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 10 ---

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
ASN 300 0.02 SER 1 -0.22 GLU 74

LYS 8 0.04 THR 2 -0.41 GLU 74

ILE 7 0.19 ALA 3 -0.08 PRO 85

ASN 300 0.09 GLY 4 -0.07 LYS 5

ASN 300 0.08 LYS 5 -0.08 SER 1

ALA 3 0.11 VAL 6 -0.08 SER 1

ALA 3 0.19 ILE 7 -0.10 SER 1

ALA 3 0.15 LYS 8 -0.09 GLU 234

ALA 3 0.13 CYS 9 -0.10 ASP 227

ALA 3 0.10 LYS 10 -0.10 ASP 227

ALA 3 0.08 ALA 11 -0.10 ASP 227

GLY 316 0.08 ALA 12 -0.09 ASP 227

GLY 316 0.09 VAL 13 -0.08 ASP 227

PRO 305 0.09 LEU 14 -0.07 ASP 227

PRO 305 0.10 TRP 15 -0.07 ASP 227

PRO 305 0.10 GLU 16 -0.07 PRO 60

PRO 305 0.09 GLU 17 -0.10 PRO 60

PRO 305 0.07 LYS 18 -0.08 LEU 116

PRO 305 0.07 LYS 19 -0.08 ASP 227

PRO 305 0.06 PRO 20 -0.10 ASP 227

GLY 316 0.07 PHE 21 -0.09 ASP 227

GLY 316 0.07 SER 22 -0.09 ASP 227

ALA 3 0.08 ILE 23 -0.10 ASP 227

ALA 3 0.09 GLU 24 -0.09 ASP 227

ALA 3 0.09 GLU 25 -0.09 ASP 227

ALA 3 0.09 VAL 26 -0.08 ASP 227

ALA 3 0.11 GLU 27 -0.07 GLU 234

ALA 3 0.10 VAL 28 -0.10 THR 2

ASN 300 0.10 ALA 29 -0.09 THR 2

ASN 300 0.09 PRO 30 -0.15 THR 2

ASN 300 0.10 PRO 31 -0.16 THR 2

ASN 300 0.11 LYS 32 -0.10 THR 2

ASN 300 0.10 ALA 33 -0.09 THR 2

ASN 300 0.10 HIS 34 -0.11 THR 2

ASN 300 0.10 GLU 35 -0.14 THR 2

ASN 300 0.09 VAL 36 -0.19 THR 2

ASN 300 0.09 ARG 37 -0.28 THR 2

ILE 318 0.08 ILE 38 -0.29 THR 2

ILE 318 0.07 LYS 39 -0.30 THR 2

ILE 318 0.08 MET 40 -0.22 THR 2

ILE 318 0.07 VAL 41 -0.20 THR 2

ILE 318 0.07 ALA 42 -0.17 THR 2

ILE 318 0.09 THR 43 -0.14 THR 2

ILE 318 0.09 GLY 44 -0.12 THR 2

ILE 318 0.08 ILE 45 -0.12 ASP 227

GLY 316 0.08 CYS 46 -0.10 GLY 202

GLY 293 0.10 ARG 47 -0.09 PRO 296

GLY 293 0.15 SER 48 -0.08 THR 2

GLY 293 0.10 ASP 49 -0.08 THR 2

GLY 293 0.09 ASP 50 -0.07 ASP 227

GLY 293 0.10 HIS 51 -0.09 LEU 112

PRO 305 0.10 VAL 52 -0.11 LEU 116

PRO 305 0.08 VAL 53 -0.10 PRO 60

PRO 305 0.08 SER 54 -0.09 LEU 116

PRO 305 0.10 GLY 55 -0.11 LEU 116

ASP 297 0.14 THR 56 -0.10 LEU 116

PRO 295 0.16 LEU 57 -0.15 LEU 116

GLN 299 0.16 VAL 58 -0.16 LEU 116

PRO 305 0.14 THR 59 -0.14 LEU 116

PRO 305 0.14 PRO 60 -0.10 GLU 17

PRO 305 0.13 LEU 61 -0.07 PRO 60

PRO 305 0.12 PRO 62 -0.05 ASP 227

GLY 316 0.12 VAL 63 -0.06 THR 2

GLY 316 0.11 ILE 64 -0.08 THR 2

GLY 316 0.12 ALA 65 -0.08 THR 2

ILE 318 0.12 GLY 66 -0.11 THR 2

ILE 318 0.15 HIS 67 -0.12 THR 2

ILE 318 0.12 GLU 68 -0.13 THR 2

ILE 318 0.10 ALA 69 -0.16 THR 2

ILE 318 0.07 ALA 70 -0.18 THR 2

ILE 318 0.07 GLY 71 -0.22 THR 2

ASN 300 0.07 ILE 72 -0.26 THR 2

ASN 300 0.07 VAL 73 -0.28 THR 2

ASN 300 0.07 GLU 74 -0.41 THR 2

ASN 300 0.08 SER 75 -0.32 THR 2

ASN 300 0.08 ILE 76 -0.19 THR 2

ASN 300 0.09 GLY 77 -0.13 THR 2

ASN 300 0.09 GLU 78 -0.08 THR 2

ASN 300 0.09 GLY 79 -0.08 THR 2

ASN 300 0.09 VAL 80 -0.12 THR 2

ASN 300 0.08 THR 81 -0.12 THR 2

ASN 300 0.08 THR 82 -0.13 THR 2

ASN 300 0.07 VAL 83 -0.16 THR 2

ASN 300 0.07 ARG 84 -0.18 THR 2

ASN 300 0.07 PRO 85 -0.24 THR 2

ASN 300 0.06 GLY 86 -0.23 THR 2

ASN 300 0.06 ASP 87 -0.20 THR 2

ASN 300 0.06 LYS 88 -0.19 THR 2

ASN 300 0.07 VAL 89 -0.19 THR 2

ILE 318 0.08 ILE 90 -0.17 THR 2

ILE 318 0.10 PRO 91 -0.15 THR 2

ILE 318 0.13 LEU 92 -0.12 THR 2

ILE 318 0.19 PHE 93 -0.10 THR 2

ILE 318 0.17 THR 94 -0.09 CYS 174

ASN 300 0.11 PRO 95 -0.09 THR 2

ASN 300 0.11 GLN 96 -0.09 THR 2

ASN 300 0.11 CYS 97 -0.08 THR 2

ASN 300 0.10 GLY 98 -0.07 SER 298

GLY 311 0.12 LYS 99 -0.08 SER 298

GLY 311 0.16 CYS 100 -0.09 LEU 57

GLY 311 0.18 ARG 101 -0.11 SER 298

GLY 311 0.17 VAL 102 -0.11 SER 298

TYR 286 0.12 CYS 103 -0.10 SER 298

TYR 286 0.13 LYS 104 -0.10 LEU 301

LYS 188 0.17 HIS 105 -0.13 LEU 301

LYS 185 0.18 PRO 106 -0.13 LEU 301

LYS 185 0.26 GLU 107 -0.15 LEU 301

VAL 186 0.20 GLY 108 -0.13 LEU 301

VAL 186 0.17 ASN 109 -0.11 SER 298

LYS 315 0.19 PHE 110 -0.12 SER 298

LYS 315 0.15 CYS 111 -0.10 SER 298

LYS 315 0.17 LEU 112 -0.14 SER 117

LYS 315 0.17 LYS 113 -0.08 CYS 100

GLY 316 0.19 ASN 114 -0.10 LEU 112

GLY 316 0.21 ASP 115 -0.09 THR 59

GLY 316 0.27 LEU 116 -0.16 VAL 58

GLY 316 0.31 SER 117 -0.14 LEU 112

ASN 300 0.26 MET 118 -0.08 LEU 112

GLY 316 0.22 PRO 119 -0.07 LEU 112

ASN 300 0.19 ARG 120 -0.06 THR 2

GLY 316 0.17 GLY 121 -0.06 THR 2

GLY 316 0.15 THR 122 -0.07 THR 2

ASN 300 0.14 MET 123 -0.08 THR 2

ASN 300 0.15 GLN 124 -0.07 THR 2

ASN 300 0.14 ASP 125 -0.07 THR 2

ASN 300 0.16 GLY 126 -0.06 THR 2

PRO 305 0.14 THR 127 -0.06 THR 2

ASN 300 0.12 SER 128 -0.07 THR 2

ASN 300 0.11 ARG 129 -0.09 THR 2

GLY 316 0.10 PHE 130 -0.06 THR 2

PRO 305 0.10 THR 131 -0.06 ASP 227

PRO 305 0.10 CYS 132 -0.07 ASP 227

PRO 305 0.10 ARG 133 -0.06 ASP 227

PRO 305 0.11 GLY 134 -0.05 ASP 227

PRO 305 0.12 LYS 135 -0.05 ASP 227

PRO 305 0.12 PRO 136 -0.05 ASP 227

PRO 305 0.12 ILE 137 -0.05 ASP 227

GLY 316 0.13 HIS 138 -0.06 THR 2

GLY 316 0.14 HIS 139 -0.09 THR 2

GLY 316 0.16 PHE 140 -0.09 THR 2

ILE 318 0.18 LEU 141 -0.09 THR 2

ILE 318 0.14 GLY 142 -0.10 THR 2

ILE 318 0.14 THR 143 -0.13 THR 2

ILE 318 0.12 SER 144 -0.12 THR 2

ILE 318 0.11 THR 145 -0.14 THR 2

ILE 318 0.09 PHE 146 -0.11 THR 2

ILE 318 0.09 SER 147 -0.13 THR 2

ILE 318 0.07 GLN 148 -0.17 THR 2

ALA 3 0.09 TYR 149 -0.21 THR 2

ILE 318 0.09 THR 150 -0.18 THR 2

ASN 300 0.10 VAL 151 -0.17 THR 2

ASN 300 0.11 VAL 152 -0.15 THR 2

ASN 300 0.11 ASP 153 -0.12 THR 2

ASN 300 0.10 GLU 154 -0.12 THR 2

ASN 300 0.11 ILE 155 -0.10 THR 2

ASN 300 0.11 SER 156 -0.12 THR 2

ASN 300 0.09 VAL 157 -0.14 THR 2

ASN 300 0.08 ALA 158 -0.14 THR 2

ASN 300 0.07 LYS 159 -0.15 THR 2

PRO 106 0.06 ILE 160 -0.15 THR 2

PRO 106 0.05 ASP 161 -0.15 ALA 213

ASN 300 0.05 ALA 162 -0.15 THR 2

PRO 106 0.05 ALA 163 -0.16 ALA 213

PRO 106 0.05 SER 164 -0.16 ALA 213

ALA 333 0.05 PRO 165 -0.17 ASP 343

PHE 319 0.06 LEU 166 -0.19 THR 2

HIS 348 0.07 GLU 167 -0.17 THR 2

MET 336 0.10 LYS 168 -0.16 VAL 235

MET 336 0.06 VAL 169 -0.15 THR 2

PHE 319 0.07 CYS 170 -0.15 THR 2

ILE 346 0.11 LEU 171 -0.13 THR 2

PRO 344 0.09 ILE 172 -0.14 THR 2

PHE 319 0.13 GLY 173 -0.14 THR 2

PRO 344 0.13 CYS 174 -0.12 THR 2

PRO 344 0.19 GLY 175 -0.12 PRO 296

PRO 344 0.19 PHE 176 -0.12 THR 2

PRO 344 0.15 SER 177 -0.11 THR 2

PRO 344 0.15 THR 178 -0.09 PRO 296

PRO 344 0.15 GLY 179 -0.10 THR 2

PRO 344 0.13 TYR 180 -0.14 LEU 331

GLU 107 0.12 GLY 181 -0.13 LEU 331

ASN 300 0.13 SER 182 -0.10 LEU 331

GLU 107 0.14 ALA 183 -0.14 ASP 334

GLU 107 0.21 VAL 184 -0.18 ASP 334

GLU 107 0.26 LYS 185 -0.12 ASP 334

GLY 108 0.20 VAL 186 -0.11 LEU 301

GLY 108 0.17 ALA 187 -0.11 ASP 334

GLU 107 0.24 LYS 188 -0.14 ASP 334

GLU 107 0.19 VAL 189 -0.16 ASP 334

GLU 107 0.19 THR 190 -0.16 ASP 334

GLU 107 0.17 GLN 191 -0.19 LYS 339

GLU 107 0.14 GLY 192 -0.18 LYS 339

GLU 107 0.14 SER 193 -0.16 LYS 339

GLU 107 0.12 THR 194 -0.15 LYS 339

ASN 300 0.12 CYS 195 -0.13 LYS 339

SER 117 0.12 ALA 196 -0.10 LYS 339

SER 117 0.11 VAL 197 -0.10 LEU 254

SER 117 0.11 PHE 198 -0.09 LEU 254

PRO 344 0.09 GLY 199 -0.11 GLY 365

PRO 344 0.10 LEU 200 -0.14 GLU 366

PRO 344 0.18 GLY 201 -0.10 THR 2

PRO 344 0.25 GLY 202 -0.12 THR 2

PRO 344 0.19 VAL 203 -0.10 THR 2

PRO 344 0.16 GLY 204 -0.10 THR 2

PRO 344 0.20 LEU 205 -0.12 THR 2

PRO 344 0.18 SER 206 -0.12 THR 2

PRO 344 0.12 VAL 207 -0.10 ASP 334

GLU 107 0.09 ILE 208 -0.11 THR 2

GLU 107 0.10 MET 209 -0.13 ASP 334

GLU 107 0.13 GLY 210 -0.18 ASP 334

GLU 107 0.13 CYS 211 -0.17 ASP 334

GLU 107 0.13 LYS 212 -0.24 LYS 339

GLU 107 0.14 ALA 213 -0.33 LYS 339

GLU 107 0.18 ALA 214 -0.23 ASP 334

GLU 107 0.16 GLY 215 -0.25 LYS 339

GLU 107 0.14 ALA 216 -0.20 LYS 339

GLU 107 0.12 ALA 217 -0.19 LYS 339

GLU 107 0.11 ARG 218 -0.15 LYS 339

GLU 107 0.10 ILE 219 -0.13 SER 258

SER 117 0.10 ILE 220 -0.18 MET 257

SER 117 0.08 GLY 221 -0.14 LEU 254

SER 117 0.09 VAL 222 -0.13 LEU 254

SER 117 0.07 ASP 223 -0.17 GLU 366

ASP 273 0.08 ILE 224 -0.19 GLU 366

ASP 273 0.06 ASN 225 -0.27 GLU 366

CYS 240 0.06 LYS 226 -0.24 GLU 366

ASP 273 0.04 ASP 227 -0.31 GLU 366

ASP 273 0.04 LYS 228 -0.27 GLU 366

GLU 107 0.05 PHE 229 -0.18 ILE 368

PRO 106 0.05 ALA 230 -0.21 THR 347

PRO 106 0.06 LYS 231 -0.28 LEU 345

GLU 107 0.07 ALA 232 -0.20 LEU 345

GLU 107 0.07 LYS 233 -0.19 LEU 345

PRO 106 0.07 GLU 234 -0.25 LEU 345

PRO 106 0.07 VAL 235 -0.24 LEU 345

GLU 107 0.09 GLY 236 -0.16 PHE 340

GLU 107 0.09 ALA 237 -0.14 LEU 345

GLU 107 0.09 THR 238 -0.15 MET 257

GLU 107 0.08 GLU 239 -0.19 MET 257

SER 117 0.07 CYS 240 -0.17 MET 257

SER 117 0.08 VAL 241 -0.17 VAL 253

ASP 273 0.09 ASN 242 -0.16 GLU 366

ASP 273 0.12 PRO 243 -0.14 GLU 366

ASP 273 0.13 GLN 244 -0.15 GLU 366

LEU 301 0.10 ASP 245 -0.14 GLU 366

LEU 301 0.10 TYR 246 -0.12 GLU 366

LEU 301 0.11 LYS 247 -0.11 GLU 366

LEU 301 0.12 LYS 248 -0.10 GLU 366

LEU 301 0.13 PRO 249 -0.10 GLU 366

SER 117 0.10 ILE 250 -0.12 GLU 366

SER 117 0.12 GLN 251 -0.10 GLU 366

SER 117 0.11 GLU 252 -0.10 GLU 366

SER 117 0.09 VAL 253 -0.17 VAL 241

SER 117 0.10 LEU 254 -0.15 ILE 220

SER 117 0.12 THR 255 -0.12 ILE 220

SER 117 0.10 GLU 256 -0.14 GLU 239

SER 117 0.09 MET 257 -0.19 GLU 239

SER 117 0.10 SER 258 -0.17 ILE 220

SER 117 0.11 ASN 259 -0.13 GLU 239

ASN 300 0.13 GLY 260 -0.11 LYS 339

ASN 300 0.14 GLY 261 -0.11 LYS 339

ASN 300 0.14 VAL 262 -0.12 LYS 339

ASN 300 0.15 ASP 263 -0.11 LYS 339

ASN 300 0.16 PHE 264 -0.11 ASP 334

ASN 300 0.16 SER 265 -0.09 ASP 334

SER 117 0.15 PHE 266 -0.09 ASP 334

SER 117 0.15 GLU 267 -0.06 ASP 334

SER 117 0.12 VAL 268 -0.07 THR 2

PRO 344 0.11 ILE 269 -0.11 GLN 299

SER 117 0.11 GLY 270 -0.11 GLN 299

MET 118 0.10 ARG 271 -0.21 GLN 299

MET 118 0.12 LEU 272 -0.15 GLN 299

GLN 244 0.13 ASP 273 -0.14 GLN 299

SER 117 0.12 THR 274 -0.09 GLN 299

ASN 300 0.20 MET 275 -0.07 MET 303

ASN 300 0.22 VAL 276 -0.08 ASN 304

SER 117 0.15 THR 277 -0.07 GLY 365

ASN 300 0.16 ALA 278 -0.07 ASP 334

ASN 300 0.25 LEU 279 -0.07 ASP 334

ASN 300 0.20 SER 280 -0.07 ASP 334

ASN 300 0.15 CYS 281 -0.08 LYS 339

ASN 300 0.18 CYS 282 -0.09 LYS 339

ASN 300 0.17 GLN 283 -0.10 LYS 339

ASN 300 0.20 GLU 284 -0.08 LYS 339

ASN 300 0.19 ALA 285 -0.08 ALA 337

ASN 300 0.19 TYR 286 -0.09 ALA 337

ASN 300 0.19 GLY 287 -0.09 ASP 334

ASN 300 0.21 VAL 288 -0.09 ASP 334

ASN 300 0.23 SER 289 -0.08 ASP 334

ASN 300 0.22 VAL 290 -0.11 LEU 301

ASN 300 0.22 ILE 291 -0.14 LEU 301

SER 117 0.18 VAL 292 -0.11 LEU 301

SER 117 0.18 GLY 293 -0.10 LEU 301

ASN 300 0.17 VAL 294 -0.09 SER 298

LEU 57 0.16 PRO 295 -0.09 GLY 175

ASN 300 0.17 PRO 296 -0.12 GLY 175

VAL 58 0.15 ASP 297 -0.10 GLY 108

THR 56 0.10 SER 298 -0.13 GLY 108

MET 118 0.26 GLN 299 -0.21 ARG 271

PRO 305 0.33 ASN 300 -0.08 ASP 273

PRO 249 0.13 LEU 301 -0.18 GLY 316

PRO 249 0.12 SER 302 -0.13 GLY 316

ASN 300 0.22 MET 303 -0.11 TRP 314

ASN 300 0.20 ASN 304 -0.09 ASP 273

ASN 300 0.33 PRO 305 -0.07 ASN 304

ASN 300 0.25 MET 306 -0.05 ASP 334

ASN 300 0.26 LEU 307 -0.06 ASP 334

ASN 300 0.30 LEU 308 -0.06 ASP 334

ASN 300 0.25 LEU 309 -0.06 ALA 337

ASN 300 0.22 SER 310 -0.07 ALA 337

ASN 300 0.23 GLY 311 -0.07 ALA 337

ASN 300 0.25 ARG 312 -0.07 ASP 334

ASN 300 0.26 THR 313 -0.09 LEU 301

ASN 300 0.31 TRP 314 -0.14 LEU 301

SER 117 0.29 LYS 315 -0.16 LEU 301

SER 117 0.31 GLY 316 -0.18 LEU 301

SER 117 0.25 ALA 317 -0.15 LEU 301

LEU 116 0.23 ILE 318 -0.14 LEU 301

GLY 173 0.13 PHE 319 -0.11 LEU 301

PRO 344 0.12 GLY 320 -0.10 LEU 301

ASN 300 0.13 GLY 321 -0.11 LEU 301

ASN 300 0.11 PHE 322 -0.10 LEU 301

ASN 300 0.10 LYS 323 -0.10 LEU 301

ASN 300 0.09 SER 324 -0.09 THR 2

ASN 300 0.08 LYS 325 -0.11 THR 2

PRO 106 0.11 ASP 326 -0.10 THR 2

PRO 106 0.10 SER 327 -0.10 THR 2

PRO 106 0.07 VAL 328 -0.12 THR 2

PRO 106 0.07 PRO 329 -0.12 THR 2

PRO 106 0.09 LYS 330 -0.14 ALA 213

PRO 106 0.08 LEU 331 -0.18 ALA 213

PRO 106 0.07 VAL 332 -0.19 ALA 213

LEU 166 0.06 ALA 333 -0.21 ALA 213

PRO 106 0.08 ASP 334 -0.29 ALA 213

PRO 106 0.08 PHE 335 -0.24 ALA 213

LYS 168 0.10 MET 336 -0.20 ALA 213

LYS 168 0.07 ALA 337 -0.24 ALA 213

PRO 106 0.08 LYS 338 -0.21 ALA 213

PRO 106 0.11 LYS 339 -0.33 ALA 213

PRO 106 0.13 PHE 340 -0.22 ALA 213

PRO 106 0.11 ALA 341 -0.16 VAL 235

PHE 176 0.10 LEU 342 -0.22 VAL 235

GLY 175 0.11 ASP 343 -0.17 PRO 165

GLY 202 0.25 PRO 344 -0.24 GLU 234

GLY 175 0.18 LEU 345 -0.28 LYS 231

GLY 175 0.14 ILE 346 -0.22 LYS 231

GLY 175 0.10 THR 347 -0.23 LYS 231

MET 336 0.08 HIS 348 -0.20 ASP 227

MET 336 0.06 VAL 349 -0.16 ASP 227

ILE 318 0.06 LEU 350 -0.15 ASP 227

ILE 318 0.06 PRO 351 -0.13 ASP 227

ILE 318 0.06 PHE 352 -0.12 ASP 227

ILE 318 0.06 GLU 353 -0.12 ASP 227

ILE 318 0.05 LYS 354 -0.14 ASP 227

ILE 318 0.06 ILE 355 -0.13 ASP 227

GLY 316 0.06 ASN 356 -0.13 ASP 227

ILE 318 0.04 GLU 357 -0.16 ASP 227

ILE 318 0.05 GLY 358 -0.16 ASP 227

GLY 316 0.05 PHE 359 -0.13 ASP 227

GLY 316 0.03 ASP 360 -0.15 ASP 227

LEU 350 0.04 LEU 361 -0.20 ASP 227

PRO 344 0.05 LEU 362 -0.15 ASP 227

PRO 344 0.05 ARG 363 -0.11 ASP 227

PRO 344 0.05 SER 364 -0.15 ASN 225

PRO 344 0.06 GLY 365 -0.23 ASN 225

PRO 344 0.07 GLU 366 -0.31 ASP 227

GLY 175 0.06 SER 367 -0.25 ASP 227

GLY 175 0.10 ILE 368 -0.25 LYS 228

GLY 175 0.11 ARG 369 -0.18 LYS 228

GLY 175 0.07 THR 370 -0.17 ASP 227

ILE 318 0.07 ILE 371 -0.15 LYS 231

ILE 318 0.07 LEU 372 -0.13 THR 2

ILE 318 0.07 THR 373 -0.15 THR 2

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 10 ---

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 *