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CA distance fluctuations for 2501100054483836345

---  normal mode 25  ---

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
PHE 212 0.93 SER 96 -1.20 ASN 263
PHE 212 1.47 VAL 97 -1.02 ASN 263
THR 211 1.29 PRO 98 -1.04 SER 185
THR 211 1.61 SER 99 -0.94 SER 185
THR 211 1.53 GLN 100 -0.91 SER 185
THR 211 1.40 LYS 101 -0.88 SER 185
THR 211 1.32 THR 102 -0.85 SER 185
THR 211 1.22 TYR 103 -0.93 ASP 186
PRO 222 1.15 GLN 104 -0.92 ASP 186
PRO 222 1.56 GLY 105 -1.13 LEU 206
PRO 222 1.73 SER 106 -1.28 LEU 206
PRO 223 1.29 TYR 107 -1.31 LEU 206
ALA 129 1.15 GLY 108 -1.02 ASP 186
ASN 131 1.09 PHE 109 -1.07 ASP 186
ASN 131 1.44 ARG 110 -0.96 ASP 186
ASN 131 1.58 LEU 111 -0.90 THR 256
ASN 131 1.41 GLY 112 -0.92 VAL 157
PRO 151 1.09 PHE 113 -1.05 ILE 255
PRO 151 1.26 LEU 114 -0.89 ARG 158
PRO 151 1.04 VAL 122 -0.68 GLY 262
PRO 151 0.98 THR 123 -0.77 GLY 262
PRO 151 0.99 CYS 124 -0.79 GLY 262
PRO 151 0.99 THR 125 -0.71 GLY 262
PRO 151 0.94 TYR 126 -0.73 SER 185
GLY 112 1.07 SER 127 -0.99 ARG 282
TRP 146 1.46 PRO 128 -1.21 GLU 286
TRP 146 1.33 ALA 129 -1.47 GLU 287
ARG 110 1.36 LEU 130 -1.56 GLU 286
LEU 111 1.58 ASN 131 -1.27 GLU 286
LEU 111 1.23 LYS 132 -0.99 GLU 285
GLY 112 0.84 MET 133 -0.75 GLY 262
PRO 151 0.84 MET 133 -0.75 GLY 262
PRO 151 0.80 PHE 134 -0.82 GLY 262
PRO 151 0.83 CYS 135 -0.89 GLY 262
TYR 205 0.82 GLN 136 -0.91 GLY 262
TYR 205 1.00 LEU 137 -1.04 GLY 262
TYR 205 1.07 ALA 138 -1.10 GLY 262
TYR 205 0.85 LYS 139 -0.98 GLY 262
PRO 151 0.93 THR 140 -0.93 GLY 262
PRO 151 0.94 CYS 141 -0.94 SER 185
PRO 151 0.94 CYS 141 -0.94 SER 185
PRO 151 1.07 PRO 142 -1.06 ARG 158
PRO 151 0.88 VAL 143 -1.26 ARG 158
ASN 131 0.98 GLN 144 -1.21 VAL 157
ASN 131 1.12 LEU 145 -1.74 VAL 157
PRO 128 1.46 TRP 146 -1.18 VAL 157
ALA 129 1.23 VAL 147 -1.28 ASP 186
ALA 129 1.21 ASP 148 -1.15 TYR 220
ALA 129 0.95 SER 149 -1.30 LEU 206
ALA 129 0.69 THR 150 -1.60 ASP 207
ASP 228 1.38 PRO 151 -1.05 LEU 206
CYS 229 1.31 PRO 152 -1.12 LEU 206
PRO 223 1.40 PRO 153 -1.31 ASP 207
GLU 224 1.75 GLY 154 -1.56 ASP 207
GLU 221 1.56 THR 155 -1.50 ASP 186
ASN 210 1.05 ARG 156 -1.44 ASP 186
ASN 210 1.34 VAL 157 -1.74 LEU 145
ASN 210 1.37 ARG 158 -1.33 ILE 232
ASN 210 1.13 ALA 159 -1.40 SER 185
ARG 209 0.99 MET 160 -1.44 SER 185
MET 243 0.87 ALA 161 -1.24 GLY 262
GLY 244 0.99 ILE 162 -1.21 ASN 263
GLY 244 0.89 TYR 163 -1.14 GLY 262
LEU 111 0.79 LYS 164 -0.84 GLY 262
ARG 110 0.86 GLN 165 -0.97 ARG 174
THR 102 1.15 SER 166 -0.72 ARG 174
THR 102 1.15 SER 166 -0.72 ARG 174
THR 102 0.81 GLN 167 -1.00 ARG 174
THR 102 0.60 HIS 168 -1.26 GLN 192
GLN 100 0.75 MET 169 -1.11 HIS 193
GLY 245 1.20 THR 170 -1.24 ASN 263
ARG 248 1.39 GLU 171 -1.46 SER 261
GLY 245 1.72 VAL 172 -1.88 ASN 263
MET 243 1.30 VAL 173 -1.61 ASN 263
SER 215 1.88 ARG 174 -1.24 HIS 168
HIS 214 1.34 ARG 175 -1.21 GLY 262
HIS 214 1.74 CYS 176 -0.97 GLY 262
ASP 207 1.42 PRO 177 -1.03 SER 261
ASP 207 1.06 HIS 178 -1.01 SER 261
LEU 206 1.02 HIS 179 -1.21 GLY 262
LEU 206 1.23 GLU 180 -1.33 GLY 262
LEU 206 1.30 ARG 181 -1.26 SER 261
LEU 206 0.59 SER 185 -1.74 VAL 216
PRO 190 0.16 ASP 186 -1.60 GLU 258
PRO 190 0.25 GLY 187 -1.64 SER 260
LYS 139 0.57 LEU 188 -1.62 SER 260
ALA 138 0.66 ALA 189 -1.68 SER 260
TYR 205 0.62 PRO 190 -1.69 SER 261
TYR 205 1.26 PRO 191 -1.77 SER 261
TYR 205 1.39 GLN 192 -1.50 SER 261
TYR 205 1.35 HIS 193 -1.52 GLY 262
TYR 205 0.93 LEU 194 -1.49 GLY 262
TYR 220 0.77 ILE 195 -1.60 GLY 262
TYR 220 0.77 ARG 196 -1.36 GLY 262
TYR 220 0.79 VAL 197 -1.24 SER 185
PRO 151 0.77 GLU 198 -0.90 SER 185
GLY 226 0.88 GLY 199 -0.78 SER 185
GLY 226 0.73 ASN 200 -0.90 SER 185
GLY 226 0.65 LEU 201 -0.76 SER 185
ARG 174 0.65 ARG 202 -0.97 ASP 186
ARG 174 0.75 VAL 203 -1.16 ASP 186
ARG 174 1.15 GLU 204 -1.50 ASP 186
GLN 192 1.39 TYR 205 -1.57 ASP 207
ARG 181 1.30 LEU 206 -1.41 THR 150
PRO 177 1.42 ASP 207 -1.60 THR 150
ARG 174 1.64 ASP 208 -1.16 ALA 189
ARG 158 1.14 ARG 209 -1.33 LEU 188
THR 256 1.71 ASN 210 -0.97 PRO 190
SER 99 1.61 THR 211 -1.13 PRO 190
VAL 97 1.47 PHE 212 -1.66 SER 261
GLY 245 1.24 ARG 213 -1.68 ALA 189
CYS 176 1.74 HIS 214 -1.77 ASP 259
ARG 174 1.88 SER 215 -1.41 LEU 264
ARG 174 1.15 VAL 216 -1.74 SER 185
ASN 210 0.98 VAL 217 -1.51 ILE 232
ASN 210 0.98 VAL 218 -1.21 THR 230
ASN 210 0.83 PRO 219 -1.30 ASP 186
PHE 270 0.99 TYR 220 -1.15 VAL 147
THR 155 1.56 GLU 221 -0.98 ASP 186
SER 106 1.73 PRO 222 -0.76 ASP 186
PRO 153 1.40 PRO 223 -0.81 SER 185
GLY 154 1.75 GLU 224 -0.49 SER 185
GLY 154 1.67 VAL 225 -0.41 SER 185
GLY 154 1.07 GLY 226 -0.32 GLY 112
PRO 151 1.14 SER 227 -0.45 SER 185
PRO 151 1.38 ASP 228 -0.90 VAL 157
PRO 152 1.31 CYS 229 -1.14 VAL 157
PRO 152 1.10 THR 230 -1.21 VAL 218
PRO 151 1.00 THR 231 -1.15 VAL 218
PRO 151 0.87 ILE 232 -1.51 VAL 217
PRO 151 0.92 HIS 233 -1.19 SER 185
PRO 151 0.76 TYR 234 -1.28 SER 185
TYR 205 0.83 ASN 235 -1.19 GLY 262
TYR 205 0.91 TYR 236 -1.27 GLY 262
TYR 205 1.20 MET 237 -1.27 GLY 262
TYR 205 1.06 CYS 238 -1.15 GLY 262
TYR 205 1.06 CYS 238 -1.15 GLY 262
TYR 205 0.88 ASN 239 -1.01 GLY 262
HIS 214 0.83 SER 240 -0.93 GLY 262
VAL 173 0.95 SER 241 -0.84 GLY 262
VAL 173 1.22 CYS 242 -0.90 GLY 262
VAL 173 1.30 MET 243 -0.90 GLY 262
GLU 171 1.26 GLY 244 -0.79 GLY 262
VAL 172 1.72 GLY 245 -0.57 GLY 262
VAL 172 1.27 MET 246 -0.74 THR 284
GLU 171 1.37 ASN 247 -0.86 THR 284
GLU 171 1.39 ARG 248 -0.81 GLY 262
GLU 171 1.36 ARG 249 -0.88 GLY 262
GLU 171 0.69 PRO 250 -1.00 GLY 262
MET 243 0.72 ILE 251 -1.06 GLY 262
MET 243 0.69 LEU 252 -0.89 GLY 262
THR 211 0.81 THR 253 -1.03 SER 185
THR 211 1.23 ILE 254 -1.14 SER 185
THR 211 1.23 ILE 254 -1.14 SER 185
ASN 210 1.35 ILE 255 -1.13 SER 185
ASN 210 1.71 THR 256 -1.16 SER 185
ASN 210 1.70 THR 256 -1.16 SER 185
ASN 210 1.32 LEU 257 -1.24 ASP 186
ASN 210 0.96 GLU 258 -1.60 ASP 186
GLU 224 1.48 ASP 259 -1.77 HIS 214
GLU 224 1.30 SER 260 -1.68 ALA 189
GLU 224 0.81 SER 261 -1.77 PRO 191
GLU 224 0.65 GLY 262 -1.60 ILE 195
GLU 224 0.89 ASN 263 -1.88 VAL 172
PRO 222 1.14 LEU 264 -1.41 SER 185
PRO 222 1.58 LEU 265 -1.28 ASP 186
PRO 222 1.22 GLY 266 -1.12 ASP 186
THR 211 1.46 ARG 267 -1.02 SER 185
THR 211 1.27 ASN 268 -0.93 SER 185
THR 211 1.16 SER 269 -0.94 SER 185
LEU 111 1.28 PHE 270 -0.73 SER 185
LEU 111 1.10 GLU 271 -0.73 SER 185
LEU 111 0.86 VAL 272 -0.85 GLY 262
LEU 111 0.86 VAL 272 -0.86 GLY 262
LEU 111 0.68 ARG 273 -0.88 GLY 262
TYR 205 0.74 VAL 274 -0.97 GLY 262
TYR 205 0.74 CYS 275 -0.87 GLY 262
TYR 205 0.81 ALA 276 -0.80 GLY 262
PRO 151 0.80 CYS 277 -0.73 GLY 262
PRO 151 0.80 CYS 277 -0.73 GLY 262
PRO 151 0.83 PRO 278 -0.75 GLY 262
PRO 151 0.89 GLY 279 -0.67 GLY 262
PRO 151 0.79 ARG 280 -0.76 LEU 130
PRO 151 0.70 ASP 281 -0.86 LEU 130
PRO 151 0.75 ARG 282 -0.99 SER 127
PRO 151 0.77 ARG 283 -1.14 ALA 129
PRO 151 0.65 THR 284 -1.33 LEU 130
PRO 151 0.57 GLU 285 -1.52 LEU 130
PRO 151 0.64 GLU 286 -1.56 LEU 130
PRO 151 0.61 GLU 287 -1.47 ALA 129

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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.