data_27882 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, 15N chemical shift assignments for the ShkA kinase Rec2 domain from Caulobacter crescentus ; _BMRB_accession_number 27882 _BMRB_flat_file_name bmr27882.str _Entry_type original _Submission_date 2019-04-23 _Accession_date 2019-04-23 _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 Boehm Raphael . . 2 Hiller Sebastian . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 99 "13C chemical shifts" 183 "15N chemical shifts" 99 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-12-12 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 27768 'Different Receiver domain (Rec1) of the same ShkA kinase protein of Caulobacter crescentus' stop_ _Original_release_date 2019-04-23 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Hybrid Histidine kinase activation by cyclic-di-GMP induced domain liberation ; _Citation_status 'in preparation' _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Boehm Raphael . . 2 Hiller Sebastian . . 3 Dubey Badri N. . 4 Agustoni Elia . . 5 Mangia Francesca . . 6 Mazur Adam . . 7 Kaczmarczyk Andreas . . 8 Jenal Urs . . 9 Plaza-Menacho Ivan . . 10 Schirmer Tilman . . stop_ _Journal_abbreviation 'Not known' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . loop_ _Keyword Cyclic-di-GMP ShkA auto-inhibition 'cell cycle' 'histidine kinase' phosphorelay phosphorylation 'second messenger' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name ShkA-Rec2 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Rec2 $ShkA-Rec2 stop_ _System_molecular_weight 17700 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_ShkA-Rec2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common ShkA-Rec2 _Molecular_mass 17700 _Mol_thiol_state 'not present' loop_ _Biological_function 'Phosphotransfer domain' stop_ _Details ; The actual protein starts from amino acid Proline 21. Residues 1 to 20 are from the HisTag plus a linker. Residue Proline 21 refers to residue Pro366 of the full-length protein. ; ############################## # Polymer residue sequence # ############################## _Residue_count 169 _Mol_residue_sequence ; MGSSHHHHHHSSGLVPRGSH PAHDDRIAGAVASGARVLLA EDNPINALLARTLLEREGCI VDRVADGEQAIAAASAGVYD LILMDLRMPGLTGIEAARAL RAKGVATPIAALTADAFDED RRTCLAAGMDDFLVKPLTQE ALRDALKRWTTGGVSGGWTK PATRAKVAG ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 MET 2 2 GLY 3 3 SER 4 4 SER 5 5 HIS 6 6 HIS 7 7 HIS 8 8 HIS 9 9 HIS 10 10 HIS 11 11 SER 12 12 SER 13 13 GLY 14 14 LEU 15 15 VAL 16 16 PRO 17 17 ARG 18 18 GLY 19 19 SER 20 20 HIS 21 366 PRO 22 367 ALA 23 368 HIS 24 369 ASP 25 370 ASP 26 371 ARG 27 372 ILE 28 373 ALA 29 374 GLY 30 375 ALA 31 376 VAL 32 377 ALA 33 378 SER 34 379 GLY 35 380 ALA 36 381 ARG 37 382 VAL 38 383 LEU 39 384 LEU 40 385 ALA 41 386 GLU 42 387 ASP 43 388 ASN 44 389 PRO 45 390 ILE 46 391 ASN 47 392 ALA 48 393 LEU 49 394 LEU 50 395 ALA 51 396 ARG 52 397 THR 53 398 LEU 54 399 LEU 55 400 GLU 56 401 ARG 57 402 GLU 58 403 GLY 59 404 CYS 60 405 ILE 61 406 VAL 62 407 ASP 63 408 ARG 64 409 VAL 65 410 ALA 66 411 ASP 67 412 GLY 68 413 GLU 69 414 GLN 70 415 ALA 71 416 ILE 72 417 ALA 73 418 ALA 74 419 ALA 75 420 SER 76 421 ALA 77 422 GLY 78 423 VAL 79 424 TYR 80 425 ASP 81 426 LEU 82 427 ILE 83 428 LEU 84 429 MET 85 430 ASP 86 431 LEU 87 432 ARG 88 433 MET 89 434 PRO 90 435 GLY 91 436 LEU 92 437 THR 93 438 GLY 94 439 ILE 95 440 GLU 96 441 ALA 97 442 ALA 98 443 ARG 99 444 ALA 100 445 LEU 101 446 ARG 102 447 ALA 103 448 LYS 104 449 GLY 105 450 VAL 106 451 ALA 107 452 THR 108 453 PRO 109 454 ILE 110 455 ALA 111 456 ALA 112 457 LEU 113 458 THR 114 459 ALA 115 460 ASP 116 461 ALA 117 462 PHE 118 463 ASP 119 464 GLU 120 465 ASP 121 466 ARG 122 467 ARG 123 468 THR 124 469 CYS 125 470 LEU 126 471 ALA 127 472 ALA 128 473 GLY 129 474 MET 130 475 ASP 131 476 ASP 132 477 PHE 133 478 LEU 134 479 VAL 135 480 LYS 136 481 PRO 137 482 LEU 138 483 THR 139 484 GLN 140 485 GLU 141 486 ALA 142 487 LEU 143 488 ARG 144 489 ASP 145 490 ALA 146 491 LEU 147 492 LYS 148 493 ARG 149 494 TRP 150 495 THR 151 496 THR 152 497 GLY 153 498 GLY 154 499 VAL 155 500 SER 156 501 GLY 157 502 GLY 158 503 TRP 159 504 THR 160 505 LYS 161 506 PRO 162 507 ALA 163 508 THR 164 509 ARG 165 510 ALA 166 511 LYS 167 512 VAL 168 513 ALA 169 514 GLY 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 $ShkA-Rec2 'Caulobacter crescentus' 155892 Bacteria . Caulobacter crescentus 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 $ShkA-Rec2 'recombinant technology' . Escherichia coli . pET 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $ShkA-Rec2 375 uM 250 500 '[U-99% 13C; U-99% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 3.0 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ save_CARA _Saveframe_category software _Name CARA _Version . loop_ _Vendor _Address _Electronic_address 'Keller and Wuthrich' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_NMRPipe _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_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . 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_ save_3D_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _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_CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _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' 0.195 . M pH 7.2 . pH pressure 1 . atm temperature 298.15 . 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 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 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_ _Software_label $CARA stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCA' '3D HNCACB' '3D CBCA(CO)NH' 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 Rec2 _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 13 13 GLY H H 8.30 0.02 . 2 13 13 GLY CA C 45.1 0.3 . 3 13 13 GLY N N 110.4 0.3 . 4 14 14 LEU H H 7.96 0.02 . 5 14 14 LEU CA C 54.9 0.3 . 6 14 14 LEU CB C 42.1 0.3 . 7 14 14 LEU N N 121.4 0.3 . 8 15 15 VAL H H 8.01 0.02 . 9 15 15 VAL CA C 59.5 0.3 . 10 15 15 VAL CB C 32.3 0.3 . 11 15 15 VAL N N 122.4 0.3 . 12 17 17 ARG H H 8.40 0.02 . 13 17 17 ARG CA C 56.2 0.3 . 14 17 17 ARG CB C 30.5 0.3 . 15 17 17 ARG N N 121.9 0.3 . 16 18 18 GLY H H 8.40 0.02 . 17 18 18 GLY CA C 45.0 0.3 . 18 18 18 GLY N N 110.3 0.3 . 19 19 19 SER H H 8.10 0.02 . 20 19 19 SER CA C 58.1 0.3 . 21 19 19 SER CB C 63.8 0.3 . 22 19 19 SER N N 115.3 0.3 . 23 367 22 ALA H H 8.57 0.02 . 24 367 22 ALA CA C 52.1 0.3 . 25 367 22 ALA CB C 18.9 0.3 . 26 367 22 ALA N N 124.2 0.3 . 27 368 23 HIS H H 8.14 0.02 . 28 368 23 HIS CA C 56.0 0.3 . 29 368 23 HIS CB C 30.4 0.3 . 30 368 23 HIS N N 118.2 0.3 . 31 369 24 ASP H H 8.11 0.02 . 32 369 24 ASP CA C 53.8 0.3 . 33 369 24 ASP CB C 40.9 0.3 . 34 369 24 ASP N N 121.7 0.3 . 35 370 25 ASP H H 8.29 0.02 . 36 370 25 ASP CA C 54.3 0.3 . 37 370 25 ASP CB C 40.7 0.3 . 38 370 25 ASP N N 121.7 0.3 . 39 371 26 ARG H H 8.14 0.02 . 40 371 26 ARG CA C 56.4 0.3 . 41 371 26 ARG CB C 30.2 0.3 . 42 371 26 ARG N N 120.3 0.3 . 43 372 27 ILE H H 7.95 0.02 . 44 372 27 ILE CA C 61.0 0.3 . 45 372 27 ILE CB C 38.2 0.3 . 46 372 27 ILE N N 120.7 0.3 . 47 373 28 ALA H H 8.24 0.02 . 48 373 28 ALA CA C 52.5 0.3 . 49 373 28 ALA CB C 18.7 0.3 . 50 373 28 ALA N N 127.6 0.3 . 51 374 29 GLY H H 8.21 0.02 . 52 374 29 GLY CA C 44.9 0.3 . 53 374 29 GLY N N 108.3 0.3 . 54 375 30 ALA H H 7.95 0.02 . 55 375 30 ALA CA C 52.0 0.3 . 56 375 30 ALA CB C 19.0 0.3 . 57 375 30 ALA N N 123.7 0.3 . 58 376 31 VAL H H 8.24 0.02 . 59 376 31 VAL CA C 61.9 0.3 . 60 376 31 VAL CB C 32.7 0.3 . 61 376 31 VAL N N 118.4 0.3 . 62 377 32 ALA H H 8.33 0.02 . 63 377 32 ALA CA C 51.6 0.3 . 64 377 32 ALA CB C 19.6 0.3 . 65 377 32 ALA N N 127.1 0.3 . 66 378 33 SER H H 8.09 0.02 . 67 378 33 SER CA C 58.6 0.3 . 68 378 33 SER CB C 63.5 0.3 . 69 378 33 SER N N 114.5 0.3 . 70 379 34 GLY H H 8.15 0.02 . 71 379 34 GLY CA C 44.8 0.3 . 72 379 34 GLY N N 111.5 0.3 . 73 380 35 ALA H H 7.99 0.02 . 74 380 35 ALA CA C 52.1 0.3 . 75 380 35 ALA CB C 18.8 0.3 . 76 380 35 ALA N N 123.1 0.3 . 77 381 36 ARG H H 9.91 0.02 . 78 381 36 ARG CA C 55.0 0.3 . 79 381 36 ARG CB C 30.7 0.3 . 80 381 36 ARG N N 124.0 0.3 . 81 382 37 VAL H H 9.24 0.02 . 82 382 37 VAL CA C 60.0 0.3 . 83 382 37 VAL CB C 35.6 0.3 . 84 382 37 VAL N N 127.4 0.3 . 85 383 38 LEU H H 7.79 0.02 . 86 383 38 LEU CA C 52.1 0.3 . 87 383 38 LEU CB C 41.3 0.3 . 88 383 38 LEU N N 128.3 0.3 . 89 384 39 LEU H H 9.17 0.02 . 90 384 39 LEU CA C 52.3 0.3 . 91 384 39 LEU CB C 45.0 0.3 . 92 384 39 LEU N N 129.6 0.3 . 93 385 40 ALA H H 9.00 0.02 . 94 385 40 ALA CA C 49.8 0.3 . 95 385 40 ALA CB C 19.5 0.3 . 96 385 40 ALA N N 132.3 0.3 . 97 392 47 ALA H H 8.66 0.02 . 98 392 47 ALA CA C 55.1 0.3 . 99 392 47 ALA CB C 17.4 0.3 . 100 392 47 ALA N N 122.8 0.3 . 101 393 48 LEU H H 7.57 0.02 . 102 393 48 LEU CA C 57.9 0.3 . 103 393 48 LEU CB C 41.3 0.3 . 104 393 48 LEU N N 120.1 0.3 . 105 394 49 LEU H H 7.74 0.02 . 106 394 49 LEU CA C 58.2 0.3 . 107 394 49 LEU CB C 41.5 0.3 . 108 394 49 LEU N N 121.6 0.3 . 109 395 50 ALA H H 7.93 0.02 . 110 395 50 ALA CA C 55.1 0.3 . 111 395 50 ALA CB C 18.3 0.3 . 112 395 50 ALA N N 118.6 0.3 . 113 396 51 ARG H H 8.43 0.02 . 114 396 51 ARG CA C 60.4 0.3 . 115 396 51 ARG CB C 29.9 0.3 . 116 396 51 ARG N N 116.7 0.3 . 117 397 52 THR H H 8.17 0.02 . 118 397 52 THR CA C 66.6 0.3 . 119 397 52 THR CB C 68.8 0.3 . 120 397 52 THR N N 114.9 0.3 . 121 398 53 LEU H H 7.68 0.02 . 122 398 53 LEU CA C 58.1 0.3 . 123 398 53 LEU CB C 42.5 0.3 . 124 398 53 LEU N N 120.2 0.3 . 125 399 54 LEU H H 8.27 0.02 . 126 399 54 LEU CA C 57.8 0.3 . 127 399 54 LEU CB C 42.9 0.3 . 128 399 54 LEU N N 118.1 0.3 . 129 400 55 GLU H H 8.97 0.02 . 130 400 55 GLU CA C 59.5 0.3 . 131 400 55 GLU CB C 28.3 0.3 . 132 400 55 GLU N N 120.5 0.3 . 133 401 56 ARG H H 7.85 0.02 . 134 401 56 ARG CA C 58.9 0.3 . 135 401 56 ARG CB C 29.7 0.3 . 136 401 56 ARG N N 121.5 0.3 . 137 402 57 GLU H H 7.09 0.02 . 138 402 57 GLU CA C 54.9 0.3 . 139 402 57 GLU CB C 29.4 0.3 . 140 402 57 GLU N N 115.5 0.3 . 141 403 58 GLY H H 7.79 0.02 . 142 403 58 GLY CA C 45.1 0.3 . 143 403 58 GLY N N 106.0 0.3 . 144 404 59 CYS H H 7.57 0.02 . 145 404 59 CYS CA C 58.8 0.3 . 146 404 59 CYS CB C 28.6 0.3 . 147 404 59 CYS N N 117.0 0.3 . 148 405 60 ILE H H 8.84 0.02 . 149 405 60 ILE CA C 60.8 0.3 . 150 405 60 ILE CB C 38.7 0.3 . 151 405 60 ILE N N 124.0 0.3 . 152 406 61 VAL H H 9.12 0.02 . 153 406 61 VAL CA C 61.1 0.3 . 154 406 61 VAL CB C 34.3 0.3 . 155 406 61 VAL N N 128.6 0.3 . 156 407 62 ASP H H 8.67 0.02 . 157 407 62 ASP CA C 52.1 0.3 . 158 407 62 ASP CB C 42.0 0.3 . 159 407 62 ASP N N 127.9 0.3 . 160 408 63 ARG H H 8.77 0.02 . 161 408 63 ARG CA C 53.6 0.3 . 162 408 63 ARG CB C 32.1 0.3 . 163 408 63 ARG N N 123.8 0.3 . 164 416 71 ILE H H 7.95 0.02 . 165 416 71 ILE CA C 65.0 0.3 . 166 416 71 ILE CB C 37.9 0.3 . 167 416 71 ILE N N 117.0 0.3 . 168 417 72 ALA H H 7.65 0.02 . 169 417 72 ALA CA C 54.9 0.3 . 170 417 72 ALA CB C 17.7 0.3 . 171 417 72 ALA N N 122.6 0.3 . 172 418 73 ALA H H 8.31 0.02 . 173 418 73 ALA CA C 54.9 0.3 . 174 418 73 ALA CB C 18.2 0.3 . 175 418 73 ALA N N 119.9 0.3 . 176 419 74 ALA H H 8.30 0.02 . 177 419 74 ALA CA C 53.3 0.3 . 178 419 74 ALA CB C 19.1 0.3 . 179 419 74 ALA N N 117.7 0.3 . 180 420 75 SER H H 7.64 0.02 . 181 420 75 SER CA C 60.8 0.3 . 182 420 75 SER CB C 63.2 0.3 . 183 420 75 SER N N 111.8 0.3 . 184 421 76 ALA H H 7.45 0.02 . 185 421 76 ALA CA C 52.5 0.3 . 186 421 76 ALA CB C 19.8 0.3 . 187 421 76 ALA N N 122.3 0.3 . 188 422 77 GLY H H 7.75 0.02 . 189 422 77 GLY CA C 44.8 0.3 . 190 422 77 GLY N N 105.5 0.3 . 191 438 93 GLY H H 8.47 0.02 . 192 438 93 GLY N N 110.6 0.3 . 193 441 96 ALA H H 8.79 0.02 . 194 441 96 ALA CA C 54.9 0.3 . 195 441 96 ALA CB C 17.6 0.3 . 196 441 96 ALA N N 123.0 0.3 . 197 442 97 ALA H H 8.22 0.02 . 198 442 97 ALA CA C 55.3 0.3 . 199 442 97 ALA CB C 18.3 0.3 . 200 442 97 ALA N N 120.0 0.3 . 201 444 99 ALA H H 7.91 0.02 . 202 444 99 ALA CA C 54.8 0.3 . 203 444 99 ALA CB C 17.9 0.3 . 204 444 99 ALA N N 121.7 0.3 . 205 445 100 LEU H H 8.16 0.02 . 206 445 100 LEU CA C 57.8 0.3 . 207 445 100 LEU CB C 41.1 0.3 . 208 445 100 LEU N N 118.6 0.3 . 209 446 101 ARG H H 8.46 0.02 . 210 446 101 ARG CA C 57.4 0.3 . 211 446 101 ARG CB C 28.1 0.3 . 212 446 101 ARG N N 117.7 0.3 . 213 447 102 ALA H H 8.10 0.02 . 214 447 102 ALA CA C 54.5 0.3 . 215 447 102 ALA CB C 17.4 0.3 . 216 447 102 ALA N N 122.7 0.3 . 217 448 103 LYS H H 7.32 0.02 . 218 448 103 LYS CA C 55.8 0.3 . 219 448 103 LYS CB C 32.5 0.3 . 220 448 103 LYS N N 115.9 0.3 . 221 449 104 GLY H H 7.79 0.02 . 222 449 104 GLY CA C 45.2 0.3 . 223 449 104 GLY N N 107.2 0.3 . 224 450 105 VAL H H 7.73 0.02 . 225 450 105 VAL CA C 63.3 0.3 . 226 450 105 VAL CB C 30.8 0.3 . 227 450 105 VAL N N 121.4 0.3 . 228 451 106 ALA H H 9.07 0.02 . 229 451 106 ALA CA C 51.8 0.3 . 230 451 106 ALA CB C 19.6 0.3 . 231 451 106 ALA N N 132.6 0.3 . 232 452 107 THR H H 7.20 0.02 . 233 452 107 THR CA C 61.3 0.3 . 234 452 107 THR CB C 72.1 0.3 . 235 452 107 THR N N 116.6 0.3 . 236 454 109 ILE H H 9.16 0.02 . 237 454 109 ILE CA C 59.1 0.3 . 238 454 109 ILE CB C 42.2 0.3 . 239 454 109 ILE N N 122.0 0.3 . 240 455 110 ALA H H 9.17 0.02 . 241 455 110 ALA CA C 48.4 0.3 . 242 455 110 ALA CB C 19.8 0.3 . 243 455 110 ALA N N 129.2 0.3 . 244 471 126 ALA H H 7.93 0.02 . 245 471 126 ALA CA C 54.0 0.3 . 246 471 126 ALA CB C 17.6 0.3 . 247 471 126 ALA N N 122.3 0.3 . 248 472 127 ALA H H 7.39 0.02 . 249 472 127 ALA CA C 52.1 0.3 . 250 472 127 ALA CB C 19.6 0.3 . 251 472 127 ALA N N 118.9 0.3 . 252 473 128 GLY H H 7.53 0.02 . 253 473 128 GLY CA C 44.5 0.3 . 254 473 128 GLY N N 101.8 0.3 . 255 474 129 MET H H 7.66 0.02 . 256 474 129 MET CA C 56.5 0.3 . 257 474 129 MET CB C 32.5 0.3 . 258 474 129 MET N N 116.8 0.3 . 259 475 130 ASP H H 8.61 0.02 . 260 475 130 ASP CA C 55.7 0.3 . 261 475 130 ASP CB C 43.4 0.3 . 262 475 130 ASP N N 118.2 0.3 . 263 483 138 THR H H 7.00 0.02 . 264 483 138 THR CA C 58.3 0.3 . 265 483 138 THR CB C 72.2 0.3 . 266 483 138 THR N N 108.1 0.3 . 267 484 139 GLN H H 9.19 0.02 . 268 484 139 GLN CA C 59.6 0.3 . 269 484 139 GLN CB C 28.3 0.3 . 270 484 139 GLN N N 122.0 0.3 . 271 485 140 GLU H H 9.01 0.02 . 272 485 140 GLU CA C 60.1 0.3 . 273 485 140 GLU CB C 28.5 0.3 . 274 485 140 GLU N N 118.0 0.3 . 275 486 141 ALA H H 7.64 0.02 . 276 486 141 ALA CA C 54.5 0.3 . 277 486 141 ALA CB C 18.6 0.3 . 278 486 141 ALA N N 121.1 0.3 . 279 487 142 LEU H H 8.02 0.02 . 280 487 142 LEU CA C 57.2 0.3 . 281 487 142 LEU CB C 41.5 0.3 . 282 487 142 LEU N N 117.9 0.3 . 283 488 143 ARG H H 8.68 0.02 . 284 488 143 ARG CA C 60.3 0.3 . 285 488 143 ARG CB C 29.7 0.3 . 286 488 143 ARG N N 120.0 0.3 . 287 489 144 ASP H H 7.80 0.02 . 288 489 144 ASP CA C 57.2 0.3 . 289 489 144 ASP CB C 40.1 0.3 . 290 489 144 ASP N N 118.4 0.3 . 291 490 145 ALA H H 7.71 0.02 . 292 490 145 ALA CA C 55.0 0.3 . 293 490 145 ALA CB C 17.2 0.3 . 294 490 145 ALA N N 122.4 0.3 . 295 491 146 LEU H H 8.69 0.02 . 296 491 146 LEU CA C 57.8 0.3 . 297 491 146 LEU CB C 41.2 0.3 . 298 491 146 LEU N N 117.7 0.3 . 299 492 147 LYS H H 8.14 0.02 . 300 492 147 LYS CA C 58.7 0.3 . 301 492 147 LYS CB C 31.8 0.3 . 302 492 147 LYS N N 120.5 0.3 . 303 493 148 ARG H H 7.59 0.02 . 304 493 148 ARG CA C 58.5 0.3 . 305 493 148 ARG CB C 30.0 0.3 . 306 493 148 ARG N N 117.7 0.3 . 307 494 149 TRP H H 7.61 0.02 . 308 494 149 TRP CA C 56.9 0.3 . 309 494 149 TRP CB C 32.4 0.3 . 310 494 149 TRP N N 113.2 0.3 . 311 495 150 THR H H 7.81 0.02 . 312 495 150 THR CA C 61.2 0.3 . 313 495 150 THR CB C 70.3 0.3 . 314 495 150 THR N N 107.4 0.3 . 315 496 151 THR H H 7.99 0.02 . 316 496 151 THR CA C 61.8 0.3 . 317 496 151 THR CB C 69.8 0.3 . 318 496 151 THR N N 112.9 0.3 . 319 497 152 GLY H H 8.38 0.02 . 320 497 152 GLY CA C 45.3 0.3 . 321 497 152 GLY N N 110.7 0.3 . 322 498 153 GLY H H 8.18 0.02 . 323 498 153 GLY CA C 45.2 0.3 . 324 498 153 GLY N N 108.6 0.3 . 325 499 154 VAL H H 7.93 0.02 . 326 499 154 VAL CA C 62.2 0.3 . 327 499 154 VAL CB C 32.4 0.3 . 328 499 154 VAL N N 118.5 0.3 . 329 500 155 SER H H 8.38 0.02 . 330 500 155 SER CA C 58.3 0.3 . 331 500 155 SER CB C 63.5 0.3 . 332 500 155 SER N N 118.6 0.3 . 333 501 156 GLY H H 8.26 0.02 . 334 501 156 GLY CA C 45.2 0.3 . 335 501 156 GLY N N 110.7 0.3 . 336 502 157 GLY H H 8.16 0.02 . 337 502 157 GLY CA C 45.2 0.3 . 338 502 157 GLY N N 108.4 0.3 . 339 503 158 TRP H H 7.95 0.02 . 340 503 158 TRP CA C 57.2 0.3 . 341 503 158 TRP CB C 29.3 0.3 . 342 503 158 TRP N N 120.6 0.3 . 343 504 159 THR H H 7.80 0.02 . 344 504 159 THR CA C 61.4 0.3 . 345 504 159 THR CB C 69.9 0.3 . 346 504 159 THR N N 116.2 0.3 . 347 505 160 LYS H H 8.05 0.02 . 348 505 160 LYS CA C 54.0 0.3 . 349 505 160 LYS CB C 32.2 0.3 . 350 505 160 LYS N N 124.8 0.3 . 351 507 162 ALA H H 8.37 0.02 . 352 507 162 ALA CA C 52.2 0.3 . 353 507 162 ALA CB C 18.9 0.3 . 354 507 162 ALA N N 124.3 0.3 . 355 508 163 THR H H 8.04 0.02 . 356 508 163 THR CA C 61.7 0.3 . 357 508 163 THR CB C 69.7 0.3 . 358 508 163 THR N N 113.5 0.3 . 359 509 164 ARG H H 8.24 0.02 . 360 509 164 ARG CA C 55.6 0.3 . 361 509 164 ARG CB C 30.5 0.3 . 362 509 164 ARG N N 123.5 0.3 . 363 510 165 ALA H H 8.24 0.02 . 364 510 165 ALA CA C 52.1 0.3 . 365 510 165 ALA CB C 19.0 0.3 . 366 510 165 ALA N N 125.5 0.3 . 367 511 166 LYS H H 8.24 0.02 . 368 511 166 LYS CA C 56.1 0.3 . 369 511 166 LYS CB C 32.7 0.3 . 370 511 166 LYS N N 121.1 0.3 . 371 512 167 VAL H H 8.09 0.02 . 372 512 167 VAL CA C 61.9 0.3 . 373 512 167 VAL CB C 32.5 0.3 . 374 512 167 VAL N N 121.7 0.3 . 375 513 168 ALA H H 8.31 0.02 . 376 513 168 ALA CA C 52.0 0.3 . 377 513 168 ALA CB C 19.2 0.3 . 378 513 168 ALA N N 127.9 0.3 . 379 514 169 GLY H H 7.84 0.02 . 380 514 169 GLY CA C 45.8 0.3 . 381 514 169 GLY N N 114.7 0.3 . stop_ save_