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CA distance fluctuations for 2404110322003549768

---  normal mode 14  ---

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 0.82 SER 96 -0.64 ASN 263
GLU 285 0.93 VAL 97 -0.71 ASN 263
ILE 162 1.52 PRO 98 -0.65 GLY 105
ILE 255 1.60 SER 99 -0.83 SER 166
GLU 285 1.24 GLN 100 -0.55 PHE 113
GLU 285 1.22 LYS 101 -0.64 PHE 113
GLU 285 1.61 THR 102 -0.45 PHE 113
LEU 130 1.53 TYR 103 -0.63 PRO 98
LEU 130 1.79 GLN 104 -0.45 PRO 98
LEU 130 1.76 GLY 105 -0.65 PRO 98
LEU 130 1.55 SER 106 -0.58 PRO 98
ALA 129 1.78 TYR 107 -0.45 ARG 213
ALA 129 1.70 GLY 108 -0.34 PRO 98
ASN 131 1.51 PHE 109 -0.28 ARG 213
ASN 131 1.64 ARG 110 -0.42 PRO 223
ASN 131 1.32 LEU 111 -0.56 CYS 229
SER 127 1.21 GLY 112 -0.69 CYS 229
PRO 128 0.64 PHE 113 -1.37 PHE 270
SER 183 0.52 LEU 114 -0.89 PHE 270
ASP 148 0.50 HIS 115 -0.94 ASP 228
SER 183 0.49 SER 116 -1.02 SER 227
ARG 110 0.57 GLY 117 -0.93 GLY 226
PRO 98 0.60 THR 118 -0.80 GLY 226
PRO 98 0.54 ALA 119 -0.93 GLY 226
PRO 98 0.55 LYS 120 -0.84 GLY 226
ALA 276 0.56 SER 121 -0.97 GLY 226
PRO 98 0.48 VAL 122 -0.92 GLY 226
SER 183 0.53 THR 123 -0.79 GLY 226
SER 183 0.57 CYS 124 -0.73 SER 227
LEU 111 0.67 THR 125 -0.63 GLY 226
LEU 111 1.18 TYR 126 -0.41 GLY 226
ARG 110 1.52 SER 127 -0.49 ARG 248
TRP 146 1.74 PRO 128 -0.50 ARG 248
TYR 107 1.78 ALA 129 -0.67 ARG 248
GLN 104 1.79 LEU 130 -0.84 ARG 248
ARG 110 1.64 ASN 131 -0.64 ARG 248
ARG 110 0.96 LYS 132 -0.53 PRO 250
LEU 111 0.84 MET 133 -0.45 SER 227
LEU 111 0.84 MET 133 -0.45 SER 227
PRO 98 0.84 PHE 134 -0.45 GLY 226
PRO 98 0.72 CYS 135 -0.54 SER 227
PRO 98 0.63 GLN 136 -0.70 GLY 262
PRO 98 0.66 LEU 137 -0.81 GLY 262
SER 183 0.79 ALA 138 -0.92 GLY 262
SER 183 0.84 LYS 139 -0.81 ARG 158
SER 183 0.88 THR 140 -0.98 ARG 158
ASP 184 0.76 CYS 141 -0.95 ARG 158
ASP 184 0.76 CYS 141 -0.95 ARG 158
ASP 184 0.75 PRO 142 -0.98 ARG 158
TYR 126 0.87 VAL 143 -1.27 ILE 255
PRO 128 1.12 GLN 144 -0.94 ILE 255
PRO 128 1.45 LEU 145 -0.66 ILE 255
PRO 128 1.74 TRP 146 -0.51 PRO 223
ALA 129 1.67 VAL 147 -0.58 PRO 222
ALA 129 1.71 ASP 148 -0.50 PRO 222
ALA 129 1.72 SER 149 -0.39 TYR 220
ALA 129 1.60 THR 150 -0.36 TYR 220
ALA 129 1.45 PRO 151 -0.54 GLU 204
ALA 129 1.29 PRO 152 -0.51 GLU 204
ASP 228 1.29 PRO 153 -0.48 GLU 204
PRO 128 1.01 GLY 154 -0.84 GLU 204
PRO 128 1.13 THR 155 -0.77 GLU 204
SER 99 0.91 ARG 156 -0.78 ILE 232
SER 99 1.23 VAL 157 -1.24 ILE 232
SER 99 1.32 ARG 158 -1.33 HIS 233
SER 99 1.60 ALA 159 -1.21 TYR 234
SER 99 1.13 MET 160 -0.74 GLY 262
PRO 98 1.52 ALA 161 -0.70 GLY 262
PRO 98 1.52 ILE 162 -0.63 PHE 113
PRO 98 1.23 TYR 163 -0.60 PHE 113
PRO 98 1.01 LYS 164 -0.72 PHE 113
PRO 98 0.68 GLN 165 -0.63 PHE 113
THR 284 0.66 SER 166 -0.83 SER 99
THR 284 0.53 GLN 167 -0.75 SER 99
PRO 98 0.58 HIS 168 -0.50 GLY 262
THR 284 0.58 MET 169 -0.56 PHE 113
THR 211 0.80 THR 170 -0.56 ASN 263
PRO 98 0.55 GLU 171 -0.68 ASN 263
PRO 98 0.61 VAL 172 -0.87 ASN 263
PRO 98 0.97 VAL 173 -0.90 GLY 262
PRO 98 0.76 ARG 174 -1.04 GLY 262
PRO 98 0.70 ARG 175 -1.03 GLY 262
PRO 98 0.56 CYS 176 -0.94 GLY 262
PRO 98 0.42 PRO 177 -0.94 GLY 262
PRO 98 0.45 HIS 178 -0.88 GLY 262
PRO 98 0.55 HIS 179 -0.98 GLY 262
PRO 98 0.51 GLU 180 -1.06 GLY 262
ALA 138 0.46 ARG 181 -1.02 SER 261
ALA 138 0.75 CYS 182 -0.92 SER 261
THR 140 0.88 SER 183 -0.97 SER 261
GLU 198 1.26 ASP 184 -0.68 SER 261
PRO 223 0.49 SER 185 -0.95 GLY 262
PRO 223 0.57 ASP 186 -0.87 GLY 262
SER 99 0.53 GLY 187 -0.91 SER 261
SER 99 0.66 LEU 188 -1.02 GLY 262
SER 99 0.66 ALA 189 -1.30 GLY 262
SER 99 0.57 PRO 190 -1.45 GLY 262
PRO 98 0.51 PRO 191 -1.26 GLY 262
PRO 98 0.56 GLN 192 -1.27 GLY 262
PRO 98 0.73 HIS 193 -1.32 GLY 262
PRO 98 0.91 LEU 194 -1.09 GLY 262
PRO 98 0.91 ILE 195 -1.08 GLY 262
ASP 184 0.93 ARG 196 -1.08 GLY 262
ASP 184 1.07 VAL 197 -1.14 VAL 217
ASP 184 1.26 GLU 198 -0.92 VAL 217
ASP 184 0.91 GLY 199 -0.69 SER 121
PRO 223 0.92 ASN 200 -0.54 GLY 262
PRO 223 0.94 LEU 201 -0.63 GLY 262
GLU 221 0.82 ARG 202 -0.65 SER 260
SER 99 0.93 VAL 203 -0.85 GLY 262
SER 99 0.83 GLU 204 -1.16 SER 260
SER 99 0.80 TYR 205 -1.47 GLY 262
SER 99 0.82 LEU 206 -1.65 GLY 262
SER 99 0.66 ASP 207 -1.55 GLY 262
SER 99 0.83 ASP 208 -1.51 ASN 263
SER 99 0.70 ARG 209 -1.29 SER 261
ASN 288 0.75 ASN 210 -1.08 ASN 263
THR 170 0.80 THR 211 -1.19 ASN 263
ASN 288 0.49 PHE 212 -1.18 ASN 263
GLU 285 0.50 ARG 213 -1.15 ASN 263
PRO 98 0.58 HIS 214 -1.21 GLY 262
SER 99 0.91 SER 215 -1.11 GLY 262
SER 99 1.05 VAL 216 -1.12 GLY 262
SER 99 1.13 VAL 217 -1.14 VAL 197
SER 99 1.06 VAL 218 -0.82 GLU 198
SER 99 0.93 PRO 219 -0.68 HIS 233
PRO 128 1.10 TYR 220 -0.51 PRO 151
PRO 128 0.89 GLU 221 -0.55 VAL 147
PRO 128 0.98 PRO 222 -0.58 VAL 147
LEU 201 0.94 PRO 223 -0.51 TRP 146
LEU 201 0.76 GLU 224 -0.50 SER 121
PRO 153 0.92 VAL 225 -0.63 SER 121
PRO 153 0.98 GLY 226 -0.99 SER 116
PRO 153 1.03 SER 227 -1.02 SER 116
PRO 153 1.29 ASP 228 -0.94 HIS 115
PRO 128 1.14 CYS 229 -0.69 GLY 112
PRO 128 1.11 THR 230 -0.43 SER 121
PRO 128 0.95 THR 231 -0.82 ARG 158
ASP 184 0.88 ILE 232 -1.27 ARG 158
ASP 184 0.99 HIS 233 -1.33 ARG 158
ASP 184 1.02 TYR 234 -1.28 ARG 158
ASP 184 1.08 ASN 235 -0.90 GLY 262
PRO 98 0.74 TYR 236 -0.90 GLY 262
PRO 98 0.77 MET 237 -0.97 GLY 262
PRO 98 0.81 CYS 238 -0.88 GLY 262
PRO 98 0.84 ASN 239 -0.73 GLY 262
PRO 98 0.90 SER 240 -0.66 GLY 262
PRO 98 0.73 SER 241 -0.80 LEU 130
PRO 98 0.67 CYS 242 -0.75 GLY 262
PRO 98 0.56 MET 243 -0.73 GLY 262
PRO 98 0.48 GLY 244 -0.78 GLY 262
PRO 98 0.64 GLY 245 -0.83 GLY 262
PRO 98 0.81 MET 246 -0.75 GLY 262
PRO 98 0.69 ASN 247 -0.72 LEU 130
PRO 98 0.77 ARG 248 -0.84 LEU 130
PRO 98 0.89 ARG 249 -0.64 LEU 130
PRO 98 1.04 PRO 250 -0.60 PHE 113
PRO 98 1.36 ILE 251 -0.66 PHE 113
PRO 98 1.39 LEU 252 -0.87 PHE 113
PRO 98 1.26 THR 253 -0.88 PHE 113
SER 99 1.29 ILE 254 -1.07 VAL 143
SER 99 1.60 ILE 255 -1.27 VAL 143
SER 99 1.15 THR 256 -0.87 ILE 232
ASN 131 1.09 LEU 257 -0.55 ILE 232
ASN 288 1.05 GLU 258 -0.86 SER 215
ASN 288 1.07 ASP 259 -0.98 LEU 206
ASN 288 0.90 SER 260 -1.16 LEU 206
ASN 288 0.84 SER 261 -1.31 PRO 190
ASN 288 0.86 GLY 262 -1.65 LEU 206
ASN 288 1.13 ASN 263 -1.51 ASP 208
ASN 288 1.26 LEU 264 -1.07 ARG 213
LEU 130 1.35 LEU 265 -0.72 ARG 213
LEU 130 1.42 GLY 266 -0.59 ARG 213
GLU 285 1.26 ARG 267 -0.50 VAL 143
GLU 285 1.27 ASN 268 -0.62 VAL 143
GLU 285 1.09 SER 269 -1.00 PHE 113
PRO 98 0.99 PHE 270 -1.37 PHE 113
PRO 98 0.98 GLU 271 -0.95 PHE 113
PRO 98 1.04 VAL 272 -0.66 PHE 113
PRO 98 0.94 ARG 273 -0.50 GLY 262
PRO 98 0.90 VAL 274 -0.61 GLY 262
PRO 98 0.82 CYS 275 -0.57 ASP 186
PRO 98 0.68 ALA 276 -0.72 ASP 186
PRO 98 0.74 CYS 277 -0.66 ASP 186
PRO 98 0.74 CYS 277 -0.66 ASP 186
PRO 98 0.77 PRO 278 -0.60 GLY 226
PRO 98 0.71 GLY 279 -0.70 GLY 226
PRO 98 0.78 ARG 280 -0.60 GLY 226
PRO 98 0.93 ASP 281 -0.47 GLY 226
ARG 110 0.96 ARG 282 -0.45 LEU 130
GLN 104 0.90 ARG 283 -0.47 GLY 226
THR 102 1.12 THR 284 -0.30 GLY 226
THR 102 1.61 GLU 285 -0.21 GLU 286
GLN 104 1.63 GLU 286 -0.27 SER 241
TYR 103 1.34 GLU 287 -0.16 ALA 276
GLY 105 1.42 ASN 288 -0.15 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.