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

* citrate_open_cutoff8 *

CA distance fluctuations for 2604281742252934881

--- 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
LYS 206 0.07 ALA 1 -0.10 SER 424

ALA 432 0.04 SER 2 -0.12 SER 424

ARG 421 0.05 SER 3 -0.13 SER 424

ARG 421 0.08 THR 4 -0.14 SER 424

ARG 421 0.08 ASN 5 -0.14 SER 424

ARG 421 0.08 LEU 6 -0.16 SER 424

ARG 421 0.07 LYS 7 -0.15 SER 424

ARG 421 0.12 ASP 8 -0.15 SER 424

ARG 421 0.16 VAL 9 -0.16 SER 424

ARG 421 0.17 LEU 10 -0.18 SER 424

ARG 421 0.19 ALA 11 -0.17 SER 424

ARG 421 0.24 ALA 12 -0.17 SER 424

ARG 421 0.29 LEU 13 -0.19 SER 424

ARG 421 0.33 ILE 14 -0.20 SER 424

ARG 421 0.39 PRO 15 -0.25 PRO 422

ARG 421 0.41 LYS 16 -0.22 PRO 422

ARG 421 0.46 GLU 17 -0.23 SER 424

ARG 421 0.52 GLN 18 -0.30 PRO 422

ARG 421 0.56 ALA 19 -0.34 PRO 422

ARG 421 0.60 ARG 20 -0.30 PRO 422

ARG 421 0.71 ILE 21 -0.35 PRO 422

ARG 421 0.75 LYS 22 -0.47 PRO 422

ARG 421 0.72 THR 23 -0.43 PRO 422

ARG 421 0.80 PHE 24 -0.42 PRO 422

ARG 421 0.98 ARG 25 -0.55 PRO 422

ARG 421 0.88 GLN 26 -0.58 PRO 422

ARG 421 0.84 GLN 27 -0.52 PRO 422

ARG 421 0.90 HIS 28 -0.48 PRO 422

ARG 421 1.09 GLY 29 -0.60 PRO 422

ARG 421 1.15 GLY 30 -0.68 PRO 422

ARG 421 0.98 THR 31 -0.49 PRO 422

ARG 421 0.91 ALA 32 -0.41 PRO 422

ARG 421 0.85 LEU 33 -0.38 SER 424

ARG 421 0.73 GLY 34 -0.40 SER 424

LYS 423 0.65 GLN 35 -0.39 SER 424

LYS 423 0.85 ILE 36 -0.44 SER 424

LYS 423 0.77 THR 37 -0.30 SER 424

LYS 423 0.72 VAL 38 -0.17 SER 424

LYS 423 0.70 ASP 39 -0.18 SER 424

LYS 423 0.85 MET 40 -0.34 SER 424

LYS 423 1.00 SER 41 -0.36 SER 424

PRO 422 0.80 TYR 42 -0.19 THR 427

PRO 422 0.85 GLY 43 -0.24 SER 424

PRO 422 1.11 GLY 44 -0.34 SER 424

LYS 423 0.93 MET 45 -0.52 SER 424

LYS 423 0.74 ARG 46 -0.38 SER 424

LYS 423 0.67 GLY 47 -0.39 SER 424

LYS 423 0.80 MET 48 -0.52 SER 424

LYS 423 0.63 LYS 49 -0.50 SER 424

ARG 421 0.62 GLY 50 -0.57 SER 424

ARG 421 0.48 LEU 51 -0.47 SER 424

ARG 421 0.55 VAL 52 -0.39 SER 424

ARG 421 0.32 TYR 53 -0.35 SER 424

ARG 421 0.33 GLU 54 -0.30 SER 424

LYS 423 0.21 THR 55 -0.27 SER 424

LYS 423 0.26 SER 56 -0.27 SER 424

LYS 423 0.31 VAL 57 -0.29 SER 424

LYS 423 0.34 LEU 58 -0.27 SER 424

LYS 423 0.32 ASP 59 -0.25 SER 424

LYS 423 0.33 PRO 60 -0.24 SER 424

LYS 423 0.29 ASP 61 -0.22 SER 424

LYS 423 0.27 GLU 62 -0.21 SER 424

LYS 423 0.29 GLY 63 -0.22 SER 424

LYS 423 0.28 ILE 64 -0.24 SER 424

LYS 423 0.25 ARG 65 -0.24 SER 424

LYS 423 0.21 PHE 66 -0.23 SER 424

ARG 421 0.26 ARG 67 -0.24 SER 424

ARG 421 0.27 GLY 68 -0.23 SER 424

LYS 423 0.20 PHE 69 -0.21 SER 424

LYS 423 0.23 SER 70 -0.21 SER 424

PRO 422 0.23 ILE 71 -0.19 SER 424

LYS 423 0.20 PRO 72 -0.18 SER 424

LYS 423 0.19 GLU 73 -0.18 SER 424

LYS 423 0.18 CYS 74 -0.18 SER 424

PRO 422 0.19 GLN 75 -0.17 SER 424

LYS 423 0.16 LYS 76 -0.16 SER 424

LYS 423 0.15 LEU 77 -0.17 SER 424

PRO 422 0.15 LEU 78 -0.17 SER 424

PRO 422 0.14 PRO 79 -0.15 SER 424

PRO 422 0.17 LYS 80 -0.14 SER 424

PRO 422 0.18 GLY 81 -0.13 SER 424

PRO 422 0.15 GLY 82 -0.12 SER 424

PRO 422 0.19 GLY 84 -0.12 SER 424

PRO 422 0.20 GLY 85 -0.13 SER 424

PRO 422 0.22 GLU 86 -0.14 SER 424

PRO 422 0.21 PRO 87 -0.15 SER 424

PRO 422 0.21 LEU 88 -0.15 SER 424

PRO 422 0.23 PRO 89 -0.16 SER 424

PRO 422 0.18 GLU 90 -0.15 SER 424

PRO 422 0.15 GLY 91 -0.16 SER 424

PRO 422 0.19 LEU 92 -0.18 SER 424

PRO 422 0.18 PHE 93 -0.18 SER 424

PRO 422 0.12 TRP 94 -0.18 SER 424

LYS 423 0.13 LEU 95 -0.19 SER 424

LYS 423 0.15 LEU 96 -0.21 SER 424

ARG 421 0.13 VAL 97 -0.21 SER 424

ARG 421 0.19 THR 98 -0.20 SER 424

ARG 421 0.24 GLY 99 -0.21 SER 424

ARG 421 0.19 GLN 100 -0.19 SER 424

ARG 421 0.14 ILE 101 -0.18 SER 424

LYS 423 0.10 PRO 102 -0.16 SER 424

ARG 421 0.09 THR 103 -0.15 SER 424

PRO 422 0.09 GLY 104 -0.14 SER 424

PRO 422 0.07 ALA 105 -0.13 SER 424

LYS 423 0.07 GLN 106 -0.14 SER 424

PRO 422 0.11 VAL 107 -0.14 SER 424

PRO 422 0.12 SER 108 -0.13 SER 424

PRO 422 0.09 TRP 109 -0.13 SER 424

PRO 422 0.12 LEU 110 -0.13 SER 424

PRO 422 0.15 SER 111 -0.12 SER 424

PRO 422 0.12 LYS 112 -0.11 SER 424

PRO 422 0.12 GLU 113 -0.12 SER 424

PRO 422 0.16 TRP 114 -0.12 ARG 421

PRO 422 0.16 ALA 115 -0.13 ARG 421

PRO 422 0.14 LYS 116 -0.14 ARG 421

PRO 422 0.15 ARG 117 -0.17 ARG 421

PRO 422 0.19 ALA 118 -0.20 ARG 421

PRO 422 0.19 ALA 119 -0.24 ARG 421

PRO 422 0.22 LEU 120 -0.30 ARG 421

PRO 422 0.21 PRO 121 -0.34 ARG 421

PRO 422 0.22 SER 122 -0.34 ARG 421

PRO 422 0.24 HIS 123 -0.40 ARG 421

PRO 422 0.28 VAL 124 -0.41 ARG 421

PRO 422 0.27 VAL 125 -0.37 ARG 421

PRO 422 0.27 THR 126 -0.39 ARG 421

PRO 422 0.31 MET 127 -0.44 ARG 421

PRO 422 0.34 LEU 128 -0.42 ARG 421

PRO 422 0.31 ASP 129 -0.39 ARG 421

PRO 422 0.32 ASN 130 -0.42 ARG 421

PRO 422 0.37 PHE 131 -0.45 ARG 421

PRO 422 0.39 PRO 132 -0.44 ARG 421

PRO 422 0.40 THR 133 -0.41 ARG 421

PRO 422 0.44 ASN 134 -0.44 ARG 421

PRO 422 0.46 LEU 135 -0.48 ARG 421

PRO 422 0.50 HIS 136 -0.45 ARG 421

PRO 422 0.47 PRO 137 -0.42 ARG 421

PRO 422 0.53 MET 138 -0.46 ARG 421

PRO 422 0.52 SER 139 -0.53 ARG 421

PRO 422 0.44 GLN 140 -0.49 ARG 421

PRO 422 0.44 LEU 141 -0.46 ARG 421

PRO 422 0.48 SER 142 -0.54 ARG 421

PRO 422 0.43 ALA 143 -0.56 ARG 421

PRO 422 0.36 ALA 144 -0.48 ARG 421

PRO 422 0.35 ILE 145 -0.47 ARG 421

PRO 422 0.36 THR 146 -0.57 ARG 421

PRO 422 0.30 ALA 147 -0.51 ARG 421

PRO 422 0.26 LEU 148 -0.43 ARG 421

PRO 422 0.24 ASN 149 -0.46 ARG 421

PRO 422 0.19 SER 150 -0.43 ARG 421

PRO 422 0.16 GLU 151 -0.34 ARG 421

PRO 422 0.13 SER 152 -0.32 ARG 421

ALA 432 0.06 ASN 153 -0.23 ARG 421

ALA 432 0.06 PHE 154 -0.23 ARG 421

ALA 432 0.06 ALA 155 -0.34 ARG 421

ALA 432 0.06 ARG 156 -0.29 ARG 421

ALA 432 0.07 ALA 157 -0.19 ARG 421

ALA 432 0.07 TYR 158 -0.24 ARG 421

ALA 432 0.07 ALA 159 -0.28 ARG 421

ALA 432 0.07 GLU 160 -0.19 LYS 423

ALA 432 0.08 GLY 161 -0.21 LYS 423

ALA 432 0.08 ILE 162 -0.17 LYS 423

ALA 432 0.09 LEU 163 -0.25 PRO 422

ARG 421 0.14 ARG 164 -0.29 PRO 422

ARG 421 0.21 THR 165 -0.26 PRO 422

ARG 421 0.09 LYS 166 -0.18 PRO 422

ALA 432 0.08 TYR 167 -0.16 SER 424

ALA 432 0.08 TRP 168 -0.17 SER 424

ALA 432 0.07 GLU 169 -0.15 SER 424

ALA 432 0.07 MET 170 -0.13 SER 424

ALA 432 0.07 VAL 171 -0.15 SER 424

ALA 432 0.06 TYR 172 -0.16 SER 424

PRO 422 0.07 GLU 173 -0.13 SER 424

PRO 422 0.13 SER 174 -0.21 ARG 421

PRO 422 0.16 ALA 175 -0.16 ARG 421

PRO 422 0.15 MET 176 -0.14 SER 424

PRO 422 0.17 ASP 177 -0.20 ARG 421

PRO 422 0.24 LEU 178 -0.26 ARG 421

PRO 422 0.25 ILE 179 -0.20 ARG 421

PRO 422 0.22 ALA 180 -0.19 ARG 421

PRO 422 0.25 LYS 181 -0.26 ARG 421

PRO 422 0.31 LEU 182 -0.28 ARG 421

PRO 422 0.30 PRO 183 -0.25 ARG 421

PRO 422 0.29 CYS 184 -0.28 ARG 421

PRO 422 0.33 VAL 185 -0.34 ARG 421

PRO 422 0.36 ALA 186 -0.32 ARG 421

PRO 422 0.32 ALA 187 -0.28 ARG 421

PRO 422 0.32 LYS 188 -0.32 ARG 421

PRO 422 0.37 ILE 189 -0.35 ARG 421

PRO 422 0.37 TYR 190 -0.31 ARG 421

PRO 422 0.33 ARG 191 -0.30 ARG 421

PRO 422 0.34 ASN 192 -0.34 ARG 421

PRO 422 0.38 LEU 193 -0.35 ARG 421

PRO 422 0.36 TYR 194 -0.30 ARG 421

PRO 422 0.33 ARG 195 -0.28 ARG 421

PRO 422 0.32 ALA 196 -0.30 ARG 421

PRO 422 0.31 GLY 197 -0.32 ARG 421

PRO 422 0.28 SER 198 -0.28 ARG 421

PRO 422 0.27 SER 199 -0.27 ARG 421

PRO 422 0.27 ILE 200 -0.26 ARG 421

PRO 422 0.24 GLY 201 -0.23 ARG 421

PRO 422 0.21 ALA 202 -0.20 ARG 421

PRO 422 0.20 ILE 203 -0.18 ARG 421

PRO 422 0.18 ASP 204 -0.14 ARG 421

PRO 422 0.15 SER 205 -0.11 ARG 421

PRO 422 0.15 LYS 206 -0.10 SER 424

PRO 422 0.18 LEU 207 -0.11 SER 424

PRO 422 0.19 ASP 208 -0.12 SER 424

PRO 422 0.22 TRP 209 -0.12 SER 424

PRO 422 0.25 SER 210 -0.12 ARG 421

PRO 422 0.24 HIS 211 -0.13 ARG 421

PRO 422 0.23 ASN 212 -0.16 ARG 421

PRO 422 0.28 PHE 213 -0.19 ARG 421

PRO 422 0.28 THR 214 -0.18 ARG 421

PRO 422 0.26 ASN 215 -0.18 ARG 421

PRO 422 0.27 MET 216 -0.22 ARG 421

PRO 422 0.30 LEU 217 -0.23 ARG 421

PRO 422 0.28 GLY 218 -0.21 ARG 421

PRO 422 0.28 TYR 219 -0.18 ARG 421

PRO 422 0.25 THR 220 -0.15 ARG 421

PRO 422 0.26 ASP 221 -0.13 ARG 421

PRO 422 0.24 ALA 222 -0.10 ARG 421

PRO 422 0.25 GLN 223 -0.11 SER 424

PRO 422 0.28 PHE 224 -0.12 ARG 421

PRO 422 0.26 THR 225 -0.11 ARG 421

PRO 422 0.25 GLU 226 -0.12 SER 424

PRO 422 0.29 LEU 227 -0.13 SER 424

PRO 422 0.30 MET 228 -0.13 SER 424

PRO 422 0.26 ARG 229 -0.14 SER 424

PRO 422 0.28 LEU 230 -0.15 SER 424

PRO 422 0.33 TYR 231 -0.15 SER 424

PRO 422 0.32 LEU 232 -0.15 SER 424

PRO 422 0.28 THR 233 -0.17 SER 424

PRO 422 0.32 ILE 234 -0.18 SER 424

PRO 422 0.40 HIS 235 -0.18 SER 424

PRO 422 0.35 SER 236 -0.20 SER 424

PRO 422 0.36 ASP 237 -0.23 SER 424

PRO 422 0.40 HIS 238 -0.26 SER 424

PRO 422 0.38 GLU 239 -0.31 SER 424

PRO 422 0.42 GLY 240 -0.35 SER 424

PRO 422 0.61 GLY 241 -0.38 SER 424

PRO 422 0.70 ASN 242 -0.30 SER 424

PRO 422 0.84 VAL 243 -0.34 ARG 421

PRO 422 0.66 SER 244 -0.33 ARG 421

PRO 422 0.54 ALA 245 -0.27 SER 424

PRO 422 0.67 HIS 246 -0.34 SER 424

PRO 422 0.71 THR 247 -0.49 ARG 421

PRO 422 0.48 SER 248 -0.39 ARG 421

PRO 422 0.38 HIS 249 -0.30 SER 424

PRO 422 0.49 LEU 250 -0.49 ARG 421

PRO 422 0.43 VAL 251 -0.70 ARG 421

PRO 422 0.25 GLY 252 -0.40 ARG 421

ALA 432 0.09 SER 253 -0.25 SER 424

ALA 432 0.09 ALA 254 -0.52 ARG 421

ALA 432 0.08 LEU 255 -0.33 ARG 421

PRO 422 0.17 SER 256 -0.51 ARG 421

PRO 422 0.16 ASP 257 -0.39 ARG 421

PRO 422 0.22 PRO 258 -0.33 ARG 421

PRO 422 0.29 TYR 259 -0.43 ARG 421

PRO 422 0.34 LEU 260 -0.58 ARG 421

PRO 422 0.40 SER 261 -0.53 ARG 421

PRO 422 0.43 PHE 262 -0.45 ARG 421

PRO 422 0.48 ALA 263 -0.56 ARG 421

PRO 422 0.60 ALA 264 -0.68 ARG 421

PRO 422 0.61 ALA 265 -0.51 ARG 421

PRO 422 0.61 MET 266 -0.50 ARG 421

PRO 422 0.69 ASN 267 -0.63 ARG 421

PRO 422 0.80 GLY 268 -0.55 ARG 421

PRO 422 0.69 LEU 269 -0.42 ARG 421

PRO 422 0.68 ALA 270 -0.49 ARG 421

PRO 422 0.77 GLY 271 -0.48 ARG 421

PRO 422 0.73 PRO 272 -0.40 ARG 421

PRO 422 0.78 LEU 273 -0.34 ARG 421

PRO 422 0.74 HIS 274 -0.33 ARG 421

PRO 422 0.65 GLY 275 -0.34 ARG 421

PRO 422 0.60 LEU 276 -0.30 ARG 421

PRO 422 0.56 ALA 277 -0.22 ARG 421

PRO 422 0.49 ASN 278 -0.20 ARG 421

PRO 422 0.50 GLN 279 -0.24 ARG 421

PRO 422 0.52 GLU 280 -0.23 ARG 421

PRO 422 0.47 VAL 281 -0.18 ARG 421

PRO 422 0.44 LEU 282 -0.19 ARG 421

PRO 422 0.46 GLY 283 -0.21 ARG 421

PRO 422 0.45 TRP 284 -0.18 ARG 421

PRO 422 0.41 LEU 285 -0.15 ARG 421

PRO 422 0.40 ALA 286 -0.18 ARG 421

PRO 422 0.41 GLN 287 -0.18 ARG 421

PRO 422 0.38 LEU 288 -0.15 ARG 421

PRO 422 0.37 GLN 289 -0.15 ARG 421

PRO 422 0.36 LYS 290 -0.16 ARG 421

PRO 422 0.36 ALA 291 -0.15 ARG 421

PRO 422 0.30 ALA 295 -0.09 ARG 421

PRO 422 0.30 GLY 296 -0.08 ARG 421

PRO 422 0.29 ALA 297 -0.08 SER 424

PRO 422 0.29 ASP 298 -0.09 SER 424

PRO 422 0.29 ALA 299 -0.08 SER 424

PRO 422 0.31 SER 300 -0.08 SER 424

PRO 422 0.33 LEU 301 -0.09 SER 424

PRO 422 0.32 ARG 302 -0.09 SER 424

PRO 422 0.32 ASP 303 -0.08 SER 424

PRO 422 0.35 TYR 304 -0.09 ARG 421

PRO 422 0.37 ILE 305 -0.09 SER 424

PRO 422 0.35 TRP 306 -0.09 SER 424

PRO 422 0.36 ASN 307 -0.09 ARG 421

PRO 422 0.40 THR 308 -0.10 ARG 421

PRO 422 0.40 LEU 309 -0.09 SER 424

PRO 422 0.37 ASN 310 -0.08 SER 424

PRO 422 0.40 SER 311 -0.11 ARG 421

PRO 422 0.43 GLY 312 -0.11 ARG 421

PRO 422 0.45 ARG 313 -0.13 ARG 421

PRO 422 0.46 VAL 314 -0.11 ARG 421

PRO 422 0.45 VAL 315 -0.11 SER 424

PRO 422 0.49 PRO 316 -0.14 ARG 421

PRO 422 0.46 GLY 317 -0.14 SER 424

PRO 422 0.43 TYR 318 -0.15 SER 424

PRO 422 0.43 GLY 319 -0.17 SER 424

PRO 422 0.44 HIS 320 -0.20 SER 424

PRO 422 0.44 ALA 321 -0.23 SER 424

LYS 423 0.39 VAL 322 -0.24 SER 424

LYS 423 0.34 LEU 323 -0.22 SER 424

LYS 423 0.32 ARG 324 -0.20 SER 424

LYS 423 0.29 LYS 325 -0.19 SER 424

PRO 422 0.30 THR 326 -0.18 SER 424

PRO 422 0.33 ASP 327 -0.19 SER 424

PRO 422 0.29 PRO 328 -0.18 SER 424

PRO 422 0.33 ARG 329 -0.18 SER 424

PRO 422 0.34 TYR 330 -0.16 SER 424

PRO 422 0.29 THR 331 -0.16 SER 424

PRO 422 0.29 CYS 332 -0.16 SER 424

PRO 422 0.31 GLN 333 -0.14 SER 424

PRO 422 0.30 ARG 334 -0.14 SER 424

PRO 422 0.26 GLU 335 -0.14 SER 424

PRO 422 0.27 PHE 336 -0.13 SER 424

PRO 422 0.29 ALA 337 -0.12 SER 424

PRO 422 0.26 LEU 338 -0.12 SER 424

PRO 422 0.24 LYS 339 -0.12 SER 424

PRO 422 0.26 HIS 340 -0.11 SER 424

PRO 422 0.28 LEU 341 -0.10 SER 424

PRO 422 0.27 PRO 342 -0.10 SER 424

PRO 422 0.27 GLY 343 -0.09 SER 424

PRO 422 0.30 ASP 344 -0.10 ARG 421

PRO 422 0.31 PRO 345 -0.11 ARG 421

PRO 422 0.34 MET 346 -0.12 ARG 421

PRO 422 0.33 PHE 347 -0.10 SER 424

PRO 422 0.31 LYS 348 -0.10 SER 424

PRO 422 0.33 LEU 349 -0.10 SER 424

PRO 422 0.35 VAL 350 -0.11 SER 424

PRO 422 0.32 ALA 351 -0.12 SER 424

PRO 422 0.32 GLN 352 -0.11 SER 424

PRO 422 0.35 LEU 353 -0.11 SER 424

PRO 422 0.32 TYR 354 -0.13 SER 424

PRO 422 0.30 LYS 355 -0.12 SER 424

PRO 422 0.31 ILE 356 -0.11 SER 424

PRO 422 0.35 VAL 357 -0.12 SER 424

PRO 422 0.33 PRO 358 -0.13 SER 424

PRO 422 0.30 ASN 359 -0.12 SER 424

PRO 422 0.32 VAL 360 -0.11 SER 424

PRO 422 0.35 LEU 361 -0.13 SER 424

PRO 422 0.31 LEU 362 -0.13 SER 424

PRO 422 0.30 GLU 363 -0.12 SER 424

PRO 422 0.33 GLN 364 -0.11 SER 424

PRO 422 0.33 GLY 365 -0.12 SER 424

PRO 422 0.38 ALA 366 -0.14 SER 424

PRO 422 0.35 ALA 367 -0.16 SER 424

LYS 423 0.33 ALA 368 -0.18 SER 424

PRO 422 0.34 ASN 369 -0.18 SER 424

PRO 422 0.36 PRO 370 -0.16 SER 424

PRO 422 0.35 TRP 371 -0.16 SER 424

PRO 422 0.38 PRO 372 -0.16 SER 424

PRO 422 0.41 ASN 373 -0.17 SER 424

PRO 422 0.41 VAL 374 -0.17 SER 424

PRO 422 0.46 ASP 375 -0.15 SER 424

PRO 422 0.42 ALA 376 -0.14 SER 424

PRO 422 0.38 HIS 377 -0.14 SER 424

PRO 422 0.39 SER 378 -0.13 SER 424

PRO 422 0.41 GLY 379 -0.17 ARG 421

PRO 422 0.37 VAL 380 -0.14 ARG 421

PRO 422 0.35 LEU 381 -0.13 ARG 421

PRO 422 0.37 LEU 382 -0.17 ARG 421

PRO 422 0.37 GLN 383 -0.18 ARG 421

PRO 422 0.33 TYR 384 -0.15 ARG 421

PRO 422 0.32 TYR 385 -0.16 ARG 421

PRO 422 0.33 GLY 386 -0.19 ARG 421

PRO 422 0.36 MET 387 -0.21 ARG 421

PRO 422 0.39 THR 388 -0.23 ARG 421

PRO 422 0.41 GLU 389 -0.27 ARG 421

PRO 422 0.45 MET 390 -0.28 ARG 421

PRO 422 0.49 ASN 391 -0.34 ARG 421

PRO 422 0.46 TYR 392 -0.32 ARG 421

PRO 422 0.46 TYR 393 -0.27 ARG 421

PRO 422 0.52 THR 394 -0.32 ARG 421

PRO 422 0.46 VAL 395 -0.32 ARG 421

PRO 422 0.42 LEU 396 -0.25 ARG 421

PRO 422 0.46 PHE 397 -0.24 ARG 421

PRO 422 0.47 GLY 398 -0.29 ARG 421

PRO 422 0.39 VAL 399 -0.24 ARG 421

PRO 422 0.37 SER 400 -0.17 ARG 421

PRO 422 0.42 ARG 401 -0.19 SER 424

PRO 422 0.36 ALA 402 -0.20 ARG 421

PRO 422 0.28 LEU 403 -0.19 SER 424

PRO 422 0.29 GLY 404 -0.22 SER 424

PRO 422 0.34 VAL 405 -0.23 SER 424

PRO 422 0.24 LEU 406 -0.20 SER 424

PRO 422 0.17 ALA 407 -0.21 SER 424

PRO 422 0.14 GLN 408 -0.25 SER 424

PRO 422 0.15 LEU 409 -0.24 SER 424

ALA 432 0.07 ILE 410 -0.21 SER 424

ARG 421 0.21 TRP 411 -0.24 SER 424

ARG 421 0.23 SER 412 -0.27 SER 424

ARG 421 0.13 ARG 413 -0.22 SER 424

ARG 421 0.25 ALA 414 -0.22 SER 424

ARG 421 0.43 LEU 415 -0.25 SER 424

ARG 421 0.38 GLY 416 -0.31 PRO 422

ARG 421 0.47 PHE 417 -0.31 PRO 422

ARG 421 0.39 PRO 418 -0.42 PRO 422

ALA 432 0.12 LEU 419 -0.29 SER 424

ALA 432 0.12 GLU 420 -0.44 SER 424

GLY 30 1.15 ARG 421 -0.70 VAL 251

GLY 44 1.11 PRO 422 -0.68 GLY 30

SER 41 1.00 LYS 423 -0.21 GLY 161

GLY 429 0.43 SER 424 -0.57 GLY 50

TYR 42 0.29 MET 425 -0.36 ILE 36

PRO 422 0.12 SER 426 -0.48 ARG 421

PRO 422 0.17 THR 427 -0.41 ARG 421

SER 424 0.16 ASP 428 -0.32 ARG 421

SER 424 0.43 GLY 429 -0.08 ARG 421

LYS 423 0.42 LEU 430 -0.02 GLY 365

LYS 423 0.29 ILE 431 -0.13 TYR 42

SER 424 0.33 ALA 432 -0.07 GLY 312

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.

*** citrate_open_cutoff8 ***

CA distance fluctuations for 2604281742252934881

--- 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.

* citrate_open_cutoff8 *