CNRS Nantes University US2B US2B
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CA distance fluctuations for 2404111610033706944

---  normal mode 10  ---

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 210 0.51 VAL 97 -1.04 GLY 262
ASN 210 0.82 PRO 98 -1.19 GLY 262
ASN 210 1.20 SER 99 -0.95 LEU 264
ASN 210 1.03 GLN 100 -0.74 LEU 264
ASN 210 1.37 LYS 101 -0.99 LEU 289
ASN 210 1.26 THR 102 -1.20 LEU 130
ASN 210 1.30 TYR 103 -1.03 LEU 130
ASN 210 1.08 GLN 104 -1.05 ALA 129
ASN 210 1.03 GLY 105 -0.87 LEU 289
ASN 210 0.86 SER 106 -0.78 LEU 289
ASN 210 0.79 TYR 107 -0.74 ALA 129
ASN 210 0.88 GLY 108 -0.91 ALA 129
ASN 210 0.91 PHE 109 -0.88 ALA 129
ASN 210 0.91 ARG 110 -0.95 ALA 129
ASN 210 0.78 LEU 111 -0.63 PRO 128
PHE 270 0.94 GLY 112 -0.32 ALA 129
SER 227 0.83 PHE 113 -0.21 HIS 233
SER 227 1.13 LEU 114 -0.18 CYS 141
SER 227 1.49 HIS 115 -0.18 THR 102
SER 227 1.54 SER 116 -0.13 LYS 139
SER 227 1.45 SER 121 -0.27 ALA 276
SER 227 1.68 VAL 122 -0.28 THR 102
SER 227 1.61 THR 123 -0.25 THR 102
SER 227 1.67 CYS 124 -0.29 THR 102
SER 227 1.63 THR 125 -0.39 THR 102
SER 227 1.27 TYR 126 -0.54 ASN 268
SER 227 1.07 SER 127 -0.71 THR 102
SER 227 0.76 PRO 128 -0.93 ARG 110
SER 227 0.63 ALA 129 -1.05 GLN 104
SER 227 0.76 LEU 130 -1.20 THR 102
SER 227 0.77 ASN 131 -0.99 THR 102
SER 227 1.01 LYS 132 -0.77 THR 102
SER 227 1.18 MET 133 -0.62 ASN 268
SER 227 1.37 PHE 134 -0.52 THR 102
SER 227 1.42 CYS 135 -0.36 THR 102
SER 227 1.34 GLN 136 -0.31 THR 102
SER 227 1.14 LEU 137 -0.25 THR 102
GLU 224 1.13 ALA 138 -0.26 LEU 111
GLU 224 1.35 LYS 139 -0.28 LEU 111
GLU 224 1.46 THR 140 -0.30 LEU 111
SER 227 1.18 CYS 141 -0.38 LEU 111
SER 227 0.97 PRO 142 -0.21 LEU 111
THR 253 0.93 VAL 143 -0.36 LEU 111
THR 253 0.76 GLN 144 -0.26 ALA 129
ASN 210 0.71 LEU 145 -0.49 ALA 129
ASN 210 0.69 TRP 146 -0.58 ALA 129
ASN 210 0.71 VAL 147 -0.69 ALA 129
ASN 210 0.69 ASP 148 -0.67 ALA 129
ASN 210 0.62 SER 149 -0.58 ALA 129
ASN 210 0.51 THR 150 -0.48 ALA 129
ASN 210 0.54 PRO 151 -0.51 ALA 129
ASN 210 0.40 PRO 152 -0.54 PRO 98
GLY 199 0.41 PRO 153 -0.51 PRO 98
GLY 199 0.37 GLY 154 -0.59 PRO 98
ASN 210 0.43 THR 155 -0.60 PRO 98
THR 231 0.49 ARG 156 -0.58 PRO 98
THR 231 0.63 VAL 157 -0.42 ALA 129
THR 231 0.75 ARG 158 -0.41 PRO 98
THR 231 0.92 ALA 159 -0.30 LEU 289
THR 231 0.75 MET 160 -0.37 GLY 262
THR 231 0.71 ALA 161 -0.39 GLY 262
SER 227 0.65 ILE 162 -0.52 GLY 262
SER 227 0.71 TYR 163 -0.49 GLY 262
SER 227 0.72 LYS 164 -0.48 ASN 263
SER 227 0.67 GLN 165 -0.52 ASN 263
SER 227 0.53 GLU 171 -0.52 GLY 262
SER 227 0.55 VAL 172 -0.44 GLY 262
SER 227 0.65 VAL 173 -0.37 GLY 262
SER 227 0.67 ARG 174 -0.53 PHE 212
SER 227 0.73 ARG 175 -0.48 PHE 212
SER 227 0.74 CYS 176 -0.52 ARG 209
SER 227 0.68 PRO 177 -0.69 ARG 209
SER 227 0.75 HIS 178 -0.59 ARG 209
SER 227 0.78 HIS 179 -0.50 ARG 209
GLU 224 0.69 GLU 180 -0.63 ARG 209
GLU 224 0.73 ARG 181 -0.64 ARG 209
GLU 224 0.84 SER 185 -0.37 ARG 209
GLU 224 0.80 ASP 186 -0.27 ARG 209
GLU 224 0.62 GLY 187 -0.37 ARG 209
GLU 224 0.55 LEU 188 -0.39 GLY 199
GLU 224 0.62 ALA 189 -0.28 ARG 209
GLU 224 0.55 PRO 190 -0.48 ARG 209
GLU 224 0.63 PRO 191 -0.61 ARG 209
SER 227 0.58 GLN 192 -0.62 ARG 209
GLU 224 0.62 HIS 193 -0.36 PHE 212
SER 227 0.75 LEU 194 -0.28 PHE 212
GLU 224 0.75 ILE 195 -0.20 ILE 255
GLU 224 0.81 ARG 196 -0.25 LEU 111
GLU 224 0.84 VAL 197 -0.36 LEU 111
GLU 224 1.11 GLU 198 -0.30 LEU 188
GLU 224 1.11 GLY 199 -0.39 LEU 188
GLU 224 0.72 ASN 200 -0.33 LEU 111
GLU 224 0.49 LEU 201 -0.31 LEU 111
GLY 262 0.36 ARG 202 -0.29 PRO 222
GLU 224 0.46 VAL 203 -0.24 LEU 111
GLU 224 0.37 GLU 204 -0.24 PRO 222
GLU 224 0.43 TYR 205 -0.21 PRO 222
THR 231 0.42 LEU 206 -0.24 PRO 222
THR 231 0.43 ASP 207 -0.35 GLN 192
THR 256 0.87 ASP 208 -0.39 GLN 192
TYR 103 1.05 ARG 209 -0.69 PRO 177
LYS 101 1.37 ASN 210 -0.65 PRO 177
PHE 212 0.62 THR 211 -0.60 SER 261
THR 211 0.62 PHE 212 -0.61 GLN 192
THR 231 0.49 ARG 213 -0.47 SER 261
THR 231 0.50 HIS 214 -0.33 SER 260
THR 231 0.64 SER 215 -0.30 SER 260
THR 231 0.58 VAL 216 -0.22 VAL 97
THR 231 0.56 VAL 217 -0.32 PRO 98
THR 231 0.38 VAL 218 -0.35 PRO 222
GLY 199 0.49 PRO 219 -0.39 PRO 98
ASN 210 0.41 TYR 220 -0.59 PRO 222
GLY 199 0.50 GLU 221 -0.61 PRO 222
SER 116 0.54 PRO 222 -0.61 GLU 221
SER 116 0.84 PRO 223 -0.39 GLU 221
THR 140 1.46 GLU 224 -0.81 SER 227
SER 121 1.26 VAL 225 -0.44 PRO 152
ALA 276 0.71 GLY 226 -0.29 SER 106
VAL 122 1.68 SER 227 -0.81 GLU 224
SER 116 0.83 ASP 228 -0.45 ASP 148
LEU 114 0.68 CYS 229 -0.26 ASP 228
ASN 210 0.66 THR 230 -0.25 CYS 229
ALA 159 0.92 THR 231 -0.13 CYS 229
THR 231 0.75 ILE 232 -0.32 LEU 111
GLU 224 1.02 HIS 233 -0.37 LEU 111
GLU 224 0.94 TYR 234 -0.47 LEU 111
GLU 224 1.06 ASN 235 -0.36 LEU 111
SER 227 0.96 TYR 236 -0.31 ILE 255
SER 227 0.89 MET 237 -0.27 PHE 212
SER 227 0.93 CYS 238 -0.29 PHE 212
SER 227 1.02 ASN 239 -0.27 THR 102
SER 227 1.01 SER 240 -0.32 LYS 101
SER 227 0.97 SER 241 -0.28 LYS 101
SER 227 0.89 CYS 242 -0.33 ARG 209
SER 227 0.80 MET 243 -0.39 ARG 209
SER 227 0.72 GLY 244 -0.50 ASN 210
SER 227 0.77 GLY 245 -0.40 PHE 212
SER 227 0.82 MET 246 -0.31 GLY 262
SER 227 0.84 ASN 247 -0.29 GLY 262
SER 227 0.91 ARG 248 -0.30 ASN 263
SER 227 0.86 ARG 249 -0.35 GLY 262
SER 227 0.91 PRO 250 -0.40 LYS 101
SER 227 0.86 ILE 251 -0.41 LYS 101
SER 227 0.80 LEU 252 -0.42 LYS 101
VAL 143 0.93 THR 253 -0.34 THR 284
ASN 210 0.78 ILE 254 -0.43 LEU 289
ASN 210 0.92 ILE 255 -0.54 MET 133
ASN 210 1.04 THR 256 -0.58 LEU 130
ASN 210 0.84 LEU 257 -0.58 ALA 129
ARG 209 0.71 GLU 258 -0.82 PRO 98
ARG 209 0.54 ASP 259 -0.82 PRO 98
ARG 209 0.32 SER 260 -0.83 PRO 98
ARG 209 0.40 SER 261 -0.98 PRO 98
ARG 209 0.62 GLY 262 -1.19 PRO 98
ARG 209 0.83 ASN 263 -1.03 PRO 98
ARG 209 1.05 LEU 264 -0.95 SER 99
ASN 210 0.93 LEU 265 -0.71 LEU 289
ASN 210 1.10 GLY 266 -0.77 LEU 130
ASN 210 1.23 ARG 267 -0.84 LEU 130
ASN 210 1.08 ASN 268 -0.98 ASN 131
GLY 112 0.83 SER 269 -0.55 LEU 289
GLY 112 0.94 PHE 270 -0.58 THR 102
SER 227 0.95 GLU 271 -0.57 THR 102
SER 227 1.09 VAL 272 -0.47 ASP 281
SER 227 1.17 ARG 273 -0.45 THR 102
SER 227 1.19 VAL 274 -0.37 THR 102
SER 227 1.23 CYS 275 -0.37 THR 102
SER 227 1.26 ALA 276 -0.34 THR 102
SER 227 1.36 CYS 277 -0.42 THR 102
SER 227 1.51 PRO 278 -0.46 THR 102
SER 227 1.56 GLY 279 -0.47 THR 102
SER 227 1.35 ARG 280 -0.52 THR 102
SER 227 1.25 ASP 281 -0.63 THR 102
SER 227 1.32 ARG 282 -0.67 THR 102
SER 227 1.25 ARG 283 -0.66 THR 102
SER 227 1.07 THR 284 -0.76 THR 102
SER 227 1.03 GLU 285 -0.84 THR 102
SER 227 0.95 GLU 286 -0.91 THR 102
SER 227 0.91 GLU 287 -0.83 THR 102
SER 227 0.77 ASN 288 -0.93 THR 102
SER 227 0.67 LEU 289 -1.08 THR 102
SER 227 0.60 ARG 290 -0.97 THR 102

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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.