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 2604241152241960399

--- 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
ARG 40 0.82 ALA 1 -0.94 ALA 61

PRO 3 0.48 LEU 2 -0.18 GLN 4

LEU 2 0.48 PRO 3 -0.26 GLN 4

THR 5 0.14 GLN 4 -0.26 PRO 3

GLN 4 0.14 THR 5 -0.17 PRO 3

LEU 2 0.14 VAL 6 -0.14 PRO 3

LEU 2 0.11 ARG 7 -0.21 ALA 1

LEU 2 0.09 ILE 8 -0.15 ALA 1

LEU 2 0.07 GLY 9 -0.25 ALA 1

LEU 2 0.06 THR 10 -0.17 ALA 1

LEU 2 0.05 ASP 11 -0.19 ALA 1

LEU 2 0.05 THR 12 -0.10 ALA 1

LEU 2 0.04 THR 13 -0.11 ALA 1

LEU 2 0.04 TYR 14 -0.05 ALA 1

LEU 2 0.05 ALA 15 -0.02 PRO 3

ALA 1 0.12 PRO 16 -0.01 ALA 22

ALA 1 0.09 PHE 17 -0.02 PRO 3

LEU 2 0.05 SER 18 -0.03 PRO 3

LEU 2 0.05 SER 19 -0.03 PRO 3

LEU 2 0.05 LYS 20 -0.03 PRO 3

ALA 1 0.10 ASP 21 -0.03 TYR 230

ALA 1 0.08 ALA 22 -0.04 LYS 229

ALA 1 0.08 LYS 23 -0.03 LYS 229

GLN 4 0.06 GLY 24 -0.02 PRO 3

ALA 1 0.10 GLU 25 -0.02 PRO 3

ALA 1 0.08 PHE 26 -0.03 PRO 3

ALA 1 0.16 ILE 27 -0.02 ALA 22

ALA 1 0.18 GLY 28 -0.02 PHE 29

ALA 1 0.24 PHE 29 -0.02 ALA 22

ALA 1 0.15 ASP 30 -0.01 PRO 3

ALA 1 0.20 ILE 31 -0.02 ASP 32

ALA 1 0.35 ASP 32 -0.02 ILE 31

ALA 1 0.35 LEU 33 -0.01 ASP 32

ALA 1 0.26 GLY 34 -0.02 ASN 35

ALA 1 0.39 ASN 35 -0.02 ILE 8

ALA 1 0.56 GLU 36 -0.01 LYS 207

ALA 1 0.51 MET 37 -0.02 GLN 4

ALA 1 0.47 CYS 38 -0.02 LYS 39

ALA 1 0.69 LYS 39 -0.02 CYS 38

ALA 1 0.82 ARG 40 -0.03 GLN 4

ALA 1 0.68 MET 41 -0.07 GLN 4

ALA 1 0.75 GLN 42 -0.03 GLN 4

ALA 1 0.44 VAL 43 -0.06 LEU 206

ALA 1 0.30 LYS 44 -0.03 THR 5

ALA 1 0.14 CYS 45 -0.05 PRO 3

LEU 2 0.08 THR 46 -0.09 PRO 3

LEU 2 0.07 TRP 47 -0.07 PRO 3

LEU 2 0.06 VAL 48 -0.22 ALA 1

LEU 2 0.05 ALA 49 -0.23 ALA 1

LEU 2 0.04 SER 50 -0.35 ALA 1

LEU 2 0.03 ASP 51 -0.36 ALA 1

LEU 2 0.03 PHE 52 -0.34 ALA 1

LEU 2 0.03 ASP 53 -0.46 ALA 1

LEU 2 0.03 ALA 54 -0.53 ALA 1

LEU 2 0.04 LEU 55 -0.47 ALA 1

LEU 2 0.03 ILE 56 -0.56 ALA 1

LEU 2 0.02 PRO 57 -0.71 ALA 1

LEU 2 0.03 SER 58 -0.67 ALA 1

LEU 2 0.04 LEU 59 -0.64 ALA 1

LEU 2 0.02 LYS 60 -0.83 ALA 1

GLY 24 0.02 ALA 61 -0.94 ALA 1

LEU 2 0.02 LYS 62 -0.82 ALA 1

LEU 2 0.04 LYS 63 -0.68 ALA 1

LEU 2 0.06 ILE 64 -0.49 ALA 1

LEU 2 0.10 ASP 65 -0.40 ALA 1

LEU 2 0.08 ALA 66 -0.25 ALA 1

LEU 2 0.07 ILE 67 -0.22 ALA 1

LEU 2 0.07 ILE 68 -0.06 ALA 1

LEU 2 0.06 SER 69 -0.10 ALA 1

LEU 2 0.05 SER 70 -0.05 ALA 1

LEU 2 0.04 LEU 71 -0.16 ALA 1

LEU 2 0.04 SER 72 -0.15 ALA 1

LEU 2 0.03 ILE 73 -0.17 ALA 1

LEU 2 0.02 THR 74 -0.26 ALA 1

LEU 2 0.01 ASP 75 -0.32 ALA 1

ALA 54 0.02 LYS 76 -0.43 ALA 1

LEU 2 0.02 ARG 77 -0.43 ALA 1

LEU 2 0.01 GLN 78 -0.41 ALA 1

ALA 54 0.01 GLN 79 -0.55 ALA 1

LEU 2 0.01 GLU 80 -0.63 ALA 1

LEU 2 0.02 ILE 81 -0.53 ALA 1

LEU 2 0.02 ALA 82 -0.36 ALA 1

LEU 2 0.04 PHE 83 -0.16 ALA 1

LEU 2 0.05 SER 84 -0.06 GLN 4

ALA 1 0.15 ASP 85 -0.05 GLN 4

ALA 1 0.14 LYS 86 -0.03 GLN 4

ALA 1 0.20 LEU 87 -0.02 GLN 4

ALA 1 0.18 TYR 88 -0.01 GLN 4

ALA 1 0.11 ALA 89 -0.02 GLN 4

LEU 2 0.04 ALA 90 -0.01 GLN 4

LEU 2 0.03 ASP 91 -0.01 ALA 1

LEU 2 0.03 SER 92 -0.08 ALA 1

LEU 2 0.03 ARG 93 -0.06 ALA 1

LEU 2 0.03 LEU 94 -0.09 ALA 1

LEU 2 0.03 ILE 95 -0.07 ALA 1

LEU 2 0.02 ALA 96 -0.08 ALA 1

LEU 2 0.02 ALA 97 -0.06 ALA 1

ASP 232 0.03 LYS 98 -0.01 ALA 1

ASP 232 0.03 GLY 99 -0.02 ALA 1

ASP 232 0.02 SER 100 -0.06 ALA 1

PHE 233 0.03 PRO 101 -0.08 ALA 1

PHE 233 0.02 ILE 102 -0.11 ALA 1

PHE 233 0.03 GLN 103 -0.10 ALA 1

PHE 233 0.02 PRO 104 -0.13 ALA 1

PHE 233 0.02 THR 105 -0.16 ALA 1

PHE 233 0.02 LEU 106 -0.21 ALA 1

PHE 233 0.02 GLU 107 -0.19 ALA 1

PHE 233 0.02 SER 108 -0.16 ALA 1

PHE 233 0.02 LEU 109 -0.19 ALA 1

PHE 233 0.02 LYS 110 -0.23 ALA 1

PHE 233 0.02 GLY 111 -0.24 ALA 1

PHE 233 0.02 LYS 112 -0.22 ALA 1

LEU 2 0.02 HIS 113 -0.24 ALA 1

LEU 2 0.02 VAL 114 -0.23 ALA 1

LEU 2 0.02 GLY 115 -0.24 ALA 1

LEU 2 0.02 VAL 116 -0.26 ALA 1

LEU 2 0.02 LEU 117 -0.28 ALA 1

LEU 2 0.02 GLN 118 -0.38 ALA 1

LEU 2 0.02 GLY 119 -0.41 ALA 1

LEU 2 0.02 SER 120 -0.31 ALA 1

LEU 2 0.02 THR 121 -0.28 ALA 1

LEU 2 0.02 GLN 122 -0.25 ALA 1

LEU 2 0.02 GLU 123 -0.33 ALA 1

LEU 2 0.01 ALA 124 -0.36 ALA 1

LEU 2 0.01 TYR 125 -0.29 ALA 1

LEU 2 0.01 ALA 126 -0.29 ALA 1

LYS 186 0.01 ASN 127 -0.36 ALA 1

LYS 186 0.02 ASP 128 -0.36 ALA 1

LYS 186 0.02 ASN 129 -0.30 ALA 1

PHE 233 0.02 TRP 130 -0.29 ALA 1

PHE 233 0.01 ARG 131 -0.34 ALA 1

LYS 186 0.01 THR 132 -0.37 ALA 1

PHE 233 0.01 LYS 133 -0.31 ALA 1

PHE 233 0.01 GLY 134 -0.31 ALA 1

PHE 233 0.02 VAL 135 -0.28 ALA 1

PHE 233 0.01 ASP 136 -0.30 ALA 1

LEU 2 0.01 VAL 137 -0.31 ALA 1

LEU 2 0.02 VAL 138 -0.32 ALA 1

LEU 2 0.02 ALA 139 -0.35 ALA 1

LEU 2 0.02 TYR 140 -0.32 ALA 1

LEU 2 0.03 ALA 141 -0.35 ALA 1

LEU 2 0.03 ASN 142 -0.25 ALA 1

LEU 2 0.03 GLN 143 -0.18 ALA 1

LEU 2 0.03 ASP 144 -0.14 ALA 1

LEU 2 0.03 LEU 145 -0.20 ALA 1

LEU 2 0.03 ILE 146 -0.19 ALA 1

LEU 2 0.03 TYR 147 -0.12 ALA 1

LEU 2 0.03 SER 148 -0.14 ALA 1

LEU 2 0.02 ASP 149 -0.18 ALA 1

LEU 2 0.03 LEU 150 -0.14 ALA 1

LEU 2 0.03 THR 151 -0.10 ALA 1

LEU 2 0.02 ALA 152 -0.14 ALA 1

LEU 2 0.02 GLY 153 -0.15 ALA 1

LEU 2 0.02 ARG 154 -0.20 ALA 1

LEU 2 0.02 LEU 155 -0.19 ALA 1

LEU 2 0.02 ASP 156 -0.16 ALA 1

LEU 2 0.02 ALA 157 -0.15 ALA 1

LEU 2 0.02 ALA 158 -0.16 ALA 1

LEU 2 0.02 LEU 159 -0.16 ALA 1

LEU 2 0.03 GLN 160 -0.13 ALA 1

LEU 2 0.03 ASP 161 -0.06 ALA 1

LEU 2 0.04 GLU 162 -0.01 PRO 3

ALA 1 0.08 VAL 163 -0.01 ALA 22

LEU 2 0.04 ALA 164 -0.02 PRO 3

LEU 2 0.04 ALA 165 -0.02 PRO 3

ALA 1 0.07 SER 166 -0.01 PRO 3

ALA 1 0.11 GLU 167 -0.02 ALA 22

ALA 1 0.05 GLY 168 -0.01 PRO 3

LEU 2 0.04 PHE 169 -0.02 PRO 3

ALA 1 0.05 LEU 170 -0.01 PRO 3

ALA 1 0.11 LYS 171 -0.01 ALA 22

ALA 1 0.09 GLN 172 -0.01 ALA 22

ALA 1 0.07 PRO 173 -0.01 PRO 3

LEU 2 0.03 ALA 174 -0.02 PRO 3

LEU 2 0.03 GLY 175 -0.02 PRO 3

ALA 1 0.05 LYS 176 -0.01 PRO 3

LEU 2 0.03 GLU 177 -0.01 PRO 3

LEU 2 0.03 TYR 178 -0.02 PRO 3

ASP 232 0.03 ALA 179 -0.01 PRO 3

PHE 233 0.03 PHE 180 -0.01 PRO 3

PHE 233 0.03 ALA 181 -0.05 ALA 1

PHE 233 0.03 GLY 182 -0.03 ALA 1

PHE 233 0.04 PRO 183 -0.01 PRO 3

PHE 233 0.03 SER 184 -0.02 ALA 1

LEU 2 0.02 VAL 185 -0.09 ALA 1

LEU 2 0.02 LYS 186 -0.08 ALA 1

LEU 2 0.02 ASP 187 -0.15 ALA 1

LEU 2 0.02 LYS 188 -0.15 ALA 1

LEU 2 0.02 LYS 189 -0.24 ALA 1

LEU 2 0.02 TYR 190 -0.25 ALA 1

LEU 2 0.02 PHE 191 -0.17 ALA 1

LEU 2 0.02 GLY 192 -0.15 ALA 1

LEU 2 0.03 ASP 193 -0.04 ALA 1

LEU 2 0.04 GLY 194 -0.02 GLN 4

LEU 2 0.04 THR 195 -0.02 GLN 4

LEU 2 0.05 GLY 196 -0.03 GLN 4

LEU 2 0.06 VAL 197 -0.05 ALA 1

LEU 2 0.05 GLY 198 -0.26 ALA 1

LEU 2 0.05 LEU 199 -0.36 ALA 1

LEU 2 0.02 ARG 200 -0.59 ALA 1

GLY 24 0.01 LYS 201 -0.58 ALA 1

GLY 24 0.01 ASP 202 -0.65 ALA 1

THR 204 0.01 ASP 203 -0.43 ALA 1

PRO 3 0.03 THR 204 -0.22 ALA 1

PRO 3 0.11 GLU 205 -0.10 GLN 4

LEU 2 0.07 LEU 206 -0.14 GLN 4

LEU 2 0.04 LYS 207 -0.10 GLN 4

ALA 1 0.24 ALA 208 -0.09 GLN 4

ALA 1 0.40 ALA 209 -0.09 GLN 4

ALA 1 0.31 PHE 210 -0.07 GLN 4

ALA 1 0.35 ASP 211 -0.06 GLN 4

ALA 1 0.59 LYS 212 -0.06 GLN 4

ALA 1 0.64 ALA 213 -0.04 GLN 4

ALA 1 0.50 LEU 214 -0.04 GLN 4

ALA 1 0.60 THR 215 -0.04 GLN 4

ALA 1 0.79 GLU 216 -0.03 GLN 4

ALA 1 0.70 LEU 217 -0.02 GLN 4

ALA 1 0.60 ARG 218 -0.02 GLN 4

ALA 1 0.72 GLN 219 -0.02 GLN 4

ALA 1 0.81 ASP 220 -0.02 ALA 22

ALA 1 0.69 GLY 221 -0.02 ALA 22

ALA 1 0.67 THR 222 -0.02 ALA 22

ALA 1 0.53 TYR 223 -0.02 ALA 22

ALA 1 0.51 ASP 224 -0.02 ALA 22

ALA 1 0.56 LYS 225 -0.03 ALA 22

ALA 1 0.48 MET 226 -0.03 ALA 22

ALA 1 0.39 ALA 227 -0.03 ALA 22

ALA 1 0.41 LYS 228 -0.03 ALA 22

ALA 1 0.38 LYS 229 -0.04 ALA 22

ALA 1 0.29 TYR 230 -0.03 ALA 22

ALA 1 0.29 PHE 231 -0.03 ALA 22

ALA 1 0.31 ASP 232 -0.03 ALA 22

ALA 1 0.29 PHE 233 -0.02 ALA 22

ALA 1 0.31 ASN 234 -0.02 ALA 22

ALA 1 0.24 VAL 235 -0.02 ALA 22

ALA 1 0.27 TYR 236 -0.01 ALA 22

ALA 1 0.22 GLY 237 -0.01 GLN 4

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 2604241152241960399

--- 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.

* *