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

* 4XFX *

CA distance fluctuations for 240228060830932497

--- normal mode 11 ---

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 88 0.38 PRO 1 -0.11 GLU 207

PRO 88 0.35 ILE 2 -0.08 PRO 118

SER 173 0.38 VAL 3 -0.09 SER 11

SER 173 0.45 GLN 4 -0.08 PRO 117

SER 173 0.35 MET 5 -0.06 PRO 117

PRO 88 0.38 VAL 6 -0.07 THR 49

PRO 88 0.47 HIS 7 -0.09 ASN 52

PRO 88 0.46 GLN 8 -0.10 THR 49

PRO 88 0.50 ALA 9 -0.15 THR 53

PRO 88 0.42 ILE 10 -0.16 GLU 207

PRO 88 0.40 SER 11 -0.18 GLU 207

PRO 88 0.40 PRO 12 -0.21 GLU 207

PRO 88 0.34 ARG 13 -0.23 GLU 207

PRO 88 0.32 THR 14 -0.23 GLU 207

PRO 88 0.35 LEU 15 -0.24 GLU 207

PRO 88 0.32 ASN 16 -0.27 GLU 207

PRO 88 0.28 ALA 17 -0.29 GLU 207

PRO 88 0.27 TRP 18 -0.30 GLU 207

PRO 88 0.27 VAL 19 -0.30 GLU 207

PRO 88 0.25 LYS 20 -0.33 GLU 207

PRO 88 0.22 VAL 21 -0.36 GLU 207

PRO 88 0.21 VAL 22 -0.34 GLU 207

PRO 88 0.22 GLU 23 -0.34 GLU 207

PRO 88 0.20 GLU 24 -0.38 GLU 207

PRO 142 0.18 LYS 25 -0.40 GLU 207

PRO 88 0.16 ALA 26 -0.37 ASP 161

PRO 142 0.16 PHE 27 -0.37 ASP 161

PRO 142 0.28 SER 28 -0.45 ASP 161

ALA 169 0.32 PRO 29 -0.39 GLU 207

GLN 4 0.23 GLU 30 -0.46 GLU 207

SER 173 0.21 VAL 31 -0.39 GLU 207

SER 173 0.26 ILE 32 -0.36 GLU 207

SER 173 0.35 PRO 33 -0.36 GLU 207

SER 173 0.27 MET 34 -0.35 GLU 207

SER 173 0.25 PHE 35 -0.31 GLU 207

SER 173 0.34 SER 36 -0.27 GLU 207

SER 173 0.33 ALA 37 -0.26 GLU 207

PRO 88 0.27 LEU 38 -0.26 GLU 207

SER 173 0.28 SER 39 -0.21 GLU 207

SER 173 0.36 GLU 40 -0.16 GLU 207

SER 173 0.34 GLY 41 -0.12 SER 11

PRO 88 0.31 ALA 42 -0.16 GLU 207

PRO 88 0.34 THR 43 -0.15 GLU 207

PRO 88 0.31 PRO 44 -0.18 GLU 207

PRO 88 0.41 GLN 45 -0.18 GLU 207

PRO 88 0.37 ASP 46 -0.18 GLU 207

PRO 88 0.29 LEU 47 -0.22 GLU 207

PRO 88 0.30 ASN 48 -0.22 GLU 207

PRO 88 0.35 THR 49 -0.22 GLU 207

PRO 88 0.30 MET 50 -0.25 GLU 207

PRO 88 0.25 LEU 51 -0.26 GLU 207

PRO 88 0.28 ASN 52 -0.24 GLU 207

PRO 88 0.29 THR 53 -0.25 GLU 207

PRO 88 0.25 VAL 54 -0.27 GLU 207

PRO 88 0.23 GLY 55 -0.26 GLU 207

PRO 88 0.19 GLY 56 -0.27 ASP 158

PRO 88 0.15 HIS 57 -0.28 ASP 158

PRO 88 0.14 GLN 58 -0.25 ASP 158

PRO 88 0.09 ALA 59 -0.25 ASP 161

PRO 88 0.11 ALA 60 -0.27 ASP 161

PRO 88 0.13 MET 61 -0.25 GLU 207

PRO 88 0.09 GLN 62 -0.23 ASP 161

GLY 132 0.07 MET 63 -0.25 ASP 161

PRO 88 0.10 LEU 64 -0.25 GLU 207

GLY 55 0.09 LYS 65 -0.26 THR 102

TRP 128 0.07 GLU 66 -0.23 THR 102

TRP 128 0.11 THR 67 -0.26 GLU 207

TRP 128 0.08 ILE 68 -0.25 GLU 207

ASN 52 0.10 ASN 69 -0.25 SER 97

GLN 4 0.07 GLU 70 -0.27 GLN 171

GLN 4 0.08 GLU 71 -0.27 GLU 207

ASN 52 0.10 ALA 72 -0.24 GLU 207

ASN 52 0.12 ALA 73 -0.30 GLN 174

ASN 52 0.06 GLU 74 -0.37 GLN 174

ASN 52 0.06 TRP 75 -0.27 GLN 174

ASN 52 0.09 ASP 76 -0.27 GLN 174

ASN 52 0.08 ARG 77 -0.38 GLN 174

ASP 76 0.05 LEU 78 -0.36 GLN 174

THR 103 0.06 HIS 79 -0.29 ALA 87

THR 103 0.09 PRO 80 -0.33 ALA 87

THR 103 0.10 VAL 81 -0.34 ALA 87

THR 105 0.11 HIS 82 -0.48 ALA 87

ARG 92 0.18 ALA 83 -0.25 ALA 87

MET 91 0.18 GLY 84 -0.27 ALA 87

GLN 107 0.17 PRO 85 -0.13 ASN 69

GLN 107 0.28 ILE 86 -0.21 HIS 82

GLN 107 0.44 ALA 87 -0.48 HIS 82

GLN 107 0.74 PRO 88 -0.26 HIS 82

GLN 107 0.58 GLY 89 -0.30 HIS 82

GLN 107 0.39 GLN 90 -0.27 HIS 82

GLY 84 0.18 MET 91 -0.09 GLU 207

ALA 83 0.18 ARG 92 -0.13 GLU 207

ALA 83 0.07 GLU 93 -0.27 GLN 90

PRO 88 0.08 PRO 94 -0.17 GLU 207

THR 49 0.09 ARG 95 -0.20 GLU 207

ASP 76 0.09 GLY 96 -0.22 GLU 207

PRO 88 0.16 SER 97 -0.25 ASN 69

PRO 88 0.22 ASP 98 -0.18 GLU 207

PRO 88 0.17 ILE 99 -0.19 GLU 207

PRO 88 0.20 ALA 100 -0.22 GLU 207

PRO 88 0.31 GLY 101 -0.19 LYS 65

PRO 88 0.30 THR 102 -0.26 LYS 65

PRO 88 0.32 THR 103 -0.22 GLU 66

PRO 88 0.42 SER 104 -0.16 LYS 65

PRO 88 0.60 THR 105 -0.17 LYS 65

PRO 88 0.61 LEU 106 -0.14 GLN 62

PRO 88 0.74 GLN 107 -0.12 GLN 62

PRO 88 0.57 GLU 108 -0.11 GLU 207

PRO 88 0.43 GLN 109 -0.12 GLU 207

PRO 88 0.48 ILE 110 -0.09 GLU 207

PRO 88 0.45 GLY 111 -0.08 GLU 207

PRO 88 0.23 TRP 112 -0.10 GLU 207

PRO 88 0.22 MET 113 -0.09 GLU 207

SER 173 0.25 THR 114 -0.05 ILE 110

SER 173 0.21 HIS 115 -0.05 GLY 111

SER 173 0.22 ASN 116 -0.08 GLY 89

SER 173 0.21 PRO 117 -0.17 GLY 89

SER 173 0.24 PRO 118 -0.08 GLU 207

SER 173 0.17 ILE 119 -0.12 GLU 207

SER 173 0.22 PRO 120 -0.14 GLU 207

PRO 88 0.16 VAL 121 -0.17 GLU 207

PRO 88 0.22 GLY 122 -0.17 GLU 207

SER 173 0.26 GLU 123 -0.19 GLU 207

SER 173 0.15 ILE 124 -0.21 GLU 207

PRO 88 0.14 TYR 125 -0.22 GLU 207

SER 173 0.19 LYS 126 -0.24 GLU 207

SER 173 0.19 ARG 127 -0.27 GLU 207

GLN 4 0.12 TRP 128 -0.28 GLU 207

PRO 88 0.13 ILE 129 -0.27 GLU 207

GLN 4 0.19 ILE 130 -0.30 GLU 207

GLN 4 0.17 LEU 131 -0.30 GLU 207

GLN 4 0.13 GLY 132 -0.28 GLU 207

GLN 4 0.16 LEU 133 -0.30 GLU 207

GLN 4 0.20 ASN 134 -0.31 LYS 165

GLN 4 0.16 LYS 135 -0.33 LYS 165

GLN 4 0.14 ILE 136 -0.32 LYS 165

GLN 4 0.19 VAL 137 -0.36 LYS 165

GLN 4 0.20 ARG 138 -0.34 LYS 165

GLN 4 0.16 MET 139 -0.30 LYS 165

GLN 4 0.15 TYR 140 -0.35 ASP 161

PRO 29 0.28 SER 141 -0.36 ARG 162

SER 28 0.28 PRO 142 -0.25 ARG 162

PRO 29 0.26 THR 143 -0.18 GLU 74

GLN 4 0.24 SER 144 -0.19 ARG 77

GLN 4 0.25 ILE 145 -0.21 ARG 77

GLN 4 0.24 LEU 146 -0.17 ARG 77

GLN 4 0.22 ASP 147 -0.16 ARG 77

GLN 4 0.21 ILE 148 -0.18 ARG 77

GLN 4 0.19 ARG 149 -0.17 ARG 77

GLN 4 0.17 GLN 150 -0.17 ARG 77

GLN 4 0.16 GLY 151 -0.16 ARG 77

GLN 4 0.14 PRO 152 -0.15 ARG 77

GLN 4 0.12 LYS 153 -0.20 GLU 24

GLN 4 0.13 GLU 154 -0.23 GLU 24

GLN 4 0.12 PRO 155 -0.31 LYS 25

GLN 4 0.13 PHE 156 -0.30 LYS 25

ASN 178 0.13 ARG 157 -0.40 LYS 25

GLN 4 0.15 ASP 158 -0.38 LYS 25

GLN 4 0.17 TYR 159 -0.26 SER 28

GLN 4 0.18 VAL 160 -0.33 SER 28

GLN 4 0.19 ASP 161 -0.45 SER 28

GLN 4 0.21 ARG 162 -0.36 SER 141

GLN 4 0.23 PHE 163 -0.23 GLU 74

GLN 4 0.25 TYR 164 -0.29 LYS 135

GLN 4 0.25 LYS 165 -0.36 VAL 137

GLN 4 0.25 THR 166 -0.30 ARG 138

GLN 4 0.27 LEU 167 -0.28 GLU 74

GLN 4 0.29 ARG 168 -0.29 GLU 74

PRO 29 0.32 ALA 169 -0.31 LYS 135

GLN 4 0.28 GLU 170 -0.27 GLU 74

GLN 4 0.30 GLN 171 -0.30 GLU 74

GLN 4 0.36 ALA 172 -0.32 GLU 74

GLN 4 0.45 SER 173 -0.36 ARG 77

GLN 4 0.44 GLN 174 -0.38 ARG 77

GLN 4 0.42 GLU 175 -0.32 ARG 77

GLN 4 0.38 VAL 176 -0.26 ARG 77

GLN 4 0.34 LYS 177 -0.29 ARG 77

GLN 4 0.34 ASN 178 -0.29 ARG 77

GLN 4 0.32 TRP 179 -0.23 ARG 77

GLN 4 0.29 MET 180 -0.23 ARG 77

GLN 4 0.26 THR 181 -0.25 ARG 77

GLN 4 0.25 GLU 182 -0.22 ARG 77

GLN 4 0.25 THR 183 -0.19 ARG 77

GLN 4 0.24 LEU 184 -0.18 ARG 77

GLN 4 0.21 LEU 185 -0.21 ARG 77

GLN 4 0.19 VAL 186 -0.19 ARG 77

GLN 4 0.20 GLN 187 -0.16 ARG 77

GLN 4 0.20 ASN 188 -0.16 ARG 77

GLN 4 0.17 ALA 189 -0.17 ARG 77

GLN 4 0.15 ASN 190 -0.15 ARG 77

GLN 4 0.14 PRO 191 -0.14 ARG 77

GLN 4 0.11 ASP 192 -0.17 GLU 24

GLN 4 0.12 CYS 193 -0.20 GLU 24

GLN 4 0.14 LYS 194 -0.16 ARG 77

GLN 4 0.11 THR 195 -0.16 ARG 77

GLN 4 0.09 ILE 196 -0.20 GLU 24

GLN 4 0.11 LEU 197 -0.21 GLU 30

GLN 4 0.12 LYS 198 -0.17 ARG 77

GLN 4 0.09 ALA 199 -0.19 GLU 30

GLN 4 0.08 LEU 200 -0.24 GLU 30

GLN 4 0.10 GLY 201 -0.21 GLU 30

GLN 4 0.13 PRO 202 -0.22 ARG 77

THR 183 0.13 GLY 203 -0.26 GLU 30

THR 183 0.13 ALA 204 -0.30 GLU 30

GLU 182 0.21 THR 205 -0.37 GLU 30

GLU 182 0.22 LEU 206 -0.40 GLU 30

GLU 182 0.15 GLU 207 -0.46 GLU 30

GLU 182 0.13 GLU 208 -0.37 GLU 30

GLU 182 0.12 MET 209 -0.32 GLU 30

GLU 182 0.12 MET 210 -0.37 GLU 30

GLU 182 0.09 THR 211 -0.37 LYS 25

GLU 182 0.07 ALA 212 -0.31 LYS 25

GLN 4 0.09 CYS 213 -0.29 LYS 25

GLU 182 0.07 GLN 214 -0.35 GLU 24

GLN 4 0.05 GLY 215 -0.33 GLU 24

GLN 4 0.08 VAL 216 -0.28 GLU 24

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.

*** 4XFX ***

CA distance fluctuations for 240228060830932497

--- normal mode 11 ---

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

* 4XFX *