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

* EXP_1AOL_unrelaxed_rank_001_alphafold2_ptm_model_2_seed_000 *

CA distance fluctuations for 24021912362632576

--- 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
PRO 225 0.55 GLN 1 -0.05 SER 58

PRO 225 0.31 VAL 2 -0.06 SER 58

PRO 225 0.20 TYR 3 -0.08 VAL 227

PRO 225 0.06 ASN 4 -0.27 VAL 227

PRO 225 0.09 ILE 5 -0.21 VAL 227

PRO 225 0.04 THR 6 -0.30 VAL 227

PRO 225 0.05 TRP 7 -0.25 VAL 227

PRO 225 0.02 GLU 8 -0.33 VAL 227

PRO 225 0.02 VAL 9 -0.31 VAL 227

LEU 26 0.01 THR 10 -0.35 VAL 227

LEU 26 0.01 ASN 11 -0.36 VAL 227

LEU 26 0.01 GLY 12 -0.33 VAL 227

ALA 54 0.01 ASP 13 -0.38 VAL 227

LEU 26 0.01 ARG 14 -0.37 VAL 227

THR 34 0.01 GLU 15 -0.46 VAL 227

THR 34 0.01 THR 16 -0.46 VAL 227

PRO 35 0.01 VAL 17 -0.46 VAL 227

THR 34 0.01 TRP 18 -0.42 VAL 227

GLU 8 0.02 ALA 19 -0.40 VAL 227

GLU 8 0.01 ILE 20 -0.35 VAL 227

THR 6 0.03 SER 21 -0.35 VAL 227

GLN 221 0.02 GLY 22 -0.23 VAL 227

PRO 225 0.07 ASN 23 -0.12 VAL 227

PRO 225 0.18 HIS 24 -0.04 SER 58

PRO 225 0.31 PRO 25 -0.03 SER 58

PRO 225 0.30 LEU 26 -0.03 TYR 220

PRO 225 0.27 TRP 27 -0.03 TYR 220

PRO 225 0.22 THR 28 -0.02 SER 58

PRO 225 0.18 TRP 29 -0.02 LYS 174

PRO 225 0.12 TRP 30 -0.02 LYS 174

PRO 225 0.08 PRO 31 -0.06 VAL 227

PRO 225 0.07 VAL 32 -0.08 VAL 227

PRO 225 0.05 LEU 33 -0.18 VAL 227

PRO 225 0.01 THR 34 -0.24 PRO 228

TYR 56 0.01 PRO 35 -0.31 PRO 228

TYR 56 0.01 ASP 36 -0.35 PRO 228

LEU 26 0.01 LEU 37 -0.31 PRO 228

ALA 54 0.00 CYS 38 -0.39 PRO 228

PRO 55 0.01 MET 39 -0.43 PRO 228

PRO 55 0.01 LEU 40 -0.36 PRO 228

THR 213 0.01 ALA 41 -0.40 PRO 228

THR 213 0.01 LEU 42 -0.48 PRO 228

THR 213 0.01 SER 43 -0.50 PRO 228

THR 213 0.01 GLY 44 -0.42 PRO 228

ASP 129 0.02 PRO 45 -0.40 PRO 228

ASP 129 0.01 PRO 46 -0.44 PRO 228

ASP 129 0.01 HIS 47 -0.39 PRO 228

ASP 129 0.01 TRP 48 -0.41 PRO 228

ASP 129 0.01 GLY 49 -0.47 PRO 228

ASP 129 0.01 LEU 50 -0.51 PRO 228

ASP 129 0.01 GLU 51 -0.51 PRO 228

ASP 129 0.01 TYR 52 -0.59 PRO 228

GLY 12 0.01 GLN 53 -0.61 PRO 228

ASP 13 0.01 ALA 54 -0.63 PRO 228

ASP 36 0.01 PRO 55 -0.58 PRO 228

ASP 36 0.01 TYR 56 -0.62 PRO 228

ALA 54 0.01 SER 57 -0.66 PRO 228

GLN 53 0.01 SER 58 -0.65 PRO 228

LEU 50 0.01 PRO 59 -0.58 PRO 228

GLY 49 0.01 PRO 60 -0.61 PRO 228

ASN 91 0.01 GLY 61 -0.59 PRO 228

THR 87 0.01 PRO 62 -0.59 PRO 228

THR 87 0.01 PRO 63 -0.53 PRO 228

THR 84 0.01 CYS 64 -0.51 PRO 228

THR 84 0.01 CYS 65 -0.47 PRO 228

GLY 207 0.01 SER 66 -0.48 PRO 228

SER 206 0.01 GLY 67 -0.43 PRO 228

SER 206 0.01 SER 68 -0.43 PRO 228

GLY 207 0.01 SER 69 -0.45 PRO 228

GLY 207 0.01 GLY 70 -0.49 PRO 228

GLY 207 0.01 SER 71 -0.54 PRO 228

THR 84 0.01 SER 72 -0.57 PRO 228

LEU 86 0.01 ALA 73 -0.60 PRO 228

LEU 86 0.01 GLY 74 -0.59 PRO 228

THR 84 0.01 CYS 75 -0.53 PRO 228

THR 84 0.01 SER 76 -0.47 PRO 228

THR 84 0.01 ARG 77 -0.45 PRO 228

LEU 83 0.02 ASP 78 -0.40 PRO 228

SER 206 0.01 CYS 79 -0.39 PRO 228

SER 107 0.01 ASP 80 -0.34 PRO 228

SER 206 0.01 GLU 81 -0.32 PRO 228

VAL 205 0.02 PRO 82 -0.28 PRO 228

ASP 78 0.02 LEU 83 -0.29 PRO 228

ASP 78 0.02 THR 84 -0.28 PRO 228

ALA 134 0.01 SER 85 -0.27 PRO 228

SER 130 0.01 LEU 86 -0.32 PRO 228

SER 130 0.01 THR 87 -0.35 PRO 228

SER 130 0.01 PRO 88 -0.33 PRO 228

ASP 129 0.01 ARG 89 -0.40 PRO 228

ASP 129 0.01 CYS 90 -0.44 PRO 228

GLY 61 0.01 ASN 91 -0.51 PRO 228

ASP 129 0.01 THR 92 -0.51 PRO 228

ASP 129 0.01 ALA 93 -0.48 PRO 228

ASP 129 0.01 TRP 94 -0.43 PRO 228

ASP 129 0.01 ASN 95 -0.41 PRO 228

GLY 211 0.01 ARG 96 -0.40 PRO 228

ASP 129 0.00 LEU 97 -0.36 PRO 228

VAL 102 0.01 LYS 98 -0.32 PRO 228

LEU 26 0.01 LEU 99 -0.30 PRO 228

LEU 26 0.01 ASP 100 -0.28 PRO 228

LEU 26 0.01 GLN 101 -0.25 PRO 228

LEU 26 0.01 VAL 102 -0.22 PRO 228

PRO 225 0.02 THR 103 -0.19 PRO 228

PRO 225 0.03 HIS 104 -0.16 PRO 228

PRO 225 0.03 LYS 105 -0.15 PRO 228

PRO 225 0.04 SER 106 -0.08 PRO 228

PRO 225 0.04 SER 107 -0.10 PRO 228

PRO 225 0.03 GLU 108 -0.14 PRO 228

PRO 225 0.04 GLY 109 -0.14 PRO 228

PRO 225 0.04 PHE 110 -0.14 VAL 227

PRO 225 0.06 TYR 111 -0.11 VAL 227

PRO 225 0.07 VAL 112 -0.11 VAL 227

PRO 225 0.08 CYS 113 -0.09 VAL 227

PRO 225 0.10 PRO 114 -0.07 VAL 227

PRO 225 0.09 GLY 115 -0.10 VAL 227

PRO 225 0.11 SER 116 -0.07 VAL 227

PRO 225 0.14 HIS 117 -0.02 LEU 223

PRO 225 0.13 ARG 118 -0.01 GLN 221

PRO 225 0.14 PRO 119 -0.01 SER 149

PRO 225 0.13 ARG 120 -0.01 SER 149

PRO 225 0.12 GLU 121 -0.01 PRO 148

PRO 225 0.11 ALA 122 -0.01 GLN 221

PRO 225 0.10 LYS 123 -0.03 VAL 227

PRO 225 0.09 SER 124 -0.05 VAL 227

PRO 225 0.08 CYS 125 -0.08 VAL 227

PRO 225 0.07 GLY 126 -0.11 VAL 227

PRO 225 0.07 GLY 127 -0.15 VAL 227

PRO 225 0.05 PRO 128 -0.20 VAL 227

PRO 225 0.04 ASP 129 -0.22 VAL 227

PRO 225 0.05 SER 130 -0.18 VAL 227

PRO 225 0.05 PHE 131 -0.18 VAL 227

PRO 225 0.07 TYR 132 -0.13 VAL 227

PRO 225 0.07 CYS 133 -0.12 VAL 227

PRO 225 0.06 ALA 134 -0.12 VAL 227

PRO 225 0.07 SER 135 -0.08 VAL 227

PRO 225 0.08 TRP 136 -0.05 VAL 227

PRO 225 0.09 GLY 137 -0.02 VAL 227

PRO 225 0.09 CYS 138 -0.04 VAL 227

PRO 225 0.09 GLU 139 -0.05 VAL 227

PRO 225 0.10 THR 140 -0.02 LEU 223

PRO 225 0.09 THR 141 -0.03 VAL 227

PRO 225 0.07 GLY 142 -0.07 VAL 227

PRO 225 0.06 ARG 143 -0.08 VAL 227

PRO 225 0.06 VAL 144 -0.07 VAL 227

PRO 225 0.06 TYR 145 -0.04 VAL 227

PRO 225 0.08 TRP 146 -0.01 LEU 223

PRO 225 0.08 LYS 147 -0.01 LEU 223

PRO 225 0.09 PRO 148 -0.01 LEU 223

PRO 225 0.11 SER 149 -0.01 ASP 158

PRO 228 0.15 SER 150 -0.01 THR 156

PRO 228 0.22 SER 151 -0.02 THR 156

PRO 228 0.19 TRP 152 -0.01 ASP 153

PRO 225 0.14 ASP 153 -0.01 TRP 152

PRO 225 0.14 TYR 154 -0.01 GLN 221

PRO 225 0.12 ILE 155 -0.02 LEU 223

PRO 225 0.10 THR 156 -0.02 LEU 223

PRO 225 0.07 VAL 157 -0.08 VAL 227

PRO 225 0.06 ASP 158 -0.09 VAL 227

PRO 225 0.03 ASN 159 -0.15 PRO 228

PRO 225 0.02 ASN 160 -0.17 PRO 228

TYR 56 0.01 LEU 161 -0.21 PRO 228

PRO 225 0.01 THR 162 -0.18 PRO 228

LEU 26 0.01 THR 163 -0.22 PRO 228

TYR 56 0.01 SER 164 -0.25 PRO 228

TYR 56 0.01 GLN 165 -0.28 PRO 228

CYS 176 0.01 ALA 166 -0.31 PRO 228

GLN 101 0.00 VAL 167 -0.34 PRO 228

ALA 54 0.00 GLN 168 -0.38 PRO 228

ALA 54 0.00 VAL 169 -0.42 PRO 228

ASP 129 0.00 CYS 170 -0.43 PRO 228

ASP 129 0.00 LYS 171 -0.46 PRO 228

GLY 49 0.00 ASP 172 -0.52 PRO 228

GLY 49 0.01 ASN 173 -0.55 PRO 228

LEU 50 0.01 LYS 174 -0.52 PRO 228

ALA 54 0.01 TRP 175 -0.46 PRO 228

ALA 166 0.01 CYS 176 -0.38 PRO 228

TYR 56 0.01 ASN 177 -0.32 PRO 228

TYR 56 0.01 PRO 178 -0.29 PRO 228

PRO 225 0.02 LEU 179 -0.20 PRO 228

PRO 225 0.05 ALA 180 -0.13 VAL 227

PRO 225 0.07 ILE 181 -0.11 VAL 227

PRO 225 0.10 GLN 182 -0.02 VAL 227

PRO 225 0.14 PHE 183 -0.01 LEU 223

PRO 228 0.16 THR 184 -0.01 ASN 185

PRO 228 0.26 ASN 185 -0.01 GLY 187

PRO 228 0.24 ALA 186 -0.01 LEU 33

PRO 225 0.17 GLY 187 -0.01 ASN 185

PRO 228 0.22 LYS 188 -0.01 LYS 174

PRO 228 0.28 GLN 189 -0.01 LYS 174

PRO 225 0.21 VAL 190 -0.01 SER 192

PRO 225 0.23 THR 191 -0.02 GLN 221

PRO 225 0.19 SER 192 -0.02 GLN 221

PRO 225 0.16 TRP 193 -0.07 VAL 227

PRO 225 0.14 THR 194 -0.15 VAL 227

PRO 225 0.12 THR 195 -0.16 VAL 227

PRO 225 0.10 GLY 196 -0.18 VAL 227

PRO 225 0.10 HIS 197 -0.13 VAL 227

PRO 225 0.08 TYR 198 -0.17 VAL 227

PRO 225 0.07 TRP 199 -0.15 VAL 227

PRO 225 0.06 GLY 200 -0.17 VAL 227

PRO 225 0.04 LEU 201 -0.18 VAL 227

PRO 225 0.04 ARG 202 -0.18 VAL 227

PRO 225 0.03 LEU 203 -0.19 PRO 228

PRO 225 0.04 TYR 204 -0.15 PRO 228

PRO 225 0.03 VAL 205 -0.18 PRO 228

PRO 225 0.02 SER 206 -0.18 PRO 228

PRO 225 0.02 GLY 207 -0.19 PRO 228

PRO 225 0.03 ARG 208 -0.20 PRO 228

PRO 225 0.03 ASP 209 -0.19 PRO 228

PRO 225 0.02 PRO 210 -0.24 PRO 228

PRO 225 0.02 GLY 211 -0.24 PRO 228

PRO 225 0.02 LEU 212 -0.26 PRO 228

PRO 225 0.03 THR 213 -0.25 VAL 227

PRO 225 0.03 PHE 214 -0.26 VAL 227

PRO 225 0.05 GLY 215 -0.24 VAL 227

PRO 225 0.07 ILE 216 -0.21 VAL 227

PRO 225 0.09 ARG 217 -0.21 VAL 227

PRO 225 0.11 LEU 218 -0.19 VAL 227

PRO 225 0.08 ARG 219 -0.28 VAL 227

PRO 225 0.11 TYR 220 -0.24 VAL 227

PRO 225 0.11 GLN 221 -0.30 VAL 227

PRO 225 0.20 ASN 222 -0.19 VAL 227

PRO 225 0.11 LEU 223 -0.29 ARG 226

PRO 225 0.30 GLY 224 -0.16 ASN 222

GLN 1 0.55 PRO 225 -0.10 SER 58

GLN 1 0.45 ARG 226 -0.32 TYR 56

GLN 1 0.31 VAL 227 -0.58 SER 57

GLN 189 0.28 PRO 228 -0.66 SER 57

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_1AOL_unrelaxed_rank_001_alphafold2_ptm_model_2_seed_000 ***

CA distance fluctuations for 24021912362632576

--- normal mode 7 ---

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

* EXP_1AOL_unrelaxed_rank_001_alphafold2_ptm_model_2_seed_000 *