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

* *

CA strain for 2407140045133527185

--- normal mode 28 ---

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 ALA 2 0.0003

ALA 2 GLU 3 0.0001

GLU 3 GLU 4 -0.0002

GLU 4 LEU 5 -0.1617

LEU 5 LEU 6 0.0000

LEU 6 LEU 7 0.0000

LEU 7 GLU 8 -0.0002

GLU 8 ARG 9 0.1070

ARG 9 CYS 10 0.0001

CYS 10 ASP 11 0.0004

ASP 11 LEU 12 -0.0000

LEU 12 GLU 13 -0.0591

GLU 13 ILE 14 0.0002

ILE 14 GLN 15 -0.0002

GLN 15 ALA 16 -0.0000

ALA 16 ASN 17 0.0102

ASN 17 GLY 18 -0.0002

GLY 18 ARG 19 0.0000

ARG 19 ASP 20 -0.0001

ASP 20 HIS 21 0.0533

HIS 21 HIS 22 -0.0004

HIS 22 THR 23 0.0001

THR 23 ALA 24 -0.0004

ALA 24 ASP 25 -0.1892

ASP 25 LEU 26 0.0001

LEU 26 CYS 27 -0.0003

CYS 27 GLN 28 0.0001

GLN 28 GLU 29 0.0600

GLU 29 LYS 30 -0.0001

LYS 30 LEU 31 0.0001

LEU 31 VAL 32 -0.0002

VAL 32 LEU 33 -0.0049

LEU 33 ARG 34 -0.0000

ARG 34 ARG 35 -0.0001

ARG 35 GLY 36 -0.0002

GLY 36 GLN 37 0.0585

GLN 37 ARG 38 0.0001

ARG 38 PHE 39 0.0003

PHE 39 ARG 40 0.0003

ARG 40 LEU 41 0.0344

LEU 41 THR 42 0.0001

THR 42 LEU 43 -0.0001

LEU 43 TYR 44 -0.0001

TYR 44 PHE 45 0.0488

PHE 45 GLU 46 -0.0004

GLU 46 GLY 47 0.0005

GLY 47 ARG 48 0.0001

ARG 48 GLY 49 -0.1249

GLY 49 TYR 50 0.0001

TYR 50 GLU 51 0.0001

GLU 51 ALA 52 0.0002

ALA 52 SER 53 0.1364

SER 53 VAL 54 0.0000

VAL 54 ASP 55 0.0002

ASP 55 SER 56 0.0004

SER 56 LEU 57 -0.1890

LEU 57 THR 58 0.0000

THR 58 PHE 59 0.0001

PHE 59 GLY 60 -0.0005

GLY 60 ALA 61 -0.0350

ALA 61 VAL 62 -0.0001

VAL 62 THR 63 0.0001

THR 63 GLY 64 0.0002

GLY 64 PRO 65 0.0243

PRO 65 ASP 66 0.0003

ASP 66 PRO 67 0.0000

PRO 67 SER 68 -0.0001

SER 68 GLU 69 -0.0185

GLU 69 GLU 70 -0.0001

GLU 70 ALA 71 0.0001

ALA 71 GLY 72 0.0001

GLY 72 THR 73 -0.0525

THR 73 LYS 74 -0.0003

LYS 74 ALA 75 -0.0003

ALA 75 ARG 76 -0.0000

ARG 76 PHE 77 -0.1957

PHE 77 SER 78 -0.0003

SER 78 LEU 79 -0.0001

LEU 79 SER 80 -0.0001

SER 80 ASP 81 0.1024

ASP 81 ASN 82 -0.0001

ASN 82 VAL 83 0.0001

VAL 83 GLU 84 0.0004

GLU 84 GLU 85 -0.1175

GLU 85 GLY 86 -0.0000

GLY 86 SER 87 0.0002

SER 87 TRP 88 -0.0002

TRP 88 SER 89 -0.1533

SER 89 ALA 90 0.0001

ALA 90 SER 91 -0.0000

SER 91 VAL 92 0.0002

VAL 92 LEU 93 0.0462

LEU 93 ASP 94 -0.0001

ASP 94 GLN 95 -0.0000

GLN 95 GLN 96 -0.0002

GLN 96 ASP 97 -0.1939

ASP 97 ASN 98 -0.0000

ASN 98 VAL 99 -0.0002

VAL 99 LEU 100 -0.0001

LEU 100 SER 101 -0.0120

SER 101 LEU 102 -0.0001

LEU 102 GLN 103 -0.0001

GLN 103 LEU 104 0.0002

LEU 104 CYS 105 -0.0154

CYS 105 THR 106 0.0001

THR 106 PRO 107 0.0000

PRO 107 ALA 108 -0.0001

ALA 108 ASN 109 -0.0256

ASN 109 ALA 110 0.0001

ALA 110 PRO 111 0.0005

PRO 111 ILE 112 -0.0002

ILE 112 GLY 113 0.0715

GLY 113 LEU 114 0.0004

LEU 114 TYR 115 0.0001

TYR 115 ARG 116 -0.0003

ARG 116 LEU 117 0.0456

LEU 117 SER 118 -0.0001

SER 118 LEU 119 0.0001

LEU 119 GLU 120 -0.0003

GLU 120 ALA 121 0.1057

ALA 121 SER 122 -0.0000

SER 122 THR 123 0.0002

THR 123 GLY 124 0.0001

GLY 124 TYR 125 0.3262

TYR 125 GLN 126 0.0000

GLN 126 GLY 127 -0.0001

GLY 127 SER 128 -0.0000

SER 128 SER 129 -0.0125

SER 129 PHE 130 -0.0000

PHE 130 VAL 131 0.0005

VAL 131 LEU 132 0.0002

LEU 132 GLY 133 0.1835

GLY 133 HIS 134 0.0005

HIS 134 PHE 135 -0.0001

PHE 135 ILE 136 0.0002

ILE 136 LEU 137 0.0738

LEU 137 LEU 138 -0.0001

LEU 138 TYR 139 0.0003

TYR 139 ASN 140 -0.0001

ASN 140 ALA 141 0.0356

ALA 141 TRP 142 0.0001

TRP 142 CYS 143 0.0002

CYS 143 PRO 144 -0.0002

PRO 144 ALA 145 -0.0187

ALA 145 ASP 146 0.0002

ASP 146 ASP 147 -0.0002

ASP 147 VAL 148 -0.0001

VAL 148 TYR 149 -0.0430

TYR 149 LEU 150 -0.0001

LEU 150 ASP 151 0.0002

ASP 151 SER 152 0.0000

SER 152 GLU 153 -0.0173

GLU 153 GLU 154 -0.0001

GLU 154 GLU 155 -0.0002

GLU 155 ARG 156 0.0002

ARG 156 ARG 157 -0.0433

ARG 157 GLU 158 0.0001

GLU 158 TYR 159 -0.0003

TYR 159 VAL 160 0.0002

VAL 160 LEU 161 0.0229

LEU 161 THR 162 -0.0000

THR 162 GLN 163 -0.0000

GLN 163 GLN 164 0.0001

GLN 164 GLY 165 0.0170

GLY 165 PHE 166 0.0000

PHE 166 ILE 167 -0.0002

ILE 167 TYR 168 0.0001

TYR 168 GLN 169 -0.0619

GLN 169 GLY 170 -0.0001

GLY 170 SER 171 0.0002

SER 171 VAL 172 -0.0002

VAL 172 LYS 173 -0.1574

LYS 173 PHE 174 0.0001

PHE 174 ILE 175 -0.0001

ILE 175 LYS 176 -0.0000

LYS 176 SER 177 0.0668

SER 177 VAL 178 -0.0000

VAL 178 PRO 179 0.0001

PRO 179 TRP 180 0.0000

TRP 180 ASN 181 -0.0116

ASN 181 PHE 182 0.0002

PHE 182 GLY 183 -0.0000

GLY 183 GLN 184 -0.0003

GLN 184 PHE 185 0.0022

PHE 185 GLU 186 -0.0002

GLU 186 ASP 187 0.0003

ASP 187 GLY 188 -0.0002

GLY 188 ILE 189 -0.0419

ILE 189 LEU 190 0.0002

LEU 190 ASP 191 0.0002

ASP 191 THR 192 -0.0001

THR 192 CYS 193 -0.0133

CYS 193 LEU 194 0.0001

LEU 194 MET 195 -0.0002

MET 195 LEU 196 0.0002

LEU 196 LEU 197 0.0608

LEU 197 ASP 198 0.0003

ASP 198 MET 199 -0.0002

MET 199 ASN 200 -0.0002

ASN 200 PRO 201 0.0015

PRO 201 LYS 202 -0.0000

LYS 202 PHE 203 -0.0001

PHE 203 LEU 204 -0.0002

LEU 204 LYS 205 0.0871

LYS 205 ASN 206 -0.0000

ASN 206 ARG 207 -0.0002

ARG 207 SER 208 -0.0000

SER 208 ARG 209 -0.0623

ARG 209 ASP 210 0.0004

ASP 210 CYS 211 0.0002

CYS 211 SER 212 0.0001

SER 212 ARG 213 -0.0836

ARG 213 ARG 214 -0.0000

ARG 214 SER 215 0.0002

SER 215 SER 216 0.0000

SER 216 PRO 217 -0.1021

PRO 217 ILE 218 0.0000

ILE 218 TYR 219 -0.0001

TYR 219 VAL 220 0.0000

VAL 220 GLY 221 -0.0229

GLY 221 ARG 222 0.0000

ARG 222 VAL 223 0.0003

VAL 223 VAL 224 -0.0001

VAL 224 SER 225 -0.0257

SER 225 ALA 226 0.0002

ALA 226 MET 227 -0.0000

MET 227 VAL 228 0.0001

VAL 228 ASN 229 -0.0118

ASN 229 CYS 230 0.0002

CYS 230 ASN 231 0.0000

ASN 231 ASP 232 0.0001

ASP 232 ASP 233 0.0627

ASP 233 GLN 234 0.0002

GLN 234 GLY 235 -0.0001

GLY 235 VAL 236 -0.0001

VAL 236 LEU 237 -0.0198

LEU 237 LEU 238 0.0002

LEU 238 GLY 239 -0.0001

GLY 239 ARG 240 -0.0001

ARG 240 TRP 241 0.0149

TRP 241 ASP 242 -0.0002

ASP 242 ASN 243 -0.0001

ASN 243 ASN 244 0.0002

ASN 244 TYR 245 -0.0533

TYR 245 GLY 246 0.0000

GLY 246 ASP 247 0.0001

ASP 247 GLY 248 0.0005

GLY 248 ILE 249 -0.0272

ILE 249 SER 250 -0.0002

SER 250 PRO 251 0.0003

PRO 251 MET 252 -0.0002

MET 252 ALA 253 -0.0310

ALA 253 TRP 254 -0.0002

TRP 254 ILE 255 -0.0002

ILE 255 GLY 256 0.0001

GLY 256 SER 257 0.0054

SER 257 VAL 258 0.0004

VAL 258 ASP 259 -0.0004

ASP 259 ILE 260 0.0000

ILE 260 LEU 261 -0.0249

LEU 261 ARG 262 0.0001

ARG 262 ARG 263 -0.0002

ARG 263 TRP 264 -0.0001

TRP 264 LYS 265 0.0046

LYS 265 GLU 266 -0.0000

GLU 266 HIS 267 -0.0000

HIS 267 GLY 268 0.0001

GLY 268 CYS 269 0.0457

CYS 269 GLN 270 -0.0002

GLN 270 GLN 271 0.0001

GLN 271 VAL 272 0.0003

VAL 272 LYS 273 -0.0613

LYS 273 TYR 274 -0.0003

TYR 274 GLY 275 0.0001

GLY 275 GLN 276 0.0003

GLN 276 CYS 277 0.0652

CYS 277 TRP 278 0.0002

TRP 278 VAL 279 -0.0001

VAL 279 PHE 280 -0.0000

PHE 280 ALA 281 0.0397

ALA 281 ALA 282 0.0001

ALA 282 VAL 283 0.0001

VAL 283 ALA 284 0.0000

ALA 284 CYS 285 0.0086

CYS 285 THR 286 0.0003

THR 286 VAL 287 -0.0000

VAL 287 LEU 288 -0.0001

LEU 288 ARG 289 0.0094

ARG 289 CYS 290 -0.0002

CYS 290 LEU 291 0.0001

LEU 291 GLY 292 0.0001

GLY 292 ILE 293 0.0455

ILE 293 PRO 294 -0.0001

PRO 294 THR 295 -0.0004

THR 295 ARG 296 -0.0000

ARG 296 VAL 297 -0.0814

VAL 297 VAL 298 -0.0003

VAL 298 THR 299 -0.0002

THR 299 ASN 300 0.0002

ASN 300 TYR 301 -0.0930

TYR 301 ASN 302 -0.0004

ASN 302 SER 303 0.0005

SER 303 ALA 304 -0.0003

ALA 304 HIS 305 -0.0650

HIS 305 ASP 306 0.0001

ASP 306 GLN 307 0.0000

GLN 307 ASN 308 0.0001

ASN 308 SER 309 0.0563

SER 309 ASN 310 0.0002

ASN 310 LEU 311 -0.0002

LEU 311 LEU 312 0.0005

LEU 312 ILE 313 -0.0325

ILE 313 GLU 314 -0.0002

GLU 314 TYR 315 -0.0004

TYR 315 PHE 316 -0.0001

PHE 316 ARG 317 0.0419

ARG 317 ASN 318 0.0000

ASN 318 GLU 319 -0.0002

GLU 319 PHE 320 0.0001

PHE 320 GLY 321 0.1188

GLY 321 GLU 322 0.0003

GLU 322 LEU 323 -0.0000

LEU 323 GLU 324 -0.0000

GLU 324 SER 325 0.0305

SER 325 ASN 326 -0.0003

ASN 326 LYS 327 0.0001

LYS 327 SER 328 0.0001

SER 328 GLU 329 0.0032

GLU 329 MET 330 -0.0001

MET 330 ILE 331 0.0001

ILE 331 TRP 332 -0.0002

TRP 332 ASN 333 -0.2356

ASN 333 PHE 334 0.0004

PHE 334 HIS 335 0.0000

HIS 335 CYS 336 0.0002

CYS 336 TRP 337 -0.0643

TRP 337 VAL 338 -0.0002

VAL 338 GLU 339 0.0002

GLU 339 SER 340 0.0001

SER 340 TRP 341 0.0133

TRP 341 MET 342 -0.0002

MET 342 THR 343 0.0001

THR 343 ARG 344 0.0002

ARG 344 PRO 345 -0.0248

PRO 345 ASP 346 0.0002

ASP 346 LEU 347 -0.0002

LEU 347 GLN 348 -0.0003

GLN 348 PRO 349 -0.0017

PRO 349 GLY 350 0.0001

GLY 350 TYR 351 -0.0001

TYR 351 GLU 352 0.0002

GLU 352 GLY 353 -0.0164

GLY 353 TRP 354 -0.0004

TRP 354 GLN 355 0.0001

GLN 355 ALA 356 -0.0002

ALA 356 ILE 357 0.0828

ILE 357 ASP 358 0.0002

ASP 358 PRO 359 0.0003

PRO 359 THR 360 0.0003

THR 360 PRO 361 0.0051

PRO 361 GLN 362 0.0001

GLN 362 GLU 363 -0.0001

GLU 363 LYS 364 0.0003

LYS 364 SER 365 0.0275

SER 365 GLU 366 -0.0001

GLU 366 GLY 367 0.0004

GLY 367 THR 368 -0.0005

THR 368 TYR 369 -0.0240

TYR 369 CYS 370 0.0001

CYS 370 CYS 371 -0.0003

CYS 371 GLY 372 -0.0003

GLY 372 PRO 373 0.0616

PRO 373 VAL 374 0.0001

VAL 374 SER 375 -0.0001

SER 375 VAL 376 0.0002

VAL 376 ARG 377 0.0499

ARG 377 ALA 378 -0.0000

ALA 378 ILE 379 -0.0000

ILE 379 LYS 380 -0.0001

LYS 380 GLU 381 -0.0690

GLU 381 GLY 382 -0.0003

GLY 382 ASP 383 0.0001

ASP 383 LEU 384 -0.0001

LEU 384 SER 385 -0.0222

SER 385 THR 386 -0.0005

THR 386 LYS 387 0.0001

LYS 387 TYR 388 0.0000

TYR 388 ASP 389 -0.0445

ASP 389 ALA 390 0.0000

ALA 390 PRO 391 0.0002

PRO 391 PHE 392 0.0000

PHE 392 VAL 393 -0.0007

VAL 393 PHE 394 -0.0002

PHE 394 ALA 395 0.0001

ALA 395 GLU 396 -0.0002

GLU 396 VAL 397 -0.0280

VAL 397 ASN 398 0.0002

ASN 398 ALA 399 -0.0000

ALA 399 ASP 400 -0.0004

ASP 400 VAL 401 -0.2076

VAL 401 VAL 402 0.0001

VAL 402 ASP 403 -0.0001

ASP 403 TRP 404 0.0001

TRP 404 ILE 405 -0.0457

ILE 405 ARG 406 0.0000

ARG 406 GLN 407 0.0000

GLN 407 GLU 408 0.0002

GLU 408 ASP 409 -0.0454

ASP 409 GLY 410 0.0002

GLY 410 SER 411 0.0001

SER 411 VAL 412 -0.0001

VAL 412 LEU 413 -0.0330

LEU 413 LYS 414 -0.0003

LYS 414 SER 415 0.0005

SER 415 ILE 416 -0.0001

ILE 416 ASN 417 -0.0195

ASN 417 ARG 418 0.0000

ARG 418 SER 419 0.0006

SER 419 LEU 420 -0.0000

LEU 420 VAL 421 -0.2734

VAL 421 VAL 422 0.0001

VAL 422 GLY 423 0.0000

GLY 423 GLN 424 0.0001

GLN 424 LYS 425 -0.3407

LYS 425 ILE 426 -0.0001

ILE 426 SER 427 0.0002

SER 427 THR 428 -0.0002

THR 428 LYS 429 -0.1073

LYS 429 SER 430 0.0004

SER 430 VAL 431 -0.0003

VAL 431 GLY 432 0.0001

GLY 432 ARG 433 0.0007

ARG 433 ASP 434 -0.0000

ASP 434 ASP 435 -0.0003

ASP 435 ARG 436 0.0001

ARG 436 GLU 437 -0.0195

GLU 437 ASP 438 -0.0002

ASP 438 ILE 439 -0.0002

ILE 439 THR 440 -0.0001

THR 440 HIS 441 -0.0147

HIS 441 THR 442 0.0002

THR 442 TYR 443 -0.0001

TYR 443 LYS 444 0.0001

LYS 444 TYR 445 0.0022

TYR 445 PRO 446 0.0004

PRO 446 GLU 447 -0.0001

GLU 447 GLY 448 -0.0001

GLY 448 SER 449 -0.1049

SER 449 PRO 450 0.0002

PRO 450 GLU 451 0.0003

GLU 451 GLU 452 0.0004

GLU 452 ARG 453 -0.0771

ARG 453 GLU 454 -0.0004

GLU 454 VAL 455 -0.0002

VAL 455 PHE 456 0.0003

PHE 456 THR 457 -0.0736

THR 457 LYS 458 -0.0002

LYS 458 ALA 459 0.0002

ALA 459 ASN 460 0.0000

ASN 460 HIS 461 0.0319

HIS 461 LEU 462 0.0001

LEU 462 ASN 463 0.0002

ASN 463 LYS 464 0.0002

LYS 464 LEU 465 0.1060

LEU 465 ALA 466 0.0001

ALA 466 GLU 467 0.0000

GLU 467 LYS 468 0.0001

LYS 468 GLU 469 0.0724

GLU 469 GLU 470 -0.0001

GLU 470 THR 471 0.0001

THR 471 GLY 472 -0.0001

GLY 472 VAL 473 0.0468

VAL 473 ALA 474 -0.0001

ALA 474 MET 475 0.0006

MET 475 ARG 476 -0.0003

ARG 476 ILE 477 -0.0388

ILE 477 ARG 478 0.0002

ARG 478 VAL 479 -0.0001

VAL 479 GLY 480 0.0002

GLY 480 ASP 481 -0.1923

ASP 481 SER 482 -0.0002

SER 482 MET 483 0.0001

MET 483 SER 484 0.0000

SER 484 MET 485 -0.0813

MET 485 GLY 486 0.0001

GLY 486 ASN 487 -0.0002

ASN 487 ASP 488 0.0003

ASP 488 PHE 489 -0.0204

PHE 489 ASP 490 0.0000

ASP 490 VAL 491 -0.0003

VAL 491 PHE 492 0.0003

PHE 492 ALA 493 -0.1029

ALA 493 HIS 494 -0.0005

HIS 494 ILE 495 0.0002

ILE 495 GLY 496 -0.0001

GLY 496 ASN 497 -0.1373

ASN 497 ASP 498 0.0002

ASP 498 THR 499 -0.0001

THR 499 SER 500 0.0002

SER 500 GLU 501 0.0885

GLU 501 THR 502 0.0001

THR 502 ARG 503 -0.0001

ARG 503 GLU 504 0.0003

GLU 504 CYS 505 0.1141

CYS 505 ARG 506 0.0002

ARG 506 LEU 507 -0.0001

LEU 507 LEU 508 0.0000

LEU 508 LEU 509 -0.0718

LEU 509 CYS 510 -0.0000

CYS 510 ALA 511 0.0003

ALA 511 ARG 512 -0.0004

ARG 512 THR 513 -0.0507

THR 513 VAL 514 -0.0003

VAL 514 SER 515 -0.0000

SER 515 TYR 516 -0.0002

TYR 516 ASN 517 -0.0285

ASN 517 GLY 518 0.0001

GLY 518 VAL 519 -0.0004

VAL 519 LEU 520 0.0002

LEU 520 GLY 521 0.0355

GLY 521 PRO 522 0.0002

PRO 522 GLU 523 -0.0001

GLU 523 CYS 524 -0.0003

CYS 524 GLY 525 -0.0904

GLY 525 THR 526 -0.0003

THR 526 GLU 527 -0.0002

GLU 527 ASP 528 0.0002

ASP 528 ILE 529 -0.0562

ILE 529 ASN 530 -0.0003

ASN 530 LEU 531 -0.0000

LEU 531 THR 532 0.0002

THR 532 LEU 533 0.1299

LEU 533 ASP 534 -0.0002

ASP 534 PRO 535 -0.0001

PRO 535 TYR 536 -0.0001

TYR 536 SER 537 -0.1584

SER 537 GLU 538 -0.0001

GLU 538 ASN 539 0.0001

ASN 539 SER 540 0.0002

SER 540 ILE 541 -0.0225

ILE 541 PRO 542 -0.0002

PRO 542 LEU 543 0.0002

LEU 543 ARG 544 0.0003

ARG 544 ILE 545 -0.0180

ILE 545 LEU 546 -0.0004

LEU 546 TYR 547 0.0001

TYR 547 GLU 548 -0.0003

GLU 548 LYS 549 0.0993

LYS 549 TYR 550 -0.0004

TYR 550 SER 551 -0.0001

SER 551 GLY 552 -0.0001

GLY 552 CYS 553 0.0007

CYS 553 LEU 554 0.0001

LEU 554 THR 555 0.0000

THR 555 GLU 556 0.0002

GLU 556 SER 557 -0.1020

SER 557 ASN 558 -0.0002

ASN 558 LEU 559 -0.0000

LEU 559 ILE 560 0.0002

ILE 560 LYS 561 0.0329

LYS 561 VAL 562 0.0005

VAL 562 ARG 563 0.0000

ARG 563 GLY 564 0.0002

GLY 564 LEU 565 -0.1024

LEU 565 LEU 566 0.0001

LEU 566 ILE 567 0.0002

ILE 567 GLU 568 -0.0002

GLU 568 PRO 569 -0.0792

PRO 569 ALA 570 -0.0000

ALA 570 ALA 571 0.0000

ALA 571 ASN 572 0.0001

ASN 572 SER 573 -0.0754

SER 573 TYR 574 -0.0001

TYR 574 LEU 575 0.0003

LEU 575 LEU 576 -0.0000

LEU 576 ALA 577 -0.1124

ALA 577 GLU 578 -0.0006

GLU 578 ARG 579 0.0000

ARG 579 ASP 580 0.0001

ASP 580 LEU 581 0.0963

LEU 581 TYR 582 -0.0002

TYR 582 LEU 583 0.0000

LEU 583 GLU 584 0.0001

GLU 584 ASN 585 0.1869

ASN 585 PRO 586 -0.0003

PRO 586 GLU 587 0.0000

GLU 587 ILE 588 0.0000

ILE 588 LYS 589 0.0163

LYS 589 ILE 590 0.0003

ILE 590 ARG 591 -0.0000

ARG 591 VAL 592 0.0000

VAL 592 LEU 593 -0.0580

LEU 593 GLY 594 0.0003

GLY 594 GLU 595 -0.0002

GLU 595 PRO 596 0.0001

PRO 596 LYS 597 0.0105

LYS 597 GLN 598 0.0004

GLN 598 ASN 599 0.0001

ASN 599 ARG 600 -0.0001

ARG 600 LYS 601 0.1614

LYS 601 LEU 602 0.0004

LEU 602 VAL 603 -0.0000

VAL 603 ALA 604 -0.0002

ALA 604 GLU 605 0.1130

GLU 605 VAL 606 -0.0002

VAL 606 SER 607 -0.0003

SER 607 LEU 608 0.0002

LEU 608 LYS 609 0.0861

LYS 609 ASN 610 0.0001

ASN 610 PRO 611 0.0001

PRO 611 LEU 612 -0.0003

LEU 612 SER 613 -0.0420

SER 613 ASP 614 0.0001

ASP 614 PRO 615 -0.0002

PRO 615 LEU 616 -0.0000

LEU 616 TYR 617 0.0737

TYR 617 ASP 618 -0.0002

ASP 618 CYS 619 -0.0003

CYS 619 ILE 620 0.0000

ILE 620 PHE 621 0.0343

PHE 621 THR 622 0.0001

THR 622 VAL 623 0.0000

VAL 623 GLU 624 0.0003

GLU 624 GLY 625 -0.0212

GLY 625 ALA 626 -0.0002

ALA 626 GLY 627 0.0000

GLY 627 LEU 628 0.0003

LEU 628 THR 629 0.0381

THR 629 LYS 630 0.0001

LYS 630 GLU 631 -0.0001

GLU 631 GLN 632 -0.0001

GLN 632 LYS 633 -0.0786

LYS 633 SER 634 0.0001

SER 634 VAL 635 0.0001

VAL 635 GLU 636 -0.0000

GLU 636 VAL 637 0.0445

VAL 637 SER 638 -0.0000

SER 638 ASP 639 0.0004

ASP 639 PRO 640 -0.0001

PRO 640 VAL 641 0.0139

VAL 641 PRO 642 -0.0002

PRO 642 ALA 643 -0.0002

ALA 643 GLY 644 -0.0001

GLY 644 ASP 645 0.0345

ASP 645 LEU 646 0.0003

LEU 646 VAL 647 -0.0001

VAL 647 LYS 648 -0.0001

LYS 648 ALA 649 0.1201

ALA 649 ARG 650 0.0001

ARG 650 VAL 651 0.0001

VAL 651 ASP 652 0.0000

ASP 652 LEU 653 0.0602

LEU 653 PHE 654 -0.0001

PHE 654 PRO 655 -0.0002

PRO 655 THR 656 0.0001

THR 656 ASP 657 0.0296

ASP 657 ILE 658 0.0002

ILE 658 GLY 659 -0.0005

GLY 659 LEU 660 0.0001

LEU 660 HIS 661 -0.0145

HIS 661 LYS 662 -0.0001

LYS 662 LEU 663 0.0000

LEU 663 VAL 664 0.0001

VAL 664 VAL 665 -0.0375

VAL 665 ASN 666 -0.0002

ASN 666 PHE 667 0.0000

PHE 667 GLN 668 0.0004

GLN 668 CYS 669 0.0302

CYS 669 ASP 670 -0.0000

ASP 670 LYS 671 0.0002

LYS 671 LEU 672 0.0000

LEU 672 LYS 673 0.0014

LYS 673 SER 674 0.0000

SER 674 VAL 675 0.0001

VAL 675 LYS 676 -0.0004

LYS 676 GLY 677 -0.1493

GLY 677 TYR 678 0.0000

TYR 678 ARG 679 0.0003

ARG 679 ASN 680 -0.0002

ASN 680 VAL 681 -0.1822

VAL 681 ILE 682 -0.0002

ILE 682 ILE 683 0.0001

ILE 683 GLY 684 0.0001

GLY 684 PRO 685 -0.1376

PRO 685 ALA 686 -0.0002

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.

*** ***

CA strain for 2407140045133527185

--- normal mode 28 ---

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

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