CNRS Nantes University US2B US2B
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CA distance fluctuations for 25030919391653391

---  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
PRO 177 1.05 SER 96 -1.00 HIS 233
PRO 177 1.50 VAL 97 -1.13 ILE 232
ASN 210 1.78 PRO 98 -1.18 ILE 232
ARG 209 1.41 SER 99 -1.43 ILE 232
ASN 210 1.15 GLN 100 -1.69 ILE 232
ASN 210 0.92 LYS 101 -1.55 ILE 232
SER 166 0.81 THR 102 -1.53 THR 231
PRO 152 0.70 TYR 103 -1.61 PRO 222
ARG 174 0.90 GLN 104 -1.60 PRO 222
PRO 152 1.09 GLY 105 -1.70 PRO 222
ALA 129 0.62 SER 106 -1.37 GLU 224
PRO 152 0.82 TYR 107 -1.87 LEU 265
ARG 174 0.93 GLY 108 -1.26 PRO 223
LEU 257 1.79 PHE 109 -1.14 PRO 223
ARG 158 1.80 ARG 110 -0.57 THR 102
SER 215 1.76 LEU 111 -0.56 THR 102
ILE 195 1.61 GLY 112 -0.61 THR 102
ILE 195 1.74 PHE 113 -0.77 LYS 101
ILE 195 0.72 LEU 114 -0.88 GLY 199
ILE 195 0.57 VAL 122 -0.41 THR 150
PHE 113 0.76 THR 123 -0.45 THR 150
PHE 113 0.69 CYS 124 -0.64 LYS 139
ASP 148 0.68 THR 125 -0.68 LYS 139
ASP 148 0.79 TYR 126 -0.89 THR 140
ASP 148 0.95 SER 127 -0.94 ARG 282
ASP 148 1.21 PRO 128 -1.13 GLU 286
ASP 148 1.03 ALA 129 -1.34 GLU 286
ASP 148 0.84 LEU 130 -1.05 CYS 141
ASP 148 0.89 ASN 131 -1.31 CYS 141
ASP 148 0.73 LYS 132 -1.27 CYS 141
ASP 148 0.70 MET 133 -1.17 LYS 139
ASP 148 0.70 MET 133 -1.18 LYS 139
ASP 148 0.65 PHE 134 -0.71 LYS 139
PHE 113 0.86 CYS 135 -0.48 ASP 186
PHE 113 0.87 GLN 136 -0.48 PRO 191
ARG 213 0.78 LEU 137 -0.66 PRO 191
LEU 111 0.53 ALA 138 -1.01 VAL 272
HIS 193 0.44 LYS 139 -1.20 VAL 272
HIS 193 0.47 THR 140 -1.60 SER 269
HIS 193 0.52 CYS 141 -1.72 PHE 270
HIS 193 0.52 CYS 141 -1.75 PHE 270
HIS 193 0.66 PRO 142 -1.47 PHE 270
HIS 193 1.43 VAL 143 -1.54 LYS 101
VAL 203 1.41 GLN 144 -1.22 THR 102
VAL 203 1.65 LEU 145 -1.19 THR 102
VAL 217 1.70 TRP 146 -0.59 THR 102
ARG 156 1.70 VAL 147 -0.95 PRO 223
PRO 128 1.21 ASP 148 -1.02 PRO 223
ALA 129 0.69 SER 149 -1.65 GLU 224
ASP 228 0.24 THR 150 -1.46 ASN 200
ASP 228 1.55 PRO 151 -1.36 GLU 224
GLY 105 1.09 PRO 152 -1.45 VAL 225
GLY 105 0.55 PRO 153 -1.32 GLY 226
ASP 228 1.24 GLY 154 -0.86 GLY 187
VAL 147 1.51 THR 155 -1.00 GLU 224
VAL 147 1.70 ARG 156 -0.86 GLY 187
TRP 146 1.40 VAL 157 -1.02 LEU 188
ARG 110 1.80 ARG 158 -1.05 LEU 188
GLY 112 1.49 ALA 159 -1.29 LEU 188
ARG 175 1.31 MET 160 -1.24 THR 170
MET 243 1.25 ALA 161 -1.30 VAL 197
MET 243 0.99 ILE 162 -1.24 TYR 234
ASN 210 0.82 TYR 163 -1.14 TYR 234
ASN 210 0.72 LYS 164 -1.18 TYR 234
ASN 268 0.71 GLN 165 -0.95 TYR 234
THR 102 0.81 SER 166 -0.94 TYR 234
THR 102 0.81 SER 166 -0.94 TYR 234
THR 102 0.62 GLN 167 -0.89 HIS 193
GLY 244 0.56 HIS 168 -1.06 HIS 193
ASN 210 0.85 MET 169 -1.06 TYR 234
HIS 178 0.70 THR 170 -1.38 HIS 214
GLY 245 0.92 GLU 171 -1.31 HIS 214
ASN 210 1.15 VAL 172 -1.51 ILE 195
THR 211 1.37 VAL 173 -1.70 ILE 195
GLY 262 1.59 ARG 174 -0.98 MET 243
ASP 208 1.49 ARG 175 -0.79 PRO 191
PRO 98 1.70 CYS 176 -0.36 PRO 191
PRO 98 1.53 PRO 177 -0.38 ALA 276
THR 211 1.40 HIS 178 -0.48 ALA 276
ARG 213 1.50 HIS 179 -0.66 PRO 191
PHE 212 1.54 GLU 180 -0.17 PRO 190
PHE 212 1.55 ARG 181 -0.19 THR 150
LEU 111 1.01 SER 185 -0.71 THR 150
LEU 111 0.45 ASP 186 -1.15 THR 150
ARG 181 0.48 GLY 187 -1.35 THR 150
GLY 199 0.48 LEU 188 -1.45 VAL 216
LEU 111 0.99 ALA 189 -1.47 VAL 173
GLY 262 1.48 PRO 190 -0.81 VAL 172
GLY 262 1.26 PRO 191 -1.05 CYS 238
GLY 262 1.66 GLN 192 -0.54 ARG 249
ARG 196 1.62 HIS 193 -1.15 VAL 172
GLY 112 1.59 LEU 194 -0.96 PRO 191
PHE 113 1.74 ILE 195 -1.70 VAL 173
HIS 193 1.62 ARG 196 -1.22 VAL 173
VAL 143 1.17 VAL 197 -1.45 THR 253
HIS 193 0.68 GLU 198 -1.53 SER 269
ALA 189 0.64 GLY 199 -1.73 ASN 268
ALA 189 0.72 ASN 200 -1.46 THR 150
ALA 189 0.81 LEU 201 -1.43 THR 150
LEU 145 1.37 ARG 202 -1.29 GLY 187
LEU 145 1.65 VAL 203 -1.20 GLY 187
LEU 145 1.61 GLU 204 -0.88 LEU 188
LEU 111 1.62 TYR 205 -0.94 VAL 172
GLY 262 1.79 LEU 206 -0.90 THR 170
LEU 111 1.46 ASP 207 -0.86 THR 170
CYS 176 1.52 ASP 208 -0.51 LEU 188
LEU 264 1.48 ARG 209 -0.41 LEU 188
PRO 98 1.78 ASN 210 -0.34 LEU 188
CYS 176 1.61 THR 211 -0.38 PRO 222
ARG 181 1.55 PHE 212 -0.71 THR 170
GLU 180 1.53 ARG 213 -0.95 THR 170
LEU 111 1.52 HIS 214 -1.38 THR 170
LEU 111 1.76 SER 215 -1.23 THR 170
LEU 111 1.75 VAL 216 -1.45 LEU 188
TRP 146 1.70 VAL 217 -1.13 LEU 188
TRP 146 1.56 VAL 218 -1.13 GLY 187
TRP 146 1.43 PRO 219 -1.16 GLY 187
CYS 229 1.38 TYR 220 -1.16 ASN 200
ARG 202 0.80 GLU 221 -1.40 ASN 268
ARG 202 0.62 PRO 222 -1.70 GLY 105
HIS 193 0.77 PRO 223 -1.50 LEU 265
PRO 142 0.65 GLU 224 -1.65 SER 149
VAL 122 0.55 VAL 225 -1.45 PRO 152
ALA 129 0.75 GLY 226 -1.32 PRO 153
PRO 128 0.75 SER 227 -0.89 PRO 153
PRO 151 1.55 ASP 228 -0.66 GLY 199
VAL 218 1.46 CYS 229 -0.82 THR 102
ARG 202 1.32 THR 230 -1.29 THR 102
ARG 202 0.94 THR 231 -1.57 ASN 268
ASN 200 0.71 ILE 232 -1.69 GLN 100
HIS 193 0.45 HIS 233 -1.58 ILE 254
VAL 143 0.86 TYR 234 -1.60 LEU 252
VAL 143 0.80 ASN 235 -1.48 LEU 252
PHE 113 1.21 TYR 236 -1.15 ILE 251
LEU 111 1.07 MET 237 -0.85 PRO 191
ARG 213 1.31 CYS 238 -1.05 PRO 191
ARG 213 1.33 CYS 238 -1.04 PRO 191
ARG 213 1.09 ASN 239 -0.74 PRO 191
THR 211 1.01 SER 240 -0.70 PRO 191
THR 211 1.19 SER 241 -0.56 LEU 130
THR 211 1.58 CYS 242 -0.53 ARG 174
THR 211 1.35 MET 243 -0.98 ARG 174
THR 211 1.12 GLY 244 -0.95 ARG 174
THR 211 1.23 GLY 245 -0.89 ARG 174
THR 211 0.89 MET 246 -0.66 ARG 174
THR 211 0.63 ASN 247 -0.79 GLN 165
THR 211 0.81 ARG 248 -0.64 ARG 174
THR 211 0.64 ARG 249 -0.94 TYR 236
ASN 210 0.58 PRO 250 -1.12 TYR 236
MET 243 0.80 ILE 251 -1.36 ASN 235
MET 243 0.84 LEU 252 -1.60 TYR 234
MET 243 0.82 THR 253 -1.55 TYR 234
ARG 175 0.95 ILE 254 -1.58 HIS 233
ARG 175 0.95 ILE 254 -1.58 HIS 233
ARG 110 1.08 ILE 255 -1.36 ASN 200
ARG 110 1.21 THR 256 -1.14 ASN 200
PHE 109 1.21 THR 256 -1.14 ASN 200
PHE 109 1.79 LEU 257 -1.25 ASN 200
ARG 174 1.26 GLU 258 -0.97 GLU 224
ARG 174 1.25 ASP 259 -1.32 PRO 151
TRP 146 1.23 SER 260 -0.81 GLU 224
ARG 174 1.46 SER 261 -0.86 SER 106
LEU 206 1.79 GLY 262 -0.81 SER 106
ARG 174 1.56 ASN 263 -1.05 SER 106
ARG 209 1.48 LEU 264 -1.36 PRO 222
ARG 174 1.05 LEU 265 -1.87 TYR 107
ARG 174 0.94 GLY 266 -1.45 PRO 222
ARG 174 0.93 ARG 267 -1.42 GLY 199
SER 166 0.75 ASN 268 -1.73 GLY 199
ASN 210 0.74 SER 269 -1.60 THR 140
GLY 108 0.72 PHE 270 -1.75 CYS 141
ASP 148 0.61 GLU 271 -1.49 CYS 141
THR 211 0.61 VAL 272 -1.41 ASN 235
THR 211 0.61 VAL 272 -1.41 ASN 235
THR 211 0.71 ARG 273 -0.87 ASN 235
THR 211 0.88 VAL 274 -0.53 PRO 191
THR 211 0.81 CYS 275 -0.53 PRO 191
THR 211 0.75 ALA 276 -0.48 HIS 178
THR 211 0.66 CYS 277 -0.40 HIS 178
THR 211 0.66 CYS 277 -0.41 HIS 178
THR 211 0.64 PRO 278 -0.41 SER 127
THR 211 0.55 GLY 279 -0.40 SER 127
THR 211 0.57 ARG 280 -0.53 ALA 129
THR 211 0.60 ASP 281 -0.69 ALA 129
ASP 148 0.54 ARG 282 -0.94 SER 127
THR 211 0.48 ARG 283 -0.75 ALA 129
THR 211 0.50 THR 284 -0.95 ALA 129
THR 211 0.49 GLU 285 -1.30 ALA 129
ASP 148 0.45 GLU 286 -1.34 ALA 129
ASN 210 0.41 GLU 287 -1.07 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 8th, 2025.