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

* EXP_1F0N_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000 *

CA distance fluctuations for 24021912142413056

--- 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
ALA 89 0.47 SER 1 -0.16 ALA 166

ALA 89 0.48 ARG 2 -0.16 VAL 7

ILE 52 0.67 PRO 3 -0.14 GLY 29

ALA 89 0.57 GLY 4 -0.23 GLY 29

ALA 89 0.45 LEU 5 -0.19 GLY 29

ALA 89 0.44 PRO 6 -0.20 GLY 29

ALA 89 0.48 VAL 7 -0.17 ALA 166

ALA 89 0.49 GLU 8 -0.16 ALA 166

ALA 89 0.56 TYR 9 -0.16 ASN 222

ALA 89 0.50 LEU 10 -0.18 ASN 222

ALA 89 0.48 GLN 11 -0.18 ASN 222

ALA 89 0.37 VAL 12 -0.22 ASN 222

GLN 140 0.39 PRO 13 -0.23 ASN 222

GLN 140 0.42 SER 14 -0.26 PRO 224

GLN 140 0.42 PRO 15 -0.25 PRO 224

GLN 140 0.39 SER 16 -0.27 PRO 224

GLN 140 0.36 MET 17 -0.27 PRO 224

GLN 140 0.35 GLY 18 -0.24 ILE 223

GLN 140 0.35 ARG 19 -0.27 ASP 45

GLN 140 0.36 ASP 20 -0.31 ASP 45

ALA 89 0.49 ILE 21 -0.23 ASN 222

ALA 89 0.62 LYS 22 -0.21 ASN 222

ALA 89 0.55 VAL 23 -0.22 ASN 222

ALA 89 0.55 GLN 24 -0.22 ALA 166

ALA 89 0.45 PHE 25 -0.23 ALA 166

ALA 89 0.40 GLN 26 -0.24 LEU 218

ALA 89 0.34 SER 27 -0.26 LEU 218

ALA 89 0.31 GLY 28 -0.29 LEU 218

ALA 89 0.28 GLY 29 -0.27 GLU 217

ASN 250 0.25 ASN 30 -0.25 GLU 217

ASN 250 0.28 ASN 31 -0.26 LEU 218

ASN 250 0.32 SER 32 -0.29 LEU 218

ASN 250 0.37 PRO 33 -0.31 LEU 218

ASN 250 0.37 ALA 34 -0.32 LEU 218

ASN 250 0.41 VAL 35 -0.34 LEU 218

ALA 89 0.41 TYR 36 -0.34 PRO 224

ALA 89 0.46 LEU 37 -0.32 PRO 224

ALA 89 0.50 LEU 38 -0.36 PRO 224

ALA 89 0.53 ASP 39 -0.38 ALA 166

ALA 150 0.47 GLY 40 -0.52 ALA 166

LEU 151 0.53 LEU 41 -0.45 ALA 166

LYS 88 0.52 ARG 42 -0.36 ALA 43

ALA 89 0.63 ALA 43 -0.36 ARG 42

ALA 89 0.87 GLN 44 -0.27 ASP 20

ALA 89 1.07 ASP 45 -0.31 ASP 20

ALA 89 0.91 ASP 46 -0.26 ASP 20

ALA 89 0.75 TYR 47 -0.23 ALA 166

ALA 89 0.64 ASN 48 -0.29 ALA 166

ALA 89 0.56 GLY 49 -0.40 ALA 166

ALA 89 0.49 TRP 50 -0.36 ALA 166

PRO 3 0.52 ASP 51 -0.30 ALA 166

PRO 3 0.67 ILE 52 -0.35 ALA 166

PRO 3 0.60 ASN 53 -0.42 ALA 166

PRO 3 0.49 THR 54 -0.35 ALA 166

SER 1 0.39 PRO 55 -0.28 ALA 166

ALA 89 0.39 ALA 56 -0.34 LEU 218

ALA 89 0.41 PHE 57 -0.27 LEU 218

ALA 89 0.37 GLU 58 -0.29 GLU 217

ALA 89 0.32 TRP 59 -0.41 LEU 218

ALA 89 0.34 TYR 60 -0.36 LEU 218

ALA 89 0.35 TYR 61 -0.30 GLU 217

ALA 89 0.32 GLN 62 -0.32 GLU 217

ALA 89 0.30 SER 63 -0.37 GLU 217

ALA 89 0.29 GLY 64 -0.33 GLU 217

ASN 250 0.34 LEU 65 -0.34 LEU 218

ALA 89 0.34 SER 66 -0.31 LEU 218

ALA 89 0.39 ILE 67 -0.31 LEU 218

ALA 89 0.43 VAL 68 -0.27 ASN 222

ALA 89 0.52 MET 69 -0.27 ASN 222

ALA 89 0.57 PRO 70 -0.26 ASN 222

ALA 89 0.71 VAL 71 -0.23 ASN 222

ALA 89 0.80 GLY 72 -0.27 ASP 20

ALA 89 0.59 GLY 73 -0.27 PRO 224

ALA 89 0.49 GLN 74 -0.27 ILE 223

LEU 151 0.37 SER 75 -0.40 PRO 224

PRO 192 0.33 SER 76 -0.39 PRO 224

PRO 192 0.36 PHE 77 -0.45 PRO 224

ALA 89 0.38 TYR 78 -0.37 PRO 224

GLN 195 0.33 SER 79 -0.38 PRO 224

ALA 136 0.28 ASP 80 -0.34 PRO 224

GLN 195 0.22 TRP 81 -0.33 PRO 224

LEU 165 0.21 TYR 82 -0.30 PRO 224

LEU 165 0.21 SER 83 -0.27 PRO 181

PRO 3 0.19 PRO 84 -0.24 PRO 224

PRO 3 0.22 ALA 85 -0.27 PRO 224

PRO 3 0.30 CYS 86 -0.29 PRO 181

ASP 45 0.39 GLY 87 -0.32 SER 161

ASP 45 0.81 LYS 88 -0.29 SER 161

ASP 45 1.07 ALA 89 -0.21 SER 161

ASP 45 0.73 GLY 90 -0.26 PRO 181

PRO 3 0.33 CYS 91 -0.23 PRO 181

ALA 135 0.28 GLN 92 -0.21 ILE 223

ALA 136 0.27 THR 93 -0.25 PRO 224

ALA 136 0.32 TYR 94 -0.29 PRO 224

ALA 136 0.35 LYS 95 -0.30 PRO 224

ALA 135 0.41 TRP 96 -0.33 PRO 224

TRP 96 0.41 GLU 97 -0.35 PRO 224

GLN 140 0.38 THR 98 -0.32 PRO 224

GLN 140 0.41 PHE 99 -0.30 PRO 224

ALA 135 0.48 LEU 100 -0.32 PRO 224

GLN 140 0.50 THR 101 -0.33 PRO 224

GLN 140 0.53 SER 102 -0.31 PRO 224

GLN 140 0.51 GLU 103 -0.28 PRO 224

GLN 140 0.44 LEU 104 -0.28 PRO 224

GLN 140 0.43 PRO 105 -0.28 PRO 224

GLN 140 0.42 GLN 106 -0.26 PRO 224

GLN 140 0.35 TRP 107 -0.24 PRO 224

ASN 203 0.33 LEU 108 -0.25 PRO 224

ASN 203 0.29 SER 109 -0.25 PRO 224

ASN 203 0.25 ALA 110 -0.23 PRO 224

ALA 89 0.28 ASN 111 -0.20 PRO 224

ALA 89 0.30 ARG 112 -0.21 LEU 218

ASN 250 0.26 ALA 113 -0.24 LEU 218

ASN 250 0.30 VAL 114 -0.26 LEU 218

ASN 203 0.31 LYS 115 -0.28 PRO 224

ASN 203 0.34 PRO 116 -0.30 PRO 224

ASN 203 0.37 THR 117 -0.29 PRO 224

ASN 203 0.45 GLY 118 -0.28 LEU 218

ASN 250 0.39 SER 119 -0.31 LEU 218

ASN 250 0.41 ALA 120 -0.36 TRP 266

ALA 89 0.42 ALA 121 -0.33 PRO 224

ALA 89 0.42 ILE 122 -0.42 TRP 266

ALA 89 0.45 GLY 123 -0.36 PRO 224

ALA 89 0.40 LEU 124 -0.45 PRO 224

GLY 40 0.46 SER 125 -0.58 PRO 224

LEU 41 0.50 MET 126 -0.53 PRO 224

ALA 89 0.45 ALA 127 -0.44 PRO 224

ALA 89 0.37 GLY 128 -0.46 PRO 224

PHE 239 0.34 SER 129 -0.44 PRO 224

ALA 89 0.38 SER 130 -0.41 PRO 224

ALA 89 0.44 ALA 131 -0.38 PRO 224

ALA 89 0.37 MET 132 -0.35 PRO 224

TRP 96 0.36 ILE 133 -0.36 PRO 224

TRP 96 0.40 LEU 134 -0.34 PRO 224

LEU 100 0.48 ALA 135 -0.32 PRO 224

TRP 96 0.40 ALA 136 -0.30 PRO 224

TRP 96 0.36 TYR 137 -0.30 PRO 224

LEU 100 0.40 HIS 138 -0.29 PRO 224

ASN 202 0.42 PRO 139 -0.32 PRO 224

SER 102 0.53 GLN 140 -0.43 ILE 143

ASN 203 0.44 GLN 141 -0.29 PRO 224

THR 204 0.55 PHE 142 -0.32 PRO 224

THR 204 0.45 ILE 143 -0.43 GLN 140

ALA 120 0.41 TYR 144 -0.30 PRO 224

ALA 89 0.41 ALA 145 -0.30 PRO 224

ALA 89 0.40 GLY 146 -0.34 PRO 224

ALA 89 0.40 SER 147 -0.33 PRO 224

ALA 89 0.37 LEU 148 -0.38 PRO 224

ARG 42 0.40 SER 149 -0.36 PRO 224

LEU 41 0.51 ALA 150 -0.41 PRO 224

LEU 41 0.53 LEU 151 -0.46 PRO 224

LEU 41 0.46 LEU 152 -0.36 PRO 224

LEU 41 0.35 ASP 153 -0.38 PRO 224

ALA 170 0.32 PRO 154 -0.48 PRO 224

ALA 170 0.21 SER 155 -0.41 PRO 224

ALA 170 0.20 GLN 156 -0.38 PRO 224

SER 234 0.31 GLY 157 -0.35 PRO 224

SER 234 0.23 MET 158 -0.47 PRO 224

ALA 170 0.23 GLY 159 -0.55 PRO 224

SER 182 0.17 PRO 160 -0.55 PRO 224

SER 182 0.28 SER 161 -0.65 PRO 224

ALA 166 0.35 LEU 162 -0.82 PRO 224

ALA 170 0.24 ILE 163 -0.75 PRO 224

PRO 181 0.34 GLY 164 -0.70 PRO 224

PRO 181 0.41 LEU 165 -0.93 PRO 224

LEU 162 0.35 ALA 166 -0.78 PRO 224

PHE 231 0.23 MET 167 -0.52 PRO 224

PRO 3 0.17 GLY 168 -0.46 PRO 224

PHE 231 0.36 ASP 169 -0.42 ILE 223

PHE 231 0.49 ALA 170 -0.28 ILE 223

VAL 232 0.40 GLY 171 -0.18 ILE 223

PRO 3 0.27 GLY 172 -0.34 SER 161

PRO 3 0.22 TYR 173 -0.35 PRO 224

LEU 165 0.28 LYS 174 -0.47 SER 161

LEU 165 0.40 ALA 175 -0.47 PRO 224

LEU 165 0.38 ALA 176 -0.40 PRO 224

LEU 165 0.30 ASP 177 -0.34 PRO 224

LEU 165 0.22 MET 178 -0.38 PRO 224

LEU 165 0.27 TRP 179 -0.38 PRO 224

LEU 165 0.36 GLY 180 -0.34 PRO 224

LEU 165 0.41 PRO 181 -0.33 PRO 224

LEU 165 0.30 SER 182 -0.38 PRO 224

LEU 165 0.26 SER 183 -0.32 PRO 224

LEU 165 0.26 ASP 184 -0.32 PRO 224

LEU 165 0.20 PRO 185 -0.31 PRO 224

LEU 165 0.19 ALA 186 -0.36 PRO 224

LEU 165 0.18 TRP 187 -0.39 PRO 224

ALA 170 0.18 GLU 188 -0.35 PRO 224

TYR 94 0.19 ARG 189 -0.34 PRO 224

SER 79 0.26 ASN 190 -0.39 PRO 224

SER 75 0.30 ASP 191 -0.36 PRO 224

PHE 77 0.36 PRO 192 -0.34 PRO 224

LEU 41 0.32 THR 193 -0.30 PRO 224

LEU 41 0.25 GLN 194 -0.29 PRO 224

SER 79 0.33 GLN 195 -0.30 PRO 224

TRP 96 0.33 ILE 196 -0.26 PRO 224

TRP 96 0.30 PRO 197 -0.24 PRO 224

TRP 96 0.34 LYS 198 -0.27 PRO 224

LEU 100 0.41 LEU 199 -0.27 PRO 224

LEU 100 0.36 VAL 200 -0.26 PRO 224

LEU 100 0.32 ALA 201 -0.25 PRO 224

PRO 139 0.42 ASN 202 -0.27 PRO 224

PHE 142 0.47 ASN 203 -0.26 TYR 209

PHE 142 0.55 THR 204 -0.28 ARG 205

ASN 250 0.47 ARG 205 -0.28 THR 204

ILE 122 0.39 LEU 206 -0.33 TYR 209

ALA 89 0.38 TRP 207 -0.30 TYR 209

ALA 89 0.37 VAL 208 -0.41 TYR 209

ALA 89 0.35 TYR 209 -0.41 VAL 208

ALA 89 0.33 CYS 210 -0.24 VAL 208

ALA 89 0.30 GLY 211 -0.26 ASN 250

ARG 42 0.27 ASN 212 -0.26 HIS 249

ALA 89 0.23 GLY 213 -0.31 LEU 165

ILE 223 0.25 THR 214 -0.30 LEU 165

ILE 223 0.25 PRO 215 -0.37 ALA 272

ALA 221 0.25 ASN 216 -0.45 ALA 272

ALA 221 0.44 GLU 217 -0.55 ALA 272

GLY 219 0.31 LEU 218 -0.57 ALA 272

LEU 218 0.31 GLY 219 -0.39 LEU 165

PRO 3 0.23 GLY 220 -0.46 LEU 165

GLU 217 0.44 ALA 221 -0.55 LEU 165

GLU 217 0.31 ASN 222 -0.69 LEU 165

GLU 217 0.28 ILE 223 -0.80 LEU 165

GLU 217 0.21 PRO 224 -0.93 LEU 165

PRO 3 0.28 ALA 225 -0.65 LEU 165

PRO 3 0.23 GLU 226 -0.48 LEU 165

PRO 3 0.25 PHE 227 -0.44 LEU 165

ARG 42 0.43 LEU 228 -0.53 LEU 162

ARG 42 0.39 GLU 229 -0.32 LEU 162

ARG 42 0.36 ASN 230 -0.26 HIS 249

ALA 170 0.49 PHE 231 -0.28 LYS 238

ARG 42 0.51 VAL 232 -0.29 SER 235

ARG 42 0.41 ARG 233 -0.28 HIS 249

LEU 41 0.39 SER 234 -0.30 LEU 237

LEU 41 0.41 SER 235 -0.30 LEU 228

LEU 41 0.40 ASN 236 -0.27 HIS 249

LEU 41 0.35 LEU 237 -0.30 SER 234

LEU 41 0.34 LYS 238 -0.28 PHE 231

LEU 41 0.36 PHE 239 -0.25 VAL 232

GLY 128 0.34 GLN 240 -0.29 HIS 249

GLY 128 0.30 ASP 241 -0.24 SER 234

LEU 41 0.29 ALA 242 -0.23 PHE 231

LEU 37 0.32 TYR 243 -0.21 PRO 224

LEU 37 0.31 ASN 244 -0.21 SER 234

SER 280 0.30 ALA 245 -0.19 PHE 231

LEU 100 0.30 ALA 246 -0.19 PRO 224

PHE 142 0.34 GLY 247 -0.18 PHE 231

PHE 142 0.40 GLY 248 -0.20 SER 234

SER 280 0.42 HIS 249 -0.32 PHE 255

SER 280 0.51 ASN 250 -0.41 ALA 251

LEU 37 0.37 ALA 251 -0.41 ASN 250

ALA 89 0.33 VAL 252 -0.32 PHE 255

ALA 89 0.33 PHE 253 -0.34 ASN 250

ALA 89 0.32 ASN 254 -0.29 PRO 256

ALA 89 0.30 PHE 255 -0.33 ASN 250

ALA 89 0.28 PRO 256 -0.31 VAL 252

ALA 89 0.24 PRO 257 -0.28 ASN 250

ALA 89 0.24 ASN 258 -0.30 ALA 272

ALA 89 0.26 GLY 259 -0.33 ALA 272

PRO 3 0.27 THR 260 -0.39 LEU 165

PRO 3 0.33 HIS 261 -0.46 LEU 165

PRO 3 0.37 SER 262 -0.50 LEU 165

PRO 3 0.39 TRP 263 -0.48 ALA 166

PRO 3 0.34 GLU 264 -0.40 LEU 165

ALA 89 0.29 TYR 265 -0.38 GLN 269

PRO 3 0.34 TRP 266 -0.42 ILE 122

PRO 3 0.34 GLY 267 -0.38 LEU 218

ALA 89 0.28 ALA 268 -0.56 LEU 218

ALA 89 0.32 GLN 269 -0.42 LEU 218

ALA 89 0.35 LEU 270 -0.43 LEU 218

ALA 89 0.31 ASN 271 -0.54 LEU 218

ALA 89 0.28 ALA 272 -0.57 LEU 218

VAL 252 0.32 MET 273 -0.44 LEU 218

ALA 89 0.31 LYS 274 -0.44 LEU 218

ALA 89 0.28 GLY 275 -0.45 GLU 217

ASN 250 0.34 ASP 276 -0.40 GLU 217

ASN 250 0.42 LEU 277 -0.39 LEU 218

ASN 250 0.37 GLN 278 -0.38 GLU 217

ASN 250 0.40 SER 279 -0.37 GLU 217

ASN 250 0.51 SER 280 -0.33 GLU 217

ASN 250 0.46 LEU 281 -0.33 GLU 217

ASN 250 0.38 GLY 282 -0.33 GLU 217

ASN 250 0.33 ALA 283 -0.35 GLU 217

ALA 89 0.25 GLY 284 -0.38 GLU 217

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_1F0N_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000 ***

CA distance fluctuations for 24021912142413056

--- normal mode 16 ---

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

* EXP_1F0N_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000 *