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 9 ---

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
LYS 432 0.10 ALA 1 -0.08 THR 23

LYS 432 0.10 SER 2 -0.06 ARG 20

LYS 432 0.10 SER 3 -0.05 THR 427

LYS 432 0.10 THR 4 -0.05 THR 427

LYS 432 0.11 ASN 5 -0.05 THR 427

LYS 432 0.12 LEU 6 -0.06 THR 427

LYS 432 0.13 LYS 7 -0.06 THR 427

LYS 432 0.13 ASP 8 -0.05 THR 427

LYS 432 0.13 VAL 9 -0.05 SER 426

LYS 432 0.14 LEU 10 -0.06 SER 426

LYS 432 0.15 ALA 11 -0.06 SER 426

LYS 432 0.15 SER 12 -0.08 SER 424

LYS 432 0.15 LEU 13 -0.09 SER 424

LYS 432 0.17 ILE 14 -0.10 SER 424

LYS 432 0.17 PRO 15 -0.14 SER 424

LYS 432 0.17 LYS 16 -0.15 SER 424

LYS 432 0.17 GLU 17 -0.16 SER 424

LYS 432 0.19 GLN 18 -0.19 SER 424

LYS 432 0.19 ALA 19 -0.21 SER 424

LYS 432 0.18 ARG 20 -0.23 SER 424

LYS 432 0.19 ILE 21 -0.25 SER 424

LYS 432 0.22 LYS 22 -0.29 PRO 422

LYS 432 0.21 THR 23 -0.28 SER 424

LYS 432 0.20 PHE 24 -0.31 SER 424

LYS 432 0.23 ARG 25 -0.34 SER 424

LYS 432 0.26 GLN 26 -0.35 PRO 422

LYS 432 0.23 GLN 27 -0.34 SER 424

LYS 432 0.22 HIS 28 -0.40 SER 424

LYS 432 0.27 GLY 29 -0.43 SER 424

LYS 432 0.30 ASN 30 -0.48 SER 424

LYS 432 0.21 THR 31 -0.47 SER 424

GLU 431 0.19 ALA 32 -0.54 SER 424

LYS 423 0.18 VAL 33 -0.50 SER 424

LYS 423 0.22 GLY 34 -0.59 SER 424

LYS 423 0.33 GLN 35 -0.59 SER 424

LYS 423 0.50 ILE 36 -0.60 SER 424

LYS 423 0.62 THR 37 -0.35 SER 424

LYS 423 0.75 VAL 38 -0.20 LYS 366

LYS 423 0.83 ASP 39 -0.24 LYS 366

LYS 423 0.94 MET 40 -0.14 LYS 366

LYS 423 1.23 SER 41 -0.24 THR 427

LYS 423 1.13 TYR 42 -0.19 LYS 366

LYS 423 1.03 GLY 43 -0.16 ALA 367

LYS 423 1.15 GLY 44 -0.16 THR 427

LYS 423 1.08 MET 45 -0.17 THR 427

LYS 423 0.85 ARG 46 -0.09 THR 427

LYS 423 0.65 GLY 47 -0.20 SER 424

LYS 423 0.63 MET 48 -0.36 SER 424

LYS 423 0.48 LYS 49 -0.36 SER 424

LYS 423 0.45 GLY 50 -0.40 SER 424

LYS 423 0.41 LEU 51 -0.24 SER 424

LYS 423 0.27 ILE 52 -0.21 SER 424

LYS 423 0.30 TYR 53 -0.13 PHE 24

LYS 423 0.23 GLU 54 -0.15 ILE 21

LYS 423 0.26 THR 55 -0.13 PHE 24

LYS 423 0.32 SER 56 -0.14 PHE 24

LYS 423 0.36 VAL 57 -0.16 PHE 24

LYS 423 0.41 LEU 58 -0.14 PHE 24

LYS 423 0.39 ASP 59 -0.14 PHE 24

LYS 423 0.44 PRO 60 -0.12 PHE 24

LYS 423 0.39 ASP 61 -0.13 GLN 27

LYS 423 0.35 GLU 62 -0.13 GLN 27

LYS 423 0.38 GLY 63 -0.12 PHE 24

LYS 423 0.37 ILE 64 -0.13 PHE 24

LYS 423 0.31 ARG 65 -0.14 PHE 24

LYS 423 0.28 PHE 66 -0.13 PHE 24

LYS 423 0.23 ARG 67 -0.15 PHE 24

LYS 423 0.24 GLY 68 -0.16 PHE 24

LYS 423 0.25 PHE 69 -0.14 PHE 24

LYS 423 0.28 SER 70 -0.12 PHE 24

LYS 423 0.29 ILE 71 -0.11 PHE 24

LYS 423 0.26 PRO 72 -0.10 PHE 24

LYS 423 0.24 GLU 73 -0.11 PHE 24

LYS 423 0.24 CYS 74 -0.10 PHE 24

LYS 423 0.24 GLN 75 -0.09 PHE 24

LYS 423 0.22 LYS 76 -0.09 PHE 24

LYS 423 0.20 LEU 77 -0.09 PHE 24

LYS 423 0.20 LEU 78 -0.08 PHE 24

PRO 422 0.19 PRO 79 -0.07 PHE 24

PRO 422 0.21 LYS 80 -0.07 PHE 24

PRO 422 0.21 ALA 81 -0.06 PHE 24

PRO 422 0.19 GLY 82 -0.05 PHE 24

PRO 422 0.22 GLY 84 -0.06 PHE 24

PRO 422 0.22 GLU 85 -0.07 PHE 24

PRO 422 0.25 GLU 86 -0.07 PHE 24

PRO 422 0.24 PRO 87 -0.08 PHE 24

PRO 422 0.24 LEU 88 -0.07 PHE 24

PRO 422 0.27 PRO 89 -0.07 PHE 24

PRO 422 0.23 GLU 90 -0.06 THR 427

PRO 422 0.21 GLY 91 -0.07 ARG 20

PRO 422 0.24 LEU 92 -0.08 ARG 20

PRO 422 0.24 PHE 93 -0.08 ARG 20

PRO 422 0.18 TRP 94 -0.08 ARG 20

LYS 423 0.19 LEU 95 -0.10 ARG 20

LYS 423 0.21 LEU 96 -0.11 ARG 20

LYS 423 0.17 VAL 97 -0.10 ARG 20

LYS 423 0.14 THR 98 -0.11 ARG 20

LYS 423 0.17 GLY 99 -0.14 ARG 20

LYS 423 0.15 GLN 100 -0.12 ARG 20

LYS 423 0.17 ILE 101 -0.10 ARG 20

LYS 423 0.15 PRO 102 -0.08 ARG 20

LYS 423 0.14 THR 103 -0.07 ARG 20

PRO 422 0.15 PRO 104 -0.06 ARG 20

PRO 422 0.13 GLU 105 -0.05 ARG 20

PRO 422 0.13 GLN 106 -0.06 ARG 20

PRO 422 0.17 VAL 107 -0.06 ARG 20

PRO 422 0.16 SER 108 -0.06 THR 427

PRO 422 0.15 TRP 109 -0.06 THR 427

PRO 422 0.18 VAL 110 -0.06 THR 427

PRO 422 0.20 SER 111 -0.06 THR 427

PRO 422 0.17 LYS 112 -0.06 THR 427

PRO 422 0.17 GLU 113 -0.06 THR 427

PRO 422 0.21 TRP 114 -0.07 THR 427

PRO 422 0.21 ALA 115 -0.06 THR 427

PRO 422 0.18 LYS 116 -0.06 THR 427

PRO 422 0.20 ARG 117 -0.07 THR 427

PRO 422 0.23 ALA 118 -0.07 THR 427

PRO 422 0.23 ALA 119 -0.07 THR 427

PRO 422 0.25 LEU 120 -0.07 THR 427

PRO 422 0.23 PRO 121 -0.07 THR 427

PRO 422 0.23 SER 122 -0.07 THR 427

PRO 422 0.25 HIS 123 -0.08 THR 427

PRO 422 0.29 VAL 124 -0.08 THR 427

PRO 422 0.28 VAL 125 -0.08 THR 427

PRO 422 0.27 THR 126 -0.08 THR 427

PRO 422 0.31 MET 127 -0.08 THR 427

PRO 422 0.33 LEU 128 -0.08 THR 427

PRO 422 0.30 ASP 129 -0.08 THR 427

PRO 422 0.31 ASN 130 -0.08 THR 427

PRO 422 0.35 PHE 131 -0.09 THR 427

PRO 422 0.35 PRO 132 -0.08 THR 427

PRO 422 0.36 THR 133 -0.08 THR 427

PRO 422 0.39 ASN 134 -0.09 GLU 431

PRO 422 0.42 LEU 135 -0.09 THR 427

PRO 422 0.45 HIS 136 -0.10 THR 427

PRO 422 0.44 PRO 137 -0.09 THR 427

PRO 422 0.49 MET 138 -0.10 THR 427

PRO 422 0.48 SER 139 -0.11 THR 427

PRO 422 0.42 GLN 140 -0.10 THR 427

PRO 422 0.43 LEU 141 -0.10 THR 427

PRO 422 0.48 SER 142 -0.11 THR 427

PRO 422 0.42 ALA 143 -0.10 THR 427

PRO 422 0.37 ALA 144 -0.09 THR 427

PRO 422 0.38 ILE 145 -0.10 THR 427

PRO 422 0.38 THR 146 -0.10 THR 427

PRO 422 0.32 ALA 147 -0.09 THR 427

PRO 422 0.29 LEU 148 -0.09 THR 427

PRO 422 0.27 ASN 149 -0.09 THR 427

PRO 422 0.22 SER 150 -0.08 THR 427

PRO 422 0.20 GLU 151 -0.08 THR 427

PRO 422 0.19 SER 152 -0.08 THR 427

LYS 432 0.16 ASN 153 -0.07 THR 427

LYS 432 0.17 PHE 154 -0.08 THR 427

LYS 432 0.18 ALA 155 -0.08 THR 427

LYS 432 0.18 ARG 156 -0.07 THR 427

LYS 432 0.19 ALA 157 -0.07 THR 427

LYS 432 0.21 TYR 158 -0.08 LYS 423

LYS 432 0.21 ALA 159 -0.10 LYS 423

LYS 432 0.21 GLU 160 -0.11 LYS 423

LYS 432 0.23 GLY 161 -0.15 LYS 423

LYS 432 0.22 ILE 162 -0.12 LYS 423

LYS 432 0.23 ASN 163 -0.15 LYS 423

LYS 432 0.24 ARG 164 -0.15 PRO 422

LYS 432 0.22 THR 165 -0.13 PRO 422

LYS 432 0.20 LYS 166 -0.07 SER 426

LYS 432 0.20 TYR 167 -0.07 THR 427

LYS 432 0.18 TRP 168 -0.07 THR 427

LYS 432 0.17 GLU 169 -0.07 THR 427

LYS 432 0.16 PHE 170 -0.07 THR 427

LYS 432 0.16 VAL 171 -0.08 THR 427

LYS 432 0.14 TYR 172 -0.07 THR 427

PRO 422 0.15 GLU 173 -0.07 THR 427

PRO 422 0.20 ASP 174 -0.08 THR 427

PRO 422 0.24 ALA 175 -0.08 THR 427

PRO 422 0.21 MET 176 -0.07 THR 427

PRO 422 0.23 ASP 177 -0.08 THR 427

PRO 422 0.29 LEU 178 -0.08 THR 427

PRO 422 0.29 ILE 179 -0.08 THR 427

PRO 422 0.26 ALA 180 -0.07 THR 427

PRO 422 0.28 LYS 181 -0.08 THR 427

PRO 422 0.34 LEU 182 -0.08 THR 427

PRO 422 0.32 PRO 183 -0.08 THR 427

PRO 422 0.30 CYS 184 -0.08 THR 427

PRO 422 0.33 VAL 185 -0.08 THR 427

PRO 422 0.36 ALA 186 -0.08 THR 427

PRO 422 0.33 ALA 187 -0.08 THR 427

PRO 422 0.32 LYS 188 -0.08 THR 427

PRO 422 0.36 ILE 189 -0.08 THR 427

PRO 422 0.35 TYR 190 -0.08 THR 427

PRO 422 0.32 ARG 191 -0.07 THR 427

PRO 422 0.32 ASN 192 -0.08 THR 427

PRO 422 0.34 LEU 193 -0.08 THR 427

PRO 422 0.33 TYR 194 -0.07 THR 427

PRO 422 0.30 ARG 195 -0.07 THR 427

PRO 422 0.29 ALA 196 -0.07 THR 427

PRO 422 0.29 GLY 197 -0.07 THR 427

PRO 422 0.27 SER 198 -0.07 THR 427

PRO 422 0.26 SER 199 -0.07 THR 427

PRO 422 0.27 ILE 200 -0.07 THR 427

PRO 422 0.24 GLY 201 -0.06 THR 427

PRO 422 0.23 ALA 202 -0.06 THR 427

PRO 422 0.22 ILE 203 -0.06 THR 427

PRO 422 0.20 ASP 204 -0.06 THR 427

PRO 422 0.19 SER 205 -0.06 THR 427

PRO 422 0.18 LYS 206 -0.06 THR 427

PRO 422 0.21 LEU 207 -0.06 THR 427

PRO 422 0.22 ASP 208 -0.06 THR 427

PRO 422 0.25 TRP 209 -0.07 THR 427

PRO 422 0.28 SER 210 -0.07 THR 427

PRO 422 0.26 HIS 211 -0.06 THR 427

PRO 422 0.25 ASN 212 -0.06 THR 427

PRO 422 0.29 PHE 213 -0.07 THR 427

PRO 422 0.29 THR 214 -0.07 THR 427

PRO 422 0.26 ASN 215 -0.06 THR 427

PRO 422 0.28 MET 216 -0.07 THR 427

PRO 422 0.30 LEU 217 -0.07 THR 427

PRO 422 0.28 GLY 218 -0.06 THR 427

PRO 422 0.28 TYR 219 -0.06 THR 427

PRO 422 0.26 THR 220 -0.06 THR 427

PRO 422 0.26 ASP 221 -0.06 THR 427

PRO 422 0.25 PRO 222 -0.06 THR 427

PRO 422 0.26 GLN 223 -0.06 THR 427

PRO 422 0.29 PHE 224 -0.06 THR 427

PRO 422 0.27 THR 225 -0.06 THR 427

PRO 422 0.27 GLU 226 -0.06 PHE 24

PRO 422 0.30 LEU 227 -0.06 PHE 24

PRO 422 0.31 MET 228 -0.07 THR 427

PRO 422 0.29 ARG 229 -0.07 PHE 24

PRO 422 0.30 LEU 230 -0.07 PHE 24

PRO 422 0.35 TYR 231 -0.07 THR 427

PRO 422 0.35 LEU 232 -0.07 THR 427

PRO 422 0.32 THR 233 -0.08 PHE 24

PRO 422 0.35 ILE 234 -0.09 PHE 24

PRO 422 0.41 HIS 235 -0.08 PHE 24

PRO 422 0.38 SER 236 -0.08 PHE 24

PRO 422 0.41 ASP 237 -0.10 PHE 24

PRO 422 0.45 HIS 238 -0.11 PHE 24

PRO 422 0.42 GLU 239 -0.12 PHE 24

PRO 422 0.51 GLY 240 -0.10 PHE 24

PRO 422 0.67 GLY 241 -0.11 THR 427

PRO 422 0.71 ASN 242 -0.12 THR 427

PRO 422 0.86 VAL 243 -0.14 THR 427

PRO 422 0.71 SER 244 -0.12 THR 427

PRO 422 0.62 ALA 245 -0.11 THR 427

PRO 422 0.77 HIS 246 -0.13 THR 427

PRO 422 0.82 THR 247 -0.14 THR 427

PRO 422 0.58 SER 248 -0.12 THR 427

PRO 422 0.51 HIS 249 -0.12 THR 427

PRO 422 0.62 LEU 250 -0.13 THR 427

PRO 422 0.52 VAL 251 -0.13 THR 427

PRO 422 0.33 GLY 252 -0.11 THR 427

LYS 432 0.23 SER 253 -0.10 THR 427

LYS 432 0.25 ALA 254 -0.10 THR 427

LYS 432 0.23 LEU 255 -0.09 THR 427

PRO 422 0.25 SER 256 -0.10 THR 427

PRO 422 0.25 ASP 257 -0.09 THR 427

PRO 422 0.31 PRO 258 -0.09 THR 427

PRO 422 0.34 TYR 259 -0.10 THR 427

PRO 422 0.40 LEU 260 -0.11 THR 427

PRO 422 0.46 SER 261 -0.11 THR 427

PRO 422 0.47 PHE 262 -0.11 THR 427

PRO 422 0.50 ALA 263 -0.11 THR 427

PRO 422 0.62 ALA 264 -0.13 THR 427

PRO 422 0.65 ALA 265 -0.12 THR 427

PRO 422 0.59 MET 266 -0.12 THR 427

PRO 422 0.66 ASN 267 -0.13 THR 427

PRO 422 0.77 GLY 268 -0.14 THR 427

PRO 422 0.66 LEU 269 -0.12 THR 427

PRO 422 0.62 ALA 270 -0.12 THR 427

PRO 422 0.69 GLY 271 -0.13 THR 427

PRO 422 0.63 PRO 272 -0.15 GLU 431

PRO 422 0.67 LEU 273 -0.15 GLU 431

PRO 422 0.67 HIS 274 -0.12 THR 427

PRO 422 0.59 GLY 275 -0.11 THR 427

PRO 422 0.57 LEU 276 -0.11 GLU 431

PRO 422 0.54 ALA 277 -0.13 GLU 431

PRO 422 0.48 ASN 278 -0.11 GLU 431

PRO 422 0.47 GLN 279 -0.12 GLU 431

PRO 422 0.48 GLU 280 -0.14 GLU 431

PRO 422 0.45 VAL 281 -0.14 GLU 431

PRO 422 0.42 LEU 282 -0.13 GLU 431

PRO 422 0.42 LEU 283 -0.14 GLU 431

PRO 422 0.42 TRP 284 -0.16 GLU 431

PRO 422 0.39 LEU 285 -0.15 GLU 431

PRO 422 0.37 SER 286 -0.14 GLU 431

PRO 422 0.37 GLN 287 -0.16 GLU 431

PRO 422 0.36 LEU 288 -0.16 GLU 431

PRO 422 0.34 GLN 289 -0.15 GLU 431

PRO 422 0.33 LYS 290 -0.15 GLU 431

PRO 422 0.32 ASP 291 -0.17 GLU 431

PRO 422 0.28 ASP 295 -0.13 GLU 431

PRO 422 0.29 ALA 296 -0.15 GLU 431

LYS 423 0.28 SER 297 -0.15 GLU 431

LYS 423 0.30 ASP 298 -0.16 GLU 431

LYS 423 0.30 GLU 299 -0.17 GLU 431

PRO 422 0.30 LYS 300 -0.17 GLU 431

PRO 422 0.32 LEU 301 -0.17 GLU 431

LYS 423 0.33 ARG 302 -0.19 GLU 431

LYS 423 0.32 ASP 303 -0.20 GLU 431

PRO 422 0.34 TYR 304 -0.20 GLU 431

PRO 422 0.36 ILE 305 -0.20 GLU 431

LYS 423 0.36 TRP 306 -0.23 GLU 431

PRO 422 0.36 ASN 307 -0.23 GLU 431

PRO 422 0.40 THR 308 -0.23 GLU 431

LYS 423 0.40 LEU 309 -0.25 GLU 431

LYS 423 0.37 ASN 310 -0.27 GLU 431

PRO 422 0.39 SER 311 -0.27 GLU 431

PRO 422 0.43 GLY 312 -0.29 GLU 431

PRO 422 0.46 ARG 313 -0.25 GLU 431

PRO 422 0.48 VAL 314 -0.23 GLU 431

PRO 422 0.45 VAL 315 -0.19 GLU 431

PRO 422 0.48 PRO 316 -0.17 GLU 431

PRO 422 0.48 GLY 317 -0.14 GLU 431

PRO 422 0.46 TYR 318 -0.15 GLU 431

LYS 423 0.51 GLY 319 -0.15 GLU 431

LYS 423 0.56 HIS 320 -0.13 GLY 43

LYS 423 0.64 ALA 321 -0.13 GLY 43

LYS 423 0.57 VAL 322 -0.10 PHE 24

LYS 423 0.49 LEU 323 -0.10 PHE 24

LYS 423 0.46 ARG 324 -0.12 ASP 39

LYS 423 0.41 LYS 325 -0.10 ASP 39

LYS 423 0.39 THR 326 -0.10 GLU 431

LYS 423 0.40 ASP 327 -0.10 PHE 24

LYS 423 0.35 PRO 328 -0.10 PHE 24

PRO 422 0.36 ARG 329 -0.09 PHE 24

PRO 422 0.37 TYR 330 -0.08 PHE 24

LYS 423 0.33 THR 331 -0.09 PHE 24

LYS 423 0.31 CYS 332 -0.09 PHE 24

PRO 422 0.33 GLN 333 -0.08 PHE 24

PRO 422 0.31 ARG 334 -0.08 GLU 431

LYS 423 0.28 GLU 335 -0.08 PHE 24

PRO 422 0.29 PHE 336 -0.07 PHE 24

PRO 422 0.30 ALA 337 -0.08 GLU 431

PRO 422 0.27 LEU 338 -0.08 GLU 431

PRO 422 0.26 LYS 339 -0.07 GLN 27

PRO 422 0.27 HIS 340 -0.07 GLU 431

PRO 422 0.28 LEU 341 -0.08 GLU 431

PRO 422 0.27 PRO 342 -0.09 GLU 431

PRO 422 0.27 SER 343 -0.09 GLU 431

PRO 422 0.30 ASP 344 -0.10 GLU 431

PRO 422 0.30 PRO 345 -0.11 GLU 431

PRO 422 0.33 MET 346 -0.12 GLU 431

PRO 422 0.32 PHE 347 -0.11 GLU 431

PRO 422 0.31 LYS 348 -0.11 GLU 431

PRO 422 0.33 LEU 349 -0.13 GLU 431

PRO 422 0.35 VAL 350 -0.13 GLU 431

PRO 422 0.32 ALA 351 -0.12 GLU 431

LYS 423 0.32 GLN 352 -0.13 GLU 431

PRO 422 0.34 LEU 353 -0.15 GLU 431

LYS 423 0.35 TYR 354 -0.13 GLU 431

LYS 423 0.33 LYS 355 -0.14 GLU 431

LYS 423 0.34 ILE 356 -0.16 GLU 431

LYS 423 0.38 VAL 357 -0.17 GLU 431

LYS 423 0.39 PRO 358 -0.16 GLU 431

LYS 423 0.36 ASN 359 -0.18 GLU 431

LYS 423 0.37 VAL 360 -0.20 GLU 431

LYS 423 0.41 LEU 361 -0.21 GLU 431

LYS 423 0.40 LEU 362 -0.20 GLU 431

LYS 423 0.37 GLU 363 -0.22 GLU 431

LYS 423 0.40 GLN 364 -0.25 GLU 431

LYS 423 0.42 GLY 365 -0.25 GLU 431

LYS 423 0.48 LYS 366 -0.27 GLU 431

LYS 423 0.50 ALA 367 -0.22 GLU 431

LYS 423 0.51 LYS 368 -0.21 ASP 39

LYS 423 0.48 ASN 369 -0.16 ASP 39

LYS 423 0.44 PRO 370 -0.17 GLU 431

LYS 423 0.42 TRP 371 -0.13 GLU 431

LYS 423 0.42 PRO 372 -0.12 GLU 431

PRO 422 0.45 ASN 373 -0.10 GLU 431

PRO 422 0.44 VAL 374 -0.09 GLU 431

PRO 422 0.47 ASP 375 -0.10 GLU 431

PRO 422 0.43 ALA 376 -0.12 GLU 431

PRO 422 0.39 HIS 377 -0.10 GLU 431

PRO 422 0.40 SER 378 -0.09 GLU 431

PRO 422 0.40 GLY 379 -0.10 GLU 431

PRO 422 0.36 VAL 380 -0.10 GLU 431

PRO 422 0.34 LEU 381 -0.08 GLU 431

PRO 422 0.35 LEU 382 -0.08 GLU 431

PRO 422 0.35 GLN 383 -0.09 GLU 431

PRO 422 0.32 TYR 384 -0.09 GLU 431

PRO 422 0.31 TYR 385 -0.07 GLU 431

PRO 422 0.31 GLY 386 -0.08 GLU 431

PRO 422 0.34 MET 387 -0.08 GLU 431

PRO 422 0.35 THR 388 -0.09 GLU 431

PRO 422 0.38 GLU 389 -0.09 GLU 431

PRO 422 0.41 MET 390 -0.10 GLU 431

PRO 422 0.44 ASN 391 -0.10 GLU 431

PRO 422 0.42 TYR 392 -0.09 THR 427

PRO 422 0.44 TYR 393 -0.09 THR 427

PRO 422 0.49 THR 394 -0.10 THR 427

PRO 422 0.45 VAL 395 -0.09 THR 427

PRO 422 0.41 LEU 396 -0.09 THR 427

PRO 422 0.46 PHE 397 -0.09 THR 427

PRO 422 0.48 GLY 398 -0.10 THR 427

PRO 422 0.40 VAL 399 -0.09 THR 427

PRO 422 0.40 SER 400 -0.08 THR 427

PRO 422 0.45 ARG 401 -0.09 THR 427

PRO 422 0.40 ALA 402 -0.09 THR 427

PRO 422 0.34 LEU 403 -0.08 THR 427

PRO 422 0.36 GLY 404 -0.08 THR 427

PRO 422 0.41 VAL 405 -0.09 THR 427

PRO 422 0.32 LEU 406 -0.09 THR 427

PRO 422 0.25 ALA 407 -0.08 THR 427

PRO 422 0.25 GLN 408 -0.08 THR 427

PRO 422 0.25 LEU 409 -0.09 THR 427

LYS 432 0.16 ILE 410 -0.08 THR 427

LYS 432 0.16 TRP 411 -0.07 SER 426

LYS 432 0.19 SER 412 -0.09 SER 426

LYS 432 0.20 ARG 413 -0.08 SER 426

LYS 432 0.19 ALA 414 -0.08 SER 426

LYS 432 0.21 LEU 415 -0.13 SER 424

LYS 432 0.24 GLY 416 -0.15 PRO 422

LYS 432 0.25 PHE 417 -0.16 SER 424

LYS 432 0.29 PRO 418 -0.22 PRO 422

LYS 432 0.31 LEU 419 -0.12 SER 426

LYS 432 0.27 GLU 420 -0.15 SER 426

LYS 432 0.34 ARG 421 -0.16 SER 426

GLY 44 0.94 PRO 422 -0.46 ASN 30

SER 41 1.23 LYS 423 -0.15 GLY 161

ASN 267 0.38 SER 424 -0.60 ILE 36

TYR 42 0.38 MET 425 -0.47 ILE 36

TYR 42 0.26 SER 426 -0.31 ILE 36

LYS 423 0.26 THR 427 -0.24 SER 41

LYS 423 0.15 ALA 428 -0.14 SER 41

LYS 423 0.21 GLY 429 -0.19 ILE 36

LYS 423 0.47 LEU 430 -0.15 LYS 366

LYS 423 0.37 GLU 431 -0.29 GLY 312

ARG 421 0.34 LYS 432 -0.24 GLY 365

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 9 ---

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 *