3

ASN 250 0.42 PRO 33 -0.16 PRO 3

ASN 250 0.32 ALA 34 -0.19 PRO 3

PRO 224 0.34 VAL 35 -0.17 GLN 278

PRO 224 0.38 TYR 36 -0.17 PRO 3

PRO 224 0.43 LEU 37 -0.19 LYS 274

PRO 224 0.47 LEU 38 -0.17 LEU 41

PRO 224 0.58 ASP 39 -0.17 LYS 274

PRO 224 0.68 GLY 40 -0.24 LEU 41

PRO 224 0.65 LEU 41 -0.26 ALA 127

PRO 224 0.65 ARG 42 -0.20 ALA 43

PRO 224 0.56 ALA 43 -0.20 ARG 42

PRO 224 0.46 GLN 44 -0.20 PRO 3

ILE 223 0.37 ASP 45 -0.26 PRO 3

ILE 223 0.37 ASP 46 -0.30 PRO 3

PRO 224 0.39 TYR 47 -0.32 PRO 3

PRO 224 0.46 ASN 48 -0.25 PRO 3

PRO 224 0.57 GLY 49 -0.16 ASP 169

PRO 224 0.50 TRP 50 -0.16 ASP 169

PRO 224 0.45 ASP 51 -0.14 PRO 3

ILE 223 0.48 ILE 52 -0.14 ASP 169

ASN 222 0.54 ASN 53 -0.16 ASP 169

ASN 222 0.47 THR 54 -0.14 ASP 169

ASN 222 0.45 PRO 55 -0.10 GLY 29

PRO 224 0.42 ALA 56 -0.13 TRP 59

PRO 224 0.38 PHE 57 -0.12 GLY 29

TRP 59 0.45 GLU 58 -0.15 GLY 29

GLU 58 0.45 TRP 59 -0.13 ALA 166

LEU 218 0.31 TYR 60 -0.13 ALA 166

LEU 218 0.31 TYR 61 -0.19 GLY 29

ASN 250 0.30 GLN 62 -0.21 GLY 29

ASN 250 0.34 SER 63 -0.12 ALA 166

ASN 250 0.38 GLY 64 -0.11 GLN 62

ASN 250 0.38 LEU 65 -0.11 ALA 166

ASN 250 0.32 SER 66 -0.23 PRO 3

PRO 224 0.35 ILE 67 -0.23 PRO 3

PRO 224 0.36 VAL 68 -0.30 PRO 3

PRO 224 0.41 MET 69 -0.29 PRO 3

PRO 224 0.39 PRO 70 -0.31 PRO 3

PRO 224 0.39 VAL 71 -0.31 PRO 3

PRO 224 0.40 GLY 72 -0.24 PRO 3

PRO 224 0.42 GLY 73 -0.18 PRO 3

PRO 224 0.45 GLN 74 -0.18 ALA 246

PRO 224 0.40 SER 75 -0.27 ALA 150

PRO 224 0.37 SER 76 -0.26 ALA 246

PRO 224 0.39 PHE 77 -0.26 TYR 243

PRO 224 0.37 TYR 78 -0.21 MET 132

ALA 186 0.34 SER 79 -0.36 ILE 133

TRP 179 0.31 ASP 80 -0.32 LYS 198

LYS 95 0.27 TRP 81 -0.44 GLN 195

SER 16 0.23 TYR 82 -0.44 ARG 189

LEU 165 0.20 SER 83 -0.41 ALA 246

ILE 223 0.18 PRO 84 -0.35 ALA 246

ILE 223 0.19 ALA 85 -0.35 ASP 191

ASP 45 0.20 CYS 86 -0.35 ALA 245

ILE 223 0.17 GLY 87 -0.34 ALA 242

ILE 223 0.23 LYS 88 -0.29 SER 161

ASP 45 0.35 ALA 89 -0.23 ALA 245

ASP 45 0.36 GLY 90 -0.27 ALA 245

ASP 45 0.26 CYS 91 -0.30 ALA 246

ASP 45 0.24 GLN 92 -0.27 GLN 195

PRO 224 0.22 THR 93 -0.26 GLN 195

PRO 224 0.26 TYR 94 -0.28 GLN 195

TRP 81 0.27 LYS 95 -0.26 TYR 137

PRO 224 0.32 TRP 96 -0.24 GLU 97

ALA 186 0.42 GLU 97 -0.24 TRP 96

ALA 186 0.39 THR 98 -0.21 PRO 3

ALA 186 0.33 PHE 99 -0.26 PRO 3

ALA 186 0.34 LEU 100 -0.24 PRO 3

ALA 186 0.38 THR 101 -0.23 PRO 3

ALA 186 0.37 SER 102 -0.27 PRO 3

ALA 186 0.32 GLU 103 -0.31 PRO 3

ALA 186 0.29 LEU 104 -0.35 PRO 3

ALA 186 0.30 PRO 105 -0.33 PRO 3

PRO 185 0.30 GLN 106 -0.36 PRO 3

ALA 186 0.27 TRP 107 -0.40 PRO 3

ASN 203 0.29 LEU 108 -0.42 PRO 3

ASN 203 0.35 SER 109 -0.38 PRO 3

ASN 203 0.30 ALA 110 -0.40 PRO 3

ASN 203 0.28 ASN 111 -0.46 PRO 3

ASN 203 0.32 ARG 112 -0.47 PRO 3

ASN 203 0.36 ALA 113 -0.39 PRO 3

ASN 203 0.38 VAL 114 -0.34 PRO 3

ASN 203 0.40 LYS 115 -0.28 PRO 3

GLN 141 0.35 PRO 116 -0.27 PRO 3

ASN 202 0.40 THR 117 -0.21 THR 101

ASN 203 0.51 GLY 118 -0.17 THR 101

THR 204 0.34 SER 119 -0.21 LEU 281

PRO 224 0.31 ALA 120 -0.17 SER 279

PRO 224 0.34 ALA 121 -0.18 LEU 277

PRO 224 0.39 ILE 122 -0.21 ALA 166

PRO 224 0.43 GLY 123 -0.27 ALA 166

PRO 224 0.53 LEU 124 -0.34 ALA 166

PRO 224 0.56 SER 125 -0.49 ALA 166

PRO 224 0.51 MET 126 -0.38 ALA 166

PRO 224 0.46 ALA 127 -0.26 ALA 166

PRO 224 0.40 GLY 128 -0.35 SER 147

PRO 224 0.33 SER 129 -0.30 ALA 166

PRO 224 0.34 SER 130 -0.26 MET 132

PRO 224 0.35 ALA 131 -0.21 ALA 145

PRO 224 0.27 MET 132 -0.28 SER 79

PRO 224 0.27 ILE 133 -0.36 SER 79

PRO 224 0.29 LEU 134 -0.30 SER 79

PRO 224 0.27 ALA 135 -0.26 SER 79

GLN 195 0.24 ALA 136 -0.33 TRP 81

PRO 224 0.22 TYR 137 -0.32 ASP 80

PRO 105 0.28 HIS 138 -0.23 ASP 80

LYS 198 0.30 PRO 139 -0.18 TRP 81

ASN 202 0.37 GLN 140 -0.18 ASP 80

PRO 116 0.35 GLN 141 -0.16 LEU 281

LEU 199 0.28 PHE 142 -0.18 SER 280

THR 204 0.42 ILE 143 -0.18 SER 79

PRO 33 0.33 TYR 144 -0.19 ALA 166

PRO 224 0.28 ALA 145 -0.24 ALA 166

PRO 224 0.32 GLY 146 -0.27 ALA 166

PRO 224 0.29 SER 147 -0.38 ALA 166

PRO 224 0.35 LEU 148 -0.41 ALA 166

PRO 224 0.28 SER 149 -0.55 ALA 166

PRO 224 0.30 ALA 150 -0.59 ALA 166

PRO 224 0.20 LEU 151 -0.58 ALA 166

SER 109 0.16 LEU 152 -0.44 ALA 166

ILE 133 0.22 ASP 153 -0.54 PHE 239

SER 129 0.21 PRO 154 -0.50 LYS 174

ASN 190 0.26 SER 155 -0.57 ALA 245

THR 101 0.20 GLN 156 -0.65 ALA 242

THR 101 0.20 GLY 157 -0.56 ALA 245

MET 126 0.21 MET 158 -0.46 ALA 245

MET 126 0.25 GLY 159 -0.49 ALA 242

PHE 77 0.22 PRO 160 -0.46 LYS 174

GLU 97 0.15 SER 161 -0.42 LYS 174

LEU 41 0.23 LEU 162 -0.43 SER 235

LEU 162 0.18 ILE 163 -0.53 LEU 151

ALA 175 0.30 GLY 164 -0.39 ALA 242

ALA 175 0.37 LEU 165 -0.63 LEU 228

ALA 175 0.16 ALA 166 -0.59 ALA 150

ILE 223 0.15 MET 167 -0.47 LEU 151

LYS 174 0.21 GLY 168 -0.42 LEU 151

LYS 174 0.17 ASP 169 -0.48 HIS 261

ILE 223 0.30 ALA 170 -0.35 ALA 150

ILE 223 0.28 GLY 171 -0.28 ALA 242

PRO 84 0.12 GLY 172 -0.38 GLY 164

SER 83 0.15 TYR 173 -0.38 ALA 242

GLY 168 0.21 LYS 174 -0.57 ALA 175

LEU 165 0.37 ALA 175 -0.57 LYS 174

LEU 165 0.33 ALA 176 -0.47 ALA 245

LEU 165 0.26 ASP 177 -0.43 ALA 246

LEU 165 0.23 MET 178 -0.45 ASP 191

ASP 80 0.31 TRP 179 -0.46 ALA 246

LEU 165 0.30 GLY 180 -0.48 ALA 245

LEU 165 0.29 PRO 181 -0.49 ALA 245

GLU 97 0.26 SER 182 -0.55 ALA 245

SER 102 0.27 SER 183 -0.62 ALA 245

THR 98 0.33 ASP 184 -0.57 ALA 245

SER 102 0.36 PRO 185 -0.62 ALA 246

GLU 97 0.42 ALA 186 -0.52 ALA 246

GLU 97 0.29 TRP 187 -0.52 ALA 246

ARG 189 0.34 GLU 188 -0.63 ALA 246

GLU 188 0.34 ARG 189 -0.47 GLN 195

SER 155 0.26 ASN 190 -0.42 GLN 195

ILE 133 0.27 ASP 191 -0.45 MET 178

SER 109 0.19 PRO 192 -0.37 LYS 174

ASN 31 0.19 THR 193 -0.54 TYR 243

ALA 136 0.22 GLN 194 -0.62 ALA 246

PRO 139 0.24 GLN 195 -0.48 GLU 188

GLY 118 0.26 ILE 196 -0.43 GLY 248

ALA 242 0.30 PRO 197 -0.46 GLU 188

PRO 139 0.30 LYS 198 -0.40 TYR 82

GLY 118 0.36 LEU 199 -0.35 TRP 81

GLY 118 0.40 VAL 200 -0.36 GLU 188

ASN 31 0.35 ALA 201 -0.35 TYR 82

GLY 118 0.44 ASN 202 -0.29 TRP 81

GLY 118 0.51 ASN 203 -0.28 TRP 81

GLY 118 0.47 THR 204 -0.25 TRP 81

LEU 281 0.41 ARG 205 -0.24 ALA 166

SER 32 0.30 LEU 206 -0.29 ALA 166

SER 32 0.25 TRP 207 -0.32 ALA 166

GLU 58 0.20 VAL 208 -0.38 ALA 166

GLU 58 0.21 TYR 209 -0.41 ALA 166

ARG 2 0.20 CYS 210 -0.45 ALA 166

ARG 2 0.24 GLY 211 -0.40 ALA 166

ARG 2 0.24 ASN 212 -0.39 LEU 165

ARG 2 0.27 GLY 213 -0.40 LEU 165

ARG 2 0.31 THR 214 -0.34 LEU 165

ARG 2 0.38 PRO 215 -0.36 LEU 165

ARG 2 0.39 ASN 216 -0.32 LEU 165

ARG 2 0.47 GLU 217 -0.40 ALA 221

ARG 2 0.50 LEU 218 -0.33 LEU 165

ARG 2 0.47 GLY 219 -0.36 LEU 165

ARG 2 0.44 GLY 220 -0.42 LEU 165

ARG 2 0.45 ALA 221 -0.40 GLU 217

ASN 53 0.54 ASN 222 -0.30 LEU 165

ARG 42 0.56 ILE 223 -0.25 GLU 217

GLY 40 0.68 PRO 224 -0.32 LEU 165

TRP 263 0.40 ALA 225 -0.47 LEU 165

ARG 2 0.30 GLU 226 -0.42 LEU 165

GLY 40 0.29 PHE 227 -0.45 LEU 165

SER 125 0.36 LEU 228 -0.63 LEU 165

ARG 2 0.22 GLU 229 -0.53 LEU 165

ARG 2 0.20 ASN 230 -0.46 LEU 165

ARG 2 0.16 PHE 231 -0.53 LEU 165

GLU 58 0.15 VAL 232 -0.56 ALA 166

ARG 2 0.17 ARG 233 -0.46 LEU 165

SER 32 0.16 SER 234 -0.45 LEU 165

ASN 31 0.17 SER 235 -0.48 ALA 166

SER 32 0.19 ASN 236 -0.45 ALA 166

SER 32 0.20 LEU 237 -0.40 LEU 165

PHE 239 0.25 LYS 238 -0.50 GLN 156

LYS 238 0.25 PHE 239 -0.54 ASP 153

ASN 31 0.26 GLN 240 -0.37 ALA 166

ASN 31 0.27 ASP 241 -0.52 GLN 156

PRO 197 0.30 ALA 242 -0.65 GLN 156

ASN 31 0.31 TYR 243 -0.54 THR 193

SER 280 0.34 ASN 244 -0.46 GLN 156

SER 280 0.36 ALA 245 -0.63 GLN 156

ASN 31 0.35 ALA 246 -0.63 GLU 188

GLY 282 0.41 GLY 247 -0.52 GLU 188

SER 280 0.46 GLY 248 -0.46 GLU 188

SER 280 0.48 HIS 249 -0.40 GLU 188

SER 280 0.62 ASN 250 -0.30 GLU 188

SER 280 0.37 ALA 251 -0.32 ALA 166

MET 273 0.28 VAL 252 -0.32 ALA 166

GLU 58 0.24 PHE 253 -0.36 ALA 166

ARG 2 0.25 ASN 254 -0.36 ALA 166

ARG 2 0.22 PHE 255 -0.36 ALA 166

ARG 2 0.24 PRO 256 -0.32 LEU 165

ARG 2 0.24 PRO 257 -0.31 LEU 165

ARG 2 0.28 ASN 258 -0.34 LEU 165

ARG 2 0.30 GLY 259 -0.38 LEU 165

ARG 2 0.30 THR 260 -0.44 LEU 165

PRO 224 0.38 HIS 261 -0.53 ALA 166

PRO 224 0.44 SER 262 -0.43 ASP 169

PRO 224 0.51 TRP 263 -0.32 ASP 169

PRO 55 0.44 GLU 264 -0.31 ASP 169

ARG 2 0.35 TYR 265 -0.34 ALA 166

PRO 224 0.35 TRP 266 -0.34 ALA 166

PRO 224 0.36 GLY 267 -0.25 ALA 166

LEU 218 0.39 ALA 268 -0.26 ALA 166

LEU 218 0.31 GLN 269 -0.30 ALA 166

PRO 224 0.31 LEU 270 -0.26 ALA 166

LEU 218 0.40 ASN 271 -0.24 ALA 166

GLU 217 0.38 ALA 272 -0.26 ALA 166

LEU 218 0.30 MET 273 -0.25 ALA 166

GLU 217 0.31 LYS 274 -0.22 ALA 166

ASN 250 0.31 GLY 275 -0.23 ALA 166

ASN 250 0.40 ASP 276 -0.24 ALA 166

ASN 250 0.44 LEU 277 -0.21 ALA 166

ASN 250 0.44 GLN 278 -0.19 ALA 166

ASN 250 0.52 SER 279 -0.20 ALA 166

ASN 250 0.62 SER 280 -0.19 ALA 166

ASN 250 0.54 LEU 281 -0.21 SER 119

ASN 250 0.51 GLY 282 -0.15 SER 119

ASN 250 0.42 ALA 283 -0.15 ALA 166

ASN 250 0.36 GLY 284 -0.14 ALA 166

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 14 ---

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

* 1F0N_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000 *