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

* open cutoff 10 melek new *

CA distance fluctuations for 260522120748406586

--- normal mode 16 ---

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
ALA 321 0.12 ALA 1 -0.22 GLY 43

ALA 321 0.14 SER 2 -0.22 GLY 44

ALA 321 0.17 SER 3 -0.23 GLY 44

ALA 321 0.20 THR 4 -0.24 GLY 44

ALA 321 0.22 ASN 5 -0.26 GLY 44

ALA 321 0.24 LEU 6 -0.29 GLY 44

ALA 321 0.24 LYS 7 -0.31 GLY 44

ALA 321 0.25 ASP 8 -0.26 GLY 44

ALA 321 0.28 VAL 9 -0.25 GLY 44

ALA 321 0.31 LEU 10 -0.27 GLY 44

ALA 321 0.31 ALA 11 -0.24 GLY 44

ALA 321 0.32 ALA 12 -0.19 GLY 44

ALA 321 0.34 LEU 13 -0.24 GLU 17

ALA 321 0.38 ILE 14 -0.20 GLY 44

LEU 33 0.38 PRO 15 -0.16 GLY 44

LEU 33 0.39 LYS 16 -0.14 GLY 44

LEU 33 0.44 GLU 17 -0.24 LEU 13

LEU 33 0.45 GLN 18 -0.18 GLY 44

LEU 33 0.39 ALA 19 -0.18 GLY 44

LEU 33 0.46 ARG 20 -0.37 THR 98

LEU 33 0.53 ILE 21 -0.43 THR 98

PRO 422 0.40 LYS 22 -0.32 VAL 52

PRO 422 0.35 THR 23 -0.40 GLY 99

LEU 33 0.42 PHE 24 -0.65 GLU 54

PRO 422 0.45 ARG 25 -0.61 VAL 52

PRO 422 0.45 GLN 26 -0.47 GLY 50

PRO 422 0.40 GLN 27 -0.56 GLY 68

THR 31 0.48 HIS 28 -0.70 VAL 57

PRO 422 0.42 GLY 29 -0.82 LEU 51

PRO 422 0.55 GLY 30 -0.92 GLY 50

PRO 422 0.51 THR 31 -0.55 LYS 49

PRO 422 0.56 ALA 32 -0.53 LYS 423

PRO 422 0.68 LEU 33 -0.37 LYS 423

PRO 422 0.55 GLY 34 -0.76 LYS 423

PRO 422 0.56 GLN 35 -0.75 LYS 423

PRO 422 0.57 ILE 36 -0.75 LYS 423

ILE 36 0.50 THR 37 -0.60 LEU 273

GLY 44 0.33 VAL 38 -0.67 LEU 273

GLY 43 0.38 ASP 39 -0.99 LEU 273

GLY 43 0.40 MET 40 -0.79 LEU 273

THR 37 0.34 SER 41 -0.56 VAL 243

GLY 44 0.38 TYR 42 -0.89 GLY 271

ALA 367 0.46 GLY 43 -1.10 VAL 243

ALA 321 0.62 GLY 44 -1.17 VAL 243

ALA 321 0.62 MET 45 -0.96 LYS 423

ALA 321 0.68 ARG 46 -1.21 ASN 242

ALA 321 0.72 GLY 47 -1.00 LYS 423

ALA 321 0.60 MET 48 -1.22 LYS 423

ALA 321 0.65 LYS 49 -0.79 GLY 30

PRO 422 0.65 GLY 50 -0.92 GLY 30

ALA 321 0.61 LEU 51 -0.82 GLY 29

ALA 321 0.60 VAL 52 -0.72 GLY 29

ALA 321 0.56 TYR 53 -0.70 GLY 29

ALA 321 0.49 GLU 54 -0.70 GLY 29

ALA 321 0.41 THR 55 -0.63 GLY 29

ALA 321 0.46 SER 56 -0.66 HIS 28

LEU 58 0.68 VAL 57 -0.70 HIS 28

VAL 57 0.68 LEU 58 -0.52 LYS 423

LYS 355 0.40 ASP 59 -0.50 LYS 423

ALA 368 0.43 PRO 60 -0.44 LYS 423

LYS 355 0.50 ASP 61 -0.40 LYS 423

LYS 355 0.51 GLU 62 -0.44 HIS 28

LYS 355 0.47 GLY 63 -0.41 LYS 423

LYS 355 0.44 ILE 64 -0.51 HIS 28

LYS 355 0.40 ARG 65 -0.60 HIS 28

LYS 355 0.36 PHE 66 -0.59 HIS 28

LYS 355 0.36 ARG 67 -0.67 HIS 28

LYS 355 0.38 GLY 68 -0.68 HIS 28

LYS 355 0.39 PHE 69 -0.57 HIS 28

LYS 355 0.43 SER 70 -0.53 HIS 28

LYS 355 0.43 ILE 71 -0.45 HIS 28

LYS 355 0.46 PRO 72 -0.43 HIS 28

LYS 355 0.42 GLU 73 -0.47 HIS 28

LYS 355 0.37 CYS 74 -0.46 HIS 28

LYS 355 0.36 GLN 75 -0.41 HIS 28

LYS 355 0.35 LYS 76 -0.40 HIS 28

LYS 355 0.33 LEU 77 -0.41 HIS 28

LYS 355 0.29 LEU 78 -0.40 HIS 28

LYS 355 0.24 PRO 79 -0.35 HIS 28

LYS 355 0.21 LYS 80 -0.33 HIS 28

LYS 355 0.15 GLY 81 -0.30 HIS 28

LYS 355 0.14 GLY 82 -0.28 HIS 28

ASP 298 0.15 GLY 84 -0.30 HIS 28

ASP 298 0.22 GLY 85 -0.33 HIS 28

LYS 355 0.23 GLU 86 -0.34 HIS 28

LYS 355 0.25 PRO 87 -0.37 HIS 28

LYS 355 0.21 LEU 88 -0.35 HIS 28

LYS 355 0.22 PRO 89 -0.37 GLY 43

LYS 355 0.20 GLU 90 -0.35 GLY 43

LYS 355 0.24 GLY 91 -0.36 HIS 28

LYS 355 0.27 LEU 92 -0.41 HIS 28

ALA 321 0.26 PHE 93 -0.38 ARG 46

LYS 355 0.24 TRP 94 -0.38 PHE 24

LYS 355 0.29 LEU 95 -0.45 PHE 24

ALA 321 0.33 LEU 96 -0.49 PHE 24

ALA 321 0.32 VAL 97 -0.43 PHE 24

ALA 321 0.30 THR 98 -0.48 PHE 24

LYS 355 0.30 GLY 99 -0.59 PHE 24

LYS 355 0.29 GLN 100 -0.50 PHE 24

LYS 355 0.29 ILE 101 -0.42 PHE 24

LYS 355 0.25 PRO 102 -0.36 PHE 24

LYS 355 0.23 THR 103 -0.32 PHE 24

LYS 355 0.19 GLY 104 -0.29 HIS 28

LYS 355 0.16 ALA 105 -0.25 PHE 24

LYS 355 0.19 GLN 106 -0.28 PHE 24

LYS 355 0.18 VAL 107 -0.29 GLY 43

ALA 321 0.14 SER 108 -0.28 GLY 43

ALA 321 0.16 TRP 109 -0.28 GLY 43

ALA 321 0.18 LEU 110 -0.31 GLY 43

ALA 321 0.15 SER 111 -0.31 GLY 43

ALA 321 0.14 LYS 112 -0.30 GLY 43

ALA 321 0.17 GLU 113 -0.31 GLY 43

ALA 321 0.17 TRP 114 -0.34 GLY 43

ALA 321 0.14 ALA 115 -0.32 GLY 43

ALA 321 0.15 LYS 116 -0.31 GLY 43

ALA 321 0.18 ARG 117 -0.33 GLY 43

ALA 321 0.15 ALA 118 -0.35 GLY 43

ALA 321 0.15 ALA 119 -0.35 PRO 422

ALA 321 0.14 LEU 120 -0.39 PRO 422

ALA 321 0.14 PRO 121 -0.38 LYS 290

ALA 321 0.12 SER 122 -0.45 LYS 290

ALA 321 0.13 HIS 123 -0.41 PRO 422

ALA 321 0.13 VAL 124 -0.48 PRO 422

ALA 119 0.14 VAL 125 -0.49 LYS 290

ALA 119 0.10 THR 126 -0.50 LYS 290

ALA 321 0.10 MET 127 -0.52 PRO 422

ALA 119 0.10 LEU 128 -0.56 PRO 422

LYS 188 0.11 ASP 129 -0.59 LYS 290

ALA 119 0.09 ASN 130 -0.59 LYS 290

THR 220 0.09 PHE 131 -0.58 PRO 422

TYR 219 0.10 PRO 132 -0.63 LYS 290

TYR 219 0.12 THR 133 -0.69 LYS 290

TYR 219 0.11 ASN 134 -0.63 GLN 287

TYR 219 0.13 LEU 135 -0.69 PRO 422

TYR 219 0.15 HIS 136 -0.75 PRO 422

TYR 219 0.16 PRO 137 -0.72 PRO 422

TYR 219 0.15 MET 138 -0.85 PRO 422

ALA 321 0.13 SER 139 -0.86 PRO 422

ALA 321 0.12 GLN 140 -0.74 PRO 422

ALA 321 0.15 LEU 141 -0.74 PRO 422

ALA 321 0.19 SER 142 -0.86 PRO 422

ALA 321 0.17 ALA 143 -0.75 PRO 422

ALA 321 0.16 ALA 144 -0.63 PRO 422

ALA 321 0.21 ILE 145 -0.62 PRO 422

ALA 321 0.22 THR 146 -0.63 PRO 422

ALA 321 0.19 ALA 147 -0.53 PRO 422

ALA 321 0.20 LEU 148 -0.47 PRO 422

ALA 321 0.23 ASN 149 -0.43 PRO 422

ALA 321 0.21 SER 150 -0.34 PRO 422

ALA 321 0.21 GLU 151 -0.32 GLY 43

ALA 321 0.24 SER 152 -0.33 GLY 44

ALA 321 0.25 ASN 153 -0.30 GLY 44

ALA 321 0.28 PHE 154 -0.30 GLY 44

ALA 321 0.28 ALA 155 -0.29 GLY 44

ALA 321 0.26 ARG 156 -0.24 GLY 44

LEU 33 0.28 ALA 157 -0.23 GLY 44

LEU 33 0.30 TYR 158 -0.22 GLY 44

LYS 423 0.34 ALA 159 -0.17 GLY 44

LYS 423 0.32 GLU 160 -0.16 GLY 44

LYS 423 0.36 GLY 161 -0.13 GLY 44

LEU 33 0.34 ILE 162 -0.17 GLY 44

LEU 33 0.37 LEU 163 -0.18 GLY 44

LEU 33 0.41 ARG 164 -0.20 GLY 44

LEU 33 0.39 THR 165 -0.20 GLY 44

LEU 33 0.34 LYS 166 -0.23 GLY 44

ALA 321 0.34 TYR 167 -0.27 GLY 44

ALA 321 0.34 TRP 168 -0.30 GLY 44

ALA 321 0.30 GLU 169 -0.28 GLY 44

ALA 321 0.29 MET 170 -0.31 GLY 44

ALA 321 0.31 VAL 171 -0.36 GLY 44

ALA 321 0.30 TYR 172 -0.36 GLY 44

ALA 321 0.26 GLU 173 -0.33 GLY 44

ALA 321 0.26 SER 174 -0.38 GLY 44

ALA 321 0.28 ALA 175 -0.42 GLY 44

ALA 321 0.24 MET 176 -0.38 GLY 44

ALA 321 0.21 ASP 177 -0.37 GLY 43

ALA 321 0.22 LEU 178 -0.43 GLY 43

ALA 321 0.21 ILE 179 -0.43 GLY 43

ALA 321 0.18 ALA 180 -0.39 GLY 43

ALA 321 0.17 LYS 181 -0.43 PRO 422

ALA 321 0.17 LEU 182 -0.51 PRO 422

ALA 321 0.13 PRO 183 -0.48 PRO 422

ALA 321 0.12 CYS 184 -0.48 PRO 422

ALA 321 0.12 VAL 185 -0.55 PRO 422

ALA 321 0.11 ALA 186 -0.57 PRO 422

TYR 219 0.09 ALA 187 -0.50 PRO 422

ASP 129 0.11 LYS 188 -0.51 PRO 422

TYR 219 0.12 ILE 189 -0.57 PRO 422

TYR 219 0.19 TYR 190 -0.60 ALA 286

THR 220 0.14 ARG 191 -0.62 LYS 290

THR 220 0.12 ASN 192 -0.65 LYS 290

TYR 219 0.17 LEU 193 -0.69 LYS 290

TYR 219 0.23 TYR 194 -0.79 LYS 290

THR 220 0.16 ARG 195 -0.79 LYS 290

THR 220 0.12 ALA 196 -0.91 LYS 290

THR 220 0.10 GLY 197 -0.75 LYS 290

ASN 130 0.08 SER 198 -0.71 LYS 290

ASP 129 0.08 SER 199 -0.59 LYS 290

ASP 129 0.09 ILE 200 -0.49 LYS 290

ASP 129 0.07 GLY 201 -0.44 LYS 290

ASP 129 0.08 ALA 202 -0.37 LYS 290

ASP 129 0.10 ILE 203 -0.33 PRO 422

ALA 321 0.09 ASP 204 -0.30 GLY 43

ALA 321 0.11 SER 205 -0.29 GLY 43

ALA 321 0.09 LYS 206 -0.28 GLY 43

ALA 321 0.09 LEU 207 -0.31 GLY 43

ALA 321 0.11 ASP 208 -0.32 GLY 43

ALA 321 0.13 TRP 209 -0.36 GLY 43

ALA 321 0.11 SER 210 -0.37 GLY 43

GLY 82 0.08 HIS 211 -0.35 PRO 422

GLY 82 0.10 ASN 212 -0.37 PRO 422

ALA 321 0.09 PHE 213 -0.42 PRO 422

TYR 219 0.09 THR 214 -0.39 PRO 422

GLY 82 0.08 ASN 215 -0.38 PRO 422

GLY 82 0.07 MET 216 -0.42 PRO 422

TYR 219 0.16 LEU 217 -0.55 GLY 386

THR 220 0.21 GLY 218 -0.57 GLY 386

GLU 389 0.25 TYR 219 -0.35 ASP 344

GLY 218 0.21 THR 220 -0.34 ASP 344

GLU 389 0.18 ASP 221 -0.39 LEU 341

GLU 389 0.15 ALA 222 -0.29 PRO 422

TYR 385 0.15 GLN 223 -0.31 LEU 341

GLU 389 0.18 PHE 224 -0.32 PRO 422

GLU 389 0.14 THR 225 -0.32 PRO 422

GLU 389 0.13 GLU 226 -0.30 HIS 28

GLU 389 0.14 LEU 227 -0.33 PRO 422

TYR 219 0.13 MET 228 -0.36 PRO 422

LYS 355 0.17 ARG 229 -0.34 GLY 43

LYS 355 0.24 LEU 230 -0.36 HIS 28

LYS 355 0.22 TYR 231 -0.39 GLY 43

LYS 355 0.21 LEU 232 -0.43 GLY 43

LYS 355 0.27 THR 233 -0.40 HIS 28

LYS 355 0.32 ILE 234 -0.42 HIS 28

LYS 355 0.30 HIS 235 -0.50 GLY 43

ALA 321 0.30 SER 236 -0.48 ARG 46

ALA 321 0.42 ASP 237 -0.57 ARG 46

ALA 321 0.55 HIS 238 -0.67 ARG 46

ALA 321 0.63 GLU 239 -0.70 ARG 46

ALA 321 0.64 GLY 240 -0.64 ARG 46

ALA 321 0.73 GLY 241 -0.92 ARG 46

ALA 321 0.65 ASN 242 -1.21 ARG 46

ALA 321 0.50 VAL 243 -1.17 GLY 44

ALA 321 0.43 SER 244 -0.92 GLY 44

ALA 321 0.50 ALA 245 -0.84 GLY 44

ALA 321 0.54 HIS 246 -1.03 GLY 44

ALA 321 0.45 THR 247 -1.00 GLY 44

ALA 321 0.41 SER 248 -0.74 GLY 44

ALA 321 0.47 HIS 249 -0.65 GLY 44

ALA 321 0.45 LEU 250 -0.62 GLY 44

ALA 321 0.39 VAL 251 -0.57 GLY 44

ALA 321 0.39 GLY 252 -0.51 GLY 44

ALA 321 0.42 SER 253 -0.40 GLY 44

ALA 321 0.37 ALA 254 -0.36 GLY 44

ALA 321 0.36 LEU 255 -0.34 GLY 44

ALA 321 0.33 SER 256 -0.40 GLY 44

ALA 321 0.31 ASP 257 -0.40 GLY 44

ALA 321 0.31 PRO 258 -0.47 GLY 44

ALA 321 0.27 TYR 259 -0.49 PRO 422

ALA 321 0.29 LEU 260 -0.55 PRO 422

ALA 321 0.34 SER 261 -0.58 GLY 44

ALA 321 0.31 PHE 262 -0.69 PRO 422

ALA 321 0.26 ALA 263 -0.85 PRO 422

ALA 321 0.30 ALA 264 -1.06 PRO 422

ALA 321 0.34 ALA 265 -0.96 PRO 422

ALA 321 0.27 MET 266 -1.02 PRO 422

ALA 321 0.25 ASN 267 -1.27 PRO 422

ALA 321 0.32 GLY 268 -1.29 PRO 422

ALA 321 0.28 LEU 269 -0.99 PRO 422

ALA 321 0.18 ALA 270 -1.04 PRO 422

GLY 319 0.21 GLY 271 -1.09 GLY 43

LEU 288 0.16 PRO 272 -0.90 ASP 39

LEU 288 0.26 LEU 273 -0.99 ASP 39

GLY 319 0.31 HIS 274 -0.98 GLY 43

GLY 319 0.20 GLY 275 -0.83 GLY 43

LEU 288 0.17 LEU 276 -0.68 PRO 422

LEU 288 0.29 ALA 277 -0.58 ASP 39

LEU 288 0.25 ASN 278 -0.49 PRO 422

LEU 288 0.21 GLN 279 -0.58 PRO 422

LEU 288 0.31 GLU 280 -0.54 ASP 39

LEU 288 0.40 VAL 281 -0.40 ASP 39

LYS 290 0.33 LEU 282 -0.47 PRO 422

LYS 290 0.37 GLY 283 -0.54 ASN 391

GLN 287 0.52 TRP 284 -0.51 ILE 305

GLN 289 0.48 LEU 285 -0.44 TYR 194

LYS 290 0.43 ALA 286 -0.84 THR 388

TRP 284 0.52 GLN 287 -0.72 TYR 194

VAL 315 0.56 LEU 288 -0.58 ALA 196

LEU 285 0.48 GLN 289 -0.78 ALA 196

VAL 315 0.48 LYS 290 -0.91 ALA 196

VAL 315 0.53 ALA 291 -0.68 ALA 196

LYS 348 0.37 ALA 295 -0.55 ALA 196

THR 326 0.39 GLY 296 -0.49 ALA 196

THR 326 0.43 ALA 297 -0.42 ALA 196

THR 326 0.49 ASP 298 -0.35 ALA 196

LYS 325 0.48 ALA 299 -0.39 ALA 196

LYS 325 0.41 SER 300 -0.50 ALA 196

LYS 325 0.39 LEU 301 -0.47 ALA 196

LYS 325 0.44 ARG 302 -0.38 ALA 196

LYS 325 0.40 ASP 303 -0.44 ASN 134

PRO 370 0.39 TYR 304 -0.56 ASN 134

PRO 370 0.41 ILE 305 -0.51 TRP 284

PRO 370 0.39 TRP 306 -0.40 ASN 134

PRO 370 0.38 ASN 307 -0.48 ASN 134

ALA 291 0.49 THR 308 -0.49 ASN 134

ALA 291 0.42 LEU 309 -0.33 ASN 134

ALA 291 0.34 ASN 310 -0.36 ASN 134

ALA 291 0.40 SER 311 -0.46 ASN 134

ALA 291 0.43 GLY 312 -0.35 ASN 134

ALA 291 0.53 ARG 313 -0.46 ASP 39

ALA 291 0.51 VAL 314 -0.41 ASP 39

LEU 288 0.56 VAL 315 -0.34 ASP 39

LEU 288 0.47 PRO 316 -0.34 VAL 315

LEU 288 0.44 GLY 317 -0.28 ASP 39

ALA 291 0.43 TYR 318 -0.19 ARG 334

GLY 241 0.52 GLY 319 -0.18 GLU 335

GLY 241 0.60 HIS 320 -0.21 ALA 366

GLY 241 0.73 ALA 321 -0.27 ALA 366

LYS 49 0.54 VAL 322 -0.22 LYS 423

GLU 239 0.45 LEU 323 -0.24 LYS 423

ASN 359 0.50 ARG 324 -0.22 LYS 423

LYS 355 0.62 LYS 325 -0.23 LYS 423

LYS 355 0.67 THR 326 -0.25 HIS 28

LYS 355 0.51 ASP 327 -0.29 HIS 28

LYS 355 0.54 PRO 328 -0.33 HIS 28

LYS 355 0.44 ARG 329 -0.34 HIS 28

LYS 355 0.49 TYR 330 -0.29 HIS 28

LYS 355 0.58 THR 331 -0.28 HIS 28

LYS 355 0.43 CYS 332 -0.30 HIS 28

LYS 355 0.34 GLN 333 -0.29 HIS 28

LYS 355 0.34 ARG 334 -0.26 PRO 372

ASP 298 0.33 GLU 335 -0.26 PRO 372

ASP 298 0.26 PHE 336 -0.26 HIS 28

ALA 295 0.27 ALA 337 -0.26 PRO 422

ALA 295 0.30 LEU 338 -0.21 PRO 422

ALA 295 0.25 LYS 339 -0.23 HIS 28

ALA 295 0.24 HIS 340 -0.26 GLN 223

ALA 295 0.25 LEU 341 -0.39 ASP 221

ALA 295 0.31 PRO 342 -0.27 ASP 221

ALA 295 0.34 GLY 343 -0.32 ARG 195

ALA 295 0.29 ASP 344 -0.42 GLY 218

LYS 290 0.30 PRO 345 -0.50 ARG 195

LYS 290 0.32 MET 346 -0.50 ARG 195

THR 331 0.30 PHE 347 -0.36 ARG 195

ALA 295 0.37 LYS 348 -0.34 ARG 195

LYS 290 0.40 LEU 349 -0.42 ARG 195

THR 331 0.37 VAL 350 -0.35 ARG 195

THR 331 0.50 ALA 351 -0.27 ARG 195

THR 331 0.46 GLN 352 -0.30 ARG 195

THR 326 0.43 LEU 353 -0.30 ARG 195

THR 326 0.59 TYR 354 -0.21 ARG 195

THR 326 0.67 LYS 355 -0.20 ALA 196

LYS 325 0.55 ILE 356 -0.27 ALA 196

LYS 325 0.45 VAL 357 -0.26 ARG 195

LYS 325 0.57 PRO 358 -0.18 ARG 195

LYS 325 0.60 ASN 359 -0.20 ALA 196

LYS 325 0.44 VAL 360 -0.27 ALA 196

ALA 291 0.38 LEU 361 -0.21 ARG 195

GLY 47 0.46 LEU 362 -0.16 ARG 195

GLY 47 0.42 GLU 363 -0.19 ALA 196

ARG 46 0.38 GLN 364 -0.22 ALA 196

ARG 46 0.48 GLY 365 -0.16 ARG 195

GLY 44 0.47 ALA 366 -0.27 ALA 321

ARG 46 0.56 ALA 367 -0.14 LEU 338

GLY 47 0.59 ALA 368 -0.13 GLU 335

GLY 241 0.49 ASN 369 -0.16 GLU 335

GLY 241 0.47 PRO 370 -0.18 GLU 335

GLY 241 0.44 TRP 371 -0.24 GLU 335

GLY 241 0.41 PRO 372 -0.26 ARG 334

HIS 238 0.40 ASN 373 -0.25 ASP 39

LYS 355 0.37 VAL 374 -0.33 ASP 39

LEU 288 0.29 ASP 375 -0.39 ASP 39

LEU 288 0.37 ALA 376 -0.31 ASP 39

ALA 291 0.31 HIS 377 -0.29 ASP 39

LYS 355 0.23 SER 378 -0.37 PRO 422

ALA 291 0.20 GLY 379 -0.44 PRO 422

LYS 290 0.24 VAL 380 -0.39 PRO 422

ALA 291 0.17 LEU 381 -0.38 PRO 422

HIS 340 0.12 LEU 382 -0.45 PRO 422

GLN 279 0.11 GLN 383 -0.44 PRO 422

HIS 340 0.13 TYR 384 -0.48 GLY 218

HIS 340 0.15 TYR 385 -0.50 GLY 218

THR 388 0.18 GLY 386 -0.57 GLY 218

THR 388 0.38 MET 387 -0.55 LEU 217

MET 387 0.38 THR 388 -0.84 ALA 286

TYR 219 0.25 GLU 389 -0.81 ALA 286

TYR 219 0.14 MET 390 -0.59 PRO 422

TYR 219 0.19 ASN 391 -0.66 PRO 422

TYR 219 0.22 TYR 392 -0.65 PRO 422

TYR 219 0.19 TYR 393 -0.61 PRO 422

TYR 219 0.18 THR 394 -0.72 PRO 422

TYR 219 0.17 VAL 395 -0.68 PRO 422

TYR 219 0.19 LEU 396 -0.58 PRO 422

ALA 321 0.19 PHE 397 -0.61 GLY 43

ALA 321 0.23 GLY 398 -0.67 PRO 422

ALA 321 0.20 VAL 399 -0.56 PRO 422

ALA 321 0.23 SER 400 -0.52 GLY 43

ALA 321 0.32 ARG 401 -0.59 GLY 43

ALA 321 0.29 ALA 402 -0.54 GLY 43

ALA 321 0.30 LEU 403 -0.45 GLY 43

ALA 321 0.37 GLY 404 -0.51 ARG 46

ALA 321 0.40 VAL 405 -0.59 GLY 44

ALA 321 0.35 LEU 406 -0.51 GLY 44

ALA 321 0.35 ALA 407 -0.44 GLY 44

ALA 321 0.42 GLN 408 -0.46 GLY 44

ALA 321 0.40 LEU 409 -0.48 GLY 44

ALA 321 0.37 ILE 410 -0.39 GLY 44

ALA 321 0.41 TRP 411 -0.35 GLY 44

ALA 321 0.45 SER 412 -0.34 GLY 44

ALA 321 0.39 ARG 413 -0.33 GLY 44

ALA 321 0.40 ALA 414 -0.27 GLY 44

LEU 33 0.47 LEU 415 -0.21 GLY 44

LEU 33 0.48 GLY 416 -0.21 GLY 44

LEU 33 0.51 PHE 417 -0.21 GLY 44

PRO 422 0.66 PRO 418 -0.16 GLY 44

PRO 422 0.61 LEU 419 -0.26 GLY 44

PRO 422 0.71 GLU 420 -0.28 GLY 44

PRO 422 1.09 ARG 421 -0.17 GLY 44

ARG 421 1.09 PRO 422 -1.29 GLY 268

PRO 422 1.09 LYS 423 -1.22 MET 48

LYS 423 0.98 SER 424 -0.19 GLY 268

LYS 423 0.47 MET 425 -0.36 GLY 271

LYS 423 0.37 SER 426 -0.26 GLY 271

TYR 42 0.36 THR 427 -0.25 PRO 272

TYR 42 0.28 ASP 428 -0.32 GLN 35

PRO 422 0.28 GLY 429 -0.40 GLN 35

ALA 432 0.25 LEU 430 -0.57 ILE 36

TYR 42 0.37 ILE 431 -0.52 GLN 35

ASP 39 0.26 ALA 432 -0.74 GLN 35

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.

*** open cutoff 10 melek new ***

CA distance fluctuations for 260522120748406586

--- normal mode 16 ---

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

* open cutoff 10 melek new *