CNRS Nantes University US2B US2B
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CA distance fluctuations for 240504105524328659

---  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
PRO 177 0.34 SER 96 -1.19 GLY 262
GLY 112 0.45 VAL 97 -1.06 GLY 262
ASP 208 0.57 PRO 98 -1.13 GLU 258
ASP 208 0.59 SER 99 -0.97 LEU 264
GLY 112 0.68 GLN 100 -0.82 LEU 264
LEU 206 0.45 LYS 101 -1.19 LEU 130
LEU 206 0.39 THR 102 -1.56 PRO 128
LEU 206 0.50 TYR 103 -1.46 ALA 129
LEU 206 0.34 GLN 104 -1.28 PRO 128
LEU 206 0.40 GLY 105 -1.08 ALA 129
LEU 206 0.33 SER 106 -0.90 ALA 129
GLU 258 0.19 TYR 107 -0.76 PRO 128
THR 102 0.23 GLY 108 -0.90 PRO 128
LEU 206 0.20 PHE 109 -0.91 PRO 128
TRP 146 0.44 ARG 110 -0.90 PRO 128
TRP 146 0.66 LEU 111 -0.77 VAL 143
PHE 270 1.52 GLY 112 -0.50 ASN 200
PHE 270 0.96 PHE 113 -0.60 ARG 110
THR 231 1.31 LEU 114 -0.36 TYR 103
THR 231 1.10 HIS 115 -0.55 THR 102
THR 231 0.93 SER 116 -0.57 THR 102
GLY 226 0.87 VAL 122 -0.55 THR 102
GLY 226 0.73 THR 123 -0.53 THR 102
GLY 226 0.72 CYS 124 -0.61 THR 102
GLY 226 0.84 THR 125 -0.78 THR 102
GLY 226 0.81 TYR 126 -1.01 THR 102
GLY 226 0.89 SER 127 -1.24 THR 102
SER 227 0.89 PRO 128 -1.56 THR 102
GLY 226 0.84 ALA 129 -1.46 TYR 103
PRO 250 0.94 LEU 130 -1.37 THR 102
GLY 112 0.91 ASN 131 -1.25 THR 102
GLY 112 0.79 LYS 132 -0.92 THR 102
GLY 226 0.69 MET 133 -0.85 THR 102
GLY 226 0.76 PHE 134 -0.75 THR 102
GLY 226 0.67 CYS 135 -0.58 THR 102
GLY 226 0.62 GLN 136 -0.47 THR 102
GLY 226 0.49 LEU 137 -0.36 THR 102
PRO 219 0.48 ALA 138 -0.37 SER 269
PRO 219 0.66 LYS 139 -0.40 SER 269
PRO 219 0.83 THR 140 -0.49 LEU 111
PRO 219 0.72 CYS 141 -0.56 LEU 111
VAL 272 0.82 PRO 142 -0.54 LEU 111
GLU 271 0.99 VAL 143 -0.77 LEU 111
PHE 270 1.12 GLN 144 -0.55 ASN 200
PHE 270 0.64 LEU 145 -0.90 ASN 200
LEU 111 0.66 TRP 146 -0.76 ASN 200
PHE 270 0.28 VAL 147 -0.70 ASN 200
SER 166 0.25 ASP 148 -0.61 ASN 200
LEU 114 0.24 SER 149 -0.72 ASN 210
LEU 114 0.43 THR 150 -0.96 ASN 210
LEU 114 0.37 PRO 151 -1.07 ASN 210
LEU 114 0.38 PRO 152 -1.28 ASN 210
SER 116 0.52 PRO 153 -1.48 ASN 210
HIS 233 0.55 GLY 154 -1.66 ASN 210
HIS 233 0.57 THR 155 -1.48 ASN 210
HIS 233 0.80 ARG 156 -1.50 ASN 210
HIS 233 0.77 VAL 157 -1.02 ASN 210
GLN 144 0.77 ARG 158 -0.91 THR 211
GLN 144 0.70 ALA 159 -0.65 ILE 232
GLN 144 0.65 MET 160 -0.52 ILE 232
GLY 112 0.73 ALA 161 -0.38 ILE 232
GLY 112 0.79 ILE 162 -0.48 GLY 262
GLY 112 0.84 TYR 163 -0.51 GLY 262
GLY 112 1.00 LYS 164 -0.58 GLY 262
GLY 112 0.90 GLN 165 -0.62 GLY 262
GLY 112 0.86 SER 166 -0.72 GLY 262
GLY 112 0.72 GLN 167 -0.67 GLY 262
GLY 112 0.70 HIS 168 -0.62 GLY 262
GLY 112 0.75 MET 169 -0.72 GLY 262
GLY 112 0.57 THR 170 -0.80 GLY 262
GLY 112 0.55 GLU 171 -0.60 GLY 262
GLY 112 0.53 VAL 172 -0.52 ARG 156
GLY 112 0.59 VAL 173 -0.32 ARG 156
PHE 212 0.49 ARG 174 -0.39 GLU 224
ASN 288 0.53 ARG 175 -0.39 GLU 224
ASN 288 0.66 CYS 176 -0.34 GLU 224
ASN 288 0.66 PRO 177 -0.42 GLU 224
ASN 288 0.64 HIS 178 -0.40 GLU 224
ASN 288 0.55 HIS 179 -0.42 GLU 224
PHE 212 0.67 GLU 180 -0.54 GLU 224
PHE 212 0.63 ARG 181 -0.57 GLU 224
PHE 212 0.50 CYS 182 -0.54 GLU 224
PHE 212 0.49 CYS 182 -0.54 GLU 224
PHE 212 0.50 SER 183 -0.63 GLU 224
SER 261 0.41 ASP 184 -0.60 GLU 224
SER 261 0.49 SER 185 -0.73 GLU 224
SER 261 0.61 ASP 186 -0.77 GLU 224
SER 261 0.64 GLY 187 -0.97 GLU 224
GLY 262 0.66 LEU 188 -0.99 GLU 224
GLY 262 0.52 ALA 189 -0.80 GLU 224
PHE 212 0.51 PRO 190 -0.79 GLU 224
PHE 212 0.64 PRO 191 -0.68 GLU 224
PHE 212 0.77 GLN 192 -0.59 GLU 224
PHE 212 0.47 HIS 193 -0.54 GLU 224
GLY 112 0.35 LEU 194 -0.38 GLU 224
GLN 144 0.33 ILE 195 -0.46 ILE 232
GLY 262 0.38 ARG 196 -0.51 ILE 232
VAL 218 0.50 VAL 197 -0.73 THR 231
VAL 218 0.72 GLU 198 -0.68 THR 231
SER 261 0.63 GLY 199 -1.14 THR 231
SER 261 0.67 ASN 200 -1.54 THR 231
SER 261 0.85 LEU 201 -1.33 THR 230
GLY 262 0.98 ARG 202 -1.21 PRO 223
GLY 262 0.81 VAL 203 -1.00 THR 230
GLY 262 0.85 GLU 204 -0.87 GLU 224
LEU 264 0.59 TYR 205 -0.79 GLU 224
LEU 264 0.58 LEU 206 -0.77 GLU 224
SER 99 0.58 ASP 207 -0.69 GLU 224
SER 99 0.59 ASP 208 -0.99 PRO 219
ARG 181 0.55 ARG 209 -1.17 PRO 219
ARG 181 0.62 ASN 210 -1.66 GLY 154
PRO 177 0.49 THR 211 -1.24 ARG 156
GLN 192 0.77 PHE 212 -0.82 ARG 156
PRO 98 0.43 ARG 213 -0.73 ARG 156
SER 99 0.48 HIS 214 -0.54 GLU 224
GLN 144 0.43 SER 215 -0.54 ILE 232
LEU 264 0.40 VAL 216 -0.61 ILE 232
GLY 262 0.49 VAL 217 -0.78 ASN 210
HIS 233 0.84 VAL 218 -0.99 ASN 210
ILE 232 1.09 PRO 219 -1.51 ASN 210
LEU 114 0.68 TYR 220 -1.26 ASN 210
SER 116 0.79 GLU 221 -1.22 ASN 210
HIS 115 0.80 PRO 222 -1.12 ASN 210
HIS 115 0.95 PRO 223 -1.21 ARG 202
HIS 115 0.74 GLU 224 -1.10 LEU 201
HIS 115 0.64 VAL 225 -0.77 LEU 201
ARG 283 1.10 GLY 226 -0.47 ASN 210
HIS 115 0.92 SER 227 -0.81 LEU 201
ASN 131 0.82 ASP 228 -0.93 LEU 201
LEU 114 0.87 CYS 229 -1.06 ASN 200
LEU 114 1.08 THR 230 -1.53 ASN 200
LEU 114 1.31 THR 231 -1.54 ASN 200
PRO 219 1.09 ILE 232 -0.88 ILE 255
PRO 219 0.98 HIS 233 -0.56 LEU 111
PRO 219 0.65 TYR 234 -0.46 LEU 111
PRO 219 0.51 ASN 235 -0.39 SER 269
GLY 226 0.34 TYR 236 -0.42 SER 269
ASN 288 0.37 MET 237 -0.30 GLU 224
ASN 288 0.52 CYS 238 -0.24 SER 269
ASN 288 0.52 CYS 238 -0.24 SER 269
GLU 285 0.66 ASN 239 -0.29 THR 102
GLU 285 0.81 SER 240 -0.27 THR 102
ASN 288 0.97 SER 241 -0.23 THR 102
ASN 288 0.87 CYS 242 -0.16 THR 102
ASN 288 0.97 MET 243 -0.17 GLU 224
ASN 288 0.84 GLY 244 -0.25 GLU 224
ASN 288 0.75 GLY 245 -0.24 GLU 224
ASN 288 0.74 MET 246 -0.26 GLY 262
ASN 288 0.98 ASN 247 -0.27 GLY 262
ASN 288 0.99 ARG 248 -0.30 ASN 263
LEU 130 0.90 ARG 249 -0.37 GLY 262
LEU 130 0.94 PRO 250 -0.38 ASN 263
GLY 112 0.87 ILE 251 -0.38 ASN 263
GLY 112 1.09 LEU 252 -0.42 LEU 264
GLN 144 1.03 THR 253 -0.37 PHE 134
GLN 144 0.84 ILE 254 -0.56 ILE 232
GLN 144 0.70 ILE 255 -0.88 ILE 232
LEU 206 0.49 THR 256 -0.78 PRO 128
LEU 206 0.49 THR 256 -0.77 PRO 128
GLN 144 0.50 LEU 257 -0.78 ASN 210
GLU 204 0.58 GLU 258 -1.13 PRO 98
ARG 202 0.61 ASP 259 -1.13 ASN 210
ARG 202 0.78 SER 260 -1.28 ASN 210
ARG 202 0.94 SER 261 -1.01 SER 96
ARG 202 0.98 GLY 262 -1.19 SER 96
GLU 204 0.78 ASN 263 -0.86 SER 99
GLU 204 0.71 LEU 264 -0.97 SER 99
GLU 204 0.51 LEU 265 -0.83 PRO 128
LEU 206 0.46 GLY 266 -1.06 PRO 128
LEU 206 0.50 ARG 267 -1.23 PRO 128
GLN 144 0.43 ASN 268 -1.27 PRO 128
GLY 112 1.05 SER 269 -0.82 MET 133
GLY 112 1.52 PHE 270 -0.66 LYS 101
GLY 112 1.11 GLU 271 -0.65 LYS 101
VAL 143 0.85 VAL 272 -0.52 LYS 101
GLY 226 0.70 ARG 273 -0.49 THR 102
GLY 226 0.62 VAL 274 -0.45 THR 102
GLY 226 0.71 CYS 275 -0.47 THR 102
GLY 226 0.72 ALA 276 -0.47 THR 102
GLY 226 0.85 CYS 277 -0.59 THR 102
GLY 226 0.85 CYS 277 -0.59 THR 102
GLY 226 0.86 PRO 278 -0.68 THR 102
GLY 226 1.00 GLY 279 -0.71 THR 102
GLY 226 1.05 ARG 280 -0.69 THR 102
GLY 226 0.94 ASP 281 -0.81 THR 102
GLY 226 0.99 ARG 282 -0.88 THR 102
GLY 226 1.10 ARG 283 -0.83 THR 102
GLY 226 1.00 THR 284 -0.85 THR 102
ARG 248 0.97 GLU 285 -0.86 THR 102
GLY 226 0.93 GLU 286 -1.01 THR 102
GLY 226 0.93 GLU 287 -0.88 THR 102
ARG 248 0.99 ASN 288 -0.91 TYR 103

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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.