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CA distance fluctuations for 2404111555113701030

---  normal mode 16  ---

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 288 0.74 VAL 97 -1.07 GLU 171
ILE 254 1.04 PRO 98 -0.78 ARG 213
GLU 285 1.07 SER 99 -0.63 ARG 213
GLU 285 1.17 GLN 100 -0.56 HIS 214
GLU 285 1.42 LYS 101 -0.46 ARG 213
GLU 285 1.63 THR 102 -0.33 LEU 206
GLU 285 1.65 TYR 103 -0.40 LEU 206
LEU 130 1.66 GLN 104 -0.30 LEU 206
LEU 289 1.55 GLY 105 -0.42 LEU 206
LEU 289 1.75 SER 106 -0.54 PRO 151
LEU 289 1.60 TYR 107 -0.35 LEU 206
LEU 130 1.78 GLY 108 -0.24 LEU 206
LEU 130 1.49 PHE 109 -0.16 THR 256
ASN 131 1.75 ARG 110 -0.10 THR 256
SER 127 1.45 LEU 111 -0.25 ILE 254
SER 127 1.51 GLY 112 -0.51 ILE 254
PRO 151 1.02 PHE 113 -1.65 PHE 270
PRO 151 0.80 LEU 114 -0.99 PHE 270
PRO 151 0.72 HIS 115 -0.57 PHE 270
SER 121 0.58 SER 116 -0.69 GLY 226
PRO 151 0.59 SER 121 -0.99 ARG 280
PRO 151 0.54 VAL 122 -0.63 VAL 225
PRO 151 0.49 THR 123 -0.60 VAL 225
PRO 151 0.63 CYS 124 -0.45 GLY 226
PRO 151 0.87 THR 125 -0.25 GLY 226
LEU 111 1.16 TYR 126 -0.29 PRO 250
GLY 112 1.51 SER 127 -0.57 ARG 248
PRO 151 1.77 PRO 128 -0.47 ARG 248
VAL 147 1.73 ALA 129 -0.68 ARG 248
GLY 108 1.78 LEU 130 -0.95 ARG 248
ARG 110 1.75 ASN 131 -0.57 PRO 250
ARG 282 0.89 LYS 132 -0.60 PHE 113
LEU 111 0.80 MET 133 -0.55 LEU 114
PRO 151 0.76 PHE 134 -0.34 LEU 130
PRO 151 0.58 CYS 135 -0.35 GLY 226
PRO 151 0.44 GLN 136 -0.46 GLY 262
PRO 151 0.37 LEU 137 -0.55 GLY 262
PRO 151 0.32 ALA 138 -0.67 GLY 262
PRO 151 0.38 LYS 139 -0.60 GLY 262
PRO 151 0.43 THR 140 -0.64 ARG 158
TYR 126 0.58 CYS 141 -0.65 ILE 254
PRO 151 0.66 PRO 142 -0.78 ILE 255
TYR 126 1.07 VAL 143 -1.00 ILE 255
PRO 128 1.18 GLN 144 -0.59 ILE 255
PRO 128 1.51 LEU 145 -0.48 ILE 255
PRO 128 1.73 TRP 146 -0.24 THR 256
ALA 129 1.73 VAL 147 -0.37 LEU 257
ALA 129 1.72 ASP 148 -0.37 ARG 156
LEU 289 1.60 SER 149 -0.57 THR 155
LEU 289 1.42 THR 150 -1.18 THR 155
PRO 128 1.77 PRO 151 -0.54 SER 106
LEU 289 1.54 PRO 152 -0.24 LEU 188
LEU 289 1.22 PRO 153 -0.55 THR 150
LEU 289 1.10 GLY 154 -0.68 THR 150
LEU 289 1.12 THR 155 -1.18 THR 150
ASN 210 1.00 ARG 156 -0.98 THR 150
ASN 210 0.96 VAL 157 -1.01 ILE 232
ASP 208 1.17 ARG 158 -0.92 TYR 234
ASP 208 0.80 ALA 159 -0.85 TYR 234
ASP 208 0.65 MET 160 -0.56 PHE 113
THR 211 0.51 ALA 161 -0.70 PHE 113
THR 211 0.52 ILE 162 -0.76 PHE 113
THR 284 0.46 TYR 163 -0.76 PHE 113
THR 284 0.64 LYS 164 -0.85 PHE 113
THR 284 0.57 GLN 165 -0.73 PHE 113
THR 284 0.31 GLU 171 -1.07 VAL 97
THR 284 0.27 VAL 172 -0.78 VAL 97
THR 284 0.27 VAL 173 -0.53 PHE 113
THR 284 0.16 ARG 174 -0.58 PHE 212
PRO 151 0.17 ARG 175 -0.58 GLY 262
PRO 151 0.16 CYS 176 -0.58 PHE 212
PRO 151 0.13 PRO 177 -0.63 PHE 212
ALA 138 0.18 HIS 178 -0.55 SER 261
ALA 138 0.21 HIS 179 -0.60 SER 261
TYR 126 0.19 GLU 180 -0.67 SER 261
THR 140 0.21 ARG 181 -0.67 SER 261
GLU 198 0.42 SER 185 -0.79 SER 261
GLU 198 0.46 ASP 186 -1.01 LEU 201
PRO 128 0.42 GLY 187 -1.04 LEU 201
PRO 128 0.50 LEU 188 -1.08 SER 261
PRO 128 0.46 ALA 189 -1.02 GLY 262
PRO 128 0.38 PRO 190 -0.92 GLY 262
TYR 126 0.28 PRO 191 -0.80 SER 261
TYR 126 0.23 GLN 192 -0.80 PHE 212
PRO 128 0.32 HIS 193 -0.80 GLY 262
TYR 126 0.31 LEU 194 -0.67 GLY 262
TYR 126 0.52 ILE 195 -0.73 GLY 262
PRO 128 0.53 ARG 196 -0.83 GLY 262
PRO 128 0.63 VAL 197 -0.87 ARG 158
PRO 128 0.56 GLU 198 -0.80 PRO 219
PRO 128 0.66 GLY 199 -0.88 PRO 219
PRO 128 1.12 ASN 200 -0.69 SER 261
PRO 128 1.03 LEU 201 -1.04 GLY 187
PRO 128 1.00 ARG 202 -0.93 SER 261
PRO 128 0.92 VAL 203 -1.04 GLY 262
PRO 128 0.75 GLU 204 -1.54 GLY 262
PRO 128 0.62 TYR 205 -1.30 GLY 262
PRO 128 0.51 LEU 206 -1.14 GLY 262
PRO 128 0.43 ASP 207 -0.69 ASN 263
ARG 158 1.17 ASP 208 -0.41 GLN 192
ARG 156 0.95 ARG 209 -0.59 PRO 191
ARG 156 1.00 ASN 210 -0.54 PRO 177
ARG 158 0.92 THR 211 -0.43 PRO 177
ARG 158 0.51 PHE 212 -0.80 GLN 192
ASN 288 0.42 ARG 213 -0.78 PRO 98
ASN 288 0.37 HIS 214 -0.73 GLY 262
PRO 128 0.53 SER 215 -0.84 GLY 262
PRO 128 0.72 VAL 216 -1.06 GLY 262
ASP 208 0.86 VAL 217 -0.91 GLY 262
PRO 128 0.99 VAL 218 -0.76 VAL 197
PRO 128 0.93 PRO 219 -0.88 GLY 199
PRO 128 1.16 TYR 220 -0.65 GLY 199
PRO 128 1.27 GLU 221 -0.50 GLY 199
PRO 128 1.42 PRO 222 -0.35 GLY 199
PRO 128 1.40 PRO 223 -0.38 SER 116
PRO 128 1.00 GLU 224 -0.65 SER 116
LEU 289 0.88 VAL 225 -0.63 SER 116
PRO 151 0.83 GLY 226 -0.69 SER 116
PRO 128 1.00 SER 227 -0.61 SER 116
PRO 128 1.36 ASP 228 -0.24 ILE 255
PRO 128 1.48 CYS 229 -0.35 ILE 255
PRO 128 1.36 THR 230 -0.52 VAL 157
PRO 128 1.08 THR 231 -0.66 VAL 157
ASN 200 0.99 ILE 232 -1.01 VAL 157
PRO 128 0.67 HIS 233 -0.88 VAL 157
TYR 126 0.63 TYR 234 -0.92 ARG 158
TYR 126 0.41 ASN 235 -0.67 GLY 262
PRO 151 0.37 TYR 236 -0.60 GLY 262
PRO 151 0.31 MET 237 -0.63 GLY 262
PRO 151 0.29 CYS 238 -0.53 GLY 262
PRO 151 0.35 ASN 239 -0.50 LEU 130
PRO 151 0.34 SER 240 -0.65 LEU 130
PRO 151 0.30 SER 241 -0.84 LEU 130
PRO 151 0.25 CYS 242 -0.68 LEU 130
PRO 151 0.20 MET 243 -0.71 LEU 130
PRO 151 0.14 GLY 244 -0.58 LEU 130
PRO 151 0.18 GLY 245 -0.53 LEU 130
PRO 151 0.22 MET 246 -0.60 LEU 130
PRO 151 0.22 ASN 247 -0.79 LEU 130
CYS 277 0.28 ARG 248 -0.95 LEU 130
ARG 280 0.34 ARG 249 -0.80 LEU 130
ASP 281 0.49 PRO 250 -0.74 PHE 113
ASP 281 0.50 ILE 251 -0.82 PHE 113
THR 284 0.63 LEU 252 -1.04 PHE 113
GLU 285 0.63 THR 253 -1.01 PHE 113
PRO 98 1.04 ILE 254 -0.96 PHE 113
GLU 285 0.87 ILE 255 -1.00 VAL 143
GLU 285 0.96 THR 256 -0.76 ILE 232
LEU 289 1.07 LEU 257 -0.91 THR 150
LEU 289 1.08 GLU 258 -1.13 THR 150
LEU 289 1.18 ASP 259 -0.98 THR 150
LEU 289 1.02 SER 260 -1.04 GLU 204
LEU 289 0.98 SER 261 -1.27 GLU 204
LEU 289 0.94 GLY 262 -1.54 GLU 204
LEU 289 1.15 ASN 263 -1.14 LEU 206
ASN 288 1.23 LEU 264 -0.95 LEU 206
LEU 289 1.38 LEU 265 -0.68 THR 150
GLU 285 1.32 GLY 266 -0.52 THR 150
GLU 285 1.30 ARG 267 -0.45 VAL 143
GLU 285 1.25 ASN 268 -0.55 PHE 113
GLU 285 1.01 SER 269 -0.97 PHE 113
GLU 285 0.81 PHE 270 -1.65 PHE 113
ASP 281 0.90 GLU 271 -1.20 PHE 113
ASP 281 0.64 VAL 272 -0.86 PHE 113
PRO 151 0.52 ARG 273 -0.52 PHE 113
PRO 151 0.47 VAL 274 -0.41 LEU 130
PRO 151 0.48 CYS 275 -0.46 LEU 130
PRO 151 0.46 ALA 276 -0.37 LEU 130
PRO 151 0.55 CYS 277 -0.97 SER 121
PRO 151 0.66 PRO 278 -0.64 SER 121
PRO 151 0.72 GLY 279 -0.85 SER 121
THR 102 0.75 ARG 280 -0.99 SER 121
THR 102 0.99 ASP 281 -0.66 SER 121
ARG 110 1.05 ARG 282 -0.45 SER 241
THR 102 0.94 ARG 283 -0.50 SER 121
LYS 101 1.32 THR 284 -0.50 SER 121
GLN 104 1.65 GLU 285 -0.36 MET 243
ASP 148 1.48 GLU 286 -0.55 SER 241
TYR 103 1.30 GLU 287 -0.35 SER 121
GLY 105 1.47 ASN 288 -0.23 SER 121
SER 106 1.75 LEU 289 -0.33 MET 243
SER 106 1.62 ARG 290 -0.32 MET 243

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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.