Should you encounter any unexpected behaviour,
please let us know.
elNémo has been hacked on november 27th.
It has been moved away and runs again.
Still some additional cleaning from time to time
Sorry for the inconvenience.

* 7LO8 A3 single *

CA distance fluctuations for 2603140610172731181

--- 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
ILE 249 0.13 MET 1 -0.10 GLY 145

ILE 256 0.18 ASN 2 -0.10 PHE 149

ILE 249 0.19 LYS 3 -0.11 PHE 149

ILE 249 0.17 GLN 4 -0.09 ILE 146

ILE 249 0.18 ILE 5 -0.10 ILE 146

ILE 249 0.23 LEU 6 -0.12 ILE 146

ILE 249 0.23 VAL 7 -0.10 ILE 146

SER 241 0.22 LEU 8 -0.08 GLY 348

THR 245 0.25 TYR 9 -0.10 GLY 143

THR 245 0.29 PHE 10 -0.11 GLY 348

LYS 238 0.29 ASN 11 -0.11 GLY 348

SER 241 0.31 ILE 12 -0.11 GLY 348

THR 245 0.36 PHE 13 -0.12 GLY 348

LYS 238 0.37 LEU 14 -0.14 GLY 348

LYS 238 0.38 ILE 15 -0.16 GLY 348

SER 241 0.43 PHE 16 -0.16 GLY 348

LYS 238 0.47 LEU 17 -0.16 GLY 348

LYS 238 0.46 GLY 18 -0.20 GLY 348

LYS 238 0.47 ILE 19 -0.23 GLY 348

LYS 238 0.56 GLY 20 -0.21 GLY 348

LYS 238 0.57 LEU 21 -0.23 GLY 348

LYS 238 0.52 VAL 22 -0.32 GLY 348

LYS 238 0.55 ILE 23 -0.34 GLY 348

LYS 238 0.63 PRO 24 -0.29 GLY 348

LYS 238 0.51 VAL 25 -0.35 GLY 348

LYS 238 0.43 LEU 26 -0.46 GLY 348

LYS 238 0.35 PRO 27 -0.52 GLY 348

LYS 238 0.35 VAL 28 -0.44 ALA 349

LYS 238 0.33 TYR 29 -0.47 ALA 349

LYS 238 0.27 LEU 30 -0.58 ALA 349

LYS 238 0.21 LYS 31 -0.59 ALA 349

LYS 238 0.22 ASP 32 -0.51 ALA 349

LYS 238 0.24 LEU 33 -0.52 ALA 349

LYS 238 0.18 GLY 34 -0.61 ALA 349

LYS 238 0.19 LEU 35 -0.70 ALA 349

LYS 238 0.12 THR 36 -0.85 ALA 349

LYS 238 0.13 GLY 37 -0.99 ALA 349

LYS 238 0.14 SER 38 -1.04 ALA 349

LYS 238 0.22 ASP 39 -0.78 ALA 349

LYS 238 0.25 LEU 40 -0.77 ALA 349

LYS 238 0.25 GLY 41 -0.93 LEU 345

LYS 238 0.28 LEU 42 -0.65 LEU 345

LYS 238 0.33 LEU 43 -0.55 LEU 345

LYS 238 0.37 VAL 44 -0.53 LEU 345

PRO 237 0.37 ALA 45 -0.45 LEU 345

LYS 238 0.36 ALA 46 -0.33 LEU 345

LYS 238 0.40 PHE 47 -0.25 LEU 345

PRO 237 0.40 ALA 48 -0.22 MET 338

PRO 237 0.36 LEU 49 -0.16 ILE 346

LYS 238 0.35 SER 50 -0.15 ALA 349

LYS 238 0.35 GLN 51 -0.11 MET 103

PRO 237 0.32 MET 52 -0.09 LEU 212

LYS 238 0.30 ILE 53 -0.09 ALA 368

LYS 238 0.30 ILE 54 -0.07 ILE 73

LYS 238 0.29 SER 55 -0.08 MET 107

LYS 238 0.25 PRO 56 -0.06 VAL 371

LYS 238 0.25 PHE 57 -0.06 VAL 371

LYS 238 0.27 GLY 58 -0.08 ILE 70

LYS 238 0.24 GLY 59 -0.05 ILE 70

LYS 238 0.22 THR 60 -0.05 VAL 371

LYS 238 0.22 LEU 61 -0.05 ILE 174

LYS 238 0.22 ALA 62 -0.05 ILE 174

LYS 238 0.19 ASP 63 -0.06 ASP 179

LYS 238 0.19 LYS 64 -0.06 ASP 179

LYS 238 0.21 LEU 65 -0.05 ILE 174

LYS 238 0.20 GLY 66 -0.06 ASP 179

LYS 238 0.20 LYS 67 -0.06 GLY 348

LYS 238 0.21 LYS 68 -0.07 GLY 348

LYS 238 0.23 LEU 69 -0.08 ILE 174

LYS 238 0.25 ILE 70 -0.08 ALA 349

LYS 238 0.26 ILE 71 -0.09 GLY 348

LYS 238 0.26 CYS 72 -0.11 ALA 349

LYS 238 0.28 ILE 73 -0.12 ALA 349

LYS 238 0.30 GLY 74 -0.13 ALA 349

LYS 238 0.31 LEU 75 -0.14 ALA 349

LYS 238 0.31 ILE 76 -0.16 ALA 349

LYS 238 0.32 LEU 77 -0.17 ALA 349

LYS 238 0.35 PHE 78 -0.18 ALA 349

LYS 238 0.35 SER 79 -0.19 ALA 349

LYS 238 0.34 VAL 80 -0.21 ALA 349

LYS 238 0.36 SER 81 -0.24 ALA 349

LYS 238 0.40 GLU 82 -0.25 ALA 349

LYS 238 0.36 PHE 83 -0.26 ALA 349

LYS 238 0.34 MET 84 -0.30 ALA 349

LYS 238 0.37 PHE 85 -0.33 ALA 349

LYS 238 0.38 ALA 86 -0.31 ALA 349

LYS 238 0.32 VAL 87 -0.32 ALA 349

LYS 238 0.29 GLY 88 -0.37 ALA 349

LYS 238 0.25 HIS 89 -0.43 ALA 349

LYS 238 0.24 ASN 90 -0.47 ALA 349

LYS 238 0.25 PHE 91 -0.51 ALA 349

LYS 238 0.25 SER 92 -0.46 ALA 349

LYS 238 0.29 VAL 93 -0.39 ALA 349

LYS 238 0.32 LEU 94 -0.42 ALA 349

LYS 238 0.30 MET 95 -0.43 ALA 349

LYS 238 0.31 LEU 96 -0.35 ALA 349

LYS 238 0.35 SER 97 -0.31 ALA 349

LYS 238 0.37 ARG 98 -0.32 ALA 349

LYS 238 0.34 VAL 99 -0.26 ALA 349

LYS 238 0.34 ILE 100 -0.22 ALA 349

LYS 238 0.38 GLY 101 -0.22 ALA 349

LYS 238 0.37 GLY 102 -0.18 ALA 349

LYS 238 0.33 MET 103 -0.16 ALA 349

LYS 238 0.34 SER 104 -0.15 ALA 349

LYS 238 0.35 ALA 105 -0.13 ALA 349

LYS 238 0.31 GLY 106 -0.10 ALA 349

LYS 238 0.28 MET 107 -0.09 ALA 349

LYS 238 0.29 VAL 108 -0.09 GLY 348

LYS 238 0.28 MET 109 -0.10 VAL 44

LYS 238 0.25 PRO 110 -0.07 VAL 44

LYS 238 0.23 GLY 111 -0.06 GLY 348

LYS 238 0.22 VAL 112 -0.08 VAL 44

LYS 238 0.20 THR 113 -0.10 VAL 44

LYS 238 0.18 GLY 114 -0.07 VAL 44

LYS 238 0.17 LEU 115 -0.07 VAL 44

LYS 238 0.15 ILE 116 -0.09 VAL 44

LYS 238 0.13 ALA 117 -0.08 VAL 44

LYS 238 0.12 ASP 118 -0.07 VAL 44

LYS 238 0.11 VAL 119 -0.07 GLY 145

LYS 238 0.08 SER 120 -0.09 LEU 142

SER 267 0.10 PRO 121 -0.08 LEU 142

SER 267 0.12 SER 122 -0.09 GLY 37

SER 267 0.13 HIS 123 -0.10 GLY 37

ASN 2 0.14 GLN 124 -0.12 GLY 37

ASN 2 0.10 LYS 125 -0.11 GLY 37

ASN 2 0.11 ALA 126 -0.14 GLY 37

ASN 2 0.15 LYS 127 -0.14 GLY 37

ASN 2 0.12 ASN 128 -0.12 GLY 37

SER 241 0.11 PHE 129 -0.14 GLY 37

LEU 6 0.12 GLY 130 -0.16 GLY 37

ALA 252 0.16 TYR 131 -0.15 GLY 37

GLY 248 0.20 MET 132 -0.14 GLY 37

GLY 248 0.21 SER 133 -0.17 GLY 37

GLY 248 0.28 ALA 134 -0.17 GLY 37

GLY 248 0.36 ILE 135 -0.14 GLY 37

THR 245 0.35 ILE 136 -0.16 GLY 37

THR 245 0.41 ASN 137 -0.19 GLY 37

THR 245 0.55 SER 138 -0.15 GLY 37

SER 241 0.47 GLY 139 -0.13 GLY 37

SER 241 0.56 PHE 140 -0.18 ILE 23

SER 241 0.66 ILE 141 -0.17 PRO 24

SER 241 0.61 LEU 142 -0.12 GLY 348

LYS 238 0.60 GLY 143 -0.14 GLY 348

LYS 238 0.73 PRO 144 -0.16 PRO 24

LYS 238 0.81 GLY 145 -0.12 LEU 6

LYS 238 0.68 ILE 146 -0.13 GLY 348

LYS 238 0.68 GLY 147 -0.18 GLY 348

LYS 238 0.81 GLY 148 -0.15 ALA 349

LYS 238 0.73 PHE 149 -0.12 ALA 349

LYS 238 0.60 MET 150 -0.17 ALA 349

LYS 238 0.59 ALA 151 -0.18 ALA 349

LYS 238 0.51 GLU 152 -0.17 ALA 349

LYS 238 0.48 VAL 153 -0.19 ALA 349

LYS 238 0.43 SER 154 -0.25 ALA 349

LYS 238 0.46 HIS 155 -0.28 ALA 349

LYS 238 0.42 ARG 156 -0.30 ALA 349

LYS 238 0.45 MET 157 -0.24 ALA 349

LYS 238 0.50 PRO 158 -0.22 ALA 349

LYS 238 0.45 PHE 159 -0.24 ALA 349

LYS 238 0.41 TYR 160 -0.22 ALA 349

LYS 238 0.43 PHE 161 -0.19 ALA 349

LYS 238 0.44 ALA 162 -0.18 ALA 349

LYS 238 0.39 GLY 163 -0.20 ALA 349

LYS 238 0.37 ALA 164 -0.17 ALA 349

LYS 238 0.36 LEU 165 -0.15 ALA 349

LYS 238 0.35 GLY 166 -0.16 ALA 349

LYS 238 0.32 VAL 167 -0.15 ALA 349

LYS 238 0.30 LEU 168 -0.13 ALA 349

LYS 238 0.29 ALA 169 -0.12 GLY 348

LYS 238 0.28 PHE 170 -0.12 ALA 349

LYS 238 0.25 ILE 171 -0.11 ALA 349

LYS 238 0.24 MET 172 -0.10 GLY 348

LYS 238 0.24 SER 173 -0.10 GLY 348

LYS 238 0.22 ILE 174 -0.09 ALA 349

LYS 238 0.20 VAL 175 -0.09 GLY 348

LYS 238 0.19 LEU 176 -0.08 PHE 149

LYS 238 0.19 ILE 177 -0.07 GLY 348

LYS 238 0.17 HIS 178 -0.07 GLY 348

LYS 238 0.17 ASP 179 -0.06 GLY 66

LYS 238 0.14 PRO 180 -0.06 PHE 149

LYS 238 0.12 LYS 181 -0.07 ASN 2

LYS 238 0.13 LYS 182 -0.05 ASN 2

LYS 238 0.14 VAL 183 -0.04 ASN 2

PRO 237 0.13 LYS 198 -0.09 MET 263

PRO 237 0.15 ILE 199 -0.07 MET 263

PRO 237 0.15 ASN 200 -0.07 SER 267

PRO 237 0.17 TRP 201 -0.07 ILE 375

PRO 237 0.15 LYS 202 -0.09 ILE 375

LEU 383 0.14 VAL 203 -0.09 SER 267

PRO 237 0.16 PHE 204 -0.08 GLY 37

PRO 237 0.16 ILE 205 -0.11 SER 38

PRO 237 0.14 THR 206 -0.15 SER 38

PRO 237 0.15 PRO 207 -0.16 SER 38

PRO 237 0.19 ALA 208 -0.16 SER 38

PRO 237 0.19 ILE 209 -0.21 SER 38

PRO 237 0.16 LEU 210 -0.23 SER 38

PRO 237 0.19 THR 211 -0.23 GLY 41

PRO 237 0.22 LEU 212 -0.27 SER 38

PRO 237 0.19 VAL 213 -0.32 SER 38

PRO 237 0.18 LEU 214 -0.33 SER 38

PRO 237 0.23 ALA 215 -0.35 GLY 41

PRO 237 0.23 PHE 216 -0.42 GLY 41

PRO 237 0.18 GLY 217 -0.44 SER 38

PRO 237 0.19 LEU 218 -0.39 SER 38

PRO 237 0.26 SER 219 -0.42 GLY 41

PRO 237 0.23 ALA 220 -0.52 GLY 37

PRO 237 0.20 PHE 221 -0.46 GLY 37

PRO 237 0.26 GLU 222 -0.39 GLY 37

PRO 237 0.35 THR 223 -0.43 GLY 37

PRO 237 0.26 LEU 224 -0.49 GLY 37

PRO 237 0.22 TYR 225 -0.38 GLY 37

PRO 237 0.33 SER 226 -0.29 GLY 37

PRO 237 0.21 LEU 227 -0.42 GLY 37

PRO 237 0.12 TYR 228 -0.45 GLY 37

GLY 145 0.18 THR 229 -0.33 GLY 37

PHE 341 0.18 ALA 230 -0.29 GLY 37

GLY 145 0.11 ASP 231 -0.38 GLY 37

GLY 145 0.15 LYS 232 -0.37 GLY 37

GLY 145 0.23 VAL 233 -0.27 GLY 37

GLY 145 0.26 ASN 234 -0.21 GLY 37

GLY 145 0.36 TYR 235 -0.14 GLY 37

GLY 148 0.50 SER 236 -0.07 GLY 291

PRO 144 0.57 PRO 237 -0.06 ILE 249

GLY 145 0.81 LYS 238 -0.07 LEU 253

GLY 145 0.65 ASP 239 -0.08 LYS 264

GLY 145 0.52 ILE 240 -0.10 ALA 230

GLY 145 0.76 SER 241 -0.08 GLY 246

GLY 145 0.64 ILE 242 -0.09 LYS 264

ILE 141 0.43 ALA 243 -0.15 GLY 37

ILE 141 0.49 ILE 244 -0.18 SER 226

ILE 141 0.60 THR 245 -0.12 GLY 37

SER 138 0.43 GLY 246 -0.15 GLY 37

SER 138 0.37 GLY 247 -0.21 GLY 37

SER 138 0.46 GLY 248 -0.20 GLY 37

SER 138 0.38 ILE 249 -0.17 GLY 37

SER 138 0.25 PHE 250 -0.19 GLY 37

ILE 135 0.24 GLY 251 -0.22 GLY 37

ILE 135 0.25 ALA 252 -0.20 GLY 37

LEU 6 0.20 LEU 253 -0.18 GLY 37

LEU 6 0.16 PHE 254 -0.20 GLY 37

LEU 6 0.15 GLN 255 -0.19 GLY 37

LEU 6 0.18 ILE 256 -0.17 GLY 37

ASN 2 0.16 TYR 257 -0.17 GLY 37

ASN 2 0.14 PHE 258 -0.18 GLY 37

ASN 2 0.16 PHE 259 -0.16 GLY 37

ASN 2 0.17 ASP 260 -0.16 GLY 37

ASN 2 0.14 LYS 261 -0.18 GLY 37

ASN 2 0.14 PHE 262 -0.16 GLY 37

ASN 2 0.15 MET 263 -0.15 GLY 37

ASN 2 0.14 LYS 264 -0.16 GLY 37

ASN 2 0.12 TYR 265 -0.17 GLY 37

HIS 123 0.12 PHE 266 -0.19 LEU 383

HIS 123 0.13 SER 267 -0.16 GLY 37

HIS 123 0.11 GLU 268 -0.18 GLY 37

SER 122 0.09 LEU 269 -0.19 SER 38

VAL 370 0.10 THR 270 -0.20 SER 38

ASN 2 0.10 PHE 271 -0.21 GLY 37

ASN 2 0.09 ILE 272 -0.23 SER 38

LEU 367 0.11 ALA 273 -0.24 SER 38

ASN 2 0.10 TRP 274 -0.24 SER 38

ASN 2 0.11 SER 275 -0.26 SER 38

ILE 363 0.10 LEU 276 -0.29 SER 38

ILE 363 0.12 LEU 277 -0.28 SER 38

TYR 257 0.15 TYR 278 -0.28 SER 38

ASN 2 0.11 SER 279 -0.31 SER 38

TYR 257 0.10 VAL 280 -0.34 SER 38

TYR 257 0.13 VAL 281 -0.31 SER 38

SER 138 0.14 VAL 282 -0.30 SER 38

SER 138 0.12 LEU 283 -0.35 SER 38

SER 138 0.11 ILE 284 -0.36 SER 38

SER 138 0.15 LEU 285 -0.32 SER 38

GLY 145 0.16 LEU 286 -0.34 GLY 37

GLY 145 0.12 VAL 287 -0.39 SER 38

GLY 145 0.14 PHE 288 -0.36 SER 38

GLY 145 0.19 ALA 289 -0.30 SER 38

GLY 145 0.20 ASN 290 -0.30 GLY 37

GLY 145 0.26 GLY 291 -0.23 GLY 37

GLY 145 0.33 TYR 292 -0.18 GLY 37

GLY 145 0.35 TRP 293 -0.16 GLY 37

GLY 145 0.27 SER 294 -0.21 GLY 37

GLY 145 0.27 ILE 295 -0.24 GLY 37

GLY 145 0.34 MET 296 -0.18 GLY 37

GLY 145 0.31 LEU 297 -0.18 GLY 37

GLY 145 0.22 ILE 298 -0.24 GLY 37

SER 138 0.25 SER 299 -0.24 GLY 37

SER 138 0.30 PHE 300 -0.20 GLY 37

SER 138 0.22 VAL 301 -0.24 GLY 37

SER 138 0.17 VAL 302 -0.29 GLY 37

SER 138 0.18 PHE 303 -0.27 GLY 37

ILE 135 0.16 ILE 304 -0.24 GLY 37

ILE 135 0.11 GLY 305 -0.26 GLY 37

ILE 244 0.10 PHE 306 -0.28 GLY 37

ILE 135 0.14 ASP 307 -0.25 GLY 37

TYR 278 0.11 MET 308 -0.23 GLY 37

PRO 237 0.09 ILE 309 -0.24 GLY 37

SER 241 0.14 ARG 310 -0.22 GLY 37

SER 241 0.11 PRO 311 -0.18 GLY 37

PRO 237 0.08 ALA 312 -0.19 GLY 37

PRO 237 0.13 ILE 313 -0.19 GLY 41

SER 241 0.14 THR 314 -0.16 GLY 41

PRO 237 0.10 ASN 315 -0.14 GLY 41

PRO 237 0.11 TYR 316 -0.14 GLY 37

PRO 237 0.14 PHE 317 -0.12 GLY 41

PRO 237 0.12 SER 318 -0.10 GLY 41

PRO 237 0.10 ASN 319 -0.10 GLY 41

PRO 237 0.11 ILE 320 -0.09 GLY 41

PRO 237 0.13 ALA 321 -0.07 GLY 41

PRO 237 0.11 GLY 322 -0.07 MET 263

LYS 238 0.13 GLU 323 -0.05 MET 263

LYS 238 0.17 ARG 324 -0.04 ASP 179

LYS 238 0.16 GLN 325 -0.06 VAL 44

LYS 238 0.20 GLY 326 -0.05 LYS 67

LYS 238 0.21 PHE 327 -0.05 LYS 67

LYS 238 0.18 ALA 328 -0.07 VAL 44

LYS 238 0.21 GLY 329 -0.09 VAL 44

LYS 238 0.24 GLY 330 -0.07 VAL 44

PRO 237 0.23 LEU 331 -0.09 GLY 41

PRO 237 0.23 ASN 332 -0.14 GLY 41

LYS 238 0.28 SER 333 -0.14 VAL 44

PRO 237 0.29 THR 334 -0.11 VAL 44

PRO 237 0.28 PHE 335 -0.17 GLY 41

PRO 237 0.29 THR 336 -0.22 GLY 41

PRO 237 0.35 SER 337 -0.24 VAL 44

PRO 237 0.32 MET 338 -0.25 ALA 45

PRO 237 0.29 GLY 339 -0.35 GLY 41

PRO 237 0.36 ASN 340 -0.41 VAL 44

PRO 237 0.40 PHE 341 -0.44 GLY 41

PRO 237 0.32 ILE 342 -0.52 GLY 41

PRO 237 0.27 GLY 343 -0.57 GLY 41

PRO 237 0.30 PRO 344 -0.72 GLY 41

PRO 237 0.30 LEU 345 -0.93 GLY 41

PRO 237 0.22 ILE 346 -0.81 SER 38

PRO 237 0.19 ALA 347 -0.75 SER 38

PRO 237 0.19 GLY 348 -0.91 GLY 37

ALA 368 0.15 ALA 349 -1.04 SER 38

ALA 368 0.16 LEU 350 -0.83 SER 38

ALA 368 0.12 PHE 351 -0.76 GLY 37

ALA 368 0.12 ASP 352 -0.84 GLY 37

ALA 368 0.15 VAL 353 -0.75 GLY 37

ALA 368 0.09 HIS 354 -0.64 GLY 37

ALA 368 0.07 ILE 355 -0.58 GLY 37

PRO 237 0.06 GLU 356 -0.53 GLY 37

ALA 368 0.10 ALA 357 -0.61 SER 38

PRO 237 0.14 PRO 358 -0.57 SER 38

PRO 237 0.10 ILE 359 -0.48 SER 38

LEU 277 0.12 TYR 360 -0.50 SER 38

GLY 364 0.15 MET 361 -0.52 SER 38

PRO 237 0.12 ALA 362 -0.44 SER 38

LEU 277 0.12 ILE 363 -0.42 SER 38

MET 361 0.15 GLY 364 -0.43 SER 38

PRO 237 0.13 VAL 365 -0.39 SER 38

VAL 353 0.10 SER 366 -0.35 SER 38

VAL 353 0.13 LEU 367 -0.34 SER 38

LEU 350 0.16 ALA 368 -0.33 SER 38

LEU 350 0.12 GLY 369 -0.29 SER 38

VAL 353 0.11 VAL 370 -0.28 SER 38

LEU 350 0.15 VAL 371 -0.27 SER 38

LEU 350 0.14 ILE 372 -0.23 SER 38

LEU 350 0.11 VAL 373 -0.22 SER 38

LEU 350 0.11 LEU 374 -0.22 SER 38

LEU 350 0.14 ILE 375 -0.19 SER 38

LEU 350 0.12 GLU 376 -0.16 SER 38

LEU 350 0.09 LYS 377 -0.17 SER 38

LEU 350 0.11 GLN 378 -0.16 SER 38

ALA 349 0.13 HIS 379 -0.12 SER 38

ALA 349 0.10 ARG 380 -0.13 PHE 266

ALA 349 0.09 ALA 381 -0.15 PHE 266

ALA 349 0.12 LYS 382 -0.13 PHE 266

VAL 203 0.14 LEU 383 -0.19 PHE 266

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: december 26th, 2025.

Should you encounter any unexpected behaviour, please let us know. elNémo has been hacked on november 27th. It has been moved away and runs again. **Still some additional cleaning from time to time** Sorry for the inconvenience.

*** 7LO8 A3 single ***

CA distance fluctuations for 2603140610172731181

--- normal mode 9 ---

Should you encounter any unexpected behaviour,
please let us know.
elNémo has been hacked on november 27th.
It has been moved away and runs again.
Still some additional cleaning from time to time
Sorry for the inconvenience.

* 7LO8 A3 single *