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CA distance fluctuations for 250309234742866450

---  normal mode 24  ---

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
GLY 244 0.98 SER 96 -1.63 ARG 213
ASN 210 1.65 VAL 97 -0.80 ARG 213
ARG 209 1.56 PRO 98 -0.79 PRO 152
ARG 209 1.41 SER 99 -0.56 LEU 289
ARG 209 0.95 GLN 100 -1.12 ILE 195
ARG 209 0.84 LYS 101 -1.32 ASN 131
ARG 209 0.76 THR 102 -1.75 ASN 131
ARG 209 0.56 TYR 103 -1.13 ASN 131
TYR 220 0.83 GLN 104 -1.00 PRO 128
TYR 220 0.90 GLY 105 -0.99 PRO 128
TYR 220 1.11 SER 106 -1.00 PRO 128
TYR 220 1.11 SER 106 -1.01 PRO 128
TYR 220 1.57 TYR 107 -1.20 PRO 128
TYR 220 1.36 GLY 108 -1.16 ALA 129
VAL 157 1.54 PHE 109 -1.22 PRO 128
VAL 157 1.41 ARG 110 -1.23 SER 127
ALA 159 1.65 LEU 111 -1.57 SER 127
ALA 159 1.22 GLY 112 -1.40 SER 127
VAL 272 1.63 PHE 113 -0.81 SER 127
CYS 229 1.05 LEU 114 -0.54 SER 127
CYS 229 1.20 HIS 115 -0.44 GLY 226
SER 227 1.17 SER 116 -0.70 GLY 226
SER 227 1.48 VAL 122 -0.55 GLY 226
SER 227 1.40 THR 123 -0.72 GLY 226
SER 227 1.14 CYS 124 -0.62 THR 102
SER 227 0.98 THR 125 -0.68 THR 102
ARG 282 0.90 TYR 126 -1.58 CYS 141
GLU 285 1.52 SER 127 -1.57 LEU 111
ASN 288 1.59 PRO 128 -1.54 TRP 146
GLN 167 1.39 ALA 129 -1.43 VAL 147
GLU 171 1.45 LEU 130 -1.25 LEU 111
GLN 165 1.11 ASN 131 -1.75 THR 102
ASN 210 1.11 LYS 132 -1.19 LYS 101
PHE 113 1.30 MET 133 -0.89 LYS 101
THR 211 1.04 PHE 134 -0.79 LYS 101
SER 227 1.10 CYS 135 -0.67 LYS 101
SER 227 1.22 GLN 136 -0.67 GLY 226
ARG 213 1.20 LEU 137 -0.74 GLY 226
SER 227 1.11 ALA 138 -1.04 THR 253
SER 227 1.30 LYS 139 -0.90 GLY 226
SER 227 1.30 LYS 139 -0.90 GLY 226
SER 227 1.22 THR 140 -1.05 GLY 199
HIS 214 1.07 CYS 141 -1.58 TYR 126
HIS 214 0.88 PRO 142 -1.04 TYR 126
VAL 216 1.35 VAL 143 -1.38 SER 127
VAL 216 1.17 GLN 144 -1.39 PRO 128
VAL 218 1.39 LEU 145 -1.52 PRO 128
GLU 221 1.39 TRP 146 -1.54 PRO 128
PRO 219 1.46 VAL 147 -1.43 ALA 129
GLU 221 1.47 ASP 148 -1.29 ALA 129
TYR 220 0.89 SER 149 -1.38 PRO 128
ARG 202 0.52 THR 150 -1.56 LEU 265
ARG 202 1.07 PRO 151 -1.50 LEU 264
LEU 201 1.35 PRO 152 -1.53 ASN 263
LEU 201 1.41 PRO 152 -1.48 ASN 263
LEU 201 1.61 PRO 153 -1.12 SER 261
ARG 202 1.63 PRO 153 -1.30 ASP 228
ARG 202 0.58 GLY 154 -1.19 THR 230
ARG 202 0.66 GLY 154 -1.22 THR 230
PHE 109 0.75 THR 155 -1.41 THR 230
PHE 109 1.26 ARG 156 -1.22 LEU 188
PHE 109 1.54 VAL 157 -1.55 LEU 188
LEU 111 1.46 ARG 158 -1.54 LEU 188
LEU 111 1.65 ALA 159 -1.56 LEU 188
ARG 209 1.15 MET 160 -1.49 ALA 189
ARG 209 1.55 ALA 161 -1.44 ILE 195
PRO 98 1.53 ILE 162 -1.44 ILE 195
ASN 210 1.68 TYR 163 -1.16 HIS 193
ASN 210 1.25 LYS 164 -0.92 HIS 193
LEU 130 1.43 GLN 165 -0.87 HIS 193
LEU 130 1.28 SER 166 -1.01 HIS 193
ALA 129 1.39 GLN 167 -0.99 HIS 214
LEU 130 1.41 HIS 168 -1.23 HIS 193
LEU 130 1.10 MET 169 -1.39 HIS 193
ASN 247 1.12 THR 170 -1.37 HIS 214
LEU 130 1.45 GLU 171 -1.37 HIS 214
LEU 130 1.45 GLU 171 -1.38 HIS 214
ASN 247 1.58 VAL 172 -1.52 SER 215
THR 211 1.31 VAL 173 -1.40 HIS 193
ASP 207 1.63 ARG 174 -0.95 ARG 249
PHE 212 1.73 ARG 175 -0.54 MET 246
PHE 212 1.63 CYS 176 -0.51 LEU 201
PHE 212 1.33 PRO 177 -0.60 LEU 201
THR 211 1.18 HIS 178 -1.01 LEU 201
ARG 213 1.22 HIS 179 -1.22 LEU 201
ARG 213 1.26 GLU 180 -0.84 LEU 201
ARG 213 0.96 ARG 181 -1.23 LEU 201
ARG 213 0.68 CYS 182 -1.79 LEU 201
SER 227 0.81 SER 185 -1.31 VAL 203
SER 227 0.44 ASP 186 -1.31 ASN 200
PRO 190 0.45 GLY 187 -1.58 VAL 218
SER 227 0.17 LEU 188 -1.56 ALA 159
SER 227 0.46 ALA 189 -1.51 ALA 159
SER 227 0.46 PRO 190 -1.51 VAL 216
ARG 213 0.63 PRO 191 -1.04 MET 160
PHE 212 0.88 GLN 192 -1.06 VAL 173
PHE 212 0.90 GLN 192 -1.03 VAL 173
SER 185 0.74 HIS 193 -1.40 VAL 173
HIS 214 1.46 LEU 194 -1.33 ALA 161
HIS 214 1.20 ILE 195 -1.44 ILE 162
TYR 205 0.94 ARG 196 -1.46 THR 253
TYR 205 0.96 VAL 197 -1.47 ILE 255
TYR 205 0.70 GLU 198 -1.05 ILE 255
PRO 153 0.60 GLY 199 -1.16 GLU 224
PRO 153 1.05 ASN 200 -1.51 GLY 187
PRO 153 1.61 LEU 201 -1.79 CYS 182
PRO 153 1.63 ARG 202 -1.56 CYS 182
PRO 153 1.53 VAL 203 -1.45 CYS 182
PRO 153 1.16 GLU 204 -1.05 CYS 182
VAL 143 1.21 TYR 205 -1.01 VAL 172
ARG 174 1.18 LEU 206 -1.04 VAL 172
ARG 174 1.63 ASP 207 -1.04 GLU 171
GLY 245 1.45 ASP 208 -0.38 SER 96
PRO 98 1.56 ARG 209 -0.32 TYR 205
TYR 163 1.68 ASN 210 -0.20 PRO 152
ASN 247 1.76 THR 211 -0.44 PRO 152
ARG 175 1.73 PHE 212 -1.19 SER 96
CYS 238 1.73 ARG 213 -1.63 SER 96
LEU 194 1.46 HIS 214 -1.38 GLU 171
VAL 143 1.22 SER 215 -1.52 VAL 172
VAL 143 1.35 VAL 216 -1.51 PRO 190
LEU 111 1.28 VAL 217 -1.22 LEU 188
LEU 145 1.39 VAL 218 -1.58 GLY 187
VAL 147 1.46 PRO 219 -1.48 GLY 187
TYR 107 1.57 TYR 220 -1.52 GLY 187
ASP 148 1.47 GLU 221 -1.11 GLY 187
ASP 148 1.47 GLU 221 -1.11 GLY 187
ASP 148 1.29 PRO 222 -1.16 GLY 154
ASP 148 0.77 PRO 223 -1.15 GLY 154
ASP 148 0.57 GLU 224 -1.32 GLY 187
SER 149 0.64 VAL 225 -1.19 GLY 187
SER 149 0.60 GLY 226 -1.09 GLY 187
VAL 122 1.48 SER 227 -0.61 SER 149
VAL 122 1.13 ASP 228 -1.30 PRO 153
HIS 115 1.20 CYS 229 -1.26 PRO 128
HIS 115 0.91 THR 230 -1.44 ASP 259
SER 116 0.92 THR 231 -1.31 PRO 128
TYR 205 0.71 ILE 232 -1.49 ASN 268
SER 227 0.83 HIS 233 -1.37 ASN 268
TYR 205 1.11 TYR 234 -1.52 SER 269
SER 227 0.89 ASN 235 -1.57 THR 253
HIS 214 1.15 TYR 236 -1.40 THR 253
ARG 213 1.27 MET 237 -1.30 ALA 161
ARG 213 1.73 CYS 238 -0.79 ALA 161
ARG 213 1.72 CYS 238 -0.79 ALA 161
ARG 213 1.54 ASN 239 -0.57 GLY 226
THR 211 1.61 SER 240 -0.52 LYS 101
THR 211 1.74 SER 241 -0.46 GLY 226
THR 211 1.74 CYS 242 -0.51 GLY 226
THR 211 1.58 MET 243 -0.43 GLY 226
THR 211 1.37 GLY 244 -0.38 GLY 226
THR 211 1.47 GLY 245 -0.34 GLY 226
ASN 210 1.60 MET 246 -0.67 ARG 174
THR 211 1.76 ASN 247 -0.38 ARG 174
THR 211 1.58 TRP 248 -0.50 ARG 174
LEU 130 1.42 ARG 249 -0.95 ARG 174
ASN 210 1.36 PRO 250 -0.69 TYR 236
ASN 210 1.48 ILE 251 -0.86 TYR 236
ASN 210 1.27 LEU 252 -1.06 ASN 235
ARG 209 1.19 THR 253 -1.57 ASN 235
ARG 209 1.08 ILE 254 -1.43 ARG 196
LEU 111 1.08 ILE 255 -1.47 VAL 197
LEU 111 0.87 THR 256 -1.32 LEU 188
PHE 109 0.93 LEU 257 -1.28 ILE 232
PHE 109 0.58 GLU 258 -1.33 THR 230
ARG 209 0.48 ASP 259 -1.44 THR 230
ARG 174 0.63 SER 260 -1.05 THR 230
ARG 174 0.79 SER 261 -1.12 PRO 153
ARG 174 0.79 GLY 262 -1.06 PRO 152
ARG 209 0.72 ASN 263 -1.53 PRO 152
ARG 209 0.76 LEU 264 -1.50 PRO 151
ARG 209 0.61 LEU 265 -1.56 THR 150
ARG 209 0.65 GLY 266 -1.26 PRO 128
ARG 209 0.75 ARG 267 -1.26 ILE 232
ARG 209 0.86 ASN 268 -1.45 ILE 232
ARG 209 0.88 ASN 268 -1.49 ILE 232
ARG 209 0.95 SER 269 -1.52 TYR 234
ASN 210 1.01 PHE 270 -1.36 ASN 235
PHE 113 1.27 GLU 271 -1.16 LYS 101
PHE 113 1.28 GLU 271 -1.14 LYS 101
PHE 113 1.63 VAL 272 -0.86 LYS 101
THR 211 1.27 ARG 273 -0.72 LYS 101
THR 211 1.27 VAL 274 -0.63 LYS 101
THR 211 1.26 CYS 275 -0.56 LYS 101
THR 211 1.17 ALA 276 -0.59 GLY 226
SER 227 1.26 CYS 277 -0.58 LYS 101
SER 227 1.18 PRO 278 -0.68 LYS 101
SER 227 1.20 GLY 279 -0.69 LYS 101
SER 227 1.13 ARG 280 -0.67 LYS 101
SER 127 1.03 ASP 281 -0.72 LYS 101
SER 227 0.94 ARG 282 -0.83 LYS 101
SER 227 0.94 ARG 283 -0.81 LYS 101
SER 127 1.40 THR 284 -0.78 LYS 101
SER 127 1.52 GLU 285 -0.91 LYS 101
PRO 128 1.05 GLU 286 -1.02 LYS 101
PRO 128 1.28 GLU 287 -0.91 LYS 101
PRO 128 1.59 ASN 288 -0.91 LYS 101
PRO 128 1.49 LEU 289 -1.07 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 8th, 2025.