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

* test *

CA distance fluctuations for 2605171448103278031

--- normal mode 7 ---

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
LYS 149 0.02 GLY 2 -0.28 GLN 113

LYS 149 0.01 VAL 3 -0.32 GLN 114

LYS 149 0.01 LEU 4 -0.37 GLN 114

LYS 149 0.03 PHE 5 -0.33 ASP 117

LYS 149 0.04 TYR 6 -0.31 ASP 117

LYS 149 0.03 ILE 7 -0.36 GLN 114

LYS 149 0.03 LEU 8 -0.40 ASP 117

LYS 149 0.06 LEU 9 -0.35 ASP 117

LYS 149 0.06 CYS 10 -0.33 ASP 117

LYS 149 0.03 GLY 11 -0.37 GLN 114

LYS 149 0.03 TYR 12 -0.35 GLN 114

LYS 149 0.02 PRO 13 -0.37 GLN 114

LYS 149 0.03 PRO 14 -0.32 GLN 114

LYS 149 0.03 PHE 15 -0.30 GLN 114

LYS 149 0.04 PHE 16 -0.26 GLN 114

LYS 149 0.06 GLY 17 -0.24 GLN 114

LYS 149 0.07 PHE 34 -0.24 GLN 114

LYS 149 0.08 LYS 35 -0.24 GLN 114

LYS 149 0.08 GLY 36 -0.25 GLN 114

LYS 149 0.08 LYS 37 -0.26 GLN 114

LYS 149 0.08 GLU 38 -0.28 ASP 117

LYS 149 0.09 TRP 39 -0.26 ASP 117

LYS 149 0.11 ASN 40 -0.23 ASP 117

LYS 149 0.12 ASN 41 -0.24 ASP 117

LYS 149 0.12 ILE 42 -0.25 ASP 117

LYS 149 0.14 SER 43 -0.22 ASP 117

LYS 149 0.14 GLU 44 -0.19 ASP 117

LYS 149 0.15 GLU 45 -0.18 ASP 117

LYS 149 0.11 ALA 46 -0.23 ASP 117

LYS 149 0.11 LYS 47 -0.22 ASP 117

LYS 149 0.11 ASP 48 -0.18 ASP 117

LYS 149 0.09 LEU 49 -0.19 ASP 117

LYS 149 0.07 ILE 50 -0.22 ASP 117

LYS 149 0.08 LYS 51 -0.19 ASP 117

LYS 149 0.07 ARG 52 -0.16 ASP 117

LYS 149 0.04 CYS 53 -0.20 GLN 113

LYS 149 0.04 LEU 54 -0.22 GLN 113

LYS 149 0.05 THR 55 -0.18 GLN 114

LYS 149 0.04 MET 56 -0.19 VAL 202

LYS 149 0.03 ASP 57 -0.16 VAL 202

LYS 149 0.02 ALA 58 -0.16 THR 227

LYS 149 0.03 ASP 59 -0.11 VAL 202

LYS 145 0.05 LYS 60 -0.11 GLN 114

LYS 149 0.04 ARG 61 -0.14 GLN 113

LYS 145 0.05 ILE 62 -0.12 GLN 113

LYS 149 0.02 CYS 63 -0.12 GLY 136

GLU 66 0.01 ALA 64 -0.17 GLY 136

GLU 141 0.03 SER 65 -0.08 GLY 136

GLU 141 0.08 GLU 66 -0.09 ASP 117

LYS 145 0.06 ALA 67 -0.15 GLY 136

LYS 145 0.07 LEU 68 -0.12 GLY 136

LYS 145 0.13 GLN 69 -0.09 ASP 117

LYS 145 0.15 HIS 70 -0.13 ASP 117

LYS 145 0.19 PRO 71 -0.13 ASP 117

LYS 149 0.15 TRP 72 -0.19 ASP 117

LYS 149 0.12 PHE 73 -0.19 ASP 117

LYS 145 0.19 LYS 74 -0.12 ASP 117

LYS 149 0.22 LYS 75 -0.14 ASP 117

LYS 149 0.16 LYS 76 -0.21 ASP 117

LYS 149 0.13 LYS 77 -0.20 ASP 117

LYS 149 0.23 TYR 78 -0.11 ASP 117

LYS 149 0.22 ALA 79 -0.09 ASP 117

LYS 149 0.29 PHE 80 -0.06 ASP 117

ASP 150 0.21 ASN 81 -0.04 ASP 117

ASP 150 0.08 MET 82 -0.06 LYS 77

ILE 88 0.02 ASP 83 -0.07 LEU 8

ASN 81 0.02 MET 84 -0.12 LEU 8

ASN 81 0.01 LYS 85 -0.14 LEU 8

ASN 81 0.04 MET 86 -0.15 LEU 8

ASN 81 0.06 ASP 87 -0.14 LEU 8

ASN 81 0.09 ILE 88 -0.12 LEU 4

PHE 80 0.07 HIS 89 -0.14 LEU 4

PHE 80 0.08 VAL 90 -0.15 LEU 4

PHE 80 0.10 LEU 91 -0.13 LEU 4

PHE 80 0.08 GLU 92 -0.13 LEU 4

PHE 80 0.06 ASN 93 -0.17 LEU 4

PHE 80 0.07 PHE 94 -0.16 LEU 4

PHE 80 0.08 LYS 95 -0.14 LEU 4

PHE 80 0.06 ASN 96 -0.16 LEU 4

PHE 80 0.05 TYR 97 -0.19 LEU 4

PHE 80 0.05 GLY 98 -0.18 LEU 4

PHE 80 0.05 LEU 99 -0.17 LEU 4

PHE 80 0.04 LEU 100 -0.19 LEU 4

PHE 80 0.04 LEU 101 -0.21 PRO 13

PHE 80 0.03 LYS 102 -0.23 PRO 13

PHE 80 0.02 PHE 103 -0.25 PRO 13

PHE 80 0.02 GLN 104 -0.24 PRO 13

PHE 80 0.03 LYS 105 -0.24 LEU 4

PHE 80 0.02 LEU 106 -0.27 LEU 4

ASN 81 0.01 ALA 107 -0.28 PRO 13

ASN 81 0.02 MET 108 -0.27 LEU 4

ASN 81 0.01 THR 109 -0.30 LEU 4

LYS 85 0.00 ILE 110 -0.33 LEU 4

LYS 85 0.00 ILE 111 -0.31 LEU 4

LYS 85 0.00 ALA 112 -0.31 LEU 4

LYS 85 0.00 GLN 113 -0.37 LEU 4

LYS 85 0.00 GLN 114 -0.38 LEU 8

LYS 85 0.01 SER 115 -0.35 LEU 8

LYS 85 0.01 ASN 116 -0.35 LEU 8

LYS 85 0.01 ASP 117 -0.40 LEU 8

LYS 85 0.01 TYR 118 -0.36 LEU 8

LYS 85 0.01 ASP 119 -0.30 LEU 8

LYS 85 0.01 VAL 120 -0.28 LEU 8

LYS 85 0.01 GLU 121 -0.30 LEU 8

LYS 85 0.01 LYS 122 -0.22 LEU 8

ASN 81 0.02 LEU 123 -0.22 LEU 8

LYS 85 0.01 LYS 124 -0.26 LEU 8

LYS 85 0.01 SER 125 -0.21 LEU 8

PHE 80 0.04 THR 126 -0.15 LEU 8

PHE 80 0.03 PHE 127 -0.19 LEU 4

GLY 136 0.01 LEU 128 -0.18 LEU 4

TYR 78 0.05 VAL 129 -0.10 LEU 4

TYR 78 0.11 LEU 130 -0.10 LEU 4

TYR 78 0.07 ASP 131 -0.12 LEU 4

LYS 74 0.15 GLU 132 -0.04 LEU 4

LYS 74 0.11 ASP 133 -0.05 LEU 4

TYR 78 0.01 GLY 134 -0.12 LEU 4

TYR 78 0.02 LYS 135 -0.18 LEU 4

LEU 128 0.01 GLY 136 -0.26 LEU 4

PHE 80 0.03 TYR 137 -0.22 LEU 4

TYR 78 0.06 ILE 138 -0.16 LEU 4

PRO 71 0.10 THR 139 -0.12 LEU 4

PRO 71 0.11 LYS 140 -0.10 LEU 4

PRO 71 0.16 GLU 141 -0.06 LEU 4

LYS 74 0.15 GLN 142 -0.07 LEU 4

PHE 80 0.13 LEU 143 -0.09 LEU 4

LYS 75 0.15 LYS 144 -0.06 LEU 4

LYS 75 0.20 LYS 145 -0.02 LEU 4

PHE 80 0.19 GLY 146 -0.04 LEU 4

PHE 80 0.19 LEU 147 -0.05 LEU 4

PHE 80 0.22 GLU 148 -0.01 LEU 4

PHE 80 0.29 LYS 149 -0.01 LYS 85

PHE 80 0.26 ASP 150 -0.02 LEU 4

PHE 80 0.24 GLY 151 -0.01 LYS 85

PHE 80 0.19 LEU 152 -0.03 LEU 4

PHE 80 0.17 LYS 153 -0.03 LEU 4

PHE 80 0.14 LEU 154 -0.06 LEU 4

PHE 80 0.13 PRO 155 -0.07 LEU 4

PHE 80 0.11 TYR 156 -0.08 LEU 4

PHE 80 0.10 ASN 157 -0.10 LEU 4

PHE 80 0.11 PHE 158 -0.10 LEU 4

PHE 80 0.11 ASP 159 -0.08 LEU 4

PHE 80 0.09 LEU 160 -0.11 LEU 4

PHE 80 0.09 LEU 161 -0.13 LEU 4

PRO 71 0.10 LEU 162 -0.11 LEU 4

PRO 71 0.10 ASP 163 -0.11 LEU 4

PHE 80 0.07 GLN 164 -0.14 LEU 4

PHE 80 0.07 ILE 165 -0.15 LEU 4

PRO 71 0.09 ASP 166 -0.12 LEU 4

PRO 71 0.08 SER 167 -0.13 LEU 4

PHE 80 0.05 ASP 168 -0.17 LEU 4

PHE 80 0.04 GLY 169 -0.19 LEU 4

GLN 69 0.05 SER 170 -0.17 LEU 4

PRO 71 0.07 GLY 171 -0.14 LEU 4

PHE 80 0.05 LYS 172 -0.17 LEU 4

PHE 80 0.05 ILE 173 -0.20 LEU 4

PHE 80 0.03 ASP 174 -0.26 LEU 4

PHE 80 0.01 TYR 175 -0.29 LEU 4

PHE 80 0.01 THR 176 -0.31 LEU 4

PHE 80 0.03 GLU 177 -0.26 LEU 4

PHE 80 0.04 PHE 178 -0.23 LEU 4

PHE 80 0.02 ILE 179 -0.26 LEU 4

PHE 80 0.02 ALA 180 -0.25 LEU 4

PHE 80 0.04 ALA 181 -0.21 LEU 4

PHE 80 0.05 ALA 182 -0.20 LEU 4

ASN 81 0.03 LEU 183 -0.22 LEU 8

ASN 81 0.03 ASP 184 -0.20 LEU 8

ASN 81 0.03 ARG 185 -0.21 GLY 11

ASN 81 0.02 LYS 186 -0.24 GLY 11

ASN 81 0.01 GLN 187 -0.26 GLY 11

ASN 81 0.02 LEU 188 -0.25 GLY 11

ASN 81 0.01 SER 189 -0.26 GLY 11

ASN 81 0.01 LYS 190 -0.28 GLY 11

LYS 85 0.00 LYS 191 -0.31 GLY 11

LYS 85 0.00 LEU 192 -0.31 GLY 11

ASN 81 0.01 ILE 193 -0.29 GLY 11

LYS 85 0.00 TYR 194 -0.31 PRO 13

LYS 85 0.00 CYS 195 -0.34 PRO 13

LEU 160 0.00 ALA 196 -0.32 PRO 13

ASN 81 0.00 PHE 197 -0.31 PRO 13

LEU 160 0.00 ARG 198 -0.34 PRO 13

LEU 160 0.00 VAL 199 -0.35 PRO 13

ASN 157 0.00 PHE 200 -0.32 PRO 13

ASN 157 0.00 ASP 201 -0.32 PRO 13

ASN 157 0.00 VAL 202 -0.34 PRO 13

ASN 157 0.00 ASP 203 -0.34 PRO 13

ASN 157 0.00 ASN 204 -0.34 PRO 13

ASN 157 0.00 ASP 205 -0.31 PRO 13

ASN 157 0.00 GLY 206 -0.30 PRO 13

ASN 81 0.01 GLU 207 -0.28 PRO 13

ASN 81 0.01 ILE 208 -0.28 PRO 13

ASN 81 0.01 THR 209 -0.27 PRO 13

PHE 80 0.01 THR 210 -0.26 PRO 13

ASN 81 0.01 ALA 211 -0.28 PRO 13

ASN 81 0.00 GLU 212 -0.30 PRO 13

PHE 80 0.01 LEU 213 -0.28 PRO 13

PHE 80 0.01 ALA 214 -0.27 PRO 13

ASN 81 0.00 HIS 215 -0.30 PRO 13

ASN 81 0.01 ILE 216 -0.30 PRO 13

PHE 80 0.01 LEU 217 -0.27 PRO 13

PHE 80 0.01 THR 227 -0.28 PRO 13

PHE 80 0.01 GLN 228 -0.26 PRO 13

PHE 80 0.01 ARG 229 -0.25 PRO 13

PHE 80 0.02 ASP 230 -0.22 PRO 13

PHE 80 0.02 VAL 231 -0.21 PRO 13

PHE 80 0.03 ASN 232 -0.20 PRO 13

PHE 80 0.03 ARG 233 -0.21 PRO 13

PHE 80 0.02 VAL 234 -0.23 PRO 13

PHE 80 0.02 LYS 235 -0.21 PRO 13

PHE 80 0.03 ARG 236 -0.20 PRO 13

PHE 80 0.03 MET 237 -0.22 PRO 13

PHE 80 0.02 ILE 238 -0.22 PRO 13

PHE 80 0.03 ARG 239 -0.20 PRO 13

PHE 80 0.03 ASP 240 -0.20 PRO 13

PHE 80 0.02 VAL 241 -0.22 PRO 13

PHE 80 0.02 ASP 242 -0.22 PRO 13

PHE 80 0.02 LYS 243 -0.21 PRO 13

ASN 81 0.02 ASN 244 -0.22 PRO 13

PHE 80 0.02 ASN 245 -0.22 PRO 13

ASN 81 0.01 ASP 246 -0.23 PRO 13

PHE 80 0.01 GLY 247 -0.24 PRO 13

ASN 81 0.01 LYS 248 -0.25 PRO 13

ASN 81 0.01 ILE 249 -0.26 PRO 13

ASN 81 0.01 ASP 250 -0.26 PRO 13

ASN 81 0.01 PHE 251 -0.27 PRO 13

ASN 81 0.01 HIS 252 -0.25 PRO 13

ASN 81 0.02 GLU 253 -0.24 PRO 13

ASN 81 0.01 PHE 254 -0.25 PRO 13

ASN 81 0.02 SER 255 -0.24 PRO 13

ASN 81 0.02 GLU 256 -0.22 PRO 13

PHE 80 0.02 MET 257 -0.22 PRO 13

ASN 81 0.02 MET 258 -0.23 PRO 13

ASN 81 0.03 LYS 259 -0.21 PRO 13

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.

*** test ***

CA distance fluctuations for 2605171448103278031

--- normal mode 7 ---

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

* test *