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 2604241126091943151

--- 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
ASP 8 0.03 ALA 1 -0.12 LYS 206

SER 424 0.01 SER 2 -0.05 THR 427

SER 424 0.01 SER 3 -0.06 THR 427

ALA 1 0.02 THR 4 -0.06 THR 427

ALA 1 0.03 ASN 5 -0.06 THR 427

SER 424 0.01 LEU 6 -0.07 THR 427

ALA 1 0.01 LYS 7 -0.07 THR 427

ALA 1 0.03 ASP 8 -0.07 THR 427

ALA 1 0.02 VAL 9 -0.07 THR 427

ALA 1 0.01 LEU 10 -0.08 THR 427

ALA 1 0.02 ALA 11 -0.07 THR 427

ALA 1 0.03 ALA 12 -0.08 LYS 423

ALA 1 0.02 LEU 13 -0.10 LYS 423

ALA 1 0.02 ILE 14 -0.11 LYS 423

ALA 1 0.02 PRO 15 -0.12 LYS 423

ALA 1 0.02 LYS 16 -0.14 LYS 423

ALA 1 0.01 GLU 17 -0.15 LYS 423

ALA 1 0.01 GLN 18 -0.16 LYS 423

ALA 1 0.02 ALA 19 -0.18 LYS 423

ALA 1 0.01 ARG 20 -0.20 LYS 423

ALA 1 0.01 ILE 21 -0.23 LYS 423

ALA 1 0.01 LYS 22 -0.23 LYS 423

ALA 1 0.01 THR 23 -0.24 LYS 423

ALA 1 0.01 PHE 24 -0.27 LYS 423

ALA 1 0.01 ARG 25 -0.32 LYS 423

ALA 1 0.01 GLN 26 -0.29 LYS 423

ALA 1 0.01 GLN 27 -0.30 LYS 423

ALA 1 0.01 HIS 28 -0.33 LYS 423

ALA 1 0.00 GLY 29 -0.38 LYS 423

ALA 1 0.00 GLY 30 -0.45 LYS 423

ALA 432 0.01 THR 31 -0.40 LYS 423

ALA 432 0.01 ALA 32 -0.44 LYS 423

ALA 432 0.01 LEU 33 -0.41 LYS 423

ALA 432 0.02 GLY 34 -0.42 LYS 423

ALA 432 0.03 GLN 35 -0.43 LYS 423

ALA 432 0.03 ILE 36 -0.42 LYS 423

SER 424 0.05 THR 37 -0.31 THR 427

SER 424 0.12 VAL 38 -0.41 THR 427

SER 424 0.20 ASP 39 -0.33 THR 427

SER 424 0.23 MET 40 -0.32 THR 427

SER 424 0.35 SER 41 -0.42 THR 427

SER 424 0.41 TYR 42 -0.37 THR 427

SER 424 0.35 GLY 43 -0.27 THR 427

SER 424 0.41 GLY 44 -0.25 THR 427

SER 424 0.28 MET 45 -0.27 THR 427

SER 424 0.23 ARG 46 -0.23 THR 427

SER 424 0.13 GLY 47 -0.21 THR 427

SER 424 0.09 MET 48 -0.28 LYS 423

SER 424 0.02 LYS 49 -0.32 LYS 423

ALA 432 0.01 GLY 50 -0.32 LYS 423

SER 424 0.02 LEU 51 -0.21 PRO 422

ALA 432 0.00 VAL 52 -0.21 LYS 423

SER 424 0.03 TYR 53 -0.13 LYS 423

SER 424 0.02 GLU 54 -0.13 LYS 423

SER 424 0.04 THR 55 -0.11 THR 427

SER 424 0.06 SER 56 -0.11 THR 427

SER 424 0.06 VAL 57 -0.12 THR 427

SER 424 0.08 LEU 58 -0.12 THR 427

SER 424 0.07 ASP 59 -0.12 LYS 423

SER 424 0.08 PRO 60 -0.11 THR 427

SER 424 0.07 ASP 61 -0.11 LYS 423

SER 424 0.07 GLU 62 -0.10 THR 427

SER 424 0.09 GLY 63 -0.10 THR 427

SER 424 0.08 ILE 64 -0.11 THR 427

SER 424 0.06 ARG 65 -0.10 THR 427

SER 424 0.05 PHE 66 -0.10 THR 427

SER 424 0.03 ARG 67 -0.11 LYS 423

SER 424 0.03 GLY 68 -0.11 LYS 423

SER 424 0.04 PHE 69 -0.09 THR 427

SER 424 0.06 SER 70 -0.09 THR 427

SER 424 0.07 ILE 71 -0.09 THR 427

SER 424 0.06 PRO 72 -0.08 THR 427

SER 424 0.05 GLU 73 -0.08 THR 427

SER 424 0.05 CYS 74 -0.08 THR 427

SER 424 0.06 GLN 75 -0.08 THR 427

SER 424 0.05 LYS 76 -0.07 THR 427

SER 424 0.04 LEU 77 -0.07 THR 427

SER 424 0.05 LEU 78 -0.07 THR 427

SER 424 0.04 PRO 79 -0.07 THR 427

SER 424 0.05 LYS 80 -0.07 ALA 1

SER 424 0.06 GLY 81 -0.08 ALA 1

SER 424 0.05 GLY 82 -0.09 ALA 1

SER 424 0.06 GLY 84 -0.07 ALA 1

SER 424 0.06 GLY 85 -0.06 THR 427

SER 424 0.07 GLU 86 -0.06 THR 427

SER 424 0.06 PRO 87 -0.07 THR 427

SER 424 0.06 LEU 88 -0.07 THR 427

SER 424 0.07 PRO 89 -0.07 THR 427

SER 424 0.05 GLU 90 -0.07 THR 427

SER 424 0.04 GLY 91 -0.07 THR 427

SER 424 0.05 LEU 92 -0.08 THR 427

SER 424 0.05 PHE 93 -0.08 THR 427

SER 424 0.03 TRP 94 -0.08 THR 427

SER 424 0.03 LEU 95 -0.08 THR 427

SER 424 0.04 LEU 96 -0.09 THR 427

SER 424 0.02 VAL 97 -0.09 THR 427

SER 424 0.01 THR 98 -0.08 THR 427

SER 424 0.01 GLY 99 -0.09 LYS 423

SER 424 0.01 GLN 100 -0.08 THR 427

SER 424 0.02 ILE 101 -0.08 THR 427

SER 424 0.02 PRO 102 -0.07 THR 427

SER 424 0.02 THR 103 -0.07 THR 427

SER 424 0.03 GLY 104 -0.08 ALA 1

SER 424 0.02 ALA 105 -0.09 ALA 1

SER 424 0.02 GLN 106 -0.06 THR 427

SER 424 0.04 VAL 107 -0.07 ALA 1

SER 424 0.04 SER 108 -0.12 ALA 1

SER 424 0.03 TRP 109 -0.09 ALA 1

SER 424 0.04 LEU 110 -0.07 ALA 1

SER 424 0.04 SER 111 -0.09 ALA 1

SER 424 0.04 LYS 112 -0.11 ALA 1

SER 424 0.03 GLU 113 -0.06 ALA 1

SER 424 0.05 TRP 114 -0.06 ALA 1

SER 424 0.05 ALA 115 -0.08 ALA 1

SER 424 0.04 LYS 116 -0.06 ALA 1

LYS 423 0.04 ARG 117 -0.05 THR 427

SER 424 0.06 ALA 118 -0.05 ALA 1

LYS 423 0.07 ALA 119 -0.04 THR 427

LYS 423 0.09 LEU 120 -0.04 ASP 428

LYS 423 0.10 PRO 121 -0.04 ASP 428

LYS 423 0.11 SER 122 -0.03 ASP 428

LYS 423 0.13 HIS 123 -0.03 ASP 428

LYS 423 0.13 VAL 124 -0.04 ASP 428

LYS 423 0.11 VAL 125 -0.04 ASP 428

LYS 423 0.13 THR 126 -0.03 ASP 428

LYS 423 0.14 MET 127 -0.04 ASP 428

LYS 423 0.13 LEU 128 -0.04 ASP 428

LYS 423 0.12 ASP 129 -0.04 ASP 428

LYS 423 0.14 ASN 130 -0.03 ASP 428

LYS 423 0.15 PHE 131 -0.04 ASP 428

LYS 423 0.15 PRO 132 -0.04 ASP 428

SER 424 0.14 THR 133 -0.04 ASP 428

SER 424 0.15 ASN 134 -0.04 ASP 428

LYS 423 0.16 LEU 135 -0.05 ASP 428

SER 424 0.17 HIS 136 -0.05 ASP 428

SER 424 0.15 PRO 137 -0.05 ASP 428

SER 424 0.17 MET 138 -0.06 ASP 428

SER 424 0.17 SER 139 -0.06 ASP 428

LYS 423 0.15 GLN 140 -0.05 ASP 428

SER 424 0.14 LEU 141 -0.05 ASP 428

LYS 423 0.16 SER 142 -0.06 ASP 428

LYS 423 0.17 ALA 143 -0.05 ASP 428

LYS 423 0.14 ALA 144 -0.05 ASP 428

LYS 423 0.13 ILE 145 -0.05 ASP 428

LYS 423 0.17 THR 146 -0.05 ASP 428

LYS 423 0.15 ALA 147 -0.04 ASP 428

LYS 423 0.13 LEU 148 -0.04 ASP 428

LYS 423 0.13 ASN 149 -0.04 THR 427

LYS 423 0.13 SER 150 -0.04 THR 427

LYS 423 0.10 GLU 151 -0.04 THR 427

LYS 423 0.09 SER 152 -0.05 THR 427

LYS 423 0.07 ASN 153 -0.05 THR 427

LYS 423 0.07 PHE 154 -0.06 THR 427

LYS 423 0.10 ALA 155 -0.05 THR 427

LYS 423 0.09 ARG 156 -0.04 THR 427

LYS 423 0.06 ALA 157 -0.05 THR 427

LYS 423 0.08 TYR 158 -0.05 MET 425

LYS 423 0.10 ALA 159 -0.05 MET 425

LYS 423 0.07 GLU 160 -0.05 MET 425

LYS 423 0.05 GLY 161 -0.06 SER 424

LYS 423 0.02 ILE 162 -0.06 MET 425

ALA 1 0.02 LEU 163 -0.08 SER 424

ALA 1 0.01 ARG 164 -0.09 SER 424

ALA 1 0.02 THR 165 -0.08 MET 425

ALA 1 0.02 LYS 166 -0.07 MET 425

ALA 1 0.01 TYR 167 -0.07 THR 427

ALA 1 0.01 TRP 168 -0.07 THR 427

ALA 1 0.01 GLU 169 -0.07 THR 427

ARG 421 0.02 MET 170 -0.06 THR 427

ARG 421 0.03 VAL 171 -0.07 THR 427

ARG 421 0.02 TYR 172 -0.07 THR 427

ARG 421 0.03 GLU 173 -0.06 THR 427

ARG 421 0.06 SER 174 -0.06 THR 427

ARG 421 0.04 ALA 175 -0.07 THR 427

SER 424 0.04 MET 176 -0.06 THR 427

LYS 423 0.05 ASP 177 -0.06 THR 427

LYS 423 0.07 LEU 178 -0.06 THR 427

SER 424 0.07 ILE 179 -0.06 THR 427

SER 424 0.06 ALA 180 -0.06 THR 427

SER 424 0.07 LYS 181 -0.05 THR 427

SER 424 0.09 LEU 182 -0.06 THR 427

SER 424 0.09 PRO 183 -0.05 THR 427

SER 424 0.09 CYS 184 -0.05 ALA 1

SER 424 0.10 VAL 185 -0.05 ASP 428

SER 424 0.11 ALA 186 -0.05 ASP 428

SER 424 0.10 ALA 187 -0.05 ASP 428

SER 424 0.10 LYS 188 -0.04 ASP 428

SER 424 0.12 ILE 189 -0.05 ASP 428

SER 424 0.12 TYR 190 -0.05 ASP 428

SER 424 0.11 ARG 191 -0.04 ASP 428

SER 424 0.11 ASN 192 -0.04 ASP 428

SER 424 0.12 LEU 193 -0.04 ASP 428

SER 424 0.12 TYR 194 -0.04 ASP 428

SER 424 0.11 ARG 195 -0.04 ASP 428

SER 424 0.11 ALA 196 -0.04 ASP 428

SER 424 0.10 GLY 197 -0.04 ASP 428

SER 424 0.09 SER 198 -0.04 ALA 1

SER 424 0.09 SER 199 -0.04 ALA 1

SER 424 0.09 ILE 200 -0.05 ALA 1

SER 424 0.08 GLY 201 -0.05 ALA 1

SER 424 0.07 ALA 202 -0.06 ALA 1

SER 424 0.06 ILE 203 -0.07 ALA 1

SER 424 0.06 ASP 204 -0.09 ALA 1

SER 424 0.05 SER 205 -0.10 ALA 1

SER 424 0.05 LYS 206 -0.12 ALA 1

SER 424 0.06 LEU 207 -0.10 ALA 1

SER 424 0.06 ASP 208 -0.09 ALA 1

SER 424 0.07 TRP 209 -0.07 ALA 1

SER 424 0.08 SER 210 -0.07 ALA 1

SER 424 0.07 HIS 211 -0.07 ALA 1

SER 424 0.07 ASN 212 -0.07 ALA 1

SER 424 0.09 PHE 213 -0.06 ALA 1

SER 424 0.09 THR 214 -0.06 ALA 1

SER 424 0.08 ASN 215 -0.06 ALA 1

SER 424 0.08 MET 216 -0.06 ALA 1

SER 424 0.10 LEU 217 -0.05 ALA 1

SER 424 0.09 GLY 218 -0.05 ALA 1

SER 424 0.09 TYR 219 -0.06 ALA 1

SER 424 0.08 THR 220 -0.06 ALA 1

SER 424 0.08 ASP 221 -0.06 ALA 1

SER 424 0.08 ALA 222 -0.06 ALA 1

SER 424 0.08 GLN 223 -0.06 ALA 1

SER 424 0.09 PHE 224 -0.06 ALA 1

SER 424 0.08 THR 225 -0.06 ALA 1

SER 424 0.08 GLU 226 -0.06 ALA 1

SER 424 0.09 LEU 227 -0.06 THR 427

SER 424 0.09 MET 228 -0.06 THR 427

SER 424 0.08 ARG 229 -0.06 THR 427

SER 424 0.09 LEU 230 -0.07 THR 427

SER 424 0.10 TYR 231 -0.07 THR 427

SER 424 0.10 LEU 232 -0.07 THR 427

SER 424 0.09 THR 233 -0.08 THR 427

SER 424 0.10 ILE 234 -0.08 THR 427

SER 424 0.12 HIS 235 -0.08 THR 427

SER 424 0.10 SER 236 -0.09 THR 427

SER 424 0.10 ASP 237 -0.10 THR 427

SER 424 0.11 HIS 238 -0.11 THR 427

SER 424 0.10 GLU 239 -0.13 THR 427

SER 424 0.10 GLY 240 -0.13 THR 427

SER 424 0.16 GLY 241 -0.15 THR 427

SER 424 0.19 ASN 242 -0.13 THR 427

SER 424 0.23 VAL 243 -0.12 THR 427

SER 424 0.18 SER 244 -0.10 THR 427

SER 424 0.14 ALA 245 -0.11 THR 427

SER 424 0.17 HIS 246 -0.13 THR 427

SER 424 0.18 THR 247 -0.11 THR 427

ARG 421 0.13 SER 248 -0.10 THR 427

ARG 421 0.09 HIS 249 -0.11 THR 427

ARG 421 0.24 LEU 250 -0.12 THR 427

ARG 421 0.26 VAL 251 -0.09 THR 427

ARG 421 0.15 GLY 252 -0.09 THR 427

ARG 421 0.11 SER 253 -0.10 THR 427

ARG 421 0.22 ALA 254 -0.08 THR 427

ARG 421 0.12 LEU 255 -0.07 THR 427

ARG 421 0.16 SER 256 -0.07 THR 427

ARG 421 0.11 ASP 257 -0.06 THR 427

ARG 421 0.10 PRO 258 -0.07 THR 427

ARG 421 0.12 TYR 259 -0.06 THR 427

ARG 421 0.16 LEU 260 -0.06 THR 427

ARG 421 0.16 SER 261 -0.08 THR 427

ARG 421 0.13 PHE 262 -0.07 THR 427

LYS 423 0.16 ALA 263 -0.06 THR 427

LYS 423 0.19 ALA 264 -0.07 THR 427

SER 424 0.17 ALA 265 -0.08 THR 427

SER 424 0.18 MET 266 -0.07 THR 427

SER 424 0.21 ASN 267 -0.07 ASP 428

SER 424 0.24 GLY 268 -0.09 THR 427

SER 424 0.21 LEU 269 -0.08 THR 427

SER 424 0.22 ALA 270 -0.07 ASP 428

SER 424 0.25 GLY 271 -0.08 ASP 428

SER 424 0.25 PRO 272 -0.08 ASP 428

SER 424 0.26 LEU 273 -0.10 ASP 428

SER 424 0.23 HIS 274 -0.09 THR 427

SER 424 0.20 GLY 275 -0.08 ASP 428

SER 424 0.20 LEU 276 -0.07 ASP 428

SER 424 0.18 ALA 277 -0.08 ASP 428

SER 424 0.16 ASN 278 -0.07 ASP 428

SER 424 0.17 GLN 279 -0.07 ASP 428

SER 424 0.18 GLU 280 -0.07 ASP 428

SER 424 0.16 VAL 281 -0.07 ASP 428

SER 424 0.15 LEU 282 -0.06 ASP 428

SER 424 0.16 GLY 283 -0.06 ASP 428

SER 424 0.16 TRP 284 -0.06 ASP 428

SER 424 0.14 LEU 285 -0.06 ASP 428

SER 424 0.14 ALA 286 -0.06 ASP 428

SER 424 0.14 GLN 287 -0.06 ASP 428

SER 424 0.13 LEU 288 -0.06 ASP 428

SER 424 0.13 GLN 289 -0.05 ASP 428

SER 424 0.13 LYS 290 -0.05 ASP 428

SER 424 0.13 ALA 291 -0.05 ASP 428

SER 424 0.10 ALA 295 -0.05 ASP 428

SER 424 0.10 GLY 296 -0.05 ASP 428

SER 424 0.10 ALA 297 -0.05 ASP 428

SER 424 0.10 ASP 298 -0.05 ASP 428

SER 424 0.10 ALA 299 -0.05 ASP 428

SER 424 0.11 SER 300 -0.05 ASP 428

SER 424 0.12 LEU 301 -0.05 ASP 428

SER 424 0.11 ARG 302 -0.06 ASP 428

SER 424 0.12 ASP 303 -0.05 ASP 428

SER 424 0.13 TYR 304 -0.06 ASP 428

SER 424 0.13 ILE 305 -0.06 ASP 428

SER 424 0.13 TRP 306 -0.06 ASP 428

SER 424 0.13 ASN 307 -0.06 ASP 428

SER 424 0.14 THR 308 -0.06 ASP 428

SER 424 0.14 LEU 309 -0.07 ASP 428

SER 424 0.14 ASN 310 -0.06 ASP 428

SER 424 0.15 SER 311 -0.06 ASP 428

SER 424 0.16 GLY 312 -0.07 ASP 428

SER 424 0.16 ARG 313 -0.07 ASP 428

SER 424 0.16 VAL 314 -0.07 ASP 428

SER 424 0.16 VAL 315 -0.07 ASP 428

SER 424 0.17 PRO 316 -0.07 ASP 428

SER 424 0.15 GLY 317 -0.08 THR 427

SER 424 0.14 TYR 318 -0.08 THR 427

SER 424 0.14 GLY 319 -0.09 THR 427

SER 424 0.14 HIS 320 -0.11 THR 427

SER 424 0.14 ALA 321 -0.12 THR 427

SER 424 0.11 VAL 322 -0.12 THR 427

SER 424 0.11 LEU 323 -0.11 THR 427

SER 424 0.09 ARG 324 -0.10 THR 427

SER 424 0.09 LYS 325 -0.09 THR 427

SER 424 0.10 THR 326 -0.09 THR 427

SER 424 0.11 ASP 327 -0.09 THR 427

SER 424 0.09 PRO 328 -0.09 THR 427

SER 424 0.10 ARG 329 -0.08 THR 427

SER 424 0.11 TYR 330 -0.08 THR 427

SER 424 0.10 THR 331 -0.08 THR 427

SER 424 0.09 CYS 332 -0.07 THR 427

SER 424 0.10 GLN 333 -0.07 THR 427

SER 424 0.10 ARG 334 -0.07 THR 427

SER 424 0.08 GLU 335 -0.07 THR 427

SER 424 0.09 PHE 336 -0.06 THR 427

SER 424 0.09 ALA 337 -0.06 THR 427

SER 424 0.09 LEU 338 -0.06 THR 427

SER 424 0.08 LYS 339 -0.06 THR 427

SER 424 0.09 HIS 340 -0.05 THR 427

SER 424 0.09 LEU 341 -0.05 THR 427

SER 424 0.09 PRO 342 -0.05 THR 427

SER 424 0.09 GLY 343 -0.05 ASP 428

SER 424 0.10 ASP 344 -0.05 ASP 428

SER 424 0.11 PRO 345 -0.05 ASP 428

SER 424 0.12 MET 346 -0.05 ASP 428

SER 424 0.11 PHE 347 -0.05 ASP 428

SER 424 0.10 LYS 348 -0.05 ASP 428

SER 424 0.11 LEU 349 -0.05 ASP 428

SER 424 0.12 VAL 350 -0.06 ASP 428

SER 424 0.11 ALA 351 -0.06 THR 427

SER 424 0.11 GLN 352 -0.06 THR 427

SER 424 0.12 LEU 353 -0.06 THR 427

SER 424 0.11 TYR 354 -0.07 THR 427

SER 424 0.10 LYS 355 -0.06 THR 427

SER 424 0.11 ILE 356 -0.06 THR 427

SER 424 0.12 VAL 357 -0.07 THR 427

SER 424 0.11 PRO 358 -0.07 THR 427

SER 424 0.10 ASN 359 -0.07 THR 427

SER 424 0.11 VAL 360 -0.06 THR 427

SER 424 0.12 LEU 361 -0.07 THR 427

SER 424 0.11 LEU 362 -0.08 THR 427

SER 424 0.11 GLU 363 -0.07 THR 427

SER 424 0.12 GLN 364 -0.07 THR 427

SER 424 0.12 GLY 365 -0.08 THR 427

SER 424 0.13 ALA 366 -0.08 THR 427

SER 424 0.12 ALA 367 -0.09 THR 427

SER 424 0.11 ALA 368 -0.10 THR 427

SER 424 0.11 ASN 369 -0.10 THR 427

SER 424 0.12 PRO 370 -0.09 THR 427

SER 424 0.12 TRP 371 -0.09 THR 427

SER 424 0.13 PRO 372 -0.08 THR 427

SER 424 0.13 ASN 373 -0.09 THR 427

SER 424 0.13 VAL 374 -0.08 THR 427

SER 424 0.15 ASP 375 -0.08 THR 427

SER 424 0.14 ALA 376 -0.07 THR 427

SER 424 0.12 HIS 377 -0.07 THR 427

SER 424 0.13 SER 378 -0.07 THR 427

SER 424 0.13 GLY 379 -0.06 ASP 428

SER 424 0.12 VAL 380 -0.06 ASP 428

SER 424 0.11 LEU 381 -0.06 THR 427

SER 424 0.12 LEU 382 -0.06 ASP 428

SER 424 0.12 GLN 383 -0.05 ASP 428

SER 424 0.11 TYR 384 -0.05 ASP 428

SER 424 0.10 TYR 385 -0.05 ASP 428

SER 424 0.11 GLY 386 -0.05 ASP 428

SER 424 0.12 MET 387 -0.05 ASP 428

SER 424 0.13 THR 388 -0.05 ASP 428

SER 424 0.14 GLU 389 -0.05 ASP 428

SER 424 0.15 MET 390 -0.06 ASP 428

SER 424 0.16 ASN 391 -0.06 ASP 428

SER 424 0.15 TYR 392 -0.06 ASP 428

SER 424 0.15 TYR 393 -0.06 ASP 428

SER 424 0.16 THR 394 -0.07 ASP 428

SER 424 0.14 VAL 395 -0.06 ASP 428

SER 424 0.13 LEU 396 -0.06 THR 427

SER 424 0.14 PHE 397 -0.07 THR 427

SER 424 0.14 GLY 398 -0.07 THR 427

SER 424 0.11 VAL 399 -0.07 THR 427

SER 424 0.11 SER 400 -0.08 THR 427

SER 424 0.12 ARG 401 -0.09 THR 427

SER 424 0.10 ALA 402 -0.08 THR 427

SER 424 0.08 LEU 403 -0.08 THR 427

SER 424 0.08 GLY 404 -0.09 THR 427

SER 424 0.09 VAL 405 -0.09 THR 427

SER 424 0.06 LEU 406 -0.09 THR 427

SER 424 0.04 ALA 407 -0.09 THR 427

SER 424 0.03 GLN 408 -0.10 THR 427

SER 424 0.03 LEU 409 -0.09 THR 427

SER 424 0.01 ILE 410 -0.09 THR 427

GLY 47 0.00 TRP 411 -0.09 THR 427

GLY 47 0.00 SER 412 -0.10 THR 427

ALA 1 0.00 ARG 413 -0.09 THR 427

ALA 1 0.01 ALA 414 -0.09 THR 427

ALA 1 0.01 LEU 415 -0.13 LYS 423

ALA 1 0.01 GLY 416 -0.12 ARG 421

ALA 1 0.00 PHE 417 -0.18 ARG 421

ALA 1 0.00 PRO 418 -0.20 ARG 421

PRO 422 0.04 LEU 419 -0.13 MET 425

ALA 32 0.00 GLU 420 -0.15 MET 425

VAL 251 0.26 ARG 421 -0.28 GLY 30

ALA 254 0.09 PRO 422 -0.32 GLY 50

VAL 251 0.19 LYS 423 -0.45 GLY 30

TYR 42 0.41 SER 424 -0.19 GLY 30

TYR 42 0.15 MET 425 -0.16 ILE 36

LYS 423 0.14 SER 426 -0.27 SER 41

SER 424 0.02 THR 427 -0.42 SER 41

LYS 423 0.08 ASP 428 -0.24 TYR 42

LYS 423 0.05 GLY 429 -0.14 SER 424

TYR 42 0.09 LEU 430 -0.14 LYS 423

SER 311 0.00 ILE 431 -0.19 VAL 38

VAL 38 0.06 ALA 432 -0.11 SER 424

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 2604241126091943151

--- 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.

* 5csc_open_aligned *