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CA distance fluctuations for 2503091552154099480

---  normal mode 30  ---

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
PRO 177 0.98 SER 96 -0.88 SER 261
PRO 177 1.06 VAL 97 -0.86 ILE 254
THR 211 1.45 PRO 98 -1.50 ILE 254
ILE 162 1.18 SER 99 -0.17 GLY 262
LEU 252 1.44 GLN 100 -0.34 GLY 262
LEU 252 1.43 LYS 101 -0.50 ASN 263
TYR 126 1.10 THR 102 -0.32 PRO 222
ILE 162 0.88 TYR 103 -0.46 PRO 222
ASN 200 0.90 GLN 104 -0.64 PRO 222
ASN 200 0.90 GLY 105 -0.64 PRO 222
ASN 200 0.90 SER 106 -0.75 GLU 221
ASN 200 1.03 TYR 107 -0.97 GLU 221
ASN 200 0.93 GLY 108 -1.01 PRO 222
ASN 200 1.07 PHE 109 -0.88 PRO 222
ASN 200 0.92 ARG 110 -0.71 PRO 222
CYS 124 0.83 LEU 111 -0.96 PHE 270
SER 227 0.98 GLY 112 -1.38 LEU 130
THR 123 0.87 PHE 113 -1.64 LEU 130
THR 123 1.10 LEU 114 -1.58 ASN 131
LEU 114 1.05 VAL 122 -1.05 HIS 178
SER 269 1.11 THR 123 -1.09 HIS 178
SER 269 1.35 CYS 124 -0.82 HIS 178
LYS 101 1.02 THR 125 -0.80 VAL 218
THR 102 1.10 TYR 126 -0.84 CYS 141
LYS 101 0.95 SER 127 -0.89 VAL 218
SER 166 0.99 PRO 128 -1.38 LEU 114
GLU 285 1.03 ALA 129 -1.28 LEU 114
THR 284 1.13 LEU 130 -1.64 PHE 113
GLN 165 1.17 ASN 131 -1.58 LEU 114
LYS 101 1.05 LYS 132 -1.45 VAL 143
LYS 101 1.20 MET 133 -1.39 CYS 141
LYS 101 1.21 MET 133 -1.39 CYS 141
LYS 101 1.11 PHE 134 -0.81 ASN 235
SER 269 1.18 CYS 135 -0.68 HIS 178
SER 269 1.03 GLN 136 -0.86 HIS 179
GLN 100 1.00 LEU 137 -0.87 HIS 179
GLN 100 0.78 ALA 138 -1.20 GLU 198
SER 269 0.89 LYS 139 -1.17 GLU 198
SER 269 0.95 THR 140 -0.96 MET 133
SER 269 1.23 CYS 141 -1.39 MET 133
SER 269 1.24 CYS 141 -1.39 MET 133
SER 269 0.83 PRO 142 -1.36 LYS 132
THR 150 0.75 VAL 143 -1.58 PHE 270
ASN 200 0.79 GLN 144 -1.63 PHE 270
ASN 200 1.12 LEU 145 -1.20 PHE 270
ASN 200 1.17 TRP 146 -1.01 ASN 131
ASN 200 0.86 VAL 147 -1.52 PRO 222
ASN 200 0.86 ASP 148 -1.37 PRO 222
ASN 200 1.13 SER 149 -1.00 GLY 226
ASN 200 1.56 THR 150 -0.76 GLY 226
ASN 200 1.21 PRO 151 -1.27 GLU 221
ASN 200 1.29 PRO 152 -0.73 GLU 204
ASN 200 1.44 PRO 153 -0.81 ARG 209
ASN 200 1.30 GLY 154 -0.97 ARG 209
ASN 200 1.53 THR 155 -0.89 GLU 204
ASN 200 1.18 ARG 156 -1.16 GLU 204
ASN 200 0.93 VAL 157 -0.82 VAL 147
VAL 197 0.72 ARG 158 -0.75 PHE 270
VAL 197 0.82 ALA 159 -0.83 PHE 270
ARG 175 1.01 MET 160 -0.72 VAL 97
GLN 100 1.32 ALA 161 -0.58 GLU 286
SER 99 1.18 ILE 162 -0.63 ILE 195
LYS 101 1.14 TYR 163 -0.69 ILE 195
LYS 101 1.17 LYS 164 -0.54 ILE 195
ASN 131 1.17 GLN 165 -0.63 MET 246
ASN 131 1.11 SER 166 -0.71 MET 246
ASN 131 1.11 SER 166 -0.71 MET 246
ASN 131 0.91 GLN 167 -0.66 PRO 190
ASN 131 0.73 HIS 168 -0.84 HIS 193
LYS 101 0.75 MET 169 -0.65 PRO 190
PRO 177 0.96 THR 170 -0.77 PRO 190
ARG 249 0.93 GLU 171 -0.82 PRO 190
CYS 176 1.03 VAL 172 -0.98 PRO 190
CYS 176 1.10 VAL 173 -0.80 HIS 193
SER 99 1.17 ARG 174 -0.73 HIS 168
GLN 100 1.16 ARG 175 -0.72 SER 185
VAL 173 1.10 CYS 176 -0.70 SER 185
ARG 209 1.39 PRO 177 -0.83 LEU 201
ARG 209 0.96 HIS 178 -1.16 GLY 199
GLY 245 1.46 HIS 179 -1.38 GLY 199
GLY 245 1.20 GLU 180 -1.12 ASP 186
ARG 209 1.06 ARG 181 -1.19 ASN 200
GLU 204 0.50 SER 185 -1.01 GLU 180
ASN 235 0.58 ASP 186 -1.12 GLU 180
GLU 221 0.58 GLY 187 -0.85 GLU 180
GLU 204 0.78 LEU 188 -0.70 VAL 225
GLU 204 0.80 ALA 189 -0.71 VAL 172
GLU 204 0.64 PRO 190 -1.00 PHE 212
MET 237 1.06 PRO 191 -0.73 VAL 172
TYR 205 0.83 GLN 192 -0.92 SER 185
GLN 100 0.72 HIS 193 -0.90 VAL 172
GLN 100 0.95 LEU 194 -0.74 VAL 173
GLN 100 0.66 ILE 195 -1.13 VAL 272
ILE 255 0.58 ARG 196 -1.01 VAL 272
ILE 255 0.96 VAL 197 -0.84 VAL 272
GLU 221 1.30 GLU 198 -1.29 HIS 179
GLU 221 1.60 GLY 199 -1.38 HIS 179
THR 150 1.56 ASN 200 -1.19 ARG 181
SER 149 0.67 LEU 201 -0.83 PRO 177
GLY 262 0.89 ARG 202 -1.34 VAL 225
LEU 188 0.64 VAL 203 -0.99 GLU 224
ALA 189 0.80 GLU 204 -1.19 PRO 219
GLN 192 0.83 TYR 205 -0.91 GLU 224
GLN 192 0.76 LEU 206 -0.82 GLU 224
PRO 177 0.85 ASP 207 -0.88 PRO 190
PRO 177 1.03 ASP 208 -0.81 SER 96
PRO 177 1.39 ARG 209 -1.11 SER 260
PRO 177 1.34 ASN 210 -0.67 SER 260
PRO 98 1.45 THR 211 -0.78 PRO 190
PRO 177 1.25 PHE 212 -1.00 PRO 190
PRO 98 1.00 ARG 213 -0.97 PRO 190
SER 99 0.82 HIS 214 -1.00 PRO 190
ARG 174 0.83 SER 215 -0.69 GLU 224
HIS 193 0.68 VAL 216 -0.93 PHE 270
GLY 262 0.60 VAL 217 -1.13 PHE 270
GLY 262 1.05 VAL 218 -1.54 THR 231
GLY 199 1.22 PRO 219 -1.19 GLU 204
GLY 199 1.46 TYR 220 -1.10 VAL 147
GLY 199 1.60 GLU 221 -1.51 VAL 147
GLY 199 1.34 PRO 222 -1.52 VAL 147
ASN 200 0.89 PRO 223 -1.08 VAL 218
LEU 201 0.49 GLU 224 -1.46 VAL 218
LEU 201 0.58 VAL 225 -1.34 ARG 202
VAL 122 0.87 GLY 226 -1.00 SER 149
GLY 112 0.98 SER 227 -0.98 VAL 218
ASN 200 0.82 ASP 228 -1.23 ASN 131
ASN 200 1.09 CYS 229 -1.38 ASN 131
ASN 200 0.99 THR 230 -1.32 VAL 218
ASN 200 0.70 THR 231 -1.54 VAL 218
GLU 198 0.78 ILE 232 -1.23 PHE 270
ILE 255 0.92 HIS 233 -1.11 VAL 218
ILE 255 1.19 TYR 234 -1.12 VAL 272
ILE 254 0.72 ASN 235 -1.33 VAL 272
GLN 100 0.86 TYR 236 -1.11 VAL 272
PRO 191 1.06 MET 237 -0.93 VAL 272
GLN 100 0.92 CYS 238 -0.82 GLU 286
GLN 100 0.92 CYS 238 -0.81 GLU 286
GLN 100 1.08 ASN 239 -0.77 GLU 286
GLN 100 1.14 SER 240 -0.93 GLU 286
GLN 100 0.96 SER 241 -0.83 GLU 285
GLN 100 0.94 CYS 242 -0.71 GLU 286
GLN 100 1.25 MET 243 -0.62 CYS 242
CYS 176 0.98 GLY 244 -0.96 GLU 286
HIS 179 1.46 GLY 245 -0.98 GLU 285
HIS 179 1.02 MET 246 -0.71 SER 166
HIS 179 0.95 ASN 247 -1.17 GLU 286
GLU 171 0.74 ARG 248 -1.32 GLU 286
GLU 171 0.93 ARG 249 -1.15 GLU 286
LYS 101 0.94 PRO 250 -0.99 GLU 286
LYS 101 1.12 ILE 251 -0.82 GLU 286
GLN 100 1.44 LEU 252 -0.82 GLY 112
VAL 274 1.10 THR 253 -0.92 PRO 98
CYS 141 1.18 ILE 254 -1.50 PRO 98
CYS 141 1.18 ILE 254 -1.50 PRO 98
TYR 234 1.19 ILE 255 -1.02 PRO 98
ASN 200 0.96 THR 256 -0.61 PRO 98
ASN 200 0.96 THR 256 -0.61 PRO 98
ASN 200 1.18 LEU 257 -0.50 GLU 204
ASN 200 1.11 GLU 258 -0.55 ARG 209
ASN 200 1.20 ASP 259 -0.75 ARG 209
ASN 200 1.08 SER 260 -1.11 ARG 209
VAL 218 0.92 SER 261 -1.01 ARG 209
VAL 218 1.05 GLY 262 -0.86 SER 96
ASN 200 0.93 ASN 263 -0.50 LYS 101
ASN 200 0.93 LEU 264 -0.50 LYS 101
ASN 200 1.03 LEU 265 -0.57 GLU 221
ASN 200 1.01 GLY 266 -0.50 PRO 222
ASN 200 0.89 ARG 267 -0.37 PRO 222
CYS 124 1.11 ASN 268 -0.61 PRO 98
CYS 124 1.35 SER 269 -0.90 PRO 98
LYS 101 1.40 PHE 270 -1.63 GLN 144
LYS 101 1.43 GLU 271 -1.26 VAL 143
LYS 101 1.25 VAL 272 -1.33 ASN 235
LYS 101 1.26 VAL 272 -1.32 ASN 235
LYS 101 1.09 ARG 273 -1.03 TYR 236
GLN 100 1.19 VAL 274 -0.94 GLU 286
LYS 101 1.00 CYS 275 -0.66 GLU 286
LYS 101 0.89 ALA 276 -0.80 HIS 178
LYS 101 0.95 CYS 277 -0.83 HIS 178
LYS 101 0.95 CYS 277 -0.84 HIS 178
LYS 101 1.02 PRO 278 -0.73 HIS 178
LYS 101 0.87 GLY 279 -0.77 HIS 178
LYS 101 0.90 ARG 280 -0.63 HIS 178
LYS 101 1.05 ASP 281 -0.52 HIS 178
LYS 101 0.89 ARG 282 -0.66 VAL 274
LYS 101 0.66 ARG 283 -0.72 VAL 218
LEU 130 1.13 THR 284 -0.48 VAL 218
LEU 130 1.08 GLU 285 -0.98 GLY 245
LYS 101 0.33 GLU 286 -1.32 ARG 248
LYS 101 0.39 GLU 287 -0.92 ASN 247

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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.