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CA distance fluctuations for 2501100054483836345

---  normal mode 31  ---

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 1.05 SER 96 -0.97 ILE 162
ASN 263 1.32 VAL 97 -1.07 ILE 162
ASN 263 1.65 PRO 98 -1.01 ILE 162
ARG 213 1.34 SER 99 -0.70 ILE 195
LEU 264 1.50 GLN 100 -0.92 LYS 164
ARG 213 1.56 LYS 101 -0.75 ILE 195
ARG 213 1.19 THR 102 -0.79 PHE 113
ARG 213 1.00 TYR 103 -0.73 ARG 209
PRO 128 0.91 GLN 104 -0.83 ARG 209
PRO 152 1.00 GLY 105 -0.91 ARG 209
GLY 199 1.06 SER 106 -0.98 ARG 209
PRO 128 1.20 TYR 107 -0.96 ARG 209
PRO 128 1.34 GLY 108 -0.89 ARG 209
PRO 128 1.36 PHE 109 -1.03 LEU 265
ASN 131 1.35 ARG 110 -0.76 THR 155
ASN 131 1.26 LEU 111 -0.78 TYR 220
SER 127 1.19 GLY 112 -0.80 LEU 188
GLU 221 1.15 PHE 113 -0.87 LEU 188
GLU 221 1.03 LEU 114 -1.00 CYS 141
GLU 221 1.23 VAL 122 -0.60 GLU 198
GLU 221 1.44 THR 123 -0.71 GLU 198
GLU 221 1.47 CYS 124 -0.89 LYS 139
GLU 221 1.17 THR 125 -1.01 ASN 235
GLY 112 1.07 TYR 126 -1.30 ASN 235
TRP 146 1.47 SER 127 -1.31 ARG 282
VAL 147 1.78 PRO 128 -1.45 GLU 286
ASP 228 1.50 ALA 129 -1.19 ASN 247
ASP 228 1.22 LEU 130 -1.45 ARG 248
ARG 110 1.35 ASN 131 -1.38 GLN 165
GLY 112 1.08 LYS 132 -1.64 ASN 235
GLU 285 1.19 MET 133 -1.76 ASN 235
GLU 285 1.19 MET 133 -1.76 ASN 235
GLU 221 1.13 PHE 134 -1.18 ASN 235
GLU 221 1.26 CYS 135 -0.98 LYS 139
GLU 221 1.28 GLN 136 -0.90 GLU 198
GLU 221 1.03 LEU 137 -1.11 GLU 198
SER 185 1.36 ALA 138 -1.26 VAL 272
SER 185 1.70 LYS 139 -1.19 MET 133
SER 185 1.59 THR 140 -1.01 MET 133
SER 185 1.35 CYS 141 -1.00 LEU 114
SER 185 1.37 CYS 141 -1.02 TYR 126
GLU 221 1.40 PRO 142 -1.04 LEU 188
GLU 221 1.34 VAL 143 -1.02 LEU 188
GLU 221 1.12 GLN 144 -0.92 TYR 220
PRO 128 1.35 LEU 145 -1.28 TYR 220
PRO 128 1.66 TRP 146 -1.51 THR 155
PRO 128 1.78 VAL 147 -1.21 LEU 265
PRO 128 1.26 ASP 148 -0.82 ARG 209
GLY 199 1.32 SER 149 -0.66 ARG 209
ILE 232 1.42 THR 150 -0.44 ARG 209
GLY 199 1.29 PRO 151 -0.70 ARG 209
ASN 200 1.05 PRO 152 -1.19 GLU 221
THR 211 0.86 PRO 153 -1.80 ASP 228
ASN 200 1.35 GLY 154 -1.51 CYS 229
ASN 200 1.27 THR 155 -1.51 TRP 146
VAL 197 1.04 ARG 156 -1.35 THR 230
PRO 151 1.10 VAL 157 -0.89 PRO 190
THR 150 0.85 ARG 158 -1.20 ASP 208
VAL 274 0.95 ALA 159 -1.16 ASP 208
VAL 274 1.21 MET 160 -1.34 ASN 210
SER 240 1.45 ALA 161 -1.33 ASN 210
SER 240 1.13 ILE 162 -1.07 VAL 97
HIS 214 1.07 TYR 163 -0.96 LEU 194
PHE 212 1.24 LYS 164 -1.13 ILE 195
PHE 212 1.54 GLN 165 -1.38 ASN 131
PHE 212 1.44 SER 166 -1.03 ALA 129
PHE 212 1.44 SER 166 -1.03 ALA 129
PHE 212 1.20 GLN 167 -1.18 ALA 129
ASP 207 1.45 HIS 168 -1.06 LEU 130
HIS 214 1.51 MET 169 -0.82 LEU 130
SER 261 1.28 THR 170 -0.87 LEU 130
ASP 207 1.48 GLU 171 -1.08 LEU 130
GLY 262 1.23 VAL 172 -0.87 SER 96
GLY 262 1.00 VAL 173 -0.76 ASN 210
LEU 206 1.13 ARG 174 -0.97 THR 211
LEU 206 1.05 ARG 175 -1.04 ILE 251
ASP 207 0.98 CYS 176 -1.19 THR 211
ASP 207 0.70 PRO 177 -1.48 THR 211
THR 284 0.58 HIS 178 -1.43 ARG 213
PRO 191 0.67 HIS 179 -1.24 ASP 186
ARG 209 0.51 GLU 180 -1.11 ARG 213
ARG 209 0.41 ARG 181 -1.34 ARG 213
LYS 139 1.70 SER 185 -1.60 ARG 213
THR 150 0.93 ASP 186 -1.24 HIS 179
PRO 190 0.84 GLY 187 -1.24 LEU 201
SER 261 0.49 LEU 188 -1.42 HIS 233
SER 261 0.73 ALA 189 -1.01 VAL 272
GLY 187 0.84 PRO 190 -1.66 SER 215
MET 237 1.28 PRO 191 -1.24 PHE 212
LEU 206 0.82 GLN 192 -0.96 THR 211
LEU 206 1.28 HIS 193 -1.38 VAL 272
LEU 206 0.77 LEU 194 -1.75 ILE 251
SER 185 0.85 ILE 195 -1.63 LEU 252
THR 150 0.96 ARG 196 -1.67 VAL 272
VAL 218 1.36 VAL 197 -1.18 ALA 138
THR 150 1.41 GLU 198 -1.11 LEU 137
SER 149 1.32 GLY 199 -0.80 ARG 181
GLY 154 1.35 ASN 200 -0.99 GLY 187
GLY 154 1.04 LEU 201 -1.24 GLY 187
SER 260 0.78 ARG 202 -1.09 SER 227
SER 261 0.85 VAL 203 -1.44 ILE 232
SER 261 1.34 GLU 204 -1.13 GLY 187
GLY 262 1.05 TYR 205 -1.10 PRO 190
HIS 193 1.28 LEU 206 -1.23 THR 230
GLU 171 1.48 ASP 207 -0.94 THR 230
SER 261 1.00 ASP 208 -1.32 MET 160
GLU 171 0.86 ARG 209 -1.15 GLU 258
SER 261 0.96 ASN 210 -1.34 MET 160
ASN 263 1.06 THR 211 -1.48 PRO 177
GLN 165 1.54 PHE 212 -1.24 PRO 191
LYS 101 1.56 ARG 213 -1.60 SER 185
MET 169 1.51 HIS 214 -1.20 PRO 190
GLY 262 1.40 SER 215 -1.66 PRO 190
GLY 262 1.27 VAL 216 -1.30 PRO 190
GLY 262 0.92 VAL 217 -1.18 PRO 190
VAL 197 1.36 VAL 218 -1.25 THR 231
GLU 198 1.27 PRO 219 -1.62 THR 230
PRO 151 1.28 TYR 220 -1.28 LEU 145
CYS 124 1.47 GLU 221 -1.19 PRO 152
PRO 128 1.38 PRO 222 -1.40 PRO 153
PRO 128 1.58 PRO 223 -1.22 PRO 153
PRO 128 1.40 GLU 224 -1.17 PRO 153
ALA 129 1.21 VAL 225 -1.28 PRO 153
LEU 114 1.02 GLY 226 -1.52 PRO 153
ALA 129 1.30 SER 227 -1.53 PRO 153
ALA 129 1.50 ASP 228 -1.80 PRO 153
SER 127 1.46 CYS 229 -1.51 GLY 154
PRO 128 1.25 THR 230 -1.62 PRO 219
GLU 221 1.28 THR 231 -1.25 VAL 218
GLU 221 1.42 ILE 232 -1.44 VAL 203
THR 150 1.41 HIS 233 -1.42 LEU 188
THR 150 1.15 TYR 234 -1.17 MET 133
SER 185 1.28 ASN 235 -1.76 MET 133
SER 185 1.21 TYR 236 -1.49 VAL 272
PRO 191 1.28 MET 237 -1.49 VAL 272
PRO 191 1.05 CYS 238 -0.93 PRO 250
PRO 191 1.04 CYS 238 -0.94 PRO 250
ALA 161 1.07 ASN 239 -0.84 LEU 130
ALA 161 1.45 SER 240 -1.06 LEU 130
ALA 161 0.98 SER 241 -0.77 LEU 130
ASP 207 0.89 CYS 242 -0.79 LEU 130
ASP 207 1.01 MET 243 -0.97 LEU 130
ASP 207 0.86 GLY 244 -0.99 LEU 130
ASP 207 1.08 GLY 245 -1.03 LEU 130
ASP 207 0.93 MET 246 -1.17 LEU 130
ASP 207 0.69 ASN 247 -1.40 LEU 130
THR 284 0.80 ARG 248 -1.45 LEU 130
THR 284 0.84 ARG 249 -1.14 LEU 130
THR 284 0.95 PRO 250 -1.42 LEU 194
GLU 285 1.06 ILE 251 -1.75 LEU 194
GLU 285 0.94 LEU 252 -1.63 ILE 195
GLU 285 1.01 THR 253 -1.30 ILE 195
LEU 264 0.82 ILE 254 -0.89 ASN 210
LEU 264 0.81 ILE 254 -0.89 ASN 210
GLU 221 0.78 ILE 255 -1.07 ASP 208
PRO 151 0.84 THR 256 -1.13 ASP 208
PRO 151 0.84 THR 256 -1.12 ASP 208
PRO 151 1.07 LEU 257 -1.02 ARG 209
ASN 200 0.90 GLU 258 -1.15 ARG 209
ASN 200 0.97 ASP 259 -1.18 VAL 147
GLU 204 1.21 SER 260 -1.10 GLU 221
GLU 204 1.34 SER 261 -0.81 GLU 221
SER 215 1.40 GLY 262 -0.88 ARG 209
PRO 98 1.65 ASN 263 -0.77 VAL 147
GLN 100 1.50 LEU 264 -1.14 ARG 209
ARG 213 1.09 LEU 265 -1.21 VAL 147
PRO 152 1.04 GLY 266 -1.01 ARG 209
PRO 152 0.90 ARG 267 -0.85 ASP 208
ARG 213 0.79 ASN 268 -0.81 ILE 195
LEU 264 0.74 SER 269 -1.21 ILE 195
LEU 111 0.87 PHE 270 -1.52 ILE 195
GLU 285 1.10 GLU 271 -1.61 ILE 195
GLU 285 1.57 VAL 272 -1.67 ARG 196
GLU 285 1.56 VAL 272 -1.67 ARG 196
GLU 285 1.24 ARG 273 -1.41 TYR 236
ALA 161 1.31 VAL 274 -0.86 LEU 130
GLU 221 1.05 CYS 275 -0.81 LEU 130
GLU 221 1.05 ALA 276 -0.70 ALA 129
GLU 221 1.01 CYS 277 -0.74 SER 127
GLU 221 1.02 CYS 277 -0.73 SER 127
GLU 221 1.10 PRO 278 -0.93 SER 127
GLU 221 0.96 GLY 279 -0.79 SER 127
GLU 221 0.89 ARG 280 -0.74 PRO 128
GLU 221 1.05 ASP 281 -0.91 ALA 129
GLU 221 1.00 ARG 282 -1.31 SER 127
GLU 221 0.78 ARG 283 -0.99 PRO 128
VAL 272 1.00 THR 284 -0.91 PRO 128
VAL 272 1.57 GLU 285 -1.07 PRO 128
VAL 272 0.91 GLU 286 -1.45 PRO 128
PRO 250 0.92 GLU 287 -0.94 PRO 128

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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.