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CA distance fluctuations for 2606032003402649896

---  normal mode 7  ---

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 279 0.24 VAL 233 -0.03 ALA 301
PRO 279 0.27 SER 234 -0.02 ALA 301
PRO 279 0.27 GLU 235 -0.02 ALA 301
PRO 279 0.28 ARG 236 -0.02 ALA 301
PRO 279 0.25 PRO 237 -0.03 ALA 301
PRO 279 0.23 PRO 238 -0.03 ALA 301
PRO 279 0.23 TYR 239 -0.04 ALA 301
PRO 279 0.24 SER 240 -0.03 ALA 301
PRO 279 0.25 TYR 241 -0.03 ALA 301
PRO 279 0.21 MET 242 -0.04 ALA 301
PRO 279 0.20 ALA 243 -0.05 ALA 301
PRO 279 0.22 MET 244 -0.04 ALA 301
PRO 279 0.21 ILE 245 -0.05 ALA 301
PRO 279 0.17 GLN 246 -0.07 ALA 301
PRO 279 0.18 PHE 247 -0.06 ALA 301
ASN 283 0.19 ALA 248 -0.06 ALA 301
ASN 283 0.16 ILE 249 -0.08 ALA 301
ASN 283 0.13 ASN 250 -0.09 ALA 301
ASN 283 0.15 SER 251 -0.07 ALA 301
ASN 283 0.13 THR 252 -0.08 ARG 254
ASN 283 0.10 GLU 253 -0.11 ARG 254
ASN 283 0.08 ARG 254 -0.13 ARG 254
ASN 283 0.10 LYS 255 -0.11 ALA 301
ASN 283 0.12 ARG 256 -0.08 ALA 301
ASN 283 0.17 MET 257 -0.05 ALA 301
ASN 283 0.20 THR 258 -0.02 ALA 301
ASN 283 0.27 LEU 259 -0.01 SER 290
ASN 283 0.30 LYS 260 -0.01 SER 290
ASN 283 0.24 ASP 261 -0.03 ALA 301
ASN 283 0.25 ILE 262 -0.03 ALA 301
ASN 283 0.30 TYR 263 -0.01 ALA 301
ASN 283 0.28 THR 264 -0.02 ALA 301
ASN 283 0.24 TRP 265 -0.03 ALA 301
GLY 280 0.26 ILE 266 -0.03 ALA 301
GLY 280 0.28 GLU 267 -0.02 ALA 301
GLY 280 0.25 ASP 268 -0.03 ALA 301
GLY 280 0.23 HIS 269 -0.03 ALA 301
PRO 279 0.26 PHE 270 -0.03 ALA 301
GLY 280 0.28 PRO 271 -0.02 ALA 301
PRO 279 0.30 TYR 272 -0.02 ALA 301
PRO 279 0.32 PHE 273 -0.01 ALA 301
GLY 280 0.32 LYS 274 -0.01 ALA 301
GLY 280 0.33 HIS 275 -0.01 THR 252
PRO 279 0.35 ILE 276 -0.01 THR 252
PRO 279 0.37 ALA 277 -0.01 THR 252
PRO 279 0.42 LYS 278 -0.00 THR 252
PRO 279 0.45 PRO 279 -0.00 TRP 265
PRO 279 0.45 GLY 280 -0.00 SER 240
PRO 279 0.38 TRP 281 -0.00 ALA 248
PRO 279 0.38 LYS 282 -0.00 ASP 261
PRO 279 0.42 ASN 283 -0.00 ASP 261
PRO 279 0.36 SER 284 -0.00 MET 242
PRO 279 0.31 ILE 285 -0.00 THR 258
ASN 283 0.32 ARG 286 -0.01 THR 258
PRO 279 0.31 HIS 287 -0.01 THR 258
PRO 279 0.25 ASN 288 -0.01 ALA 301
PRO 279 0.22 LEU 289 -0.01 ALA 301
LYS 260 0.25 SER 290 -0.02 THR 258
LYS 260 0.23 LEU 291 -0.01 THR 258
PRO 279 0.16 HIS 292 -0.03 ALA 301
LYS 260 0.11 ASP 293 -0.04 ALA 301
PRO 279 0.11 MET 294 -0.09 ALA 301
PRO 279 0.13 PHE 295 -0.07 ALA 301
ASN 283 0.09 VAL 296 -0.07 ALA 301
ASN 283 0.10 ARG 297 -0.03 SER 300
ASN 283 0.07 GLU 298 -0.07 GLU 298
ASN 283 0.06 THR 299 -0.06 GLU 298
ASN 283 0.05 SER 300 -0.10 HIS 311
ALA 301 0.05 ALA 301 -0.14 HIS 311
ALA 301 0.04 ASN 302 -0.08 HIS 311
ASN 283 0.05 GLY 303 -0.04 HIS 311
SER 290 0.12 LYS 304 -0.02 THR 299
SER 290 0.14 VAL 305 -0.02 SER 306
ARG 286 0.14 SER 306 -0.02 VAL 305
ASN 283 0.14 PHE 307 -0.04 HIS 311
ASN 283 0.15 TRP 308 -0.05 ALA 301
ASN 283 0.11 THR 309 -0.11 ALA 301
ASN 283 0.10 ILE 310 -0.13 ALA 301
PRO 279 0.07 HIS 311 -0.16 ALA 301
PRO 279 0.25 SER 232 -0.05 HIS 269
PRO 279 0.27 VAL 233 -0.03 HIS 269
PRO 279 0.28 SER 234 -0.02 PHE 270
PRO 279 0.28 GLU 235 -0.01 SER 232
PRO 279 0.28 ARG 236 -0.02 SER 232
PRO 279 0.25 PRO 237 -0.05 SER 232
PRO 279 0.23 PRO 238 -0.04 SER 232
PRO 279 0.23 TYR 239 -0.04 SER 232
PRO 279 0.23 SER 240 -0.02 ALA 301
PRO 279 0.25 TYR 241 -0.02 ALA 301
PRO 279 0.21 MET 242 -0.03 ALA 301
PRO 279 0.20 ALA 243 -0.04 ALA 301
PRO 279 0.22 MET 244 -0.03 SER 232
ASN 283 0.21 ILE 245 -0.03 ALA 301
ASN 283 0.17 GLN 246 -0.05 ALA 301
ASN 283 0.17 PHE 247 -0.05 ARG 254
ASN 283 0.19 ALA 248 -0.05 ARG 254
ASN 283 0.16 ILE 249 -0.06 ARG 254
ASN 283 0.14 ASN 250 -0.09 ARG 254
ASN 283 0.15 SER 251 -0.08 ARG 254
ASN 283 0.14 THR 252 -0.09 ARG 254
ASN 283 0.11 GLU 253 -0.11 ARG 254
ASN 283 0.09 ARG 254 -0.13 ARG 254
ASN 283 0.11 LYS 255 -0.12 ARG 254
ASN 283 0.13 ARG 256 -0.09 ARG 254
ASN 283 0.18 MET 257 -0.05 ARG 254
ASN 283 0.22 THR 258 -0.01 SER 232
ASN 283 0.28 LEU 259 -0.01 THR 258
ASN 283 0.32 LYS 260 -0.01 SER 232
ASN 283 0.26 ASP 261 -0.02 SER 232
ASN 283 0.26 ILE 262 -0.02 SER 232
ASN 283 0.31 TYR 263 -0.01 SER 232
ASN 283 0.28 THR 264 -0.02 SER 232
ASN 283 0.24 TRP 265 -0.03 SER 232
ASN 283 0.26 ILE 266 -0.03 SER 232
GLY 280 0.29 GLU 267 -0.02 SER 232
GLY 280 0.26 ASP 268 -0.03 SER 232
GLY 280 0.23 HIS 269 -0.05 SER 232
GLY 280 0.26 PHE 270 -0.04 SER 232
GLY 280 0.28 PRO 271 -0.03 SER 232
PRO 279 0.30 TYR 272 -0.02 SER 232
GLY 280 0.32 PHE 273 -0.01 SER 232
GLY 280 0.33 LYS 274 -0.01 SER 232
GLY 280 0.34 HIS 275 -0.01 GLU 253
PRO 279 0.35 ILE 276 -0.01 GLU 253
PRO 279 0.36 ALA 277 -0.01 THR 252
PRO 279 0.42 LYS 278 -0.01 SER 240
PRO 279 0.45 PRO 279 -0.00 SER 240
PRO 279 0.45 GLY 280 -0.00 TRP 281
PRO 279 0.38 TRP 281 -0.00 GLY 280
ASN 283 0.39 LYS 282 -0.00 THR 264
PRO 279 0.42 ASN 283 -0.00 ASP 261
PRO 279 0.35 SER 284 -0.00 MET 242
PRO 279 0.31 ILE 285 -0.01 SER 232
ASN 283 0.32 ARG 286 -0.01 THR 258
PRO 279 0.31 HIS 287 -0.01 THR 258
PRO 279 0.25 ASN 288 -0.01 SER 232
PRO 279 0.21 LEU 289 -0.01 SER 232
LYS 260 0.23 SER 290 -0.01 THR 258
LYS 260 0.20 LEU 291 -0.01 THR 258
PRO 279 0.16 HIS 292 -0.02 ALA 301
PRO 279 0.11 ASP 293 -0.04 ALA 301
PRO 279 0.11 MET 294 -0.07 ALA 301
ASN 283 0.13 PHE 295 -0.05 ALA 301
ASN 283 0.09 VAL 296 -0.05 ARG 254
ASN 283 0.10 ARG 297 -0.04 ARG 254
ASN 283 0.07 GLU 298 -0.08 ARG 254
ARG 286 0.06 THR 299 -0.06 GLU 298
ASN 283 0.05 SER 300 -0.10 HIS 311
ALA 301 0.05 ALA 301 -0.16 HIS 311
ALA 301 0.04 ASN 302 -0.10 HIS 311
SER 290 0.04 GLY 303 -0.05 HIS 311
SER 290 0.13 LYS 304 -0.02 THR 299
SER 290 0.15 VAL 305 -0.02 HIS 311
ARG 286 0.15 SER 306 -0.02 VAL 305
ASN 283 0.14 PHE 307 -0.04 ARG 254
ASN 283 0.15 TRP 308 -0.04 ARG 254
ASN 283 0.12 THR 309 -0.08 ARG 254
ASN 283 0.11 ILE 310 -0.10 ALA 301
ASN 283 0.07 HIS 311 -0.14 ALA 301

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).
Between 2015 and 2025, it was hosted by US2B (Nantes).
Last modification: april 24th, 2026.