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

* 1AOL_unrelaxed_rank_001_alphafold2_ptm_model_4_seed_000 *

CA distance fluctuations for 240220085659142820

--- 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
PRO 228 0.18 GLN 1 -0.31 GLN 168

PRO 228 0.27 VAL 2 -0.32 GLN 168

ARG 120 0.18 TYR 3 -0.29 GLN 168

ARG 226 0.22 ASN 4 -0.28 GLN 168

PRO 228 0.21 ILE 5 -0.31 VAL 169

VAL 227 0.19 THR 6 -0.29 VAL 169

PRO 228 0.21 TRP 7 -0.28 VAL 169

PRO 228 0.16 GLU 8 -0.22 VAL 169

PRO 228 0.16 VAL 9 -0.16 VAL 169

PRO 45 0.16 THR 10 -0.09 LYS 174

PRO 45 0.17 ASN 11 -0.07 ASP 13

PRO 45 0.31 GLY 12 -0.10 ASP 13

PRO 45 0.30 ASP 13 -0.11 PRO 128

PRO 45 0.23 ARG 14 -0.11 GLU 15

ARG 219 0.19 GLU 15 -0.11 ARG 14

VAL 227 0.18 THR 16 -0.11 LYS 174

VAL 227 0.20 VAL 17 -0.14 LYS 174

VAL 227 0.23 TRP 18 -0.25 LYS 174

VAL 227 0.26 ALA 19 -0.29 LYS 174

VAL 227 0.32 ILE 20 -0.38 VAL 169

VAL 227 0.36 SER 21 -0.37 VAL 169

PRO 228 0.43 GLY 22 -0.40 VAL 169

PRO 228 0.44 ASN 23 -0.36 GLN 168

PRO 228 0.43 HIS 24 -0.38 GLN 168

PRO 228 0.32 PRO 25 -0.35 GLN 168

ARG 120 0.21 LEU 26 -0.32 GLN 165

PRO 228 0.24 TRP 27 -0.32 GLN 165

PRO 228 0.37 THR 28 -0.38 GLN 165

PRO 228 0.40 TRP 29 -0.39 GLN 165

PRO 228 0.36 TRP 30 -0.41 LEU 161

PRO 228 0.36 PRO 31 -0.40 LEU 161

PRO 228 0.34 VAL 32 -0.48 LEU 161

PRO 228 0.26 LEU 33 -0.31 VAL 169

PRO 228 0.24 THR 34 -0.42 PRO 178

GLY 70 0.20 PRO 35 -0.20 TRP 30

GLY 70 0.22 ASP 36 -0.18 CYS 176

GLY 70 0.19 LEU 37 -0.14 TRP 30

GLY 70 0.17 CYS 38 -0.12 TRP 30

VAL 227 0.18 MET 39 -0.09 ILE 20

VAL 227 0.16 LEU 40 -0.07 ALA 122

VAL 227 0.16 ALA 41 -0.10 PRO 210

VAL 227 0.18 LEU 42 -0.08 ARG 208

GLY 74 0.19 SER 43 -0.11 SER 69

ASP 13 0.26 GLY 44 -0.13 SER 69

GLY 12 0.31 PRO 45 -0.22 SER 69

ASP 13 0.24 PRO 46 -0.30 SER 69

ASP 129 0.22 HIS 47 -0.29 SER 69

GLY 12 0.20 TRP 48 -0.18 SER 69

SER 76 0.20 GLY 49 -0.23 SER 69

VAL 227 0.18 LEU 50 -0.15 SER 69

ASP 13 0.22 GLU 51 -0.21 SER 69

GLY 74 0.25 TYR 52 -0.20 SER 69

VAL 227 0.20 GLN 53 -0.10 SER 69

VAL 227 0.23 ALA 54 -0.08 ARG 208

VAL 227 0.22 PRO 55 -0.06 ARG 208

VAL 227 0.24 TYR 56 -0.10 SER 57

VAL 227 0.23 SER 57 -0.10 TYR 56

GLY 70 0.27 SER 58 -0.17 ILE 20

GLY 70 0.30 PRO 59 -0.19 ILE 20

GLY 70 0.21 PRO 60 -0.14 ILE 20

GLY 70 0.26 GLY 61 -0.16 GLY 22

GLY 70 0.54 PRO 62 -0.21 GLY 22

GLY 70 0.68 PRO 63 -0.24 GLY 22

GLY 70 0.54 CYS 64 -0.20 GLY 22

SER 68 0.41 CYS 65 -0.23 GLY 67

TYR 52 0.18 SER 66 -0.16 SER 69

ALA 73 0.29 GLY 67 -0.36 CYS 79

CYS 64 0.48 SER 68 -0.15 SER 71

ASP 172 0.68 SER 69 -0.38 ARG 77

ASP 172 0.82 GLY 70 -0.38 ALA 73

GLY 67 0.24 SER 71 -0.17 ARG 77

GLY 67 0.24 SER 72 -0.14 GLY 22

GLY 67 0.29 ALA 73 -0.38 GLY 70

TYR 52 0.25 GLY 74 -0.28 SER 69

TYR 52 0.21 CYS 75 -0.14 VAL 32

GLY 49 0.20 SER 76 -0.15 SER 69

PRO 46 0.21 ARG 77 -0.38 SER 69

ASP 129 0.20 ASP 78 -0.28 GLY 67

SER 68 0.27 CYS 79 -0.36 GLY 67

SER 68 0.28 ASP 80 -0.36 GLY 67

ASP 129 0.19 GLU 81 -0.29 GLY 67

SER 68 0.16 PRO 82 -0.21 GLY 67

ASP 129 0.16 LEU 83 -0.16 GLY 67

ASP 129 0.22 THR 84 -0.20 SER 69

ASP 129 0.25 SER 85 -0.23 SER 69

ASP 129 0.30 LEU 86 -0.34 SER 69

ASP 129 0.24 THR 87 -0.27 SER 69

ASP 129 0.19 PRO 88 -0.14 SER 69

ASP 129 0.17 ARG 89 -0.15 SER 69

VAL 227 0.15 CYS 90 -0.12 VAL 32

LEU 50 0.17 ASN 91 -0.11 SER 69

GLY 70 0.21 THR 92 -0.15 VAL 32

GLY 70 0.43 ALA 93 -0.22 VAL 32

GLY 70 0.36 TRP 94 -0.22 VAL 32

SER 68 0.18 ASN 95 -0.17 VAL 32

GLY 70 0.27 ARG 96 -0.21 VAL 32

GLY 70 0.38 LEU 97 -0.27 VAL 32

GLY 70 0.25 LYS 98 -0.24 GLY 67

GLY 70 0.20 LEU 99 -0.19 VAL 32

GLY 70 0.29 ASP 100 -0.26 VAL 32

GLY 70 0.29 GLN 101 -0.25 GLY 67

GLY 70 0.18 VAL 102 -0.22 GLY 67

GLY 70 0.20 THR 103 -0.19 GLY 67

GLY 70 0.24 HIS 104 -0.23 GLY 67

GLY 70 0.21 LYS 105 -0.24 GLY 67

GLY 70 0.18 SER 106 -0.21 GLY 67

PRO 228 0.15 SER 107 -0.21 GLY 67

PRO 228 0.14 GLU 108 -0.19 GLY 67

PRO 228 0.16 GLY 109 -0.17 GLY 67

PRO 228 0.16 PHE 110 -0.16 GLU 121

PRO 228 0.16 TYR 111 -0.20 GLU 121

PRO 228 0.17 VAL 112 -0.18 GLU 121

PRO 228 0.14 CYS 113 -0.18 ALA 122

PRO 228 0.14 PRO 114 -0.14 ALA 122

ARG 120 0.29 GLY 115 -0.06 LEU 161

ARG 120 0.49 SER 116 -0.07 LEU 161

ARG 120 0.37 HIS 117 -0.09 LEU 161

PRO 119 0.28 ARG 118 -0.09 LEU 161

ARG 118 0.28 PRO 119 -0.19 SER 150

SER 116 0.49 ARG 120 -0.20 GLY 137

SER 192 0.22 GLU 121 -0.46 GLY 137

SER 192 0.13 ALA 122 -0.32 CYS 138

GLY 126 0.21 LYS 123 -0.16 GLY 137

LEU 86 0.17 SER 124 -0.06 PRO 148

LEU 86 0.17 CYS 125 -0.11 ALA 122

LEU 86 0.23 GLY 126 -0.07 ASP 13

ARG 120 0.30 GLY 127 -0.08 ASP 13

ARG 120 0.25 PRO 128 -0.11 ASP 13

LEU 86 0.30 ASP 129 -0.11 SER 69

LEU 86 0.26 SER 130 -0.09 SER 69

LEU 86 0.21 PHE 131 -0.09 ASP 13

ARG 120 0.18 TYR 132 -0.08 ASP 13

SER 85 0.15 CYS 133 -0.12 ALA 122

ARG 208 0.22 ALA 134 -0.08 ASP 13

ARG 208 0.16 SER 135 -0.19 GLU 121

PRO 228 0.13 TRP 136 -0.30 GLU 121

PRO 228 0.14 GLY 137 -0.46 GLU 121

PRO 228 0.14 CYS 138 -0.34 GLU 121

PRO 228 0.16 GLU 139 -0.32 GLU 121

PRO 228 0.18 THR 140 -0.33 GLU 121

PRO 228 0.20 THR 141 -0.28 GLU 121

PRO 228 0.19 GLY 142 -0.23 GLU 121

PRO 228 0.18 ARG 143 -0.23 GLU 121

PRO 228 0.17 VAL 144 -0.24 GLU 121

PRO 228 0.18 TYR 145 -0.26 GLU 121

PRO 228 0.18 TRP 146 -0.32 GLU 121

PRO 228 0.20 LYS 147 -0.33 GLU 121

PRO 228 0.19 PRO 148 -0.37 GLU 121

PRO 228 0.21 SER 149 -0.35 GLU 121

PRO 228 0.19 SER 150 -0.34 GLU 121

PRO 228 0.19 SER 151 -0.21 GLU 121

PRO 228 0.17 TRP 152 -0.15 LEU 161

PRO 228 0.18 ASP 153 -0.15 LEU 161

PRO 228 0.19 TYR 154 -0.19 LEU 161

PRO 228 0.22 ILE 155 -0.20 LEU 161

PRO 228 0.23 THR 156 -0.21 VAL 157

PRO 228 0.22 VAL 157 -0.21 THR 156

PRO 228 0.22 ASP 158 -0.20 ASN 159

GLY 70 0.24 ASN 159 -0.30 VAL 32

GLY 70 0.27 ASN 160 -0.45 VAL 32

GLY 70 0.36 LEU 161 -0.48 VAL 32

GLY 70 0.37 THR 162 -0.38 VAL 32

GLY 70 0.38 THR 163 -0.33 VAL 32

SER 69 0.50 SER 164 -0.34 VAL 32

GLY 70 0.50 GLN 165 -0.42 VAL 32

GLY 70 0.48 ALA 166 -0.40 VAL 32

GLY 70 0.55 VAL 167 -0.35 VAL 32

GLY 70 0.69 GLN 168 -0.40 VAL 32

GLY 70 0.62 VAL 169 -0.40 GLY 22

GLY 70 0.58 CYS 170 -0.32 VAL 32

GLY 70 0.78 LYS 171 -0.33 GLY 22

GLY 70 0.82 ASP 172 -0.39 GLY 22

GLY 70 0.62 ASN 173 -0.30 GLY 22

GLY 70 0.52 LYS 174 -0.36 ILE 20

GLY 70 0.37 TRP 175 -0.31 ILE 20

GLY 70 0.40 CYS 176 -0.37 THR 34

GLY 70 0.28 ASN 177 -0.26 VAL 32

GLY 70 0.28 PRO 178 -0.42 THR 34

PRO 228 0.21 LEU 179 -0.24 PRO 178

PRO 228 0.24 ALA 180 -0.30 ILE 181

PRO 228 0.25 ILE 181 -0.30 ALA 180

PRO 228 0.28 GLN 182 -0.33 LEU 161

PRO 228 0.27 PHE 183 -0.32 LEU 161

PRO 228 0.26 THR 184 -0.28 LEU 161

PRO 228 0.27 ASN 185 -0.28 LEU 161

PRO 228 0.20 ALA 186 -0.22 LEU 161

PRO 228 0.20 GLY 187 -0.24 LEU 161

PRO 228 0.24 LYS 188 -0.28 LEU 161

ARG 120 0.21 GLN 189 -0.24 LEU 161

ARG 120 0.29 VAL 190 -0.21 LEU 161

ARG 120 0.32 THR 191 -0.21 LEU 161

ARG 120 0.38 SER 192 -0.17 LEU 161

ARG 120 0.29 TRP 193 -0.18 VAL 169

ARG 120 0.29 THR 194 -0.17 VAL 169

ARG 120 0.32 THR 195 -0.13 VAL 169

ARG 120 0.28 GLY 196 -0.13 VAL 169

ARG 120 0.28 HIS 197 -0.12 VAL 169

ARG 120 0.22 TYR 198 -0.08 VAL 169

ARG 120 0.16 TRP 199 -0.09 ALA 122

LEU 86 0.15 GLY 200 -0.10 ALA 122

PRO 228 0.15 LEU 201 -0.10 ALA 122

PRO 228 0.14 ARG 202 -0.10 GLU 121

PRO 228 0.14 LEU 203 -0.10 GLU 121

PRO 228 0.14 TYR 204 -0.13 GLU 121

ALA 134 0.13 VAL 205 -0.12 GLY 67

GLY 207 0.17 SER 206 -0.13 SER 69

ALA 134 0.17 GLY 207 -0.20 SER 69

ALA 134 0.22 ARG 208 -0.19 SER 69

ALA 134 0.18 ASP 209 -0.12 PRO 45

SER 130 0.21 PRO 210 -0.16 PRO 45

PRO 88 0.17 GLY 211 -0.11 GLY 44

THR 213 0.20 LEU 212 -0.10 GLY 44

LEU 212 0.20 THR 213 -0.09 ASP 13

GLY 215 0.16 PHE 214 -0.08 ASP 13

ARG 120 0.18 GLY 215 -0.10 VAL 169

ARG 120 0.18 ILE 216 -0.16 VAL 169

ARG 120 0.22 ARG 217 -0.18 VAL 169

ARG 120 0.22 LEU 218 -0.23 VAL 169

ARG 120 0.22 ARG 219 -0.22 VAL 169

ARG 120 0.20 TYR 220 -0.24 VAL 169

GLU 15 0.19 GLN 221 -0.22 GLN 168

GLU 15 0.15 ASN 222 -0.22 GLN 168

PRO 225 0.22 LEU 223 -0.19 GLN 168

ALA 54 0.15 GLY 224 -0.31 ARG 226

ASN 23 0.24 PRO 225 -0.20 THR 191

ASN 23 0.44 ARG 226 -0.31 GLY 224

GLY 22 0.42 VAL 227 -0.21 GLY 224

ASN 23 0.44 PRO 228 -0.14 GLY 224

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.

*** 1AOL_unrelaxed_rank_001_alphafold2_ptm_model_4_seed_000 ***

CA distance fluctuations for 240220085659142820

--- normal mode 13 ---

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

* 1AOL_unrelaxed_rank_001_alphafold2_ptm_model_4_seed_000 *