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

* 2QLE_unrelaxed_rank_001_alphafold2_ptm_model_5_seed_000 *

CA distance fluctuations for 240220090021146876

--- normal mode 11 ---

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
ASN 206 0.52 GLY 1 -0.24 GLY 226

ASN 206 0.52 GLU 2 -0.25 GLY 226

ASN 206 0.57 GLU 3 -0.25 GLY 226

ASN 206 0.63 LEU 4 -0.20 GLY 226

ASN 206 0.63 PHE 5 -0.18 GLY 226

ASN 206 0.65 THR 6 -0.19 GLY 226

ASN 206 0.74 GLY 7 -0.16 GLY 226

ASN 206 0.83 VAL 8 -0.15 GLU 136

ASN 206 0.83 VAL 9 -0.14 HIS 133

ASN 206 0.91 PRO 10 -0.15 HIS 133

ASN 206 0.77 ILE 11 -0.14 HIS 133

ASN 206 0.70 LEU 12 -0.15 VAL 26

ASN 206 0.51 VAL 13 -0.12 LEU 12

ASN 206 0.41 GLU 14 -0.13 SER 25

ASN 206 0.25 LEU 15 -0.10 GLU 14

ASN 206 0.15 ASP 16 -0.15 LYS 208

GLN 151 0.14 GLY 17 -0.26 LYS 208

GLN 151 0.20 ASP 18 -0.37 LYS 208

GLN 151 0.24 VAL 19 -0.47 LYS 208

GLN 151 0.29 ASN 20 -0.53 PRO 205

GLN 151 0.24 GLY 21 -0.49 LYS 208

GLN 151 0.19 HIS 22 -0.58 LYS 208

HIS 133 0.16 LYS 23 -0.42 LYS 208

LEU 135 0.15 PHE 24 -0.38 LYS 208

TYR 137 0.14 SER 25 -0.21 LYS 208

ASN 206 0.18 VAL 26 -0.15 LEU 12

ASN 206 0.38 SER 27 -0.15 VAL 26

ASN 206 0.50 GLY 28 -0.20 GLU 29

ASN 206 0.74 GLU 29 -0.20 GLY 28

ASN 206 0.86 GLY 30 -0.19 HIS 133

ASN 206 0.85 GLU 31 -0.17 HIS 133

ASN 206 0.71 GLY 32 -0.16 GLU 136

ASN 206 0.68 ASP 33 -0.17 GLU 136

ASN 206 0.57 ALA 34 -0.15 GLU 136

ASN 206 0.56 THR 35 -0.21 ASP 70

ASN 206 0.52 TYR 36 -0.19 GLU 136

ASN 206 0.48 GLY 37 -0.18 GLU 136

ASN 206 0.54 LYS 38 -0.20 GLU 136

ASN 206 0.56 LEU 39 -0.20 GLU 136

ASP 204 0.69 THR 40 -0.22 HIS 133

ASP 204 0.56 LEU 41 -0.24 HIS 133

ASP 204 0.53 LYS 42 -0.30 HIS 133

ASP 204 0.34 PHE 43 -0.23 HIS 133

VAL 26 0.17 ILE 44 -0.23 ASP 127

TYR 137 0.19 CYS 45 -0.28 LYS 208

TYR 137 0.16 THR 46 -0.19 LYS 208

TYR 137 0.20 THR 47 -0.35 LYS 208

TYR 137 0.25 GLY 48 -0.58 LYS 208

TYR 137 0.31 LYS 49 -0.78 LYS 208

TYR 137 0.26 LEU 50 -0.59 LYS 208

GLU 136 0.17 PRO 51 -0.69 LYS 208

LEU 135 0.20 VAL 52 -0.59 PRO 205

LEU 50 0.25 PRO 53 -0.57 PRO 205

TYR 137 0.19 TRP 54 -0.37 PRO 205

LEU 50 0.15 PRO 55 -0.31 PRO 205

GLN 151 0.13 THR 56 -0.32 PRO 205

GLN 177 0.12 LEU 57 -0.16 LYS 208

ASP 204 0.17 VAL 58 -0.11 LEU 39

ASP 204 0.20 THR 59 -0.06 GLN 63

ASP 204 0.22 THR 60 -0.05 ILE 117

ASN 206 0.32 PHE 61 -0.09 VAL 58

ASN 206 0.43 VAL 62 -0.07 VAL 58

ASN 206 0.41 GLN 63 -0.09 ASN 140

ASN 206 0.48 CYS 64 -0.11 GLY 226

ASN 206 0.52 PHE 65 -0.14 ASN 138

ASN 206 0.43 SER 66 -0.14 ASN 138

ASN 206 0.43 ARG 67 -0.16 ASN 138

ASN 206 0.39 TYR 68 -0.14 GLY 226

ASN 206 0.35 PRO 69 -0.14 ASN 138

ASN 206 0.35 ASP 70 -0.21 THR 35

ASN 206 0.31 HIS 71 -0.29 GLY 226

ASN 206 0.33 MET 72 -0.25 GLY 226

ASN 206 0.38 LYS 73 -0.30 GLY 226

ASN 206 0.35 ARG 74 -0.38 GLY 226

ASN 206 0.34 HIS 75 -0.26 GLY 226

ASN 206 0.38 ASP 76 -0.21 GLY 226

ASN 206 0.38 PHE 77 -0.19 GLY 226

ASN 206 0.42 PHE 78 -0.15 GLY 226

ASN 206 0.48 LYS 79 -0.20 GLY 226

ASN 206 0.44 SER 80 -0.24 GLY 226

ASN 206 0.44 ALA 81 -0.21 GLY 226

ASN 206 0.51 MET 82 -0.20 GLY 226

ASN 206 0.55 PRO 83 -0.19 GLY 226

ASN 206 0.49 GLU 84 -0.18 GLY 226

ASN 206 0.48 GLY 85 -0.16 GLY 226

ASN 206 0.41 TYR 86 -0.13 GLY 226

ASN 206 0.36 VAL 87 -0.09 GLY 226

ASN 206 0.31 GLN 88 -0.06 ASN 158

LYS 101 0.29 GLU 89 -0.12 GLN 177

TYR 100 0.32 ARG 90 -0.09 TYR 176

GLN 178 0.39 THR 91 -0.16 LYS 208

LYS 156 0.31 ILE 92 -0.21 PRO 205

LYS 156 0.33 PHE 93 -0.31 PRO 205

GLN 151 0.28 PHE 94 -0.42 PRO 205

GLN 151 0.31 LYS 95 -0.46 PRO 205

GLN 151 0.36 ASP 96 -0.58 PRO 205

GLN 151 0.34 ASP 97 -0.60 PRO 205

GLN 151 0.36 GLY 98 -0.52 PRO 205

GLN 151 0.35 ASN 99 -0.36 PRO 205

ARG 90 0.32 TYR 100 -0.26 PRO 205

LYS 152 0.33 LYS 101 -0.20 LYS 208

GLU 89 0.23 THR 102 -0.11 LYS 208

LYS 120 0.23 ARG 103 -0.08 ARG 90

ASN 206 0.33 ALA 104 -0.06 ASN 158

ASN 206 0.41 GLU 105 -0.09 GLY 226

ASN 206 0.48 VAL 106 -0.11 GLY 226

ASN 206 0.54 LYS 107 -0.14 GLY 226

ASN 206 0.63 PHE 108 -0.15 GLY 226

ASN 206 0.67 GLU 109 -0.14 GLY 226

ASN 206 0.73 GLY 110 -0.16 GLY 226

ASN 206 0.80 ASP 111 -0.16 GLY 226

ASN 206 0.80 THR 112 -0.13 GLY 226

ASN 206 0.69 LEU 113 -0.12 GLY 226

ASN 206 0.62 VAL 114 -0.10 GLY 226

ASN 206 0.50 ASN 115 -0.08 GLY 226

ASN 206 0.42 ARG 116 -0.07 GLY 226

ASN 206 0.30 ILE 117 -0.05 THR 60

ASN 206 0.19 GLU 118 -0.10 LYS 208

LYS 152 0.19 LEU 119 -0.18 LYS 208

LYS 152 0.27 LYS 120 -0.27 LYS 208

GLN 151 0.30 GLY 121 -0.37 LYS 208

GLN 151 0.36 ILE 122 -0.44 PRO 205

GLN 151 0.41 ASP 123 -0.55 PRO 205

GLN 151 0.33 PHE 124 -0.65 PRO 205

GLN 151 0.33 LYS 125 -0.80 PRO 205

GLN 151 0.28 GLU 126 -0.93 PRO 205

GLN 151 0.27 ASP 127 -1.05 PRO 205

GLN 151 0.29 GLY 128 -0.88 PRO 205

GLN 151 0.23 ASN 129 -0.82 PRO 205

GLN 151 0.22 ILE 130 -0.74 PRO 205

GLN 151 0.23 LEU 131 -0.87 PRO 205

GLN 151 0.21 GLY 132 -1.06 PRO 205

HIS 22 0.19 HIS 133 -1.02 PRO 205

GLN 151 0.17 LYS 134 -1.01 PRO 205

VAL 52 0.20 LEU 135 -0.74 PRO 205

LYS 49 0.27 GLU 136 -0.70 TYR 137

LYS 49 0.31 TYR 137 -0.70 GLU 136

LYS 49 0.21 ASN 138 -0.33 ALA 200

LYS 49 0.15 TYR 139 -0.22 GLN 198

LYS 49 0.12 ASN 140 -0.22 GLN 198

ASP 204 0.15 SER 141 -0.18 ASN 140

ASP 204 0.16 HIS 142 -0.08 SER 196

ASP 204 0.19 ASN 143 -0.04 GLY 168

ASP 204 0.22 VAL 144 -0.05 GLN 178

PHE 159 0.28 TYR 145 -0.06 GLN 178

ASN 206 0.25 ILE 146 -0.09 MET 147

TYR 176 0.29 MET 147 -0.09 ILE 146

TYR 176 0.29 ALA 148 -0.11 GLY 226

THR 91 0.36 ASP 149 -0.12 GLY 226

ASP 123 0.34 LYS 150 -0.17 GLY 226

ASP 123 0.41 GLN 151 -0.15 GLY 226

ASP 123 0.38 LYS 152 -0.14 GLY 226

ASP 123 0.31 ASN 153 -0.18 GLY 226

ASN 206 0.30 GLY 154 -0.14 GLY 226

THR 91 0.30 ILE 155 -0.08 GLY 226

TYR 176 0.45 LYS 156 -0.05 THR 180

TYR 176 0.25 VAL 157 -0.10 GLN 178

ASP 174 0.30 ASN 158 -0.09 GLU 89

TYR 145 0.28 PHE 159 -0.05 ARG 103

THR 224 0.19 LYS 160 -0.13 PRO 205

THR 224 0.14 ILE 161 -0.18 PRO 205

GLY 226 0.12 ARG 162 -0.28 PRO 205

GLN 151 0.12 HIS 163 -0.40 PRO 205

LYS 49 0.16 ASN 164 -0.51 PRO 205

GLN 151 0.14 ILE 165 -0.72 PRO 205

LYS 49 0.18 GLU 166 -0.87 PRO 205

LYS 134 0.15 ASP 167 -0.85 PRO 205

LYS 49 0.15 GLY 168 -0.66 PRO 205

GLN 151 0.14 SER 169 -0.62 PRO 205

GLN 151 0.15 VAL 170 -0.52 PRO 205

GLN 151 0.18 GLN 171 -0.52 PRO 205

LYS 156 0.19 LEU 172 -0.38 PRO 205

LYS 156 0.21 ALA 173 -0.30 PRO 205

ASN 158 0.30 ASP 174 -0.21 PRO 205

LYS 156 0.29 HIS 175 -0.10 LYS 208

LYS 156 0.45 TYR 176 -0.09 ARG 90

THR 91 0.35 GLN 177 -0.12 GLU 89

THR 91 0.39 GLN 178 -0.10 VAL 157

ASN 206 0.31 ASN 179 -0.07 GLY 226

ASN 206 0.33 THR 180 -0.12 GLY 226

ASN 206 0.38 PRO 181 -0.16 GLY 226

ASN 206 0.40 ILE 182 -0.15 GLY 226

ASN 206 0.41 GLY 183 -0.20 GLY 226

ASN 206 0.38 ASP 184 -0.23 GLY 226

ASN 206 0.40 GLY 185 -0.26 GLY 226

ASN 206 0.38 PRO 186 -0.30 GLY 226

ASN 206 0.38 VAL 187 -0.26 GLY 226

ASN 206 0.36 LEU 188 -0.30 GLY 226

ASN 206 0.31 LEU 189 -0.24 GLY 226

ASN 206 0.30 PRO 190 -0.21 GLY 226

ASN 206 0.26 ASP 191 -0.13 GLY 226

LYS 95 0.26 ASN 192 -0.07 HIS 193

ASN 206 0.25 HIS 193 -0.07 ALA 148

ASN 206 0.24 TYR 194 -0.08 MET 147

ASN 206 0.28 LEU 195 -0.08 ASN 140

ASN 206 0.24 SER 196 -0.13 ASN 140

ASP 204 0.25 THR 197 -0.16 ASN 140

ASP 204 0.25 GLN 198 -0.22 ASN 140

ASP 204 0.23 VAL 199 -0.26 ASN 138

ASP 204 0.21 ALA 200 -0.33 ASN 138

SER 141 0.14 LEU 201 -0.34 GLU 136

ALA 200 0.16 SER 202 -0.44 HIS 133

THR 40 0.35 LYS 203 -0.77 HIS 133

GLY 30 0.72 ASP 204 -0.63 HIS 133

VAL 8 0.74 PRO 205 -1.06 GLY 132

PRO 10 0.91 ASN 206 -0.78 ASP 127

GLY 30 0.57 GLU 207 -0.62 GLY 132

GLY 30 0.28 LYS 208 -0.78 LYS 49

TYR 137 0.11 ARG 209 -0.43 GLU 126

TYR 137 0.18 ASP 210 -0.51 LYS 208

ARG 209 0.08 HIS 211 -0.43 HIS 133

ASP 204 0.13 MET 212 -0.42 HIS 133

ASP 204 0.41 VAL 213 -0.36 HIS 133

ASP 204 0.37 LEU 214 -0.28 HIS 133

ASP 204 0.49 LEU 215 -0.26 GLU 136

ASP 204 0.39 GLU 216 -0.24 ASN 138

ASN 206 0.38 PHE 217 -0.22 ASN 138

ASN 206 0.36 VAL 218 -0.17 GLU 136

ASN 206 0.35 THR 219 -0.15 ASN 140

ASN 206 0.33 ALA 220 -0.10 ASN 140

ASN 206 0.27 ALA 221 -0.08 GLU 136

ASN 206 0.24 GLY 222 -0.06 PRO 190

ASN 206 0.26 ILE 223 -0.06 PRO 186

ASN 206 0.26 THR 224 -0.12 ARG 74

ASN 206 0.26 HIS 225 -0.26 HIS 71

ASN 206 0.23 GLY 226 -0.38 ARG 74

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.

*** 2QLE_unrelaxed_rank_001_alphafold2_ptm_model_5_seed_000 ***

CA distance fluctuations for 240220090021146876

--- normal mode 11 ---

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

* 2QLE_unrelaxed_rank_001_alphafold2_ptm_model_5_seed_000 *