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 elNémo has been hacked on november 27th.
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***  FXIa G216A  ***

CA distance fluctuations for 2602061636333075550

---  normal mode 30  ---

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
THR 24 0.50 ILE 1 -0.28 PRO 23
THR 24 0.51 VAL 2 -0.26 PRO 23
ARG 138 0.50 GLY 3 -0.22 LYS 140
ARG 138 0.46 GLY 4 -0.22 LYS 140
ARG 138 0.51 THR 5 -0.29 LYS 140
ARG 138 0.50 ALA 6 -0.29 LYS 140
ASP 70 0.38 SER 7 -0.20 LYS 140
ASP 70 0.43 VAL 8 -0.19 GLU 11
ASP 70 0.45 ARG 9 -0.13 ASP 229
ASP 70 0.38 GLY 10 -0.16 SER 113
ASP 70 0.33 GLU 11 -0.19 VAL 8
ALA 237 0.29 TRP 12 -0.16 ASP 229
ALA 237 0.37 PRO 13 -0.16 ASP 229
ALA 237 0.35 TRP 14 -0.16 ASP 229
ALA 237 0.23 GLN 15 -0.15 PRO 23
VAL 238 0.21 VAL 16 -0.13 PRO 23
LYS 140 0.23 THR 17 -0.15 PRO 23
LYS 140 0.37 LEU 18 -0.20 PRO 23
LYS 140 0.44 HIS 19 -0.14 LYS 68
LYS 140 0.53 THR 20 -0.25 ASP 70
LYS 140 0.49 THR 21 -0.52 THR 24
LYS 140 0.56 SER 22 -0.56 THR 24
GLU 69 0.35 PRO 23 -0.94 GLY 48
LYS 140 1.13 THR 24 -0.75 LYS 53
THR 21 0.44 GLN 25 -0.33 LYS 68
THR 24 0.60 ARG 26 -0.25 LYS 68
LYS 140 0.51 HIS 27 -0.26 PRO 23
LYS 140 0.64 LEU 28 -0.50 PRO 23
LYS 140 0.48 CYS 29 -0.45 PRO 23
LYS 140 0.29 GLY 30 -0.32 PRO 23
LYS 140 0.24 GLY 31 -0.28 PRO 23
ALA 237 0.22 SER 32 -0.21 PRO 23
ALA 237 0.38 ILE 33 -0.17 GLU 50
ALA 237 0.48 ILE 34 -0.20 GLU 233
ALA 237 0.63 GLY 35 -0.23 GLU 233
ALA 237 0.63 ASN 36 -0.18 GLU 233
VAL 238 0.46 GLN 37 -0.19 GLU 50
ALA 237 0.28 TRP 38 -0.21 GLU 50
TRP 38 0.25 ILE 39 -0.20 GLU 50
GLY 164 0.24 LEU 40 -0.24 PRO 23
LYS 140 0.31 THR 41 -0.32 PRO 23
LYS 140 0.41 ALA 42 -0.40 PRO 23
LYS 140 0.47 ALA 43 -0.44 ALA 237
LYS 140 0.58 HIS 44 -0.53 PRO 23
LYS 140 0.61 CYS 45 -0.57 PRO 23
LYS 140 0.57 PHE 46 -0.54 PRO 23
LYS 140 0.59 TYR 47 -0.65 PRO 23
GLU 50 1.16 GLY 48 -0.94 PRO 23
GLY 48 0.88 VAL 49 -0.56 ALA 237
GLY 48 1.16 GLU 50 -0.73 ALA 237
GLY 48 0.69 SER 51 -0.60 THR 24
LYS 53 0.57 PRO 52 -0.50 THR 24
GLY 48 0.58 LYS 53 -0.75 THR 24
LYS 140 0.42 ILE 54 -0.70 THR 24
LYS 140 0.42 LEU 55 -0.38 THR 24
VAL 238 0.35 ARG 56 -0.31 ASP 70
VAL 238 0.34 VAL 57 -0.20 LYS 53
VAL 238 0.33 TYR 58 -0.19 LYS 53
VAL 238 0.29 SER 59 -0.18 LYS 53
ASP 70 0.34 GLY 60 -0.16 LYS 53
ASP 70 0.43 ILE 61 -0.19 GLN 63
ASP 70 0.49 LEU 62 -0.18 GLN 63
ASP 70 0.51 GLN 63 -0.19 ILE 61
THR 24 0.55 GLN 64 -0.08 LYS 53
THR 24 0.57 SER 65 -0.31 ILE 67
ASP 70 0.71 GLU 66 -0.17 LYS 53
ASP 70 0.55 ILE 67 -0.31 SER 65
ASP 70 0.71 LYS 68 -0.33 GLN 25
LYS 68 0.54 GLU 69 -0.42 LYS 53
LYS 68 0.71 ASP 70 -0.73 LYS 53
GLU 69 0.53 THR 71 -0.24 LYS 53
VAL 238 0.43 SER 72 -0.26 LYS 53
VAL 238 0.42 PHE 73 -0.28 LYS 53
VAL 238 0.48 PHE 74 -0.29 ASP 70
VAL 238 0.49 GLY 75 -0.46 ASP 70
VAL 238 0.44 VAL 76 -0.37 ASP 70
VAL 238 0.48 GLN 77 -0.37 THR 24
LYS 140 0.32 GLU 78 -0.42 ALA 237
LYS 140 0.36 ILE 79 -0.50 ALA 237
LYS 140 0.32 ILE 80 -0.60 ALA 237
LYS 140 0.39 ILE 81 -0.66 ALA 237
GLY 164 0.36 HIS 82 -0.65 ALA 237
GLY 48 0.55 ASP 83 -0.90 ALA 237
GLY 164 0.45 GLN 84 -0.74 ALA 237
GLY 164 0.50 TYR 85 -0.73 ALA 237
LYS 140 0.58 LYS 86 -0.76 ALA 237
LYS 140 0.63 MET 87 -0.58 ALA 237
LYS 140 0.53 ALA 88 -0.40 PRO 23
LYS 140 0.48 GLU 89 -0.36 PRO 23
GLY 164 0.63 SER 90 -0.42 ALA 237
GLY 164 0.56 GLY 91 -0.36 ALA 237
GLY 164 0.45 TYR 92 -0.41 ALA 237
LYS 140 0.41 ASP 93 -0.36 PRO 23
LYS 140 0.35 ILE 94 -0.31 PRO 23
LYS 140 0.35 ALA 95 -0.33 ALA 237
LYS 140 0.29 LEU 96 -0.22 PRO 23
LYS 140 0.32 LEU 97 -0.25 GLU 50
VAL 238 0.40 LYS 98 -0.25 GLU 50
VAL 238 0.54 LEU 99 -0.25 THR 24
VAL 238 0.68 GLU 100 -0.33 ASP 70
VAL 238 0.74 THR 101 -0.26 ASP 70
VAL 238 0.60 THR 102 -0.16 THR 24
ALA 237 0.51 VAL 103 -0.17 LYS 53
ALA 237 0.59 GLN 104 -0.15 LYS 53
ALA 237 0.60 TYR 105 -0.18 GLY 118
ALA 237 0.53 THR 106 -0.18 GLY 118
ALA 237 0.42 ASP 107 -0.25 GLY 118
ALA 237 0.39 SER 108 -0.16 GLY 118
ALA 237 0.43 GLN 109 -0.15 LYS 53
ALA 237 0.53 ARG 110 -0.20 ASP 107
ALA 237 0.57 PRO 111 -0.21 ASP 229
ALA 237 0.49 ILE 112 -0.23 ASP 229
ALA 237 0.58 SER 113 -0.32 GLU 198
ALA 237 0.46 LEU 114 -0.30 ASP 229
ALA 237 0.38 PRO 115 -0.29 ASP 229
ALA 237 0.40 SER 116 -0.40 LYS 117
ASN 155 0.43 LYS 117 -0.40 SER 116
ARG 120 0.65 GLY 118 -0.45 ASN 197
ALA 237 0.32 ASP 119 -0.24 ASN 197
GLY 118 0.65 ARG 120 -0.41 ASN 121
THR 154 0.41 ASN 121 -0.41 ARG 120
ALA 237 0.25 VAL 122 -0.25 ARG 120
ASN 197 0.28 ILE 123 -0.34 HIS 169
ASN 197 0.27 TYR 124 -0.35 THR 125
ASN 197 0.29 THR 125 -0.35 TYR 124
ALA 237 0.22 ASP 126 -0.22 HIS 169
THR 24 0.21 CYS 127 -0.22 PRO 23
THR 24 0.25 TRP 128 -0.22 PRO 23
THR 24 0.28 VAL 129 -0.27 PRO 23
THR 24 0.31 THR 130 -0.24 PRO 23
THR 24 0.38 GLY 131 -0.26 PRO 23
THR 24 0.54 TRP 132 -0.23 PRO 23
THR 24 0.59 GLY 133 -0.34 PRO 23
THR 24 0.71 TYR 134 -0.30 PRO 23
ARG 138 0.78 ARG 135 -0.25 LYS 140
ARG 138 0.82 LYS 136 -0.28 PRO 23
THR 24 0.52 LEU 137 -0.59 CYS 184
LYS 136 0.82 ARG 138 -0.56 PRO 23
THR 24 0.96 ASP 139 -0.17 ARG 135
THR 24 1.13 LYS 140 -0.38 GLN 142
THR 24 0.91 ILE 141 -0.20 PRO 23
THR 24 0.82 GLN 142 -0.38 LYS 140
THR 24 0.76 ASN 143 -0.27 LYS 140
THR 24 0.58 THR 144 -0.24 LYS 140
THR 24 0.45 LEU 145 -0.17 THR 144
THR 24 0.45 GLN 146 -0.20 LYS 140
THR 24 0.36 LYS 147 -0.19 PRO 23
THR 24 0.35 ALA 148 -0.21 PRO 23
THR 24 0.30 LYS 149 -0.21 GLU 156
THR 24 0.28 ILE 150 -0.25 GLU 156
THR 24 0.25 PRO 151 -0.33 GLU 156
THR 24 0.22 LEU 152 -0.31 GLU 156
GLY 118 0.33 VAL 153 -0.45 GLU 156
GLY 118 0.45 THR 154 -0.61 GLU 156
GLY 118 0.49 ASN 155 -0.28 THR 154
GLY 118 0.43 GLU 156 -0.61 THR 154
GLY 118 0.44 GLU 157 -0.57 GLU 156
GLY 118 0.38 CYS 158 -0.29 PRO 23
GLY 118 0.39 GLN 159 -0.33 ARG 163
GLY 118 0.42 LYS 160 -0.51 ARG 163
GLY 118 0.35 ARG 161 -0.32 PRO 23
GLY 118 0.31 TYR 162 -0.34 PRO 23
THR 24 0.26 ARG 163 -0.51 LYS 160
LYS 166 1.09 GLY 164 -0.41 ARG 138
GLY 164 1.06 HIS 165 -0.33 PRO 23
GLY 164 1.09 LYS 166 -0.28 PRO 23
GLY 164 0.61 ILE 167 -0.29 PRO 23
GLY 164 0.57 THR 168 -0.25 PRO 23
GLY 164 0.47 HIS 169 -0.34 ILE 123
GLY 164 0.46 LYS 170 -0.30 ILE 123
GLY 164 0.36 MET 171 -0.29 PRO 23
GLY 118 0.30 ILE 172 -0.28 PRO 23
GLY 118 0.28 CYS 173 -0.30 PRO 23
THR 24 0.25 ALA 174 -0.29 PRO 23
THR 24 0.30 GLY 175 -0.29 PRO 23
THR 24 0.31 TYR 176 -0.34 GLU 156
THR 24 0.33 ARG 177 -0.56 ARG 215
GLU 216 0.43 GLU 178 -0.37 ARG 215
THR 24 0.39 GLY 179 -0.32 ARG 215
THR 24 0.43 GLY 180 -0.24 PRO 23
THR 24 0.40 LYS 181 -0.26 PRO 23
THR 24 0.40 ASP 182 -0.30 PRO 23
THR 24 0.41 ALA 183 -0.36 LEU 137
THR 24 0.49 CYS 184 -0.59 LEU 137
LYS 140 0.58 LYS 185 -0.56 LEU 137
LYS 140 0.57 GLY 186 -0.46 PRO 23
THR 24 0.39 ASP 187 -0.41 PRO 23
LYS 140 0.42 SER 188 -0.48 PRO 23
LYS 140 0.33 GLY 189 -0.41 PRO 23
THR 24 0.20 GLY 190 -0.33 PRO 23
THR 24 0.17 PRO 191 -0.28 PRO 23
THR 24 0.19 LEU 192 -0.28 PRO 23
ALA 237 0.24 SER 193 -0.22 PRO 23
ALA 237 0.28 CYS 194 -0.21 PRO 23
ALA 237 0.35 LYS 195 -0.20 ASP 229
ALA 237 0.38 HIS 196 -0.22 ASP 229
ALA 237 0.33 ASN 197 -0.45 GLY 118
ALA 237 0.36 GLU 198 -0.59 VAL 199
ALA 237 0.48 VAL 199 -0.59 GLU 198
ALA 237 0.42 TRP 200 -0.26 ASP 229
ALA 237 0.40 HIS 201 -0.23 ASP 229
ALA 237 0.30 LEU 202 -0.23 PRO 23
ALA 237 0.21 VAL 203 -0.25 PRO 23
GLY 164 0.21 GLY 204 -0.29 PRO 23
GLY 164 0.22 ILE 205 -0.33 PRO 23
LYS 140 0.26 THR 206 -0.39 PRO 23
LYS 140 0.39 SER 207 -0.42 PRO 23
LYS 140 0.42 TRP 208 -0.45 PRO 23
THR 24 0.36 ALA 209 -0.41 PRO 23
ARG 215 0.42 GLU 210 -0.38 PRO 23
THR 24 0.47 GLY 211 -0.40 PRO 23
THR 24 0.48 CYS 212 -0.36 PRO 23
THR 24 0.45 ALA 213 -0.29 PRO 23
THR 24 0.45 GLN 214 -0.27 PRO 23
THR 24 0.44 ARG 215 -0.56 ARG 177
GLU 178 0.43 GLU 216 -0.27 PRO 23
THR 24 0.35 ARG 217 -0.31 PRO 23
THR 24 0.30 PRO 218 -0.33 PRO 23
THR 24 0.31 GLY 219 -0.36 PRO 23
THR 24 0.26 VAL 220 -0.36 PRO 23
LYS 140 0.24 TYR 221 -0.34 PRO 23
GLY 164 0.31 THR 222 -0.32 PRO 23
GLY 164 0.32 ASN 223 -0.27 PRO 23
GLY 164 0.28 VAL 224 -0.25 PRO 23
GLY 164 0.31 VAL 225 -0.25 GLN 84
GLY 164 0.37 GLU 226 -0.32 GLN 84
GLY 164 0.37 TYR 227 -0.31 VAL 238
GLY 164 0.32 VAL 228 -0.33 VAL 238
GLY 164 0.38 ASP 229 -0.52 VAL 238
GLY 164 0.37 TRP 230 -0.50 VAL 238
GLY 164 0.31 ILE 231 -0.32 VAL 238
GLY 164 0.30 LEU 232 -0.45 VAL 238
GLY 164 0.29 GLU 233 -0.68 VAL 238
GLY 164 0.27 LYS 234 -0.43 VAL 238
ALA 237 0.26 THR 235 -0.43 LYS 234
ALA 237 0.47 GLN 236 -0.56 VAL 238
GLY 35 0.63 ALA 237 -0.90 ASP 83
THR 101 0.74 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.