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

* secYG_ALPHA_SECE_ITASSER_NEMO_RE *

CA distance fluctuations for 260812054906533160

--- normal mode 22 ---

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
LEU 422 0.69 MET 1 -0.46 LYS 174

ARG 418 0.72 ASN 2 -0.32 GLY 10

SER 420 0.39 VAL 3 -0.40 GLY 10

GLY 417 0.73 GLY 4 -0.38 TRP 429

LEU 103 0.47 ALA 5 -0.33 LEU 214

LEU 103 0.46 ARG 6 -0.51 GLY 10

LEU 103 0.57 GLY 7 -0.40 LYS 425

LEU 103 0.56 ASN 8 -0.37 PHE 221

LEU 103 0.56 ALA 9 -0.39 ARG 6

LEU 103 0.65 GLY 10 -0.53 LYS 425

LEU 103 0.63 LEU 11 -0.43 LYS 425

LEU 103 0.56 PHE 12 -0.41 PRO 193

LEU 103 0.58 TRP 13 -0.46 LYS 425

LEU 103 0.65 ARG 14 -0.50 LYS 425

LEU 103 0.57 PHE 15 -0.38 ILE 189

LEU 103 0.50 GLY 16 -0.38 LYS 425

LEU 103 0.52 PHE 17 -0.46 LYS 425

LEU 103 0.54 THR 18 -0.42 LYS 425

GLU 102 0.48 LEU 19 -0.35 LYS 425

LEU 103 0.42 LEU 20 -0.39 LYS 425

LEU 103 0.42 ALA 21 -0.42 LYS 425

GLU 102 0.43 LEU 22 -0.38 LYS 425

GLU 102 0.36 ILE 23 -0.35 LYS 425

LEU 103 0.31 VAL 24 -0.37 LYS 425

GLU 102 0.33 TYR 25 -0.37 LYS 425

GLU 102 0.32 ARG 26 -0.35 LYS 425

GLU 102 0.27 LEU 27 -0.33 LYS 425

GLU 102 0.25 GLY 28 -0.34 LYS 425

GLU 102 0.26 THR 29 -0.32 LYS 425

GLU 102 0.23 TYR 30 -0.31 LYS 425

GLU 102 0.19 ILE 31 -0.31 LYS 425

GLU 102 0.17 PRO 32 -0.30 LYS 425

GLU 102 0.14 ILE 33 -0.29 LYS 425

GLU 102 0.12 PRO 34 -0.28 LYS 425

GLU 102 0.11 GLY 35 -0.26 LYS 425

GLU 102 0.13 VAL 36 -0.27 LYS 425

GLU 102 0.14 ASN 37 -0.26 LYS 425

GLU 102 0.17 PRO 38 -0.28 LYS 425

GLU 102 0.17 SER 39 -0.27 LYS 425

GLU 102 0.16 VAL 40 -0.26 LYS 425

GLU 102 0.17 VAL 41 -0.27 LYS 425

GLU 102 0.19 GLU 42 -0.27 LYS 425

GLU 102 0.18 ASP 43 -0.26 LYS 425

GLU 102 0.18 ILE 44 -0.25 LYS 425

GLU 102 0.20 ILE 45 -0.27 LYS 425

GLU 102 0.21 SER 46 -0.26 LYS 425

GLU 102 0.19 SER 47 -0.25 LYS 425

GLU 102 0.20 HIS 48 -0.25 LYS 425

GLU 102 0.22 ALA 49 -0.26 LYS 425

GLU 102 0.22 THR 50 -0.26 LYS 425

GLU 102 0.22 GLY 51 -0.26 LYS 425

GLU 102 0.22 VAL 52 -0.28 LYS 425

GLU 102 0.22 LEU 53 -0.28 LYS 425

GLU 102 0.25 GLY 54 -0.28 LYS 425

GLU 102 0.28 ILE 55 -0.29 LYS 425

GLU 102 0.27 PHE 56 -0.30 LYS 425

GLU 102 0.27 ASN 57 -0.30 LYS 425

GLU 102 0.31 VAL 58 -0.31 LYS 425

GLU 102 0.34 PHE 59 -0.33 LYS 425

GLU 102 0.31 SER 60 -0.33 LYS 425

GLU 102 0.32 GLY 61 -0.33 LYS 425

GLU 102 0.27 GLY 62 -0.31 LYS 425

GLU 102 0.25 ALA 63 -0.31 LYS 425

GLU 102 0.23 LEU 64 -0.30 LYS 425

GLU 102 0.22 GLY 65 -0.29 LYS 425

GLU 102 0.20 ARG 66 -0.29 LYS 425

GLU 102 0.19 MET 67 -0.29 LYS 425

GLU 102 0.19 THR 68 -0.31 LYS 425

GLU 102 0.18 ILE 69 -0.32 LYS 425

GLU 102 0.23 PHE 70 -0.34 LYS 425

GLU 102 0.22 ALA 71 -0.32 LYS 425

GLU 102 0.22 LEU 72 -0.33 LYS 425

GLU 102 0.28 ASN 73 -0.35 LYS 425

GLU 102 0.32 VAL 74 -0.37 SER 420

GLU 102 0.28 MET 75 -0.35 SER 420

ARG 105 0.20 PRO 76 -0.36 SER 420

ARG 105 0.27 TYR 77 -0.39 SER 420

ARG 105 0.32 ILE 78 -0.39 SER 420

ARG 105 0.23 VAL 79 -0.36 SER 420

ARG 105 0.20 SER 80 -0.37 SER 420

ARG 105 0.33 SER 81 -0.40 SER 420

ARG 105 0.27 ILE 82 -0.38 SER 420

GLU 331 0.16 ILE 83 -0.35 SER 420

GLU 331 0.19 VAL 84 -0.36 SER 420

ARG 105 0.25 GLN 85 -0.38 SER 420

GLU 331 0.18 LEU 86 -0.34 SER 420

GLU 331 0.20 LEU 87 -0.32 SER 420

GLU 331 0.25 SER 88 -0.32 SER 420

LYS 330 0.22 VAL 89 -0.32 SER 420

GLU 334 0.21 ALA 90 -0.28 SER 420

GLU 334 0.27 ILE 91 -0.24 LYS 424

GLU 334 0.34 PRO 92 -0.22 LYS 424

GLU 334 0.34 THR 93 -0.20 LYS 424

GLU 331 0.31 LEU 94 -0.26 LYS 424

GLU 331 0.38 ASN 95 -0.28 LYS 424

GLU 331 0.44 GLU 96 -0.22 LYS 424

MET 335 0.41 MET 97 -0.23 LYS 424

GLU 331 0.41 ARG 98 -0.33 LYS 424

GLU 331 0.58 GLN 99 -0.30 LYS 424

MET 335 0.62 ASP 100 -0.17 LYS 424

ASP 405 0.64 GLY 101 -0.29 LYS 424

ASN 178 0.82 GLU 102 -0.30 LYS 424

ALA 173 0.87 LEU 103 -0.15 LYS 424

ALA 173 0.60 GLY 104 -0.23 LYS 424

ASN 178 0.55 ARG 105 -0.40 LYS 424

ASN 172 0.79 MET 106 -0.33 LYS 424

ALA 173 0.63 LYS 107 -0.25 LYS 424

ALA 173 0.35 MET 108 -0.35 LYS 424

GLU 169 0.32 SER 109 -0.42 SER 420

ALA 173 0.37 THR 110 -0.35 SER 420

ALA 173 0.25 TYR 111 -0.33 SER 420

GLU 331 0.17 THR 112 -0.39 SER 420

LYS 338 0.15 ARG 113 -0.39 SER 420

LYS 338 0.16 TYR 114 -0.35 SER 420

GLU 331 0.16 LEU 115 -0.34 SER 420

GLU 331 0.15 SER 116 -0.36 SER 420

LYS 338 0.14 VAL 117 -0.34 SER 420

GLU 334 0.14 ALA 118 -0.31 SER 420

GLU 331 0.14 PHE 119 -0.32 SER 420

ASN 252 0.13 CYS 120 -0.32 LYS 425

GLU 331 0.12 ILE 121 -0.30 LYS 425

GLU 331 0.13 ALA 122 -0.29 LYS 425

ARG 105 0.13 GLN 123 -0.30 LYS 425

ASN 252 0.12 GLY 124 -0.30 LYS 425

GLU 331 0.12 LEU 125 -0.28 LYS 425

GLU 331 0.11 VAL 126 -0.27 LYS 425

GLU 102 0.14 ILE 127 -0.28 LYS 425

GLU 102 0.11 LEU 128 -0.27 LYS 425

ASN 252 0.11 LEU 129 -0.26 LYS 425

GLU 102 0.12 GLY 130 -0.26 LYS 425

GLU 102 0.12 LEU 131 -0.26 LYS 425

GLU 102 0.10 GLU 132 -0.25 LYS 425

GLU 102 0.10 ARG 133 -0.24 LYS 425

GLU 102 0.12 MET 134 -0.24 LYS 425

GLU 102 0.11 ASN 135 -0.24 LYS 425

GLU 102 0.11 SER 136 -0.23 LYS 425

GLU 102 0.10 ASP 137 -0.22 LYS 425

GLU 102 0.11 GLU 138 -0.23 LYS 425

GLU 102 0.12 VAL 139 -0.24 LYS 425

GLU 102 0.11 MET 140 -0.24 LYS 425

GLU 102 0.13 VAL 141 -0.25 LYS 425

GLU 102 0.11 VAL 142 -0.25 LYS 425

GLU 102 0.10 ILE 143 -0.24 LYS 425

ASN 252 0.10 ASN 144 -0.24 LYS 425

ASN 252 0.10 PRO 145 -0.24 LYS 425

ASN 252 0.10 GLY 146 -0.24 LYS 425

LYS 338 0.11 ILE 147 -0.24 LYS 425

ASN 252 0.11 MET 148 -0.25 LYS 425

ASN 252 0.11 PHE 149 -0.26 LYS 425

ASN 252 0.11 ARG 150 -0.26 LYS 425

ASN 252 0.12 VAL 151 -0.27 LYS 425

ASN 252 0.12 VAL 152 -0.28 LYS 425

ASN 252 0.12 GLY 153 -0.29 LYS 425

ASN 252 0.12 ILE 154 -0.29 LYS 425

ASN 252 0.13 SER 155 -0.30 LYS 425

ASN 252 0.13 SER 156 -0.31 LYS 425

GLU 102 0.14 LEU 157 -0.32 LYS 425

ASN 252 0.13 LEU 158 -0.33 LYS 425

ASN 252 0.14 ALA 159 -0.34 LYS 425

GLU 102 0.17 GLY 160 -0.35 LYS 425

MET 106 0.20 THR 161 -0.36 LYS 425

MET 106 0.18 MET 162 -0.38 LYS 425

MET 106 0.22 PHE 163 -0.39 LYS 425

MET 106 0.30 LEU 164 -0.40 LYS 425

MET 106 0.35 LEU 165 -0.43 SER 420

MET 106 0.34 TRP 166 -0.46 SER 420

MET 106 0.40 LEU 167 -0.45 LYS 425

MET 106 0.53 GLY 168 -0.48 SER 420

MET 106 0.65 GLU 169 -0.55 SER 420

LEU 103 0.54 ARG 170 -0.54 SER 420

LEU 103 0.62 ILE 171 -0.52 SER 420

LEU 103 0.81 ASN 172 -0.63 SER 420

LEU 103 0.87 ALA 173 -0.71 SER 420

LEU 103 0.73 LYS 174 -0.65 ALA 421

LEU 103 0.71 GLY 175 -0.54 ALA 421

GLU 102 0.75 ILE 176 -0.50 GLY 417

GLU 102 0.80 GLY 177 -0.47 SER 420

GLU 102 0.82 ASN 178 -0.51 SER 420

GLU 102 0.63 GLY 179 -0.49 SER 420

GLU 102 0.57 ILE 180 -0.44 SER 420

GLU 102 0.62 SER 181 -0.41 SER 420

GLU 102 0.58 LEU 182 -0.40 SER 420

GLU 102 0.47 ILE 183 -0.39 LYS 425

GLU 102 0.46 ILE 184 -0.37 LYS 425

GLU 102 0.49 PHE 185 -0.36 LYS 425

GLU 102 0.43 VAL 186 -0.36 LYS 425

GLU 102 0.37 GLY 187 -0.35 LYS 425

GLU 102 0.39 ILE 188 -0.33 LYS 425

GLU 102 0.39 ILE 189 -0.39 PHE 12

GLU 102 0.33 SER 190 -0.37 PHE 12

GLU 102 0.31 GLU 191 -0.33 PHE 12

GLU 102 0.33 LEU 192 -0.38 PHE 12

GLU 102 0.29 PRO 193 -0.41 PHE 12

GLU 102 0.26 SER 194 -0.35 PHE 12

GLU 102 0.28 SER 195 -0.34 PHE 12

GLU 102 0.28 ILE 196 -0.38 PHE 12

GLU 102 0.24 SER 197 -0.38 PHE 12

GLU 102 0.24 SER 198 -0.33 PHE 12

GLU 102 0.25 VAL 199 -0.34 PHE 12

GLU 102 0.24 PHE 200 -0.37 PHE 12

GLU 102 0.21 LEU 201 -0.35 PHE 12

GLU 102 0.22 LEU 202 -0.31 PHE 12

GLU 102 0.23 GLY 203 -0.33 ALA 9

GLU 102 0.20 LYS 204 -0.34 ALA 9

GLU 102 0.19 ASN 205 -0.31 ALA 9

GLU 102 0.20 GLY 206 -0.30 ALA 9

GLU 102 0.21 GLU 207 -0.28 ALA 9

GLU 102 0.23 VAL 208 -0.29 ALA 9

GLU 102 0.23 SER 209 -0.31 ALA 9

GLU 102 0.23 GLY 210 -0.35 ALA 9

GLU 102 0.25 LEU 211 -0.33 ASN 8

GLU 102 0.26 VAL 212 -0.31 ASN 8

GLU 102 0.26 VAL 213 -0.33 ASN 8

GLU 102 0.26 LEU 214 -0.36 ASN 8

GLU 102 0.29 SER 215 -0.33 ASN 8

GLU 102 0.30 MET 216 -0.32 ASN 8

GLU 102 0.30 LEU 217 -0.37 ASN 8

GLU 102 0.32 LEU 218 -0.36 ASN 8

GLU 102 0.34 ALA 219 -0.31 ASN 8

GLU 102 0.35 PHE 220 -0.33 ASN 8

GLU 102 0.36 PHE 221 -0.37 ASN 8

GLU 102 0.37 ALA 222 -0.33 ASN 8

GLU 102 0.39 LEU 223 -0.31 ASN 8

GLU 102 0.42 PHE 224 -0.35 ASN 8

GLU 102 0.42 LEU 225 -0.36 ASN 8

GLU 102 0.42 LEU 226 -0.32 LYS 433

GLU 102 0.46 ILE 227 -0.32 TRP 429

GLU 102 0.49 ILE 228 -0.35 ASN 8

GLU 102 0.46 PHE 229 -0.35 LYS 433

GLU 102 0.47 PHE 230 -0.34 LYS 433

GLU 102 0.54 GLU 231 -0.36 TRP 429

GLU 102 0.54 ARG 232 -0.38 LYS 433

GLU 102 0.49 SER 233 -0.38 LYS 433

GLU 102 0.50 TYR 234 -0.39 LYS 433

GLY 101 0.45 ARG 235 -0.39 LYS 433

GLY 101 0.47 LYS 236 -0.41 LYS 433

GLY 101 0.46 VAL 237 -0.39 LYS 433

GLY 101 0.44 PHE 238 -0.39 LYS 433

GLY 101 0.46 VAL 239 -0.38 LYS 433

GLY 101 0.42 GLN 240 -0.36 LYS 433

ASP 100 0.42 TYR 241 -0.35 LYS 433

ASP 100 0.35 PRO 242 -0.27 LYS 433

MET 1 0.34 LYS 243 -0.28 LYS 433

MET 1 0.26 ARG 244 -0.36 ASN 339

MET 1 0.29 GLN 245 -0.35 LYS 433

MET 1 0.25 THR 246 -0.42 LYS 433

MET 1 0.27 GLY 247 -0.44 LYS 433

MET 1 0.34 GLY 248 -0.39 LYS 433

MET 1 0.42 ARG 249 -0.40 LYS 433

MET 1 0.44 PHE 250 -0.37 LYS 433

MET 1 0.47 TYR 251 -0.40 LYS 433

MET 1 0.52 ASN 252 -0.35 LYS 433

GLY 101 0.43 SER 253 -0.36 LYS 433

GLY 101 0.49 ASP 254 -0.45 LYS 433

GLY 101 0.45 SER 255 -0.44 LYS 433

GLY 101 0.51 SER 256 -0.46 LYS 433

GLY 101 0.52 TYR 257 -0.44 LYS 433

GLY 101 0.58 ILE 258 -0.44 LYS 433

GLY 101 0.57 PRO 259 -0.42 LYS 433

GLY 101 0.54 LEU 260 -0.39 LYS 433

GLU 102 0.55 LYS 261 -0.41 TYR 415

GLU 102 0.47 ILE 262 -0.35 TRP 429

GLU 102 0.51 ASN 263 -0.37 TYR 415

GLU 102 0.56 THR 264 -0.42 TYR 419

GLU 102 0.54 ALA 265 -0.41 TYR 419

GLU 102 0.61 GLY 266 -0.40 SER 416

GLU 102 0.55 VAL 267 -0.37 SER 420

GLU 102 0.50 ILE 268 -0.41 SER 420

GLU 102 0.40 PRO 269 -0.36 SER 420

GLU 102 0.38 PRO 270 -0.34 SER 420

GLU 102 0.39 ILE 271 -0.36 SER 420

GLU 102 0.32 PHE 272 -0.36 SER 420

GLU 102 0.28 ALA 273 -0.33 SER 420

GLU 102 0.29 ASN 274 -0.32 SER 420

GLU 102 0.26 ALA 275 -0.34 SER 420

GLU 102 0.21 LEU 276 -0.32 SER 420

GLU 102 0.21 LEU 277 -0.30 SER 420

GLU 102 0.21 LEU 278 -0.30 SER 420

GLU 102 0.17 SER 279 -0.30 SER 420

GLU 102 0.15 SER 280 -0.28 SER 420

GLU 102 0.15 ILE 281 -0.27 LYS 425

GLU 102 0.14 SER 282 -0.28 LYS 425

GLU 102 0.11 LEU 283 -0.27 LYS 425

GLU 102 0.11 VAL 284 -0.26 LYS 425

GLU 102 0.12 ARG 285 -0.26 LYS 425

GLU 102 0.09 PHE 286 -0.26 LYS 425

GLU 331 0.09 HIS 287 -0.24 LYS 425

GLU 102 0.09 SER 288 -0.24 LYS 425

GLU 102 0.08 GLY 289 -0.23 LYS 425

GLU 334 0.08 SER 290 -0.22 LYS 425

GLU 102 0.08 GLU 291 -0.22 LYS 425

GLU 102 0.08 TRP 292 -0.22 LYS 425

GLU 102 0.09 ALA 293 -0.24 LYS 425

GLU 102 0.10 ASP 294 -0.23 LYS 425

GLU 102 0.11 VAL 295 -0.23 LYS 425

GLU 102 0.12 LEU 296 -0.24 LYS 425

GLU 102 0.13 LEU 297 -0.25 LYS 425

GLU 102 0.14 ARG 298 -0.24 LYS 425

GLU 102 0.15 TYR 299 -0.24 LYS 425

GLU 102 0.16 LEU 300 -0.25 LYS 425

GLU 102 0.18 SER 301 -0.25 LYS 425

GLU 102 0.21 SER 302 -0.26 LYS 425

GLU 102 0.21 GLU 303 -0.25 TRP 429

GLU 102 0.19 GLY 304 -0.24 TRP 429

GLU 102 0.19 ILE 305 -0.24 TRP 429

GLU 102 0.18 LEU 306 -0.24 TRP 429

GLU 102 0.20 TYR 307 -0.26 LYS 425

GLU 102 0.23 VAL 308 -0.26 TRP 429

GLU 102 0.21 SER 309 -0.25 TRP 429

GLU 102 0.20 VAL 310 -0.26 SER 420

GLU 102 0.25 TYR 311 -0.28 SER 420

GLU 102 0.26 ILE 312 -0.27 TRP 429

GLU 102 0.23 ALA 313 -0.27 SER 420

GLU 102 0.24 LEU 314 -0.30 SER 420

GLU 102 0.31 ILE 315 -0.31 SER 420

GLU 102 0.29 MET 316 -0.29 SER 420

GLU 102 0.24 PHE 317 -0.31 SER 420

GLU 102 0.30 PHE 318 -0.34 SER 420

GLU 102 0.36 THR 319 -0.34 SER 420

GLU 102 0.29 PHE 320 -0.33 TYR 419

GLU 102 0.26 PHE 321 -0.35 SER 420

GLU 102 0.36 TYR 322 -0.39 SER 420

GLY 101 0.41 THR 323 -0.39 TYR 419

GLY 101 0.31 SER 324 -0.38 TYR 419

GLY 101 0.33 LEU 325 -0.41 TYR 419

GLY 101 0.55 VAL 326 -0.46 TYR 419

GLY 101 0.53 PHE 327 -0.43 TYR 419

GLY 101 0.46 ASP 328 -0.38 TYR 419

GLY 101 0.40 THR 329 -0.35 TYR 419

GLN 99 0.37 LYS 330 -0.33 MET 423

GLN 99 0.58 GLU 331 -0.35 MET 423

GLY 101 0.52 THR 332 -0.37 TYR 419

ASP 100 0.42 SER 333 -0.32 LYS 430

ASP 100 0.49 GLU 334 -0.30 MET 423

ASP 100 0.62 MET 335 -0.34 MET 423

ASP 100 0.52 LEU 336 -0.34 LYS 430

ASP 100 0.46 LYS 337 -0.28 LYS 430

ASP 100 0.52 LYS 338 -0.32 ARG 244

ASP 100 0.54 ASN 339 -0.36 ARG 244

ASP 100 0.44 GLY 340 -0.33 ARG 244

ASP 100 0.45 GLY 341 -0.33 LYS 433

ASP 100 0.39 PHE 342 -0.31 LYS 433

GLY 101 0.39 VAL 343 -0.32 LYS 433

GLY 101 0.35 PRO 344 -0.30 LYS 433

GLY 101 0.30 GLY 345 -0.27 LYS 433

GLY 101 0.30 LYS 346 -0.26 LYS 433

ASP 100 0.29 ARG 347 -0.24 LYS 433

ASP 100 0.34 PRO 348 -0.25 LYS 433

ASP 100 0.31 GLY 349 -0.25 LYS 430

ASP 100 0.25 LYS 350 -0.24 LYS 430

GLY 101 0.26 ALA 351 -0.25 LYS 433

GLY 101 0.32 THR 352 -0.28 LYS 433

GLY 101 0.32 LYS 353 -0.28 LYS 430

GLY 101 0.27 GLU 354 -0.27 LYS 433

GLY 101 0.31 TYR 355 -0.29 LYS 433

GLY 101 0.37 PHE 356 -0.31 LYS 433

GLY 101 0.31 ASP 357 -0.30 TYR 419

GLY 101 0.29 GLN 358 -0.29 LYS 433

GLY 101 0.35 VAL 359 -0.32 LYS 433

GLY 101 0.38 ILE 360 -0.32 TYR 419

GLY 101 0.31 GLY 361 -0.29 TYR 419

GLY 101 0.31 ARG 362 -0.30 LYS 433

GLU 102 0.37 ILE 363 -0.32 LYS 433

GLU 102 0.36 THR 364 -0.31 TRP 429

GLU 102 0.31 VAL 365 -0.29 TRP 429

GLU 102 0.35 LEU 366 -0.30 LYS 433

GLU 102 0.40 GLY 367 -0.32 TRP 429

GLU 102 0.35 ALA 368 -0.30 TRP 429

GLU 102 0.33 ILE 369 -0.29 TRP 429

GLU 102 0.38 TYR 370 -0.30 TRP 429

GLU 102 0.40 LEU 371 -0.31 TRP 429

GLU 102 0.34 SER 372 -0.29 TRP 429

GLU 102 0.34 VAL 373 -0.28 TRP 429

GLU 102 0.38 VAL 374 -0.29 TRP 429

GLU 102 0.36 CYS 375 -0.29 TRP 429

GLU 102 0.31 VAL 376 -0.27 TRP 429

GLU 102 0.32 VAL 377 -0.27 TRP 429

GLU 102 0.32 PRO 378 -0.28 TRP 429

GLU 102 0.29 GLU 379 -0.27 TRP 429

GLU 102 0.27 ILE 380 -0.26 TRP 429

GLU 102 0.28 VAL 381 -0.26 TRP 429

GLU 102 0.27 ARG 382 -0.26 TRP 429

GLU 102 0.24 HIS 383 -0.25 TRP 429

GLU 102 0.24 TYR 384 -0.24 TRP 429

GLU 102 0.24 CYS 385 -0.25 ASN 8

GLU 102 0.23 ALA 386 -0.25 TRP 429

GLU 102 0.25 VAL 387 -0.26 PHE 12

GLU 102 0.25 SER 388 -0.26 TRP 429

GLU 102 0.28 PHE 389 -0.28 PHE 12

GLU 102 0.29 THR 390 -0.28 TRP 429

GLU 102 0.33 LEU 391 -0.29 TRP 429

GLU 102 0.34 GLY 392 -0.29 TRP 429

GLU 102 0.38 GLY 393 -0.29 TRP 429

GLU 102 0.41 THR 394 -0.30 TRP 429

GLU 102 0.42 SER 395 -0.31 LYS 425

GLU 102 0.44 PHE 396 -0.32 TRP 429

GLU 102 0.49 LEU 397 -0.32 TRP 429

GLU 102 0.53 ILE 398 -0.34 LYS 425

GLU 102 0.52 ILE 399 -0.34 TRP 429

GLU 102 0.56 VAL 400 -0.34 TRP 429

GLU 102 0.64 ASN 401 -0.35 TRP 429

GLU 102 0.67 VAL 402 -0.37 GLY 417

GLU 102 0.63 ILE 403 -0.36 TRP 429

GLU 102 0.68 ASN 404 -0.36 TRP 429

GLU 102 0.80 ASP 405 -0.39 GLY 417

GLU 102 0.76 THR 406 -0.40 GLY 417

GLU 102 0.67 PHE 407 -0.38 TRP 429

GLU 102 0.74 SER 408 -0.37 TRP 429

GLU 102 0.78 GLN 409 -0.44 GLY 417

GLU 102 0.64 VAL 410 -0.41 GLY 417

GLU 102 0.58 GLN 411 -0.41 TRP 429

GLU 102 0.52 THR 412 -0.40 GLN 409

LEU 103 0.54 GLN 413 -0.61 GLY 417

LEU 103 0.45 VAL 414 -0.44 TRP 429

ASN 2 0.50 TYR 415 -0.41 TRP 429

GLY 4 0.52 SER 416 -0.50 ALA 173

GLY 4 0.73 GLY 417 -0.61 GLN 413

ASN 2 0.72 ARG 418 -0.54 SER 426

MET 1 0.58 TYR 419 -0.54 ALA 173

ASN 2 0.54 SER 420 -0.71 ALA 173

ASN 2 0.62 ALA 421 -0.68 ALA 173

MET 1 0.69 LEU 422 -0.62 SER 426

MET 1 0.48 MET 423 -0.58 ALA 173

MET 1 0.45 LYS 424 -0.61 ALA 173

MET 1 0.39 LYS 425 -0.64 ALA 173

MET 1 0.27 SER 426 -0.62 LEU 422

MET 1 0.25 GLU 427 -0.39 ALA 173

MET 1 0.19 LEU 428 -0.43 ALA 173

MET 1 0.06 TRP 429 -0.50 ARG 418

MET 1 0.10 LYS 430 -0.43 ILE 258

ARG 6 0.20 LYS 431 -0.39 GLY 247

LYS 433 0.05 VAL 432 -0.36 ILE 258

VAL 432 0.05 LYS 433 -0.46 SER 256

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.

*** secYG_ALPHA_SECE_ITASSER_NEMO_RE ***

CA distance fluctuations for 260812054906533160

--- normal mode 22 ---

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

* secYG_ALPHA_SECE_ITASSER_NEMO_RE *