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

* AF-1A0L_recycle_9 *

CA distance fluctuations for 2402070231571793153

--- normal mode 15 ---

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
ALA 73 0.30 GLN 1 -0.28 ARG 120

ALA 73 0.32 VAL 2 -0.31 ARG 120

ALA 73 0.34 TYR 3 -0.32 ARG 120

ALA 73 0.36 ASN 4 -0.32 ARG 120

ALA 73 0.37 ILE 5 -0.33 ARG 120

ALA 73 0.40 THR 6 -0.31 ARG 120

ALA 73 0.38 TRP 7 -0.29 ARG 120

ALA 73 0.40 GLU 8 -0.27 ARG 120

ALA 73 0.38 VAL 9 -0.21 VAL 227

ALA 73 0.40 THR 10 -0.19 ARG 120

ALA 73 0.40 ASN 11 -0.18 VAL 227

ALA 73 0.35 GLY 12 -0.14 LEU 212

ALA 73 0.40 ASP 13 -0.14 ARG 120

ALA 73 0.39 ARG 14 -0.20 ARG 120

ALA 73 0.46 GLU 15 -0.17 VAL 227

ALA 73 0.47 THR 16 -0.22 VAL 227

ALA 73 0.50 VAL 17 -0.25 VAL 227

ALA 73 0.47 TRP 18 -0.30 VAL 227

ALA 73 0.45 ALA 19 -0.32 VAL 227

ALA 73 0.43 ILE 20 -0.41 VAL 227

ALA 73 0.41 SER 21 -0.43 VAL 227

ALA 73 0.39 GLY 22 -0.50 VAL 227

ALA 73 0.35 ASN 23 -0.45 VAL 227

ALA 73 0.33 HIS 24 -0.47 PRO 228

ALA 73 0.32 PRO 25 -0.42 PRO 228

ALA 73 0.31 LEU 26 -0.36 ARG 120

ALA 73 0.29 TRP 27 -0.38 ARG 120

ALA 73 0.30 THR 28 -0.47 PRO 228

ALA 73 0.29 TRP 29 -0.47 PRO 228

PRO 31 0.42 TRP 30 -0.51 PRO 228

TRP 30 0.42 PRO 31 -0.45 PRO 228

ASN 160 0.29 VAL 32 -0.40 PRO 228

ALA 73 0.31 LEU 33 -0.31 PRO 228

ALA 73 0.33 THR 34 -0.30 VAL 227

ALA 73 0.36 PRO 35 -0.27 VAL 227

ALA 73 0.36 ASP 36 -0.26 VAL 227

ALA 73 0.30 LEU 37 -0.22 VAL 227

ALA 73 0.39 CYS 38 -0.22 VAL 227

ALA 73 0.47 MET 39 -0.24 VAL 227

ALA 73 0.39 LEU 40 -0.21 VAL 227

ALA 73 0.41 ALA 41 -0.19 VAL 227

ALA 73 0.54 LEU 42 -0.21 VAL 227

ALA 73 0.55 SER 43 -0.19 VAL 227

ALA 73 0.43 GLY 44 -0.17 VAL 227

ALA 73 0.36 PRO 45 -0.16 VAL 227

GLY 74 0.43 PRO 46 -0.17 VAL 227

GLY 67 0.32 HIS 47 -0.16 VAL 227

GLY 74 0.39 TRP 48 -0.18 VAL 227

GLY 74 0.59 GLY 49 -0.18 VAL 227

ALA 73 0.61 LEU 50 -0.20 VAL 227

ALA 73 0.59 GLU 51 -0.19 VAL 227

ALA 73 0.76 TYR 52 -0.21 VAL 227

ALA 73 0.77 GLN 53 -0.23 VAL 227

ALA 73 0.70 ALA 54 -0.24 VAL 227

ALA 73 0.61 PRO 55 -0.25 VAL 227

ALA 73 0.63 TYR 56 -0.30 VAL 227

ALA 73 0.72 SER 57 -0.34 SER 68

ALA 73 0.70 SER 58 -0.42 SER 68

ALA 73 0.62 PRO 59 -0.35 SER 68

ALA 73 0.79 PRO 60 -0.33 SER 68

SER 72 0.91 GLY 61 -0.36 SER 68

SER 72 0.65 PRO 62 -0.48 SER 68

SER 72 0.39 PRO 63 -0.23 SER 66

SER 72 0.26 CYS 64 -0.17 VAL 227

CYS 79 0.37 CYS 65 -0.39 GLY 70

ASP 80 0.23 SER 66 -0.51 LYS 171

ASP 80 1.13 GLY 67 -0.56 ASP 172

ASP 80 0.89 SER 68 -0.55 ASP 172

ASP 80 0.37 SER 69 -0.24 PRO 62

SER 76 0.69 GLY 70 -0.39 CYS 65

GLY 61 0.52 SER 71 -0.20 ASP 80

GLY 61 0.91 SER 72 -0.22 SER 76

PRO 60 0.79 ALA 73 -0.35 SER 76

TYR 52 0.64 GLY 74 -0.31 ARG 77

PRO 60 0.42 CYS 75 -0.12 ARG 77

GLY 70 0.69 SER 76 -0.35 ALA 73

GLY 67 0.67 ARG 77 -0.31 ALA 73

GLY 67 0.57 ASP 78 -0.15 VAL 227

GLY 67 0.80 CYS 79 -0.22 LYS 105

GLY 67 1.13 ASP 80 -0.31 LYS 105

GLY 67 0.95 GLU 81 -0.28 ALA 73

GLY 67 0.88 PRO 82 -0.25 SER 107

GLY 67 0.64 LEU 83 -0.16 VAL 227

GLY 67 0.61 THR 84 -0.15 VAL 227

GLY 67 0.51 SER 85 -0.14 VAL 227

GLY 67 0.49 LEU 86 -0.15 VAL 227

GLY 67 0.48 THR 87 -0.16 VAL 227

GLY 67 0.41 PRO 88 -0.17 VAL 227

GLY 67 0.31 ARG 89 -0.17 VAL 227

GLY 74 0.39 CYS 90 -0.19 VAL 227

GLY 74 0.56 ASN 91 -0.17 VAL 227

SER 72 0.50 THR 92 -0.18 VAL 227

SER 72 0.41 ALA 93 -0.21 SER 66

GLY 67 0.25 TRP 94 -0.19 VAL 227

GLY 67 0.32 ASN 95 -0.18 VAL 227

SER 72 0.28 ARG 96 -0.20 VAL 227

GLY 67 0.25 LEU 97 -0.20 VAL 227

GLY 67 0.48 LYS 98 -0.19 VAL 227

GLY 67 0.35 LEU 99 -0.19 VAL 227

GLY 67 0.26 ASP 100 -0.20 VAL 227

GLY 67 0.40 GLN 101 -0.26 ASP 80

GLY 67 0.44 VAL 102 -0.24 ASP 80

GLY 67 0.30 THR 103 -0.18 PRO 228

GLY 67 0.28 HIS 104 -0.22 ASP 80

GLY 67 0.38 LYS 105 -0.31 ASP 80

GLY 67 0.35 SER 106 -0.29 ASP 80

GLY 67 0.44 SER 107 -0.29 ASP 80

GLY 67 0.43 GLU 108 -0.25 ASP 80

GLY 67 0.34 GLY 109 -0.19 ASP 80

GLY 67 0.28 PHE 110 -0.19 PRO 228

GLY 67 0.25 TYR 111 -0.20 PRO 228

GLY 67 0.20 VAL 112 -0.21 PRO 228

ALA 122 0.20 CYS 113 -0.20 PRO 228

ALA 73 0.18 PRO 114 -0.21 PRO 228

ALA 73 0.21 GLY 115 -0.32 ARG 120

ALA 73 0.21 SER 116 -0.59 ARG 120

ALA 73 0.18 HIS 117 -0.52 ARG 120

ALA 73 0.15 ARG 118 -0.49 PRO 119

GLY 67 0.13 PRO 119 -0.49 ARG 118

GLY 137 0.26 ARG 120 -0.64 SER 192

GLY 137 0.48 GLU 121 -0.39 SER 192

CYS 138 0.34 ALA 122 -0.26 SER 192

GLY 67 0.21 LYS 123 -0.36 SER 192

GLY 67 0.27 SER 124 -0.27 SER 192

GLY 67 0.25 CYS 125 -0.21 SER 192

GLY 67 0.24 GLY 126 -0.23 SER 192

GLY 67 0.21 GLY 127 -0.25 THR 195

ALA 73 0.25 PRO 128 -0.23 THR 195

GLY 67 0.26 ASP 129 -0.20 THR 195

GLY 67 0.28 SER 130 -0.17 THR 195

GLY 67 0.24 PHE 131 -0.16 PRO 228

GLY 67 0.22 TYR 132 -0.17 PRO 228

GLY 67 0.27 CYS 133 -0.17 PRO 228

GLY 67 0.31 ALA 134 -0.17 SER 192

GLY 67 0.32 SER 135 -0.17 PRO 228

GLU 121 0.38 TRP 136 -0.18 PRO 228

GLU 121 0.48 GLY 137 -0.20 PRO 228

GLU 121 0.36 CYS 138 -0.20 PRO 228

GLU 121 0.29 GLU 139 -0.21 PRO 228

GLU 121 0.25 THR 140 -0.23 PRO 228

GLU 121 0.19 THR 141 -0.24 PRO 228

GLY 67 0.19 GLY 142 -0.22 PRO 228

GLY 67 0.23 ARG 143 -0.21 PRO 228

GLY 67 0.29 VAL 144 -0.19 PRO 228

GLY 67 0.30 TYR 145 -0.22 ASP 80

GLY 67 0.28 TRP 146 -0.19 PRO 228

GLU 121 0.25 LYS 147 -0.21 PRO 228

GLU 121 0.29 PRO 148 -0.22 PRO 228

GLU 121 0.27 SER 149 -0.24 PRO 228

GLU 121 0.24 SER 150 -0.25 PRO 228

PRO 225 0.13 SER 151 -0.26 PRO 228

SER 72 0.13 TRP 152 -0.26 PRO 228

ALA 73 0.15 ASP 153 -0.25 PRO 228

ALA 73 0.19 TYR 154 -0.27 PRO 228

ALA 73 0.19 ILE 155 -0.28 PRO 228

SER 72 0.17 THR 156 -0.29 PRO 228

SER 72 0.18 VAL 157 -0.26 PRO 228

TRP 30 0.21 ASP 158 -0.25 PRO 228

TRP 30 0.24 ASN 159 -0.23 PRO 228

TRP 30 0.31 ASN 160 -0.25 PRO 228

TRP 30 0.31 LEU 161 -0.23 VAL 227

TRP 30 0.27 THR 162 -0.21 VAL 227

TRP 30 0.23 THR 163 -0.24 GLY 70

TRP 30 0.24 SER 164 -0.31 GLY 70

GLY 22 0.28 GLN 165 -0.25 GLY 70

TRP 30 0.25 ALA 166 -0.22 VAL 227

GLY 22 0.23 VAL 167 -0.30 GLY 70

GLY 22 0.27 GLN 168 -0.35 SER 66

SER 72 0.29 VAL 169 -0.32 SER 68

SER 72 0.31 CYS 170 -0.31 SER 66

SER 72 0.29 LYS 171 -0.51 SER 66

SER 72 0.37 ASP 172 -0.56 GLY 67

SER 72 0.49 ASN 173 -0.47 SER 68

SER 72 0.44 LYS 174 -0.42 SER 68

SER 72 0.42 TRP 175 -0.26 SER 68

SER 72 0.31 CYS 176 -0.23 VAL 227

SER 72 0.28 ASN 177 -0.23 VAL 227

SER 72 0.28 PRO 178 -0.25 VAL 227

SER 72 0.26 LEU 179 -0.25 PRO 228

VAL 32 0.27 ALA 180 -0.29 PRO 228

ALA 73 0.24 ILE 181 -0.30 PRO 228

SER 72 0.21 GLN 182 -0.34 PRO 228

ALA 73 0.22 PHE 183 -0.35 PRO 228

ALA 73 0.18 THR 184 -0.34 PRO 228

ALA 73 0.18 ASN 185 -0.36 PRO 228

ALA 73 0.17 ALA 186 -0.29 PRO 228

ALA 73 0.21 GLY 187 -0.34 ARG 120

ALA 73 0.23 LYS 188 -0.33 ARG 120

PRO 225 0.23 GLN 189 -0.43 ARG 120

ALA 73 0.23 VAL 190 -0.55 ARG 120

PRO 225 0.28 THR 191 -0.60 ARG 120

ALA 73 0.26 SER 192 -0.64 ARG 120

ALA 73 0.29 TRP 193 -0.50 ARG 120

ALA 73 0.32 THR 194 -0.49 ARG 120

ALA 73 0.31 THR 195 -0.53 ARG 120

ALA 73 0.31 GLY 196 -0.45 ARG 120

ALA 73 0.26 HIS 197 -0.40 ARG 120

ALA 73 0.25 TYR 198 -0.28 ARG 120

ALA 73 0.23 TRP 199 -0.19 PRO 228

ALA 73 0.20 GLY 200 -0.18 PRO 228

GLY 67 0.21 LEU 201 -0.18 PRO 228

GLY 67 0.29 ARG 202 -0.17 PRO 228

GLY 67 0.36 LEU 203 -0.16 PRO 228

GLY 67 0.41 TYR 204 -0.18 PRO 82

GLY 67 0.52 VAL 205 -0.21 PRO 82

GLY 67 0.61 SER 206 -0.18 ALA 73

GLY 67 0.55 GLY 207 -0.15 ALA 73

GLY 67 0.47 ARG 208 -0.14 PRO 228

GLY 67 0.42 ASP 209 -0.15 PRO 228

GLY 67 0.38 PRO 210 -0.15 VAL 227

GLY 67 0.29 GLY 211 -0.15 PRO 228

ALA 73 0.25 LEU 212 -0.16 VAL 227

ALA 73 0.28 THR 213 -0.16 PRO 228

ALA 73 0.31 PHE 214 -0.17 PRO 228

ALA 73 0.31 GLY 215 -0.24 ARG 120

ALA 73 0.32 ILE 216 -0.29 ARG 120

ALA 73 0.33 ARG 217 -0.37 ARG 120

ALA 73 0.35 LEU 218 -0.38 ARG 120

ALA 73 0.37 ARG 219 -0.38 ARG 120

ALA 73 0.36 TYR 220 -0.36 ARG 120

ALA 73 0.36 GLN 221 -0.32 ARG 120

ALA 73 0.33 ASN 222 -0.26 ARG 120

ALA 73 0.31 LEU 223 -0.25 ARG 120

ARG 226 0.40 GLY 224 -0.19 SER 68

GLN 1 0.29 PRO 225 -0.27 SER 68

GLY 224 0.40 ARG 226 -0.40 GLY 22

GLY 224 0.27 VAL 227 -0.50 GLY 22

ALA 73 0.21 PRO 228 -0.51 TRP 30

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-1A0L_recycle_9 ***

CA distance fluctuations for 2402070231571793153

--- normal mode 15 ---

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

* AF-1A0L_recycle_9 *