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

* bacteriorhodopsin *

CA distance fluctuations for 2404222055381936730

--- 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
LEU 109 0.10 ILE 4 -0.11 VAL 173

LEU 109 0.08 THR 5 -0.14 VAL 173

LEU 109 0.08 GLY 6 -0.13 VAL 173

LEU 109 0.08 ARG 7 -0.14 VAL 173

GLY 113 0.06 PRO 8 -0.17 VAL 173

GLY 113 0.06 GLU 9 -0.18 VAL 173

ILE 52 0.07 TRP 10 -0.16 VAL 173

THR 55 0.06 ILE 11 -0.19 VAL 173

ALA 51 0.06 TRP 12 -0.20 VAL 173

TYR 57 0.09 LEU 13 -0.16 GLY 218

ALA 51 0.09 ALA 14 -0.16 GLY 218

ALA 51 0.07 LEU 15 -0.22 GLY 218

LEU 206 0.08 GLY 16 -0.20 GLY 218

ALA 51 0.10 THR 17 -0.14 GLY 218

GLY 21 0.10 ALA 18 -0.13 LEU 221

VAL 210 0.08 LEU 19 -0.19 LEU 221

VAL 210 0.07 MET 20 -0.12 LEU 221

ALA 18 0.10 GLY 21 -0.14 LEU 22

VAL 210 0.09 LEU 22 -0.14 GLY 21

VAL 213 0.08 GLY 23 -0.09 ARG 225

LYS 40 0.07 THR 24 -0.08 ILE 52

ALA 18 0.07 LEU 25 -0.07 ILE 52

VAL 180 0.07 TYR 26 -0.06 ILE 52

VAL 180 0.06 PHE 27 -0.06 GLU 234

VAL 34 0.09 LEU 28 -0.09 LEU 48

VAL 180 0.05 VAL 29 -0.11 GLU 234

ILE 222 0.06 LYS 30 -0.09 GLU 234

LEU 28 0.09 GLY 31 -0.13 GLU 234

VAL 34 0.05 MET 32 -0.18 GLU 234

ARG 227 0.07 GLY 33 -0.20 GLU 234

THR 55 0.10 VAL 34 -0.29 GLU 234

THR 55 0.13 SER 35 -0.46 GLU 234

THR 55 0.12 ASP 36 -0.43 GLU 234

THR 55 0.15 PRO 37 -0.36 GLU 234

THR 55 0.13 ASP 38 -0.21 GLU 234

THR 55 0.11 ALA 39 -0.15 GLU 234

THR 55 0.16 LYS 40 -0.22 GLU 234

THR 55 0.17 LYS 41 -0.15 GLU 234

THR 55 0.12 PHE 42 -0.07 LEU 109

THR 55 0.12 TYR 43 -0.09 GLU 234

THR 55 0.17 ALA 44 -0.14 MET 32

THR 55 0.16 ILE 45 -0.10 MET 32

THR 55 0.09 THR 46 -0.06 GLY 116

ALA 51 0.11 THR 47 -0.08 GLY 116

THR 55 0.17 LEU 48 -0.09 LEU 28

THR 55 0.10 VAL 49 -0.08 GLY 116

ALA 44 0.09 PRO 50 -0.06 GLY 116

ALA 44 0.15 ALA 51 -0.12 ILE 52

LYS 41 0.16 ILE 52 -0.12 ALA 51

LYS 41 0.11 ALA 53 -0.06 GLY 120

LEU 48 0.14 PHE 54 -0.07 LEU 22

ALA 44 0.17 THR 55 -0.08 VAL 124

LYS 41 0.14 MET 56 -0.07 THR 55

ALA 44 0.11 TYR 57 -0.10 GLY 218

ALA 44 0.13 LEU 58 -0.09 GLY 218

LYS 41 0.15 SER 59 -0.07 GLY 218

LEU 109 0.13 MET 60 -0.09 GLY 218

ALA 44 0.11 LEU 61 -0.11 GLY 218

LYS 41 0.13 LEU 62 -0.09 GLY 218

LEU 109 0.14 GLY 63 -0.08 GLY 218

LEU 109 0.18 TYR 64 -0.06 GLY 218

LEU 109 0.18 GLY 65 -0.06 GLY 218

LEU 109 0.16 LEU 66 -0.08 VAL 177

LEU 109 0.18 THR 67 -0.07 VAL 177

LEU 109 0.17 MET 68 -0.07 VAL 177

LEU 109 0.17 VAL 69 -0.07 VAL 177

LEU 109 0.16 PRO 70 -0.07 VAL 180

LEU 109 0.13 PHE 71 -0.08 VAL 180

LEU 109 0.09 GLY 72 -0.15 ALA 196

LEU 109 0.11 GLY 73 -0.14 GLY 197

LEU 109 0.11 GLU 74 -0.16 GLY 197

LEU 109 0.13 GLN 75 -0.12 GLY 197

LEU 109 0.12 ASN 76 -0.11 VAL 180

LEU 109 0.13 PRO 77 -0.11 VAL 177

LEU 109 0.14 ILE 78 -0.10 VAL 177

LEU 109 0.14 TYR 79 -0.09 VAL 177

LEU 109 0.18 TRP 80 -0.06 TYR 185

LEU 109 0.18 ALA 81 -0.07 THR 55

LEU 109 0.13 ARG 82 -0.07 VAL 177

LEU 109 0.18 TYR 83 -0.07 THR 55

LEU 109 0.20 ALA 84 -0.08 GLY 120

GLN 105 0.14 ASP 85 -0.07 GLY 120

LEU 109 0.12 TRP 86 -0.05 ALA 51

VAL 112 0.21 LEU 87 -0.08 GLY 120

LEU 95 0.17 PHE 88 -0.10 GLY 116

LEU 95 0.11 THR 89 -0.08 GLY 116

ALA 84 0.09 THR 90 -0.07 GLY 116

LEU 95 0.14 PRO 91 -0.08 GLY 116

PHE 88 0.15 LEU 92 -0.08 GLY 116

ALA 84 0.08 LEU 93 -0.06 LEU 211

PRO 91 0.13 LEU 94 -0.08 LEU 211

PHE 88 0.17 LEU 95 -0.08 MET 32

PHE 88 0.13 ASP 96 -0.08 LEU 211

PHE 88 0.11 LEU 97 -0.11 LEU 211

PHE 88 0.15 ALA 98 -0.09 LEU 211

PHE 88 0.14 LEU 99 -0.08 SER 214

PHE 88 0.12 LEU 100 -0.11 VAL 210

PHE 88 0.12 VAL 101 -0.11 LEU 207

PHE 88 0.14 ASP 102 -0.09 ASP 38

PHE 88 0.15 ALA 103 -0.08 ASP 38

ALA 84 0.15 ASP 104 -0.09 GLY 155

ALA 84 0.19 GLN 105 -0.10 PRO 37

GLY 120 0.18 GLY 106 -0.09 PRO 37

GLY 120 0.17 THR 107 -0.07 PRO 37

LEU 87 0.18 ILE 108 -0.08 MET 32

GLY 120 0.23 LEU 109 -0.09 MET 32

GLY 120 0.20 ALA 110 -0.08 MET 32

GLY 120 0.18 LEU 111 -0.07 MET 32

LEU 87 0.21 VAL 112 -0.08 MET 32

GLY 120 0.26 GLY 113 -0.08 MET 32

GLY 120 0.19 ALA 114 -0.07 GLY 113

GLY 120 0.15 ASP 115 -0.06 MET 32

GLY 113 0.25 GLY 116 -0.10 PHE 88

GLY 120 0.20 ILE 117 -0.08 PHE 88

LEU 111 0.10 MET 118 -0.06 PHE 88

GLY 113 0.16 ILE 119 -0.06 PHE 88

GLY 113 0.26 GLY 120 -0.08 LEU 87

GLY 113 0.18 THR 121 -0.07 ALA 84

GLY 113 0.14 GLY 122 -0.05 ALA 84

GLY 113 0.21 LEU 123 -0.07 VAL 124

GLY 113 0.22 VAL 124 -0.08 THR 55

GLY 113 0.16 GLY 125 -0.05 THR 55

GLY 113 0.16 ALA 126 -0.06 TYR 185

GLY 113 0.19 LEU 127 -0.06 THR 128

GLY 113 0.18 THR 128 -0.06 LEU 127

LEU 109 0.16 LYS 129 -0.05 ALA 184

LEU 109 0.13 VAL 130 -0.04 VAL 177

LEU 109 0.10 TYR 131 -0.06 VAL 180

LEU 109 0.07 SER 132 -0.05 VAL 173

LEU 109 0.10 TYR 133 -0.04 THR 55

LEU 109 0.11 ARG 134 -0.04 VAL 177

LEU 109 0.06 PHE 135 -0.05 LEU 146

LEU 109 0.07 VAL 136 -0.04 ALA 84

LEU 109 0.11 TRP 137 -0.05 ALA 84

LEU 109 0.06 TRP 138 -0.04 ALA 84

GLU 234 0.04 ALA 139 -0.04 PHE 135

TYR 147 0.10 ILE 140 -0.05 PHE 88

TYR 147 0.08 SER 141 -0.05 PHE 88

SER 183 0.06 THR 142 -0.05 GLY 72

ILE 140 0.08 ALA 143 -0.07 ALA 144

TYR 147 0.12 ALA 144 -0.07 ALA 143

VAL 180 0.08 MET 145 -0.06 VAL 187

ASN 176 0.07 LEU 146 -0.13 VAL 187

ALA 144 0.12 TYR 147 -0.08 VAL 187

GLY 120 0.10 ILE 148 -0.09 VAL 187

ASN 176 0.09 LEU 149 -0.15 VAL 187

GLU 234 0.09 TYR 150 -0.15 VAL 187

GLY 120 0.11 VAL 151 -0.11 VAL 187

GLU 234 0.10 LEU 152 -0.13 VAL 187

GLU 234 0.13 PHE 153 -0.16 VAL 187

GLU 234 0.12 PHE 154 -0.15 VAL 187

GLY 120 0.12 GLY 155 -0.11 LEU 207

GLU 234 0.12 PHE 156 -0.13 LEU 207

GLU 234 0.17 THR 157 -0.17 LEU 207

GLU 234 0.17 SER 158 -0.15 LEU 207

GLU 234 0.14 LYS 159 -0.13 LEU 207

GLU 234 0.20 ALA 160 -0.15 LEU 207

GLU 234 0.26 GLU 161 -0.17 LEU 207

GLU 234 0.22 SER 162 -0.14 LEU 207

GLU 234 0.24 MET 163 -0.14 LEU 207

GLU 234 0.36 ARG 164 -0.14 VAL 210

GLU 234 0.45 PRO 165 -0.18 VAL 210

GLU 234 0.44 GLU 166 -0.19 VAL 210

GLU 234 0.27 VAL 167 -0.16 VAL 210

GLU 234 0.29 ALA 168 -0.18 LEU 207

GLU 234 0.32 SER 169 -0.22 VAL 210

GLU 234 0.25 THR 170 -0.21 VAL 210

GLU 234 0.19 PHE 171 -0.19 VAL 210

GLU 234 0.21 LYS 172 -0.22 LEU 207

GLU 234 0.20 VAL 173 -0.26 VAL 210

GLU 234 0.14 LEU 174 -0.23 VAL 210

GLU 234 0.13 ARG 175 -0.21 LEU 207

GLU 234 0.14 ASN 176 -0.25 LEU 207

GLU 234 0.11 VAL 177 -0.28 LEU 207

GLU 234 0.08 THR 178 -0.21 LEU 207

GLU 234 0.09 VAL 179 -0.21 ALA 184

GLY 218 0.10 VAL 180 -0.25 LEU 207

GLY 218 0.08 LEU 181 -0.26 LEU 207

LEU 181 0.07 TRP 182 -0.14 LEU 207

GLY 218 0.06 SER 183 -0.19 VAL 187

SER 214 0.06 ALA 184 -0.21 VAL 179

GLY 23 0.04 TYR 185 -0.14 VAL 179

VAL 210 0.04 PRO 186 -0.11 VAL 179

VAL 210 0.06 VAL 187 -0.19 SER 183

LEU 19 0.05 VAL 188 -0.20 VAL 180

GLY 113 0.05 TRP 189 -0.13 VAL 179

LEU 19 0.04 LEU 190 -0.13 VAL 179

LEU 19 0.05 ILE 191 -0.18 VAL 180

GLY 113 0.05 GLY 192 -0.18 VAL 180

GLY 113 0.08 SER 193 -0.14 VAL 180

GLY 113 0.09 GLU 194 -0.11 VAL 180

GLY 113 0.06 GLY 195 -0.12 VAL 180

PHE 135 0.05 ALA 196 -0.15 GLY 72

GLY 113 0.05 GLY 197 -0.16 GLU 74

SER 132 0.05 ILE 198 -0.18 VAL 180

LEU 19 0.05 VAL 199 -0.21 VAL 180

GLY 113 0.05 PRO 200 -0.18 VAL 180

GLY 113 0.07 LEU 201 -0.17 VAL 177

GLY 113 0.06 ASN 202 -0.19 VAL 173

LEU 15 0.05 ILE 203 -0.23 VAL 177

ILE 191 0.05 GLU 204 -0.21 VAL 177

ALA 53 0.06 THR 205 -0.20 VAL 177

GLY 16 0.08 LEU 206 -0.24 VAL 177

LEU 19 0.08 LEU 207 -0.28 VAL 177

LEU 19 0.05 PHE 208 -0.21 VAL 177

LEU 19 0.07 MET 209 -0.22 VAL 177

LEU 22 0.09 VAL 210 -0.27 VAL 177

LEU 22 0.07 LEU 211 -0.27 VAL 177

VAL 187 0.05 ASP 212 -0.15 VAL 177

GLY 23 0.08 VAL 213 -0.22 GLY 218

GLY 23 0.08 SER 214 -0.22 VAL 173

TRP 182 0.06 ALA 215 -0.16 LEU 174

VAL 180 0.06 LYS 216 -0.09 LEU 15

VAL 180 0.07 VAL 217 -0.14 GLY 220

VAL 180 0.10 GLY 218 -0.22 VAL 213

THR 178 0.08 PHE 219 -0.19 SER 214

THR 178 0.06 GLY 220 -0.14 VAL 217

VAL 177 0.09 LEU 221 -0.19 LEU 19

GLU 234 0.11 ILE 222 -0.20 VAL 210

GLU 234 0.09 LEU 223 -0.15 VAL 210

LEU 223 0.06 LEU 224 -0.12 LEU 19

GLU 234 0.11 ARG 225 -0.16 LEU 15

GLU 234 0.21 SER 226 -0.17 VAL 210

GLU 234 0.27 ARG 227 -0.14 VAL 210

GLU 234 0.23 ALA 228 -0.14 VAL 210

PHE 88 0.08 ILE 229 -0.10 VAL 210

PHE 88 0.07 PHE 230 -0.09 VAL 210

GLU 232 0.11 GLY 231 -0.09 VAL 210

GLU 234 0.12 GLU 232 -0.10 VAL 210

PRO 165 0.12 ALA 233 -0.15 ASP 36

PRO 165 0.45 GLU 234 -0.46 SER 35

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.

*** bacteriorhodopsin ***

CA distance fluctuations for 2404222055381936730

--- normal mode 11 ---

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

* bacteriorhodopsin *