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CA distance fluctuations for 250309233605806127

---  normal mode 23  ---

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 130 0.69 SER 96 -1.53 ARG 213
TYR 163 1.24 VAL 97 -1.30 LEU 264
ARG 209 1.22 PRO 98 -1.44 LEU 264
ARG 209 1.03 SER 99 -1.20 ARG 267
ARG 209 0.78 GLN 100 -0.55 CYS 238
ARG 209 0.76 LYS 101 -0.63 PHE 270
ASP 228 0.74 THR 102 -0.68 PRO 128
ASP 228 0.98 TYR 103 -0.75 SER 99
ASP 228 1.11 GLN 104 -0.72 THR 155
ASP 228 1.33 GLY 105 -0.81 THR 155
ASP 228 1.76 SER 106 -1.41 THR 155
ASP 228 1.77 SER 106 -1.44 THR 155
ASP 228 1.32 TYR 107 -1.03 THR 155
ASP 228 1.23 GLY 108 -0.78 PRO 128
ASP 228 0.91 PHE 109 -1.06 THR 155
ASP 228 0.60 ARG 110 -0.86 VAL 157
GLN 165 0.39 LEU 111 -1.11 VAL 157
GLN 165 0.51 GLY 112 -1.11 PRO 153
ASN 131 0.95 PHE 113 -1.30 PRO 153
ASN 131 0.83 LEU 114 -1.32 PRO 153
VAL 225 0.92 HIS 115 -1.27 PRO 151
VAL 225 0.94 SER 116 -1.27 PRO 153
GLY 226 1.26 VAL 122 -1.09 PRO 151
GLY 226 1.11 THR 123 -1.14 PRO 153
GLY 226 0.95 CYS 124 -1.20 PRO 153
GLY 226 0.91 THR 125 -1.16 PRO 153
GLN 165 0.77 TYR 126 -1.02 PRO 153
GLU 285 1.31 SER 127 -0.89 PRO 153
LEU 289 1.18 PRO 128 -0.99 ASP 148
GLN 165 1.28 ALA 129 -0.93 ASP 148
GLN 165 1.56 LEU 130 -0.82 ARG 283
VAL 143 1.10 ASN 131 -0.62 LYS 101
PRO 142 1.05 LYS 132 -0.64 PRO 153
PRO 142 1.10 MET 133 -0.83 PRO 153
GLY 226 0.87 PHE 134 -0.94 PRO 153
GLY 226 0.95 CYS 135 -1.03 PRO 153
GLY 226 1.03 GLN 136 -1.01 PRO 153
GLY 226 0.94 LEU 137 -0.97 PRO 153
GLY 226 0.88 ALA 138 -1.06 CYS 182
GLY 226 0.93 LYS 139 -1.16 PRO 153
GLY 226 0.93 LYS 139 -1.16 PRO 153
GLU 198 0.81 THR 140 -1.36 PRO 153
VAL 272 1.07 CYS 141 -1.49 PRO 153
PHE 270 1.15 PRO 142 -1.71 PRO 153
PHE 270 1.23 VAL 143 -1.53 PRO 153
PHE 270 0.82 GLN 144 -1.31 PRO 153
PHE 270 0.77 LEU 145 -1.15 TYR 220
ARG 267 0.48 TRP 146 -0.91 TYR 220
LEU 265 0.95 VAL 147 -0.79 PRO 128
LEU 265 1.07 ASP 148 -0.99 PRO 128
TYR 220 1.22 SER 149 -0.62 PRO 128
VAL 217 1.39 THR 150 -0.69 GLY 226
SER 261 0.90 PRO 151 -1.31 LEU 114
SER 261 0.94 PRO 152 -1.22 LEU 114
SER 261 0.93 PRO 152 -1.28 LEU 114
SER 261 1.11 PRO 153 -1.51 THR 231
ASN 263 0.76 PRO 153 -1.75 HIS 233
THR 150 1.01 GLY 154 -1.24 SER 106
SER 149 1.01 GLY 154 -1.12 SER 106
SER 149 1.13 THR 155 -1.44 SER 106
THR 150 1.33 ARG 156 -0.97 SER 106
THR 150 1.22 VAL 157 -1.11 LEU 111
THR 150 1.29 ARG 158 -0.79 GLY 262
THR 150 1.10 ALA 159 -1.05 LEU 194
THR 150 1.09 MET 160 -1.45 LEU 194
ASP 208 1.18 ALA 161 -1.32 CYS 238
ASN 210 1.17 ILE 162 -0.98 GLY 245
VAL 97 1.24 TYR 163 -1.01 GLY 245
LEU 130 1.14 LYS 164 -0.75 GLY 244
LEU 130 1.56 GLN 165 -0.75 LEU 264
LEU 130 1.09 SER 166 -1.04 LEU 264
THR 284 1.11 GLN 167 -0.99 ASN 263
LEU 130 0.93 HIS 168 -1.12 ASN 263
LEU 130 0.79 MET 169 -1.39 LEU 264
ARG 249 1.05 THR 170 -1.32 LEU 264
ARG 249 1.45 GLU 171 -1.31 ASN 263
ARG 249 1.45 GLU 171 -1.31 ASN 263
THR 211 1.40 VAL 172 -1.55 ASN 263
SER 240 1.01 VAL 173 -1.02 ASN 263
ARG 213 1.25 ARG 174 -1.12 ASN 263
ARG 213 0.87 ARG 175 -1.10 MET 160
ARG 213 0.68 CYS 176 -0.90 ASN 263
ARG 213 0.59 PRO 177 -0.83 GLY 262
GLY 226 0.62 HIS 178 -0.91 SER 227
GLY 226 0.63 HIS 179 -0.96 SER 227
ARG 213 0.60 GLU 180 -0.96 SER 227
THR 150 0.52 ARG 181 -1.07 SER 227
GLY 226 0.54 CYS 182 -1.17 SER 227
THR 150 0.66 SER 185 -1.17 SER 227
THR 150 0.67 ASP 186 -1.24 SER 227
THR 150 0.79 GLY 187 -1.10 SER 227
THR 150 0.88 LEU 188 -0.98 SER 227
THR 150 0.85 ALA 189 -1.11 GLY 262
THR 150 0.83 PRO 190 -1.21 GLY 262
THR 150 0.71 PRO 191 -1.08 GLY 262
ARG 213 0.77 GLN 192 -1.15 GLY 262
ARG 213 0.78 GLN 192 -1.14 GLY 262
ARG 213 0.89 HIS 193 -1.34 GLY 262
ARG 213 1.11 LEU 194 -1.45 MET 160
HIS 214 1.05 ILE 195 -1.00 PRO 153
THR 150 0.81 ARG 196 -1.09 PRO 153
THR 150 0.77 VAL 197 -1.24 PRO 153
THR 140 0.81 GLU 198 -1.30 PRO 153
GLU 221 0.67 GLY 199 -1.50 PRO 153
THR 150 0.58 ASN 200 -1.28 PRO 153
THR 150 0.59 LEU 201 -1.05 PRO 153
THR 150 0.84 ARG 202 -0.85 PRO 153
THR 150 1.01 VAL 203 -0.95 GLY 262
THR 150 1.16 GLU 204 -1.23 SER 261
THR 150 1.14 TYR 205 -1.38 GLY 262
THR 150 1.31 LEU 206 -1.52 GLY 262
THR 150 1.16 ASP 207 -1.28 SER 261
ALA 161 1.18 ASP 208 -1.17 SER 261
PRO 98 1.22 ARG 209 -0.77 SER 261
VAL 97 1.24 ASN 210 -0.75 SER 261
ARG 249 1.41 THR 211 -1.07 ASN 263
SER 240 0.90 PHE 212 -1.40 ASN 263
ARG 174 1.25 ARG 213 -1.65 ASN 263
ILE 195 1.05 HIS 214 -1.55 ASN 263
THR 150 1.19 SER 215 -1.42 GLY 262
THR 150 1.16 VAL 216 -1.40 GLY 262
THR 150 1.39 VAL 217 -1.07 GLY 262
THR 150 1.23 VAL 218 -0.91 LEU 111
THR 150 1.09 PRO 219 -0.87 LEU 111
SER 149 1.22 TYR 220 -1.15 LEU 145
GLU 198 0.75 GLU 221 -0.92 GLY 154
GLU 198 0.74 GLU 221 -0.93 GLY 154
GLU 198 0.51 PRO 222 -0.89 TYR 107
PHE 270 0.47 PRO 223 -1.10 PRO 153
SER 116 0.86 GLU 224 -1.07 PRO 153
SER 116 0.94 VAL 225 -0.92 PRO 153
VAL 122 1.26 GLY 226 -0.69 THR 150
GLY 108 0.64 SER 227 -1.24 ASP 186
SER 106 1.77 ASP 228 -1.27 PRO 151
ARG 267 0.54 CYS 229 -1.29 PRO 153
PHE 270 0.76 THR 230 -1.39 PRO 153
PHE 270 0.91 THR 231 -1.51 PRO 153
PHE 270 1.27 ILE 232 -1.69 PRO 153
PHE 270 1.08 HIS 233 -1.75 PRO 153
VAL 272 1.13 TYR 234 -1.47 PRO 153
VAL 272 0.79 ASN 235 -1.26 PRO 153
ARG 213 0.92 TYR 236 -1.08 PRO 153
ARG 213 0.78 MET 237 -0.94 PRO 153
GLY 226 0.76 CYS 238 -1.31 ALA 161
GLY 226 0.76 CYS 238 -1.32 ALA 161
ARG 213 0.95 ASN 239 -0.73 PRO 153
ARG 213 1.18 SER 240 -0.58 PRO 153
THR 211 0.97 SER 241 -0.58 PRO 153
GLY 226 0.83 CYS 242 -0.67 PRO 153
GLY 226 0.78 MET 243 -0.74 ASN 263
GLY 226 0.66 GLY 244 -0.92 TYR 163
THR 211 0.86 GLY 245 -1.06 ALA 161
THR 211 1.23 MET 246 -0.85 ILE 251
THR 211 1.06 ASN 247 -0.65 LEU 264
GLU 171 1.31 GLN 248 -0.48 PRO 153
GLU 171 1.45 ARG 249 -0.49 LEU 264
THR 211 1.13 PRO 250 -0.64 MET 246
THR 211 1.05 ILE 251 -0.85 MET 246
ILE 232 0.94 LEU 252 -0.71 MET 246
ILE 232 0.90 THR 253 -0.93 CYS 238
ILE 232 0.88 ILE 254 -0.78 CYS 238
THR 150 0.90 ILE 255 -0.72 LEU 194
THR 150 0.98 THR 256 -0.82 PRO 98
THR 150 0.96 LEU 257 -0.82 SER 106
THR 150 1.06 GLU 258 -0.85 SER 96
SER 149 1.09 ASP 259 -1.02 SER 96
THR 150 1.22 SER 260 -0.85 SER 96
PRO 153 1.11 SER 261 -1.41 LEU 206
THR 150 0.90 GLY 262 -1.52 LEU 206
ASP 228 1.04 ASN 263 -1.65 ARG 213
ASP 228 1.20 LEU 264 -1.44 PRO 98
ASP 228 1.15 LEU 265 -1.37 PRO 98
ASP 228 1.02 GLY 266 -1.10 SER 99
ASP 228 0.84 ARG 267 -1.20 SER 99
ILE 232 0.73 ASN 268 -0.65 PRO 128
ILE 232 0.73 ASN 268 -0.64 PRO 128
ILE 232 0.98 SER 269 -0.66 CYS 238
ILE 232 1.27 PHE 270 -0.63 LYS 101
PRO 142 1.03 GLU 271 -0.53 CYS 238
PRO 142 1.04 GLU 271 -0.53 CYS 238
TYR 234 1.13 VAL 272 -0.60 PRO 153
THR 211 0.93 ARG 273 -0.68 PRO 153
GLY 226 0.87 VAL 274 -0.83 PRO 153
GLY 226 0.96 CYS 275 -0.84 PRO 153
GLY 226 1.06 ALA 276 -0.87 PRO 153
GLY 226 1.11 CYS 277 -0.96 PRO 153
GLY 226 1.08 PRO 278 -0.95 PRO 153
GLY 226 1.18 GLY 279 -1.00 PRO 151
GLY 226 1.07 ARG 280 -0.92 PRO 151
GLY 226 0.98 ASP 281 -0.76 PRO 153
GLY 226 1.00 ARG 282 -0.77 PRO 153
GLY 226 1.00 ARG 283 -0.82 LEU 130
GLN 167 1.11 THR 284 -0.65 PRO 151
SER 127 1.31 GLU 285 -0.55 PRO 153
PRO 128 0.93 GLU 286 -0.60 LYS 101
GLN 167 0.92 GLU 287 -0.58 PRO 151
ALA 129 1.23 ASN 288 -0.44 PRO 153
PRO 128 1.18 LEU 289 -0.47 LYS 101

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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.