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CA distance fluctuations for 250309233605806127

---  normal mode 26  ---

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
ASN 210 0.94 SER 96 -1.82 ARG 213
ASN 210 1.10 VAL 97 -0.96 ARG 213
ASP 208 1.63 PRO 98 -0.62 GLY 244
ASP 208 1.42 SER 99 -0.68 GLY 244
ASP 208 1.09 GLN 100 -0.78 GLY 245
ARG 209 1.07 LYS 101 -0.67 PHE 270
ARG 209 0.82 THR 102 -0.67 THR 125
LEU 206 0.71 TYR 103 -0.65 GLY 245
ASN 131 1.06 GLN 104 -0.57 ASP 228
ASN 131 1.00 GLY 105 -0.66 ASP 228
ASN 131 1.10 SER 106 -0.77 ASP 228
ASN 131 1.10 SER 106 -0.77 ASP 228
ASN 131 1.37 TYR 107 -0.92 ASP 228
ASN 131 1.39 GLY 108 -0.83 ASP 228
ASN 131 1.49 PHE 109 -0.64 ASP 228
ASN 131 1.40 ARG 110 -0.64 THR 125
ASN 131 1.18 LEU 111 -0.75 THR 125
LYS 132 1.17 GLY 112 -0.97 LEU 114
CYS 229 0.89 PHE 113 -1.38 THR 125
TYR 126 1.26 LEU 114 -1.01 GLN 144
SER 227 0.80 HIS 115 -0.92 TYR 220
SER 227 1.01 SER 116 -1.08 GLY 226
SER 227 0.68 VAL 122 -1.20 GLY 226
SER 227 0.93 THR 123 -1.18 GLY 226
SER 227 0.87 CYS 124 -0.96 GLY 226
SER 227 0.62 THR 125 -1.38 PHE 113
PRO 142 1.40 TYR 126 -1.00 GLU 286
ASP 148 1.50 SER 127 -1.21 ASN 288
PRO 152 1.64 PRO 128 -0.88 ASN 288
GLY 226 1.47 ALA 129 -0.64 GLN 248
ASP 148 1.27 LEU 130 -1.06 GLN 248
TRP 146 1.81 ASN 131 -1.66 LEU 289
GLY 112 1.17 LYS 132 -1.32 MET 246
SER 227 0.74 MET 133 -0.91 PHE 113
SER 227 0.67 PHE 134 -0.87 PHE 113
SER 227 0.83 CYS 135 -0.89 GLY 226
SER 227 0.87 GLN 136 -1.01 GLY 226
SER 227 0.93 LEU 137 -0.89 GLY 226
SER 227 1.01 ALA 138 -0.94 GLY 226
SER 227 1.16 LYS 139 -1.08 GLY 226
SER 227 1.16 LYS 139 -1.08 GLY 226
SER 227 1.26 THR 140 -1.07 GLY 226
TYR 126 1.14 CYS 141 -1.07 TYR 220
TYR 126 1.40 PRO 142 -1.15 TYR 220
PHE 270 1.29 VAL 143 -1.15 TYR 220
PHE 270 1.38 GLN 144 -1.01 LEU 114
ASN 131 1.49 LEU 145 -0.68 LEU 257
ASN 131 1.81 TRP 146 -0.62 LEU 114
ASN 131 1.77 VAL 147 -0.84 ASP 228
SER 127 1.50 ASP 148 -1.32 ASP 228
SER 127 1.39 SER 149 -1.30 ASP 228
PRO 128 1.49 THR 150 -0.89 PRO 153
PRO 128 1.42 PRO 151 -0.61 LEU 265
PRO 128 1.64 PRO 152 -0.75 THR 211
PRO 128 1.60 PRO 152 -0.70 THR 211
PRO 128 1.44 PRO 153 -0.59 ASP 259
PRO 128 1.29 PRO 153 -0.89 THR 150
PRO 128 1.08 GLY 154 -1.37 ASN 200
LEU 206 1.08 GLY 154 -1.29 ASN 200
LEU 206 1.24 THR 155 -1.08 ILE 232
LEU 206 1.54 ARG 156 -1.14 ILE 232
LEU 206 1.13 VAL 157 -1.03 TYR 234
LEU 206 0.79 ARG 158 -1.02 GLY 262
SER 185 0.78 ALA 159 -0.96 GLY 245
SER 185 1.00 MET 160 -1.07 GLY 245
SER 185 1.00 ALA 161 -1.41 GLY 245
ASP 208 0.95 ILE 162 -1.52 GLY 245
ASN 210 0.99 TYR 163 -1.35 GLY 244
ASN 210 0.89 LYS 164 -1.12 GLY 244
PRO 250 1.07 GLN 165 -0.94 GLY 244
ASN 210 1.06 SER 166 -0.77 GLY 244
GLN 248 1.10 GLN 167 -0.55 HIS 214
ARG 249 1.19 HIS 168 -0.99 GLY 244
ASN 210 1.32 MET 169 -1.06 GLY 244
ASN 210 1.54 THR 170 -0.89 GLY 244
ARG 249 1.48 GLU 171 -1.06 HIS 214
ARG 249 1.48 GLU 171 -1.06 HIS 214
ARG 249 1.33 VAL 172 -1.57 HIS 214
SER 240 1.13 VAL 173 -1.25 GLY 244
SER 240 1.26 ARG 174 -1.31 SER 215
THR 211 0.98 ARG 175 -1.04 TYR 205
THR 211 0.77 CYS 176 -1.14 VAL 173
THR 211 0.67 PRO 177 -1.16 ASP 207
SER 227 0.66 HIS 178 -1.22 MET 243
GLY 187 0.83 HIS 179 -1.21 CYS 242
PHE 212 0.99 GLU 180 -1.06 LEU 206
GLY 187 0.93 ARG 181 -0.89 LEU 206
GLY 187 0.98 CYS 182 -0.88 LEU 130
ARG 196 1.56 SER 185 -0.52 GLY 226
HIS 214 1.48 ASP 186 -0.78 GLY 226
PHE 212 1.40 GLY 187 -0.85 GLY 226
PHE 212 1.16 LEU 188 -1.00 GLY 226
HIS 214 1.38 ALA 189 -0.84 GLY 226
PHE 212 1.41 PRO 190 -0.77 GLY 226
PHE 212 1.47 PRO 191 -0.93 ALA 138
PHE 212 1.37 GLN 192 -1.54 TYR 205
PHE 212 1.36 GLN 192 -1.54 TYR 205
ARG 213 1.58 HIS 193 -1.42 TYR 205
ARG 213 1.13 LEU 194 -1.05 TYR 205
SER 185 1.54 ILE 195 -0.94 GLY 262
SER 185 1.56 ARG 196 -1.20 VAL 218
SER 185 1.06 VAL 197 -1.46 VAL 218
SER 227 1.12 GLU 198 -1.31 PRO 219
SER 227 1.13 GLY 199 -1.32 PRO 219
SER 227 0.97 ASN 200 -1.37 GLY 154
PRO 128 0.83 LEU 201 -1.11 GLY 154
PRO 128 0.98 ARG 202 -1.26 SER 261
PRO 128 0.86 VAL 203 -1.16 SER 261
ASP 186 0.82 GLU 204 -1.11 HIS 193
PRO 153 0.72 TYR 205 -1.54 GLN 192
ARG 156 1.54 LEU 206 -1.24 GLN 192
ARG 156 0.91 ASP 207 -1.16 PRO 177
PRO 98 1.63 ASP 208 -0.70 GLU 204
SER 99 1.31 ARG 209 -0.65 ARG 202
THR 170 1.54 ASN 210 -0.62 SER 261
MET 246 1.53 THR 211 -0.75 PRO 152
PRO 191 1.47 PHE 212 -1.25 SER 96
HIS 193 1.58 ARG 213 -1.82 SER 96
ASP 186 1.48 HIS 214 -1.57 VAL 172
SER 185 1.10 SER 215 -1.31 ARG 174
ASP 186 1.02 VAL 216 -1.11 GLY 262
PRO 128 0.81 VAL 217 -1.29 GLY 262
PRO 153 1.12 VAL 218 -1.46 VAL 197
PRO 153 1.23 PRO 219 -1.32 GLY 199
PRO 128 1.15 TYR 220 -1.85 ILE 232
ASN 131 1.38 GLU 221 -0.99 GLY 154
ASN 131 1.37 GLU 221 -0.99 GLY 154
ASN 131 1.43 PRO 222 -0.70 GLY 154
ASN 131 1.33 PRO 223 -0.69 GLY 154
PRO 128 1.17 GLU 224 -0.61 GLY 154
PRO 128 1.31 VAL 225 -0.68 SER 116
ALA 129 1.47 GLY 226 -1.20 VAL 122
THR 140 1.26 SER 227 -0.66 ASP 148
SER 127 1.02 ASP 228 -1.32 ASP 148
ASN 131 1.40 CYS 229 -0.68 THR 155
ASN 131 1.25 THR 230 -1.05 THR 155
PHE 270 1.18 THR 231 -1.26 TYR 220
PHE 270 1.28 ILE 232 -1.85 TYR 220
SER 227 1.08 HIS 233 -1.38 TYR 220
SER 185 0.93 TYR 234 -1.15 PRO 219
SER 227 0.96 ASN 235 -0.92 VAL 218
SER 185 1.00 TYR 236 -0.79 GLY 262
SER 185 0.86 MET 237 -0.98 TYR 205
THR 211 0.76 CYS 238 -1.12 VAL 272
THR 211 0.76 CYS 238 -1.12 VAL 272
THR 211 1.04 ASN 239 -0.71 LEU 130
ARG 174 1.26 SER 240 -0.93 LYS 132
THR 211 1.08 SER 241 -0.98 LEU 130
ALA 276 1.03 CYS 242 -1.21 HIS 179
ALA 276 0.92 MET 243 -1.22 HIS 178
ALA 276 0.60 GLY 244 -1.35 TYR 163
THR 211 0.96 GLY 245 -1.52 ILE 162
THR 211 1.53 MET 246 -1.50 GLU 271
THR 211 1.27 ASN 247 -0.99 LEU 130
THR 211 1.33 GLN 248 -1.08 SER 127
THR 211 1.49 ARG 249 -1.06 ASN 131
HIS 168 1.11 PRO 250 -1.34 MET 246
ASN 210 0.77 ILE 251 -1.47 MET 246
SER 185 0.81 LEU 252 -1.26 GLY 245
SER 185 0.93 THR 253 -1.12 GLY 245
ASP 208 0.82 ILE 254 -0.96 GLY 245
ASN 131 0.81 ILE 255 -0.85 GLY 245
LEU 206 0.97 THR 256 -0.77 THR 125
LEU 206 1.22 LEU 257 -0.84 THR 125
LEU 206 1.37 GLU 258 -0.77 THR 150
LEU 206 1.20 ASP 259 -0.94 ASN 200
LEU 206 1.11 SER 260 -1.20 ASN 200
PRO 128 0.73 SER 261 -1.26 ARG 202
LEU 206 0.75 GLY 262 -1.29 VAL 217
LEU 206 0.76 ASN 263 -0.85 ARG 174
LEU 206 0.88 LEU 264 -0.71 GLY 245
LEU 206 0.97 LEU 265 -0.73 THR 150
ASN 131 0.94 GLY 266 -0.65 GLY 245
LEU 206 0.81 ARG 267 -0.73 THR 125
ASN 131 0.74 ASN 268 -0.83 THR 125
ASN 131 0.76 ASN 268 -0.83 THR 125
ASP 208 0.71 SER 269 -0.82 GLY 245
GLN 144 1.38 PHE 270 -0.87 MET 246
LEU 111 0.99 GLU 271 -1.50 MET 246
LEU 111 0.94 GLU 271 -1.46 MET 246
SER 227 0.71 VAL 272 -1.12 CYS 238
THR 211 0.85 ARG 273 -0.93 LYS 132
THR 211 0.85 VAL 274 -0.72 GLY 226
SER 241 1.07 CYS 275 -0.88 GLY 226
CYS 242 1.03 ALA 276 -1.06 GLY 226
GLN 167 0.80 CYS 277 -1.16 GLY 226
GLN 167 0.67 PRO 278 -0.96 GLY 226
GLN 167 0.55 GLY 279 -0.96 GLY 226
GLN 167 0.78 ARG 280 -0.98 GLY 226
GLN 167 0.90 ASP 281 -0.79 GLY 226
SER 227 0.54 ARG 282 -0.78 TYR 126
GLN 167 0.55 ARG 283 -0.92 TYR 126
GLN 167 0.89 THR 284 -0.85 SER 127
ASN 210 0.65 GLU 285 -1.05 SER 127
SER 227 0.43 GLU 286 -1.00 ASN 131
ASN 210 0.53 GLU 287 -0.96 ASN 131
ASN 210 0.69 ASN 288 -1.21 SER 127
SER 227 0.43 LEU 289 -1.66 ASN 131

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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.