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

* EXP_1QNX_unrelaxed_rank_001_alphafold2_ptm_model_1_seed_000 *

CA distance fluctuations for 24021912510351363

--- normal mode 16 ---

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
SER 26 0.53 ALA 1 -0.33 ALA 110

GLY 25 0.64 GLU 2 -0.11 ALA 3

ASP 86 0.33 ALA 3 -0.25 ILE 11

ASP 86 0.47 GLU 4 -0.36 ILE 11

LEU 88 0.29 PHE 5 -0.13 ILE 11

ALA 110 0.45 ASN 6 -0.15 GLY 32

ALA 110 0.50 ASN 7 -0.33 ILE 11

VAL 109 0.50 TYR 8 -0.29 ILE 11

ALA 110 0.59 CYS 9 -0.43 LYS 23

ALA 110 0.94 LYS 10 -0.29 LYS 23

TYR 112 0.68 ILE 11 -0.36 GLU 4

GLN 113 0.73 LYS 12 -0.40 GLY 16

GLY 160 0.52 CYS 13 -0.27 GLU 4

LEU 157 0.71 LEU 14 -0.31 ALA 110

LEU 157 0.76 LYS 15 -0.19 ALA 110

LEU 157 0.57 GLY 16 -0.40 LYS 12

LEU 157 0.34 GLY 17 -0.20 GLY 32

GLY 115 0.28 VAL 18 -0.24 GLY 32

GLY 115 0.32 HIS 19 -0.20 LYS 201

GLU 2 0.32 THR 20 -0.30 LYS 201

GLU 2 0.35 ALA 21 -0.23 LYS 201

GLU 2 0.37 CYS 22 -0.29 CYS 9

GLU 2 0.38 LYS 23 -0.43 CYS 9

GLU 2 0.51 TYR 24 -0.27 CYS 9

GLU 2 0.64 GLY 25 -0.26 CYS 9

GLU 2 0.56 SER 26 -0.26 LYS 201

ALA 1 0.49 LEU 27 -0.31 LYS 201

ALA 1 0.49 LYS 28 -0.31 LYS 201

ALA 1 0.35 PRO 29 -0.35 LYS 201

ALA 1 0.33 ASN 30 -0.34 LYS 201

ALA 1 0.26 CYS 31 -0.39 LYS 201

ALA 1 0.25 GLY 32 -0.36 LYS 201

ALA 1 0.21 ASN 33 -0.35 LYS 201

ALA 1 0.21 LYS 34 -0.37 LYS 201

ALA 1 0.19 VAL 35 -0.34 LYS 201

ALA 1 0.22 VAL 36 -0.36 LYS 201

ALA 1 0.19 VAL 37 -0.35 LYS 201

ALA 1 0.21 SER 38 -0.37 LYS 201

ALA 1 0.25 TYR 39 -0.38 LYS 201

GLU 4 0.25 GLY 40 -0.38 LYS 201

GLU 4 0.27 LEU 41 -0.35 LYS 201

GLU 4 0.25 THR 42 -0.30 LYS 201

GLU 4 0.24 LYS 43 -0.29 LYS 201

GLU 4 0.24 GLN 44 -0.25 LYS 201

GLU 4 0.27 GLU 45 -0.29 LYS 201

GLU 4 0.32 LYS 46 -0.31 LYS 201

GLU 4 0.32 GLN 47 -0.30 LYS 80

GLU 4 0.28 ASP 48 -0.26 ALA 126

GLU 4 0.30 ILE 49 -0.28 LYS 201

LYS 10 0.34 LEU 50 -0.29 LYS 80

LYS 10 0.35 LYS 51 -0.26 TYR 128

LYS 10 0.34 GLU 52 -0.29 TYR 128

LYS 10 0.39 HIS 53 -0.28 TYR 128

LYS 10 0.42 ASN 54 -0.25 TYR 128

LYS 10 0.39 ASP 55 -0.27 TYR 128

LYS 10 0.40 PHE 56 -0.23 TYR 128

LYS 10 0.42 ARG 57 -0.24 TYR 128

LYS 10 0.41 GLN 58 -0.23 TYR 128

LYS 10 0.39 LYS 59 -0.19 ALA 126

LYS 10 0.39 ILE 60 -0.17 TYR 128

LYS 10 0.41 ALA 61 -0.20 TYR 128

LYS 10 0.37 ARG 62 -0.17 ALA 126

LYS 10 0.35 GLY 63 -0.12 LYS 143

LYS 10 0.35 LEU 64 -0.17 GLU 65

LYS 10 0.36 GLU 65 -0.17 LYS 143

LEU 14 0.31 THR 66 -0.17 LYS 143

LEU 14 0.34 ARG 67 -0.21 LYS 143

LEU 14 0.34 GLY 68 -0.14 GLU 204

LYS 15 0.32 ASN 69 -0.21 GLY 71

LEU 14 0.26 PRO 70 -0.22 GLU 204

LEU 14 0.28 GLY 71 -0.21 ASN 69

LEU 14 0.29 PRO 72 -0.17 THR 208

LEU 14 0.33 GLN 73 -0.13 LYS 143

LYS 150 0.47 PRO 74 -0.19 THR 208

LYS 150 0.43 PRO 75 -0.15 TYR 128

ASN 202 0.39 ALA 76 -0.19 TYR 128

ASN 202 0.46 LYS 77 -0.22 GLN 47

LYS 10 0.41 ASN 78 -0.28 MET 79

LYS 10 0.46 MET 79 -0.28 ASN 78

LYS 10 0.48 LYS 80 -0.30 ASN 81

LYS 10 0.48 ASN 81 -0.30 LYS 80

LYS 10 0.50 LEU 82 -0.28 GLN 47

LYS 10 0.47 VAL 83 -0.26 ASN 78

ASN 7 0.40 TRP 84 -0.25 LYS 201

ASN 7 0.43 ASN 85 -0.27 LYS 201

GLU 4 0.47 ASP 86 -0.28 LYS 201

GLU 4 0.42 GLU 87 -0.28 LYS 201

TYR 8 0.38 LEU 88 -0.34 LYS 201

GLU 4 0.31 ALA 89 -0.36 LYS 201

GLU 4 0.36 TYR 90 -0.33 LYS 201

GLU 139 0.26 VAL 91 -0.36 LYS 201

VAL 135 0.30 ALA 92 -0.45 LYS 201

GLU 2 0.26 GLN 93 -0.41 LYS 201

GLU 2 0.34 VAL 94 -0.37 LYS 201

GLU 2 0.31 TRP 95 -0.45 LYS 201

GLU 2 0.27 ALA 96 -0.46 LYS 201

GLU 2 0.29 ASN 97 -0.41 LYS 201

GLU 2 0.30 GLN 98 -0.41 LYS 201

GLU 2 0.25 CYS 99 -0.45 LYS 201

GLU 2 0.24 GLN 100 -0.49 LYS 201

GLU 2 0.22 TYR 101 -0.54 LYS 201

ASP 140 0.22 GLY 102 -0.63 LYS 201

GLU 141 0.28 HIS 103 -0.65 LYS 201

GLU 2 0.26 ASP 104 -0.56 LYS 201

HIS 161 0.33 THR 105 -0.43 LYS 201

GLY 115 0.39 CYS 106 -0.31 LYS 201

GLU 139 0.33 ARG 107 -0.36 LYS 201

VAL 114 0.53 ASP 108 -0.27 VAL 109

LYS 10 0.65 VAL 109 -0.28 ALA 1

LYS 10 0.94 ALA 110 -0.33 ALA 1

LYS 10 0.90 LYS 111 -0.33 ALA 1

LYS 10 0.74 TYR 112 -0.26 ALA 1

LYS 12 0.73 GLN 113 -0.28 LYS 201

LYS 12 0.53 VAL 114 -0.40 LYS 201

CYS 13 0.50 GLY 115 -0.58 LYS 201

LYS 15 0.37 GLN 116 -0.60 LYS 201

LYS 15 0.37 ASN 117 -0.60 LYS 201

ASP 140 0.30 VAL 118 -0.57 LYS 201

GLU 2 0.21 ALA 119 -0.64 LEU 157

GLU 2 0.21 LEU 120 -0.64 LEU 157

GLU 2 0.19 THR 121 -0.62 LEU 157

GLU 2 0.17 GLY 122 -0.52 LEU 157

GLU 2 0.14 SER 123 -0.45 LEU 157

PRO 70 0.15 THR 124 -0.35 LEU 157

ALA 1 0.11 ALA 125 -0.38 LEU 157

ALA 1 0.11 ALA 126 -0.36 LEU 157

ALA 1 0.12 LYS 127 -0.41 LEU 157

GLU 4 0.13 TYR 128 -0.45 LEU 157

GLU 4 0.18 ASP 129 -0.48 LEU 157

GLU 4 0.22 ASP 130 -0.40 LEU 157

GLU 4 0.24 PRO 131 -0.40 LEU 157

GLU 4 0.27 VAL 132 -0.35 LEU 157

GLU 4 0.23 LYS 133 -0.45 LEU 157

GLU 4 0.24 LEU 134 -0.53 LEU 157

CYS 192 0.30 VAL 135 -0.41 LEU 157

LYS 15 0.31 LYS 136 -0.39 LEU 157

ASP 140 0.33 MET 137 -0.54 LEU 157

LYS 15 0.40 TRP 138 -0.42 LEU 157

LYS 15 0.42 GLU 139 -0.29 LYS 158

LYS 15 0.41 ASP 140 -0.36 LYS 158

LYS 15 0.48 GLU 141 -0.35 LYS 158

LEU 14 0.43 VAL 142 -0.14 LYS 158

LYS 15 0.40 LYS 143 -0.21 ARG 67

LYS 15 0.42 ASP 144 -0.16 SER 152

LEU 14 0.40 TYR 145 -0.17 GLU 204

LEU 14 0.29 ASN 146 -0.25 GLU 204

LYS 149 0.32 PRO 147 -0.39 GLU 204

GLY 63 0.16 LYS 148 -0.48 GLU 204

LYS 209 0.39 LYS 149 -0.30 GLU 203

THR 208 0.62 LYS 150 -0.41 GLU 203

THR 208 0.51 PHE 151 -0.34 GLY 102

THR 208 0.43 SER 152 -0.49 GLY 102

LEU 14 0.43 GLY 153 -0.54 GLY 102

LEU 14 0.37 ASN 154 -0.49 GLY 102

LEU 14 0.51 ASP 155 -0.40 ALA 119

LEU 14 0.63 PHE 156 -0.53 ALA 119

LYS 15 0.76 LEU 157 -0.64 LEU 120

LYS 15 0.63 LYS 158 -0.45 MET 137

LYS 15 0.56 THR 159 -0.31 TRP 138

LYS 15 0.67 GLY 160 -0.42 ALA 119

LYS 15 0.57 HIS 161 -0.40 LYS 201

LEU 14 0.50 TYR 162 -0.27 TRP 138

LEU 14 0.52 THR 163 -0.28 TRP 138

LEU 14 0.56 GLN 164 -0.31 LYS 201

LEU 14 0.48 MET 165 -0.26 TYR 128

LYS 12 0.46 VAL 166 -0.22 TYR 128

LYS 12 0.48 TRP 167 -0.25 TYR 128

LYS 12 0.47 ALA 168 -0.25 LYS 148

LYS 10 0.55 ASN 169 -0.28 LYS 148

LYS 10 0.56 THR 170 -0.24 VAL 173

LYS 10 0.57 LYS 171 -0.20 LYS 43

LYS 10 0.53 GLU 172 -0.22 LYS 201

LYS 10 0.44 VAL 173 -0.31 LYS 201

LYS 10 0.33 GLY 174 -0.35 LYS 201

GLU 4 0.30 CYS 175 -0.42 LYS 201

GLU 4 0.27 GLY 176 -0.43 LYS 201

GLU 4 0.23 SER 177 -0.44 LYS 201

ALA 1 0.23 ILE 178 -0.42 LYS 201

ALA 1 0.20 LYS 179 -0.40 LYS 201

ALA 1 0.20 TYR 180 -0.38 LYS 201

ALA 1 0.16 ILE 181 -0.36 LYS 201

ALA 1 0.18 GLN 182 -0.33 LYS 201

TYR 101 0.16 GLU 183 -0.32 VAL 35

PRO 70 0.15 LYS 184 -0.35 ILE 181

TYR 101 0.17 TRP 185 -0.34 LEU 157

ALA 1 0.15 HIS 186 -0.41 LEU 157

ALA 1 0.18 LYS 187 -0.46 LEU 157

GLU 2 0.19 HIS 188 -0.49 LEU 157

GLU 2 0.22 TYR 189 -0.47 LYS 201

GLU 4 0.23 LEU 190 -0.48 LYS 201

VAL 135 0.28 VAL 191 -0.50 LYS 201

VAL 135 0.30 CYS 192 -0.48 LYS 201

LYS 10 0.36 ASN 193 -0.46 LYS 201

ASP 108 0.49 TYR 194 -0.42 GLY 198

LYS 10 0.58 GLY 195 -0.28 LYS 201

LYS 10 0.62 PRO 196 -0.25 LYS 201

LYS 12 0.62 SER 197 -0.42 GLY 115

LEU 14 0.56 GLY 198 -0.42 TYR 194

LEU 14 0.59 ASN 199 -0.54 ASN 117

LEU 14 0.44 PHE 200 -0.47 GLY 115

GLU 203 0.46 LYS 201 -0.65 HIS 103

GLN 207 0.61 ASN 202 -0.49 HIS 103

LYS 201 0.46 GLU 203 -0.44 LYS 148

GLN 207 0.54 GLU 204 -0.48 LYS 148

LEU 14 0.42 LEU 205 -0.35 LYS 148

LYS 12 0.40 TYR 206 -0.29 LYS 148

ASN 202 0.61 GLN 207 -0.23 LYS 148

LYS 150 0.62 THR 208 -0.19 PRO 74

LYS 150 0.60 LYS 209 -0.17 GLN 47

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.

*** EXP_1QNX_unrelaxed_rank_001_alphafold2_ptm_model_1_seed_000 ***

CA distance fluctuations for 24021912510351363

--- normal mode 16 ---

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

* EXP_1QNX_unrelaxed_rank_001_alphafold2_ptm_model_1_seed_000 *