CNRS Nantes University US2B US2B
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***  4tgl  ***

CA distance fluctuations for 24012217403134968

---  normal mode 10  ---

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 212 0.43 GLY 5 -0.19 SER 190
ALA 212 0.39 ILE 6 -0.17 ASP 44
ALA 212 0.31 ARG 7 -0.20 ASP 44
LEU 92 0.29 ALA 8 -0.21 ASP 44
LEU 92 0.26 ALA 9 -0.25 ASP 44
SER 135 0.29 THR 10 -0.30 ASP 44
LYS 73 0.35 SER 11 -0.35 ASP 44
LYS 73 0.40 GLN 12 -0.39 ASP 44
LYS 73 0.33 GLU 13 -0.33 ASP 44
GLU 72 0.35 ILE 14 -0.32 ASP 44
GLU 72 0.45 ASN 15 -0.43 ASP 44
GLU 72 0.46 GLU 16 -0.40 ALA 45
GLU 72 0.36 LEU 17 -0.27 ASP 44
GLU 72 0.42 THR 18 -0.38 HIS 42
GLU 72 0.40 TYR 19 -0.36 ALA 45
GLU 72 0.30 TYR 20 -0.22 ASP 44
GLU 72 0.34 THR 21 -0.17 ARG 196
GLU 72 0.33 THR 22 -0.25 THR 18
GLU 72 0.26 LEU 23 -0.13 PRO 194
GLU 72 0.21 SER 24 -0.14 PRO 209
GLU 72 0.23 ALA 25 -0.16 PRO 209
GLU 72 0.17 ASN 26 -0.18 THR 18
VAL 254 0.16 SER 27 -0.17 PRO 209
VAL 254 0.22 TYR 28 -0.18 PRO 209
VAL 254 0.16 CYS 29 -0.16 PRO 209
PRO 100 0.20 ARG 30 -0.14 ASN 15
PRO 100 0.18 THR 31 -0.19 ASN 15
ASN 120 0.16 VAL 32 -0.17 ASN 15
PRO 101 0.21 ILE 33 -0.15 LYS 50
PRO 101 0.24 PRO 34 -0.20 LYS 50
ASN 120 0.21 GLY 35 -0.15 ASN 15
ALA 124 0.22 ALA 36 -0.21 LYS 50
ALA 124 0.21 THR 37 -0.18 ASN 15
ALA 124 0.15 TRP 38 -0.25 ASN 15
ALA 124 0.15 ASP 39 -0.28 ASN 15
SER 83 0.16 CYS 40 -0.31 ASN 15
SER 83 0.20 ILE 41 -0.32 ASN 15
GLU 72 0.19 HIS 42 -0.40 ASN 15
SER 83 0.14 CYS 43 -0.36 ASN 15
ASP 128 0.14 ASP 44 -0.43 ASN 15
SER 71 0.22 ALA 45 -0.42 ASN 15
GLY 69 0.21 THR 46 -0.27 TYR 19
ASP 128 0.16 GLU 47 -0.26 ASN 15
ASP 128 0.16 ASP 48 -0.15 SER 167
THR 46 0.18 LEU 49 -0.16 THR 57
ASP 128 0.24 LYS 50 -0.27 ILE 51
ASP 128 0.18 ILE 51 -0.27 LYS 50
ALA 124 0.26 ILE 52 -0.37 LYS 53
ALA 124 0.25 LYS 53 -0.37 ILE 52
PRO 101 0.25 THR 54 -0.28 THR 57
PRO 101 0.30 TRP 55 -0.33 THR 57
PRO 100 0.34 SER 56 -0.29 ASP 61
PRO 100 0.34 THR 57 -0.44 THR 125
VAL 254 0.41 LEU 58 -0.41 ASP 128
VAL 254 0.43 ILE 59 -0.41 GLU 121
VAL 254 0.47 TYR 60 -0.36 GLU 121
VAL 254 0.44 ASP 61 -0.29 SER 56
VAL 254 0.36 THR 62 -0.27 THR 125
VAL 254 0.27 ASN 63 -0.21 ASN 87
PRO 101 0.24 ALA 64 -0.31 MET 65
VAL 123 0.18 MET 65 -0.31 ALA 64
ALA 124 0.18 VAL 66 -0.30 THR 57
ASP 128 0.20 ALA 67 -0.27 THR 57
THR 21 0.20 ARG 68 -0.26 THR 57
THR 22 0.26 GLY 69 -0.20 THR 57
GLU 16 0.29 ASP 70 -0.23 THR 57
ASN 15 0.34 SER 71 -0.18 VAL 118
GLU 16 0.46 GLU 72 -0.23 ASN 168
GLU 16 0.44 LYS 73 -0.23 VAL 118
GLU 16 0.37 THR 74 -0.22 VAL 118
GLU 16 0.20 ILE 75 -0.27 VAL 118
THR 21 0.17 TYR 76 -0.21 VAL 118
LEU 127 0.15 ILE 77 -0.19 VAL 118
VAL 254 0.17 VAL 78 -0.12 ALA 90
VAL 254 0.20 PHE 79 -0.16 PRO 209
VAL 254 0.27 ARG 80 -0.19 PRO 209
VAL 254 0.37 GLY 81 -0.25 PRO 209
VAL 254 0.62 SER 82 -0.22 PRO 209
VAL 254 0.56 SER 83 -0.21 PRO 209
VAL 254 0.64 SER 84 -0.25 SER 56
VAL 254 0.74 ILE 85 -0.25 SER 56
VAL 254 0.64 ARG 86 -0.30 GLU 121
VAL 254 0.69 ASN 87 -0.26 GLU 121
VAL 254 0.89 TRP 88 -0.23 GLU 121
VAL 254 0.81 ILE 89 -0.34 GLU 117
VAL 254 0.61 ALA 90 -0.41 SER 114
ILE 204 0.79 ASP 91 -0.25 GLY 116
PRO 250 0.88 LEU 92 -0.29 GLY 116
PRO 250 0.66 THR 93 -0.32 GLY 116
LEU 208 0.68 PHE 94 -0.25 ALA 124
PRO 250 0.48 VAL 95 -0.25 ALA 124
LEU 208 0.34 PRO 96 -0.22 ASP 156
LEU 208 0.28 VAL 97 -0.28 ARG 160
ASP 113 0.29 SER 98 -0.27 ARG 160
GLY 116 0.40 TYR 99 -0.25 SER 98
GLY 116 0.58 PRO 100 -0.36 GLU 161
GLY 116 0.53 PRO 101 -0.32 GLU 161
GLY 116 0.39 VAL 102 -0.21 SER 190
GLY 116 0.38 SER 103 -0.26 SER 190
GLY 116 0.28 GLY 104 -0.20 ASN 186
GLY 116 0.24 THR 105 -0.12 LEU 239
ASP 113 0.20 LYS 106 -0.15 ARG 160
LEU 208 0.26 VAL 107 -0.23 ASP 156
LEU 208 0.44 HIS 108 -0.23 ASP 156
LEU 208 0.45 LYS 109 -0.32 ASP 156
LEU 208 0.50 GLY 110 -0.35 GLY 116
VAL 205 0.37 PHE 111 -0.23 VAL 123
ASP 113 0.32 LEU 112 -0.32 ASP 156
PRO 100 0.38 ASP 113 -0.52 GLY 116
VAL 254 0.35 SER 114 -0.41 ALA 90
PRO 100 0.40 TYR 115 -0.35 ALA 90
PRO 100 0.58 GLY 116 -0.52 ASP 113
PRO 100 0.49 GLU 117 -0.43 ASP 128
PRO 101 0.37 VAL 118 -0.53 LEU 122
PRO 101 0.37 GLN 119 -0.40 ASP 113
PRO 101 0.33 ASN 120 -0.46 ALA 124
PRO 101 0.30 GLU 121 -0.47 ASP 128
PRO 101 0.25 LEU 122 -0.53 VAL 118
THR 54 0.22 VAL 123 -0.38 ASP 113
THR 125 0.28 ALA 124 -0.46 ASN 120
ALA 124 0.28 THR 125 -0.47 VAL 118
LEU 127 0.21 VAL 126 -0.41 VAL 118
ILE 52 0.23 LEU 127 -0.39 ASN 120
ILE 52 0.25 ASP 128 -0.47 GLU 121
LYS 50 0.19 GLN 129 -0.42 VAL 118
GLN 12 0.22 PHE 130 -0.37 VAL 118
GLN 12 0.24 LYS 131 -0.37 ASN 120
GLN 12 0.26 GLN 132 -0.35 LEU 58
GLN 12 0.30 TYR 133 -0.32 VAL 118
GLN 12 0.32 PRO 134 -0.30 VAL 118
GLN 12 0.39 SER 135 -0.31 GLY 163
GLN 12 0.38 TYR 136 -0.26 VAL 118
GLN 12 0.29 LYS 137 -0.21 VAL 118
ALA 139 0.26 VAL 138 -0.23 VAL 118
VAL 138 0.26 ALA 139 -0.14 THR 46
LEU 127 0.14 VAL 140 -0.12 LEU 112
THR 74 0.16 THR 141 -0.12 LEU 151
HIS 143 0.22 GLY 142 -0.14 PRO 209
GLY 142 0.22 HIS 143 -0.21 PRO 209
LEU 145 0.31 SER 144 -0.28 PRO 209
ILE 204 0.36 LEU 145 -0.26 PRO 209
VAL 254 0.23 GLY 146 -0.20 PRO 209
ILE 204 0.14 GLY 147 -0.16 PRO 209
ILE 204 0.20 ALA 148 -0.16 PRO 209
PRO 101 0.21 THR 149 -0.16 PHE 94
VAL 254 0.15 ALA 150 -0.11 PRO 209
PRO 101 0.11 LEU 151 -0.12 THR 141
PRO 101 0.21 LEU 152 -0.19 LYS 109
PRO 101 0.17 CYS 153 -0.25 LEU 112
VAL 254 0.10 ALA 154 -0.18 LYS 109
SER 56 0.12 LEU 155 -0.20 LYS 109
GLU 121 0.16 ASP 156 -0.32 LEU 112
THR 54 0.15 LEU 157 -0.26 LYS 109
THR 125 0.11 TYR 158 -0.25 PRO 100
GLU 121 0.14 GLN 159 -0.35 PRO 100
THR 125 0.16 ARG 160 -0.33 PRO 100
THR 125 0.15 GLU 161 -0.36 PRO 100
ILE 52 0.15 GLU 162 -0.29 PRO 100
LYS 131 0.19 GLY 163 -0.31 SER 135
GLN 12 0.14 LEU 164 -0.23 PRO 100
LYS 131 0.15 SER 165 -0.24 PRO 100
LYS 131 0.14 SER 166 -0.19 PRO 101
PRO 134 0.19 SER 167 -0.23 GLU 72
PRO 134 0.22 ASN 168 -0.23 GLU 72
LYS 131 0.18 LEU 169 -0.15 GLU 72
LEU 171 0.18 PHE 170 -0.18 ALA 45
PHE 170 0.18 LEU 171 -0.16 ALA 45
THR 173 0.19 TYR 172 -0.17 ASP 44
TYR 172 0.19 THR 173 -0.12 HIS 42
LEU 92 0.26 GLN 174 -0.12 ALA 25
ASP 91 0.40 GLY 175 -0.14 THR 265
ASP 91 0.34 GLN 176 -0.15 LEU 216
LEU 92 0.36 PRO 177 -0.23 PRO 209
SER 242 0.26 ARG 178 -0.17 PHE 215
SER 242 0.20 VAL 179 -0.12 ALA 148
LEU 208 0.15 GLY 180 -0.11 ASP 156
ASP 113 0.12 ASN 181 -0.10 GLY 266
GLY 214 0.14 PRO 182 -0.18 ASN 246
GLY 116 0.15 ALA 183 -0.20 LEU 239
GLY 116 0.17 PHE 184 -0.15 ALA 185
GLU 117 0.12 ALA 185 -0.15 ASN 246
SER 190 0.14 ASN 186 -0.25 SER 103
GLY 116 0.17 TYR 187 -0.24 SER 103
GLY 116 0.14 VAL 188 -0.19 SER 220
GLY 192 0.17 VAL 189 -0.21 SER 103
ASN 186 0.14 SER 190 -0.26 SER 103
GLU 162 0.11 THR 191 -0.22 SER 103
VAL 189 0.17 GLY 192 -0.18 SER 103
ALA 218 0.16 ILE 193 -0.16 ALA 45
GLY 219 0.20 PRO 194 -0.22 ALA 45
PRO 194 0.18 TYR 195 -0.18 ALA 45
TYR 136 0.20 ARG 196 -0.20 ASP 44
LEU 92 0.25 ARG 197 -0.16 HIS 42
LEU 92 0.31 THR 198 -0.18 HIS 42
LEU 92 0.42 VAL 199 -0.15 GLU 240
LEU 92 0.44 ASN 200 -0.14 GLU 240
LEU 92 0.50 GLU 201 -0.15 GLU 240
LEU 92 0.64 ARG 202 -0.19 GLU 240
LEU 92 0.66 ASP 203 -0.19 GLU 240
LEU 92 0.87 ILE 204 -0.18 GLU 240
ASP 91 0.78 VAL 205 -0.17 LEU 208
LEU 92 0.57 PRO 206 -0.21 LEU 216
LEU 92 0.70 HIS 207 -0.25 LEU 216
LEU 92 0.81 LEU 208 -0.27 ALA 211
SER 242 0.51 PRO 209 -0.28 SER 144
SER 242 0.68 PRO 210 -0.26 LEU 208
SER 242 0.66 ALA 211 -0.27 LEU 208
SER 242 0.63 ALA 212 -0.21 LEU 208
SER 242 0.48 PHE 213 -0.19 LEU 145
SER 242 0.33 GLY 214 -0.14 SER 144
SER 242 0.32 PHE 215 -0.17 ARG 178
LEU 239 0.26 LEU 216 -0.25 HIS 207
LEU 92 0.23 HIS 217 -0.16 ALA 183
PRO 194 0.18 ALA 218 -0.18 ASN 246
PRO 194 0.20 GLY 219 -0.18 VAL 188
ALA 211 0.24 SER 220 -0.20 VAL 189
LEU 92 0.33 GLU 221 -0.17 SER 220
LEU 92 0.32 TYR 222 -0.19 HIS 42
LEU 92 0.40 TRP 223 -0.15 HIS 42
LEU 92 0.38 ILE 224 -0.15 HIS 42
LEU 92 0.42 THR 225 -0.11 ASN 186
LEU 92 0.38 ASP 226 -0.10 PHE 251
LEU 92 0.33 ASN 227 -0.12 ILE 41
GLU 72 0.33 SER 228 -0.12 ILE 41
GLU 72 0.33 PRO 229 -0.17 ILE 41
GLU 72 0.33 GLU 230 -0.18 ILE 41
LEU 92 0.32 THR 231 -0.18 HIS 42
LEU 92 0.33 VAL 232 -0.19 ASP 44
LEU 92 0.35 GLN 233 -0.18 ASP 44
LEU 92 0.32 VAL 234 -0.19 ASP 44
ALA 211 0.38 CYS 235 -0.17 ASP 44
ALA 211 0.34 THR 236 -0.22 SER 190
ALA 212 0.34 SER 237 -0.27 ASP 243
ALA 211 0.26 ASP 238 -0.21 SER 103
ALA 211 0.29 LEU 239 -0.26 ASN 246
ALA 211 0.38 GLU 240 -0.34 ASN 246
ALA 211 0.61 THR 241 -0.26 LEU 239
PRO 210 0.68 SER 242 -0.29 SER 247
PRO 210 0.53 ASP 243 -0.27 SER 237
LEU 92 0.46 CYS 244 -0.23 SER 237
LEU 92 0.54 SER 245 -0.26 GLU 240
LEU 92 0.57 ASN 246 -0.34 GLU 240
LEU 92 0.59 SER 247 -0.29 SER 242
LEU 92 0.64 ILE 248 -0.22 GLU 240
LEU 92 0.77 VAL 249 -0.27 GLU 240
LEU 92 0.88 PRO 250 -0.20 GLU 240
LEU 92 0.79 PHE 251 -0.21 GLU 240
LEU 92 0.84 THR 252 -0.20 GLU 240
TRP 88 0.77 SER 253 -0.17 GLU 240
TRP 88 0.89 VAL 254 -0.16 ALA 212
TRP 88 0.67 LEU 255 -0.13 GLU 240
TRP 88 0.57 ASP 256 -0.15 GLU 240
TRP 88 0.56 HIS 257 -0.16 LEU 216
TRP 88 0.50 LEU 258 -0.13 LEU 208
TRP 88 0.38 SER 259 -0.12 LEU 216
TRP 88 0.31 TYR 260 -0.14 ILE 263
GLU 72 0.36 PHE 261 -0.19 ILE 41
GLU 72 0.36 GLY 262 -0.15 ILE 41
GLU 72 0.31 ILE 263 -0.16 SER 11
SER 83 0.28 ASN 264 -0.14 PRO 209
SER 83 0.30 THR 265 -0.18 PRO 209
SER 83 0.46 GLY 266 -0.23 PRO 209
SER 83 0.46 LEU 267 -0.18 PRO 209
SER 83 0.29 CYS 268 -0.16 PRO 209
SER 83 0.30 THR 269 -0.17 SER 11

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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).
Last modification: April 25th, 2023.