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 9 ---

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 0.42 PRO 1 -0.41 THR 205

GLY 89 0.46 ILE 2 -0.35 THR 205

GLY 89 0.31 VAL 3 -0.33 THR 205

GLN 107 0.29 GLN 4 -0.26 THR 205

GLN 107 0.10 MET 5 -0.27 GLY 41

GLN 4 0.05 VAL 6 -0.22 GLU 207

GLN 4 0.07 HIS 7 -0.19 GLU 207

THR 49 0.03 GLN 8 -0.22 GLU 207

GLN 4 0.06 ALA 9 -0.21 GLU 207

GLY 41 0.04 ILE 10 -0.22 GLU 207

GLY 41 0.04 SER 11 -0.26 GLU 207

THR 53 0.04 PRO 12 -0.26 GLU 207

GLY 41 0.04 ARG 13 -0.31 GLU 207

GLU 40 0.04 THR 14 -0.28 GLU 207

GLU 40 0.03 LEU 15 -0.25 GLU 207

GLY 55 0.04 ASN 16 -0.29 GLU 207

GLU 40 0.03 ALA 17 -0.31 GLU 207

SER 39 0.03 TRP 18 -0.26 GLU 207

PRO 142 0.03 VAL 19 -0.25 GLU 207

LEU 38 0.03 LYS 20 -0.30 GLU 207

PHE 35 0.04 VAL 21 -0.28 GLU 207

PRO 142 0.04 VAL 22 -0.23 GLU 207

PRO 142 0.05 GLU 23 -0.24 ARG 157

MET 34 0.04 GLU 24 -0.31 ASP 161

VAL 31 0.06 LYS 25 -0.30 ASP 161

PRO 142 0.05 ALA 26 -0.22 ASP 161

PRO 142 0.05 PHE 27 -0.17 ASP 161

LEU 78 0.04 SER 28 -0.21 LYS 165

LEU 78 0.06 PRO 29 -0.20 PRO 1

LEU 78 0.05 GLU 30 -0.23 PRO 1

LYS 25 0.06 VAL 31 -0.19 PRO 1

LEU 78 0.05 ILE 32 -0.21 PRO 1

LEU 78 0.06 PRO 33 -0.26 PRO 1

LYS 25 0.05 MET 34 -0.25 GLU 207

VAL 21 0.04 PHE 35 -0.19 PRO 1

LEU 78 0.04 SER 36 -0.25 PRO 1

LEU 78 0.04 ALA 37 -0.29 PRO 1

LYS 20 0.03 LEU 38 -0.24 GLU 207

TRP 18 0.03 SER 39 -0.21 VAL 3

THR 14 0.04 GLU 40 -0.29 VAL 3

PRO 118 0.04 GLY 41 -0.28 VAL 3

PRO 120 0.03 ALA 42 -0.17 MET 5

PRO 120 0.03 THR 43 -0.13 GLU 207

SER 173 0.06 PRO 44 -0.10 GLU 207

GLN 4 0.08 GLN 45 -0.13 GLU 207

GLN 4 0.04 ASP 46 -0.16 GLU 207

SER 144 0.03 LEU 47 -0.14 GLU 207

SER 173 0.05 ASN 48 -0.13 GLU 207

GLN 4 0.06 THR 49 -0.16 GLU 207

GLN 58 0.03 MET 50 -0.18 GLU 207

SER 144 0.05 LEU 51 -0.14 GLU 207

GLN 4 0.06 ASN 52 -0.15 GLU 207

GLN 4 0.04 THR 53 -0.19 GLU 207

PRO 142 0.04 VAL 54 -0.18 GLU 207

PRO 142 0.05 GLY 55 -0.18 GLU 207

PRO 142 0.06 GLY 56 -0.16 ASP 158

SER 144 0.07 HIS 57 -0.14 ASP 158

SER 144 0.09 GLN 58 -0.11 ASP 158

SER 144 0.11 ALA 59 -0.09 ASP 158

SER 144 0.10 ALA 60 -0.10 ASP 158

SER 144 0.09 MET 61 -0.10 ASP 158

SER 173 0.11 GLN 62 -0.07 ASP 158

SER 173 0.13 MET 63 -0.05 ASP 158

SER 173 0.12 LEU 64 -0.06 ASP 158

SER 173 0.13 LYS 65 -0.05 ASP 158

SER 173 0.17 GLU 66 -0.04 MET 5

SER 173 0.21 THR 67 -0.06 MET 5

SER 173 0.18 ILE 68 -0.06 MET 5

SER 173 0.20 ASN 69 -0.05 ALA 73

SER 173 0.25 GLU 70 -0.05 MET 5

SER 173 0.26 GLU 71 -0.07 MET 5

SER 173 0.22 ALA 72 -0.05 MET 5

SER 173 0.25 ALA 73 -0.05 ASN 69

SER 173 0.31 GLU 74 -0.06 MET 5

SER 173 0.26 TRP 75 -0.06 MET 5

SER 173 0.24 ASP 76 -0.04 MET 5

SER 173 0.29 ARG 77 -0.04 MET 5

SER 173 0.30 LEU 78 -0.05 MET 5

SER 173 0.24 HIS 79 -0.04 MET 5

SER 173 0.23 PRO 80 -0.03 ASN 52

SER 173 0.19 VAL 81 -0.04 ASN 52

SER 173 0.18 HIS 82 -0.04 ARG 92

GLU 175 0.19 ALA 83 -0.06 THR 103

PRO 1 0.19 GLY 84 -0.06 THR 103

PRO 1 0.25 PRO 85 -0.06 THR 105

ILE 2 0.27 ILE 86 -0.06 THR 105

ILE 2 0.31 ALA 87 -0.05 THR 105

ILE 2 0.40 PRO 88 -0.07 THR 105

ILE 2 0.46 GLY 89 -0.06 GLN 107

ILE 2 0.34 GLN 90 -0.05 THR 105

ILE 2 0.30 MET 91 -0.03 THR 105

ILE 2 0.22 ARG 92 -0.04 HIS 82

SER 173 0.14 GLU 93 -0.03 ASN 52

SER 173 0.14 PRO 94 -0.03 ASN 52

SER 173 0.17 ARG 95 -0.04 ASN 52

SER 173 0.19 GLY 96 -0.04 ASN 52

SER 173 0.16 SER 97 -0.06 ASN 52

SER 173 0.13 ASP 98 -0.05 ASN 52

SER 173 0.13 ILE 99 -0.05 MET 5

SER 173 0.12 ALA 100 -0.05 GLU 207

ILE 2 0.10 GLY 101 -0.08 GLU 207

ILE 2 0.13 THR 102 -0.07 ASN 52

ILE 2 0.18 THR 103 -0.06 GLY 84

ILE 2 0.20 SER 104 -0.07 GLU 207

ILE 2 0.25 THR 105 -0.10 GLU 207

ILE 2 0.22 LEU 106 -0.12 GLU 207

ILE 2 0.34 GLN 107 -0.11 GLU 207

ILE 2 0.27 GLU 108 -0.08 GLU 207

ILE 2 0.14 GLN 109 -0.09 GLU 207

ILE 2 0.14 ILE 110 -0.11 GLU 207

ILE 2 0.25 GLY 111 -0.08 GLU 207

ILE 2 0.09 TRP 112 -0.05 GLU 207

PRO 118 0.03 MET 113 -0.12 MET 5

GLY 111 0.03 THR 114 -0.18 GLN 4

VAL 3 0.10 HIS 115 -0.10 GLN 4

VAL 3 0.04 ASN 116 -0.16 GLN 4

SER 173 0.05 PRO 117 -0.16 GLN 4

GLY 41 0.04 PRO 118 -0.17 GLN 4

SER 173 0.07 ILE 119 -0.11 GLN 4

SER 173 0.05 PRO 120 -0.15 ILE 2

SER 173 0.08 VAL 121 -0.11 MET 5

SER 173 0.04 GLY 122 -0.15 MET 5

SER 173 0.04 GLU 123 -0.20 ILE 2

SER 173 0.11 ILE 124 -0.13 ILE 2

SER 173 0.11 TYR 125 -0.11 MET 5

SER 173 0.06 LYS 126 -0.14 PRO 1

SER 173 0.11 ARG 127 -0.17 PRO 1

SER 173 0.17 TRP 128 -0.11 PRO 1

SER 173 0.10 ILE 129 -0.10 PRO 1

SER 173 0.07 ILE 130 -0.16 PRO 1

SER 173 0.18 LEU 131 -0.15 PRO 1

GLN 171 0.14 GLY 132 -0.10 PRO 1

SER 144 0.06 LEU 133 -0.13 PRO 1

GLN 171 0.10 ASN 134 -0.16 PRO 1

GLN 171 0.19 LYS 135 -0.13 PRO 1

SER 144 0.11 ILE 136 -0.11 PRO 1

SER 144 0.09 VAL 137 -0.15 PRO 1

SER 144 0.15 ARG 138 -0.15 PRO 1

SER 144 0.17 MET 139 -0.11 PRO 1

PRO 142 0.09 TYR 140 -0.12 PRO 1

SER 144 0.07 SER 141 -0.15 PRO 1

TYR 140 0.09 PRO 142 -0.14 PRO 1

MET 139 0.11 THR 143 -0.16 PRO 1

MET 139 0.17 SER 144 -0.17 PRO 1

GLU 74 0.15 ILE 145 -0.20 PRO 1

GLU 74 0.17 LEU 146 -0.20 PRO 1

GLU 74 0.13 ASP 147 -0.18 PRO 1

GLU 74 0.12 ILE 148 -0.21 PRO 1

LEU 78 0.12 ARG 149 -0.22 PRO 1

LEU 78 0.11 GLN 150 -0.23 PRO 1

LEU 78 0.09 GLY 151 -0.21 PRO 1

LEU 78 0.09 PRO 152 -0.21 PRO 1

LEU 78 0.08 LYS 153 -0.22 PRO 1

LEU 78 0.08 GLU 154 -0.23 PRO 1

LEU 78 0.08 PRO 155 -0.26 PRO 1

LEU 78 0.10 PHE 156 -0.28 PRO 1

LEU 78 0.08 ARG 157 -0.30 GLU 24

LEU 78 0.07 ASP 158 -0.29 GLU 24

LEU 78 0.09 TYR 159 -0.25 PRO 1

LEU 78 0.10 VAL 160 -0.28 PRO 1

LEU 78 0.08 ASP 161 -0.31 GLU 24

LEU 78 0.08 ARG 162 -0.23 PRO 1

LEU 78 0.11 PHE 163 -0.25 PRO 1

LEU 78 0.11 TYR 164 -0.27 PRO 1

LEU 78 0.08 LYS 165 -0.24 PRO 1

LEU 78 0.10 THR 166 -0.22 PRO 1

LEU 78 0.14 LEU 167 -0.25 PRO 1

LEU 78 0.12 ARG 168 -0.25 PRO 1

GLU 74 0.10 ALA 169 -0.21 PRO 1

LYS 135 0.16 GLU 170 -0.21 PRO 1

GLU 74 0.20 GLN 171 -0.21 PRO 1

GLU 74 0.26 ALA 172 -0.24 PRO 1

GLU 74 0.31 SER 173 -0.27 PRO 1

LEU 78 0.26 GLN 174 -0.32 PRO 1

LEU 78 0.28 GLU 175 -0.32 PRO 1

GLU 74 0.27 VAL 176 -0.28 PRO 1

LEU 78 0.22 LYS 177 -0.30 PRO 1

LEU 78 0.22 ASN 178 -0.34 PRO 1

LEU 78 0.23 TRP 179 -0.31 PRO 1

LEU 78 0.20 MET 180 -0.28 PRO 1

LEU 78 0.18 THR 181 -0.32 PRO 1

LEU 78 0.20 GLU 182 -0.33 PRO 1

LEU 78 0.20 THR 183 -0.30 PRO 1

ARG 77 0.19 LEU 184 -0.27 PRO 1

LEU 78 0.16 LEU 185 -0.28 PRO 1

LEU 78 0.16 VAL 186 -0.29 PRO 1

ARG 77 0.17 GLN 187 -0.26 PRO 1

ARG 77 0.15 ASN 188 -0.24 PRO 1

LEU 78 0.13 ALA 189 -0.26 PRO 1

LEU 78 0.12 ASN 190 -0.24 PRO 1

LEU 78 0.13 PRO 191 -0.25 PRO 1

LEU 78 0.12 ASP 192 -0.27 PRO 1

LEU 78 0.12 CYS 193 -0.28 PRO 1

LEU 78 0.14 LYS 194 -0.28 PRO 1

LEU 78 0.14 THR 195 -0.29 PRO 1

LEU 78 0.14 ILE 196 -0.31 PRO 1

LEU 78 0.15 LEU 197 -0.33 PRO 1

LEU 78 0.17 LYS 198 -0.32 PRO 1

LEU 78 0.16 ALA 199 -0.34 PRO 1

LEU 78 0.16 LEU 200 -0.36 PRO 1

LEU 78 0.18 GLY 201 -0.37 PRO 1

LEU 78 0.20 PRO 202 -0.38 PRO 1

LEU 78 0.19 GLY 203 -0.41 PRO 1

LEU 78 0.16 ALA 204 -0.40 PRO 1

LEU 78 0.15 THR 205 -0.41 PRO 1

LEU 78 0.13 LEU 206 -0.38 PRO 1

LEU 78 0.11 GLU 207 -0.40 PRO 1

LEU 78 0.12 GLU 208 -0.39 PRO 1

LEU 78 0.13 MET 209 -0.36 PRO 1

LEU 78 0.10 MET 210 -0.34 PRO 1

LEU 78 0.10 THR 211 -0.36 PRO 1

LEU 78 0.11 ALA 212 -0.34 PRO 1

LEU 78 0.11 CYS 213 -0.31 PRO 1

LEU 78 0.09 GLN 214 -0.31 PRO 1

LEU 78 0.08 GLY 215 -0.29 PRO 1

LEU 78 0.09 VAL 216 -0.27 PRO 1

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 9 ---

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

* 4XFX_unrelaxed_rank_001_alphafold2_ptm_model_4_seed_000 *