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

* *

CA distance fluctuations for 2604241005481913808

--- 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
GLN 42 0.88 ALA 1 -1.00 ALA 61

MET 41 1.51 LEU 2 -0.72 ASP 202

MET 41 0.19 PRO 3 -0.29 ASP 65

ALA 1 0.15 GLN 4 -0.20 LEU 206

LEU 2 0.31 THR 5 -0.04 PRO 3

LEU 2 0.31 VAL 6 -0.12 PRO 3

LEU 2 0.13 ARG 7 -0.17 PRO 3

LEU 2 0.20 ILE 8 -0.14 ALA 1

LEU 2 0.08 GLY 9 -0.26 ALA 1

LEU 2 0.14 THR 10 -0.19 ALA 1

LEU 2 0.11 ASP 11 -0.22 ALA 1

LEU 2 0.17 THR 12 -0.11 ALA 1

LEU 2 0.14 THR 13 -0.13 ALA 1

LEU 2 0.18 TYR 14 -0.09 ALA 1

LEU 2 0.23 ALA 15 -0.11 GLU 167

LEU 2 0.27 PRO 16 -0.16 GLU 167

LEU 2 0.28 PHE 17 -0.10 GLU 167

LEU 2 0.26 SER 18 -0.08 GLU 167

LEU 2 0.24 SER 19 -0.08 GLU 167

LEU 2 0.25 LYS 20 -0.07 GLU 167

LEU 2 0.27 ASP 21 -0.08 GLN 172

LEU 2 0.25 ALA 22 -0.08 GLN 172

LEU 2 0.27 LYS 23 -0.07 GLN 172

LEU 2 0.25 GLY 24 -0.06 GLN 172

LEU 2 0.32 GLU 25 -0.07 GLU 167

LEU 2 0.32 PHE 26 -0.07 GLU 167

LEU 2 0.36 ILE 27 -0.09 GLU 167

LEU 2 0.36 GLY 28 -0.11 GLU 167

LEU 2 0.39 PHE 29 -0.10 GLU 167

LEU 2 0.38 ASP 30 -0.07 GLU 167

LEU 2 0.44 ILE 31 -0.07 GLU 167

LEU 2 0.53 ASP 32 -0.08 GLU 167

LEU 2 0.56 LEU 33 -0.07 GLU 167

LEU 2 0.58 GLY 34 -0.06 GLU 167

LEU 2 0.70 ASN 35 -0.06 GLU 167

LEU 2 0.78 GLU 36 -0.06 LYS 171

LEU 2 0.88 MET 37 -0.05 LYS 171

LEU 2 1.03 CYS 38 -0.05 LYS 171

LEU 2 1.05 LYS 39 -0.05 LYS 171

LEU 2 1.14 ARG 40 -0.05 LYS 171

LEU 2 1.51 MET 41 -0.05 GLN 4

LEU 2 1.45 GLN 42 -0.06 LEU 206

LEU 2 1.11 VAL 43 -0.15 LEU 206

LEU 2 0.71 LYS 44 -0.05 LEU 199

LEU 2 0.57 CYS 45 -0.04 GLU 167

LEU 2 0.35 THR 46 -0.06 PRO 3

LEU 2 0.28 TRP 47 -0.07 PRO 3

LEU 2 0.12 VAL 48 -0.18 ALA 1

LEU 2 0.10 ALA 49 -0.20 ALA 1

GLU 205 0.04 SER 50 -0.34 ALA 1

GLU 205 0.03 ASP 51 -0.38 ALA 1

LEU 206 0.03 PHE 52 -0.39 ALA 1

ALA 141 0.04 ASP 53 -0.52 ALA 1

ALA 141 0.03 ALA 54 -0.58 ALA 1

LEU 206 0.04 LEU 55 -0.52 ALA 1

LEU 206 0.04 ILE 56 -0.66 ALA 1

LEU 206 0.04 PRO 57 -0.79 ALA 1

GLU 205 0.05 SER 58 -0.71 ALA 1

LEU 206 0.05 LEU 59 -0.71 ALA 1

LEU 206 0.04 LYS 60 -0.96 ALA 1

GLU 205 0.05 ALA 61 -1.00 ALA 1

GLU 205 0.07 LYS 62 -0.83 ALA 1

GLU 205 0.07 LYS 63 -0.65 ALA 1

GLU 205 0.09 ILE 64 -0.47 ALA 1

GLU 205 0.11 ASP 65 -0.40 ALA 1

LEU 206 0.09 ALA 66 -0.29 ALA 1

LEU 2 0.07 ILE 67 -0.28 ALA 1

LEU 2 0.22 ILE 68 -0.11 ALA 1

LEU 2 0.16 SER 69 -0.16 ALA 1

LEU 2 0.17 SER 70 -0.13 ALA 1

LEU 2 0.08 LEU 71 -0.26 ALA 1

LEU 2 0.06 SER 72 -0.26 ALA 1

SER 120 0.04 ILE 73 -0.30 ALA 1

THR 121 0.04 THR 74 -0.39 ALA 1

THR 121 0.04 ASP 75 -0.47 ALA 1

GLY 119 0.07 LYS 76 -0.58 ALA 1

GLY 119 0.06 ARG 77 -0.58 ALA 1

GLY 119 0.05 GLN 78 -0.56 ALA 1

GLY 119 0.05 GLN 79 -0.72 ALA 1

GLY 119 0.06 GLU 80 -0.81 ALA 1

GLY 119 0.05 ILE 81 -0.70 ALA 1

GLY 119 0.04 ALA 82 -0.51 ALA 1

GLY 119 0.03 PHE 83 -0.29 ALA 1

LEU 2 0.19 SER 84 -0.10 GLN 4

LEU 2 0.24 ASP 85 -0.08 GLN 4

LEU 2 0.25 LYS 86 -0.06 GLN 4

LEU 2 0.33 LEU 87 -0.06 PRO 183

LEU 2 0.28 TYR 88 -0.07 PRO 183

LEU 2 0.20 ALA 89 -0.07 SER 184

LEU 2 0.15 ALA 90 -0.09 ALA 1

LEU 2 0.12 ASP 91 -0.10 ALA 1

LEU 2 0.11 SER 92 -0.11 ALA 1

LEU 2 0.11 ARG 93 -0.13 PHE 233

LEU 2 0.10 LEU 94 -0.13 PHE 233

LEU 2 0.11 ILE 95 -0.14 PHE 233

LEU 2 0.11 ALA 96 -0.13 PHE 233

LEU 2 0.11 ALA 97 -0.13 ASP 232

LEU 2 0.13 LYS 98 -0.14 ASP 232

LEU 2 0.12 GLY 99 -0.13 ASP 232

LEU 2 0.11 SER 100 -0.12 PHE 233

LEU 2 0.10 PRO 101 -0.11 PHE 233

LEU 2 0.09 ILE 102 -0.11 PHE 233

LEU 2 0.09 GLN 103 -0.11 PHE 233

LEU 2 0.08 PRO 104 -0.10 PHE 233

LEU 2 0.06 THR 105 -0.10 ALA 1

LEU 2 0.05 LEU 106 -0.13 ALA 1

LEU 2 0.05 GLU 107 -0.10 ALA 1

LEU 2 0.07 SER 108 -0.09 PHE 233

LEU 2 0.06 LEU 109 -0.12 ALA 1

LEU 2 0.04 LYS 110 -0.13 ALA 1

LEU 2 0.05 GLY 111 -0.13 ALA 1

LEU 2 0.05 LYS 112 -0.12 ALA 1

LEU 2 0.05 HIS 113 -0.15 ALA 1

LEU 2 0.06 VAL 114 -0.15 ALA 1

LEU 2 0.05 GLY 115 -0.17 ALA 1

LEU 2 0.05 VAL 116 -0.20 ALA 1

LYS 76 0.04 LEU 117 -0.23 ALA 1

LYS 76 0.05 GLN 118 -0.28 ALA 1

LYS 76 0.07 GLY 119 -0.33 ALA 1

LYS 76 0.06 SER 120 -0.29 ALA 1

LYS 76 0.06 THR 121 -0.29 ALA 1

LYS 76 0.04 GLN 122 -0.23 ALA 1

LYS 76 0.05 GLU 123 -0.26 ALA 1

LYS 76 0.06 ALA 124 -0.30 ALA 1

LYS 76 0.04 TYR 125 -0.26 ALA 1

LYS 76 0.04 ALA 126 -0.23 ALA 1

LYS 76 0.05 ASN 127 -0.27 ALA 1

LYS 76 0.05 ASP 128 -0.28 ALA 1

LYS 76 0.03 ASN 129 -0.23 ALA 1

LYS 76 0.03 TRP 130 -0.21 ALA 1

LYS 76 0.04 ARG 131 -0.23 ALA 1

LYS 76 0.04 THR 132 -0.25 ALA 1

LYS 76 0.03 LYS 133 -0.21 ALA 1

LYS 76 0.03 GLY 134 -0.20 ALA 1

LYS 76 0.03 VAL 135 -0.18 ALA 1

LYS 76 0.03 ASP 136 -0.19 ALA 1

LYS 76 0.04 VAL 137 -0.20 ALA 1

LYS 76 0.04 VAL 138 -0.21 ALA 1

LYS 76 0.04 ALA 139 -0.24 ALA 1

LYS 76 0.04 TYR 140 -0.22 ALA 1

LYS 76 0.04 ALA 141 -0.25 ALA 1

LEU 2 0.05 ASN 142 -0.21 ALA 1

LEU 2 0.07 GLN 143 -0.17 ALA 1

LEU 2 0.08 ASP 144 -0.14 ALA 1

LEU 2 0.07 LEU 145 -0.15 ALA 1

LEU 2 0.07 ILE 146 -0.14 ALA 1

LEU 2 0.09 TYR 147 -0.10 ALA 1

LEU 2 0.08 SER 148 -0.10 ALA 1

LEU 2 0.07 ASP 149 -0.12 ALA 1

LEU 2 0.09 LEU 150 -0.09 ASP 232

LEU 2 0.10 THR 151 -0.09 ASP 232

LEU 2 0.08 ALA 152 -0.08 ALA 1

LEU 2 0.08 GLY 153 -0.09 ASP 232

LEU 2 0.06 ARG 154 -0.12 ALA 1

LEU 2 0.07 LEU 155 -0.12 ALA 1

LEU 2 0.08 ASP 156 -0.10 ALA 1

LEU 2 0.08 ALA 157 -0.11 PHE 233

LEU 2 0.08 ALA 158 -0.12 ALA 1

LEU 2 0.08 LEU 159 -0.14 ALA 1

LEU 2 0.09 GLN 160 -0.13 ALA 1

LEU 2 0.11 ASP 161 -0.12 ALA 1

LEU 2 0.15 GLU 162 -0.13 PHE 233

LEU 2 0.17 VAL 163 -0.13 PHE 231

LEU 2 0.14 ALA 164 -0.12 PRO 16

LEU 2 0.14 ALA 165 -0.13 PHE 231

LEU 2 0.17 SER 166 -0.20 PHE 231

LEU 2 0.18 GLU 167 -0.19 TYR 230

LEU 2 0.15 GLY 168 -0.13 TYR 230

LEU 2 0.14 PHE 169 -0.13 TYR 230

LEU 2 0.15 LEU 170 -0.18 ASP 232

LEU 2 0.17 LYS 171 -0.18 TYR 230

LEU 2 0.15 GLN 172 -0.14 TYR 230

LEU 2 0.14 PRO 173 -0.12 LYS 229

LEU 2 0.13 ALA 174 -0.12 ASP 232

LEU 2 0.14 GLY 175 -0.14 ASP 232

LEU 2 0.15 LYS 176 -0.15 ASP 232

LEU 2 0.13 GLU 177 -0.14 ASP 232

LEU 2 0.13 TYR 178 -0.15 ASP 232

LEU 2 0.14 ALA 179 -0.18 ASP 232

LEU 2 0.14 PHE 180 -0.19 PHE 233

LEU 2 0.12 ALA 181 -0.16 PHE 233

LEU 2 0.12 GLY 182 -0.15 PHE 233

LEU 2 0.13 PRO 183 -0.16 ASN 234

LEU 2 0.13 SER 184 -0.12 ASN 234

LEU 2 0.10 VAL 185 -0.09 ALA 1

LEU 2 0.09 LYS 186 -0.11 ALA 1

LEU 2 0.05 ASP 187 -0.18 ALA 1

LEU 2 0.03 LYS 188 -0.23 ALA 1

THR 105 0.02 LYS 189 -0.32 ALA 1

PRO 104 0.03 TYR 190 -0.30 ALA 1

LEU 2 0.05 PHE 191 -0.24 ALA 1

LEU 2 0.04 GLY 192 -0.26 ALA 1

LEU 2 0.09 ASP 193 -0.16 ALA 1

LEU 2 0.15 GLY 194 -0.09 ALA 1

LEU 2 0.16 THR 195 -0.12 ALA 1

LEU 2 0.18 GLY 196 -0.11 ALA 1

LEU 2 0.19 VAL 197 -0.13 ALA 1

LEU 206 0.04 GLY 198 -0.36 ALA 1

GLY 119 0.04 LEU 199 -0.45 ALA 1

GLY 119 0.04 ARG 200 -0.73 ALA 1

GLY 119 0.04 LYS 201 -0.75 ALA 1

GLY 119 0.04 ASP 202 -0.81 ALA 1

ASP 65 0.05 ASP 203 -0.61 LEU 2

ASP 65 0.05 THR 204 -0.32 LEU 2

PRO 3 0.16 GLU 205 -0.10 GLN 4

ASP 65 0.10 LEU 206 -0.20 GLN 4

LEU 2 0.12 LYS 207 -0.14 GLN 4

LEU 2 0.31 ALA 208 -0.11 GLN 4

LEU 2 0.71 ALA 209 -0.11 GLN 4

LEU 2 0.62 PHE 210 -0.10 GLN 4

LEU 2 0.48 ASP 211 -0.09 GLN 4

LEU 2 0.66 LYS 212 -0.07 GLN 4

LEU 2 0.84 ALA 213 -0.06 GLN 4

LEU 2 0.62 LEU 214 -0.06 GLN 4

LEU 2 0.56 THR 215 -0.06 PRO 183

ALA 1 0.69 GLU 216 -0.06 PRO 183

LEU 2 0.67 LEU 217 -0.07 LYS 171

LEU 2 0.54 ARG 218 -0.07 PRO 183

ALA 1 0.61 GLN 219 -0.07 PRO 183

ALA 1 0.70 ASP 220 -0.07 LYS 171

ALA 1 0.59 GLY 221 -0.08 LYS 171

ALA 1 0.59 THR 222 -0.08 LYS 171

LEU 2 0.52 TYR 223 -0.08 LYS 171

LEU 2 0.46 ASP 224 -0.10 LYS 171

LEU 2 0.48 LYS 225 -0.11 LYS 171

LEU 2 0.49 MET 226 -0.11 LYS 171

LEU 2 0.41 ALA 227 -0.12 SER 166

LEU 2 0.40 LYS 228 -0.14 LYS 171

LEU 2 0.39 LYS 229 -0.16 LYS 171

LEU 2 0.34 TYR 230 -0.19 GLU 167

LEU 2 0.32 PHE 231 -0.20 SER 166

LEU 2 0.31 ASP 232 -0.18 ALA 179

LEU 2 0.29 PHE 233 -0.19 PHE 180

LEU 2 0.30 ASN 234 -0.16 PRO 183

LEU 2 0.29 VAL 235 -0.11 PRO 183

LEU 2 0.30 TYR 236 -0.10 PRO 183

LEU 2 0.24 GLY 237 -0.12 PRO 183

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.

*** ***

CA distance fluctuations for 2604241005481913808

--- normal mode 11 ---

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

* *