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

* closed-open-cutoff10 *

CA distance fluctuations for 2604270914072637783

--- normal mode 16 ---

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
MET 11 0.10 SER 3 -0.03 LYS 25

MET 11 0.13 SER 4 -0.04 PRO 293

PRO 14 0.13 TRP 5 -0.04 PRO 293

PRO 14 0.14 TRP 6 -0.06 LYS 25

MET 11 0.13 SER 7 -0.05 LYS 25

GLY 151 0.11 HIS 8 -0.07 GLU 22

GLY 151 0.14 VAL 9 -0.10 GLU 22

GLU 368 0.12 GLU 10 -0.07 GLU 22

TRP 6 0.13 MET 11 -0.09 LYS 164

GLU 368 0.16 GLY 12 -0.13 LEU 18

ALA 23 0.26 PRO 13 -0.16 ASN 142

GLY 264 0.20 PRO 14 -0.21 PRO 163

GLY 264 0.14 ASP 15 -0.18 PRO 163

PRO 145 0.15 PRO 16 -0.21 PRO 163

PRO 145 0.10 ILE 17 -0.16 PRO 163

ALA 39 0.14 LEU 18 -0.14 PRO 163

ALA 61 0.12 GLY 19 -0.14 PRO 163

PRO 13 0.15 VAL 20 -0.10 PRO 163

GLY 45 0.12 THR 21 -0.09 TYR 295

PRO 13 0.15 GLU 22 -0.10 VAL 9

PRO 13 0.26 ALA 23 -0.07 PRO 163

PRO 13 0.19 PHE 24 -0.13 GLY 264

PRO 13 0.16 LYS 25 -0.20 GLY 264

PRO 13 0.22 ARG 26 -0.15 GLY 264

PRO 13 0.22 ASP 27 -0.16 GLY 264

PRO 13 0.19 THR 28 -0.20 GLY 264

PRO 13 0.17 ASN 29 -0.18 LYS 46

PRO 13 0.14 SER 30 -0.27 LYS 46

PRO 13 0.13 LYS 31 -0.25 LYS 46

PRO 13 0.15 LYS 32 -0.19 LYS 46

PRO 13 0.13 MET 33 -0.14 PRO 47

PRO 13 0.12 ASN 34 -0.13 GLY 264

ASN 396 0.11 LEU 35 -0.08 GLY 264

GLY 141 0.09 GLY 36 -0.07 PRO 163

LEU 18 0.08 VAL 37 -0.09 PRO 163

ASN 142 0.08 GLY 38 -0.08 SER 30

LEU 18 0.14 ALA 39 -0.13 SER 30

LEU 18 0.11 TYR 40 -0.14 SER 30

LEU 18 0.11 ARG 41 -0.18 SER 30

LEU 18 0.09 ASP 42 -0.16 LEU 50

LEU 18 0.09 ASP 43 -0.16 ASN 51

THR 21 0.11 ASN 44 -0.16 ASN 51

THR 21 0.12 GLY 45 -0.22 LYS 31

LEU 18 0.11 LYS 46 -0.27 SER 30

LEU 18 0.11 PRO 47 -0.24 SER 30

LEU 18 0.10 TYR 48 -0.22 SER 30

LEU 18 0.13 VAL 49 -0.19 SER 30

PRO 14 0.11 LEU 50 -0.17 SER 30

PRO 14 0.10 ASN 51 -0.17 SER 30

PRO 14 0.10 CYS 52 -0.16 SER 30

PRO 14 0.12 VAL 53 -0.17 SER 30

PRO 14 0.14 ARG 54 -0.19 SER 30

PRO 14 0.12 LYS 55 -0.17 SER 30

PRO 14 0.12 ALA 56 -0.17 SER 30

PRO 14 0.14 GLU 57 -0.18 SER 30

PRO 14 0.14 ALA 58 -0.17 SER 30

PRO 14 0.13 MET 59 -0.16 SER 30

PRO 14 0.13 ILE 60 -0.17 SER 30

PRO 14 0.18 ALA 61 -0.14 SER 30

PRO 14 0.16 ALA 62 -0.13 THR 312

PRO 14 0.13 LYS 63 -0.18 THR 312

PRO 14 0.16 LYS 64 -0.12 ASP 78

PRO 14 0.14 MET 66 -0.15 ASP 78

PRO 14 0.14 ASP 67 -0.15 SER 30

PRO 14 0.15 LYS 68 -0.17 SER 30

PRO 14 0.10 GLU 69 -0.17 SER 30

PRO 14 0.10 TYR 70 -0.16 SER 30

PRO 14 0.10 LEU 71 -0.15 SER 30

PRO 14 0.09 PRO 72 -0.13 SER 30

PRO 14 0.09 ILE 73 -0.12 SER 30

PRO 14 0.09 ALA 74 -0.12 SER 30

PRO 14 0.10 GLY 75 -0.13 SER 30

PRO 14 0.09 LEU 76 -0.14 SER 30

PRO 14 0.08 ALA 77 -0.13 MET 66

PRO 14 0.08 ASP 78 -0.16 LYS 63

PRO 14 0.09 PHE 79 -0.13 SER 30

PRO 14 0.08 THR 80 -0.11 SER 30

PRO 14 0.07 ARG 81 -0.12 LYS 63

PRO 14 0.07 ALA 82 -0.13 LYS 63

PRO 14 0.07 SER 83 -0.10 SER 30

ASP 384 0.06 ALA 84 -0.10 LYS 63

ASP 384 0.05 GLU 85 -0.12 LYS 63

ASP 384 0.05 LEU 86 -0.10 SER 30

ASP 384 0.06 ALA 87 -0.09 SER 30

LYS 366 0.07 LEU 88 -0.09 LYS 63

GLY 364 0.05 GLY 89 -0.11 LYS 63

ASP 384 0.04 GLU 90 -0.13 LYS 63

ASN 349 0.05 ASN 91 -0.12 LYS 63

LYS 366 0.07 SER 92 -0.11 LYS 63

LYS 366 0.07 GLU 93 -0.11 LYS 63

LYS 366 0.08 ALA 94 -0.10 LYS 63

LYS 366 0.06 PHE 95 -0.12 LYS 63

LYS 366 0.06 LYS 96 -0.13 LYS 63

LYS 366 0.07 SER 97 -0.12 LYS 63

LYS 366 0.07 GLY 98 -0.12 LYS 63

LYS 366 0.08 ARG 99 -0.10 LYS 63

LYS 366 0.08 TYR 100 -0.09 LYS 63

LYS 366 0.08 VAL 101 -0.08 SER 30

ASP 384 0.07 THR 102 -0.09 SER 30

PRO 14 0.08 VAL 103 -0.10 SER 30

PRO 14 0.10 GLN 104 -0.12 SER 30

PRO 14 0.11 GLY 105 -0.12 LYS 25

PRO 14 0.14 ILE 106 -0.14 LYS 25

PRO 14 0.12 SER 107 -0.13 LYS 25

ASP 384 0.10 GLY 108 -0.11 LYS 25

PRO 14 0.12 THR 109 -0.11 LYS 25

PRO 14 0.13 GLY 110 -0.12 LYS 25

ASP 384 0.10 SER 111 -0.10 LYS 25

ASP 384 0.12 LEU 112 -0.09 LYS 25

ASP 384 0.12 ARG 113 -0.09 LYS 25

ASP 384 0.10 VAL 114 -0.09 LYS 25

LYS 366 0.12 GLY 115 -0.08 LYS 25

LYS 366 0.14 ALA 116 -0.08 PRO 13

LYS 366 0.13 ASN 117 -0.06 LYS 25

LYS 366 0.12 PHE 118 -0.06 LYS 25

LYS 366 0.14 LEU 119 -0.06 PRO 13

LYS 366 0.15 GLN 120 -0.06 PRO 13

LYS 366 0.13 ARG 121 -0.06 CYS 274

LYS 366 0.13 PHE 122 -0.08 CYS 274

LYS 366 0.14 PHE 123 -0.08 ILE 273

LYS 366 0.15 LYS 124 -0.08 CYS 274

LYS 366 0.16 PHE 125 -0.06 ILE 273

LYS 366 0.18 SER 126 -0.07 PRO 13

LYS 366 0.19 ARG 129 -0.07 PRO 13

LYS 366 0.21 ASP 130 -0.09 PRO 13

LYS 366 0.21 VAL 133 -0.10 PRO 13

LYS 366 0.22 TYR 134 -0.11 PRO 13

LYS 366 0.24 LEU 135 -0.12 PRO 13

LYS 366 0.23 PRO 136 -0.14 PRO 13

LYS 366 0.30 LYS 137 -0.15 PRO 13

LYS 366 0.31 PRO 138 -0.16 PRO 13

ASP 384 0.28 SER 139 -0.12 PRO 13

ASP 384 0.28 TRP 140 -0.12 PRO 13

ASP 384 0.35 GLY 141 -0.16 PRO 13

ASP 384 0.22 ASN 142 -0.16 PRO 13

ASP 384 0.22 HIS 143 -0.14 PRO 13

ASP 384 0.25 THR 144 -0.15 PRO 13

LYS 383 0.22 PRO 145 -0.15 PRO 13

ASP 384 0.18 ILE 146 -0.11 PRO 13

LYS 366 0.19 PHE 147 -0.10 PRO 13

PRO 367 0.21 ARG 148 -0.11 PRO 13

PRO 367 0.17 ASP 149 -0.09 PRO 13

LYS 366 0.16 ALA 150 -0.07 PRO 13

LYS 366 0.18 GLY 151 -0.07 PRO 13

LYS 366 0.19 LEU 152 -0.09 PRO 13

LYS 366 0.23 GLN 154 -0.10 PRO 13

LYS 366 0.25 LEU 155 -0.12 PRO 13

LYS 366 0.27 GLN 156 -0.11 PRO 13

LYS 366 0.28 ALA 157 -0.13 PRO 13

LYS 366 0.25 TYR 158 -0.12 PRO 13

LYS 366 0.25 ARG 159 -0.13 PRO 13

GLY 364 0.21 TYR 160 -0.12 PRO 13

GLY 364 0.26 TYR 161 -0.13 PRO 16

HIS 348 0.30 ASP 162 -0.14 PRO 14

HIS 348 0.35 PRO 163 -0.21 PRO 16

HIS 348 0.40 LYS 164 -0.20 PRO 14

ASN 349 0.35 THR 165 -0.16 PRO 14

ASN 349 0.33 CYS 166 -0.15 PRO 16

ASN 349 0.24 SER 167 -0.12 PRO 16

HIS 348 0.19 LEU 168 -0.11 PRO 16

HIS 348 0.23 ASP 169 -0.11 PRO 13

HIS 348 0.19 PHE 170 -0.11 PRO 13

HIS 348 0.20 THR 171 -0.10 PRO 13

HIS 348 0.22 GLY 172 -0.11 PRO 13

HIS 348 0.19 ALA 173 -0.11 PRO 13

HIS 348 0.17 MET 174 -0.10 PRO 13

HIS 348 0.18 GLU 175 -0.10 PRO 13

LYS 366 0.21 ASP 176 -0.10 PRO 13

LYS 366 0.19 ILE 177 -0.09 PRO 13

LYS 366 0.17 SER 178 -0.09 PRO 13

LYS 366 0.19 LYS 179 -0.09 PRO 13

LYS 366 0.20 ILE 180 -0.09 PRO 13

LYS 366 0.18 PRO 181 -0.08 PRO 13

LYS 366 0.17 GLU 182 -0.07 PRO 13

LYS 366 0.16 LYS 183 -0.07 PRO 13

LYS 366 0.18 SER 184 -0.08 PRO 13

LYS 366 0.18 ILE 185 -0.08 PRO 13

LYS 366 0.19 ILE 186 -0.09 PRO 13

LYS 366 0.18 LEU 187 -0.09 PRO 13

LYS 366 0.16 LEU 188 -0.09 PRO 13

LYS 366 0.13 HIS 189 -0.08 PRO 13

GLY 364 0.09 ALA 190 -0.07 PRO 13

HIS 348 0.08 CYS 191 -0.07 GLN 202

HIS 348 0.09 ALA 192 -0.06 PRO 16

GLY 364 0.11 HIS 193 -0.10 PRO 16

GLY 364 0.11 ASN 194 -0.12 PRO 16

GLY 364 0.14 PRO 195 -0.15 PRO 16

GLY 364 0.16 THR 196 -0.14 PRO 16

HIS 348 0.10 GLY 197 -0.10 PRO 16

HIS 348 0.13 VAL 198 -0.10 PRO 16

ASN 349 0.13 ASP 199 -0.09 PRO 16

ASN 349 0.15 PRO 200 -0.08 PRO 13

ASN 349 0.14 ARG 201 -0.07 SER 230

ASN 349 0.11 GLN 202 -0.11 ARG 235

ASN 349 0.12 GLU 203 -0.09 ARG 235

ASN 349 0.15 GLN 204 -0.07 PRO 13

ASN 349 0.13 TRP 205 -0.07 PRO 13

HIS 348 0.12 LYS 206 -0.09 ARG 235

HIS 348 0.14 GLU 207 -0.07 PRO 13

HIS 348 0.15 LEU 208 -0.07 PRO 13

HIS 348 0.13 ALA 209 -0.06 PRO 13

HIS 348 0.13 SER 210 -0.06 PRO 13

LYS 366 0.15 VAL 211 -0.07 PRO 13

LYS 366 0.15 VAL 212 -0.07 PRO 13

LYS 366 0.13 LYS 213 -0.06 PRO 13

LYS 366 0.14 LYS 214 -0.06 PRO 13

LYS 366 0.16 ARG 215 -0.07 PRO 13

LYS 366 0.15 ASN 216 -0.06 PRO 13

LYS 366 0.16 LEU 217 -0.07 PRO 13

LYS 366 0.15 LEU 218 -0.07 PRO 13

LYS 366 0.15 ALA 219 -0.07 PRO 13

LYS 366 0.15 TYR 220 -0.07 PRO 13

LYS 366 0.13 PHE 221 -0.07 PRO 13

ASP 384 0.12 ASP 222 -0.07 PRO 13

ASP 384 0.09 MET 223 -0.07 LYS 25

ASP 384 0.09 ALA 224 -0.09 LYS 25

ASP 384 0.06 TYR 225 -0.08 SER 30

ASP 384 0.06 GLN 226 -0.08 SER 30

ASP 384 0.04 GLY 227 -0.08 GLN 202

ASN 142 0.04 PHE 228 -0.08 GLN 202

HIS 348 0.05 ALA 229 -0.09 GLN 202

GLN 351 0.04 SER 230 -0.11 GLN 202

TYR 48 0.04 GLY 231 -0.09 GLN 202

LEU 310 0.04 ASP 232 -0.10 GLN 202

LEU 310 0.05 ILE 233 -0.08 GLN 202

ASP 236 0.06 ASN 234 -0.07 LYS 63

ASN 234 0.06 ARG 235 -0.11 GLN 202

HIS 348 0.06 ASP 236 -0.10 GLN 202

ASN 349 0.07 ALA 237 -0.06 SER 30

ASN 349 0.09 TRP 238 -0.07 LYS 206

ASN 349 0.10 ALA 239 -0.06 PRO 13

LYS 366 0.09 LEU 240 -0.06 LYS 63

HIS 348 0.09 ARG 241 -0.08 LYS 63

ASN 349 0.10 HIS 242 -0.07 LYS 63

LYS 366 0.11 PHE 243 -0.06 LYS 63

LYS 366 0.10 ILE 244 -0.07 LYS 63

HIS 348 0.09 GLU 245 -0.08 LYS 63

HIS 348 0.10 GLN 246 -0.07 LYS 63

LYS 366 0.11 GLY 247 -0.07 LYS 63

LYS 366 0.12 ILE 248 -0.06 LYS 63

LYS 366 0.12 ASP 249 -0.06 LYS 124

LYS 366 0.12 VAL 250 -0.06 PHE 123

LYS 366 0.12 VAL 251 -0.06 LYS 25

LYS 366 0.11 LEU 252 -0.07 LYS 25

ASP 384 0.10 SER 253 -0.08 LYS 25

ASP 384 0.09 GLN 254 -0.09 SER 30

PRO 14 0.08 SER 255 -0.11 SER 30

PRO 14 0.10 TYR 256 -0.12 SER 30

PRO 14 0.12 ALA 257 -0.14 SER 30

PRO 14 0.09 LYS 258 -0.13 SER 30

PRO 14 0.08 ASN 259 -0.11 SER 30

PRO 14 0.11 MET 260 -0.14 SER 30

PRO 14 0.13 GLY 261 -0.16 SER 30

PRO 14 0.14 LEU 262 -0.18 SER 30

PRO 14 0.16 TYR 263 -0.18 SER 30

PRO 14 0.20 GLY 264 -0.21 SER 30

PRO 14 0.16 GLU 265 -0.20 SER 30

PRO 14 0.16 ARG 266 -0.16 SER 30

PRO 14 0.13 ALA 267 -0.15 SER 30

PRO 14 0.10 GLY 268 -0.12 SER 30

PRO 14 0.09 ALA 269 -0.10 SER 30

ASP 384 0.09 PHE 270 -0.09 LYS 25

LYS 366 0.09 THR 271 -0.08 LYS 25

LYS 366 0.10 VAL 272 -0.08 PHE 123

LYS 366 0.10 ILE 273 -0.08 PHE 123

LYS 366 0.10 CYS 274 -0.08 LYS 124

LYS 366 0.10 ARG 275 -0.08 LYS 63

LYS 366 0.09 ASP 276 -0.10 LYS 63

LYS 366 0.08 ALA 277 -0.11 LYS 63

LYS 366 0.08 GLU 278 -0.10 LYS 63

LYS 366 0.09 GLU 279 -0.09 LYS 63

LYS 366 0.09 ALA 280 -0.09 LYS 63

LYS 366 0.08 LYS 281 -0.10 LYS 63

LYS 366 0.09 ARG 282 -0.08 LYS 63

LYS 366 0.10 VAL 283 -0.07 LYS 25

LYS 366 0.08 GLU 284 -0.08 LYS 25

LYS 366 0.08 SER 285 -0.08 LYS 25

LYS 366 0.09 GLN 286 -0.08 LYS 25

LYS 366 0.09 LEU 287 -0.09 LYS 25

PRO 14 0.08 LYS 288 -0.10 LYS 25

PRO 14 0.08 ILE 289 -0.09 LYS 25

PRO 14 0.09 LEU 290 -0.09 LYS 25

PRO 14 0.10 ILE 291 -0.11 LYS 25

PRO 14 0.10 ARG 292 -0.12 LYS 25

PRO 14 0.10 PRO 293 -0.12 LYS 25

PRO 14 0.11 MET 294 -0.13 LYS 25

PRO 14 0.13 TYR 295 -0.14 LYS 25

PRO 14 0.11 SER 296 -0.13 LYS 25

PRO 14 0.11 ASN 297 -0.14 SER 30

PRO 14 0.13 PRO 298 -0.15 SER 30

PRO 14 0.14 PRO 299 -0.17 SER 30

PRO 14 0.13 MET 300 -0.17 SER 30

PRO 14 0.14 ASN 301 -0.19 SER 30

PRO 14 0.13 GLY 302 -0.18 SER 30

PRO 14 0.12 ALA 303 -0.16 SER 30

PRO 14 0.11 ARG 304 -0.17 SER 30

PRO 14 0.12 ILE 305 -0.17 SER 30

PRO 14 0.10 ALA 306 -0.15 SER 30

PRO 14 0.09 SER 307 -0.14 SER 30

PRO 14 0.10 LEU 308 -0.17 LYS 63

PRO 14 0.09 ILE 309 -0.14 SER 30

PRO 14 0.08 LEU 310 -0.14 LYS 63

PRO 14 0.08 ASN 311 -0.17 LYS 63

PRO 14 0.08 THR 312 -0.18 LYS 63

PRO 14 0.07 PRO 313 -0.13 LYS 63

PRO 14 0.08 GLU 314 -0.11 SER 30

PRO 14 0.09 LEU 315 -0.13 SER 30

PRO 14 0.07 ARG 316 -0.12 GLU 90

PRO 14 0.06 LYS 317 -0.12 GLU 90

PRO 14 0.08 GLU 318 -0.11 SER 30

PRO 14 0.08 TRP 319 -0.12 SER 30

PRO 14 0.06 LEU 320 -0.10 SER 30

TYR 48 0.07 VAL 321 -0.09 SER 30

TYR 48 0.09 GLU 322 -0.11 SER 30

LEU 18 0.06 VAL 323 -0.10 SER 30

TYR 48 0.07 LYS 324 -0.08 SER 30

TYR 48 0.08 GLY 325 -0.10 SER 30

TYR 48 0.08 MET 326 -0.10 SER 30

TYR 48 0.05 ALA 327 -0.08 SER 30

TYR 48 0.07 ASP 328 -0.07 GLN 336

LEU 18 0.05 ARG 329 -0.08 ASN 51

ASN 142 0.05 ILE 330 -0.06 SER 30

ASN 142 0.04 ILE 331 -0.05 LEU 365

GLY 141 0.04 SER 332 -0.09 GLN 336

GLY 141 0.06 MET 333 -0.08 ASN 51

PRO 138 0.06 ARG 334 -0.07 LEU 365

ASP 162 0.06 THR 335 -0.07 LEU 365

LYS 164 0.08 GLN 336 -0.09 SER 332

ASP 162 0.11 LEU 337 -0.07 ASN 51

CYS 166 0.15 VAL 338 -0.07 THR 335

LYS 164 0.14 SER 339 -0.08 ASN 51

LYS 164 0.16 ASN 340 -0.09 ASN 51

LYS 164 0.20 LEU 341 -0.07 ASN 51

LYS 164 0.22 LYS 342 -0.07 ASN 51

LYS 164 0.19 LYS 343 -0.09 ASN 51

LYS 164 0.20 GLU 344 -0.09 ASN 51

LYS 164 0.24 GLY 345 -0.07 ASN 51

LYS 164 0.28 SER 346 -0.06 ASN 51

LYS 164 0.34 SER 347 -0.06 PRO 14

LYS 164 0.40 HIS 348 -0.07 PRO 14

LYS 164 0.38 ASN 349 -0.09 LEU 365

CYS 166 0.28 TRP 350 -0.11 LEU 365

CYS 166 0.13 GLN 351 -0.14 LEU 365

TRP 350 0.20 HIS 352 -0.09 PRO 14

TYR 161 0.10 ILE 353 -0.09 LEU 365

GLN 356 0.08 THR 354 -0.07 LEU 365

ASP 199 0.07 ASP 355 -0.08 PRO 16

TRP 350 0.09 GLN 356 -0.08 PRO 16

ALA 192 0.06 ILE 357 -0.06 PRO 16

ASN 142 0.05 GLY 358 -0.05 GLN 202

ASN 142 0.07 MET 359 -0.06 SER 30

GLY 141 0.08 PHE 360 -0.06 PRO 16

ALA 401 0.11 CYS 361 -0.09 PRO 16

PRO 138 0.17 PHE 362 -0.12 PRO 16

PRO 138 0.17 THR 363 -0.12 PRO 14

PRO 138 0.30 GLY 364 -0.13 GLN 351

PRO 138 0.27 LEU 365 -0.14 GLN 351

PRO 138 0.31 LYS 366 -0.14 PRO 14

GLN 156 0.25 PRO 367 -0.17 PRO 14

GLN 156 0.23 GLU 368 -0.14 PRO 14

PRO 138 0.20 GLN 369 -0.12 PRO 14

GLY 141 0.20 VAL 370 -0.12 PRO 14

GLN 156 0.17 GLU 371 -0.14 PRO 14

GLN 156 0.16 ARG 372 -0.10 PRO 14

GLY 141 0.15 LEU 373 -0.08 LYS 46

PRO 13 0.19 THR 374 -0.08 LYS 46

PRO 13 0.21 LYS 375 -0.08 LYS 46

PRO 13 0.17 GLU 376 -0.10 LYS 46

PRO 13 0.15 PHE 377 -0.13 LYS 46

PRO 13 0.18 SER 378 -0.12 LYS 46

PRO 13 0.15 ILE 379 -0.10 LYS 46

PRO 13 0.15 TYR 380 -0.07 GLY 264

GLY 141 0.17 MET 381 -0.08 PRO 14

GLY 141 0.25 THR 382 -0.12 PRO 14

GLY 141 0.30 LYS 383 -0.18 PRO 14

GLY 141 0.35 ASP 384 -0.18 PRO 163

GLY 141 0.23 GLY 385 -0.14 PRO 14

GLY 141 0.20 ARG 386 -0.11 PRO 14

GLY 141 0.13 ILE 387 -0.07 PRO 14

GLY 141 0.10 SER 388 -0.04 GLY 264

GLY 141 0.08 VAL 389 -0.05 ILE 379

ASN 142 0.06 ALA 390 -0.08 SER 30

LEU 18 0.09 GLY 391 -0.11 LYS 31

GLY 141 0.08 VAL 392 -0.08 LYS 31

PRO 13 0.08 ALA 393 -0.12 ASN 51

PRO 13 0.08 SER 394 -0.14 ASN 51

PRO 13 0.11 SER 395 -0.13 ASN 51

PRO 13 0.11 ASN 396 -0.11 ASN 51

PRO 138 0.10 VAL 397 -0.11 ASN 51

ASP 162 0.11 GLY 398 -0.11 ASN 51

ASP 162 0.11 TYR 399 -0.11 GLY 45

PRO 138 0.13 LEU 400 -0.09 GLY 45

ASP 162 0.15 ALA 401 -0.08 ASN 51

LYS 164 0.16 HIS 402 -0.08 ASN 51

PRO 138 0.14 ALA 403 -0.09 GLY 45

PRO 138 0.18 ILE 404 -0.06 GLY 45

PRO 163 0.21 HIS 405 -0.06 ASN 51

PRO 163 0.19 GLN 406 -0.07 GLY 45

PRO 138 0.19 VAL 408 -0.08 PRO 14

PRO 163 0.26 THR 409 -0.08 PRO 14

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.

*** closed-open-cutoff10 ***

CA distance fluctuations for 2604270914072637783

--- normal mode 16 ---

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

* closed-open-cutoff10 *