data_27188 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; N, H, CA, CB chemical shifts of E.coli CheA ; _BMRB_accession_number 27188 _BMRB_flat_file_name bmr27188.str _Entry_type original _Submission_date 2017-07-21 _Accession_date 2017-07-21 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Minato Yuichi . . 2 Ueda Takumi . . 3 Machiyama Asako . . 4 Iwai Hideo . . 5 Shimada Ichio . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 187 "13C chemical shifts" 350 "15N chemical shifts" 187 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2017-12-14 original BMRB . stop_ _Original_release_date 2017-07-21 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Dynamic domain arrangement of CheA-CheY complex regulates bacterial thermotaxis, as revealed by NMR ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 29184123 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Minato Yuichi . . 2 Ueda Takumi . . 3 Machiyama Asako . . 4 Iwai Hideo . . 5 Shimada Ichio . . stop_ _Journal_abbreviation 'Sci. Rep.' _Journal_volume 7 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 16462 _Page_last 16462 _Year 2017 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name CheA _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label CheA $CheA stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_CheA _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common CheA _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 654 _Mol_residue_sequence ; MSMDISDFYQTFFDEADELL ADMEQHLLVLQPEAPDAEQL NAIFRAAHSIKGGAGTFGFS VLQETTHLMENLLDEARRGE MQLNTDIINLFLETKDIMQE QLDAYKQSQEPDAASFDYIC QALRQLALEAKGETPSAVTR LSVVAKSEPQDEQSRSQSPR RIILSRLKAGEVDLLEEELG HLTTLTDVVKGADSLSAILP GDIAEDDITAVLCFVIEADQ ITFETVEVSPKISTPPVLKL AAEQAPTGRVEREKTTRSNE STSIRVAVEKVDQLINLVGE LVITQSMLAQRSSELDPVNH GDLITSMGQLQRNARDLQES VMSIRMMPMEYVFSRYPRLV RDLAGKLGKQVELTLVGSST ELDKSLIERIIDPLTHLVRN SLDHGIELPEKRLAAGKNSV GNLILSAEHQGGNICIEVTD DGAGLNRERILAKAASQGLT VSENMSDDEVAMLIFAPGFS TAEQVTDVSGRGVGMDVVKR NIQEMGGHVEIQSKQGTGTT IRILLPLTLAILDGMSVRVA DEVFILPLNAVMESLQPREA DLHPLAGGERVLEVRGEYLP IVELWKVFNVAGAKTEATQG IVVILQSGGRRYALLVDQLI GQHQVVVKNLESNYRKVPGI SAATILGDGSVALIVDVSAL QAINREQRMANTAA ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 MET 2 2 SER 3 3 MET 4 4 ASP 5 5 ILE 6 6 SER 7 7 ASP 8 8 PHE 9 9 TYR 10 10 GLN 11 11 THR 12 12 PHE 13 13 PHE 14 14 ASP 15 15 GLU 16 16 ALA 17 17 ASP 18 18 GLU 19 19 LEU 20 20 LEU 21 21 ALA 22 22 ASP 23 23 MET 24 24 GLU 25 25 GLN 26 26 HIS 27 27 LEU 28 28 LEU 29 29 VAL 30 30 LEU 31 31 GLN 32 32 PRO 33 33 GLU 34 34 ALA 35 35 PRO 36 36 ASP 37 37 ALA 38 38 GLU 39 39 GLN 40 40 LEU 41 41 ASN 42 42 ALA 43 43 ILE 44 44 PHE 45 45 ARG 46 46 ALA 47 47 ALA 48 48 HIS 49 49 SER 50 50 ILE 51 51 LYS 52 52 GLY 53 53 GLY 54 54 ALA 55 55 GLY 56 56 THR 57 57 PHE 58 58 GLY 59 59 PHE 60 60 SER 61 61 VAL 62 62 LEU 63 63 GLN 64 64 GLU 65 65 THR 66 66 THR 67 67 HIS 68 68 LEU 69 69 MET 70 70 GLU 71 71 ASN 72 72 LEU 73 73 LEU 74 74 ASP 75 75 GLU 76 76 ALA 77 77 ARG 78 78 ARG 79 79 GLY 80 80 GLU 81 81 MET 82 82 GLN 83 83 LEU 84 84 ASN 85 85 THR 86 86 ASP 87 87 ILE 88 88 ILE 89 89 ASN 90 90 LEU 91 91 PHE 92 92 LEU 93 93 GLU 94 94 THR 95 95 LYS 96 96 ASP 97 97 ILE 98 98 MET 99 99 GLN 100 100 GLU 101 101 GLN 102 102 LEU 103 103 ASP 104 104 ALA 105 105 TYR 106 106 LYS 107 107 GLN 108 108 SER 109 109 GLN 110 110 GLU 111 111 PRO 112 112 ASP 113 113 ALA 114 114 ALA 115 115 SER 116 116 PHE 117 117 ASP 118 118 TYR 119 119 ILE 120 120 CYS 121 121 GLN 122 122 ALA 123 123 LEU 124 124 ARG 125 125 GLN 126 126 LEU 127 127 ALA 128 128 LEU 129 129 GLU 130 130 ALA 131 131 LYS 132 132 GLY 133 133 GLU 134 134 THR 135 135 PRO 136 136 SER 137 137 ALA 138 138 VAL 139 139 THR 140 140 ARG 141 141 LEU 142 142 SER 143 143 VAL 144 144 VAL 145 145 ALA 146 146 LYS 147 147 SER 148 148 GLU 149 149 PRO 150 150 GLN 151 151 ASP 152 152 GLU 153 153 GLN 154 154 SER 155 155 ARG 156 156 SER 157 157 GLN 158 158 SER 159 159 PRO 160 160 ARG 161 161 ARG 162 162 ILE 163 163 ILE 164 164 LEU 165 165 SER 166 166 ARG 167 167 LEU 168 168 LYS 169 169 ALA 170 170 GLY 171 171 GLU 172 172 VAL 173 173 ASP 174 174 LEU 175 175 LEU 176 176 GLU 177 177 GLU 178 178 GLU 179 179 LEU 180 180 GLY 181 181 HIS 182 182 LEU 183 183 THR 184 184 THR 185 185 LEU 186 186 THR 187 187 ASP 188 188 VAL 189 189 VAL 190 190 LYS 191 191 GLY 192 192 ALA 193 193 ASP 194 194 SER 195 195 LEU 196 196 SER 197 197 ALA 198 198 ILE 199 199 LEU 200 200 PRO 201 201 GLY 202 202 ASP 203 203 ILE 204 204 ALA 205 205 GLU 206 206 ASP 207 207 ASP 208 208 ILE 209 209 THR 210 210 ALA 211 211 VAL 212 212 LEU 213 213 CYS 214 214 PHE 215 215 VAL 216 216 ILE 217 217 GLU 218 218 ALA 219 219 ASP 220 220 GLN 221 221 ILE 222 222 THR 223 223 PHE 224 224 GLU 225 225 THR 226 226 VAL 227 227 GLU 228 228 VAL 229 229 SER 230 230 PRO 231 231 LYS 232 232 ILE 233 233 SER 234 234 THR 235 235 PRO 236 236 PRO 237 237 VAL 238 238 LEU 239 239 LYS 240 240 LEU 241 241 ALA 242 242 ALA 243 243 GLU 244 244 GLN 245 245 ALA 246 246 PRO 247 247 THR 248 248 GLY 249 249 ARG 250 250 VAL 251 251 GLU 252 252 ARG 253 253 GLU 254 254 LYS 255 255 THR 256 256 THR 257 257 ARG 258 258 SER 259 259 ASN 260 260 GLU 261 261 SER 262 262 THR 263 263 SER 264 264 ILE 265 265 ARG 266 266 VAL 267 267 ALA 268 268 VAL 269 269 GLU 270 270 LYS 271 271 VAL 272 272 ASP 273 273 GLN 274 274 LEU 275 275 ILE 276 276 ASN 277 277 LEU 278 278 VAL 279 279 GLY 280 280 GLU 281 281 LEU 282 282 VAL 283 283 ILE 284 284 THR 285 285 GLN 286 286 SER 287 287 MET 288 288 LEU 289 289 ALA 290 290 GLN 291 291 ARG 292 292 SER 293 293 SER 294 294 GLU 295 295 LEU 296 296 ASP 297 297 PRO 298 298 VAL 299 299 ASN 300 300 HIS 301 301 GLY 302 302 ASP 303 303 LEU 304 304 ILE 305 305 THR 306 306 SER 307 307 MET 308 308 GLY 309 309 GLN 310 310 LEU 311 311 GLN 312 312 ARG 313 313 ASN 314 314 ALA 315 315 ARG 316 316 ASP 317 317 LEU 318 318 GLN 319 319 GLU 320 320 SER 321 321 VAL 322 322 MET 323 323 SER 324 324 ILE 325 325 ARG 326 326 MET 327 327 MET 328 328 PRO 329 329 MET 330 330 GLU 331 331 TYR 332 332 VAL 333 333 PHE 334 334 SER 335 335 ARG 336 336 TYR 337 337 PRO 338 338 ARG 339 339 LEU 340 340 VAL 341 341 ARG 342 342 ASP 343 343 LEU 344 344 ALA 345 345 GLY 346 346 LYS 347 347 LEU 348 348 GLY 349 349 LYS 350 350 GLN 351 351 VAL 352 352 GLU 353 353 LEU 354 354 THR 355 355 LEU 356 356 VAL 357 357 GLY 358 358 SER 359 359 SER 360 360 THR 361 361 GLU 362 362 LEU 363 363 ASP 364 364 LYS 365 365 SER 366 366 LEU 367 367 ILE 368 368 GLU 369 369 ARG 370 370 ILE 371 371 ILE 372 372 ASP 373 373 PRO 374 374 LEU 375 375 THR 376 376 HIS 377 377 LEU 378 378 VAL 379 379 ARG 380 380 ASN 381 381 SER 382 382 LEU 383 383 ASP 384 384 HIS 385 385 GLY 386 386 ILE 387 387 GLU 388 388 LEU 389 389 PRO 390 390 GLU 391 391 LYS 392 392 ARG 393 393 LEU 394 394 ALA 395 395 ALA 396 396 GLY 397 397 LYS 398 398 ASN 399 399 SER 400 400 VAL 401 401 GLY 402 402 ASN 403 403 LEU 404 404 ILE 405 405 LEU 406 406 SER 407 407 ALA 408 408 GLU 409 409 HIS 410 410 GLN 411 411 GLY 412 412 GLY 413 413 ASN 414 414 ILE 415 415 CYS 416 416 ILE 417 417 GLU 418 418 VAL 419 419 THR 420 420 ASP 421 421 ASP 422 422 GLY 423 423 ALA 424 424 GLY 425 425 LEU 426 426 ASN 427 427 ARG 428 428 GLU 429 429 ARG 430 430 ILE 431 431 LEU 432 432 ALA 433 433 LYS 434 434 ALA 435 435 ALA 436 436 SER 437 437 GLN 438 438 GLY 439 439 LEU 440 440 THR 441 441 VAL 442 442 SER 443 443 GLU 444 444 ASN 445 445 MET 446 446 SER 447 447 ASP 448 448 ASP 449 449 GLU 450 450 VAL 451 451 ALA 452 452 MET 453 453 LEU 454 454 ILE 455 455 PHE 456 456 ALA 457 457 PRO 458 458 GLY 459 459 PHE 460 460 SER 461 461 THR 462 462 ALA 463 463 GLU 464 464 GLN 465 465 VAL 466 466 THR 467 467 ASP 468 468 VAL 469 469 SER 470 470 GLY 471 471 ARG 472 472 GLY 473 473 VAL 474 474 GLY 475 475 MET 476 476 ASP 477 477 VAL 478 478 VAL 479 479 LYS 480 480 ARG 481 481 ASN 482 482 ILE 483 483 GLN 484 484 GLU 485 485 MET 486 486 GLY 487 487 GLY 488 488 HIS 489 489 VAL 490 490 GLU 491 491 ILE 492 492 GLN 493 493 SER 494 494 LYS 495 495 GLN 496 496 GLY 497 497 THR 498 498 GLY 499 499 THR 500 500 THR 501 501 ILE 502 502 ARG 503 503 ILE 504 504 LEU 505 505 LEU 506 506 PRO 507 507 LEU 508 508 THR 509 509 LEU 510 510 ALA 511 511 ILE 512 512 LEU 513 513 ASP 514 514 GLY 515 515 MET 516 516 SER 517 517 VAL 518 518 ARG 519 519 VAL 520 520 ALA 521 521 ASP 522 522 GLU 523 523 VAL 524 524 PHE 525 525 ILE 526 526 LEU 527 527 PRO 528 528 LEU 529 529 ASN 530 530 ALA 531 531 VAL 532 532 MET 533 533 GLU 534 534 SER 535 535 LEU 536 536 GLN 537 537 PRO 538 538 ARG 539 539 GLU 540 540 ALA 541 541 ASP 542 542 LEU 543 543 HIS 544 544 PRO 545 545 LEU 546 546 ALA 547 547 GLY 548 548 GLY 549 549 GLU 550 550 ARG 551 551 VAL 552 552 LEU 553 553 GLU 554 554 VAL 555 555 ARG 556 556 GLY 557 557 GLU 558 558 TYR 559 559 LEU 560 560 PRO 561 561 ILE 562 562 VAL 563 563 GLU 564 564 LEU 565 565 TRP 566 566 LYS 567 567 VAL 568 568 PHE 569 569 ASN 570 570 VAL 571 571 ALA 572 572 GLY 573 573 ALA 574 574 LYS 575 575 THR 576 576 GLU 577 577 ALA 578 578 THR 579 579 GLN 580 580 GLY 581 581 ILE 582 582 VAL 583 583 VAL 584 584 ILE 585 585 LEU 586 586 GLN 587 587 SER 588 588 GLY 589 589 GLY 590 590 ARG 591 591 ARG 592 592 TYR 593 593 ALA 594 594 LEU 595 595 LEU 596 596 VAL 597 597 ASP 598 598 GLN 599 599 LEU 600 600 ILE 601 601 GLY 602 602 GLN 603 603 HIS 604 604 GLN 605 605 VAL 606 606 VAL 607 607 VAL 608 608 LYS 609 609 ASN 610 610 LEU 611 611 GLU 612 612 SER 613 613 ASN 614 614 TYR 615 615 ARG 616 616 LYS 617 617 VAL 618 618 PRO 619 619 GLY 620 620 ILE 621 621 SER 622 622 ALA 623 623 ALA 624 624 THR 625 625 ILE 626 626 LEU 627 627 GLY 628 628 ASP 629 629 GLY 630 630 SER 631 631 VAL 632 632 ALA 633 633 LEU 634 634 ILE 635 635 VAL 636 636 ASP 637 637 VAL 638 638 SER 639 639 ALA 640 640 LEU 641 641 GLN 642 642 ALA 643 643 ILE 644 644 ASN 645 645 ARG 646 646 GLU 647 647 GLN 648 648 ARG 649 649 MET 650 650 ALA 651 651 ASN 652 652 THR 653 653 ALA 654 654 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $CheA 'E. coli' 562 Bacteria . Escherichia coli stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $CheA 'recombinant technology' . Escherichia coli . pET43a stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $CheA 0.3 mM '[U-13C; U-15N; U-2H]' TRIS 50 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(COCA)CB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(COCA)CB' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0 . M pH 7.5 . pH pressure 1 . atm temperature 303 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0 external indirect . . . .25144953 DSS H 1 'methyl protons' ppm 0 external direct . . . 1 DSS N 15 'methyl protons' ppm 0 external indirect . . . .101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D HNCA' '3D HN(CO)CA' '3D HNCACB' '3D HN(COCA)CB' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name CheA _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 4 4 ASP H H 8.39 0.02 1 2 4 4 ASP CA C 53.8 0.2 1 3 4 4 ASP CB C 40.6 0.2 1 4 4 4 ASP N N 122.5 0.2 1 5 5 5 ILE H H 8.12 0.02 1 6 5 5 ILE CA C 61.1 0.2 1 7 5 5 ILE CB C 37.4 0.2 1 8 5 5 ILE N N 122.0 0.2 1 9 7 7 ASP H H 8.18 0.02 1 10 7 7 ASP CA C 55.2 0.2 1 11 7 7 ASP CB C 40.1 0.2 1 12 7 7 ASP N N 122.6 0.2 1 13 8 8 PHE H H 7.89 0.02 1 14 8 8 PHE CA C 58.6 0.2 1 15 8 8 PHE CB C 37.8 0.2 1 16 8 8 PHE N N 119.8 0.2 1 17 9 9 TYR H H 7.64 0.02 1 18 9 9 TYR CA C 58.5 0.2 1 19 9 9 TYR CB C 36.8 0.2 1 20 9 9 TYR N N 119.2 0.2 1 21 10 10 GLN H H 7.86 0.02 1 22 10 10 GLN CA C 58.4 0.2 1 23 10 10 GLN CB C 27.5 0.2 1 24 10 10 GLN N N 118.7 0.2 1 25 11 11 THR H H 7.83 0.02 1 26 11 11 THR CA C 65.0 0.2 1 27 11 11 THR CB C 68.2 0.2 1 28 11 11 THR N N 112.5 0.2 1 29 12 12 PHE H H 7.42 0.02 1 30 12 12 PHE CA C 60.3 0.2 1 31 12 12 PHE CB C 37.7 0.2 1 32 12 12 PHE N N 122.5 0.2 1 33 13 13 PHE H H 8.20 0.02 1 34 13 13 PHE CA C 59.2 0.2 1 35 13 13 PHE CB C 36.4 0.2 1 36 13 13 PHE N N 119.2 0.2 1 37 14 14 ASP H H 8.22 0.02 1 38 14 14 ASP CA C 57.1 0.2 1 39 14 14 ASP CB C 39.2 0.2 1 40 14 14 ASP N N 118.2 0.2 1 41 15 15 GLU H H 7.98 0.02 1 42 15 15 GLU CA C 58.8 0.2 1 43 15 15 GLU CB C 28.9 0.2 1 44 15 15 GLU N N 122.0 0.2 1 45 16 16 ALA H H 9.11 0.02 1 46 16 16 ALA CA C 54.8 0.2 1 47 16 16 ALA CB C 16.9 0.2 1 48 16 16 ALA N N 122.5 0.2 1 49 17 17 ASP H H 8.21 0.02 1 50 17 17 ASP CA C 57.2 0.2 1 51 17 17 ASP CB C 39.7 0.2 1 52 17 17 ASP N N 118.6 0.2 1 53 18 18 GLU H H 7.35 0.02 1 54 18 18 GLU CA C 58.9 0.2 1 55 18 18 GLU CB C 28.4 0.2 1 56 18 18 GLU N N 120.9 0.2 1 57 19 19 LEU H H 8.57 0.02 1 58 19 19 LEU CA C 57.4 0.2 1 59 19 19 LEU CB C 41.1 0.2 1 60 19 19 LEU N N 122.5 0.2 1 61 20 20 LEU H H 8.82 0.02 1 62 20 20 LEU CA C 57.7 0.2 1 63 20 20 LEU CB C 40.6 0.2 1 64 20 20 LEU N N 121.1 0.2 1 65 21 21 ALA H H 7.54 0.02 1 66 21 21 ALA CA C 54.6 0.2 1 67 21 21 ALA CB C 16.7 0.2 1 68 21 21 ALA N N 122.6 0.2 1 69 23 23 MET H H 8.77 0.02 1 70 23 23 MET CA C 59.7 0.2 1 71 23 23 MET CB C 33.1 0.2 1 72 23 23 MET N N 120.0 0.2 1 73 24 24 GLU H H 8.11 0.02 1 74 24 24 GLU CA C 59.7 0.2 1 75 24 24 GLU CB C 29.3 0.2 1 76 24 24 GLU N N 118.7 0.2 1 77 25 25 GLN H H 7.79 0.02 1 78 25 25 GLN CA C 58.5 0.2 1 79 25 25 GLN CB C 27.0 0.2 1 80 25 25 GLN N N 115.9 0.2 1 81 26 26 HIS H H 7.80 0.02 1 82 26 26 HIS CA C 59.2 0.2 1 83 26 26 HIS CB C 29.8 0.2 1 84 26 26 HIS N N 115.7 0.2 1 85 27 27 LEU H H 8.44 0.02 1 86 27 27 LEU CA C 57.8 0.2 1 87 27 27 LEU CB C 41.3 0.2 1 88 27 27 LEU N N 120.2 0.2 1 89 28 28 LEU H H 7.87 0.02 1 90 28 28 LEU CA C 56.6 0.2 1 91 28 28 LEU CB C 41.5 0.2 1 92 28 28 LEU N N 115.7 0.2 1 93 29 29 VAL H H 7.03 0.02 1 94 29 29 VAL CA C 60.3 0.2 1 95 29 29 VAL CB C 31.2 0.2 1 96 29 29 VAL N N 109.4 0.2 1 97 30 30 LEU H H 7.17 0.02 1 98 30 30 LEU CA C 55.1 0.2 1 99 30 30 LEU CB C 41.9 0.2 1 100 30 30 LEU N N 125.9 0.2 1 101 31 31 GLN H H 8.85 0.02 1 102 31 31 GLN CA C 51.7 0.2 1 103 31 31 GLN CB C 27.9 0.2 1 104 31 31 GLN N N 127.0 0.2 1 105 33 33 GLU H H 8.72 0.02 1 106 33 33 GLU CA C 57.1 0.2 1 107 33 33 GLU CB C 27.9 0.2 1 108 33 33 GLU N N 113.8 0.2 1 109 34 34 ALA H H 7.32 0.02 1 110 34 34 ALA CA C 50.1 0.2 1 111 34 34 ALA CB C 17.1 0.2 1 112 34 34 ALA N N 121.5 0.2 1 113 36 36 ASP H H 8.28 0.02 1 114 36 36 ASP CA C 53.8 0.2 1 115 36 36 ASP CB C 41.8 0.2 1 116 36 36 ASP N N 125.6 0.2 1 117 37 37 ALA H H 8.88 0.02 1 118 37 37 ALA CA C 55.2 0.2 1 119 37 37 ALA CB C 17.7 0.2 1 120 37 37 ALA N N 130.6 0.2 1 121 38 38 GLU H H 8.31 0.02 1 122 38 38 GLU CA C 58.4 0.2 1 123 38 38 GLU CB C 27.5 0.2 1 124 38 38 GLU N N 117.7 0.2 1 125 39 39 GLN H H 8.08 0.02 1 126 39 39 GLN CA C 58.5 0.2 1 127 39 39 GLN CB C 27.4 0.2 1 128 39 39 GLN N N 121.3 0.2 1 129 40 40 LEU H H 7.94 0.02 1 130 40 40 LEU CA C 57.7 0.2 1 131 40 40 LEU CB C 40.7 0.2 1 132 40 40 LEU N N 117.4 0.2 1 133 41 41 ASN H H 8.44 0.02 1 134 41 41 ASN CA C 55.9 0.2 1 135 41 41 ASN CB C 37.3 0.2 1 136 41 41 ASN N N 117.7 0.2 1 137 42 42 ALA H H 7.85 0.02 1 138 42 42 ALA CA C 54.9 0.2 1 139 42 42 ALA CB C 16.4 0.2 1 140 42 42 ALA N N 123.5 0.2 1 141 43 43 ILE H H 7.82 0.02 1 142 43 43 ILE CA C 65.0 0.2 1 143 43 43 ILE CB C 37.3 0.2 1 144 43 43 ILE N N 120.4 0.2 1 145 44 44 PHE H H 8.32 0.02 1 146 44 44 PHE CA C 62.1 0.2 1 147 44 44 PHE CB C 38.2 0.2 1 148 44 44 PHE N N 119.6 0.2 1 149 45 45 ARG H H 8.79 0.02 1 150 45 45 ARG CA C 59.2 0.2 1 151 45 45 ARG CB C 28.9 0.2 1 152 45 45 ARG N N 118.8 0.2 1 153 46 46 ALA H H 7.56 0.02 1 154 46 46 ALA CA C 54.7 0.2 1 155 46 46 ALA CB C 17.6 0.2 1 156 46 46 ALA N N 122.1 0.2 1 157 47 47 ALA H H 7.82 0.02 1 158 47 47 ALA CA C 54.9 0.2 1 159 47 47 ALA CB C 15.7 0.2 1 160 47 47 ALA N N 119.8 0.2 1 161 48 48 HIS H H 8.79 0.02 1 162 48 48 HIS CA C 58.9 0.2 1 163 48 48 HIS CB C 27.9 0.2 1 164 48 48 HIS N N 116.8 0.2 1 165 49 49 SER H H 8.31 0.02 1 166 49 49 SER CA C 61.7 0.2 1 167 49 49 SER CB C 62.6 0.2 1 168 49 49 SER N N 116.7 0.2 1 169 50 50 ILE H H 8.12 0.02 1 170 50 50 ILE CB C 36.3 0.2 1 171 50 50 ILE N N 124.4 0.2 1 172 51 51 LYS H H 8.48 0.02 1 173 51 51 LYS CB C 31.1 0.2 1 174 51 51 LYS N N 121.5 0.2 1 175 52 52 GLY H H 7.77 0.02 1 176 52 52 GLY CA C 46.4 0.2 1 177 52 52 GLY N N 105.1 0.2 1 178 53 53 GLY H H 7.86 0.02 1 179 53 53 GLY CA C 46.5 0.2 1 180 53 53 GLY N N 110.5 0.2 1 181 54 54 ALA H H 8.82 0.02 1 182 54 54 ALA CA C 54.6 0.2 1 183 54 54 ALA CB C 16.6 0.2 1 184 54 54 ALA N N 123.2 0.2 1 185 55 55 GLY H H 7.99 0.02 1 186 55 55 GLY CA C 45.9 0.2 1 187 55 55 GLY N N 103.1 0.2 1 188 56 56 THR H H 7.52 0.02 1 189 56 56 THR CA C 65.4 0.2 1 190 56 56 THR CB C 67.8 0.2 1 191 56 56 THR N N 120.3 0.2 1 192 57 57 PHE H H 6.83 0.02 1 193 57 57 PHE CA C 57.2 0.2 1 194 57 57 PHE CB C 37.3 0.2 1 195 57 57 PHE N N 116.1 0.2 1 196 58 58 GLY H H 7.13 0.02 1 197 58 58 GLY CA C 45.5 0.2 1 198 58 58 GLY N N 106.8 0.2 1 199 59 59 PHE H H 8.08 0.02 1 200 59 59 PHE CA C 51.7 0.2 1 201 59 59 PHE CB C 34.5 0.2 1 202 59 59 PHE N N 122.4 0.2 1 203 60 60 SER H H 7.96 0.02 1 204 60 60 SER CA C 62.2 0.2 1 205 60 60 SER N N 119.3 0.2 1 206 61 61 VAL H H 7.83 0.02 1 207 61 61 VAL CA C 65.4 0.2 1 208 61 61 VAL CB C 30.0 0.2 1 209 61 61 VAL N N 121.8 0.2 1 210 62 62 LEU H H 6.71 0.02 1 211 62 62 LEU CA C 56.4 0.2 1 212 62 62 LEU CB C 42.5 0.2 1 213 62 62 LEU N N 122.2 0.2 1 214 63 63 GLN H H 8.55 0.02 1 215 63 63 GLN CA C 59.9 0.2 1 216 63 63 GLN CB C 27.5 0.2 1 217 63 63 GLN N N 122.4 0.2 1 218 64 64 GLU H H 8.32 0.02 1 219 64 64 GLU CA C 59.1 0.2 1 220 64 64 GLU CB C 28.4 0.2 1 221 64 64 GLU N N 118.7 0.2 1 222 65 65 THR H H 8.06 0.02 1 223 65 65 THR CB C 68.2 0.2 1 224 65 65 THR N N 116.3 0.2 1 225 66 66 THR H H 8.14 0.02 1 226 66 66 THR CB C 67.8 0.2 1 227 66 66 THR N N 112.8 0.2 1 228 67 67 HIS H H 8.53 0.02 1 229 67 67 HIS CA C 59.1 0.2 1 230 67 67 HIS CB C 30.4 0.2 1 231 67 67 HIS N N 122.8 0.2 1 232 68 68 LEU H H 7.73 0.02 1 233 68 68 LEU CA C 57.2 0.2 1 234 68 68 LEU CB C 41.5 0.2 1 235 68 68 LEU N N 117.8 0.2 1 236 69 69 MET H H 7.68 0.02 1 237 69 69 MET CA C 59.3 0.2 1 238 69 69 MET N N 119.2 0.2 1 239 70 70 GLU H H 9.35 0.02 1 240 70 70 GLU CA C 59.7 0.2 1 241 70 70 GLU CB C 28.4 0.2 1 242 70 70 GLU N N 121.3 0.2 1 243 71 71 ASN H H 7.96 0.02 1 244 71 71 ASN CA C 55.9 0.2 1 245 71 71 ASN CB C 37.5 0.2 1 246 71 71 ASN N N 117.2 0.2 1 247 72 72 LEU H H 7.22 0.02 1 248 72 72 LEU CA C 57.2 0.2 1 249 72 72 LEU CB C 41.5 0.2 1 250 72 72 LEU N N 119.6 0.2 1 251 74 74 ASP H H 8.74 0.02 1 252 74 74 ASP CA C 56.7 0.2 1 253 74 74 ASP CB C 40.6 0.2 1 254 74 74 ASP N N 120.3 0.2 1 255 75 75 GLU H H 7.59 0.02 1 256 75 75 GLU CA C 59.2 0.2 1 257 75 75 GLU CB C 28.4 0.2 1 258 75 75 GLU N N 117.6 0.2 1 259 76 76 ALA H H 8.32 0.02 1 260 76 76 ALA CA C 54.4 0.2 1 261 76 76 ALA CB C 16.7 0.2 1 262 76 76 ALA N N 121.0 0.2 1 263 77 77 ARG H H 8.82 0.02 1 264 77 77 ARG CA C 58.5 0.2 1 265 77 77 ARG CB C 27.9 0.2 1 266 77 77 ARG N N 120.6 0.2 1 267 78 78 ARG H H 7.55 0.02 1 268 78 78 ARG CA C 56.3 0.2 1 269 78 78 ARG CB C 30.3 0.2 1 270 78 78 ARG N N 117.4 0.2 1 271 79 79 GLY H H 7.75 0.02 1 272 79 79 GLY CA C 45.1 0.2 1 273 79 79 GLY N N 107.3 0.2 1 274 80 80 GLU H H 7.93 0.02 1 275 80 80 GLU CA C 56.1 0.2 1 276 80 80 GLU CB C 29.3 0.2 1 277 80 80 GLU N N 118.1 0.2 1 278 81 81 MET H H 6.92 0.02 1 279 81 81 MET CA C 54.1 0.2 1 280 81 81 MET CB C 35.0 0.2 1 281 81 81 MET N N 117.2 0.2 1 282 82 82 GLN H H 8.61 0.02 1 283 82 82 GLN CA C 54.6 0.2 1 284 82 82 GLN CB C 28.4 0.2 1 285 82 82 GLN N N 126.3 0.2 1 286 83 83 LEU H H 8.84 0.02 1 287 83 83 LEU CA C 53.6 0.2 1 288 83 83 LEU CB C 42.0 0.2 1 289 83 83 LEU N N 122.1 0.2 1 290 84 84 ASN H H 6.60 0.02 1 291 84 84 ASN CA C 51.4 0.2 1 292 84 84 ASN CB C 39.2 0.2 1 293 84 84 ASN N N 111.6 0.2 1 294 85 85 THR H H 8.67 0.02 1 295 85 85 THR N N 113.9 0.2 1 296 86 86 ASP H H 7.89 0.02 1 297 86 86 ASP CA C 57.4 0.2 1 298 86 86 ASP CB C 39.1 0.2 1 299 86 86 ASP N N 122.2 0.2 1 300 87 87 ILE H H 8.28 0.02 1 301 87 87 ILE CA C 65.0 0.2 1 302 87 87 ILE CB C 37.5 0.2 1 303 87 87 ILE N N 122.5 0.2 1 304 88 88 ILE H H 7.69 0.02 1 305 88 88 ILE CA C 65.0 0.2 1 306 88 88 ILE CB C 35.2 0.2 1 307 88 88 ILE N N 119.8 0.2 1 308 89 89 ASN H H 8.36 0.02 1 309 89 89 ASN CA C 55.8 0.2 1 310 89 89 ASN CB C 36.4 0.2 1 311 89 89 ASN N N 118.3 0.2 1 312 90 90 LEU H H 7.88 0.02 1 313 90 90 LEU CA C 57.1 0.2 1 314 90 90 LEU CB C 39.8 0.2 1 315 90 90 LEU N N 124.7 0.2 1 316 91 91 PHE H H 8.79 0.02 1 317 91 91 PHE CA C 57.3 0.2 1 318 91 91 PHE CB C 36.4 0.2 1 319 91 91 PHE N N 123.6 0.2 1 320 92 92 LEU H H 8.67 0.02 1 321 92 92 LEU CA C 58.3 0.2 1 322 92 92 LEU CB C 40.1 0.2 1 323 92 92 LEU N N 123.0 0.2 1 324 93 93 GLU H H 8.34 0.02 1 325 93 93 GLU CA C 59.3 0.2 1 326 93 93 GLU CB C 28.9 0.2 1 327 93 93 GLU N N 121.3 0.2 1 328 94 94 THR H H 8.57 0.02 1 329 94 94 THR N N 117.6 0.2 1 330 95 95 LYS H H 8.28 0.02 1 331 95 95 LYS CA C 59.9 0.2 1 332 95 95 LYS CB C 28.4 0.2 1 333 95 95 LYS N N 124.1 0.2 1 334 97 97 ILE H H 8.30 0.02 1 335 97 97 ILE CB C 37.3 0.2 1 336 97 97 ILE N N 123.9 0.2 1 337 98 98 MET H H 9.14 0.02 1 338 98 98 MET CA C 58.9 0.2 1 339 98 98 MET CB C 33.6 0.2 1 340 98 98 MET N N 122.4 0.2 1 341 99 99 GLN H H 8.32 0.02 1 342 99 99 GLN CA C 59.1 0.2 1 343 99 99 GLN CB C 28.9 0.2 1 344 99 99 GLN N N 119.3 0.2 1 345 100 100 GLU H H 7.76 0.02 1 346 100 100 GLU CA C 59.1 0.2 1 347 100 100 GLU CB C 28.4 0.2 1 348 100 100 GLU N N 119.4 0.2 1 349 101 101 GLN H H 8.54 0.02 1 350 101 101 GLN CA C 58.6 0.2 1 351 101 101 GLN CB C 26.5 0.2 1 352 101 101 GLN N N 122.1 0.2 1 353 102 102 LEU H H 8.51 0.02 1 354 102 102 LEU CA C 57.5 0.2 1 355 102 102 LEU CB C 41.5 0.2 1 356 102 102 LEU N N 119.5 0.2 1 357 103 103 ASP H H 8.53 0.02 1 358 103 103 ASP CA C 56.6 0.2 1 359 103 103 ASP CB C 38.7 0.2 1 360 103 103 ASP N N 118.3 0.2 1 361 104 104 ALA H H 7.64 0.02 1 362 104 104 ALA CA C 54.7 0.2 1 363 104 104 ALA CB C 15.3 0.2 1 364 104 104 ALA N N 124.6 0.2 1 365 105 105 TYR H H 7.80 0.02 1 366 105 105 TYR CA C 60.8 0.2 1 367 105 105 TYR CB C 35.9 0.2 1 368 105 105 TYR N N 119.2 0.2 1 369 106 106 LYS H H 8.33 0.02 1 370 106 106 LYS CA C 59.1 0.2 1 371 106 106 LYS CB C 31.7 0.2 1 372 106 106 LYS N N 120.7 0.2 1 373 107 107 GLN H H 7.19 0.02 1 374 107 107 GLN CA C 54.1 0.2 1 375 107 107 GLN CB C 28.4 0.2 1 376 107 107 GLN N N 115.8 0.2 1 377 108 108 SER H H 8.09 0.02 1 378 108 108 SER CA C 58.8 0.2 1 379 108 108 SER CB C 60.7 0.2 1 380 108 108 SER N N 113.2 0.2 1 381 109 109 GLN H H 8.11 0.02 1 382 109 109 GLN CA C 52.5 0.2 1 383 109 109 GLN CB C 29.8 0.2 1 384 109 109 GLN N N 118.1 0.2 1 385 110 110 GLU H H 8.23 0.02 1 386 110 110 GLU CA C 53.0 0.2 1 387 110 110 GLU CB C 28.8 0.2 1 388 110 110 GLU N N 120.6 0.2 1 389 112 112 ASP H H 8.85 0.02 1 390 112 112 ASP CA C 54.7 0.2 1 391 112 112 ASP CB C 42.0 0.2 1 392 112 112 ASP N N 122.1 0.2 1 393 113 113 ALA H H 8.78 0.02 1 394 113 113 ALA CA C 54.7 0.2 1 395 113 113 ALA CB C 18.1 0.2 1 396 113 113 ALA N N 133.0 0.2 1 397 114 114 ALA H H 8.26 0.02 1 398 114 114 ALA CA C 54.9 0.2 1 399 114 114 ALA CB C 16.7 0.2 1 400 114 114 ALA N N 121.5 0.2 1 401 115 115 SER H H 8.35 0.02 1 402 115 115 SER CA C 61.3 0.2 1 403 115 115 SER CB C 62.1 0.2 1 404 115 115 SER N N 116.3 0.2 1 405 116 116 PHE H H 7.22 0.02 1 406 116 116 PHE CA C 58.6 0.2 1 407 116 116 PHE CB C 37.8 0.2 1 408 116 116 PHE N N 122.9 0.2 1 409 117 117 ASP H H 8.34 0.02 1 410 117 117 ASP CA C 57.1 0.2 1 411 117 117 ASP CB C 40.1 0.2 1 412 117 117 ASP N N 120.6 0.2 1 413 118 118 TYR H H 7.94 0.02 1 414 118 118 TYR CA C 59.9 0.2 1 415 118 118 TYR CB C 36.8 0.2 1 416 118 118 TYR N N 119.2 0.2 1 417 119 119 ILE H H 8.34 0.02 1 418 119 119 ILE CA C 59.3 0.2 1 419 119 119 ILE CB C 37.3 0.2 1 420 119 119 ILE N N 122.4 0.2 1 421 120 120 CYS H H 8.04 0.02 1 422 120 120 CYS CA C 63.5 0.2 1 423 120 120 CYS CB C 25.7 0.2 1 424 120 120 CYS N N 121.1 0.2 1 425 121 121 GLN H H 7.58 0.02 1 426 121 121 GLN CA C 58.5 0.2 1 427 121 121 GLN CB C 26.8 0.2 1 428 121 121 GLN N N 118.1 0.2 1 429 122 122 ALA H H 7.72 0.02 1 430 122 122 ALA CA C 54.5 0.2 1 431 122 122 ALA CB C 17.3 0.2 1 432 122 122 ALA N N 122.8 0.2 1 433 123 123 LEU H H 8.49 0.02 1 434 123 123 LEU CA C 57.4 0.2 1 435 123 123 LEU CB C 41.1 0.2 1 436 123 123 LEU N N 118.4 0.2 1 437 124 124 ARG H H 8.30 0.02 1 438 124 124 ARG CA C 59.6 0.2 1 439 124 124 ARG CB C 28.9 0.2 1 440 124 124 ARG N N 119.7 0.2 1 441 125 125 GLN H H 8.05 0.02 1 442 125 125 GLN CA C 58.0 0.2 1 443 125 125 GLN CB C 27.0 0.2 1 444 125 125 GLN N N 119.3 0.2 1 445 126 126 LEU H H 7.50 0.02 1 446 126 126 LEU CA C 56.7 0.2 1 447 126 126 LEU CB C 40.1 0.2 1 448 126 126 LEU N N 119.5 0.2 1 449 127 127 ALA H H 7.49 0.02 1 450 127 127 ALA CA C 53.9 0.2 1 451 127 127 ALA CB C 17.6 0.2 1 452 127 127 ALA N N 120.4 0.2 1 453 128 128 LEU H H 7.71 0.02 1 454 128 128 LEU CA C 56.7 0.2 1 455 128 128 LEU CB C 40.8 0.2 1 456 128 128 LEU N N 118.9 0.2 1 457 129 129 GLU H H 8.10 0.02 1 458 129 129 GLU CA C 57.7 0.2 1 459 129 129 GLU CB C 28.4 0.2 1 460 129 129 GLU N N 120.3 0.2 1 461 130 130 ALA H H 8.18 0.02 1 462 130 130 ALA CA C 53.3 0.2 1 463 130 130 ALA CB C 17.6 0.2 1 464 130 130 ALA N N 122.8 0.2 1 465 131 131 LYS H H 7.66 0.02 1 466 131 131 LYS CA C 55.7 0.2 1 467 131 131 LYS CB C 31.7 0.2 1 468 131 131 LYS N N 117.6 0.2 1 469 132 132 GLY H H 7.96 0.02 1 470 132 132 GLY CA C 44.8 0.2 1 471 132 132 GLY N N 108.4 0.2 1 472 160 160 ARG H H 8.26 0.02 1 473 160 160 ARG CA C 53.7 0.2 1 474 160 160 ARG CB C 32.6 0.2 1 475 160 160 ARG N N 118.8 0.2 1 476 161 161 ARG H H 9.17 0.02 1 477 161 161 ARG CA C 53.7 0.2 1 478 161 161 ARG CB C 32.1 0.2 1 479 161 161 ARG N N 123.7 0.2 1 480 162 162 ILE H H 9.19 0.02 1 481 162 162 ILE CA C 58.0 0.2 1 482 162 162 ILE CB C 39.8 0.2 1 483 162 162 ILE N N 126.3 0.2 1 484 163 163 ILE H H 8.63 0.02 1 485 163 163 ILE CA C 60.7 0.2 1 486 163 163 ILE N N 126.3 0.2 1 487 164 164 LEU H H 9.28 0.02 1 488 164 164 LEU CA C 52.0 0.2 1 489 164 164 LEU CB C 42.0 0.2 1 490 164 164 LEU N N 129.1 0.2 1 491 165 165 SER H H 8.52 0.02 1 492 165 165 SER CA C 56.7 0.2 1 493 165 165 SER CB C 65.7 0.2 1 494 165 165 SER N N 116.5 0.2 1 495 166 166 ARG H H 8.89 0.02 1 496 166 166 ARG CA C 56.1 0.2 1 497 166 166 ARG CB C 26.0 0.2 1 498 166 166 ARG N N 116.5 0.2 1 499 167 167 LEU H H 8.30 0.02 1 500 167 167 LEU CA C 53.8 0.2 1 501 167 167 LEU CB C 40.6 0.2 1 502 167 167 LEU N N 117.3 0.2 1 503 168 168 LYS H H 8.87 0.02 1 504 168 168 LYS CA C 54.6 0.2 1 505 168 168 LYS CB C 32.6 0.2 1 506 168 168 LYS N N 122.9 0.2 1 507 169 169 ALA H H 8.43 0.02 1 508 169 169 ALA CA C 54.3 0.2 1 509 169 169 ALA CB C 17.1 0.2 1 510 169 169 ALA N N 124.8 0.2 1 511 170 170 GLY H H 8.67 0.02 1 512 170 170 GLY N N 109.9 0.2 1 513 172 172 VAL H H 7.78 0.02 1 514 172 172 VAL CA C 66.8 0.2 1 515 172 172 VAL CB C 30.3 0.2 1 516 172 172 VAL N N 119.6 0.2 1 517 173 173 ASP H H 7.73 0.02 1 518 173 173 ASP CA C 56.6 0.2 1 519 173 173 ASP CB C 39.2 0.2 1 520 173 173 ASP N N 117.0 0.2 1 521 174 174 LEU H H 7.20 0.02 1 522 174 174 LEU CA C 57.6 0.2 1 523 174 174 LEU CB C 41.5 0.2 1 524 174 174 LEU N N 121.5 0.2 1 525 175 175 LEU H H 8.49 0.02 1 526 175 175 LEU CA C 56.7 0.2 1 527 175 175 LEU CB C 39.2 0.2 1 528 175 175 LEU N N 118.9 0.2 1 529 176 176 GLU H H 7.84 0.02 1 530 176 176 GLU CA C 59.9 0.2 1 531 176 176 GLU CB C 28.3 0.2 1 532 176 176 GLU N N 121.1 0.2 1 533 177 177 GLU H H 7.50 0.02 1 534 177 177 GLU CA C 58.6 0.2 1 535 177 177 GLU CB C 28.4 0.2 1 536 177 177 GLU N N 120.2 0.2 1 537 178 178 GLU H H 8.26 0.02 1 538 178 178 GLU CA C 58.5 0.2 1 539 178 178 GLU CB C 28.4 0.2 1 540 178 178 GLU N N 118.7 0.2 1 541 179 179 LEU H H 8.53 0.02 1 542 179 179 LEU CA C 57.5 0.2 1 543 179 179 LEU CB C 41.5 0.2 1 544 179 179 LEU N N 119.2 0.2 1 545 180 180 GLY H H 7.87 0.02 1 546 180 180 GLY CA C 45.3 0.2 1 547 180 180 GLY N N 105.0 0.2 1 548 181 181 HIS H H 7.34 0.02 1 549 181 181 HIS CA C 56.0 0.2 1 550 181 181 HIS CB C 28.4 0.2 1 551 181 181 HIS N N 116.1 0.2 1 552 182 182 LEU H H 7.71 0.02 1 553 182 182 LEU CA C 55.5 0.2 1 554 182 182 LEU CB C 42.5 0.2 1 555 182 182 LEU N N 118.9 0.2 1 556 183 183 THR H H 8.01 0.02 1 557 183 183 THR CA C 59.4 0.2 1 558 183 183 THR CB C 67.3 0.2 1 559 183 183 THR N N 113.9 0.2 1 560 184 184 THR H H 7.91 0.02 1 561 184 184 THR CA C 61.1 0.2 1 562 184 184 THR CB C 69.7 0.2 1 563 184 184 THR N N 116.5 0.2 1 564 185 185 LEU H H 8.50 0.02 1 565 185 185 LEU CA C 53.6 0.2 1 566 185 185 LEU CB C 42.5 0.2 1 567 185 185 LEU N N 125.0 0.2 1 568 186 186 THR H H 8.38 0.02 1 569 186 186 THR CA C 60.0 0.2 1 570 186 186 THR CB C 71.1 0.2 1 571 186 186 THR N N 114.3 0.2 1 572 187 187 ASP H H 8.74 0.02 1 573 187 187 ASP CA C 54.6 0.2 1 574 187 187 ASP CB C 38.8 0.2 1 575 187 187 ASP N N 122.0 0.2 1 576 188 188 VAL H H 7.98 0.02 1 577 188 188 VAL CA C 62.9 0.2 1 578 188 188 VAL CB C 30.7 0.2 1 579 188 188 VAL N N 118.0 0.2 1 580 189 189 VAL H H 9.20 0.02 1 581 189 189 VAL CA C 61.7 0.2 1 582 189 189 VAL CB C 32.6 0.2 1 583 189 189 VAL N N 131.7 0.2 1 584 190 190 LYS H H 8.83 0.02 1 585 190 190 LYS CA C 55.5 0.2 1 586 190 190 LYS CB C 32.6 0.2 1 587 190 190 LYS N N 129.5 0.2 1 588 191 191 GLY H H 8.37 0.02 1 589 191 191 GLY CA C 42.5 0.2 1 590 191 191 GLY N N 112.8 0.2 1 591 193 193 ASP H H 7.90 0.02 1 592 193 193 ASP CA C 51.6 0.2 1 593 193 193 ASP CB C 41.0 0.2 1 594 193 193 ASP N N 112.8 0.2 1 595 194 194 SER H H 6.92 0.02 1 596 194 194 SER CA C 56.4 0.2 1 597 194 194 SER CB C 65.9 0.2 1 598 194 194 SER N N 110.3 0.2 1 599 195 195 LEU H H 8.40 0.02 1 600 195 195 LEU CA C 53.8 0.2 1 601 195 195 LEU CB C 45.4 0.2 1 602 195 195 LEU N N 122.0 0.2 1 603 196 196 SER H H 8.74 0.02 1 604 196 196 SER CA C 55.3 0.2 1 605 196 196 SER CB C 65.5 0.2 1 606 196 196 SER N N 120.5 0.2 1 607 197 197 ALA H H 8.56 0.02 1 608 197 197 ALA CA C 51.2 0.2 1 609 197 197 ALA CB C 22.8 0.2 1 610 197 197 ALA N N 122.6 0.2 1 611 198 198 ILE H H 8.84 0.02 1 612 198 198 ILE CA C 60.3 0.2 1 613 198 198 ILE CB C 35.9 0.2 1 614 198 198 ILE N N 121.0 0.2 1 615 199 199 LEU H H 9.07 0.02 1 616 199 199 LEU CA C 51.3 0.2 1 617 199 199 LEU CB C 41.5 0.2 1 618 199 199 LEU N N 128.2 0.2 1 619 201 201 GLY H H 8.48 0.02 1 620 201 201 GLY CA C 45.6 0.2 1 621 201 201 GLY N N 105.7 0.2 1 622 202 202 ASP H H 8.03 0.02 1 623 202 202 ASP CA C 53.3 0.2 1 624 202 202 ASP CB C 39.2 0.2 1 625 202 202 ASP N N 116.6 0.2 1 626 203 203 ILE H H 7.04 0.02 1 627 203 203 ILE CA C 58.8 0.2 1 628 203 203 ILE CB C 37.8 0.2 1 629 203 203 ILE N N 118.3 0.2 1 630 204 204 ALA H H 8.71 0.02 1 631 204 204 ALA CA C 51.1 0.2 1 632 204 204 ALA CB C 17.7 0.2 1 633 204 204 ALA N N 130.6 0.2 1 634 205 205 GLU H H 8.77 0.02 1 635 205 205 GLU CA C 59.9 0.2 1 636 205 205 GLU CB C 27.9 0.2 1 637 205 205 GLU N N 124.3 0.2 1 638 206 206 ASP H H 8.68 0.02 1 639 206 206 ASP CA C 56.1 0.2 1 640 206 206 ASP CB C 39.2 0.2 1 641 206 206 ASP N N 116.3 0.2 1 642 207 207 ASP H H 7.13 0.02 1 643 207 207 ASP CA C 56.6 0.2 1 644 207 207 ASP N N 120.2 0.2 1 645 208 208 ILE H H 7.39 0.02 1 646 208 208 ILE CA C 63.6 0.2 1 647 208 208 ILE CB C 36.8 0.2 1 648 208 208 ILE N N 119.1 0.2 1 649 209 209 THR H H 8.65 0.02 1 650 209 209 THR CA C 66.6 0.2 1 651 209 209 THR CB C 67.8 0.2 1 652 209 209 THR N N 114.8 0.2 1 653 210 210 ALA H H 7.59 0.02 1 654 210 210 ALA CA C 54.7 0.2 1 655 210 210 ALA CB C 17.2 0.2 1 656 210 210 ALA N N 122.1 0.2 1 657 211 211 VAL H H 7.01 0.02 1 658 211 211 VAL CA C 64.4 0.2 1 659 211 211 VAL CB C 31.2 0.2 1 660 211 211 VAL N N 114.4 0.2 1 661 212 212 LEU H H 8.06 0.02 1 662 212 212 LEU CA C 56.8 0.2 1 663 212 212 LEU CB C 40.3 0.2 1 664 212 212 LEU N N 118.3 0.2 1 665 213 213 CYS H H 8.15 0.02 1 666 213 213 CYS CA C 61.1 0.2 1 667 213 213 CYS CB C 25.6 0.2 1 668 213 213 CYS N N 115.7 0.2 1 669 214 214 PHE H H 7.20 0.02 1 670 214 214 PHE CA C 59.5 0.2 1 671 214 214 PHE CB C 37.8 0.2 1 672 214 214 PHE N N 117.2 0.2 1 673 215 215 VAL H H 8.06 0.02 1 674 215 215 VAL CA C 63.3 0.2 1 675 215 215 VAL CB C 33.5 0.2 1 676 215 215 VAL N N 118.1 0.2 1 677 216 216 ILE H H 7.78 0.02 1 678 216 216 ILE CA C 59.1 0.2 1 679 216 216 ILE CB C 39.6 0.2 1 680 216 216 ILE N N 113.9 0.2 1 681 217 217 GLU H H 7.98 0.02 1 682 217 217 GLU CA C 54.7 0.2 1 683 217 217 GLU CB C 30.3 0.2 1 684 217 217 GLU N N 116.9 0.2 1 685 218 218 ALA H H 8.71 0.02 1 686 218 218 ALA CA C 54.9 0.2 1 687 218 218 ALA CB C 17.3 0.2 1 688 218 218 ALA N N 122.9 0.2 1 689 219 219 ASP H H 8.02 0.02 1 690 219 219 ASP CA C 54.4 0.2 1 691 219 219 ASP CB C 38.7 0.2 1 692 219 219 ASP N N 112.8 0.2 1 693 220 220 GLN H H 7.87 0.02 1 694 220 220 GLN CA C 56.4 0.2 1 695 220 220 GLN CB C 30.3 0.2 1 696 220 220 GLN N N 118.7 0.2 1 697 221 221 ILE H H 7.37 0.02 1 698 221 221 ILE CA C 60.5 0.2 1 699 221 221 ILE CB C 38.7 0.2 1 700 221 221 ILE N N 119.8 0.2 1 701 222 222 THR H H 8.48 0.02 1 702 222 222 THR CA C 60.6 0.2 1 703 222 222 THR CB C 71.3 0.2 1 704 222 222 THR N N 122.2 0.2 1 705 223 223 PHE H H 8.52 0.02 1 706 223 223 PHE CA C 56.0 0.2 1 707 223 223 PHE CB C 41.9 0.2 1 708 223 223 PHE N N 120.6 0.2 1 709 224 224 GLU H H 9.24 0.02 1 710 224 224 GLU CA C 53.9 0.2 1 711 224 224 GLU CB C 32.6 0.2 1 712 224 224 GLU N N 121.0 0.2 1 713 225 225 THR H H 8.68 0.02 1 714 225 225 THR CA C 62.7 0.2 1 715 225 225 THR CB C 68.7 0.2 1 716 225 225 THR N N 119.5 0.2 1 717 226 226 VAL H H 8.20 0.02 1 718 226 226 VAL CA C 61.7 0.2 1 719 226 226 VAL CB C 31.1 0.2 1 720 226 226 VAL N N 125.9 0.2 1 721 227 227 GLU H H 8.34 0.02 1 722 227 227 GLU CA C 55.5 0.2 1 723 227 227 GLU CB C 29.2 0.2 1 724 227 227 GLU N N 125.8 0.2 1 stop_ save_