data_50031 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; CDC25B-R482A ; _BMRB_accession_number 50031 _BMRB_flat_file_name bmr50031.str _Entry_type original _Submission_date 2019-10-04 _Accession_date 2019-10-04 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; CDC25B R482A mutant HSQC NMR assigned peaks. Spectrum was acquired in phosphate buffer (20mM NaH2PO4, 50mM NaCl, 5mM BMER, 2mM dithiotreitol, 5%D2O, pH = 6.7). ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Reis Andre . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 146 "15N chemical shifts" 146 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2020-03-12 update BMRB 'update entry citation' 2019-10-29 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 50030 'CDC25B; wild type' 50032 'CDC25B; R544A mutant' 50033 'CDC25B; W550A mutant' stop_ _Original_release_date 2019-10-04 save_ ############################# # Citation for this entry # ############################# save_citations_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Combining free energy simulations and NMR chemical-shift perturbation to identify transient cation-pi contacts in proteins ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 31738549 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Reis Andre . . 2 Sayegh Raphael . . 3 Marana Sandro R. . 4 Arantes Guilherme M. . stop_ _Journal_abbreviation 'J. Chem. Inf. Model.' _Journal_name_full 'Journal of chemical information and modeling' _Journal_volume 60 _Journal_issue 2 _Journal_ISSN 1549-960X _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 890 _Page_last 897 _Year 2020 _Details . save_ ################################## # Molecular system description # ################################## save_assembly_1 _Saveframe_category molecular_system _Mol_system_name CDC25B-R482A _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label CDC25B-R482A $entity_1 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_entity_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity_1 _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 200 _Mol_residue_sequence ; GSMEFQSDHRELIGDYSKAF LLQTVDGKHQDLKYISPETM VALLTGKFSNIVDKFVIVDC RYPYEYEGGHIKTAVNLPLE RDAESFLLKSPIAPCSLDKR VILIFHCEFSSERGPAMCRF IRERDRAVNDYPSLYYPEMY ILKGGYKEFFPQHPNFCEPQ DYRPMNHEAFKDELKTFRLK TRSWAGERSRRELCSRLQDQ ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 367 GLY 2 368 SER 3 369 MET 4 370 GLU 5 371 PHE 6 372 GLN 7 373 SER 8 374 ASP 9 375 HIS 10 376 ARG 11 377 GLU 12 378 LEU 13 379 ILE 14 380 GLY 15 381 ASP 16 382 TYR 17 383 SER 18 384 LYS 19 385 ALA 20 386 PHE 21 387 LEU 22 388 LEU 23 389 GLN 24 390 THR 25 391 VAL 26 392 ASP 27 393 GLY 28 394 LYS 29 395 HIS 30 396 GLN 31 397 ASP 32 398 LEU 33 399 LYS 34 400 TYR 35 401 ILE 36 402 SER 37 403 PRO 38 404 GLU 39 405 THR 40 406 MET 41 407 VAL 42 408 ALA 43 409 LEU 44 410 LEU 45 411 THR 46 412 GLY 47 413 LYS 48 414 PHE 49 415 SER 50 416 ASN 51 417 ILE 52 418 VAL 53 419 ASP 54 420 LYS 55 421 PHE 56 422 VAL 57 423 ILE 58 424 VAL 59 425 ASP 60 426 CYS 61 427 ARG 62 428 TYR 63 429 PRO 64 430 TYR 65 431 GLU 66 432 TYR 67 433 GLU 68 434 GLY 69 435 GLY 70 436 HIS 71 437 ILE 72 438 LYS 73 439 THR 74 440 ALA 75 441 VAL 76 442 ASN 77 443 LEU 78 444 PRO 79 445 LEU 80 446 GLU 81 447 ARG 82 448 ASP 83 449 ALA 84 450 GLU 85 451 SER 86 452 PHE 87 453 LEU 88 454 LEU 89 455 LYS 90 456 SER 91 457 PRO 92 458 ILE 93 459 ALA 94 460 PRO 95 461 CYS 96 462 SER 97 463 LEU 98 464 ASP 99 465 LYS 100 466 ARG 101 467 VAL 102 468 ILE 103 469 LEU 104 470 ILE 105 471 PHE 106 472 HIS 107 473 CYS 108 474 GLU 109 475 PHE 110 476 SER 111 477 SER 112 478 GLU 113 479 ARG 114 480 GLY 115 481 PRO 116 482 ALA 117 483 MET 118 484 CYS 119 485 ARG 120 486 PHE 121 487 ILE 122 488 ARG 123 489 GLU 124 490 ARG 125 491 ASP 126 492 ARG 127 493 ALA 128 494 VAL 129 495 ASN 130 496 ASP 131 497 TYR 132 498 PRO 133 499 SER 134 500 LEU 135 501 TYR 136 502 TYR 137 503 PRO 138 504 GLU 139 505 MET 140 506 TYR 141 507 ILE 142 508 LEU 143 509 LYS 144 510 GLY 145 511 GLY 146 512 TYR 147 513 LYS 148 514 GLU 149 515 PHE 150 516 PHE 151 517 PRO 152 518 GLN 153 519 HIS 154 520 PRO 155 521 ASN 156 522 PHE 157 523 CYS 158 524 GLU 159 525 PRO 160 526 GLN 161 527 ASP 162 528 TYR 163 529 ARG 164 530 PRO 165 531 MET 166 532 ASN 167 533 HIS 168 534 GLU 169 535 ALA 170 536 PHE 171 537 LYS 172 538 ASP 173 539 GLU 174 540 LEU 175 541 LYS 176 542 THR 177 543 PHE 178 544 ARG 179 545 LEU 180 546 LYS 181 547 THR 182 548 ARG 183 549 SER 184 550 TRP 185 551 ALA 186 552 GLY 187 553 GLU 188 554 ARG 189 555 SER 190 556 ARG 191 557 ARG 192 558 GLU 193 559 LEU 194 560 CYS 195 561 SER 196 562 ARG 197 563 LEU 198 564 GLN 199 565 ASP 200 566 GLN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source_1 _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $entity_1 Human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source_1 _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name _Details $entity_1 'recombinant technology' . Escherichia coli BL21-GOLD plasmid pET-28a 'Catalytic subunit R482A mutant.' 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 $entity_1 0.2 mM '[U-100% 15N]' NaH2PO4 20 mM 'natural abundance' NaCl 50 mM 'natural abundance' BMER 5 mM 'natural abundance' dithiotreitol 2 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AIII _Field_strength 800 _Details 'Avance III' save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _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' 0.075 . M pH 6.7 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_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 TMS H 1 'methyl protons' ppm 0 internal direct . . . 1 '[15N] ammonium chloride' N 15 nitrogen ppm 0 internal direct . . . 1 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_chemical_shifts_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chem_shift_reference_1 _Mol_system_component_name CDC25B-R482A _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 1 369 3 MET H H 8.170 . 1 2 369 3 MET N N 121.354 . 1 3 370 4 GLU H H 8.239 . 1 4 370 4 GLU N N 121.919 . 1 5 371 5 PHE H H 8.123 . 1 6 371 5 PHE N N 120.627 . 1 7 372 6 GLN H H 8.186 . 1 8 372 6 GLN N N 121.904 . 1 9 373 7 SER H H 8.237 . 1 10 373 7 SER N N 117.106 . 1 11 374 8 ASP H H 8.235 . 1 12 374 8 ASP N N 121.835 . 1 13 375 9 HIS H H 8.264 . 1 14 375 9 HIS N N 119.848 . 1 15 376 10 ARG H H 8.128 . 1 16 376 10 ARG N N 121.415 . 1 17 377 11 GLU H H 8.596 . 1 18 377 11 GLU N N 120.973 . 1 19 389 23 GLN H H 8.446 . 1 20 389 23 GLN N N 120.758 . 1 21 390 24 THR H H 8.006 . 1 22 390 24 THR N N 114.927 . 1 23 391 25 VAL H H 8.241 . 1 24 391 25 VAL N N 113.562 . 1 25 392 26 ASP H H 8.280 . 1 26 392 26 ASP N N 121.335 . 1 27 393 27 GLY H H 7.653 . 1 28 393 27 GLY N N 108.613 . 1 29 394 28 LYS H H 7.647 . 1 30 394 28 LYS N N 119.338 . 1 31 395 29 HIS H H 7.924 . 1 32 395 29 HIS N N 115.753 . 1 33 396 30 GLN H H 8.956 . 1 34 396 30 GLN N N 123.685 . 1 35 397 31 ASP H H 9.369 . 1 36 397 31 ASP N N 114.637 . 1 37 398 32 LEU H H 7.377 . 1 38 398 32 LEU N N 120.321 . 1 39 399 33 LYS H H 8.460 . 1 40 399 33 LYS N N 118.693 . 1 41 400 34 TYR H H 8.822 . 1 42 400 34 TYR N N 122.083 . 1 43 401 35 ILE H H 8.771 . 1 44 401 35 ILE N N 110.025 . 1 45 402 36 SER H H 8.717 . 1 46 402 36 SER N N 116.825 . 1 47 404 38 GLU H H 8.278 . 1 48 404 38 GLU N N 116.292 . 1 49 405 39 THR H H 7.794 . 1 50 405 39 THR N N 121.711 . 1 51 406 40 MET H H 7.669 . 1 52 406 40 MET N N 121.853 . 1 53 407 41 VAL H H 8.020 . 1 54 407 41 VAL N N 119.323 . 1 55 408 42 ALA H H 7.659 . 1 56 408 42 ALA N N 125.078 . 1 57 409 43 LEU H H 7.677 . 1 58 409 43 LEU N N 118.261 . 1 59 410 44 LEU H H 8.030 . 1 60 410 44 LEU N N 119.699 . 1 61 411 45 THR H H 7.904 . 1 62 411 45 THR N N 107.357 . 1 63 412 46 GLY H H 7.587 . 1 64 412 46 GLY N N 108.192 . 1 65 413 47 LYS H H 8.164 . 1 66 413 47 LYS N N 119.523 . 1 67 414 48 PHE H H 8.342 . 1 68 414 48 PHE N N 114.057 . 1 69 415 49 SER H H 7.590 . 1 70 415 49 SER N N 117.991 . 1 71 416 50 ASN H H 8.634 . 1 72 416 50 ASN N N 117.129 . 1 73 419 53 ASP H H 9.142 . 1 74 419 53 ASP N N 128.688 . 1 75 421 55 PHE H H 7.935 . 1 76 421 55 PHE N N 118.340 . 1 77 422 56 VAL H H 7.950 . 1 78 422 56 VAL N N 121.547 . 1 79 423 57 ILE H H 8.940 . 1 80 423 57 ILE N N 128.027 . 1 81 424 58 VAL H H 9.433 . 1 82 424 58 VAL N N 128.795 . 1 83 425 59 ASP H H 8.679 . 1 84 425 59 ASP N N 127.270 . 1 85 426 60 CYS H H 8.254 . 1 86 426 60 CYS N N 124.681 . 1 87 427 61 ARG H H 7.599 . 1 88 427 61 ARG N N 117.357 . 1 89 428 62 TYR H H 7.586 . 1 90 428 62 TYR N N 118.196 . 1 91 430 64 TYR H H 7.035 . 1 92 430 64 TYR N N 110.382 . 1 93 431 65 GLU H H 6.126 . 1 94 431 65 GLU N N 123.289 . 1 95 432 66 TYR H H 6.959 . 1 96 432 66 TYR N N 120.718 . 1 97 433 67 GLU H H 9.058 . 1 98 433 67 GLU N N 120.771 . 1 99 434 68 GLY H H 6.936 . 1 100 434 68 GLY N N 103.885 . 1 101 435 69 GLY H H 6.456 . 1 102 435 69 GLY N N 106.550 . 1 103 436 70 HIS H H 7.523 . 1 104 436 70 HIS N N 123.926 . 1 105 437 71 ILE H H 10.600 . 1 106 437 71 ILE N N 123.870 . 1 107 439 73 THR H H 8.761 . 1 108 439 73 THR N N 113.582 . 1 109 440 74 ALA H H 8.645 . 1 110 440 74 ALA N N 125.862 . 1 111 441 75 VAL H H 8.980 . 1 112 441 75 VAL N N 121.200 . 1 113 442 76 ASN H H 8.454 . 1 114 442 76 ASN N N 124.824 . 1 115 443 77 LEU H H 7.017 . 1 116 443 77 LEU N N 124.294 . 1 117 445 79 LEU H H 7.359 . 1 118 445 79 LEU N N 114.854 . 1 119 446 80 GLU H H 9.092 . 1 120 446 80 GLU N N 125.074 . 1 121 447 81 ARG H H 8.391 . 1 122 447 81 ARG N N 115.301 . 1 123 448 82 ASP H H 6.875 . 1 124 448 82 ASP N N 119.048 . 1 125 449 83 ALA H H 8.115 . 1 126 449 83 ALA N N 123.490 . 1 127 450 84 GLU H H 9.011 . 1 128 450 84 GLU N N 118.601 . 1 129 451 85 SER H H 7.860 . 1 130 451 85 SER N N 113.781 . 1 131 452 86 PHE H H 8.186 . 1 132 452 86 PHE N N 119.700 . 1 133 453 87 LEU H H 8.191 . 1 134 453 87 LEU N N 111.944 . 1 135 454 88 LEU H H 8.182 . 1 136 454 88 LEU N N 117.143 . 1 137 455 89 LYS H H 7.181 . 1 138 455 89 LYS N N 120.988 . 1 139 456 90 SER H H 7.778 . 1 140 456 90 SER N N 112.983 . 1 141 468 102 ILE H H 8.014 . 1 142 468 102 ILE N N 123.314 . 1 143 469 103 LEU H H 7.434 . 1 144 469 103 LEU N N 121.489 . 1 145 470 104 ILE H H 8.798 . 1 146 470 104 ILE N N 122.159 . 1 147 471 105 PHE H H 9.533 . 1 148 471 105 PHE N N 123.721 . 1 149 472 106 HIS H H 8.917 . 1 150 472 106 HIS N N 113.943 . 1 151 483 117 MET H H 7.993 . 1 152 483 117 MET N N 120.510 . 1 153 484 118 CYS H H 7.628 . 1 154 484 118 CYS N N 119.983 . 1 155 485 119 ARG H H 7.705 . 1 156 485 119 ARG N N 116.405 . 1 157 486 120 PHE H H 8.083 . 1 158 486 120 PHE N N 121.493 . 1 159 487 121 ILE H H 8.253 . 1 160 487 121 ILE N N 118.858 . 1 161 488 122 ARG H H 7.568 . 1 162 488 122 ARG N N 118.421 . 1 163 489 123 GLU H H 7.994 . 1 164 489 123 GLU N N 119.645 . 1 165 490 124 ARG H H 7.943 . 1 166 490 124 ARG N N 119.328 . 1 167 491 125 ASP H H 8.758 . 1 168 491 125 ASP N N 121.780 . 1 169 492 126 ARG H H 8.457 . 1 170 492 126 ARG N N 116.598 . 1 171 493 127 ALA H H 7.569 . 1 172 493 127 ALA N N 119.025 . 1 173 494 128 VAL H H 7.345 . 1 174 494 128 VAL N N 108.900 . 1 175 495 129 ASN H H 7.027 . 1 176 495 129 ASN N N 120.457 . 1 177 496 130 ASP H H 8.739 . 1 178 496 130 ASP N N 120.572 . 1 179 497 131 TYR H H 8.780 . 1 180 497 131 TYR N N 128.174 . 1 181 505 139 MET H H 9.852 . 1 182 505 139 MET N N 116.120 . 1 183 506 140 TYR H H 8.809 . 1 184 506 140 TYR N N 117.764 . 1 185 507 141 ILE H H 9.378 . 1 186 507 141 ILE N N 120.239 . 1 187 508 142 LEU H H 7.705 . 1 188 508 142 LEU N N 125.192 . 1 189 509 143 LYS H H 9.643 . 1 190 509 143 LYS N N 136.791 . 1 191 510 144 GLY H H 9.520 . 1 192 510 144 GLY N N 118.367 . 1 193 511 145 GLY H H 7.361 . 1 194 511 145 GLY N N 101.771 . 1 195 513 147 LYS H H 8.857 . 1 196 513 147 LYS N N 115.519 . 1 197 514 148 GLU H H 6.564 . 1 198 514 148 GLU N N 111.374 . 1 199 515 149 PHE H H 7.361 . 1 200 515 149 PHE N N 121.265 . 1 201 516 150 PHE H H 7.719 . 1 202 516 150 PHE N N 117.932 . 1 203 518 152 GLN H H 6.276 . 1 204 518 152 GLN N N 112.436 . 1 205 519 153 HIS H H 7.079 . 1 206 519 153 HIS N N 115.516 . 1 207 521 155 ASN H H 8.315 . 1 208 521 155 ASN N N 111.608 . 1 209 522 156 PHE H H 7.982 . 1 210 522 156 PHE N N 117.917 . 1 211 523 157 CYS H H 7.685 . 1 212 523 157 CYS N N 119.307 . 1 213 524 158 GLU H H 9.264 . 1 214 524 158 GLU N N 122.087 . 1 215 526 160 GLN H H 8.486 . 1 216 526 160 GLN N N 119.341 . 1 217 527 161 ASP H H 7.965 . 1 218 527 161 ASP N N 123.809 . 1 219 528 162 TYR H H 8.996 . 1 220 528 162 TYR N N 120.152 . 1 221 529 163 ARG H H 9.080 . 1 222 529 163 ARG N N 133.842 . 1 223 531 165 MET H H 8.322 . 1 224 531 165 MET N N 122.778 . 1 225 532 166 ASN H H 8.478 . 1 226 532 166 ASN N N 113.860 . 1 227 533 167 HIS H H 7.463 . 1 228 533 167 HIS N N 120.474 . 1 229 534 168 GLU H H 8.875 . 1 230 534 168 GLU N N 130.253 . 1 231 535 169 ALA H H 10.591 . 1 232 535 169 ALA N N 124.327 . 1 233 536 170 PHE H H 7.768 . 1 234 536 170 PHE N N 117.204 . 1 235 537 171 LYS H H 7.154 . 1 236 537 171 LYS N N 119.318 . 1 237 538 172 ASP H H 8.626 . 1 238 538 172 ASP N N 119.818 . 1 239 539 173 GLU H H 8.060 . 1 240 539 173 GLU N N 123.463 . 1 241 540 174 LEU H H 8.307 . 1 242 540 174 LEU N N 122.086 . 1 243 541 175 LYS H H 7.678 . 1 244 541 175 LYS N N 117.889 . 1 245 542 176 THR H H 7.920 . 1 246 542 176 THR N N 114.082 . 1 247 543 177 PHE H H 8.346 . 1 248 543 177 PHE N N 121.615 . 1 249 544 178 ARG H H 8.544 . 1 250 544 178 ARG N N 119.611 . 1 251 545 179 LEU H H 7.503 . 1 252 545 179 LEU N N 118.892 . 1 253 546 180 LYS H H 7.698 . 1 254 546 180 LYS N N 117.038 . 1 255 547 181 THR H H 7.581 . 1 256 547 181 THR N N 110.640 . 1 257 548 182 ARG H H 7.818 . 1 258 548 182 ARG N N 121.670 . 1 259 549 183 SER H H 8.198 . 1 260 549 183 SER N N 116.032 . 1 261 550 184 TRP H H 8.050 . 1 262 550 184 TRP HE1 H 10.188 . 1 263 550 184 TRP N N 123.090 . 1 264 550 184 TRP NE1 N 129.808 . 1 265 551 185 ALA H H 8.048 . 1 266 551 185 ALA N N 125.189 . 1 267 552 186 GLY H H 7.618 . 1 268 552 186 GLY N N 107.066 . 1 269 553 187 GLU H H 8.157 . 1 270 553 187 GLU N N 120.905 . 1 271 554 188 ARG H H 8.312 . 1 272 554 188 ARG N N 121.376 . 1 273 556 190 ARG H H 8.184 . 1 274 556 190 ARG N N 122.653 . 1 275 557 191 ARG H H 8.161 . 1 276 557 191 ARG N N 121.164 . 1 277 558 192 GLU H H 8.282 . 1 278 558 192 GLU N N 121.013 . 1 279 559 193 LEU H H 8.102 . 1 280 559 193 LEU N N 122.251 . 1 281 560 194 CYS H H 8.162 . 1 282 560 194 CYS N N 119.366 . 1 283 562 196 ARG H H 8.261 . 1 284 562 196 ARG N N 122.774 . 1 285 563 197 LEU H H 8.146 . 1 286 563 197 LEU N N 122.721 . 1 287 564 198 GLN H H 8.209 . 1 288 564 198 GLN N N 119.881 . 1 289 565 199 ASP H H 8.218 . 1 290 565 199 ASP N N 121.426 . 1 291 566 200 GLN H H 7.742 . 1 292 566 200 GLN N N 124.576 . 1 stop_ save_