Should you encounter any unexpected behaviour,
please let us know.
elNémo has been relocated.
Some cleaning from time to time
Sorry for the inconvenience.

* open_8 *

CA distance fluctuations for 260611224051872834

--- 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
ASP 202 0.34 ALA 1 -0.48 GLN 42

ASN 234 0.31 LEU 2 -0.36 ASP 65

ASN 234 0.36 PRO 3 -0.16 LYS 23

ASN 234 0.35 GLN 4 -0.19 LYS 23

ASN 234 0.34 THR 5 -0.20 LYS 23

ASN 234 0.33 VAL 6 -0.32 LEU 2

ASN 234 0.25 ARG 7 -0.27 LEU 2

ASN 234 0.23 ILE 8 -0.22 LEU 2

LEU 87 0.16 GLY 9 -0.19 LEU 2

TYR 88 0.18 THR 10 -0.14 LEU 2

TYR 88 0.17 ASP 11 -0.21 PHE 233

TYR 88 0.18 THR 12 -0.20 PHE 233

TYR 88 0.20 THR 13 -0.30 PHE 233

TYR 88 0.22 TYR 14 -0.37 PHE 233

TYR 88 0.21 ALA 15 -0.35 PHE 233

TYR 88 0.21 PRO 16 -0.29 PHE 233

TYR 88 0.28 PHE 17 -0.20 PHE 231

TYR 88 0.22 SER 18 -0.16 PHE 233

TYR 88 0.18 SER 19 -0.18 PHE 233

ASP 144 0.22 LYS 20 -0.15 ASN 35

ALA 174 0.24 ASP 21 -0.17 ASN 35

SER 148 0.43 ALA 22 -0.22 ASN 35

SER 148 0.36 LYS 23 -0.32 LYS 39

ASP 144 0.32 GLY 24 -0.25 ASN 35

SER 148 0.20 GLU 25 -0.36 ASN 35

LYS 229 0.15 PHE 26 -0.26 ASN 35

LYS 229 0.17 ILE 27 -0.15 LEU 217

TYR 88 0.18 GLY 28 -0.13 THR 222

ASN 234 0.29 PHE 29 -0.12 THR 222

TYR 236 0.26 ASP 30 -0.13 LEU 217

ASN 234 0.27 ILE 31 -0.18 GLU 25

ASN 234 0.44 ASP 32 -0.23 LEU 217

ASN 234 0.55 LEU 33 -0.24 LEU 217

ASN 234 0.42 GLY 34 -0.23 GLU 25

ASN 234 0.51 ASN 35 -0.36 GLU 25

ASN 234 0.70 GLU 36 -0.31 GLU 25

ASN 234 0.62 MET 37 -0.25 GLU 25

ASN 234 0.52 CYS 38 -0.28 GLU 25

ASN 234 0.60 LYS 39 -0.32 LYS 23

ASN 234 0.65 ARG 40 -0.35 ALA 1

ASN 234 0.52 MET 41 -0.43 ALA 1

ASN 234 0.50 GLN 42 -0.48 ALA 1

ASN 234 0.44 VAL 43 -0.44 ALA 1

ASN 234 0.41 LYS 44 -0.26 ALA 1

ASN 234 0.37 CYS 45 -0.25 GLU 25

ASN 234 0.30 THR 46 -0.21 GLU 25

ASN 234 0.25 TRP 47 -0.20 GLU 25

TYR 236 0.17 VAL 48 -0.18 LEU 2

TYR 88 0.15 ALA 49 -0.15 LEU 2

SER 58 0.14 SER 50 -0.16 PHE 233

GLY 24 0.16 ASP 51 -0.24 PHE 233

TYR 88 0.11 PHE 52 -0.27 PHE 233

ALA 22 0.10 ASP 53 -0.26 PHE 233

GLY 24 0.09 ALA 54 -0.22 GLU 80

LEU 87 0.11 LEU 55 -0.24 GLU 80

ALA 1 0.08 ILE 56 -0.37 GLU 80

ALA 1 0.09 PRO 57 -0.45 GLU 80

SER 50 0.14 SER 58 -0.35 GLU 80

ALA 1 0.10 LEU 59 -0.37 GLU 80

ALA 1 0.15 LYS 60 -0.54 GLU 80

ALA 1 0.12 ALA 61 -0.40 GLU 80

ALA 1 0.12 LYS 62 -0.33 LEU 2

TYR 236 0.12 LYS 63 -0.29 LEU 2

ASN 234 0.14 ILE 64 -0.28 LEU 2

ASN 234 0.18 ASP 65 -0.36 LEU 2

ASN 234 0.18 ALA 66 -0.25 LEU 2

LEU 87 0.17 ILE 67 -0.18 LEU 2

LEU 87 0.26 ILE 68 -0.12 GLU 25

TYR 88 0.22 SER 69 -0.16 PHE 233

TYR 88 0.22 SER 70 -0.25 PHE 233

THR 13 0.11 LEU 71 -0.23 PHE 233

THR 13 0.10 SER 72 -0.26 PHE 233

ASP 85 0.11 ILE 73 -0.16 PHE 233

ASP 85 0.11 THR 74 -0.21 PHE 233

ASP 85 0.16 ASP 75 -0.24 ALA 124

ASP 85 0.10 LYS 76 -0.35 ALA 124

ASP 85 0.08 ARG 77 -0.31 ILE 56

ASP 85 0.14 GLN 78 -0.28 LYS 60

ASP 85 0.13 GLN 79 -0.38 LYS 60

ALA 1 0.09 GLU 80 -0.54 LYS 60

ALA 1 0.10 ILE 81 -0.31 LYS 60

THR 204 0.13 ALA 82 -0.14 LYS 60

PRO 3 0.13 PHE 83 -0.10 LYS 228

ASN 234 0.24 SER 84 -0.10 GLU 25

ASN 234 0.28 ASP 85 -0.12 ASP 224

TYR 236 0.29 LYS 86 -0.10 LYS 228

ILE 68 0.26 LEU 87 -0.20 ASP 224

LEU 33 0.28 TYR 88 -0.18 LYS 228

GLN 219 0.20 ALA 89 -0.20 ASN 234

GLN 219 0.12 ALA 90 -0.48 PHE 233

GLN 219 0.12 ASP 91 -0.70 PHE 233

ALA 22 0.12 SER 92 -0.75 PHE 233

ALA 22 0.14 ARG 93 -0.90 PHE 233

ALA 22 0.18 LEU 94 -0.82 PHE 233

ALA 22 0.21 ILE 95 -0.82 PHE 233

ALA 22 0.23 ALA 96 -0.71 PHE 233

ALA 22 0.24 ALA 97 -0.65 PHE 233

ALA 22 0.22 LYS 98 -0.67 PHE 233

ALA 22 0.20 GLY 99 -0.62 PHE 233

ALA 22 0.20 SER 100 -0.63 PHE 233

ALA 22 0.18 PRO 101 -0.60 PHE 233

ALA 22 0.18 ILE 102 -0.64 PHE 233

ALA 22 0.16 GLN 103 -0.67 PHE 233

ALA 22 0.15 PRO 104 -0.66 PHE 233

ALA 22 0.14 THR 105 -0.58 PHE 233

ALA 22 0.14 LEU 106 -0.51 PHE 233

ALA 22 0.15 GLU 107 -0.50 PHE 233

ALA 22 0.17 SER 108 -0.55 PHE 233

ALA 22 0.18 LEU 109 -0.54 PHE 233

ALA 22 0.17 LYS 110 -0.48 PHE 233

ALA 22 0.19 GLY 111 -0.46 PHE 233

ALA 22 0.21 LYS 112 -0.51 PHE 233

ALA 22 0.23 HIS 113 -0.50 PHE 233

ALA 22 0.22 VAL 114 -0.55 PHE 233

ALA 22 0.24 GLY 115 -0.53 PHE 233

ALA 22 0.20 VAL 116 -0.52 PHE 233

ALA 22 0.19 LEU 117 -0.45 PHE 233

ALA 22 0.16 GLN 118 -0.38 PHE 233

ALA 22 0.12 GLY 119 -0.34 PHE 233

ALA 22 0.12 SER 120 -0.40 PHE 233

ALA 22 0.11 THR 121 -0.42 PHE 233

ALA 22 0.14 GLN 122 -0.51 PHE 233

ALA 22 0.14 GLU 123 -0.45 PHE 233

ALA 22 0.12 ALA 124 -0.40 PHE 233

ALA 22 0.12 TYR 125 -0.46 PHE 233

ALA 22 0.15 ALA 126 -0.48 PHE 233

ALA 22 0.14 ASN 127 -0.41 PHE 233

ALA 22 0.12 ASP 128 -0.39 PHE 233

ALA 22 0.13 ASN 129 -0.43 PHE 233

ALA 22 0.15 TRP 130 -0.45 PHE 233

ALA 22 0.16 ARG 131 -0.42 PHE 233

ALA 22 0.14 THR 132 -0.38 PHE 233

ALA 22 0.14 LYS 133 -0.40 PHE 233

ALA 22 0.16 GLY 134 -0.41 PHE 233

ALA 22 0.18 VAL 135 -0.46 PHE 233

ALA 22 0.19 ASP 136 -0.45 PHE 233

ALA 22 0.19 VAL 137 -0.47 PHE 233

ALA 22 0.21 VAL 138 -0.44 PHE 233

ALA 22 0.19 ALA 139 -0.42 PHE 233

ALA 22 0.22 TYR 140 -0.41 PHE 233

ALA 22 0.21 ALA 141 -0.35 PHE 233

ALA 22 0.24 ASN 142 -0.39 PHE 233

ALA 22 0.27 GLN 143 -0.47 PHE 233

ALA 22 0.38 ASP 144 -0.44 PHE 233

ALA 22 0.35 LEU 145 -0.43 PHE 233

ALA 22 0.31 ILE 146 -0.51 PHE 233

ALA 22 0.38 TYR 147 -0.54 PHE 233

ALA 22 0.43 SER 148 -0.46 PHE 233

ALA 22 0.36 ASP 149 -0.47 PHE 233

ALA 22 0.33 LEU 150 -0.54 PHE 233

ALA 22 0.38 THR 151 -0.50 PHE 233

ALA 22 0.37 ALA 152 -0.44 PHE 233

ALA 22 0.32 GLY 153 -0.47 PHE 233

ALA 22 0.30 ARG 154 -0.46 PHE 233

ALA 22 0.28 LEU 155 -0.52 PHE 233

ALA 22 0.25 ASP 156 -0.56 PHE 233

ALA 22 0.24 ALA 157 -0.63 PHE 233

ALA 22 0.23 ALA 158 -0.65 PHE 233

ALA 22 0.19 LEU 159 -0.68 PHE 233

ALA 22 0.18 GLN 160 -0.67 PHE 233

ALA 22 0.14 ASP 161 -0.70 PHE 233

ALA 22 0.12 GLU 162 -0.98 PHE 233

TYR 88 0.13 VAL 163 -0.86 PHE 233

TYR 88 0.19 ALA 164 -0.65 PHE 233

ALA 22 0.20 ALA 165 -0.82 PHE 233

ALA 22 0.16 SER 166 -1.00 PHE 233

TYR 88 0.16 GLU 167 -0.69 PHE 233

ALA 22 0.22 GLY 168 -0.57 PHE 233

ALA 22 0.28 PHE 169 -0.66 PHE 233

ALA 22 0.23 LEU 170 -0.80 PHE 233

ALA 22 0.20 LYS 171 -0.69 PHE 233

ALA 22 0.28 GLN 172 -0.52 PHE 233

ALA 22 0.32 PRO 173 -0.45 PHE 233

ALA 22 0.38 ALA 174 -0.50 PHE 233

ALA 22 0.30 GLY 175 -0.64 PHE 233

ALA 22 0.26 LYS 176 -0.61 PHE 233

ALA 22 0.26 GLU 177 -0.61 PHE 233

ALA 22 0.25 TYR 178 -0.72 PHE 233

ALA 22 0.21 ALA 179 -0.86 PHE 233

ALA 22 0.19 PHE 180 -0.96 PHE 233

ALA 22 0.18 ALA 181 -0.82 PHE 233

ALA 22 0.15 GLY 182 -0.82 PHE 233

ALA 22 0.12 PRO 183 -0.92 PHE 233

GLN 219 0.11 SER 184 -0.91 PHE 233

ALA 22 0.11 VAL 185 -0.72 PHE 233

GLN 219 0.10 LYS 186 -0.60 PHE 233

GLN 219 0.09 ASP 187 -0.48 PHE 233

GLN 219 0.11 LYS 188 -0.36 ASN 234

LYS 76 0.09 LYS 189 -0.33 PHE 233

ALA 22 0.09 TYR 190 -0.40 PHE 233

ALA 22 0.09 PHE 191 -0.43 PHE 233

GLN 219 0.10 GLY 192 -0.28 PHE 233

THR 215 0.14 ASP 193 -0.18 PHE 233

THR 215 0.14 GLY 194 -0.17 PHE 233

THR 13 0.11 THR 195 -0.17 LYS 228

TYR 236 0.15 GLY 196 -0.15 LYS 228

TYR 236 0.17 VAL 197 -0.12 GLU 25

TYR 236 0.11 GLY 198 -0.16 LEU 2

ASN 234 0.13 LEU 199 -0.21 LEU 2

ALA 1 0.13 ARG 200 -0.27 LEU 2

ALA 1 0.20 LYS 201 -0.14 LEU 2

ALA 1 0.34 ASP 202 -0.11 LEU 2

ALA 1 0.27 ASP 203 -0.18 LEU 2

ASN 234 0.23 THR 204 -0.09 GLU 25

ASN 234 0.29 GLU 205 -0.12 GLU 25

PRO 3 0.32 LEU 206 -0.13 GLU 25

ASN 234 0.29 LYS 207 -0.11 GLU 25

ASN 234 0.35 ALA 208 -0.13 GLU 25

ASN 234 0.42 ALA 209 -0.25 ALA 1

ASN 234 0.44 PHE 210 -0.17 GLU 25

ASN 234 0.45 ASP 211 -0.15 GLU 25

ASN 234 0.53 LYS 212 -0.22 ALA 1

ASN 234 0.62 ALA 213 -0.23 ALA 1

ASN 234 0.67 LEU 214 -0.19 GLU 25

ASN 234 0.72 THR 215 -0.18 ALA 1

ASN 234 0.78 GLU 216 -0.24 LYS 23

ASN 234 0.89 LEU 217 -0.24 LYS 23

ASN 234 1.10 ARG 218 -0.15 LYS 23

ASN 234 1.01 GLN 219 -0.18 ALA 1

ASN 234 0.97 ASP 220 -0.24 LYS 23

ASN 234 1.16 GLY 221 -0.18 LYS 23

ASN 234 0.98 THR 222 -0.23 LYS 23

ASN 234 1.11 TYR 223 -0.14 LEU 87

ASN 234 1.25 ASP 224 -0.20 LEU 87

ASN 234 0.78 LYS 225 -0.12 LYS 23

ASN 234 0.67 MET 226 -0.13 LYS 23

ASN 234 0.60 ALA 227 -0.16 ALA 90

PHE 233 0.39 LYS 228 -0.24 VAL 163

GLU 36 0.27 LYS 229 -0.12 VAL 163

ASN 234 0.15 TYR 230 -0.12 VAL 163

ASP 224 0.25 PHE 231 -0.40 VAL 163

ASP 224 0.45 ASP 232 -0.44 SER 166

GLY 221 1.07 PHE 233 -1.00 SER 166

ASP 224 1.25 ASN 234 -0.78 SER 184

ARG 218 0.35 VAL 235 -0.30 ALA 90

ARG 218 0.49 TYR 236 -0.20 LYS 228

ARG 218 0.64 GLY 237 -0.46 ASP 91

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).
Between 2015 and 2025, it was hosted by US2B (Nantes).
Last modification: april 24th, 2026.

Should you encounter any unexpected behaviour, please let us know. elNémo has been relocated. **Some cleaning from time to time** Sorry for the inconvenience.

*** open_8 ***

CA distance fluctuations for 260611224051872834

--- normal mode 15 ---

Should you encounter any unexpected behaviour,
please let us know.
elNémo has been relocated.
Some cleaning from time to time
Sorry for the inconvenience.

* open_8 *