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CA distance fluctuations for 2404131437433984339

---  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
THR 150 0.48 SER 96 -1.28 LYS 164
GLN 167 0.46 VAL 97 -1.71 GLN 192
ARG 213 1.16 PRO 98 -1.05 ASN 131
SER 260 1.56 SER 99 -0.80 THR 284
THR 170 1.30 GLN 100 -1.17 ASN 131
THR 170 1.62 LYS 101 -1.34 LEU 130
THR 170 1.39 THR 102 -1.57 LEU 130
THR 170 1.16 TYR 103 -1.56 ALA 129
THR 170 0.96 GLN 104 -1.61 ALA 129
THR 170 0.92 GLY 105 -1.39 ALA 129
THR 170 0.80 SER 106 -1.25 ALA 129
SER 99 0.77 TYR 107 -1.25 PRO 128
SER 166 0.77 GLY 108 -1.46 ALA 129
SER 166 0.84 PHE 109 -1.54 PRO 128
SER 166 0.94 ARG 110 -1.49 PRO 128
SER 166 0.89 LEU 111 -1.19 TYR 126
PHE 270 1.05 GLY 112 -1.28 PRO 151
PHE 270 1.75 PHE 113 -1.48 PRO 151
PHE 270 1.33 LEU 114 -1.19 PRO 151
GLY 226 0.92 SER 121 -0.76 VAL 97
GLY 226 0.96 VAL 122 -0.82 PRO 151
GLY 226 0.91 THR 123 -0.87 VAL 97
GLY 226 1.02 CYS 124 -0.90 PRO 151
GLY 226 1.06 THR 125 -1.01 PRO 151
GLY 226 0.93 TYR 126 -1.19 LEU 111
GLY 226 0.59 SER 127 -1.33 THR 102
ARG 248 0.47 PRO 128 -1.56 GLN 104
ARG 248 0.73 ALA 129 -1.61 GLN 104
ARG 248 0.94 LEU 130 -1.57 THR 102
GLY 226 0.80 ASN 131 -1.24 ASN 268
GLY 226 0.94 LYS 132 -0.83 SER 96
GLY 226 1.00 MET 133 -0.84 SER 269
GLY 226 0.87 PHE 134 -0.83 VAL 97
GLY 226 0.84 CYS 135 -0.94 VAL 97
SER 185 0.97 GLN 136 -0.99 VAL 97
SER 185 1.19 LEU 137 -1.14 VAL 97
ASP 186 1.06 ALA 138 -1.21 VAL 97
ASP 186 0.75 LYS 139 -1.05 VAL 97
GLY 226 0.71 THR 140 -0.96 VAL 97
THR 253 0.82 CYS 141 -0.94 PRO 151
THR 253 1.08 PRO 142 -1.14 PRO 151
ILE 254 1.31 VAL 143 -1.22 PRO 151
ILE 255 1.04 GLN 144 -1.45 PRO 151
ILE 255 0.93 LEU 145 -1.21 PRO 151
SER 166 0.81 TRP 146 -1.23 PRO 151
SER 99 0.75 VAL 147 -1.18 PRO 128
SER 99 0.74 ASP 148 -1.28 ALA 129
SER 99 1.03 SER 149 -1.09 LEU 289
SER 99 1.36 THR 150 -0.85 LEU 289
SER 99 0.83 PRO 151 -1.49 CYS 229
SER 99 1.32 PRO 152 -1.32 PRO 128
SER 99 1.43 PRO 153 -0.87 PRO 128
SER 99 1.54 GLY 154 -0.84 PRO 128
SER 99 1.36 THR 155 -0.96 PRO 128
SER 99 1.14 ARG 156 -0.83 PRO 128
ILE 232 0.99 VAL 157 -0.89 PRO 128
ILE 232 1.01 ARG 158 -1.03 ASP 208
ILE 232 0.91 ALA 159 -0.79 VAL 97
VAL 143 0.75 MET 160 -0.82 VAL 97
PHE 113 0.85 ALA 161 -0.86 VAL 97
PHE 113 1.00 ILE 162 -1.03 SER 96
PHE 113 0.96 TYR 163 -0.95 SER 96
PHE 113 1.20 LYS 164 -1.28 SER 96
PHE 113 0.97 GLN 165 -0.86 SER 96
THR 102 1.09 SER 166 -0.46 ASN 247
THR 102 1.02 GLN 167 -0.81 ASN 247
LYS 101 1.05 HIS 168 -1.03 ASN 247
THR 102 1.35 MET 169 -0.58 ASN 247
LYS 101 1.62 THR 170 -0.43 ASN 247
LYS 101 1.14 GLU 171 -0.52 GLY 245
PRO 98 1.05 VAL 172 -0.81 VAL 97
PRO 98 0.73 VAL 173 -1.09 VAL 97
PRO 98 0.77 ARG 174 -1.46 VAL 97
SER 185 0.90 ARG 175 -1.70 VAL 97
SER 185 0.86 CYS 176 -1.44 VAL 97
PHE 212 0.73 PRO 177 -1.37 VAL 97
SER 185 0.80 HIS 178 -1.33 VAL 97
SER 185 1.08 HIS 179 -1.49 VAL 97
PHE 212 0.90 GLU 180 -1.57 VAL 97
ARG 209 0.85 ARG 181 -1.35 VAL 97
GLY 187 1.22 CYS 182 -1.33 VAL 97
CYS 238 1.55 SER 185 -0.86 VAL 97
LEU 137 1.19 ASP 186 -0.89 VAL 97
CYS 182 1.22 GLY 187 -0.90 VAL 97
CYS 182 0.69 LEU 188 -1.01 VAL 97
GLY 262 0.79 ALA 189 -1.21 VAL 97
ASP 207 1.13 PRO 190 -1.37 VAL 97
PHE 212 1.07 PRO 191 -1.52 VAL 97
PHE 212 1.28 GLN 192 -1.71 VAL 97
ASP 207 0.81 HIS 193 -1.58 VAL 97
SER 185 0.87 LEU 194 -1.50 VAL 97
GLY 262 0.73 ILE 195 -1.24 VAL 97
GLY 262 0.82 ARG 196 -1.28 VAL 97
GLY 262 0.85 VAL 197 -1.12 VAL 97
GLY 262 0.79 GLU 198 -1.10 VAL 97
SER 99 0.80 GLY 199 -0.99 VAL 97
SER 99 0.90 ASN 200 -0.93 VAL 97
SER 99 0.95 LEU 201 -0.85 VAL 97
SER 99 1.11 ARG 202 -0.84 VAL 97
GLY 262 1.03 VAL 203 -0.95 VAL 97
GLY 262 1.35 GLU 204 -0.93 VAL 97
GLY 262 1.15 TYR 205 -1.04 VAL 97
GLY 262 1.13 LEU 206 -0.88 VAL 97
PRO 190 1.13 ASP 207 -0.74 VAL 97
PRO 190 0.78 ASP 208 -1.03 ARG 158
PRO 191 0.95 ARG 209 -0.87 GLU 258
PRO 191 0.80 ASN 210 -0.86 GLU 258
PRO 191 0.67 THR 211 -0.84 ILE 254
GLN 192 1.28 PHE 212 -0.58 VAL 97
PRO 98 1.16 ARG 213 -0.79 VAL 97
GLN 100 0.90 HIS 214 -1.04 VAL 97
GLY 262 0.94 SER 215 -0.97 VAL 97
GLY 262 1.12 VAL 216 -1.01 VAL 97
GLY 262 1.09 VAL 217 -0.80 VAL 97
SER 99 1.05 VAL 218 -0.78 PRO 128
SER 99 1.07 PRO 219 -0.71 PRO 128
SER 99 1.02 TYR 220 -0.91 PRO 128
SER 99 0.93 GLU 221 -0.81 PRO 128
SER 99 0.82 PRO 222 -0.89 PRO 152
SER 99 0.70 PRO 223 -0.99 PRO 151
SER 99 0.68 GLU 224 -0.90 PRO 151
SER 121 0.84 VAL 225 -0.77 PRO 151
THR 125 1.06 GLY 226 -0.79 PRO 151
PHE 270 1.03 SER 227 -1.05 PRO 151
PHE 270 0.79 ASP 228 -1.21 PRO 151
SER 166 0.75 CYS 229 -1.49 PRO 151
SER 99 0.77 THR 230 -1.24 PRO 151
ILE 255 0.96 THR 231 -1.28 PRO 151
ILE 255 1.02 ILE 232 -1.01 PRO 151
ALA 159 0.83 HIS 233 -0.91 PRO 151
ALA 159 0.86 TYR 234 -0.98 VAL 97
GLY 262 0.69 ASN 235 -1.18 VAL 97
SER 185 0.94 TYR 236 -1.27 VAL 97
SER 185 1.27 MET 237 -1.46 VAL 97
SER 185 1.55 CYS 238 -1.42 VAL 97
SER 185 1.36 ASN 239 -1.16 VAL 97
SER 185 1.05 SER 240 -1.01 VAL 97
SER 185 0.98 SER 241 -0.96 VAL 97
SER 185 1.03 CYS 242 -1.13 VAL 97
SER 185 0.78 GLY 245 -1.20 VAL 97
SER 185 0.82 MET 246 -1.04 VAL 97
GLU 286 0.84 ASN 247 -1.03 HIS 168
LEU 130 0.94 ARG 248 -0.87 HIS 168
LEU 130 0.82 ARG 249 -0.76 HIS 168
PHE 113 0.95 PRO 250 -0.92 SER 96
PHE 113 1.06 ILE 251 -1.02 SER 96
PHE 113 1.31 LEU 252 -1.27 SER 96
VAL 143 1.24 THR 253 -0.99 SER 96
VAL 143 1.31 ILE 254 -0.87 SER 96
VAL 143 1.22 ILE 255 -0.85 ASP 208
ILE 232 0.84 THR 256 -1.01 PRO 128
THR 150 1.06 LEU 257 -1.16 PRO 128
THR 150 1.28 GLU 258 -0.98 PRO 128
SER 99 1.48 ASP 259 -0.93 PRO 128
SER 99 1.56 SER 260 -0.76 ARG 209
SER 99 1.24 SER 261 -0.62 PRO 128
GLU 204 1.35 GLY 262 -0.81 ARG 209
SER 99 1.10 ASN 263 -0.81 PRO 128
THR 150 0.95 LEU 264 -1.02 PRO 128
THR 150 1.05 LEU 265 -1.24 PRO 128
THR 170 0.92 GLY 266 -1.44 PRO 128
THR 170 1.00 ARG 267 -1.41 PRO 128
MET 169 1.13 ASN 268 -1.40 PRO 128
MET 169 1.04 SER 269 -1.11 ASN 131
PHE 113 1.75 PHE 270 -1.08 SER 96
PHE 113 1.45 GLU 271 -1.09 SER 96
PHE 113 0.96 VAL 272 -0.90 SER 96
SER 185 0.88 ARG 273 -0.87 VAL 97
SER 185 1.08 VAL 274 -1.02 VAL 97
SER 185 1.17 CYS 275 -0.91 VAL 97
SER 185 1.11 ALA 276 -0.87 VAL 97
SER 185 0.89 CYS 277 -0.78 VAL 97
SER 185 0.84 PRO 278 -0.78 VAL 97
GLY 226 0.85 GLY 279 -0.82 PRO 151
GLY 226 0.75 ARG 280 -0.73 SER 96
SER 185 0.82 ASP 281 -0.90 GLN 100
SER 185 0.76 ARG 282 -0.99 THR 102
SER 185 0.69 ARG 283 -0.87 THR 102
SER 185 0.73 THR 284 -1.03 LYS 101
SER 185 0.79 GLU 285 -1.22 THR 102
ARG 248 0.90 GLU 286 -1.04 ASP 148
SER 185 0.67 GLU 287 -0.96 THR 102
SER 185 0.65 ASN 288 -1.05 LYS 101
ASN 247 0.71 LEU 289 -1.19 ASP 148

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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.