CNRS Nantes University US2B US2B
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CA distance fluctuations for 2404131437433984339

---  normal mode 9  ---

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
VAL 172 0.68 SER 96 -1.59 ASN 263
ARG 213 1.10 VAL 97 -1.60 LEU 264
ARG 213 0.77 PRO 98 -1.18 LEU 264
LEU 206 0.56 SER 99 -0.83 LEU 264
LEU 206 0.56 GLN 100 -0.88 ASN 131
LEU 206 0.50 LYS 101 -0.84 ASN 131
LEU 206 0.28 THR 102 -0.69 PHE 113
LEU 206 0.21 TYR 103 -0.66 ASN 210
ALA 129 0.23 GLN 104 -0.80 ASN 210
THR 230 0.41 GLY 105 -1.03 ASN 210
THR 230 0.46 SER 106 -1.19 ASN 210
PRO 128 0.58 TYR 107 -1.17 ASN 210
ALA 129 0.63 GLY 108 -0.88 ASN 210
PRO 128 0.63 PHE 109 -0.87 ASN 210
ASN 131 0.75 ARG 110 -0.78 ASN 200
PHE 270 0.92 LEU 111 -0.72 ASN 200
ASN 131 1.07 GLY 112 -0.65 ASN 200
SER 227 1.39 PHE 113 -0.78 SER 269
SER 227 1.58 LEU 114 -0.56 THR 102
GLY 226 1.44 SER 121 -0.37 SER 185
GLY 226 1.49 VAL 122 -0.38 SER 185
TYR 220 1.30 THR 123 -0.47 SER 185
TYR 220 1.37 CYS 124 -0.46 SER 185
GLY 226 1.44 THR 125 -0.46 LYS 101
SER 227 1.36 TYR 126 -0.60 LYS 101
SER 227 1.30 SER 127 -0.64 LYS 101
SER 227 1.19 PRO 128 -0.78 LYS 101
SER 227 1.06 ALA 129 -0.75 LYS 101
SER 227 0.99 LEU 130 -0.79 GLN 100
GLY 112 1.07 ASN 131 -0.88 GLN 100
SER 227 1.01 LYS 132 -0.66 GLN 100
SER 227 1.08 MET 133 -0.51 GLN 100
GLY 226 1.15 PHE 134 -0.41 GLN 100
GLY 226 1.12 CYS 135 -0.49 SER 185
GLY 226 1.05 GLN 136 -0.53 SER 185
TYR 220 0.90 LEU 137 -0.62 SER 185
TYR 220 0.91 ALA 138 -0.88 SER 185
TYR 220 1.15 LYS 139 -0.72 SER 185
TYR 220 1.33 THR 140 -0.67 SER 185
TYR 220 1.36 CYS 141 -0.54 SER 185
TYR 220 1.45 PRO 142 -0.47 SER 185
TYR 220 1.05 VAL 143 -0.69 ASN 200
LEU 257 1.16 GLN 144 -0.79 ASN 200
LEU 257 1.10 LEU 145 -1.09 ASN 200
PRO 128 0.90 TRP 146 -0.93 ASN 200
PRO 128 0.88 VAL 147 -1.14 VAL 218
ALA 129 0.89 ASP 148 -1.06 LEU 201
ALA 129 0.69 SER 149 -1.10 ARG 209
PRO 128 0.56 THR 150 -1.68 PRO 219
PRO 223 1.27 PRO 151 -1.32 ARG 209
GLU 224 1.16 PRO 152 -1.21 ARG 209
VAL 225 1.09 PRO 153 -1.02 ARG 209
GLU 224 1.10 GLY 154 -1.19 ARG 209
GLU 224 1.44 THR 155 -1.51 ARG 209
THR 231 1.43 ARG 156 -1.61 ARG 209
ILE 232 1.69 VAL 157 -1.27 ASP 208
ILE 232 0.59 ARG 158 -1.29 GLU 221
GLN 100 0.30 ALA 159 -1.23 GLU 221
VAL 97 0.42 MET 160 -1.03 GLU 221
VAL 97 0.44 ALA 161 -0.83 GLU 221
VAL 97 0.44 ILE 162 -0.86 GLY 262
GLY 226 0.50 TYR 163 -0.98 GLY 262
GLY 226 0.54 LYS 164 -0.94 GLY 262
GLY 226 0.55 GLN 165 -1.08 GLY 262
GLY 226 0.41 SER 166 -1.32 GLY 262
GLY 226 0.44 GLN 167 -1.45 GLY 262
GLY 226 0.44 HIS 168 -1.41 GLY 262
GLY 226 0.34 MET 169 -1.39 GLY 262
GLY 245 0.29 THR 170 -1.56 GLY 262
VAL 97 0.45 GLU 171 -1.38 GLY 262
VAL 97 1.04 VAL 172 -1.04 GLY 262
VAL 97 0.73 VAL 173 -0.82 GLY 262
VAL 97 0.72 ARG 174 -0.70 GLU 221
VAL 97 0.58 ARG 175 -0.62 GLU 221
PHE 212 0.54 CYS 176 -0.56 GLY 262
PHE 212 0.63 PRO 177 -0.54 SER 261
GLY 226 0.54 HIS 178 -0.45 GLU 221
GLY 226 0.55 HIS 179 -0.48 GLU 221
PHE 212 0.67 GLU 180 -0.56 GLU 221
PHE 212 0.59 ARG 181 -0.47 GLU 221
GLY 226 0.55 CYS 182 -0.41 GLU 221
LEU 201 0.65 SER 185 -0.88 ALA 138
LEU 201 0.88 ASP 186 -0.96 GLU 198
LEU 201 0.78 GLY 187 -0.63 GLU 221
LEU 201 0.78 LEU 188 -0.75 GLU 221
LEU 201 0.57 ALA 189 -0.82 GLU 221
ASP 207 0.72 PRO 190 -0.76 GLU 221
PHE 212 0.73 PRO 191 -0.68 GLU 221
PHE 212 0.81 GLN 192 -0.71 GLU 221
VAL 97 0.63 HIS 193 -0.80 GLU 221
VAL 97 0.51 LEU 194 -0.74 GLU 221
VAL 218 0.50 ILE 195 -0.84 GLU 221
VAL 218 0.74 ARG 196 -0.83 GLU 221
VAL 218 1.23 VAL 197 -0.80 GLU 221
VAL 218 1.04 GLU 198 -0.96 ASP 186
PRO 219 1.02 GLY 199 -0.58 ILE 232
PRO 219 0.47 ASN 200 -1.20 THR 230
ASP 186 0.88 LEU 201 -1.46 PRO 223
GLY 262 0.49 ARG 202 -1.46 PRO 222
LEU 188 0.43 VAL 203 -1.28 GLU 221
LEU 264 0.39 GLU 204 -1.14 GLU 221
VAL 97 0.49 TYR 205 -1.07 GLU 221
PRO 98 0.73 LEU 206 -1.02 GLU 221
PRO 190 0.72 ASP 207 -1.13 THR 150
PRO 190 0.46 ASP 208 -1.50 ARG 156
PRO 191 0.57 ARG 209 -1.61 ARG 156
PRO 177 0.49 ASN 210 -1.54 LEU 265
GLN 192 0.44 THR 211 -1.85 GLU 258
GLN 192 0.81 PHE 212 -1.32 GLU 258
VAL 97 1.10 ARG 213 -0.94 GLU 221
VAL 97 0.82 HIS 214 -0.97 GLU 221
PRO 98 0.56 SER 215 -1.14 GLU 221
VAL 97 0.39 VAL 216 -1.33 GLU 221
LEU 264 0.38 VAL 217 -1.58 GLU 221
VAL 197 1.23 VAL 218 -1.25 GLU 221
PRO 142 1.34 PRO 219 -1.68 THR 150
LEU 114 1.53 TYR 220 -1.15 THR 150
ASP 259 1.61 GLU 221 -1.58 VAL 217
ASP 259 1.15 PRO 222 -1.46 ARG 202
THR 155 1.29 PRO 223 -1.46 LEU 201
THR 155 1.44 GLU 224 -1.25 LEU 201
LEU 114 1.28 VAL 225 -0.79 ASP 148
VAL 122 1.49 GLY 226 -0.48 ASP 148
LEU 114 1.58 SER 227 -0.68 LEU 201
PRO 128 1.19 ASP 228 -0.84 LEU 201
PRO 151 1.02 CYS 229 -0.99 LEU 201
LEU 257 1.35 THR 230 -1.20 ASN 200
ARG 156 1.43 THR 231 -0.85 ASN 200
VAL 157 1.69 ILE 232 -0.97 ASN 200
PRO 219 1.32 HIS 233 -0.63 ASP 186
PRO 219 0.94 TYR 234 -0.62 SER 185
TYR 220 0.92 ASN 235 -0.81 SER 185
TYR 220 0.77 TYR 236 -0.64 SER 185
TYR 220 0.65 MET 237 -0.62 SER 185
GLY 226 0.68 CYS 238 -0.53 GLU 221
GLY 226 0.79 ASN 239 -0.44 GLU 221
GLY 226 0.78 SER 240 -0.53 GLY 262
GLY 226 0.76 SER 241 -0.54 GLY 262
GLY 226 0.67 CYS 242 -0.55 GLY 262
GLY 226 0.55 GLY 245 -0.70 GLY 262
GLY 226 0.61 MET 246 -0.73 GLY 262
GLY 226 0.64 ASN 247 -0.70 GLY 262
GLY 226 0.72 ARG 248 -0.67 GLY 262
GLY 226 0.66 ARG 249 -0.79 GLY 262
GLY 226 0.71 PRO 250 -0.72 GLY 262
GLY 226 0.63 ILE 251 -0.70 GLY 262
GLY 226 0.58 LEU 252 -0.62 GLY 262
GLY 226 0.50 THR 253 -0.75 GLU 221
GLY 226 0.34 ILE 254 -0.82 GLU 221
GLN 144 0.39 ILE 255 -1.01 GLU 221
THR 231 0.69 THR 256 -1.02 THR 211
THR 231 1.35 LEU 257 -1.38 ASP 208
THR 230 1.14 GLU 258 -1.85 THR 211
GLU 221 1.61 ASP 259 -1.39 ASN 210
GLU 221 1.27 SER 260 -1.24 PHE 212
GLU 221 0.84 SER 261 -1.24 THR 170
GLU 221 0.64 GLY 262 -1.56 THR 170
THR 230 0.68 ASN 263 -1.59 SER 96
THR 230 0.79 LEU 264 -1.60 VAL 97
THR 230 1.09 LEU 265 -1.54 ASN 210
THR 230 0.72 GLY 266 -1.09 ASN 210
THR 230 0.36 ARG 267 -0.78 SER 99
SER 227 0.17 ASN 268 -0.70 GLU 221
LYS 164 0.32 SER 269 -0.78 PHE 113
LEU 111 0.92 PHE 270 -0.77 GLN 100
SER 227 0.76 GLU 271 -0.65 GLN 100
GLY 226 0.85 VAL 272 -0.43 GLN 100
GLY 226 0.93 ARG 273 -0.39 GLY 262
GLY 226 0.92 VAL 274 -0.43 SER 185
GLY 226 1.00 CYS 275 -0.42 SER 185
GLY 226 1.05 ALA 276 -0.39 SER 185
GLY 226 1.19 CYS 277 -0.37 SER 185
GLY 226 1.28 PRO 278 -0.39 SER 185
GLY 226 1.45 GLY 279 -0.41 LYS 101
GLY 226 1.29 ARG 280 -0.38 LYS 101
GLY 226 1.19 ASP 281 -0.38 GLN 100
GLY 226 1.27 ARG 282 -0.48 LYS 101
GLY 226 1.32 ARG 283 -0.48 LYS 101
GLY 226 1.15 THR 284 -0.44 GLN 100
GLY 226 1.07 GLU 285 -0.52 GLN 100
GLY 226 1.17 GLU 286 -0.55 LYS 101
GLY 226 1.13 GLU 287 -0.50 LYS 101
GLY 226 0.99 ASN 288 -0.50 GLN 100
GLY 226 0.98 LEU 289 -0.58 GLN 100

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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.