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 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
LYS 185 0.06 SER 1 -0.07 ASP 227

SER 75 0.11 THR 2 -0.07 ASP 227

LYS 185 0.05 ALA 3 -0.07 ASP 227

LYS 185 0.05 GLY 4 -0.07 ASP 227

LYS 185 0.04 LYS 5 -0.07 ASN 225

LYS 185 0.04 VAL 6 -0.07 ASN 225

LYS 185 0.04 ILE 7 -0.08 ASN 225

ALA 213 0.03 LYS 8 -0.09 ASN 225

ALA 213 0.03 CYS 9 -0.10 ASN 225

ALA 213 0.02 LYS 10 -0.12 ASN 225

ALA 213 0.02 ALA 11 -0.12 ASN 225

PRO 60 0.01 ALA 12 -0.13 ASN 225

PRO 60 0.01 VAL 13 -0.12 ARG 271

PRO 60 0.03 LEU 14 -0.14 ARG 271

ARG 363 0.02 TRP 15 -0.13 ARG 271

ARG 363 0.03 GLU 16 -0.15 ARG 271

PRO 60 0.05 GLU 17 -0.17 ARG 271

ARG 363 0.05 LYS 18 -0.20 ARG 271

ARG 363 0.04 LYS 19 -0.17 ARG 271

PRO 60 0.03 PRO 20 -0.17 ARG 271

PRO 60 0.02 PHE 21 -0.16 ARG 271

PRO 60 0.01 SER 22 -0.14 ASN 225

ALA 213 0.01 ILE 23 -0.14 ASN 225

ALA 213 0.02 GLU 24 -0.12 ASN 225

ALA 213 0.02 GLU 25 -0.11 ASN 225

ALA 213 0.02 VAL 26 -0.10 ASN 225

ALA 213 0.02 GLU 27 -0.09 ASN 225

LYS 185 0.03 VAL 28 -0.08 ASN 225

ASN 304 0.03 ALA 29 -0.07 ASN 225

THR 2 0.05 PRO 30 -0.06 ASN 225

ASN 304 0.06 PRO 31 -0.06 ASP 227

ASN 304 0.07 LYS 32 -0.05 GLN 299

ASN 304 0.08 ALA 33 -0.05 GLN 299

ASN 304 0.09 HIS 34 -0.05 GLN 299

ASN 304 0.08 GLU 35 -0.05 ASP 227

ASN 304 0.07 VAL 36 -0.06 ASP 227

THR 2 0.07 ARG 37 -0.07 ASP 227

LYS 185 0.06 ILE 38 -0.07 ASP 227

LYS 185 0.05 LYS 39 -0.09 ASP 227

LYS 185 0.05 MET 40 -0.10 ASP 227

ALA 213 0.05 VAL 41 -0.11 ASP 227

ALA 213 0.05 ALA 42 -0.12 ASP 227

PRO 296 0.05 THR 43 -0.12 ASN 225

PRO 296 0.08 GLY 44 -0.14 ASN 225

PRO 296 0.09 ILE 45 -0.16 ILE 269

PRO 296 0.13 CYS 46 -0.20 ILE 269

PRO 296 0.18 ARG 47 -0.27 ILE 269

PRO 296 0.17 SER 48 -0.20 GLY 270

PRO 296 0.08 ASP 49 -0.18 ILE 269

PRO 296 0.07 ASP 50 -0.24 GLY 270

PRO 296 0.07 HIS 51 -0.25 GLY 270

THR 59 0.06 VAL 52 -0.18 PRO 295

PRO 60 0.07 VAL 53 -0.20 ARG 271

ILE 368 0.05 SER 54 -0.23 ARG 271

ILE 368 0.05 GLY 55 -0.19 PRO 295

ILE 368 0.07 THR 56 -0.28 PRO 295

ILE 368 0.05 LEU 57 -0.24 PRO 295

ILE 368 0.05 VAL 58 -0.19 PRO 295

VAL 52 0.06 THR 59 -0.13 PRO 295

VAL 53 0.07 PRO 60 -0.11 ASP 297

ILE 368 0.03 LEU 61 -0.13 PRO 295

ILE 368 0.02 PRO 62 -0.11 ARG 271

ILE 368 0.02 VAL 63 -0.11 ARG 271

ILE 368 0.02 ILE 64 -0.11 ILE 269

PRO 60 0.04 ALA 65 -0.13 ILE 269

PRO 60 0.03 GLY 66 -0.12 ILE 269

PRO 296 0.04 HIS 67 -0.10 ILE 269

PRO 296 0.06 GLU 68 -0.09 ILE 269

LYS 185 0.05 ALA 69 -0.09 ASP 227

LYS 185 0.07 ALA 70 -0.09 ASP 227

LYS 185 0.07 GLY 71 -0.09 ASP 227

LYS 185 0.07 ILE 72 -0.08 ASP 227

THR 2 0.07 VAL 73 -0.07 ASP 227

THR 2 0.11 GLU 74 -0.07 ASP 227

THR 2 0.11 SER 75 -0.06 ASP 227

THR 2 0.07 ILE 76 -0.05 ASP 227

ASN 304 0.07 GLY 77 -0.05 ASP 227

ASN 304 0.08 GLU 78 -0.04 ASP 227

ASN 304 0.10 GLY 79 -0.04 GLN 299

ASN 304 0.09 VAL 80 -0.04 ASN 300

ASN 304 0.10 THR 81 -0.04 ASN 300

LYS 185 0.10 THR 82 -0.05 ASN 300

LYS 185 0.09 VAL 83 -0.05 ASP 227

LYS 185 0.08 ARG 84 -0.05 ASP 227

THR 2 0.08 PRO 85 -0.06 ASP 227

LYS 185 0.07 GLY 86 -0.07 ASP 227

LYS 185 0.09 ASP 87 -0.06 ASP 227

LYS 185 0.09 LYS 88 -0.07 ASP 227

LYS 185 0.09 VAL 89 -0.06 ASP 227

LYS 185 0.08 ILE 90 -0.06 ASP 227

ASN 304 0.07 PRO 91 -0.06 ASP 227

ASN 304 0.08 LEU 92 -0.06 ASN 300

MET 303 0.08 PHE 93 -0.07 ASN 300

MET 303 0.11 THR 94 -0.08 ASN 300

ASN 304 0.12 PRO 95 -0.08 ASN 300

ASN 304 0.13 GLN 96 -0.07 ASN 300

ASN 304 0.14 CYS 97 -0.06 ASN 300

ASN 304 0.16 GLY 98 -0.07 ASP 326

ASN 304 0.17 LYS 99 -0.06 ASN 300

ASN 304 0.18 CYS 100 -0.07 GLN 299

ASN 304 0.22 ARG 101 -0.07 GLN 299

ASN 304 0.21 VAL 102 -0.08 ASN 300

ASN 304 0.18 CYS 103 -0.08 ASN 300

ASN 304 0.20 LYS 104 -0.07 ASN 300

ASN 304 0.23 HIS 105 -0.08 ASN 300

THR 313 0.24 PRO 106 -0.09 ASN 300

THR 313 0.26 GLU 107 -0.10 ASN 300

ASN 304 0.22 GLY 108 -0.11 ASN 300

MET 303 0.17 ASN 109 -0.11 ASN 300

MET 303 0.17 PHE 110 -0.11 ASN 300

MET 303 0.16 CYS 111 -0.09 ASN 300

MET 303 0.17 LEU 112 -0.08 GLN 299

ASN 304 0.14 LYS 113 -0.07 GLN 299

LEU 301 0.12 ASN 114 -0.08 GLN 299

LEU 301 0.09 ASP 115 -0.08 GLN 299

LEU 301 0.10 LEU 116 -0.09 GLN 299

LEU 301 0.13 SER 117 -0.12 GLN 299

LEU 301 0.10 MET 118 -0.14 ASP 297

LEU 301 0.06 PRO 119 -0.13 ASP 297

ASN 304 0.06 ARG 120 -0.11 ASP 297

ASN 304 0.04 GLY 121 -0.10 PRO 295

ASN 304 0.05 THR 122 -0.08 ASP 297

ASN 304 0.07 MET 123 -0.06 ASP 297

ASN 304 0.09 GLN 124 -0.06 GLN 299

ASN 304 0.08 ASP 125 -0.06 ASP 297

ASN 304 0.07 GLY 126 -0.08 ASP 297

ASN 304 0.05 THR 127 -0.07 ASP 297

ASN 304 0.04 SER 128 -0.07 PRO 295

ASN 304 0.04 ARG 129 -0.07 ASN 225

LYS 185 0.02 PHE 130 -0.08 ASN 225

ALA 213 0.02 THR 131 -0.08 ASN 225

ALA 213 0.01 CYS 132 -0.09 ASN 225

GLU 27 0.02 ARG 133 -0.09 ASN 225

ALA 29 0.02 GLY 134 -0.08 ASN 225

CYS 97 0.01 LYS 135 -0.09 ARG 271

CYS 97 0.02 PRO 136 -0.08 PRO 295

ILE 368 0.01 ILE 137 -0.09 PRO 295

ILE 368 0.02 HIS 138 -0.10 PRO 295

ASN 304 0.03 HIS 139 -0.09 PRO 295

PRO 60 0.04 PHE 140 -0.10 PRO 295

ASN 304 0.06 LEU 141 -0.08 PRO 295

ASN 304 0.06 GLY 142 -0.06 PRO 295

ASN 304 0.05 THR 143 -0.07 ILE 269

ASN 304 0.02 SER 144 -0.09 ILE 269

LYS 185 0.03 THR 145 -0.10 ASN 225

PRO 60 0.02 PHE 146 -0.12 ASN 225

ALA 213 0.03 SER 147 -0.11 ASN 225

ALA 213 0.04 GLN 148 -0.10 ASN 225

LYS 185 0.04 TYR 149 -0.09 ASN 225

LYS 185 0.04 THR 150 -0.08 ASN 225

ASN 304 0.05 VAL 151 -0.07 ASN 225

ASN 304 0.07 VAL 152 -0.06 ASP 227

ASN 304 0.08 ASP 153 -0.05 ASN 300

ASN 304 0.09 GLU 154 -0.05 ASN 300

ASN 304 0.11 ILE 155 -0.06 ASN 300

ASN 304 0.09 SER 156 -0.06 ASN 300

ASN 304 0.08 VAL 157 -0.06 ASN 300

LYS 185 0.10 ALA 158 -0.06 ASN 300

LYS 185 0.11 LYS 159 -0.05 ASN 300

LYS 185 0.12 ILE 160 -0.05 ASP 227

LYS 185 0.12 ASP 161 -0.05 ASP 227

ALA 214 0.10 ALA 162 -0.06 ASP 227

ALA 214 0.10 ALA 163 -0.07 ASP 227

ALA 213 0.10 SER 164 -0.07 ASP 227

ALA 213 0.09 PRO 165 -0.09 ASP 227

ALA 213 0.08 LEU 166 -0.09 ASP 227

ALA 213 0.07 GLU 167 -0.12 ASP 227

ALA 213 0.08 LYS 168 -0.11 ASP 227

ALA 213 0.09 VAL 169 -0.08 ASP 227

ALA 213 0.06 CYS 170 -0.09 ASP 227

PRO 296 0.07 LEU 171 -0.09 LYS 228

SER 177 0.08 ILE 172 -0.06 ASP 227

LEU 301 0.07 GLY 173 -0.06 SER 324

PRO 296 0.08 CYS 174 -0.07 SER 324

PRO 296 0.10 GLY 175 -0.09 VAL 203

PRO 296 0.08 PHE 176 -0.06 SER 324

ILE 172 0.08 SER 177 -0.09 ASN 300

LEU 301 0.09 THR 178 -0.10 ASN 300

LEU 301 0.07 GLY 179 -0.10 ASN 300

LEU 331 0.11 TYR 180 -0.10 ASN 300

LEU 331 0.17 GLY 181 -0.13 ASN 300

LEU 331 0.12 SER 182 -0.16 ASN 300

LEU 331 0.14 ALA 183 -0.15 ASN 300

LEU 331 0.19 VAL 184 -0.15 ASN 300

LYS 330 0.21 LYS 185 -0.18 ASN 300

LYS 330 0.15 VAL 186 -0.22 ASN 300

LYS 330 0.14 ALA 187 -0.22 ASN 300

LYS 330 0.17 LYS 188 -0.19 ASN 300

ASP 334 0.15 VAL 189 -0.17 ASN 300

ASP 334 0.16 THR 190 -0.16 ASN 300

ASP 334 0.16 GLN 191 -0.14 ASN 300

ASP 334 0.13 GLY 192 -0.13 ASN 300

ASP 334 0.12 SER 193 -0.14 ASN 300

ASP 334 0.10 THR 194 -0.13 ASN 300

ASP 334 0.09 CYS 195 -0.14 ASN 300

ASP 334 0.07 ALA 196 -0.16 SER 364

ASP 334 0.07 VAL 197 -0.17 SER 364

GLU 107 0.07 PHE 198 -0.22 SER 364

ASP 297 0.10 GLY 199 -0.26 GLY 365

ASP 297 0.11 LEU 200 -0.24 GLY 365

ASP 297 0.14 GLY 201 -0.22 LEU 362

ASP 297 0.13 GLY 202 -0.13 ARG 369

PRO 295 0.12 VAL 203 -0.11 CYS 46

PRO 295 0.10 GLY 204 -0.13 ARG 363

ASP 297 0.09 LEU 205 -0.10 LEU 362

PRO 344 0.08 SER 206 -0.07 ASN 300

ASP 334 0.08 VAL 207 -0.10 ASN 300

ASP 334 0.08 ILE 208 -0.09 ARG 363

ASP 334 0.08 MET 209 -0.07 ASN 300

ASP 334 0.15 GLY 210 -0.11 ASN 300

ASP 334 0.14 CYS 211 -0.12 ASN 300

LYS 339 0.14 LYS 212 -0.09 ASN 300

LYS 339 0.23 ALA 213 -0.10 ASN 300

ASP 334 0.21 ALA 214 -0.13 ASN 300

ASP 334 0.17 GLY 215 -0.12 ASN 300

ASP 334 0.13 ALA 216 -0.12 ASN 300

ASP 334 0.11 ALA 217 -0.11 ASN 300

ASP 334 0.09 ARG 218 -0.11 GLY 365

ASP 334 0.08 ILE 219 -0.13 GLY 365

ASP 334 0.06 ILE 220 -0.16 GLY 365

ASP 297 0.06 GLY 221 -0.19 GLY 365

GLN 299 0.08 VAL 222 -0.25 GLY 365

GLN 299 0.12 ASP 223 -0.34 GLY 365

GLN 299 0.16 ILE 224 -0.40 GLY 365

GLN 299 0.16 ASN 225 -0.45 GLU 366

GLN 299 0.13 LYS 226 -0.35 GLU 366

GLN 299 0.13 ASP 227 -0.40 GLU 366

ASP 297 0.13 LYS 228 -0.36 GLU 366

ASP 297 0.10 PHE 229 -0.23 GLU 366

ASP 297 0.10 ALA 230 -0.14 ILE 368

ASP 297 0.11 LYS 231 -0.14 ILE 368

ASP 297 0.09 ALA 232 -0.14 ILE 368

ASP 297 0.07 LYS 233 -0.11 ILE 368

ASP 297 0.08 GLU 234 -0.08 ILE 368

ASP 297 0.07 VAL 235 -0.07 ILE 368

LYS 339 0.06 GLY 236 -0.08 GLY 365

ASP 334 0.06 ALA 237 -0.12 GLY 365

LYS 339 0.06 THR 238 -0.12 GLY 365

ASP 334 0.05 GLU 239 -0.15 GLY 365

ASP 297 0.06 CYS 240 -0.19 GLY 365

GLN 299 0.07 VAL 241 -0.23 GLY 365

GLN 299 0.11 ASN 242 -0.29 GLY 365

GLN 299 0.11 PRO 243 -0.29 SER 364

GLN 299 0.15 GLN 244 -0.31 SER 364

GLN 299 0.11 ASP 245 -0.26 GLY 365

GLN 299 0.09 TYR 246 -0.24 SER 364

GLN 299 0.06 LYS 247 -0.25 SER 364

GLU 107 0.07 LYS 248 -0.24 SER 364

GLU 107 0.08 PRO 249 -0.25 SER 364

GLU 107 0.08 ILE 250 -0.25 SER 364

GLU 107 0.10 GLN 251 -0.22 SER 364

GLU 107 0.09 GLU 252 -0.21 SER 364

GLU 107 0.07 VAL 253 -0.22 SER 364

GLU 107 0.08 LEU 254 -0.21 SER 364

PRO 106 0.09 THR 255 -0.18 SER 364

PRO 106 0.08 GLU 256 -0.18 SER 364

PRO 106 0.07 MET 257 -0.18 SER 364

PRO 106 0.08 SER 258 -0.16 SER 364

PRO 106 0.09 ASN 259 -0.15 SER 364

PRO 106 0.11 GLY 260 -0.15 SER 364

PRO 106 0.11 GLY 261 -0.16 SER 364

GLU 107 0.10 VAL 262 -0.16 ASN 300

PRO 106 0.12 ASP 263 -0.18 ASN 300

GLU 107 0.11 PHE 264 -0.19 ASN 300

GLU 107 0.11 SER 265 -0.18 ASN 300

GLU 107 0.09 PHE 266 -0.17 ASN 300

GLU 107 0.09 GLU 267 -0.20 ARG 363

LEU 301 0.07 VAL 268 -0.20 ARG 363

GLN 299 0.12 ILE 269 -0.29 ARG 363

GLN 299 0.12 GLY 270 -0.25 HIS 51

GLN 299 0.21 ARG 271 -0.28 ARG 363

GLN 299 0.11 LEU 272 -0.22 ARG 363

GLN 299 0.12 ASP 273 -0.25 SER 364

GLU 107 0.09 THR 274 -0.25 SER 364

GLU 107 0.12 MET 275 -0.20 ASN 300

GLU 107 0.14 VAL 276 -0.21 ASN 300

GLU 107 0.11 THR 277 -0.22 SER 364

GLU 107 0.11 ALA 278 -0.20 SER 364

GLU 107 0.15 LEU 279 -0.26 ASN 300

GLU 107 0.14 SER 280 -0.19 ASN 300

GLU 107 0.11 CYS 281 -0.18 SER 364

GLU 107 0.13 CYS 282 -0.20 ASN 300

PRO 106 0.14 GLN 283 -0.19 ASN 300

PRO 106 0.16 GLU 284 -0.22 ASN 300

PRO 106 0.17 ALA 285 -0.23 ASN 300

PRO 106 0.18 TYR 286 -0.24 ASN 300

GLU 107 0.16 GLY 287 -0.24 ASN 300

GLU 107 0.19 VAL 288 -0.27 ASN 300

GLU 107 0.16 SER 289 -0.27 ASN 300

GLU 107 0.15 VAL 290 -0.26 ASN 300

MET 303 0.14 ILE 291 -0.25 ASN 300

LEU 301 0.12 VAL 292 -0.16 ASN 300

LEU 301 0.12 GLY 293 -0.18 HIS 51

LEU 301 0.10 VAL 294 -0.17 HIS 51

ILE 368 0.14 PRO 295 -0.28 THR 56

ARG 47 0.18 PRO 296 -0.14 VAL 58

ILE 368 0.17 ASP 297 -0.19 VAL 58

ILE 368 0.10 SER 298 -0.13 LEU 308

ARG 271 0.21 GLN 299 -0.25 TRP 314

GLN 244 0.09 ASN 300 -0.41 TRP 314

GLY 108 0.20 LEU 301 -0.14 SER 364

GLY 108 0.20 SER 302 -0.14 SER 364

GLU 107 0.22 MET 303 -0.16 ASN 300

HIS 105 0.23 ASN 304 -0.15 ASN 300

HIS 105 0.23 PRO 305 -0.35 ASN 300

PRO 106 0.20 MET 306 -0.25 ASN 300

GLU 107 0.20 LEU 307 -0.27 ASN 300

PRO 106 0.23 LEU 308 -0.37 ASN 300

PRO 106 0.21 LEU 309 -0.31 ASN 300

PRO 106 0.19 SER 310 -0.26 ASN 300

PRO 106 0.21 GLY 311 -0.29 ASN 300

GLU 107 0.22 ARG 312 -0.32 ASN 300

GLU 107 0.26 THR 313 -0.36 ASN 300

GLU 107 0.24 TRP 314 -0.41 ASN 300

GLU 107 0.25 LYS 315 -0.36 ASN 300

GLY 108 0.17 GLY 316 -0.30 ASN 300

LEU 301 0.16 ALA 317 -0.21 ASN 300

LEU 301 0.14 ILE 318 -0.15 ASN 300

LEU 301 0.11 PHE 319 -0.12 ASN 300

MET 303 0.11 GLY 320 -0.14 ASN 300

LYS 315 0.16 GLY 321 -0.13 ASN 300

MET 303 0.13 PHE 322 -0.11 ASN 300

ASN 304 0.14 LYS 323 -0.10 ASN 300

ASN 304 0.11 SER 324 -0.09 ASN 300

ASN 304 0.11 LYS 325 -0.07 ASN 300

LYS 185 0.13 ASP 326 -0.08 ASN 300

LYS 185 0.19 SER 327 -0.08 ASN 300

LYS 185 0.16 VAL 328 -0.06 ASN 300

LYS 185 0.16 PRO 329 -0.05 ASN 300

LYS 185 0.21 LYS 330 -0.05 ASN 300

VAL 184 0.19 LEU 331 -0.05 ASN 300

VAL 184 0.14 VAL 332 -0.05 ASN 300

ALA 214 0.17 ALA 333 -0.04 ASN 300

ALA 213 0.22 ASP 334 -0.05 ASN 300

ALA 213 0.17 PHE 335 -0.05 ASN 300

ALA 213 0.15 MET 336 -0.06 ASP 343

ALA 213 0.17 ALA 337 -0.04 ASN 300

ALA 213 0.15 LYS 338 -0.05 ASN 300

ALA 213 0.23 LYS 339 -0.05 ASN 300

ALA 213 0.17 PHE 340 -0.06 ASN 300

ALA 213 0.10 ALA 341 -0.06 LYS 228

ALA 213 0.08 LEU 342 -0.09 LYS 228

ASP 297 0.09 ASP 343 -0.09 ASP 227

ASP 297 0.11 PRO 344 -0.10 ASP 227

ASP 297 0.12 LEU 345 -0.15 LYS 228

PRO 296 0.11 ILE 346 -0.17 ASP 227

ASP 297 0.12 THR 347 -0.24 ASP 227

ASP 297 0.10 HIS 348 -0.22 ASP 227

PRO 296 0.08 VAL 349 -0.18 ASP 227

PRO 296 0.06 LEU 350 -0.18 ASP 227

PRO 296 0.05 PRO 351 -0.15 ASN 225

PRO 296 0.04 PHE 352 -0.15 ASN 225

PRO 296 0.03 GLU 353 -0.16 ASN 225

PRO 296 0.04 LYS 354 -0.18 ASN 225

PRO 296 0.04 ILE 355 -0.18 ASN 225

PRO 296 0.03 ASN 356 -0.20 ASN 225

ASP 297 0.05 GLU 357 -0.22 ASN 225

PRO 296 0.07 GLY 358 -0.23 ASN 225

ASP 297 0.07 PHE 359 -0.22 ASN 225

ASP 297 0.08 ASP 360 -0.27 ASN 225

ASP 297 0.11 LEU 361 -0.30 ASN 225

ASP 297 0.14 LEU 362 -0.28 ASN 225

ASP 297 0.13 ARG 363 -0.30 ILE 224

ASP 297 0.14 SER 364 -0.37 ILE 224

ASP 297 0.16 GLY 365 -0.45 ASN 225

ASP 297 0.16 GLU 366 -0.45 ASN 225

ASP 297 0.15 SER 367 -0.31 ASN 225

ASP 297 0.17 ILE 368 -0.29 LYS 228

PRO 296 0.13 ARG 369 -0.21 LYS 228

PRO 296 0.10 THR 370 -0.19 ASN 225

PRO 296 0.08 ILE 371 -0.16 ASP 227

PRO 296 0.06 LEU 372 -0.15 ASN 225

ALA 213 0.05 THR 373 -0.13 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 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.

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