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

* 5csc_open_aligned *

CA distance fluctuations for 2604241127051943378

--- 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
SER 426 0.09 ALA 1 -0.09 PRO 422

SER 424 0.10 SER 2 -0.08 PRO 422

SER 424 0.11 SER 3 -0.08 PRO 422

SER 424 0.12 THR 4 -0.06 LYS 423

SER 424 0.13 ASN 5 -0.04 PRO 422

SER 424 0.14 LEU 6 -0.07 PRO 422

SER 424 0.15 LYS 7 -0.04 PRO 422

SER 424 0.15 ASP 8 -0.02 ALA 432

SER 424 0.15 VAL 9 -0.05 LYS 423

SER 424 0.17 LEU 10 -0.05 LYS 423

SER 424 0.17 ALA 11 -0.03 ALA 432

SER 424 0.17 ALA 12 -0.04 ALA 432

SER 424 0.19 LEU 13 -0.05 LYS 423

SER 424 0.21 ILE 14 -0.04 ALA 432

PRO 422 0.25 PRO 15 -0.05 ALA 432

PRO 422 0.23 LYS 16 -0.06 ALA 432

SER 424 0.23 GLU 17 -0.08 LYS 423

PRO 422 0.31 GLN 18 -0.06 ALA 432

PRO 422 0.38 ALA 19 -0.07 ALA 432

PRO 422 0.36 ARG 20 -0.08 LYS 423

PRO 422 0.41 ILE 21 -0.09 LYS 423

PRO 422 0.54 LYS 22 -0.08 ALA 432

PRO 422 0.54 THR 23 -0.08 ALA 432

PRO 422 0.53 PHE 24 -0.09 LYS 423

PRO 422 0.68 ARG 25 -0.09 ALA 432

PRO 422 0.74 GLN 26 -0.09 ALA 432

PRO 422 0.70 GLN 27 -0.09 ALA 432

PRO 422 0.67 HIS 28 -0.12 LYS 423

PRO 422 0.79 GLY 29 -0.10 ALA 432

PRO 422 0.95 GLY 30 -0.12 ALA 432

PRO 422 0.73 THR 31 -0.20 LYS 423

PRO 422 0.64 ALA 32 -0.32 LYS 423

PRO 422 0.41 LEU 33 -0.48 LYS 423

PRO 422 0.29 GLY 34 -0.64 LYS 423

SER 424 0.25 GLN 35 -0.74 LYS 423

SER 424 0.25 ILE 36 -0.96 LYS 423

SER 424 0.16 THR 37 -0.84 LYS 423

GLY 365 0.08 VAL 38 -0.75 LYS 423

GLY 365 0.09 ASP 39 -0.79 LYS 423

GLY 365 0.11 MET 40 -1.04 LYS 423

THR 427 0.11 SER 41 -1.12 LYS 423

ILE 431 0.18 TYR 42 -0.81 LYS 423

ILE 431 0.12 GLY 43 -0.90 LYS 423

THR 427 0.13 GLY 44 -0.99 LYS 423

SER 424 0.14 MET 45 -1.22 LYS 423

GLY 365 0.11 ARG 46 -0.96 LYS 423

SER 424 0.16 GLY 47 -0.86 LYS 423

SER 424 0.26 MET 48 -1.00 LYS 423

SER 424 0.33 LYS 49 -0.75 LYS 423

SER 424 0.42 GLY 50 -0.68 LYS 423

SER 424 0.35 LEU 51 -0.50 LYS 423

SER 424 0.32 VAL 52 -0.35 LYS 423

SER 424 0.26 TYR 53 -0.34 LYS 423

SER 424 0.23 GLU 54 -0.27 LYS 423

SER 424 0.19 THR 55 -0.27 LYS 423

SER 424 0.17 SER 56 -0.34 LYS 423

SER 424 0.18 VAL 57 -0.39 LYS 423

SER 424 0.15 LEU 58 -0.43 LYS 423

SER 424 0.15 ASP 59 -0.39 LYS 423

SER 424 0.13 PRO 60 -0.41 LYS 423

SER 424 0.12 ASP 61 -0.36 LYS 423

SER 424 0.12 GLU 62 -0.34 LYS 423

SER 424 0.11 GLY 63 -0.37 LYS 423

SER 424 0.12 ILE 64 -0.37 LYS 423

SER 424 0.14 ARG 65 -0.32 LYS 423

SER 424 0.15 PHE 66 -0.28 LYS 423

SER 424 0.17 ARG 67 -0.26 LYS 423

SER 424 0.16 GLY 68 -0.27 LYS 423

SER 424 0.14 PHE 69 -0.26 LYS 423

SER 424 0.12 SER 70 -0.29 LYS 423

SER 424 0.10 ILE 71 -0.29 LYS 423

SER 424 0.10 PRO 72 -0.26 LYS 423

SER 424 0.11 GLU 73 -0.24 LYS 423

SER 424 0.11 CYS 74 -0.23 LYS 423

SER 424 0.09 GLN 75 -0.23 LYS 423

SER 424 0.09 LYS 76 -0.21 LYS 423

SER 424 0.11 LEU 77 -0.19 LYS 423

SER 424 0.10 LEU 78 -0.19 LYS 423

SER 424 0.09 PRO 79 -0.18 PRO 422

SER 424 0.08 LYS 80 -0.21 PRO 422

THR 427 0.08 GLY 81 -0.24 PRO 422

THR 427 0.07 GLY 82 -0.21 PRO 422

THR 427 0.06 GLY 84 -0.25 PRO 422

SER 424 0.06 GLY 85 -0.25 PRO 422

THR 427 0.07 GLU 86 -0.28 PRO 422

SER 424 0.08 PRO 87 -0.26 PRO 422

THR 427 0.09 LEU 88 -0.27 PRO 422

THR 427 0.10 PRO 89 -0.31 PRO 422

THR 427 0.10 GLU 90 -0.25 PRO 422

SER 424 0.11 GLY 91 -0.20 PRO 422

SER 424 0.11 LEU 92 -0.24 PRO 422

SER 424 0.12 PHE 93 -0.25 PRO 422

SER 424 0.13 TRP 94 -0.17 PRO 422

SER 424 0.14 LEU 95 -0.17 LYS 423

SER 424 0.15 LEU 96 -0.20 LYS 423

SER 424 0.16 VAL 97 -0.14 LYS 423

SER 424 0.17 THR 98 -0.13 LYS 423

SER 424 0.17 GLY 99 -0.17 LYS 423

SER 424 0.15 GLN 100 -0.15 LYS 423

SER 424 0.13 ILE 101 -0.16 LYS 423

SER 424 0.12 PRO 102 -0.13 LYS 423

SER 424 0.11 THR 103 -0.12 LYS 423

SER 424 0.10 GLY 104 -0.13 PRO 422

SER 424 0.10 ALA 105 -0.12 PRO 422

SER 424 0.11 GLN 106 -0.12 PRO 422

SER 424 0.10 VAL 107 -0.17 PRO 422

THR 427 0.10 SER 108 -0.17 PRO 422

THR 427 0.10 TRP 109 -0.15 PRO 422

THR 427 0.11 LEU 110 -0.19 PRO 422

THR 427 0.10 SER 111 -0.22 PRO 422

THR 427 0.11 LYS 112 -0.20 PRO 422

THR 427 0.12 GLU 113 -0.19 PRO 422

THR 427 0.12 TRP 114 -0.26 PRO 422

THR 427 0.11 ALA 115 -0.26 PRO 422

THR 427 0.12 LYS 116 -0.23 PRO 422

THR 427 0.13 ARG 117 -0.25 PRO 422

THR 427 0.12 ALA 118 -0.30 PRO 422

THR 427 0.13 ALA 119 -0.31 PRO 422

THR 427 0.13 LEU 120 -0.36 PRO 422

THR 427 0.14 PRO 121 -0.34 PRO 422

THR 427 0.13 SER 122 -0.35 PRO 422

THR 427 0.15 HIS 123 -0.39 PRO 422

THR 427 0.15 VAL 124 -0.44 PRO 422

THR 427 0.13 VAL 125 -0.42 PRO 422

THR 427 0.13 THR 126 -0.42 PRO 422

THR 427 0.14 MET 127 -0.47 PRO 422

THR 427 0.13 LEU 128 -0.50 PRO 422

THR 427 0.12 ASP 129 -0.47 PRO 422

THR 427 0.12 ASN 130 -0.48 PRO 422

THR 427 0.13 PHE 131 -0.54 PRO 422

ASP 428 0.12 PRO 132 -0.55 PRO 422

GLY 312 0.11 THR 133 -0.57 PRO 422

GLY 312 0.13 ASN 134 -0.61 PRO 422

GLY 312 0.13 LEU 135 -0.65 PRO 422

GLY 312 0.13 HIS 136 -0.69 PRO 422

THR 427 0.12 PRO 137 -0.65 PRO 422

THR 427 0.13 MET 138 -0.73 PRO 422

THR 427 0.15 SER 139 -0.73 PRO 422

THR 427 0.14 GLN 140 -0.64 PRO 422

THR 427 0.15 LEU 141 -0.63 PRO 422

THR 427 0.17 SER 142 -0.70 PRO 422

THR 427 0.17 ALA 143 -0.63 PRO 422

THR 427 0.16 ALA 144 -0.54 PRO 422

THR 427 0.17 ILE 145 -0.54 PRO 422

THR 427 0.19 THR 146 -0.56 PRO 422

THR 427 0.18 ALA 147 -0.48 PRO 422

THR 427 0.17 LEU 148 -0.43 PRO 422

THR 427 0.18 ASN 149 -0.41 PRO 422

THR 427 0.18 SER 150 -0.34 PRO 422

THR 427 0.17 GLU 151 -0.29 PRO 422

THR 427 0.18 SER 152 -0.27 PRO 422

THR 427 0.17 ASN 153 -0.17 PRO 422

THR 427 0.18 PHE 154 -0.15 PRO 422

THR 427 0.20 ALA 155 -0.19 PRO 422

THR 427 0.18 ARG 156 -0.14 PRO 422

SER 426 0.18 ALA 157 -0.05 PRO 422

LYS 423 0.23 TYR 158 -0.04 PRO 422

LYS 423 0.26 ALA 159 -0.05 PRO 422

LYS 423 0.24 GLU 160 -0.02 ASN 5

LYS 423 0.27 GLY 161 -0.01 LYS 7

LYS 423 0.22 ILE 162 -0.02 GLN 35

LYS 423 0.23 LEU 163 -0.02 ALA 432

PRO 422 0.22 ARG 164 -0.03 ALA 432

PRO 422 0.21 THR 165 -0.03 ALA 432

SER 424 0.18 LYS 166 -0.02 ALA 432

SER 426 0.19 TYR 167 -0.02 GLN 35

SER 424 0.18 TRP 168 -0.02 ALA 432

SER 426 0.16 GLU 169 -0.02 ALA 432

SER 426 0.17 MET 170 -0.09 PRO 422

SER 426 0.17 VAL 171 -0.15 PRO 422

SER 426 0.16 TYR 172 -0.15 PRO 422

THR 427 0.15 GLU 173 -0.17 PRO 422

THR 427 0.16 SER 174 -0.26 PRO 422

THR 427 0.16 ALA 175 -0.27 PRO 422

THR 427 0.14 MET 176 -0.26 PRO 422

THR 427 0.14 ASP 177 -0.29 PRO 422

THR 427 0.15 LEU 178 -0.38 PRO 422

THR 427 0.14 ILE 179 -0.37 PRO 422

THR 427 0.13 ALA 180 -0.33 PRO 422

THR 427 0.13 LYS 181 -0.38 PRO 422

THR 427 0.13 LEU 182 -0.45 PRO 422

THR 427 0.12 PRO 183 -0.43 PRO 422

THR 427 0.12 CYS 184 -0.42 PRO 422

THR 427 0.13 VAL 185 -0.48 PRO 422

THR 427 0.12 ALA 186 -0.52 PRO 422

THR 427 0.11 ALA 187 -0.46 PRO 422

THR 427 0.11 LYS 188 -0.47 PRO 422

THR 427 0.11 ILE 189 -0.53 PRO 422

THR 427 0.10 TYR 190 -0.52 PRO 422

THR 427 0.09 ARG 191 -0.47 PRO 422

THR 427 0.10 ASN 192 -0.49 PRO 422

THR 427 0.09 LEU 193 -0.53 PRO 422

SER 311 0.08 TYR 194 -0.50 PRO 422

THR 427 0.08 ARG 195 -0.46 PRO 422

ASP 428 0.08 ALA 196 -0.45 PRO 422

THR 427 0.09 GLY 197 -0.45 PRO 422

THR 427 0.09 SER 198 -0.41 PRO 422

THR 427 0.09 SER 199 -0.39 PRO 422

THR 427 0.10 ILE 200 -0.39 PRO 422

THR 427 0.10 GLY 201 -0.35 PRO 422

THR 427 0.10 ALA 202 -0.32 PRO 422

THR 427 0.10 ILE 203 -0.30 PRO 422

THR 427 0.10 ASP 204 -0.27 PRO 422

THR 427 0.10 SER 205 -0.23 PRO 422

THR 427 0.09 LYS 206 -0.22 PRO 422

THR 427 0.09 LEU 207 -0.26 PRO 422

THR 427 0.10 ASP 208 -0.27 PRO 422

THR 427 0.10 TRP 209 -0.31 PRO 422

THR 427 0.09 SER 210 -0.35 PRO 422

THR 427 0.09 HIS 211 -0.33 PRO 422

THR 427 0.10 ASN 212 -0.33 PRO 422

THR 427 0.10 PHE 213 -0.39 PRO 422

THR 427 0.09 THR 214 -0.39 PRO 422

THR 427 0.09 ASN 215 -0.36 PRO 422

THR 427 0.10 MET 216 -0.38 PRO 422

THR 427 0.09 LEU 217 -0.42 PRO 422

THR 427 0.08 GLY 218 -0.39 PRO 422

THR 427 0.07 TYR 219 -0.39 PRO 422

THR 427 0.07 THR 220 -0.35 PRO 422

THR 427 0.06 ASP 221 -0.34 PRO 422

THR 427 0.06 ALA 222 -0.32 PRO 422

THR 427 0.06 GLN 223 -0.33 PRO 422

THR 427 0.06 PHE 224 -0.37 PRO 422

THR 427 0.07 THR 225 -0.35 PRO 422

THR 427 0.07 GLU 226 -0.33 PRO 422

THR 427 0.07 LEU 227 -0.37 PRO 422

THR 427 0.08 MET 228 -0.39 PRO 422

THR 427 0.08 ARG 229 -0.34 PRO 422

THR 427 0.08 LEU 230 -0.35 PRO 422

THR 427 0.08 TYR 231 -0.42 PRO 422

THR 427 0.10 LEU 232 -0.42 PRO 422

THR 427 0.09 THR 233 -0.36 PRO 422

THR 427 0.09 ILE 234 -0.39 PRO 422

THR 427 0.10 HIS 235 -0.49 PRO 422

THR 427 0.11 SER 236 -0.44 PRO 422

THR 427 0.12 ASP 237 -0.43 PRO 422

SER 424 0.12 HIS 238 -0.45 PRO 422

SER 424 0.17 GLU 239 -0.44 LYS 423

SER 424 0.20 GLY 240 -0.45 PRO 422

SER 424 0.17 GLY 241 -0.62 PRO 422

THR 427 0.15 ASN 242 -0.77 PRO 422

THR 427 0.18 VAL 243 -0.99 PRO 422

THR 427 0.17 SER 244 -0.83 PRO 422

THR 427 0.18 ALA 245 -0.66 PRO 422

THR 427 0.21 HIS 246 -0.76 PRO 422

THR 427 0.23 THR 247 -0.89 PRO 422

THR 427 0.21 SER 248 -0.65 PRO 422

SER 426 0.23 HIS 249 -0.50 PRO 422

SER 426 0.27 LEU 250 -0.63 PRO 422

THR 427 0.27 VAL 251 -0.62 PRO 422

THR 427 0.23 GLY 252 -0.41 PRO 422

SER 426 0.26 SER 253 -0.23 PRO 422

SER 426 0.28 ALA 254 -0.24 PRO 422

SER 426 0.24 LEU 255 -0.16 PRO 422

THR 427 0.23 SER 256 -0.34 PRO 422

THR 427 0.20 ASP 257 -0.32 PRO 422

THR 427 0.19 PRO 258 -0.37 PRO 422

THR 427 0.19 TYR 259 -0.46 PRO 422

THR 427 0.21 LEU 260 -0.53 PRO 422

THR 427 0.22 SER 261 -0.59 PRO 422

THR 427 0.19 PHE 262 -0.62 PRO 422

THR 427 0.19 ALA 263 -0.70 PRO 422

THR 427 0.22 ALA 264 -0.85 PRO 422

THR 427 0.20 ALA 265 -0.82 PRO 422

THR 427 0.18 MET 266 -0.83 PRO 422

THR 427 0.19 ASN 267 -0.96 PRO 422

THR 427 0.19 GLY 268 -1.06 PRO 422

THR 427 0.15 LEU 269 -0.90 PRO 422

THR 427 0.15 ALA 270 -0.91 PRO 422

ARG 313 0.15 GLY 271 -1.01 PRO 422

ARG 313 0.18 PRO 272 -0.92 PRO 422

VAL 314 0.19 LEU 273 -0.95 PRO 422

VAL 314 0.14 HIS 274 -0.92 PRO 422

VAL 314 0.13 GLY 275 -0.83 PRO 422

VAL 314 0.13 LEU 276 -0.76 PRO 422

VAL 314 0.13 ALA 277 -0.69 PRO 422

VAL 314 0.08 ASN 278 -0.61 PRO 422

THR 308 0.09 GLN 279 -0.64 PRO 422

THR 308 0.13 GLU 280 -0.65 PRO 422

ILE 305 0.11 VAL 281 -0.58 PRO 422

ILE 305 0.08 LEU 282 -0.55 PRO 422

THR 308 0.10 GLY 283 -0.57 PRO 422

TYR 304 0.13 TRP 284 -0.55 PRO 422

TYR 304 0.09 LEU 285 -0.50 PRO 422

THR 388 0.07 ALA 286 -0.50 PRO 422

TYR 304 0.07 GLN 287 -0.50 PRO 422

SER 300 0.07 LEU 288 -0.47 PRO 422

THR 388 0.06 GLN 289 -0.45 PRO 422

THR 388 0.06 LYS 290 -0.44 PRO 422

ASN 134 0.07 ALA 291 -0.44 PRO 422

ILE 431 0.04 ALA 295 -0.35 PRO 422

ILE 431 0.05 GLY 296 -0.34 PRO 422

TRP 284 0.05 ALA 297 -0.32 PRO 422

LEU 273 0.06 ASP 298 -0.30 PRO 422

TRP 284 0.07 ALA 299 -0.30 PRO 422

TRP 284 0.09 SER 300 -0.33 PRO 422

TRP 284 0.10 LEU 301 -0.35 PRO 422

TRP 284 0.09 ARG 302 -0.32 PRO 422

TRP 284 0.10 ASP 303 -0.32 PRO 422

TRP 284 0.13 TYR 304 -0.37 PRO 422

TRP 284 0.13 ILE 305 -0.37 PRO 422

LEU 273 0.12 TRP 306 -0.33 PRO 422

PRO 272 0.12 ASN 307 -0.36 PRO 422

PRO 272 0.14 THR 308 -0.40 PRO 422

LEU 273 0.15 LEU 309 -0.38 PRO 422

PRO 272 0.14 ASN 310 -0.35 PRO 422

PRO 272 0.15 SER 311 -0.39 PRO 422

PRO 272 0.17 GLY 312 -0.41 PRO 422

PRO 272 0.18 ARG 313 -0.45 PRO 422

LEU 273 0.19 VAL 314 -0.46 PRO 422

PRO 316 0.20 VAL 315 -0.46 PRO 422

VAL 315 0.20 PRO 316 -0.55 PRO 422

LEU 273 0.10 GLY 317 -0.51 PRO 422

LEU 273 0.12 TYR 318 -0.44 PRO 422

LEU 273 0.14 GLY 319 -0.40 LYS 423

LEU 273 0.13 HIS 320 -0.44 LYS 423

LEU 273 0.13 ALA 321 -0.48 LYS 423

SER 424 0.12 VAL 322 -0.47 LYS 423

SER 424 0.11 LEU 323 -0.42 LYS 423

SER 424 0.10 ARG 324 -0.39 LYS 423

SER 424 0.09 LYS 325 -0.35 LYS 423

SER 424 0.07 THR 326 -0.34 LYS 423

SER 424 0.07 ASP 327 -0.36 LYS 423

SER 424 0.08 PRO 328 -0.32 LYS 423

SER 424 0.07 ARG 329 -0.37 PRO 422

THR 427 0.05 TYR 330 -0.39 PRO 422

SER 424 0.06 THR 331 -0.33 PRO 422

SER 424 0.06 CYS 332 -0.33 PRO 422

THR 427 0.05 GLN 333 -0.37 PRO 422

THR 427 0.04 ARG 334 -0.34 PRO 422

SER 424 0.05 GLU 335 -0.30 PRO 422

THR 427 0.05 PHE 336 -0.33 PRO 422

THR 427 0.04 ALA 337 -0.35 PRO 422

THR 427 0.04 LEU 338 -0.31 PRO 422

THR 427 0.04 LYS 339 -0.29 PRO 422

THR 427 0.04 HIS 340 -0.32 PRO 422

ILE 431 0.04 LEU 341 -0.35 PRO 422

ILE 431 0.04 PRO 342 -0.32 PRO 422

ILE 431 0.04 GLY 343 -0.33 PRO 422

ILE 431 0.04 ASP 344 -0.37 PRO 422

ILE 431 0.04 PRO 345 -0.38 PRO 422

ILE 431 0.04 MET 346 -0.42 PRO 422

ILE 431 0.04 PHE 347 -0.39 PRO 422

ILE 431 0.04 LYS 348 -0.36 PRO 422

ILE 431 0.04 LEU 349 -0.39 PRO 422

ILE 431 0.05 VAL 350 -0.41 PRO 422

ILE 431 0.04 ALA 351 -0.36 PRO 422

ILE 431 0.05 GLN 352 -0.35 PRO 422

PRO 316 0.06 LEU 353 -0.37 PRO 422

LEU 273 0.06 TYR 354 -0.35 PRO 422

LEU 273 0.06 LYS 355 -0.30 PRO 422

LEU 273 0.08 ILE 356 -0.31 PRO 422

LEU 273 0.10 VAL 357 -0.34 PRO 422

LEU 273 0.10 PRO 358 -0.32 LYS 423

LEU 273 0.10 ASN 359 -0.30 LYS 423

LEU 273 0.12 VAL 360 -0.30 LYS 423

LEU 273 0.14 LEU 361 -0.33 LYS 423

LEU 273 0.12 LEU 362 -0.32 LYS 423

LEU 273 0.12 GLU 363 -0.29 LYS 423

LEU 273 0.15 GLN 364 -0.30 LYS 423

LEU 273 0.15 GLY 365 -0.32 LYS 423

LEU 273 0.18 ALA 366 -0.35 LYS 423

LEU 273 0.13 ALA 367 -0.37 LYS 423

LEU 273 0.11 ALA 368 -0.38 LYS 423

LEU 273 0.10 ASN 369 -0.39 LYS 423

LEU 273 0.10 PRO 370 -0.37 LYS 423

LEU 273 0.08 TRP 371 -0.36 LYS 423

LEU 273 0.08 PRO 372 -0.41 PRO 422

LEU 273 0.07 ASN 373 -0.44 PRO 422

THR 427 0.06 VAL 374 -0.47 PRO 422

ILE 431 0.05 ASP 375 -0.55 PRO 422

ILE 431 0.05 ALA 376 -0.49 PRO 422

ILE 431 0.05 HIS 377 -0.45 PRO 422

THR 427 0.05 SER 378 -0.48 PRO 422

ILE 431 0.05 GLY 379 -0.52 PRO 422

ILE 431 0.05 VAL 380 -0.47 PRO 422

ILE 431 0.05 LEU 381 -0.44 PRO 422

THR 427 0.05 LEU 382 -0.48 PRO 422

ALA 286 0.06 GLN 383 -0.48 PRO 422

ALA 286 0.05 TYR 384 -0.43 PRO 422

THR 427 0.05 TYR 385 -0.42 PRO 422

LYS 290 0.06 GLY 386 -0.45 PRO 422

ALA 286 0.06 MET 387 -0.49 PRO 422

ALA 286 0.07 THR 388 -0.51 PRO 422

SER 311 0.07 GLU 389 -0.56 PRO 422

SER 311 0.08 MET 390 -0.60 PRO 422

ARG 313 0.11 ASN 391 -0.66 PRO 422

ARG 313 0.08 TYR 392 -0.62 PRO 422

THR 427 0.08 TYR 393 -0.61 PRO 422

THR 427 0.10 THR 394 -0.68 PRO 422

THR 427 0.11 VAL 395 -0.63 PRO 422

THR 427 0.10 LEU 396 -0.56 PRO 422

THR 427 0.11 PHE 397 -0.60 PRO 422

THR 427 0.13 GLY 398 -0.63 PRO 422

THR 427 0.12 VAL 399 -0.53 PRO 422

THR 427 0.12 SER 400 -0.49 PRO 422

THR 427 0.13 ARG 401 -0.54 PRO 422

THR 427 0.14 ALA 402 -0.49 PRO 422

THR 427 0.13 LEU 403 -0.38 PRO 422

THR 427 0.13 GLY 404 -0.38 PRO 422

THR 427 0.16 VAL 405 -0.46 PRO 422

THR 427 0.16 LEU 406 -0.35 PRO 422

SER 424 0.16 ALA 407 -0.25 PRO 422

SER 424 0.20 GLN 408 -0.21 PRO 422

SER 424 0.19 LEU 409 -0.25 PRO 422

SER 424 0.19 ILE 410 -0.13 PRO 422

SER 424 0.22 TRP 411 -0.09 LYS 423

SER 424 0.26 SER 412 -0.08 LYS 423

SER 424 0.23 ARG 413 -0.03 ALA 432

SER 424 0.23 ALA 414 -0.04 ALA 432

SER 424 0.26 LEU 415 -0.05 ALA 432

SER 424 0.27 GLY 416 -0.05 ALA 432

SER 424 0.33 PHE 417 -0.05 ALA 432

SER 424 0.34 PRO 418 -0.07 GLN 35

SER 424 0.33 LEU 419 -0.06 GLN 35

SER 424 0.45 GLU 420 -0.12 PRO 422

SER 424 0.42 ARG 421 -0.15 GLY 268

GLY 30 0.95 PRO 422 -1.06 GLY 268

GLY 161 0.27 LYS 423 -1.22 MET 45

GLU 420 0.45 SER 424 -0.12 ALA 432

GLU 420 0.31 MET 425 -0.13 TYR 42

GLU 420 0.33 SER 426 -0.07 PRO 422

GLU 420 0.27 THR 427 -0.09 PRO 422

VAL 251 0.23 ASP 428 -0.06 VAL 38

GLU 420 0.13 GLY 429 -0.11 SER 424

VAL 251 0.07 LEU 430 -0.30 LYS 423

TYR 42 0.18 ILE 431 -0.20 LYS 423

GLY 365 0.09 ALA 432 -0.18 LYS 423

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.

*** 5csc_open_aligned ***

CA distance fluctuations for 2604241127051943378

--- 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.

* 5csc_open_aligned *