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CA distance fluctuations for 250309222730602077

---  normal mode 17  ---

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
LEU 264 1.03 SER 96 -0.57 GLY 244
ASN 263 0.79 VAL 97 -0.76 THR 211
TYR 103 1.10 PRO 98 -1.20 ASP 208
ASN 131 1.12 SER 99 -1.05 ASP 208
ASN 131 1.55 GLN 100 -0.79 THR 256
PRO 128 1.52 LYS 101 -0.74 THR 256
PRO 128 1.26 THR 102 -0.46 GLU 221
PRO 98 1.10 TYR 103 -0.81 GLU 221
PRO 98 0.77 GLN 104 -1.13 GLU 221
SER 96 0.78 GLY 105 -1.20 GLU 221
SER 96 0.73 SER 106 -1.34 GLU 221
SER 96 0.74 SER 106 -1.33 GLU 221
THR 230 0.75 TYR 107 -1.72 GLU 221
PRO 98 0.52 GLY 108 -1.61 GLU 221
ILE 232 0.60 PHE 109 -1.21 TYR 220
THR 102 0.62 ARG 110 -1.20 VAL 218
THR 150 0.76 LEU 111 -1.36 ALA 159
PRO 151 0.95 GLY 112 -1.09 PHE 270
PRO 151 1.02 PHE 113 -1.11 CYS 229
PRO 151 1.07 LEU 114 -1.27 CYS 229
PRO 151 1.02 HIS 115 -1.36 SER 227
PRO 151 1.13 SER 116 -1.27 PRO 191
GLY 262 1.08 VAL 122 -1.15 GLY 226
GLY 262 1.22 THR 123 -1.22 PRO 191
GLY 262 1.12 CYS 124 -1.13 PRO 191
GLY 262 0.99 THR 125 -1.19 ASP 228
GLN 100 1.05 TYR 126 -1.28 ASP 228
LYS 101 1.20 SER 127 -1.33 ASP 228
LYS 101 1.52 PRO 128 -1.32 ASP 228
LYS 101 1.52 ALA 129 -1.20 ASP 228
LYS 101 1.34 LEU 130 -1.10 ASP 228
GLN 100 1.55 ASN 131 -1.05 ASP 228
GLN 100 1.06 LYS 132 -1.04 ASP 228
GLN 100 0.93 MET 133 -1.05 CYS 229
GLY 262 1.08 PHE 134 -1.00 ASP 228
GLY 262 1.24 CYS 135 -0.95 PRO 191
GLY 262 1.36 GLN 136 -0.99 PRO 191
GLY 262 1.53 LEU 137 -0.98 GLU 180
GLY 262 1.68 ALA 138 -1.17 GLU 180
GLY 262 1.48 LYS 139 -1.43 PRO 191
GLY 262 1.48 LYS 139 -1.43 PRO 191
GLY 262 1.32 THR 140 -1.74 PRO 191
SER 269 1.31 CYS 141 -1.39 PRO 191
PRO 151 1.27 PRO 142 -1.28 PRO 191
PRO 151 1.19 VAL 143 -1.11 PRO 191
PRO 151 1.33 GLN 144 -1.06 ILE 195
THR 150 1.03 LEU 145 -1.41 VAL 218
THR 150 1.10 TRP 146 -1.40 VAL 218
LEU 289 0.53 VAL 147 -1.80 PRO 219
LEU 289 0.39 ASP 148 -1.23 PRO 219
CYS 229 0.42 SER 149 -1.30 GLU 221
GLN 144 1.22 THR 150 -1.16 ASP 259
THR 231 1.50 PRO 151 -1.00 ASN 263
CYS 229 1.56 PRO 152 -0.86 SER 260
CYS 229 1.54 PRO 152 -0.85 SER 260
CYS 229 1.36 PRO 153 -1.05 LEU 188
CYS 229 1.20 PRO 153 -0.92 LEU 188
THR 230 0.97 GLY 154 -1.19 LEU 188
THR 230 0.94 GLY 154 -1.17 LEU 188
THR 230 1.15 THR 155 -0.78 THR 150
HIS 233 0.97 ARG 156 -0.86 VAL 147
VAL 197 1.39 VAL 157 -0.89 VAL 147
VAL 197 1.20 ARG 158 -0.82 LEU 111
ASN 263 1.18 ALA 159 -1.36 LEU 111
ASN 263 1.40 MET 160 -1.10 LEU 111
ASN 263 1.32 ALA 161 -0.98 LEU 111
ASN 263 1.18 ILE 162 -0.75 LEU 111
ASN 263 0.99 TYR 163 -0.69 LEU 111
ASN 263 0.78 LYS 164 -0.71 SER 269
SER 185 0.74 GLN 165 -0.65 SER 269
ASN 263 0.72 SER 166 -0.50 SER 269
ASN 263 0.82 GLN 167 -0.87 ARG 248
ASN 263 0.98 HIS 168 -1.03 ARG 249
ASN 263 0.98 MET 169 -0.62 ASN 247
ASN 263 1.13 THR 170 -0.75 ASN 247
ASN 263 1.20 GLU 171 -1.03 ASN 247
ASN 263 1.20 GLU 171 -1.03 ASN 247
ASN 263 1.34 VAL 172 -0.67 LEU 111
ASN 263 1.27 VAL 173 -0.81 LEU 111
ASN 263 1.30 ARG 174 -0.66 LEU 111
SER 261 1.43 ARG 175 -0.67 LEU 111
SER 261 1.28 CYS 176 -0.64 GLU 171
SER 185 1.32 PRO 177 -0.59 LEU 111
LEU 188 1.67 HIS 178 -0.55 GLU 171
SER 261 1.68 HIS 179 -0.67 CYS 242
SER 261 1.47 GLU 180 -1.17 ALA 138
SER 261 1.40 ARG 181 -0.94 ALA 138
SER 261 1.50 CYS 182 -0.75 ALA 276
GLY 244 1.41 SER 185 -1.05 GLY 199
MET 243 1.34 ASP 186 -0.98 VAL 147
HIS 178 1.54 GLY 187 -1.01 GLY 154
HIS 178 1.67 LEU 188 -1.19 GLY 154
HIS 179 1.61 ALA 189 -1.02 VAL 147
SER 261 1.46 PRO 190 -1.35 VAL 197
SER 261 1.04 PRO 191 -1.74 THR 140
ASN 263 1.39 GLN 192 -0.84 ASN 235
ASN 263 1.39 GLN 192 -0.86 ASN 235
SER 261 1.61 HIS 193 -0.88 LEU 111
SER 261 1.52 LEU 194 -0.90 LEU 111
GLY 262 1.61 ILE 195 -1.08 LEU 111
GLY 262 1.69 ARG 196 -0.91 GLN 144
VAL 157 1.39 VAL 197 -1.35 PRO 190
GLY 262 1.33 GLU 198 -1.18 PRO 190
GLU 224 1.31 GLY 199 -1.05 SER 185
GLU 224 1.65 ASN 200 -0.96 LEU 145
GLU 224 1.11 LEU 201 -1.26 VAL 147
GLU 224 1.01 ARG 202 -1.40 VAL 147
GLY 262 1.13 VAL 203 -1.20 VAL 147
SER 261 1.21 GLU 204 -1.11 VAL 147
SER 261 1.54 TYR 205 -0.86 VAL 147
SER 261 1.44 LEU 206 -0.91 SER 99
ASN 263 1.38 ASP 207 -0.91 SER 99
ASN 263 1.30 ASP 208 -1.20 PRO 98
ASN 263 1.05 ARG 209 -1.03 PRO 98
ASN 263 1.02 ASN 210 -0.98 PRO 98
ASN 263 1.18 THR 211 -1.15 PRO 98
ASN 263 1.31 PHE 212 -0.94 PRO 98
ASN 263 1.57 ARG 213 -0.89 PRO 98
ASN 263 1.87 HIS 214 -0.85 LEU 111
ASN 263 1.67 SER 215 -1.04 LEU 111
ASN 263 1.39 VAL 216 -1.17 LEU 111
ASN 263 1.05 VAL 217 -1.16 LEU 111
SER 260 0.91 VAL 218 -1.48 VAL 147
SER 260 1.06 PRO 219 -1.80 VAL 147
ASN 200 1.21 TYR 220 -1.21 PHE 109
ASN 200 1.33 GLU 221 -1.71 TYR 107
ASN 200 1.32 GLU 221 -1.72 TYR 107
PRO 153 0.92 PRO 222 -1.31 GLY 108
PRO 153 1.10 PRO 223 -0.98 ASP 148
ASN 200 1.65 GLU 224 -0.85 ASP 148
CYS 182 1.06 VAL 225 -0.55 SER 106
PRO 152 0.89 GLY 226 -1.26 HIS 115
PRO 152 1.12 SER 227 -1.36 HIS 115
PRO 153 1.12 ASP 228 -1.33 SER 127
PRO 152 1.56 CYS 229 -1.27 LEU 114
PRO 152 1.52 THR 230 -0.88 PRO 191
PRO 151 1.50 THR 231 -1.03 PRO 191
LEU 257 1.70 ILE 232 -1.09 PRO 191
THR 256 1.52 HIS 233 -1.35 PRO 191
ILE 255 1.66 TYR 234 -1.27 PRO 191
GLY 262 1.50 ASN 235 -1.29 PRO 191
GLY 262 1.62 TYR 236 -0.85 PRO 191
GLY 262 1.71 MET 237 -0.95 GLU 180
GLY 262 1.43 CYS 238 -0.63 GLY 112
GLY 262 1.43 CYS 238 -0.63 GLY 112
GLY 262 1.30 ASN 239 -0.61 ASP 228
GLY 262 1.17 SER 240 -0.65 ASP 228
GLY 262 1.05 SER 241 -0.68 HIS 168
ASP 186 1.18 CYS 242 -0.72 GLU 171
ASP 186 1.34 MET 243 -0.91 GLU 171
SER 185 1.41 GLY 244 -0.98 GLU 171
SER 185 1.14 GLY 245 -0.94 GLU 171
SER 261 1.02 MET 246 -0.93 GLU 171
ASP 186 1.07 ASN 247 -1.03 GLU 171
ASP 186 0.93 ARG 248 -0.99 HIS 168
SER 261 0.86 ARG 249 -1.03 HIS 168
ASN 263 0.85 PRO 250 -0.73 ASP 228
ASN 263 0.97 ILE 251 -0.79 GLY 112
ASN 263 0.92 LEU 252 -0.89 GLY 112
ASN 263 0.99 THR 253 -1.14 LEU 111
TYR 234 1.11 ILE 254 -0.82 LEU 111
TYR 234 1.66 ILE 255 -0.73 LEU 111
ILE 232 1.61 THR 256 -0.79 GLN 100
ILE 232 1.70 LEU 257 -0.66 LEU 206
ILE 232 1.37 GLU 258 -0.71 LYS 101
ILE 232 0.87 ASP 259 -1.16 THR 150
PRO 219 1.06 SER 260 -0.86 THR 150
HIS 179 1.68 SER 261 -0.80 PRO 151
MET 237 1.71 GLY 262 -0.41 PRO 151
HIS 214 1.87 ASN 263 -1.00 PRO 151
TYR 234 1.07 LEU 264 -0.63 PRO 151
ILE 232 0.93 LEU 265 -0.90 TYR 220
ILE 232 1.14 GLY 266 -0.81 TYR 220
ILE 232 1.15 ARG 267 -0.59 GLU 221
ILE 232 1.21 ASN 268 -0.46 GLN 165
ILE 232 1.22 ASN 268 -0.47 LYS 164
CYS 141 1.31 SER 269 -0.71 LYS 164
GLN 100 1.17 PHE 270 -1.09 GLY 112
GLU 271 1.05 GLU 271 -1.01 GLY 112
GLU 271 1.05 GLU 271 -1.02 GLY 112
GLY 262 0.96 VAL 272 -1.02 GLY 112
GLY 262 1.05 ARG 273 -0.85 ASP 228
GLY 262 1.28 VAL 274 -0.76 ASP 228
GLY 262 1.20 CYS 275 -0.77 ASP 228
GLY 262 1.18 ALA 276 -0.75 GLY 226
GLY 262 1.08 CYS 277 -0.92 GLY 226
GLY 262 1.07 PRO 278 -1.00 ASP 228
GLY 262 0.95 GLY 279 -1.15 ASP 228
GLY 262 0.91 ARG 280 -1.08 ASP 228
GLY 262 0.93 ASP 281 -1.00 ASP 228
GLY 262 0.87 ARG 282 -1.10 ASP 228
GLY 262 0.78 ARG 283 -1.16 ASP 228
LYS 101 0.83 THR 284 -0.98 ASP 228
LYS 101 0.99 GLU 285 -0.86 ASP 228
LYS 101 0.96 GLU 286 -0.91 ASP 228
LYS 101 0.95 GLU 287 -0.92 ASP 228
LYS 101 1.14 ASN 288 -0.73 ASP 228
LYS 101 1.28 LEU 289 -0.64 ASP 228

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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 8th, 2025.