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CA distance fluctuations for 2402190101113366437

---  normal mode 10  ---

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
LEU 206 0.79 SER 96 -0.61 TYR 103
SER 215 0.76 VAL 97 -0.50 PHE 113
SER 215 0.87 PRO 98 -0.61 TYR 103
ARG 158 1.10 SER 99 -0.57 PRO 98
ARG 158 0.63 GLN 100 -0.74 PHE 113
SER 166 0.67 LYS 101 -0.76 PHE 113
LEU 130 1.13 THR 102 -1.18 ASP 208
LEU 130 1.30 TYR 103 -1.60 THR 211
ALA 129 1.73 GLN 104 -1.66 ASP 208
ALA 129 1.36 GLY 105 -1.56 ASP 208
ALA 129 1.21 SER 106 -1.42 ASP 208
ALA 129 1.28 TYR 107 -1.60 ASP 208
ALA 129 1.53 GLY 108 -1.64 ASP 208
ALA 129 1.43 PHE 109 -1.76 ASP 208
ASN 131 1.58 ARG 110 -1.37 ASP 208
ASN 131 1.13 LEU 111 -1.04 ASP 208
TRP 146 0.88 GLY 112 -0.89 ASP 208
TRP 146 0.59 PHE 113 -1.15 PHE 270
ASP 148 0.36 LEU 114 -0.80 SER 227
ASP 148 0.55 HIS 115 -0.71 SER 227
ARG 110 0.41 SER 116 -0.95 GLY 226
ARG 110 0.59 GLY 117 -0.87 GLY 226
ARG 110 0.60 THR 118 -0.84 GLY 226
GLN 104 0.45 ALA 119 -1.03 GLY 226
GLN 104 0.40 LYS 120 -0.99 GLY 226
ALA 276 0.44 SER 121 -1.17 GLY 226
ALA 276 0.43 VAL 122 -1.12 GLY 226
ARG 110 0.36 THR 123 -0.94 GLY 226
ARG 110 0.48 CYS 124 -0.81 GLY 226
ARG 110 0.69 THR 125 -0.69 GLY 226
ARG 110 0.99 TYR 126 -0.45 GLY 226
ARG 110 1.25 SER 127 -0.35 ASP 208
ARG 110 1.54 PRO 128 -0.41 ASP 208
GLN 104 1.73 ALA 129 -0.47 ARG 249
GLN 104 1.55 LEU 130 -0.58 ARG 249
ARG 110 1.58 ASN 131 -0.52 ARG 249
ARG 110 0.95 LYS 132 -0.36 ASP 208
ARG 110 0.84 MET 133 -0.42 SER 227
ARG 110 0.84 MET 133 -0.42 SER 227
ARG 110 0.69 PHE 134 -0.53 GLY 226
LEU 111 0.53 CYS 135 -0.61 GLY 226
LEU 111 0.41 GLN 136 -0.66 GLY 226
CYS 182 0.47 LEU 137 -0.61 SER 261
CYS 182 0.60 ALA 138 -0.65 SER 261
CYS 182 0.55 LYS 139 -0.73 GLY 226
SER 183 0.61 THR 140 -0.83 GLY 226
LEU 111 0.49 CYS 141 -0.77 ALA 159
LEU 111 0.49 CYS 141 -0.77 ALA 159
SER 183 0.40 PRO 142 -0.81 ALA 159
ASN 131 0.43 VAL 143 -0.80 ASP 208
ASN 131 0.57 GLN 144 -0.96 ASP 208
ASN 131 0.89 LEU 145 -1.10 ASP 208
PRO 128 1.06 TRP 146 -1.33 ASP 208
ALA 129 1.20 VAL 147 -1.57 ASP 208
ALA 129 1.23 ASP 148 -1.43 ASP 208
ALA 129 1.10 SER 149 -1.43 ASP 208
ALA 129 1.02 THR 150 -1.32 ASP 208
ALA 129 0.98 PRO 151 -1.33 ASP 208
VAL 225 1.26 PRO 152 -1.12 ASP 208
VAL 225 1.31 PRO 153 -0.94 ASP 208
VAL 225 0.94 GLY 154 -0.99 LEU 206
VAL 225 0.80 THR 155 -1.06 LEU 206
SER 99 0.64 ARG 156 -0.91 LEU 206
SER 99 0.83 VAL 157 -0.85 ASP 208
SER 99 1.10 ARG 158 -0.74 PRO 142
SER 99 0.92 ALA 159 -0.81 PRO 142
SER 99 0.56 MET 160 -0.63 THR 256
ARG 196 0.38 ALA 161 -0.48 PHE 113
GLU 285 0.42 ILE 162 -0.49 PHE 113
GLU 285 0.47 TYR 163 -0.42 MET 246
GLU 285 0.66 LYS 164 -0.44 PRO 98
GLU 285 0.61 GLN 165 -0.41 GLY 244
LYS 101 0.67 SER 166 -0.59 GLY 244
ASN 288 0.53 GLN 167 -0.85 GLY 244
ASN 288 0.48 HIS 168 -0.86 GLY 244
ASN 288 0.46 MET 169 -0.50 GLY 244
ASN 288 0.40 THR 170 -0.47 LEU 264
ARG 249 0.64 GLU 171 -0.71 ASN 263
ARG 249 0.66 VAL 172 -0.95 LEU 264
ARG 249 0.56 VAL 173 -0.80 GLY 262
PHE 212 0.66 ARG 174 -0.93 GLY 262
PHE 212 0.75 ARG 175 -0.89 GLY 262
PHE 212 0.82 CYS 176 -0.85 SER 261
PHE 212 0.81 PRO 177 -0.95 SER 261
PHE 212 0.66 HIS 178 -0.90 SER 261
PHE 212 0.62 HIS 179 -0.92 SER 261
PHE 212 0.70 GLU 180 -1.06 SER 261
ARG 209 0.60 ARG 181 -1.09 SER 261
ALA 138 0.60 CYS 182 -0.96 SER 261
THR 140 0.61 SER 183 -0.99 SER 261
THR 140 0.57 ASP 184 -0.85 SER 261
PHE 212 0.42 SER 185 -0.96 SER 261
GLY 199 0.47 ASP 186 -0.85 SER 261
GLY 199 0.42 GLY 187 -0.99 SER 261
PRO 98 0.50 LEU 188 -1.02 SER 261
PRO 98 0.49 ALA 189 -1.04 SER 261
ASP 207 0.55 PRO 190 -1.35 GLY 262
PHE 212 0.59 PRO 191 -1.20 SER 261
PHE 212 0.72 GLN 192 -1.19 GLY 262
PHE 212 0.46 HIS 193 -1.09 GLY 262
PHE 212 0.42 LEU 194 -0.84 GLY 262
ARG 196 0.41 ILE 195 -0.74 GLY 262
SER 99 0.52 ARG 196 -0.70 GLY 262
SER 99 0.50 VAL 197 -0.64 VAL 218
LEU 111 0.44 GLU 198 -0.67 GLU 224
ASP 186 0.47 GLY 199 -0.77 GLU 224
SER 99 0.54 ASN 200 -0.59 GLU 224
SER 99 0.57 LEU 201 -0.57 SER 121
SER 99 0.65 ARG 202 -0.62 SER 260
SER 99 0.70 VAL 203 -0.72 SER 260
PRO 98 0.77 GLU 204 -1.04 SER 260
PRO 98 0.75 TYR 205 -1.23 GLY 262
SER 96 0.79 LEU 206 -1.43 GLU 258
PRO 190 0.55 ASP 207 -1.68 LEU 264
PRO 177 0.45 ASP 208 -1.76 PHE 109
PRO 177 0.65 ARG 209 -1.41 SER 106
PRO 177 0.52 ASN 210 -1.32 ASP 148
PRO 177 0.48 THR 211 -1.60 TYR 103
CYS 176 0.82 PHE 212 -1.50 LEU 265
PRO 190 0.41 ARG 213 -1.23 LEU 264
SER 96 0.57 HIS 214 -1.10 LEU 264
PRO 98 0.87 SER 215 -0.85 GLU 258
SER 99 0.79 VAL 216 -0.80 GLY 262
SER 99 0.90 VAL 217 -0.77 VAL 216
SER 99 0.76 VAL 218 -0.64 VAL 197
SER 99 0.68 PRO 219 -0.63 ASP 208
ASN 131 0.66 TYR 220 -0.90 ASP 208
ASN 131 0.64 GLU 221 -0.84 ASP 208
ASN 131 0.71 PRO 222 -0.97 ASP 208
ASN 131 0.53 PRO 223 -0.92 ASP 208
PRO 153 0.64 GLU 224 -0.93 SER 121
PRO 153 1.31 VAL 225 -0.84 SER 121
PRO 152 0.87 GLY 226 -1.17 SER 121
THR 150 0.56 SER 227 -0.94 THR 231
ALA 129 0.60 ASP 228 -1.01 ASP 208
ASN 131 0.56 CYS 229 -1.08 ASP 208
ASN 131 0.49 THR 230 -1.02 ASP 208
ASN 131 0.39 THR 231 -0.94 SER 227
ASN 131 0.54 ILE 232 -0.79 GLU 224
LEU 111 0.48 HIS 233 -0.86 GLU 224
LEU 111 0.52 TYR 234 -0.72 ARG 158
LEU 111 0.45 ASN 235 -0.62 ARG 158
LEU 111 0.39 TYR 236 -0.63 GLY 262
PHE 212 0.44 MET 237 -0.76 SER 261
PHE 212 0.52 CYS 238 -0.71 SER 261
PHE 212 0.49 ASN 239 -0.59 SER 261
PHE 212 0.47 SER 240 -0.49 SER 261
PHE 212 0.52 SER 241 -0.53 SER 261
PHE 212 0.60 CYS 242 -0.66 SER 261
PHE 212 0.69 MET 243 -0.72 GLN 167
PHE 212 0.82 GLY 244 -0.86 HIS 168
PHE 212 0.78 GLY 245 -0.77 HIS 168
PHE 212 0.61 MET 246 -0.64 HIS 168
PHE 212 0.65 ASN 247 -0.72 GLN 167
PHE 212 0.52 ARG 248 -0.55 LEU 130
VAL 172 0.66 ARG 249 -0.58 LEU 130
ASP 281 0.52 PRO 250 -0.50 ASN 131
ASP 281 0.43 ILE 251 -0.46 PHE 113
GLU 285 0.54 LEU 252 -0.61 PHE 113
ARG 196 0.42 THR 253 -0.66 PHE 113
ASN 288 0.48 ILE 254 -0.70 ASP 208
ASN 131 0.64 ILE 255 -0.95 ASP 208
ASN 131 0.67 THR 256 -1.14 ASP 208
ASN 131 0.78 LEU 257 -1.32 ASP 208
ALA 129 0.65 GLU 258 -1.43 LEU 206
VAL 225 0.89 ASP 259 -1.32 LEU 206
VAL 225 0.77 SER 260 -1.17 LEU 206
VAL 225 0.65 SER 261 -1.29 PRO 190
VAL 225 0.59 GLY 262 -1.35 PRO 190
VAL 225 0.71 ASN 263 -1.41 ASP 207
ALA 129 0.76 LEU 264 -1.68 ASP 207
ALA 129 0.95 LEU 265 -1.50 PHE 212
ALA 129 1.13 GLY 266 -1.58 ASP 208
LEU 130 1.03 ARG 267 -1.36 ASP 208
ASN 131 0.89 ASN 268 -1.03 ASP 208
GLU 285 0.66 SER 269 -0.91 PHE 113
GLU 271 0.70 PHE 270 -1.15 PHE 113
PHE 270 0.70 GLU 271 -0.62 PHE 113
PHE 270 0.60 VAL 272 -0.44 SER 227
ARG 110 0.46 ARG 273 -0.45 GLY 226
ARG 110 0.43 VAL 274 -0.50 GLY 226
ARG 110 0.44 CYS 275 -0.56 GLY 226
SER 121 0.44 ALA 276 -0.62 GLY 226
ARG 110 0.47 CYS 277 -0.75 GLY 226
ARG 110 0.47 CYS 277 -0.75 GLY 226
ARG 110 0.58 PRO 278 -0.70 GLY 226
ARG 110 0.59 GLY 279 -0.79 GLY 226
GLN 104 0.61 ARG 280 -0.69 GLY 226
GLN 104 0.70 ASP 281 -0.54 GLY 226
GLN 104 0.81 ARG 282 -0.49 GLY 226
GLN 104 0.82 ARG 283 -0.54 GLY 226
GLN 104 0.84 THR 284 -0.44 GLY 226
THR 102 1.04 GLU 285 -0.27 ALA 276
GLN 104 1.15 GLU 286 -0.22 GLY 226
GLN 104 0.99 GLU 287 -0.29 GLY 226
TYR 103 1.10 ASN 288 -0.20 ALA 276

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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.