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 hacked on november 27th.
It has been moved away and runs again.
**Still some additional cleaning from time to time**
Sorry for the inconvenience.


***  FXIa G216A  ***

CA distance fluctuations for 2602051414582688829

---  normal mode 20  ---

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
PRO 23 0.31 ILE 1 -0.09 ARG 215
PRO 23 0.33 VAL 2 -0.22 LYS 136
PRO 23 0.29 GLY 3 -0.22 ASN 197
PRO 23 0.25 GLY 4 -0.16 ASN 197
PRO 23 0.21 THR 5 -0.11 ASN 197
ASP 70 0.19 ALA 6 -0.12 SER 7
GLU 198 0.18 SER 7 -0.12 ALA 6
GLU 198 0.29 VAL 8 -0.15 GLY 10
GLU 198 0.43 ARG 9 -0.09 ALA 6
GLU 198 0.56 GLY 10 -0.15 VAL 8
GLU 198 0.42 GLU 11 -0.13 PRO 13
GLU 198 0.39 TRP 12 -0.13 PRO 111
GLU 198 0.48 PRO 13 -0.13 GLU 11
GLU 198 0.40 TRP 14 -0.11 TRP 12
GLU 198 0.33 GLN 15 -0.05 ALA 6
GLU 198 0.29 VAL 16 -0.05 TYR 105
VAL 238 0.27 THR 17 -0.06 GLY 186
VAL 238 0.30 LEU 18 -0.05 TYR 47
VAL 238 0.33 HIS 19 -0.05 THR 106
VAL 238 0.33 THR 20 -0.08 ASP 70
VAL 238 0.34 THR 21 -0.49 PRO 23
LYS 140 0.36 SER 22 -0.29 PRO 23
LYS 140 0.70 PRO 23 -0.49 THR 21
LYS 140 0.47 THR 24 -0.38 GLN 25
VAL 238 0.35 GLN 25 -0.38 THR 24
LYS 140 0.31 ARG 26 -0.10 SER 65
VAL 238 0.27 HIS 27 -0.05 SER 65
PRO 23 0.31 LEU 28 -0.04 ALA 237
PRO 23 0.26 CYS 29 -0.05 ALA 237
GLU 198 0.18 GLY 30 -0.08 GLY 186
GLU 198 0.19 GLY 31 -0.05 GLY 211
ASN 197 0.26 SER 32 -0.06 TRP 12
ASN 197 0.37 ILE 33 -0.08 TRP 12
ASN 197 0.37 ILE 34 -0.09 TRP 12
ALA 237 0.48 GLY 35 -0.07 ASP 70
ALA 237 0.57 ASN 36 -0.11 GLN 37
VAL 238 0.51 GLN 37 -0.11 ASN 36
ASN 197 0.31 TRP 38 -0.09 ASP 70
ASN 197 0.27 ILE 39 -0.08 ASP 70
ASN 197 0.19 LEU 40 -0.06 GLY 211
PRO 23 0.13 THR 41 -0.11 ALA 237
PRO 23 0.21 ALA 42 -0.23 ALA 237
PRO 23 0.22 ALA 43 -0.34 ALA 237
PRO 23 0.34 HIS 44 -0.30 ALA 237
PRO 23 0.32 CYS 45 -0.20 ALA 237
PRO 23 0.25 PHE 46 -0.24 ALA 237
PRO 23 0.39 TYR 47 -0.32 ALA 237
PRO 23 0.41 GLY 48 -0.30 ALA 237
LYS 140 0.28 VAL 49 -0.23 ALA 237
LYS 140 0.24 GLU 50 -0.30 SER 51
VAL 238 0.30 SER 51 -0.30 GLU 50
VAL 238 0.39 PRO 52 -0.22 ASP 70
VAL 238 0.46 LYS 53 -0.36 PRO 23
VAL 238 0.37 ILE 54 -0.37 PRO 23
VAL 238 0.40 LEU 55 -0.22 PRO 23
VAL 238 0.45 ARG 56 -0.24 PRO 23
VAL 238 0.42 VAL 57 -0.15 PRO 23
VAL 238 0.39 TYR 58 -0.14 PRO 23
GLU 198 0.38 SER 59 -0.10 PRO 23
GLU 198 0.44 GLY 60 -0.12 THR 106
GLU 198 0.37 ILE 61 -0.10 THR 24
GLU 198 0.33 LEU 62 -0.10 THR 144
ASP 70 0.27 ASN 63 -0.08 THR 106
ASP 70 0.30 GLN 64 -0.07 THR 106
ASP 70 0.38 SER 65 -0.17 THR 24
ASP 70 0.41 GLU 66 -0.20 THR 24
VAL 238 0.32 ILE 67 -0.20 THR 71
GLU 69 0.45 LYS 68 -0.41 THR 71
LYS 68 0.45 GLU 69 -0.45 PRO 23
GLU 66 0.41 ASP 70 -0.44 PRO 23
VAL 238 0.42 THR 71 -0.41 LYS 68
VAL 238 0.49 SER 72 -0.37 ASP 70
VAL 238 0.51 PHE 73 -0.29 PRO 23
VAL 238 0.58 PHE 74 -0.26 PRO 23
VAL 238 0.62 GLY 75 -0.29 PRO 23
VAL 238 0.56 VAL 76 -0.21 ASP 70
VAL 238 0.60 GLN 77 -0.17 ASP 70
VAL 238 0.42 GLU 78 -0.16 ASP 70
VAL 238 0.24 ILE 79 -0.24 ALA 237
ASN 197 0.13 ILE 80 -0.44 ALA 237
LYS 140 0.12 ILE 81 -0.52 ALA 237
PRO 23 0.11 HIS 82 -0.66 ALA 237
PRO 23 0.12 ASP 83 -0.81 ALA 237
PRO 23 0.19 GLN 84 -0.71 ALA 237
PRO 23 0.23 TYR 85 -0.60 ALA 237
PRO 23 0.34 LYS 86 -0.53 ALA 237
PRO 23 0.40 MET 87 -0.43 ALA 237
PRO 23 0.36 ALA 88 -0.35 ALA 237
PRO 23 0.39 GLU 89 -0.36 ALA 237
PRO 23 0.34 SER 90 -0.44 ALA 237
PRO 23 0.27 GLY 91 -0.43 ALA 237
PRO 23 0.22 TYR 92 -0.50 ALA 237
PRO 23 0.24 ASP 93 -0.38 ALA 237
PRO 23 0.17 ILE 94 -0.35 ALA 237
LYS 140 0.11 ALA 95 -0.31 ALA 237
ASN 197 0.17 LEU 96 -0.16 ALA 237
VAL 238 0.29 LEU 97 -0.11 ASP 70
VAL 238 0.48 LYS 98 -0.12 ASP 70
VAL 238 0.65 LEU 99 -0.17 ASP 70
VAL 238 0.83 GLU 100 -0.21 PRO 23
VAL 238 0.83 THR 101 -0.23 PRO 23
VAL 238 0.67 THR 102 -0.18 PRO 23
VAL 238 0.54 VAL 103 -0.19 ASP 70
ALA 237 0.57 ASN 104 -0.24 ASP 70
ASN 197 0.64 TYR 105 -0.15 PRO 23
GLU 198 0.73 THR 106 -0.16 LYS 68
GLU 198 0.78 ASP 107 -0.10 LYS 53
GLU 198 0.61 SER 108 -0.10 VAL 8
GLU 198 0.51 GLN 109 -0.11 VAL 8
GLU 198 0.58 ARG 110 -0.10 PRO 111
ASN 197 0.51 PRO 111 -0.13 TRP 12
ASN 197 0.46 ILE 112 -0.09 GLU 11
ASN 197 0.41 SER 113 -0.15 TRP 200
ASN 197 0.23 LEU 114 -0.14 VAL 238
LEU 114 0.20 PRO 115 -0.19 VAL 238
GLY 118 0.24 SER 116 -0.25 VAL 238
ASN 104 0.17 LYS 117 -0.34 VAL 238
SER 116 0.24 GLY 118 -0.30 GLY 164
ASN 121 0.39 ASP 119 -0.26 GLY 164
THR 106 0.18 ARG 120 -0.31 GLY 164
ASP 119 0.39 ASN 121 -0.49 LYS 166
THR 106 0.29 VAL 122 -0.38 LYS 166
ASP 107 0.22 ILE 123 -0.49 ASN 197
CYS 194 0.30 TYR 124 -0.53 ASN 197
ASP 107 0.21 THR 125 -0.58 ASN 197
ASP 107 0.22 ASP 126 -0.46 ASN 197
PRO 23 0.16 CYS 127 -0.29 ASN 197
PRO 23 0.17 TRP 128 -0.15 ASN 197
PRO 23 0.20 VAL 129 -0.10 LYS 136
PRO 23 0.20 THR 130 -0.07 LYS 136
PRO 23 0.22 GLY 131 -0.06 ARG 215
PRO 23 0.26 TRP 132 -0.07 ARG 215
PRO 23 0.39 GLY 133 -0.09 ARG 215
PRO 23 0.45 TYR 134 -0.13 ARG 215
PRO 23 0.41 ARG 135 -0.16 ARG 215
PRO 23 0.49 LYS 136 -0.29 ARG 215
PRO 23 0.55 LEU 137 -0.29 ARG 215
PRO 23 0.62 ARG 138 -0.24 ARG 215
PRO 23 0.63 ASP 139 -0.21 ARG 215
PRO 23 0.70 LYS 140 -0.20 GLN 142
PRO 23 0.43 ILE 141 -0.09 ARG 215
PRO 23 0.31 GLN 142 -0.20 LYS 140
ASP 70 0.28 ASN 143 -0.12 LYS 140
ASP 70 0.23 THR 144 -0.11 LYS 140
ASP 70 0.18 LEU 145 -0.07 THR 106
PRO 23 0.21 GLN 146 -0.08 LYS 140
PRO 23 0.19 LYS 147 -0.08 SER 113
PRO 23 0.21 ALA 148 -0.18 ASN 197
PRO 23 0.19 LYS 149 -0.28 ASN 197
PRO 23 0.20 ILE 150 -0.33 ASN 197
PRO 23 0.20 PRO 151 -0.44 ASN 197
PRO 23 0.19 LEU 152 -0.41 ASN 197
PRO 23 0.22 VAL 153 -0.40 ASN 197
PRO 23 0.21 THR 154 -0.38 ASN 197
PRO 23 0.23 ASN 155 -0.45 ASN 121
HIS 169 0.24 GLU 156 -0.41 ASN 121
PRO 23 0.24 GLU 157 -0.35 ASN 197
PRO 23 0.26 CYS 158 -0.32 ASN 121
PRO 23 0.30 GLN 159 -0.39 ASN 121
PRO 23 0.25 LYS 160 -0.28 ASN 197
PRO 23 0.28 ARG 161 -0.27 ASN 197
PRO 23 0.31 TYR 162 -0.29 ASN 121
PRO 23 0.35 ARG 163 -0.32 ASN 121
GLU 210 0.48 GLY 164 -0.57 HIS 165
PRO 23 0.40 HIS 165 -0.57 GLY 164
PRO 23 0.36 LYS 166 -0.55 GLY 164
PRO 23 0.29 ILE 167 -0.45 GLY 164
PRO 23 0.26 THR 168 -0.48 ASN 121
GLU 156 0.24 HIS 169 -0.46 ASN 121
PRO 23 0.20 LYS 170 -0.35 ALA 237
PRO 23 0.23 MET 171 -0.30 ASN 121
PRO 23 0.21 ILE 172 -0.28 ASN 121
PRO 23 0.24 CYS 173 -0.28 ASN 197
PRO 23 0.23 ALA 174 -0.30 ASN 197
PRO 23 0.25 GLY 175 -0.32 ASN 197
PRO 23 0.24 TYR 176 -0.36 ASN 197
PRO 23 0.24 ARG 177 -0.35 ASN 197
GLY 164 0.27 GLU 178 -0.33 ASN 197
PRO 23 0.28 GLY 179 -0.30 ASN 197
PRO 23 0.29 GLY 180 -0.28 ASN 197
PRO 23 0.27 LYS 181 -0.26 ASN 197
PRO 23 0.30 ASP 182 -0.21 ASN 197
PRO 23 0.32 ALA 183 -0.12 ASN 197
PRO 23 0.40 CYS 184 -0.11 ARG 215
PRO 23 0.48 LYS 185 -0.11 ALA 237
PRO 23 0.44 GLY 186 -0.08 GLY 30
PRO 23 0.32 ASP 187 -0.07 ALA 237
PRO 23 0.32 SER 188 -0.13 ALA 237
PRO 23 0.22 GLY 189 -0.11 ALA 237
PRO 23 0.19 GLY 190 -0.06 GLY 211
PRO 23 0.17 PRO 191 -0.06 VAL 129
PRO 23 0.17 LEU 192 -0.09 LYS 136
TYR 124 0.17 SER 193 -0.10 SER 113
TYR 124 0.30 CYS 194 -0.21 LYS 195
ASP 107 0.29 LYS 195 -0.21 CYS 194
ASP 107 0.35 HIS 196 -0.47 GLU 198
VAL 199 0.74 ASN 197 -0.58 THR 125
ASP 107 0.78 GLU 198 -0.47 HIS 196
ASN 197 0.74 VAL 199 -0.12 LYS 166
ASN 197 0.35 TRP 200 -0.15 SER 113
VAL 122 0.24 HIS 201 -0.13 LYS 195
VAL 122 0.14 LEU 202 -0.10 SER 193
PRO 23 0.14 VAL 203 -0.14 VAL 238
PRO 23 0.17 GLY 204 -0.12 VAL 238
PRO 23 0.20 ILE 205 -0.14 ALA 237
PRO 23 0.26 THR 206 -0.14 ALA 237
PRO 23 0.31 SER 207 -0.22 ALA 237
PRO 23 0.38 TRP 208 -0.23 ALA 237
PRO 23 0.37 ALA 209 -0.22 ALA 237
GLY 164 0.48 GLU 210 -0.22 ALA 237
GLY 164 0.45 GLY 211 -0.19 ALA 237
PRO 23 0.37 CYS 212 -0.17 ASN 197
PRO 23 0.32 ALA 213 -0.24 ARG 215
GLY 164 0.35 GLN 214 -0.38 ARG 215
GLY 164 0.35 ARG 215 -0.38 GLN 214
GLY 164 0.29 GLU 216 -0.28 ASN 197
PRO 23 0.29 ARG 217 -0.25 ASN 197
PRO 23 0.28 PRO 218 -0.28 ASN 197
PRO 23 0.30 GLY 219 -0.20 ASN 197
PRO 23 0.29 VAL 220 -0.22 ASN 121
PRO 23 0.25 TYR 221 -0.20 ALA 237
PRO 23 0.21 THR 222 -0.26 ALA 237
PRO 23 0.17 ASN 223 -0.23 ALA 237
PRO 23 0.14 VAL 224 -0.23 VAL 238
PRO 23 0.12 VAL 225 -0.32 VAL 238
PRO 23 0.13 GLU 226 -0.40 VAL 238
PRO 23 0.11 TYR 227 -0.39 VAL 238
LYS 117 0.09 VAL 228 -0.41 VAL 238
ASN 104 0.06 ASP 229 -0.61 VAL 238
ASN 197 0.07 TRP 230 -0.54 ALA 237
ASN 197 0.12 ILE 231 -0.34 VAL 238
GLU 233 0.22 LEU 232 -0.49 VAL 238
LEU 232 0.22 GLU 233 -0.68 VAL 238
ASN 197 0.16 LYS 234 -0.45 ALA 237
ALA 237 0.22 THR 235 -0.14 VAL 238
ALA 237 0.54 GLN 236 -0.44 VAL 238
ASN 36 0.57 ALA 237 -0.81 ASP 83
THR 101 0.83 VAL 238 -0.68 GLU 233

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: december 26th, 2025.