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

* 1P5V_unrelaxed_rank_001_alphafold2_ptm_model_4_seed_000 *

CA distance fluctuations for 240220090321150899

--- 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
VAL 98 1.03 PHE 1 -0.28 ARG 190

PHE 99 0.84 ALA 2 -0.47 LYS 62

PHE 102 0.52 SER 3 -0.11 LYS 4

PHE 102 0.12 LYS 4 -0.13 THR 34

SER 3 0.15 GLU 5 -0.18 ALA 2

SER 3 0.20 TYR 6 -0.06 ALA 2

SER 3 0.17 GLY 7 -0.18 ALA 2

PHE 1 0.15 VAL 8 -0.19 ALA 2

SER 3 0.09 THR 9 -0.30 ALA 2

SER 3 0.08 ILE 10 -0.28 ALA 2

PRO 160 0.02 GLY 11 -0.40 ALA 2

SER 3 0.04 GLU 12 -0.33 ALA 2

SER 3 0.06 SER 13 -0.28 ALA 2

SER 3 0.08 ARG 14 -0.22 ALA 2

SER 3 0.08 ILE 15 -0.20 ALA 2

SER 3 0.07 ILE 16 -0.19 ALA 2

PHE 1 0.11 TYR 17 -0.15 ALA 2

PHE 1 0.09 PRO 18 -0.15 ALA 2

PHE 1 0.14 LEU 19 -0.11 ALA 2

PHE 1 0.12 ASP 20 -0.12 ALA 2

PHE 1 0.15 ALA 21 -0.09 ALA 2

PHE 1 0.14 ALA 22 -0.11 ALA 2

PHE 1 0.17 GLY 23 -0.10 ALA 2

PHE 1 0.17 VAL 24 -0.11 ALA 2

PHE 1 0.11 MET 25 -0.16 ALA 2

PHE 1 0.10 VAL 26 -0.18 ALA 2

PHE 1 0.07 SER 27 -0.21 ALA 2

SER 3 0.04 SER 28 -0.25 ALA 2

SER 3 0.06 VAL 29 -0.25 ALA 2

SER 3 0.03 VAL 30 -0.32 ALA 2

PHE 1 0.06 VAL 31 -0.27 ALA 2

SER 3 0.02 LYS 32 -0.36 ALA 2

PHE 1 0.04 ASN 33 -0.31 ALA 2

ASN 105 0.01 THR 34 -0.45 ALA 2

ASP 36 0.02 GLN 35 -0.32 ALA 2

GLU 5 0.02 ASP 36 -0.34 ALA 2

PHE 1 0.12 TYR 37 -0.16 ALA 2

PHE 1 0.20 PRO 38 -0.11 ALA 2

PHE 1 0.31 VAL 39 -0.02 ALA 2

PHE 1 0.39 LEU 40 -0.01 PRO 160

PHE 1 0.36 ILE 41 -0.01 PRO 160

PHE 1 0.45 GLN 42 -0.02 PRO 160

PHE 1 0.38 SER 43 -0.02 PRO 160

PHE 1 0.44 ARG 44 -0.02 PRO 55

PHE 1 0.40 ILE 45 -0.02 PRO 160

PHE 1 0.47 TYR 46 -0.02 PRO 160

PHE 1 0.44 ASP 47 -0.02 PRO 160

PHE 1 0.46 PRO 48 -0.02 ALA 171

PHE 1 0.38 PHE 49 -0.02 ALA 171

PHE 1 0.34 VAL 50 -0.01 ALA 171

PHE 1 0.35 VAL 51 -0.01 PRO 160

PHE 1 0.30 VAL 52 -0.04 ALA 2

PHE 1 0.28 THR 53 -0.06 ALA 2

PHE 1 0.30 PRO 54 -0.05 ALA 2

PHE 1 0.39 PRO 55 -0.02 ARG 44

PHE 1 0.40 LEU 56 -0.01 PRO 160

PHE 1 0.32 PHE 57 -0.04 ALA 2

PHE 1 0.27 ARG 58 -0.07 ALA 2

PHE 1 0.16 LEU 59 -0.17 ALA 2

PHE 1 0.08 ASP 60 -0.23 ALA 2

TYR 37 0.01 ALA 61 -0.32 ALA 2

PRO 160 0.01 LYS 62 -0.47 ALA 2

PRO 160 0.01 GLN 63 -0.40 ALA 2

GLY 11 0.02 GLN 64 -0.38 ALA 2

PHE 1 0.03 ASN 65 -0.29 ALA 2

SER 3 0.03 SER 66 -0.29 ALA 2

PHE 1 0.09 SER 67 -0.22 ALA 2

PHE 1 0.16 LEU 68 -0.16 ALA 2

PHE 1 0.17 ARG 69 -0.14 ALA 2

PHE 1 0.21 ILE 70 -0.10 ALA 2

PHE 1 0.24 ALA 71 -0.07 ALA 2

PHE 1 0.27 GLN 72 -0.04 ALA 2

PHE 1 0.33 ALA 73 -0.01 ALA 171

PHE 1 0.34 GLY 74 -0.01 ALA 171

PHE 1 0.34 GLY 75 -0.02 TRP 170

PHE 1 0.30 VAL 76 -0.01 TRP 170

PHE 1 0.26 PHE 77 -0.01 ALA 2

PHE 1 0.23 PRO 78 -0.02 ALA 2

PHE 1 0.17 ARG 79 -0.06 ALA 2

PHE 1 0.15 ASP 80 -0.07 ALA 2

PHE 1 0.15 LYS 81 -0.07 ALA 2

PHE 1 0.16 GLU 82 -0.07 ALA 2

PHE 1 0.23 SER 83 -0.03 ALA 2

PHE 1 0.25 LEU 84 -0.02 ALA 2

PHE 1 0.31 LYS 85 -0.02 HIS 162

PHE 1 0.33 TRP 86 -0.02 SER 161

PHE 1 0.31 LEU 87 -0.03 ALA 2

PHE 1 0.37 CYS 88 -0.02 PRO 160

PHE 1 0.35 VAL 89 -0.02 SER 13

PHE 1 0.45 LYS 90 -0.02 PRO 160

PHE 1 0.41 GLY 91 -0.02 GLY 150

PHE 1 0.54 ILE 92 -0.02 PRO 160

PHE 1 0.50 PRO 93 -0.02 SER 158

PHE 1 0.51 LYS 94 -0.02 SER 158

PHE 1 0.61 ASP 95 -0.03 SER 158

PHE 1 0.81 VAL 96 -0.04 SER 158

PHE 1 0.82 GLY 97 -0.04 SER 158

PHE 1 1.03 VAL 98 -0.05 SER 158

PHE 1 0.87 PHE 99 -0.05 SER 158

PHE 1 0.88 VAL 100 -0.05 SER 158

PHE 1 0.91 GLN 101 -0.05 SER 158

PHE 1 0.70 PHE 102 -0.05 SER 158

PHE 1 0.63 ALA 103 -0.04 SER 158

PHE 1 0.45 ILE 104 -0.04 LEU 188

PHE 1 0.46 ASN 105 -0.03 GLY 150

PHE 1 0.30 ASN 106 -0.04 SER 13

PHE 1 0.30 CYS 107 -0.02 GLY 150

PHE 1 0.19 ILE 108 -0.10 ALA 2

PHE 1 0.19 LYS 109 -0.09 ALA 2

PHE 1 0.19 LEU 110 -0.09 ALA 2

PHE 1 0.15 LEU 111 -0.11 ALA 2

PHE 1 0.18 VAL 112 -0.09 ALA 2

PHE 1 0.12 ARG 113 -0.12 ALA 2

PHE 1 0.12 PRO 114 -0.11 ALA 2

PHE 1 0.07 ASN 115 -0.14 ALA 2

PHE 1 0.07 GLU 116 -0.13 ALA 2

SER 3 0.05 LEU 117 -0.14 ALA 2

SER 3 0.04 LYS 118 -0.17 ALA 2

SER 3 0.03 GLY 119 -0.21 ALA 2

SER 3 0.03 THR 120 -0.22 ALA 2

SER 3 0.04 PRO 121 -0.20 ALA 2

VAL 26 0.02 ILE 122 -0.24 ALA 2

SER 3 0.01 GLN 123 -0.23 ALA 2

SER 3 0.03 PHE 124 -0.18 ALA 2

SER 3 0.03 ALA 125 -0.19 ALA 2

SER 3 0.02 GLU 126 -0.18 ALA 2

SER 3 0.04 ASN 127 -0.14 ALA 2

SER 3 0.05 LEU 128 -0.12 ALA 2

SER 3 0.06 SER 129 -0.09 ALA 2

SER 3 0.06 TRP 130 -0.06 ALA 2

SER 3 0.07 LYS 131 -0.03 ALA 2

SER 3 0.08 VAL 132 -0.02 GLN 101

PHE 1 0.14 ASP 133 -0.02 VAL 96

PHE 1 0.18 GLY 134 -0.02 VAL 96

PHE 1 0.14 GLY 135 -0.02 GLN 101

PHE 1 0.15 LYS 136 -0.02 GLN 101

PHE 1 0.09 LEU 137 -0.02 GLN 101

PHE 1 0.12 ILE 138 -0.02 GLN 101

PHE 1 0.09 ALA 139 -0.04 ALA 2

PHE 1 0.10 GLU 140 -0.04 ALA 2

PHE 1 0.09 ASN 141 -0.07 ALA 2

PHE 1 0.08 PRO 142 -0.07 ALA 2

SER 3 0.07 SER 143 -0.10 ALA 2

PHE 1 0.10 PRO 144 -0.09 ALA 2

PHE 1 0.08 PHE 145 -0.12 ALA 2

PHE 1 0.11 TYR 146 -0.10 ALA 2

SER 3 0.07 MET 147 -0.13 ALA 2

SER 3 0.08 ASN 148 -0.15 ALA 2

SER 3 0.06 ILE 149 -0.16 ALA 2

SER 3 0.03 GLY 150 -0.23 ALA 2

SER 3 0.02 GLU 151 -0.22 ALA 2

SER 3 0.04 LEU 152 -0.15 ALA 2

SER 3 0.02 THR 153 -0.15 ALA 2

SER 3 0.03 PHE 154 -0.10 ALA 2

SER 3 0.02 GLY 155 -0.14 PHE 1

GLY 11 0.01 GLY 156 -0.21 PHE 1

SER 3 0.02 LYS 157 -0.15 PHE 1

SER 3 0.03 SER 158 -0.13 PHE 1

SER 3 0.07 ILE 159 -0.06 ALA 2

SER 3 0.10 PRO 160 -0.05 GLN 101

SER 3 0.09 SER 161 -0.08 ALA 2

PHE 1 0.13 HIS 162 -0.04 ALA 2

PHE 1 0.13 TYR 163 -0.06 ALA 2

PHE 1 0.14 ILE 164 -0.04 ALA 2

PHE 1 0.19 PRO 165 -0.02 ALA 2

PHE 1 0.15 PRO 166 -0.05 ALA 2

PHE 1 0.16 LYS 167 -0.03 ALA 2

PHE 1 0.20 SER 168 -0.01 GLY 75

PHE 1 0.19 THR 169 -0.01 GLY 75

PHE 1 0.19 TRP 170 -0.02 PRO 48

PHE 1 0.19 ALA 171 -0.02 PRO 48

PHE 1 0.15 PHE 172 -0.03 GLN 101

PHE 1 0.15 ASP 173 -0.03 GLN 101

SER 3 0.08 LEU 174 -0.03 GLN 101

SER 3 0.06 PRO 175 -0.03 GLN 101

SER 3 0.03 ASN 176 -0.09 ALA 2

SER 3 0.03 VAL 177 -0.12 ALA 2

SER 3 0.01 SER 178 -0.18 ALA 2

SER 3 0.02 TRP 179 -0.20 ALA 2

SER 28 0.01 ARG 180 -0.25 ALA 2

SER 3 0.02 ILE 181 -0.24 ALA 2

SER 3 0.02 ILE 182 -0.27 ALA 2

SER 27 0.02 ASN 183 -0.29 ALA 2

SER 27 0.02 ASP 184 -0.28 ALA 2

SER 28 0.03 GLN 185 -0.36 ALA 2

SER 28 0.03 GLY 186 -0.35 ALA 2

SER 28 0.02 GLY 187 -0.40 ALA 2

SER 28 0.02 LEU 188 -0.37 ALA 2

SER 28 0.02 ASP 189 -0.34 ALA 2

SER 28 0.02 ARG 190 -0.33 ALA 2

SER 28 0.01 LEU 191 -0.29 ALA 2

SER 28 0.01 TYR 192 -0.23 ALA 2

SER 28 0.01 SER 193 -0.19 ALA 2

SER 3 0.02 LYS 194 -0.15 ALA 2

SER 3 0.02 ASN 195 -0.12 ALA 2

SER 3 0.04 VAL 196 -0.08 ALA 2

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.

*** 1P5V_unrelaxed_rank_001_alphafold2_ptm_model_4_seed_000 ***

CA distance fluctuations for 240220090321150899

--- normal mode 7 ---

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

* 1P5V_unrelaxed_rank_001_alphafold2_ptm_model_4_seed_000 *