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CA distance fluctuations for 240415022434281025

---  normal mode 13  ---

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
LYS 164 1.41 SER 96 -0.54 ASN 263
GLU 180 1.74 VAL 97 -0.54 GLN 167
ASN 131 0.90 PRO 98 -1.41 ARG 213
THR 284 0.70 SER 99 -1.57 GLY 154
ASN 131 1.07 GLN 100 -1.38 THR 170
LEU 130 1.20 LYS 101 -1.82 THR 170
LEU 130 1.50 THR 102 -1.54 THR 170
ALA 129 1.48 TYR 103 -1.33 THR 170
ALA 129 1.62 GLN 104 -1.10 THR 170
ALA 129 1.39 GLY 105 -1.06 THR 170
ALA 129 1.27 SER 106 -0.92 THR 170
PRO 128 1.31 TYR 107 -0.86 THR 170
ALA 129 1.51 GLY 108 -0.87 THR 170
PRO 128 1.66 PHE 109 -0.92 THR 170
PRO 128 1.60 ARG 110 -0.91 SER 166
SER 127 1.25 LEU 111 -0.84 SER 166
PRO 151 1.15 GLY 112 -0.90 PHE 270
PRO 151 1.26 PHE 113 -1.81 PHE 270
PRO 151 1.08 LEU 114 -1.15 PHE 270
ALA 276 0.84 SER 121 -1.18 GLY 226
VAL 97 0.73 VAL 122 -1.16 GLY 226
VAL 97 0.83 THR 123 -1.13 GLY 226
PRO 151 0.81 CYS 124 -1.18 GLY 226
PRO 151 0.96 THR 125 -1.08 GLY 226
LEU 111 1.05 TYR 126 -0.91 GLY 226
ARG 110 1.40 SER 127 -0.65 ARG 248
PHE 109 1.66 PRO 128 -0.48 ARG 248
GLN 104 1.62 ALA 129 -0.74 ARG 248
THR 102 1.50 LEU 130 -0.97 ARG 248
ASN 268 1.31 ASN 131 -0.64 GLY 226
ASP 281 0.82 LYS 132 -0.87 GLY 226
PRO 151 0.74 MET 133 -0.99 GLY 226
VAL 97 0.77 PHE 134 -0.92 GLY 226
VAL 97 0.88 CYS 135 -0.97 GLY 226
VAL 97 0.95 GLN 136 -0.91 GLY 226
VAL 97 1.10 LEU 137 -0.98 SER 185
VAL 97 1.15 ALA 138 -0.88 SER 185
VAL 97 1.00 LYS 139 -0.87 GLY 226
VAL 97 0.89 THR 140 -0.93 GLY 226
PRO 151 0.86 CYS 141 -0.91 GLY 226
PRO 151 1.02 PRO 142 -0.96 THR 253
PRO 151 1.12 VAL 143 -1.19 ILE 254
PRO 151 1.40 GLN 144 -1.00 ILE 255
PRO 151 1.34 LEU 145 -0.87 ILE 255
PRO 151 1.31 TRP 146 -0.77 THR 170
PRO 128 1.27 VAL 147 -0.82 THR 170
ALA 129 1.34 ASP 148 -0.72 THR 170
ALA 129 1.15 SER 149 -0.96 SER 99
ALA 129 0.88 THR 150 -1.22 SER 99
CYS 229 1.80 PRO 151 -0.86 SER 99
PRO 128 1.33 PRO 152 -1.32 SER 99
PRO 128 0.88 PRO 153 -1.46 SER 99
PRO 128 0.85 GLY 154 -1.57 SER 99
PRO 128 0.96 THR 155 -1.30 SER 99
ASP 208 0.97 ARG 156 -1.12 SER 99
ASP 208 0.99 VAL 157 -1.09 ILE 232
ASP 208 1.15 ARG 158 -1.05 ILE 232
ASP 208 0.82 ALA 159 -0.89 ILE 232
VAL 97 0.73 MET 160 -0.65 VAL 143
VAL 97 0.78 ALA 161 -0.74 PHE 113
SER 96 0.93 ILE 162 -0.87 PHE 113
SER 96 0.98 TYR 163 -0.79 PHE 113
SER 96 1.41 LYS 164 -1.00 PHE 113
SER 96 1.07 GLN 165 -0.79 PHE 113
ASN 247 0.55 SER 166 -1.14 THR 102
ASN 247 0.91 GLN 167 -1.02 THR 102
ASN 247 1.23 HIS 168 -1.10 LYS 101
ASN 247 0.71 MET 169 -1.44 THR 102
ASN 247 0.54 THR 170 -1.82 LYS 101
GLY 245 0.73 GLU 171 -1.20 LYS 101
VAL 97 0.83 VAL 172 -1.00 PRO 98
VAL 97 1.06 VAL 173 -0.73 PRO 98
VAL 97 1.41 ARG 174 -0.76 PRO 98
VAL 97 1.68 ARG 175 -0.76 PHE 212
VAL 97 1.54 CYS 176 -0.74 PHE 212
VAL 97 1.54 PRO 177 -0.86 PHE 212
VAL 97 1.46 HIS 178 -0.72 PHE 212
VAL 97 1.59 HIS 179 -0.71 PHE 212
VAL 97 1.74 GLU 180 -0.90 PHE 212
VAL 97 1.48 ARG 181 -0.84 ARG 209
VAL 97 1.40 CYS 182 -0.68 ARG 209
VAL 97 1.15 SER 185 -1.15 MET 237
VAL 97 1.07 ASP 186 -0.75 ALA 138
VAL 97 1.04 GLY 187 -0.65 SER 99
VAL 97 1.06 LEU 188 -0.74 SER 99
VAL 97 1.22 ALA 189 -0.77 GLY 262
VAL 97 1.36 PRO 190 -1.00 ASP 207
VAL 97 1.58 PRO 191 -0.93 PHE 212
VAL 97 1.69 GLN 192 -1.16 PHE 212
VAL 97 1.46 HIS 193 -0.78 ASP 207
VAL 97 1.36 LEU 194 -0.68 SER 185
VAL 97 1.12 ILE 195 -0.67 SER 185
VAL 97 1.16 ARG 196 -0.75 GLY 262
VAL 97 1.01 VAL 197 -0.81 GLY 262
VAL 97 1.00 GLU 198 -0.80 SER 99
VAL 97 0.91 GLY 199 -0.88 SER 99
PRO 151 0.86 ASN 200 -0.99 SER 99
PRO 151 0.77 LEU 201 -1.01 SER 99
VAL 97 0.75 ARG 202 -1.17 SER 99
VAL 97 0.85 VAL 203 -1.04 SER 99
VAL 97 0.85 GLU 204 -1.30 GLY 262
VAL 97 0.99 TYR 205 -1.06 GLY 262
VAL 97 0.85 LEU 206 -1.00 GLY 262
VAL 97 0.72 ASP 207 -1.00 PRO 190
ARG 158 1.15 ASP 208 -0.63 PRO 190
GLY 262 1.26 ARG 209 -0.84 ARG 181
GLY 262 1.24 ASN 210 -0.75 ARG 181
ILE 254 0.95 THR 211 -0.57 GLN 192
VAL 97 0.57 PHE 212 -1.16 GLN 192
VAL 97 0.78 ARG 213 -1.41 PRO 98
VAL 97 0.99 HIS 214 -0.95 PRO 98
VAL 97 0.89 SER 215 -0.84 GLY 262
VAL 97 0.90 VAL 216 -1.04 GLY 262
PRO 128 0.77 VAL 217 -1.09 GLY 262
PRO 128 0.85 VAL 218 -1.07 SER 99
PRO 128 0.79 PRO 219 -1.14 SER 99
PRO 128 1.00 TYR 220 -1.07 SER 99
PRO 128 1.03 GLU 221 -1.07 SER 99
PRO 152 0.98 PRO 222 -0.94 SER 99
PRO 151 1.20 PRO 223 -0.81 SER 99
PRO 151 1.03 GLU 224 -0.82 SER 99
PRO 151 0.82 VAL 225 -0.98 SER 121
PRO 151 0.78 GLY 226 -1.18 CYS 124
PRO 151 1.06 SER 227 -1.06 LEU 114
PRO 151 1.27 ASP 228 -0.69 SER 166
PRO 151 1.80 CYS 229 -0.73 SER 99
PRO 151 1.50 THR 230 -0.86 SER 99
PRO 151 1.30 THR 231 -0.95 ILE 255
PRO 151 1.02 ILE 232 -1.09 VAL 157
PRO 151 0.87 HIS 233 -0.80 ARG 158
VAL 97 0.88 TYR 234 -0.81 ALA 159
VAL 97 1.08 ASN 235 -0.68 GLY 226
VAL 97 1.16 TYR 236 -0.73 SER 185
VAL 97 1.37 MET 237 -1.15 SER 185
VAL 97 1.37 CYS 238 -0.90 SER 185
VAL 97 1.13 ASN 239 -0.75 SER 185
VAL 97 0.99 SER 240 -0.71 GLY 226
VAL 97 0.97 SER 241 -0.92 GLU 286
VAL 97 1.16 CYS 242 -0.83 GLU 286
VAL 97 1.25 GLY 245 -0.68 GLU 286
VAL 97 1.04 MET 246 -0.68 GLU 286
HIS 168 1.23 ASN 247 -0.91 GLU 286
HIS 168 1.01 ARG 248 -0.97 LEU 130
HIS 168 0.81 ARG 249 -0.84 LEU 130
SER 96 0.96 PRO 250 -0.80 LEU 130
SER 96 0.98 ILE 251 -0.88 PHE 113
SER 96 1.08 LEU 252 -1.13 PHE 113
SER 96 0.79 THR 253 -1.09 VAL 143
THR 211 0.95 ILE 254 -1.19 VAL 143
ASP 208 0.94 ILE 255 -1.18 VAL 143
PRO 128 1.00 THR 256 -0.87 ILE 232
PRO 128 1.17 LEU 257 -1.00 THR 150
ASN 210 1.07 GLU 258 -1.17 THR 150
ARG 209 0.98 ASP 259 -1.31 SER 99
ARG 209 1.08 SER 260 -1.47 SER 99
ARG 209 0.91 SER 261 -1.22 SER 99
ARG 209 1.26 GLY 262 -1.30 GLU 204
ASN 210 0.96 ASN 263 -0.97 SER 99
PRO 128 1.00 LEU 264 -0.91 THR 170
PRO 128 1.23 LEU 265 -0.95 THR 170
PRO 128 1.42 GLY 266 -1.06 THR 170
PRO 128 1.33 ARG 267 -1.14 THR 170
PRO 128 1.32 ASN 268 -1.12 MET 169
ASN 131 1.17 SER 269 -0.99 MET 169
SER 96 0.88 PHE 270 -1.81 PHE 113
SER 96 0.97 GLU 271 -1.28 PHE 113
SER 96 0.80 VAL 272 -0.89 GLY 226
VAL 97 0.82 ARG 273 -0.83 GLY 226
VAL 97 0.97 VAL 274 -0.81 GLY 226
VAL 97 0.87 CYS 275 -0.80 GLY 226
VAL 97 0.84 ALA 276 -0.81 SER 185
VAL 97 0.75 CYS 277 -0.85 GLY 226
VAL 97 0.73 PRO 278 -0.91 GLY 226
PRO 151 0.76 GLY 279 -0.92 GLY 226
SER 96 0.75 ARG 280 -0.79 GLY 226
GLN 100 0.88 ASP 281 -0.64 GLY 226
THR 102 0.97 ARG 282 -0.60 SER 241
THR 102 0.83 ARG 283 -0.55 GLY 226
LYS 101 1.01 THR 284 -0.50 SER 185
THR 102 1.18 GLU 285 -0.77 SER 241
ASP 148 1.04 GLU 286 -0.94 ARG 248
ASP 148 0.90 GLU 287 -0.71 SER 241
TYR 103 0.98 ASN 288 -0.64 CYS 242
ASP 148 1.14 LEU 289 -0.74 ASN 247
ASP 148 1.07 ARG 290 -0.72 ASN 247

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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.