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

* 1P5V *

CA distance fluctuations for 240228061130936516

--- 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
ASP 90 0.26 PHE 1 -0.80 VAL 93

PRO 170 0.54 ALA 2 -0.41 VAL 93

PRO 170 0.72 SER 3 -0.31 ASP 33

PRO 170 0.58 LYS 4 -0.17 TYR 34

PRO 155 0.54 GLU 5 -0.24 PHE 1

PRO 155 0.52 TYR 6 -0.28 PHE 1

PRO 155 0.52 GLY 7 -0.24 PHE 1

PRO 155 0.45 VAL 8 -0.21 PHE 1

PRO 155 0.43 THR 9 -0.19 PHE 1

PRO 155 0.35 ILE 10 -0.18 PHE 1

PRO 155 0.30 GLY 11 -0.15 PHE 1

PRO 155 0.26 GLU 12 -0.17 PHE 1

PRO 155 0.27 SER 13 -0.19 PHE 1

PRO 155 0.17 ARG 14 -0.18 PHE 1

PRO 155 0.14 ILE 15 -0.16 PHE 1

GLN 180 0.12 ILE 16 -0.15 PHE 1

GLN 180 0.12 TYR 17 -0.14 PHE 1

GLN 180 0.13 PRO 18 -0.15 MET 25

GLN 180 0.09 LEU 19 -0.13 PHE 1

GLN 180 0.11 ASP 20 -0.14 ARG 74

GLN 180 0.14 ALA 21 -0.12 PHE 1

GLN 180 0.13 ALA 22 -0.12 PHE 1

GLN 180 0.13 GLY 23 -0.13 PHE 1

GLN 180 0.14 VAL 24 -0.17 MET 25

PRO 155 0.16 MET 25 -0.17 VAL 24

PRO 155 0.21 VAL 26 -0.14 PHE 1

PRO 155 0.25 SER 27 -0.13 PHE 1

PRO 155 0.25 SER 27 -0.12 PHE 1

PRO 155 0.31 VAL 28 -0.14 PHE 1

PRO 155 0.31 VAL 28 -0.14 PHE 1

PRO 155 0.31 VAL 28 -0.14 PHE 1

PRO 155 0.35 LYS 29 -0.11 PHE 1

PRO 155 0.38 ASN 30 -0.12 SER 3

PRO 155 0.43 THR 31 -0.14 SER 3

PRO 155 0.44 GLN 32 -0.21 SER 3

PRO 155 0.40 ASP 33 -0.31 SER 3

PRO 155 0.37 TYR 34 -0.27 SER 3

PRO 155 0.33 PRO 35 -0.19 SER 3

PRO 155 0.33 VAL 36 -0.12 SER 3

PRO 155 0.28 LEU 37 -0.12 PHE 1

PRO 155 0.28 ILE 38 -0.16 PHE 1

PRO 155 0.23 GLN 39 -0.19 PHE 1

PRO 155 0.20 SER 40 -0.19 PHE 1

ASP 168 0.15 ARG 41 -0.20 PHE 1

ASP 168 0.11 ILE 42 -0.18 PHE 1

SER 3 0.13 TYR 43 -0.19 PHE 1

PHE 94 0.09 ASP 44 -0.15 PHE 1

PHE 94 0.08 PRO 45 -0.14 PHE 1

PHE 94 0.07 PHE 46 -0.15 PHE 1

PRO 155 0.09 VAL 47 -0.15 PHE 1

PRO 155 0.13 VAL 48 -0.15 PHE 1

PRO 155 0.13 VAL 48 -0.15 PHE 1

PRO 155 0.15 THR 49 -0.13 PHE 1

PRO 155 0.17 PRO 50 -0.12 PHE 1

PRO 155 0.16 PRO 51 -0.15 PHE 1

PRO 155 0.20 LEU 52 -0.14 PHE 1

PRO 155 0.22 PHE 53 -0.10 PHE 1

PRO 155 0.25 ARG 54 -0.11 SER 3

PRO 155 0.29 LEU 55 -0.13 SER 3

PRO 155 0.31 ASP 56 -0.17 SER 3

PRO 155 0.35 ALA 57 -0.21 SER 3

PRO 155 0.36 LYS 58 -0.19 SER 3

PRO 155 0.32 GLN 59 -0.15 SER 3

PRO 155 0.29 GLN 60 -0.11 SER 3

PRO 155 0.25 ASN 61 -0.11 ASN 110

PRO 155 0.22 SER 62 -0.12 ASN 110

PRO 155 0.22 SER 62 -0.12 ASN 110

PRO 155 0.19 LEU 63 -0.13 PHE 1

PRO 155 0.15 ARG 64 -0.13 PHE 1

PRO 155 0.13 ILE 65 -0.15 PHE 1

PRO 155 0.09 ALA 66 -0.13 PHE 1

GLN 180 0.08 GLN 67 -0.13 PHE 1

GLN 180 0.07 ALA 68 -0.13 PHE 1

PHE 94 0.06 GLY 69 -0.13 PHE 1

PHE 94 0.09 GLY 70 -0.13 PHE 1

VAL 95 0.09 VAL 71 -0.12 PHE 1

VAL 95 0.11 PHE 72 -0.12 SER 163

SER 3 0.13 PRO 73 -0.13 SER 163

SER 3 0.11 ARG 74 -0.14 ASP 20

SER 3 0.14 ASP 75 -0.12 ASP 20

SER 3 0.16 LYS 76 -0.11 ASP 20

SER 3 0.15 GLU 77 -0.11 PHE 1

SER 3 0.16 SER 78 -0.12 PHE 1

SER 3 0.17 LEU 79 -0.13 PHE 1

SER 3 0.15 LYS 80 -0.16 PHE 1

SER 3 0.15 TRP 81 -0.18 PHE 1

PRO 155 0.17 LEU 82 -0.19 PHE 1

PRO 155 0.24 CYS 83 -0.22 PHE 1

PRO 155 0.29 VAL 84 -0.22 PHE 1

PRO 155 0.32 LYS 85 -0.25 PHE 1

PRO 155 0.36 GLY 86 -0.21 PHE 1

PRO 155 0.33 ILE 87 -0.21 PHE 1

PRO 155 0.36 PRO 88 -0.15 PHE 1

TYR 34 0.35 LYS 89 -0.12 LEU 183

TYR 34 0.34 ASP 90 -0.04 TYR 43

GLY 130 0.20 VAL 91 -0.16 PHE 1

GLY 130 0.36 GLY 92 -0.21 PHE 1

GLY 130 0.40 VAL 93 -0.80 PHE 1

ASP 168 0.46 PHE 94 -0.51 PHE 1

ASP 168 0.51 VAL 95 -0.64 PHE 1

ASP 168 0.48 GLN 96 -0.45 PHE 1

ASP 168 0.49 PHE 97 -0.48 PHE 1

ASP 168 0.43 ALA 98 -0.37 PHE 1

PRO 155 0.47 ILE 99 -0.35 PHE 1

PRO 155 0.39 ASN 100 -0.30 PHE 1

PRO 155 0.42 ASN 101 -0.27 PHE 1

HIS 157 0.32 CYS 102 -0.23 PHE 1

HIS 157 0.27 ILE 103 -0.20 PHE 1

ILE 103 0.17 LYS 104 -0.17 PHE 1

PRO 155 0.11 LEU 105 -0.16 PHE 1

SER 3 0.12 LEU 106 -0.14 PHE 1

SER 3 0.10 VAL 107 -0.13 PHE 1

SER 3 0.09 ARG 108 -0.12 PHE 1

PHE 94 0.08 PRO 109 -0.13 MET 25

GLN 180 0.09 ASN 110 -0.15 MET 25

PHE 94 0.06 GLU 111 -0.13 MET 25

SER 3 0.09 LEU 112 -0.12 MET 25

SER 3 0.08 LYS 113 -0.13 MET 25

SER 3 0.07 GLY 114 -0.13 MET 25

SER 3 0.09 THR 115 -0.12 PHE 1

SER 3 0.14 PRO 116 -0.11 PHE 1

SER 3 0.14 ILE 117 -0.11 PHE 1

SER 3 0.13 GLN 118 -0.10 PHE 1

SER 3 0.18 PHE 119 -0.08 LYS 89

SER 3 0.21 ALA 120 -0.09 LYS 89

SER 3 0.23 GLU 121 -0.08 LYS 89

SER 3 0.24 ASN 122 -0.08 LYS 89

SER 3 0.30 LEU 123 -0.08 LYS 89

SER 3 0.34 SER 124 -0.08 ASP 75

SER 3 0.40 TRP 125 -0.08 PRO 73

SER 3 0.44 LYS 126 -0.08 PRO 73

SER 3 0.50 VAL 127 -0.08 PRO 73

SER 3 0.52 ASP 128 -0.09 PRO 73

SER 3 0.57 GLY 129 -0.09 PRO 73

SER 3 0.62 GLY 130 -0.07 PRO 73

SER 3 0.59 LYS 131 -0.08 PRO 73

SER 3 0.53 LEU 132 -0.07 PRO 73

SER 3 0.47 ILE 133 -0.09 PRO 73

SER 3 0.40 ALA 134 -0.08 PRO 73

SER 3 0.34 GLU 135 -0.09 PRO 73

SER 3 0.28 ASN 136 -0.08 PRO 73

SER 3 0.25 PRO 137 -0.10 ASP 75

SER 3 0.20 SER 138 -0.09 LEU 112

SER 3 0.18 PRO 139 -0.09 PRO 109

SER 3 0.18 PHE 140 -0.09 PHE 1

SER 3 0.22 TYR 141 -0.09 LYS 89

SER 3 0.25 MET 142 -0.10 LYS 89

SER 3 0.27 ASN 143 -0.11 LYS 89

SER 3 0.33 ILE 144 -0.11 LYS 89

SER 3 0.34 GLY 145 -0.12 LYS 89

SER 3 0.41 GLU 146 -0.11 LYS 89

SER 3 0.46 LEU 147 -0.10 LYS 89

SER 3 0.51 THR 148 -0.09 LYS 89

SER 3 0.53 PHE 149 -0.07 LYS 89

SER 3 0.54 GLY 150 -0.06 LYS 89

SER 3 0.53 GLY 151 -0.07 LYS 89

SER 3 0.62 LYS 152 -0.08 LYS 89

SER 3 0.62 SER 153 -0.09 LYS 89

SER 3 0.63 ILE 154 -0.08 LYS 89

SER 3 0.64 PRO 155 -0.10 LYS 89

SER 3 0.51 SER 156 -0.10 LYS 89

SER 3 0.45 HIS 157 -0.10 LYS 89

SER 3 0.34 TYR 158 -0.10 LYS 89

SER 3 0.34 ILE 159 -0.09 LYS 89

SER 3 0.29 PRO 160 -0.10 PHE 72

SER 3 0.24 PRO 161 -0.09 PHE 72

SER 3 0.25 LYS 162 -0.12 PRO 73

SER 3 0.31 SER 163 -0.13 PRO 73

SER 3 0.37 THR 164 -0.11 PHE 72

SER 3 0.43 TRP 165 -0.10 PHE 72

SER 3 0.51 ALA 166 -0.09 PHE 72

SER 3 0.58 PHE 167 -0.07 PHE 72

SER 3 0.67 ASP 168 -0.06 PHE 72

SER 3 0.66 LEU 169 -0.05 PRO 73

SER 3 0.72 PRO 170 -0.05 LYS 89

SER 3 0.44 ASN 171 -0.06 LYS 89

SER 3 0.43 VAL 172 -0.07 LYS 89

SER 3 0.39 SER 173 -0.09 LYS 89

SER 3 0.36 TRP 174 -0.10 LYS 89

SER 3 0.28 ARG 175 -0.11 LYS 89

SER 3 0.25 ILE 176 -0.11 LYS 89

SER 3 0.19 ILE 177 -0.13 PHE 1

SER 3 0.11 ASN 178 -0.15 PHE 1

PRO 18 0.10 ASP 179 -0.16 PHE 1

VAL 24 0.14 GLN 180 -0.19 PHE 1

GLU 12 0.15 GLY 181 -0.19 PHE 1

GLY 11 0.13 GLY 182 -0.18 PHE 1

SER 3 0.16 LEU 183 -0.14 PHE 1

SER 3 0.16 ASP 184 -0.12 PHE 1

SER 3 0.18 ARG 185 -0.11 LYS 89

SER 3 0.25 LEU 186 -0.10 LYS 89

SER 3 0.28 TYR 187 -0.09 LYS 89

SER 3 0.33 SER 188 -0.08 LYS 89

SER 3 0.35 LYS 189 -0.07 LYS 89

SER 3 0.39 ASN 190 -0.06 LYS 89

SER 3 0.42 VAL 191 -0.07 ASP 75

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 ***

CA distance fluctuations for 240228061130936516

--- normal mode 14 ---

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

* 1P5V *