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

* open cutoff 10 melek new *

CA distance fluctuations for 260522120818411546

--- normal mode 11 ---

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
ALA 432 0.35 ALA 1 -0.16 LEU 33

ALA 432 0.37 SER 2 -0.17 LEU 33

ALA 432 0.39 SER 3 -0.18 LEU 33

ALA 432 0.41 THR 4 -0.21 LEU 33

ALA 432 0.44 ASN 5 -0.20 LEU 33

ALA 432 0.46 LEU 6 -0.19 LEU 33

ALA 432 0.48 LYS 7 -0.18 LEU 33

ALA 432 0.47 ASP 8 -0.21 LEU 33

ALA 432 0.48 VAL 9 -0.25 LEU 33

ALA 432 0.51 LEU 10 -0.24 LEU 33

ALA 432 0.53 ALA 11 -0.23 LEU 33

ALA 432 0.53 ALA 12 -0.27 LEU 33

ALA 432 0.54 LEU 13 -0.33 LEU 33

ALA 432 0.58 ILE 14 -0.29 LEU 33

ALA 432 0.61 PRO 15 -0.29 GLN 35

ALA 432 0.61 LYS 16 -0.32 LEU 33

ALA 432 0.63 GLU 17 -0.39 LEU 33

ALA 432 0.66 GLN 18 -0.34 GLN 35

ALA 432 0.69 ALA 19 -0.33 GLN 35

ALA 432 0.72 ARG 20 -0.32 LEU 33

ALA 432 0.75 ILE 21 -0.43 LEU 33

ALA 432 0.78 LYS 22 -0.46 GLN 35

ALA 432 0.83 THR 23 -0.18 GLN 35

ALA 432 0.87 PHE 24 -0.08 LEU 33

ALA 432 0.92 ARG 25 -0.29 GLY 34

ALA 432 0.94 GLN 26 -0.22 GLN 35

ALA 432 1.01 GLN 27 -0.02 SER 2

ALA 432 1.07 HIS 28 0.00 ALA 1

PRO 422 1.11 GLY 29 0.00 ALA 1

PRO 422 1.33 GLY 30 0.00 ALA 1

ALA 432 1.21 THR 31 -0.09 LEU 77

ALA 432 1.28 ALA 32 -0.12 LEU 77

ALA 32 1.07 LEU 33 -0.43 ILE 21

ALA 432 1.03 GLY 34 -0.40 LYS 22

ALA 432 1.10 GLN 35 -0.46 LYS 22

ALA 432 1.12 ILE 36 -0.33 PRO 418

ALA 432 1.04 THR 37 -0.39 LYS 423

ILE 431 1.01 VAL 38 -0.39 LYS 423

ALA 432 0.82 ASP 39 -0.70 LYS 423

ALA 432 0.83 MET 40 -1.06 LYS 423

ALA 432 0.90 SER 41 -0.53 LYS 423

ALA 432 0.71 TYR 42 -0.71 LYS 423

LEU 273 0.76 GLY 43 -0.96 LYS 423

LEU 273 0.67 GLY 44 -0.79 LYS 423

ALA 432 0.79 MET 45 -1.01 LYS 423

LEU 273 0.67 ARG 46 -1.61 LYS 423

GLN 35 0.74 GLY 47 -1.38 LYS 423

ALA 432 0.87 MET 48 -0.98 LYS 423

ALA 432 0.88 LYS 49 -0.54 LYS 423

GLY 30 0.92 GLY 50 -0.35 LEU 415

GLY 30 0.90 LEU 51 -0.27 LEU 415

GLY 30 0.86 VAL 52 -0.22 LEU 415

GLY 30 0.73 TYR 53 -0.11 LYS 423

ALA 432 0.61 GLU 54 -0.19 VAL 52

ALA 432 0.54 THR 55 -0.14 LYS 423

ALA 432 0.52 SER 56 -0.22 LYS 423

ALA 432 0.53 VAL 57 -0.33 LYS 423

GLN 35 0.52 LEU 58 -0.36 LYS 423

GLN 35 0.51 ASP 59 -0.41 LYS 423

GLN 35 0.59 PRO 60 -0.43 LYS 423

GLN 35 0.51 ASP 61 -0.40 LYS 423

GLN 35 0.44 GLU 62 -0.34 LYS 423

GLN 35 0.47 GLY 63 -0.30 LYS 423

ALA 432 0.43 ILE 64 -0.27 LYS 423

ALA 432 0.46 ARG 65 -0.27 LYS 423

ALA 432 0.47 PHE 66 -0.20 LYS 423

ALA 432 0.49 ARG 67 -0.24 LYS 423

ALA 432 0.47 GLY 68 -0.30 LYS 423

ALA 432 0.43 PHE 69 -0.25 LYS 423

ALA 432 0.41 SER 70 -0.25 LYS 423

ALA 432 0.37 ILE 71 -0.20 LYS 423

ALA 432 0.35 PRO 72 -0.21 LYS 423

ALA 432 0.37 GLU 73 -0.21 LYS 423

ALA 432 0.38 CYS 74 -0.17 LYS 423

ALA 432 0.34 GLN 75 -0.15 LYS 423

ALA 432 0.33 LYS 76 -0.16 LYS 423

ALA 432 0.36 LEU 77 -0.16 LEU 33

ALA 432 0.37 LEU 78 -0.14 LEU 33

ALA 432 0.35 PRO 79 -0.14 LEU 33

ALA 432 0.33 LYS 80 -0.11 PRO 422

ALA 432 0.31 GLY 81 -0.13 PRO 422

ALA 432 0.30 GLY 82 -0.11 PRO 422

ALA 432 0.28 GLY 84 -0.14 PRO 422

ALA 432 0.29 GLY 85 -0.14 PRO 422

ALA 432 0.31 GLU 86 -0.16 PRO 422

ALA 432 0.34 PRO 87 -0.14 PRO 422

ALA 432 0.35 LEU 88 -0.14 PRO 422

ALA 432 0.38 PRO 89 -0.16 PRO 422

ALA 432 0.39 GLU 90 -0.12 PRO 422

ALA 432 0.40 GLY 91 -0.14 LEU 33

ALA 432 0.41 LEU 92 -0.11 LEU 33

ALA 432 0.44 PHE 93 -0.11 LEU 33

ALA 432 0.44 TRP 94 -0.17 LEU 33

ALA 432 0.45 LEU 95 -0.19 LEU 33

ALA 432 0.48 LEU 96 -0.16 LEU 33

ALA 432 0.50 VAL 97 -0.19 LEU 33

ALA 432 0.49 THR 98 -0.26 LEU 33

ALA 432 0.49 GLY 99 -0.30 LEU 33

ALA 432 0.45 GLN 100 -0.28 LEU 33

ALA 432 0.42 ILE 101 -0.23 LEU 33

ALA 432 0.41 PRO 102 -0.20 LEU 33

ALA 432 0.38 THR 103 -0.20 LEU 33

ALA 432 0.36 GLY 104 -0.17 LEU 33

ALA 432 0.37 ALA 105 -0.17 LEU 33

ALA 432 0.40 GLN 106 -0.18 LEU 33

ALA 432 0.38 VAL 107 -0.15 LEU 33

ALA 432 0.36 SER 108 -0.13 LEU 33

ALA 432 0.38 TRP 109 -0.15 LEU 33

ALA 432 0.39 LEU 110 -0.13 LEU 33

ALA 432 0.36 SER 111 -0.10 LEU 33

ALA 432 0.36 LYS 112 -0.11 LEU 33

ALA 432 0.38 GLU 113 -0.12 LEU 33

ALA 432 0.38 TRP 114 -0.12 PRO 422

ALA 432 0.35 ALA 115 -0.13 PRO 422

ALA 432 0.36 LYS 116 -0.10 PRO 422

ALA 432 0.38 ARG 117 -0.11 PRO 422

ALA 432 0.36 ALA 118 -0.15 PRO 422

GLY 30 0.36 ALA 119 -0.16 PRO 422

GLY 30 0.38 LEU 120 -0.20 PRO 422

GLY 30 0.38 PRO 121 -0.19 PRO 422

GLY 30 0.37 SER 122 -0.20 PRO 422

GLY 30 0.40 HIS 123 -0.23 PRO 422

GLY 30 0.41 VAL 124 -0.26 PRO 422

GLY 30 0.38 VAL 125 -0.26 PRO 422

GLY 30 0.38 THR 126 -0.26 PRO 422

GLY 30 0.41 MET 127 -0.31 PRO 422

GLY 30 0.40 LEU 128 -0.33 PRO 422

GLY 30 0.38 ASP 129 -0.31 PRO 422

GLY 30 0.38 ASN 130 -0.32 PRO 422

GLY 30 0.41 PHE 131 -0.37 PRO 422

GLY 30 0.40 PRO 132 -0.39 PRO 422

GLY 30 0.39 THR 133 -0.41 PRO 422

GLY 30 0.40 ASN 134 -0.45 PRO 422

GLY 30 0.43 LEU 135 -0.48 PRO 422

GLY 30 0.44 HIS 136 -0.51 PRO 422

GLY 30 0.43 PRO 137 -0.47 PRO 422

GLY 30 0.47 MET 138 -0.54 PRO 422

GLY 30 0.48 SER 139 -0.54 PRO 422

GLY 30 0.45 GLN 140 -0.45 PRO 422

GLY 30 0.46 LEU 141 -0.43 PRO 422

GLY 30 0.50 SER 142 -0.48 PRO 422

GLY 30 0.49 ALA 143 -0.42 PRO 422

GLY 30 0.46 ALA 144 -0.34 PRO 422

GLY 30 0.49 ILE 145 -0.32 PRO 422

GLY 30 0.51 THR 146 -0.32 PRO 422

GLY 30 0.48 ALA 147 -0.28 PRO 422

GLY 30 0.46 LEU 148 -0.23 PRO 422

GLY 30 0.50 ASN 149 -0.19 PRO 422

GLY 30 0.47 SER 150 -0.15 PRO 422

GLY 30 0.44 GLU 151 -0.12 PRO 422

GLY 30 0.48 SER 152 -0.08 PRO 422

ALA 432 0.47 ASN 153 -0.13 GLN 35

ALA 432 0.51 PHE 154 -0.15 GLN 35

GLY 30 0.53 ALA 155 -0.14 GLN 35

ALA 432 0.49 ARG 156 -0.17 GLN 35

ALA 432 0.51 ALA 157 -0.23 GLN 35

ALA 432 0.54 TYR 158 -0.24 GLN 35

ALA 432 0.52 ALA 159 -0.24 GLN 35

ALA 432 0.50 GLU 160 -0.27 GLN 35

ALA 432 0.54 GLY 161 -0.33 GLN 35

ALA 432 0.55 ILE 162 -0.33 GLN 35

ALA 432 0.58 LEU 163 -0.40 GLN 35

ALA 432 0.62 ARG 164 -0.41 GLN 35

ALA 432 0.60 THR 165 -0.40 GLN 35

ALA 432 0.56 LYS 166 -0.33 GLN 35

ALA 432 0.58 TYR 167 -0.27 GLN 35

ALA 432 0.56 TRP 168 -0.20 GLN 35

ALA 432 0.52 GLU 169 -0.20 GLN 35

ALA 432 0.51 MET 170 -0.16 GLN 35

ALA 432 0.53 VAL 171 -0.12 LEU 51

ALA 432 0.50 TYR 172 -0.12 LEU 33

ALA 432 0.47 GLU 173 -0.10 LEU 33

ALA 432 0.47 SER 174 -0.08 LEU 51

ALA 432 0.48 ALA 175 -0.08 LEU 51

ALA 432 0.44 MET 176 -0.10 LYS 7

ALA 432 0.42 ASP 177 -0.12 PRO 422

GLY 30 0.45 LEU 178 -0.18 PRO 422

GLY 30 0.42 ILE 179 -0.19 PRO 422

ALA 432 0.38 ALA 180 -0.17 PRO 422

GLY 30 0.39 LYS 181 -0.21 PRO 422

GLY 30 0.41 LEU 182 -0.26 PRO 422

GLY 30 0.38 PRO 183 -0.26 PRO 422

GLY 30 0.37 CYS 184 -0.26 PRO 422

GLY 30 0.40 VAL 185 -0.30 PRO 422

GLY 30 0.40 ALA 186 -0.34 PRO 422

GLY 30 0.36 ALA 187 -0.30 PRO 422

GLY 30 0.37 LYS 188 -0.31 PRO 422

GLY 30 0.39 ILE 189 -0.36 PRO 422

GLY 30 0.37 TYR 190 -0.35 PRO 422

GLY 30 0.34 ARG 191 -0.31 PRO 422

GLY 30 0.36 ASN 192 -0.33 PRO 422

GLY 30 0.37 LEU 193 -0.37 PRO 422

GLY 30 0.35 TYR 194 -0.35 PRO 422

GLY 30 0.32 ARG 195 -0.31 PRO 422

GLY 30 0.32 ALA 196 -0.31 PRO 422

GLY 30 0.34 GLY 197 -0.30 PRO 422

GLY 30 0.32 SER 198 -0.27 PRO 422

GLY 30 0.31 SER 199 -0.25 PRO 422

GLY 30 0.32 ILE 200 -0.25 PRO 422

GLY 30 0.30 GLY 201 -0.22 PRO 422

GLY 30 0.29 ALA 202 -0.19 PRO 422

ALA 432 0.30 ILE 203 -0.17 PRO 422

ALA 432 0.30 ASP 204 -0.15 PRO 422

ALA 432 0.32 SER 205 -0.12 PRO 422

ALA 432 0.31 LYS 206 -0.12 PRO 422

ALA 432 0.31 LEU 207 -0.14 PRO 422

ALA 432 0.33 ASP 208 -0.14 PRO 422

ALA 432 0.34 TRP 209 -0.17 PRO 422

ALA 432 0.32 SER 210 -0.21 PRO 422

ALA 432 0.30 HIS 211 -0.20 PRO 422

ALA 432 0.30 ASN 212 -0.20 PRO 422

GLY 30 0.33 PHE 213 -0.24 PRO 422

GLY 30 0.31 THR 214 -0.25 PRO 422

GLY 30 0.29 ASN 215 -0.22 PRO 422

GLY 30 0.31 MET 216 -0.24 PRO 422

GLY 30 0.32 LEU 217 -0.28 PRO 422

GLY 30 0.30 GLY 218 -0.25 PRO 422

SER 424 0.29 TYR 219 -0.24 PRO 422

SER 424 0.27 THR 220 -0.22 PRO 422

SER 424 0.27 ASP 221 -0.22 PRO 422

SER 424 0.26 ALA 222 -0.20 PRO 422

SER 424 0.27 GLN 223 -0.21 PRO 422

SER 424 0.29 PHE 224 -0.23 PRO 422

SER 424 0.29 THR 225 -0.22 PRO 422

SER 424 0.28 GLU 226 -0.20 PRO 422

SER 424 0.30 LEU 227 -0.24 PRO 422

SER 424 0.31 MET 228 -0.25 PRO 422

ALA 432 0.32 ARG 229 -0.21 PRO 422

ALA 432 0.32 LEU 230 -0.22 PRO 422

GLY 30 0.34 TYR 231 -0.27 PRO 422

GLY 30 0.36 LEU 232 -0.25 PRO 422

ALA 432 0.37 THR 233 -0.20 PRO 422

ALA 432 0.37 ILE 234 -0.23 PRO 422

GLY 30 0.41 HIS 235 -0.31 PRO 422

GLY 30 0.43 SER 236 -0.25 PRO 422

GLY 30 0.49 ASP 237 -0.22 PRO 422

GLY 30 0.51 HIS 238 -0.24 PRO 422

GLY 30 0.59 GLU 239 -0.21 LYS 423

GLY 30 0.68 GLY 240 -0.11 LYS 423

GLY 30 0.67 GLY 241 -0.24 LYS 423

GLY 30 0.62 ASN 242 -0.48 PRO 422

GLY 30 0.64 VAL 243 -0.66 PRO 422

GLY 30 0.60 SER 244 -0.55 PRO 422

GLY 30 0.64 ALA 245 -0.32 PRO 422

GLY 30 0.73 HIS 246 -0.30 PRO 422

GLY 30 0.70 THR 247 -0.47 PRO 422

GLY 30 0.67 SER 248 -0.27 PRO 422

GLY 30 0.76 HIS 249 -0.06 PRO 418

GLY 30 0.81 LEU 250 -0.07 PRO 422

GLY 30 0.73 VAL 251 -0.15 PRO 422

GLY 30 0.71 GLY 252 -0.08 LEU 51

GLY 30 0.80 SER 253 -0.12 LEU 51

GLY 30 0.76 ALA 254 -0.09 GLN 35

GLY 30 0.69 LEU 255 -0.15 GLN 35

GLY 30 0.65 SER 256 -0.07 LEU 51

GLY 30 0.58 ASP 257 -0.08 LEU 51

GLY 30 0.57 PRO 258 -0.11 PRO 422

GLY 30 0.54 TYR 259 -0.21 PRO 422

GLY 30 0.58 LEU 260 -0.24 PRO 422

GLY 30 0.62 SER 261 -0.26 PRO 422

GLY 30 0.57 PHE 262 -0.34 PRO 422

GLY 30 0.55 ALA 263 -0.44 PRO 422

GLY 30 0.61 ALA 264 -0.55 PRO 422

GLY 30 0.60 ALA 265 -0.53 PRO 422

GLY 30 0.55 MET 266 -0.59 PRO 422

GLY 30 0.57 ASN 267 -0.73 PRO 422

SER 424 0.60 GLY 268 -0.82 PRO 422

GLY 30 0.54 LEU 269 -0.67 PRO 422

GLY 43 0.54 ALA 270 -0.72 PRO 422

GLY 43 0.63 GLY 271 -0.84 PRO 422

GLY 43 0.66 PRO 272 -0.77 PRO 422

GLY 43 0.76 LEU 273 -0.76 PRO 422

GLY 43 0.65 HIS 274 -0.69 PRO 422

GLY 43 0.56 GLY 275 -0.63 PRO 422

GLY 43 0.56 LEU 276 -0.57 PRO 422

GLY 43 0.55 ALA 277 -0.49 PRO 422

GLY 43 0.47 ASN 278 -0.43 PRO 422

GLY 43 0.49 GLN 279 -0.46 PRO 422

GLY 43 0.53 GLU 280 -0.47 PRO 422

ASP 39 0.49 VAL 281 -0.40 PRO 422

ASP 39 0.44 LEU 282 -0.38 PRO 422

ASP 39 0.47 GLY 283 -0.40 PRO 422

ASP 39 0.49 TRP 284 -0.38 PRO 422

ASP 39 0.44 LEU 285 -0.34 PRO 422

ASP 39 0.43 ALA 286 -0.35 PRO 422

ASP 39 0.45 GLN 287 -0.34 PRO 422

GLN 35 0.44 LEU 288 -0.32 PRO 422

ASP 39 0.40 GLN 289 -0.31 PRO 422

ASP 39 0.40 LYS 290 -0.30 PRO 422

ASP 39 0.42 ALA 291 -0.30 PRO 422

GLN 35 0.36 ALA 295 -0.24 PRO 422

GLN 35 0.39 GLY 296 -0.24 PRO 422

GLN 35 0.40 ALA 297 -0.23 PRO 422

GLN 35 0.42 ASP 298 -0.23 PRO 422

GLN 35 0.43 ALA 299 -0.23 PRO 422

GLN 35 0.43 SER 300 -0.25 PRO 422

GLN 35 0.45 LEU 301 -0.27 PRO 422

GLN 35 0.48 ARG 302 -0.25 PRO 422

GLN 35 0.48 ASP 303 -0.26 PRO 422

GLN 35 0.48 TYR 304 -0.29 PRO 422

GLN 35 0.52 ILE 305 -0.30 PRO 422

GLN 35 0.53 TRP 306 -0.28 PRO 422

GLN 35 0.53 ASN 307 -0.29 PRO 422

GLN 35 0.54 THR 308 -0.32 PRO 422

GLN 35 0.59 LEU 309 -0.32 PRO 422

GLN 35 0.58 ASN 310 -0.29 PRO 422

GLN 35 0.57 SER 311 -0.32 PRO 422

ASP 39 0.62 GLY 312 -0.34 PRO 422

ASP 39 0.60 ARG 313 -0.37 PRO 422

GLN 35 0.60 VAL 314 -0.38 PRO 422

GLN 35 0.56 VAL 315 -0.37 PRO 422

GLN 35 0.55 PRO 316 -0.40 PRO 422

GLN 35 0.55 GLY 317 -0.37 PRO 422

GLN 35 0.58 TYR 318 -0.33 PRO 422

GLN 35 0.65 GLY 319 -0.32 PRO 422

GLN 35 0.68 HIS 320 -0.31 PRO 422

GLN 35 0.79 ALA 321 -0.32 LYS 423

GLN 35 0.74 VAL 322 -0.40 LYS 423

GLN 35 0.63 LEU 323 -0.34 LYS 423

GLN 35 0.60 ARG 324 -0.36 LYS 423

GLN 35 0.53 LYS 325 -0.31 LYS 423

GLN 35 0.49 THR 326 -0.25 LYS 423

GLN 35 0.48 ASP 327 -0.23 PRO 422

GLN 35 0.41 PRO 328 -0.21 LYS 423

GLN 35 0.39 ARG 329 -0.24 PRO 422

GLN 35 0.42 TYR 330 -0.26 PRO 422

GLN 35 0.39 THR 331 -0.21 PRO 422

GLN 35 0.34 CYS 332 -0.21 PRO 422

GLN 35 0.34 GLN 333 -0.24 PRO 422

GLN 35 0.35 ARG 334 -0.23 PRO 422

GLN 35 0.32 GLU 335 -0.19 PRO 422

GLN 35 0.30 PHE 336 -0.21 PRO 422

GLN 35 0.31 ALA 337 -0.23 PRO 422

GLN 35 0.30 LEU 338 -0.20 PRO 422

GLN 35 0.27 LYS 339 -0.19 PRO 422

GLN 35 0.27 HIS 340 -0.21 PRO 422

GLN 35 0.29 LEU 341 -0.23 PRO 422

GLN 35 0.30 PRO 342 -0.21 PRO 422

GLN 35 0.31 GLY 343 -0.22 PRO 422

GLN 35 0.32 ASP 344 -0.24 PRO 422

GLN 35 0.34 PRO 345 -0.26 PRO 422

GLN 35 0.36 MET 346 -0.28 PRO 422

GLN 35 0.36 PHE 347 -0.27 PRO 422

GLN 35 0.37 LYS 348 -0.25 PRO 422

GLN 35 0.40 LEU 349 -0.27 PRO 422

GLN 35 0.41 VAL 350 -0.28 PRO 422

GLN 35 0.41 ALA 351 -0.25 PRO 422

GLN 35 0.42 GLN 352 -0.25 PRO 422

GLN 35 0.46 LEU 353 -0.27 PRO 422

GLN 35 0.46 TYR 354 -0.25 PRO 422

GLN 35 0.45 LYS 355 -0.22 PRO 422

GLN 35 0.48 ILE 356 -0.24 PRO 422

GLN 35 0.52 VAL 357 -0.27 PRO 422

GLN 35 0.54 PRO 358 -0.24 PRO 422

GLN 35 0.53 ASN 359 -0.22 PRO 422

GLN 35 0.55 VAL 360 -0.25 PRO 422

GLN 35 0.60 LEU 361 -0.26 PRO 422

GLN 35 0.61 LEU 362 -0.25 LYS 423

GLN 35 0.58 GLU 363 -0.23 LYS 423

GLN 35 0.61 GLN 364 -0.25 PRO 422

GLN 35 0.67 GLY 365 -0.25 LYS 423

GLN 35 0.69 ALA 366 -0.28 PRO 422

GLN 35 0.69 ALA 367 -0.28 LYS 423

GLN 35 0.70 ALA 368 -0.34 LYS 423

GLN 35 0.65 ASN 369 -0.30 LYS 423

GLN 35 0.61 PRO 370 -0.25 PRO 422

GLN 35 0.55 TRP 371 -0.25 PRO 422

GLN 35 0.53 PRO 372 -0.29 PRO 422

GLN 35 0.51 ASN 373 -0.31 PRO 422

GLN 35 0.44 VAL 374 -0.32 PRO 422

GLN 35 0.46 ASP 375 -0.38 PRO 422

GLN 35 0.46 ALA 376 -0.34 PRO 422

GLN 35 0.41 HIS 377 -0.31 PRO 422

GLN 35 0.37 SER 378 -0.32 PRO 422

GLY 43 0.38 GLY 379 -0.35 PRO 422

GLN 35 0.36 VAL 380 -0.32 PRO 422

GLN 35 0.33 LEU 381 -0.29 PRO 422

GLY 43 0.34 LEU 382 -0.32 PRO 422

GLY 43 0.34 GLN 383 -0.32 PRO 422

ASP 39 0.31 TYR 384 -0.28 PRO 422

SER 424 0.30 TYR 385 -0.27 PRO 422

GLY 43 0.31 GLY 386 -0.30 PRO 422

GLY 43 0.34 MET 387 -0.33 PRO 422

GLY 43 0.36 THR 388 -0.35 PRO 422

GLY 43 0.38 GLU 389 -0.39 PRO 422

GLY 43 0.42 MET 390 -0.42 PRO 422

GLY 43 0.44 ASN 391 -0.47 PRO 422

GLY 43 0.41 TYR 392 -0.44 PRO 422

GLY 43 0.41 TYR 393 -0.42 PRO 422

GLY 43 0.44 THR 394 -0.49 PRO 422

GLY 30 0.43 VAL 395 -0.43 PRO 422

GLY 30 0.40 LEU 396 -0.38 PRO 422

GLY 30 0.44 PHE 397 -0.41 PRO 422

GLY 30 0.47 GLY 398 -0.42 PRO 422

GLY 30 0.43 VAL 399 -0.33 PRO 422

GLY 30 0.43 SER 400 -0.30 PRO 422

GLY 30 0.49 ARG 401 -0.32 PRO 422

GLY 30 0.48 ALA 402 -0.26 PRO 422

GLY 30 0.45 LEU 403 -0.18 PRO 422

GLY 30 0.50 GLY 404 -0.16 PRO 422

GLY 30 0.57 VAL 405 -0.18 PRO 422

GLY 30 0.54 LEU 406 -0.11 PRO 422

ALA 432 0.51 ALA 407 -0.10 LEU 51

GLY 30 0.59 GLN 408 -0.15 LEU 51

GLY 30 0.62 LEU 409 -0.15 LEU 51

ALA 432 0.56 ILE 410 -0.16 LEU 51

ALA 432 0.60 TRP 411 -0.21 LEU 51

GLY 30 0.73 SER 412 -0.26 LEU 51

GLY 30 0.66 ARG 413 -0.22 LEU 51

ALA 432 0.61 ALA 414 -0.23 GLY 50

GLY 30 0.65 LEU 415 -0.35 GLY 50

GLY 30 0.74 GLY 416 -0.34 GLN 35

GLY 30 0.90 PHE 417 -0.32 GLY 50

GLY 30 0.94 PRO 418 -0.33 ILE 36

GLY 30 0.94 LEU 419 -0.25 GLU 420

GLY 30 1.00 GLU 420 -0.25 LEU 419

GLY 30 1.07 ARG 421 -0.18 GLY 241

GLY 30 1.33 PRO 422 -0.84 GLY 271

PRO 422 1.18 LYS 423 -1.61 ARG 46

LYS 423 1.14 SER 424 -0.03 VAL 38

ALA 432 0.95 MET 425 0.00 ALA 1

ALA 432 0.91 SER 426 0.00 ALA 1

ALA 432 0.91 THR 427 -0.15 GLY 365

ALA 32 0.96 ASP 428 -0.26 GLY 312

ALA 32 1.11 GLY 429 -0.00 SER 311

ALA 32 1.12 LEU 430 0.00 ALA 1

ALA 32 1.08 ILE 431 -0.28 GLY 312

ALA 32 1.28 ALA 432 -0.02 SER 311

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.

*** open cutoff 10 melek new ***

CA distance fluctuations for 260522120818411546

--- normal mode 11 ---

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

* open cutoff 10 melek new *