data_27185 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; ProXp-ala free form ; _BMRB_accession_number 27185 _BMRB_flat_file_name bmr27185.str _Entry_type original _Submission_date 2017-07-20 _Accession_date 2017-07-20 _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 Danhart Eric . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 156 "13C chemical shifts" 182 "15N chemical shifts" 156 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2017-11-02 update BMRB 'update entry citation' 2017-08-21 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 27191 'ProXp-ala bound to microhelixPro' stop_ _Original_release_date 2017-07-21 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Conformational and chemical selection by a trans-acting editing domain. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 28768811 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Danhart Eric M. . 2 Bakhtina Marina . . 3 Cantara William A. . 4 Kuzmishin Alexandra B. . 5 Ma Xiao . . 6 Sanford Brianne L. . 7 Kosutic Marija . . 8 Goto Yuki . . 9 Suga Hiroaki . . 10 Nakanishi Kotaro . . 11 Micura Ronald . . 12 Foster Mark P. . 13 Musier-Forsyth Karin . . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U.S.A.' _Journal_name_full 'Proceedings of the National Academy of Sciences of the United States of America' _Journal_volume 114 _Journal_issue 33 _Journal_ISSN 1091-6490 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first E6774 _Page_last E6783 _Year 2017 _Details . loop_ _Keyword NMR 'aminoacyl-tRNA synthetases' 'conformational selection' 'molecular dynamics' trans-editing stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name ProXp-ala _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label ProXp-ala $ProXp-ala 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_ProXp-ala _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common ProXp-ala _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 171 _Mol_residue_sequence ; GSHMKTRADLFAFFDAHGVD HKTLDHPPVFRVEEGLEIKA AMPGGHTKNLFLKDAKGQLW LISALGETTIDLKKLHHVIG SGRLSFGPQEMMLETLGVTP GSVTAFGLINDTEKRVRFVL DKALADSDPVNFHPLKNDAT TAVSQAGLRRFLAALGVEPM IVDFAAMEVVG ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -2 GLY 2 -1 SER 3 0 HIS 4 1 MET 5 2 LYS 6 3 THR 7 4 ARG 8 5 ALA 9 6 ASP 10 7 LEU 11 8 PHE 12 9 ALA 13 10 PHE 14 11 PHE 15 12 ASP 16 13 ALA 17 14 HIS 18 15 GLY 19 16 VAL 20 17 ASP 21 18 HIS 22 19 LYS 23 20 THR 24 21 LEU 25 22 ASP 26 23 HIS 27 24 PRO 28 25 PRO 29 26 VAL 30 27 PHE 31 28 ARG 32 29 VAL 33 30 GLU 34 31 GLU 35 32 GLY 36 33 LEU 37 34 GLU 38 35 ILE 39 36 LYS 40 37 ALA 41 38 ALA 42 39 MET 43 40 PRO 44 41 GLY 45 42 GLY 46 43 HIS 47 44 THR 48 45 LYS 49 46 ASN 50 47 LEU 51 48 PHE 52 49 LEU 53 50 LYS 54 51 ASP 55 52 ALA 56 53 LYS 57 54 GLY 58 55 GLN 59 56 LEU 60 57 TRP 61 58 LEU 62 59 ILE 63 60 SER 64 61 ALA 65 62 LEU 66 63 GLY 67 64 GLU 68 65 THR 69 66 THR 70 67 ILE 71 68 ASP 72 69 LEU 73 70 LYS 74 71 LYS 75 72 LEU 76 73 HIS 77 74 HIS 78 75 VAL 79 76 ILE 80 77 GLY 81 78 SER 82 79 GLY 83 80 ARG 84 81 LEU 85 82 SER 86 83 PHE 87 84 GLY 88 85 PRO 89 86 GLN 90 87 GLU 91 88 MET 92 89 MET 93 90 LEU 94 91 GLU 95 92 THR 96 93 LEU 97 94 GLY 98 95 VAL 99 96 THR 100 97 PRO 101 98 GLY 102 99 SER 103 100 VAL 104 101 THR 105 102 ALA 106 103 PHE 107 104 GLY 108 105 LEU 109 106 ILE 110 107 ASN 111 108 ASP 112 109 THR 113 110 GLU 114 111 LYS 115 112 ARG 116 113 VAL 117 114 ARG 118 115 PHE 119 116 VAL 120 117 LEU 121 118 ASP 122 119 LYS 123 120 ALA 124 121 LEU 125 122 ALA 126 123 ASP 127 124 SER 128 125 ASP 129 126 PRO 130 127 VAL 131 128 ASN 132 129 PHE 133 130 HIS 134 131 PRO 135 132 LEU 136 133 LYS 137 134 ASN 138 135 ASP 139 136 ALA 140 137 THR 141 138 THR 142 139 ALA 143 140 VAL 144 141 SER 145 142 GLN 146 143 ALA 147 144 GLY 148 145 LEU 149 146 ARG 150 147 ARG 151 148 PHE 152 149 LEU 153 150 ALA 154 151 ALA 155 152 LEU 156 153 GLY 157 154 VAL 158 155 GLU 159 156 PRO 160 157 MET 161 158 ILE 162 159 VAL 163 160 ASP 164 161 PHE 165 162 ALA 166 163 ALA 167 164 MET 168 165 GLU 169 166 VAL 170 167 VAL 171 168 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 $ProXp-ala 'Caulobacter vibrioides' 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 $ProXp-ala 'recombinant technology' . Escherichia coli . pET15b stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details ProXp-ala loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $ProXp-ala 0.7 mM '[U-100% 13C; U-100% 15N]' 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_ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ save_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _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_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _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' 0.16 . M pH 7.5 . 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 0.00 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_ _Experiment_label '3D CBCA(CO)NH' '3D HNCO' '3D HNCA' '3D HNCACB' 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 ProXp-ala _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 0 3 HIS CA C 53.2371 0.0000 1 2 0 3 HIS CB C 28.0191 0.0000 1 3 1 4 MET H H 8.2004 0.0000 1 4 1 4 MET CA C 55.3864 0.0000 1 5 1 4 MET N N 122.2349 0.0000 1 6 2 5 LYS H H 8.9369 0.0000 1 7 2 5 LYS CA C 56.2662 0.0000 1 8 2 5 LYS N N 123.6043 0.0000 1 9 3 6 THR H H 9.1213 0.0000 1 10 3 6 THR CA C 59.9580 0.0000 1 11 3 6 THR N N 112.4858 0.0000 1 12 4 7 ARG H H 8.8440 0.0000 1 13 4 7 ARG CA C 60.0282 0.0000 1 14 4 7 ARG N N 121.4095 0.0000 1 15 5 8 ALA H H 8.0264 0.0000 1 16 5 8 ALA CA C 55.2395 0.0000 1 17 5 8 ALA N N 118.7584 0.0000 1 18 6 9 ASP H H 7.4708 0.0000 1 19 6 9 ASP CA C 56.9958 0.0000 1 20 6 9 ASP CB C 38.5904 0.0000 1 21 6 9 ASP N N 118.2632 0.0000 1 22 7 10 LEU H H 8.0244 0.0000 1 23 7 10 LEU CA C 57.7128 0.0000 1 24 7 10 LEU N N 122.8644 0.0000 1 25 8 11 PHE H H 7.9973 0.0000 1 26 8 11 PHE CA C 58.2735 0.0000 1 27 8 11 PHE N N 117.2390 0.0000 1 28 9 12 ALA H H 7.9333 0.0000 1 29 9 12 ALA CA C 55.2324 0.0000 1 30 9 12 ALA N N 121.3546 0.0000 1 31 10 13 PHE H H 8.0538 0.0000 1 32 10 13 PHE CA C 62.1024 0.0000 1 33 10 13 PHE N N 122.9286 0.0000 1 34 11 14 PHE H H 8.8781 0.0000 1 35 11 14 PHE CA C 57.3444 0.0000 1 36 11 14 PHE N N 118.6125 0.0000 1 37 12 15 ASP H H 8.7133 0.0000 1 38 12 15 ASP CA C 57.3854 0.0000 1 39 12 15 ASP N N 119.9619 0.0000 1 40 13 16 ALA H H 8.0797 0.0000 1 41 13 16 ALA CA C 54.1326 0.0000 1 42 13 16 ALA CB C 15.1651 0.0000 1 43 13 16 ALA N N 122.0956 0.0000 1 44 14 17 HIS H H 7.4235 0.0000 1 45 14 17 HIS CA C 56.5971 0.0000 1 46 14 17 HIS N N 113.4828 0.0000 1 47 15 18 GLY H H 7.6500 0.0000 1 48 15 18 GLY CA C 47.2935 0.0000 1 49 15 18 GLY N N 108.5116 0.0000 1 50 16 19 VAL H H 8.7611 0.0000 1 51 16 19 VAL CA C 62.6274 0.0000 1 52 16 19 VAL CB C 28.9095 0.0000 1 53 16 19 VAL N N 122.8818 0.0000 1 54 17 20 ASP H H 8.3995 0.0000 1 55 17 20 ASP CA C 53.7979 0.0000 1 56 17 20 ASP N N 127.9635 0.0000 1 57 18 21 HIS H H 7.7675 0.0000 1 58 18 21 HIS CA C 53.9588 0.0000 1 59 18 21 HIS N N 113.7546 0.0000 1 60 19 22 LYS H H 8.1632 0.0000 1 61 19 22 LYS CA C 55.8851 0.0000 1 62 19 22 LYS N N 121.9614 0.0000 1 63 20 23 THR H H 8.7870 0.0000 1 64 20 23 THR CA C 63.1399 0.0000 1 65 20 23 THR N N 123.1246 0.0000 1 66 21 24 LEU H H 9.3371 0.0000 1 67 21 24 LEU CA C 53.6919 0.0000 1 68 21 24 LEU N N 131.7124 0.0000 1 69 22 25 ASP H H 8.5806 0.0000 1 70 22 25 ASP CA C 54.7062 0.0000 1 71 22 25 ASP N N 126.6085 0.0000 1 72 23 26 HIS H H 7.9736 0.0000 1 73 23 26 HIS C C 178.4573 0.0000 1 74 23 26 HIS N N 118.9935 0.0000 1 75 25 28 PRO CA C 60.4346 0.0000 1 76 25 28 PRO CB C 28.9977 0.0000 1 77 26 29 VAL H H 7.9732 0.0000 1 78 26 29 VAL CA C 62.2795 0.0000 1 79 26 29 VAL N N 121.8781 0.0000 1 80 27 30 PHE H H 9.0054 0.0000 1 81 27 30 PHE CA C 58.4203 0.0000 1 82 27 30 PHE N N 124.9348 0.0000 1 83 28 31 ARG H H 8.1698 0.0000 1 84 28 31 ARG CA C 54.9079 0.0000 1 85 28 31 ARG N N 119.7563 0.0000 1 86 29 32 VAL H H 8.6979 0.0000 1 87 29 32 VAL CA C 65.4800 0.0000 1 88 29 32 VAL N N 122.4209 0.0000 1 89 30 33 GLU H H 9.6821 0.0000 1 90 30 33 GLU CA C 59.8308 0.0000 1 91 30 33 GLU N N 120.4024 0.0000 1 92 31 34 GLU H H 7.6548 0.0000 1 93 31 34 GLU CA C 57.7466 0.0000 1 94 31 34 GLU CB C 27.3192 0.0000 1 95 31 34 GLU N N 118.3834 0.0000 1 96 32 35 GLY H H 7.9886 0.0000 1 97 32 35 GLY CA C 46.4875 0.0000 1 98 32 35 GLY N N 107.1829 0.0000 1 99 33 36 LEU H H 7.8644 0.0000 1 100 33 36 LEU CA C 57.7846 0.0000 1 101 33 36 LEU N N 121.2895 0.0000 1 102 34 37 GLU H H 8.1728 0.0000 1 103 34 37 GLU CA C 58.9321 0.0000 1 104 34 37 GLU N N 119.4824 0.0000 1 105 35 38 ILE H H 7.3606 0.0000 1 106 35 38 ILE CA C 63.9606 0.0000 1 107 35 38 ILE N N 121.0010 0.0000 1 108 36 39 LYS H H 7.4924 0.0000 1 109 36 39 LYS CA C 59.0089 0.0000 1 110 36 39 LYS N N 118.4272 0.0000 1 111 37 40 ALA H H 7.5115 0.0000 1 112 37 40 ALA CA C 53.7592 0.0000 1 113 37 40 ALA N N 118.4223 0.0000 1 114 38 41 ALA H H 7.3877 0.0000 1 115 38 41 ALA CA C 52.7538 0.0000 1 116 38 41 ALA N N 118.8012 0.0000 1 117 39 42 MET H H 7.6081 0.0000 1 118 39 42 MET CA C 52.6741 0.0000 1 119 39 42 MET N N 118.0430 0.0000 1 120 40 43 PRO CA C 59.8445 0.0000 1 121 40 43 PRO CB C 30.6156 0.0000 1 122 41 44 GLY H H 8.6069 0.0000 1 123 41 44 GLY CA C 43.8117 0.0000 1 124 41 44 GLY N N 106.7884 0.0000 1 125 42 45 GLY H H 8.7364 0.0000 1 126 42 45 GLY CA C 46.7179 0.0000 1 127 42 45 GLY N N 105.5254 0.0000 1 128 43 46 HIS H H 9.1964 0.0000 1 129 43 46 HIS CA C 57.3995 0.0000 1 130 43 46 HIS N N 129.0677 0.0000 1 131 44 47 THR H H 8.2563 0.0000 1 132 44 47 THR CA C 61.4658 0.0000 1 133 44 47 THR N N 109.7051 0.0000 1 134 45 48 LYS H H 9.1882 0.0000 1 135 45 48 LYS CA C 54.8670 0.0000 1 136 45 48 LYS N N 118.8368 0.0000 1 137 46 49 ASN H H 8.3549 0.0000 1 138 46 49 ASN CA C 52.7333 0.0000 1 139 46 49 ASN N N 120.3213 0.0000 1 140 47 50 LEU H H 9.7365 0.0000 1 141 47 50 LEU CA C 54.3707 0.0000 1 142 47 50 LEU N N 124.0895 0.0000 1 143 48 51 PHE H H 9.4652 0.0000 1 144 48 51 PHE CA C 57.0495 0.0000 1 145 48 51 PHE N N 125.4343 0.0000 1 146 49 52 LEU H H 9.4446 0.0000 1 147 49 52 LEU CA C 53.3252 0.0000 1 148 49 52 LEU N N 129.0133 0.0000 1 149 50 53 LYS H H 8.7082 0.0000 1 150 50 53 LYS CA C 54.5416 0.0000 1 151 50 53 LYS N N 119.5177 0.0000 1 152 51 54 ASP H H 9.1540 0.0000 1 153 51 54 ASP CA C 51.4362 0.0000 1 154 51 54 ASP CB C 41.1429 0.0000 1 155 51 54 ASP N N 126.2392 0.0000 1 156 52 55 ALA H H 7.7268 0.0000 1 157 52 55 ALA CA C 54.2175 0.0000 1 158 52 55 ALA N N 118.5378 0.0000 1 159 53 56 LYS H H 8.2682 0.0000 1 160 53 56 LYS CA C 55.7385 0.0000 1 161 53 56 LYS N N 116.4827 0.0000 1 162 54 57 GLY H H 8.1945 0.0000 1 163 54 57 GLY CA C 45.1382 0.0000 1 164 54 57 GLY N N 108.6031 0.0000 1 165 55 58 GLN H H 8.3098 0.0000 1 166 55 58 GLN CA C 54.9920 0.0000 1 167 55 58 GLN N N 122.8987 0.0000 1 168 56 59 LEU H H 8.1614 0.0000 1 169 56 59 LEU CA C 53.9616 0.0000 1 170 56 59 LEU N N 125.7074 0.0000 1 171 57 60 TRP H H 9.0208 0.0000 1 172 57 60 TRP CA C 56.1366 0.0000 1 173 57 60 TRP N N 122.0051 0.0000 1 174 58 61 LEU H H 9.3183 0.0000 1 175 58 61 LEU CA C 53.1165 0.0000 1 176 58 61 LEU N N 123.6665 0.0000 1 177 59 62 ILE H H 9.3489 0.0000 1 178 59 62 ILE CA C 59.2513 0.0000 1 179 59 62 ILE N N 125.4407 0.0000 1 180 60 63 SER H H 8.8601 0.0000 1 181 60 63 SER CA C 62.2318 0.0000 1 182 60 63 SER N N 124.0694 0.0000 1 183 61 64 ALA H H 9.1354 0.0000 1 184 61 64 ALA CA C 49.7237 0.0000 1 185 61 64 ALA N N 126.3404 0.0000 1 186 62 65 LEU H H 8.9672 0.0000 1 187 62 65 LEU CA C 55.4772 0.0000 1 188 62 65 LEU N N 121.9801 0.0000 1 189 63 66 GLY H H 8.6694 0.0000 1 190 63 66 GLY CA C 47.7773 0.0000 1 191 63 66 GLY N N 109.8107 0.0000 1 192 64 67 GLU H H 8.2401 0.0000 1 193 64 67 GLU CA C 57.0584 0.0000 1 194 64 67 GLU N N 115.4312 0.0000 1 195 65 68 THR H H 7.7073 0.0000 1 196 65 68 THR CA C 63.5456 0.0000 1 197 65 68 THR N N 120.9979 0.0000 1 198 66 69 THR CA C 60.4068 0.0000 1 199 66 69 THR CB C 65.9694 0.0000 1 200 67 70 ILE H H 8.7150 0.0000 1 201 67 70 ILE CA C 60.3267 0.0000 1 202 67 70 ILE N N 127.9200 0.0000 1 203 68 71 ASP H H 8.7927 0.0000 1 204 68 71 ASP CA C 52.3973 0.0000 1 205 68 71 ASP N N 128.0976 0.0000 1 206 69 72 LEU H H 8.5567 0.0000 1 207 69 72 LEU CA C 57.6154 0.0000 1 208 69 72 LEU N N 125.3564 0.0000 1 209 70 73 LYS H H 8.2648 0.0000 1 210 70 73 LYS CA C 58.7007 0.0000 1 211 70 73 LYS N N 116.2779 0.0000 1 212 71 74 LYS H H 7.1122 0.0000 1 213 71 74 LYS CA C 55.5734 0.0000 1 214 71 74 LYS N N 113.8866 0.0000 1 215 72 75 LEU H H 7.4270 0.0000 1 216 72 75 LEU CA C 57.1869 0.0000 1 217 72 75 LEU N N 118.9616 0.0000 1 218 73 76 HIS H H 8.2745 0.0000 1 219 73 76 HIS CA C 58.7399 0.0000 1 220 73 76 HIS N N 116.2986 0.0000 1 221 74 77 HIS H H 6.2916 0.0000 1 222 74 77 HIS CA C 57.6960 0.0000 1 223 74 77 HIS N N 116.9950 0.0000 1 224 75 78 VAL H H 7.3986 0.0000 1 225 75 78 VAL CA C 64.3139 0.0000 1 226 75 78 VAL N N 117.7435 0.0000 1 227 76 79 ILE H H 7.0864 0.0000 1 228 76 79 ILE CA C 61.7268 0.0000 1 229 76 79 ILE N N 133.7567 0.0000 1 230 77 80 GLY H H 7.4329 0.0000 1 231 77 80 GLY CA C 46.5211 0.0000 1 232 77 80 GLY N N 108.6799 0.0000 1 233 78 81 SER H H 7.8121 0.0000 1 234 78 81 SER CA C 63.8214 0.0000 1 235 78 81 SER N N 115.4038 0.0000 1 236 79 82 GLY H H 8.1642 0.0000 1 237 79 82 GLY CA C 44.6966 0.0000 1 238 79 82 GLY N N 102.6587 0.0000 1 239 80 83 ARG H H 8.6772 0.0000 1 240 80 83 ARG CA C 58.4752 0.0000 1 241 80 83 ARG N N 120.8435 0.0000 1 242 81 84 LEU H H 8.7033 0.0000 1 243 81 84 LEU CA C 55.7438 0.0000 1 244 81 84 LEU N N 126.0167 0.0000 1 245 82 85 SER H H 8.0100 0.0000 1 246 82 85 SER CA C 56.7189 0.0000 1 247 82 85 SER N N 113.8814 0.0000 1 248 84 87 GLY H H 9.5197 0.0000 1 249 84 87 GLY C C 175.4956 0.0000 1 250 84 87 GLY N N 111.0849 0.0000 1 251 87 90 GLU H H 10.4102 0.0000 1 252 87 90 GLU C C 174.6999 0.0000 1 253 87 90 GLU CA C 57.6952 0.0000 1 254 87 90 GLU CB C 25.4237 0.0000 1 255 87 90 GLU N N 122.4090 0.0000 1 256 88 91 MET H H 6.9899 0.0000 1 257 88 91 MET CA C 57.5348 0.0000 1 258 88 91 MET CB C 30.1930 0.0000 1 259 88 91 MET N N 116.5548 0.0000 1 260 89 92 MET H H 7.8654 0.0000 1 261 89 92 MET CA C 59.2617 0.0000 1 262 89 92 MET N N 124.3779 0.0000 1 263 90 93 LEU H H 7.7792 0.0000 1 264 90 93 LEU CA C 58.1559 0.0000 1 265 90 93 LEU N N 120.5125 0.0000 1 266 91 94 GLU H H 7.3779 0.0000 1 267 91 94 GLU CA C 59.1282 0.0000 1 268 91 94 GLU N N 115.2691 0.0000 1 269 92 95 THR H H 7.5674 0.0000 1 270 92 95 THR CA C 63.5007 0.0000 1 271 92 95 THR N N 106.2401 0.0000 1 272 93 96 LEU H H 7.3831 0.0000 1 273 93 96 LEU CA C 53.3485 0.0000 1 274 93 96 LEU N N 114.0785 0.0000 1 275 94 97 GLY H H 7.7973 0.0000 1 276 94 97 GLY CA C 47.0765 0.0000 1 277 94 97 GLY N N 107.4351 0.0000 1 278 95 98 VAL H H 6.5470 0.0000 1 279 95 98 VAL CA C 57.5063 0.0000 1 280 95 98 VAL N N 132.7551 0.0000 1 281 96 99 THR H H 7.4891 0.0000 1 282 96 99 THR CA C 58.4926 0.0000 1 283 96 99 THR N N 108.4147 0.0000 1 284 98 101 GLY CA C 42.6796 0.0000 1 285 99 102 SER H H 8.2569 0.0000 1 286 99 102 SER CA C 61.2806 0.0000 1 287 99 102 SER N N 115.4727 0.0000 1 288 100 103 VAL H H 8.0493 0.0000 1 289 100 103 VAL CA C 65.8578 0.0000 1 290 100 103 VAL N N 119.0812 0.0000 1 291 101 104 THR H H 6.0918 0.0000 1 292 101 104 THR CA C 57.5423 0.0000 1 293 101 104 THR N N 115.6836 0.0000 1 294 102 105 ALA H H 5.9404 0.0000 1 295 102 105 ALA CA C 54.5930 0.0000 1 296 102 105 ALA N N 129.6961 0.0000 1 297 103 106 PHE H H 7.5793 0.0000 1 298 103 106 PHE CA C 55.9671 0.0000 1 299 103 106 PHE N N 112.8467 0.0000 1 300 104 107 GLY H H 7.8434 0.0000 1 301 104 107 GLY CA C 46.5088 0.0000 1 302 104 107 GLY N N 105.2166 0.0000 1 303 105 108 LEU H H 7.5714 0.0000 1 304 105 108 LEU CA C 57.6045 0.0000 1 305 105 108 LEU N N 120.0837 0.0000 1 306 106 109 ILE H H 7.4925 0.0000 1 307 106 109 ILE CA C 63.9309 0.0000 1 308 106 109 ILE N N 118.3880 0.0000 1 309 107 110 ASN H H 7.8800 0.0000 1 310 107 110 ASN CA C 54.1159 0.0000 1 311 107 110 ASN N N 117.9313 0.0000 1 312 108 111 ASP H H 7.3473 0.0000 1 313 108 111 ASP CA C 53.4778 0.0000 1 314 108 111 ASP N N 122.7653 0.0000 1 315 109 112 THR H H 8.2718 0.0000 1 316 109 112 THR CA C 65.6210 0.0000 1 317 109 112 THR N N 116.9516 0.0000 1 318 110 113 GLU H H 8.8833 0.0000 1 319 110 113 GLU CA C 55.6188 0.0000 1 320 110 113 GLU N N 118.8293 0.0000 1 321 111 114 LYS H H 7.9322 0.0000 1 322 111 114 LYS CA C 56.3043 0.0000 1 323 111 114 LYS N N 118.6204 0.0000 1 324 112 115 ARG H H 10.3607 0.0000 1 325 112 115 ARG CA C 57.4187 0.0000 1 326 112 115 ARG N N 122.0481 0.0000 1 327 113 116 VAL H H 9.9246 0.0000 1 328 113 116 VAL CA C 61.8176 0.0000 1 329 113 116 VAL N N 123.1453 0.0000 1 330 114 117 ARG H H 7.7229 0.0000 1 331 114 117 ARG CA C 55.6434 0.0000 1 332 114 117 ARG N N 126.9213 0.0000 1 333 115 118 PHE H H 8.8585 0.0000 1 334 115 118 PHE CA C 56.0656 0.0000 1 335 115 118 PHE N N 124.0289 0.0000 1 336 116 119 VAL H H 9.2258 0.0000 1 337 116 119 VAL CA C 60.4578 0.0000 1 338 116 119 VAL CB C 31.6288 0.0000 1 339 116 119 VAL N N 131.1319 0.0000 1 340 117 120 LEU H H 8.8309 0.0000 1 341 117 120 LEU CA C 51.7522 0.0000 1 342 117 120 LEU N N 126.8013 0.0000 1 343 118 121 ASP H H 8.2118 0.0000 1 344 118 121 ASP CA C 53.8398 0.0000 1 345 118 121 ASP N N 124.4663 0.0000 1 346 119 122 LYS H H 9.6099 0.0000 1 347 119 122 LYS CA C 59.1129 0.0000 1 348 119 122 LYS CB C 30.5178 0.0000 1 349 119 122 LYS N N 108.5994 0.0000 1 350 120 123 ALA H H 8.3878 0.0000 1 351 120 123 ALA CA C 54.7028 0.0000 1 352 120 123 ALA N N 118.1334 0.0000 1 353 121 124 LEU H H 7.2454 0.0000 1 354 121 124 LEU CA C 56.5156 0.0000 1 355 121 124 LEU N N 119.1176 0.0000 1 356 122 125 ALA H H 8.6238 0.0000 1 357 122 125 ALA CA C 53.7590 0.0000 1 358 122 125 ALA N N 124.2174 0.0000 1 359 123 126 ASP H H 7.4066 0.0000 1 360 123 126 ASP CA C 54.1058 0.0000 1 361 123 126 ASP N N 113.4665 0.0000 1 362 124 127 SER H H 7.5017 0.0000 1 363 124 127 SER CA C 59.3271 0.0000 1 364 124 127 SER N N 117.1291 0.0000 1 365 125 128 ASP H H 8.5616 0.0000 1 366 125 128 ASP C C 181.4574 0.0000 1 367 125 128 ASP CA C 59.8075 0.0000 1 368 125 128 ASP N N 122.2783 0.0000 1 369 127 130 VAL H H 9.1309 0.0000 1 370 127 130 VAL C C 178.3486 0.0000 1 371 127 130 VAL N N 110.0983 0.0000 1 372 128 131 ASN H H 6.9749 0.0000 1 373 128 131 ASN C C 179.6504 0.0000 1 374 128 131 ASN N N 118.2462 0.0000 1 375 129 132 PHE H H 9.2307 0.0000 1 376 129 132 PHE C C 179.5552 0.0000 1 377 129 132 PHE N N 118.4597 0.0000 1 378 130 133 HIS H H 9.7099 0.0000 1 379 130 133 HIS C C 177.0809 0.0000 1 380 130 133 HIS CA C 52.1167 0.0000 1 381 130 133 HIS N N 119.4667 0.0000 1 382 132 135 LEU H H 7.7182 0.0000 1 383 132 135 LEU C C 179.1815 0.0000 1 384 132 135 LEU CA C 58.2079 0.0000 1 385 132 135 LEU CB C 35.1927 0.0000 1 386 132 135 LEU N N 109.1936 0.0000 1 387 133 136 LYS H H 7.1122 0.0000 1 388 133 136 LYS CA C 55.8675 0.0000 1 389 133 136 LYS N N 116.6143 0.0000 1 390 134 137 ASN H H 7.8252 0.0000 1 391 134 137 ASN CA C 52.7878 0.0000 1 392 134 137 ASN N N 120.7967 0.0000 1 393 135 138 ASP H H 7.6046 0.0000 1 394 135 138 ASP CA C 52.1941 0.0000 1 395 135 138 ASP CB C 36.3563 0.0000 1 396 135 138 ASP N N 118.6056 0.0000 1 397 136 139 ALA H H 7.3444 0.0000 1 398 136 139 ALA CA C 51.6481 0.0000 1 399 136 139 ALA N N 118.7282 0.0000 1 400 137 140 THR H H 9.1909 0.0000 1 401 137 140 THR CA C 65.2801 0.0000 1 402 137 140 THR N N 118.9087 0.0000 1 403 138 141 THR H H 9.5749 0.0000 1 404 138 141 THR CA C 63.0873 0.0000 1 405 138 141 THR N N 127.2549 0.0000 1 406 139 142 ALA H H 9.5181 0.0000 1 407 139 142 ALA CA C 50.4385 0.0000 1 408 139 142 ALA N N 129.8366 0.0000 1 409 140 143 VAL H H 9.0229 0.0000 1 410 140 143 VAL CA C 58.7005 0.0000 1 411 140 143 VAL N N 117.6612 0.0000 1 412 141 144 SER H H 9.3692 0.0000 1 413 141 144 SER CA C 61.8729 0.0000 1 414 141 144 SER N N 118.3708 0.0000 1 415 142 145 GLN H H 9.2276 0.0000 1 416 142 145 GLN CA C 59.2750 0.0000 1 417 142 145 GLN N N 123.2191 0.0000 1 418 143 146 ALA H H 8.8516 0.0000 1 419 143 146 ALA CA C 55.2433 0.0000 1 420 143 146 ALA N N 119.7708 0.0000 1 421 144 147 GLY H H 8.9887 0.0000 1 422 144 147 GLY CA C 47.4017 0.0000 1 423 144 147 GLY N N 111.6561 0.0000 1 424 145 148 LEU H H 9.0892 0.0000 1 425 145 148 LEU CA C 58.5307 0.0000 1 426 145 148 LEU N N 124.4301 0.0000 1 427 146 149 ARG H H 8.4708 0.0000 1 428 146 149 ARG CA C 58.4236 0.0000 1 429 146 149 ARG N N 115.4309 0.0000 1 430 147 150 ARG H H 8.5530 0.0000 1 431 147 150 ARG CA C 57.5944 0.0000 1 432 147 150 ARG N N 122.3181 0.0000 1 433 148 151 PHE H H 8.7096 0.0000 1 434 148 151 PHE CA C 61.3865 0.0000 1 435 148 151 PHE N N 122.0294 0.0000 1 436 149 152 LEU H H 8.2871 0.0000 1 437 149 152 LEU CA C 57.7716 0.0000 1 438 149 152 LEU N N 116.3168 0.0000 1 439 150 153 ALA H H 8.3400 0.0000 1 440 150 153 ALA CA C 55.0792 0.0000 1 441 150 153 ALA N N 120.9450 0.0000 1 442 151 154 ALA H H 8.1477 0.0000 1 443 151 154 ALA CA C 54.5160 0.0000 1 444 151 154 ALA N N 122.1191 0.0000 1 445 152 155 LEU H H 7.1334 0.0000 1 446 152 155 LEU CA C 54.4514 0.0000 1 447 152 155 LEU N N 116.1429 0.0000 1 448 153 156 GLY H H 7.9084 0.0000 1 449 153 156 GLY CA C 46.1800 0.0000 1 450 153 156 GLY N N 108.9670 0.0000 1 451 154 157 VAL H H 8.0180 0.0000 1 452 154 157 VAL C C 178.4339 0.0000 1 453 154 157 VAL N N 121.4244 0.0000 1 454 155 158 GLU H H 8.8185 0.0000 1 455 155 158 GLU C C 178.4486 0.0000 1 456 155 158 GLU N N 129.2941 0.0000 1 457 156 159 PRO CA C 59.5213 0.0000 1 458 156 159 PRO CB C 29.6221 0.0000 1 459 157 160 MET H H 8.4275 0.0000 1 460 157 160 MET CA C 55.5414 0.0000 1 461 157 160 MET N N 123.7128 0.0000 1 462 158 161 ILE H H 9.0621 0.0000 1 463 158 161 ILE CA C 60.5307 0.0000 1 464 158 161 ILE N N 129.3180 0.0000 1 465 159 162 VAL H H 8.0954 0.0000 1 466 159 162 VAL CA C 60.6104 0.0000 1 467 159 162 VAL N N 126.8781 0.0000 1 468 160 163 ASP H H 8.7156 0.0000 1 469 160 163 ASP CA C 52.3637 0.0000 1 470 160 163 ASP N N 126.3773 0.0000 1 471 161 164 PHE H H 9.2932 0.0000 1 472 161 164 PHE CA C 61.8506 0.0000 1 473 161 164 PHE N N 126.1357 0.0000 1 474 162 165 ALA H H 8.3589 0.0000 1 475 162 165 ALA CA C 54.3226 0.0000 1 476 162 165 ALA N N 123.5148 0.0000 1 477 163 166 ALA H H 7.7138 0.0000 1 478 163 166 ALA CA C 52.1101 0.0000 1 479 163 166 ALA N N 119.7690 0.0000 1 480 164 167 MET H H 7.9631 0.0000 1 481 164 167 MET CA C 55.1915 0.0000 1 482 164 167 MET N N 114.3873 0.0000 1 483 165 168 GLU H H 7.6395 0.0000 1 484 165 168 GLU CA C 54.8347 0.0000 1 485 165 168 GLU N N 115.9642 0.0000 1 486 166 169 VAL H H 8.7491 0.0000 1 487 166 169 VAL CA C 63.3068 0.0000 1 488 166 169 VAL N N 123.9386 0.0000 1 489 167 170 VAL H H 8.7322 0.0000 1 490 167 170 VAL CA C 61.4423 0.0000 1 491 167 170 VAL N N 124.6599 0.0000 1 492 168 171 GLY H H 7.9726 0.0000 1 493 168 171 GLY C C 177.9656 0.0000 1 494 168 171 GLY N N 118.8840 0.0000 1 stop_ save_