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

* 1FC7C6F2933742E0 *

CA distance fluctuations for 2605201334553922152

--- 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
PRO 41 0.42 LEU 1 -0.06 GLN 1

PRO 41 0.33 PRO 2 -0.05 GLY 185

GLY 109 0.31 ASN 3 -0.07 GLN 1

GLY 109 0.24 ILE 4 -0.06 ASN 3

GLY 109 0.22 THR 5 -0.06 ASP 28

PRO 227 0.21 ILE 6 -0.07 ASP 28

PRO 227 0.22 LEU 7 -0.08 SER 19

PRO 227 0.25 ALA 8 -0.12 SER 19

PRO 227 0.28 THR 9 -0.15 SER 19

PRO 227 0.30 GLY 10 -0.21 SER 19

PRO 227 0.31 GLY 11 -0.18 LYS 22

PRO 227 0.28 THR 12 -0.14 LYS 22

PRO 227 0.27 ILE 13 -0.08 LYS 22

PRO 227 0.24 ALA 14 -0.05 GLY 31

PRO 227 0.24 GLY 15 -0.14 GLY 31

PRO 227 0.21 GLY 16 -0.08 THR 58

LEU 226 0.20 GLY 17 -0.11 GLY 57

LEU 226 0.19 ASP 18 -0.17 GLY 57

LEU 226 0.20 SER 19 -0.23 GLY 57

LEU 226 0.18 ALA 20 -0.21 ILE 56

LEU 226 0.17 THR 21 -0.25 GLY 57

LEU 226 0.16 LYS 22 -0.26 GLY 57

LEU 226 0.16 SER 23 -0.19 GLY 57

LEU 226 0.16 ASN 24 -0.19 GLN 59

LEU 226 0.16 TYR 25 -0.14 GLN 59

LEU 226 0.18 THR 26 -0.18 PRO 117

LEU 226 0.20 ALA 27 -0.18 PRO 117

LEU 226 0.18 GLY 28 -0.14 THR 58

LEU 226 0.18 LYS 29 -0.20 THR 58

LEU 226 0.20 VAL 30 -0.14 PRO 117

LEU 226 0.19 GLY 31 -0.14 GLY 15

LEU 226 0.18 VAL 32 -0.12 MET 121

LEU 226 0.19 GLU 33 -0.17 MET 121

PRO 227 0.20 ASN 34 -0.14 MET 121

PRO 227 0.19 LEU 35 -0.10 MET 121

PRO 227 0.18 VAL 36 -0.13 MET 121

SER 224 0.19 ASN 37 -0.14 MET 121

PRO 227 0.21 ALA 38 -0.09 MET 121

PRO 227 0.20 VAL 39 -0.08 MET 121

GLU 46 0.21 PRO 40 -0.09 MET 121

GLY 185 0.20 GLN 41 -0.09 MET 121

PRO 227 0.20 LEU 42 -0.07 SER 122

ALA 137 0.21 LYS 43 -0.06 GLN 3

GLY 44 0.29 ASP 44 -0.06 GLN 3

ASP 138 0.29 ILE 45 -0.09 ALA 46

PRO 41 0.26 ALA 46 -0.09 ILE 45

VAL 93 0.28 ASN 47 -0.08 GLN 3

GLY 109 0.22 VAL 48 -0.11 LYS 49

GLY 109 0.22 LYS 49 -0.11 VAL 48

PRO 227 0.21 GLY 50 -0.07 ASP 28

PRO 227 0.21 GLU 51 -0.10 ASP 28

PRO 227 0.23 GLN 52 -0.13 ASP 28

PRO 227 0.23 VAL 53 -0.11 ASP 28

PRO 227 0.26 VAL 54 -0.15 THR 21

PRO 227 0.29 ASN 55 -0.20 SER 19

PRO 227 0.34 ILE 56 -0.24 THR 21

PRO 227 0.39 GLY 57 -0.26 LYS 22

PRO 227 0.40 SER 58 -0.21 LYS 22

PRO 227 0.51 GLN 59 -0.24 LYS 22

PRO 227 0.46 ASP 60 -0.24 THR 21

PRO 227 0.36 MET 61 -0.18 THR 21

LEU 231 0.32 ASN 62 -0.15 THR 21

LEU 231 0.21 ASP 63 -0.13 THR 21

ALA 234 0.22 ASP 64 -0.14 THR 21

PRO 227 0.22 VAL 65 -0.14 THR 21

PRO 227 0.19 TRP 66 -0.12 THR 21

GLY 109 0.14 LEU 67 -0.12 THR 21

PRO 227 0.16 THR 68 -0.12 THR 21

PRO 227 0.17 LEU 69 -0.11 THR 21

GLY 109 0.16 ALA 70 -0.11 THR 21

GLN 108 0.17 LYS 71 -0.10 THR 21

GLN 108 0.19 LYS 72 -0.09 THR 21

GLN 108 0.20 ILE 73 -0.08 THR 21

PRO 41 0.20 ASN 74 -0.08 THR 21

GLN 108 0.21 THR 75 -0.07 THR 21

GLN 108 0.24 ASP 76 -0.07 ASP 28

GLN 108 0.24 CYS 77 -0.06 SER 19

GLN 108 0.27 ASP 78 -0.05 SER 19

GLN 108 0.30 LYS 79 -0.05 GLY 27

GLN 108 0.30 THR 80 -0.05 GLU 51

PRO 41 0.29 ASP 81 -0.05 ALA 136

PRO 41 0.25 GLY 82 -0.05 SER 19

PRO 41 0.20 PHE 83 -0.07 SER 19

PRO 227 0.21 VAL 84 -0.08 SER 19

PRO 227 0.23 ILE 85 -0.09 SER 19

PRO 227 0.26 THR 86 -0.11 SER 19

PRO 227 0.30 HIS 87 -0.14 LYS 22

PRO 227 0.35 GLY 88 -0.18 LYS 22

PRO 227 0.36 THR 89 -0.16 LYS 22

PRO 227 0.43 ASP 90 -0.19 LYS 22

PRO 227 0.38 THR 91 -0.17 LYS 22

PRO 227 0.30 MET 92 -0.14 LYS 22

TYR 218 0.27 GLU 93 -0.12 LYS 22

VAL 217 0.26 GLU 94 -0.12 LYS 22

PRO 227 0.23 THR 95 -0.13 LYS 22

PRO 227 0.19 ALA 96 -0.11 LYS 22

GLY 42 0.18 TYR 97 -0.11 LYS 22

GLY 42 0.17 PHE 98 -0.11 LYS 22

GLY 42 0.18 LEU 99 -0.10 LYS 22

GLY 42 0.19 ASP 100 -0.10 LYS 22

GLY 42 0.18 LEU 101 -0.10 LYS 22

GLY 42 0.18 THR 102 -0.10 THR 21

GLY 42 0.19 VAL 103 -0.09 THR 21

PRO 41 0.21 LYS 104 -0.08 THR 21

PRO 41 0.23 CYS 105 -0.07 THR 21

GLY 42 0.25 ASP 106 -0.07 THR 21

GLY 42 0.27 LYS 107 -0.06 SER 19

GLY 42 0.25 PRO 108 -0.07 SER 19

GLY 42 0.22 VAL 109 -0.08 LYS 22

GLY 42 0.20 VAL 110 -0.08 LYS 22

PRO 227 0.23 MET 111 -0.10 LYS 22

PRO 227 0.26 VAL 112 -0.09 LYS 22

PRO 227 0.29 GLY 113 -0.11 LYS 22

PRO 227 0.30 ALA 114 -0.11 LYS 22

PRO 227 0.33 MET 115 -0.12 ASN 24

SER 224 0.32 ARG 116 -0.12 ASN 24

PRO 227 0.31 PRO 117 -0.18 ALA 27

LEU 226 0.26 SER 118 -0.15 PRO 117

LEU 226 0.26 THR 119 -0.17 PRO 117

SER 224 0.29 SER 120 -0.15 TYR 59

SER 224 0.30 MET 121 -0.18 ASP 62

SER 224 0.29 SER 122 -0.13 ASP 62

SER 224 0.28 ALA 123 -0.10 TYR 59

SER 224 0.27 ASP 124 -0.07 ALA 123

PRO 227 0.27 GLY 125 -0.06 THR 58

PRO 227 0.24 PRO 126 -0.06 SER 122

PRO 227 0.23 PHE 127 -0.08 SER 122

PRO 227 0.25 ASN 128 -0.05 SER 122

PRO 227 0.24 LEU 129 -0.04 THR 135

PRO 227 0.22 TYR 130 -0.06 SER 122

TYR 218 0.22 ASN 131 -0.06 SER 122

PRO 227 0.22 ALA 132 -0.05 LYS 22

PRO 227 0.21 VAL 133 -0.05 SER 122

GLY 42 0.24 VAL 134 -0.06 ALA 137

GLY 42 0.24 THR 135 -0.06 LYS 186

GLY 42 0.24 ALA 136 -0.05 SER 19

GLY 42 0.31 ALA 137 -0.07 GLY 185

GLY 42 0.34 ASP 138 -0.08 LYS 186

GLY 42 0.37 LYS 139 -0.06 ALA 287

GLY 42 0.33 ALA 140 -0.07 LYS 186

GLY 42 0.29 SER 141 -0.06 LYS 186

GLY 42 0.29 ALA 142 -0.07 ALA 287

GLY 42 0.27 ASN 143 -0.08 GLN 318

GLY 42 0.25 ARG 144 -0.07 LYS 22

GLY 42 0.23 GLY 145 -0.08 LYS 22

GLY 42 0.21 VAL 146 -0.09 LYS 22

GLY 42 0.21 LEU 147 -0.09 LYS 22

TYR 218 0.23 VAL 148 -0.09 LYS 22

TYR 218 0.23 VAL 149 -0.08 LYS 22

TYR 218 0.26 MET 150 -0.08 LYS 22

TYR 220 0.26 ASN 151 -0.07 LYS 22

TYR 220 0.23 ASP 152 -0.06 SER 122

TYR 220 0.23 THR 153 -0.07 LYS 22

GLY 42 0.21 VAL 154 -0.07 LYS 22

TYR 218 0.21 LEU 155 -0.09 LYS 22

GLY 42 0.21 ASP 156 -0.09 LYS 22

GLY 42 0.19 GLY 157 -0.10 LYS 22

GLY 42 0.18 ARG 158 -0.10 LYS 22

ARG 272 0.20 ASP 159 -0.11 LYS 22

TYR 218 0.24 VAL 160 -0.11 LYS 22

TYR 218 0.33 THR 161 -0.13 LYS 22

TYR 218 0.40 LYS 162 -0.14 LYS 22

TYR 220 0.41 THR 163 -0.13 LYS 22

TYR 220 0.46 ASN 164 -0.14 LYS 22

TYR 220 0.48 THR 165 -0.17 ASN 24

ALA 223 0.42 THR 166 -0.15 ASN 24

TYR 220 0.38 ASP 167 -0.11 ASN 24

TYR 220 0.32 VAL 168 -0.08 ASN 24

TYR 220 0.31 ALA 169 -0.08 LYS 22

TYR 220 0.35 THR 170 -0.11 LYS 22

TYR 218 0.32 PHE 171 -0.11 LYS 22

ARG 272 0.29 LYS 172 -0.10 LYS 22

ARG 272 0.24 SER 173 -0.10 LYS 22

VAL 273 0.28 VAL 174 -0.11 LYS 22

THR 275 0.23 ASN 175 -0.10 LYS 22

GLY 42 0.19 TYR 176 -0.10 ASP 281

VAL 273 0.19 GLY 177 -0.09 LYS 22

ARG 272 0.20 PRO 178 -0.08 LYS 22

GLY 42 0.23 LEU 179 -0.09 PRO 193

GLY 42 0.24 GLY 180 -0.07 PRO 193

GLY 42 0.21 TYR 181 -0.06 SER 122

GLY 42 0.21 ILE 182 -0.06 SER 122

GLY 42 0.20 HIS 183 -0.05 SER 122

GLY 42 0.19 ASN 184 -0.05 ALA 137

GLY 42 0.25 GLY 185 -0.07 ALA 137

GLY 42 0.30 LYS 186 -0.08 ASP 138

GLY 42 0.28 ILE 187 -0.05 SER 122

GLY 42 0.28 ASP 188 -0.06 ALA 287

GLY 42 0.28 TYR 189 -0.08 ALA 287

GLY 42 0.26 GLN 190 -0.09 ALA 287

GLY 42 0.24 ARG 191 -0.10 ALA 287

GLY 42 0.24 THR 192 -0.10 PRO 193

GLY 42 0.21 PRO 193 -0.10 THR 192

GLY 42 0.20 ALA 194 -0.13 ALA 287

GLY 42 0.19 ARG 195 -0.13 GLN 325

GLY 42 0.19 LYS 196 -0.11 ALA 287

GLY 42 0.20 HIS 197 -0.09 GLN 318

GLY 42 0.21 THR 198 -0.09 LYS 22

GLY 42 0.21 SER 199 -0.09 GLN 318

GLY 42 0.20 ASP 200 -0.12 GLN 318

GLY 42 0.18 THR 201 -0.12 GLN 318

GLY 42 0.16 PRO 202 -0.13 THR 313

GLY 42 0.16 PHE 203 -0.09 THR 313

PRO 41 0.16 ASP 204 -0.09 THR 21

PRO 41 0.16 VAL 205 -0.10 THR 21

PRO 41 0.16 SER 206 -0.09 THR 21

PRO 41 0.15 LYS 207 -0.10 THR 21

PRO 41 0.13 LEU 208 -0.10 THR 21

GLN 108 0.13 ASN 209 -0.11 THR 21

GLN 108 0.12 GLU 210 -0.11 THR 21

GLY 42 0.14 LEU 211 -0.09 PRO 274

GLY 42 0.13 PRO 212 -0.08 PRO 274

ASN 62 0.23 LYS 213 -0.12 VAL 214

ASP 60 0.24 VAL 214 -0.12 LYS 213

GLN 59 0.34 GLY 215 -0.07 PRO 274

GLN 59 0.35 ILE 216 -0.09 ARG 272

GLN 59 0.40 VAL 217 -0.06 TYR 236

THR 165 0.48 TYR 218 -0.04 TYR 236

THR 165 0.43 ASN 219 -0.04 LEU 249

THR 165 0.48 TYR 220 -0.06 LEU 249

THR 165 0.44 ALA 221 -0.06 GLU 283

THR 165 0.44 ASN 222 -0.06 GLU 283

THR 165 0.47 ALA 223 -0.05 GLU 283

THR 165 0.46 SER 224 -0.05 ASP 315

THR 165 0.40 ASP 225 -0.06 ASP 315

GLN 59 0.45 LEU 226 -0.07 ASP 315

GLN 59 0.51 PRO 227 -0.05 THR 265

GLN 59 0.41 ALA 228 -0.07 THR 265

GLN 59 0.39 LYS 229 -0.09 THR 265

ASP 60 0.45 ALA 230 -0.07 LYS 314

ASP 60 0.42 LEU 231 -0.07 LYS 314

ASP 60 0.34 VAL 232 -0.11 THR 265

ASP 60 0.36 ASP 233 -0.10 LYS 314

ASP 60 0.39 ALA 234 -0.14 GLY 235

ASP 60 0.28 GLY 235 -0.14 ALA 234

ASP 60 0.29 TYR 236 -0.07 LEU 310

ASP 60 0.20 ASP 237 -0.12 LEU 310

ASP 60 0.21 GLY 238 -0.09 LEU 310

GLN 59 0.25 ILE 239 -0.05 VAL 217

GLN 59 0.21 VAL 240 -0.06 PRO 274

THR 165 0.26 SER 241 -0.05 ILE 239

THR 165 0.31 ALA 242 -0.07 ILE 216

THR 165 0.28 GLY 243 -0.04 GLY 247

ASN 164 0.28 VAL 244 -0.04 ILE 216

THR 163 0.20 GLY 245 -0.04 LYS 22

GLY 42 0.14 ASN 246 -0.06 LYS 22

THR 165 0.17 GLY 247 -0.04 GLY 243

THR 165 0.22 ASN 248 -0.05 TYR 220

THR 165 0.28 LEU 249 -0.06 TYR 220

THR 165 0.34 TYR 250 -0.06 VAL 284

THR 165 0.31 LYS 251 -0.08 VAL 284

THR 165 0.34 THR 252 -0.06 PRO 316

THR 165 0.34 VAL 253 -0.06 PRO 316

THR 165 0.28 PHE 254 -0.07 PRO 316

THR 165 0.27 ASP 255 -0.09 PRO 316

GLN 59 0.29 THR 256 -0.09 PRO 316

GLN 59 0.27 LEU 257 -0.10 PRO 316

GLN 59 0.22 ALA 258 -0.13 PRO 316

GLN 59 0.24 THR 259 -0.12 PRO 316

GLN 59 0.26 ALA 260 -0.12 ASP 315

GLN 59 0.20 ALA 261 -0.18 PRO 316

ASP 60 0.18 LYS 262 -0.21 PRO 316

ASP 60 0.21 ASN 263 -0.16 ASP 315

ASP 60 0.17 GLY 264 -0.17 LYS 314

ASP 60 0.21 THR 265 -0.11 LYS 314

ASP 60 0.17 ALA 266 -0.09 ILE 319

GLN 59 0.19 VAL 267 -0.06 GLN 320

THR 165 0.15 VAL 268 -0.04 ILE 322

THR 165 0.16 ARG 269 -0.04 LYS 22

THR 165 0.16 SER 270 -0.06 LYS 22

THR 163 0.23 SER 271 -0.06 ILE 216

THR 163 0.41 ARG 272 -0.09 ILE 216

PRO 274 0.41 VAL 273 -0.08 LYS 22

VAL 273 0.41 PRO 274 -0.19 ASN 298

ASN 175 0.23 THR 275 -0.14 ASN 298

GLY 42 0.15 GLY 276 -0.12 LYS 22

GLY 42 0.14 ALA 277 -0.10 LYS 22

GLY 42 0.14 THR 278 -0.08 LYS 22

GLY 42 0.12 THR 279 -0.09 TYR 176

GLY 42 0.11 GLN 280 -0.10 TYR 176

GLY 42 0.10 ASP 281 -0.10 TYR 176

GLY 42 0.11 ALA 282 -0.07 TYR 176

THR 165 0.13 GLU 283 -0.07 LYS 251

THR 165 0.14 VAL 284 -0.08 LYS 251

THR 165 0.12 ASP 285 -0.09 ASN 324

THR 165 0.12 ASP 286 -0.11 ASN 324

GLN 59 0.10 ALA 287 -0.15 ASN 324

GLN 59 0.13 LYS 288 -0.12 GLN 321

GLN 59 0.16 TYR 289 -0.11 GLN 320

GLN 59 0.14 GLY 290 -0.16 GLN 317

GLN 59 0.15 PHE 291 -0.13 GLN 320

GLY 42 0.13 VAL 292 -0.10 PHE 291

GLY 42 0.13 ALA 293 -0.06 LYS 22

GLY 42 0.14 SER 294 -0.08 LYS 22

GLY 42 0.15 GLY 295 -0.09 LYS 22

GLY 42 0.16 THR 296 -0.10 LYS 22

GLY 42 0.16 LEU 297 -0.10 LYS 22

THR 161 0.19 ASN 298 -0.19 PRO 274

ALA 242 0.21 PRO 299 -0.17 PRO 274

VAL 217 0.25 GLN 300 -0.16 PRO 274

GLY 42 0.16 LYS 301 -0.13 PRO 274

GLY 42 0.16 ALA 302 -0.11 PRO 274

GLY 42 0.15 ARG 303 -0.13 PRO 274

GLY 42 0.16 VAL 304 -0.10 PRO 274

GLY 42 0.15 LEU 305 -0.09 LYS 22

GLY 42 0.14 LEU 306 -0.08 PRO 274

GLY 42 0.14 GLN 307 -0.09 PRO 274

GLY 42 0.15 LEU 308 -0.08 LYS 22

GLY 42 0.14 ALA 309 -0.09 ASP 237

GLY 42 0.13 LEU 310 -0.12 ASP 237

GLY 42 0.14 THR 311 -0.10 ASP 237

GLY 42 0.13 GLN 312 -0.11 GLY 264

GLY 42 0.12 THR 313 -0.13 PRO 202

GLY 42 0.12 LYS 314 -0.17 GLY 264

GLY 42 0.11 ASP 315 -0.20 LYS 262

GLY 42 0.12 PRO 316 -0.21 LYS 262

GLY 42 0.11 GLN 317 -0.18 LYS 262

GLY 42 0.12 GLN 318 -0.15 LYS 262

GLY 42 0.13 ILE 319 -0.14 LYS 262

GLY 42 0.13 GLN 320 -0.15 GLY 290

GLY 42 0.13 GLN 321 -0.15 ALA 287

GLY 42 0.14 ILE 322 -0.12 LYS 262

GLY 42 0.15 PHE 323 -0.10 ALA 287

GLY 42 0.14 ASN 324 -0.15 ALA 287

GLY 42 0.16 GLN 325 -0.14 ALA 287

GLY 42 0.17 TYR 326 -0.10 ALA 287

PRO 227 0.20 GLN 1 -0.08 GLY 27

PRO 227 0.20 VAL 2 -0.07 VAL 48

PRO 227 0.18 GLN 3 -0.08 ILE 45

PRO 227 0.19 LEU 4 -0.04 ILE 45

LYS 79 0.19 VAL 5 -0.03 MET 121

LYS 79 0.19 GLU 6 -0.05 MET 121

LYS 79 0.21 SER 7 -0.05 MET 121

LYS 79 0.19 GLY 8 -0.06 MET 121

LYS 79 0.23 GLY 9 -0.07 MET 121

ASP 78 0.25 GLY 10 -0.08 ARG 19

LEU 1 0.25 LEU 11 -0.07 MET 121

LEU 1 0.23 VAL 12 -0.08 MET 121

LEU 1 0.22 GLN 13 -0.09 MET 121

LEU 1 0.22 PRO 14 -0.10 MET 121

LEU 1 0.19 GLY 15 -0.11 MET 121

LEU 1 0.19 GLY 16 -0.10 MET 121

LEU 1 0.18 SER 17 -0.10 THR 56

LEU 1 0.18 LEU 18 -0.09 THR 56

LYS 79 0.14 ARG 19 -0.08 GLY 10

LYS 79 0.16 LEU 20 -0.07 MET 121

PRO 227 0.14 SER 21 -0.06 MET 121

PRO 227 0.16 CYS 22 -0.05 MET 121

PRO 227 0.16 ALA 23 -0.03 MET 121

PRO 227 0.17 ALA 24 -0.04 ILE 45

PRO 227 0.17 SER 25 -0.06 ILE 45

PRO 227 0.19 GLY 26 -0.07 GLN 1

PRO 227 0.19 GLY 27 -0.08 GLN 1

LEU 226 0.17 ASP 28 -0.13 ASN 55

LEU 226 0.16 PHE 29 -0.10 ASN 55

LEU 226 0.15 ARG 30 -0.14 ASN 55

LEU 226 0.18 THR 31 -0.15 ASN 55

LEU 226 0.18 TYR 32 -0.09 ASN 55

LEU 226 0.18 SER 33 -0.08 GLY 57

LEU 226 0.17 LEU 34 -0.07 MET 121

PRO 227 0.17 GLY 35 -0.09 MET 121

PRO 227 0.16 TRP 36 -0.10 MET 121

LEU 1 0.18 PHE 37 -0.10 MET 121

LEU 1 0.25 ARG 38 -0.10 MET 121

LEU 1 0.34 GLN 39 -0.09 MET 121

LEU 1 0.35 ALA 40 -0.09 MET 121

LEU 1 0.42 PRO 41 -0.07 MET 121

LEU 1 0.41 GLY 42 -0.07 MET 121

LEU 1 0.31 GLN 43 -0.10 MET 121

ASP 44 0.29 GLY 44 -0.09 MET 121

LEU 1 0.23 LEU 45 -0.10 MET 121

PRO 40 0.21 GLU 46 -0.13 MET 121

PRO 40 0.18 ALA 47 -0.14 MET 121

LEU 1 0.15 VAL 48 -0.14 MET 121

LEU 226 0.15 ALA 49 -0.13 MET 121

LEU 226 0.16 ALA 50 -0.12 MET 121

LEU 226 0.15 ILE 51 -0.10 PRO 117

LEU 226 0.16 SER 52 -0.11 GLY 57

LEU 226 0.16 SER 53 -0.13 GLY 57

LEU 226 0.14 ASP 54 -0.14 GLY 57

LEU 226 0.13 GLY 55 -0.12 GLY 57

LEU 226 0.13 THR 56 -0.14 THR 69

LEU 226 0.14 THR 57 -0.17 THR 58

LEU 226 0.13 THR 58 -0.20 LYS 29

LEU 226 0.14 TYR 59 -0.18 MET 121

LEU 226 0.14 TYR 60 -0.16 MET 121

LEU 226 0.14 ALA 61 -0.18 MET 121

LYS 186 0.13 ASP 62 -0.18 MET 121

LEU 1 0.17 SER 63 -0.15 MET 121

LEU 1 0.16 VAL 64 -0.15 MET 121

LEU 1 0.13 LYS 65 -0.17 MET 121

LEU 1 0.12 GLY 66 -0.16 MET 121

LEU 1 0.15 ARG 67 -0.14 MET 121

LEU 1 0.15 PHE 68 -0.13 MET 121

LEU 1 0.12 THR 69 -0.15 THR 57

LEU 226 0.13 ILE 70 -0.10 MET 121

LEU 226 0.13 SER 71 -0.11 GLN 82

LEU 226 0.13 ARG 72 -0.09 GLY 57

LEU 226 0.13 ASP 73 -0.09 GLY 57

LEU 226 0.13 ASN 74 -0.11 ASN 55

LEU 226 0.12 SER 75 -0.10 ASN 55

LEU 226 0.13 LYS 76 -0.07 ASN 55

LEU 226 0.14 ASN 77 -0.07 ASN 55

LEU 226 0.14 THR 78 -0.05 GLY 57

LEU 226 0.14 LEU 79 -0.06 GLY 57

LEU 226 0.13 TYR 80 -0.07 MET 121

LEU 226 0.13 LEU 81 -0.09 MET 121

LEU 1 0.14 GLN 82 -0.11 THR 56

LEU 1 0.17 MET 83 -0.11 MET 121

LEU 1 0.16 ASN 84 -0.12 MET 121

LEU 1 0.18 SER 85 -0.12 MET 121

LEU 1 0.21 LEU 86 -0.11 MET 121

LEU 1 0.23 ARG 87 -0.11 MET 121

LEU 1 0.25 ALA 88 -0.10 MET 121

LEU 1 0.26 GLU 89 -0.10 MET 121

LEU 1 0.25 ASP 90 -0.11 MET 121

LEU 1 0.29 THR 91 -0.09 MET 121

LEU 1 0.33 ALA 92 -0.08 MET 121

LEU 1 0.35 VAL 93 -0.07 MET 121

LEU 1 0.25 TYR 94 -0.08 MET 121

ASN 3 0.23 TYR 95 -0.07 MET 121

PRO 227 0.18 CYS 96 -0.07 MET 121

PRO 227 0.19 ALA 97 -0.06 MET 121

PRO 227 0.19 ALA 98 -0.04 MET 121

PRO 227 0.20 LEU 99 -0.04 MET 121

PRO 227 0.21 GLY 100 -0.06 TYR 32

PRO 227 0.24 GLU 101 -0.09 GLY 17

PRO 227 0.25 ASN 102 -0.06 VAL 84

PRO 227 0.23 TYR 103 -0.05 VAL 48

PRO 227 0.22 LEU 104 -0.06 ILE 45

PRO 227 0.20 ALA 105 -0.06 ILE 45

PRO 227 0.20 TRP 106 -0.05 GLN 3

LYS 79 0.22 GLY 107 -0.06 PRO 40

LYS 79 0.30 GLN 108 -0.07 PRO 40

ASN 3 0.31 GLY 109 -0.05 GLN 43

LYS 79 0.27 THR 110 -0.06 MET 121

LEU 1 0.30 LEU 111 -0.06 MET 121

LEU 1 0.28 VAL 112 -0.08 MET 121

LEU 1 0.29 THR 113 -0.07 MET 121

LEU 1 0.26 VAL 114 -0.09 MET 121

LEU 1 0.26 SER 115 -0.08 MET 121

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.

*** 1FC7C6F2933742E0 ***

CA distance fluctuations for 2605201334553922152

--- 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.

* 1FC7C6F2933742E0 *