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 8 ---

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 0.18 PRO 1 -0.41 GLU 175

GLY 89 0.19 ILE 2 -0.39 GLU 175

GLY 89 0.14 VAL 3 -0.37 GLU 175

GLN 107 0.11 GLN 4 -0.33 GLU 175

GLY 215 0.07 MET 5 -0.34 GLU 175

ASP 158 0.10 VAL 6 -0.29 GLU 175

ASP 158 0.11 HIS 7 -0.28 SER 173

ASP 158 0.13 GLN 8 -0.27 GLN 174

ASP 158 0.14 ALA 9 -0.24 GLN 174

ASP 158 0.15 ILE 10 -0.25 GLN 174

ASP 158 0.18 SER 11 -0.23 GLN 174

ASP 158 0.19 PRO 12 -0.20 GLN 174

ASP 158 0.21 ARG 13 -0.21 GLN 174

ASP 158 0.20 THR 14 -0.24 GLN 174

ASP 158 0.18 LEU 15 -0.21 GLN 174

GLU 154 0.21 ASN 16 -0.18 GLN 174

ASP 158 0.24 ALA 17 -0.21 GLN 174

ASP 158 0.20 TRP 18 -0.21 GLN 174

GLU 154 0.19 VAL 19 -0.16 GLN 174

GLU 154 0.24 LYS 20 -0.16 GLN 174

ASP 158 0.24 VAL 21 -0.17 GLN 174

GLU 154 0.18 VAL 22 -0.13 GLN 174

GLU 154 0.22 GLU 23 -0.10 GLN 174

GLU 154 0.27 GLU 24 -0.10 GLN 174

ARG 162 0.24 LYS 25 -0.10 GLN 174

THR 143 0.20 ALA 26 -0.08 GLN 174

THR 143 0.11 PHE 27 -0.08 GLN 174

THR 143 0.14 SER 28 -0.08 GLN 174

ASP 161 0.10 PRO 29 -0.13 GLN 174

ASP 161 0.18 GLU 30 -0.20 GLN 174

ASP 158 0.16 VAL 31 -0.20 GLN 174

ASP 161 0.13 ILE 32 -0.27 GLN 174

ASP 158 0.16 PRO 33 -0.39 GLN 174

ASP 158 0.20 MET 34 -0.31 GLN 174

ASP 158 0.16 PHE 35 -0.29 GLN 174

ASP 158 0.14 SER 36 -0.39 GLN 174

ASP 158 0.18 ALA 37 -0.39 GLN 174

ASP 158 0.18 LEU 38 -0.32 GLN 174

ASP 158 0.15 SER 39 -0.32 GLN 174

ASP 158 0.14 GLU 40 -0.38 GLN 174

ASP 158 0.12 GLY 41 -0.36 SER 173

ASP 158 0.12 ALA 42 -0.31 SER 173

ASP 158 0.10 THR 43 -0.28 SER 173

ASP 158 0.09 PRO 44 -0.25 SER 173

ASP 158 0.10 GLN 45 -0.21 SER 173

ASP 158 0.12 ASP 46 -0.23 SER 173

ASP 158 0.11 LEU 47 -0.23 SER 173

ASP 158 0.10 ASN 48 -0.18 SER 173

ASP 158 0.12 THR 49 -0.18 GLN 174

ASP 158 0.13 MET 50 -0.19 GLN 174

ASP 158 0.11 LEU 51 -0.15 GLN 174

ASP 158 0.11 ASN 52 -0.13 GLN 174

GLU 154 0.13 THR 53 -0.14 GLN 174

GLU 154 0.13 VAL 54 -0.12 GLN 174

GLY 151 0.13 GLY 55 -0.09 GLN 174

THR 143 0.12 GLY 56 -0.06 GLN 174

THR 143 0.10 HIS 57 -0.04 GLN 174

THR 102 0.07 GLN 58 -0.03 GLN 174

THR 102 0.06 ALA 59 -0.02 ALA 26

THR 102 0.06 ALA 60 -0.03 ILE 2

THR 102 0.06 MET 61 -0.05 GLN 174

THR 102 0.07 GLN 62 -0.04 SER 144

THR 102 0.04 MET 63 -0.08 SER 144

THR 102 0.04 LEU 64 -0.09 SER 144

THR 102 0.06 LYS 65 -0.09 SER 144

THR 102 0.03 GLU 66 -0.11 SER 144

GLU 207 0.04 THR 67 -0.16 SER 144

GLU 207 0.04 ILE 68 -0.14 SER 144

GLU 207 0.04 ASN 69 -0.13 SER 144

GLU 207 0.04 GLU 70 -0.17 SER 144

GLU 207 0.05 GLU 71 -0.19 SER 144

GLU 207 0.05 ALA 72 -0.16 SER 144

GLU 207 0.04 ALA 73 -0.17 SER 144

GLU 207 0.05 GLU 74 -0.21 LEU 146

GLU 207 0.05 TRP 75 -0.20 LEU 146

GLU 207 0.04 ASP 76 -0.18 LEU 146

GLU 207 0.04 ARG 77 -0.20 LEU 146

GLU 207 0.04 LEU 78 -0.23 LEU 146

GLU 207 0.04 HIS 79 -0.21 SER 173

GLU 207 0.04 PRO 80 -0.18 LEU 146

GLU 207 0.04 VAL 81 -0.17 SER 173

VAL 3 0.04 HIS 82 -0.18 SER 173

ILE 2 0.04 ALA 83 -0.16 VAL 176

PRO 1 0.06 GLY 84 -0.16 VAL 176

PRO 1 0.09 PRO 85 -0.17 SER 173

PRO 1 0.09 ILE 86 -0.19 SER 173

PRO 1 0.12 ALA 87 -0.21 SER 173

PRO 1 0.17 PRO 88 -0.20 GLU 175

ILE 2 0.19 GLY 89 -0.22 SER 173

ILE 2 0.13 GLN 90 -0.23 SER 173

ILE 2 0.09 MET 91 -0.23 SER 173

ILE 2 0.06 ARG 92 -0.21 SER 173

GLU 207 0.04 GLU 93 -0.23 SER 173

GLU 207 0.04 PRO 94 -0.23 SER 173

GLU 207 0.04 ARG 95 -0.19 SER 173

GLU 207 0.04 GLY 96 -0.18 SER 173

LYS 65 0.05 SER 97 -0.15 SER 173

ARG 157 0.05 ASP 98 -0.19 SER 173

ARG 157 0.05 ILE 99 -0.23 SER 173

ASP 158 0.06 ALA 100 -0.19 SER 173

ASP 158 0.07 GLY 101 -0.19 SER 173

GLN 58 0.07 THR 102 -0.14 SER 173

GLN 58 0.06 THR 103 -0.15 SER 173

ASP 158 0.06 SER 104 -0.19 SER 173

PRO 1 0.09 THR 105 -0.19 SER 173

ASP 158 0.09 LEU 106 -0.22 SER 173

PRO 1 0.12 GLN 107 -0.23 SER 173

PRO 1 0.08 GLU 108 -0.23 SER 173

ASP 158 0.07 GLN 109 -0.26 SER 173

ASP 158 0.08 ILE 110 -0.28 SER 173

VAL 3 0.07 GLY 111 -0.27 SER 173

ASP 158 0.06 TRP 112 -0.29 SER 173

ASP 158 0.06 MET 113 -0.34 SER 173

ASP 158 0.06 THR 114 -0.33 SER 173

ASP 158 0.05 HIS 115 -0.31 SER 173

ARG 157 0.04 ASN 116 -0.33 SER 173

ARG 157 0.04 PRO 117 -0.35 SER 173

ARG 157 0.05 PRO 118 -0.36 SER 173

ARG 157 0.05 ILE 119 -0.35 SER 173

ARG 157 0.06 PRO 120 -0.38 SER 173

ARG 157 0.06 VAL 121 -0.32 SER 173

ASP 158 0.08 GLY 122 -0.33 SER 173

ARG 157 0.07 GLU 123 -0.41 SER 173

GLU 207 0.05 ILE 124 -0.37 SER 173

ARG 157 0.06 TYR 125 -0.29 SER 173

ASP 158 0.08 LYS 126 -0.34 SER 173

GLU 207 0.06 ARG 127 -0.39 SER 173

GLU 207 0.05 TRP 128 -0.26 SER 173

ASP 161 0.06 ILE 129 -0.22 SER 173

ASP 161 0.07 ILE 130 -0.28 SER 173

GLU 207 0.06 LEU 131 -0.21 SER 144

GLU 207 0.04 GLY 132 -0.15 SER 144

ASP 161 0.06 LEU 133 -0.11 SER 173

GLU 207 0.05 ASN 134 -0.18 SER 144

GLN 171 0.07 LYS 135 -0.19 SER 144

GLN 171 0.06 ILE 136 -0.08 SER 144

GLN 171 0.06 VAL 137 -0.08 PRO 1

MET 139 0.14 ARG 138 -0.15 SER 144

ALA 172 0.15 MET 139 -0.07 ARG 162

SER 141 0.12 TYR 140 -0.06 PRO 1

ALA 26 0.15 SER 141 -0.11 ARG 162

VAL 176 0.13 PRO 142 -0.16 ARG 162

GLU 24 0.22 THR 143 -0.15 LEU 78

GLU 24 0.15 SER 144 -0.21 LEU 131

GLU 24 0.14 ILE 145 -0.18 LEU 78

GLU 24 0.14 LEU 146 -0.23 LEU 78

GLU 24 0.20 ASP 147 -0.21 LEU 78

GLU 24 0.22 ILE 148 -0.16 LEU 78

GLU 24 0.22 ARG 149 -0.15 LEU 78

GLU 24 0.23 GLN 150 -0.12 LEU 78

GLU 24 0.27 GLY 151 -0.12 LEU 78

GLU 24 0.24 PRO 152 -0.12 LEU 78

GLU 24 0.26 LYS 153 -0.10 PRO 142

GLU 24 0.27 GLU 154 -0.12 PRO 142

GLU 24 0.23 PRO 155 -0.11 PRO 142

GLU 24 0.18 PHE 156 -0.09 PRO 142

ALA 17 0.19 ARG 157 -0.10 PRO 142

GLU 24 0.25 ASP 158 -0.14 PRO 142

GLU 24 0.22 TYR 159 -0.12 PRO 142

GLU 24 0.15 VAL 160 -0.09 PRO 142

VAL 21 0.19 ASP 161 -0.12 PRO 142

GLU 24 0.25 ARG 162 -0.16 PRO 142

GLU 24 0.15 PHE 163 -0.12 PRO 1

LYS 25 0.07 TYR 164 -0.12 PRO 1

LYS 25 0.14 LYS 165 -0.09 PRO 1

LYS 25 0.15 THR 166 -0.12 PRO 1

LYS 25 0.06 LEU 167 -0.17 PRO 1

GLN 171 0.07 ARG 168 -0.15 PRO 1

GLN 171 0.06 ALA 169 -0.14 PRO 1

MET 139 0.12 GLU 170 -0.20 ARG 127

MET 139 0.14 GLN 171 -0.26 ARG 127

MET 139 0.15 ALA 172 -0.30 ARG 127

MET 139 0.11 SER 173 -0.41 GLU 123

THR 205 0.07 GLN 174 -0.39 ALA 37

PRO 142 0.09 GLU 175 -0.41 PRO 1

PRO 142 0.13 VAL 176 -0.35 PRO 1

PRO 142 0.08 LYS 177 -0.30 PRO 1

THR 205 0.07 ASN 178 -0.32 PRO 1

PRO 142 0.08 TRP 179 -0.32 PRO 1

PRO 142 0.08 MET 180 -0.26 PRO 1

LEU 206 0.05 THR 181 -0.24 PRO 1

THR 205 0.05 GLU 182 -0.27 PRO 1

SER 144 0.05 THR 183 -0.26 PRO 1

GLU 24 0.08 LEU 184 -0.23 PRO 1

GLU 24 0.09 LEU 185 -0.19 PRO 1

GLU 24 0.09 VAL 186 -0.19 PRO 1

GLU 24 0.11 GLN 187 -0.20 PRO 1

GLU 24 0.15 ASN 188 -0.17 LEU 78

GLU 24 0.16 ALA 189 -0.13 PRO 1

GLU 24 0.19 ASN 190 -0.13 LEU 78

GLU 24 0.16 PRO 191 -0.14 LEU 78

GLU 24 0.15 ASP 192 -0.11 LEU 78

GLU 24 0.14 CYS 193 -0.11 PRO 1

GLU 24 0.12 LYS 194 -0.15 PRO 1

GLU 24 0.11 THR 195 -0.16 PRO 1

GLU 24 0.09 ILE 196 -0.14 PRO 1

GLU 24 0.07 LEU 197 -0.17 PRO 1

GLU 24 0.06 LYS 198 -0.21 PRO 1

GLU 24 0.05 ALA 199 -0.19 PRO 1

GLU 24 0.03 LEU 200 -0.19 PRO 1

SER 144 0.02 GLY 201 -0.25 PRO 1

SER 144 0.04 PRO 202 -0.29 PRO 1

GLN 174 0.03 GLY 203 -0.28 PRO 1

GLN 174 0.04 ALA 204 -0.22 PRO 1

GLN 174 0.07 THR 205 -0.18 PRO 1

GLN 174 0.06 LEU 206 -0.14 PRO 1

ARG 127 0.06 GLU 207 -0.09 PRO 1

GLN 174 0.05 GLU 208 -0.12 PRO 1

ALA 17 0.05 MET 209 -0.12 PRO 1

ALA 17 0.10 MET 210 -0.07 PRO 1

ALA 37 0.10 THR 211 -0.05 PRO 142

ALA 17 0.09 ALA 212 -0.08 PRO 1

ALA 17 0.12 CYS 213 -0.07 PRO 1

ARG 13 0.16 GLN 214 -0.07 PRO 142

ARG 13 0.18 GLY 215 -0.07 PRO 142

GLU 24 0.17 VAL 216 -0.07 PRO 142

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 8 ---

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

* 4XFX_unrelaxed_rank_001_alphafold2_ptm_model_4_seed_000 *