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 15 ---

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 0.30 ALA 1 -0.84 GLU 87

CYS 22 0.51 GLU 2 -0.20 LEU 27

LYS 43 0.41 ALA 3 -0.17 ILE 11

LYS 43 0.55 GLU 4 -0.34 ILE 11

LYS 43 0.38 PHE 5 -0.22 GLY 25

ALA 110 0.46 ASN 6 -0.25 GLY 25

ALA 110 0.50 ASN 7 -0.25 GLU 4

VAL 109 0.50 TYR 8 -0.27 ILE 11

ALA 110 0.57 CYS 9 -0.46 LYS 23

ALA 110 0.95 LYS 10 -0.31 LYS 23

LYS 111 0.69 ILE 11 -0.34 GLU 4

GLN 113 0.71 LYS 12 -0.27 GLY 16

GLY 115 0.47 CYS 13 -0.29 ALA 1

LEU 157 0.66 LEU 14 -0.31 ALA 110

LEU 157 0.57 LYS 15 -0.28 ASN 202

LEU 157 0.41 GLY 16 -0.27 LYS 12

GLU 2 0.30 GLY 17 -0.25 LYS 201

GLU 2 0.40 VAL 18 -0.23 LYS 201

GLU 2 0.30 HIS 19 -0.24 LYS 201

LYS 43 0.26 THR 20 -0.33 LYS 201

LYS 43 0.32 ALA 21 -0.27 LYS 201

GLU 2 0.51 CYS 22 -0.36 CYS 9

GLU 2 0.44 LYS 23 -0.46 CYS 9

GLU 2 0.33 TYR 24 -0.34 CYS 9

ALA 1 0.30 GLY 25 -0.36 CYS 9

ALA 1 0.30 SER 26 -0.28 LYS 201

LYS 43 0.18 LEU 27 -0.32 LYS 201

ALA 1 0.18 LYS 28 -0.31 LYS 201

ALA 1 0.09 PRO 29 -0.35 LYS 201

ALA 1 0.15 ASN 30 -0.34 LYS 201

ALA 1 0.09 CYS 31 -0.38 LYS 201

ALA 1 0.13 GLY 32 -0.35 LYS 201

ALA 1 0.10 ASN 33 -0.34 LYS 201

ASN 69 0.05 LYS 34 -0.36 LYS 201

ASN 69 0.05 VAL 35 -0.34 LYS 201

LYS 143 0.05 VAL 36 -0.36 LYS 201

TYR 180 0.06 VAL 37 -0.38 THR 42

LYS 187 0.05 SER 38 -0.43 THR 42

ASP 130 0.11 TYR 39 -0.37 LYS 201

ASP 130 0.15 GLY 40 -0.37 LYS 201

GLU 4 0.28 LEU 41 -0.39 SER 38

GLU 4 0.37 THR 42 -0.43 SER 38

ASP 86 0.58 LYS 43 -0.43 LYS 127

GLU 4 0.43 GLN 44 -0.52 LYS 127

GLU 4 0.30 GLU 45 -0.42 TYR 128

ALA 89 0.39 LYS 46 -0.29 TYR 128

GLU 87 0.40 GLN 47 -0.35 LYS 127

ASN 7 0.31 ASP 48 -0.40 TYR 128

LYS 10 0.30 ILE 49 -0.38 TYR 128

LYS 10 0.38 LEU 50 -0.31 LYS 80

LYS 10 0.38 LYS 51 -0.35 TYR 128

LYS 10 0.35 GLU 52 -0.36 TYR 128

LYS 10 0.39 HIS 53 -0.34 TYR 128

LYS 10 0.43 ASN 54 -0.32 TYR 128

LYS 10 0.39 ASP 55 -0.33 TYR 128

LYS 10 0.39 PHE 56 -0.29 TYR 128

LYS 10 0.41 ARG 57 -0.30 TYR 128

LYS 10 0.39 GLN 58 -0.28 TYR 128

LYS 10 0.37 LYS 59 -0.25 ALA 125

LYS 10 0.36 ILE 60 -0.22 TYR 128

LYS 10 0.37 ALA 61 -0.24 TYR 128

LYS 10 0.35 ARG 62 -0.22 ALA 125

LYS 10 0.32 GLY 63 -0.18 ALA 1

LYS 10 0.33 LEU 64 -0.16 ALA 125

LYS 10 0.34 GLU 65 -0.16 LEU 64

LYS 10 0.29 THR 66 -0.15 LYS 143

LEU 14 0.31 ARG 67 -0.18 LYS 143

LEU 14 0.31 GLY 68 -0.10 THR 66

LEU 14 0.29 ASN 69 -0.17 GLY 71

LEU 14 0.23 PRO 70 -0.21 GLY 71

LEU 14 0.25 GLY 71 -0.21 PRO 70

LYS 10 0.26 PRO 72 -0.13 THR 208

LYS 10 0.28 GLN 73 -0.17 ALA 1

LYS 150 0.35 PRO 74 -0.22 ALA 1

LYS 150 0.33 PRO 75 -0.23 ALA 1

ASN 202 0.37 ALA 76 -0.28 ALA 1

ASN 202 0.43 LYS 77 -0.33 ALA 1

ASN 202 0.37 ASN 78 -0.37 ALA 1

LYS 10 0.42 MET 79 -0.31 ALA 1

LYS 10 0.46 LYS 80 -0.34 ALA 1

LYS 10 0.48 ASN 81 -0.34 LYS 80

LYS 10 0.50 LEU 82 -0.35 ALA 1

LYS 10 0.49 VAL 83 -0.40 ALA 1

LYS 10 0.45 TRP 84 -0.44 ALA 1

ASN 7 0.47 ASN 85 -0.59 ALA 1

LYS 43 0.58 ASP 86 -0.70 ALA 1

LYS 43 0.54 GLU 87 -0.84 ALA 1

TYR 8 0.42 LEU 88 -0.57 ALA 1

LYS 43 0.48 ALA 89 -0.51 ALA 1

LYS 43 0.50 TYR 90 -0.52 ALA 1

LYS 43 0.39 VAL 91 -0.37 ALA 1

LYS 43 0.32 ALA 92 -0.44 LYS 201

LYS 43 0.28 GLN 93 -0.41 LYS 201

LYS 43 0.25 VAL 94 -0.38 LYS 201

LYS 43 0.20 TRP 95 -0.45 LYS 201

LYS 143 0.14 ALA 96 -0.46 LYS 201

LYS 143 0.11 ASN 97 -0.40 LYS 201

LYS 143 0.11 GLN 98 -0.41 LYS 201

LYS 143 0.10 CYS 99 -0.44 LYS 201

LYS 143 0.13 GLN 100 -0.48 LYS 201

LYS 143 0.16 TYR 101 -0.53 LYS 201

LYS 143 0.19 GLY 102 -0.62 LYS 201

GLU 141 0.23 HIS 103 -0.66 LYS 201

GLU 141 0.21 ASP 104 -0.57 LYS 201

GLU 141 0.23 THR 105 -0.52 LYS 201

HIS 161 0.30 CYS 106 -0.36 LYS 201

ASN 193 0.30 ARG 107 -0.36 LYS 201

TYR 194 0.48 ASP 108 -0.41 ALA 1

LYS 10 0.69 VAL 109 -0.53 ALA 1

LYS 10 0.95 ALA 110 -0.52 ALA 1

LYS 10 0.89 LYS 111 -0.57 ALA 1

LYS 10 0.73 TYR 112 -0.48 ALA 1

LYS 12 0.71 GLN 113 -0.41 ALA 1

LYS 12 0.51 VAL 114 -0.42 ALA 1

LEU 14 0.51 GLY 115 -0.54 LYS 201

LEU 14 0.38 GLN 116 -0.58 LYS 201

LEU 14 0.36 ASN 117 -0.59 LYS 201

ASP 140 0.27 VAL 118 -0.57 LYS 201

LEU 14 0.19 ALA 119 -0.53 LYS 201

LEU 14 0.14 LEU 120 -0.52 LEU 157

LEU 14 0.12 THR 121 -0.53 LEU 157

LYS 127 0.13 GLY 122 -0.45 LEU 157

LEU 14 0.09 SER 123 -0.44 ASP 129

LEU 14 0.08 THR 124 -0.36 LEU 157

LEU 14 0.06 ALA 125 -0.44 GLN 44

PRO 70 0.04 ALA 126 -0.48 GLN 44

GLY 122 0.13 LYS 127 -0.52 GLN 44

GLY 122 0.12 TYR 128 -0.50 GLN 44

GLU 4 0.13 ASP 129 -0.44 SER 123

GLU 4 0.19 ASP 130 -0.43 TYR 128

GLY 176 0.21 PRO 131 -0.42 TYR 128

ALA 89 0.25 VAL 132 -0.37 TYR 128

LEU 14 0.21 LYS 133 -0.37 LEU 157

LEU 14 0.22 LEU 134 -0.43 LEU 157

CYS 192 0.30 VAL 135 -0.33 LYS 201

LEU 14 0.30 LYS 136 -0.34 LYS 158

LEU 14 0.30 MET 137 -0.45 LEU 157

LEU 14 0.37 TRP 138 -0.38 GLY 160

LEU 14 0.40 GLU 139 -0.28 LYS 158

LEU 14 0.38 ASP 140 -0.35 LYS 158

LEU 14 0.44 GLU 141 -0.34 LYS 158

LEU 14 0.40 VAL 142 -0.14 ASN 154

LEU 14 0.37 LYS 143 -0.18 ARG 67

LEU 14 0.39 ASP 144 -0.20 ASN 154

LEU 14 0.37 TYR 145 -0.12 ALA 1

LEU 14 0.27 ASN 146 -0.19 GLU 203

LYS 149 0.24 PRO 147 -0.32 LEU 205

ASN 154 0.12 LYS 148 -0.41 GLU 204

LYS 209 0.29 LYS 149 -0.29 GLU 203

THR 208 0.47 LYS 150 -0.34 GLU 203

GLN 207 0.37 PHE 151 -0.33 ALA 119

GLN 207 0.31 SER 152 -0.40 GLY 102

LEU 14 0.48 GLY 153 -0.47 GLY 102

LEU 14 0.48 ASN 154 -0.41 THR 121

LEU 14 0.46 ASP 155 -0.34 THR 121

LEU 14 0.58 PHE 156 -0.45 ALA 119

LEU 14 0.66 LEU 157 -0.53 THR 121

LEU 14 0.57 LYS 158 -0.43 MET 137

LEU 14 0.52 THR 159 -0.34 TRP 138

LEU 14 0.62 GLY 160 -0.41 ALA 119

LEU 14 0.52 HIS 161 -0.40 LYS 201

LEU 14 0.46 TYR 162 -0.30 TRP 138

LEU 14 0.46 THR 163 -0.29 TRP 138

LEU 14 0.52 GLN 164 -0.31 ASN 117

LEU 14 0.45 MET 165 -0.30 TYR 128

LYS 12 0.42 VAL 166 -0.26 TYR 128

LYS 12 0.42 TRP 167 -0.32 ALA 1

LYS 10 0.43 ALA 168 -0.34 ALA 1

LYS 10 0.51 ASN 169 -0.36 ALA 1

LYS 10 0.54 THR 170 -0.39 ALA 1

LYS 10 0.57 LYS 171 -0.41 ALA 1

LYS 10 0.53 GLU 172 -0.47 ALA 1

LYS 10 0.47 VAL 173 -0.40 ALA 1

LYS 10 0.36 GLY 174 -0.44 ALA 1

VAL 135 0.30 CYS 175 -0.38 LYS 201

LYS 43 0.25 GLY 176 -0.40 LYS 201

ASP 130 0.18 SER 177 -0.43 LYS 201

ASP 130 0.10 ILE 178 -0.41 LYS 201

LYS 187 0.05 LYS 179 -0.40 LYS 201

ASN 69 0.06 TYR 180 -0.38 LYS 201

ASN 69 0.05 ILE 181 -0.37 LYS 201

ASN 69 0.06 GLN 182 -0.37 LYS 201

LEU 14 0.06 GLU 183 -0.34 LYS 201

LEU 14 0.05 LYS 184 -0.33 LYS 201

LEU 14 0.07 TRP 185 -0.36 LEU 157

LEU 14 0.06 HIS 186 -0.37 LYS 201

TYR 128 0.10 LYS 187 -0.40 LYS 201

LEU 14 0.08 HIS 188 -0.43 LYS 201

LYS 143 0.12 TYR 189 -0.46 LYS 201

ALA 92 0.16 LEU 190 -0.48 LYS 201

VAL 135 0.26 VAL 191 -0.49 LYS 201

VAL 135 0.30 CYS 192 -0.46 LYS 201

LYS 10 0.37 ASN 193 -0.43 LYS 201

LYS 10 0.49 TYR 194 -0.38 ALA 1

LYS 10 0.58 GLY 195 -0.48 ALA 1

LYS 10 0.60 PRO 196 -0.44 ALA 1

LYS 12 0.57 SER 197 -0.50 GLY 115

LEU 14 0.50 GLY 198 -0.46 GLY 115

LEU 14 0.51 ASN 199 -0.54 ASN 117

LYS 12 0.33 PHE 200 -0.46 LYS 201

GLU 203 0.43 LYS 201 -0.66 HIS 103

GLN 207 0.58 ASN 202 -0.50 HIS 103

ASN 202 0.45 GLU 203 -0.39 LYS 148

GLN 207 0.49 GLU 204 -0.41 LYS 148

LYS 12 0.36 LEU 205 -0.33 LYS 148

ASN 202 0.38 TYR 206 -0.31 ALA 1

ASN 202 0.58 GLN 207 -0.33 ALA 1

ASN 202 0.51 THR 208 -0.29 ALA 1

ASN 202 0.49 LYS 209 -0.29 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 15 ---

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

* 1QNX_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000 *