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

* 1QNX_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000 *

CA distance fluctuations for 240220091312161517

--- 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 25 0.29 ALA 1 -1.36 ASP 86

LYS 23 0.60 GLU 2 -0.73 ASP 86

LYS 23 0.27 ALA 3 -0.45 GLU 87

PHE 5 0.32 GLU 4 -0.57 GLU 87

GLU 4 0.32 PHE 5 -0.36 LEU 157

GLU 2 0.37 ASN 6 -0.29 LEU 157

GLU 2 0.12 ASN 7 -0.35 LEU 157

GLU 2 0.17 TYR 8 -0.38 LEU 157

GLU 2 0.38 CYS 9 -0.31 LEU 157

GLU 2 0.26 LYS 10 -0.29 LEU 157

ASN 78 0.18 ILE 11 -0.35 GLY 153

TYR 112 0.26 LYS 12 -0.35 GLY 153

CYS 9 0.22 CYS 13 -0.45 GLY 153

GLU 183 0.19 LEU 14 -0.45 GLY 153

GLU 183 0.23 LYS 15 -0.55 GLY 153

GLU 2 0.31 GLY 16 -0.48 ASN 154

GLU 2 0.38 GLY 17 -0.49 ASN 154

GLU 2 0.48 VAL 18 -0.45 ASN 154

GLU 2 0.33 HIS 19 -0.45 LEU 157

GLU 2 0.26 THR 20 -0.51 LEU 157

GLU 2 0.22 ALA 21 -0.46 LEU 157

GLU 2 0.51 CYS 22 -0.39 LEU 157

GLU 2 0.60 LYS 23 -0.42 LEU 157

GLU 2 0.48 TYR 24 -0.43 LEU 157

GLU 2 0.39 GLY 25 -0.40 LEU 157

ALA 1 0.26 SER 26 -0.41 LEU 157

GLU 4 0.07 LEU 27 -0.43 LEU 157

ALA 1 0.15 LYS 28 -0.40 LEU 157

SER 38 0.14 PRO 29 -0.41 LEU 157

GLU 2 0.18 ASN 30 -0.40 LEU 157

TYR 101 0.17 CYS 31 -0.33 LEU 157

TYR 101 0.27 GLY 32 -0.27 GLU 183

TYR 101 0.35 ASN 33 -0.37 LYS 28

TYR 101 0.35 LYS 34 -0.37 GLU 183

TYR 101 0.27 VAL 35 -0.53 GLU 183

TYR 101 0.18 VAL 36 -0.37 LYS 184

ALA 126 0.15 VAL 37 -0.43 LYS 184

LYS 127 0.15 SER 38 -0.54 THR 42

TYR 128 0.13 TYR 39 -0.41 LEU 157

TYR 128 0.12 GLY 40 -0.45 LEU 157

LYS 80 0.13 LEU 41 -0.51 ALA 1

ASP 86 0.18 THR 42 -0.54 SER 38

TRP 84 0.35 LYS 43 -0.59 ALA 1

LYS 80 0.23 GLN 44 -0.56 ALA 1

SER 123 0.22 GLU 45 -0.58 ALA 1

LYS 80 0.21 LYS 46 -0.74 ALA 1

LYS 80 0.30 GLN 47 -0.75 ALA 1

SER 123 0.30 ASP 48 -0.64 ALA 1

THR 121 0.35 ILE 49 -0.68 ALA 1

THR 121 0.29 LEU 50 -0.79 ALA 1

SER 123 0.34 LYS 51 -0.72 ALA 1

SER 123 0.37 GLU 52 -0.64 ALA 1

THR 121 0.35 HIS 53 -0.68 ALA 1

SER 123 0.31 ASN 54 -0.69 ALA 1

SER 123 0.34 ASP 55 -0.62 ALA 1

SER 123 0.30 PHE 56 -0.59 ALA 1

SER 123 0.27 ARG 57 -0.59 ALA 1

SER 123 0.27 GLN 58 -0.56 ALA 1

SER 123 0.25 LYS 59 -0.52 ALA 1

GLU 183 0.23 ILE 60 -0.51 ALA 1

GLU 183 0.22 ALA 61 -0.49 ALA 1

GLU 183 0.20 ARG 62 -0.46 ALA 1

GLU 183 0.19 GLY 63 -0.44 ALA 1

GLU 183 0.19 LEU 64 -0.46 ALA 1

GLU 183 0.21 GLU 65 -0.47 ALA 1

ASN 154 0.19 THR 66 -0.44 ALA 1

ASN 154 0.21 ARG 67 -0.44 ALA 1

ASN 154 0.26 GLY 68 -0.44 ALA 1

ASN 154 0.28 ASN 69 -0.42 ALA 1

ASN 154 0.23 PRO 70 -0.40 ALA 1

ASN 154 0.20 GLY 71 -0.42 ALA 1

GLY 63 0.18 PRO 72 -0.42 ALA 1

GLU 183 0.19 GLN 73 -0.44 ALA 1

LYS 148 0.25 PRO 74 -0.41 ALA 1

LYS 148 0.24 PRO 75 -0.43 ALA 1

LYS 148 0.24 ALA 76 -0.44 ALA 1

VAL 83 0.25 LYS 77 -0.41 ALA 1

LYS 171 0.34 ASN 78 -0.43 ALA 1

ALA 76 0.23 MET 79 -0.54 ALA 1

ASN 81 0.34 LYS 80 -0.59 ALA 1

LYS 80 0.34 ASN 81 -0.71 ALA 1

LYS 43 0.27 LEU 82 -0.80 ALA 1

LYS 80 0.32 VAL 83 -0.97 ALA 1

LYS 43 0.35 TRP 84 -1.07 ALA 1

LYS 43 0.33 ASN 85 -1.22 ALA 1

LYS 43 0.31 ASP 86 -1.36 ALA 1

LYS 43 0.24 GLU 87 -1.13 ALA 1

LYS 43 0.19 LEU 88 -0.88 ALA 1

GLU 87 0.16 ALA 89 -0.83 ALA 1

ASN 78 0.09 TYR 90 -0.73 ALA 1

ALA 89 0.13 VAL 91 -0.52 LEU 157

ASN 78 0.11 ALA 92 -0.58 LEU 157

ASN 78 0.09 GLN 93 -0.53 LEU 157

ASN 78 0.09 VAL 94 -0.52 LEU 157

ASN 78 0.10 TRP 95 -0.58 LEU 157

LYS 80 0.10 ALA 96 -0.57 LEU 157

ASN 78 0.08 ASN 97 -0.49 LEU 157

GLU 2 0.17 GLN 98 -0.49 LEU 157

VAL 35 0.20 CYS 99 -0.45 LEU 157

ASN 33 0.28 GLN 100 -0.50 LEU 157

GLN 182 0.43 TYR 101 -0.62 LEU 157

GLU 183 0.41 GLY 102 -0.80 LEU 157

GLU 183 0.32 HIS 103 -0.88 LEU 157

GLU 183 0.22 ASP 104 -0.70 LEU 157

GLU 2 0.23 THR 105 -0.64 ASN 154

GLU 2 0.19 CYS 106 -0.55 LEU 157

GLU 183 0.13 ARG 107 -0.55 LEU 157

ASN 78 0.15 ASP 108 -0.48 GLY 153

LYS 43 0.18 VAL 109 -0.55 ALA 1

LYS 43 0.19 ALA 110 -0.48 ALA 1

LYS 12 0.22 LYS 111 -0.62 ALA 1

LYS 12 0.26 TYR 112 -0.56 ALA 1

LYS 12 0.23 GLN 113 -0.48 ALA 1

GLU 183 0.20 VAL 114 -0.56 ALA 1

SER 197 0.30 GLY 115 -0.55 ALA 1

GLU 183 0.29 GLN 116 -0.69 LEU 157

GLU 183 0.32 ASN 117 -0.65 LEU 157

GLU 183 0.37 VAL 118 -0.72 LEU 157

GLU 183 0.36 ALA 119 -0.57 LYS 158

TRP 185 0.42 LEU 120 -0.46 LYS 158

LEU 134 0.51 THR 121 -0.32 ASP 144

TRP 185 0.46 GLY 122 -0.25 ASN 69

ASP 129 0.46 SER 123 -0.19 ASN 69

LYS 136 0.32 THR 124 -0.14 GLN 182

ASP 55 0.19 ALA 125 -0.23 ASN 69

VAL 35 0.17 ALA 126 -0.27 ASN 69

SER 38 0.15 LYS 127 -0.34 ASP 144

SER 123 0.19 TYR 128 -0.38 ASP 144

SER 123 0.46 ASP 129 -0.40 ASP 144

SER 123 0.31 ASP 130 -0.36 ASP 144

THR 121 0.35 PRO 131 -0.45 ALA 1

SER 123 0.40 VAL 132 -0.51 ALA 1

SER 123 0.43 LYS 133 -0.42 ALA 1

THR 121 0.51 LEU 134 -0.43 ALA 1

THR 121 0.44 VAL 135 -0.56 ALA 1

SER 123 0.37 LYS 136 -0.51 ALA 1

GLU 183 0.41 MET 137 -0.46 ALA 1

GLU 183 0.39 TRP 138 -0.51 ALA 1

GLU 183 0.32 GLU 139 -0.54 ALA 1

GLU 183 0.33 ASP 140 -0.49 ALA 1

GLU 183 0.30 GLU 141 -0.50 ALA 1

GLU 183 0.26 VAL 142 -0.49 ALA 1

ASN 154 0.21 LYS 143 -0.46 ALA 1

ASN 154 0.29 ASP 144 -0.47 ALA 1

ASN 154 0.29 TYR 145 -0.47 ALA 1

ASN 154 0.25 ASN 146 -0.41 ALA 1

TYR 206 0.19 PRO 147 -0.39 ALA 1

THR 208 0.33 LYS 148 -0.35 ALA 1

THR 208 0.23 LYS 149 -0.37 ALA 1

TYR 206 0.17 LYS 150 -0.37 ALA 1

GLU 183 0.21 PHE 151 -0.41 ALA 1

GLU 183 0.20 SER 152 -0.43 ALA 1

GLU 183 0.20 GLY 153 -0.60 THR 105

ASP 144 0.29 ASN 154 -0.69 HIS 103

GLU 183 0.20 ASP 155 -0.47 HIS 103

GLU 183 0.27 PHE 156 -0.53 GLN 116

GLU 183 0.22 LEU 157 -0.88 HIS 103

GLU 183 0.23 LYS 158 -0.64 GLY 102

GLU 183 0.29 THR 159 -0.50 ALA 1

GLU 183 0.34 GLY 160 -0.54 ALA 1

GLU 183 0.36 HIS 161 -0.54 ALA 1

GLU 183 0.33 TYR 162 -0.54 ALA 1

GLU 183 0.31 THR 163 -0.52 ALA 1

GLU 183 0.32 GLN 164 -0.58 ALA 1

GLU 183 0.30 MET 165 -0.63 ALA 1

GLU 183 0.28 VAL 166 -0.58 ALA 1

GLU 183 0.28 TRP 167 -0.56 ALA 1

GLU 183 0.25 ALA 168 -0.54 ALA 1

GLU 204 0.25 ASN 169 -0.58 ALA 1

GLU 183 0.24 THR 170 -0.67 ALA 1

ASN 78 0.34 LYS 171 -0.79 ALA 1

ASN 78 0.25 GLU 172 -0.90 ALA 1

THR 121 0.24 VAL 173 -0.87 ALA 1

THR 121 0.21 GLY 174 -0.90 ALA 1

THR 121 0.20 CYS 175 -0.70 ALA 1

HIS 188 0.14 GLY 176 -0.53 ALA 1

GLY 176 0.14 SER 177 -0.50 LEU 157

LYS 80 0.10 ILE 178 -0.44 LEU 157

LYS 80 0.10 LYS 179 -0.36 LEU 157

ALA 126 0.16 TYR 180 -0.30 LYS 184

TYR 101 0.26 ILE 181 -0.37 LYS 184

TYR 101 0.43 GLN 182 -0.23 TRP 185

TYR 101 0.42 GLU 183 -0.53 VAL 35

MET 137 0.30 LYS 184 -0.48 VAL 35

GLY 122 0.46 TRP 185 -0.23 GLN 182

LEU 120 0.19 HIS 186 -0.20 ASN 69

LEU 120 0.25 LYS 187 -0.25 LEU 157

ILE 49 0.25 HIS 188 -0.37 LEU 157

GLN 182 0.23 TYR 189 -0.49 LEU 157

THR 121 0.22 LEU 190 -0.52 LEU 157

TRP 185 0.22 VAL 191 -0.62 LEU 157

THR 121 0.25 CYS 192 -0.64 ALA 1

THR 121 0.22 ASN 193 -0.69 ALA 1

THR 121 0.22 TYR 194 -0.73 ALA 1

THR 121 0.20 GLY 195 -0.75 ALA 1

GLU 183 0.21 PRO 196 -0.66 ALA 1

GLY 115 0.30 SER 197 -0.58 ALA 1

GLU 183 0.31 GLY 198 -0.54 ALA 1

GLU 183 0.32 ASN 199 -0.49 ALA 1

GLU 183 0.30 PHE 200 -0.43 ALA 1

GLU 183 0.27 LYS 201 -0.41 ALA 1

GLU 183 0.23 ASN 202 -0.35 ALA 1

GLU 183 0.24 GLU 203 -0.37 ALA 1

ASN 169 0.25 GLU 204 -0.39 ALA 1

GLU 183 0.25 LEU 205 -0.47 ALA 1

LYS 148 0.25 TYR 206 -0.45 ALA 1

LYS 148 0.26 GLN 207 -0.39 ALA 1

LYS 148 0.33 THR 208 -0.39 ALA 1

LYS 148 0.23 LYS 209 -0.36 ALA 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.

*** 1QNX_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000 ***

CA distance fluctuations for 240220091312161517

--- normal mode 13 ---

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

* 1QNX_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000 *