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 7 ---

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 58 0.03 GLN 1 -0.82 PRO 225

TYR 56 0.04 VAL 2 -0.53 PRO 225

LEU 223 0.06 TYR 3 -0.33 PRO 225

VAL 227 0.21 ASN 4 -0.13 PRO 225

VAL 227 0.16 ILE 5 -0.17 PRO 225

VAL 227 0.25 THR 6 -0.09 PRO 225

VAL 227 0.20 TRP 7 -0.11 PRO 225

VAL 227 0.28 GLU 8 -0.07 PRO 225

VAL 227 0.27 VAL 9 -0.06 PRO 225

VAL 227 0.31 THR 10 -0.04 PRO 225

VAL 227 0.32 ASN 11 -0.02 PRO 225

VAL 227 0.29 GLY 12 -0.03 PRO 225

VAL 227 0.35 ASP 13 -0.01 PRO 225

VAL 227 0.34 ARG 14 -0.02 PRO 225

VAL 227 0.42 GLU 15 -0.00 THR 34

VAL 227 0.42 THR 16 -0.00 THR 34

VAL 227 0.42 VAL 17 -0.01 PRO 35

VAL 227 0.37 TRP 18 -0.00 THR 34

VAL 227 0.35 ALA 19 -0.02 PRO 225

VAL 227 0.29 ILE 20 -0.04 PRO 225

VAL 227 0.28 SER 21 -0.05 PRO 225

VAL 227 0.16 GLY 22 -0.11 PRO 225

VAL 227 0.06 ASN 23 -0.19 PRO 225

SER 58 0.03 HIS 24 -0.33 PRO 225

SER 58 0.02 PRO 25 -0.48 PRO 225

TYR 220 0.02 LEU 26 -0.42 PRO 225

TYR 220 0.02 TRP 27 -0.37 PRO 225

TRP 29 0.02 THR 28 -0.35 PRO 225

THR 28 0.02 TRP 29 -0.27 PRO 225

LEU 223 0.02 TRP 30 -0.23 PRO 225

LEU 223 0.03 PRO 31 -0.17 PRO 225

VAL 227 0.04 VAL 32 -0.13 PRO 225

VAL 227 0.14 LEU 33 -0.10 PRO 225

VAL 227 0.19 THR 34 -0.06 PRO 225

VAL 227 0.26 PRO 35 -0.03 PRO 225

VAL 227 0.28 ASP 36 -0.02 PRO 225

VAL 227 0.25 LEU 37 -0.03 PRO 225

PRO 228 0.32 CYS 38 -0.00 PRO 225

VAL 227 0.36 MET 39 -0.01 TYR 56

VAL 227 0.31 LEU 40 -0.02 PRO 225

VAL 227 0.34 ALA 41 -0.01 THR 213

PRO 228 0.41 LEU 42 -0.01 THR 213

PRO 228 0.43 SER 43 -0.01 THR 213

VAL 227 0.36 GLY 44 -0.01 THR 213

PRO 228 0.33 PRO 45 -0.01 ASP 129

PRO 228 0.37 PRO 46 -0.01 ASP 129

PRO 228 0.33 HIS 47 -0.01 ASP 129

PRO 228 0.34 TRP 48 -0.01 ASP 129

PRO 228 0.40 GLY 49 -0.01 ASP 129

PRO 228 0.44 LEU 50 -0.01 ASP 129

PRO 228 0.44 GLU 51 -0.01 ASP 129

PRO 228 0.52 TYR 52 -0.01 ASP 129

PRO 228 0.53 GLN 53 -0.00 THR 213

PRO 228 0.55 ALA 54 -0.00 ASP 13

VAL 227 0.51 PRO 55 -0.01 PRO 35

PRO 228 0.54 TYR 56 -0.01 PRO 35

PRO 228 0.57 SER 57 -0.00 PRO 178

PRO 228 0.56 SER 58 -0.00 LYS 174

PRO 228 0.49 PRO 59 -0.00 GLY 49

PRO 228 0.51 PRO 60 -0.00 GLY 49

PRO 228 0.50 GLY 61 -0.00 HIS 47

PRO 228 0.50 PRO 62 -0.00 THR 87

PRO 228 0.43 PRO 63 -0.00 THR 87

PRO 228 0.43 CYS 64 -0.01 LEU 83

PRO 228 0.39 CYS 65 -0.01 LEU 83

PRO 228 0.41 SER 66 -0.01 THR 84

PRO 228 0.39 GLY 67 -0.01 GLU 81

PRO 228 0.41 SER 68 -0.01 GLU 81

PRO 228 0.44 SER 69 -0.01 GLY 207

PRO 228 0.49 GLY 70 -0.01 ARG 77

PRO 228 0.48 SER 71 -0.01 SER 66

PRO 228 0.52 SER 72 -0.01 LEU 86

PRO 228 0.53 ALA 73 -0.01 LEU 86

PRO 228 0.50 GLY 74 -0.01 LEU 86

PRO 228 0.45 CYS 75 -0.01 LEU 86

PRO 228 0.40 SER 76 -0.01 THR 87

PRO 228 0.38 ARG 77 -0.01 GLY 67

PRO 228 0.33 ASP 78 -0.01 GLY 67

PRO 228 0.32 CYS 79 -0.01 GLY 67

PRO 228 0.27 ASP 80 -0.01 GLY 67

PRO 228 0.26 GLU 81 -0.01 GLY 67

PRO 228 0.22 PRO 82 -0.02 PRO 225

PRO 228 0.22 LEU 83 -0.02 PRO 225

PRO 228 0.21 THR 84 -0.03 PRO 225

VAL 227 0.21 SER 85 -0.03 PRO 225

PRO 228 0.26 LEU 86 -0.01 PRO 225

PRO 228 0.29 THR 87 -0.01 GLY 67

PRO 228 0.27 PRO 88 -0.02 PRO 225

PRO 228 0.33 ARG 89 -0.01 ASP 129

PRO 228 0.36 CYS 90 -0.00 ASP 129

PRO 228 0.43 ASN 91 -0.01 ASP 129

PRO 228 0.43 THR 92 -0.00 ASP 129

PRO 228 0.40 ALA 93 -0.00 ASP 129

PRO 228 0.36 TRP 94 -0.00 LEU 83

PRO 228 0.34 ASN 95 -0.00 SER 130

PRO 228 0.32 ARG 96 -0.00 GLY 211

PRO 228 0.29 LEU 97 -0.00 GLY 211

PRO 228 0.26 LYS 98 -0.01 PRO 225

PRO 228 0.24 LEU 99 -0.02 PRO 225

PRO 228 0.21 ASP 100 -0.03 PRO 225

PRO 228 0.18 GLN 101 -0.03 PRO 225

VAL 227 0.16 VAL 102 -0.04 PRO 225

VAL 227 0.15 THR 103 -0.06 PRO 225

VAL 227 0.11 HIS 104 -0.06 PRO 225

VAL 227 0.10 LYS 105 -0.06 PRO 225

VAL 227 0.06 SER 106 -0.08 PRO 225

VAL 227 0.07 SER 107 -0.07 PRO 225

VAL 227 0.10 GLU 108 -0.07 PRO 225

VAL 227 0.11 GLY 109 -0.07 PRO 225

VAL 227 0.11 PHE 110 -0.08 PRO 225

VAL 227 0.08 TYR 111 -0.10 PRO 225

VAL 227 0.07 VAL 112 -0.11 PRO 225

VAL 227 0.06 CYS 113 -0.12 PRO 225

VAL 227 0.04 PRO 114 -0.14 PRO 225

VAL 227 0.07 GLY 115 -0.13 PRO 225

VAL 227 0.04 SER 116 -0.14 PRO 225

LEU 223 0.02 HIS 117 -0.17 PRO 225

LEU 223 0.01 ARG 118 -0.17 PRO 225

GLN 221 0.01 PRO 119 -0.18 PRO 228

GLN 221 0.01 ARG 120 -0.17 PRO 225

GLN 221 0.01 GLU 121 -0.16 PRO 228

LEU 223 0.01 ALA 122 -0.14 PRO 225

LEU 223 0.02 LYS 123 -0.13 PRO 225

VAL 227 0.02 SER 124 -0.11 PRO 225

VAL 227 0.05 CYS 125 -0.11 PRO 225

VAL 227 0.09 GLY 126 -0.10 PRO 225

VAL 227 0.13 GLY 127 -0.09 PRO 225

VAL 227 0.18 PRO 128 -0.07 PRO 225

VAL 227 0.19 ASP 129 -0.06 PRO 225

VAL 227 0.15 SER 130 -0.07 PRO 225

VAL 227 0.15 PHE 131 -0.08 PRO 225

VAL 227 0.10 TYR 132 -0.10 PRO 225

VAL 227 0.08 CYS 133 -0.10 PRO 225

VAL 227 0.09 ALA 134 -0.09 PRO 225

VAL 227 0.05 SER 135 -0.10 PRO 225

VAL 227 0.02 TRP 136 -0.11 PRO 225

LEU 223 0.02 GLY 137 -0.13 PRO 225

LEU 223 0.02 CYS 138 -0.13 PRO 225

LEU 223 0.02 GLU 139 -0.12 PRO 225

LEU 223 0.02 THR 140 -0.14 PRO 225

LEU 223 0.02 THR 141 -0.13 PRO 225

VAL 227 0.04 GLY 142 -0.11 PRO 225

VAL 227 0.05 ARG 143 -0.10 PRO 225

VAL 227 0.04 VAL 144 -0.09 PRO 225

LEU 223 0.02 TYR 145 -0.10 PRO 225

LEU 223 0.02 TRP 146 -0.11 PRO 225

LEU 223 0.01 LYS 147 -0.12 PRO 225

LEU 223 0.02 PRO 148 -0.13 PRO 225

LEU 223 0.01 SER 149 -0.15 PRO 225

THR 156 0.01 SER 150 -0.19 PRO 228

THR 156 0.01 SER 151 -0.26 PRO 228

ASP 153 0.01 TRP 152 -0.24 PRO 228

LEU 223 0.01 ASP 153 -0.19 PRO 225

LEU 223 0.02 TYR 154 -0.20 PRO 225

LEU 223 0.02 ILE 155 -0.17 PRO 225

LEU 223 0.02 THR 156 -0.15 PRO 225

VAL 227 0.05 VAL 157 -0.12 PRO 225

VAL 227 0.07 ASP 158 -0.10 PRO 225

VAL 227 0.11 ASN 159 -0.07 PRO 225

VAL 227 0.13 ASN 160 -0.07 PRO 225

VAL 227 0.15 LEU 161 -0.05 PRO 225

VAL 227 0.12 THR 162 -0.05 PRO 225

PRO 228 0.15 THR 163 -0.04 PRO 225

PRO 228 0.18 SER 164 -0.02 PRO 225

PRO 228 0.21 GLN 165 -0.02 PRO 225

PRO 228 0.24 ALA 166 -0.01 PRO 225

PRO 228 0.27 VAL 167 -0.00 GLN 101

PRO 228 0.31 GLN 168 -0.00 ALA 54

PRO 228 0.34 VAL 169 -0.00 SER 57

PRO 228 0.36 CYS 170 -0.00 ASP 129

PRO 228 0.38 LYS 171 -0.00 THR 87

PRO 228 0.44 ASP 172 -0.00 GLY 49

PRO 228 0.46 ASN 173 -0.00 GLY 49

PRO 228 0.43 LYS 174 -0.00 GLY 49

PRO 228 0.38 TRP 175 -0.00 SER 57

PRO 228 0.31 CYS 176 -0.00 ALA 166

PRO 228 0.25 ASN 177 -0.02 PRO 225

VAL 227 0.22 PRO 178 -0.03 PRO 225

VAL 227 0.16 LEU 179 -0.07 PRO 225

VAL 227 0.10 ALA 180 -0.10 PRO 225

VAL 227 0.07 ILE 181 -0.12 PRO 225

LEU 223 0.02 GLN 182 -0.16 PRO 225

LEU 223 0.02 PHE 183 -0.20 PRO 225

GLN 221 0.01 THR 184 -0.22 PRO 228

GLY 187 0.01 ASN 185 -0.31 PRO 228

VAL 32 0.01 ALA 186 -0.29 PRO 228

GLN 221 0.01 GLY 187 -0.24 PRO 225

GLN 189 0.01 LYS 188 -0.28 PRO 225

LYS 188 0.01 GLN 189 -0.33 PRO 228

SER 192 0.01 VAL 190 -0.28 PRO 225

GLN 221 0.01 THR 191 -0.30 PRO 225

LEU 223 0.02 SER 192 -0.24 PRO 225

LEU 223 0.04 TRP 193 -0.21 PRO 225

VAL 227 0.09 THR 194 -0.19 PRO 225

VAL 227 0.12 THR 195 -0.16 PRO 225

VAL 227 0.13 GLY 196 -0.14 PRO 225

VAL 227 0.09 HIS 197 -0.14 PRO 225

VAL 227 0.13 TYR 198 -0.11 PRO 225

VAL 227 0.12 TRP 199 -0.11 PRO 225

VAL 227 0.14 GLY 200 -0.09 PRO 225

VAL 227 0.15 LEU 201 -0.08 PRO 225

VAL 227 0.15 ARG 202 -0.07 PRO 225

VAL 227 0.16 LEU 203 -0.06 PRO 225

VAL 227 0.12 TYR 204 -0.07 PRO 225

VAL 227 0.15 VAL 205 -0.05 PRO 225

VAL 227 0.15 SER 206 -0.05 PRO 225

VAL 227 0.16 GLY 207 -0.05 PRO 225

VAL 227 0.16 ARG 208 -0.05 PRO 225

VAL 227 0.16 ASP 209 -0.06 PRO 225

VAL 227 0.20 PRO 210 -0.04 PRO 225

VAL 227 0.20 GLY 211 -0.05 PRO 225

VAL 227 0.23 LEU 212 -0.05 PRO 225

VAL 227 0.21 THR 213 -0.06 PRO 225

VAL 227 0.22 PHE 214 -0.07 PRO 225

VAL 227 0.20 GLY 215 -0.09 PRO 225

VAL 227 0.16 ILE 216 -0.12 PRO 225

VAL 227 0.16 ARG 217 -0.13 PRO 225

VAL 227 0.14 LEU 218 -0.16 PRO 225

VAL 227 0.23 ARG 219 -0.13 PRO 225

VAL 227 0.20 TYR 220 -0.16 PRO 225

VAL 227 0.27 GLN 221 -0.13 PRO 225

GLY 224 0.17 ASN 222 -0.23 PRO 225

ARG 226 0.25 LEU 223 -0.13 PRO 225

ASN 222 0.17 GLY 224 -0.17 PRO 225

SER 57 0.08 PRO 225 -0.82 GLN 1

TYR 56 0.31 ARG 226 -0.54 GLN 1

SER 57 0.54 VAL 227 -0.39 GLN 1

SER 57 0.57 PRO 228 -0.33 GLN 189

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 7 ---

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

* 1AOL_unrelaxed_rank_001_alphafold2_ptm_model_4_seed_000 *