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

* 4XFX_unrelaxed_rank_001_alphafold2_ptm_model_4_seed_000 *

CA distance fluctuations for 240220091228160354

--- 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
GLY 89 0.30 PRO 1 -0.73 PRO 117

GLY 89 0.27 ILE 2 -0.70 ASN 116

GLY 89 0.28 VAL 3 -0.18 SER 11

GLY 89 0.23 GLN 4 -0.15 ASN 116

GLU 175 0.25 MET 5 -0.21 ILE 2

GLN 174 0.28 VAL 6 -0.11 GLN 107

GLY 41 0.28 HIS 7 -0.10 ILE 2

GLU 40 0.30 GLN 8 -0.15 VAL 3

PRO 88 0.22 ALA 9 -0.15 THR 49

SER 173 0.20 ILE 10 -0.17 ILE 2

PRO 88 0.18 SER 11 -0.19 THR 211

PRO 88 0.20 PRO 12 -0.23 THR 211

PRO 88 0.16 ARG 13 -0.25 THR 211

SER 173 0.18 THR 14 -0.23 THR 211

PRO 88 0.16 LEU 15 -0.25 THR 211

PRO 88 0.15 ASN 16 -0.30 THR 211

SER 173 0.15 ALA 17 -0.31 GLU 207

SER 173 0.16 TRP 18 -0.30 GLU 207

PRO 88 0.13 VAL 19 -0.32 THR 211

PRO 88 0.11 LYS 20 -0.37 THR 211

SER 173 0.13 VAL 21 -0.38 GLU 207

SER 173 0.11 VAL 22 -0.36 ARG 157

PRO 88 0.10 GLU 23 -0.40 ARG 157

THR 143 0.09 GLU 24 -0.47 ARG 157

THR 143 0.11 LYS 25 -0.47 ARG 157

SER 173 0.08 ALA 26 -0.44 ASP 158

SER 173 0.10 PHE 27 -0.39 ASP 161

SER 141 0.15 SER 28 -0.48 ASP 161

ALA 169 0.23 PRO 29 -0.32 GLU 207

GLN 8 0.16 GLU 30 -0.40 GLU 207

SER 173 0.18 VAL 31 -0.35 GLU 207

SER 173 0.24 ILE 32 -0.30 GLU 207

SER 173 0.29 PRO 33 -0.30 GLU 207

SER 173 0.23 MET 34 -0.33 GLU 207

SER 173 0.24 PHE 35 -0.27 GLU 207

SER 173 0.31 SER 36 -0.29 PRO 1

SER 173 0.29 ALA 37 -0.29 PRO 1

GLN 8 0.28 LEU 38 -0.24 GLU 207

SER 173 0.26 SER 39 -0.25 ILE 2

SER 173 0.31 GLU 40 -0.33 ILE 2

SER 173 0.31 GLY 41 -0.38 ILE 2

SER 173 0.24 ALA 42 -0.27 ILE 2

SER 173 0.20 THR 43 -0.24 ILE 2

SER 173 0.15 PRO 44 -0.19 ILE 2

PRO 88 0.20 GLN 45 -0.15 GLN 214

SER 173 0.18 ASP 46 -0.17 ILE 2

SER 173 0.17 LEU 47 -0.19 ILE 2

GLY 84 0.17 ASN 48 -0.19 GLN 214

THR 102 0.22 THR 49 -0.20 GLN 214

SER 173 0.15 MET 50 -0.22 GLU 207

THR 102 0.15 LEU 51 -0.24 ASP 158

THR 102 0.22 ASN 52 -0.24 ASP 158

THR 102 0.19 THR 53 -0.26 GLN 214

GLY 84 0.15 VAL 54 -0.29 ASP 158

GLY 84 0.17 GLY 55 -0.31 ASP 158

GLY 84 0.14 GLY 56 -0.33 ASP 158

GLY 84 0.09 HIS 57 -0.34 ASP 158

GLY 84 0.12 GLN 58 -0.30 ASP 158

GLY 84 0.07 ALA 59 -0.30 ASP 158

SER 173 0.07 ALA 60 -0.31 ASP 158

GLY 84 0.08 MET 61 -0.28 ASP 158

GLY 84 0.08 GLN 62 -0.26 ASP 158

GLY 132 0.05 MET 63 -0.26 ASP 158

SER 173 0.08 LEU 64 -0.25 ASP 158

GLY 55 0.09 LYS 65 -0.23 ASP 158

THR 67 0.06 GLU 66 -0.22 ASP 158

TRP 128 0.08 THR 67 -0.23 ARG 162

TRP 128 0.08 ILE 68 -0.21 ASP 158

ALA 73 0.13 ASN 69 -0.20 ASP 158

PRO 117 0.07 GLU 70 -0.23 ARG 162

PRO 117 0.08 GLU 71 -0.23 ARG 162

ASN 52 0.11 ALA 72 -0.19 ASP 161

ASN 69 0.13 ALA 73 -0.22 GLN 171

PRO 117 0.10 GLU 74 -0.31 GLN 171

PRO 117 0.09 TRP 75 -0.24 GLN 171

ASN 52 0.11 ASP 76 -0.22 GLN 171

ASN 52 0.09 ARG 77 -0.30 GLN 171

PRO 117 0.11 LEU 78 -0.33 GLN 171

PRO 117 0.10 HIS 79 -0.26 GLN 171

ASN 52 0.10 PRO 80 -0.25 ALA 172

THR 103 0.14 VAL 81 -0.20 ALA 172

ARG 92 0.22 HIS 82 -0.23 ALA 172

THR 103 0.26 ALA 83 -0.25 GLN 174

THR 103 0.30 GLY 84 -0.20 GLN 174

THR 105 0.28 PRO 85 -0.17 ALA 172

THR 105 0.28 ILE 86 -0.17 VAL 81

THR 105 0.23 ALA 87 -0.20 PRO 117

GLN 107 0.32 PRO 88 -0.10 PRO 117

PRO 1 0.30 GLY 89 -0.07 VAL 81

GLN 107 0.19 GLN 90 -0.11 GLU 207

GLY 84 0.15 MET 91 -0.10 GLU 207

HIS 82 0.22 ARG 92 -0.13 GLU 207

SER 104 0.08 GLU 93 -0.16 ILE 2

ASN 52 0.09 PRO 94 -0.17 ILE 2

ASN 52 0.13 ARG 95 -0.16 ASP 158

ASN 52 0.12 GLY 96 -0.18 ASP 158

ASN 52 0.18 SER 97 -0.17 ASN 69

GLY 84 0.18 ASP 98 -0.14 ASP 158

ASN 52 0.09 ILE 99 -0.19 ILE 2

ASN 52 0.13 ALA 100 -0.17 ILE 2

GLY 84 0.19 GLY 101 -0.15 ASP 158

GLY 84 0.25 THR 102 -0.19 ASN 69

GLY 84 0.30 THR 103 -0.17 ASN 69

GLY 84 0.27 SER 104 -0.13 ASN 69

PRO 88 0.31 THR 105 -0.12 ASN 69

PRO 88 0.28 LEU 106 -0.11 LYS 65

PRO 88 0.32 GLN 107 -0.11 VAL 6

PRO 88 0.27 GLU 108 -0.10 GLN 214

PRO 88 0.18 GLN 109 -0.15 ILE 2

GLY 89 0.18 ILE 110 -0.18 ILE 2

GLY 89 0.20 GLY 111 -0.15 ILE 2

SER 173 0.11 TRP 112 -0.30 ILE 2

SER 173 0.17 MET 113 -0.44 ILE 2

SER 173 0.18 THR 114 -0.57 ILE 2

SER 173 0.12 HIS 115 -0.52 ILE 2

SER 173 0.12 ASN 116 -0.70 ILE 2

LEU 78 0.11 PRO 117 -0.73 PRO 1

SER 173 0.14 PRO 118 -0.60 ILE 2

SER 173 0.12 ILE 119 -0.42 ILE 2

SER 173 0.17 PRO 120 -0.41 ILE 2

SER 173 0.13 VAL 121 -0.30 ILE 2

SER 173 0.19 GLY 122 -0.30 ILE 2

SER 173 0.23 GLU 123 -0.35 PRO 1

SER 173 0.15 ILE 124 -0.31 PRO 1

SER 173 0.14 TYR 125 -0.24 ILE 2

SER 173 0.21 LYS 126 -0.26 ILE 2

SER 173 0.21 ARG 127 -0.29 PRO 1

SER 173 0.10 TRP 128 -0.23 PRO 1

SER 173 0.15 ILE 129 -0.21 GLU 207

SER 173 0.22 ILE 130 -0.24 PRO 1

SER 173 0.14 LEU 131 -0.24 ASP 161

SER 173 0.10 GLY 132 -0.25 ASP 161

SER 173 0.14 LEU 133 -0.28 ASP 161

SER 173 0.15 ASN 134 -0.28 ASP 161

GLN 8 0.07 LYS 135 -0.29 ARG 162

SER 173 0.08 ILE 136 -0.31 ASP 161

ILE 32 0.10 VAL 137 -0.35 ASP 161

PRO 33 0.09 ARG 138 -0.33 ARG 162

PRO 33 0.07 MET 139 -0.34 ARG 162

GLN 8 0.06 TYR 140 -0.42 ARG 162

PRO 29 0.17 SER 141 -0.43 ARG 162

PRO 29 0.12 PRO 142 -0.32 ARG 162

PRO 29 0.18 THR 143 -0.21 LEU 78

PRO 29 0.15 SER 144 -0.22 LEU 78

GLN 8 0.13 ILE 145 -0.23 LEU 78

GLN 8 0.13 LEU 146 -0.19 LEU 78

GLN 8 0.11 ASP 147 -0.19 LEU 78

GLN 8 0.10 ILE 148 -0.20 LEU 78

VAL 6 0.09 ARG 149 -0.18 LEU 78

VAL 6 0.07 GLN 150 -0.22 TYR 140

VAL 6 0.05 GLY 151 -0.22 TYR 140

VAL 6 0.05 PRO 152 -0.21 GLU 24

VAL 216 0.05 LYS 153 -0.29 GLU 24

ASN 178 0.05 GLU 154 -0.33 GLU 24

ASN 178 0.06 PRO 155 -0.40 GLU 24

GLU 182 0.08 PHE 156 -0.38 GLU 24

ASN 178 0.12 ARG 157 -0.47 LYS 25

ASN 178 0.09 ASP 158 -0.47 LYS 25

ASN 178 0.07 TYR 159 -0.32 TYR 140

ASN 178 0.11 VAL 160 -0.35 SER 28

ASN 178 0.11 ASP 161 -0.48 SER 28

VAL 6 0.07 ARG 162 -0.43 SER 141

VAL 6 0.11 PHE 163 -0.24 TYR 140

VAL 6 0.12 TYR 164 -0.29 SER 28

GLN 8 0.11 LYS 165 -0.36 SER 28

GLN 8 0.12 THR 166 -0.27 ARG 138

GLN 8 0.15 LEU 167 -0.28 LEU 78

GLN 8 0.16 ARG 168 -0.29 LEU 78

PRO 29 0.23 ALA 169 -0.29 LEU 78

PRO 33 0.19 GLU 170 -0.29 LEU 78

PRO 33 0.21 GLN 171 -0.33 LEU 78

GLN 8 0.20 ALA 172 -0.32 LEU 78

GLU 40 0.31 SER 173 -0.29 LEU 78

GLU 40 0.30 GLN 174 -0.31 LEU 78

GLN 8 0.28 GLU 175 -0.25 LEU 78

GLN 8 0.24 VAL 176 -0.22 LEU 78

GLN 8 0.22 LYS 177 -0.26 LEU 78

VAL 6 0.22 ASN 178 -0.24 LEU 78

VAL 6 0.20 TRP 179 -0.20 PRO 1

VAL 6 0.17 MET 180 -0.21 LEU 78

VAL 6 0.16 THR 181 -0.23 LEU 78

LEU 206 0.19 GLU 182 -0.22 PRO 1

VAL 6 0.16 THR 183 -0.20 PRO 1

VAL 6 0.15 LEU 184 -0.19 PRO 1

VAL 6 0.13 LEU 185 -0.21 PRO 1

VAL 6 0.12 VAL 186 -0.20 PRO 1

VAL 6 0.13 GLN 187 -0.18 PRO 1

VAL 6 0.11 ASN 188 -0.18 PRO 1

VAL 6 0.09 ALA 189 -0.19 PRO 1

VAL 6 0.07 ASN 190 -0.20 GLU 24

VAL 6 0.07 PRO 191 -0.18 GLU 24

VAL 6 0.05 ASP 192 -0.24 GLU 24

VAL 6 0.06 CYS 193 -0.27 GLU 24

VAL 6 0.08 LYS 194 -0.21 GLU 24

VAL 6 0.07 THR 195 -0.21 GLU 24

THR 183 0.06 ILE 196 -0.27 GLU 24

THR 183 0.09 LEU 197 -0.25 GLU 24

VAL 6 0.10 LYS 198 -0.22 PRO 1

VAL 6 0.08 ALA 199 -0.23 PRO 1

THR 183 0.09 LEU 200 -0.26 GLU 24

VAL 6 0.10 GLY 201 -0.25 PRO 1

VAL 6 0.13 PRO 202 -0.25 PRO 1

VAL 6 0.12 GLY 203 -0.28 PRO 1

GLU 175 0.11 ALA 204 -0.28 PRO 1

GLU 182 0.17 THR 205 -0.32 GLU 24

GLU 182 0.19 LEU 206 -0.36 LYS 25

GLU 182 0.12 GLU 207 -0.44 GLU 24

GLU 182 0.11 GLU 208 -0.38 GLU 24

GLU 182 0.11 MET 209 -0.35 GLU 24

GLU 182 0.10 MET 210 -0.43 GLU 24

GLU 182 0.08 THR 211 -0.45 GLU 24

THR 183 0.08 ALA 212 -0.38 GLU 24

THR 183 0.08 CYS 213 -0.37 GLU 24

GLU 182 0.06 GLN 214 -0.45 GLU 24

GLU 182 0.05 GLY 215 -0.42 GLU 24

GLU 182 0.05 VAL 216 -0.36 GLU 24

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.

*** 4XFX_unrelaxed_rank_001_alphafold2_ptm_model_4_seed_000 ***

CA distance fluctuations for 240220091228160354

--- normal mode 13 ---

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

* 4XFX_unrelaxed_rank_001_alphafold2_ptm_model_4_seed_000 *