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

* Xilanase_model-Aalphafold_complete *

CA strain for 2404070639312775027

--- normal mode 8 ---

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
MET 1 LYS 2 0.0004

LYS 2 LEU 3 -0.0003

LEU 3 GLY 4 -0.0031

GLY 4 GLU 5 -0.0003

GLU 5 LYS 6 0.0002

LYS 6 ASN 7 -0.0021

ASN 7 LEU 8 -0.0000

LEU 8 GLN 9 -0.0001

GLN 9 PHE 10 -0.0030

PHE 10 TYR 11 0.0002

TYR 11 PHE 12 -0.0004

PHE 12 LEU 13 -0.0014

LEU 13 LEU 14 0.0001

LEU 14 VAL 15 -0.0000

VAL 15 LEU 16 -0.0037

LEU 16 PRO 17 0.0000

PRO 17 TYR 18 -0.0000

TYR 18 ALA 19 0.0099

ALA 19 LEU 20 0.0001

LEU 20 LEU 21 0.0001

LEU 21 PHE 22 -0.0042

PHE 22 PRO 23 0.0004

PRO 23 GLY 24 0.0001

GLY 24 LEU 25 -0.0049

LEU 25 GLU 26 -0.0002

GLU 26 THR 27 -0.0001

THR 27 ASN 28 0.0190

ASN 28 ALA 29 0.0000

ALA 29 LEU 30 0.0002

LEU 30 SER 31 0.0034

SER 31 TYR 32 0.0003

TYR 32 ASP 33 -0.0005

ASP 33 TYR 34 0.0009

TYR 34 THR 35 -0.0002

THR 35 ALA 36 -0.0003

ALA 36 SER 37 -0.0002

SER 37 ILE 38 -0.0004

ILE 38 GLN 39 -0.0003

GLN 39 CYS 40 0.0000

CYS 40 LEU 41 -0.0002

LEU 41 GLU 42 0.0001

GLU 42 ASN 43 0.0001

ASN 43 PRO 44 0.0003

PRO 44 GLN 45 0.0001

GLN 45 LYS 46 0.0004

LYS 46 ALA 47 -0.0002

ALA 47 GLN 48 -0.0002

GLN 48 TYR 49 -0.0000

TYR 49 GLY 50 -0.0001

GLY 50 GLY 51 0.0001

GLY 51 GLY 52 0.0001

GLY 52 ILE 53 -0.0000

ILE 53 ILE 54 -0.0002

ILE 54 THR 55 -0.0000

THR 55 ASN 56 0.0001

ASN 56 PRO 57 0.0000

PRO 57 GLU 58 -0.0003

GLU 58 LEU 59 -0.0001

LEU 59 ASN 60 -0.0001

ASN 60 GLN 61 -0.0000

GLN 61 GLY 62 0.0004

GLY 62 LEU 63 -0.0001

LEU 63 LYS 64 0.0000

LYS 64 GLY 65 0.0001

GLY 65 TRP 66 0.0001

TRP 66 SER 67 0.0002

SER 67 THR 68 -0.0002

THR 68 PHE 69 0.0001

PHE 69 GLY 70 -0.0001

GLY 70 ASP 71 0.0005

ASP 71 ALA 72 -0.0004

ALA 72 LYS 73 -0.0002

LYS 73 ILE 74 0.0000

ILE 74 GLN 75 0.0002

GLN 75 HIS 76 -0.0000

HIS 76 ARG 77 -0.0001

ARG 77 VAL 78 -0.0000

VAL 78 ALA 79 0.0004

ALA 79 GLY 80 -0.0000

GLY 80 SER 81 -0.0003

SER 81 ASN 82 0.0001

ASN 82 SER 83 -0.0002

SER 83 PHE 84 -0.0003

PHE 84 ILE 85 -0.0002

ILE 85 VAL 86 0.0004

VAL 86 ALA 87 -0.0003

ALA 87 HIS 88 -0.0001

HIS 88 THR 89 0.0002

THR 89 ARG 90 -0.0000

ARG 90 SER 91 -0.0002

SER 91 GLN 92 -0.0002

GLN 92 PRO 93 0.0001

PRO 93 HIS 94 0.0001

HIS 94 ASP 95 -0.0001

ASP 95 SER 96 0.0001

SER 96 VAL 97 -0.0000

VAL 97 SER 98 -0.0003

SER 98 GLN 99 0.0001

GLN 99 THR 100 -0.0000

THR 100 LEU 101 0.0001

LEU 101 TYR 102 -0.0001

TYR 102 LEU 103 0.0001

LEU 103 GLN 104 0.0003

GLN 104 SER 105 -0.0001

SER 105 ASN 106 0.0002

ASN 106 LYS 107 0.0003

LYS 107 LEU 108 0.0001

LEU 108 TYR 109 0.0000

TYR 109 THR 110 -0.0003

THR 110 PHE 111 -0.0000

PHE 111 SER 112 0.0001

SER 112 ALA 113 -0.0003

ALA 113 TRP 114 -0.0001

TRP 114 ILE 115 -0.0000

ILE 115 ARG 116 -0.0001

ARG 116 VAL 117 -0.0003

VAL 117 SER 118 0.0002

SER 118 GLU 119 -0.0002

GLU 119 GLY 120 0.0001

GLY 120 LYS 121 -0.0001

LYS 121 THR 122 0.0002

THR 122 PRO 123 -0.0001

PRO 123 VAL 124 0.0001

VAL 124 LYS 125 0.0000

LYS 125 ALA 126 -0.0001

ALA 126 ILE 127 0.0000

ILE 127 PHE 128 0.0004

PHE 128 LYS 129 -0.0001

LYS 129 THR 130 0.0001

THR 130 LYS 131 -0.0003

LYS 131 SER 132 0.0001

SER 132 GLY 133 -0.0000

GLY 133 TYR 134 -0.0002

TYR 134 LYS 135 -0.0000

LYS 135 TYR 136 -0.0001

TYR 136 ALA 137 0.0000

ALA 137 GLY 138 -0.0002

GLY 138 ALA 139 0.0002

ALA 139 VAL 140 -0.0001

VAL 140 VAL 141 0.0000

VAL 141 ALA 142 0.0000

ALA 142 GLU 143 0.0002

GLU 143 SER 144 -0.0004

SER 144 ASN 145 0.0002

ASN 145 CYS 146 0.0002

CYS 146 TRP 147 -0.0001

TRP 147 SER 148 0.0001

SER 148 MET 149 0.0001

MET 149 LEU 150 0.0001

LEU 150 LYS 151 -0.0001

LYS 151 GLY 152 0.0002

GLY 152 GLY 153 -0.0003

GLY 153 LEU 154 -0.0000

LEU 154 THR 155 0.0001

THR 155 VAL 156 -0.0000

VAL 156 ASP 157 0.0001

ASP 157 ALA 158 0.0003

ALA 158 SER 159 -0.0002

SER 159 GLY 160 0.0000

GLY 160 PRO 161 -0.0003

PRO 161 ALA 162 0.0002

ALA 162 GLU 163 0.0002

GLU 163 LEU 164 -0.0003

LEU 164 TYR 165 0.0000

TYR 165 PHE 166 0.0003

PHE 166 GLU 167 -0.0002

GLU 167 THR 168 -0.0001

THR 168 ASP 169 -0.0001

ASP 169 ASN 170 -0.0002

ASN 170 THR 171 -0.0005

THR 171 SER 172 0.0000

SER 172 VAL 173 -0.0001

VAL 173 GLU 174 0.0002

GLU 174 ILE 175 0.0001

ILE 175 TRP 176 -0.0003

TRP 176 ILE 177 0.0000

ILE 177 ASP 178 0.0002

ASP 178 SER 179 -0.0001

SER 179 ILE 180 0.0003

ILE 180 SER 181 -0.0000

SER 181 LEU 182 -0.0000

LEU 182 GLN 183 0.0001

GLN 183 PRO 184 0.0004

PRO 184 PHE 185 0.0002

PHE 185 THR 186 -0.0002

THR 186 GLN 187 -0.0001

GLN 187 GLN 188 -0.0001

GLN 188 GLU 189 0.0001

GLU 189 TRP 190 0.0004

TRP 190 LYS 191 -0.0001

LYS 191 SER 192 0.0003

SER 192 HIS 193 -0.0007

HIS 193 GLN 194 0.0003

GLN 194 ASP 195 -0.0002

ASP 195 GLN 196 -0.0003

GLN 196 SER 197 0.0002

SER 197 ILE 198 -0.0003

ILE 198 LYS 199 -0.0003

LYS 199 LYS 200 -0.0001

LYS 200 ILE 201 -0.0003

ILE 201 ARG 202 0.0004

ARG 202 LYS 203 -0.0001

LYS 203 LYS 204 0.0001

LYS 204 ASN 205 -0.0001

ASN 205 VAL 206 -0.0001

VAL 206 ARG 207 0.0001

ARG 207 ILE 208 0.0001

ILE 208 GLN 209 0.0000

GLN 209 ALA 210 0.0001

ALA 210 VAL 211 -0.0003

VAL 211 ASP 212 -0.0000

ASP 212 LYS 213 -0.0002

LYS 213 LEU 214 0.0001

LEU 214 GLY 215 -0.0002

GLY 215 ASN 216 0.0000

ASN 216 PRO 217 0.0001

PRO 217 LEU 218 0.0003

LEU 218 PRO 219 0.0001

PRO 219 ASN 220 -0.0003

ASN 220 THR 221 -0.0000

THR 221 THR 222 0.0000

THR 222 VAL 223 -0.0004

VAL 223 SER 224 0.0001

SER 224 ILE 225 0.0001

ILE 225 SER 226 0.0003

SER 226 PRO 227 -0.0003

PRO 227 LYS 228 0.0000

LYS 228 LYS 229 0.0000

LYS 229 ILE 230 0.0002

ILE 230 GLY 231 0.0000

GLY 231 PHE 232 0.0005

PHE 232 PRO 233 -0.0002

PRO 233 PHE 234 0.0001

PHE 234 GLY 235 0.0000

GLY 235 CYS 236 0.0002

CYS 236 ALA 237 -0.0001

ALA 237 ILE 238 -0.0000

ILE 238 ASN 239 -0.0001

ASN 239 ARG 240 -0.0002

ARG 240 ASN 241 -0.0002

ASN 241 ILE 242 0.0000

ILE 242 LEU 243 -0.0001

LEU 243 ASN 244 0.0000

ASN 244 ASN 245 0.0002

ASN 245 ASN 246 -0.0003

ASN 246 ALA 247 -0.0002

ALA 247 TYR 248 -0.0002

TYR 248 GLN 249 -0.0002

GLN 249 SER 250 0.0002

SER 250 TRP 251 0.0004

TRP 251 PHE 252 -0.0002

PHE 252 SER 253 0.0001

SER 253 SER 254 0.0000

SER 254 ARG 255 -0.0002

ARG 255 PHE 256 0.0000

PHE 256 THR 257 -0.0003

THR 257 VAL 258 -0.0004

VAL 258 THR 259 0.0004

THR 259 THR 260 -0.0000

THR 260 PHE 261 -0.0004

PHE 261 GLU 262 0.0002

GLU 262 ASN 263 0.0002

ASN 263 GLU 264 -0.0003

GLU 264 MET 265 0.0000

MET 265 LYS 266 0.0002

LYS 266 TRP 267 -0.0006

TRP 267 ALA 268 0.0003

ALA 268 SER 269 0.0003

SER 269 THR 270 -0.0001

THR 270 GLU 271 0.0001

GLU 271 PRO 272 0.0001

PRO 272 SER 273 0.0001

SER 273 GLN 274 0.0000

GLN 274 GLY 275 -0.0001

GLY 275 HIS 276 -0.0002

HIS 276 GLU 277 -0.0004

GLU 277 ASP 278 -0.0003

ASP 278 TYR 279 -0.0000

TYR 279 SER 280 -0.0000

SER 280 THR 281 -0.0000

THR 281 ALA 282 0.0000

ALA 282 ASP 283 0.0002

ASP 283 ALA 284 0.0002

ALA 284 MET 285 0.0000

MET 285 VAL 286 0.0001

VAL 286 GLN 287 -0.0000

GLN 287 PHE 288 0.0000

PHE 288 ALA 289 -0.0003

ALA 289 LYS 290 -0.0002

LYS 290 LYS 291 -0.0001

LYS 291 ASN 292 -0.0001

ASN 292 GLY 293 0.0000

GLY 293 ILE 294 0.0003

ILE 294 ALA 295 0.0000

ALA 295 ILE 296 0.0000

ILE 296 ARG 297 0.0002

ARG 297 GLY 298 -0.0005

GLY 298 HIS 299 0.0001

HIS 299 ASN 300 0.0004

ASN 300 VAL 301 -0.0003

VAL 301 PHE 302 0.0002

PHE 302 TRP 303 -0.0001

TRP 303 ASP 304 0.0001

ASP 304 ASP 305 0.0002

ASP 305 PRO 306 -0.0003

PRO 306 LYS 307 -0.0003

LYS 307 TYR 308 0.0004

TYR 308 GLN 309 -0.0000

GLN 309 SER 310 -0.0004

SER 310 GLY 311 0.0003

GLY 311 TRP 312 -0.0000

TRP 312 VAL 313 0.0002

VAL 313 SER 314 0.0001

SER 314 SER 315 0.0002

SER 315 LEU 316 -0.0004

LEU 316 SER 317 -0.0000

SER 317 PRO 318 0.0002

PRO 318 ASN 319 -0.0005

ASN 319 ASP 320 0.0000

ASP 320 LEU 321 0.0001

LEU 321 ASN 322 -0.0000

ASN 322 ALA 323 -0.0000

ALA 323 ALA 324 -0.0002

ALA 324 ALA 325 -0.0001

ALA 325 THR 326 -0.0000

THR 326 LYS 327 0.0002

LYS 327 ARG 328 0.0004

ARG 328 ILE 329 0.0002

ILE 329 ASN 330 0.0001

ASN 330 SER 331 -0.0000

SER 331 VAL 332 0.0001

VAL 332 MET 333 0.0001

MET 333 ASN 334 0.0003

ASN 334 ARG 335 -0.0000

ARG 335 TYR 336 -0.0000

TYR 336 LYS 337 0.0001

LYS 337 GLY 338 0.0002

GLY 338 GLN 339 -0.0003

GLN 339 VAL 340 -0.0001

VAL 340 ILE 341 -0.0002

ILE 341 GLY 342 -0.0002

GLY 342 TRP 343 0.0000

TRP 343 ASP 344 -0.0000

ASP 344 VAL 345 -0.0003

VAL 345 VAL 346 0.0002

VAL 346 ASN 347 -0.0000

ASN 347 GLU 348 0.0001

GLU 348 ASN 349 0.0001

ASN 349 LEU 350 0.0000

LEU 350 HIS 351 -0.0003

HIS 351 PHE 352 0.0001

PHE 352 SER 353 -0.0003

SER 353 PHE 354 -0.0004

PHE 354 PHE 355 0.0000

PHE 355 GLU 356 -0.0000

GLU 356 SER 357 0.0003

SER 357 LYS 358 -0.0001

LYS 358 LEU 359 0.0001

LEU 359 GLY 360 -0.0002

GLY 360 ALA 361 0.0001

ALA 361 ASN 362 -0.0000

ASN 362 ALA 363 -0.0003

ALA 363 SER 364 0.0001

SER 364 ALA 365 0.0001

ALA 365 VAL 366 0.0004

VAL 366 PHE 367 0.0002

PHE 367 TYR 368 -0.0001

TYR 368 GLY 369 -0.0003

GLY 369 GLU 370 0.0000

GLU 370 ALA 371 -0.0001

ALA 371 HIS 372 -0.0001

HIS 372 LYS 373 0.0002

LYS 373 THR 374 -0.0002

THR 374 ASP 375 -0.0003

ASP 375 PRO 376 0.0001

PRO 376 SER 377 0.0002

SER 377 THR 378 -0.0001

THR 378 THR 379 0.0002

THR 379 LEU 380 0.0000

LEU 380 PHE 381 -0.0002

PHE 381 MET 382 -0.0002

MET 382 ASN 383 -0.0000

ASN 383 GLU 384 0.0001

GLU 384 TYR 385 -0.0002

TYR 385 ASN 386 -0.0003

ASN 386 THR 387 -0.0001

THR 387 VAL 388 -0.0001

VAL 388 GLU 389 0.0002

GLU 389 ASP 390 -0.0002

ASP 390 SER 391 -0.0000

SER 391 ARG 392 0.0000

ARG 392 ASP 393 0.0002

ASP 393 GLY 394 -0.0003

GLY 394 GLN 395 -0.0001

GLN 395 ALA 396 0.0003

ALA 396 THR 397 -0.0004

THR 397 PRO 398 0.0002

PRO 398 ALA 399 -0.0000

ALA 399 LYS 400 0.0001

LYS 400 TYR 401 -0.0001

TYR 401 LEU 402 0.0001

LEU 402 GLU 403 0.0002

GLU 403 LYS 404 -0.0000

LYS 404 LEU 405 0.0000

LEU 405 ARG 406 0.0003

ARG 406 SER 407 -0.0001

SER 407 ILE 408 -0.0004

ILE 408 GLN 409 0.0002

GLN 409 SER 410 -0.0000

SER 410 LEU 411 -0.0003

LEU 411 PRO 412 0.0000

PRO 412 GLY 413 0.0003

GLY 413 ASN 414 0.0000

ASN 414 GLY 415 -0.0001

GLY 415 ASN 416 0.0003

ASN 416 MET 417 0.0001

MET 417 GLY 418 -0.0001

GLY 418 ILE 419 -0.0001

ILE 419 GLY 420 0.0000

GLY 420 LEU 421 0.0003

LEU 421 GLU 422 -0.0002

GLU 422 SER 423 -0.0000

SER 423 HIS 424 0.0003

HIS 424 PHE 425 -0.0003

PHE 425 SER 426 0.0006

SER 426 SER 427 -0.0002

SER 427 SER 428 0.0001

SER 428 PRO 429 0.0001

PRO 429 PRO 430 0.0002

PRO 430 ASN 431 0.0001

ASN 431 ILE 432 0.0001

ILE 432 PRO 433 -0.0001

PRO 433 TYR 434 -0.0001

TYR 434 MET 435 0.0001

MET 435 ARG 436 -0.0000

ARG 436 SER 437 -0.0000

SER 437 ALA 438 -0.0001

ALA 438 ILE 439 -0.0004

ILE 439 ASP 440 0.0003

ASP 440 THR 441 0.0000

THR 441 LEU 442 0.0004

LEU 442 ALA 443 -0.0002

ALA 443 ALA 444 0.0001

ALA 444 THR 445 0.0003

THR 445 GLY 446 0.0000

GLY 446 LEU 447 0.0000

LEU 447 PRO 448 0.0002

PRO 448 VAL 449 0.0001

VAL 449 TRP 450 -0.0001

TRP 450 LEU 451 0.0000

LEU 451 THR 452 0.0003

THR 452 GLU 453 -0.0000

GLU 453 VAL 454 -0.0002

VAL 454 ASP 455 -0.0003

ASP 455 VAL 456 0.0001

VAL 456 GLN 457 -0.0000

GLN 457 SER 458 0.0002

SER 458 GLY 459 0.0000

GLY 459 GLY 460 -0.0005

GLY 460 ASN 461 0.0002

ASN 461 GLN 462 0.0000

GLN 462 ALA 463 -0.0001

ALA 463 GLN 464 0.0004

GLN 464 SER 465 0.0001

SER 465 LEU 466 -0.0002

LEU 466 GLU 467 0.0000

GLU 467 GLN 468 0.0000

GLN 468 ILE 469 0.0001

ILE 469 LEU 470 -0.0001

LEU 470 ARG 471 -0.0001

ARG 471 GLU 472 -0.0000

GLU 472 ALA 473 -0.0004

ALA 473 HIS 474 0.0003

HIS 474 SER 475 -0.0005

SER 475 HIS 476 0.0005

HIS 476 PRO 477 -0.0000

PRO 477 LYS 478 -0.0001

LYS 478 VAL 479 0.0001

VAL 479 ARG 480 -0.0000

ARG 480 GLY 481 -0.0002

GLY 481 ILE 482 0.0001

ILE 482 VAL 483 0.0003

VAL 483 ILE 484 0.0000

ILE 484 TRP 485 0.0001

TRP 485 SER 486 0.0001

SER 486 ALA 487 0.0001

ALA 487 TRP 488 0.0001

TRP 488 SER 489 0.0004

SER 489 PRO 490 -0.0000

PRO 490 ASN 491 -0.0001

ASN 491 GLY 492 -0.0000

GLY 492 CYS 493 -0.0004

CYS 493 TYR 494 -0.0000

TYR 494 ARG 495 0.0001

ARG 495 MET 496 0.0003

MET 496 CYS 497 -0.0000

CYS 497 LEU 498 0.0000

LEU 498 THR 499 -0.0000

THR 499 ASP 500 -0.0002

ASP 500 ASN 501 0.0002

ASN 501 ASN 502 -0.0003

ASN 502 PHE 503 -0.0002

PHE 503 HIS 504 0.0003

HIS 504 ASN 505 -0.0002

ASN 505 LEU 506 -0.0002

LEU 506 PRO 507 -0.0001

PRO 507 THR 508 -0.0002

THR 508 GLY 509 -0.0001

GLY 509 ASP 510 -0.0001

ASP 510 VAL 511 0.0001

VAL 511 VAL 512 0.0000

VAL 512 ASP 513 -0.0000

ASP 513 LYS 514 0.0002

LYS 514 LEU 515 0.0003

LEU 515 LEU 516 0.0006

LEU 516 ARG 517 -0.0002

ARG 517 GLU 518 0.0002

GLU 518 TRP 519 -0.0000

TRP 519 GLY 520 0.0005

GLY 520 GLY 521 -0.0001

GLY 521 GLY 522 -0.0002

GLY 522 ALA 523 -0.0002

ALA 523 THR 524 0.0001

THR 524 VAL 525 -0.0002

VAL 525 LYS 526 -0.0005

LYS 526 GLY 527 -0.0000

GLY 527 LYS 528 -0.0000

LYS 528 THR 529 0.0001

THR 529 ASP 530 0.0001

ASP 530 GLN 531 0.0001

GLN 531 ASN 532 -0.0004

ASN 532 GLY 533 -0.0002

GLY 533 PHE 534 -0.0002

PHE 534 PHE 535 0.0003

PHE 535 GLN 536 -0.0004

GLN 536 SER 537 0.0002

SER 537 SER 538 -0.0004

SER 538 LEU 539 0.0003

LEU 539 PHE 540 -0.0002

PHE 540 HIS 541 -0.0001

HIS 541 GLY 542 0.0005

GLY 542 ASP 543 -0.0001

ASP 543 TYR 544 0.0001

TYR 544 GLU 545 -0.0000

GLU 545 ILE 546 0.0002

ILE 546 LYS 547 -0.0001

LYS 547 VAL 548 0.0003

VAL 548 GLN 549 -0.0001

GLN 549 VAL 550 -0.0002

VAL 550 ASN 551 -0.0000

ASN 551 HIS 552 -0.0000

HIS 552 PRO 553 0.0003

PRO 553 SER 554 0.0002

SER 554 LYS 555 0.0000

LYS 555 LEU 556 0.0001

LEU 556 PRO 557 -0.0003

PRO 557 SER 558 0.0001

SER 558 SER 559 -0.0000

SER 559 SER 560 -0.0003

SER 560 SER 561 -0.0001

SER 561 HIS 562 0.0002

HIS 562 HIS 563 0.0005

HIS 563 THR 564 -0.0001

THR 564 PHE 565 -0.0000

PHE 565 LYS 566 0.0001

LYS 566 LEU 567 -0.0003

LEU 567 ASN 568 0.0002

ASN 568 SER 569 -0.0003

SER 569 THR 570 -0.0000

THR 570 ASP 571 0.0003

ASP 571 ASP 572 -0.0004

ASP 572 GLU 573 0.0002

GLU 573 SER 574 0.0002

SER 574 LYS 575 -0.0002

LYS 575 GLN 576 -0.0000

GLN 576 THR 577 -0.0003

THR 577 ARG 578 -0.0002

ARG 578 LEU 579 0.0005

LEU 579 LEU 580 0.0000

LEU 580 LEU 581 -0.0003

LEU 581 ILE 582 -0.0002

ILE 582 LYS 583 0.0005

LYS 583 VAL 584 -0.0003

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.

*** Xilanase_model-Aalphafold_complete ***

CA strain for 2404070639312775027

--- normal mode 8 ---

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

* Xilanase_model-Aalphafold_complete *