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

* AF-1P5V_recycle_9 *

CA distance fluctuations for 2402070228301791804

--- normal mode 14 ---

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
LYS 157 0.37 PHE 1 -1.87 CYS 107

LYS 62 0.32 ALA 2 -0.63 ASN 105

GLY 150 0.59 SER 3 -0.41 ASP 95

GLY 187 0.52 LYS 4 -0.46 ASP 95

GLY 187 0.41 GLU 5 -0.45 ASP 95

PHE 102 0.38 TYR 6 -0.46 PHE 1

GLN 101 0.62 GLY 7 -0.49 PHE 1

GLN 101 0.38 VAL 8 -0.78 PHE 1

GLN 101 0.28 THR 9 -0.90 PHE 1

GLN 185 0.23 ILE 10 -1.10 PHE 1

LYS 4 0.31 GLY 11 -0.86 PHE 1

LYS 4 0.34 GLU 12 -0.97 PHE 1

LYS 4 0.46 SER 13 -0.99 PHE 1

LYS 4 0.35 ARG 14 -1.06 PHE 1

LYS 4 0.26 ILE 15 -1.03 PHE 1

LYS 4 0.25 ILE 16 -0.87 PHE 1

VAL 96 0.19 TYR 17 -0.88 PHE 1

LYS 4 0.18 PRO 18 -0.75 PHE 1

VAL 96 0.18 LEU 19 -0.74 PHE 1

VAL 96 0.15 ASP 20 -0.69 PHE 1

VAL 96 0.13 ALA 21 -0.69 PHE 1

GLY 119 0.13 ALA 22 -0.65 PHE 1

GLY 119 0.11 GLY 23 -0.71 PHE 1

VAL 96 0.12 VAL 24 -0.79 PHE 1

VAL 96 0.13 MET 25 -0.80 PHE 1

LYS 4 0.13 VAL 26 -0.80 PHE 1

LYS 4 0.17 SER 27 -0.87 PHE 1

LYS 4 0.16 SER 28 -0.83 PHE 1

GLN 185 0.19 VAL 29 -0.98 PHE 1

GLN 101 0.19 VAL 30 -0.88 PHE 1

GLN 101 0.22 VAL 31 -0.92 PHE 1

GLN 101 0.32 LYS 32 -0.71 PHE 1

GLN 101 0.43 ASN 33 -0.59 PHE 1

GLN 101 0.53 THR 34 -0.41 PHE 1

GLN 101 0.70 GLN 35 -0.42 ASP 95

GLN 101 0.66 ASP 36 -0.44 ASP 95

GLN 101 0.59 TYR 37 -0.43 ASP 95

PHE 99 0.43 PRO 38 -0.45 PHE 1

PHE 99 0.36 VAL 39 -0.59 PHE 1

PHE 99 0.24 LEU 40 -0.71 PHE 1

VAL 96 0.21 ILE 41 -0.87 PHE 1

VAL 96 0.32 GLN 42 -1.00 PHE 1

VAL 96 0.28 SER 43 -1.16 PHE 1

VAL 96 0.33 ARG 44 -1.24 PHE 1

VAL 96 0.32 ILE 45 -1.27 PHE 1

VAL 96 0.37 TYR 46 -1.22 PHE 1

VAL 96 0.32 ASP 47 -1.08 PHE 1

VAL 96 0.30 PRO 48 -0.97 PHE 1

VAL 96 0.25 PHE 49 -0.93 PHE 1

VAL 96 0.25 VAL 50 -1.01 PHE 1

VAL 96 0.24 VAL 51 -1.03 PHE 1

VAL 96 0.22 VAL 52 -1.07 PHE 1

VAL 96 0.17 THR 53 -0.94 PHE 1

VAL 96 0.17 PRO 54 -0.90 PHE 1

VAL 96 0.24 PRO 55 -0.97 PHE 1

VAL 96 0.22 LEU 56 -0.87 PHE 1

PHE 99 0.16 PHE 57 -0.79 PHE 1

PHE 99 0.23 ARG 58 -0.67 PHE 1

GLN 101 0.28 LEU 59 -0.62 PHE 1

GLN 101 0.37 ASP 60 -0.46 PHE 1

GLN 101 0.48 ALA 61 -0.35 PHE 1

GLN 101 0.46 LYS 62 -0.35 PHE 1

GLN 101 0.36 GLN 63 -0.48 PHE 1

GLN 101 0.28 GLN 64 -0.63 PHE 1

GLN 101 0.20 ASN 65 -0.75 PHE 1

GLN 101 0.17 SER 66 -0.77 PHE 1

GLN 185 0.12 SER 67 -0.80 PHE 1

VAL 96 0.14 LEU 68 -0.96 PHE 1

VAL 96 0.14 ARG 69 -0.93 PHE 1

VAL 96 0.18 ILE 70 -0.99 PHE 1

VAL 96 0.18 ALA 71 -0.91 PHE 1

VAL 96 0.19 GLN 72 -0.89 PHE 1

VAL 96 0.19 ALA 73 -0.86 PHE 1

VAL 96 0.20 GLY 74 -0.81 PHE 1

VAL 96 0.23 GLY 75 -0.80 PHE 1

VAL 96 0.23 VAL 76 -0.74 PHE 1

VAL 96 0.24 PHE 77 -0.75 PHE 1

VAL 96 0.24 PRO 78 -0.67 PHE 1

VAL 96 0.21 ARG 79 -0.61 PHE 1

VAL 96 0.22 ASP 80 -0.55 PHE 1

VAL 96 0.23 LYS 81 -0.61 PHE 1

VAL 96 0.24 GLU 82 -0.72 PHE 1

VAL 96 0.27 SER 83 -0.85 PHE 1

VAL 96 0.28 LEU 84 -1.00 PHE 1

VAL 96 0.30 LYS 85 -1.19 PHE 1

VAL 96 0.32 TRP 86 -1.44 PHE 1

VAL 96 0.29 LEU 87 -1.51 PHE 1

VAL 96 0.33 CYS 88 -1.55 PHE 1

VAL 96 0.29 VAL 89 -1.28 PHE 1

VAL 96 0.33 LYS 90 -1.05 PHE 1

VAL 96 0.24 GLY 91 -0.82 PHE 1

VAL 96 0.32 ILE 92 -0.70 PHE 1

PHE 99 0.40 PRO 93 -0.56 PHE 1

PHE 99 0.43 LYS 94 -0.46 PHE 1

TYR 46 0.23 ASP 95 -0.46 LYS 4

TYR 46 0.37 VAL 96 -0.33 PHE 1

TYR 46 0.24 GLY 97 -0.42 LYS 4

TYR 37 0.26 VAL 98 -0.25 LYS 4

TYR 37 0.52 PHE 99 -0.37 LYS 4

ASP 36 0.25 VAL 100 -0.30 PHE 1

GLN 35 0.70 GLN 101 -0.27 PHE 1

GLY 7 0.53 PHE 102 -0.46 PHE 1

VAL 96 0.31 ALA 103 -0.73 PHE 1

SER 13 0.24 ILE 104 -0.87 PHE 1

VAL 96 0.35 ASN 105 -1.23 PHE 1

VAL 96 0.26 ASN 106 -1.40 PHE 1

VAL 96 0.30 CYS 107 -1.87 PHE 1

VAL 96 0.26 ILE 108 -1.61 PHE 1

VAL 96 0.27 LYS 109 -1.32 PHE 1

VAL 96 0.26 LEU 110 -1.19 PHE 1

VAL 96 0.24 LEU 111 -0.96 PHE 1

VAL 96 0.23 VAL 112 -0.89 PHE 1

VAL 96 0.21 ARG 113 -0.75 PHE 1

VAL 96 0.20 PRO 114 -0.67 PHE 1

LYS 4 0.18 ASN 115 -0.60 PHE 1

LYS 4 0.18 GLU 116 -0.54 PHE 1

LYS 4 0.21 LEU 117 -0.53 PHE 1

SER 3 0.23 LYS 118 -0.44 PHE 1

SER 3 0.28 GLY 119 -0.39 PHE 1

SER 3 0.32 THR 120 -0.41 PHE 1

SER 3 0.36 PRO 121 -0.41 PHE 1

SER 3 0.38 ILE 122 -0.28 PHE 1

SER 3 0.33 GLN 123 -0.26 PHE 1

SER 3 0.32 PHE 124 -0.29 PHE 1

SER 3 0.35 ALA 125 -0.23 PHE 1

SER 3 0.32 GLU 126 -0.15 PHE 1

SER 3 0.29 ASN 127 -0.21 PHE 1

SER 3 0.30 LEU 128 -0.22 PHE 1

SER 3 0.26 SER 129 -0.18 PHE 1

SER 3 0.24 TRP 130 -0.23 ALA 2

SER 3 0.19 LYS 131 -0.27 ALA 2

SER 3 0.15 VAL 132 -0.33 ALA 2

SER 3 0.12 ASP 133 -0.37 ALA 2

PRO 160 0.08 GLY 134 -0.43 ALA 2

PRO 160 0.09 GLY 135 -0.45 ALA 2

PRO 160 0.12 LYS 136 -0.46 ALA 2

SER 3 0.18 LEU 137 -0.38 ALA 2

SER 3 0.21 ILE 138 -0.34 ALA 2

SER 3 0.26 ALA 139 -0.28 ALA 2

SER 3 0.26 GLU 140 -0.29 PHE 1

SER 3 0.28 ASN 141 -0.36 PHE 1

SER 3 0.26 PRO 142 -0.35 PHE 1

SER 3 0.28 SER 143 -0.41 PHE 1

SER 3 0.26 PRO 144 -0.51 PHE 1

SER 3 0.30 PHE 145 -0.55 PHE 1

SER 3 0.33 TYR 146 -0.63 PHE 1

SER 3 0.39 MET 147 -0.48 PHE 1

SER 3 0.46 ASN 148 -0.53 PHE 1

SER 3 0.49 ILE 149 -0.32 PHE 1

SER 3 0.59 GLY 150 -0.22 PRO 160

SER 3 0.50 GLU 151 -0.17 PRO 160

SER 3 0.37 LEU 152 -0.20 ALA 2

SER 3 0.28 THR 153 -0.20 ALA 2

SER 3 0.21 PHE 154 -0.26 ALA 2

PHE 1 0.25 GLY 155 -0.22 ALA 2

PHE 1 0.36 GLY 156 -0.15 ALA 2

PHE 1 0.37 LYS 157 -0.27 ALA 2

PHE 1 0.30 SER 158 -0.30 ALA 2

LYS 4 0.22 ILE 159 -0.46 ALA 2

LYS 4 0.24 PRO 160 -0.59 ALA 2

SER 3 0.42 SER 161 -0.36 ALA 2

SER 3 0.43 HIS 162 -0.51 PHE 1

SER 3 0.41 TYR 163 -0.59 PHE 1

SER 3 0.33 ILE 164 -0.51 PHE 1

LYS 4 0.29 PRO 165 -0.60 PHE 1

LYS 4 0.27 PRO 166 -0.54 PHE 1

LYS 4 0.25 LYS 167 -0.46 PHE 1

LYS 4 0.25 SER 168 -0.45 PHE 1

SER 3 0.24 THR 169 -0.38 PHE 1

LYS 4 0.25 TRP 170 -0.38 PHE 1

LYS 4 0.20 ALA 171 -0.43 ALA 2

LYS 4 0.19 PHE 172 -0.48 ALA 2

PRO 160 0.14 ASP 173 -0.56 ALA 2

LYS 4 0.11 LEU 174 -0.44 ALA 2

SER 3 0.12 PRO 175 -0.35 ALA 2

SER 3 0.19 ASN 176 -0.23 ALA 2

SER 3 0.25 VAL 177 -0.20 ALA 2

SER 3 0.32 SER 178 -0.10 ASP 47

SER 3 0.39 TRP 179 -0.09 LYS 85

SER 3 0.47 ARG 180 -0.11 PRO 160

SER 3 0.48 ILE 181 -0.24 PHE 1

SER 3 0.53 ILE 182 -0.35 PHE 1

SER 3 0.46 ASN 183 -0.38 PHE 1

SER 3 0.40 ASP 184 -0.52 PHE 1

SER 3 0.45 GLN 185 -0.45 PHE 1

SER 3 0.54 GLY 186 -0.45 PHE 1

SER 3 0.58 GLY 187 -0.22 PHE 1

SER 3 0.58 LEU 188 -0.13 PRO 160

SER 3 0.48 ASP 189 -0.10 PRO 160

SER 3 0.43 ARG 190 -0.07 PRO 160

SER 3 0.40 LEU 191 -0.06 PRO 160

SER 3 0.36 TYR 192 -0.05 ASP 47

SER 3 0.30 SER 193 -0.07 ASP 47

SER 3 0.26 LYS 194 -0.11 ALA 2

SER 3 0.21 ASN 195 -0.14 ALA 2

SER 3 0.19 VAL 196 -0.21 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.

*** AF-1P5V_recycle_9 ***

CA distance fluctuations for 2402070228301791804

--- normal mode 14 ---

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

* AF-1P5V_recycle_9 *