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 8 ---

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
PRO 296 0.02 SER 1 -0.03 ASN 300

PRO 296 0.03 THR 2 -0.04 GLU 74

PRO 296 0.04 ALA 3 -0.03 ALA 213

PRO 296 0.04 GLY 4 -0.03 ALA 213

PRO 296 0.04 LYS 5 -0.02 ALA 214

ASN 225 0.05 VAL 6 -0.02 ALA 214

ASN 225 0.05 ILE 7 -0.02 ASN 300

ASN 225 0.06 LYS 8 -0.02 ASN 300

ASN 225 0.06 CYS 9 -0.03 ASN 300

ASP 227 0.08 LYS 10 -0.03 ASN 300

ASN 225 0.09 ALA 11 -0.04 ASN 300

ASP 227 0.11 ALA 12 -0.06 GLU 353

ASN 225 0.13 VAL 13 -0.04 GLU 353

ASN 225 0.15 LEU 14 -0.04 GLU 353

ASN 225 0.15 TRP 15 -0.03 GLU 353

ASN 225 0.18 GLU 16 -0.03 GLU 353

ASN 225 0.20 GLU 17 -0.05 PRO 60

ASN 225 0.23 LYS 18 -0.08 SER 298

ASN 225 0.20 LYS 19 -0.07 SER 298

ASP 227 0.19 PRO 20 -0.08 SER 298

ASP 227 0.16 PHE 21 -0.07 GLU 353

ASP 227 0.14 SER 22 -0.04 GLU 353

ASP 227 0.12 ILE 23 -0.03 SER 298

ASP 227 0.10 GLU 24 -0.02 ASN 300

ASN 225 0.08 GLU 25 -0.02 ASN 300

ASN 225 0.08 VAL 26 -0.01 GLY 321

ASN 225 0.07 GLU 27 -0.01 GLY 321

ASN 225 0.07 VAL 28 -0.02 ASN 300

ASN 225 0.06 ALA 29 -0.02 ALA 214

PRO 296 0.05 PRO 30 -0.03 ALA 214

SER 298 0.06 PRO 31 -0.04 ALA 213

SER 298 0.08 LYS 32 -0.04 ALA 214

SER 298 0.08 ALA 33 -0.05 ALA 213

SER 298 0.08 HIS 34 -0.06 ALA 213

SER 298 0.07 GLU 35 -0.05 ALA 213

SER 298 0.05 VAL 36 -0.05 ALA 213

PRO 296 0.04 ARG 37 -0.04 ASN 300

PRO 296 0.03 ILE 38 -0.05 ASN 300

ASN 225 0.03 LYS 39 -0.06 ASN 300

ALA 230 0.03 MET 40 -0.07 ASN 300

ALA 333 0.03 VAL 41 -0.08 ASN 300

LYS 231 0.04 ALA 42 -0.09 ASN 300

LYS 231 0.07 THR 43 -0.09 ASN 300

LYS 231 0.10 GLY 44 -0.11 ASN 300

LYS 231 0.14 ILE 45 -0.13 PRO 295

GLY 202 0.20 CYS 46 -0.17 PRO 295

GLY 201 0.30 ARG 47 -0.26 PRO 295

GLY 201 0.23 SER 48 -0.14 ASN 300

GLY 201 0.19 ASP 49 -0.10 ASN 300

GLY 201 0.23 ASP 50 -0.14 ASP 297

ASN 225 0.23 HIS 51 -0.16 ASP 297

ASN 225 0.19 VAL 52 -0.06 ILE 318

ASN 225 0.22 VAL 53 -0.08 ASP 297

ASN 225 0.25 SER 54 -0.13 ASP 297

ASN 225 0.22 GLY 55 -0.05 ALA 317

ILE 224 0.23 THR 56 -0.06 ALA 317

ASN 225 0.19 LEU 57 -0.07 ALA 317

PRO 296 0.20 VAL 58 -0.06 ILE 318

PRO 296 0.15 THR 59 -0.06 LEU 116

ASN 225 0.13 PRO 60 -0.06 VAL 53

ASN 225 0.15 LEU 61 -0.03 PHE 110

ASN 225 0.14 PRO 62 -0.03 GLY 321

ASN 225 0.13 VAL 63 -0.03 GLU 353

ASN 225 0.12 ILE 64 -0.04 GLU 353

ASN 225 0.12 ALA 65 -0.05 ASN 300

GLY 201 0.11 GLY 66 -0.08 ASN 300

GLY 201 0.09 HIS 67 -0.09 ASN 300

GLY 201 0.07 GLU 68 -0.11 ASN 300

LYS 231 0.04 ALA 69 -0.10 ASN 300

ALA 333 0.02 ALA 70 -0.09 ASN 300

ALA 333 0.02 GLY 71 -0.07 ASN 300

ASP 326 0.02 ILE 72 -0.06 ASN 300

PRO 296 0.03 VAL 73 -0.05 ASN 300

PRO 296 0.03 GLU 74 -0.04 ASN 300

PRO 296 0.04 SER 75 -0.04 ALA 213

SER 298 0.05 ILE 76 -0.05 ALA 213

SER 298 0.06 GLY 77 -0.05 ALA 213

SER 298 0.07 GLU 78 -0.06 ALA 213

SER 298 0.07 GLY 79 -0.07 ALA 213

SER 298 0.06 VAL 80 -0.07 ALA 213

SER 298 0.06 THR 81 -0.08 ALA 213

SER 298 0.05 THR 82 -0.09 ALA 213

SER 298 0.04 VAL 83 -0.07 ALA 213

SER 298 0.03 ARG 84 -0.07 ALA 213

PRO 296 0.03 PRO 85 -0.05 GLY 236

GLY 98 0.02 GLY 86 -0.06 ASN 300

ASP 326 0.02 ASP 87 -0.07 GLY 236

ASP 326 0.02 LYS 88 -0.08 ASN 300

ASP 326 0.02 VAL 89 -0.08 ASN 300

ASN 304 0.02 ILE 90 -0.09 ASN 300

GLN 244 0.04 PRO 91 -0.08 ASN 300

SER 298 0.05 LEU 92 -0.09 ASN 300

GLY 201 0.07 PHE 93 -0.09 ASN 300

VAL 294 0.10 THR 94 -0.10 ASN 300

SER 298 0.10 PRO 95 -0.08 ASN 300

SER 298 0.09 GLN 96 -0.08 ALA 214

SER 298 0.11 CYS 97 -0.08 ALA 214

SER 298 0.09 GLY 98 -0.10 ALA 214

SER 298 0.11 LYS 99 -0.09 ALA 214

SER 298 0.13 CYS 100 -0.08 ALA 214

SER 298 0.14 ARG 101 -0.08 THR 190

SER 298 0.13 VAL 102 -0.08 LYS 185

SER 298 0.10 CYS 103 -0.10 ALA 214

SER 298 0.09 LYS 104 -0.11 ALA 214

SER 298 0.09 HIS 105 -0.11 THR 190

PRO 305 0.07 PRO 106 -0.15 THR 190

PRO 305 0.07 GLU 107 -0.16 LYS 185

ALA 317 0.10 GLY 108 -0.14 ASN 300

SER 298 0.08 ASN 109 -0.14 ASN 300

VAL 294 0.13 PHE 110 -0.12 ASN 300

SER 298 0.13 CYS 111 -0.08 ASN 300

SER 298 0.17 LEU 112 -0.06 SER 117

SER 298 0.16 LYS 113 -0.05 LYS 185

SER 298 0.17 ASN 114 -0.04 LYS 185

SER 298 0.18 ASP 115 -0.04 PRO 60

PRO 296 0.23 LEU 116 -0.06 THR 59

SER 298 0.31 SER 117 -0.07 PHE 110

SER 298 0.28 MET 118 -0.05 LEU 112

PRO 296 0.23 PRO 119 -0.04 PHE 110

PRO 296 0.17 ARG 120 -0.03 LYS 185

PRO 296 0.14 GLY 121 -0.03 GLY 321

PRO 296 0.12 THR 122 -0.03 LYS 185

SER 298 0.11 MET 123 -0.03 LYS 185

SER 298 0.13 GLN 124 -0.04 ALA 214

SER 298 0.12 ASP 125 -0.04 ALA 214

SER 298 0.13 GLY 126 -0.03 LYS 185

SER 298 0.11 THR 127 -0.03 LYS 185

PRO 296 0.09 SER 128 -0.02 LYS 185

ASN 225 0.08 ARG 129 -0.02 LYS 185

ASN 225 0.09 PHE 130 -0.02 GLY 321

ASN 225 0.09 THR 131 -0.02 GLY 321

ASN 225 0.10 CYS 132 -0.01 GLY 321

ASN 225 0.10 ARG 133 -0.01 GLY 321

ASN 225 0.10 GLY 134 -0.02 GLY 321

ASN 225 0.11 LYS 135 -0.02 GLY 321

ASN 225 0.11 PRO 136 -0.02 GLY 321

ASN 225 0.11 ILE 137 -0.02 GLY 321

ASN 225 0.11 HIS 138 -0.03 GLY 321

ASN 225 0.10 HIS 139 -0.03 GLY 321

ASN 225 0.11 PHE 140 -0.03 ASN 300

PRO 296 0.12 LEU 141 -0.05 ASN 300

PRO 296 0.10 GLY 142 -0.04 ASN 300

ASN 225 0.08 THR 143 -0.06 ASN 300

ASN 225 0.09 SER 144 -0.05 ASN 300

GLY 201 0.08 THR 145 -0.06 ASN 300

LYS 228 0.09 PHE 146 -0.06 ASN 300

ASN 225 0.07 SER 147 -0.05 ASN 300

ASN 225 0.05 GLN 148 -0.05 ASN 300

ASN 225 0.05 TYR 149 -0.04 ASN 300

ASN 225 0.06 THR 150 -0.04 ASN 300

PRO 296 0.06 VAL 151 -0.03 ASN 300

SER 298 0.07 VAL 152 -0.04 ASN 300

SER 298 0.09 ASP 153 -0.05 ALA 214

SER 298 0.07 GLU 154 -0.06 ALA 213

SER 298 0.09 ILE 155 -0.07 ALA 213

SER 298 0.07 SER 156 -0.06 ASN 300

SER 298 0.05 VAL 157 -0.07 ASN 300

SER 298 0.03 ALA 158 -0.08 ASN 300

ASP 326 0.03 LYS 159 -0.08 ALA 213

ASP 326 0.03 ILE 160 -0.10 VAL 235

GLU 107 0.02 ASP 161 -0.11 VAL 235

VAL 41 0.03 ALA 162 -0.10 VAL 235

VAL 41 0.03 ALA 163 -0.11 GLU 234

ALA 333 0.05 SER 164 -0.10 VAL 235

MET 336 0.07 PRO 165 -0.09 ASN 300

ALA 333 0.05 LEU 166 -0.09 ASN 300

MET 336 0.05 GLU 167 -0.09 ASN 300

MET 336 0.08 LYS 168 -0.11 ASN 300

MET 336 0.06 VAL 169 -0.11 ASN 300

MET 336 0.05 CYS 170 -0.11 ASN 300

MET 336 0.04 LEU 171 -0.12 ASN 300

PHE 340 0.07 ILE 172 -0.12 ASN 300

PHE 340 0.05 GLY 173 -0.12 ASN 300

PHE 93 0.06 CYS 174 -0.14 ASN 300

SER 48 0.08 GLY 175 -0.14 ASN 300

ARG 47 0.06 PHE 176 -0.14 ASN 300

PHE 340 0.12 SER 177 -0.15 ASN 300

PHE 319 0.08 THR 178 -0.17 ASN 300

SER 48 0.07 GLY 179 -0.16 ASN 300

PHE 340 0.12 TYR 180 -0.15 ASN 300

PHE 340 0.15 GLY 181 -0.18 ASN 300

PHE 340 0.10 SER 182 -0.20 ASN 300

PHE 340 0.12 ALA 183 -0.17 ASN 300

PHE 340 0.19 VAL 184 -0.17 ASN 300

PHE 340 0.17 LYS 185 -0.19 ASN 300

PHE 340 0.12 VAL 186 -0.22 ASN 300

PHE 340 0.11 ALA 187 -0.21 ASN 300

PHE 340 0.15 LYS 188 -0.18 ASN 300

PHE 340 0.12 VAL 189 -0.16 ASN 300

PHE 340 0.11 THR 190 -0.15 PRO 106

ALA 341 0.11 GLN 191 -0.14 PRO 106

ALA 341 0.08 GLY 192 -0.12 PRO 106

ALA 341 0.07 SER 193 -0.11 ASN 300

SER 54 0.07 THR 194 -0.10 ASN 300

SER 54 0.07 CYS 195 -0.12 ASN 300

THR 56 0.09 ALA 196 -0.10 ASN 300

THR 56 0.11 VAL 197 -0.11 ASN 300

THR 56 0.15 PHE 198 -0.08 ASN 300

HIS 51 0.20 GLY 199 -0.11 PRO 344

ARG 47 0.23 LEU 200 -0.14 PRO 344

ARG 47 0.30 GLY 201 -0.16 PRO 344

ARG 47 0.25 GLY 202 -0.14 LEU 345

ARG 47 0.18 VAL 203 -0.14 ASN 300

ARG 47 0.19 GLY 204 -0.11 ASN 300

ARG 47 0.18 LEU 205 -0.14 PHE 340

ARG 47 0.13 SER 206 -0.14 LEU 331

ARG 47 0.10 VAL 207 -0.14 ASN 300

ARG 47 0.11 ILE 208 -0.13 ASP 334

LEU 345 0.16 MET 209 -0.17 ASP 334

ALA 341 0.15 GLY 210 -0.14 LYS 330

ALA 341 0.11 CYS 211 -0.13 ASN 300

PRO 344 0.13 LYS 212 -0.15 ASP 334

ALA 341 0.22 ALA 213 -0.18 LYS 330

PHE 340 0.17 ALA 214 -0.15 PRO 106

ALA 341 0.13 GLY 215 -0.13 PRO 106

ALA 341 0.09 ALA 216 -0.11 PRO 106

GLU 366 0.10 ALA 217 -0.10 PRO 106

GLU 366 0.10 ARG 218 -0.10 ASP 334

GLU 366 0.10 ILE 219 -0.11 ASP 334

SER 54 0.11 ILE 220 -0.10 ASP 334

SER 54 0.14 GLY 221 -0.10 LYS 339

THR 56 0.17 VAL 222 -0.08 LYS 339

SER 54 0.21 ASP 223 -0.11 PRO 344

SER 54 0.24 ILE 224 -0.11 PRO 344

SER 364 0.29 ASN 225 -0.14 PRO 344

GLY 365 0.29 LYS 226 -0.12 PRO 344

GLY 365 0.42 ASP 227 -0.17 PRO 344

GLY 365 0.38 LYS 228 -0.19 PRO 344

GLU 366 0.30 PHE 229 -0.15 PHE 340

GLU 366 0.37 ALA 230 -0.18 PHE 340

GLU 366 0.36 LYS 231 -0.22 PHE 340

GLU 366 0.24 ALA 232 -0.19 PHE 340

GLU 366 0.24 LYS 233 -0.20 PHE 340

GLU 366 0.26 GLU 234 -0.27 PHE 340

GLU 366 0.20 VAL 235 -0.31 PHE 340

GLU 366 0.16 GLY 236 -0.23 LYS 339

GLU 366 0.16 ALA 237 -0.17 LYS 339

GLU 366 0.15 THR 238 -0.16 LYS 339

GLU 366 0.15 GLU 239 -0.13 LYS 339

GLY 365 0.17 CYS 240 -0.12 LYS 339

SER 54 0.16 VAL 241 -0.10 LYS 339

SER 54 0.20 ASN 242 -0.09 LYS 339

THR 56 0.20 PRO 243 -0.07 PRO 344

THR 56 0.22 GLN 244 -0.09 PRO 344

SER 54 0.20 ASP 245 -0.09 LYS 339

THR 56 0.17 TYR 246 -0.08 LYS 339

GLN 299 0.18 LYS 247 -0.06 LYS 339

GLN 299 0.17 LYS 248 -0.05 LYS 339

GLN 299 0.17 PRO 249 -0.05 PRO 344

THR 56 0.15 ILE 250 -0.05 LYS 339

THR 56 0.11 GLN 251 -0.04 ASP 334

THR 56 0.11 GLU 252 -0.05 ASP 334

THR 56 0.12 VAL 253 -0.06 ASP 334

THR 56 0.11 LEU 254 -0.06 ASP 334

THR 56 0.09 THR 255 -0.05 ASP 334

SER 54 0.09 GLU 256 -0.05 ASP 334

SER 54 0.10 MET 257 -0.06 ASP 334

SER 54 0.08 SER 258 -0.06 PRO 106

SER 54 0.07 ASN 259 -0.06 PRO 106

SER 54 0.06 GLY 260 -0.07 ASN 300

SER 54 0.06 GLY 261 -0.09 ASN 300

SER 54 0.06 VAL 262 -0.11 ASN 300

ALA 341 0.06 ASP 263 -0.14 ASN 300

ALA 341 0.05 PHE 264 -0.16 ASN 300

THR 56 0.06 SER 265 -0.16 ASN 300

THR 56 0.08 PHE 266 -0.17 ASN 300

SER 117 0.12 GLU 267 -0.17 ASN 300

THR 56 0.14 VAL 268 -0.15 ASN 300

THR 56 0.20 ILE 269 -0.19 GLU 366

SER 117 0.20 GLY 270 -0.22 GLY 365

GLN 299 0.23 ARG 271 -0.23 GLY 365

GLN 299 0.23 LEU 272 -0.20 GLY 365

GLN 299 0.24 ASP 273 -0.17 GLY 365

GLN 299 0.15 THR 274 -0.14 GLU 366

SER 117 0.14 MET 275 -0.17 ASN 300

SER 117 0.12 VAL 276 -0.12 ASN 300

SER 117 0.12 THR 277 -0.09 GLU 366

SER 117 0.10 ALA 278 -0.12 ASN 300

SER 117 0.08 LEU 279 -0.18 ASN 300

SER 117 0.08 SER 280 -0.10 ASN 300

THR 56 0.07 CYS 281 -0.08 ASN 300

THR 56 0.05 CYS 282 -0.13 ASN 300

ALA 341 0.04 GLN 283 -0.13 ASN 300

ALA 341 0.04 GLU 284 -0.14 ASN 300

PHE 340 0.05 ALA 285 -0.16 ASN 300

PHE 340 0.07 TYR 286 -0.18 ASN 300

PHE 340 0.06 GLY 287 -0.18 ASN 300

PHE 340 0.07 VAL 288 -0.22 ASN 300

PHE 340 0.04 SER 289 -0.24 ASN 300

PHE 340 0.05 VAL 290 -0.26 ASN 300

SER 117 0.10 ILE 291 -0.29 ASN 300

SER 117 0.11 VAL 292 -0.23 ASN 300

SER 117 0.19 GLY 293 -0.22 ASN 300

SER 117 0.26 VAL 294 -0.23 ASN 300

SER 117 0.22 PRO 295 -0.26 ARG 47

SER 117 0.28 PRO 296 -0.18 ARG 47

MET 118 0.23 ASP 297 -0.23 ARG 363

SER 117 0.31 SER 298 -0.27 SER 364

ASP 273 0.24 GLN 299 -0.18 GLY 316

LYS 247 0.12 ASN 300 -0.34 TRP 314

SER 117 0.16 LEU 301 -0.18 GLY 365

SER 117 0.12 SER 302 -0.16 GLY 365

SER 117 0.12 MET 303 -0.13 GLY 365

ARG 101 0.11 ASN 304 -0.11 GLY 365

ARG 101 0.11 PRO 305 -0.22 ASN 300

ARG 101 0.08 MET 306 -0.15 ASN 300

ARG 101 0.07 LEU 307 -0.18 ASN 300

ARG 101 0.06 LEU 308 -0.25 ASN 300

ARG 101 0.05 LEU 309 -0.20 ASN 300

PHE 340 0.05 SER 310 -0.17 ASN 300

PHE 340 0.06 GLY 311 -0.20 ASN 300

PHE 340 0.06 ARG 312 -0.23 ASN 300

PHE 340 0.07 THR 313 -0.28 ASN 300

PHE 340 0.06 TRP 314 -0.34 ASN 300

PHE 340 0.07 LYS 315 -0.34 ASN 300

PHE 110 0.09 GLY 316 -0.33 ASN 300

PHE 110 0.10 ALA 317 -0.26 ASN 300

PHE 110 0.11 ILE 318 -0.21 ASN 300

PHE 340 0.09 PHE 319 -0.17 ASN 300

PHE 340 0.10 GLY 320 -0.19 ASN 300

PHE 340 0.11 GLY 321 -0.19 ASN 300

PHE 340 0.10 PHE 322 -0.16 ASN 300

PHE 340 0.07 LYS 323 -0.12 ASN 300

ILE 318 0.06 SER 324 -0.11 ASN 300

SER 298 0.05 LYS 325 -0.11 ALA 213

PRO 305 0.04 ASP 326 -0.15 ALA 213

PHE 340 0.04 SER 327 -0.16 ALA 213

PHE 340 0.04 VAL 328 -0.11 ASN 300

PRO 305 0.02 PRO 329 -0.13 ALA 213

PHE 322 0.04 LYS 330 -0.18 ALA 213

PHE 322 0.06 LEU 331 -0.17 MET 209

ALA 333 0.04 VAL 332 -0.14 VAL 235

PRO 165 0.06 ALA 333 -0.15 GLY 236

LYS 185 0.08 ASP 334 -0.20 VAL 235

LYS 185 0.09 PHE 335 -0.17 VAL 235

LYS 168 0.08 MET 336 -0.13 GLU 234

LYS 185 0.08 ALA 337 -0.17 GLU 234

LYS 185 0.11 LYS 338 -0.19 GLU 234

LYS 185 0.14 LYS 339 -0.26 VAL 235

ALA 213 0.21 PHE 340 -0.31 VAL 235

ALA 213 0.22 ALA 341 -0.17 LYS 231

ALA 213 0.14 LEU 342 -0.10 LYS 228

ALA 213 0.14 ASP 343 -0.13 ASP 227

ALA 213 0.15 PRO 344 -0.19 LYS 228

MET 209 0.16 LEU 345 -0.14 GLY 202

MET 209 0.11 ILE 346 -0.11 ASN 300

LYS 231 0.18 THR 347 -0.12 ILE 269

LYS 231 0.14 HIS 348 -0.12 SER 298

LYS 231 0.09 VAL 349 -0.10 ASN 300

LYS 231 0.10 LEU 350 -0.10 SER 298

ALA 230 0.08 PRO 351 -0.09 PRO 295

ALA 230 0.08 PHE 352 -0.08 PRO 295

ALA 230 0.09 GLU 353 -0.08 SER 298

ALA 230 0.11 LYS 354 -0.11 SER 298

ALA 230 0.12 ILE 355 -0.11 PRO 295

ASP 227 0.15 ASN 356 -0.14 SER 298

ALA 230 0.16 GLU 357 -0.15 SER 298

LYS 231 0.16 GLY 358 -0.14 SER 298

ASP 227 0.18 PHE 359 -0.17 SER 298

ASP 227 0.22 ASP 360 -0.19 SER 298

ASP 227 0.23 LEU 361 -0.19 SER 298

LYS 228 0.25 LEU 362 -0.21 SER 298

ASP 227 0.29 ARG 363 -0.26 SER 298

ASP 227 0.37 SER 364 -0.27 SER 298

ASP 227 0.42 GLY 365 -0.26 SER 298

LYS 228 0.38 GLU 366 -0.21 SER 298

LYS 231 0.30 SER 367 -0.18 SER 298

LYS 231 0.32 ILE 368 -0.17 ILE 269

LYS 231 0.19 ARG 369 -0.14 PRO 295

LYS 231 0.15 THR 370 -0.13 PRO 295

LYS 231 0.09 ILE 371 -0.11 ASN 300

LYS 231 0.08 LEU 372 -0.09 ASN 300

LYS 231 0.05 THR 373 -0.08 ASN 300

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 8 ---

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 *