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CA distance fluctuations for 2404131342263939023

---  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
TYR 163 1.29 SER 96 -0.60 LEU 289
HIS 178 1.85 VAL 97 -0.62 LEU 289
THR 150 0.49 PRO 98 -1.29 GLU 171
GLN 165 0.46 SER 99 -1.33 LEU 201
PHE 270 0.49 GLN 100 -1.45 MET 169
PHE 113 0.44 LYS 101 -1.69 MET 169
PHE 113 0.48 THR 102 -1.64 LEU 289
LEU 206 0.50 TYR 103 -1.42 LEU 289
LEU 206 0.50 GLN 104 -1.29 LEU 289
LEU 206 0.68 GLY 105 -1.16 LEU 289
LEU 206 0.69 SER 106 -1.03 LEU 289
LEU 188 0.65 TYR 107 -1.18 PRO 152
LEU 188 0.51 GLY 108 -1.33 LEU 130
LEU 188 0.46 PHE 109 -1.19 LEU 130
THR 102 0.41 ARG 110 -1.32 LEU 130
THR 102 0.47 LEU 111 -1.43 ASN 131
THR 102 0.44 GLY 112 -1.51 ASN 131
SER 269 0.62 PHE 113 -1.49 PRO 151
SER 121 0.52 LEU 114 -1.62 PRO 151
GLY 226 1.30 SER 121 -1.15 ALA 276
VAL 97 0.70 VAL 122 -1.14 PRO 151
VAL 97 0.78 THR 123 -1.11 PRO 151
VAL 97 0.69 CYS 124 -1.21 PRO 151
VAL 97 0.54 THR 125 -1.38 PRO 151
SER 96 0.52 TYR 126 -1.41 PRO 151
SER 96 0.48 SER 127 -1.47 PRO 151
SER 96 0.41 PRO 128 -1.52 PRO 151
GLN 165 0.50 ALA 129 -1.38 PRO 151
ASP 281 0.53 LEU 130 -1.33 GLY 108
GLN 165 0.52 ASN 131 -1.51 GLY 112
SER 96 0.65 LYS 132 -1.16 PRO 151
SER 96 0.60 MET 133 -1.17 PRO 151
SER 96 0.60 PHE 134 -1.15 PRO 151
VAL 97 0.77 CYS 135 -1.05 PRO 151
VAL 97 0.93 GLN 136 -0.94 PRO 151
VAL 97 1.09 LEU 137 -0.81 PRO 151
VAL 97 1.12 ALA 138 -0.77 PRO 151
VAL 97 0.96 LYS 139 -0.91 PRO 151
VAL 97 0.83 THR 140 -0.99 PRO 151
GLY 262 0.73 CYS 141 -1.08 PRO 151
GLY 262 0.61 PRO 142 -1.17 PRO 151
VAL 157 0.71 VAL 143 -1.09 PRO 151
VAL 157 0.56 GLN 144 -1.07 PRO 151
VAL 157 0.61 LEU 145 -1.08 ASN 131
VAL 157 0.43 TRP 146 -1.21 ASN 131
ARG 156 0.74 VAL 147 -1.50 PRO 152
LEU 188 0.65 ASP 148 -1.29 LEU 130
THR 155 0.94 SER 149 -0.98 ALA 129
ASP 259 1.52 THR 150 -0.73 ALA 129
SER 106 0.28 PRO 151 -1.62 LEU 114
GLY 187 0.59 PRO 152 -1.50 VAL 147
GLY 187 1.13 PRO 153 -0.99 SER 99
GLY 187 1.41 GLY 154 -1.01 SER 99
THR 150 1.20 THR 155 -1.07 THR 170
ASP 186 0.98 ARG 156 -1.17 THR 170
ILE 232 0.80 VAL 157 -1.23 THR 170
VAL 197 0.85 ARG 158 -1.22 THR 170
GLY 262 0.83 ALA 159 -0.84 LEU 289
GLY 262 0.80 MET 160 -0.91 LEU 289
SER 96 0.77 ALA 161 -0.92 LEU 289
SER 96 1.03 ILE 162 -1.00 LEU 289
SER 96 1.29 TYR 163 -1.11 ASN 288
SER 96 1.10 LYS 164 -1.32 ASN 288
SER 96 0.85 GLN 165 -1.33 ASN 288
ARG 248 0.59 SER 166 -1.56 LYS 101
ARG 248 0.91 GLN 167 -1.08 LYS 101
ARG 248 1.30 HIS 168 -1.19 LYS 101
ASN 247 0.81 MET 169 -1.69 LYS 101
ASN 247 0.66 THR 170 -1.45 THR 256
ASN 247 1.16 GLU 171 -1.29 PRO 98
SER 96 1.06 VAL 172 -1.08 PRO 98
SER 96 0.98 VAL 173 -0.81 ASN 288
VAL 97 1.09 ARG 174 -0.71 ASN 288
VAL 97 1.35 ARG 175 -0.62 ASN 288
VAL 97 1.46 CYS 176 -0.61 SER 121
VAL 97 1.65 PRO 177 -0.62 SER 121
VAL 97 1.85 HIS 178 -0.73 SER 121
VAL 97 1.74 HIS 179 -0.73 SER 121
VAL 97 1.66 GLU 180 -0.61 SER 121
VAL 97 1.74 ARG 181 -0.63 SER 121
VAL 97 1.65 CYS 182 -0.70 SER 121
LEU 201 1.54 SER 185 -0.52 SER 121
ARG 202 1.80 ASP 186 -0.50 SER 99
ARG 202 1.58 GLY 187 -0.52 SER 99
SER 260 1.77 LEU 188 -0.59 SER 99
GLY 262 1.84 ALA 189 -0.52 SER 99
SER 261 1.62 PRO 190 -0.66 LEU 206
SER 261 1.45 PRO 191 -0.50 LEU 289
VAL 97 1.29 GLN 192 -0.57 LEU 289
GLY 262 1.32 HIS 193 -0.61 LEU 289
VAL 97 1.11 LEU 194 -0.63 LEU 289
GLY 262 1.13 ILE 195 -0.68 TYR 205
GLY 262 1.26 ARG 196 -1.06 TYR 205
GLY 262 1.17 VAL 197 -0.95 TYR 205
GLY 262 0.99 GLU 198 -0.79 SER 99
PRO 219 0.88 GLY 199 -0.96 SER 99
ASP 186 1.38 ASN 200 -1.27 THR 231
SER 185 1.54 LEU 201 -1.45 GLU 224
ASP 186 1.80 ARG 202 -1.33 SER 99
GLY 262 1.44 VAL 203 -1.11 SER 99
GLY 262 1.54 GLU 204 -0.93 SER 99
ASN 263 1.68 TYR 205 -1.06 ARG 196
ASN 263 1.52 LEU 206 -0.66 PRO 190
ASN 263 1.22 ASP 207 -0.69 LEU 289
ASN 263 0.72 ASP 208 -0.88 VAL 217
THR 150 0.60 ARG 209 -0.85 VAL 217
PRO 177 0.37 ASN 210 -1.06 ARG 158
THR 150 0.38 THR 211 -1.24 PRO 98
SER 261 0.69 PHE 212 -1.19 PRO 98
ASN 263 0.78 ARG 213 -0.92 PRO 98
ASN 263 1.06 HIS 214 -0.77 LEU 289
GLY 262 1.12 SER 215 -0.77 LEU 289
GLY 262 1.49 VAL 216 -0.74 LEU 289
GLY 262 1.08 VAL 217 -0.93 SER 99
ASP 186 1.14 VAL 218 -1.13 SER 99
ASP 186 1.08 PRO 219 -1.22 SER 99
ASP 186 0.80 TYR 220 -1.08 SER 99
ASP 186 0.74 GLU 221 -1.21 SER 99
ASP 186 0.62 PRO 222 -1.08 SER 99
SER 121 0.69 PRO 223 -1.08 SER 99
SER 121 0.97 GLU 224 -1.45 LEU 201
SER 121 1.16 VAL 225 -1.30 SER 99
SER 121 1.30 GLY 226 -1.07 LEU 201
SER 121 0.91 SER 227 -1.17 LEU 201
SER 121 0.58 ASP 228 -1.06 PRO 152
SER 121 0.52 CYS 229 -0.99 PRO 152
SER 121 0.61 THR 230 -1.09 ASN 200
SER 121 0.60 THR 231 -1.27 ASN 200
VAL 157 0.80 ILE 232 -0.98 ASN 200
GLY 262 0.79 HIS 233 -0.90 PRO 151
GLY 262 0.94 TYR 234 -0.80 PRO 151
GLY 262 0.97 ASN 235 -0.77 PRO 151
VAL 97 1.02 TYR 236 -0.73 PRO 151
VAL 97 1.25 MET 237 -0.62 PRO 151
VAL 97 1.27 CYS 238 -0.64 SER 121
VAL 97 1.09 ASN 239 -0.74 SER 121
VAL 97 0.92 SER 240 -0.72 GLU 285
HIS 168 1.09 SER 241 -0.77 SER 121
VAL 97 1.17 CYS 242 -0.78 SER 121
VAL 97 1.16 GLY 245 -0.71 ASN 288
SER 96 1.09 MET 246 -0.81 ASN 288
HIS 168 1.20 ASN 247 -0.73 ASN 288
HIS 168 1.30 ARG 248 -0.81 THR 284
SER 96 1.16 ARG 249 -0.99 ASN 288
SER 96 1.06 PRO 250 -1.19 GLU 285
SER 96 1.07 ILE 251 -1.21 GLU 285
SER 96 0.81 LEU 252 -1.20 GLU 285
SER 96 0.65 THR 253 -0.97 GLU 285
GLY 262 0.45 ILE 254 -1.09 LEU 289
THR 150 0.46 ILE 255 -1.07 THR 170
THR 150 0.65 THR 256 -1.45 THR 170
THR 150 0.74 LEU 257 -1.29 THR 170
THR 150 1.11 GLU 258 -1.37 THR 170
THR 150 1.52 ASP 259 -0.98 THR 170
LEU 188 1.77 SER 260 -0.85 SER 99
PRO 190 1.62 SER 261 -0.64 SER 99
ALA 189 1.84 GLY 262 -0.72 THR 170
TYR 205 1.68 ASN 263 -0.82 LEU 289
LEU 206 1.33 LEU 264 -1.18 THR 170
LEU 206 0.99 LEU 265 -1.06 THR 170
LEU 206 0.72 GLY 266 -1.16 LEU 289
LEU 206 0.53 ARG 267 -1.28 LEU 289
PHE 113 0.48 ASN 268 -1.34 LEU 289
PHE 113 0.62 SER 269 -1.28 LEU 289
SER 96 0.50 PHE 270 -1.08 GLU 285
SER 96 0.75 GLU 271 -1.40 GLU 285
SER 96 0.76 VAL 272 -1.11 GLU 285
SER 96 0.80 ARG 273 -0.90 PRO 151
VAL 97 0.87 VAL 274 -0.87 PRO 151
VAL 97 0.86 CYS 275 -0.89 PRO 151
VAL 97 0.92 ALA 276 -1.15 SER 121
VAL 97 0.76 CYS 277 -1.00 PRO 151
VAL 97 0.67 PRO 278 -1.12 PRO 151
VAL 97 0.56 GLY 279 -1.19 PRO 151
VAL 97 0.49 ARG 280 -1.07 PRO 151
LEU 130 0.53 ASP 281 -1.06 PRO 151
LEU 130 0.44 ARG 282 -1.20 PRO 151
GLY 226 0.54 ARG 283 -1.07 PRO 151
GLY 226 0.39 THR 284 -1.01 PRO 250
ALA 129 0.18 GLU 285 -1.40 GLU 271
GLY 226 0.32 GLU 286 -1.09 PRO 151
GLY 226 0.49 GLU 287 -0.95 LYS 164
GLY 226 0.22 ASN 288 -1.33 GLN 165
GLY 226 0.07 LEU 289 -1.64 THR 102

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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.