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CA distance fluctuations for 2605111359451716543

---  normal mode 7  ---

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

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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.