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CA distance fluctuations for 240415152934446788

---  normal mode 11  ---

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
LEU 310 0.06 MET 1 -0.20 GLU 61
LYS 309 0.05 GLY 2 -0.29 GLU 61
CYS 313 0.10 GLY 3 -0.30 GLU 61
CYS 313 0.11 GLN 4 -0.36 GLU 61
CYS 313 0.08 VAL 5 -0.45 GLU 61
VAL 86 0.08 SER 6 -0.38 GLU 61
CYS 313 0.08 ALA 7 -0.37 LYS 55
GLU 260 0.09 SER 8 -0.49 LYS 55
CYS 313 0.10 ASN 9 -0.52 LYS 55
CYS 313 0.09 SER 10 -0.54 LYS 55
CYS 313 0.09 PHE 11 -0.42 LYS 55
CYS 313 0.14 SER 12 -0.39 LYS 55
CYS 313 0.15 ARG 13 -0.41 LYS 55
CYS 313 0.13 LEU 14 -0.37 LYS 55
CYS 313 0.15 HIS 15 -0.32 LYS 55
CYS 313 0.21 CYS 16 -0.28 LYS 55
CYS 313 0.20 ARG 17 -0.26 LYS 55
CYS 313 0.22 ASN 18 -0.22 LYS 55
CYS 313 0.21 ALA 19 -0.19 LYS 55
CYS 313 0.22 ASN 20 -0.16 LYS 55
CYS 313 0.18 GLU 21 -0.14 LYS 55
CYS 313 0.16 ASP 22 -0.11 LYS 55
LEU 310 0.17 TRP 23 -0.11 LYS 55
LEU 310 0.12 MET 24 -0.09 LYS 55
LEU 310 0.12 SER 25 -0.09 LYS 55
CYS 313 0.19 ALA 26 -0.10 LYS 55
LEU 310 0.14 LEU 27 -0.10 LYS 55
LEU 311 0.13 CYS 28 -0.10 ALA 305
LEU 311 0.05 PRO 29 -0.08 LYS 55
ALA 72 0.05 ARG 30 -0.09 CYS 313
ALA 72 0.05 LEU 31 -0.11 CYS 313
ALA 72 0.06 TRP 32 -0.08 CYS 313
ALA 72 0.07 ASP 33 -0.19 CYS 313
ALA 72 0.07 VAL 34 -0.24 CYS 313
ALA 72 0.08 PRO 35 -0.25 CYS 313
ARG 182 0.08 LEU 36 -0.18 CYS 313
ARG 182 0.12 HIS 37 -0.24 CYS 313
ARG 182 0.10 HIS 38 -0.31 CYS 313
ARG 182 0.09 LEU 39 -0.21 CYS 313
ARG 182 0.09 SER 40 -0.15 CYS 313
PRO 216 0.08 ILE 41 -0.11 LYS 55
LYS 309 0.08 PRO 42 -0.13 LYS 55
GLU 203 0.08 GLY 43 -0.11 LYS 55
GLU 203 0.07 SER 44 -0.12 SER 59
ASP 292 0.10 HIS 45 -0.10 SER 59
MET 262 0.09 ASP 46 -0.09 SER 59
ALA 72 0.06 THR 47 -0.11 GLU 61
SER 85 0.06 MET 48 -0.14 THR 126
VAL 86 0.07 THR 49 -0.16 GLU 61
SER 6 0.07 TYR 50 -0.24 GLU 61
LYS 83 0.03 CYS 51 -0.27 THR 126
ALA 128 0.06 LEU 52 -0.29 SER 59
ALA 108 0.09 ASN 53 -0.39 SER 8
HIS 122 0.09 LYS 54 -0.38 SER 10
ALA 108 0.11 LYS 55 -0.54 SER 10
TYR 125 0.15 SER 56 -0.40 SER 10
LEU 159 0.15 PRO 57 -0.34 SER 10
LEU 159 0.18 ILE 58 -0.28 SER 10
SER 160 0.16 SER 59 -0.37 VAL 5
SER 160 0.20 HIS 60 -0.36 VAL 5
GLU 112 0.21 GLU 61 -0.45 VAL 5
GLU 112 0.27 GLU 62 -0.37 VAL 5
GLU 112 0.25 SER 63 -0.31 VAL 5
SER 160 0.32 ARG 64 -0.25 VAL 5
LEU 159 0.31 LEU 65 -0.22 VAL 5
SER 160 0.24 LEU 66 -0.27 VAL 5
SER 160 0.29 GLN 67 -0.26 VAL 5
LEU 159 0.34 LEU 68 -0.19 VAL 5
LEU 159 0.30 LEU 69 -0.18 VAL 5
LEU 159 0.26 ASN 70 -0.21 VAL 5
GLY 158 0.34 LYS 71 -0.20 ASN 70
GLU 157 0.35 ALA 72 -0.12 VAL 5
GLU 157 0.28 LEU 73 -0.12 ASN 9
GLU 157 0.24 PRO 74 -0.14 SER 10
LEU 159 0.21 CYS 75 -0.21 SER 10
LEU 159 0.18 ILE 76 -0.16 SER 10
GLU 157 0.20 THR 77 -0.10 SER 10
LEU 159 0.19 ARG 78 -0.17 SER 10
LEU 159 0.15 PRO 79 -0.19 SER 10
ASN 155 0.15 VAL 80 -0.13 THR 228
ASN 155 0.18 VAL 81 -0.08 CYS 313
HIS 122 0.14 LEU 82 -0.13 THR 263
ASN 155 0.13 LYS 83 -0.17 PRO 57
ASN 155 0.16 TRP 84 -0.14 LEU 254
ASN 155 0.15 SER 85 -0.11 SER 59
ASN 155 0.09 VAL 86 -0.17 SER 59
MET 262 0.12 THR 87 -0.18 SER 59
ALA 89 0.07 GLN 88 -0.21 SER 59
GLN 88 0.07 ALA 89 -0.29 LYS 55
GLN 4 0.07 LEU 90 -0.24 GLU 61
LYS 309 0.06 ASP 91 -0.22 GLU 61
LYS 309 0.07 VAL 92 -0.16 GLU 61
LYS 309 0.08 THR 93 -0.15 GLU 61
CYS 313 0.10 GLU 94 -0.19 GLU 61
LYS 309 0.09 GLN 95 -0.16 GLU 61
LYS 309 0.10 LEU 96 -0.13 GLU 61
CYS 313 0.13 ASP 97 -0.15 GLU 61
CYS 313 0.13 ALA 98 -0.17 LYS 55
LYS 309 0.13 GLY 99 -0.14 LYS 55
LYS 309 0.10 VAL 100 -0.12 LYS 55
LYS 309 0.09 ARG 101 -0.09 LYS 55
ALA 72 0.09 TYR 102 -0.07 LYS 55
ALA 72 0.09 LEU 103 -0.07 SER 59
ALA 72 0.12 ASP 104 -0.08 CYS 313
ALA 72 0.13 LEU 105 -0.06 CYS 313
ALA 72 0.17 ARG 106 -0.07 CYS 313
ALA 72 0.18 ILE 107 -0.09 GLY 158
LEU 69 0.17 ALA 108 -0.13 GLY 158
LEU 159 0.26 HIS 109 -0.12 VAL 5
LEU 159 0.41 MET 110 -0.17 VAL 5
LEU 65 0.28 LEU 111 -0.18 GLY 158
GLU 62 0.27 GLU 112 -0.15 VAL 5
GLU 62 0.23 GLY 113 -0.14 VAL 5
GLU 62 0.21 SER 114 -0.16 VAL 5
GLU 62 0.18 GLU 115 -0.18 VAL 5
GLU 62 0.15 LYS 116 -0.17 VAL 5
LEU 65 0.14 ASN 117 -0.17 VAL 5
LEU 65 0.14 LEU 118 -0.14 VAL 5
SER 56 0.11 HIS 119 -0.14 VAL 5
ALA 72 0.10 PHE 120 -0.09 VAL 5
SER 56 0.10 VAL 121 -0.07 GLY 158
MET 123 0.20 HIS 122 -0.06 GLY 158
HIS 122 0.20 MET 123 -0.08 VAL 5
ALA 108 0.15 VAL 124 -0.12 VAL 5
ALA 108 0.15 TYR 125 -0.23 VAL 5
SER 56 0.14 THR 126 -0.30 VAL 5
SER 56 0.10 THR 127 -0.25 VAL 5
SER 56 0.07 ALA 128 -0.16 VAL 5
SER 56 0.08 LEU 129 -0.17 VAL 5
ALA 72 0.09 VAL 130 -0.13 GLY 3
ALA 72 0.08 GLU 131 -0.14 GLY 3
LEU 310 0.05 ASP 132 -0.19 GLY 3
THR 135 0.06 THR 133 -0.14 GLY 3
ALA 72 0.08 LEU 134 -0.11 GLY 3
LEU 310 0.07 THR 135 -0.13 ARG 209
LEU 310 0.07 GLU 136 -0.12 GLY 3
LEU 310 0.07 ILE 137 -0.10 THR 93
LEU 310 0.07 SER 138 -0.11 ARG 209
LEU 310 0.08 GLU 139 -0.12 ARG 209
LEU 310 0.09 TRP 140 -0.09 GLU 61
LEU 310 0.08 LEU 141 -0.08 ARG 209
LEU 310 0.08 GLU 142 -0.10 ARG 209
CYS 313 0.11 ARG 143 -0.09 ASN 18
LEU 310 0.11 HIS 144 -0.08 ASN 18
LEU 310 0.08 PRO 145 -0.08 GLY 195
LEU 310 0.08 ARG 146 -0.08 ASN 20
LEU 310 0.09 GLU 147 -0.08 LYS 55
ALA 72 0.08 VAL 148 -0.07 LYS 55
ALA 72 0.08 VAL 149 -0.06 LYS 55
ALA 72 0.11 ILE 150 -0.08 CYS 313
ALA 72 0.12 LEU 151 -0.06 CYS 313
ALA 72 0.15 ALA 152 -0.09 CYS 313
ALA 72 0.18 CYS 153 -0.08 CYS 313
ALA 72 0.23 ARG 154 -0.10 CYS 313
ALA 72 0.29 ASN 155 -0.09 CYS 313
ALA 72 0.32 PHE 156 -0.09 CYS 313
ALA 72 0.35 GLU 157 -0.13 LEU 159
ALA 72 0.35 GLY 158 -0.18 LEU 111
MET 110 0.41 LEU 159 -0.13 GLU 157
MET 110 0.38 SER 160 -0.09 VAL 5
MET 110 0.33 GLU 161 -0.08 VAL 5
MET 110 0.25 ASP 162 -0.11 VAL 5
MET 110 0.26 LEU 163 -0.12 VAL 5
MET 110 0.25 HIS 164 -0.09 VAL 5
MET 110 0.23 GLU 165 -0.10 GLU 131
MET 110 0.18 TYR 166 -0.13 GLU 131
MET 110 0.19 LEU 167 -0.12 GLU 131
ALA 72 0.19 VAL 168 -0.11 GLU 131
MET 110 0.17 ALA 169 -0.18 ARG 209
ALA 72 0.14 CYS 170 -0.12 ARG 209
ALA 72 0.15 ILE 171 -0.11 THR 135
ALA 72 0.15 LYS 172 -0.14 ARG 209
ALA 72 0.13 ASN 173 -0.19 ARG 209
ALA 72 0.11 ILE 174 -0.14 ARG 209
ALA 72 0.11 PHE 175 -0.12 ARG 209
ASP 177 0.13 GLY 176 -0.13 ARG 209
GLY 176 0.13 ASP 177 -0.10 ARG 209
ALA 72 0.11 MET 178 -0.08 GLU 142
ALA 72 0.13 LEU 179 -0.07 GLU 142
ALA 72 0.13 CYS 180 -0.09 CYS 313
PRO 244 0.16 PRO 181 -0.12 CYS 313
GLY 246 0.23 ARG 182 -0.13 CYS 313
GLY 245 0.26 GLY 183 -0.18 CYS 313
GLY 246 0.19 GLU 184 -0.19 CYS 313
ARG 284 0.11 VAL 185 -0.22 CYS 313
ALA 72 0.10 PRO 186 -0.17 CYS 313
ALA 72 0.08 THR 187 -0.15 CYS 313
ALA 72 0.08 LEU 188 -0.08 CYS 313
ALA 72 0.08 ARG 189 -0.09 CYS 313
ALA 72 0.09 GLN 190 -0.13 CYS 313
ALA 72 0.09 LEU 191 -0.08 CYS 313
ALA 72 0.08 TRP 192 -0.06 ASN 20
ALA 72 0.09 SER 193 -0.06 CYS 313
ALA 72 0.10 ARG 194 -0.06 CYS 313
ALA 72 0.09 GLY 195 -0.08 PRO 145
ALA 72 0.10 GLN 196 -0.06 PRO 145
ALA 72 0.09 GLN 197 -0.04 ASP 97
ALA 72 0.11 VAL 198 -0.05 CYS 313
ALA 72 0.12 ILE 199 -0.09 CYS 313
ALA 72 0.15 VAL 200 -0.09 CYS 313
PRO 219 0.18 SER 201 -0.11 CYS 313
ALA 72 0.21 TYR 202 -0.10 CYS 313
GLY 217 0.29 GLU 203 -0.11 CYS 313
ALA 72 0.28 ASP 204 -0.11 CYS 313
ALA 72 0.27 GLU 205 -0.10 CYS 313
ALA 72 0.30 SER 206 -0.11 ALA 169
ALA 72 0.27 SER 207 -0.13 ALA 169
ALA 72 0.24 LEU 208 -0.14 ALA 169
ALA 72 0.24 ARG 209 -0.19 ASN 173
PRO 244 0.21 ARG 210 -0.14 ASN 173
ALA 72 0.20 HIS 211 -0.09 ASN 173
PRO 244 0.21 HIS 212 -0.10 CYS 313
ALA 72 0.16 GLU 213 -0.09 CYS 313
ALA 72 0.18 LEU 214 -0.10 CYS 313
PRO 219 0.21 TRP 215 -0.13 CYS 313
PRO 219 0.30 PRO 216 -0.13 CYS 313
GLU 203 0.29 GLY 217 -0.17 CYS 313
PRO 219 0.30 VAL 218 -0.18 CYS 313
PRO 216 0.30 PRO 219 -0.24 CYS 313
GLU 203 0.26 TYR 220 -0.21 CYS 313
GLU 203 0.28 TRP 221 -0.24 CYS 313
GLU 203 0.23 TRP 222 -0.22 CYS 313
GLU 203 0.23 GLY 223 -0.24 CYS 313
GLU 157 0.26 ASN 224 -0.23 CYS 313
GLU 157 0.23 ARG 225 -0.20 CYS 313
GLU 157 0.20 VAL 226 -0.16 CYS 313
GLU 157 0.18 LYS 227 -0.17 GLU 257
GLU 203 0.15 THR 228 -0.19 LEU 259
GLU 205 0.16 GLU 229 -0.18 CYS 313
GLU 205 0.19 ALA 230 -0.22 CYS 313
GLU 203 0.17 LEU 231 -0.18 CYS 313
GLU 205 0.16 ILE 232 -0.21 CYS 313
GLU 205 0.17 ARG 233 -0.29 CYS 313
GLU 205 0.19 TYR 234 -0.29 CYS 313
GLU 205 0.17 LEU 235 -0.28 CYS 313
GLU 205 0.16 GLU 236 -0.36 CYS 313
GLU 205 0.19 THR 237 -0.39 CYS 313
GLU 205 0.20 MET 238 -0.40 CYS 313
GLU 205 0.17 LYS 239 -0.46 CYS 313
GLU 205 0.17 SER 240 -0.55 CYS 313
GLU 205 0.20 CYS 241 -0.50 CYS 313
GLU 205 0.20 GLY 242 -0.50 CYS 313
GLU 205 0.21 ARG 243 -0.41 CYS 313
PRO 216 0.26 PRO 244 -0.38 CYS 313
GLY 183 0.26 GLY 245 -0.37 CYS 313
GLY 183 0.24 GLY 246 -0.30 CYS 313
ARG 182 0.20 LEU 247 -0.24 CYS 313
PRO 216 0.20 PHE 248 -0.26 CYS 313
PRO 216 0.18 VAL 249 -0.20 CYS 313
GLU 203 0.17 ALA 250 -0.20 CYS 313
GLU 203 0.19 GLY 251 -0.16 CYS 313
GLU 203 0.17 ILE 252 -0.14 CYS 313
ASN 155 0.21 ASN 253 -0.16 CYS 313
ASN 155 0.19 LEU 254 -0.14 TRP 84
GLU 157 0.22 THR 255 -0.13 CYS 313
GLU 157 0.18 SER 256 -0.16 THR 228
GLU 157 0.19 GLU 257 -0.17 THR 228
GLU 157 0.16 SER 258 -0.15 THR 228
ASN 155 0.14 LEU 259 -0.19 THR 228
ASN 155 0.12 GLU 260 -0.25 LYS 261
ASN 155 0.13 LYS 261 -0.27 LYS 55
ASN 155 0.12 MET 262 -0.29 LYS 55
ASN 155 0.12 THR 263 -0.25 LYS 55
ASN 155 0.11 LEU 264 -0.27 LYS 55
GLU 203 0.12 PRO 265 -0.22 LYS 55
GLU 203 0.13 ASN 266 -0.21 LYS 55
GLU 203 0.11 LEU 267 -0.22 LYS 55
GLU 203 0.11 PRO 268 -0.21 LYS 55
GLU 203 0.12 ARG 269 -0.20 LYS 55
GLU 203 0.12 LEU 270 -0.19 LYS 55
GLU 203 0.10 SER 271 -0.19 LYS 55
GLU 203 0.10 ALA 272 -0.18 LYS 55
GLU 205 0.11 TRP 273 -0.17 LYS 55
PRO 216 0.10 VAL 274 -0.16 LYS 55
CYS 278 0.12 ARG 275 -0.16 LYS 55
GLN 277 0.16 GLU 276 -0.16 LYS 55
GLU 276 0.16 GLN 277 -0.16 GLU 236
GLU 276 0.15 CYS 278 -0.25 CYS 313
ASN 20 0.06 PRO 279 -0.21 LYS 239
ARG 210 0.03 GLY 280 -0.26 CYS 313
GLU 276 0.09 PRO 281 -0.37 CYS 313
GLU 276 0.12 GLY 282 -0.55 CYS 313
GLY 183 0.14 SER 283 -0.70 CYS 313
GLY 183 0.17 ARG 284 -0.58 CYS 313
GLY 183 0.15 CYS 285 -0.44 CYS 313
PRO 216 0.16 THR 286 -0.32 CYS 313
PRO 216 0.12 ASN 287 -0.24 CYS 313
PRO 216 0.12 ILE 288 -0.16 CYS 313
GLU 203 0.13 ILE 289 -0.14 CYS 313
GLU 203 0.12 ALA 290 -0.12 LYS 55
GLU 203 0.11 GLY 291 -0.15 LYS 55
ASN 155 0.10 ASP 292 -0.18 LYS 55
ASN 155 0.08 PHE 293 -0.23 LYS 55
ASN 155 0.06 ILE 294 -0.20 LYS 55
CYS 313 0.12 GLY 295 -0.24 LYS 55
CYS 313 0.13 ALA 296 -0.26 LYS 55
CYS 313 0.19 ASP 297 -0.24 LYS 55
CYS 313 0.15 GLY 298 -0.21 LYS 55
GLU 203 0.08 PHE 299 -0.19 LYS 55
LYS 309 0.10 VAL 300 -0.17 LYS 55
CYS 313 0.19 SER 301 -0.17 LYS 55
CYS 313 0.16 ASP 302 -0.17 LYS 55
LYS 309 0.10 VAL 303 -0.15 LYS 55
LYS 309 0.19 ILE 304 -0.13 LYS 55
CYS 313 0.22 ALA 305 -0.13 LYS 55
LEU 311 0.09 LEU 306 -0.13 LYS 55
LYS 309 0.11 ASN 307 -0.11 LYS 55
LYS 309 0.25 GLN 308 -0.11 LYS 55
GLN 308 0.25 LYS 309 -0.12 SER 240
CYS 313 0.24 LEU 310 -0.19 SER 283
GLN 308 0.20 LEU 311 -0.27 SER 283
GLN 308 0.17 TRP 312 -0.42 SER 283
LEU 310 0.24 CYS 313 -0.70 SER 283

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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.