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

* AF-1A0L_recycle_9 *

CA distance fluctuations for 2402070223221789221

--- 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 225 0.56 GLN 1 -0.09 LYS 147

PRO 225 0.30 VAL 2 -0.12 THR 162

PRO 228 0.34 TYR 3 -0.16 VAL 227

PRO 228 0.52 ASN 4 -0.37 VAL 227

PRO 228 0.52 ILE 5 -0.28 VAL 227

PRO 228 0.58 THR 6 -0.35 VAL 227

PRO 228 0.57 TRP 7 -0.27 VAL 227

PRO 228 0.56 GLU 8 -0.32 VAL 227

PRO 228 0.55 VAL 9 -0.29 VAL 227

PRO 228 0.51 THR 10 -0.29 VAL 227

PRO 228 0.50 ASN 11 -0.28 VAL 227

PRO 228 0.44 GLY 12 -0.24 VAL 227

PRO 228 0.43 ASP 13 -0.27 VAL 227

PRO 228 0.44 ARG 14 -0.27 VAL 227

PRO 228 0.51 GLU 15 -0.34 VAL 227

PRO 228 0.57 THR 16 -0.37 VAL 227

PRO 228 0.63 VAL 17 -0.38 VAL 227

PRO 228 0.69 TRP 18 -0.38 VAL 227

PRO 228 0.70 ALA 19 -0.41 VAL 227

PRO 228 0.77 ILE 20 -0.39 VAL 227

PRO 228 0.77 SER 21 -0.42 VAL 227

PRO 228 0.80 GLY 22 -0.31 VAL 227

PRO 228 0.69 ASN 23 -0.22 VAL 227

PRO 228 0.54 HIS 24 -0.14 LYS 147

PRO 228 0.32 PRO 25 -0.12 LYS 147

PRO 228 0.25 LEU 26 -0.10 LYS 147

PRO 228 0.29 TRP 27 -0.12 LYS 147

PRO 228 0.42 THR 28 -0.15 LYS 147

PRO 228 0.48 TRP 29 -0.17 LYS 147

PRO 228 0.63 TRP 30 -0.19 GLN 182

PRO 228 0.67 PRO 31 -0.18 GLY 22

PRO 228 0.63 VAL 32 -0.23 ASP 158

PRO 228 0.63 LEU 33 -0.24 VAL 227

PRO 228 0.66 THR 34 -0.29 VAL 227

PRO 228 0.65 PRO 35 -0.31 VAL 227

PRO 228 0.64 ASP 36 -0.32 VAL 227

PRO 228 0.57 LEU 37 -0.27 VAL 227

PRO 228 0.60 CYS 38 -0.30 VAL 227

PRO 228 0.63 MET 39 -0.33 VAL 227

PRO 228 0.56 LEU 40 -0.28 VAL 227

PRO 228 0.55 ALA 41 -0.28 VAL 227

PRO 228 0.59 LEU 42 -0.31 VAL 227

PRO 228 0.55 SER 43 -0.30 VAL 227

PRO 228 0.50 GLY 44 -0.26 VAL 227

PRO 228 0.47 PRO 45 -0.29 ASP 129

PRO 228 0.49 PRO 46 -0.24 VAL 227

PRO 228 0.48 HIS 47 -0.23 VAL 227

PRO 228 0.52 TRP 48 -0.25 VAL 227

PRO 228 0.55 GLY 49 -0.27 VAL 227

PRO 228 0.59 LEU 50 -0.30 VAL 227

PRO 228 0.54 GLU 51 -0.28 VAL 227

PRO 228 0.58 TYR 52 -0.31 VAL 227

PRO 228 0.63 GLN 53 -0.35 VAL 227

PRO 228 0.65 ALA 54 -0.37 VAL 227

PRO 228 0.66 PRO 55 -0.39 VAL 227

PRO 228 0.76 TYR 56 -0.43 VAL 227

PRO 228 0.76 SER 57 -0.41 VAL 227

PRO 228 0.80 SER 58 -0.39 VAL 227

PRO 228 0.74 PRO 59 -0.35 VAL 227

PRO 228 0.71 PRO 60 -0.33 VAL 227

PRO 228 0.70 GLY 61 -0.31 VAL 227

PRO 228 0.71 PRO 62 -0.31 VAL 227

PRO 228 0.67 PRO 63 -0.29 VAL 227

PRO 228 0.62 CYS 64 -0.27 VAL 227

PRO 228 0.60 CYS 65 -0.26 VAL 227

PRO 228 0.64 SER 66 -0.26 VAL 227

PRO 228 0.62 GLY 67 -0.24 VAL 227

PRO 228 0.65 SER 68 -0.20 VAL 227

PRO 228 0.65 SER 69 -0.20 VAL 227

PRO 228 0.60 GLY 70 -0.20 VAL 227

PRO 228 0.63 SER 71 -0.19 VAL 227

PRO 228 0.65 SER 72 -0.20 VAL 227

PRO 228 0.62 ALA 73 -0.19 VAL 227

PRO 228 0.58 GLY 74 -0.22 VAL 227

PRO 228 0.59 CYS 75 -0.23 VAL 227

PRO 228 0.54 SER 76 -0.22 VAL 227

PRO 228 0.51 ARG 77 -0.22 VAL 227

PRO 228 0.54 ASP 78 -0.24 VAL 227

PRO 228 0.53 CYS 79 -0.24 VAL 227

PRO 228 0.49 ASP 80 -0.23 VAL 227

PRO 228 0.47 GLU 81 -0.21 VAL 227

PRO 228 0.45 PRO 82 -0.22 VAL 227

PRO 228 0.46 LEU 83 -0.22 VAL 227

PRO 228 0.43 THR 84 -0.20 VAL 227

PRO 228 0.42 SER 85 -0.18 VAL 227

PRO 228 0.44 LEU 86 -0.20 VAL 227

PRO 228 0.47 THR 87 -0.22 VAL 227

PRO 228 0.49 PRO 88 -0.23 VAL 227

PRO 228 0.54 ARG 89 -0.25 VAL 227

PRO 228 0.59 CYS 90 -0.28 VAL 227

PRO 228 0.62 ASN 91 -0.29 VAL 227

PRO 228 0.64 THR 92 -0.29 VAL 227

PRO 228 0.66 ALA 93 -0.30 VAL 227

PRO 228 0.60 TRP 94 -0.28 VAL 227

PRO 228 0.57 ASN 95 -0.27 VAL 227

PRO 228 0.60 ARG 96 -0.28 VAL 227

PRO 228 0.58 LEU 97 -0.28 VAL 227

PRO 228 0.52 LYS 98 -0.25 VAL 227

PRO 228 0.52 LEU 99 -0.25 VAL 227

PRO 228 0.53 ASP 100 -0.26 VAL 227

PRO 228 0.49 GLN 101 -0.24 VAL 227

PRO 228 0.46 VAL 102 -0.22 VAL 227

PRO 228 0.46 THR 103 -0.22 VAL 227

PRO 228 0.45 HIS 104 -0.22 VAL 227

PRO 228 0.42 LYS 105 -0.21 VAL 227

PRO 228 0.37 SER 106 -0.18 VAL 227

PRO 228 0.36 SER 107 -0.17 VAL 227

PRO 228 0.39 GLU 108 -0.18 VAL 227

PRO 228 0.41 GLY 109 -0.18 VAL 227

PRO 228 0.42 PHE 110 -0.18 VAL 227

PRO 228 0.38 TYR 111 -0.15 VAL 227

PRO 228 0.38 VAL 112 -0.14 VAL 227

PRO 228 0.34 CYS 113 -0.10 VAL 227

PRO 228 0.32 PRO 114 -0.09 GLY 44

PRO 228 0.30 GLY 115 -0.18 ARG 120

PRO 228 0.24 SER 116 -0.25 ARG 120

PRO 228 0.23 HIS 117 -0.15 ARG 120

PRO 228 0.22 ARG 118 -0.20 PRO 119

PRO 228 0.18 PRO 119 -0.20 ARG 118

PRO 228 0.14 ARG 120 -0.25 SER 116

GLY 137 0.23 GLU 121 -0.12 GLY 127

PRO 228 0.22 ALA 122 -0.11 PRO 45

PRO 228 0.21 LYS 123 -0.20 GLY 126

PRO 228 0.23 SER 124 -0.15 PRO 45

PRO 228 0.26 CYS 125 -0.14 PRO 45

PRO 228 0.27 GLY 126 -0.20 LYS 123

PRO 228 0.29 GLY 127 -0.23 ARG 120

PRO 228 0.33 PRO 128 -0.23 PRO 45

PRO 228 0.33 ASP 129 -0.29 PRO 45

PRO 228 0.33 SER 130 -0.21 PRO 45

PRO 228 0.36 PHE 131 -0.16 PRO 45

PRO 228 0.31 TYR 132 -0.16 ARG 120

PRO 228 0.31 CYS 133 -0.12 PRO 45

PRO 228 0.29 ALA 134 -0.16 LEU 86

PRO 228 0.27 SER 135 -0.18 ARG 208

PRO 228 0.27 TRP 136 -0.15 ARG 208

PRO 228 0.26 GLY 137 -0.11 ARG 208

PRO 228 0.28 CYS 138 -0.09 ARG 208

PRO 228 0.31 GLU 139 -0.09 THR 184

PRO 228 0.31 THR 140 -0.14 THR 184

PRO 228 0.36 THR 141 -0.15 THR 156

PRO 228 0.39 GLY 142 -0.16 VAL 32

PRO 228 0.39 ARG 143 -0.19 VAL 32

PRO 228 0.37 VAL 144 -0.15 VAL 32

PRO 228 0.33 TYR 145 -0.16 TRP 30

PRO 228 0.30 TRP 146 -0.15 TRP 30

PRO 228 0.31 LYS 147 -0.18 TRP 30

PRO 228 0.30 PRO 148 -0.16 THR 184

PRO 228 0.30 SER 149 -0.17 THR 184

PRO 228 0.27 SER 150 -0.12 ASN 185

PRO 228 0.26 SER 151 -0.11 GLY 137

PRO 228 0.24 TRP 152 -0.07 GLY 137

PRO 228 0.29 ASP 153 -0.07 THR 140

PRO 228 0.32 TYR 154 -0.08 SER 149

PRO 228 0.39 ILE 155 -0.11 PHE 183

PRO 228 0.41 THR 156 -0.15 LYS 147

PRO 228 0.45 VAL 157 -0.19 VAL 32

PRO 228 0.47 ASP 158 -0.23 VAL 32

PRO 228 0.52 ASN 159 -0.23 VAL 227

PRO 228 0.57 ASN 160 -0.27 VAL 227

PRO 228 0.58 LEU 161 -0.30 VAL 227

PRO 228 0.53 THR 162 -0.27 VAL 227

PRO 228 0.52 THR 163 -0.27 VAL 227

PRO 228 0.55 SER 164 -0.29 VAL 227

PRO 228 0.60 GLN 165 -0.32 VAL 227

PRO 228 0.61 ALA 166 -0.31 VAL 227

PRO 228 0.60 VAL 167 -0.30 VAL 227

PRO 228 0.66 GLN 168 -0.33 VAL 227

PRO 228 0.70 VAL 169 -0.35 VAL 227

PRO 228 0.67 CYS 170 -0.32 VAL 227

PRO 228 0.68 LYS 171 -0.32 VAL 227

PRO 228 0.75 ASP 172 -0.35 VAL 227

PRO 228 0.74 ASN 173 -0.34 VAL 227

PRO 228 0.77 LYS 174 -0.36 VAL 227

PRO 228 0.72 TRP 175 -0.35 VAL 227

PRO 228 0.66 CYS 176 -0.33 VAL 227

PRO 228 0.61 ASN 177 -0.30 VAL 227

PRO 228 0.63 PRO 178 -0.30 VAL 227

PRO 228 0.57 LEU 179 -0.25 VAL 227

PRO 228 0.56 ALA 180 -0.22 VAL 227

PRO 228 0.52 ILE 181 -0.18 VAL 227

PRO 228 0.48 GLN 182 -0.19 TRP 30

PRO 228 0.42 PHE 183 -0.16 LYS 147

PRO 228 0.35 THR 184 -0.17 SER 149

PRO 228 0.29 ASN 185 -0.16 SER 149

PRO 228 0.25 ALA 186 -0.10 SER 149

PRO 228 0.30 GLY 187 -0.09 SER 149

PRO 228 0.29 LYS 188 -0.11 LYS 147

PRO 228 0.19 GLN 189 -0.08 LYS 147

PRO 228 0.20 VAL 190 -0.05 LYS 147

PRO 225 0.19 THR 191 -0.05 LYS 147

PRO 228 0.18 SER 192 -0.05 GLU 15

PRO 228 0.28 TRP 193 -0.09 VAL 227

PRO 228 0.26 THR 194 -0.15 VAL 227

PRO 228 0.24 THR 195 -0.14 VAL 227

PRO 228 0.32 GLY 196 -0.15 VAL 227

PRO 228 0.33 HIS 197 -0.12 ARG 120

PRO 228 0.36 TYR 198 -0.14 VAL 227

PRO 228 0.38 TRP 199 -0.14 VAL 227

PRO 228 0.38 GLY 200 -0.15 VAL 227

PRO 228 0.42 LEU 201 -0.18 VAL 227

PRO 228 0.40 ARG 202 -0.17 VAL 227

PRO 228 0.42 LEU 203 -0.18 VAL 227

PRO 228 0.38 TYR 204 -0.17 VAL 227

PRO 228 0.39 VAL 205 -0.17 VAL 227

PRO 228 0.37 SER 206 -0.16 VAL 227

PRO 228 0.36 GLY 207 -0.15 VAL 227

PRO 228 0.36 ARG 208 -0.18 SER 135

PRO 228 0.38 ASP 209 -0.16 VAL 227

PRO 228 0.42 PRO 210 -0.18 VAL 227

PRO 228 0.42 GLY 211 -0.19 VAL 227

PRO 228 0.44 LEU 212 -0.20 VAL 227

PRO 228 0.42 THR 213 -0.19 VAL 227

PRO 228 0.45 PHE 214 -0.21 VAL 227

PRO 228 0.43 GLY 215 -0.21 VAL 227

PRO 228 0.44 ILE 216 -0.20 VAL 227

PRO 228 0.40 ARG 217 -0.21 VAL 227

PRO 228 0.40 LEU 218 -0.20 VAL 227

PRO 228 0.39 ARG 219 -0.31 VAL 227

PRO 228 0.34 TYR 220 -0.30 VAL 227

PRO 228 0.27 GLN 221 -0.42 VAL 227

PRO 228 0.12 ASN 222 -0.31 VAL 227

PRO 228 0.22 LEU 223 -0.44 VAL 227

ALA 73 0.09 GLY 224 -0.27 VAL 227

GLN 1 0.56 PRO 225 -0.21 GLY 224

GLN 1 0.35 ARG 226 -0.16 GLN 165

GLN 1 0.31 VAL 227 -0.44 LEU 223

GLY 22 0.80 PRO 228 -0.19 PRO 225

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 2402070223221789221

--- normal mode 11 ---

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

* AF-1A0L_recycle_9 *