CNRS Nantes University US2B US2B
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 elNémo has been hacked on november 27th.
It has been moved away and runs again.
**Still some additional cleaning from time to time**
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***    ***

CA distance fluctuations for 2604151205022182167

---  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
ALA 61 0.84 ALA 1 -0.74 GLN 42
ASP 202 0.40 LEU 2 -0.53 GLY 237
LYS 62 0.77 PRO 3 -0.33 GLY 237
LYS 62 0.49 GLN 4 -0.46 GLY 237
LYS 62 0.41 THR 5 -0.50 GLY 237
CYS 38 0.42 VAL 6 -0.52 LEU 2
ASN 35 0.51 ARG 7 -0.38 GLU 25
ASN 35 0.69 ILE 8 -0.32 GLY 24
ASN 35 0.60 GLY 9 -0.57 SER 58
ASN 35 0.47 THR 10 -0.42 SER 58
LYS 229 0.43 ASP 11 -0.56 PHE 231
LYS 229 0.53 THR 12 -0.63 PHE 231
LYS 229 0.46 THR 13 -0.81 PHE 231
LYS 229 0.39 TYR 14 -0.90 PHE 231
LYS 229 0.51 ALA 15 -0.98 PHE 231
LYS 229 0.52 PRO 16 -1.03 TYR 236
LYS 229 0.53 PHE 17 -0.92 TYR 236
LYS 229 0.61 SER 18 -0.76 TYR 236
LYS 229 0.66 SER 19 -0.73 TYR 236
LYS 229 0.68 LYS 20 -0.69 TYR 236
LYS 229 0.79 ASP 21 -0.67 TYR 236
LYS 229 0.70 ALA 22 -0.56 TYR 236
LYS 229 0.68 LYS 23 -0.54 TYR 236
LYS 229 0.63 GLY 24 -0.58 TYR 236
LYS 229 0.70 GLU 25 -0.63 TYR 236
LYS 229 0.65 PHE 26 -0.72 TYR 236
LYS 229 0.89 ILE 27 -0.86 TYR 236
LYS 229 0.89 GLY 28 -1.03 TYR 236
LYS 229 0.62 PHE 29 -1.19 TYR 236
ASP 211 0.46 ASP 30 -0.79 TYR 236
ALA 49 0.47 ILE 31 -0.82 TYR 236
TRP 47 0.59 ASP 32 -1.08 TYR 236
LEU 214 0.53 LEU 33 -1.07 LEU 87
TRP 47 0.73 GLY 34 -0.76 GLY 237
TRP 47 1.14 ASN 35 -0.85 GLY 237
TRP 47 0.76 GLU 36 -1.23 GLY 237
TRP 47 0.64 MET 37 -1.09 GLY 237
TRP 47 0.61 CYS 38 -0.86 GLY 237
TRP 47 0.59 LYS 39 -0.92 GLY 237
TRP 47 0.47 ARG 40 -0.96 GLY 237
ASN 234 0.40 MET 41 -0.77 GLY 237
GLU 216 0.40 GLN 42 -0.74 ALA 1
LYS 62 0.32 VAL 43 -0.68 GLY 237
ASP 220 0.27 LYS 44 -0.72 GLY 237
LYS 39 0.48 CYS 45 -0.74 ILE 31
ASN 35 0.56 THR 46 -0.61 GLU 25
ASN 35 1.14 TRP 47 -0.47 GLY 24
ASN 35 0.76 VAL 48 -0.54 LYS 63
ASN 35 0.66 ALA 49 -0.62 SER 58
ASN 35 0.51 SER 50 -0.53 SER 58
ASN 35 0.39 ASP 51 -0.59 PHE 231
ILE 64 0.34 PHE 52 -0.58 LYS 76
ALA 1 0.40 ASP 53 -0.84 LYS 76
ILE 64 0.53 ALA 54 -0.61 LYS 76
ILE 64 0.57 LEU 55 -0.55 ARG 77
SER 120 0.48 ILE 56 -0.57 GLU 80
ALA 1 0.60 PRO 57 -0.37 SER 50
ALA 1 0.58 SER 58 -0.62 ALA 49
ALA 1 0.51 LEU 59 -0.35 GLY 9
ALA 1 0.67 LYS 60 -0.30 ALA 49
ALA 1 0.84 ALA 61 -0.42 ALA 49
PRO 3 0.77 LYS 62 -0.40 GLY 24
PRO 3 0.60 LYS 63 -0.54 VAL 48
LEU 55 0.57 ILE 64 -0.33 GLY 24
PRO 3 0.45 ASP 65 -0.27 GLY 24
ASN 35 0.32 ALA 66 -0.25 GLY 237
ASN 35 0.28 ILE 67 -0.30 ARG 218
LYS 229 0.30 ILE 68 -0.50 CYS 45
LYS 229 0.33 SER 69 -0.41 TYR 236
ALA 89 0.28 SER 70 -0.56 ARG 218
TYR 230 0.24 LEU 71 -0.64 ARG 218
TYR 230 0.27 SER 72 -0.90 ARG 218
LYS 86 0.35 ILE 73 -0.94 ARG 218
TYR 236 0.35 THR 74 -0.94 ARG 218
TYR 236 0.53 ASP 75 -0.81 ARG 218
LYS 189 0.53 LYS 76 -0.84 ASP 53
LYS 189 0.45 ARG 77 -0.71 ARG 218
TYR 236 0.42 GLN 78 -0.68 ARG 218
ALA 1 0.57 GLN 79 -0.59 ARG 218
ALA 1 0.61 GLU 80 -0.57 ILE 56
ALA 1 0.48 ILE 81 -0.50 ARG 218
TYR 236 0.38 ALA 82 -0.51 ARG 218
TYR 236 0.37 PHE 83 -0.59 ARG 218
ASN 234 0.44 SER 84 -0.69 LEU 214
TYR 236 0.53 ASP 85 -1.16 LEU 214
TYR 236 0.49 LYS 86 -0.97 LEU 214
ASP 211 0.51 LEU 87 -1.07 LEU 33
TYR 230 0.33 TYR 88 -1.02 LEU 33
TYR 230 0.73 ALA 89 -1.40 TYR 223
TYR 230 0.43 ALA 90 -1.19 TYR 223
ASP 193 0.46 ASP 91 -1.40 ASP 224
ILE 56 0.30 SER 92 -1.28 ASP 224
ILE 56 0.26 ARG 93 -1.56 VAL 235
ILE 56 0.26 LEU 94 -1.59 VAL 235
ILE 56 0.21 ILE 95 -1.61 ASN 234
ILE 56 0.18 ALA 96 -1.65 PHE 233
GLY 237 0.18 ALA 97 -1.81 PHE 233
GLY 237 0.20 LYS 98 -1.60 ASP 232
GLY 237 0.18 GLY 99 -1.48 ASN 234
ILE 56 0.18 SER 100 -1.56 ASN 234
PRO 57 0.21 PRO 101 -1.46 ASN 234
PRO 57 0.23 ILE 102 -1.53 ASN 234
PRO 57 0.29 GLN 103 -1.44 ASN 234
PRO 57 0.36 PRO 104 -1.32 ASN 234
PRO 57 0.36 THR 105 -1.18 ASN 234
PRO 57 0.34 LEU 106 -1.10 ASN 234
PRO 57 0.31 GLU 107 -1.11 ASN 234
PRO 57 0.28 SER 108 -1.26 ASN 234
PRO 57 0.28 LEU 109 -1.26 PHE 233
PRO 57 0.29 LYS 110 -1.17 PHE 233
ALA 1 0.29 GLY 111 -1.22 PHE 233
ALA 1 0.25 LYS 112 -1.35 PHE 233
ALA 1 0.26 HIS 113 -1.32 PHE 233
PRO 104 0.27 VAL 114 -1.28 PHE 233
ALA 1 0.24 GLY 115 -1.18 PHE 233
ILE 56 0.29 VAL 116 -1.06 VAL 235
ILE 56 0.30 LEU 117 -0.89 VAL 235
ALA 1 0.37 GLN 118 -0.73 VAL 235
PRO 57 0.50 GLY 119 -0.79 LYS 76
ILE 56 0.48 SER 120 -0.77 ASP 224
ILE 56 0.46 THR 121 -0.91 ASP 224
PRO 57 0.35 GLN 122 -1.00 VAL 235
PRO 57 0.44 GLU 123 -0.87 VAL 235
PRO 57 0.55 ALA 124 -0.88 ASP 224
PRO 57 0.44 TYR 125 -1.07 ASP 224
PRO 57 0.41 ALA 126 -1.01 ASP 224
PRO 57 0.52 ASN 127 -0.88 ASP 224
PRO 57 0.52 ASP 128 -0.97 ASP 224
PRO 57 0.42 ASN 129 -1.08 ASP 224
PRO 57 0.39 TRP 130 -1.00 ASP 224
ALA 1 0.44 ARG 131 -0.96 PHE 233
ALA 1 0.49 THR 132 -0.87 PHE 233
ALA 1 0.42 LYS 133 -0.94 PHE 233
ALA 1 0.40 GLY 134 -1.02 PHE 233
ALA 1 0.34 VAL 135 -1.13 PHE 233
ALA 1 0.35 ASP 136 -1.14 PHE 233
ALA 1 0.35 VAL 137 -1.08 PHE 233
ALA 1 0.35 VAL 138 -1.05 PHE 233
ALA 1 0.37 ALA 139 -0.92 PHE 233
ALA 1 0.31 TYR 140 -0.89 PHE 233
ALA 1 0.30 ALA 141 -0.73 PHE 233
LYS 229 0.29 ASN 142 -0.81 PHE 231
LYS 229 0.23 GLN 143 -0.99 PHE 231
LYS 229 0.32 ASP 144 -1.01 PHE 231
GLY 24 0.28 LEU 145 -0.96 PHE 233
GLY 24 0.18 ILE 146 -1.11 PHE 233
GLY 24 0.15 TYR 147 -1.23 PHE 231
GLY 24 0.22 SER 148 -1.16 PHE 233
GLY 24 0.21 ASP 149 -1.27 PHE 233
GLY 24 0.14 LEU 150 -1.47 PHE 233
GLY 24 0.14 THR 151 -1.44 PHE 233
GLY 24 0.18 ALA 152 -1.37 PHE 233
GLY 24 0.15 GLY 153 -1.53 PHE 233
ALA 1 0.19 ARG 154 -1.38 PHE 233
ALA 1 0.19 LEU 155 -1.45 PHE 233
ILE 56 0.18 ASP 156 -1.60 PHE 233
ILE 56 0.21 ALA 157 -1.50 PHE 233
ILE 56 0.23 ALA 158 -1.38 VAL 235
ILE 56 0.30 LEU 159 -1.40 VAL 235
ILE 56 0.29 GLN 160 -1.34 VAL 235
ILE 56 0.24 ASP 161 -1.21 VAL 235
GLY 237 0.27 GLU 162 -1.38 VAL 235
GLY 237 0.28 VAL 163 -1.45 ALA 227
ALA 89 0.33 ALA 164 -1.12 PHE 231
GLY 237 0.21 ALA 165 -1.39 VAL 235
GLY 237 0.28 SER 166 -1.28 PHE 231
ALA 89 0.28 GLU 167 -1.26 TYR 236
ALA 89 0.26 GLY 168 -1.53 PHE 231
GLY 237 0.19 PHE 169 -1.92 PHE 231
GLY 237 0.25 LEU 170 -1.52 PHE 231
GLY 237 0.24 LYS 171 -1.27 PHE 231
ALA 89 0.18 GLN 172 -1.33 PHE 231
GLY 237 0.16 PRO 173 -1.15 ASP 232
GLY 237 0.16 ALA 174 -1.32 ASP 232
GLY 237 0.21 GLY 175 -1.54 ASP 232
GLY 237 0.23 LYS 176 -1.52 ASP 232
GLY 237 0.21 GLU 177 -1.77 ASP 232
GLY 237 0.21 TYR 178 -1.82 ASP 232
GLY 237 0.25 ALA 179 -1.64 ASN 234
GLY 237 0.21 PHE 180 -1.68 ASN 234
ILE 56 0.21 ALA 181 -1.80 ASN 234
PRO 57 0.24 GLY 182 -1.52 ASN 234
GLY 237 0.21 PRO 183 -1.37 ASP 224
GLY 237 0.31 SER 184 -1.50 ASP 224
PRO 57 0.32 VAL 185 -1.45 ASP 224
LYS 60 0.29 LYS 186 -1.54 ASP 224
LYS 60 0.32 ASP 187 -1.37 ASP 224
LYS 76 0.53 LYS 188 -1.45 ARG 218
LYS 76 0.53 LYS 189 -1.26 ARG 218
LYS 60 0.44 TYR 190 -1.15 ARG 218
LYS 60 0.36 PHE 191 -1.23 ARG 218
ASP 91 0.33 GLY 192 -1.25 ARG 218
ASP 91 0.46 ASP 193 -1.35 ARG 218
TYR 230 0.44 GLY 194 -1.18 ARG 218
TYR 230 0.39 THR 195 -0.84 ARG 218
TYR 230 0.34 GLY 196 -0.66 ARG 218
TYR 230 0.26 VAL 197 -0.44 CYS 45
PRO 3 0.24 GLY 198 -0.46 ARG 218
PRO 3 0.38 LEU 199 -0.33 ARG 218
PRO 3 0.55 ARG 200 -0.34 ILE 56
ALA 1 0.51 LYS 201 -0.35 ARG 218
ALA 1 0.54 ASP 202 -0.26 ILE 56
ASN 234 0.40 ASP 203 -0.27 ILE 64
ASN 234 0.54 THR 204 -0.17 ILE 64
ASN 234 0.57 GLU 205 -0.25 ILE 64
ASN 234 0.47 LEU 206 -0.35 GLY 237
ASN 234 0.55 LYS 207 -0.28 GLY 237
ASN 234 0.73 ALA 208 -0.30 GLY 237
ASN 234 0.63 ALA 209 -0.49 GLY 237
ASN 234 0.56 PHE 210 -0.54 GLY 237
VAL 235 0.86 ASP 211 -0.40 GLY 237
ASN 234 0.83 LYS 212 -0.65 GLY 237
ASN 234 0.59 ALA 213 -0.97 GLY 237
VAL 235 0.77 LEU 214 -1.16 ASP 85
ASN 234 0.89 THR 215 -1.11 ASP 193
ASN 234 0.48 GLU 216 -1.25 GLY 237
ARG 40 0.43 LEU 217 -1.48 GLY 237
ASP 232 0.56 ARG 218 -1.45 LYS 188
ASP 232 0.43 GLN 219 -1.30 LYS 188
LYS 23 0.38 ASP 220 -1.04 LYS 186
LYS 23 0.39 GLY 221 -1.21 LYS 186
LYS 23 0.51 THR 222 -1.22 GLY 237
THR 215 0.41 TYR 223 -1.40 ALA 89
LYS 23 0.30 ASP 224 -1.54 LYS 186
LYS 23 0.60 LYS 225 -1.13 PRO 183
GLU 25 0.55 MET 226 -1.28 GLY 237
LEU 214 0.74 ALA 227 -1.45 VAL 163
THR 215 0.44 LYS 228 -1.31 PRO 183
GLY 28 0.89 LYS 229 -1.07 TYR 236
ALA 89 0.73 TYR 230 -0.86 TYR 236
THR 215 0.55 PHE 231 -1.92 PHE 169
THR 215 0.74 ASP 232 -1.82 TYR 178
THR 215 0.72 PHE 233 -1.81 ALA 97
THR 215 0.89 ASN 234 -1.80 ALA 181
ASP 211 0.86 VAL 235 -1.59 LEU 94
ASP 85 0.53 TYR 236 -1.26 GLU 167
TYR 230 0.42 GLY 237 -1.48 LEU 217

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.