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* 2647 *

CA distance fluctuations for 2605141238122666813

--- normal mode 11 ---

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 424 0.18 SER 44 -0.31 LYS 567

ASN 424 0.19 ALA 45 -0.35 LYS 567

ASN 424 0.20 ASP 46 -0.25 LYS 567

ASN 424 0.21 THR 47 -0.20 LYS 567

ASN 424 0.24 LEU 48 -0.14 LYS 567

ASN 424 0.25 VAL 49 -0.12 LYS 567

ASN 424 0.31 ALA 50 -0.10 SER 327

ASN 424 0.35 TYR 51 -0.15 THR 325

ASN 424 0.42 THR 52 -0.20 THR 525

ASN 424 0.48 GLY 53 -0.38 GLY 258

ASN 424 0.33 GLN 54 -0.29 PHE 322

ASN 424 0.27 SER 55 -0.32 ASP 397

PRO 67 0.16 GLY 56 -0.31 ASP 397

THR 144 0.12 ASP 57 -0.25 ASP 397

THR 144 0.12 TYR 58 -0.25 ASN 281

THR 252 0.08 GLN 59 -0.29 GLY 443

THR 252 0.07 ILE 60 -0.25 GLY 443

THR 252 0.07 ASN 61 -0.27 GLY 443

ASN 424 0.13 PHE 62 -0.23 GLY 445

ASN 424 0.13 ASN 63 -0.26 GLY 445

ASN 424 0.23 PRO 64 -0.27 GLY 445

ASN 424 0.22 PHE 65 -0.33 GLY 445

ASN 424 0.18 SER 66 -0.37 GLY 445

ASN 424 0.28 PRO 67 -0.47 GLY 445

SER 55 0.17 SER 68 -0.40 GLY 443

ASN 424 0.19 LYS 69 -0.32 GLY 443

ASN 424 0.20 ILE 70 -0.29 GLY 443

ASN 424 0.26 GLY 71 -0.20 GLY 445

ASN 424 0.24 GLY 72 -0.16 GLY 445

ASN 424 0.30 LEU 73 -0.17 ALA 446

ASN 424 0.29 GLY 74 -0.10 ALA 446

ASN 424 0.25 THR 75 -0.08 ALA 446

ASN 424 0.21 ILE 76 -0.10 ALA 446

ASN 424 0.22 TYR 77 -0.12 ALA 446

ASN 424 0.25 GLU 78 -0.09 ALA 446

ASN 424 0.27 SER 79 -0.08 ALA 446

ASN 424 0.26 LEU 80 -0.06 GLY 566

ASN 424 0.26 PHE 81 -0.09 PRO 67

ASN 424 0.28 PHE 82 -0.12 PRO 67

ASN 424 0.29 VAL 83 -0.17 PRO 67

ASN 424 0.29 THR 84 -0.23 PRO 67

ASN 424 0.26 ASN 85 -0.28 PRO 67

TRP 423 0.26 ALA 86 -0.21 PRO 67

ASN 424 0.23 ASN 87 -0.19 PRO 67

ASN 424 0.20 THR 88 -0.19 PRO 67

ASN 424 0.22 ASN 89 -0.13 PRO 67

ASN 424 0.22 ASP 90 -0.12 PRO 67

ASN 424 0.24 TYR 91 -0.12 PRO 67

ASN 424 0.25 VAL 92 -0.10 GLY 536

ASN 424 0.24 PRO 93 -0.09 GLY 536

ASN 424 0.24 LEU 94 -0.09 ALA 561

ASN 424 0.22 LEU 95 -0.08 GLY 566

ASN 424 0.23 ALA 96 -0.08 GLY 566

ASN 424 0.22 THR 97 -0.09 GLY 566

ASN 424 0.21 GLU 98 -0.09 GLY 536

PRO 471 0.23 TYR 99 -0.08 GLY 536

PRO 471 0.24 ALA 100 -0.08 GLY 536

PRO 471 0.24 TRP 101 -0.12 THR 88

ALA 461 0.23 ASN 102 -0.11 THR 88

ALA 461 0.24 GLU 103 -0.12 THR 88

ALA 461 0.27 ASP 104 -0.13 GLY 145

ALA 461 0.29 GLY 105 -0.15 GLY 145

ALA 461 0.30 THR 106 -0.09 GLY 146

PRO 471 0.27 GLN 107 -0.08 THR 88

PRO 471 0.26 LEU 108 -0.07 THR 88

PRO 471 0.23 ASP 109 -0.07 GLY 566

ASN 424 0.22 ILE 110 -0.07 GLY 566

ASN 424 0.20 THR 111 -0.08 GLY 566

ASN 424 0.20 LEU 112 -0.09 GLY 566

ASN 424 0.20 ARG 113 -0.10 GLY 566

ASN 424 0.17 ASP 114 -0.11 GLY 566

ASN 424 0.16 GLY 115 -0.12 TRP 224

ASN 424 0.17 VAL 116 -0.09 GLY 566

ASN 424 0.15 THR 117 -0.09 LYS 567

ASN 424 0.15 TRP 118 -0.09 LYS 567

ASN 424 0.13 THR 119 -0.09 LYS 567

ASN 424 0.10 ASP 120 -0.09 LYS 567

ASN 424 0.11 GLY 121 -0.09 LYS 567

ASN 424 0.12 GLU 122 -0.09 LYS 567

ASN 424 0.14 ALA 123 -0.08 LYS 567

ASN 424 0.16 PHE 124 -0.08 LYS 567

ASN 424 0.17 ASP 125 -0.08 GLY 566

ASN 424 0.18 ALA 126 -0.07 GLY 566

ASN 424 0.16 ASP 127 -0.06 LYS 567

ASN 424 0.17 ASP 128 -0.06 ALA 487

ASN 424 0.20 VAL 129 -0.06 LYS 490

ASN 424 0.19 VAL 130 -0.07 LYS 490

ASN 424 0.17 PHE 131 -0.10 ALA 487

ASN 424 0.20 THR 132 -0.12 LYS 490

ASN 424 0.23 PHE 133 -0.14 LYS 490

ASN 424 0.19 GLU 134 -0.14 LYS 490

ASN 424 0.18 LEU 135 -0.17 ALA 487

ASN 424 0.23 ILE 136 -0.21 LYS 490

ASN 424 0.22 ARG 137 -0.20 LYS 490

ASN 424 0.17 ASP 138 -0.20 ALA 487

ASN 424 0.17 ASN 139 -0.24 ALA 487

ASN 424 0.21 PRO 140 -0.30 ALA 487

ASN 424 0.20 ALA 141 -0.34 ASN 455

ASN 424 0.24 LEU 142 -0.31 TYR 452

ASN 424 0.30 ASN 143 -0.31 ALA 487

ASN 424 0.38 THR 144 -0.41 ASN 455

ASN 424 0.40 GLY 145 -0.43 LYS 490

ALA 469 0.43 GLY 146 -0.40 LYS 490

ALA 469 0.35 PHE 147 -0.29 LYS 490

ALA 469 0.34 ASN 148 -0.18 LYS 490

ALA 469 0.30 GLY 149 -0.12 ALA 167

ALA 469 0.25 GLU 150 -0.07 LYS 490

ALA 469 0.23 VAL 151 -0.05 LYS 490

ALA 469 0.20 THR 152 -0.05 GLY 566

ASN 424 0.18 LYS 153 -0.06 GLY 566

ASN 424 0.18 VAL 154 -0.07 GLY 566

ASN 424 0.17 ASP 155 -0.08 GLY 566

ASN 424 0.16 THR 156 -0.09 GLY 566

ASN 424 0.18 THR 157 -0.09 GLY 566

ASN 424 0.19 HIS 158 -0.08 GLY 566

ASN 424 0.20 VAL 159 -0.07 GLY 566

PRO 471 0.23 SER 160 -0.06 GLY 566

PRO 471 0.26 ILE 161 -0.05 THR 88

PRO 471 0.27 ALA 162 -0.05 THR 88

PRO 471 0.32 PHE 163 -0.07 ARG 491

PRO 471 0.35 PRO 164 -0.08 THR 499

ALA 461 0.40 GLU 165 -0.12 GLY 146

ALA 461 0.36 PRO 166 -0.20 GLY 146

ALA 461 0.34 ALA 167 -0.26 GLY 146

PRO 471 0.29 PHE 168 -0.27 GLY 145

PRO 471 0.33 VAL 169 -0.40 GLY 145

PRO 471 0.41 THR 170 -0.31 GLY 145

PRO 471 0.33 GLY 171 -0.15 GLY 145

PRO 471 0.30 PRO 172 -0.19 PRO 67

PRO 471 0.35 GLU 173 -0.19 PHE 65

PRO 471 0.30 VAL 174 -0.11 PHE 65

ASN 424 0.28 LEU 175 -0.10 PRO 67

ASN 424 0.30 GLY 176 -0.14 PRO 67

ASN 424 0.34 LYS 177 -0.20 PHE 65

ASN 424 0.31 THR 178 -0.13 PHE 65

ASN 424 0.27 PHE 179 -0.16 ALA 446

ASN 424 0.22 ILE 180 -0.11 ALA 446

ASN 424 0.18 VAL 181 -0.11 ALA 446

ASN 424 0.14 PRO 182 -0.09 GLY 445

ASN 424 0.13 GLU 183 -0.09 ALA 487

ASN 424 0.10 HIS 184 -0.09 GLY 445

ASN 424 0.08 LEU 185 -0.12 GLY 445

ASN 424 0.09 TRP 186 -0.14 GLY 445

GLU 425 0.07 GLY 187 -0.13 ALA 487

ASP 127 0.06 ASP 188 -0.15 ASN 455

ASN 241 0.06 VAL 189 -0.18 GLY 445

ASN 241 0.08 ASP 190 -0.22 ASN 456

ASN 241 0.10 PRO 191 -0.24 GLY 445

SER 55 0.12 THR 192 -0.30 ASN 456

SER 55 0.10 THR 193 -0.30 ASN 456

SER 55 0.07 ASP 194 -0.25 GLY 443

SER 55 0.07 VAL 195 -0.26 GLY 443

GLN 54 0.05 MET 196 -0.21 GLY 443

SER 44 0.06 ALA 197 -0.20 GLY 443

VAL 206 0.06 GLU 198 -0.16 GLY 443

ASN 424 0.11 PRO 199 -0.15 GLY 445

ASN 424 0.13 VAL 200 -0.11 GLY 445

ASN 424 0.17 GLY 201 -0.09 ALA 446

ASN 424 0.18 THR 202 -0.08 LYS 567

ASN 424 0.21 GLY 203 -0.08 LYS 567

ASN 424 0.21 PRO 204 -0.09 LYS 567

ASN 424 0.19 TYR 205 -0.10 LYS 567

ASN 424 0.16 VAL 206 -0.10 LYS 567

ASN 424 0.13 LEU 207 -0.12 GLY 443

ASN 424 0.11 GLY 208 -0.10 GLY 443

SER 44 0.12 GLU 209 -0.13 GLY 443

SER 44 0.10 PHE 210 -0.16 GLY 443

SER 44 0.11 LYS 211 -0.16 GLY 443

THR 252 0.11 PRO 212 -0.20 ASN 281

THR 252 0.14 GLN 213 -0.18 PHE 322

ASN 424 0.14 ALA 214 -0.15 PHE 322

ASN 424 0.13 PHE 215 -0.15 TRP 550

ASN 424 0.16 THR 216 -0.13 TRP 550

ASN 424 0.18 LEU 217 -0.11 TRP 550

ASN 424 0.16 SER 218 -0.13 LYS 567

ASN 424 0.18 ALA 219 -0.13 LYS 567

ASN 424 0.16 ASN 220 -0.12 LYS 567

ASN 424 0.16 GLU 221 -0.13 LYS 567

ASN 424 0.15 ASP 222 -0.11 LYS 567

ASN 424 0.18 TYR 223 -0.10 LYS 567

ASN 424 0.18 TRP 224 -0.12 GLY 115

ASN 424 0.21 GLY 225 -0.12 GLY 566

ASN 424 0.19 GLY 226 -0.13 GLY 566

ASN 424 0.18 ALA 227 -0.12 LYS 567

ASN 424 0.21 PRO 228 -0.11 GLY 566

ASN 424 0.20 ALA 229 -0.15 GLY 566

ASN 424 0.21 VAL 230 -0.14 LYS 567

ASN 424 0.19 LYS 231 -0.17 LYS 567

ASN 424 0.19 ASN 232 -0.15 LYS 567

ASN 424 0.22 VAL 233 -0.12 LYS 567

ASN 424 0.21 ARG 234 -0.12 LYS 567

ASN 424 0.24 TYR 235 -0.14 TRP 550

ASN 424 0.24 LEU 236 -0.15 PHE 322

ASN 424 0.21 SER 237 -0.21 PHE 322

SER 422 0.26 LEU 238 -0.22 PHE 322

SER 422 0.24 SER 239 -0.26 PHE 322

SER 422 0.37 GLY 240 -0.26 PHE 322

SER 422 0.53 ASN 241 -0.34 PHE 322

SER 422 0.54 THR 242 -0.26 GLN 323

SER 422 0.45 ALA 243 -0.20 PHE 322

SER 422 0.45 GLY 244 -0.18 THR 325

GLY 394 0.50 ALA 245 -0.16 ALA 319

GLY 394 0.40 ASP 246 -0.14 ALA 319

SER 422 0.36 ALA 247 -0.13 LYS 567

GLY 394 0.36 LEU 248 -0.10 ASP 315

GLY 394 0.37 ALA 249 -0.10 LYS 567

SER 422 0.32 ALA 250 -0.16 LYS 567

SER 422 0.29 GLY 251 -0.16 LYS 567

SER 422 0.29 THR 252 -0.18 LYS 567

SER 422 0.31 ILE 253 -0.12 LYS 567

SER 422 0.30 ASP 254 -0.10 LYS 567

TRP 423 0.34 TRP 255 -0.09 PRO 337

TRP 423 0.40 GLN 256 -0.14 GLY 53

TRP 423 0.45 THR 257 -0.26 GLY 53

GLY 394 0.48 GLY 258 -0.38 GLY 53

GLY 394 0.56 PRO 259 -0.31 GLY 53

GLY 394 0.56 VAL 260 -0.21 ASN 241

GLY 394 0.54 PRO 261 -0.23 ASN 241

GLY 394 0.42 ASP 262 -0.17 ASN 241

GLY 394 0.34 ILE 263 -0.19 GLY 53

GLY 394 0.27 GLU 264 -0.18 ALA 354

GLY 394 0.31 ASN 265 -0.15 ALA 354

GLY 394 0.36 VAL 266 -0.12 PRO 337

GLY 394 0.31 SER 267 -0.12 PRO 337

GLY 394 0.30 GLU 268 -0.12 PRO 337

GLY 394 0.34 ASN 269 -0.11 ALA 354

GLY 394 0.34 TYR 270 -0.09 ALA 354

GLY 394 0.30 PRO 271 -0.08 ALA 354

GLY 394 0.30 GLY 272 -0.08 PRO 337

GLY 394 0.30 TYR 273 -0.09 PRO 337

GLY 394 0.31 GLU 274 -0.10 THR 539

GLY 394 0.33 ALA 275 -0.13 GLY 53

GLY 394 0.29 ILE 276 -0.14 GLY 53

TRP 395 0.29 THR 277 -0.19 GLY 53

TRP 423 0.25 VAL 278 -0.20 PRO 67

TRP 423 0.18 PRO 279 -0.26 PRO 67

TRP 423 0.20 MET 280 -0.32 PRO 67

SER 441 0.18 ASN 281 -0.36 PRO 67

SER 441 0.11 GLN 282 -0.32 PRO 67

GLU 540 0.11 MET 283 -0.30 SER 68

MET 283 0.11 ALA 284 -0.25 SER 68

THR 525 0.12 LEU 285 -0.20 SER 68

THR 170 0.14 LEU 286 -0.20 SER 68

PRO 164 0.15 SER 287 -0.15 THR 193

PRO 164 0.19 CYS 288 -0.13 THR 193

GLU 165 0.16 SER 289 -0.14 THR 193

GLU 165 0.18 ASN 290 -0.13 THR 193

PRO 164 0.18 ALA 291 -0.10 THR 193

PRO 164 0.20 ASP 292 -0.11 THR 193

PRO 164 0.23 LEU 293 -0.11 THR 193

PRO 164 0.22 GLY 294 -0.09 THR 193

PRO 164 0.20 CYS 295 -0.09 THR 193

PRO 164 0.19 GLU 296 -0.07 THR 193

PRO 164 0.16 GLY 297 -0.07 THR 193

PRO 164 0.14 PRO 298 -0.08 THR 193

PRO 164 0.14 GLN 299 -0.11 THR 193

PRO 164 0.15 THR 300 -0.11 THR 193

PRO 164 0.13 ASP 301 -0.11 THR 193

PRO 164 0.11 PRO 302 -0.13 THR 193

PRO 164 0.09 ALA 303 -0.12 SER 68

PRO 164 0.10 VAL 304 -0.12 GLN 59

PRO 164 0.10 ARG 305 -0.14 SER 68

PRO 164 0.07 GLN 306 -0.16 SER 68

PRO 164 0.07 ALA 307 -0.14 SER 68

PRO 164 0.09 ILE 308 -0.15 GLN 59

PRO 164 0.07 TYR 309 -0.17 SER 68

PRO 164 0.05 TYR 310 -0.17 SER 68

PRO 164 0.06 ALA 311 -0.15 GLN 59

LYS 567 0.06 MET 312 -0.17 GLN 59

LYS 567 0.06 ASP 313 -0.18 GLY 56

LYS 567 0.07 ARG 314 -0.21 SER 55

LYS 567 0.06 ASP 315 -0.23 ASN 241

LYS 567 0.07 GLN 316 -0.23 ASN 241

LYS 567 0.08 LEU 317 -0.23 SER 55

LYS 567 0.09 ASN 318 -0.27 ASN 241

LYS 567 0.09 ALA 319 -0.31 ASN 241

LYS 567 0.09 LEU 320 -0.31 ASN 241

ILE 263 0.14 ALA 321 -0.32 ASN 241

GLN 323 0.15 PHE 322 -0.34 ASN 241

ASP 397 0.19 GLN 323 -0.32 ASN 241

LYS 567 0.12 GLY 324 -0.27 ASN 241

GLU 540 0.15 THR 325 -0.30 GLY 53

GLU 540 0.14 ALA 326 -0.28 GLY 53

ASP 541 0.09 SER 327 -0.25 GLY 53

LYS 567 0.08 GLU 328 -0.23 PRO 67

LYS 567 0.06 MET 329 -0.26 PRO 67

LYS 567 0.06 SER 330 -0.25 PRO 67

LYS 567 0.06 PRO 331 -0.23 PRO 67

ALA 100 0.06 THR 332 -0.25 PRO 67

ALA 100 0.06 PHE 333 -0.29 PRO 67

ASN 424 0.08 ALA 334 -0.29 PRO 67

TRP 423 0.11 LEU 335 -0.29 PRO 67

TRP 423 0.09 LEU 336 -0.26 PRO 67

TRP 423 0.10 PRO 337 -0.25 PRO 67

TRP 423 0.11 ALA 338 -0.26 PRO 67

ASN 424 0.10 GLN 339 -0.27 PRO 67

ASN 424 0.08 GLU 340 -0.24 PRO 67

ASN 424 0.08 GLN 341 -0.23 PRO 67

ASN 424 0.08 PHE 342 -0.25 PRO 67

ASN 424 0.06 ILE 343 -0.24 PRO 67

LYS 567 0.05 SER 344 -0.22 PRO 67

LYS 567 0.05 GLY 345 -0.20 PRO 67

LYS 567 0.05 GLU 346 -0.19 PRO 67

LYS 567 0.05 ILE 347 -0.20 PRO 67

LYS 567 0.05 GLU 348 -0.19 PRO 67

ALA 509 0.05 GLU 349 -0.19 PRO 67

LYS 567 0.05 LYS 350 -0.21 PRO 67

LYS 567 0.06 VAL 351 -0.22 PRO 67

LYS 567 0.05 ALA 352 -0.21 PRO 67

LYS 567 0.04 PRO 353 -0.20 SER 68

LYS 567 0.05 ALA 354 -0.20 SER 68

LYS 567 0.05 LYS 355 -0.18 SER 55

LYS 567 0.05 ALA 356 -0.16 SER 68

ASP 479 0.04 ASP 357 -0.15 SER 68

PRO 164 0.05 LEU 358 -0.13 GLN 59

ASP 479 0.05 ASP 359 -0.13 SER 68

ASP 479 0.06 LYS 360 -0.14 SER 68

PRO 164 0.06 VAL 361 -0.13 GLN 59

PRO 164 0.06 ASP 362 -0.11 GLU 348

ASP 479 0.05 GLU 363 -0.15 GLU 348

ASP 479 0.06 ILE 364 -0.14 GLU 348

PRO 164 0.08 LEU 365 -0.12 GLU 348

PRO 164 0.07 THR 366 -0.12 GLU 348

PRO 164 0.06 GLY 367 -0.14 GLU 348

PRO 164 0.08 ALA 368 -0.12 GLU 346

PRO 164 0.09 GLY 369 -0.11 GLU 346

PRO 164 0.09 TYR 370 -0.10 GLU 348

PRO 164 0.09 GLU 371 -0.10 GLU 348

PRO 164 0.08 LYS 372 -0.08 GLU 348

PRO 164 0.09 GLY 373 -0.07 GLU 348

PRO 164 0.09 SER 374 -0.07 GLU 348

PRO 164 0.09 ASP 375 -0.06 GLU 348

PRO 164 0.08 GLY 376 -0.08 GLN 59

PRO 164 0.10 ILE 377 -0.07 GLN 59

PRO 164 0.10 TYR 378 -0.08 GLN 59

PRO 164 0.11 ALA 379 -0.07 GLU 348

PRO 164 0.12 LYS 380 -0.08 GLU 346

PRO 164 0.14 ASP 381 -0.07 GLU 346

PRO 164 0.14 GLY 382 -0.06 GLU 346

PRO 164 0.14 VAL 383 -0.06 GLU 346

PRO 164 0.13 LYS 384 -0.06 GLU 346

PRO 164 0.12 LEU 385 -0.07 GLN 59

PRO 261 0.14 GLU 386 -0.08 GLN 59

PRO 261 0.16 LEU 387 -0.09 GLN 59

PRO 261 0.20 THR 388 -0.09 GLN 59

PRO 261 0.20 VAL 389 -0.12 GLN 59

GLY 258 0.24 GLU 390 -0.12 GLN 59

PRO 259 0.31 VAL 391 -0.15 GLN 59

GLY 258 0.42 VAL 392 -0.16 GLN 59

THR 242 0.52 THR 393 -0.12 GLN 59

VAL 260 0.56 GLY 394 -0.21 GLY 56

PRO 259 0.56 TRP 395 -0.28 GLY 56

PRO 261 0.49 THR 396 -0.28 GLY 56

PRO 261 0.31 ASP 397 -0.32 SER 55

PRO 261 0.27 TYR 398 -0.25 GLY 56

PRO 261 0.33 ILE 399 -0.20 GLY 56

PRO 261 0.27 THR 400 -0.22 GLY 56

PRO 261 0.17 ALA 401 -0.21 GLY 56

PRO 261 0.19 ILE 402 -0.17 GLN 59

PRO 261 0.20 ASP 403 -0.16 GLY 56

PRO 261 0.12 THR 404 -0.18 GLY 56

PRO 261 0.10 MET 405 -0.16 GLN 59

PRO 261 0.13 SER 406 -0.14 GLN 59

PRO 261 0.09 GLN 407 -0.13 GLN 59

PRO 164 0.07 GLN 408 -0.15 GLN 59

PRO 164 0.08 LEU 409 -0.13 GLN 59

PRO 261 0.09 LYS 410 -0.11 GLN 59

PRO 164 0.07 ALA 411 -0.12 GLN 59

PRO 164 0.07 ALA 412 -0.12 GLN 59

PRO 164 0.08 GLY 413 -0.10 GLN 59

PRO 164 0.10 ILE 414 -0.10 GLN 59

PRO 261 0.14 GLY 415 -0.09 GLN 59

PRO 261 0.16 LEU 416 -0.11 GLN 59

PRO 261 0.21 SER 417 -0.09 GLN 59

PRO 261 0.26 ALA 418 -0.10 GLN 59

THR 242 0.29 SER 419 -0.10 ALA 418

THR 242 0.38 GLN 420 -0.08 GLN 59

THR 242 0.45 SER 421 -0.10 SER 422

THR 242 0.54 SER 422 -0.10 SER 421

GLY 258 0.46 TRP 423 -0.13 GLN 59

GLY 53 0.48 ASN 424 -0.05 THR 193

THR 242 0.41 GLU 425 -0.03 ALA 418

THR 242 0.35 TRP 426 -0.09 GLN 59

TRP 550 0.34 THR 427 -0.13 THR 193

GLY 146 0.37 ASP 428 -0.07 THR 193

GLY 146 0.30 LYS 429 -0.07 THR 193

GLY 146 0.28 LYS 430 -0.13 THR 193

GLY 146 0.36 SER 431 -0.14 THR 193

GLY 146 0.33 LYS 432 -0.09 THR 193

GLY 146 0.25 GLY 433 -0.10 THR 193

GLY 146 0.25 THR 434 -0.06 THR 193

THR 242 0.21 TYR 435 -0.08 THR 193

PRO 164 0.17 GLN 436 -0.10 GLN 59

PRO 261 0.15 LEU 437 -0.13 GLN 59

GLY 258 0.19 ALA 438 -0.16 GLN 59

THR 525 0.21 ILE 439 -0.20 GLN 59

THR 525 0.23 ASP 440 -0.27 SER 68

THR 525 0.20 SER 441 -0.33 SER 68

GLY 443 0.28 LEU 442 -0.37 PRO 67

LEU 442 0.28 GLY 443 -0.45 PRO 67

THR 427 0.20 GLN 444 -0.42 PRO 67

THR 427 0.24 GLY 445 -0.47 PRO 67

ASN 424 0.28 ALA 446 -0.37 PRO 67

ASN 424 0.23 VAL 447 -0.30 PRO 67

ASN 424 0.19 SER 448 -0.30 PRO 67

ASN 424 0.14 ASP 449 -0.32 PRO 67

ASN 424 0.10 PRO 450 -0.32 PRO 67

ALA 100 0.13 TYR 451 -0.39 GLY 145

VAL 472 0.18 TYR 452 -0.41 THR 144

THR 427 0.13 LEU 453 -0.38 PRO 67

ALA 100 0.12 TYR 454 -0.33 THR 144

VAL 169 0.23 ASN 455 -0.41 THR 144

VAL 169 0.26 ASN 456 -0.38 PRO 67

VAL 169 0.18 PHE 457 -0.31 PRO 67

GLU 165 0.17 LEU 458 -0.27 PRO 67

GLU 165 0.24 SER 459 -0.29 THR 144

GLU 165 0.28 SER 460 -0.24 ALA 141

GLU 165 0.40 ALA 461 -0.30 ALA 141

GLU 165 0.35 ASN 462 -0.26 THR 193

GLU 165 0.30 THR 463 -0.21 THR 193

PRO 164 0.32 ALA 464 -0.16 THR 193

PRO 164 0.28 GLU 465 -0.11 THR 193

PRO 164 0.26 VAL 466 -0.09 THR 193

GLY 146 0.30 GLY 467 -0.06 THR 193

GLY 146 0.36 GLN 468 -0.09 THR 193

GLY 146 0.43 ALA 469 -0.13 THR 193

GLY 146 0.34 ALA 470 -0.19 THR 193

GLY 146 0.43 PRO 471 -0.26 THR 193

THR 170 0.35 VAL 472 -0.27 THR 193

THR 170 0.27 ASN 473 -0.23 THR 193

THR 170 0.25 VAL 474 -0.20 THR 193

GLU 165 0.19 ALA 475 -0.18 THR 193

GLU 165 0.22 ARG 476 -0.17 THR 193

GLU 165 0.18 PHE 477 -0.19 THR 193

GLU 165 0.18 SER 478 -0.19 THR 193

GLU 165 0.11 ASP 479 -0.21 ALA 141

GLU 103 0.11 PRO 480 -0.24 THR 144

ALA 100 0.08 ALA 481 -0.26 THR 144

ALA 100 0.09 VAL 482 -0.28 THR 144

ASP 104 0.14 ASP 483 -0.32 THR 144

GLU 103 0.12 GLU 484 -0.32 THR 144

GLU 103 0.09 ALA 485 -0.32 THR 144

SER 459 0.13 LEU 486 -0.38 GLY 145

ALA 461 0.19 ALA 487 -0.38 GLY 145

ALA 461 0.16 VAL 488 -0.33 GLY 145

ALA 461 0.17 LEU 489 -0.36 GLY 145

ALA 461 0.29 LYS 490 -0.43 GLY 145

ALA 461 0.25 ARG 491 -0.32 GLY 145

ALA 461 0.20 THR 492 -0.29 GLY 145

ALA 100 0.19 ASN 493 -0.24 GLY 145

PRO 471 0.17 PRO 494 -0.24 GLY 145

ALA 100 0.17 ASP 495 -0.19 GLY 145

ALA 100 0.13 ASP 496 -0.21 GLY 145

ALA 100 0.11 THR 497 -0.21 GLY 145

ALA 100 0.09 ALA 498 -0.21 GLY 145

ALA 461 0.09 THR 499 -0.24 GLY 145

ALA 461 0.09 ARG 500 -0.28 GLY 145

ALA 100 0.07 GLN 501 -0.25 GLY 145

ALA 100 0.07 GLU 502 -0.24 GLY 145

ALA 100 0.08 GLN 503 -0.28 GLY 145

ALA 100 0.08 PHE 504 -0.27 GLY 145

ALA 100 0.06 ASP 505 -0.23 THR 144

ALA 100 0.07 VAL 506 -0.24 THR 144

ALA 100 0.08 ILE 507 -0.26 THR 144

ALA 100 0.06 GLN 508 -0.24 PRO 67

GLU 349 0.05 ALA 509 -0.21 PRO 67

ALA 100 0.07 ALA 510 -0.21 PRO 67

ALA 100 0.08 ILE 511 -0.22 PRO 67

ALA 100 0.05 VAL 512 -0.21 PRO 67

ALA 481 0.07 GLU 513 -0.18 PRO 67

GLU 165 0.09 ASP 514 -0.17 PRO 67

GLU 165 0.09 MET 515 -0.19 PRO 67

GLU 165 0.12 PRO 516 -0.19 SER 68

GLU 165 0.11 TYR 517 -0.22 SER 68

PRO 164 0.09 ILE 518 -0.20 SER 68

PRO 164 0.07 PRO 519 -0.23 SER 68

LYS 567 0.07 ILE 520 -0.23 SER 68

ASP 541 0.08 LEU 521 -0.25 SER 68

ASP 541 0.10 THR 522 -0.27 PRO 67

GLU 540 0.14 GLY 523 -0.29 SER 68

TRP 395 0.24 GLY 524 -0.25 GLY 53

TRP 423 0.35 THR 525 -0.29 GLY 53

TRP 395 0.39 THR 526 -0.25 GLY 53

TRP 423 0.38 SER 527 -0.18 GLY 53

GLY 394 0.36 GLU 528 -0.13 GLY 53

TRP 423 0.31 TYR 529 -0.09 PRO 337

SER 422 0.28 ASN 530 -0.07 PRO 337

GLY 394 0.26 VAL 531 -0.07 ASP 90

SER 422 0.24 GLU 532 -0.07 ALA 250

SER 422 0.23 LYS 533 -0.09 ALA 250

TRP 423 0.24 PHE 534 -0.07 THR 97

TRP 423 0.24 SER 535 -0.08 THR 97

TRP 423 0.24 GLY 536 -0.10 VAL 92

TRP 423 0.27 TRP 537 -0.08 TYR 91

TRP 423 0.28 PRO 538 -0.09 PRO 67

TRP 423 0.25 THR 539 -0.11 SER 267

TRP 423 0.24 GLU 540 -0.12 PRO 67

TRP 423 0.22 ASP 541 -0.13 ASN 89

TRP 423 0.23 ASP 542 -0.12 ASN 89

TRP 423 0.26 LEU 543 -0.14 PRO 67

ASN 424 0.25 TYR 544 -0.13 PRO 67

ASN 424 0.29 ALA 545 -0.14 PRO 67

TRP 423 0.33 PHE 546 -0.17 PRO 67

TRP 423 0.34 PRO 547 -0.13 ALA 338

TRP 423 0.40 ALA 548 -0.16 ILE 70

TRP 423 0.39 VAL 549 -0.13 ILE 70

ASN 424 0.45 TRP 550 -0.27 ILE 70

ASN 424 0.42 ALA 551 -0.23 ILE 70

ASN 424 0.37 SER 552 -0.20 ILE 70

ASN 424 0.33 PRO 553 -0.13 PRO 67

ASN 424 0.33 ASP 554 -0.14 PRO 67

ASN 424 0.33 ASN 555 -0.11 ILE 70

ASN 424 0.29 ALA 556 -0.07 ALA 338

ASN 424 0.28 GLU 557 -0.08 PRO 67

ASN 424 0.29 VAL 558 -0.06 PRO 67

ASN 424 0.27 PHE 559 -0.06 GLY 566

ASN 424 0.24 LYS 560 -0.08 LEU 94

ASN 424 0.25 ALA 561 -0.09 PRO 93

ASN 424 0.24 LEU 562 -0.07 THR 97

ASN 424 0.22 GLU 563 -0.09 THR 97

ASN 424 0.21 PRO 564 -0.12 GLY 566

ASN 424 0.21 THR 565 -0.08 ALA 250

SER 422 0.17 GLY 566 -0.15 ALA 229

ASP 541 0.17 LYS 567 -0.35 ALA 45

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.

*** 2647 ***

CA distance fluctuations for 2605141238122666813

--- normal mode 11 ---

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

* 2647 *