data_18652 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone assignment of Bt-Lon alpha sub-domain from Brevibacillus thermoruber ; _BMRB_accession_number 18652 _BMRB_flat_file_name bmr18652.str _Entry_type original _Submission_date 2012-08-09 _Accession_date 2012-08-09 _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 Chen Yu-Da . . 2 Hsu Chun-Hua . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 205 "13C chemical shifts" 214 "15N chemical shifts" 101 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-04-22 original author . stop_ _Original_release_date 2014-04-22 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Structural basis for DNA-mediated allosteric regulation facilitated by the AAA+ module of Lon protease.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 24531457 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lee 'Alan Yueh-Luen' . . 2 Chen Yu-Da . . 3 Chang Yu-Yung . . 4 Lin Yu-Ching . . 5 Chang Chi-Fon . . 6 Huang Shing-Jong . . 7 Wu Shih-Hsiung . . 8 Hsu Chun-Hua . . stop_ _Journal_abbreviation 'Acta Crystallogr. D Biol. Crystallogr.' _Journal_name_full 'Acta crystallographica. Section D, Biological crystallography' _Journal_volume 70 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 218 _Page_last 230 _Year 2014 _Details . loop_ _Keyword 'AAA+ protease' 'allosteric regulation' DNA-binding 'electrostatic interaction' 'Lon protease' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'alpha sub-domain' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'alpha sub-domain' $alpha_sub-domain 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_alpha_sub-domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common alpha_sub-domain _Molecular_mass . _Mol_thiol_state 'all free' loop_ _Biological_function 'protease, ATPase, DNA binding protein' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 124 _Mol_residue_sequence ; MAGYTELEKLHIMRDYLLPK QMEEHGLGRDKLQMNEEAML KVIRQYTREAGVRNLNREAA NICRKAARLIVSGEKKRVVV TPKTVESLLGKPRYRYGLAE REDQVGAVTGLAWTQALEHH HHHH ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 490 MET 2 491 ALA 3 492 GLY 4 493 TYR 5 494 THR 6 495 GLU 7 496 LEU 8 497 GLU 9 498 LYS 10 499 LEU 11 500 HIS 12 501 ILE 13 502 MET 14 503 ARG 15 504 ASP 16 505 TYR 17 506 LEU 18 507 LEU 19 508 PRO 20 509 LYS 21 510 GLN 22 511 MET 23 512 GLU 24 513 GLU 25 514 HIS 26 515 GLY 27 516 LEU 28 517 GLY 29 518 ARG 30 519 ASP 31 520 LYS 32 521 LEU 33 522 GLN 34 523 MET 35 524 ASN 36 525 GLU 37 526 GLU 38 527 ALA 39 528 MET 40 529 LEU 41 530 LYS 42 531 VAL 43 532 ILE 44 533 ARG 45 534 GLN 46 535 TYR 47 536 THR 48 537 ARG 49 538 GLU 50 539 ALA 51 540 GLY 52 541 VAL 53 542 ARG 54 543 ASN 55 544 LEU 56 545 ASN 57 546 ARG 58 547 GLU 59 548 ALA 60 549 ALA 61 550 ASN 62 551 ILE 63 552 CYS 64 553 ARG 65 554 LYS 66 555 ALA 67 556 ALA 68 557 ARG 69 558 LEU 70 559 ILE 71 560 VAL 72 561 SER 73 562 GLY 74 563 GLU 75 564 LYS 76 565 LYS 77 566 ARG 78 567 VAL 79 568 VAL 80 569 VAL 81 570 THR 82 571 PRO 83 572 LYS 84 573 THR 85 574 VAL 86 575 GLU 87 576 SER 88 577 LEU 89 578 LEU 90 579 GLY 91 580 LYS 92 581 PRO 93 582 ARG 94 583 TYR 95 584 ARG 96 585 TYR 97 586 GLY 98 587 LEU 99 588 ALA 100 589 GLU 101 590 ARG 102 591 GLU 103 592 ASP 104 593 GLN 105 594 VAL 106 595 GLY 107 596 ALA 108 597 VAL 109 598 THR 110 599 GLY 111 600 LEU 112 601 ALA 113 602 TRP 114 603 THR 115 604 GLN 116 605 ALA 117 606 LEU 118 607 GLU 119 608 HIS 120 609 HIS 121 610 HIS 122 611 HIS 123 612 HIS 124 613 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-05-05 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 4GIT "Crystal Structure Of Alpha Sub-domain Of Lon Protease From Brevibacillus Thermoruber" 100.00 124 100.00 100.00 3.39e-84 GB AAO43974 "Lon protease [Brevibacillus thermoruber]" 93.55 779 99.14 100.00 2.95e-71 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $alpha_sub-domain 'Brevibacillus thermoruber' 33942 Bacteria . Brevibacillus thermoruber WR-249 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 $alpha_sub-domain 'recombinant technology' . Escherichia coli BL23(DE3) pET-21a stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'phosphate (pH 6.5) containing 100 mM NaCl, and 5 mM DTT' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $alpha_sub-domain 0.5 mM '[U-98% 13C; U-98% 15N]' 'sodium phosphate' 50 mM 'natural abundance' 'sodium chloride' 100 mM 'natural abundance' DTT 5 mM 'natural abundance' D2O 10 % 'natural abundance' H2O 90 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ 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 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _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_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _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' 0.1 . M pH 6.5 . pH pressure 1 . atm temperature 298 . 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 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0 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_ _Experiment_label '2D 1H-15N HSQC' '3D HNCACB' '3D CBCA(CO)NH' '3D HNCO' '3D HN(CA)CO' 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 'alpha sub-domain' _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 1 492 3 GLY C C 170.84 0.2 1 2 492 3 GLY CA C 41.9 0.2 1 3 493 4 TYR H H 7.99 0.02 1 4 493 4 TYR HA H 5.07 0.02 1 5 493 4 TYR C C 174.98 0.2 1 6 493 4 TYR CA C 39.13 0.2 1 7 493 4 TYR N N 119.13 0.1 1 8 494 5 THR H H 9.32 0.02 1 9 494 5 THR HA H 4.56 0.02 1 10 494 5 THR C C 172.8 0.2 1 11 494 5 THR CA C 58.54 0.2 1 12 494 5 THR N N 114.29 0.1 1 13 495 6 GLU H H 8.94 0.02 1 14 495 6 GLU HA H 3.93 0.02 1 15 495 6 GLU C C 175.15 0.2 1 16 495 6 GLU CA C 58.44 0.2 1 17 495 6 GLU N N 121.35 0.1 1 18 496 7 LEU H H 8 0.02 1 19 496 7 LEU HA H 4.05 0.02 1 20 496 7 LEU C C 176.78 0.2 1 21 496 7 LEU CA C 54.97 0.2 1 22 496 7 LEU N N 117.43 0.1 1 23 497 8 GLU H H 7.67 0.02 1 24 497 8 GLU HA H 4.05 0.02 1 25 497 8 GLU C C 177.41 0.2 1 26 497 8 GLU CA C 56.95 0.2 1 27 497 8 GLU N N 118.69 0.1 1 28 498 9 LYS H H 8.4 0.02 1 29 498 9 LYS HA H 3.57 0.02 1 30 498 9 LYS C C 175.05 0.2 1 31 498 9 LYS CA C 58.34 0.2 1 32 498 9 LYS N N 117.99 0.1 1 33 499 10 LEU H H 8.34 0.02 1 34 499 10 LEU HA H 4.32 0.02 1 35 499 10 LEU C C 176.21 0.2 1 36 499 10 LEU CA C 56.26 0.2 1 37 499 10 LEU N N 121.02 0.1 1 38 500 11 HIS H H 7.85 0.02 1 39 500 11 HIS HA H 4.32 0.02 1 40 500 11 HIS CA C 55.96 0.2 1 41 500 11 HIS N N 117.49 0.1 1 42 501 12 ILE C C 176.93 0.2 1 43 501 12 ILE CA C 62.89 0.2 1 44 502 13 MET H H 9.23 0.02 1 45 502 13 MET HA H 3.96 0.02 1 46 502 13 MET C C 173.16 0.2 1 47 502 13 MET CA C 57.74 0.2 1 48 502 13 MET N N 123.22 0.1 1 49 503 14 ARG H H 8.69 0.02 1 50 503 14 ARG HA H 3.91 0.02 1 51 503 14 ARG C C 174.83 0.2 1 52 503 14 ARG CA C 57.05 0.2 1 53 503 14 ARG N N 117.36 0.1 1 54 504 15 ASP H H 8.54 0.02 1 55 504 15 ASP HA H 4.02 0.02 1 56 504 15 ASP CA C 53.19 0.2 1 57 504 15 ASP N N 113.2 0.1 1 58 507 18 LEU H H 9.18 0.02 1 59 507 18 LEU HA H 4.24 0.02 1 60 507 18 LEU C C 178.22 0.2 1 61 507 18 LEU CA C 56.95 0.2 1 62 507 18 LEU N N 118.05 0.1 1 63 508 19 PRO C C 177.01 0.2 1 64 509 20 LYS H H 7.42 0.02 1 65 509 20 LYS HA H 4.25 0.02 1 66 509 20 LYS C C 176.63 0.2 1 67 509 20 LYS CA C 56.36 0.2 1 68 509 20 LYS N N 117.3 0.1 1 69 510 21 GLN H H 8.33 0.02 1 70 510 21 GLN HA H 4.47 0.02 1 71 510 21 GLN C C 177.79 0.2 1 72 510 21 GLN CA C 55.47 0.2 1 73 510 21 GLN N N 117.94 0.1 1 74 511 22 MET H H 9.3 0.02 1 75 511 22 MET HA H 3.92 0.02 1 76 511 22 MET C C 175.53 0.2 1 77 511 22 MET CA C 58.57 0.2 1 78 511 22 MET N N 123.01 0.1 1 79 512 23 GLU H H 7.81 0.02 1 80 512 23 GLU HA H 4.13 0.02 1 81 512 23 GLU C C 178.13 0.2 1 82 512 23 GLU CA C 57.37 0.2 1 83 512 23 GLU N N 120.43 0.1 1 84 513 24 GLU H H 8.29 0.02 1 85 513 24 GLU HA H 4.05 0.02 1 86 513 24 GLU C C 174.83 0.2 1 87 513 24 GLU CA C 56.51 0.2 1 88 513 24 GLU N N 119.18 0.1 1 89 514 25 HIS H H 7.57 0.02 1 90 514 25 HIS HA H 4.57 0.02 1 91 514 25 HIS C C 171.81 0.2 1 92 514 25 HIS CA C 55.11 0.2 1 93 514 25 HIS N N 113.71 0.1 1 94 515 26 GLY H H 7.73 0.02 1 95 515 26 GLY HA2 H 4.00 0.02 . 96 515 26 GLY HA3 H 4.00 0.02 . 97 515 26 GLY C C 172.15 0.2 1 98 515 26 GLY CA C 44.34 0.2 1 99 515 26 GLY N N 108.38 0.1 1 100 516 27 LEU H H 8.46 0.02 1 101 516 27 LEU HA H 4.48 0.02 1 102 516 27 LEU C C 173.01 0.2 1 103 516 27 LEU CA C 50.99 0.2 1 104 516 27 LEU N N 119.64 0.1 1 105 517 28 GLY H H 7.8 0.02 1 106 517 28 GLY HA2 H 4.27 0.02 . 107 517 28 GLY HA3 H 3.93 0.02 . 108 517 28 GLY C C 171.9 0.2 1 109 517 28 GLY CA C 41.87 0.2 1 110 517 28 GLY N N 108.78 0.1 1 111 518 29 ARG H H 8.64 0.02 1 112 518 29 ARG HA H 4.02 0.02 1 113 518 29 ARG C C 173.99 0.2 1 114 518 29 ARG CA C 55.71 0.2 1 115 518 29 ARG N N 119.35 0.1 1 116 519 30 ASP H H 8.83 0.02 1 117 519 30 ASP HA H 4.52 0.02 1 118 519 30 ASP C C 174.39 0.2 1 119 519 30 ASP CA C 51.98 0.2 1 120 519 30 ASP N N 114.2 0.1 1 121 520 31 LYS H H 7.76 0.02 1 122 520 31 LYS HA H 4.40 0.02 1 123 520 31 LYS C C 171.92 0.2 1 124 520 31 LYS CA C 54.18 0.2 1 125 520 31 LYS N N 117.08 0.1 1 126 521 32 LEU H H 7.15 0.02 1 127 521 32 LEU HA H 5.31 0.02 1 128 521 32 LEU C C 171.62 0.2 1 129 521 32 LEU CA C 51.25 0.2 1 130 521 32 LEU N N 119.34 0.1 1 131 522 33 GLN H H 8.48 0.02 1 132 522 33 GLN HA H 4.65 0.02 1 133 522 33 GLN C C 170.94 0.2 1 134 522 33 GLN CA C 51.58 0.2 1 135 522 33 GLN N N 124.84 0.1 1 136 523 34 MET H H 8.86 0.02 1 137 523 34 MET HA H 5.08 0.02 1 138 523 34 MET C C 170.84 0.2 1 139 523 34 MET CA C 52.32 0.2 1 140 523 34 MET N N 125.84 0.1 1 141 524 35 ASN H H 7.64 0.02 1 142 524 35 ASN HA H 4.93 0.02 1 143 524 35 ASN C C 172.91 0.2 1 144 524 35 ASN CA C 48.99 0.2 1 145 524 35 ASN N N 123.03 0.1 1 146 525 36 GLU H H 8.92 0.02 1 147 525 36 GLU HA H 3.98 0.02 1 148 525 36 GLU C C 175.98 0.2 1 149 525 36 GLU CA C 58.1 0.2 1 150 525 36 GLU N N 120.41 0.1 1 151 526 37 GLU H H 8.91 0.02 1 152 526 37 GLU HA H 4.02 0.02 1 153 526 37 GLU C C 177.44 0.2 1 154 526 37 GLU CA C 57.77 0.2 1 155 526 37 GLU N N 118.78 0.1 1 156 527 38 ALA H H 8.48 0.02 1 157 527 38 ALA HA H 3.84 0.02 1 158 527 38 ALA C C 176.04 0.2 1 159 527 38 ALA CA C 53.25 0.2 1 160 527 38 ALA N N 122.71 0.1 1 161 528 39 MET H H 7.93 0.02 1 162 528 39 MET HA H 3.81 0.02 1 163 528 39 MET C C 175.19 0.2 1 164 528 39 MET CA C 58.63 0.2 1 165 528 39 MET N N 117.29 0.1 1 166 529 40 LEU H H 8.56 0.02 1 167 529 40 LEU HA H 4.01 0.02 1 168 529 40 LEU C C 175.51 0.2 1 169 529 40 LEU CA C 55.44 0.2 1 170 529 40 LEU N N 118.5 0.1 1 171 530 41 LYS H H 7.75 0.02 1 172 530 41 LYS HA H 4.22 0.02 1 173 530 41 LYS C C 176.06 0.2 1 174 530 41 LYS CA C 57.5 0.2 1 175 530 41 LYS N N 119.81 0.1 1 176 531 42 VAL H H 7.84 0.02 1 177 531 42 VAL HA H 3.82 0.02 1 178 531 42 VAL C C 175.36 0.2 1 179 531 42 VAL CA C 64.42 0.2 1 180 531 42 VAL N N 118.97 0.1 1 181 532 43 ILE H H 8.18 0.02 1 182 532 43 ILE HA H 3.50 0.02 1 183 532 43 ILE C C 174.39 0.2 1 184 532 43 ILE CA C 63.35 0.2 1 185 532 43 ILE N N 118.59 0.1 1 186 533 44 ARG H H 8.82 0.02 1 187 533 44 ARG HA H 4.18 0.02 1 188 533 44 ARG C C 176.02 0.2 1 189 533 44 ARG CA C 56.84 0.2 1 190 533 44 ARG N N 114.74 0.1 1 191 534 45 GLN H H 8.72 0.02 1 192 534 45 GLN HA H 5.06 0.02 1 193 534 45 GLN C C 174.66 0.2 1 194 534 45 GLN CA C 54.18 0.2 1 195 534 45 GLN N N 110.5 0.1 1 196 535 46 TYR H H 8.3 0.02 1 197 535 46 TYR HA H 4.72 0.02 1 198 535 46 TYR C C 172 0.2 1 199 535 46 TYR CA C 56.04 0.2 1 200 535 46 TYR N N 115.47 0.1 1 201 536 47 THR H H 7.43 0.02 1 202 536 47 THR HA H 4.93 0.02 1 203 536 47 THR C C 168.28 0.2 1 204 536 47 THR CA C 57.04 0.2 1 205 536 47 THR N N 108.1 0.1 1 206 537 48 ARG H H 8.91 0.02 1 207 537 48 ARG C C 107.79 0.2 1 208 537 48 ARG CA C 53.59 0.2 1 209 537 48 ARG N N 123.04 0.1 1 210 538 49 GLU H H 8.72 0.02 1 211 538 49 GLU HA H 4.91 0.02 1 212 538 49 GLU C C 172.55 0.2 1 213 538 49 GLU CA C 51.9 0.2 1 214 538 49 GLU N N 121.39 0.1 1 215 539 50 ALA C C 176.19 0.2 1 216 539 50 ALA CA C 51.41 0.2 1 217 540 51 GLY H H 7.68 0.02 1 218 540 51 GLY HA2 H 3.98 0.02 . 219 540 51 GLY HA3 H 3.98 0.02 . 220 540 51 GLY C C 169.72 0.2 1 221 540 51 GLY CA C 41.87 0.2 1 222 540 51 GLY N N 106.3 0.1 1 223 541 52 VAL H H 8.49 0.02 1 224 541 52 VAL HA H 4.99 0.02 1 225 541 52 VAL C C 173.54 0.2 1 226 541 52 VAL CA C 57.44 0.2 1 227 541 52 VAL N N 108.72 0.1 1 228 542 53 ARG H H 7.79 0.02 1 229 542 53 ARG HA H 4.13 0.02 1 230 542 53 ARG C C 177.24 0.2 1 231 542 53 ARG CA C 57.7 0.2 1 232 542 53 ARG N N 124.16 0.1 1 233 543 54 ASN H H 11.86 0.02 1 234 543 54 ASN HA H 4.67 0.02 1 235 543 54 ASN C C 176.34 0.2 1 236 543 54 ASN CA C 53.65 0.2 1 237 543 54 ASN N N 124.34 0.1 1 238 544 55 LEU H H 9.22 0.02 1 239 544 55 LEU HA H 3.92 0.02 1 240 544 55 LEU C C 175.62 0.2 1 241 544 55 LEU CA C 55.57 0.2 1 242 544 55 LEU N N 126.7 0.1 1 243 545 56 ASN H H 8.52 0.02 1 244 545 56 ASN HA H 4.43 0.02 1 245 545 56 ASN C C 174.18 0.2 1 246 545 56 ASN CA C 54.31 0.2 1 247 545 56 ASN N N 115.94 0.1 1 248 546 57 ARG H H 7.39 0.02 1 249 546 57 ARG HA H 4.12 0.02 1 250 546 57 ARG C C 176.4 0.2 1 251 546 57 ARG CA C 56.9 0.2 1 252 546 57 ARG N N 118.64 0.1 1 253 547 58 GLU H H 8.3 0.02 1 254 547 58 GLU HA H 4.75 0.02 1 255 547 58 GLU C C 176.86 0.2 1 256 547 58 GLU CA C 55.17 0.2 1 257 547 58 GLU N N 117.92 0.1 1 258 548 59 ALA H H 8.55 0.02 1 259 548 59 ALA HA H 3.86 0.02 1 260 548 59 ALA C C 176.48 0.2 1 261 548 59 ALA CA C 53.18 0.2 1 262 548 59 ALA N N 121.9 0.1 1 263 549 60 ALA H H 8.22 0.02 1 264 549 60 ALA HA H 3.82 0.02 1 265 549 60 ALA C C 175.98 0.2 1 266 549 60 ALA CA C 53.31 0.2 1 267 549 60 ALA N N 121.31 0.1 1 268 550 61 ASN H H 8.19 0.02 1 269 550 61 ASN HA H 4.41 0.02 1 270 550 61 ASN C C 175.28 0.2 1 271 550 61 ASN CA C 53.38 0.2 1 272 550 61 ASN N N 117.2 0.1 1 273 551 62 ILE H H 8.35 0.02 1 274 551 62 ILE HA H 3.35 0.02 1 275 551 62 ILE C C 174.33 0.2 1 276 551 62 ILE CA C 63.16 0.2 1 277 551 62 ILE N N 119.45 0.1 1 278 552 63 CYS H H 7.48 0.02 1 279 552 63 CYS HA H 3.78 0.02 1 280 552 63 CYS C C 172.82 0.2 1 281 552 63 CYS CA C 61.96 0.2 1 282 552 63 CYS N N 116.04 0.1 1 283 553 64 ARG H H 8.68 0.02 1 284 553 64 ARG HA H 3.78 0.02 1 285 553 64 ARG C C 177.03 0.2 1 286 553 64 ARG CA C 57.24 0.2 1 287 553 64 ARG N N 121 0.1 1 288 554 65 LYS H H 7.89 0.02 1 289 554 65 LYS HA H 4.08 0.02 1 290 554 65 LYS C C 176.82 0.2 1 291 554 65 LYS CA C 56.57 0.2 1 292 554 65 LYS N N 118.22 0.1 1 293 555 66 ALA H H 8.65 0.02 1 294 555 66 ALA HA H 4.05 0.02 1 295 555 66 ALA C C 176.06 0.2 1 296 555 66 ALA CA C 52.85 0.2 1 297 555 66 ALA N N 121.54 0.1 1 298 556 67 ALA H H 8.6 0.02 1 299 556 67 ALA HA H 4.04 0.02 1 300 556 67 ALA C C 177.03 0.2 1 301 556 67 ALA CA C 53.11 0.2 1 302 556 67 ALA N N 118.11 0.1 1 303 557 68 ARG H H 7.43 0.02 1 304 557 68 ARG HA H 4.19 0.02 1 305 557 68 ARG C C 176.74 0.2 1 306 557 68 ARG CA C 56.24 0.2 1 307 557 68 ARG N N 116.55 0.1 1 308 558 69 LEU H H 7.69 0.02 1 309 558 69 LEU C C 175.59 0.2 1 310 558 69 LEU CA C 55.57 0.2 1 311 558 69 LEU N N 120.01 0.1 1 312 559 70 ILE H H 7.72 0.02 1 313 559 70 ILE HA H 4.49 0.02 1 314 559 70 ILE C C 178.17 0.2 1 315 559 70 ILE CA C 60.03 0.2 1 316 559 70 ILE N N 118.51 0.1 1 317 560 71 VAL H H 8.87 0.02 1 318 560 71 VAL HA H 3.94 0.02 1 319 560 71 VAL C C 175.57 0.2 1 320 560 71 VAL CA C 63.16 0.2 1 321 560 71 VAL N N 121.71 0.1 1 322 561 72 SER H H 7.92 0.02 1 323 561 72 SER HA H 4.44 0.02 1 324 561 72 SER C C 173.01 0.2 1 325 561 72 SER CA C 57.1 0.2 1 326 561 72 SER N N 112.68 0.1 1 327 562 73 GLY H H 7.79 0.02 1 328 562 73 GLY HA2 H 4.32 0.02 . 329 562 73 GLY HA3 H 3.88 0.02 . 330 562 73 GLY C C 171.79 0.2 1 331 562 73 GLY CA C 42.61 0.2 1 332 562 73 GLY N N 109.48 0.1 1 333 563 74 GLU H H 8.1 0.02 1 334 563 74 GLU HA H 4.11 0.02 1 335 563 74 GLU C C 174.41 0.2 1 336 563 74 GLU CA C 56.51 0.2 1 337 563 74 GLU N N 121.68 0.1 1 338 564 75 LYS H H 7.53 0.02 1 339 564 75 LYS C C 172.99 0.2 1 340 564 75 LYS CA C 50.99 0.2 1 341 564 75 LYS N N 114.11 0.1 1 342 565 76 LYS C C 173.4 0.2 1 343 565 76 LYS CA C 54.64 0.2 1 344 566 77 ARG H H 7.46 0.02 1 345 566 77 ARG HA H 4.67 0.02 1 346 566 77 ARG C C 171.53 0.2 1 347 566 77 ARG CA C 52.25 0.2 1 348 566 77 ARG N N 114.56 0.1 1 349 567 78 VAL H H 8.81 0.02 1 350 567 78 VAL HA H 4.26 0.02 1 351 567 78 VAL C C 170.82 0.2 1 352 567 78 VAL CA C 59.76 0.2 1 353 567 78 VAL N N 124.45 0.1 1 354 568 79 VAL H H 8.42 0.02 1 355 568 79 VAL HA H 4.51 0.02 1 356 568 79 VAL C C 173.31 0.2 1 357 568 79 VAL CA C 59.3 0.2 1 358 568 79 VAL N N 128.75 0.1 1 359 569 80 VAL H H 9.37 0.02 1 360 569 80 VAL HA H 4.06 0.02 1 361 569 80 VAL C C 171.41 0.2 1 362 569 80 VAL CA C 59.83 0.2 1 363 569 80 VAL N N 129.47 0.1 1 364 570 81 THR H H 8.09 0.02 1 365 570 81 THR HA H 4.94 0.02 1 366 570 81 THR C C 171.4 0.2 1 367 570 81 THR CA C 56.97 0.2 1 368 570 81 THR N N 118.49 0.1 1 369 572 83 LYS C C 176.27 0.2 1 370 572 83 LYS CA C 56.24 0.2 1 371 573 84 THR H H 7.86 0.02 1 372 573 84 THR HA H 4.42 0.02 1 373 573 84 THR C C 174.83 0.2 1 374 573 84 THR CA C 61.16 0.2 1 375 573 84 THR N N 112.72 0.1 1 376 574 85 VAL H H 8.13 0.02 1 377 574 85 VAL HA H 3.39 0.02 1 378 574 85 VAL C C 174.16 0.2 1 379 574 85 VAL CA C 64.68 0.2 1 380 574 85 VAL N N 121.56 0.1 1 381 575 86 GLU H H 7.81 0.02 1 382 575 86 GLU HA H 4.44 0.02 1 383 575 86 GLU C C 176.86 0.2 1 384 575 86 GLU CA C 56.04 0.2 1 385 575 86 GLU N N 118.02 0.1 1 386 576 87 SER H H 7.64 0.02 1 387 576 87 SER HA H 4.10 0.02 1 388 576 87 SER C C 172.61 0.2 1 389 576 87 SER CA C 58.57 0.2 1 390 576 87 SER N N 115.26 0.1 1 391 577 88 LEU H H 7.55 0.02 1 392 577 88 LEU HA H 4.36 0.02 1 393 577 88 LEU C C 174.6 0.2 1 394 577 88 LEU CA C 54.04 0.2 1 395 577 88 LEU N N 118.74 0.1 1 396 578 89 LEU H H 8.31 0.02 1 397 578 89 LEU HA H 4.46 0.02 1 398 578 89 LEU C C 175.55 0.2 1 399 578 89 LEU CA C 51.85 0.2 1 400 578 89 LEU N N 114 0.1 1 401 579 90 GLY H H 7.75 0.02 1 402 579 90 GLY HA2 H 3.98 0.02 . 403 579 90 GLY HA3 H 3.98 0.02 . 404 579 90 GLY C C 170.44 0.2 1 405 579 90 GLY CA C 41.14 0.2 1 406 579 90 GLY N N 108.59 0.1 1 407 580 91 LYS H H 8.54 0.02 1 408 580 91 LYS HA H 4.32 0.02 1 409 580 91 LYS C C 173.92 0.2 1 410 580 91 LYS CA C 52.85 0.2 1 411 580 91 LYS N N 121.08 0.1 1 412 581 92 PRO C C 173.16 0.2 1 413 581 92 PRO CA C 60.91 0.2 1 414 582 93 ARG H H 6.57 0.02 1 415 582 93 ARG HA H 3.95 0.02 1 416 582 93 ARG C C 172.87 0.2 1 417 582 93 ARG CA C 54.48 0.2 1 418 582 93 ARG N N 120.64 0.1 1 419 583 94 TYR H H 7.89 0.02 1 420 583 94 TYR HA H 4.88 0.02 1 421 583 94 TYR C C 172.38 0.2 1 422 583 94 TYR CA C 53.49 0.2 1 423 583 94 TYR N N 117.14 0.1 1 424 584 95 ARG H H 8.55 0.02 1 425 584 95 ARG HA H 4.28 0.02 1 426 584 95 ARG C C 173.14 0.2 1 427 584 95 ARG CA C 28.04 0.2 1 428 584 95 ARG N N 120.46 0.1 1 429 585 96 TYR H H 8.35 0.02 1 430 585 96 TYR HA H 4.29 0.02 1 431 585 96 TYR C C 173.01 0.2 1 432 585 96 TYR CA C 55.27 0.2 1 433 585 96 TYR N N 121.79 0.1 1 434 586 97 GLY H H 8.32 0.02 1 435 586 97 GLY HA2 H 3.88 0.02 . 436 586 97 GLY HA3 H 3.88 0.02 . 437 586 97 GLY C C 171.17 0.2 1 438 586 97 GLY CA C 42.69 0.2 1 439 586 97 GLY N N 112.81 0.1 1 440 587 98 LEU H H 7.96 0.02 1 441 587 98 LEU HA H 4.35 0.02 1 442 587 98 LEU C C 174.52 0.2 1 443 587 98 LEU CA C 52.79 0.2 1 444 587 98 LEU N N 121.73 0.1 1 445 588 99 ALA H H 8.27 0.02 1 446 588 99 ALA HA H 4.38 0.02 1 447 588 99 ALA C C 175.04 0.2 1 448 588 99 ALA CA C 50.22 0.2 1 449 588 99 ALA N N 123.98 0.1 1 450 589 100 GLU H H 8.26 0.02 1 451 589 100 GLU HA H 4.30 0.02 1 452 589 100 GLU C C 173.84 0.2 1 453 589 100 GLU CA C 54.48 0.2 1 454 589 100 GLU N N 119.75 0.1 1 455 590 101 ARG H H 8.2 0.02 1 456 590 101 ARG HA H 4.40 0.02 1 457 590 101 ARG C C 173.8 0.2 1 458 590 101 ARG CA C 53.68 0.2 1 459 590 101 ARG N N 120.45 0.1 1 460 591 102 GLU H H 8.5 0.02 1 461 591 102 GLU HA H 4.30 0.02 1 462 591 102 GLU C C 173.65 0.2 1 463 591 102 GLU CA C 54.48 0.2 1 464 591 102 GLU N N 121.76 0.1 1 465 592 103 ASP H H 8.36 0.02 1 466 592 103 ASP HA H 4.61 0.02 1 467 592 103 ASP C C 173.58 0.2 1 468 592 103 ASP CA C 51.9 0.2 1 469 592 103 ASP N N 120.25 0.1 1 470 593 104 GLN H H 8.19 0.02 1 471 593 104 GLN HA H 4.40 0.02 1 472 593 104 GLN C C 173.48 0.2 1 473 593 104 GLN CA C 53.29 0.2 1 474 593 104 GLN N N 119.93 0.1 1 475 594 105 VAL H H 8.11 0.02 1 476 594 105 VAL HA H 4.14 0.02 1 477 594 105 VAL C C 174.18 0.2 1 478 594 105 VAL CA C 60.32 0.2 1 479 594 105 VAL N N 121.08 0.1 1 480 595 106 GLY H H 8.45 0.02 1 481 595 106 GLY HA2 H 4.00 0.02 . 482 595 106 GLY HA3 H 4.00 0.02 . 483 595 106 GLY C C 171.19 0.2 1 484 595 106 GLY CA C 42.89 0.2 1 485 595 106 GLY N N 112.17 0.1 1 486 596 107 ALA H H 8.06 0.02 1 487 596 107 ALA HA H 4.42 0.02 1 488 596 107 ALA C C 175.24 0.2 1 489 596 107 ALA CA C 49.92 0.2 1 490 596 107 ALA N N 123.59 0.1 1 491 597 108 VAL H H 8.17 0.02 1 492 597 108 VAL HA H 4.26 0.02 1 493 597 108 VAL C C 173.78 0.2 1 494 597 108 VAL CA C 59.92 0.2 1 495 597 108 VAL N N 119.08 0.1 1 496 598 109 THR H H 8.13 0.02 1 497 598 109 THR HA H 4.40 0.02 1 498 598 109 THR C C 172.38 0.2 1 499 598 109 THR CA C 59.43 0.2 1 500 598 109 THR N N 116.9 0.1 1 501 599 110 GLY H H 8.34 0.02 1 502 599 110 GLY HA2 H 4.02 0.02 . 503 599 110 GLY HA3 H 4.02 0.02 . 504 599 110 GLY C C 170.43 0.2 1 505 599 110 GLY CA C 42.79 0.2 1 506 599 110 GLY N N 111.35 0.1 1 507 600 111 LEU H H 7.74 0.02 1 508 600 111 LEU HA H 4.27 0.02 1 509 600 111 LEU C C 170.43 0.2 1 510 600 111 LEU CA C 54.28 0.2 1 511 600 111 LEU N N 127.26 0.1 1 512 601 112 ALA C C 175.34 0.2 1 513 601 112 ALA CA C 49.88 0.2 1 514 602 113 TRP H H 8.15 0.02 1 515 602 113 TRP C C 174.03 0.2 1 516 602 113 TRP CA C 59.91 0.2 1 517 602 113 TRP N N 118.79 0.1 1 518 603 114 THR H H 7.68 0.02 1 519 603 114 THR CA C 59.9 0.2 1 520 603 114 THR N N 114.52 0.1 1 stop_ save_