Should you encounter any unexpected behaviour,
please let us know.

* 6DNP_unrelaxed_rank_001_alphafold2_ptm_model_5_seed_000 *

CA strain for 240220091727167243

--- normal mode 15 ---

This graph displays the distance variation between successive pairs of CA atoms in the two extreme conformations that were computed for this mode (DQMIN/DQMAX). Large distance variations can be an indicator for residue pairs that support the important strain in that particular normal mode movement. Note that residue pairs between chain breaks or at flexible ends of the protein may also exhibit large CA-CA distance variations. If more than one residues ae grouped together into a rigid block (NRBL>1), CA-CA distance variations between CA atoms in the same block will be very low.

This feature is still experimental and will be further developped in the future.

CA i CA i+1 vari
THR 1 ASP 2 -0.0002

ASP 2 ARG 3 0.0003

ARG 3 VAL 4 -0.0001

VAL 4 SER 5 -0.0125

SER 5 VAL 6 0.0001

VAL 6 GLY 7 -0.0003

GLY 7 ASN 8 -0.0002

ASN 8 LEU 9 0.0135

LEU 9 ARG 10 0.0002

ARG 10 ILE 11 0.0003

ILE 11 ALA 12 -0.0001

ALA 12 ARG 13 -0.0452

ARG 13 VAL 14 0.0002

VAL 14 LEU 15 0.0002

LEU 15 TYR 16 -0.0005

TYR 16 ASP 17 0.0020

ASP 17 PHE 18 -0.0003

PHE 18 VAL 19 -0.0001

VAL 19 ASN 20 0.0000

ASN 20 ASN 21 0.0181

ASN 21 GLU 22 -0.0000

GLU 22 ALA 23 -0.0002

ALA 23 LEU 24 0.0002

LEU 24 PRO 25 -0.0071

PRO 25 GLY 26 -0.0000

GLY 26 THR 27 0.0002

THR 27 ASP 28 -0.0001

ASP 28 ILE 29 0.0169

ILE 29 ASP 30 -0.0000

ASP 30 PRO 31 0.0001

PRO 31 ASP 32 -0.0002

ASP 32 SER 33 -0.0412

SER 33 PHE 34 0.0001

PHE 34 TRP 35 -0.0003

TRP 35 ALA 36 -0.0001

ALA 36 GLY 37 -0.0520

GLY 37 VAL 38 -0.0002

VAL 38 ASP 39 0.0002

ASP 39 LYS 40 0.0002

LYS 40 VAL 41 -0.0384

VAL 41 VAL 42 -0.0001

VAL 42 ALA 43 -0.0000

ALA 43 ASP 44 0.0000

ASP 44 LEU 45 -0.0519

LEU 45 THR 46 -0.0001

THR 46 PRO 47 -0.0001

PRO 47 GLN 48 -0.0003

GLN 48 ASN 49 0.0771

ASN 49 GLN 50 0.0001

GLN 50 ALA 51 -0.0002

ALA 51 LEU 52 0.0003

LEU 52 LEU 53 0.0527

LEU 53 ASN 54 -0.0000

ASN 54 ALA 55 0.0002

ALA 55 ARG 56 -0.0002

ARG 56 ASP 57 -0.0539

ASP 57 GLU 58 -0.0002

GLU 58 LEU 59 0.0002

LEU 59 GLN 60 -0.0001

GLN 60 ALA 61 -0.0805

ALA 61 GLN 62 -0.0002

GLN 62 ILE 63 -0.0002

ILE 63 ASP 64 -0.0001

ASP 64 LYS 65 -0.0718

LYS 65 TRP 66 -0.0004

TRP 66 HIS 67 0.0002

HIS 67 ARG 68 0.0004

ARG 68 ARG 69 -0.0314

ARG 69 ARG 70 -0.0000

ARG 70 VAL 71 0.0000

VAL 71 ILE 72 0.0003

ILE 72 GLU 73 0.0217

GLU 73 PRO 74 0.0000

PRO 74 ILE 75 -0.0001

ILE 75 ASP 76 -0.0000

ASP 76 MET 77 0.2656

MET 77 ASP 78 -0.0001

ASP 78 ALA 79 -0.0003

ALA 79 TYR 80 0.0002

TYR 80 ARG 81 0.0227

ARG 81 GLN 82 0.0001

GLN 82 PHE 83 0.0002

PHE 83 LEU 84 -0.0003

LEU 84 THR 85 0.0028

THR 85 GLU 86 0.0001

GLU 86 ILE 87 -0.0000

ILE 87 GLY 88 -0.0000

GLY 88 TYR 89 -0.0035

TYR 89 LEU 90 -0.0003

LEU 90 LEU 91 -0.0001

LEU 91 PRO 92 0.0001

PRO 92 GLU 93 0.0111

GLU 93 PRO 94 -0.0001

PRO 94 ASP 95 -0.0001

ASP 95 ASP 96 0.0003

ASP 96 PHE 97 0.0873

PHE 97 THR 98 0.0000

THR 98 ILE 99 0.0002

ILE 99 THR 100 0.0002

THR 100 THR 101 0.0598

THR 101 SER 102 -0.0003

SER 102 GLY 103 0.0001

GLY 103 VAL 104 -0.0003

VAL 104 ASP 105 -0.1101

ASP 105 ALA 106 -0.0001

ALA 106 GLU 107 -0.0002

GLU 107 ILE 108 -0.0001

ILE 108 THR 109 0.0681

THR 109 THR 110 -0.0005

THR 110 THR 111 -0.0000

THR 111 ALA 112 0.0001

ALA 112 GLY 113 0.0567

GLY 113 PRO 114 0.0003

PRO 114 GLN 115 0.0004

GLN 115 LEU 116 -0.0002

LEU 116 VAL 117 0.0012

VAL 117 VAL 118 -0.0001

VAL 118 PRO 119 0.0002

PRO 119 VAL 120 -0.0001

VAL 120 LEU 121 0.0249

LEU 121 ASN 122 -0.0000

ASN 122 ALA 123 -0.0001

ALA 123 ARG 124 0.0001

ARG 124 PHE 125 0.0218

PHE 125 ALA 126 0.0004

ALA 126 LEU 127 0.0001

LEU 127 ASN 128 0.0003

ASN 128 ALA 129 0.0128

ALA 129 ALA 130 -0.0002

ALA 130 ASN 131 -0.0002

ASN 131 ALA 132 0.0002

ALA 132 ARG 133 0.0546

ARG 133 TRP 134 0.0001

TRP 134 GLY 135 0.0001

GLY 135 SER 136 -0.0002

SER 136 LEU 137 0.0018

LEU 137 TYR 138 0.0000

TYR 138 ASP 139 -0.0002

ASP 139 ALA 140 0.0002

ALA 140 LEU 141 -0.0396

LEU 141 TYR 142 -0.0003

TYR 142 GLY 143 -0.0002

GLY 143 THR 144 -0.0001

THR 144 ASP 145 0.0567

ASP 145 VAL 146 -0.0002

VAL 146 ILE 147 -0.0000

ILE 147 PRO 148 -0.0000

PRO 148 GLU 149 -0.0485

GLU 149 THR 150 -0.0000

THR 150 ASP 151 -0.0000

ASP 151 GLY 152 0.0000

GLY 152 ALA 153 -0.0125

ALA 153 GLU 154 0.0003

GLU 154 LYS 155 -0.0001

LYS 155 GLY 156 -0.0001

GLY 156 PRO 157 0.0849

PRO 157 THR 158 0.0004

THR 158 TYR 159 -0.0003

TYR 159 ASN 160 0.0003

ASN 160 LYS 161 0.1700

LYS 161 VAL 162 -0.0001

VAL 162 ARG 163 0.0001

ARG 163 GLY 164 0.0000

GLY 164 ASP 165 0.0644

ASP 165 LYS 166 -0.0004

LYS 166 VAL 167 0.0003

VAL 167 ILE 168 -0.0001

ILE 168 ALA 169 -0.0135

ALA 169 TYR 170 -0.0002

TYR 170 ALA 171 -0.0002

ALA 171 ARG 172 0.0001

ARG 172 LYS 173 -0.0024

LYS 173 PHE 174 -0.0002

PHE 174 LEU 175 0.0001

LEU 175 ASP 176 -0.0002

ASP 176 ASP 177 0.0163

ASP 177 SER 178 -0.0003

SER 178 VAL 179 0.0000

VAL 179 PRO 180 0.0000

PRO 180 LEU 181 -0.0070

LEU 181 SER 182 -0.0002

SER 182 SER 183 0.0002

SER 183 GLY 184 0.0001

GLY 184 SER 185 -0.0111

SER 185 PHE 186 -0.0004

PHE 186 GLY 187 0.0001

GLY 187 ASP 188 -0.0004

ASP 188 ALA 189 -0.0021

ALA 189 THR 190 -0.0001

THR 190 GLY 191 -0.0002

GLY 191 PHE 192 0.0003

PHE 192 THR 193 0.1067

THR 193 VAL 194 -0.0004

VAL 194 GLN 195 -0.0001

GLN 195 ASP 196 -0.0001

ASP 196 GLY 197 -0.0134

GLY 197 GLN 198 -0.0001

GLN 198 LEU 199 0.0002

LEU 199 VAL 200 -0.0000

VAL 200 VAL 201 0.0301

VAL 201 ALA 202 0.0002

ALA 202 LEU 203 0.0003

LEU 203 PRO 204 -0.0004

PRO 204 ASP 205 -0.0179

ASP 205 LYS 206 0.0000

LYS 206 SER 207 -0.0004

SER 207 THR 208 0.0001

THR 208 GLY 209 0.0269

GLY 209 LEU 210 -0.0002

LEU 210 ALA 211 0.0003

ALA 211 ASN 212 -0.0002

ASN 212 PRO 213 -0.0195

PRO 213 GLY 214 0.0002

GLY 214 GLN 215 -0.0003

GLN 215 PHE 216 0.0001

PHE 216 ALA 217 0.0289

ALA 217 GLY 218 0.0000

GLY 218 TYR 219 0.0000

TYR 219 THR 220 -0.0002

THR 220 GLY 221 -0.0637

GLY 221 ALA 222 0.0001

ALA 222 ALA 223 -0.0002

ALA 223 GLU 224 0.0001

GLU 224 SER 225 0.0371

SER 225 PRO 226 -0.0000

PRO 226 THR 227 0.0002

THR 227 SER 228 0.0002

SER 228 VAL 229 -0.0077

VAL 229 LEU 230 -0.0000

LEU 230 LEU 231 0.0000

LEU 231 ILE 232 0.0003

ILE 232 ASN 233 -0.0977

ASN 233 HIS 234 -0.0002

HIS 234 GLY 235 -0.0001

GLY 235 LEU 236 -0.0001

LEU 236 HIS 237 -0.1436

HIS 237 ILE 238 0.0002

ILE 238 GLU 239 -0.0003

GLU 239 ILE 240 -0.0002

ILE 240 LEU 241 -0.0299

LEU 241 ILE 242 -0.0001

ILE 242 ASP 243 -0.0004

ASP 243 PRO 244 0.0003

PRO 244 GLU 245 0.1160

GLU 245 SER 246 -0.0000

SER 246 GLN 247 -0.0001

GLN 247 VAL 248 -0.0001

VAL 248 GLY 249 0.0809

GLY 249 THR 250 -0.0002

THR 250 THR 251 -0.0001

THR 251 ASP 252 0.0002

ASP 252 ARG 253 0.1204

ARG 253 ALA 254 -0.0002

ALA 254 GLY 255 0.0003

GLY 255 VAL 256 -0.0002

VAL 256 LYS 257 -0.0851

LYS 257 ASP 258 -0.0003

ASP 258 VAL 259 0.0002

VAL 259 ILE 260 0.0000

ILE 260 LEU 261 -0.2607

LEU 261 GLU 262 -0.0000

GLU 262 SER 263 -0.0002

SER 263 ALA 264 0.0002

ALA 264 ILE 265 -0.0267

ILE 265 THR 266 0.0000

THR 266 THR 267 -0.0001

THR 267 ILE 268 0.0003

ILE 268 MET 269 0.0289

MET 269 ASP 270 -0.0003

ASP 270 PHE 271 0.0002

PHE 271 GLU 272 -0.0000

GLU 272 ASP 273 0.0764

ASP 273 SER 274 -0.0001

SER 274 VAL 275 0.0004

VAL 275 ALA 276 0.0000

ALA 276 ALA 277 0.1634

ALA 277 VAL 278 -0.0001

VAL 278 ASP 279 -0.0002

ASP 279 ALA 280 -0.0001

ALA 280 ALA 281 0.0310

ALA 281 ASP 282 -0.0004

ASP 282 LYS 283 -0.0003

LYS 283 VAL 284 0.0001

VAL 284 LEU 285 0.0506

LEU 285 GLY 286 -0.0002

GLY 286 TYR 287 -0.0000

TYR 287 ARG 288 0.0004

ARG 288 ASN 289 0.1101

ASN 289 TRP 290 -0.0002

TRP 290 LEU 291 0.0002

LEU 291 GLY 292 0.0000

GLY 292 LEU 293 0.1195

LEU 293 ASN 294 0.0003

ASN 294 LYS 295 0.0003

LYS 295 GLY 296 -0.0004

GLY 296 ASP 297 -0.0932

ASP 297 LEU 298 -0.0002

LEU 298 ALA 299 -0.0002

ALA 299 ALA 300 -0.0000

ALA 300 ARG 301 -0.0217

ARG 301 VAL 302 -0.0002

VAL 302 LEU 303 0.0001

LEU 303 ASN 304 0.0002

ASN 304 ARG 305 0.0407

ARG 305 ASP 306 -0.0003

ASP 306 ARG 307 -0.0002

ARG 307 ASN 308 0.0003

ASN 308 TYR 309 -0.0089

TYR 309 THR 310 0.0004

THR 310 ALA 311 -0.0001

ALA 311 PRO 312 -0.0001

PRO 312 GLY 313 -0.0218

GLY 313 GLY 314 -0.0001

GLY 314 GLY 315 -0.0001

GLY 315 GLN 316 0.0002

GLN 316 PHE 317 -0.0530

PHE 317 THR 318 -0.0000

THR 318 LEU 319 0.0001

LEU 319 PRO 320 0.0003

PRO 320 GLY 321 0.0822

GLY 321 ARG 322 -0.0000

ARG 322 SER 323 0.0000

SER 323 LEU 324 0.0001

LEU 324 MET 325 -0.0332

MET 325 PHE 326 0.0001

PHE 326 VAL 327 -0.0000

VAL 327 ARG 328 0.0002

ARG 328 ASN 329 -0.1936

ASN 329 VAL 330 -0.0001

VAL 330 GLY 331 0.0003

GLY 331 HIS 332 0.0002

HIS 332 LEU 333 0.0122

LEU 333 MET 334 -0.0000

MET 334 THR 335 -0.0002

THR 335 ASN 336 0.0004

ASN 336 ASP 337 -0.1593

ASP 337 ALA 338 -0.0001

ALA 338 ILE 339 0.0002

ILE 339 VAL 340 -0.0003

VAL 340 ASP 341 0.0775

ASP 341 THR 342 0.0001

THR 342 ASP 343 -0.0000

ASP 343 GLY 344 0.0003

GLY 344 SER 345 -0.1853

SER 345 GLU 346 -0.0003

GLU 346 VAL 347 -0.0000

VAL 347 PHE 348 0.0003

PHE 348 GLU 349 -0.0855

GLU 349 GLY 350 -0.0001

GLY 350 ILE 351 -0.0003

ILE 351 MET 352 -0.0001

MET 352 ASP 353 -0.0279

ASP 353 ALA 354 0.0002

ALA 354 LEU 355 0.0001

LEU 355 PHE 356 0.0001

PHE 356 THR 357 0.0012

THR 357 GLY 358 -0.0002

GLY 358 LEU 359 -0.0003

LEU 359 ILE 360 -0.0002

ILE 360 ALA 361 0.0291

ALA 361 ILE 362 -0.0003

ILE 362 HIS 363 -0.0002

HIS 363 GLY 364 -0.0003

GLY 364 LEU 365 0.0326

LEU 365 LYS 366 0.0001

LYS 366 ALA 367 0.0000

ALA 367 SER 368 -0.0001

SER 368 PRO 369 0.0483

PRO 369 LEU 370 0.0004

LEU 370 ILE 371 -0.0001

ILE 371 ASN 372 0.0001

ASN 372 SER 373 0.0269

SER 373 ARG 374 -0.0001

ARG 374 THR 375 -0.0000

THR 375 GLY 376 -0.0002

GLY 376 SER 377 0.0434

SER 377 ILE 378 0.0002

ILE 378 TYR 379 -0.0003

TYR 379 ILE 380 -0.0000

ILE 380 VAL 381 0.0082

VAL 381 LYS 382 -0.0000

LYS 382 PRO 383 -0.0000

PRO 383 LYS 384 0.0003

LYS 384 MET 385 0.0692

MET 385 HIS 386 -0.0001

HIS 386 GLY 387 -0.0003

GLY 387 PRO 388 0.0001

PRO 388 ALA 389 -0.1047

ALA 389 GLU 390 -0.0001

GLU 390 VAL 391 0.0001

VAL 391 ALA 392 -0.0006

ALA 392 PHE 393 -0.1338

PHE 393 THR 394 -0.0000

THR 394 CYS 395 0.0001

CYS 395 GLU 396 -0.0001

GLU 396 LEU 397 -0.0310

LEU 397 PHE 398 -0.0001

PHE 398 SER 399 -0.0005

SER 399 ARG 400 -0.0001

ARG 400 VAL 401 0.0245

VAL 401 GLU 402 -0.0002

GLU 402 ASP 403 0.0000

ASP 403 VAL 404 0.0003

VAL 404 LEU 405 -0.0152

LEU 405 GLY 406 -0.0002

GLY 406 LEU 407 -0.0000

LEU 407 PRO 408 0.0003

PRO 408 GLN 409 0.0383

GLN 409 ASN 410 -0.0002

ASN 410 THR 411 -0.0002

THR 411 MET 412 0.0000

MET 412 LYS 413 0.0149

LYS 413 ILE 414 -0.0001

ILE 414 GLY 415 0.0001

GLY 415 ILE 416 0.0001

ILE 416 MET 417 0.0906

MET 417 ASP 418 0.0000

ASP 418 GLU 419 -0.0003

GLU 419 GLU 420 -0.0002

GLU 420 ARG 421 -0.0485

ARG 421 ARG 422 0.0003

ARG 422 THR 423 -0.0003

THR 423 THR 424 -0.0001

THR 424 VAL 425 -0.0117

VAL 425 ASN 426 0.0000

ASN 426 LEU 427 -0.0003

LEU 427 LYS 428 0.0002

LYS 428 ALA 429 -0.0613

ALA 429 CYS 430 0.0000

CYS 430 ILE 431 -0.0001

ILE 431 LYS 432 0.0001

LYS 432 ALA 433 -0.0622

ALA 433 ALA 434 -0.0002

ALA 434 ALA 435 -0.0001

ALA 435 ASP 436 -0.0003

ASP 436 ARG 437 -0.0084

ARG 437 VAL 438 -0.0001

VAL 438 VAL 439 0.0002

VAL 439 PHE 440 -0.0001

PHE 440 ILE 441 0.1010

ILE 441 ASN 442 -0.0002

ASN 442 THR 443 0.0003

THR 443 GLY 444 0.0000

GLY 444 PHE 445 0.1042

PHE 445 LEU 446 -0.0000

LEU 446 ASP 447 0.0001

ASP 447 ARG 448 0.0004

ARG 448 THR 449 0.0515

THR 449 GLY 450 0.0001

GLY 450 ASP 451 0.0001

ASP 451 GLU 452 0.0002

GLU 452 ILE 453 0.0099

ILE 453 HIS 454 -0.0003

HIS 454 THR 455 0.0004

THR 455 SER 456 -0.0005

SER 456 MET 457 0.0248

MET 457 GLU 458 0.0003

GLU 458 ALA 459 -0.0001

ALA 459 GLY 460 0.0005

GLY 460 PRO 461 0.0914

PRO 461 MET 462 -0.0002

MET 462 VAL 463 0.0005

VAL 463 ARG 464 -0.0004

ARG 464 LYS 465 0.0633

LYS 465 GLY 466 -0.0003

GLY 466 THR 467 -0.0003

THR 467 MET 468 -0.0003

MET 468 LYS 469 -0.0199

LYS 469 SER 470 -0.0002

SER 470 GLN 471 -0.0000

GLN 471 PRO 472 0.0002

PRO 472 TRP 473 -0.0146

TRP 473 ILE 474 0.0001

ILE 474 LEU 475 0.0002

LEU 475 ALA 476 0.0003

ALA 476 TYR 477 -0.0156

TYR 477 GLU 478 0.0001

GLU 478 ASP 479 0.0004

ASP 479 HIS 480 0.0004

HIS 480 ASN 481 0.0329

ASN 481 VAL 482 0.0001

VAL 482 ASP 483 0.0000

ASP 483 ALA 484 -0.0002

ALA 484 GLY 485 0.0622

GLY 485 LEU 486 -0.0003

LEU 486 ALA 487 0.0003

ALA 487 ALA 488 0.0004

ALA 488 GLY 489 -0.0055

GLY 489 PHE 490 -0.0002

PHE 490 SER 491 -0.0003

SER 491 GLY 492 0.0002

GLY 492 ARG 493 -0.0169

ARG 493 ALA 494 -0.0000

ALA 494 GLN 495 0.0003

GLN 495 VAL 496 -0.0002

VAL 496 GLY 497 0.0285

GLY 497 LYS 498 -0.0000

LYS 498 GLY 499 -0.0000

GLY 499 MET 500 0.0001

MET 500 TRP 501 -0.1883

TRP 501 THR 502 -0.0000

THR 502 MET 503 0.0000

MET 503 THR 504 -0.0002

THR 504 GLU 505 -0.1501

GLU 505 LEU 506 0.0003

LEU 506 MET 507 0.0001

MET 507 ALA 508 -0.0001

ALA 508 ASP 509 -0.1166

ASP 509 MET 510 -0.0000

MET 510 VAL 511 -0.0000

VAL 511 GLU 512 -0.0002

GLU 512 THR 513 -0.1263

THR 513 LYS 514 -0.0000

LYS 514 ILE 515 -0.0002

ILE 515 ALA 516 -0.0000

ALA 516 GLN 517 -0.1876

GLN 517 PRO 518 0.0005

PRO 518 ARG 519 0.0000

ARG 519 ALA 520 0.0001

ALA 520 GLY 521 0.0076

GLY 521 ALA 522 0.0002

ALA 522 SER 523 -0.0001

SER 523 THR 524 -0.0001

THR 524 ALA 525 0.0743

ALA 525 TRP 526 -0.0000

TRP 526 VAL 527 -0.0000

VAL 527 PRO 528 -0.0002

PRO 528 SER 529 -0.0810

SER 529 PRO 530 0.0001

PRO 530 THR 531 0.0002

THR 531 ALA 532 -0.0004

ALA 532 ALA 533 0.0450

ALA 533 THR 534 -0.0000

THR 534 LEU 535 0.0002

LEU 535 HIS 536 0.0003

HIS 536 ALA 537 0.0170

ALA 537 LEU 538 -0.0001

LEU 538 HIS 539 0.0001

HIS 539 TYR 540 0.0004

TYR 540 HIS 541 -0.0062

HIS 541 GLN 542 -0.0003

GLN 542 VAL 543 -0.0002

VAL 543 ASP 544 -0.0001

ASP 544 VAL 545 -0.0637

VAL 545 ALA 546 -0.0001

ALA 546 ALA 547 0.0000

ALA 547 VAL 548 -0.0003

VAL 548 GLN 549 -0.0890

GLN 549 GLN 550 -0.0003

GLN 550 GLY 551 -0.0002

GLY 551 LEU 552 0.0001

LEU 552 ALA 553 -0.0528

ALA 553 GLY 554 -0.0000

GLY 554 LYS 555 0.0004

LYS 555 ARG 556 -0.0004

ARG 556 ARG 557 0.0113

ARG 557 ALA 558 -0.0003

ALA 558 THR 559 0.0002

THR 559 ILE 560 -0.0005

ILE 560 GLU 561 0.0302

GLU 561 GLN 562 0.0000

GLN 562 LEU 563 -0.0002

LEU 563 LEU 564 -0.0001

LEU 564 THR 565 -0.0902

THR 565 ILE 566 0.0003

ILE 566 PRO 567 -0.0003

PRO 567 LEU 568 -0.0002

LEU 568 ALA 569 -0.0696

ALA 569 LYS 570 -0.0001

LYS 570 GLU 571 -0.0002

GLU 571 LEU 572 0.0002

LEU 572 ALA 573 -0.0190

ALA 573 TRP 574 -0.0001

TRP 574 ALA 575 -0.0000

ALA 575 PRO 576 0.0006

PRO 576 ASP 577 -0.0037

ASP 577 GLU 578 0.0002

GLU 578 ILE 579 0.0004

ILE 579 ARG 580 0.0003

ARG 580 GLU 581 0.0088

GLU 581 GLU 582 -0.0002

GLU 582 VAL 583 0.0002

VAL 583 ASP 584 0.0003

ASP 584 ASN 585 0.0247

ASN 585 ASN 586 -0.0002

ASN 586 CYS 587 -0.0003

CYS 587 GLN 588 0.0000

GLN 588 SER 589 0.0622

SER 589 ILE 590 -0.0000

ILE 590 LEU 591 -0.0003

LEU 591 GLY 592 -0.0000

GLY 592 TYR 593 0.0988

TYR 593 VAL 594 -0.0001

VAL 594 VAL 595 0.0002

VAL 595 ARG 596 -0.0002

ARG 596 TRP 597 0.0463

TRP 597 VAL 598 -0.0004

VAL 598 ASP 599 -0.0000

ASP 599 GLN 600 -0.0002

GLN 600 GLY 601 0.1351

GLY 601 VAL 602 -0.0000

VAL 602 GLY 603 0.0001

GLY 603 CYS 604 -0.0001

CYS 604 SER 605 0.1100

SER 605 LYS 606 0.0003

LYS 606 VAL 607 -0.0003

VAL 607 PRO 608 0.0002

PRO 608 ASP 609 0.0461

ASP 609 ILE 610 0.0000

ILE 610 HIS 611 0.0001

HIS 611 ASP 612 0.0002

ASP 612 VAL 613 0.2441

VAL 613 ALA 614 -0.0002

ALA 614 LEU 615 0.0000

LEU 615 MET 616 -0.0001

MET 616 GLU 617 -0.0850

GLU 617 ASP 618 -0.0001

ASP 618 ARG 619 0.0006

ARG 619 ALA 620 -0.0002

ALA 620 THR 621 0.0721

THR 621 LEU 622 0.0000

LEU 622 ARG 623 -0.0002

ARG 623 ILE 624 -0.0002

ILE 624 SER 625 0.0888

SER 625 SER 626 -0.0000

SER 626 GLN 627 -0.0003

GLN 627 LEU 628 -0.0002

LEU 628 LEU 629 0.0282

LEU 629 ALA 630 0.0001

ALA 630 ASN 631 -0.0000

ASN 631 TRP 632 0.0001

TRP 632 LEU 633 -0.0126

LEU 633 ARG 634 0.0000

ARG 634 HIS 635 -0.0002

HIS 635 GLY 636 -0.0003

GLY 636 VAL 637 0.0516

VAL 637 ILE 638 0.0003

ILE 638 THR 639 0.0002

THR 639 SER 640 -0.0001

SER 640 ALA 641 -0.1073

ALA 641 ASP 642 0.0000

ASP 642 VAL 643 -0.0002

VAL 643 ARG 644 -0.0001

ARG 644 ALA 645 -0.0092

ALA 645 SER 646 0.0000

SER 646 LEU 647 -0.0001

LEU 647 GLU 648 0.0002

GLU 648 ARG 649 0.0133

ARG 649 MET 650 0.0001

MET 650 ALA 651 -0.0004

ALA 651 PRO 652 0.0000

PRO 652 LEU 653 0.0716

LEU 653 VAL 654 0.0001

VAL 654 ASP 655 0.0000

ASP 655 ARG 656 -0.0001

ARG 656 GLN 657 0.0067

GLN 657 ASN 658 0.0003

ASN 658 ALA 659 0.0002

ALA 659 GLY 660 0.0001

GLY 660 ASP 661 -0.0146

ASP 661 VAL 662 0.0003

VAL 662 ALA 663 0.0001

ALA 663 TYR 664 0.0000

TYR 664 ARG 665 -0.0607

ARG 665 PRO 666 0.0003

PRO 666 MET 667 -0.0001

MET 667 ALA 668 0.0002

ALA 668 PRO 669 0.0650

PRO 669 ASN 670 0.0002

ASN 670 PHE 671 -0.0002

PHE 671 ASP 672 -0.0001

ASP 672 ASP 673 -0.0054

ASP 673 SER 674 -0.0002

SER 674 ILE 675 0.0001

ILE 675 ALA 676 0.0000

ALA 676 PHE 677 0.0440

PHE 677 LEU 678 -0.0001

LEU 678 ALA 679 -0.0003

ALA 679 ALA 680 -0.0000

ALA 680 GLN 681 0.0010

GLN 681 GLU 682 -0.0001

GLU 682 LEU 683 0.0001

LEU 683 ILE 684 0.0006

ILE 684 LEU 685 0.0373

LEU 685 SER 686 0.0000

SER 686 GLY 687 0.0001

GLY 687 ALA 688 -0.0003

ALA 688 GLN 689 -0.0573

GLN 689 GLN 690 0.0004

GLN 690 PRO 691 -0.0002

PRO 691 ASN 692 -0.0005

ASN 692 GLY 693 0.0228

GLY 693 TYR 694 0.0002

TYR 694 THR 695 -0.0002

THR 695 GLU 696 0.0004

GLU 696 PRO 697 0.0176

PRO 697 ILE 698 0.0001

ILE 698 LEU 699 -0.0000

LEU 699 HIS 700 0.0005

HIS 700 ARG 701 0.0420

ARG 701 ARG 702 0.0002

ARG 702 ARG 703 -0.0000

ARG 703 ARG 704 -0.0003

ARG 704 GLU 705 0.0827

GLU 705 PHE 706 0.0002

PHE 706 LYS 707 -0.0000

LYS 707 ALA 708 -0.0000

ALA 708 ARG 709 0.0866

ARG 709 ALA 710 -0.0002

ALA 710 ALA 711 -0.0002

ALA 711 GLU 712 -0.0000

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).
Last modification: April 25th, 2023.

Should you encounter any unexpected behaviour, please let us know.

*** 6DNP_unrelaxed_rank_001_alphafold2_ptm_model_5_seed_000 ***

CA strain for 240220091727167243

--- normal mode 15 ---

Should you encounter any unexpected behaviour,
please let us know.

* 6DNP_unrelaxed_rank_001_alphafold2_ptm_model_5_seed_000 *