CNRS Nantes University UFIP UFIP
home |  start a new run |  job status |  references&downloads |  examples |  help  

Should you encounter any unexpected behaviour,
please let us know.


***  3BLH_A_VS_4bcg_A  ***

CA distance fluctuations for 22051216393486404

---  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
LYS 40 0.43 VAL 8 -1.57 GLY 58
LEU 72 0.16 GLU 9 -1.18 LYS 56
GLN 71 0.22 CYS 10 -0.87 GLU 55
GLN 71 0.49 PRO 11 -0.62 GLU 55
GLN 71 0.52 PHE 12 -0.52 GLU 55
LYS 68 0.30 CYS 13 -0.64 GLU 55
GLN 71 0.19 ASP 14 -0.66 GLU 55
LYS 68 0.14 GLU 15 -0.72 GLU 55
TYR 185 0.10 VAL 16 -0.65 GLU 55
VAL 8 0.22 SER 17 -0.61 GLU 55
VAL 8 0.31 LYS 18 -0.54 GLU 55
VAL 8 0.17 TYR 19 -0.49 GLU 55
VAL 8 0.16 GLU 20 -0.46 GLU 55
ARG 188 0.06 LYS 21 -0.43 GLU 55
ARG 188 0.04 LEU 22 -0.35 GLU 55
GLY 28 0.03 ALA 23 -0.30 GLU 55
PHE 12 0.04 LYS 24 -0.27 GLU 55
PHE 12 0.06 ILE 25 -0.20 GLU 9
PHE 12 0.07 GLY 26 -0.28 VAL 8
PHE 12 0.07 GLN 27 -0.37 VAL 8
PHE 12 0.11 GLY 28 -0.44 VAL 8
THR 191 0.19 THR 29 -0.55 VAL 8
ARG 188 0.21 PHE 30 -0.63 VAL 8
ARG 188 0.14 GLY 31 -0.51 VAL 8
ARG 188 0.08 GLU 32 -0.37 VAL 8
PHE 12 0.08 VAL 33 -0.29 GLU 55
PHE 12 0.06 PHE 34 -0.34 GLU 55
PHE 12 0.06 LYS 35 -0.31 GLU 55
ARG 188 0.05 ALA 36 -0.38 GLU 55
VAL 8 0.14 ARG 37 -0.38 GLU 55
VAL 8 0.23 HIS 38 -0.41 GLU 55
VAL 8 0.35 ARG 39 -0.42 GLU 55
VAL 8 0.43 LYS 40 -0.39 GLU 55
VAL 8 0.34 THR 41 -0.35 GLU 55
VAL 8 0.25 GLY 42 -0.34 GLU 55
VAL 8 0.17 GLN 43 -0.32 GLU 55
PRO 11 0.09 LYS 44 -0.31 GLU 55
PRO 11 0.11 VAL 45 -0.33 GLU 55
PHE 12 0.11 ALA 46 -0.31 GLU 55
PHE 12 0.11 LEU 47 -0.41 GLU 55
PHE 12 0.13 LYS 48 -0.36 GLU 55
ARG 188 0.13 LYS 49 -0.52 GLU 55
ARG 188 0.18 VAL 50 -0.63 VAL 8
ARG 188 0.77 GLU 55 -1.37 VAL 8
ASN 187 0.98 LYS 56 -1.40 VAL 8
ARG 184 0.77 GLU 57 -1.55 VAL 8
ARG 188 0.51 GLY 58 -1.57 VAL 8
ARG 188 0.35 PHE 59 -1.14 VAL 8
ARG 188 0.43 PRO 60 -0.99 VAL 8
TYR 185 0.38 ILE 61 -0.84 VAL 8
GLU 57 0.33 THR 62 -0.68 VAL 8
PHE 12 0.25 ALA 63 -0.64 VAL 8
PHE 12 0.35 LEU 64 -0.62 VAL 8
PHE 12 0.38 ARG 65 -0.53 VAL 8
PHE 12 0.36 GLU 66 -0.45 VAL 8
PHE 12 0.44 ILE 67 -0.41 VAL 8
PHE 12 0.50 LYS 68 -0.39 VAL 8
PHE 12 0.42 ILE 69 -0.34 VAL 8
PHE 12 0.41 LEU 70 -0.28 VAL 8
PHE 12 0.52 GLN 71 -0.24 GLY 58
PRO 11 0.45 LEU 72 -0.22 VAL 8
PRO 11 0.38 LEU 73 -0.19 VAL 8
PRO 11 0.37 LYS 74 -0.17 GLY 58
PRO 11 0.29 HIS 75 -0.14 GLY 58
PRO 11 0.23 GLU 76 -0.13 GLY 58
PRO 11 0.22 ASN 77 -0.13 VAL 8
PRO 11 0.25 VAL 78 -0.17 VAL 8
PRO 11 0.24 VAL 79 -0.17 VAL 8
PRO 11 0.28 ASN 80 -0.20 GLU 55
PRO 11 0.30 LEU 81 -0.27 GLU 55
PRO 11 0.32 ILE 82 -0.35 GLU 55
PHE 12 0.34 GLU 83 -0.43 GLU 55
PHE 12 0.27 ILE 84 -0.54 GLU 55
ILE 67 0.16 CYS 85 -0.67 GLU 55
LYS 68 0.14 ARG 86 -0.88 GLU 55
ARG 184 0.13 THR 87 -0.93 GLU 55
ARG 188 0.14 SER 98 -1.13 GLU 55
ARG 188 0.15 ILE 99 -0.85 GLU 55
PHE 12 0.13 TYR 100 -0.61 GLU 55
PHE 12 0.21 LEU 101 -0.43 GLU 55
PHE 12 0.18 VAL 102 -0.41 GLU 55
PRO 11 0.20 PHE 103 -0.29 GLU 55
PRO 11 0.18 ASP 104 -0.26 GLU 55
PRO 11 0.12 PHE 105 -0.24 GLU 55
PRO 11 0.12 CYS 106 -0.16 GLU 55
PRO 11 0.09 GLU 107 -0.13 GLU 55
PRO 11 0.09 HIS 108 -0.13 GLU 107
PHE 12 0.10 ASP 109 -0.17 VAL 8
LYS 56 0.16 LEU 110 -0.18 VAL 8
LYS 56 0.19 ALA 111 -0.20 VAL 8
LYS 56 0.11 GLY 112 -0.18 VAL 8
LYS 56 0.10 LEU 113 -0.15 VAL 8
LYS 56 0.17 LEU 114 -0.17 VAL 8
LYS 56 0.16 SER 115 -0.18 VAL 8
LYS 56 0.10 ASN 116 -0.16 ALA 23
LYS 56 0.11 VAL 117 -0.15 ALA 23
LYS 56 0.06 LEU 118 -0.17 LEU 22
LYS 56 0.08 VAL 119 -0.16 LEU 22
LYS 56 0.10 LYS 120 -0.15 GLY 42
LYS 56 0.13 PHE 121 -0.14 GLY 42
LYS 56 0.13 THR 122 -0.13 GLY 42
LYS 56 0.17 LEU 123 -0.12 GLY 42
LYS 56 0.14 SER 124 -0.12 GLY 42
LYS 56 0.13 GLU 125 -0.13 GLY 42
LYS 56 0.18 ILE 126 -0.12 VAL 8
LYS 56 0.19 LYS 127 -0.11 VAL 8
LYS 56 0.15 ARG 128 -0.10 GLY 42
LYS 56 0.16 VAL 129 -0.12 VAL 8
LYS 56 0.22 MET 130 -0.14 VAL 8
LYS 56 0.19 GLN 131 -0.12 VAL 8
PRO 11 0.18 MET 132 -0.12 VAL 8
LYS 56 0.22 LEU 133 -0.16 VAL 8
LYS 56 0.26 LEU 134 -0.16 VAL 8
PRO 11 0.22 ASN 135 -0.14 VAL 8
PRO 11 0.24 GLY 136 -0.16 VAL 8
LYS 56 0.28 LEU 137 -0.19 VAL 8
LYS 56 0.26 TYR 138 -0.17 VAL 8
PRO 11 0.29 TYR 139 -0.16 VAL 8
PRO 11 0.30 ILE 140 -0.21 VAL 8
LYS 56 0.33 HIS 141 -0.22 VAL 8
PRO 11 0.31 ARG 142 -0.19 VAL 8
PRO 11 0.35 ASN 143 -0.22 VAL 8
LYS 56 0.34 LYS 144 -0.26 VAL 8
LYS 56 0.36 ILE 145 -0.29 VAL 8
LYS 56 0.45 LEU 146 -0.30 VAL 8
LYS 56 0.40 HIS 147 -0.30 VAL 8
LYS 56 0.52 ARG 148 -0.32 VAL 8
LYS 56 0.45 ASP 149 -0.31 VAL 8
LYS 56 0.40 MET 150 -0.26 VAL 8
LYS 56 0.35 LYS 151 -0.25 VAL 8
LYS 56 0.26 ALA 152 -0.22 VAL 8
LYS 56 0.21 ALA 153 -0.24 VAL 8
LYS 56 0.22 ASN 154 -0.25 VAL 8
LYS 56 0.18 VAL 155 -0.20 VAL 8
PRO 11 0.14 LEU 156 -0.17 VAL 8
PRO 11 0.12 ILE 157 -0.12 VAL 8
PRO 11 0.12 THR 158 -0.13 GLN 43
PRO 11 0.09 ARG 159 -0.16 LEU 324
PRO 11 0.08 ASP 160 -0.20 GLN 43
PRO 11 0.10 GLY 161 -0.15 GLN 43
PRO 11 0.14 VAL 162 -0.12 GLN 43
PRO 11 0.16 LEU 163 -0.13 VAL 8
PRO 11 0.19 LYS 164 -0.15 VAL 8
PRO 11 0.21 LEU 165 -0.21 VAL 8
PHE 12 0.21 ALA 166 -0.25 VAL 8
PHE 12 0.23 ASP 167 -0.31 VAL 8
PHE 12 0.28 PHE 168 -0.35 VAL 8
LYS 56 0.28 GLY 169 -0.43 VAL 8
LYS 56 0.47 LEU 170 -0.41 VAL 8
LYS 56 0.41 ALA 171 -0.38 VAL 8
LYS 56 0.47 ARG 172 -0.38 VAL 8
LYS 56 0.42 ALA 173 -0.35 VAL 8
LYS 56 0.50 PHE 174 -0.31 VAL 8
LYS 56 0.49 SER 175 -0.29 VAL 8
LYS 56 0.52 LEU 176 -0.27 VAL 8
LYS 56 0.74 PRO 182 -0.29 VAL 8
LYS 56 0.77 ASN 183 -0.31 VAL 8
LYS 56 0.92 ARG 184 -0.34 VAL 8
LYS 56 0.87 TYR 185 -0.35 VAL 8
LYS 56 0.98 ASN 187 -0.34 VAL 8
LYS 56 0.96 ARG 188 -0.36 VAL 8
LYS 56 0.77 VAL 189 -0.35 VAL 8
LYS 56 0.63 VAL 190 -0.32 VAL 8
LYS 56 0.58 THR 191 -0.30 VAL 8
LYS 56 0.64 LEU 192 -0.29 VAL 8
LYS 56 0.54 TRP 193 -0.26 VAL 8
LYS 56 0.52 TYR 194 -0.26 VAL 8
LYS 56 0.64 ARG 195 -0.27 VAL 8
LYS 56 0.64 PRO 196 -0.26 VAL 8
LYS 56 0.69 PRO 197 -0.25 VAL 8
LYS 56 0.75 GLU 198 -0.26 VAL 8
LYS 56 0.82 LEU 199 -0.29 VAL 8
LYS 56 0.83 LEU 200 -0.28 VAL 8
LYS 56 0.86 LEU 201 -0.27 VAL 8
LYS 56 0.96 GLY 202 -0.29 VAL 8
LYS 56 0.88 GLU 203 -0.29 VAL 8
LYS 56 0.91 ARG 204 -0.31 VAL 8
LYS 56 0.78 ASP 205 -0.30 VAL 8
LYS 56 0.69 TYR 206 -0.28 VAL 8
LYS 56 0.58 GLY 207 -0.27 VAL 8
LYS 56 0.48 PRO 208 -0.25 VAL 8
LYS 56 0.52 PRO 209 -0.23 VAL 8
LYS 56 0.56 ILE 210 -0.26 VAL 8
LYS 56 0.46 ASP 211 -0.25 VAL 8
LYS 56 0.43 LEU 212 -0.22 VAL 8
LYS 56 0.49 TRP 213 -0.22 VAL 8
LYS 56 0.45 GLY 214 -0.23 VAL 8
LYS 56 0.37 ALA 215 -0.20 VAL 8
LYS 56 0.40 GLY 216 -0.20 VAL 8
LYS 56 0.41 CYS 217 -0.21 VAL 8
LYS 56 0.33 ILE 218 -0.20 VAL 8
LYS 56 0.31 MET 219 -0.17 VAL 8
LYS 56 0.33 ALA 220 -0.18 VAL 8
LYS 56 0.30 GLU 221 -0.18 VAL 8
LYS 56 0.24 MET 222 -0.16 VAL 8
LYS 56 0.25 TRP 223 -0.15 VAL 8
LYS 56 0.28 THR 224 -0.17 VAL 8
LYS 56 0.25 ARG 225 -0.17 VAL 8
LYS 56 0.30 SER 226 -0.20 VAL 8
LYS 56 0.37 PRO 227 -0.22 VAL 8
LYS 56 0.41 ILE 228 -0.21 VAL 8
LYS 56 0.48 MET 229 -0.23 VAL 8
LYS 56 0.49 GLN 230 -0.24 VAL 8
LYS 56 0.58 GLY 231 -0.26 VAL 8
LYS 56 0.61 ASN 232 -0.27 VAL 8
LYS 56 0.73 THR 233 -0.28 VAL 8
LYS 56 0.79 GLU 234 -0.28 VAL 8
LYS 56 0.76 GLN 235 -0.26 VAL 8
LYS 56 0.66 HIS 236 -0.25 VAL 8
LYS 56 0.66 GLN 237 -0.25 VAL 8
LYS 56 0.69 LEU 238 -0.25 VAL 8
LYS 56 0.64 ALA 239 -0.23 VAL 8
LYS 56 0.57 LEU 240 -0.23 VAL 8
LYS 56 0.58 ILE 241 -0.22 VAL 8
LYS 56 0.59 SER 242 -0.21 VAL 8
LYS 56 0.53 GLN 243 -0.20 VAL 8
LYS 56 0.50 LEU 244 -0.20 VAL 8
LYS 56 0.52 CYS 245 -0.20 VAL 8
LYS 56 0.54 GLY 246 -0.19 VAL 8
LYS 56 0.60 SER 247 -0.20 VAL 8
LYS 56 0.65 ILE 248 -0.21 VAL 8
LYS 56 0.63 THR 249 -0.19 VAL 8
LYS 56 0.65 PRO 250 -0.19 VAL 8
LYS 56 0.59 GLU 251 -0.18 VAL 8
LYS 56 0.57 VAL 252 -0.18 VAL 8
LYS 56 0.62 TRP 253 -0.20 VAL 8
LYS 56 0.63 PRO 254 -0.19 VAL 8
LYS 56 0.70 ASN 255 -0.20 VAL 8
LYS 56 0.73 VAL 256 -0.21 VAL 8
LYS 56 0.76 ASP 257 -0.21 VAL 8
LYS 56 0.83 ASN 258 -0.22 VAL 8
LYS 56 0.91 TYR 259 -0.25 VAL 8
LYS 56 0.71 LEU 267 -0.23 VAL 8
LYS 56 0.64 VAL 268 -0.21 VAL 8
LYS 56 0.61 LYS 269 -0.20 VAL 8
LYS 56 0.56 GLY 270 -0.19 VAL 8
LYS 56 0.54 GLN 271 -0.19 VAL 8
LYS 56 0.50 LYS 272 -0.18 VAL 8
LYS 56 0.48 ARG 273 -0.18 VAL 8
LYS 56 0.44 LYS 274 -0.17 VAL 8
LYS 56 0.43 VAL 275 -0.18 VAL 8
LYS 56 0.38 LYS 276 -0.16 VAL 8
LYS 56 0.38 ASP 277 -0.16 VAL 8
LYS 56 0.38 ARG 278 -0.17 VAL 8
LYS 56 0.35 LEU 279 -0.16 VAL 8
LYS 56 0.32 LYS 280 -0.15 VAL 8
LYS 56 0.30 ALA 281 -0.15 VAL 8
LYS 56 0.28 TYR 282 -0.15 VAL 8
LYS 56 0.27 VAL 283 -0.14 VAL 8
LYS 56 0.26 ARG 284 -0.13 VAL 8
LYS 56 0.25 ASP 285 -0.12 VAL 8
LYS 56 0.28 PRO 286 -0.12 VAL 8
LYS 56 0.28 TYR 287 -0.12 VAL 8
LYS 56 0.28 ALA 288 -0.13 VAL 8
LYS 56 0.32 LEU 289 -0.14 VAL 8
LYS 56 0.34 ASP 290 -0.14 VAL 8
LYS 56 0.34 LEU 291 -0.15 VAL 8
LYS 56 0.37 ILE 292 -0.17 VAL 8
LYS 56 0.40 ASP 293 -0.17 VAL 8
LYS 56 0.41 LYS 294 -0.17 VAL 8
LYS 56 0.42 LEU 295 -0.19 VAL 8
LYS 56 0.47 LEU 296 -0.20 VAL 8
LYS 56 0.51 VAL 297 -0.20 VAL 8
LYS 56 0.58 LEU 298 -0.21 VAL 8
LYS 56 0.59 ASP 299 -0.21 VAL 8
LYS 56 0.58 PRO 300 -0.22 VAL 8
LYS 56 0.55 ALA 301 -0.20 VAL 8
LYS 56 0.50 GLN 302 -0.19 VAL 8
LYS 56 0.48 ARG 303 -0.19 VAL 8
LYS 56 0.41 ILE 304 -0.17 VAL 8
LYS 56 0.39 ASP 305 -0.18 VAL 8
LYS 56 0.32 SER 306 -0.17 VAL 8
LYS 56 0.29 ASP 307 -0.14 VAL 8
LYS 56 0.32 ASP 308 -0.14 VAL 8
LYS 56 0.31 ALA 309 -0.14 VAL 8
LYS 56 0.25 LEU 310 -0.12 VAL 8
LYS 56 0.25 ASN 311 -0.11 VAL 8
LYS 56 0.28 HIS 312 -0.12 VAL 8
LYS 56 0.25 ASP 313 -0.10 VAL 8
LYS 56 0.24 PHE 314 -0.11 VAL 8
LYS 56 0.21 PHE 315 -0.10 VAL 8
LYS 56 0.19 TRP 316 -0.08 VAL 8
LYS 56 0.19 SER 317 -0.09 GLY 42
LYS 56 0.16 ASP 318 -0.10 GLY 42
LYS 56 0.15 PRO 319 -0.11 GLY 42
LYS 56 0.14 MET 320 -0.11 GLY 42
LYS 56 0.14 PRO 321 -0.11 GLY 42
PRO 11 0.10 SER 322 -0.13 GLY 42
PRO 11 0.10 ASP 323 -0.14 GLY 42
PRO 11 0.09 LEU 324 -0.16 ARG 159
LEU 113 0.07 LYS 325 -0.18 GLY 42

If you find results from this site helpful for your research, please cite one of our papers:

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: October 18th, 2018.