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 13 ---

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
LEU 5 0.37 SER 1 -0.68 TYR 47

TRP 59 0.46 ARG 2 -0.91 ASP 46

GLY 275 0.19 PRO 3 -1.51 ASP 20

GLY 284 0.43 GLY 4 -1.10 TYR 9

SER 1 0.37 LEU 5 -0.52 TYR 9

SER 1 0.23 PRO 6 -0.32 GLN 11

LYS 88 0.18 VAL 7 -0.46 PRO 3

ALA 89 0.18 GLU 8 -0.77 GLY 4

ALA 89 0.22 TYR 9 -1.10 GLY 4

ALA 89 0.17 LEU 10 -1.16 PRO 3

ALA 89 0.15 GLN 11 -1.40 PRO 3

ALA 89 0.10 VAL 12 -1.23 PRO 3

SER 102 0.10 PRO 13 -1.27 PRO 3

THR 98 0.11 SER 14 -1.20 PRO 3

ARG 189 0.14 PRO 15 -1.14 PRO 3

ALA 186 0.17 SER 16 -1.06 PRO 3

ALA 186 0.15 MET 17 -1.18 PRO 3

ALA 186 0.15 GLY 18 -1.26 PRO 3

ALA 186 0.11 ARG 19 -1.42 PRO 3

PRO 13 0.10 ASP 20 -1.51 PRO 3

ALA 89 0.12 ILE 21 -1.39 PRO 3

ALA 89 0.21 LYS 22 -1.41 PRO 3

ALA 89 0.20 VAL 23 -1.09 PRO 3

ALA 89 0.22 GLN 24 -0.90 PRO 3

ALA 89 0.20 PHE 25 -0.66 PRO 3

LYS 88 0.18 GLN 26 -0.39 PRO 3

ALA 89 0.17 SER 27 -0.28 PRO 3

TYR 61 0.26 GLY 28 -0.20 GLY 64

TYR 61 0.23 GLY 29 -0.20 GLY 284

TYR 61 0.17 ASN 30 -0.22 GLY 284

TYR 61 0.17 ASN 31 -0.19 PRO 3

GLN 62 0.23 SER 32 -0.16 PRO 3

GLU 58 0.21 PRO 33 -0.24 PRO 3

GLU 58 0.18 ALA 34 -0.37 PRO 3

GLU 58 0.21 VAL 35 -0.36 PRO 3

LEU 41 0.18 TYR 36 -0.54 PRO 3

ARG 42 0.22 LEU 37 -0.53 PRO 3

LEU 41 0.26 LEU 38 -0.65 PRO 3

LYS 88 0.25 ASP 39 -0.67 PRO 3

LEU 41 0.39 GLY 40 -0.60 PRO 3

GLY 40 0.39 LEU 41 -0.63 PRO 3

GLY 49 0.35 ARG 42 -0.69 PRO 3

LYS 88 0.35 ALA 43 -0.82 PRO 3

ALA 89 0.49 GLN 44 -0.97 PRO 3

ALA 89 0.43 ASP 45 -1.22 PRO 3

ALA 89 0.40 ASP 46 -1.21 PRO 3

ALA 89 0.35 TYR 47 -1.02 PRO 3

ALA 89 0.30 ASN 48 -0.84 PRO 3

LYS 88 0.36 GLY 49 -0.64 PRO 3

LYS 88 0.30 TRP 50 -0.48 PRO 3

LYS 88 0.25 ASP 51 -0.65 SER 1

LYS 88 0.33 ILE 52 -0.63 SER 1

LYS 88 0.33 ASN 53 -0.39 LEU 218

ASP 169 0.28 THR 54 -0.25 LEU 218

ASP 169 0.25 PRO 55 -0.17 TYR 9

ALA 170 0.26 ALA 56 -0.16 SER 1

LYS 88 0.21 PHE 57 -0.22 TYR 9

TRP 59 0.75 GLU 58 -0.29 TYR 9

GLU 58 0.75 TRP 59 -0.15 TYR 9

GLU 58 0.51 TYR 60 -0.21 VAL 7

ARG 2 0.34 TYR 61 -0.24 VAL 7

GLY 4 0.41 GLN 62 -0.27 PRO 6

ARG 2 0.40 SER 63 -0.14 VAL 7

GLN 62 0.38 GLY 64 -0.20 GLY 28

GLU 58 0.29 LEU 65 -0.11 PRO 3

GLU 58 0.19 SER 66 -0.29 PRO 3

LYS 88 0.19 ILE 67 -0.39 PRO 3

ALA 89 0.19 VAL 68 -0.62 PRO 3

ALA 89 0.22 MET 69 -0.76 PRO 3

ALA 89 0.21 PRO 70 -0.97 PRO 3

ALA 89 0.26 VAL 71 -1.13 PRO 3

ALA 89 0.29 GLY 72 -1.13 PRO 3

ALA 89 0.20 GLY 73 -0.99 PRO 3

LYS 88 0.22 GLN 74 -0.88 PRO 3

MET 126 0.23 SER 75 -0.76 PRO 3

ALA 150 0.14 SER 76 -0.82 PRO 3

ALA 150 0.13 PHE 77 -0.70 PRO 3

ALA 89 0.09 TYR 78 -0.78 PRO 3

ASN 190 0.12 SER 79 -0.77 PRO 3

ALA 186 0.14 ASP 80 -0.82 PRO 3

THR 93 0.16 TRP 81 -0.81 PRO 3

THR 93 0.18 TYR 82 -0.76 PRO 3

SER 161 0.20 SER 83 -0.81 PRO 3

SER 161 0.17 PRO 84 -0.90 PRO 3

VAL 232 0.18 ALA 85 -0.89 PRO 3

GLN 44 0.23 CYS 86 -0.85 PRO 3

GLN 44 0.31 GLY 87 -0.80 PRO 3

GLN 44 0.44 LYS 88 -0.74 PRO 3

GLN 44 0.49 ALA 89 -0.88 PRO 3

GLN 44 0.35 GLY 90 -0.92 PRO 3

GLN 44 0.22 CYS 91 -0.97 PRO 3

PRO 84 0.14 GLN 92 -1.08 PRO 3

TYR 82 0.18 THR 93 -1.06 PRO 3

TRP 81 0.15 TYR 94 -1.00 PRO 3

ALA 186 0.14 LYS 95 -0.96 PRO 3

GLU 188 0.08 TRP 96 -0.94 PRO 3

SER 16 0.10 GLU 97 -0.80 PRO 3

PRO 15 0.13 THR 98 -0.86 PRO 3

SER 14 0.08 PHE 99 -0.95 PRO 3

LEU 41 0.07 LEU 100 -0.82 PRO 3

PRO 13 0.08 THR 101 -0.72 PRO 3

PRO 13 0.10 SER 102 -0.78 PRO 3

PRO 13 0.10 GLU 103 -0.91 PRO 3

LEU 41 0.08 LEU 104 -0.89 PRO 3

LEU 41 0.08 PRO 105 -0.69 PRO 3

ASP 20 0.08 GLN 106 -0.72 PRO 3

VAL 12 0.08 TRP 107 -0.82 PRO 3

ALA 89 0.11 LEU 108 -0.69 PRO 3

ARG 42 0.09 SER 109 -0.55 PRO 3

GLN 11 0.09 ALA 110 -0.62 PRO 3

LYS 22 0.12 ASN 111 -0.65 PRO 3

ALA 89 0.14 ARG 112 -0.52 PRO 3

ALA 89 0.12 ALA 113 -0.38 PRO 3

ALA 89 0.12 VAL 114 -0.40 PRO 3

GLU 58 0.13 LYS 115 -0.37 PRO 3

GLU 58 0.11 PRO 116 -0.48 PRO 3

GLU 58 0.14 THR 117 -0.38 PRO 3

GLU 58 0.20 GLY 118 -0.27 PRO 3

GLU 58 0.20 SER 119 -0.33 PRO 3

GLU 58 0.21 ALA 120 -0.33 PRO 3

ALA 170 0.16 ALA 121 -0.44 PRO 3

ALA 170 0.23 ILE 122 -0.39 PRO 3

ALA 170 0.27 GLY 123 -0.46 PRO 3

ALA 166 0.36 LEU 124 -0.42 PRO 3

ALA 166 0.46 SER 125 -0.45 PRO 3

ALA 166 0.34 MET 126 -0.55 PRO 3

ALA 166 0.23 ALA 127 -0.57 PRO 3

ALA 166 0.28 GLY 128 -0.44 PRO 3

ALA 166 0.20 SER 129 -0.47 PRO 3

ALA 166 0.13 SER 130 -0.57 PRO 3

ALA 166 0.16 ALA 131 -0.49 PRO 3

ALA 166 0.15 MET 132 -0.42 PRO 3

SER 16 0.10 ILE 133 -0.50 PRO 3

GLU 58 0.09 LEU 134 -0.54 PRO 3

GLU 217 0.15 ALA 135 -0.42 PRO 3

GLU 217 0.15 ALA 136 -0.41 PRO 3

GLU 217 0.11 TYR 137 -0.49 PRO 3

GLU 217 0.11 HIS 138 -0.49 PRO 3

GLU 217 0.17 PRO 139 -0.37 PRO 3

GLU 217 0.17 GLN 140 -0.36 PRO 3

GLU 217 0.13 GLN 141 -0.44 PRO 3

GLU 58 0.16 PHE 142 -0.39 PRO 3

GLU 217 0.21 ILE 143 -0.27 PRO 3

GLU 217 0.23 TYR 144 -0.25 PRO 3

GLU 217 0.20 ALA 145 -0.31 PRO 3

ALA 166 0.25 GLY 146 -0.27 PRO 3

ALA 166 0.31 SER 147 -0.32 PRO 3

ALA 166 0.38 LEU 148 -0.28 PRO 3

ALA 166 0.49 SER 149 -0.30 PRO 3

ALA 166 0.49 ALA 150 -0.38 PRO 3

ALA 166 0.39 LEU 151 -0.39 PRO 3

ALA 166 0.26 LEU 152 -0.37 PRO 3

LYS 238 0.19 ASP 153 -0.39 PRO 3

ALA 175 0.20 PRO 154 -0.46 PRO 3

SER 234 0.19 SER 155 -0.46 PRO 3

LYS 238 0.24 GLN 156 -0.40 PRO 3

SER 182 0.31 GLY 157 -0.39 PRO 3

SER 182 0.29 MET 158 -0.43 PRO 3

SER 234 0.36 GLY 159 -0.46 PRO 3

SER 234 0.28 PRO 160 -0.50 PRO 3

ALA 176 0.36 SER 161 -0.48 PRO 3

SER 234 0.34 LEU 162 -0.49 PRO 3

VAL 232 0.42 ILE 163 -0.54 PRO 3

VAL 232 0.35 GLY 164 -0.55 PRO 3

LEU 228 0.55 LEU 165 -0.50 PRO 3

LEU 228 0.53 ALA 166 -0.52 PRO 3

ALA 150 0.37 MET 167 -0.63 PRO 3

LEU 228 0.42 GLY 168 -0.60 PRO 3

LEU 228 0.53 ASP 169 -0.55 PRO 3

SER 125 0.37 ALA 170 -0.65 PRO 3

GLY 49 0.32 GLY 171 -0.75 PRO 3

LEU 228 0.32 GLY 172 -0.70 PRO 3

VAL 232 0.28 TYR 173 -0.73 PRO 3

SER 161 0.32 LYS 174 -0.68 PRO 3

SER 161 0.30 ALA 175 -0.64 PRO 3

SER 161 0.36 ALA 176 -0.65 PRO 3

SER 161 0.27 ASP 177 -0.73 PRO 3

SER 234 0.20 MET 178 -0.73 PRO 3

SER 234 0.19 TRP 179 -0.65 PRO 3

SER 161 0.22 GLY 180 -0.63 PRO 3

MET 158 0.26 PRO 181 -0.57 PRO 3

GLY 157 0.31 SER 182 -0.53 PRO 3

GLY 157 0.29 SER 183 -0.50 PRO 3

GLY 157 0.19 ASP 184 -0.54 PRO 3

SER 16 0.15 PRO 185 -0.52 PRO 3

SER 16 0.17 ALA 186 -0.57 PRO 3

SER 234 0.16 TRP 187 -0.53 PRO 3

SER 16 0.16 GLU 188 -0.47 PRO 3

SER 16 0.16 ARG 189 -0.52 PRO 3

SER 16 0.15 ASN 190 -0.54 PRO 3

SER 16 0.13 ASP 191 -0.46 PRO 3

GLU 217 0.12 PRO 192 -0.40 PRO 3

GLU 217 0.14 THR 193 -0.34 PRO 3

SER 16 0.13 GLN 194 -0.37 PRO 3

GLU 217 0.14 GLN 195 -0.38 PRO 3

GLU 217 0.19 ILE 196 -0.30 PRO 3

GLU 217 0.20 PRO 197 -0.28 PRO 3

GLU 217 0.19 LYS 198 -0.32 PRO 3

GLU 217 0.22 LEU 199 -0.29 PRO 3

GLU 217 0.27 VAL 200 -0.21 PRO 3

GLU 217 0.25 ALA 201 -0.23 PRO 3

GLU 217 0.24 ASN 202 -0.25 PRO 3

GLU 217 0.29 ASN 203 -0.18 PRO 3

GLU 217 0.27 THR 204 -0.22 PRO 3

GLU 217 0.32 ARG 205 -0.15 PRO 3

GLU 217 0.32 LEU 206 -0.18 PRO 3

GLU 217 0.33 TRP 207 -0.15 PRO 3

GLU 217 0.30 VAL 208 -0.18 PRO 3

ALA 166 0.36 TYR 209 -0.17 PRO 3

ALA 166 0.40 CYS 210 -0.18 PRO 3

ALA 166 0.36 GLY 211 -0.17 ASP 51

LEU 165 0.36 ASN 212 -0.15 ASP 51

LEU 165 0.33 GLY 213 -0.16 PRO 3

LEU 165 0.26 THR 214 -0.18 ILE 52

ASN 254 0.28 PRO 215 -0.22 ILE 52

ASN 254 0.42 ASN 216 -0.24 ASN 53

ASN 254 0.50 GLU 217 -0.36 GLY 219

ALA 272 0.43 LEU 218 -0.39 ASN 53

ALA 272 0.29 GLY 219 -0.36 GLU 217

ALA 272 0.19 GLY 220 -0.32 GLN 44

ASN 254 0.19 ALA 221 -0.32 GLN 44

THR 214 0.14 ASN 222 -0.34 GLN 44

THR 214 0.17 ILE 223 -0.31 LEU 41

ASP 169 0.23 PRO 224 -0.39 LEU 41

ASP 169 0.36 ALA 225 -0.29 PRO 3

ASP 169 0.32 GLU 226 -0.22 PRO 3

LEU 165 0.43 PHE 227 -0.26 PRO 3

LEU 165 0.55 LEU 228 -0.30 PRO 3

ALA 166 0.49 GLU 229 -0.25 PRO 3

LEU 165 0.47 ASN 230 -0.22 PRO 3

LEU 165 0.52 PHE 231 -0.27 PRO 3

ALA 166 0.52 VAL 232 -0.29 PRO 3

ALA 166 0.42 ARG 233 -0.22 PRO 3

LEU 165 0.39 SER 234 -0.23 PRO 3

ALA 166 0.34 SER 235 -0.28 PRO 3

ALA 166 0.33 ASN 236 -0.24 PRO 3

ALA 166 0.30 LEU 237 -0.19 PRO 3

GLN 156 0.24 LYS 238 -0.23 PRO 3

ALA 166 0.22 PHE 239 -0.25 PRO 3

GLU 217 0.28 GLN 240 -0.18 PRO 3

GLU 217 0.26 ASP 241 -0.16 PRO 3

GLU 217 0.22 ALA 242 -0.21 PRO 3

GLU 217 0.27 TYR 243 -0.20 PRO 3

GLU 217 0.33 ASN 244 -0.13 PRO 3

GLU 217 0.28 ALA 245 -0.15 PRO 3

GLU 217 0.26 ALA 246 -0.18 PRO 3

GLU 217 0.32 GLY 247 -0.13 PRO 3

GLU 217 0.34 GLY 248 -0.13 PRO 3

GLU 217 0.42 HIS 249 -0.12 ASN 30

GLU 217 0.40 ASN 250 -0.13 ASN 31

GLU 217 0.39 ALA 251 -0.11 ASN 30

GLU 217 0.48 VAL 252 -0.11 ASN 30

GLU 217 0.42 PHE 253 -0.09 LEU 237

GLU 217 0.50 ASN 254 -0.10 ASP 51

GLU 217 0.36 PHE 255 -0.14 ASP 51

GLU 217 0.47 PRO 256 -0.19 ALA 268

LEU 165 0.28 PRO 257 -0.25 ALA 268

PRO 256 0.31 ASN 258 -0.23 ASN 53

ASP 169 0.31 GLY 259 -0.21 ASN 258

ASP 169 0.35 THR 260 -0.18 ILE 52

ASP 169 0.46 HIS 261 -0.28 PRO 3

ASP 169 0.41 SER 262 -0.27 PRO 3

ASP 169 0.37 TRP 263 -0.25 PRO 3

ASP 169 0.33 GLU 264 -0.28 ASN 53

ASP 169 0.33 TYR 265 -0.23 ASN 53

ASP 169 0.36 TRP 266 -0.19 PRO 3

ASP 169 0.33 GLY 267 -0.21 PRO 257

LEU 218 0.31 ALA 268 -0.25 PRO 257

LEU 218 0.33 GLN 269 -0.18 PRO 257

ASP 169 0.29 LEU 270 -0.14 PRO 257

ARG 2 0.33 ASN 271 -0.16 PRO 257

GLU 217 0.46 ALA 272 -0.13 PRO 257

GLU 217 0.37 MET 273 -0.11 VAL 7

GLU 58 0.35 LYS 274 -0.12 VAL 7

ARG 2 0.42 GLY 275 -0.10 ASN 30

GLU 217 0.39 ASP 276 -0.12 ASN 30

GLU 58 0.30 LEU 277 -0.11 ASN 30

ARG 2 0.31 GLN 278 -0.15 ASN 30

GLU 217 0.33 SER 279 -0.15 ASN 30

GLU 217 0.30 SER 280 -0.15 ASN 30

GLU 58 0.26 LEU 281 -0.16 ASN 30

GLN 62 0.27 GLY 282 -0.20 ASN 30

GLN 62 0.33 ALA 283 -0.20 ASN 30

GLY 4 0.43 GLY 284 -0.22 ASN 30

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 13 ---

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

* 1F0N_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000 *