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CA distance fluctuations for 2404111610033706944

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

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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.