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

* secYG_ALPHAFLOD *

CA distance fluctuations for 260812051709481561

--- normal mode 31 ---

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 425 0.68 MET 1 -0.39 PHE 12

TRP 429 0.25 ASN 2 -0.40 ASN 8

GLY 7 0.33 VAL 3 -0.26 ALA 5

LEU 211 0.26 GLY 4 -0.51 GLY 417

LEU 214 0.26 ALA 5 -0.39 ASN 8

LEU 214 0.28 ARG 6 -0.24 GLY 417

VAL 3 0.33 GLY 7 -0.22 ALA 5

LEU 214 0.31 ASN 8 -0.40 ASN 2

LEU 214 0.30 ALA 9 -0.35 MET 1

PRO 259 0.32 GLY 10 -0.23 LYS 174

PRO 259 0.36 LEU 11 -0.26 ASN 2

PRO 259 0.34 PHE 12 -0.39 MET 1

PRO 259 0.34 TRP 13 -0.29 MET 1

PRO 259 0.39 ARG 14 -0.22 ASN 2

PRO 259 0.39 PHE 15 -0.28 MET 1

PRO 259 0.35 GLY 16 -0.31 MET 1

PRO 259 0.36 PHE 17 -0.24 MET 1

PRO 259 0.39 THR 18 -0.22 MET 1

PRO 259 0.37 LEU 19 -0.26 MET 1

PRO 259 0.34 LEU 20 -0.24 MET 1

PRO 259 0.35 ALA 21 -0.20 MET 1

LYS 261 0.35 LEU 22 -0.21 MET 1

PRO 259 0.32 ILE 23 -0.22 MET 1

PRO 259 0.30 VAL 24 -0.19 MET 1

LYS 261 0.30 TYR 25 -0.18 MET 1

LYS 261 0.31 ARG 26 -0.19 MET 1

ARG 235 0.28 LEU 27 -0.18 MET 1

LYS 261 0.27 GLY 28 -0.16 MET 1

PRO 193 0.28 THR 29 -0.16 MET 1

PRO 193 0.34 TYR 30 -0.17 SER 46

PRO 193 0.31 ILE 31 -0.14 GLU 42

SER 194 0.31 PRO 32 -0.15 PRO 38

SER 194 0.26 ILE 33 -0.17 GLU 207

SER 194 0.28 PRO 34 -0.15 SER 156

SER 194 0.28 GLY 35 -0.17 GLU 207

SER 194 0.30 VAL 36 -0.20 GLU 207

SER 194 0.36 ASN 37 -0.17 GLU 207

SER 194 0.44 PRO 38 -0.15 PRO 32

SER 194 0.48 SER 39 -0.13 MET 1

GLY 289 0.34 VAL 40 -0.24 GLU 207

GLY 289 0.36 VAL 41 -0.29 GLU 207

SER 194 0.40 GLU 42 -0.23 GLU 207

GLY 289 0.40 ASP 43 -0.31 GLU 207

GLY 289 0.47 ILE 44 -0.43 GLU 207

GLY 289 0.41 ILE 45 -0.41 GLU 207

GLY 289 0.38 SER 46 -0.37 GLU 207

GLY 289 0.45 SER 47 -0.59 GLU 207

GLY 289 0.43 HIS 48 -0.57 GLU 207

GLY 289 0.29 ALA 49 -0.44 GLU 207

GLU 354 0.27 THR 50 -0.52 GLU 207

GLU 354 0.28 GLY 51 -0.44 GLU 207

GLU 354 0.28 VAL 52 -0.35 GLU 207

ASP 357 0.28 LEU 53 -0.36 GLU 207

ASP 357 0.28 GLY 54 -0.34 GLU 207

ASP 357 0.30 ILE 55 -0.28 GLU 207

ASP 357 0.30 PHE 56 -0.26 GLU 207

ASP 357 0.28 ASN 57 -0.25 GLU 207

ASP 357 0.30 VAL 58 -0.21 GLU 207

ASP 357 0.32 PHE 59 -0.18 GLU 207

ASP 357 0.30 SER 60 -0.19 GLU 207

ASP 357 0.31 GLY 61 -0.18 MET 1

SER 194 0.29 GLY 62 -0.21 GLU 207

ASP 357 0.27 ALA 63 -0.20 GLU 207

ASP 357 0.27 LEU 64 -0.25 GLU 207

SER 194 0.34 GLY 65 -0.26 GLU 207

SER 194 0.36 ARG 66 -0.20 GLU 207

SER 194 0.27 MET 67 -0.23 GLU 207

SER 194 0.27 THR 68 -0.18 GLU 207

ASP 357 0.24 ILE 69 -0.17 GLU 207

ASP 357 0.26 PHE 70 -0.17 GLU 207

ASP 357 0.26 ALA 71 -0.22 GLU 207

ASP 357 0.26 LEU 72 -0.22 GLU 207

ASP 357 0.29 ASN 73 -0.18 GLU 207

ASP 357 0.32 VAL 74 -0.16 GLU 207

ASP 357 0.30 MET 75 -0.19 GLU 207

ASP 357 0.26 PRO 76 -0.20 GLU 207

ASP 357 0.29 TYR 77 -0.16 GLU 207

ASP 357 0.32 ILE 78 -0.17 ASN 2

ASP 357 0.27 VAL 79 -0.19 GLU 207

GLU 354 0.25 SER 80 -0.17 ALA 5

ASP 357 0.30 SER 81 -0.19 GLN 409

ASP 357 0.31 ILE 82 -0.18 ASP 405

GLU 354 0.27 ILE 83 -0.17 GLU 207

GLU 354 0.26 VAL 84 -0.17 ALA 5

GLU 354 0.30 GLN 85 -0.16 ALA 5

GLU 354 0.32 LEU 86 -0.14 ALA 5

LYS 350 0.29 LEU 87 -0.16 ILE 147

LYS 350 0.29 SER 88 -0.14 ALA 5

LYS 350 0.36 VAL 89 -0.14 SER 290

LYS 350 0.35 ALA 90 -0.19 SER 290

LYS 350 0.30 ILE 91 -0.18 SER 290

LYS 350 0.29 PRO 92 -0.17 SER 290

THR 246 0.26 THR 93 -0.14 SER 290

LYS 330 0.25 LEU 94 -0.12 ALA 5

LYS 330 0.32 ASN 95 -0.11 SER 290

THR 246 0.28 GLU 96 -0.10 SER 290

THR 246 0.25 MET 97 -0.11 ALA 5

ASP 328 0.30 ARG 98 -0.13 ALA 5

GLU 331 0.35 GLN 99 -0.10 ALA 5

GLU 331 0.31 ASP 100 -0.09 MET 97

ASP 328 0.38 GLY 101 -0.09 ALA 5

ALA 173 0.46 GLU 102 -0.11 ALA 5

ALA 173 0.35 LEU 103 -0.10 ALA 5

ASP 328 0.29 GLY 104 -0.12 ALA 5

ASP 328 0.34 ARG 105 -0.17 ALA 5

GLU 169 0.31 MET 106 -0.18 GLY 7

ASP 328 0.24 LYS 107 -0.16 ALA 5

ASP 328 0.26 MET 108 -0.18 ALA 5

ASP 328 0.28 SER 109 -0.21 GLY 7

ASP 328 0.23 THR 110 -0.19 GLY 7

ASP 328 0.20 TYR 111 -0.18 ALA 5

ASP 357 0.24 THR 112 -0.18 ALA 5

ASP 328 0.22 ARG 113 -0.18 ALA 5

GLU 354 0.19 TYR 114 -0.16 ALA 5

GLU 354 0.20 LEU 115 -0.17 GLU 207

ASP 357 0.23 SER 116 -0.18 GLU 207

ASP 357 0.20 VAL 117 -0.18 GLU 207

GLU 354 0.17 ALA 118 -0.20 GLU 207

GLU 354 0.19 PHE 119 -0.21 GLU 207

ASP 357 0.20 CYS 120 -0.22 GLU 207

GLU 354 0.17 ILE 121 -0.22 GLU 207

GLU 354 0.15 ALA 122 -0.27 SER 279

GLU 354 0.18 GLN 123 -0.31 SER 279

GLU 354 0.18 GLY 124 -0.27 GLU 207

GLU 354 0.14 LEU 125 -0.28 GLU 207

GLU 354 0.15 VAL 126 -0.41 SER 282

GLY 289 0.18 ILE 127 -0.34 GLU 207

GLU 354 0.16 LEU 128 -0.32 GLU 207

GLY 247 0.13 LEU 129 -0.36 GLU 207

GLY 289 0.24 GLY 130 -0.42 GLU 207

GLY 289 0.24 LEU 131 -0.37 GLU 207

GLU 354 0.14 GLU 132 -0.36 GLU 207

GLY 289 0.24 ARG 133 -0.41 GLU 207

GLY 289 0.39 MET 134 -0.44 GLU 207

GLY 289 0.26 ASN 135 -0.39 GLU 207

GLY 289 0.30 SER 136 -0.47 GLU 207

GLY 289 0.19 ASP 137 -0.40 GLU 207

GLY 289 0.32 GLU 138 -0.38 GLU 207

GLY 289 0.33 VAL 139 -0.34 GLU 207

SER 197 0.24 MET 140 -0.27 GLU 207

GLY 289 0.26 VAL 141 -0.28 GLU 207

SER 194 0.24 VAL 142 -0.25 GLU 207

SER 197 0.27 ILE 143 -0.19 GLU 207

SER 194 0.23 ASN 144 -0.22 GLU 207

SER 194 0.18 PRO 145 -0.27 GLU 207

ILE 33 0.16 GLY 146 -0.26 GLU 207

VAL 24 0.15 ILE 147 -0.27 ARG 285

VAL 24 0.20 MET 148 -0.20 SER 301

ILE 33 0.24 PHE 149 -0.21 GLU 207

ILE 33 0.18 ARG 150 -0.25 GLU 207

VAL 24 0.17 VAL 151 -0.22 SER 301

VAL 24 0.23 VAL 152 -0.18 GLU 207

SER 194 0.19 GLY 153 -0.21 GLU 207

ASP 357 0.16 ILE 154 -0.22 GLU 207

PRO 259 0.18 SER 155 -0.18 GLU 207

PRO 259 0.22 SER 156 -0.17 GLU 207

ASP 357 0.22 LEU 157 -0.20 GLU 207

ASP 357 0.21 LEU 158 -0.18 GLU 207

PRO 259 0.24 ALA 159 -0.15 GLU 207

PRO 259 0.25 GLY 160 -0.15 GLU 207

ASP 357 0.27 THR 161 -0.16 GLU 207

VAL 326 0.26 MET 162 -0.14 GLU 207

PRO 259 0.28 PHE 163 -0.13 GLU 207

VAL 326 0.30 LEU 164 -0.13 MET 1

VAL 326 0.33 LEU 165 -0.14 ALA 5

GLU 102 0.32 TRP 166 -0.14 ALA 5

PRO 259 0.34 LEU 167 -0.14 MET 1

PRO 259 0.38 GLY 168 -0.15 ALA 5

GLU 102 0.43 GLU 169 -0.18 ALA 5

GLU 102 0.40 ARG 170 -0.18 ALA 5

PRO 259 0.42 ILE 171 -0.18 ALA 5

PRO 259 0.46 ASN 172 -0.21 ALA 5

GLU 102 0.46 ALA 173 -0.23 ALA 5

PRO 259 0.42 LYS 174 -0.23 ALA 5

PRO 259 0.42 GLY 175 -0.21 ALA 5

PRO 259 0.47 ILE 176 -0.21 ASN 2

PRO 259 0.51 GLY 177 -0.21 ASN 178

PRO 259 0.48 ASN 178 -0.21 GLY 177

PRO 259 0.41 GLY 179 -0.19 ASN 2

VAL 326 0.42 ILE 180 -0.17 ASN 2

LYS 261 0.43 SER 181 -0.18 ASN 2

LYS 261 0.41 LEU 182 -0.19 ASN 2

LYS 261 0.35 ILE 183 -0.18 MET 1

LYS 261 0.34 ILE 184 -0.17 ASN 2

LYS 261 0.36 PHE 185 -0.19 ASN 2

LYS 261 0.32 VAL 186 -0.22 MET 1

LYS 261 0.30 GLY 187 -0.20 MET 1

ASP 357 0.30 ILE 188 -0.19 MET 1

LEU 214 0.31 ILE 189 -0.22 MET 1

LEU 214 0.28 SER 190 -0.23 MET 1

PRO 38 0.27 GLU 191 -0.21 MET 1

LEU 214 0.33 LEU 192 -0.21 MET 1

SER 39 0.40 PRO 193 -0.23 MET 1

SER 39 0.48 SER 194 -0.22 MET 1

SER 39 0.36 SER 195 -0.19 MET 1

SER 39 0.36 ILE 196 -0.18 MET 1

SER 39 0.47 SER 197 -0.20 MET 1

SER 39 0.37 SER 198 -0.19 MET 1

SER 39 0.26 VAL 199 -0.21 GLU 303

SER 39 0.33 PHE 200 -0.20 ILE 305

SER 39 0.32 LEU 201 -0.16 TYR 299

GLY 345 0.21 LEU 202 -0.32 HIS 48

GLY 345 0.21 GLY 203 -0.37 TYR 384

SER 39 0.24 LYS 204 -0.26 TYR 299

GLY 345 0.20 ASN 205 -0.34 SER 47

GLY 345 0.22 GLY 206 -0.42 ARG 298

GLY 345 0.23 GLU 207 -0.59 SER 47

GLY 345 0.24 VAL 208 -0.52 GLU 303

SER 255 0.24 SER 209 -0.64 TYR 384

ASN 8 0.27 GLY 210 -0.55 TYR 384

ASN 8 0.29 LEU 211 -0.64 TYR 384

SER 215 0.26 VAL 212 -0.88 TYR 384

ARG 232 0.26 VAL 213 -0.56 TYR 384

LEU 192 0.33 LEU 214 -0.48 TYR 384

LEU 225 0.28 SER 215 -0.58 TYR 384

GLY 345 0.26 MET 216 -0.56 VAL 381

LEU 192 0.33 LEU 217 -0.32 ILE 305

PHE 221 0.33 LEU 218 -0.35 ILE 305

GLY 345 0.26 ALA 219 -0.42 VAL 377

GLY 345 0.27 PHE 220 -0.27 ILE 305

LEU 214 0.33 PHE 221 -0.23 ILE 305

ARG 232 0.28 ALA 222 -0.30 ILE 305

GLY 345 0.28 LEU 223 -0.22 ILE 305

ARG 232 0.29 PHE 224 -0.16 ILE 305

ARG 232 0.34 LEU 225 -0.16 ILE 305

GLY 345 0.28 LEU 226 -0.15 TRP 292

ARG 235 0.31 ILE 227 -0.13 TRP 292

ARG 232 0.39 ILE 228 -0.11 TRP 292

ARG 235 0.31 PHE 229 -0.12 TRP 292

ARG 235 0.38 PHE 230 -0.13 TRP 292

ARG 235 0.40 GLU 231 -0.14 GLY 266

ASN 404 0.54 ARG 232 -0.19 ASN 263

SER 408 0.49 SER 233 -0.13 GLY 367

SER 408 0.63 TYR 234 -0.15 LEU 366

SER 408 0.55 ARG 235 -0.15 PRO 259

SER 408 0.57 LYS 236 -0.08 ILE 258

PHE 238 0.58 VAL 237 -0.07 ILE 258

VAL 237 0.58 PHE 238 -0.11 TYR 257

ARG 244 0.36 VAL 239 -0.09 SER 256

ARG 244 0.45 GLN 240 -0.13 SER 255

ARG 244 0.49 TYR 241 -0.12 SER 426

ARG 244 0.47 PRO 242 -0.22 SER 426

GLN 245 0.30 LYS 243 -0.31 SER 426

GLY 340 0.51 ARG 244 -0.28 SER 426

GLY 340 0.32 GLN 245 -0.14 SER 426

ASN 339 0.48 THR 246 -0.05 TRP 429

ASN 339 0.40 GLY 247 0.00 MET 1

ASN 339 0.29 GLY 248 -0.00 ARG 249

ASP 254 0.32 ARG 249 -0.05 SER 426

ARG 362 0.25 PHE 250 -0.17 SER 426

SER 253 0.57 TYR 251 -0.26 SER 426

PRO 344 0.34 ASN 252 -0.34 SER 426

TYR 251 0.57 SER 253 -0.19 SER 426

TYR 251 0.48 ASP 254 -0.09 TYR 241

LYS 236 0.42 SER 255 -0.13 GLN 240

THR 412 0.44 SER 256 -0.10 PHE 238

THR 412 0.53 TYR 257 -0.11 PHE 238

GLN 409 0.54 ILE 258 -0.12 ARG 235

GLN 409 0.62 PRO 259 -0.15 ARG 235

GLN 409 0.48 LEU 260 -0.06 ARG 232

ASP 405 0.53 LYS 261 -0.10 ARG 232

ARG 235 0.34 ILE 262 -0.14 ARG 232

SER 181 0.37 ASN 263 -0.19 ARG 232

SER 181 0.42 THR 264 -0.17 ARG 232

ASP 357 0.44 ALA 265 -0.17 ARG 232

SER 181 0.42 GLY 266 -0.14 GLU 231

SER 181 0.34 VAL 267 -0.14 ASN 2

ASP 357 0.34 ILE 268 -0.18 ASP 405

ASP 357 0.41 PRO 269 -0.13 ASN 2

ASP 357 0.36 PRO 270 -0.14 ASN 2

ASP 357 0.35 ILE 271 -0.19 VAL 402

ASP 357 0.35 PHE 272 -0.16 ASP 405

ASP 357 0.35 ALA 273 -0.19 VAL 212

ASP 357 0.33 ASN 274 -0.22 VAL 212

ASP 357 0.31 ALA 275 -0.20 GLU 207

GLU 354 0.31 LEU 276 -0.22 VAL 212

GLU 354 0.30 LEU 277 -0.28 VAL 212

GLU 354 0.28 LEU 278 -0.27 GLU 207

GLU 354 0.27 SER 279 -0.32 VAL 126

GLU 354 0.24 SER 280 -0.29 VAL 212

GLU 354 0.24 ILE 281 -0.33 VAL 212

GLU 354 0.24 SER 282 -0.41 VAL 126

GLU 354 0.20 LEU 283 -0.29 GLU 207

GLU 354 0.18 VAL 284 -0.34 VAL 212

ILE 45 0.24 ARG 285 -0.34 LEU 129

ILE 44 0.25 PHE 286 -0.29 GLU 207

ILE 44 0.28 HIS 287 -0.28 SER 209

ILE 44 0.38 SER 288 -0.28 SER 209

ILE 44 0.47 GLY 289 -0.22 SER 209

ILE 44 0.34 SER 290 -0.29 SER 209

SER 47 0.29 GLU 291 -0.35 SER 209

ILE 44 0.19 TRP 292 -0.42 VAL 212

HIS 48 0.23 ALA 293 -0.37 SER 209

HIS 48 0.28 ASP 294 -0.39 SER 209

GLU 354 0.19 VAL 295 -0.49 SER 209

GLU 354 0.21 LEU 296 -0.47 VAL 212

GLU 354 0.24 LEU 297 -0.44 SER 209

GLU 354 0.24 ARG 298 -0.53 SER 209

GLU 354 0.26 TYR 299 -0.56 VAL 212

GLU 354 0.27 LEU 300 -0.46 VAL 212

GLU 354 0.25 SER 301 -0.43 VAL 212

GLU 354 0.28 SER 302 -0.44 VAL 212

GLU 354 0.28 GLU 303 -0.57 VAL 212

GLU 354 0.26 GLY 304 -0.58 VAL 212

GLU 354 0.27 ILE 305 -0.59 VAL 212

GLU 354 0.29 LEU 306 -0.48 VAL 212

GLU 354 0.30 TYR 307 -0.42 VAL 212

GLU 354 0.30 VAL 308 -0.40 VAL 212

GLU 354 0.33 SER 309 -0.37 TRP 292

GLU 354 0.34 VAL 310 -0.36 TRP 292

GLU 354 0.34 TYR 311 -0.28 VAL 212

GLU 354 0.36 ILE 312 -0.27 TRP 292

GLU 354 0.39 ALA 313 -0.30 TRP 292

GLU 354 0.38 LEU 314 -0.21 TRP 292

ASP 357 0.40 ILE 315 -0.17 TRP 292

ASP 357 0.44 MET 316 -0.20 TRP 292

GLU 354 0.46 PHE 317 -0.20 TRP 292

ASP 357 0.45 PHE 318 -0.13 ALA 90

ASP 357 0.49 THR 319 -0.13 ALA 368

ASP 357 0.62 PHE 320 -0.15 TRP 292

ASP 357 0.53 PHE 321 -0.12 ALA 90

ASP 357 0.42 TYR 322 -0.13 ARG 232

ASP 357 0.54 THR 323 -0.14 ARG 232

ASP 357 0.58 SER 324 -0.13 THR 364

ASP 357 0.32 LEU 325 -0.11 ARG 232

ILE 180 0.42 VAL 326 -0.13 ARG 232

ASN 178 0.42 PHE 327 -0.18 GLY 361

ASN 178 0.42 ASP 328 -0.20 GLY 361

SER 324 0.40 THR 329 -0.09 GLN 358

SER 324 0.35 LYS 330 -0.09 GLU 331

GLN 99 0.35 GLU 331 -0.09 LYS 330

THR 246 0.33 THR 332 -0.07 ARG 232

ARG 244 0.32 SER 333 -0.04 ARG 232

THR 246 0.30 GLU 334 -0.09 GLY 4

THR 246 0.36 MET 335 -0.11 ARG 232

THR 246 0.38 LEU 336 -0.07 ARG 232

ARG 244 0.37 LYS 337 -0.11 GLY 4

THR 246 0.38 LYS 338 -0.17 GLY 4

THR 246 0.48 ASN 339 -0.16 GLY 4

ARG 244 0.51 GLY 340 -0.14 GLY 4

ARG 244 0.47 GLY 341 -0.07 GLY 4

ARG 244 0.39 PHE 342 -0.05 GLU 427

ARG 244 0.37 VAL 343 -0.08 PHE 238

ARG 362 0.39 PRO 344 -0.09 ARG 347

ARG 362 0.44 GLY 345 -0.10 ARG 347

ARG 362 0.37 LYS 346 -0.09 PHE 238

PHE 320 0.32 ARG 347 -0.10 GLY 345

ARG 244 0.35 PRO 348 -0.08 GLU 334

SER 324 0.31 GLY 349 -0.08 LYS 346

SER 324 0.40 LYS 350 -0.07 LYS 346

PHE 320 0.42 ALA 351 -0.09 LYS 346

PHE 320 0.36 THR 352 -0.06 PHE 238

SER 324 0.48 LYS 353 -0.03 GLU 331

PHE 320 0.55 GLU 354 -0.15 TYR 355

GLY 361 0.45 TYR 355 -0.15 GLU 354

PHE 320 0.42 PHE 356 -0.03 ILE 258

PHE 320 0.62 ASP 357 -0.22 GLN 358

GLY 361 0.62 GLN 358 -0.22 ASP 357

GLY 345 0.36 VAL 359 -0.09 ASP 357

ALA 265 0.39 ILE 360 -0.18 GLY 361

GLN 358 0.62 GLY 361 -0.20 ASP 328

GLY 345 0.44 ARG 362 -0.12 ASP 328

GLY 367 0.36 ILE 363 -0.10 TRP 292

ASP 357 0.42 THR 364 -0.13 SER 324

GLN 358 0.45 VAL 365 -0.16 TRP 292

GLY 345 0.38 LEU 366 -0.16 TRP 292

GLN 358 0.36 GLY 367 -0.13 TRP 292

GLN 358 0.39 ALA 368 -0.16 TRP 292

GLN 358 0.36 ILE 369 -0.19 TRP 292

GLY 345 0.35 TYR 370 -0.17 TRP 292

ASP 357 0.34 LEU 371 -0.16 TRP 292

GLU 354 0.33 SER 372 -0.20 TRP 292

GLY 345 0.34 VAL 373 -0.24 ALA 222

GLY 345 0.31 VAL 374 -0.22 ALA 222

ASP 357 0.31 CYS 375 -0.19 ALA 219

GLY 345 0.30 VAL 376 -0.29 ALA 219

GLY 345 0.31 VAL 377 -0.42 ALA 219

GLY 345 0.28 PRO 378 -0.30 ALA 219

GLY 345 0.28 GLU 379 -0.35 VAL 212

GLY 345 0.30 ILE 380 -0.48 ILE 305

GLY 345 0.29 VAL 381 -0.56 MET 216

GLY 345 0.26 ARG 382 -0.50 VAL 212

GLY 345 0.27 HIS 383 -0.62 VAL 212

GLY 345 0.28 TYR 384 -0.88 VAL 212

GLY 345 0.28 CYS 385 -0.62 VAL 212

GLY 345 0.26 ALA 386 -0.52 GLU 303

GLY 345 0.25 VAL 387 -0.44 THR 50

GLY 345 0.24 SER 388 -0.35 GLU 207

GLY 345 0.24 PHE 389 -0.17 GLU 207

ASP 357 0.25 THR 390 -0.20 VAL 58

ASP 357 0.26 LEU 391 -0.17 MET 1

ASP 357 0.29 GLY 392 -0.15 ASN 2

ASP 357 0.31 GLY 393 -0.15 ALA 219

ASP 357 0.33 THR 394 -0.15 ASN 2

ASP 357 0.30 SER 395 -0.17 ASN 2

ILE 360 0.30 PHE 396 -0.16 ASN 2

ILE 360 0.34 LEU 397 -0.15 ASN 2

LYS 261 0.34 ILE 398 -0.18 VAL 402

LYS 261 0.34 ILE 399 -0.18 ASN 2

ARG 235 0.35 VAL 400 -0.16 ASN 2

LYS 261 0.46 ASN 401 -0.15 ILE 271

LYS 261 0.42 VAL 402 -0.19 ILE 271

ARG 232 0.38 ILE 403 -0.17 ASN 2

ARG 232 0.54 ASN 404 -0.16 ASN 2

LYS 261 0.53 ASP 405 -0.18 ILE 82

TYR 234 0.49 THR 406 -0.18 ASN 2

TYR 234 0.49 PHE 407 -0.20 ASN 2

TYR 234 0.63 SER 408 -0.19 SER 81

PRO 259 0.62 GLN 409 -0.19 SER 81

PRO 259 0.49 VAL 410 -0.22 ASN 2

LYS 236 0.49 GLN 411 -0.20 ASN 2

PRO 259 0.57 THR 412 -0.19 ALA 5

PRO 259 0.48 GLN 413 -0.28 ALA 5

LYS 236 0.39 VAL 414 -0.23 ALA 5

TYR 257 0.38 TYR 415 -0.18 GLY 4

TYR 257 0.41 SER 416 -0.32 GLY 4

TYR 257 0.33 GLY 417 -0.51 GLY 4

VAL 3 0.30 ARG 418 -0.31 GLY 4

GLY 247 0.28 TYR 419 -0.28 GLY 4

TYR 257 0.26 SER 420 -0.44 GLY 4

MET 1 0.32 ALA 421 -0.51 GLY 4

MET 1 0.44 LEU 422 -0.26 ASN 252

MET 1 0.42 MET 423 -0.30 ASN 252

MET 1 0.48 LYS 424 -0.38 GLY 4

MET 1 0.68 LYS 425 -0.29 ASN 252

MET 1 0.59 SER 426 -0.34 ASN 252

MET 1 0.54 GLU 427 -0.30 ASN 252

MET 1 0.65 LEU 428 -0.27 GLY 4

MET 1 0.68 TRP 429 -0.27 ASN 252

MET 1 0.53 LYS 430 -0.27 ARG 244

MET 1 0.51 LYS 431 -0.24 ARG 244

MET 1 0.56 VAL 432 -0.22 ARG 244

MET 1 0.49 LYS 433 -0.21 ARG 244

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.

*** secYG_ALPHAFLOD ***

CA distance fluctuations for 260812051709481561

--- normal mode 31 ---

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

* secYG_ALPHAFLOD *