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***  prova  ***

CA distance fluctuations for 2605111359451716543

---  normal mode 11  ---

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
ASP 117 0.19 ALA 1 -0.36 PRO 211
ASP 117 0.18 SER 2 -0.31 PRO 211
GLY 116 0.20 LYS 3 -0.26 PRO 211
ASP 117 0.21 GLY 4 -0.25 PRO 211
ASP 76 0.27 GLU 5 -0.33 PRO 211
ASP 117 0.29 GLU 6 -0.31 PRO 211
ASP 76 0.29 LEU 7 -0.27 PRO 211
ASP 76 0.34 PHE 8 -0.35 PRO 211
ASP 76 0.45 THR 9 -0.41 PRO 211
ASP 76 0.35 GLY 10 -0.43 PRO 211
ASP 76 0.27 VAL 11 -0.42 PRO 211
ASP 76 0.25 VAL 12 -0.31 PRO 211
ARG 215 0.25 PRO 13 -0.23 PRO 211
ARG 215 0.27 ILE 14 -0.17 PRO 211
ARG 215 0.37 LEU 15 -0.12 GLU 172
ARG 215 0.35 VAL 16 -0.14 GLU 17
ARG 215 0.44 GLU 17 -0.16 GLU 172
ARG 215 0.39 LEU 18 -0.18 ASP 19
LYS 214 0.41 ASP 19 -0.21 LYS 26
ARG 215 0.35 GLY 20 -0.17 LYS 26
PRO 211 0.41 ASP 21 -0.24 GLU 124
PRO 211 0.39 VAL 22 -0.16 GLU 95
PRO 211 0.43 ASN 23 -0.17 GLU 95
PRO 211 0.51 GLY 24 -0.20 GLU 95
PRO 211 0.57 HIS 25 -0.19 GLU 124
GLY 51 0.57 LYS 26 -0.22 GLU 124
PRO 211 0.49 PHE 27 -0.27 PRO 54
ARG 215 0.46 SER 28 -0.25 GLU 172
ARG 215 0.44 VAL 29 -0.28 GLU 172
ARG 215 0.47 SER 30 -0.25 GLU 172
ARG 215 0.36 GLY 31 -0.22 GLU 172
ARG 215 0.30 GLU 32 -0.18 GLU 172
ARG 215 0.20 GLY 33 -0.26 PRO 211
ASP 76 0.17 GLU 34 -0.36 PRO 211
ASP 76 0.16 GLY 35 -0.41 PRO 211
ASP 76 0.20 ASP 36 -0.49 PRO 211
PRO 75 0.23 ALA 37 -0.46 PRO 211
PRO 75 0.27 THR 38 -0.50 PRO 211
ALA 227 0.16 TYR 39 -0.59 PRO 211
ALA 227 0.13 GLY 40 -0.54 PRO 211
ALA 227 0.09 LYS 41 -0.58 PRO 211
GLU 32 0.06 LEU 42 -0.50 PRO 211
SER 205 0.06 THR 43 -0.50 PRO 211
LYS 45 0.12 LEU 44 -0.30 PRO 211
LEU 44 0.12 LYS 45 -0.24 GLU 172
ARG 215 0.20 PHE 46 -0.30 GLU 172
VAL 29 0.44 ILE 47 -0.41 GLU 172
PRO 211 0.39 CYS 48 -0.42 GLU 172
ARG 215 0.65 THR 49 -0.43 GLU 172
LYS 214 0.64 THR 50 -0.41 GLU 172
PRO 211 0.67 GLY 51 -0.51 GLU 172
PRO 211 0.76 LYS 52 -0.63 HIS 139
PRO 211 0.58 LEU 53 -0.40 HIS 139
PRO 211 0.58 PRO 54 -0.32 HIS 139
PRO 211 0.37 VAL 55 -0.23 THR 50
TYR 143 0.30 PRO 56 -0.39 ASP 216
SER 208 0.16 TRP 57 -0.38 GLU 142
PRO 56 0.19 PRO 58 -0.34 LYS 214
ASN 144 0.10 THR 59 -0.22 LYS 214
ILE 47 0.10 LEU 60 -0.11 GLY 228
ASN 144 0.08 VAL 61 -0.18 LYS 209
HIS 169 0.12 THR 62 -0.17 LYS 209
ILE 47 0.17 THR 63 -0.13 LEU 125
ILE 47 0.21 PHE 64 -0.11 ASP 210
ILE 47 0.16 SER 65 -0.21 PRO 211
VAL 176 0.12 TYR 66 -0.24 PRO 211
ILE 47 0.17 GLY 67 -0.16 PRO 211
ILE 47 0.16 VAL 68 -0.23 PRO 211
VAL 176 0.12 GLN 69 -0.30 PRO 211
ASP 76 0.14 CYS 70 -0.29 PRO 211
ASP 76 0.15 PHE 71 -0.38 PRO 211
ALA 227 0.13 SER 72 -0.43 PRO 211
ALA 227 0.16 ARG 73 -0.47 PRO 211
THR 9 0.22 TYR 74 -0.43 PRO 211
THR 9 0.36 PRO 75 -0.45 PRO 211
THR 9 0.45 ASP 76 -0.40 PRO 211
THR 9 0.33 HIS 77 -0.39 PRO 211
THR 9 0.26 MET 78 -0.37 PRO 211
THR 9 0.25 LYS 79 -0.35 PRO 211
THR 9 0.17 ARG 80 -0.31 PRO 211
THR 9 0.13 HIS 81 -0.30 PRO 211
ASP 117 0.13 ASP 82 -0.30 PRO 211
VAL 176 0.16 PHE 83 -0.24 PRO 211
VAL 176 0.14 PHE 84 -0.24 PRO 211
ASP 76 0.16 LYS 85 -0.27 PRO 211
ARG 215 0.15 SER 86 -0.23 PRO 211
ARG 215 0.18 ALA 87 -0.18 PRO 211
ARG 215 0.21 MET 88 -0.18 PRO 211
LYS 214 0.24 PRO 89 -0.16 PRO 211
LYS 214 0.27 GLU 90 -0.13 LYS 158
ARG 215 0.23 GLY 91 -0.13 LYS 158
ARG 215 0.21 TYR 92 -0.15 LYS 158
ARG 215 0.21 VAL 93 -0.14 LYS 158
TYR 182 0.22 GLN 94 -0.15 GLY 24
TYR 182 0.19 GLU 95 -0.23 LYS 126
ASP 180 0.23 ARG 96 -0.27 LYS 107
ARG 109 0.24 THR 97 -0.28 ASN 164
LYS 101 0.22 ILE 98 -0.23 GLY 228
LYS 101 0.24 PHE 99 -0.23 GLY 228
LYS 101 0.19 PHE 100 -0.21 LYS 214
GLN 157 0.24 LYS 101 -0.27 LYS 214
GLN 157 0.22 ASP 102 -0.27 LYS 214
ASP 173 0.12 ASP 103 -0.18 LYS 214
PRO 211 0.15 GLY 104 -0.20 GLY 228
ASP 102 0.22 ASN 105 -0.23 GLY 228
CYS 48 0.18 TYR 106 -0.21 ASN 164
LYS 101 0.20 LYS 107 -0.27 GLN 183
ILE 47 0.22 THR 108 -0.22 LYS 126
ARG 215 0.24 ARG 109 -0.19 GLY 24
ARG 215 0.26 ALA 110 -0.15 GLY 24
ARG 215 0.29 GLU 111 -0.13 LYS 158
ARG 215 0.26 VAL 112 -0.11 LYS 158
LYS 214 0.28 LYS 113 -0.12 LYS 158
LYS 214 0.31 PHE 114 -0.11 LYS 158
LYS 214 0.40 GLU 115 -0.12 LYS 158
LYS 214 0.39 GLY 116 -0.11 LYS 158
LYS 214 0.32 ASP 117 -0.14 PRO 211
LYS 214 0.32 THR 118 -0.13 PRO 211
ARG 215 0.28 LEU 119 -0.14 PRO 211
ARG 215 0.34 VAL 120 -0.08 LYS 158
ARG 215 0.30 ASN 121 -0.10 LYS 26
ARG 215 0.37 ARG 122 -0.14 LYS 26
ARG 215 0.32 ILE 123 -0.16 LYS 26
ARG 215 0.32 GLU 124 -0.24 ASP 21
CYS 48 0.28 LEU 125 -0.18 GLU 95
CYS 48 0.27 LYS 126 -0.23 GLU 95
PRO 211 0.26 GLY 127 -0.19 ASN 164
PRO 211 0.28 ILE 128 -0.20 GLY 228
PRO 211 0.25 ASP 129 -0.21 GLY 228
PRO 211 0.27 PHE 130 -0.16 GLY 228
PRO 211 0.27 LYS 131 -0.13 GLY 228
PRO 211 0.38 GLU 132 -0.12 THR 50
PRO 211 0.26 ASP 133 -0.26 LYS 214
PRO 211 0.16 GLY 134 -0.31 LYS 214
LEU 141 0.13 ASN 135 -0.44 LYS 214
TYR 143 0.19 ILE 136 -0.30 LYS 52
PRO 211 0.34 LEU 137 -0.24 LYS 52
TYR 143 0.30 GLY 138 -0.41 LYS 52
TYR 143 0.42 HIS 139 -0.63 LYS 52
GLU 142 0.25 LYS 140 -0.66 LYS 214
LYS 140 0.25 LEU 141 -0.72 LYS 214
LYS 140 0.25 GLU 142 -0.93 LYS 214
HIS 139 0.42 TYR 143 -0.77 LYS 214
HIS 139 0.32 ASN 144 -0.67 LYS 214
HIS 139 0.23 TYR 145 -0.54 LYS 214
GLU 142 0.23 ASN 146 -0.51 PRO 211
GLY 174 0.23 SER 147 -0.52 PRO 211
GLY 174 0.25 HIS 148 -0.42 PRO 211
GLY 174 0.27 ASN 149 -0.38 PRO 211
GLY 174 0.24 VAL 150 -0.32 PRO 211
GLY 174 0.28 TYR 151 -0.28 TYR 182
GLY 174 0.24 ILE 152 -0.25 PRO 211
GLY 174 0.27 MET 153 -0.21 PRO 211
VAL 176 0.24 ALA 154 -0.19 PRO 211
VAL 176 0.29 ASP 155 -0.16 GLY 24
VAL 176 0.26 LYS 156 -0.14 GLY 24
VAL 176 0.30 GLN 157 -0.16 ILE 188
VAL 176 0.26 LYS 158 -0.18 ILE 188
VAL 176 0.22 ASN 159 -0.13 PRO 211
VAL 176 0.23 GLY 160 -0.14 PRO 211
VAL 176 0.24 ILE 161 -0.16 PRO 211
PHE 165 0.32 LYS 162 -0.22 LYS 107
LYS 162 0.31 VAL 163 -0.23 LYS 107
PHE 165 0.54 ASN 164 -0.38 TYR 182
ASN 164 0.54 PHE 165 -0.26 GLY 228
VAL 176 0.39 LYS 166 -0.27 LYS 214
ASN 164 0.28 ILE 167 -0.34 LYS 214
VAL 176 0.32 ARG 168 -0.46 LYS 214
ASN 164 0.22 HIS 169 -0.55 LYS 214
ILE 171 0.27 ASN 170 -0.74 LYS 214
ARG 168 0.29 ILE 171 -0.83 LYS 214
ARG 168 0.21 GLU 172 -1.04 LYS 214
LYS 166 0.26 ASP 173 -1.00 LYS 214
LYS 166 0.32 GLY 174 -0.97 LYS 214
ASN 164 0.31 SER 175 -0.78 LYS 214
LYS 166 0.39 VAL 176 -0.66 LYS 214
GLN 157 0.23 GLN 177 -0.49 LYS 214
GLN 157 0.28 LEU 178 -0.40 LYS 214
VAL 176 0.26 ALA 179 -0.26 LYS 214
GLN 183 0.29 ASP 180 -0.24 GLY 228
GLN 183 0.28 HIS 181 -0.25 GLY 228
GLN 183 0.42 TYR 182 -0.38 ASN 164
TYR 182 0.42 GLN 183 -0.27 LYS 107
TYR 182 0.30 GLN 184 -0.22 LYS 162
TYR 182 0.25 ASN 185 -0.15 GLY 24
TYR 182 0.22 THR 186 -0.17 LYS 158
TYR 182 0.20 PRO 187 -0.18 LYS 158
LYS 214 0.24 ILE 188 -0.18 LYS 158
LYS 214 0.24 GLY 189 -0.15 GLN 157
LYS 214 0.22 ASP 190 -0.16 LEU 7
ARG 215 0.19 GLY 191 -0.17 LEU 7
ARG 215 0.16 PRO 192 -0.16 PRO 211
VAL 176 0.16 VAL 193 -0.18 PRO 211
VAL 176 0.15 LEU 194 -0.23 PRO 211
VAL 176 0.18 LEU 195 -0.21 PRO 211
GLY 174 0.18 PRO 196 -0.25 PRO 211
GLY 174 0.20 ASP 197 -0.26 PRO 211
GLY 174 0.23 ASN 198 -0.27 PRO 211
GLY 174 0.20 HIS 199 -0.33 PRO 211
GLY 174 0.21 TYR 200 -0.35 PRO 211
GLY 174 0.18 LEU 201 -0.40 PRO 211
GLY 174 0.18 SER 202 -0.47 PRO 211
GLY 174 0.16 THR 203 -0.48 PRO 211
HIS 139 0.14 GLN 204 -0.58 PRO 211
HIS 139 0.17 SER 205 -0.54 PRO 211
HIS 139 0.22 ALA 206 -0.66 PRO 211
HIS 139 0.20 LEU 207 -0.46 TYR 145
PRO 54 0.28 SER 208 -0.85 LYS 209
LEU 53 0.38 LYS 209 -0.85 SER 208
LYS 52 0.39 ASP 210 -0.53 LEU 221
LYS 52 0.76 PRO 211 -0.66 ALA 206
LYS 52 0.48 ASN 212 -0.54 GLY 174
THR 50 0.47 GLU 213 -0.76 GLU 172
THR 50 0.64 LYS 214 -1.04 GLU 172
THR 49 0.65 ARG 215 -0.80 GLU 172
PRO 211 0.59 ASP 216 -0.82 GLU 142
LEU 53 0.32 HIS 217 -0.57 GLU 142
LEU 53 0.24 MET 218 -0.42 GLU 142
LEU 53 0.16 VAL 219 -0.36 ASP 210
PRO 56 0.11 LEU 220 -0.38 PRO 211
HIS 139 0.12 LEU 221 -0.63 PRO 211
HIS 139 0.12 GLU 222 -0.56 PRO 211
HIS 139 0.09 PHE 223 -0.61 PRO 211
GLY 174 0.11 VAL 224 -0.50 PRO 211
ALA 227 0.13 THR 225 -0.50 PRO 211
ALA 227 0.15 ALA 226 -0.43 PRO 211
THR 9 0.17 ALA 227 -0.42 PRO 211
THR 9 0.16 GLY 228 -0.39 PRO 211
THR 9 0.21 ILE 229 -0.36 PRO 211
THR 9 0.25 THR 230 -0.37 PRO 211

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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.