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CA distance fluctuations for 2404111624423721609

---  normal mode 12  ---

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 0.98 VAL 97 -1.59 ASP 259
ASN 210 1.09 PRO 98 -1.66 GLU 258
ARG 209 1.10 SER 99 -1.14 TYR 103
ARG 209 0.88 GLN 100 -1.09 GLN 165
ARG 209 0.97 LYS 101 -1.44 GLN 165
ARG 209 0.74 THR 102 -1.25 LEU 289
ARG 209 0.47 TYR 103 -1.14 SER 99
PHE 113 0.42 GLN 104 -0.93 GLN 165
GLY 226 0.49 GLY 105 -1.08 PRO 98
GLY 226 0.64 SER 106 -1.03 PRO 98
GLY 226 0.51 TYR 107 -1.02 PRO 98
SER 116 0.51 GLY 108 -0.83 PRO 98
ILE 232 0.46 PHE 109 -0.83 PRO 98
ILE 232 0.52 ARG 110 -0.91 LEU 289
VAL 143 0.54 LEU 111 -0.97 SER 227
LEU 114 0.47 GLY 112 -1.05 SER 227
SER 269 0.51 PHE 113 -0.82 SER 227
HIS 115 0.53 LEU 114 -0.67 GLY 226
LEU 114 0.53 HIS 115 -0.87 GLY 226
THR 231 0.66 SER 116 -0.94 GLY 226
GLU 224 0.55 SER 121 -1.18 GLY 226
GLU 224 0.52 VAL 122 -1.11 GLY 226
GLU 224 0.61 THR 123 -0.97 GLY 226
THR 231 0.44 CYS 124 -0.86 GLY 226
ASN 210 0.31 THR 125 -0.86 GLY 226
ASN 210 0.42 TYR 126 -0.73 GLY 226
ASN 210 0.53 SER 127 -0.86 SER 227
ASN 210 0.66 PRO 128 -1.06 SER 227
ASN 210 0.68 ALA 129 -1.19 SER 227
ASN 210 0.69 LEU 130 -1.14 SER 227
ASN 210 0.72 ASN 131 -1.17 SER 227
ASN 210 0.60 LYS 132 -0.85 SER 227
ASN 210 0.43 MET 133 -0.67 GLY 226
TYR 163 0.35 PHE 134 -0.77 GLY 226
GLU 224 0.41 CYS 135 -0.80 GLY 226
GLU 224 0.56 GLN 136 -0.85 GLY 226
GLU 224 0.61 LEU 137 -0.77 SER 261
GLU 224 0.72 ALA 138 -0.80 ASP 186
GLU 224 0.75 LYS 139 -0.81 GLY 226
THR 231 0.78 THR 140 -0.76 GLY 226
PRO 142 0.46 CYS 141 -0.68 GLY 226
CYS 141 0.46 PRO 142 -0.64 ARG 158
LEU 111 0.54 VAL 143 -0.78 ARG 158
SER 116 0.64 GLN 144 -0.93 ARG 158
SER 185 0.45 LEU 145 -0.76 SER 227
SER 116 0.63 TRP 146 -0.79 PRO 98
SER 116 0.54 VAL 147 -0.87 PRO 98
SER 116 0.55 ASP 148 -0.78 PRO 98
ASP 228 0.60 SER 149 -0.87 PRO 98
ASP 228 0.81 THR 150 -0.92 PRO 98
ASP 228 0.56 PRO 151 -1.14 PRO 98
GLY 226 0.59 PRO 152 -1.20 VAL 97
SER 227 0.59 PRO 153 -1.12 THR 211
ASP 186 0.52 GLY 154 -1.35 THR 211
ASP 186 0.47 THR 155 -1.35 PRO 98
ASP 186 0.47 ARG 156 -1.08 PRO 98
ASP 186 0.44 VAL 157 -0.72 PRO 98
LYS 101 0.61 ARG 158 -0.93 GLN 144
SER 99 0.69 ALA 159 -0.77 ARG 158
SER 99 0.64 MET 160 -0.92 GLY 262
ASP 208 0.56 ALA 161 -1.09 GLY 262
ASP 208 0.69 ILE 162 -1.29 LEU 264
PRO 250 0.72 TYR 163 -1.25 LEU 264
VAL 97 0.98 LYS 164 -1.10 LYS 101
VAL 97 0.98 GLN 165 -1.44 LYS 101
GLN 165 0.96 GLU 171 -1.76 ASN 263
ARG 249 0.71 VAL 172 -1.82 ASN 263
ARG 249 0.57 VAL 173 -1.60 GLY 262
ARG 249 0.39 ARG 174 -1.57 GLY 262
VAL 225 0.38 HIS 175 -1.34 SER 261
VAL 225 0.42 CYS 176 -1.34 SER 261
VAL 225 0.53 PRO 177 -1.39 SER 261
VAL 225 0.69 HIS 178 -1.20 SER 261
VAL 225 0.70 HIS 179 -1.16 SER 261
VAL 225 0.68 GLU 180 -1.34 SER 261
VAL 225 0.93 ARG 181 -1.12 SER 261
LEU 201 1.11 SER 185 -0.65 SER 261
LEU 201 1.46 ASP 186 -0.99 SER 121
ARG 202 0.89 GLY 187 -0.77 SER 121
ARG 202 0.75 LEU 188 -0.73 GLU 198
ARG 202 0.56 ALA 189 -0.79 SER 261
VAL 225 0.48 PRO 190 -1.05 SER 261
VAL 225 0.59 PRO 191 -1.30 SER 261
VAL 225 0.41 GLN 192 -1.51 SER 261
VAL 225 0.36 HIS 193 -1.20 SER 261
VAL 225 0.35 LEU 194 -1.08 SER 261
VAL 225 0.32 ILE 195 -0.83 SER 261
VAL 197 0.52 ARG 196 -0.67 SER 261
SER 185 0.54 VAL 197 -0.50 GLY 226
GLU 221 0.81 GLU 198 -0.73 LEU 188
GLU 221 1.06 GLY 199 -0.53 GLY 226
SER 185 1.09 ASN 200 -0.51 LEU 114
ASP 186 1.46 LEU 201 -0.46 LEU 114
ASP 186 1.19 ARG 202 -0.66 THR 231
ASP 186 0.72 VAL 203 -0.52 THR 231
SER 99 0.50 GLU 204 -0.50 THR 231
SER 99 0.54 TYR 205 -0.73 SER 261
SER 99 0.60 LEU 206 -0.94 SER 260
SER 99 0.66 ASP 207 -1.14 SER 260
SER 99 1.09 ASP 208 -1.13 SER 260
SER 99 1.10 ARG 209 -0.87 SER 261
PRO 98 1.09 ASN 210 -0.99 SER 261
GLN 165 0.98 THR 211 -1.59 SER 260
GLN 165 0.65 PHE 212 -1.51 SER 260
GLN 165 0.66 ARG 213 -1.74 SER 260
GLN 165 0.36 HIS 214 -1.30 SER 260
SER 99 0.57 SER 215 -0.96 SER 260
SER 99 0.56 VAL 216 -0.64 SER 261
LYS 101 0.47 VAL 217 -0.76 THR 231
ASP 186 0.65 VAL 218 -0.82 THR 231
ASP 186 0.79 PRO 219 -0.67 THR 231
GLY 199 0.88 TYR 220 -0.76 PRO 98
GLY 199 1.06 GLU 221 -0.64 PRO 98
SER 185 0.87 PRO 222 -0.62 PRO 98
SER 185 0.90 PRO 223 -0.58 ALA 129
SER 185 1.02 GLU 224 -0.49 ALA 129
SER 185 1.09 VAL 225 -0.66 ALA 129
SER 261 0.73 GLY 226 -1.18 SER 121
THR 150 0.65 SER 227 -1.19 ALA 129
THR 150 0.81 ASP 228 -0.91 ALA 129
SER 116 0.62 CYS 229 -0.69 ASN 131
SER 185 0.63 THR 230 -0.62 ARG 158
THR 140 0.78 THR 231 -0.83 ARG 158
SER 185 0.56 ILE 232 -0.54 ARG 202
GLU 221 0.57 HIS 233 -0.59 PRO 142
ILE 232 0.47 TYR 234 -0.57 GLY 226
GLU 224 0.55 ASN 235 -0.64 GLY 226
GLU 224 0.44 TYR 236 -0.80 SER 261
GLU 224 0.56 MET 237 -0.94 SER 261
GLU 224 0.47 CYS 238 -1.02 SER 261
GLU 224 0.40 ASN 239 -0.94 SER 261
GLU 171 0.43 SER 240 -0.90 GLY 262
GLU 171 0.37 SER 241 -0.95 SER 261
GLU 224 0.34 CYS 242 -1.08 SER 261
VAL 225 0.30 MET 243 -1.12 SER 261
VAL 225 0.29 GLY 244 -1.24 SER 261
VAL 225 0.25 GLY 245 -1.27 GLY 262
GLU 171 0.45 MET 246 -1.18 GLY 262
GLU 171 0.41 ASN 247 -1.05 GLY 262
GLU 171 0.67 ARG 248 -0.88 GLY 262
GLU 171 0.93 ARG 249 -0.94 LYS 101
TYR 163 0.72 PRO 250 -0.99 LYS 101
TYR 163 0.58 ILE 251 -0.89 GLY 262
ASP 208 0.73 LEU 252 -0.96 LEU 289
ASP 208 0.57 THR 253 -0.85 LEU 289
ARG 209 0.57 ILE 254 -0.88 LEU 289
ARG 209 0.47 ILE 255 -0.89 LEU 289
LYS 101 0.63 THR 256 -0.91 LEU 289
GLY 199 0.41 LEU 257 -1.28 PRO 98
GLY 226 0.31 GLU 258 -1.66 PRO 98
GLY 226 0.53 ASP 259 -1.59 VAL 97
GLY 226 0.50 SER 260 -1.74 ARG 213
GLY 226 0.73 SER 261 -1.51 GLN 192
GLY 226 0.40 GLY 262 -1.74 VAL 172
GLY 226 0.60 ASN 263 -1.82 VAL 172
GLY 226 0.43 LEU 264 -1.49 GLU 171
GLY 226 0.46 LEU 265 -1.61 PRO 98
GLY 199 0.38 GLY 266 -1.26 PRO 98
ARG 209 0.50 ARG 267 -0.99 LEU 289
ARG 209 0.55 ASN 268 -1.11 LEU 289
ARG 209 0.56 SER 269 -1.10 LEU 289
ASN 210 0.62 PHE 270 -1.07 LEU 289
ASN 210 0.66 GLU 271 -1.15 LEU 289
ASN 210 0.48 VAL 272 -0.88 LEU 289
TYR 163 0.45 ARG 273 -0.67 LEU 289
GLU 224 0.36 VAL 274 -0.75 SER 261
GLU 224 0.41 CYS 275 -0.79 GLY 226
GLU 224 0.50 ALA 276 -0.89 GLY 226
GLU 224 0.44 CYS 277 -0.96 GLY 226
GLU 224 0.35 PRO 278 -0.92 GLY 226
ARG 283 0.38 GLY 279 -1.02 GLY 226
GLU 287 0.43 ARG 280 -0.99 GLY 226
GLU 171 0.43 ASP 281 -0.89 GLY 226
VAL 97 0.43 ARG 282 -0.86 GLY 226
GLY 279 0.38 ARG 283 -0.86 GLY 226
GLU 171 0.37 THR 284 -0.83 GLY 226
ASN 210 0.35 GLU 285 -0.77 LYS 101
ASN 210 0.39 GLU 286 -0.74 SER 227
SER 121 0.49 GLU 287 -0.92 LYS 101
SER 121 0.25 ASN 288 -1.21 LYS 101
SER 121 0.19 LEU 289 -1.31 LYS 101
SER 121 0.42 ARG 290 -1.26 LYS 101

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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.