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CA distance fluctuations for 2501100054483836345

---  normal mode 27  ---

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
HIS 233 1.00 SER 96 -1.05 PRO 177
ILE 232 1.13 VAL 97 -1.50 PRO 177
ILE 232 1.18 PRO 98 -1.78 ASN 210
ILE 232 1.43 SER 99 -1.41 ARG 209
ILE 232 1.69 GLN 100 -1.15 ASN 210
ILE 232 1.55 LYS 101 -0.92 ASN 210
THR 231 1.53 THR 102 -0.81 SER 166
PRO 222 1.61 TYR 103 -0.70 PRO 152
PRO 222 1.60 GLN 104 -0.90 ARG 174
PRO 222 1.70 GLY 105 -1.09 PRO 152
GLU 224 1.37 SER 106 -0.62 ALA 129
LEU 265 1.87 TYR 107 -0.82 PRO 152
PRO 223 1.26 GLY 108 -0.93 ARG 174
PRO 223 1.14 PHE 109 -1.79 LEU 257
THR 102 0.57 ARG 110 -1.80 ARG 158
THR 102 0.56 LEU 111 -1.76 SER 215
THR 102 0.61 GLY 112 -1.61 ILE 195
LYS 101 0.77 PHE 113 -1.74 ILE 195
GLY 199 0.88 LEU 114 -0.72 ILE 195
THR 150 0.41 VAL 122 -0.57 ILE 195
THR 150 0.45 THR 123 -0.76 PHE 113
LYS 139 0.64 CYS 124 -0.69 PHE 113
LYS 139 0.68 THR 125 -0.68 ASP 148
THR 140 0.89 TYR 126 -0.79 ASP 148
ARG 282 0.94 SER 127 -0.95 ASP 148
GLU 286 1.13 PRO 128 -1.21 ASP 148
GLU 286 1.34 ALA 129 -1.03 ASP 148
CYS 141 1.05 LEU 130 -0.84 ASP 148
CYS 141 1.31 ASN 131 -0.89 ASP 148
CYS 141 1.27 LYS 132 -0.73 ASP 148
LYS 139 1.17 MET 133 -0.70 ASP 148
LYS 139 1.18 MET 133 -0.70 ASP 148
LYS 139 0.71 PHE 134 -0.65 ASP 148
ASP 186 0.48 CYS 135 -0.86 PHE 113
PRO 191 0.48 GLN 136 -0.87 PHE 113
PRO 191 0.66 LEU 137 -0.78 ARG 213
VAL 272 1.01 ALA 138 -0.53 LEU 111
VAL 272 1.20 LYS 139 -0.44 HIS 193
SER 269 1.60 THR 140 -0.47 HIS 193
PHE 270 1.72 CYS 141 -0.52 HIS 193
PHE 270 1.75 CYS 141 -0.52 HIS 193
PHE 270 1.47 PRO 142 -0.66 HIS 193
LYS 101 1.54 VAL 143 -1.43 HIS 193
THR 102 1.22 GLN 144 -1.41 VAL 203
THR 102 1.19 LEU 145 -1.65 VAL 203
THR 102 0.59 TRP 146 -1.70 VAL 217
PRO 223 0.95 VAL 147 -1.70 ARG 156
PRO 223 1.02 ASP 148 -1.21 PRO 128
GLU 224 1.65 SER 149 -0.69 ALA 129
ASN 200 1.46 THR 150 -0.24 ASP 228
GLU 224 1.36 PRO 151 -1.55 ASP 228
VAL 225 1.45 PRO 152 -1.09 GLY 105
GLY 226 1.32 PRO 153 -0.55 GLY 105
GLY 187 0.86 GLY 154 -1.24 ASP 228
GLU 224 1.00 THR 155 -1.51 VAL 147
GLY 187 0.86 ARG 156 -1.70 VAL 147
LEU 188 1.02 VAL 157 -1.40 TRP 146
LEU 188 1.05 ARG 158 -1.80 ARG 110
LEU 188 1.29 ALA 159 -1.49 GLY 112
THR 170 1.24 MET 160 -1.31 ARG 175
VAL 197 1.30 ALA 161 -1.25 MET 243
TYR 234 1.24 ILE 162 -0.99 MET 243
TYR 234 1.14 TYR 163 -0.82 ASN 210
TYR 234 1.18 LYS 164 -0.72 ASN 210
TYR 234 0.95 GLN 165 -0.71 ASN 268
TYR 234 0.94 SER 166 -0.81 THR 102
TYR 234 0.94 SER 166 -0.81 THR 102
HIS 193 0.89 GLN 167 -0.62 THR 102
HIS 193 1.06 HIS 168 -0.56 GLY 244
TYR 234 1.06 MET 169 -0.85 ASN 210
HIS 214 1.38 THR 170 -0.70 HIS 178
HIS 214 1.31 GLU 171 -0.92 GLY 245
ILE 195 1.51 VAL 172 -1.15 ASN 210
ILE 195 1.70 VAL 173 -1.37 THR 211
MET 243 0.98 ARG 174 -1.59 GLY 262
PRO 191 0.79 ARG 175 -1.49 ASP 208
PRO 191 0.36 CYS 176 -1.70 PRO 98
ALA 276 0.38 PRO 177 -1.53 PRO 98
ALA 276 0.48 HIS 178 -1.40 THR 211
PRO 191 0.66 HIS 179 -1.50 ARG 213
PRO 190 0.17 GLU 180 -1.54 PHE 212
THR 150 0.19 ARG 181 -1.55 PHE 212
THR 150 0.71 SER 185 -1.01 LEU 111
THR 150 1.15 ASP 186 -0.45 LEU 111
THR 150 1.35 GLY 187 -0.48 ARG 181
VAL 216 1.45 LEU 188 -0.48 GLY 199
VAL 173 1.47 ALA 189 -0.99 LEU 111
VAL 172 0.81 PRO 190 -1.48 GLY 262
CYS 238 1.05 PRO 191 -1.26 GLY 262
ARG 249 0.54 GLN 192 -1.66 GLY 262
VAL 172 1.15 HIS 193 -1.62 ARG 196
PRO 191 0.96 LEU 194 -1.59 GLY 112
VAL 173 1.70 ILE 195 -1.74 PHE 113
VAL 173 1.22 ARG 196 -1.62 HIS 193
THR 253 1.45 VAL 197 -1.17 VAL 143
SER 269 1.53 GLU 198 -0.68 HIS 193
ASN 268 1.73 GLY 199 -0.64 ALA 189
THR 150 1.46 ASN 200 -0.72 ALA 189
THR 150 1.43 LEU 201 -0.81 ALA 189
GLY 187 1.29 ARG 202 -1.37 LEU 145
GLY 187 1.20 VAL 203 -1.65 LEU 145
LEU 188 0.88 GLU 204 -1.61 LEU 145
VAL 172 0.94 TYR 205 -1.62 LEU 111
THR 170 0.90 LEU 206 -1.79 GLY 262
THR 170 0.86 ASP 207 -1.46 LEU 111
LEU 188 0.51 ASP 208 -1.52 CYS 176
LEU 188 0.41 ARG 209 -1.48 LEU 264
LEU 188 0.34 ASN 210 -1.78 PRO 98
PRO 222 0.38 THR 211 -1.61 CYS 176
THR 170 0.71 PHE 212 -1.55 ARG 181
THR 170 0.95 ARG 213 -1.53 GLU 180
THR 170 1.38 HIS 214 -1.52 LEU 111
THR 170 1.23 SER 215 -1.76 LEU 111
LEU 188 1.45 VAL 216 -1.75 LEU 111
LEU 188 1.13 VAL 217 -1.70 TRP 146
GLY 187 1.13 VAL 218 -1.56 TRP 146
GLY 187 1.16 PRO 219 -1.43 TRP 146
ASN 200 1.16 TYR 220 -1.38 CYS 229
ASN 268 1.40 GLU 221 -0.80 ARG 202
GLY 105 1.70 PRO 222 -0.62 ARG 202
LEU 265 1.50 PRO 223 -0.77 HIS 193
SER 149 1.65 GLU 224 -0.65 PRO 142
PRO 152 1.45 VAL 225 -0.55 VAL 122
PRO 153 1.32 GLY 226 -0.75 ALA 129
PRO 153 0.89 SER 227 -0.75 PRO 128
GLY 199 0.66 ASP 228 -1.55 PRO 151
THR 102 0.82 CYS 229 -1.46 VAL 218
THR 102 1.29 THR 230 -1.32 ARG 202
ASN 268 1.57 THR 231 -0.94 ARG 202
GLN 100 1.69 ILE 232 -0.71 ASN 200
ILE 254 1.58 HIS 233 -0.45 HIS 193
LEU 252 1.60 TYR 234 -0.86 VAL 143
LEU 252 1.48 ASN 235 -0.80 VAL 143
ILE 251 1.15 TYR 236 -1.21 PHE 113
PRO 191 0.85 MET 237 -1.07 LEU 111
PRO 191 1.05 CYS 238 -1.31 ARG 213
PRO 191 1.04 CYS 238 -1.33 ARG 213
PRO 191 0.74 ASN 239 -1.09 ARG 213
PRO 191 0.70 SER 240 -1.01 THR 211
LEU 130 0.56 SER 241 -1.19 THR 211
ARG 174 0.53 CYS 242 -1.58 THR 211
ARG 174 0.98 MET 243 -1.35 THR 211
ARG 174 0.95 GLY 244 -1.12 THR 211
ARG 174 0.89 GLY 245 -1.23 THR 211
ARG 174 0.66 MET 246 -0.89 THR 211
GLN 165 0.79 ASN 247 -0.63 THR 211
ARG 174 0.64 ARG 248 -0.81 THR 211
TYR 236 0.94 ARG 249 -0.64 THR 211
TYR 236 1.12 PRO 250 -0.58 ASN 210
ASN 235 1.36 ILE 251 -0.80 MET 243
TYR 234 1.60 LEU 252 -0.84 MET 243
TYR 234 1.55 THR 253 -0.82 MET 243
HIS 233 1.58 ILE 254 -0.95 ARG 175
HIS 233 1.58 ILE 254 -0.95 ARG 175
ASN 200 1.36 ILE 255 -1.08 ARG 110
ASN 200 1.14 THR 256 -1.21 ARG 110
ASN 200 1.14 THR 256 -1.21 PHE 109
ASN 200 1.25 LEU 257 -1.79 PHE 109
GLU 224 0.97 GLU 258 -1.26 ARG 174
PRO 151 1.32 ASP 259 -1.25 ARG 174
GLU 224 0.81 SER 260 -1.23 TRP 146
SER 106 0.86 SER 261 -1.46 ARG 174
SER 106 0.81 GLY 262 -1.79 LEU 206
SER 106 1.05 ASN 263 -1.56 ARG 174
PRO 222 1.36 LEU 264 -1.48 ARG 209
TYR 107 1.87 LEU 265 -1.05 ARG 174
PRO 222 1.45 GLY 266 -0.94 ARG 174
GLY 199 1.42 ARG 267 -0.93 ARG 174
GLY 199 1.73 ASN 268 -0.75 SER 166
THR 140 1.60 SER 269 -0.74 ASN 210
CYS 141 1.75 PHE 270 -0.72 GLY 108
CYS 141 1.49 GLU 271 -0.61 ASP 148
ASN 235 1.41 VAL 272 -0.61 THR 211
ASN 235 1.41 VAL 272 -0.61 THR 211
ASN 235 0.87 ARG 273 -0.71 THR 211
PRO 191 0.53 VAL 274 -0.88 THR 211
PRO 191 0.53 CYS 275 -0.81 THR 211
HIS 178 0.48 ALA 276 -0.75 THR 211
HIS 178 0.40 CYS 277 -0.66 THR 211
HIS 178 0.41 CYS 277 -0.66 THR 211
SER 127 0.41 PRO 278 -0.64 THR 211
SER 127 0.40 GLY 279 -0.55 THR 211
ALA 129 0.53 ARG 280 -0.57 THR 211
ALA 129 0.69 ASP 281 -0.60 THR 211
SER 127 0.94 ARG 282 -0.54 ASP 148
ALA 129 0.76 ARG 283 -0.48 THR 211
ALA 129 0.95 THR 284 -0.50 THR 211
ALA 129 1.30 GLU 285 -0.49 THR 211
ALA 129 1.34 GLU 286 -0.45 ASP 148
ALA 129 1.07 GLU 287 -0.41 ASN 210

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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.