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

* 1AOL *

CA distance fluctuations for 240228060428927675

--- 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
THR 191 0.25 GLN 1 -0.51 PRO 225

GLN 189 0.23 VAL 2 -0.50 PRO 225

ASN 185 0.23 TYR 3 -0.29 TYR 56

VAL 227 0.45 ASN 4 -0.39 TYR 56

VAL 227 0.51 ILE 5 -0.32 TYR 56

PRO 228 0.64 THR 6 -0.36 TYR 56

PRO 228 0.66 TRP 7 -0.24 TYR 56

PRO 228 0.79 GLU 8 -0.26 SER 21

PRO 228 0.75 VAL 9 -0.27 SER 21

PRO 228 0.79 THR 10 -0.30 SER 21

PRO 228 0.73 ASN 11 -0.30 SER 21

PRO 228 0.71 GLY 12 -0.45 PRO 128

PRO 228 0.80 ASP 13 -0.47 PRO 128

PRO 228 0.85 ARG 14 -0.39 PRO 128

PRO 228 0.93 GLU 15 -0.35 SER 21

PRO 228 0.90 THR 16 -0.46 SER 21

PRO 228 0.81 VAL 17 -0.43 SER 21

PRO 228 0.76 TRP 18 -0.52 ALA 19

PRO 228 0.77 ALA 19 -0.52 TRP 18

PRO 228 0.61 ILE 20 -0.44 TYR 56

VAL 227 0.50 SER 21 -0.62 TYR 56

VAL 227 0.33 GLY 22 -0.54 TYR 56

VAL 227 0.22 ASN 23 -0.51 TYR 56

ASN 185 0.28 HIS 24 -0.42 PRO 225

ASN 185 0.25 PRO 25 -0.36 PRO 225

LYS 188 0.27 LEU 26 -0.22 TYR 56

LYS 188 0.29 TRP 27 -0.21 SER 58

ASN 185 0.37 THR 28 -0.28 SER 58

SER 149 0.29 TRP 29 -0.31 SER 58

SER 149 0.34 TRP 30 -0.38 PRO 31

PRO 228 0.39 PRO 31 -0.38 TRP 30

PRO 228 0.44 VAL 32 -0.26 SER 58

PRO 228 0.55 LEU 33 -0.25 TRP 30

PRO 228 0.57 THR 34 -0.26 SER 58

PRO 228 0.63 PRO 35 -0.23 TRP 30

PRO 228 0.61 ASP 36 -0.22 ASN 23

PRO 228 0.58 LEU 37 -0.19 ASN 23

PRO 228 0.59 CYS 38 -0.25 ASN 23

PRO 228 0.66 MET 39 -0.31 SER 21

PRO 228 0.66 LEU 40 -0.27 SER 21

PRO 228 0.62 ALA 41 -0.28 SER 21

PRO 228 0.66 LEU 42 -0.37 SER 21

PRO 228 0.66 SER 43 -0.35 SER 21

PRO 228 0.63 GLY 44 -0.28 SER 21

PRO 228 0.56 PRO 45 -0.30 GLY 74

PRO 228 0.53 PRO 46 -0.39 GLY 74

PRO 228 0.50 HIS 47 -0.35 GLY 74

PRO 228 0.53 TRP 48 -0.31 GLY 74

PRO 228 0.53 GLY 49 -0.40 GLY 74

PRO 228 0.58 LEU 50 -0.34 GLY 61

PRO 228 0.60 GLU 51 -0.36 GLY 74

PRO 228 0.61 TYR 52 -0.41 GLY 74

PRO 228 0.64 GLN 53 -0.41 SER 21

PRO 228 0.72 ALA 54 -0.48 SER 21

PRO 228 0.78 PRO 55 -0.51 SER 21

PRO 228 0.72 TYR 56 -0.62 SER 21

PRO 228 0.65 SER 57 -0.55 SER 21

PRO 228 0.57 SER 58 -0.48 GLY 22

PRO 228 0.56 PRO 59 -0.36 ASN 23

PRO 228 0.52 PRO 60 -0.34 SER 69

PRO 228 0.47 GLY 61 -0.38 GLY 49

PRO 228 0.47 PRO 62 -0.31 TYR 52

PRO 228 0.48 PRO 63 -0.30 SER 69

PRO 228 0.46 CYS 64 -0.25 THR 92

PRO 228 0.43 CYS 65 -0.22 TYR 52

PRO 228 0.43 SER 66 -0.18 GLY 67

PRO 228 0.47 GLY 67 -0.23 THR 92

PRO 228 0.47 SER 68 -0.18 PRO 60

PRO 228 0.43 SER 69 -0.34 PRO 60

PRO 228 0.41 GLY 70 -0.28 PRO 62

PRO 228 0.41 SER 71 -0.29 TYR 52

PRO 228 0.44 SER 72 -0.34 TYR 52

PRO 228 0.42 ALA 73 -0.38 TYR 52

PRO 228 0.43 GLY 74 -0.41 TYR 52

PRO 228 0.44 CYS 75 -0.30 TYR 52

PRO 228 0.44 SER 76 -0.28 GLY 49

PRO 228 0.42 ARG 77 -0.19 THR 87

PRO 228 0.42 ASP 78 -0.24 THR 87

PRO 228 0.44 CYS 79 -0.15 GLY 67

PRO 228 0.42 ASP 80 -0.10 GLY 67

PRO 228 0.40 GLU 81 -0.13 SER 206

PRO 228 0.39 PRO 82 -0.09 SER 206

PRO 228 0.41 LEU 83 -0.11 SER 206

PRO 228 0.39 THR 84 -0.18 SER 107

PRO 228 0.40 SER 85 -0.30 SER 206

PRO 228 0.43 LEU 86 -0.29 SER 206

PRO 228 0.44 THR 87 -0.29 GLY 74

PRO 228 0.46 PRO 88 -0.22 GLY 74

PRO 228 0.50 ARG 89 -0.24 GLY 74

PRO 228 0.53 CYS 90 -0.24 ASN 23

PRO 228 0.50 ASN 91 -0.36 GLY 61

PRO 228 0.48 THR 92 -0.29 PRO 63

PRO 228 0.49 ALA 93 -0.19 SER 69

PRO 228 0.46 TRP 94 -0.15 ASN 23

PRO 228 0.47 ASN 95 -0.21 GLY 74

PRO 228 0.49 ARG 96 -0.17 ASN 23

PRO 228 0.47 LEU 97 -0.12 ASN 23

PRO 228 0.45 LYS 98 -0.11 GLY 74

PRO 228 0.47 LEU 99 -0.12 ASN 23

PRO 228 0.47 ASP 100 -0.11 ASN 185

PRO 228 0.43 GLN 101 -0.10 ASN 185

PRO 228 0.44 VAL 102 -0.13 SER 85

PRO 228 0.46 THR 103 -0.09 ASN 185

PRO 228 0.43 HIS 104 -0.10 ASN 185

PRO 228 0.41 LYS 105 -0.15 THR 84

PRO 228 0.40 SER 106 -0.15 SER 85

PRO 228 0.39 SER 107 -0.21 SER 85

PRO 228 0.41 GLU 108 -0.20 SER 85

PRO 228 0.44 GLY 109 -0.15 SER 85

PRO 228 0.47 PHE 110 -0.12 SER 85

PRO 228 0.47 TYR 111 -0.11 SER 85

PRO 228 0.49 VAL 112 -0.10 GLY 61

PRO 228 0.48 CYS 113 -0.11 GLY 74

PRO 228 0.50 PRO 114 -0.11 ARG 118

PRO 228 0.52 GLY 115 -0.23 ARG 120

PRO 228 0.51 SER 116 -0.33 ARG 120

PRO 228 0.50 HIS 117 -0.17 THR 195

PRO 228 0.45 ARG 118 -0.14 GLU 139

PRO 228 0.40 PRO 119 -0.21 SER 116

ALA 186 0.36 ARG 120 -0.33 SER 116

PRO 228 0.38 GLU 121 -0.18 ASP 13

PRO 228 0.38 ALA 122 -0.26 ASP 13

PRO 228 0.34 LYS 123 -0.27 ASP 13

PRO 228 0.36 SER 124 -0.27 ASP 13

PRO 228 0.41 CYS 125 -0.24 ASP 13

PRO 228 0.41 GLY 126 -0.33 ASP 13

PRO 228 0.45 GLY 127 -0.37 ASP 13

PRO 228 0.49 PRO 128 -0.47 ASP 13

PRO 228 0.44 ASP 129 -0.46 ASP 13

PRO 228 0.44 SER 130 -0.33 ASP 13

PRO 228 0.49 PHE 131 -0.28 GLY 12

PRO 228 0.47 TYR 132 -0.23 ASP 13

PRO 228 0.44 CYS 133 -0.21 ASP 13

PRO 228 0.41 ALA 134 -0.25 ASP 13

PRO 228 0.39 SER 135 -0.20 ASP 13

PRO 228 0.39 TRP 136 -0.15 ASP 13

PRO 228 0.39 GLY 137 -0.13 ASP 13

PRO 228 0.42 CYS 138 -0.15 ASP 13

PRO 228 0.43 GLU 139 -0.14 ARG 118

PRO 228 0.44 THR 140 -0.12 ARG 118

PRO 228 0.45 THR 141 -0.12 SER 150

PRO 228 0.47 GLY 142 -0.10 SER 151

PRO 228 0.46 ARG 143 -0.14 SER 149

PRO 228 0.42 VAL 144 -0.14 SER 85

PRO 228 0.41 TYR 145 -0.15 SER 85

PRO 228 0.39 TRP 146 -0.14 SER 85

PRO 228 0.41 LYS 147 -0.13 SER 85

PRO 228 0.41 PRO 148 -0.11 SER 85

PRO 228 0.41 SER 149 -0.14 ARG 143

PRO 228 0.37 SER 150 -0.12 THR 141

ARG 120 0.33 SER 151 -0.15 VAL 157

ALA 186 0.39 TRP 152 -0.19 ASP 153

PRO 228 0.42 ASP 153 -0.19 TRP 152

PRO 228 0.46 TYR 154 -0.10 SER 58

PRO 228 0.48 ILE 155 -0.11 SER 58

PRO 228 0.46 THR 156 -0.18 VAL 157

PRO 228 0.50 VAL 157 -0.18 THR 156

PRO 228 0.48 ASP 158 -0.15 ASN 185

PRO 228 0.49 ASN 159 -0.17 ASN 185

PRO 228 0.49 ASN 160 -0.21 ASN 185

PRO 228 0.47 LEU 161 -0.16 ASN 185

PRO 228 0.43 THR 162 -0.13 ASN 185

PRO 228 0.43 THR 163 -0.11 ASN 185

PRO 228 0.41 SER 164 -0.11 ASN 185

SER 68 0.45 GLN 165 -0.12 ASN 185

PRO 228 0.48 ALA 166 -0.10 ASN 185

PRO 228 0.46 VAL 167 -0.09 GLN 1

PRO 228 0.48 GLN 168 -0.08 GLN 1

PRO 228 0.52 VAL 169 -0.12 VAL 2

PRO 228 0.51 CYS 170 -0.14 ASN 23

PRO 228 0.49 LYS 171 -0.13 THR 92

PRO 228 0.51 ASP 172 -0.15 THR 92

PRO 228 0.52 ASN 173 -0.26 SER 69

PRO 228 0.57 LYS 174 -0.23 ASN 23

PRO 228 0.57 TRP 175 -0.26 ASN 23

PRO 228 0.54 CYS 176 -0.17 ASN 23

PRO 228 0.53 ASN 177 -0.14 ASN 23

PRO 228 0.55 PRO 178 -0.17 ASN 185

PRO 228 0.55 LEU 179 -0.16 ASN 185

PRO 228 0.51 ALA 180 -0.23 ASN 185

PRO 228 0.51 ILE 181 -0.18 SER 58

PRO 228 0.45 GLN 182 -0.24 ASN 185

PRO 228 0.41 PHE 183 -0.19 SER 58

SER 149 0.39 THR 184 -0.22 ASN 185

THR 28 0.37 ASN 185 -0.24 GLN 182

TRP 152 0.39 ALA 186 -0.16 THR 184

PRO 228 0.40 GLY 187 -0.19 THR 184

PRO 228 0.33 LYS 188 -0.19 VAL 32

PRO 119 0.38 GLN 189 -0.17 VAL 32

PRO 228 0.40 VAL 190 -0.12 THR 184

PRO 228 0.44 THR 191 -0.10 LYS 188

PRO 228 0.57 SER 192 -0.09 TRP 152

PRO 228 0.64 TRP 193 -0.06 SER 192

PRO 228 0.79 THR 194 -0.13 ARG 120

PRO 228 0.81 THR 195 -0.25 ARG 120

PRO 228 0.73 GLY 196 -0.18 ARG 120

PRO 228 0.63 HIS 197 -0.15 ARG 120

PRO 228 0.62 TYR 198 -0.19 ARG 120

PRO 228 0.56 TRP 199 -0.13 ARG 120

PRO 228 0.54 GLY 200 -0.14 ARG 120

PRO 228 0.52 LEU 201 -0.13 GLY 74

PRO 228 0.48 ARG 202 -0.17 GLY 74

PRO 228 0.46 LEU 203 -0.16 GLY 74

PRO 228 0.43 TYR 204 -0.18 SER 85

PRO 228 0.42 VAL 205 -0.23 SER 85

PRO 228 0.39 SER 206 -0.30 SER 85

PRO 228 0.39 GLY 207 -0.26 GLY 74

PRO 228 0.41 ARG 208 -0.29 GLY 74

PRO 228 0.44 ASP 209 -0.22 GLY 74

PRO 228 0.46 PRO 210 -0.25 GLY 74

PRO 228 0.51 GLY 211 -0.21 GLY 74

PRO 228 0.55 LEU 212 -0.20 SER 21

PRO 228 0.59 THR 213 -0.19 ALA 19

PRO 228 0.65 PHE 214 -0.23 ALA 19

PRO 228 0.70 GLY 215 -0.18 SER 21

PRO 228 0.69 ILE 216 -0.14 SER 21

PRO 228 0.76 ARG 217 -0.14 SER 21

PRO 228 0.73 LEU 218 -0.11 TYR 56

PRO 228 0.83 ARG 219 -0.17 ASN 4

VAL 227 0.72 TYR 220 -0.15 TYR 56

VAL 227 0.79 GLN 221 -0.10 TYR 3

TYR 220 0.41 ASN 222 -0.11 SER 57

SER 149 0.19 LEU 223 -0.30 SER 57

THR 191 0.17 GLY 224 -0.30 SER 58

THR 195 0.30 PRO 225 -0.51 GLN 1

THR 194 0.53 ARG 226 -0.28 GLN 1

GLN 221 0.79 VAL 227 -0.18 ARG 226

GLU 15 0.93 PRO 228 -0.14 GLN 1

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.

*** 1AOL ***

CA distance fluctuations for 240228060428927675

--- normal mode 14 ---

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

* 1AOL *