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

* okan.logan@stu.khas.edu.tr *

CA distance fluctuations for 2604241234251995880

--- normal mode 13 ---

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
THR 373 0.11 SER 1 -0.14 PRO 106

PRO 351 0.10 THR 2 -0.14 GLY 98

LYS 39 0.11 ALA 3 -0.17 GLY 98

PRO 351 0.07 GLY 4 -0.19 GLY 98

PHE 352 0.07 LYS 5 -0.16 GLY 98

PHE 352 0.08 VAL 6 -0.13 GLY 98

PHE 352 0.10 ILE 7 -0.12 GLY 98

GLU 353 0.10 LYS 8 -0.09 GLY 98

PHE 352 0.13 CYS 9 -0.08 GLU 74

GLU 353 0.15 LYS 10 -0.06 GLU 74

ILE 318 0.09 ALA 11 -0.05 LYS 247

ILE 318 0.12 ALA 12 -0.06 LYS 247

ILE 318 0.10 VAL 13 -0.06 LYS 247

PHE 110 0.12 LEU 14 -0.07 LYS 247

GLY 108 0.11 TRP 15 -0.06 LYS 247

GLY 108 0.13 GLU 16 -0.07 LYS 247

GLY 108 0.17 GLU 17 -0.09 ARG 363

PRO 295 0.18 LYS 18 -0.12 ASN 356

PRO 295 0.16 LYS 19 -0.07 GLU 353

GLY 293 0.19 PRO 20 -0.10 GLU 353

ILE 318 0.15 PHE 21 -0.09 GLU 353

ILE 318 0.12 SER 22 -0.04 PRO 20

ASN 356 0.15 ILE 23 -0.04 GLY 86

ASN 356 0.10 GLU 24 -0.05 GLU 74

GLU 353 0.11 GLU 25 -0.06 CYS 97

GLU 353 0.09 VAL 26 -0.07 CYS 97

PHE 352 0.08 GLU 27 -0.09 GLY 98

PHE 352 0.08 VAL 28 -0.11 GLY 98

PHE 352 0.07 ALA 29 -0.15 GLY 98

THR 127 0.08 PRO 30 -0.17 GLY 98

THR 127 0.12 PRO 31 -0.20 GLY 98

ASP 125 0.20 LYS 32 -0.23 GLY 98

ASP 125 0.27 ALA 33 -0.29 GLY 98

ASP 125 0.22 HIS 34 -0.32 GLY 98

ASP 125 0.17 GLU 35 -0.22 GLY 98

ASP 125 0.10 VAL 36 -0.16 PRO 106

ASP 125 0.08 ARG 37 -0.14 PRO 106

ASP 125 0.06 ILE 38 -0.13 PRO 106

ALA 3 0.11 LYS 39 -0.11 PRO 106

ALA 3 0.08 MET 40 -0.09 ASP 227

SER 1 0.10 VAL 41 -0.10 ASP 227

ILE 318 0.10 ALA 42 -0.11 ASP 227

ILE 318 0.13 THR 43 -0.12 ASP 227

ILE 318 0.16 GLY 44 -0.14 ASP 227

ILE 318 0.18 ILE 45 -0.14 ASP 227

ILE 318 0.22 CYS 46 -0.15 SER 117

GLY 293 0.25 ARG 47 -0.18 ILE 368

ILE 318 0.29 SER 48 -0.16 SER 117

ILE 318 0.20 ASP 49 -0.12 PRO 119

GLY 293 0.21 ASP 50 -0.15 LEU 362

PRO 295 0.26 HIS 51 -0.14 ASN 225

PHE 110 0.22 VAL 52 -0.12 ASN 225

GLY 108 0.19 VAL 53 -0.13 LEU 362

PRO 295 0.25 SER 54 -0.17 ARG 363

GLY 108 0.24 GLY 55 -0.12 ARG 363

GLY 108 0.28 THR 56 -0.14 ASN 225

LEU 116 0.32 LEU 57 -0.14 ASN 225

LEU 116 0.34 VAL 58 -0.12 ASN 225

LEU 116 0.27 THR 59 -0.13 LEU 301

LEU 116 0.15 PRO 60 -0.10 ASN 300

LEU 116 0.13 LEU 61 -0.09 ASN 225

LEU 116 0.10 PRO 62 -0.08 ASN 225

PHE 110 0.10 VAL 63 -0.09 ASN 225

PHE 110 0.10 ILE 64 -0.08 ASN 225

ILE 318 0.14 ALA 65 -0.10 ASN 225

ILE 318 0.15 GLY 66 -0.11 ASN 225

ILE 318 0.16 HIS 67 -0.12 ASN 225

ILE 318 0.16 GLU 68 -0.12 ASP 227

PHE 319 0.13 ALA 69 -0.12 ASP 227

PHE 319 0.10 ALA 70 -0.11 ASP 227

ILE 318 0.07 GLY 71 -0.10 PRO 106

ALA 3 0.07 ILE 72 -0.13 PRO 106

ASP 125 0.07 VAL 73 -0.15 PRO 106

ALA 3 0.08 GLU 74 -0.14 PRO 106

ASP 125 0.09 SER 75 -0.17 PRO 106

ASP 125 0.12 ILE 76 -0.20 PRO 106

ASP 125 0.17 GLY 77 -0.23 GLY 98

ASP 125 0.18 GLU 78 -0.26 GLY 98

ASP 125 0.18 GLY 79 -0.32 GLY 98

ASP 125 0.15 VAL 80 -0.29 GLY 98

ASP 125 0.13 THR 81 -0.30 PRO 106

ASP 125 0.10 THR 82 -0.30 PRO 106

ASP 125 0.09 VAL 83 -0.24 PRO 106

ASP 125 0.09 ARG 84 -0.21 PRO 106

ASP 125 0.08 PRO 85 -0.18 PRO 106

ASP 125 0.06 GLY 86 -0.16 PRO 106

ASP 125 0.07 ASP 87 -0.17 PRO 106

PHE 319 0.05 LYS 88 -0.15 PRO 106

LEU 309 0.06 VAL 89 -0.14 PRO 106

ILE 318 0.08 ILE 90 -0.11 PRO 106

LEU 57 0.08 PRO 91 -0.12 LEU 301

LEU 57 0.12 LEU 92 -0.15 CYS 174

LEU 57 0.16 PHE 93 -0.18 CYS 174

LEU 57 0.21 THR 94 -0.17 LEU 301

LEU 57 0.17 PRO 95 -0.15 LEU 301

LEU 57 0.16 GLN 96 -0.18 PRO 106

ASP 326 0.14 CYS 97 -0.27 HIS 34

ASP 326 0.18 GLY 98 -0.32 HIS 34

LEU 309 0.18 LYS 99 -0.28 GLY 79

SER 117 0.23 CYS 100 -0.18 GLY 79

ASP 297 0.27 ARG 101 -0.17 GLY 79

ASP 297 0.29 VAL 102 -0.16 GLY 79

ASP 297 0.22 CYS 103 -0.23 GLY 79

LEU 309 0.26 LYS 104 -0.27 GLY 79

LEU 309 0.32 HIS 105 -0.23 THR 81

THR 313 0.42 PRO 106 -0.31 ASP 326

LYS 315 0.45 GLU 107 -0.28 ASP 326

ASP 297 0.33 GLY 108 -0.15 GLY 79

LEU 57 0.25 ASN 109 -0.12 GLY 79

LEU 57 0.31 PHE 110 -0.16 LEU 301

LEU 57 0.25 CYS 111 -0.15 LEU 301

SER 117 0.35 LEU 112 -0.17 LYS 113

ILE 155 0.18 LYS 113 -0.22 LEU 301

LEU 112 0.20 ASN 114 -0.22 LEU 301

VAL 58 0.20 ASP 115 -0.22 LEU 301

VAL 58 0.34 LEU 116 -0.26 GLY 293

LEU 112 0.35 SER 117 -0.39 GLY 293

LEU 112 0.19 MET 118 -0.33 LEU 301

LEU 112 0.16 PRO 119 -0.25 LEU 301

ALA 33 0.11 ARG 120 -0.22 LEU 301

ALA 33 0.09 GLY 121 -0.16 LEU 301

ALA 33 0.11 THR 122 -0.16 LEU 301

ALA 33 0.14 MET 123 -0.16 LEU 301

HIS 34 0.14 GLN 124 -0.19 CYS 97

ALA 33 0.27 ASP 125 -0.19 LEU 301

ALA 33 0.19 GLY 126 -0.19 LEU 301

LYS 32 0.18 THR 127 -0.16 LEU 301

LYS 32 0.12 SER 128 -0.13 LEU 301

LYS 32 0.08 ARG 129 -0.12 CYS 97

PHE 352 0.06 PHE 130 -0.09 CYS 97

GLU 353 0.05 THR 131 -0.08 CYS 97

GLU 353 0.06 CYS 132 -0.06 CYS 97

GLU 353 0.06 ARG 133 -0.07 LYS 99

GLU 353 0.05 GLY 134 -0.08 LYS 99

LYS 32 0.04 LYS 135 -0.06 ASN 300

LYS 32 0.06 PRO 136 -0.08 LEU 301

LYS 32 0.06 ILE 137 -0.08 LEU 301

ALA 33 0.07 HIS 138 -0.10 LEU 301

ALA 33 0.07 HIS 139 -0.12 LEU 301

PHE 110 0.11 PHE 140 -0.13 LEU 301

LEU 57 0.15 LEU 141 -0.16 LEU 301

LEU 57 0.11 GLY 142 -0.15 LEU 301

LEU 57 0.09 THR 143 -0.12 LEU 301

PHE 110 0.08 SER 144 -0.10 LEU 301

ILE 318 0.11 THR 145 -0.09 ASP 227

ILE 318 0.12 PHE 146 -0.08 ASP 227

ILE 318 0.09 SER 147 -0.07 ASP 227

PHE 352 0.09 GLN 148 -0.07 ASP 227

ALA 3 0.07 TYR 149 -0.08 PRO 106

LEU 309 0.05 THR 150 -0.09 LEU 301

ASP 125 0.07 VAL 151 -0.11 GLY 98

LEU 57 0.07 VAL 152 -0.13 CYS 97

LEU 57 0.09 ASP 153 -0.19 CYS 97

LYS 113 0.11 GLU 154 -0.18 PRO 106

LYS 113 0.18 ILE 155 -0.20 PRO 106

LEU 57 0.12 SER 156 -0.14 LEU 301

LEU 57 0.10 VAL 157 -0.16 PRO 106

LEU 57 0.08 ALA 158 -0.19 PRO 106

LEU 57 0.07 LYS 159 -0.21 PRO 106

LEU 309 0.06 ILE 160 -0.17 PRO 106

THR 313 0.05 ASP 161 -0.16 PRO 106

THR 313 0.05 ALA 162 -0.15 PRO 106

PHE 319 0.06 ALA 163 -0.12 PRO 106

PHE 319 0.07 SER 164 -0.13 ASP 227

SER 1 0.09 PRO 165 -0.15 ASP 227

SER 1 0.08 LEU 166 -0.13 ASP 227

PHE 319 0.09 GLU 167 -0.15 ASP 227

PHE 319 0.09 LYS 168 -0.17 ASP 227

PHE 319 0.10 VAL 169 -0.16 LYS 228

PHE 319 0.11 CYS 170 -0.15 ASP 227

PHE 319 0.12 LEU 171 -0.16 LYS 228

PHE 319 0.15 ILE 172 -0.13 LYS 228

PHE 319 0.21 GLY 173 -0.13 LEU 116

PHE 319 0.18 CYS 174 -0.21 LEU 116

ARG 369 0.25 GLY 175 -0.24 SER 117

LEU 345 0.24 PHE 176 -0.19 SER 117

PHE 340 0.19 SER 177 -0.20 SER 117

ARG 363 0.17 THR 178 -0.25 SER 117

LEU 345 0.18 GLY 179 -0.22 SER 117

PRO 344 0.19 TYR 180 -0.18 SER 117

PHE 340 0.21 GLY 181 -0.17 LEU 301

ARG 363 0.16 SER 182 -0.19 LEU 301

PHE 340 0.15 ALA 183 -0.15 LEU 301

PHE 340 0.22 VAL 184 -0.14 LEU 301

PHE 340 0.20 LYS 185 -0.17 LEU 301

GLU 107 0.21 VAL 186 -0.19 LEU 301

PRO 106 0.20 ALA 187 -0.17 LEU 301

PHE 340 0.16 LYS 188 -0.15 LEU 301

PHE 340 0.12 VAL 189 -0.12 LEU 301

LYS 339 0.10 THR 190 -0.10 LEU 301

ARG 363 0.09 GLN 191 -0.09 SER 117

ARG 363 0.08 GLY 192 -0.09 SER 117

ARG 363 0.09 SER 193 -0.10 SER 117

SER 364 0.09 THR 194 -0.12 SER 117

SER 364 0.11 CYS 195 -0.14 SER 117

PRO 243 0.12 ALA 196 -0.16 SER 117

SER 364 0.15 VAL 197 -0.18 SER 117

SER 364 0.16 PHE 198 -0.20 SER 117

SER 364 0.20 GLY 199 -0.21 SER 117

GLY 365 0.18 LEU 200 -0.20 SER 117

GLY 365 0.23 GLY 201 -0.21 SER 117

ILE 368 0.18 GLY 202 -0.21 SER 117

ARG 363 0.19 VAL 203 -0.22 SER 117

SER 364 0.17 GLY 204 -0.20 SER 117

GLY 365 0.16 LEU 205 -0.18 SER 117

PRO 344 0.22 SER 206 -0.18 SER 117

PRO 344 0.14 VAL 207 -0.18 SER 117

PRO 344 0.13 ILE 208 -0.16 SER 117

PRO 344 0.22 MET 209 -0.19 LEU 331

PRO 344 0.18 GLY 210 -0.15 SER 117

PRO 344 0.13 CYS 211 -0.14 SER 117

PRO 344 0.14 LYS 212 -0.14 LYS 330

PRO 344 0.17 ALA 213 -0.17 LYS 330

PHE 340 0.16 ALA 214 -0.11 SER 117

PRO 344 0.11 GLY 215 -0.11 SER 117

ARG 363 0.10 ALA 216 -0.11 SER 117

SER 364 0.08 ALA 217 -0.11 SER 117

SER 364 0.09 ARG 218 -0.18 SER 258

SER 364 0.10 ILE 219 -0.20 MET 257

SER 364 0.10 ILE 220 -0.30 MET 257

SER 364 0.12 GLY 221 -0.26 LEU 254

SER 364 0.11 VAL 222 -0.25 LEU 254

SER 364 0.10 ASP 223 -0.20 VAL 253

ASP 273 0.08 ILE 224 -0.20 ASP 297

CYS 240 0.09 ASN 225 -0.24 ILE 368

CYS 240 0.15 LYS 226 -0.21 LEU 345

CYS 240 0.09 ASP 227 -0.29 LEU 345

GLY 365 0.10 LYS 228 -0.31 LEU 345

GLY 365 0.08 PHE 229 -0.22 VAL 253

GLY 365 0.10 ALA 230 -0.22 MET 257

GLU 366 0.15 LYS 231 -0.23 ALA 341

GLY 365 0.12 ALA 232 -0.19 MET 257

GLY 365 0.09 LYS 233 -0.21 PHE 340

GLU 366 0.09 GLU 234 -0.29 PHE 340

ILE 368 0.10 VAL 235 -0.32 PHE 340

GLY 365 0.09 GLY 236 -0.22 PHE 340

SER 364 0.10 ALA 237 -0.21 MET 257

SER 364 0.08 THR 238 -0.25 MET 257

LYS 226 0.10 GLU 239 -0.35 MET 257

LYS 226 0.15 CYS 240 -0.33 MET 257

LYS 226 0.09 VAL 241 -0.36 VAL 253

ASP 273 0.08 ASN 242 -0.23 VAL 253

ALA 196 0.12 PRO 243 -0.15 VAL 253

LEU 301 0.16 GLN 244 -0.17 LYS 226

SER 302 0.13 ASP 245 -0.15 LEU 345

SER 302 0.14 TYR 246 -0.12 SER 117

SER 302 0.10 LYS 247 -0.17 ASP 297

SER 302 0.14 LYS 248 -0.14 SER 117

SER 302 0.16 PRO 249 -0.14 SER 117

PRO 106 0.12 ILE 250 -0.19 VAL 241

PRO 106 0.15 GLN 251 -0.16 VAL 241

SER 302 0.15 GLU 252 -0.21 VAL 241

PRO 106 0.11 VAL 253 -0.36 VAL 241

PRO 106 0.11 LEU 254 -0.29 VAL 241

PRO 106 0.15 THR 255 -0.21 CYS 240

PRO 106 0.13 GLU 256 -0.27 CYS 240

PRO 106 0.09 MET 257 -0.35 GLU 239

PRO 106 0.12 SER 258 -0.26 ILE 220

PRO 106 0.15 ASN 259 -0.22 GLU 239

PRO 106 0.19 GLY 260 -0.16 GLU 239

PRO 106 0.18 GLY 261 -0.15 ILE 220

PRO 106 0.16 VAL 262 -0.13 ILE 220

PRO 106 0.18 ASP 263 -0.09 SER 117

PRO 106 0.17 PHE 264 -0.12 SER 117

GLU 107 0.15 SER 265 -0.15 SER 117

SER 364 0.16 PHE 266 -0.19 SER 117

SER 364 0.19 GLU 267 -0.22 SER 117

ARG 363 0.22 VAL 268 -0.26 SER 117

SER 364 0.27 ILE 269 -0.25 SER 117

ARG 363 0.27 GLY 270 -0.28 SER 117

SER 364 0.22 ARG 271 -0.24 SER 117

GLU 107 0.18 LEU 272 -0.20 SER 117

SER 364 0.17 ASP 273 -0.19 SER 117

GLU 107 0.16 THR 274 -0.19 SER 117

GLU 107 0.19 MET 275 -0.19 SER 117

GLU 107 0.20 VAL 276 -0.15 SER 117

GLU 107 0.18 THR 277 -0.15 SER 117

GLU 107 0.18 ALA 278 -0.16 SER 117

GLU 107 0.25 LEU 279 -0.10 SER 117

GLU 107 0.23 SER 280 -0.09 SER 117

PRO 106 0.18 CYS 281 -0.12 SER 117

PRO 106 0.22 CYS 282 -0.09 SER 117

PRO 106 0.24 GLN 283 -0.09 ILE 220

PRO 106 0.29 GLU 284 -0.07 CYS 240

PRO 106 0.32 ALA 285 -0.07 LEU 301

PRO 106 0.33 TYR 286 -0.10 LEU 301

PRO 106 0.28 GLY 287 -0.11 LEU 301

GLU 107 0.29 VAL 288 -0.16 LEU 301

GLU 107 0.26 SER 289 -0.18 LEU 301

GLU 107 0.25 VAL 290 -0.24 LEU 301

GLU 107 0.23 ILE 291 -0.31 LEU 301

ARG 363 0.23 VAL 292 -0.29 SER 117

ARG 363 0.30 GLY 293 -0.39 SER 117

GLU 107 0.21 VAL 294 -0.35 SER 117

HIS 51 0.26 PRO 295 -0.23 GLY 270

GLY 108 0.33 PRO 296 -0.16 ASN 225

GLY 108 0.33 ASP 297 -0.21 ASN 225

GLU 107 0.29 SER 298 -0.21 ARG 271

GLU 107 0.25 GLN 299 -0.20 MET 118

PRO 305 0.25 ASN 300 -0.27 MET 118

GLN 244 0.16 LEU 301 -0.35 SER 117

PRO 249 0.16 SER 302 -0.27 SER 117

ASN 300 0.22 MET 303 -0.15 MET 118

PRO 106 0.26 ASN 304 -0.14 ASP 273

PRO 106 0.33 PRO 305 -0.08 ASP 273

PRO 106 0.32 MET 306 -0.08 ASP 273

PRO 106 0.32 LEU 307 -0.10 VAL 276

PRO 106 0.38 LEU 308 -0.12 LEU 301

PRO 106 0.39 LEU 309 -0.07 LEU 301

PRO 106 0.35 SER 310 -0.07 VAL 276

PRO 106 0.39 GLY 311 -0.11 LEU 301

PRO 106 0.37 ARG 312 -0.14 LEU 301

GLU 107 0.43 THR 313 -0.21 LEU 301

GLU 107 0.41 TRP 314 -0.28 LEU 301

GLU 107 0.45 LYS 315 -0.29 LEU 301

GLU 107 0.33 GLY 316 -0.30 LEU 301

PRO 296 0.26 ALA 317 -0.24 LEU 301

SER 48 0.29 ILE 318 -0.28 SER 117

GLY 173 0.21 PHE 319 -0.25 SER 117

ARG 363 0.17 GLY 320 -0.19 LEU 301

LEU 57 0.18 GLY 321 -0.16 LEU 301

LEU 57 0.15 PHE 322 -0.15 GLU 107

GLY 98 0.17 LYS 323 -0.25 GLU 107

LEU 57 0.14 SER 324 -0.16 PRO 106

CYS 97 0.13 LYS 325 -0.24 PRO 106

GLY 98 0.18 ASP 326 -0.31 PRO 106

GLY 98 0.15 SER 327 -0.21 GLU 107

GLY 98 0.09 VAL 328 -0.15 PRO 106

GLY 98 0.08 PRO 329 -0.19 PRO 106

GLY 98 0.11 LYS 330 -0.17 ALA 213

LYS 185 0.11 LEU 331 -0.19 MET 209

PHE 319 0.09 VAL 332 -0.16 VAL 235

GLY 98 0.08 ALA 333 -0.17 VAL 235

LYS 185 0.13 ASP 334 -0.21 VAL 235

LYS 185 0.13 PHE 335 -0.20 VAL 235

LYS 185 0.10 MET 336 -0.16 GLU 234

LYS 185 0.12 ALA 337 -0.17 GLU 234

VAL 184 0.15 LYS 338 -0.19 GLU 234

VAL 184 0.19 LYS 339 -0.24 GLU 234

VAL 184 0.22 PHE 340 -0.32 VAL 235

ALA 213 0.16 ALA 341 -0.25 GLU 234

SER 177 0.16 LEU 342 -0.22 LYS 228

PHE 176 0.15 ASP 343 -0.21 ASP 227

SER 206 0.22 PRO 344 -0.26 ASP 227

PHE 176 0.24 LEU 345 -0.31 LYS 228

GLY 175 0.18 ILE 346 -0.24 ASP 227

GLY 175 0.16 THR 347 -0.24 ASP 227

GLY 175 0.14 HIS 348 -0.17 ASP 227

GLY 175 0.12 VAL 349 -0.13 ASP 227

ILE 318 0.11 LEU 350 -0.10 ASP 227

CYS 9 0.12 PRO 351 -0.09 ASP 227

LYS 10 0.14 PHE 352 -0.08 ASP 227

LYS 10 0.15 GLU 353 -0.10 PRO 20

GLY 293 0.13 LYS 354 -0.09 LYS 18

ILE 318 0.15 ILE 355 -0.10 LYS 18

GLY 293 0.16 ASN 356 -0.12 LYS 18

GLY 293 0.16 GLU 357 -0.08 SER 54

GLY 293 0.17 GLY 358 -0.09 SER 54

GLY 293 0.21 PHE 359 -0.13 SER 54

GLY 293 0.21 ASP 360 -0.11 SER 54

GLY 293 0.20 LEU 361 -0.12 HIS 348

GLY 293 0.25 LEU 362 -0.15 SER 54

GLY 293 0.30 ARG 363 -0.17 SER 54

ILE 269 0.27 SER 364 -0.13 ASP 297

GLY 201 0.23 GLY 365 -0.17 ASP 297

GLY 201 0.20 GLU 366 -0.20 ASN 225

GLY 202 0.16 SER 367 -0.20 ASP 227

GLY 202 0.18 ILE 368 -0.24 ASN 225

GLY 175 0.25 ARG 369 -0.20 ASP 227

GLY 175 0.18 THR 370 -0.16 ASP 227

GLY 175 0.15 ILE 371 -0.14 ASP 227

ILE 318 0.12 LEU 372 -0.11 ASP 227

SER 1 0.11 THR 373 -0.11 ASP 227

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.

*** okan.logan@stu.khas.edu.tr ***

CA distance fluctuations for 2604241234251995880

--- normal mode 13 ---

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

* okan.logan@stu.khas.edu.tr *