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

CA distance fluctuations for 2604150925332159111

---  normal mode 9  ---

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
ALA 209 0.34 ALA 1 -0.70 ASP 202
ALA 209 0.45 LEU 2 -0.61 LYS 62
ALA 209 0.35 PRO 3 -0.62 LYS 62
GLN 172 0.36 GLN 4 -0.40 LYS 62
GLN 172 0.37 THR 5 -0.34 LYS 62
GLN 172 0.33 VAL 6 -0.34 LYS 62
GLN 172 0.28 ARG 7 -0.41 ASN 35
ILE 67 0.28 ILE 8 -0.70 ASN 35
SER 58 0.47 GLY 9 -0.63 ASN 35
SER 58 0.32 THR 10 -0.48 ASN 35
VAL 235 0.41 ASP 11 -0.37 ASN 35
ASN 234 0.47 THR 12 -0.38 LYS 229
ASN 234 0.59 THR 13 -0.35 LYS 229
VAL 235 0.70 TYR 14 -0.31 ALA 90
ASN 234 0.73 ALA 15 -0.37 LYS 229
TYR 236 0.80 PRO 16 -0.38 LYS 229
TYR 236 0.72 PHE 17 -0.44 LYS 229
TYR 236 0.55 SER 18 -0.46 LYS 229
ASN 234 0.53 SER 19 -0.49 LYS 229
ASN 234 0.49 LYS 20 -0.49 LYS 229
PRO 173 0.65 ASP 21 -0.51 LYS 229
PRO 173 0.65 ALA 22 -0.47 LYS 225
PRO 173 0.53 LYS 23 -0.52 LYS 225
PRO 173 0.44 GLY 24 -0.41 LYS 225
PRO 173 0.48 GLU 25 -0.48 MET 226
TYR 236 0.48 PHE 26 -0.46 ASN 35
TYR 236 0.62 ILE 27 -0.54 LYS 229
TYR 236 0.77 GLY 28 -0.62 LYS 229
TYR 236 0.99 PHE 29 -0.59 LYS 229
CYS 45 0.56 ASP 30 -0.43 ASP 211
CYS 45 0.70 ILE 31 -0.47 THR 10
TYR 236 0.80 ASP 32 -0.43 LEU 33
LEU 87 0.99 LEU 33 -0.51 ALA 213
CYS 45 0.61 GLY 34 -0.40 ALA 213
GLY 237 0.57 ASN 35 -0.87 TRP 47
GLY 237 0.85 GLU 36 -0.50 TRP 47
ASP 85 0.66 MET 37 -0.43 ILE 8
GLY 237 0.49 CYS 38 -0.49 ILE 8
GLY 237 0.58 LYS 39 -0.49 CYS 45
GLY 237 0.53 ARG 40 -0.40 GLU 216
GLY 237 0.34 MET 41 -0.35 ILE 8
GLY 237 0.38 GLN 42 -0.35 GLU 216
LYS 171 0.40 VAL 43 -0.29 LYS 62
ILE 31 0.62 LYS 44 -0.24 LYS 62
ILE 31 0.70 CYS 45 -0.49 LYS 39
ILE 31 0.51 THR 46 -0.43 LYS 39
SER 18 0.51 TRP 47 -0.87 ASN 35
LYS 63 0.38 VAL 48 -0.63 ASN 35
SER 58 0.58 ALA 49 -0.63 ASN 35
SER 58 0.45 SER 50 -0.53 ASN 35
VAL 235 0.47 ASP 51 -0.39 TYR 140
VAL 235 0.50 PHE 52 -0.31 ASN 35
LYS 76 0.62 ASP 53 -0.45 GLN 118
ARG 218 0.45 ALA 54 -0.54 ILE 64
ARG 218 0.43 LEU 55 -0.43 ILE 64
ARG 218 0.49 ILE 56 -0.51 ALA 124
ALA 49 0.42 PRO 57 -0.64 ALA 124
ALA 49 0.58 SER 58 -0.51 ASN 127
GLY 9 0.37 LEU 59 -0.43 ASP 128
ARG 218 0.34 LYS 60 -0.54 ASP 128
ALA 49 0.41 ALA 61 -0.60 ALA 1
ALA 49 0.28 LYS 62 -0.62 PRO 3
ALA 49 0.41 LYS 63 -0.46 PRO 3
ASP 203 0.31 ILE 64 -0.54 ALA 54
LEU 206 0.35 ASP 65 -0.40 LEU 2
LEU 214 0.32 ALA 66 -0.30 ASN 35
ARG 218 0.39 ILE 67 -0.27 ASN 35
ARG 218 0.39 ILE 68 -0.26 PHE 210
ARG 218 0.47 SER 69 -0.33 ILE 31
ARG 218 0.67 SER 70 -0.18 TYR 230
ARG 218 0.77 LEU 71 -0.16 TYR 230
ARG 218 1.02 SER 72 -0.22 LYS 60
ARG 218 1.07 ILE 73 -0.28 LYS 60
ARG 218 1.06 THR 74 -0.36 LYS 188
ARG 218 0.97 ASP 75 -0.36 TYR 236
ARG 218 0.86 LYS 76 -0.52 LYS 189
ARG 218 0.82 ARG 77 -0.42 LYS 189
ARG 218 0.81 GLN 78 -0.38 ALA 1
ARG 218 0.73 GLN 79 -0.47 ALA 1
ARG 218 0.64 GLU 80 -0.50 ALA 1
ARG 218 0.59 ILE 81 -0.46 ALA 1
THR 215 0.63 ALA 82 -0.37 ALA 1
LEU 214 0.80 PHE 83 -0.39 TYR 236
LEU 214 1.02 SER 84 -0.48 TYR 236
LEU 214 1.61 ASP 85 -0.66 TYR 236
LEU 214 1.06 LYS 86 -0.57 TYR 236
LEU 33 0.99 LEU 87 -0.50 ASP 211
TYR 223 1.08 TYR 88 -0.49 TYR 230
TYR 223 1.44 ALA 89 -0.59 TYR 230
TYR 223 1.35 ALA 90 -0.35 TYR 230
ASP 224 1.43 ASP 91 -0.31 ASP 193
ASP 224 1.30 SER 92 -0.27 ILE 56
VAL 235 1.42 ARG 93 -0.25 ILE 56
VAL 235 1.40 LEU 94 -0.26 PRO 57
PHE 233 1.56 ILE 95 -0.18 ILE 56
PHE 233 1.88 ALA 96 -0.18 ILE 56
PHE 233 1.79 ALA 97 -0.14 ILE 56
ASP 232 1.76 LYS 98 -0.14 VAL 185
ASP 232 1.50 GLY 99 -0.16 LYS 189
PHE 233 1.57 SER 100 -0.21 PRO 57
PHE 233 1.42 PRO 101 -0.24 PRO 57
PHE 233 1.48 ILE 102 -0.29 PRO 57
PHE 233 1.30 GLN 103 -0.35 PRO 57
ASP 224 1.27 PRO 104 -0.43 GLN 122
ASP 224 1.21 THR 105 -0.43 PRO 57
ASP 224 1.12 LEU 106 -0.43 PRO 57
PHE 233 1.11 GLU 107 -0.38 PRO 57
PHE 233 1.26 SER 108 -0.34 PRO 57
PHE 233 1.31 LEU 109 -0.34 PRO 57
PHE 233 1.18 LYS 110 -0.36 PRO 57
PHE 233 1.19 GLY 111 -0.31 PRO 57
PHE 233 1.33 LYS 112 -0.29 PRO 57
PHE 233 1.28 HIS 113 -0.28 PRO 57
PHE 233 1.30 VAL 114 -0.29 PRO 57
PHE 233 1.18 GLY 115 -0.27 PRO 57
VAL 235 1.04 VAL 116 -0.32 PRO 57
VAL 235 0.87 LEU 117 -0.30 ILE 56
VAL 235 0.72 GLN 118 -0.45 ASP 53
ARG 218 0.74 GLY 119 -0.52 PRO 57
ARG 218 0.87 SER 120 -0.47 ILE 56
ARG 218 1.03 THR 121 -0.44 PRO 57
ASP 224 1.04 GLN 122 -0.43 PRO 104
ASP 224 0.89 GLU 123 -0.49 PRO 57
ARG 218 0.97 ALA 124 -0.64 PRO 57
ASP 224 1.19 TYR 125 -0.51 PRO 57
ASP 224 1.11 ALA 126 -0.47 PRO 57
ASP 224 0.96 ASN 127 -0.63 PRO 57
ASP 224 1.07 ASP 128 -0.63 PRO 57
ASP 224 1.22 ASN 129 -0.50 PRO 57
ASP 224 1.13 TRP 130 -0.46 PRO 57
PHE 233 0.98 ARG 131 -0.52 PRO 57
ASP 224 0.96 THR 132 -0.53 PRO 57
ASP 224 1.00 LYS 133 -0.45 PRO 57
PHE 233 1.02 GLY 134 -0.41 PRO 57
PHE 233 1.14 VAL 135 -0.39 PRO 57
PHE 233 1.12 ASP 136 -0.36 PRO 57
PHE 233 1.07 VAL 137 -0.37 PRO 57
PHE 233 1.03 VAL 138 -0.34 PRO 57
PHE 233 0.89 ALA 139 -0.45 ASP 53
PHE 233 0.84 TYR 140 -0.39 ALA 141
PHE 233 0.68 ALA 141 -0.39 TYR 140
VAL 235 0.70 ASN 142 -0.31 GLY 24
VAL 235 0.86 GLN 143 -0.21 GLN 160
PHE 233 0.80 ASP 144 -0.30 ALA 165
PHE 233 0.89 LEU 145 -0.29 GLY 24
PHE 233 1.07 ILE 146 -0.16 GLY 24
PHE 233 1.13 TYR 147 -0.20 ALA 165
PHE 233 1.05 SER 148 -0.16 ALA 165
PHE 233 1.17 ASP 149 -0.16 GLY 24
PHE 233 1.38 LEU 150 -0.13 ILE 56
PHE 233 1.30 THR 151 -0.12 GLU 162
PHE 233 1.20 ALA 152 -0.09 ASP 53
PHE 233 1.34 GLY 153 -0.12 ASP 53
PHE 233 1.25 ARG 154 -0.16 ASP 53
PHE 233 1.38 LEU 155 -0.19 PRO 57
PHE 233 1.56 ASP 156 -0.21 PRO 57
PHE 233 1.58 ALA 157 -0.24 PRO 57
PHE 233 1.37 ALA 158 -0.24 PRO 57
VAL 235 1.34 LEU 159 -0.29 PRO 57
VAL 235 1.35 GLN 160 -0.24 ILE 56
VAL 235 1.28 ASP 161 -0.21 ASP 144
VAL 235 1.46 GLU 162 -0.26 LEU 170
ALA 227 1.61 VAL 163 -0.25 ALA 90
VAL 235 1.22 ALA 164 -0.24 ASP 144
VAL 235 1.59 ALA 165 -0.30 ASP 144
ASN 234 1.54 SER 166 -0.23 LYS 171
ASN 234 1.19 GLU 167 -0.23 ALA 89
PHE 231 1.16 GLY 168 -0.26 ASP 144
PHE 231 1.50 PHE 169 -0.14 GLU 162
PHE 231 1.88 LEU 170 -0.26 GLU 162
PHE 231 1.46 LYS 171 -0.23 SER 166
PHE 231 1.35 GLN 172 -0.17 SER 166
PHE 231 1.20 PRO 173 -0.14 SER 184
PHE 231 1.29 ALA 174 -0.11 SER 184
PHE 231 1.60 GLY 175 -0.16 SER 184
PHE 231 1.44 LYS 176 -0.21 SER 184
ASP 232 1.66 GLU 177 -0.13 SER 184
ASP 232 1.80 TYR 178 -0.14 SER 184
ASN 234 1.67 ALA 179 -0.20 SER 184
ASN 234 1.66 PHE 180 -0.26 VAL 185
PHE 233 1.46 ALA 181 -0.22 PRO 57
ASP 224 1.25 GLY 182 -0.33 VAL 185
ASP 224 1.45 PRO 183 -0.31 VAL 185
ASP 224 1.57 SER 184 -0.24 PHE 180
ASP 224 1.52 VAL 185 -0.33 GLY 182
ASP 224 1.56 LYS 186 -0.31 LYS 60
ARG 218 1.38 ASP 187 -0.35 LYS 76
ARG 218 1.53 LYS 188 -0.51 LYS 76
ARG 218 1.34 LYS 189 -0.52 LYS 76
ARG 218 1.26 TYR 190 -0.45 PRO 57
ARG 218 1.35 PHE 191 -0.34 LYS 60
ARG 218 1.38 GLY 192 -0.30 LYS 186
ARG 218 1.46 ASP 193 -0.43 GLY 237
ARG 218 1.26 GLY 194 -0.40 TYR 230
ARG 218 0.95 THR 195 -0.34 TYR 230
LEU 214 0.77 GLY 196 -0.27 TYR 230
LEU 214 0.57 VAL 197 -0.20 ALA 209
ARG 218 0.54 GLY 198 -0.27 ALA 1
LEU 214 0.45 LEU 199 -0.39 ALA 1
LEU 214 0.39 ARG 200 -0.62 ALA 1
THR 215 0.45 LYS 201 -0.56 ALA 1
LEU 214 0.30 ASP 202 -0.70 ALA 1
ASP 65 0.31 ASP 203 -0.55 ALA 1
LEU 214 0.26 THR 204 -0.53 TYR 236
ASP 65 0.29 GLU 205 -0.45 ASN 234
ASP 65 0.35 LEU 206 -0.35 ALA 209
LEU 214 0.36 LYS 207 -0.49 TYR 236
ASP 211 0.26 ALA 208 -0.60 TYR 236
LEU 2 0.45 ALA 209 -0.50 VAL 235
LEU 2 0.31 PHE 210 -0.50 VAL 235
ALA 82 0.35 ASP 211 -0.78 VAL 235
ASP 85 0.37 LYS 212 -0.73 VAL 235
ASP 85 0.64 ALA 213 -0.51 LEU 33
ASP 85 1.61 LEU 214 -0.85 ALA 227
ASP 193 1.11 THR 215 -0.85 ASP 232
ASP 193 0.87 GLU 216 -0.47 ASP 232
GLY 237 1.09 LEU 217 -0.38 ARG 40
LYS 188 1.53 ARG 218 -0.54 ASP 232
LYS 188 1.34 GLN 219 -0.33 ASP 232
LYS 186 1.07 ASP 220 -0.36 LYS 23
LYS 186 1.23 GLY 221 -0.36 LYS 23
GLY 237 1.14 THR 222 -0.51 LYS 23
ALA 89 1.44 TYR 223 -0.49 THR 215
SER 184 1.57 ASP 224 -0.39 ARG 218
GLY 237 1.30 LYS 225 -0.52 LYS 23
GLY 237 1.56 MET 226 -0.49 LYS 23
VAL 163 1.61 ALA 227 -0.85 LEU 214
PRO 183 1.28 LYS 228 -0.58 THR 215
TYR 236 0.95 LYS 229 -0.62 GLY 28
LYS 171 1.01 TYR 230 -0.59 ALA 89
LEU 170 1.88 PHE 231 -0.75 LEU 214
TYR 178 1.80 ASP 232 -0.85 THR 215
ALA 96 1.88 PHE 233 -0.74 THR 215
ALA 179 1.67 ASN 234 -0.69 ASP 211
ALA 165 1.59 VAL 235 -0.78 ASP 211
ALA 227 1.43 TYR 236 -0.66 ASP 85
MET 226 1.56 GLY 237 -0.43 ASP 193

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.