Should you encounter any unexpected behaviour,
please let us know.
elNémo has been relocated.
Some cleaning from time to time
Sorry for the inconvenience.

* 6csc_aligned_close *

CA distance fluctuations for 2604241133101949041

--- normal mode 14 ---

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 increase ref largest decrease
ILE 21 0.11 ALA 1 -0.07 ASN 359

ILE 21 0.10 SER 2 -0.06 ASN 359

GLY 29 0.08 SER 3 -0.06 VAL 33

GLY 29 0.09 THR 4 -0.06 VAL 33

GLY 29 0.10 ASN 5 -0.07 VAL 33

GLY 29 0.12 LEU 6 -0.07 VAL 33

GLY 29 0.11 LYS 7 -0.09 VAL 33

GLY 29 0.08 ASP 8 -0.09 VAL 33

GLY 29 0.09 VAL 9 -0.09 VAL 33

GLY 29 0.12 LEU 10 -0.10 VAL 33

GLY 29 0.09 ALA 11 -0.11 VAL 33

GLY 29 0.06 SER 12 -0.12 VAL 33

GLY 29 0.08 LEU 13 -0.13 VAL 33

GLY 29 0.10 ILE 14 -0.14 VAL 33

PRO 422 0.07 PRO 15 -0.14 VAL 33

ALA 1 0.09 LYS 16 -0.16 VAL 33

THR 98 0.10 GLU 17 -0.18 VAL 33

GLY 29 0.09 GLN 18 -0.18 VAL 33

PRO 422 0.11 ALA 19 -0.15 VAL 33

GLY 99 0.10 ARG 20 -0.18 VAL 33

GLU 54 0.18 ILE 21 -0.23 VAL 33

PRO 422 0.17 LYS 22 -0.17 VAL 33

PRO 422 0.20 THR 23 -0.08 VAL 33

PRO 422 0.22 PHE 24 -0.11 VAL 33

ILE 52 0.30 ARG 25 -0.14 VAL 33

PRO 422 0.34 GLN 26 -0.07 GLY 29

PRO 422 0.34 GLN 27 -0.08 GLY 29

PRO 422 0.38 HIS 28 -0.08 PHE 24

PRO 422 0.50 GLY 29 -0.08 GLN 27

PRO 422 0.62 ASN 30 -0.01 ARG 20

PRO 422 0.42 THR 31 -0.10 ARG 20

PRO 422 0.37 ALA 32 -0.13 ILE 21

ASP 61 0.09 VAL 33 -0.23 ILE 21

ALA 367 0.09 GLY 34 -0.16 ILE 21

ALA 367 0.11 GLN 35 -0.14 ILE 21

LYS 366 0.13 ILE 36 -0.12 PRO 418

GLY 365 0.15 THR 37 -0.09 PRO 418

GLY 365 0.20 VAL 38 -0.12 PRO 422

GLY 365 0.23 ASP 39 -0.13 PRO 422

LYS 366 0.21 MET 40 -0.16 PRO 422

LYS 366 0.23 SER 41 -0.24 PRO 422

LYS 366 0.29 TYR 42 -0.24 PRO 422

LYS 366 0.30 GLY 43 -0.19 PRO 422

LYS 366 0.23 GLY 44 -0.21 PRO 422

ASN 30 0.24 MET 45 -0.17 PRO 422

ASN 30 0.19 ARG 46 -0.11 PRO 422

GLY 29 0.18 GLY 47 -0.12 GLY 312

ASN 30 0.25 MET 48 -0.08 GLY 312

GLY 29 0.31 LYS 49 -0.08 LEU 415

ASN 30 0.46 GLY 50 -0.10 PRO 418

GLY 29 0.46 LEU 51 -0.11 PHE 417

GLY 29 0.49 ILE 52 -0.14 VAL 33

GLY 29 0.37 TYR 53 -0.10 VAL 33

GLY 29 0.32 GLU 54 -0.09 VAL 33

GLY 29 0.26 THR 55 -0.06 VAL 33

GLY 29 0.26 SER 56 -0.05 ASN 359

GLY 29 0.26 VAL 57 -0.07 LEU 58

GLY 29 0.23 LEU 58 -0.08 ASN 310

GLY 29 0.19 ASP 59 -0.11 ASN 310

GLY 29 0.18 PRO 60 -0.14 ASN 310

GLY 29 0.15 ASP 61 -0.16 LEU 362

GLY 29 0.15 GLU 62 -0.14 LEU 362

GLY 29 0.18 GLY 63 -0.11 LEU 362

GLY 29 0.20 ILE 64 -0.09 LEU 362

GLY 29 0.20 ARG 65 -0.09 LEU 362

GLY 29 0.21 PHE 66 -0.07 ASN 359

GLY 29 0.20 ARG 67 -0.08 ASN 359

GLY 29 0.19 GLY 68 -0.10 LEU 362

GLY 29 0.17 PHE 69 -0.10 ASN 359

GLY 29 0.16 SER 70 -0.11 ASN 359

GLY 29 0.16 ILE 71 -0.11 ASN 359

GLY 29 0.14 PRO 72 -0.13 ASN 359

GLY 29 0.14 GLU 73 -0.12 ASN 359

GLY 29 0.15 CYS 74 -0.10 LYS 355

GLY 29 0.14 GLN 75 -0.11 LYS 355

GLY 29 0.13 LYS 76 -0.11 LYS 355

GLY 29 0.13 LEU 77 -0.10 ASN 359

GLY 29 0.13 LEU 78 -0.09 LYS 355

GLY 29 0.12 PRO 79 -0.08 LYS 355

GLY 29 0.12 LYS 80 -0.08 LYS 355

GLY 29 0.12 ALA 81 -0.07 LYS 355

GLY 29 0.10 GLY 82 -0.07 LYS 355

GLY 29 0.11 GLY 84 -0.09 LYS 355

GLY 29 0.12 GLU 85 -0.11 LYS 355

GLY 29 0.13 GLU 86 -0.09 LYS 355

GLY 29 0.14 PRO 87 -0.09 LYS 355

GLY 29 0.14 LEU 88 -0.07 LYS 355

GLY 29 0.16 PRO 89 -0.06 LYS 355

GLY 29 0.15 GLU 90 -0.05 LYS 355

GLY 29 0.15 GLY 91 -0.07 LYS 355

GLY 29 0.17 LEU 92 -0.07 LYS 355

GLY 29 0.18 PHE 93 -0.05 LYS 355

GLY 29 0.16 TRP 94 -0.06 LYS 355

GLY 29 0.17 LEU 95 -0.06 LYS 355

GLY 29 0.20 LEU 96 -0.06 LYS 355

GLY 29 0.19 VAL 97 -0.07 VAL 33

GLY 29 0.16 THR 98 -0.07 VAL 33

GLY 29 0.18 GLY 99 -0.06 ASN 359

GLY 29 0.15 GLN 100 -0.07 ASN 359

GLY 29 0.13 ILE 101 -0.08 ASN 359

GLY 29 0.13 PRO 102 -0.07 LYS 355

GLY 29 0.11 THR 103 -0.07 LYS 355

GLY 29 0.11 PRO 104 -0.07 LYS 355

GLY 29 0.10 GLU 105 -0.06 LYS 355

GLY 29 0.11 GLN 106 -0.06 LYS 355

GLY 29 0.12 VAL 107 -0.06 LYS 355

GLY 29 0.11 SER 108 -0.05 LYS 355

GLY 29 0.11 TRP 109 -0.05 LYS 355

GLY 29 0.13 VAL 110 -0.04 LYS 355

GLY 29 0.13 SER 111 -0.04 LYS 355

GLY 29 0.12 LYS 112 -0.04 LYS 355

GLY 29 0.12 GLU 113 -0.04 VAL 33

GLY 29 0.13 TRP 114 -0.04 VAL 33

GLY 29 0.12 ALA 115 -0.03 VAL 33

SER 311 0.12 LYS 116 -0.04 VAL 33

GLY 29 0.12 ARG 117 -0.05 VAL 33

SER 311 0.14 ALA 118 -0.04 VAL 33

SER 311 0.15 ALA 119 -0.04 PRO 422

SER 311 0.17 LEU 120 -0.05 PRO 422

SER 311 0.17 PRO 121 -0.05 PRO 422

SER 311 0.19 SER 122 -0.05 PRO 422

SER 311 0.20 HIS 123 -0.06 PRO 422

SER 311 0.20 VAL 124 -0.07 PRO 422

SER 311 0.21 VAL 125 -0.06 PRO 422

SER 311 0.22 THR 126 -0.07 PRO 422

SER 311 0.24 MET 127 -0.08 PRO 422

SER 311 0.24 LEU 128 -0.08 PRO 422

SER 311 0.25 ASP 129 -0.07 PRO 422

SER 311 0.27 ASN 130 -0.08 PRO 422

SER 311 0.29 PHE 131 -0.09 PRO 422

SER 311 0.33 PRO 132 -0.09 PRO 422

SER 311 0.35 THR 133 -0.09 PRO 422

SER 311 0.39 ASN 134 -0.10 PRO 422

SER 311 0.36 LEU 135 -0.11 PRO 422

SER 311 0.35 HIS 136 -0.11 PRO 422

SER 311 0.29 PRO 137 -0.10 PRO 422

SER 311 0.27 MET 138 -0.12 PRO 422

SER 311 0.28 SER 139 -0.12 PRO 422

SER 311 0.27 GLN 140 -0.10 PRO 422

SER 311 0.23 LEU 141 -0.10 PRO 422

SER 311 0.22 SER 142 -0.11 PRO 422

SER 311 0.23 ALA 143 -0.11 PRO 422

SER 311 0.21 ALA 144 -0.09 PRO 422

SER 311 0.19 ILE 145 -0.09 PRO 422

SER 311 0.19 THR 146 -0.09 PRO 422

SER 311 0.19 ALA 147 -0.08 PRO 422

SER 311 0.17 LEU 148 -0.07 PRO 422

ASN 30 0.16 ASN 149 -0.06 PRO 422

SER 311 0.15 SER 150 -0.05 PRO 422

ASN 30 0.14 GLU 151 -0.05 VAL 33

ASN 30 0.16 SER 152 -0.06 VAL 33

ASN 30 0.15 ASN 153 -0.07 VAL 33

ASN 30 0.16 PHE 154 -0.08 VAL 33

ASN 30 0.17 ALA 155 -0.07 VAL 33

ASN 30 0.15 ARG 156 -0.07 VAL 33

ASN 30 0.14 ALA 157 -0.08 VAL 33

ASN 30 0.16 TYR 158 -0.08 VAL 33

ASN 30 0.16 ALA 159 -0.07 VAL 33

ASN 30 0.14 GLU 160 -0.07 VAL 33

ASN 30 0.14 GLY 161 -0.08 VAL 33

ASN 30 0.14 ILE 162 -0.09 VAL 33

ASN 30 0.13 ASN 163 -0.11 VAL 33

ASN 30 0.16 ARG 164 -0.12 VAL 33

ASN 30 0.13 THR 165 -0.13 VAL 33

ASN 30 0.13 LYS 166 -0.11 VAL 33

ASN 30 0.16 TYR 167 -0.11 VAL 33

GLY 29 0.16 TRP 168 -0.11 VAL 33

ASN 30 0.13 GLU 169 -0.10 VAL 33

ASN 30 0.15 PHE 170 -0.09 VAL 33

GLY 29 0.17 VAL 171 -0.09 VAL 33

GLY 29 0.16 TYR 172 -0.08 VAL 33

GLY 29 0.14 GLU 173 -0.07 VAL 33

GLY 29 0.16 ASP 174 -0.07 VAL 33

GLY 29 0.17 ALA 175 -0.06 VAL 33

GLY 29 0.15 MET 176 -0.06 VAL 33

GLY 29 0.14 ASP 177 -0.05 VAL 33

GLY 29 0.16 LEU 178 -0.05 VAL 33

GLY 29 0.16 ILE 179 -0.04 VAL 33

GLY 29 0.14 ALA 180 -0.04 VAL 33

SER 311 0.15 LYS 181 -0.05 PRO 422

SER 311 0.16 LEU 182 -0.06 PRO 422

SER 311 0.16 PRO 183 -0.06 PRO 422

SER 311 0.18 CYS 184 -0.06 PRO 422

SER 311 0.20 VAL 185 -0.07 PRO 422

SER 311 0.20 ALA 186 -0.07 PRO 422

SER 311 0.20 ALA 187 -0.07 PRO 422

SER 311 0.22 LYS 188 -0.07 PRO 422

SER 311 0.24 ILE 189 -0.08 PRO 422

SER 311 0.24 TYR 190 -0.08 PRO 422

SER 311 0.23 ARG 191 -0.07 PRO 422

SER 311 0.26 ASN 192 -0.08 PRO 422

SER 311 0.29 LEU 193 -0.08 PRO 422

SER 311 0.27 TYR 194 -0.08 GLY 386

SER 311 0.25 ARG 195 -0.07 PRO 422

SER 311 0.25 ALA 196 -0.07 PRO 422

SER 311 0.24 GLY 197 -0.07 PRO 422

SER 311 0.22 SER 198 -0.06 PRO 422

SER 311 0.20 SER 199 -0.06 PRO 422

SER 311 0.19 ILE 200 -0.05 PRO 422

SER 311 0.17 GLY 201 -0.05 PRO 422

SER 311 0.16 ALA 202 -0.04 PRO 422

SER 311 0.14 ILE 203 -0.03 PRO 422

SER 311 0.13 ASP 204 -0.03 LYS 355

SER 311 0.12 SER 205 -0.03 LYS 355

GLY 29 0.11 LYS 206 -0.04 LYS 355

GLY 29 0.11 LEU 207 -0.04 LYS 355

GLY 29 0.13 ASP 208 -0.05 LYS 355

GLY 29 0.14 TRP 209 -0.04 LYS 355

GLY 29 0.14 SER 210 -0.04 LYS 355

GLY 29 0.13 HIS 211 -0.04 LYS 355

SER 311 0.14 ASN 212 -0.03 PRO 422

SER 311 0.16 PHE 213 -0.04 PRO 422

SER 311 0.16 THR 214 -0.04 PRO 422

SER 311 0.16 ASN 215 -0.04 PRO 422

SER 311 0.18 MET 216 -0.05 PRO 422

SER 311 0.19 LEU 217 -0.05 PRO 422

SER 311 0.19 GLY 218 -0.05 PRO 422

SER 311 0.17 TYR 219 -0.05 PRO 422

SER 311 0.14 THR 220 -0.05 LYS 339

SER 311 0.12 ASP 221 -0.07 LYS 339

GLY 29 0.11 PRO 222 -0.07 LYS 339

GLY 29 0.11 GLN 223 -0.09 LYS 339

GLY 29 0.12 PHE 224 -0.06 LYS 339

GLY 29 0.13 THR 225 -0.05 LYS 355

GLY 29 0.13 GLU 226 -0.07 LYS 355

GLY 29 0.13 LEU 227 -0.06 LYS 355

GLY 29 0.14 MET 228 -0.05 LYS 355

GLY 29 0.14 ARG 229 -0.06 LYS 355

GLY 29 0.15 LEU 230 -0.07 LYS 355

GLY 29 0.16 TYR 231 -0.05 LYS 355

GLY 29 0.16 LEU 232 -0.05 LYS 355

GLY 29 0.17 THR 233 -0.06 LYS 355

GLY 29 0.17 ILE 234 -0.07 LYS 355

GLY 29 0.19 HIS 235 -0.05 PRO 422

GLY 29 0.20 SER 236 -0.04 LYS 355

GLY 29 0.23 ASP 237 -0.04 ASP 327

GLY 29 0.24 HIS 238 -0.05 ASP 327

GLY 29 0.28 GLU 239 -0.05 LEU 288

GLY 29 0.32 GLY 240 -0.04 LEU 288

GLY 29 0.30 GLY 241 -0.06 PRO 422

GLY 29 0.26 ASN 242 -0.10 PRO 422

GLY 29 0.24 VAL 243 -0.16 PRO 422

GLY 29 0.24 SER 244 -0.13 PRO 422

GLY 29 0.27 ALA 245 -0.08 PRO 422

GLY 29 0.29 HIS 246 -0.12 PRO 422

ASN 30 0.26 THR 247 -0.16 PRO 422

GLY 29 0.26 SER 248 -0.10 PRO 422

GLY 29 0.30 HIS 249 -0.07 VAL 33

ASN 30 0.31 LEU 250 -0.13 PRO 422

ASN 30 0.27 VAL 251 -0.12 PRO 422

ASN 30 0.26 GLY 252 -0.08 VAL 33

ASN 30 0.30 SER 253 -0.10 VAL 33

ASN 30 0.28 ALA 254 -0.08 VAL 33

ASN 30 0.23 LEU 255 -0.09 VAL 33

ASN 30 0.22 SER 256 -0.07 VAL 33

ASN 30 0.20 ASP 257 -0.07 VAL 33

ASN 30 0.20 PRO 258 -0.06 VAL 33

ASN 30 0.18 TYR 259 -0.07 PRO 422

ASN 30 0.20 LEU 260 -0.09 PRO 422

ASN 30 0.22 SER 261 -0.10 PRO 422

GLY 29 0.21 PHE 262 -0.09 PRO 422

ASN 30 0.19 ALA 263 -0.11 PRO 422

ASN 30 0.22 ALA 264 -0.14 PRO 422

GLY 29 0.22 ALA 265 -0.13 PRO 422

GLY 29 0.20 MET 266 -0.12 PRO 422

ARG 313 0.21 ASN 267 -0.16 PRO 422

ASN 30 0.21 GLY 268 -0.17 PRO 422

GLY 29 0.20 LEU 269 -0.13 PRO 422

ARG 313 0.25 ALA 270 -0.14 PRO 422

ARG 313 0.28 GLY 271 -0.16 PRO 422

ARG 313 0.36 PRO 272 -0.15 PRO 422

LYS 366 0.29 LEU 273 -0.14 PRO 422

LYS 366 0.23 HIS 274 -0.14 PRO 422

ARG 313 0.18 GLY 275 -0.12 PRO 422

ARG 313 0.26 LEU 276 -0.13 PRO 422

ARG 313 0.24 ALA 277 -0.12 PRO 422

SER 311 0.20 ASN 278 -0.10 PRO 422

SER 311 0.27 GLN 279 -0.10 PRO 422

SER 311 0.32 GLU 280 -0.11 PRO 422

SER 311 0.22 VAL 281 -0.10 PRO 422

SER 311 0.25 LEU 282 -0.09 PRO 422

SER 311 0.35 LEU 283 -0.10 PRO 422

THR 308 0.33 TRP 284 -0.11 PRO 422

SER 311 0.21 LEU 285 -0.09 PRO 422

SER 311 0.20 SER 286 -0.09 PRO 422

SER 311 0.21 GLN 287 -0.16 VAL 315

THR 388 0.13 LEU 288 -0.24 VAL 315

GLY 386 0.14 GLN 289 -0.16 VAL 315

THR 388 0.19 LYS 290 -0.16 VAL 315

TYR 194 0.14 ASP 291 -0.18 VAL 315

GLY 29 0.09 ASP 295 -0.06 VAL 315

GLY 29 0.09 ALA 296 -0.07 VAL 315

TRP 284 0.09 SER 297 -0.08 PRO 342

TRP 284 0.11 ASP 298 -0.11 PRO 342

TRP 284 0.14 GLU 299 -0.08 LEU 338

TRP 284 0.17 LYS 300 -0.05 THR 331

TRP 284 0.19 LEU 301 -0.06 THR 331

TRP 284 0.20 ARG 302 -0.08 THR 331

TRP 284 0.22 ASP 303 -0.07 ALA 367

TRP 284 0.29 TYR 304 -0.08 ALA 367

TRP 284 0.29 ILE 305 -0.10 PRO 370

TRP 284 0.24 TRP 306 -0.12 ALA 367

TRP 284 0.30 ASN 307 -0.16 ALA 367

TRP 284 0.33 THR 308 -0.16 ALA 367

ASN 134 0.24 LEU 309 -0.27 ALA 367

ASN 134 0.31 ASN 310 -0.31 ALA 367

ASN 134 0.39 SER 311 -0.24 ALA 367

ASN 134 0.36 GLY 312 -0.33 ALA 367

PRO 272 0.36 ARG 313 -0.17 ALA 367

PRO 272 0.26 VAL 314 -0.16 LEU 288

GLN 364 0.24 VAL 315 -0.24 LEU 288

VAL 360 0.22 PRO 316 -0.12 LEU 288

GLY 29 0.14 GLY 317 -0.10 LEU 288

GLY 29 0.15 TYR 318 -0.14 LEU 288

GLY 29 0.16 GLY 319 -0.16 GLY 312

GLY 29 0.18 HIS 320 -0.13 GLY 312

GLY 29 0.20 ALA 321 -0.14 GLY 312

GLY 29 0.20 VAL 322 -0.13 GLY 312

GLY 29 0.17 LEU 323 -0.13 GLY 312

GLY 29 0.15 ARG 324 -0.18 GLY 312

GLY 29 0.14 LYS 325 -0.17 LEU 362

GLY 29 0.14 THR 326 -0.13 ASN 310

GLY 29 0.15 ASP 327 -0.09 ASN 310

GLY 29 0.16 PRO 328 -0.12 ASN 359

GLY 29 0.17 ARG 329 -0.09 LYS 355

GLY 29 0.15 TYR 330 -0.10 TYR 354

GLY 29 0.14 THR 331 -0.17 LYS 355

GLY 29 0.15 CYS 332 -0.14 LYS 355

GLY 29 0.14 GLN 333 -0.11 LYS 355

GLY 29 0.13 ARG 334 -0.14 LYS 355

GLY 29 0.13 GLU 335 -0.15 LYS 355

GLY 29 0.13 PHE 336 -0.11 LYS 355

GLY 29 0.12 ALA 337 -0.10 LYS 355

GLY 29 0.12 LEU 338 -0.13 LYS 355

GLY 29 0.12 LYS 339 -0.11 LYS 355

GLY 29 0.12 HIS 340 -0.08 LYS 355

GLY 29 0.11 LEU 341 -0.07 LYS 355

GLY 29 0.11 PRO 342 -0.11 ASP 298

GLY 29 0.11 SER 343 -0.08 ASP 298

GLY 29 0.11 ASP 344 -0.05 PRO 422

GLY 29 0.11 PRO 345 -0.06 PRO 422

GLY 29 0.11 MET 346 -0.06 PRO 422

GLY 29 0.12 PHE 347 -0.05 PRO 422

GLY 29 0.11 LYS 348 -0.08 ASP 298

GLY 29 0.11 LEU 349 -0.07 VAL 315

GLY 29 0.12 VAL 350 -0.08 LEU 288

GLY 29 0.12 ALA 351 -0.12 GLN 352

GLY 29 0.10 GLN 352 -0.12 ALA 351

GLY 29 0.11 LEU 353 -0.09 THR 331

GLY 29 0.11 TYR 354 -0.15 THR 331

SER 424 0.10 LYS 355 -0.17 THR 331

PRO 316 0.13 ILE 356 -0.12 THR 331

PRO 316 0.18 VAL 357 -0.11 ASN 310

GLY 43 0.12 PRO 358 -0.16 ASN 310

TYR 42 0.15 ASN 359 -0.14 THR 331

PRO 316 0.22 VAL 360 -0.15 ASN 310

PRO 316 0.19 LEU 361 -0.23 ASN 310

TYR 42 0.18 LEU 362 -0.19 ASN 310

TYR 42 0.20 GLU 363 -0.17 ASN 310

PRO 272 0.26 GLN 364 -0.24 ASN 310

TYR 42 0.27 GLY 365 -0.22 ASN 310

GLY 43 0.30 LYS 366 -0.30 ASN 310

GLY 43 0.24 ALA 367 -0.33 GLY 312

GLY 43 0.18 LYS 368 -0.27 GLY 312

GLY 29 0.14 ASN 369 -0.22 GLY 312

GLY 29 0.13 PRO 370 -0.23 ASN 310

GLY 29 0.13 TRP 371 -0.16 ASN 310

GLY 29 0.14 PRO 372 -0.10 LEU 309

GLY 29 0.16 ASN 373 -0.08 LEU 288

GLY 29 0.16 VAL 374 -0.06 PRO 422

GLY 29 0.16 ASP 375 -0.08 PRO 422

GLY 29 0.14 ALA 376 -0.08 LEU 288

GLY 29 0.14 HIS 377 -0.06 PRO 422

GLY 29 0.14 SER 378 -0.07 PRO 422

SER 311 0.17 GLY 379 -0.08 PRO 422

SER 311 0.14 VAL 380 -0.07 PRO 422

GLY 29 0.13 LEU 381 -0.06 PRO 422

SER 311 0.16 LEU 382 -0.07 PRO 422

SER 311 0.18 GLN 383 -0.07 PRO 422

SER 311 0.14 TYR 384 -0.06 PRO 422

SER 311 0.15 TYR 385 -0.06 PRO 422

LYS 290 0.19 GLY 386 -0.08 TYR 194

SER 311 0.20 MET 387 -0.08 PRO 422

SER 311 0.23 THR 388 -0.08 PRO 422

SER 311 0.26 GLU 389 -0.09 PRO 422

SER 311 0.27 MET 390 -0.09 PRO 422

SER 311 0.30 ASN 391 -0.11 PRO 422

SER 311 0.25 TYR 392 -0.10 PRO 422

SER 311 0.22 TYR 393 -0.09 PRO 422

SER 311 0.22 THR 394 -0.10 PRO 422

SER 311 0.21 VAL 395 -0.09 PRO 422

SER 311 0.17 LEU 396 -0.08 PRO 422

GLY 29 0.17 PHE 397 -0.08 PRO 422

GLY 29 0.18 GLY 398 -0.09 PRO 422

GLY 29 0.17 VAL 399 -0.07 PRO 422

GLY 29 0.18 SER 400 -0.06 PRO 422

GLY 29 0.20 ARG 401 -0.06 PRO 422

GLY 29 0.20 ALA 402 -0.06 PRO 422

GLY 29 0.20 LEU 403 -0.04 VAL 33

GLY 29 0.23 GLY 404 -0.04 VAL 33

GLY 29 0.24 VAL 405 -0.05 VAL 33

GLY 29 0.22 LEU 406 -0.06 VAL 33

GLY 29 0.22 ALA 407 -0.07 VAL 33

GLY 29 0.27 GLN 408 -0.09 VAL 33

GLY 29 0.25 LEU 409 -0.09 VAL 33

GLY 29 0.21 ILE 410 -0.10 VAL 33

GLY 29 0.24 TRP 411 -0.12 VAL 33

GLY 29 0.29 SER 412 -0.13 VAL 33

GLY 29 0.23 ARG 413 -0.13 VAL 33

GLY 29 0.19 ALA 414 -0.14 VAL 33

GLY 29 0.22 LEU 415 -0.18 VAL 33

GLY 29 0.25 GLY 416 -0.16 VAL 33

GLY 29 0.35 PHE 417 -0.17 VAL 33

ASN 30 0.34 PRO 418 -0.16 VAL 33

ASN 30 0.36 LEU 419 -0.11 VAL 33

ASN 30 0.42 GLU 420 -0.09 ILE 36

ASN 30 0.48 ARG 421 -0.09 SER 41

ASN 30 0.62 PRO 422 -0.24 SER 41

ASN 30 0.37 LYS 423 -0.14 SER 424

ASN 30 0.28 SER 424 -0.14 LYS 423

ASN 30 0.24 MET 425 -0.10 VAL 38

LYS 366 0.21 SER 426 -0.04 GLY 429

GLY 365 0.18 THR 427 -0.04 PRO 422

ASN 30 0.17 ALA 428 -0.03 ASP 39

LYS 423 0.20 GLY 429 -0.07 VAL 38

ASN 30 0.19 LEU 430 -0.08 VAL 38

ASN 30 0.16 GLU 431 -0.08 SER 311

LYS 423 0.19 LYS 432 -0.08 ASP 39

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

K. Suhre & Y.H. Sanejouand, ElNemo: a normal mode web-server for protein movement analysis and the generation of templates for molecular replacement. Nucleic Acids Research, 32, W610-W614, 2004.
K. Suhre & Y.H. Sanejouand, On the potential of normal mode analysis for solving difficult molecular replacement problems. Acta Cryst. D vol.60, p796-799, 2004 © International Union of Crystallography.

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.

Should you encounter any unexpected behaviour, please let us know. elNémo has been relocated. **Some cleaning from time to time** Sorry for the inconvenience.

*** 6csc_aligned_close ***

CA distance fluctuations for 2604241133101949041

--- normal mode 14 ---

Should you encounter any unexpected behaviour,
please let us know.
elNémo has been relocated.
Some cleaning from time to time
Sorry for the inconvenience.

* 6csc_aligned_close *