CNRS Nantes University US2B US2B
home |  start a new run |  job status |  references&downloads |  examples |  help  

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 260812234030702023

---  normal mode 8  ---

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 increasereflargest decrease
GLU 157 0.06 PRO 1 -0.08 ASN 109
GLU 157 0.07 GLY 2 -0.07 ASN 109
GLU 157 0.08 SER 3 -0.06 ASN 109
GLU 157 0.09 SER 4 -0.05 ASN 109
GLU 157 0.09 GLY 5 -0.06 ASN 109
PRO 212 0.10 LEU 6 -0.05 ASN 109
PRO 212 0.11 PRO 7 -0.05 ASN 109
PRO 212 0.11 PRO 8 -0.05 ASN 109
PRO 212 0.13 GLU 9 -0.04 GLU 197
PRO 212 0.14 LYS 10 -0.03 GLU 197
PRO 212 0.13 PRO 11 -0.04 GLU 197
PRO 212 0.16 LYS 12 -0.03 GLU 197
PRO 212 0.17 ASN 13 -0.02 GLU 197
PRO 212 0.14 LEU 14 -0.04 GLU 197
PRO 212 0.13 SER 15 -0.05 GLU 197
PRO 212 0.11 CYS 16 -0.06 GLU 197
PRO 212 0.10 ILE 17 -0.07 GLU 197
PRO 212 0.08 VAL 18 -0.08 ASN 109
PRO 212 0.06 ASN 19 -0.10 ASN 109
PRO 212 0.05 GLU 20 -0.10 ASN 109
TYR 72 0.03 GLY 21 -0.14 ASN 109
PRO 212 0.02 LYS 22 -0.13 ASN 109
PRO 212 0.03 LYS 23 -0.12 ASN 109
PRO 212 0.06 MET 24 -0.09 ASN 109
PRO 212 0.06 ARG 25 -0.09 ASN 109
PRO 212 0.09 CYS 26 -0.07 GLU 197
PRO 212 0.10 GLU 27 -0.07 GLU 197
PRO 212 0.12 TRP 28 -0.05 GLU 197
PRO 212 0.13 ASP 29 -0.05 GLU 197
PRO 212 0.11 GLY 30 -0.05 GLU 197
PRO 212 0.13 GLY 31 -0.04 GLU 197
PRO 212 0.12 ARG 32 -0.04 GLU 197
GLU 157 0.09 GLU 33 -0.06 GLU 197
GLU 157 0.09 THR 34 -0.06 ASN 109
GLU 157 0.08 HIS 35 -0.07 ASN 109
GLU 157 0.07 LEU 36 -0.08 ASN 109
GLU 157 0.06 GLU 37 -0.09 ASN 109
GLU 157 0.07 THR 38 -0.08 ASN 109
GLU 157 0.06 ASN 39 -0.09 ASN 109
GLU 157 0.07 PHE 40 -0.08 ASN 109
PRO 212 0.07 THR 41 -0.08 ASN 109
PRO 212 0.08 LEU 42 -0.08 ASN 109
PRO 212 0.09 LYS 43 -0.07 ASN 109
PRO 212 0.09 SER 44 -0.06 ASN 109
PRO 212 0.10 GLU 45 -0.06 ASN 109
PRO 212 0.10 TRP 46 -0.05 ASN 109
PRO 212 0.12 ALA 47 -0.04 ASN 109
PRO 212 0.10 THR 48 -0.04 ASN 109
PRO 212 0.08 HIS 49 -0.06 ASN 109
PRO 212 0.08 LYS 50 -0.06 ASN 109
PRO 212 0.06 PHE 51 -0.08 ASN 109
PRO 212 0.05 ALA 52 -0.09 ASN 109
PRO 212 0.05 ASP 53 -0.09 ASN 109
PRO 212 0.05 CYS 54 -0.10 ASN 109
GLU 157 0.04 LYS 55 -0.11 ASN 109
GLU 157 0.05 ALA 56 -0.11 ASN 109
GLU 157 0.03 LYS 57 -0.12 ASN 109
GLU 157 0.04 ARG 58 -0.12 ASN 109
GLU 157 0.03 ASP 59 -0.13 ASN 109
GLU 157 0.04 THR 60 -0.11 GLU 197
GLU 157 0.06 PRO 61 -0.09 ASN 109
GLU 157 0.08 THR 62 -0.08 GLU 197
GLU 157 0.06 SER 63 -0.09 GLU 197
PRO 212 0.05 CYS 64 -0.10 ASN 109
PRO 212 0.04 THR 65 -0.12 ASN 109
PRO 212 0.04 VAL 66 -0.11 ASN 109
CYS 16 0.03 ASP 67 -0.12 ASN 109
PRO 212 0.03 TYR 68 -0.11 ASN 109
PRO 212 0.03 SER 69 -0.12 SER 130
PRO 212 0.06 THR 70 -0.10 SER 130
PRO 212 0.07 VAL 71 -0.07 SER 130
PRO 212 0.10 TYR 72 -0.04 ASN 109
PRO 212 0.12 PHE 73 -0.02 ALA 199
PRO 212 0.12 VAL 74 -0.03 ASN 109
PRO 212 0.13 ASN 75 -0.03 GLU 197
PRO 212 0.12 ILE 76 -0.04 ASN 109
PRO 212 0.13 GLU 77 -0.04 ASN 109
PRO 212 0.12 VAL 78 -0.05 ASN 109
PRO 212 0.12 TRP 79 -0.05 ASN 109
PRO 212 0.11 VAL 80 -0.06 ASN 109
PRO 212 0.10 GLU 81 -0.06 ASN 109
PRO 212 0.09 ALA 82 -0.06 ASN 109
PRO 212 0.08 GLU 83 -0.07 ASN 109
GLU 157 0.07 ASN 84 -0.07 ASN 109
GLU 157 0.07 ALA 85 -0.07 ASN 109
PRO 212 0.09 LEU 86 -0.05 ASN 109
PRO 212 0.10 GLY 87 -0.05 ASN 109
PRO 212 0.10 LYS 88 -0.05 ASN 109
PRO 212 0.12 VAL 89 -0.04 ASN 109
PRO 212 0.13 THR 90 -0.04 ASN 109
PRO 212 0.14 SER 91 -0.04 GLU 197
PRO 212 0.16 ASP 92 -0.03 GLU 197
PRO 212 0.15 HIS 93 -0.03 GLU 197
PRO 212 0.16 ILE 94 -0.03 GLU 197
PRO 212 0.16 ASN 95 -0.03 GLU 197
PRO 212 0.15 PHE 96 -0.03 GLU 197
PRO 212 0.14 ASP 97 -0.03 GLU 197
PRO 212 0.12 PRO 98 -0.04 ASN 109
PRO 212 0.13 VAL 99 -0.03 ALA 199
PRO 212 0.15 TYR 100 -0.03 GLU 197
PRO 212 0.13 LYS 101 -0.04 GLU 197
PRO 212 0.11 VAL 102 -0.05 GLU 197
PRO 212 0.10 LYS 103 -0.06 GLU 197
PRO 212 0.08 PRO 104 -0.07 HIS 108
PRO 212 0.05 ASN 105 -0.10 HIS 108
PRO 129 0.07 PRO 106 -0.08 ALA 199
PRO 212 0.06 PRO 107 -0.10 GLY 21
SER 196 0.04 HIS 108 -0.13 GLY 21
TRP 126 0.03 ASN 109 -0.14 GLY 21
TRP 126 0.03 LEU 110 -0.12 SER 111
LEU 124 0.02 SER 111 -0.13 PHE 214
LEU 124 0.03 VAL 112 -0.12 PHE 214
GLY 201 0.04 ILE 113 -0.12 PHE 214
ASP 158 0.06 ASN 114 -0.11 PHE 214
PRO 208 0.09 SER 115 -0.08 GLY 21
PRO 208 0.14 GLU 116 -0.06 GLY 21
PRO 208 0.09 GLU 117 -0.07 GLY 21
PRO 208 0.20 LEU 118 -0.05 GLY 21
PRO 208 0.12 SER 119 -0.04 GLY 21
SER 209 0.21 SER 120 -0.03 LYS 172
PRO 208 0.18 ILE 121 -0.04 GLY 21
PRO 208 0.11 LEU 122 -0.06 GLY 21
PRO 212 0.10 LYS 123 -0.07 GLY 21
PRO 212 0.09 LEU 124 -0.08 GLY 21
PRO 212 0.06 THR 125 -0.09 GLY 21
PRO 212 0.05 TRP 126 -0.12 GLY 21
PRO 212 0.04 THR 127 -0.12 GLY 21
PRO 212 0.07 ASN 128 -0.11 GLY 21
PRO 106 0.07 PRO 129 -0.13 GLY 21
PRO 212 0.05 SER 130 -0.12 SER 69
PRO 212 0.08 ILE 131 -0.10 SER 69
PRO 212 0.10 LYS 132 -0.07 SER 69
PRO 212 0.10 SER 133 -0.08 SER 69
PRO 212 0.11 VAL 134 -0.06 SER 69
PRO 212 0.13 ILE 135 -0.04 SER 69
PRO 212 0.16 ILE 136 -0.04 SER 69
PRO 212 0.16 LEU 137 -0.04 SER 69
PRO 212 0.19 LYS 138 -0.02 SER 69
PRO 212 0.17 TYR 139 -0.03 ALA 160
PRO 212 0.18 ASN 140 -0.02 ALA 160
PRO 212 0.16 ILE 141 -0.03 GLY 21
PRO 212 0.15 GLN 142 -0.02 GLN 153
PRO 212 0.12 TYR 143 -0.03 GLY 21
PRO 212 0.09 ARG 144 -0.03 GLY 21
ASN 13 0.05 THR 145 -0.06 PHE 214
ASN 13 0.02 LYS 146 -0.12 PHE 214
ASN 13 0.03 ASP 147 -0.10 PHE 214
ASN 13 0.06 ALA 148 -0.04 PHE 214
ARG 32 0.06 SER 149 -0.03 PHE 214
PRO 212 0.10 THR 150 -0.03 GLN 153
PRO 212 0.12 TRP 151 -0.03 GLN 153
PRO 212 0.18 SER 152 -0.03 PHE 166
PRO 212 0.21 GLN 153 -0.03 TRP 151
PRO 212 0.25 ILE 154 -0.03 SER 152
PRO 212 0.29 PRO 155 -0.03 THR 150
PRO 212 0.25 PRO 156 -0.02 ALA 160
PRO 212 0.29 GLU 157 -0.03 SER 161
PRO 212 0.29 ASP 158 -0.03 ARG 163
PRO 212 0.23 THR 159 -0.03 GLY 21
PRO 212 0.23 ALA 160 -0.03 TYR 139
PRO 212 0.21 SER 161 -0.03 SER 69
PRO 212 0.16 THR 162 -0.05 SER 69
PRO 212 0.15 ARG 163 -0.06 GLY 21
PRO 212 0.11 SER 164 -0.08 GLY 21
PRO 212 0.12 SER 165 -0.07 GLY 21
PRO 212 0.17 PHE 166 -0.05 GLY 21
PRO 212 0.18 THR 167 -0.04 GLY 21
PRO 212 0.20 VAL 168 -0.03 GLY 21
PRO 212 0.26 GLN 169 -0.03 LYS 123
PRO 212 0.31 ASP 170 -0.04 LEU 171
SER 209 0.20 LEU 171 -0.04 ASP 170
SER 209 0.17 LYS 172 -0.03 SER 120
PRO 155 0.12 PRO 173 -0.04 PHE 214
PRO 155 0.07 PHE 174 -0.17 LYS 210
PRO 155 0.06 THR 175 -0.13 PHE 214
PRO 155 0.04 GLU 176 -0.15 PHE 214
ASN 13 0.04 TYR 177 -0.09 PHE 214
SER 200 0.04 VAL 178 -0.09 PHE 214
PRO 212 0.06 PHE 179 -0.06 ASP 59
PRO 212 0.07 ARG 180 -0.06 ASP 59
PRO 212 0.10 ILE 181 -0.04 GLY 21
PRO 212 0.11 ARG 182 -0.04 ALA 199
PRO 212 0.13 CYS 183 -0.03 ALA 199
PRO 212 0.14 MET 184 -0.03 ALA 199
PRO 212 0.16 LYS 185 -0.02 MET 184
PRO 212 0.20 GLU 186 -0.02 ILE 135
PRO 212 0.22 ASP 187 -0.02 TRP 195
PRO 212 0.20 GLY 188 -0.03 TRP 195
PRO 212 0.18 LYS 189 -0.03 GLU 197
PRO 212 0.15 GLY 190 -0.04 GLU 197
PRO 212 0.13 TYR 191 -0.06 GLU 197
PRO 212 0.13 TRP 192 -0.06 SER 193
PRO 212 0.09 SER 193 -0.06 TRP 192
PRO 212 0.07 ASP 194 -0.09 GLU 197
PRO 212 0.06 TRP 195 -0.06 ALA 199
HIS 108 0.04 SER 196 -0.09 ALA 199
HIS 108 0.03 GLU 197 -0.12 ASP 59
LEU 110 0.03 GLU 198 -0.11 PHE 214
SER 111 0.02 ALA 199 -0.13 PHE 214
VAL 178 0.04 SER 200 -0.15 PHE 214
ILE 113 0.04 GLY 201 -0.15 PHE 214
PRO 155 0.05 ILE 202 -0.18 PHE 214
PRO 155 0.06 THR 203 -0.11 PHE 214
PRO 155 0.07 TYR 204 -0.17 GLU 205
PRO 155 0.09 GLU 205 -0.18 LYS 210
ASP 170 0.15 ASP 206 -0.09 TYR 204
ASP 170 0.16 ARG 207 -0.09 TYR 204
ASP 170 0.27 PRO 208 -0.04 PHE 174
ASP 170 0.30 SER 209 -0.07 PHE 174
ASP 170 0.16 LYS 210 -0.18 GLU 205
ASP 170 0.20 GLU 211 -0.11 GLU 205
ASP 170 0.31 PRO 212 -0.07 PHE 174
ASP 170 0.24 SER 213 -0.13 PHE 174
PRO 155 0.18 PHE 214 -0.18 ILE 202
GLU 157 0.25 TRP 215 -0.10 ILE 202

If you find results from this site helpful for your research, please cite one of our papers:

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.