CNRS Nantes University US2B US2B
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CA distance fluctuations for 2503091549044093504

---  normal mode 18  ---

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
ASN 263 1.88 SER 96 -0.79 HIS 168
HIS 178 1.54 VAL 97 -0.80 TYR 103
CYS 277 1.48 PRO 98 -0.52 SER 261
GLN 167 1.24 SER 99 -0.98 PRO 153
THR 284 1.70 GLN 100 -1.45 ASN 263
MET 160 0.90 LYS 101 -0.83 SER 166
GLU 285 0.75 THR 102 -0.69 VAL 97
SER 96 0.91 TYR 103 -0.90 THR 170
SER 96 0.87 GLN 104 -0.88 THR 170
SER 96 1.08 GLY 105 -0.95 THR 170
SER 96 1.22 SER 106 -0.88 ASP 228
SER 96 1.14 TYR 107 -1.10 ASP 228
SER 96 0.90 GLY 108 -1.12 ASP 228
SER 96 0.84 PHE 109 -0.92 ASP 228
SER 96 0.58 ARG 110 -0.85 THR 170
SER 269 0.49 LEU 111 -0.82 ILE 255
PRO 128 0.61 GLY 112 -0.99 CYS 124
PRO 128 1.17 PHE 113 -1.35 CYS 124
PRO 142 1.00 LEU 114 -1.07 GLU 224
PRO 98 1.21 VAL 122 -1.44 GLU 224
PRO 98 1.13 THR 123 -1.33 GLU 224
PRO 98 0.91 CYS 124 -1.35 PHE 113
PRO 98 0.88 THR 125 -0.90 GLU 224
CYS 141 1.17 TYR 126 -0.58 GLU 224
CYS 141 0.84 SER 127 -0.67 ASN 247
PHE 113 1.17 PRO 128 -0.59 ASN 247
PHE 113 0.84 ALA 129 -0.71 ASN 247
GLN 100 0.88 LEU 130 -0.71 ASN 247
CYS 141 0.71 ASN 131 -0.53 ASN 247
CYS 141 0.75 LYS 132 -0.61 ARG 248
CYS 141 0.98 MET 133 -0.59 ARG 248
CYS 141 0.99 MET 133 -0.59 ARG 248
PRO 98 0.94 PHE 134 -0.69 ARG 248
PRO 98 0.99 CYS 135 -0.81 GLU 224
PRO 98 1.14 GLN 136 -0.89 GLU 224
PRO 98 1.01 LEU 137 -0.64 GLU 224
PRO 98 0.84 ALA 138 -0.49 GLU 224
PRO 98 0.89 LYS 139 -0.82 GLY 199
TYR 126 1.00 THR 140 -0.91 ASN 200
TYR 126 1.17 CYS 141 -0.79 GLU 224
TYR 126 1.17 CYS 141 -0.79 GLU 224
LEU 114 1.00 PRO 142 -0.95 VAL 216
PRO 128 0.84 VAL 143 -1.11 ALA 159
PRO 128 0.63 GLN 144 -0.98 VAL 157
VAL 197 0.67 LEU 145 -1.04 VAL 157
SER 96 0.65 TRP 146 -0.78 ASP 228
SER 96 0.84 VAL 147 -1.41 ASP 228
SER 96 0.88 ASP 148 -1.60 ASP 228
SER 96 1.02 SER 149 -1.27 ASP 228
SER 96 1.10 THR 150 -0.95 ASP 228
SER 96 1.26 PRO 151 -1.12 ASP 228
SER 96 1.08 PRO 152 -0.92 THR 170
SER 96 0.98 PRO 153 -0.98 SER 99
SER 96 1.09 GLY 154 -0.86 THR 170
SER 96 1.16 THR 155 -0.95 THR 170
SER 96 1.10 ARG 156 -0.93 THR 170
SER 96 0.99 VAL 157 -1.05 THR 231
SER 96 0.92 ARG 158 -1.07 ILE 232
ARG 174 0.87 ALA 159 -1.11 VAL 143
LYS 101 0.90 MET 160 -0.83 VAL 143
GLU 285 0.90 ALA 161 -0.49 VAL 143
GLU 285 1.12 ILE 162 -0.48 GLU 171
GLU 285 1.34 TYR 163 -0.47 SER 269
GLU 285 1.58 LYS 164 -0.64 SER 269
THR 284 1.56 GLN 165 -0.72 SER 269
ARG 248 1.26 SER 166 -1.05 SER 269
ARG 248 1.27 SER 166 -1.05 SER 269
SER 99 1.24 GLN 167 -0.75 SER 96
ARG 248 1.28 HIS 168 -0.79 SER 96
ARG 248 1.78 MET 169 -0.98 SER 269
ASN 247 1.48 THR 170 -1.51 LEU 264
ARG 248 1.47 GLU 171 -0.90 LEU 264
GLY 244 1.59 VAL 172 -0.72 ALA 189
MET 243 1.55 VAL 173 -0.60 HIS 193
VAL 216 1.27 ARG 174 -0.52 PRO 250
VAL 97 1.04 ARG 175 -0.40 SER 185
VAL 97 1.30 CYS 176 -0.31 SER 185
VAL 97 1.53 PRO 177 -0.25 SER 185
VAL 97 1.54 HIS 178 -0.26 SER 185
VAL 97 1.26 HIS 179 -0.40 SER 185
VAL 97 1.22 GLU 180 -0.40 SER 185
VAL 97 1.35 ARG 181 -0.34 GLY 187
LEU 201 0.96 SER 185 -0.67 ILE 195
SER 227 1.03 ASP 186 -0.64 ARG 196
LEU 201 1.16 GLY 187 -0.57 PHE 212
ASN 200 1.22 LEU 188 -0.74 PHE 212
LEU 201 1.18 ALA 189 -0.76 PHE 212
VAL 203 1.51 PRO 190 -0.64 VAL 172
VAL 203 1.39 PRO 191 -0.40 VAL 172
VAL 203 1.49 GLN 192 -0.34 VAL 172
VAL 203 1.24 HIS 193 -0.70 VAL 172
ALA 159 0.75 LEU 194 -0.67 SER 185
GLU 221 0.76 ILE 195 -0.67 SER 185
GLU 221 1.01 ARG 196 -0.64 ASP 186
GLU 221 1.18 VAL 197 -0.80 TYR 205
GLU 221 1.17 GLU 198 -0.77 THR 140
GLU 221 1.42 GLY 199 -0.82 LYS 139
LEU 188 1.22 ASN 200 -0.91 THR 140
PRO 190 1.47 LEU 201 -0.92 VAL 225
PRO 190 1.33 ARG 202 -0.90 THR 231
PRO 190 1.51 VAL 203 -0.90 THR 231
GLN 192 1.34 GLU 204 -0.98 ILE 232
ARG 174 1.21 TYR 205 -1.05 HIS 233
ARG 174 1.05 LEU 206 -0.90 ILE 232
GLY 245 1.16 ASP 207 -0.74 HIS 233
GLY 245 1.24 ASP 208 -0.64 ILE 232
GLY 245 1.26 ARG 209 -0.69 LEU 188
GLY 245 1.32 ASN 210 -0.61 LEU 188
GLY 245 1.45 THR 211 -0.58 LEU 188
GLY 245 1.56 PHE 212 -0.76 ALA 189
GLY 245 1.34 ARG 213 -0.61 ILE 232
ARG 174 1.21 HIS 214 -0.74 TYR 234
ARG 174 1.23 SER 215 -1.00 HIS 233
ARG 174 1.27 VAL 216 -1.36 ILE 232
GLN 192 1.10 VAL 217 -1.38 ILE 232
PRO 190 1.18 VAL 218 -1.33 THR 231
PRO 190 1.04 PRO 219 -0.94 THR 231
SER 96 0.97 TYR 220 -1.08 THR 230
GLY 199 1.42 GLU 221 -0.70 GLY 154
GLY 199 1.01 PRO 222 -0.54 THR 170
GLY 199 0.87 PRO 223 -0.76 VAL 122
SER 96 0.51 GLU 224 -1.44 VAL 122
SER 96 0.56 VAL 225 -1.08 VAL 122
ASP 228 1.22 GLY 226 -0.57 VAL 122
LEU 188 1.19 SER 227 -0.92 SER 149
GLY 226 1.22 ASP 228 -1.60 ASP 148
SER 96 0.54 CYS 229 -0.88 THR 123
GLY 199 0.72 THR 230 -1.08 TYR 220
SER 227 0.74 THR 231 -1.33 VAL 218
SER 227 0.91 ILE 232 -1.38 VAL 217
SER 227 0.95 HIS 233 -1.33 VAL 216
SER 227 0.79 TYR 234 -1.00 VAL 216
SER 227 0.79 ASN 235 -0.56 MET 160
PRO 98 0.74 TYR 236 -0.42 MET 160
PRO 98 0.77 MET 237 -0.46 SER 185
PRO 98 0.88 CYS 238 -0.37 GLU 224
VAL 97 0.88 CYS 238 -0.37 GLU 224
PRO 98 1.03 ASN 239 -0.46 GLU 224
PRO 98 0.98 SER 240 -0.52 ARG 248
HIS 168 1.16 SER 241 -0.39 GLU 224
VAL 97 1.11 CYS 242 -0.31 GLU 224
VAL 173 1.55 MET 243 -0.40 ARG 249
VAL 172 1.59 GLY 244 -0.23 GLU 224
PHE 212 1.56 GLY 245 -0.38 SER 241
THR 170 1.28 MET 246 -0.50 ALA 129
THR 170 1.48 ASN 247 -0.71 LEU 130
MET 169 1.78 ARG 248 -0.75 ARG 273
MET 169 1.14 ARG 249 -0.41 ARG 273
GLU 285 1.38 PRO 250 -0.52 ARG 174
GLU 285 1.27 ILE 251 -0.36 GLU 224
GLU 285 1.13 LEU 252 -0.39 GLU 224
GLU 285 0.82 THR 253 -0.56 CYS 124
LYS 101 0.81 ILE 254 -0.80 THR 170
LYS 101 0.81 ILE 254 -0.80 THR 170
SER 96 0.73 ILE 255 -0.88 THR 170
SER 96 1.00 THR 256 -1.10 THR 170
SER 96 1.00 THR 256 -1.10 THR 170
SER 96 1.14 LEU 257 -1.09 THR 170
SER 96 1.39 GLU 258 -1.22 THR 170
SER 96 1.43 ASP 259 -1.15 THR 170
SER 96 1.31 SER 260 -1.03 GLN 100
SER 96 1.44 SER 261 -1.22 GLN 100
SER 96 1.53 GLY 262 -1.28 THR 170
SER 96 1.88 ASN 263 -1.47 THR 170
SER 96 1.53 LEU 264 -1.51 THR 170
SER 96 1.30 LEU 265 -1.25 THR 170
SER 96 1.07 GLY 266 -1.13 THR 170
SER 96 0.84 ARG 267 -1.08 THR 170
VAL 197 0.70 ASN 268 -0.90 THR 170
VAL 197 0.85 SER 269 -1.05 SER 166
ILE 195 0.75 PHE 270 -0.57 SER 166
GLU 285 0.86 GLU 271 -0.44 LYS 164
ILE 195 0.76 VAL 272 -0.54 ARG 248
ILE 195 0.76 VAL 272 -0.53 ARG 248
PRO 98 0.95 ARG 273 -0.75 ARG 248
PRO 98 1.03 VAL 274 -0.60 GLU 224
PRO 98 1.25 CYS 275 -0.68 GLU 224
PRO 98 1.47 ALA 276 -0.79 GLU 224
PRO 98 1.48 CYS 277 -0.90 GLU 224
PRO 98 1.48 CYS 277 -0.90 GLU 224
PRO 98 1.24 PRO 278 -0.88 GLU 224
PRO 98 1.26 GLY 279 -0.97 GLU 224
PRO 98 1.33 ARG 280 -0.80 GLU 224
GLN 100 1.37 ASP 281 -0.62 GLU 224
GLN 100 1.35 ARG 282 -0.64 GLU 224
GLN 100 1.63 ARG 283 -0.69 GLU 224
GLN 100 1.70 THR 284 -0.52 GLU 224
LYS 164 1.58 GLU 285 -0.46 MET 246
GLN 100 1.69 GLU 286 -0.41 GLU 224
GLN 100 1.68 GLU 287 -0.43 GLU 224

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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.