data_4134 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4134 _Entry.Title ; NMR Assignments for Denatured LysN ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 1998-04-16 _Entry.Accession_date 1998-04-16 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Details ; NMR assignments for the N-terminal anticodon binding domain of lysyl-tRNA synthesase in its denatured form (pH 2.8, 3M urea, 11 oC). The aim of this study is to determine if residual structure is conserved in the denatured states of three proteins (LysN, cold shock protein A [BMRB 4107 & 4108], microccocal nuclease) that share a similar native state OB-fold, in spite of no detectable sequence homology. ; _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 Andrei Alexandrescu . T. . 4134 2 Viktor Jaravine . A. . 4134 3 Francois Lamour . P. . 4134 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 4134 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 219 4134 '15N chemical shifts' 115 4134 '1H chemical shifts' 420 4134 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 1999-06-17 . revision author 'comments added to chemical shift saveframe' 4134 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 4107 'denatured state assignments of a protein belonging to the OB-fold superfamily' 4134 BMRB 4108 'denatured state assignments of a protein belonging to the OB-fold superfamily' 4134 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4134 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Alexandrescu, A. T., Jaravine, Viktor A., and Lamour, F. P., "NMR Assignments for Denatured LysN," ; _Citation.Title 'NMR Assignments for denatured LysN' _Citation.Status 'in preparation' _Citation.Type journal _Citation.Journal_abbrev . _Citation.Journal_name_full . _Citation.Journal_volume . _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first . _Citation.Page_last . _Citation.Year 1999 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Andrei Alexandrescu . T. . 4134 1 2 Viktor Jaravine . A. . 4134 1 3 Francois Lamour . P. . 4134 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'denatured state' 4134 1 'lysyl-tRNA synthetase' 4134 1 OB-fold 4134 1 'protein folding' 4134 1 stop_ save_ save_citation_one _Citation.Sf_category citations _Citation.Sf_framecode citation_one _Citation.Entry_ID 4134 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 8589602 _Citation.Full_citation ; Wishart D. S., Bigam C .G., Yao J., Abildgaard F., Dyson H. J., Oldfield E., Markley J. L., Sykes B. D. , '1H, 13C and 15N chemical shift referencing in biomolecular NMR,' J. Biomol. NMR 6, 135-140 (1995). ; _Citation.Title '1H, 13C and 15N chemical shift referencing in biomolecular NMR.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full 'Journal of biomolecular NMR' _Citation.Journal_volume 6 _Citation.Journal_issue 2 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0925-2738 _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 135 _Citation.Page_last 140 _Citation.Year 1995 _Citation.Details ; A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 'D S' Wishart D. S. . 4134 2 2 'C G' Bigam C. G. . 4134 2 3 J Yao J. . . 4134 2 4 F Abildgaard F. . . 4134 2 5 'H J' Dyson H. J. . 4134 2 6 E Oldfield E. . . 4134 2 7 'J L' Markley J. L. . 4134 2 8 'B D' Sykes B. D. . 4134 2 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_den-LysN _Assembly.Sf_category assembly _Assembly.Sf_framecode system_den-LysN _Assembly.Entry_ID 4134 _Assembly.ID 1 _Assembly.Name den-LysN _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state . _Assembly.Molecular_mass 13526 _Assembly.Enzyme_commission_number 'EC 6.1.1.6' _Assembly.Details ; NMR structures of native LysN ; _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 4134 1 stop_ loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 den-LysN 1 $den-LysN . . . denatured . . . . . 4134 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID den-LysN abbreviation 4134 1 den-LysN system 4134 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'LysN is the N-terminal anticodon binding domain of the lysyl-tRNA synthetase' 4134 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_den-LysN _Entity.Sf_category entity _Entity.Sf_framecode den-LysN _Entity.Entry_ID 4134 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name lysl-tRNA_synthetase _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; AEQGIAFPNDFRRDHTSDQL HAEFDGKENEELEALNIEVA VAGRMMTRRIMGKASFVTLQ DVGGRIQLYVARDDLPEGVY NEQFKKWDLGDILGAKGKLF KTKTGELSIHCTELRLLTKA ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 120 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-24 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no PDB 1BBU . "Lysyl-Trna Synthetase (Lyss) Complexed With Lysine" . . . . . 99.17 504 100.00 100.00 7.17e-77 . . . . 4134 1 2 no PDB 1BBW . "Lysyl-Trna Synthetase (Lyss)" . . . . . 99.17 504 100.00 100.00 7.17e-77 . . . . 4134 1 3 no PDB 1KRS . "Solution Structure Of The Anticodon Binding Domain Of Escherichia Coli Lysyl-Trna Synthetase And Studies Of Its Interactions Wi" . . . . . 100.00 120 100.00 100.00 8.78e-82 . . . . 4134 1 4 no PDB 1KRT . "Solution Structure Of The Anticodon Binding Domain Of Escherichia Coli Lysyl-Trna Synthetase And Studies Of Its Interactions Wi" . . . . . 100.00 120 100.00 100.00 8.78e-82 . . . . 4134 1 5 no DBJ BAB37185 . "lysine tRNA synthetase [Escherichia coli O157:H7 str. Sakai]" . . . . . 99.17 505 100.00 100.00 7.50e-77 . . . . 4134 1 6 no DBJ BAE76955 . "lysine tRNA synthetase, constitutive [Escherichia coli str. K12 substr. W3110]" . . . . . 99.17 505 100.00 100.00 7.03e-77 . . . . 4134 1 7 no DBJ BAG78677 . "lysyl-tRNA synthase [Escherichia coli SE11]" . . . . . 99.17 505 100.00 100.00 7.03e-77 . . . . 4134 1 8 no DBJ BAI27164 . "lysine tRNA synthetase LysS, constitutive [Escherichia coli O26:H11 str. 11368]" . . . . . 99.17 505 99.16 100.00 1.21e-76 . . . . 4134 1 9 no DBJ BAI32202 . "lysine tRNA synthetase LysS, constitutive [Escherichia coli O103:H2 str. 12009]" . . . . . 99.17 505 100.00 100.00 8.00e-77 . . . . 4134 1 10 no EMBL CAP77327 . "Lysyl-tRNA synthetase [Escherichia coli LF82]" . . . . . 99.17 505 100.00 100.00 7.03e-77 . . . . 4134 1 11 no EMBL CAQ33202 . "lysyl tRNA synthetase (LysRSs), constitutive, subunit of lysyl-tRNA synthetase, constitutive [Escherichia coli BL21(DE3)]" . . . . . 99.17 505 100.00 100.00 7.03e-77 . . . . 4134 1 12 no EMBL CAQ90319 . "lysine tRNA synthetase, constitutive [Escherichia fergusonii ATCC 35469]" . . . . . 99.17 505 99.16 100.00 2.68e-76 . . . . 4134 1 13 no EMBL CAQ99824 . "lysine tRNA synthetase, constitutive [Escherichia coli IAI1]" . . . . . 99.17 505 100.00 100.00 8.00e-77 . . . . 4134 1 14 no EMBL CAR04406 . "lysine tRNA synthetase, constitutive [Escherichia coli S88]" . . . . . 99.17 505 100.00 100.00 7.03e-77 . . . . 4134 1 15 no GB AAA23959 . "herC protein [Escherichia coli]" . . . . . 99.17 505 100.00 100.00 7.03e-77 . . . . 4134 1 16 no GB AAA83071 . "lysyl tRNA synthetase (LysRS), constitutive [Escherichia coli]" . . . . . 99.17 505 100.00 100.00 7.03e-77 . . . . 4134 1 17 no GB AAC75928 . "lysine tRNA synthetase, constitutive [Escherichia coli str. K-12 substr. MG1655]" . . . . . 99.17 505 100.00 100.00 7.03e-77 . . . . 4134 1 18 no GB AAG58018 . "lysine tRNA synthetase, constitutive; suppressor of ColE1 mutation in primer RNA [Escherichia coli O157:H7 str. EDL933]" . . . . . 99.17 505 100.00 100.00 7.50e-77 . . . . 4134 1 19 no GB AAN44362 . "lysine tRNA synthetase [Shigella flexneri 2a str. 301]" . . . . . 99.17 505 100.00 100.00 8.00e-77 . . . . 4134 1 20 no REF NP_311789 . "lysyl-tRNA synthetase [Escherichia coli O157:H7 str. Sakai]" . . . . . 99.17 505 100.00 100.00 7.50e-77 . . . . 4134 1 21 no REF NP_417366 . "lysine tRNA synthetase, constitutive [Escherichia coli str. K-12 substr. MG1655]" . . . . . 99.17 505 100.00 100.00 7.03e-77 . . . . 4134 1 22 no REF NP_708655 . "lysyl-tRNA synthetase [Shigella flexneri 2a str. 301]" . . . . . 99.17 505 100.00 100.00 8.00e-77 . . . . 4134 1 23 no REF WP_000003059 . "lysine--tRNA ligase [Escherichia coli]" . . . . . 99.17 505 99.16 99.16 3.87e-75 . . . . 4134 1 24 no REF WP_000003060 . "lysine--tRNA ligase [Escherichia coli]" . . . . . 99.17 505 99.16 100.00 1.25e-76 . . . . 4134 1 25 no SP B2U0Q7 . "RecName: Full=Lysine--tRNA ligase; AltName: Full=Lysyl-tRNA synthetase; Short=LysRS" . . . . . 99.17 505 100.00 100.00 8.00e-77 . . . . 4134 1 26 no SP P0A8N3 . "RecName: Full=Lysine--tRNA ligase; AltName: Full=Lysyl-tRNA synthetase; Short=LysRS" . . . . . 99.17 505 100.00 100.00 7.03e-77 . . . . 4134 1 27 no SP P0A8N4 . "RecName: Full=Lysine--tRNA ligase; AltName: Full=Lysyl-tRNA synthetase; Short=LysRS" . . . . . 99.17 505 100.00 100.00 7.03e-77 . . . . 4134 1 28 no SP Q0T106 . "RecName: Full=Lysine--tRNA ligase; AltName: Full=Lysyl-tRNA synthetase; Short=LysRS" . . . . . 99.17 505 100.00 100.00 8.00e-77 . . . . 4134 1 29 no SP Q31WF2 . "RecName: Full=Lysine--tRNA ligase; AltName: Full=Lysyl-tRNA synthetase; Short=LysRS" . . . . . 99.17 505 99.16 99.16 3.04e-76 . . . . 4134 1 stop_ loop_ _Entity_biological_function.Biological_function _Entity_biological_function.Entry_ID _Entity_biological_function.Entity_ID 'LysN is the N-terminal anticodon binding domain of the lysyl-tRNA synthetase' 4134 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID den-LysN abbreviation 4134 1 lysl-tRNA_synthetase common 4134 1 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 1 ALA . 4134 1 2 31 GLU . 4134 1 3 32 GLN . 4134 1 4 33 GLY . 4134 1 5 34 ILE . 4134 1 6 35 ALA . 4134 1 7 36 PHE . 4134 1 8 37 PRO . 4134 1 9 38 ASN . 4134 1 10 39 ASP . 4134 1 11 40 PHE . 4134 1 12 41 ARG . 4134 1 13 42 ARG . 4134 1 14 43 ASP . 4134 1 15 44 HIS . 4134 1 16 45 THR . 4134 1 17 46 SER . 4134 1 18 47 ASP . 4134 1 19 48 GLN . 4134 1 20 49 LEU . 4134 1 21 50 HIS . 4134 1 22 51 ALA . 4134 1 23 52 GLU . 4134 1 24 53 PHE . 4134 1 25 54 ASP . 4134 1 26 55 GLY . 4134 1 27 56 LYS . 4134 1 28 57 GLU . 4134 1 29 58 ASN . 4134 1 30 59 GLU . 4134 1 31 60 GLU . 4134 1 32 61 LEU . 4134 1 33 62 GLU . 4134 1 34 63 ALA . 4134 1 35 64 LEU . 4134 1 36 65 ASN . 4134 1 37 66 ILE . 4134 1 38 67 GLU . 4134 1 39 68 VAL . 4134 1 40 69 ALA . 4134 1 41 70 VAL . 4134 1 42 71 ALA . 4134 1 43 72 GLY . 4134 1 44 73 ARG . 4134 1 45 74 MET . 4134 1 46 75 MET . 4134 1 47 76 THR . 4134 1 48 77 ARG . 4134 1 49 78 ARG . 4134 1 50 79 ILE . 4134 1 51 80 MET . 4134 1 52 81 GLY . 4134 1 53 82 LYS . 4134 1 54 83 ALA . 4134 1 55 84 SER . 4134 1 56 85 PHE . 4134 1 57 86 VAL . 4134 1 58 87 THR . 4134 1 59 88 LEU . 4134 1 60 89 GLN . 4134 1 61 90 ASP . 4134 1 62 91 VAL . 4134 1 63 92 GLY . 4134 1 64 93 GLY . 4134 1 65 94 ARG . 4134 1 66 95 ILE . 4134 1 67 96 GLN . 4134 1 68 97 LEU . 4134 1 69 98 TYR . 4134 1 70 99 VAL . 4134 1 71 100 ALA . 4134 1 72 101 ARG . 4134 1 73 102 ASP . 4134 1 74 103 ASP . 4134 1 75 104 LEU . 4134 1 76 105 PRO . 4134 1 77 106 GLU . 4134 1 78 107 GLY . 4134 1 79 108 VAL . 4134 1 80 109 TYR . 4134 1 81 110 ASN . 4134 1 82 111 GLU . 4134 1 83 112 GLN . 4134 1 84 113 PHE . 4134 1 85 114 LYS . 4134 1 86 115 LYS . 4134 1 87 116 TRP . 4134 1 88 117 ASP . 4134 1 89 118 LEU . 4134 1 90 119 GLY . 4134 1 91 120 ASP . 4134 1 92 121 ILE . 4134 1 93 122 LEU . 4134 1 94 123 GLY . 4134 1 95 124 ALA . 4134 1 96 125 LYS . 4134 1 97 126 GLY . 4134 1 98 127 LYS . 4134 1 99 128 LEU . 4134 1 100 129 PHE . 4134 1 101 130 LYS . 4134 1 102 131 THR . 4134 1 103 132 LYS . 4134 1 104 133 THR . 4134 1 105 134 GLY . 4134 1 106 135 GLU . 4134 1 107 136 LEU . 4134 1 108 137 SER . 4134 1 109 138 ILE . 4134 1 110 139 HIS . 4134 1 111 140 CYS . 4134 1 112 141 THR . 4134 1 113 142 GLU . 4134 1 114 143 LEU . 4134 1 115 144 ARG . 4134 1 116 145 LEU . 4134 1 117 146 LEU . 4134 1 118 147 THR . 4134 1 119 148 LYS . 4134 1 120 149 ALA . 4134 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . ALA 1 1 4134 1 . GLU 2 2 4134 1 . GLN 3 3 4134 1 . GLY 4 4 4134 1 . ILE 5 5 4134 1 . ALA 6 6 4134 1 . PHE 7 7 4134 1 . PRO 8 8 4134 1 . ASN 9 9 4134 1 . ASP 10 10 4134 1 . PHE 11 11 4134 1 . ARG 12 12 4134 1 . ARG 13 13 4134 1 . ASP 14 14 4134 1 . HIS 15 15 4134 1 . THR 16 16 4134 1 . SER 17 17 4134 1 . ASP 18 18 4134 1 . GLN 19 19 4134 1 . LEU 20 20 4134 1 . HIS 21 21 4134 1 . ALA 22 22 4134 1 . GLU 23 23 4134 1 . PHE 24 24 4134 1 . ASP 25 25 4134 1 . GLY 26 26 4134 1 . LYS 27 27 4134 1 . GLU 28 28 4134 1 . ASN 29 29 4134 1 . GLU 30 30 4134 1 . GLU 31 31 4134 1 . LEU 32 32 4134 1 . GLU 33 33 4134 1 . ALA 34 34 4134 1 . LEU 35 35 4134 1 . ASN 36 36 4134 1 . ILE 37 37 4134 1 . GLU 38 38 4134 1 . VAL 39 39 4134 1 . ALA 40 40 4134 1 . VAL 41 41 4134 1 . ALA 42 42 4134 1 . GLY 43 43 4134 1 . ARG 44 44 4134 1 . MET 45 45 4134 1 . MET 46 46 4134 1 . THR 47 47 4134 1 . ARG 48 48 4134 1 . ARG 49 49 4134 1 . ILE 50 50 4134 1 . MET 51 51 4134 1 . GLY 52 52 4134 1 . LYS 53 53 4134 1 . ALA 54 54 4134 1 . SER 55 55 4134 1 . PHE 56 56 4134 1 . VAL 57 57 4134 1 . THR 58 58 4134 1 . LEU 59 59 4134 1 . GLN 60 60 4134 1 . ASP 61 61 4134 1 . VAL 62 62 4134 1 . GLY 63 63 4134 1 . GLY 64 64 4134 1 . ARG 65 65 4134 1 . ILE 66 66 4134 1 . GLN 67 67 4134 1 . LEU 68 68 4134 1 . TYR 69 69 4134 1 . VAL 70 70 4134 1 . ALA 71 71 4134 1 . ARG 72 72 4134 1 . ASP 73 73 4134 1 . ASP 74 74 4134 1 . LEU 75 75 4134 1 . PRO 76 76 4134 1 . GLU 77 77 4134 1 . GLY 78 78 4134 1 . VAL 79 79 4134 1 . TYR 80 80 4134 1 . ASN 81 81 4134 1 . GLU 82 82 4134 1 . GLN 83 83 4134 1 . PHE 84 84 4134 1 . LYS 85 85 4134 1 . LYS 86 86 4134 1 . TRP 87 87 4134 1 . ASP 88 88 4134 1 . LEU 89 89 4134 1 . GLY 90 90 4134 1 . ASP 91 91 4134 1 . ILE 92 92 4134 1 . LEU 93 93 4134 1 . GLY 94 94 4134 1 . ALA 95 95 4134 1 . LYS 96 96 4134 1 . GLY 97 97 4134 1 . LYS 98 98 4134 1 . LEU 99 99 4134 1 . PHE 100 100 4134 1 . LYS 101 101 4134 1 . THR 102 102 4134 1 . LYS 103 103 4134 1 . THR 104 104 4134 1 . GLY 105 105 4134 1 . GLU 106 106 4134 1 . LEU 107 107 4134 1 . SER 108 108 4134 1 . ILE 109 109 4134 1 . HIS 110 110 4134 1 . CYS 111 111 4134 1 . THR 112 112 4134 1 . GLU 113 113 4134 1 . LEU 114 114 4134 1 . ARG 115 115 4134 1 . LEU 116 116 4134 1 . LEU 117 117 4134 1 . THR 118 118 4134 1 . LYS 119 119 4134 1 . ALA 120 120 4134 1 stop_ save_ #################### # Natural source # #################### save_natural_source _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source _Entity_natural_src_list.Entry_ID 4134 _Entity_natural_src_list.ID 1 loop_ _Entity_natural_src.ID _Entity_natural_src.Entity_ID _Entity_natural_src.Entity_label _Entity_natural_src.Entity_chimera_segment_ID _Entity_natural_src.NCBI_taxonomy_ID _Entity_natural_src.Type _Entity_natural_src.Common _Entity_natural_src.Organism_name_scientific _Entity_natural_src.Organism_name_common _Entity_natural_src.Organism_acronym _Entity_natural_src.ICTVdb_decimal_code _Entity_natural_src.Superkingdom _Entity_natural_src.Kingdom _Entity_natural_src.Genus _Entity_natural_src.Species _Entity_natural_src.Strain _Entity_natural_src.Variant _Entity_natural_src.Subvariant _Entity_natural_src.Organ _Entity_natural_src.Tissue _Entity_natural_src.Tissue_fraction _Entity_natural_src.Cell_line _Entity_natural_src.Cell_type _Entity_natural_src.ATCC_number _Entity_natural_src.Organelle _Entity_natural_src.Cellular_location _Entity_natural_src.Fragment _Entity_natural_src.Fraction _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Plasmid_details _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Dev_stage _Entity_natural_src.Details _Entity_natural_src.Citation_ID _Entity_natural_src.Citation_label _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $den-LysN . 562 organism . 'Escherichia coli' 'E. coli' . . Eubacteria . Escherichia coli . K12 . . . . . . . . . . . . . . . . ; Commans, S.; Plateau,P.; Blanquet, S.; Dardel, F. (1995) "Solution structure of the anticodon-binding domain of Escherichia coli Lysyl-tRNA synthetase and studies of its interaction with tRNALys" J. Mol. Biol. 253:100-113. ; . . 4134 1 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Entity_experimental_src_list.Sf_category experimental_source _Entity_experimental_src_list.Sf_framecode experimental_source _Entity_experimental_src_list.Entry_ID 4134 _Entity_experimental_src_list.ID 1 loop_ _Entity_experimental_src.ID _Entity_experimental_src.Entity_ID _Entity_experimental_src.Entity_label _Entity_experimental_src.Entity_chimera_segment_ID _Entity_experimental_src.Production_method _Entity_experimental_src.Host_org_scientific_name _Entity_experimental_src.Host_org_name_common _Entity_experimental_src.Host_org_details _Entity_experimental_src.Host_org_NCBI_taxonomy_ID _Entity_experimental_src.Host_org_genus _Entity_experimental_src.Host_org_species _Entity_experimental_src.Host_org_strain _Entity_experimental_src.Host_org_variant _Entity_experimental_src.Host_org_subvariant _Entity_experimental_src.Host_org_organ _Entity_experimental_src.Host_org_tissue _Entity_experimental_src.Host_org_tissue_fraction _Entity_experimental_src.Host_org_cell_line _Entity_experimental_src.Host_org_cell_type _Entity_experimental_src.Host_org_cellular_location _Entity_experimental_src.Host_org_organelle _Entity_experimental_src.Host_org_gene _Entity_experimental_src.Host_org_culture_collection _Entity_experimental_src.Host_org_ATCC_number _Entity_experimental_src.Vector_type _Entity_experimental_src.PDBview_host_org_vector_name _Entity_experimental_src.PDBview_plasmid_name _Entity_experimental_src.Vector_name _Entity_experimental_src.Vector_details _Entity_experimental_src.Vendor_name _Entity_experimental_src.Host_org_dev_stage _Entity_experimental_src.Details _Entity_experimental_src.Citation_ID _Entity_experimental_src.Citation_label _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $den-LysN . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli . . . . . . . . . . . . . plasmid . . pET28a . Novagen . ; natural (A 374 bp NcoI-BamHI fragment of the pTRc-N? plasmid [Commans, S., Plateau,P., Blanquet, S., Dardel, F. (1995) "Solution structure of the anticodon-binding domain of Escherichia coli Lysyl-tRNA synthetase and studies of its interaction with tRNALys" J. Mol. Biol. 253:100-113.], encoding the gene for LysN was transferred into the NcoI-BamHI sites of the pET28a vector (Novagen) to yield the plasmid pFLI-N. E. coli strain BL21(DE3)pLysS (Novagen) was used for expression) ; . . 4134 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Sample.Sf_category sample _Sample.Sf_framecode sample_one _Sample.Entry_ID 4134 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 lysl-tRNA_synthetase '[U-15N; U-13C]' . . 1 $den-LysN . . 1.5 . . mM . . . . 4134 1 2 urea . . . . . . . 3 . . M . . . . 4134 1 3 H2O . . . . . . . 90 . . % . . . . 4134 1 4 D2O . . . . . . . 10 . . % . . . . 4134 1 stop_ save_ save_sample_two _Sample.Sf_category sample _Sample.Sf_framecode sample_two _Sample.Entry_ID 4134 _Sample.ID 2 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 lysl-tRNA_synthetase [U-15N] . . 1 $den-LysN . . 1 . . mM . . . . 4134 2 2 urea . . . . . . . 3 . . M . . . . 4134 2 3 H2O . . . . . . . 90 . . % . . . . 4134 2 4 D2O . . . . . . . 10 . . % . . . . 4134 2 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_one _Sample_condition_list.Entry_ID 4134 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pH 2.8 . na 4134 1 pressure 1 . atm 4134 1 temperature 284 . K 4134 1 stop_ save_ ############################# # Purity of the molecules # ############################# save_molecule_purity_list _Entity_purity_list.Sf_category molecule_purity _Entity_purity_list.Sf_framecode molecule_purity_list _Entity_purity_list.Entry_ID 4134 _Entity_purity_list.ID 1 _Entity_purity_list.Details . loop_ _Entity_purity.ID _Entity_purity.Sample_ID _Entity_purity.Sample_label _Entity_purity.Entity_ID _Entity_purity.Entity_label _Entity_purity.Val _Entity_purity.Val_units _Entity_purity.Measurement_method _Entity_purity.Details _Entity_purity.Entry_ID _Entity_purity.Entity_purity_list_ID 1 1 $sample_one 1 $den-LysN 95 % SDS-PAGE . 4134 1 2 2 $sample_two 1 $den-LysN 95 % SDS-PAGE . 4134 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_one _NMR_spectrometer.Entry_ID 4134 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DRX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_NMR_spectrometer_two _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_two _NMR_spectrometer.Entry_ID 4134 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model 'Unity plus' _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 4134 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 NMR_spectrometer_one Bruker DRX . 600 . . . 4134 1 2 NMR_spectrometer_two Varian 'Unity plus' . 600 . . . 4134 1 stop_ save_ ############################# # NMR applied experiments # ############################# save_experiment_list _Experiment_list.Sf_category experiment_list _Experiment_list.Sf_framecode experiment_list _Experiment_list.Entry_ID 4134 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 'NMR spectral acquisition parameters' . . . . . . . . . . . 2 $sample_two . . . 1 $sample_conditions_one . . . . . . . . . . . . . . . . . . . . . 4134 1 2 't3 H 599.9094119 146ms . 7000Hz No 1024 complex .' . . . . . . . . . . . 2 $sample_two . . . 1 $sample_conditions_one . . . . . . . . . . . . . . . . . . . . . 4134 1 3 't2 C 150.8529083 7.7ms . 8300Hz No 64 complex .' . . . . . . . . . . . 2 $sample_two . . . 1 $sample_conditions_one . . . . . . . . . . . . . . . . . . . . . 4134 1 4 't1 N 60.7952139 21ms . 1540Hz No 32 complex .' . . . . . . . . . . . 2 $sample_two . . . 1 $sample_conditions_one . . . . . . . . . . . . . . . . . . . . . 4134 1 5 'NMR spectral processing parameters' . . . . . . . . . . . 2 $sample_two . . . 1 $sample_conditions_one . . . . . . . . . . . . . . . . . . . . . 4134 1 6 'D1 H sine-bell 1024 90 Zero-fill 2048' . . . . . . . . . . . 2 $sample_two . . . 1 $sample_conditions_one . . . . . . . . . . . . . . . . . . . . . 4134 1 7 'D2 C squared-sine-bell 64 70 Zero-fill 128' . . . . . . . . . . . 2 $sample_two . . . 1 $sample_conditions_one . . . . . . . . . . . . . . . . . . . . . 4134 1 8 'D3 N linear predict 32 to 48 squaredsine-bell 48 70 Zero-fill 64' . . . . . . . . . . . 2 $sample_two . . . 1 $sample_conditions_one . . . . . . . . . . . . . . . . . . . . . 4134 1 9 '46 ms mix time' . . . . . . . . . . . 1 $sample_one . . . 1 $sample_conditions_one . . . . . . . . . . . . . . . . . . . . . 4134 1 10 'NMR spectral acquisition parameters' . . . . . . . . . . . 1 $sample_one . . . 1 $sample_conditions_one . . . . . . . . . . . . . . . . . . . . . 4134 1 11 't3 H 600.1328206MHz 85ms 46ms 6009.615Hz No 512 complex .' . . . . . . . . . . . 1 $sample_one . . . 1 $sample_conditions_one . . . . . . . . . . . . . . . . . . . . . 4134 1 12 't2 N 60.8178387MHz 21ms . 1521Hz No 32 complex .' . . . . . . . . . . . 1 $sample_one . . . 1 $sample_conditions_one . . . . . . . . . . . . . . . . . . . . . 4134 1 13 't1 H 600.1328206MHz 21ms . 6009.615Hz No 128 complex .' . . . . . . . . . . . 1 $sample_one . . . 1 $sample_conditions_one . . . . . . . . . . . . . . . . . . . . . 4134 1 14 'NMR spectral processing parameters' . . . . . . . . . . . 1 $sample_one . . . 1 $sample_conditions_one . . . . . . . . . . . . . . . . . . . . . 4134 1 15 '3D [1H-15N] TOCSY-HSQC' . . . . . . . . . . . 1 $sample_one . . . 1 $sample_conditions_one . . . . . . . . . . . . . . . . . . . . . 4134 1 16 'D1 H gm -10 0.1 Zero-fill 1024' . . . . . . . . . . . 1 $sample_one . . . 1 $sample_conditions_one . . . . . . . . . . . . . . . . . . . . . 4134 1 17 'D2 N lpl 32 to 48 gm -13 0.1 Zero-fill 64' . . . . . . . . . . . 1 $sample_one . . . 1 $sample_conditions_one . . . . . . . . . . . . . . . . . . . . . 4134 1 18 'D3 H gm -13 0.1 zf 256' . . . . . . . . . . . 1 $sample_one . . . 1 $sample_conditions_one . . . . . . . . . . . . . . . . . . . . . 4134 1 19 '200 ms mix time' . . . . . . . . . . . 1 $sample_one . . . 1 $sample_conditions_one . . . . . . . . . . . . . . . . . . . . . 4134 1 20 't3 H 599.9094183MHz 146ms 200ms 7000Hz No 1024 complex .' . . . . . . . . . . . 1 $sample_one . . . 1 $sample_conditions_one . . . . . . . . . . . . . . . . . . . . . 4134 1 21 't2 H 599.9094183MHz 18ms . 7000Hz No 128 complex .' . . . . . . . . . . . 1 $sample_one . . . 1 $sample_conditions_one . . . . . . . . . . . . . . . . . . . . . 4134 1 22 't1 N 60.7951139MHz 21ms . 1540Hz No 32 complex .' . . . . . . . . . . . 1 $sample_one . . . 1 $sample_conditions_one . . . . . . . . . . . . . . . . . . . . . 4134 1 23 '3D [1H-15N] NOESY-HSQC' . . . . . . . . . . . 1 $sample_one . . . 1 $sample_conditions_one . . . . . . . . . . . . . . . . . . . . . 4134 1 24 'D1 H gm -5 0.1 Zero-fill 2048' . . . . . . . . . . . 1 $sample_one . . . 1 $sample_conditions_one . . . . . . . . . . . . . . . . . . . . . 4134 1 25 'D2 H gm -7 0.1 Zero-fill 256' . . . . . . . . . . . 1 $sample_one . . . 1 $sample_conditions_one . . . . . . . . . . . . . . . . . . . . . 4134 1 26 'D3 N lpl 32 to 48 gm -15 0.1 Zero-fill 64' . . . . . . . . . . . 1 $sample_one . . . 1 $sample_conditions_one . . . . . . . . . . . . . . . . . . . . . 4134 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference_one _Chem_shift_reference.Entry_ID 4134 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID C 13 DSS 'methyl protons' . . . . ppm 0.000 . indirect 0.251449530 . . . 2 $citation_one . . . . 4134 1 H 1 DSS 'methyl protons' . . . . ppm 0.000 . direct . . . . 2 $citation_one . . . . 4134 1 N 15 DSS 'methyl protons' . . . . ppm 0.000 . indirect 0.101329118 . . . 2 $citation_one . . . . 4134 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_one _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chemical_shifts_one _Assigned_chem_shift_list.Entry_ID 4134 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_one _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference_one _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details ; The first 30 residues of the LysS lysyl-tRNA synthetase are missing in LysN, and the construct contains an extra N-terminal Ala (Commans et al., 1995). For consistency with the numbering scheme for LysN of Commans et al (1995), an increment of 29 should be added to the sequence position counter (e.g the second residue in the LysN sequence corresponds to Glu 31, the last residue in the sequence corresponds to Ala149 of the LysS lysyl-tRNA synthetase). Could not distinguish between the spin systems of E60 and Q112, and between L136 and L146. The HA assigned to T45 and S84 could be due to only one of the spin systems. The HA assigned to T45 and S84 could be due to only one of the spin systems. The CB assigned to H44 and H50 could be due to only one of the spin systems. The HA and HB2 assigned to N65 and D103 could be due to only one of the spin systems. Estimates of the uncertainties in reported chemical shifts are: 1HN +/- 0.01 ppm 1Hx +/- 0.03 ppm 13C +/- 0.2 ppm 15N +/- 0.05 ppm ; _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID . . 1 $sample_one . 4134 1 . . 2 $sample_two . 4134 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 1 1 ALA HA H 1 4.14 0.03 . 1 . . . . . . . . 4134 1 2 . 1 1 1 1 ALA CA C 13 51.9 0.2 . 1 . . . . . . . . 4134 1 3 . 1 1 1 1 ALA CB C 13 19.6 0.2 . 1 . . . . . . . . 4134 1 4 . 1 1 2 2 GLU H H 1 8.78 0.01 . 1 . . . . . . . . 4134 1 5 . 1 1 2 2 GLU HA H 1 4.39 0.03 . 1 . . . . . . . . 4134 1 6 . 1 1 2 2 GLU HB2 H 1 2.04 0.03 . 2 . . . . . . . . 4134 1 7 . 1 1 2 2 GLU CA C 13 55.7 0.2 . 1 . . . . . . . . 4134 1 8 . 1 1 2 2 GLU CB C 13 29.1 0.2 . 1 . . . . . . . . 4134 1 9 . 1 1 2 2 GLU N N 15 120.28 0.05 . 1 . . . . . . . . 4134 1 10 . 1 1 3 3 GLN H H 1 8.7 0.01 . 1 . . . . . . . . 4134 1 11 . 1 1 3 3 GLN HA H 1 4.39 0.03 . 1 . . . . . . . . 4134 1 12 . 1 1 3 3 GLN CA C 13 55.7 0.2 . 1 . . . . . . . . 4134 1 13 . 1 1 3 3 GLN CB C 13 29.9 0.2 . 1 . . . . . . . . 4134 1 14 . 1 1 3 3 GLN N N 15 122.64 0.05 . 1 . . . . . . . . 4134 1 15 . 1 1 4 4 GLY H H 1 8.55 0.01 . 1 . . . . . . . . 4134 1 16 . 1 1 4 4 GLY HA2 H 1 4 0.03 . 2 . . . . . . . . 4134 1 17 . 1 1 4 4 GLY CA C 13 45.4 0.2 . 1 . . . . . . . . 4134 1 18 . 1 1 4 4 GLY N N 15 110.62 0.05 . 1 . . . . . . . . 4134 1 19 . 1 1 5 5 ILE H H 1 8.03 0.01 . 1 . . . . . . . . 4134 1 20 . 1 1 5 5 ILE HA H 1 4.15 0.03 . 1 . . . . . . . . 4134 1 21 . 1 1 5 5 ILE CA C 13 60.9 0.2 . 1 . . . . . . . . 4134 1 22 . 1 1 5 5 ILE CB C 13 39 0.2 . 1 . . . . . . . . 4134 1 23 . 1 1 5 5 ILE N N 15 120.08 0.05 . 1 . . . . . . . . 4134 1 24 . 1 1 6 6 ALA H H 1 8.35 0.01 . 1 . . . . . . . . 4134 1 25 . 1 1 6 6 ALA HA H 1 4.31 0.03 . 1 . . . . . . . . 4134 1 26 . 1 1 6 6 ALA HB1 H 1 1.26 0.03 . 1 . . . . . . . . 4134 1 27 . 1 1 6 6 ALA HB2 H 1 1.26 0.03 . 1 . . . . . . . . 4134 1 28 . 1 1 6 6 ALA HB3 H 1 1.26 0.03 . 1 . . . . . . . . 4134 1 29 . 1 1 6 6 ALA CA C 13 52.3 0.2 . 1 . . . . . . . . 4134 1 30 . 1 1 6 6 ALA CB C 13 19.6 0.2 . 1 . . . . . . . . 4134 1 31 . 1 1 6 6 ALA N N 15 128.12 0.05 . 1 . . . . . . . . 4134 1 32 . 1 1 7 7 PHE H H 1 8.28 0.01 . 1 . . . . . . . . 4134 1 33 . 1 1 7 7 PHE HA H 1 4.86 0.03 . 1 . . . . . . . . 4134 1 34 . 1 1 7 7 PHE HB2 H 1 2.9 0.03 . 2 . . . . . . . . 4134 1 35 . 1 1 7 7 PHE HB3 H 1 3.14 0.03 . 2 . . . . . . . . 4134 1 36 . 1 1 7 7 PHE CA C 13 55.7 0.2 . 1 . . . . . . . . 4134 1 37 . 1 1 7 7 PHE CB C 13 39 0.2 . 1 . . . . . . . . 4134 1 38 . 1 1 7 7 PHE N N 15 120.32 0.05 . 1 . . . . . . . . 4134 1 39 . 1 1 8 8 PRO HA H 1 4.37 0.03 . 1 . . . . . . . . 4134 1 40 . 1 1 8 8 PRO CA C 13 63.5 0.2 . 1 . . . . . . . . 4134 1 41 . 1 1 8 8 PRO CB C 13 32.1 0.2 . 1 . . . . . . . . 4134 1 42 . 1 1 9 9 ASN H H 1 8.59 0.01 . 1 . . . . . . . . 4134 1 43 . 1 1 9 9 ASN HA H 1 4.62 0.03 . 1 . . . . . . . . 4134 1 44 . 1 1 9 9 ASN HB2 H 1 2.75 0.03 . 2 . . . . . . . . 4134 1 45 . 1 1 9 9 ASN CA C 13 53.6 0.2 . 1 . . . . . . . . 4134 1 46 . 1 1 9 9 ASN CB C 13 38.5 0.2 . 1 . . . . . . . . 4134 1 47 . 1 1 9 9 ASN N N 15 118.53 0.05 . 1 . . . . . . . . 4134 1 48 . 1 1 10 10 ASP H H 1 8.37 0.01 . 1 . . . . . . . . 4134 1 49 . 1 1 10 10 ASP HA H 1 4.7 0.03 . 1 . . . . . . . . 4134 1 50 . 1 1 10 10 ASP HB2 H 1 2.82 0.03 . 2 . . . . . . . . 4134 1 51 . 1 1 10 10 ASP CA C 13 53.2 0.2 . 1 . . . . . . . . 4134 1 52 . 1 1 10 10 ASP CB C 13 38.1 0.2 . 1 . . . . . . . . 4134 1 53 . 1 1 10 10 ASP N N 15 119.09 0.05 . 1 . . . . . . . . 4134 1 54 . 1 1 11 11 PHE H H 1 8.16 0.01 . 1 . . . . . . . . 4134 1 55 . 1 1 11 11 PHE HA H 1 4.54 0.03 . 1 . . . . . . . . 4134 1 56 . 1 1 11 11 PHE HB2 H 1 3.14 0.03 . 2 . . . . . . . . 4134 1 57 . 1 1 11 11 PHE CB C 13 39.4 0.2 . 1 . . . . . . . . 4134 1 58 . 1 1 11 11 PHE N N 15 120.81 0.05 . 1 . . . . . . . . 4134 1 59 . 1 1 12 12 ARG H H 1 8.27 0.01 . 1 . . . . . . . . 4134 1 60 . 1 1 12 12 ARG HA H 1 4.25 0.03 . 1 . . . . . . . . 4134 1 61 . 1 1 12 12 ARG HB2 H 1 1.72 0.03 . 4 . . . . . . . . 4134 1 62 . 1 1 12 12 ARG HB3 H 1 1.55 0.03 . 4 . . . . . . . . 4134 1 63 . 1 1 12 12 ARG HG2 H 1 1.72 0.03 . 4 . . . . . . . . 4134 1 64 . 1 1 12 12 ARG HG3 H 1 1.55 0.03 . 4 . . . . . . . . 4134 1 65 . 1 1 12 12 ARG CA C 13 56.2 0.2 . 1 . . . . . . . . 4134 1 66 . 1 1 12 12 ARG CB C 13 30.8 0.2 . 1 . . . . . . . . 4134 1 67 . 1 1 12 12 ARG N N 15 122.56 0.05 . 1 . . . . . . . . 4134 1 68 . 1 1 13 13 ARG H H 1 8.33 0.01 . 1 . . . . . . . . 4134 1 69 . 1 1 13 13 ARG HA H 1 4.23 0.03 . 1 . . . . . . . . 4134 1 70 . 1 1 13 13 ARG HB2 H 1 1.81 0.03 . 4 . . . . . . . . 4134 1 71 . 1 1 13 13 ARG HB3 H 1 1.73 0.03 . 4 . . . . . . . . 4134 1 72 . 1 1 13 13 ARG HG2 H 1 1.81 0.03 . 4 . . . . . . . . 4134 1 73 . 1 1 13 13 ARG HG3 H 1 1.73 0.03 . 4 . . . . . . . . 4134 1 74 . 1 1 13 13 ARG HD2 H 1 3.29 0.03 . 2 . . . . . . . . 4134 1 75 . 1 1 13 13 ARG CA C 13 56.2 0.2 . 1 . . . . . . . . 4134 1 76 . 1 1 13 13 ARG CB C 13 30.8 0.2 . 1 . . . . . . . . 4134 1 77 . 1 1 13 13 ARG N N 15 121.91 0.05 . 1 . . . . . . . . 4134 1 78 . 1 1 14 14 ASP H H 1 8.49 0.01 . 1 . . . . . . . . 4134 1 79 . 1 1 14 14 ASP HA H 1 4.7 0.03 . 1 . . . . . . . . 4134 1 80 . 1 1 14 14 ASP HB2 H 1 2.82 0.03 . 2 . . . . . . . . 4134 1 81 . 1 1 14 14 ASP CA C 13 53.2 0.2 . 1 . . . . . . . . 4134 1 82 . 1 1 14 14 ASP CB C 13 38.1 0.2 . 1 . . . . . . . . 4134 1 83 . 1 1 14 14 ASP N N 15 119.8 0.05 . 1 . . . . . . . . 4134 1 84 . 1 1 15 15 HIS H H 1 8.58 0.01 . 1 . . . . . . . . 4134 1 85 . 1 1 15 15 HIS HA H 1 4.78 0.03 . 1 . . . . . . . . 4134 1 86 . 1 1 15 15 HIS HB2 H 1 3.21 0.03 . 2 . . . . . . . . 4134 1 87 . 1 1 15 15 HIS CA C 13 55.3 0.2 . 1 . . . . . . . . 4134 1 88 . 1 1 15 15 HIS CB C 13 29.1 0.2 . 5 . . . . . . . . 4134 1 89 . 1 1 15 15 HIS N N 15 119.12 0.05 . 1 . . . . . . . . 4134 1 90 . 1 1 16 16 THR H H 1 8.3 0.01 . 1 . . . . . . . . 4134 1 91 . 1 1 16 16 THR HA H 1 4.38 0.03 . 5 . . . . . . . . 4134 1 92 . 1 1 16 16 THR HG21 H 1 1.22 0.03 . 1 . . . . . . . . 4134 1 93 . 1 1 16 16 THR HG22 H 1 1.22 0.03 . 1 . . . . . . . . 4134 1 94 . 1 1 16 16 THR HG23 H 1 1.22 0.03 . 1 . . . . . . . . 4134 1 95 . 1 1 16 16 THR CA C 13 61.7 0.2 . 1 . . . . . . . . 4134 1 96 . 1 1 16 16 THR CB C 13 69.9 0.2 . 1 . . . . . . . . 4134 1 97 . 1 1 16 16 THR N N 15 115.62 0.05 . 1 . . . . . . . . 4134 1 98 . 1 1 17 17 SER H H 1 8.54 0.01 . 1 . . . . . . . . 4134 1 99 . 1 1 17 17 SER HA H 1 4.47 0.03 . 1 . . . . . . . . 4134 1 100 . 1 1 17 17 SER HB2 H 1 3.92 0.03 . 2 . . . . . . . . 4134 1 101 . 1 1 17 17 SER CA C 13 58.3 0.2 . 1 . . . . . . . . 4134 1 102 . 1 1 17 17 SER CB C 13 63.9 0.2 . 1 . . . . . . . . 4134 1 103 . 1 1 17 17 SER N N 15 117.97 0.05 . 1 . . . . . . . . 4134 1 104 . 1 1 18 18 ASP H H 1 8.61 0.01 . 1 . . . . . . . . 4134 1 105 . 1 1 18 18 ASP HA H 1 4.7 0.03 . 1 . . . . . . . . 4134 1 106 . 1 1 18 18 ASP HB2 H 1 2.9 0.03 . 2 . . . . . . . . 4134 1 107 . 1 1 18 18 ASP CA C 13 53.2 0.2 . 1 . . . . . . . . 4134 1 108 . 1 1 18 18 ASP CB C 13 38.1 0.2 . 1 . . . . . . . . 4134 1 109 . 1 1 18 18 ASP N N 15 121.49 0.05 . 1 . . . . . . . . 4134 1 110 . 1 1 19 19 GLN H H 1 8.39 0.01 . 1 . . . . . . . . 4134 1 111 . 1 1 19 19 GLN HA H 1 4.31 0.03 . 1 . . . . . . . . 4134 1 112 . 1 1 19 19 GLN HB2 H 1 2.04 0.03 . 2 . . . . . . . . 4134 1 113 . 1 1 19 19 GLN HG2 H 1 2.45 0.03 . 2 . . . . . . . . 4134 1 114 . 1 1 19 19 GLN CB C 13 29.5 0.2 . 1 . . . . . . . . 4134 1 115 . 1 1 19 19 GLN N N 15 120.79 0.05 . 1 . . . . . . . . 4134 1 116 . 1 1 20 20 LEU H H 1 8.27 0.01 . 1 . . . . . . . . 4134 1 117 . 1 1 20 20 LEU HA H 1 4.3 0.03 . 1 . . . . . . . . 4134 1 118 . 1 1 20 20 LEU HB2 H 1 1.55 0.03 . 4 . . . . . . . . 4134 1 119 . 1 1 20 20 LEU HB3 H 1 1.55 0.03 . 4 . . . . . . . . 4134 1 120 . 1 1 20 20 LEU HG H 1 1.55 0.03 . 4 . . . . . . . . 4134 1 121 . 1 1 20 20 LEU HD11 H 1 0.9 0.03 . 2 . . . . . . . . 4134 1 122 . 1 1 20 20 LEU HD12 H 1 0.9 0.03 . 2 . . . . . . . . 4134 1 123 . 1 1 20 20 LEU HD13 H 1 0.9 0.03 . 2 . . . . . . . . 4134 1 124 . 1 1 20 20 LEU CA C 13 55.7 0.2 . 1 . . . . . . . . 4134 1 125 . 1 1 20 20 LEU CB C 13 42.4 0.2 . 1 . . . . . . . . 4134 1 126 . 1 1 20 20 LEU N N 15 123.05 0.05 . 1 . . . . . . . . 4134 1 127 . 1 1 21 21 HIS H H 1 8.57 0.01 . 1 . . . . . . . . 4134 1 128 . 1 1 21 21 HIS HA H 1 4.7 0.03 . 1 . . . . . . . . 4134 1 129 . 1 1 21 21 HIS HB2 H 1 3.21 0.03 . 2 . . . . . . . . 4134 1 130 . 1 1 21 21 HIS CA C 13 55.3 0.2 . 1 . . . . . . . . 4134 1 131 . 1 1 21 21 HIS CB C 13 29.1 0.2 . 5 . . . . . . . . 4134 1 132 . 1 1 21 21 HIS N N 15 119.05 0.05 . 1 . . . . . . . . 4134 1 133 . 1 1 22 22 ALA H H 1 8.41 0.01 . 1 . . . . . . . . 4134 1 134 . 1 1 22 22 ALA HA H 1 4.31 0.03 . 1 . . . . . . . . 4134 1 135 . 1 1 22 22 ALA HB1 H 1 1.34 0.03 . 1 . . . . . . . . 4134 1 136 . 1 1 22 22 ALA HB2 H 1 1.34 0.03 . 1 . . . . . . . . 4134 1 137 . 1 1 22 22 ALA HB3 H 1 1.34 0.03 . 1 . . . . . . . . 4134 1 138 . 1 1 22 22 ALA CA C 13 52.7 0.2 . 1 . . . . . . . . 4134 1 139 . 1 1 22 22 ALA CB C 13 19.6 0.2 . 1 . . . . . . . . 4134 1 140 . 1 1 22 22 ALA N N 15 125.22 0.05 . 1 . . . . . . . . 4134 1 141 . 1 1 23 23 GLU H H 1 8.42 0.01 . 1 . . . . . . . . 4134 1 142 . 1 1 23 23 GLU HA H 1 4.31 0.03 . 1 . . . . . . . . 4134 1 143 . 1 1 23 23 GLU HB2 H 1 1.96 0.03 . 2 . . . . . . . . 4134 1 144 . 1 1 23 23 GLU CA C 13 55.7 0.2 . 1 . . . . . . . . 4134 1 145 . 1 1 23 23 GLU CB C 13 29.1 0.2 . 1 . . . . . . . . 4134 1 146 . 1 1 23 23 GLU N N 15 119.98 0.05 . 1 . . . . . . . . 4134 1 147 . 1 1 24 24 PHE H H 1 8.47 0.01 . 1 . . . . . . . . 4134 1 148 . 1 1 24 24 PHE HA H 1 4.7 0.03 . 1 . . . . . . . . 4134 1 149 . 1 1 24 24 PHE HB2 H 1 3.06 0.03 . 2 . . . . . . . . 4134 1 150 . 1 1 24 24 PHE CA C 13 57.9 0.2 . 1 . . . . . . . . 4134 1 151 . 1 1 24 24 PHE CB C 13 39.8 0.2 . 1 . . . . . . . . 4134 1 152 . 1 1 24 24 PHE N N 15 121.67 0.05 . 1 . . . . . . . . 4134 1 153 . 1 1 25 25 ASP H H 1 8.52 0.01 . 1 . . . . . . . . 4134 1 154 . 1 1 25 25 ASP HA H 1 4.7 0.03 . 1 . . . . . . . . 4134 1 155 . 1 1 25 25 ASP HB2 H 1 2.9 0.03 . 2 . . . . . . . . 4134 1 156 . 1 1 25 25 ASP CA C 13 52.7 0.2 . 1 . . . . . . . . 4134 1 157 . 1 1 25 25 ASP CB C 13 38.1 0.2 . 1 . . . . . . . . 4134 1 158 . 1 1 25 25 ASP N N 15 121.89 0.05 . 1 . . . . . . . . 4134 1 159 . 1 1 26 26 GLY H H 1 7.8 0.01 . 1 . . . . . . . . 4134 1 160 . 1 1 26 26 GLY HA2 H 1 3.92 0.03 . 2 . . . . . . . . 4134 1 161 . 1 1 26 26 GLY CA C 13 45.8 0.2 . 1 . . . . . . . . 4134 1 162 . 1 1 26 26 GLY N N 15 108.63 0.05 . 1 . . . . . . . . 4134 1 163 . 1 1 27 27 LYS H H 1 8.14 0.01 . 1 . . . . . . . . 4134 1 164 . 1 1 27 27 LYS HA H 1 4.31 0.03 . 1 . . . . . . . . 4134 1 165 . 1 1 27 27 LYS HB2 H 1 1.86 0.03 . 2 . . . . . . . . 4134 1 166 . 1 1 27 27 LYS HB3 H 1 1.63 0.03 . 2 . . . . . . . . 4134 1 167 . 1 1 27 27 LYS HG2 H 1 1.4 0.03 . 2 . . . . . . . . 4134 1 168 . 1 1 27 27 LYS CA C 13 56.6 0.2 . 1 . . . . . . . . 4134 1 169 . 1 1 27 27 LYS CB C 13 32.9 0.2 . 1 . . . . . . . . 4134 1 170 . 1 1 27 27 LYS N N 15 120.58 0.05 . 1 . . . . . . . . 4134 1 171 . 1 1 28 28 GLU H H 1 8.45 0.01 . 1 . . . . . . . . 4134 1 172 . 1 1 28 28 GLU HA H 1 4.31 0.03 . 1 . . . . . . . . 4134 1 173 . 1 1 28 28 GLU HB2 H 1 2.04 0.03 . 2 . . . . . . . . 4134 1 174 . 1 1 28 28 GLU HG2 H 1 2.45 0.03 . 2 . . . . . . . . 4134 1 175 . 1 1 28 28 GLU CA C 13 56.2 0.2 . 1 . . . . . . . . 4134 1 176 . 1 1 28 28 GLU CB C 13 28.6 0.2 . 1 . . . . . . . . 4134 1 177 . 1 1 28 28 GLU N N 15 121.02 0.05 . 1 . . . . . . . . 4134 1 178 . 1 1 29 29 ASN H H 1 8.55 0.01 . 1 . . . . . . . . 4134 1 179 . 1 1 29 29 ASN HA H 1 4.7 0.03 . 1 . . . . . . . . 4134 1 180 . 1 1 29 29 ASN HB2 H 1 2.82 0.03 . 2 . . . . . . . . 4134 1 181 . 1 1 29 29 ASN CA C 13 53.6 0.2 . 1 . . . . . . . . 4134 1 182 . 1 1 29 29 ASN CB C 13 38.5 0.2 . 1 . . . . . . . . 4134 1 183 . 1 1 29 29 ASN N N 15 119.88 0.05 . 1 . . . . . . . . 4134 1 184 . 1 1 30 30 GLU H H 1 8.44 0.01 . 1 . . . . . . . . 4134 1 185 . 1 1 30 30 GLU HA H 1 4.31 0.03 . 1 . . . . . . . . 4134 1 186 . 1 1 30 30 GLU HB2 H 1 2.04 0.03 . 2 . . . . . . . . 4134 1 187 . 1 1 30 30 GLU HG2 H 1 2.45 0.03 . 2 . . . . . . . . 4134 1 188 . 1 1 30 30 GLU CA C 13 56.6 0.2 . 1 . . . . . . . . 4134 1 189 . 1 1 30 30 GLU CB C 13 28.6 0.2 . 1 . . . . . . . . 4134 1 190 . 1 1 30 30 GLU N N 15 121.08 0.05 . 1 . . . . . . . . 4134 1 191 . 1 1 31 31 GLU H H 1 8.32 0.01 . 5 . . . . . . . . 4134 1 192 . 1 1 31 31 GLU HA H 1 4.15 0.03 . 5 . . . . . . . . 4134 1 193 . 1 1 31 31 GLU CA C 13 56.6 0.2 . 5 . . . . . . . . 4134 1 194 . 1 1 31 31 GLU CB C 13 28.6 0.2 . 5 . . . . . . . . 4134 1 195 . 1 1 31 31 GLU N N 15 120.36 0.05 . 5 . . . . . . . . 4134 1 196 . 1 1 32 32 LEU H H 1 8.21 0.01 . 1 . . . . . . . . 4134 1 197 . 1 1 32 32 LEU CA C 13 55.7 0.2 . 1 . . . . . . . . 4134 1 198 . 1 1 32 32 LEU CB C 13 42.4 0.2 . 1 . . . . . . . . 4134 1 199 . 1 1 32 32 LEU N N 15 122.46 0.05 . 1 . . . . . . . . 4134 1 200 . 1 1 33 33 GLU H H 1 8.29 0.01 . 1 . . . . . . . . 4134 1 201 . 1 1 33 33 GLU HA H 1 4.23 0.03 . 1 . . . . . . . . 4134 1 202 . 1 1 33 33 GLU HB2 H 1 2.04 0.03 . 2 . . . . . . . . 4134 1 203 . 1 1 33 33 GLU HG2 H 1 2.45 0.03 . 2 . . . . . . . . 4134 1 204 . 1 1 33 33 GLU CA C 13 56.2 0.2 . 1 . . . . . . . . 4134 1 205 . 1 1 33 33 GLU CB C 13 28.6 0.2 . 1 . . . . . . . . 4134 1 206 . 1 1 33 33 GLU N N 15 120.67 0.05 . 1 . . . . . . . . 4134 1 207 . 1 1 34 34 ALA H H 1 8.27 0.01 . 1 . . . . . . . . 4134 1 208 . 1 1 34 34 ALA HA H 1 4.23 0.03 . 1 . . . . . . . . 4134 1 209 . 1 1 34 34 ALA HB1 H 1 1.42 0.03 . 1 . . . . . . . . 4134 1 210 . 1 1 34 34 ALA HB2 H 1 1.42 0.03 . 1 . . . . . . . . 4134 1 211 . 1 1 34 34 ALA HB3 H 1 1.42 0.03 . 1 . . . . . . . . 4134 1 212 . 1 1 34 34 ALA CA C 13 52.7 0.2 . 1 . . . . . . . . 4134 1 213 . 1 1 34 34 ALA CB C 13 19.2 0.2 . 1 . . . . . . . . 4134 1 214 . 1 1 34 34 ALA N N 15 124.61 0.05 . 1 . . . . . . . . 4134 1 215 . 1 1 35 35 LEU H H 1 8.16 0.01 . 1 . . . . . . . . 4134 1 216 . 1 1 35 35 LEU CA C 13 55.3 0.2 . 1 . . . . . . . . 4134 1 217 . 1 1 35 35 LEU CB C 13 42.4 0.2 . 1 . . . . . . . . 4134 1 218 . 1 1 35 35 LEU N N 15 120.81 0.05 . 1 . . . . . . . . 4134 1 219 . 1 1 36 36 ASN H H 1 8.44 0.01 . 1 . . . . . . . . 4134 1 220 . 1 1 36 36 ASN HA H 1 4.7 0.03 . 5 . . . . . . . . 4134 1 221 . 1 1 36 36 ASN HB2 H 1 2.82 0.03 . 5 . . . . . . . . 4134 1 222 . 1 1 36 36 ASN CA C 13 53.2 0.2 . 1 . . . . . . . . 4134 1 223 . 1 1 36 36 ASN CB C 13 38.5 0.2 . 1 . . . . . . . . 4134 1 224 . 1 1 36 36 ASN N N 15 119.41 0.05 . 1 . . . . . . . . 4134 1 225 . 1 1 37 37 ILE H H 1 8.09 0.01 . 1 . . . . . . . . 4134 1 226 . 1 1 37 37 ILE HA H 1 4.15 0.03 . 1 . . . . . . . . 4134 1 227 . 1 1 37 37 ILE HB H 1 1.9 0.03 . 1 . . . . . . . . 4134 1 228 . 1 1 37 37 ILE HG12 H 1 1.45 0.03 . 2 . . . . . . . . 4134 1 229 . 1 1 37 37 ILE HG13 H 1 1.18 0.03 . 2 . . . . . . . . 4134 1 230 . 1 1 37 37 ILE CA C 13 61.3 0.2 . 1 . . . . . . . . 4134 1 231 . 1 1 37 37 ILE CB C 13 39.2 0.2 . 1 . . . . . . . . 4134 1 232 . 1 1 37 37 ILE N N 15 120.86 0.05 . 1 . . . . . . . . 4134 1 233 . 1 1 39 39 VAL H H 1 8.25 0.01 . 1 . . . . . . . . 4134 1 234 . 1 1 39 39 VAL HA H 1 4.08 0.03 . 1 . . . . . . . . 4134 1 235 . 1 1 39 39 VAL HB H 1 2.04 0.03 . 1 . . . . . . . . 4134 1 236 . 1 1 39 39 VAL HG11 H 1 0.95 0.03 . 2 . . . . . . . . 4134 1 237 . 1 1 39 39 VAL HG12 H 1 0.95 0.03 . 2 . . . . . . . . 4134 1 238 . 1 1 39 39 VAL HG13 H 1 0.95 0.03 . 2 . . . . . . . . 4134 1 239 . 1 1 39 39 VAL CA C 13 62.2 0.2 . 1 . . . . . . . . 4134 1 240 . 1 1 39 39 VAL CB C 13 32.9 0.2 . 1 . . . . . . . . 4134 1 241 . 1 1 39 39 VAL N N 15 121.82 0.05 . 1 . . . . . . . . 4134 1 242 . 1 1 40 40 ALA H H 1 8.4 0.01 . 1 . . . . . . . . 4134 1 243 . 1 1 40 40 ALA HA H 1 4.39 0.03 . 1 . . . . . . . . 4134 1 244 . 1 1 40 40 ALA HB1 H 1 1.37 0.03 . 1 . . . . . . . . 4134 1 245 . 1 1 40 40 ALA HB2 H 1 1.37 0.03 . 1 . . . . . . . . 4134 1 246 . 1 1 40 40 ALA HB3 H 1 1.37 0.03 . 1 . . . . . . . . 4134 1 247 . 1 1 40 40 ALA CA C 13 52.3 0.2 . 1 . . . . . . . . 4134 1 248 . 1 1 40 40 ALA CB C 13 19.6 0.2 . 1 . . . . . . . . 4134 1 249 . 1 1 40 40 ALA N N 15 127.82 0.05 . 1 . . . . . . . . 4134 1 250 . 1 1 41 41 VAL H H 1 8.24 0.01 . 1 . . . . . . . . 4134 1 251 . 1 1 41 41 VAL HA H 1 4.08 0.03 . 1 . . . . . . . . 4134 1 252 . 1 1 41 41 VAL HB H 1 2.04 0.03 . 1 . . . . . . . . 4134 1 253 . 1 1 41 41 VAL HG11 H 1 0.95 0.03 . 2 . . . . . . . . 4134 1 254 . 1 1 41 41 VAL HG12 H 1 0.95 0.03 . 2 . . . . . . . . 4134 1 255 . 1 1 41 41 VAL HG13 H 1 0.95 0.03 . 2 . . . . . . . . 4134 1 256 . 1 1 41 41 VAL CA C 13 62.6 0.2 . 1 . . . . . . . . 4134 1 257 . 1 1 41 41 VAL CB C 13 32.9 0.2 . 1 . . . . . . . . 4134 1 258 . 1 1 41 41 VAL N N 15 120.28 0.05 . 1 . . . . . . . . 4134 1 259 . 1 1 42 42 ALA H H 1 8.49 0.01 . 1 . . . . . . . . 4134 1 260 . 1 1 42 42 ALA HA H 1 4.31 0.03 . 1 . . . . . . . . 4134 1 261 . 1 1 42 42 ALA HB1 H 1 1.42 0.03 . 1 . . . . . . . . 4134 1 262 . 1 1 42 42 ALA HB2 H 1 1.42 0.03 . 1 . . . . . . . . 4134 1 263 . 1 1 42 42 ALA HB3 H 1 1.42 0.03 . 1 . . . . . . . . 4134 1 264 . 1 1 42 42 ALA CA C 13 52.7 0.2 . 1 . . . . . . . . 4134 1 265 . 1 1 42 42 ALA CB C 13 19.2 0.2 . 1 . . . . . . . . 4134 1 266 . 1 1 42 42 ALA N N 15 127.9 0.05 . 1 . . . . . . . . 4134 1 267 . 1 1 43 43 GLY H H 1 8.42 0.01 . 1 . . . . . . . . 4134 1 268 . 1 1 43 43 GLY HA2 H 1 4 0.03 . 2 . . . . . . . . 4134 1 269 . 1 1 43 43 GLY CA C 13 45.4 0.2 . 1 . . . . . . . . 4134 1 270 . 1 1 43 43 GLY N N 15 108.04 0.05 . 1 . . . . . . . . 4134 1 271 . 1 1 44 44 ARG H H 1 8.2 0.01 . 1 . . . . . . . . 4134 1 272 . 1 1 44 44 ARG HB2 H 1 1.8 0.03 . 4 . . . . . . . . 4134 1 273 . 1 1 44 44 ARG HB3 H 1 1.8 0.03 . 4 . . . . . . . . 4134 1 274 . 1 1 44 44 ARG HG2 H 1 1.8 0.03 . 4 . . . . . . . . 4134 1 275 . 1 1 44 44 ARG HG3 H 1 1.8 0.03 . 4 . . . . . . . . 4134 1 276 . 1 1 44 44 ARG CB C 13 31.2 0.2 . 1 . . . . . . . . 4134 1 277 . 1 1 44 44 ARG N N 15 120.59 0.05 . 1 . . . . . . . . 4134 1 278 . 1 1 45 45 MET H H 1 8.55 0.01 . 1 . . . . . . . . 4134 1 279 . 1 1 45 45 MET HA H 1 4.54 0.03 . 1 . . . . . . . . 4134 1 280 . 1 1 45 45 MET HB2 H 1 2.04 0.03 . 2 . . . . . . . . 4134 1 281 . 1 1 45 45 MET CA C 13 55.7 0.2 . 1 . . . . . . . . 4134 1 282 . 1 1 45 45 MET CB C 13 32.9 0.2 . 1 . . . . . . . . 4134 1 283 . 1 1 45 45 MET N N 15 121.8 0.05 . 1 . . . . . . . . 4134 1 284 . 1 1 46 46 MET H H 1 8.59 0.01 . 1 . . . . . . . . 4134 1 285 . 1 1 46 46 MET HA H 1 4.62 0.03 . 1 . . . . . . . . 4134 1 286 . 1 1 46 46 MET HB2 H 1 2.09 0.03 . 2 . . . . . . . . 4134 1 287 . 1 1 46 46 MET CA C 13 55.3 0.2 . 1 . . . . . . . . 4134 1 288 . 1 1 46 46 MET CB C 13 32.9 0.2 . 1 . . . . . . . . 4134 1 289 . 1 1 46 46 MET N N 15 122.64 0.05 . 1 . . . . . . . . 4134 1 290 . 1 1 47 47 THR H H 1 8.28 0.01 . 1 . . . . . . . . 4134 1 291 . 1 1 47 47 THR HG21 H 1 1.22 0.03 . 1 . . . . . . . . 4134 1 292 . 1 1 47 47 THR HG22 H 1 1.22 0.03 . 1 . . . . . . . . 4134 1 293 . 1 1 47 47 THR HG23 H 1 1.22 0.03 . 1 . . . . . . . . 4134 1 294 . 1 1 47 47 THR CA C 13 61.7 0.2 . 1 . . . . . . . . 4134 1 295 . 1 1 47 47 THR CB C 13 69.9 0.2 . 1 . . . . . . . . 4134 1 296 . 1 1 47 47 THR N N 15 116.3 0.05 . 1 . . . . . . . . 4134 1 297 . 1 1 48 48 ARG H H 1 8.49 0.01 . 1 . . . . . . . . 4134 1 298 . 1 1 48 48 ARG HA H 1 4.39 0.03 . 1 . . . . . . . . 4134 1 299 . 1 1 48 48 ARG HB2 H 1 1.81 0.03 . 4 . . . . . . . . 4134 1 300 . 1 1 48 48 ARG HB3 H 1 1.81 0.03 . 4 . . . . . . . . 4134 1 301 . 1 1 48 48 ARG HG2 H 1 1.81 0.03 . 4 . . . . . . . . 4134 1 302 . 1 1 48 48 ARG HG3 H 1 1.81 0.03 . 4 . . . . . . . . 4134 1 303 . 1 1 48 48 ARG CA C 13 56.2 0.2 . 1 . . . . . . . . 4134 1 304 . 1 1 48 48 ARG CB C 13 31.2 0.2 . 1 . . . . . . . . 4134 1 305 . 1 1 48 48 ARG N N 15 124.1 0.05 . 1 . . . . . . . . 4134 1 306 . 1 1 49 49 ARG H H 1 8.55 0.01 . 1 . . . . . . . . 4134 1 307 . 1 1 49 49 ARG HA H 1 4.39 0.03 . 1 . . . . . . . . 4134 1 308 . 1 1 49 49 ARG CA C 13 56.2 0.2 . 1 . . . . . . . . 4134 1 309 . 1 1 49 49 ARG CB C 13 31.2 0.2 . 1 . . . . . . . . 4134 1 310 . 1 1 49 49 ARG N N 15 123.75 0.05 . 1 . . . . . . . . 4134 1 311 . 1 1 50 50 ILE H H 1 8.47 0.01 . 1 . . . . . . . . 4134 1 312 . 1 1 50 50 ILE HA H 1 4.15 0.03 . 1 . . . . . . . . 4134 1 313 . 1 1 50 50 ILE CA C 13 60.9 0.2 . 1 . . . . . . . . 4134 1 314 . 1 1 50 50 ILE CB C 13 38.5 0.2 . 1 . . . . . . . . 4134 1 315 . 1 1 50 50 ILE N N 15 123.65 0.05 . 1 . . . . . . . . 4134 1 316 . 1 1 51 51 MET H H 1 8.65 0.01 . 1 . . . . . . . . 4134 1 317 . 1 1 51 51 MET HA H 1 4.55 0.03 . 1 . . . . . . . . 4134 1 318 . 1 1 51 51 MET HB2 H 1 2.04 0.03 . 2 . . . . . . . . 4134 1 319 . 1 1 51 51 MET CA C 13 55.3 0.2 . 1 . . . . . . . . 4134 1 320 . 1 1 51 51 MET CB C 13 32.9 0.2 . 1 . . . . . . . . 4134 1 321 . 1 1 51 51 MET N N 15 125.78 0.05 . 1 . . . . . . . . 4134 1 322 . 1 1 52 52 GLY H H 1 8.47 0.01 . 1 . . . . . . . . 4134 1 323 . 1 1 52 52 GLY HA2 H 1 4 0.03 . 2 . . . . . . . . 4134 1 324 . 1 1 52 52 GLY CA C 13 45.4 0.2 . 1 . . . . . . . . 4134 1 325 . 1 1 52 52 GLY N N 15 110.39 0.05 . 1 . . . . . . . . 4134 1 326 . 1 1 53 53 LYS H H 1 8.33 0.01 . 1 . . . . . . . . 4134 1 327 . 1 1 53 53 LYS HA H 1 4.31 0.03 . 1 . . . . . . . . 4134 1 328 . 1 1 53 53 LYS CA C 13 56.2 0.2 . 1 . . . . . . . . 4134 1 329 . 1 1 53 53 LYS CB C 13 33.4 0.2 . 1 . . . . . . . . 4134 1 330 . 1 1 53 53 LYS N N 15 121.2 0.05 . 1 . . . . . . . . 4134 1 331 . 1 1 54 54 ALA H H 1 8.51 0.01 . 1 . . . . . . . . 4134 1 332 . 1 1 54 54 ALA HA H 1 4.31 0.03 . 1 . . . . . . . . 4134 1 333 . 1 1 54 54 ALA HB1 H 1 1.34 0.03 . 1 . . . . . . . . 4134 1 334 . 1 1 54 54 ALA HB2 H 1 1.34 0.03 . 1 . . . . . . . . 4134 1 335 . 1 1 54 54 ALA HB3 H 1 1.34 0.03 . 1 . . . . . . . . 4134 1 336 . 1 1 54 54 ALA CA C 13 52.7 0.2 . 1 . . . . . . . . 4134 1 337 . 1 1 54 54 ALA CB C 13 19.6 0.2 . 1 . . . . . . . . 4134 1 338 . 1 1 54 54 ALA N N 15 125.76 0.05 . 1 . . . . . . . . 4134 1 339 . 1 1 55 55 SER H H 1 8.32 0.01 . 1 . . . . . . . . 4134 1 340 . 1 1 55 55 SER HA H 1 4.39 0.03 . 5 . . . . . . . . 4134 1 341 . 1 1 55 55 SER HB2 H 1 3.84 0.03 . 2 . . . . . . . . 4134 1 342 . 1 1 55 55 SER CA C 13 58.3 0.2 . 1 . . . . . . . . 4134 1 343 . 1 1 55 55 SER CB C 13 63.9 0.2 . 1 . . . . . . . . 4134 1 344 . 1 1 55 55 SER N N 15 115.44 0.05 . 1 . . . . . . . . 4134 1 345 . 1 1 56 56 PHE H H 1 8.3 0.01 . 1 . . . . . . . . 4134 1 346 . 1 1 56 56 PHE HA H 1 4.7 0.03 . 1 . . . . . . . . 4134 1 347 . 1 1 56 56 PHE HB2 H 1 3.06 0.03 . 2 . . . . . . . . 4134 1 348 . 1 1 56 56 PHE CA C 13 57.9 0.2 . 1 . . . . . . . . 4134 1 349 . 1 1 56 56 PHE CB C 13 39.8 0.2 . 1 . . . . . . . . 4134 1 350 . 1 1 56 56 PHE N N 15 122.24 0.05 . 1 . . . . . . . . 4134 1 351 . 1 1 57 57 VAL H H 1 8.19 0.01 . 1 . . . . . . . . 4134 1 352 . 1 1 57 57 VAL HB H 1 1.99 0.03 . 1 . . . . . . . . 4134 1 353 . 1 1 57 57 VAL HG11 H 1 0.9 0.03 . 2 . . . . . . . . 4134 1 354 . 1 1 57 57 VAL HG12 H 1 0.9 0.03 . 2 . . . . . . . . 4134 1 355 . 1 1 57 57 VAL HG13 H 1 0.9 0.03 . 2 . . . . . . . . 4134 1 356 . 1 1 57 57 VAL CA C 13 62.2 0.2 . 1 . . . . . . . . 4134 1 357 . 1 1 57 57 VAL CB C 13 33.4 0.2 . 1 . . . . . . . . 4134 1 358 . 1 1 57 57 VAL N N 15 122.26 0.05 . 1 . . . . . . . . 4134 1 359 . 1 1 58 58 THR H H 1 8.3 0.01 . 1 . . . . . . . . 4134 1 360 . 1 1 58 58 THR HA H 1 4.39 0.03 . 1 . . . . . . . . 4134 1 361 . 1 1 58 58 THR CA C 13 61.7 0.2 . 1 . . . . . . . . 4134 1 362 . 1 1 58 58 THR CB C 13 69.9 0.2 . 1 . . . . . . . . 4134 1 363 . 1 1 58 58 THR N N 15 119 0.05 . 1 . . . . . . . . 4134 1 364 . 1 1 59 59 LEU H H 1 8.43 0.01 . 1 . . . . . . . . 4134 1 365 . 1 1 59 59 LEU HA H 1 4.39 0.03 . 1 . . . . . . . . 4134 1 366 . 1 1 59 59 LEU HB2 H 1 1.65 0.03 . 4 . . . . . . . . 4134 1 367 . 1 1 59 59 LEU HB3 H 1 1.65 0.03 . 4 . . . . . . . . 4134 1 368 . 1 1 59 59 LEU HG H 1 1.65 0.03 . 4 . . . . . . . . 4134 1 369 . 1 1 59 59 LEU CA C 13 55.4 0.2 . 1 . . . . . . . . 4134 1 370 . 1 1 59 59 LEU CB C 13 42.4 0.2 . 1 . . . . . . . . 4134 1 371 . 1 1 59 59 LEU N N 15 125.23 0.05 . 1 . . . . . . . . 4134 1 372 . 1 1 60 60 GLN H H 1 8.5 0.01 . 1 . . . . . . . . 4134 1 373 . 1 1 60 60 GLN HA H 1 4.31 0.03 . 1 . . . . . . . . 4134 1 374 . 1 1 60 60 GLN HB2 H 1 1.96 0.03 . 2 . . . . . . . . 4134 1 375 . 1 1 60 60 GLN CA C 13 55.7 0.2 . 1 . . . . . . . . 4134 1 376 . 1 1 60 60 GLN CB C 13 29.9 0.2 . 1 . . . . . . . . 4134 1 377 . 1 1 60 60 GLN N N 15 120.84 0.05 . 1 . . . . . . . . 4134 1 378 . 1 1 61 61 ASP H H 1 8.59 0.01 . 1 . . . . . . . . 4134 1 379 . 1 1 61 61 ASP HA H 1 4.78 0.03 . 1 . . . . . . . . 4134 1 380 . 1 1 61 61 ASP HB2 H 1 2.81 0.03 . 2 . . . . . . . . 4134 1 381 . 1 1 61 61 ASP HB3 H 1 2.9 0.03 . 2 . . . . . . . . 4134 1 382 . 1 1 61 61 ASP CA C 13 52.7 0.2 . 1 . . . . . . . . 4134 1 383 . 1 1 61 61 ASP CB C 13 38.1 0.2 . 1 . . . . . . . . 4134 1 384 . 1 1 61 61 ASP N N 15 120.45 0.05 . 1 . . . . . . . . 4134 1 385 . 1 1 62 62 VAL H H 1 8.25 0.01 . 1 . . . . . . . . 4134 1 386 . 1 1 62 62 VAL HA H 1 4.15 0.03 . 1 . . . . . . . . 4134 1 387 . 1 1 62 62 VAL HB H 1 2.12 0.03 . 1 . . . . . . . . 4134 1 388 . 1 1 62 62 VAL HG11 H 1 0.93 0.03 . 2 . . . . . . . . 4134 1 389 . 1 1 62 62 VAL HG12 H 1 0.93 0.03 . 2 . . . . . . . . 4134 1 390 . 1 1 62 62 VAL HG13 H 1 0.93 0.03 . 2 . . . . . . . . 4134 1 391 . 1 1 62 62 VAL CA C 13 62.6 0.2 . 1 . . . . . . . . 4134 1 392 . 1 1 62 62 VAL CB C 13 32.9 0.2 . 1 . . . . . . . . 4134 1 393 . 1 1 62 62 VAL N N 15 120.9 0.05 . 1 . . . . . . . . 4134 1 394 . 1 1 63 63 GLY H H 1 8.6 0.01 . 1 . . . . . . . . 4134 1 395 . 1 1 63 63 GLY HA2 H 1 4 0.03 . 2 . . . . . . . . 4134 1 396 . 1 1 63 63 GLY CA C 13 45.4 0.2 . 1 . . . . . . . . 4134 1 397 . 1 1 63 63 GLY N N 15 112.63 0.05 . 1 . . . . . . . . 4134 1 398 . 1 1 64 64 GLY H H 1 8.26 0.01 . 1 . . . . . . . . 4134 1 399 . 1 1 64 64 GLY HA2 H 1 4 0.03 . 2 . . . . . . . . 4134 1 400 . 1 1 64 64 GLY CA C 13 45.4 0.2 . 1 . . . . . . . . 4134 1 401 . 1 1 64 64 GLY N N 15 108.3 0.05 . 1 . . . . . . . . 4134 1 402 . 1 1 65 65 ARG H H 1 8.28 0.01 . 1 . . . . . . . . 4134 1 403 . 1 1 65 65 ARG HA H 1 4.23 0.03 . 1 . . . . . . . . 4134 1 404 . 1 1 65 65 ARG HB2 H 1 1.88 0.03 . 4 . . . . . . . . 4134 1 405 . 1 1 65 65 ARG HB3 H 1 1.88 0.03 . 4 . . . . . . . . 4134 1 406 . 1 1 65 65 ARG HG2 H 1 1.88 0.03 . 4 . . . . . . . . 4134 1 407 . 1 1 65 65 ARG HG3 H 1 1.88 0.03 . 4 . . . . . . . . 4134 1 408 . 1 1 65 65 ARG CA C 13 55.7 0.2 . 1 . . . . . . . . 4134 1 409 . 1 1 65 65 ARG CB C 13 31.2 0.2 . 1 . . . . . . . . 4134 1 410 . 1 1 65 65 ARG N N 15 120.99 0.05 . 1 . . . . . . . . 4134 1 411 . 1 1 66 66 ILE H H 1 8.36 0.01 . 1 . . . . . . . . 4134 1 412 . 1 1 66 66 ILE HA H 1 4.15 0.03 . 1 . . . . . . . . 4134 1 413 . 1 1 66 66 ILE HB H 1 1.9 0.03 . 1 . . . . . . . . 4134 1 414 . 1 1 66 66 ILE CA C 13 60.9 0.2 . 1 . . . . . . . . 4134 1 415 . 1 1 66 66 ILE CB C 13 38.5 0.2 . 1 . . . . . . . . 4134 1 416 . 1 1 66 66 ILE N N 15 123.15 0.05 . 1 . . . . . . . . 4134 1 417 . 1 1 67 67 GLN H H 1 8.59 0.01 . 1 . . . . . . . . 4134 1 418 . 1 1 67 67 GLN HA H 1 4.39 0.03 . 1 . . . . . . . . 4134 1 419 . 1 1 67 67 GLN HB2 H 1 2 0.03 . 2 . . . . . . . . 4134 1 420 . 1 1 67 67 GLN CA C 13 55.3 0.2 . 1 . . . . . . . . 4134 1 421 . 1 1 67 67 GLN CB C 13 29.9 0.2 . 1 . . . . . . . . 4134 1 422 . 1 1 67 67 GLN N N 15 125.62 0.05 . 1 . . . . . . . . 4134 1 423 . 1 1 68 68 LEU H H 1 8.38 0.01 . 1 . . . . . . . . 4134 1 424 . 1 1 68 68 LEU HA H 1 4.31 0.03 . 1 . . . . . . . . 4134 1 425 . 1 1 68 68 LEU HB2 H 1 1.49 0.03 . 4 . . . . . . . . 4134 1 426 . 1 1 68 68 LEU HB3 H 1 1.49 0.03 . 4 . . . . . . . . 4134 1 427 . 1 1 68 68 LEU HG H 1 1.49 0.03 . 4 . . . . . . . . 4134 1 428 . 1 1 68 68 LEU HD11 H 1 0.86 0.03 . 2 . . . . . . . . 4134 1 429 . 1 1 68 68 LEU HD12 H 1 0.86 0.03 . 2 . . . . . . . . 4134 1 430 . 1 1 68 68 LEU HD13 H 1 0.86 0.03 . 2 . . . . . . . . 4134 1 431 . 1 1 68 68 LEU CA C 13 55.3 0.2 . 1 . . . . . . . . 4134 1 432 . 1 1 68 68 LEU CB C 13 42.4 0.2 . 1 . . . . . . . . 4134 1 433 . 1 1 68 68 LEU N N 15 124.6 0.05 . 1 . . . . . . . . 4134 1 434 . 1 1 69 69 TYR H H 1 8.41 0.01 . 1 . . . . . . . . 4134 1 435 . 1 1 69 69 TYR HA H 1 4.61 0.03 . 1 . . . . . . . . 4134 1 436 . 1 1 69 69 TYR HB2 H 1 2.9 0.03 . 2 . . . . . . . . 4134 1 437 . 1 1 69 69 TYR CA C 13 57.9 0.2 . 1 . . . . . . . . 4134 1 438 . 1 1 69 69 TYR CB C 13 39 0.2 . 1 . . . . . . . . 4134 1 439 . 1 1 69 69 TYR N N 15 121.96 0.05 . 1 . . . . . . . . 4134 1 440 . 1 1 70 70 VAL H H 1 8.04 0.01 . 1 . . . . . . . . 4134 1 441 . 1 1 70 70 VAL HA H 1 4 0.03 . 1 . . . . . . . . 4134 1 442 . 1 1 70 70 VAL HB H 1 1.88 0.03 . 1 . . . . . . . . 4134 1 443 . 1 1 70 70 VAL HG11 H 1 0.86 0.03 . 2 . . . . . . . . 4134 1 444 . 1 1 70 70 VAL HG12 H 1 0.86 0.03 . 2 . . . . . . . . 4134 1 445 . 1 1 70 70 VAL HG13 H 1 0.86 0.03 . 2 . . . . . . . . 4134 1 446 . 1 1 70 70 VAL CA C 13 61.7 0.2 . 1 . . . . . . . . 4134 1 447 . 1 1 70 70 VAL CB C 13 33.4 0.2 . 1 . . . . . . . . 4134 1 448 . 1 1 70 70 VAL N N 15 124.31 0.05 . 1 . . . . . . . . 4134 1 449 . 1 1 71 71 ALA H H 1 8.38 0.01 . 1 . . . . . . . . 4134 1 450 . 1 1 71 71 ALA HA H 1 4.23 0.03 . 1 . . . . . . . . 4134 1 451 . 1 1 71 71 ALA HB1 H 1 1.41 0.03 . 1 . . . . . . . . 4134 1 452 . 1 1 71 71 ALA HB2 H 1 1.41 0.03 . 1 . . . . . . . . 4134 1 453 . 1 1 71 71 ALA HB3 H 1 1.41 0.03 . 1 . . . . . . . . 4134 1 454 . 1 1 71 71 ALA CA C 13 52.3 0.2 . 1 . . . . . . . . 4134 1 455 . 1 1 71 71 ALA CB C 13 19.2 0.2 . 1 . . . . . . . . 4134 1 456 . 1 1 71 71 ALA N N 15 128.51 0.05 . 1 . . . . . . . . 4134 1 457 . 1 1 72 72 ARG H H 1 8.41 0.01 . 1 . . . . . . . . 4134 1 458 . 1 1 72 72 ARG HA H 1 4.32 0.03 . 1 . . . . . . . . 4134 1 459 . 1 1 72 72 ARG CA C 13 56.6 0.2 . 1 . . . . . . . . 4134 1 460 . 1 1 72 72 ARG CB C 13 30.8 0.2 . 1 . . . . . . . . 4134 1 461 . 1 1 72 72 ARG N N 15 120.69 0.05 . 1 . . . . . . . . 4134 1 462 . 1 1 73 73 ASP H H 1 8.53 0.01 . 1 . . . . . . . . 4134 1 463 . 1 1 73 73 ASP HA H 1 4.7 0.03 . 1 . . . . . . . . 4134 1 464 . 1 1 73 73 ASP HB2 H 1 2.9 0.03 . 2 . . . . . . . . 4134 1 465 . 1 1 73 73 ASP CA C 13 52.7 0.2 . 1 . . . . . . . . 4134 1 466 . 1 1 73 73 ASP CB C 13 38.1 0.2 . 1 . . . . . . . . 4134 1 467 . 1 1 73 73 ASP N N 15 119.35 0.05 . 1 . . . . . . . . 4134 1 468 . 1 1 74 74 ASP H H 1 8.43 0.01 . 1 . . . . . . . . 4134 1 469 . 1 1 74 74 ASP HA H 1 4.7 0.03 . 5 . . . . . . . . 4134 1 470 . 1 1 74 74 ASP HB2 H 1 2.82 0.03 . 5 . . . . . . . . 4134 1 471 . 1 1 74 74 ASP CB C 13 38.1 0.2 . 1 . . . . . . . . 4134 1 472 . 1 1 74 74 ASP N N 15 119.42 0.05 . 1 . . . . . . . . 4134 1 473 . 1 1 75 75 LEU H H 1 8.1 0.01 . 1 . . . . . . . . 4134 1 474 . 1 1 75 75 LEU HA H 1 4.62 0.03 . 1 . . . . . . . . 4134 1 475 . 1 1 75 75 LEU HB2 H 1 1.63 0.03 . 2 . . . . . . . . 4134 1 476 . 1 1 75 75 LEU HD11 H 1 0.9 0.03 . 2 . . . . . . . . 4134 1 477 . 1 1 75 75 LEU HD12 H 1 0.9 0.03 . 2 . . . . . . . . 4134 1 478 . 1 1 75 75 LEU HD13 H 1 0.9 0.03 . 2 . . . . . . . . 4134 1 479 . 1 1 75 75 LEU CA C 13 53.2 0.2 . 1 . . . . . . . . 4134 1 480 . 1 1 75 75 LEU CB C 13 42 0.2 . 1 . . . . . . . . 4134 1 481 . 1 1 75 75 LEU N N 15 123.19 0.05 . 1 . . . . . . . . 4134 1 482 . 1 1 76 76 PRO CA C 13 63 0.2 . 1 . . . . . . . . 4134 1 483 . 1 1 76 76 PRO CB C 13 32.1 0.2 . 1 . . . . . . . . 4134 1 484 . 1 1 77 77 GLU H H 1 8.55 0.01 . 1 . . . . . . . . 4134 1 485 . 1 1 77 77 GLU HA H 1 4.31 0.03 . 1 . . . . . . . . 4134 1 486 . 1 1 77 77 GLU HB2 H 1 2.04 0.03 . 2 . . . . . . . . 4134 1 487 . 1 1 77 77 GLU CA C 13 56.2 0.2 . 1 . . . . . . . . 4134 1 488 . 1 1 77 77 GLU CB C 13 29.1 0.2 . 1 . . . . . . . . 4134 1 489 . 1 1 77 77 GLU N N 15 120.84 0.05 . 1 . . . . . . . . 4134 1 490 . 1 1 78 78 GLY H H 1 8.51 0.01 . 1 . . . . . . . . 4134 1 491 . 1 1 78 78 GLY HA2 H 1 3.99 0.03 . 2 . . . . . . . . 4134 1 492 . 1 1 78 78 GLY CA C 13 45.4 0.2 . 1 . . . . . . . . 4134 1 493 . 1 1 78 78 GLY N N 15 110.04 0.05 . 1 . . . . . . . . 4134 1 494 . 1 1 79 79 VAL H H 1 7.91 0.01 . 1 . . . . . . . . 4134 1 495 . 1 1 79 79 VAL HA H 1 4.08 0.03 . 1 . . . . . . . . 4134 1 496 . 1 1 79 79 VAL HB H 1 2 0.03 . 1 . . . . . . . . 4134 1 497 . 1 1 79 79 VAL HG11 H 1 0.86 0.03 . 2 . . . . . . . . 4134 1 498 . 1 1 79 79 VAL HG12 H 1 0.86 0.03 . 2 . . . . . . . . 4134 1 499 . 1 1 79 79 VAL HG13 H 1 0.86 0.03 . 2 . . . . . . . . 4134 1 500 . 1 1 79 79 VAL CA C 13 62.6 0.2 . 1 . . . . . . . . 4134 1 501 . 1 1 79 79 VAL CB C 13 32.9 0.2 . 1 . . . . . . . . 4134 1 502 . 1 1 79 79 VAL N N 15 119.28 0.05 . 1 . . . . . . . . 4134 1 503 . 1 1 80 80 TYR H H 1 8.39 0.01 . 1 . . . . . . . . 4134 1 504 . 1 1 80 80 TYR CA C 13 57.9 0.2 . 1 . . . . . . . . 4134 1 505 . 1 1 80 80 TYR CB C 13 39 0.2 . 1 . . . . . . . . 4134 1 506 . 1 1 80 80 TYR N N 15 124.03 0.05 . 1 . . . . . . . . 4134 1 507 . 1 1 81 81 ASN CB C 13 39 0.2 . 1 . . . . . . . . 4134 1 508 . 1 1 82 82 GLU H H 1 8.42 0.01 . 1 . . . . . . . . 4134 1 509 . 1 1 82 82 GLU HA H 1 4.47 0.03 . 1 . . . . . . . . 4134 1 510 . 1 1 82 82 GLU CB C 13 28.6 0.2 . 1 . . . . . . . . 4134 1 511 . 1 1 82 82 GLU N N 15 124.01 0.05 . 1 . . . . . . . . 4134 1 512 . 1 1 83 83 GLN H H 1 8.48 0.01 . 5 . . . . . . . . 4134 1 513 . 1 1 83 83 GLN HA H 1 4.39 0.03 . 5 . . . . . . . . 4134 1 514 . 1 1 83 83 GLN CA C 13 56.2 0.2 . 5 . . . . . . . . 4134 1 515 . 1 1 83 83 GLN CB C 13 29.1 0.2 . 5 . . . . . . . . 4134 1 516 . 1 1 83 83 GLN N N 15 121.57 0.05 . 5 . . . . . . . . 4134 1 517 . 1 1 84 84 PHE H H 1 8.12 0.01 . 1 . . . . . . . . 4134 1 518 . 1 1 84 84 PHE HA H 1 4.55 0.03 . 1 . . . . . . . . 4134 1 519 . 1 1 84 84 PHE HB2 H 1 2.9 0.03 . 2 . . . . . . . . 4134 1 520 . 1 1 84 84 PHE HB3 H 1 3.14 0.03 . 2 . . . . . . . . 4134 1 521 . 1 1 84 84 PHE CA C 13 57.9 0.2 . 1 . . . . . . . . 4134 1 522 . 1 1 84 84 PHE CB C 13 39.4 0.2 . 1 . . . . . . . . 4134 1 523 . 1 1 84 84 PHE N N 15 120.29 0.05 . 1 . . . . . . . . 4134 1 524 . 1 1 85 85 LYS H H 1 8.15 0.01 . 1 . . . . . . . . 4134 1 525 . 1 1 85 85 LYS HA H 1 4.15 0.03 . 1 . . . . . . . . 4134 1 526 . 1 1 85 85 LYS CA C 13 56.2 0.2 . 1 . . . . . . . . 4134 1 527 . 1 1 85 85 LYS CB C 13 32.9 0.2 . 1 . . . . . . . . 4134 1 528 . 1 1 85 85 LYS N N 15 122.66 0.05 . 1 . . . . . . . . 4134 1 529 . 1 1 86 86 LYS H H 1 8.18 0.01 . 1 . . . . . . . . 4134 1 530 . 1 1 86 86 LYS HA H 1 4.15 0.03 . 1 . . . . . . . . 4134 1 531 . 1 1 86 86 LYS HB2 H 1 1.96 0.03 . 2 . . . . . . . . 4134 1 532 . 1 1 86 86 LYS HE2 H 1 3.45 0.03 . 2 . . . . . . . . 4134 1 533 . 1 1 86 86 LYS CA C 13 56.6 0.2 . 1 . . . . . . . . 4134 1 534 . 1 1 86 86 LYS CB C 13 33.4 0.2 . 1 . . . . . . . . 4134 1 535 . 1 1 86 86 LYS N N 15 121.95 0.05 . 1 . . . . . . . . 4134 1 536 . 1 1 87 87 TRP H H 1 8.26 0.01 . 1 . . . . . . . . 4134 1 537 . 1 1 87 87 TRP HA H 1 4.7 0.03 . 1 . . . . . . . . 4134 1 538 . 1 1 87 87 TRP HB2 H 1 3.22 0.03 . 2 . . . . . . . . 4134 1 539 . 1 1 87 87 TRP CA C 13 57 0.2 . 1 . . . . . . . . 4134 1 540 . 1 1 87 87 TRP CB C 13 29.9 0.2 . 1 . . . . . . . . 4134 1 541 . 1 1 87 87 TRP N N 15 122.06 0.05 . 1 . . . . . . . . 4134 1 542 . 1 1 88 88 ASP H H 1 8.37 0.01 . 1 . . . . . . . . 4134 1 543 . 1 1 88 88 ASP HA H 1 4.7 0.03 . 1 . . . . . . . . 4134 1 544 . 1 1 88 88 ASP HB2 H 1 2.75 0.03 . 2 . . . . . . . . 4134 1 545 . 1 1 88 88 ASP N N 15 120.88 0.05 . 1 . . . . . . . . 4134 1 546 . 1 1 89 89 LEU H H 1 8.13 0.01 . 1 . . . . . . . . 4134 1 547 . 1 1 89 89 LEU HA H 1 4.23 0.03 . 1 . . . . . . . . 4134 1 548 . 1 1 89 89 LEU HB2 H 1 1.59 0.03 . 4 . . . . . . . . 4134 1 549 . 1 1 89 89 LEU HB3 H 1 1.59 0.03 . 4 . . . . . . . . 4134 1 550 . 1 1 89 89 LEU HG H 1 1.59 0.03 . 4 . . . . . . . . 4134 1 551 . 1 1 89 89 LEU HD11 H 1 0.9 0.03 . 2 . . . . . . . . 4134 1 552 . 1 1 89 89 LEU HD12 H 1 0.9 0.03 . 2 . . . . . . . . 4134 1 553 . 1 1 89 89 LEU HD13 H 1 0.9 0.03 . 2 . . . . . . . . 4134 1 554 . 1 1 89 89 LEU CA C 13 55.7 0.2 . 1 . . . . . . . . 4134 1 555 . 1 1 89 89 LEU CB C 13 42 0.2 . 1 . . . . . . . . 4134 1 556 . 1 1 89 89 LEU N N 15 122.4 0.05 . 1 . . . . . . . . 4134 1 557 . 1 1 90 90 GLY H H 1 8.35 0.01 . 1 . . . . . . . . 4134 1 558 . 1 1 90 90 GLY HA2 H 1 3.92 0.03 . 2 . . . . . . . . 4134 1 559 . 1 1 90 90 GLY CA C 13 45.4 0.2 . 1 . . . . . . . . 4134 1 560 . 1 1 90 90 GLY N N 15 108.37 0.05 . 1 . . . . . . . . 4134 1 561 . 1 1 91 91 ASP H H 1 8.23 0.01 . 1 . . . . . . . . 4134 1 562 . 1 1 91 91 ASP HA H 1 4.7 0.03 . 1 . . . . . . . . 4134 1 563 . 1 1 91 91 ASP HB2 H 1 2.82 0.03 . 2 . . . . . . . . 4134 1 564 . 1 1 91 91 ASP CA C 13 53.2 0.2 . 1 . . . . . . . . 4134 1 565 . 1 1 91 91 ASP CB C 13 38.1 0.2 . 1 . . . . . . . . 4134 1 566 . 1 1 91 91 ASP N N 15 118.81 0.05 . 1 . . . . . . . . 4134 1 567 . 1 1 92 92 ILE H H 1 8.16 0.01 . 1 . . . . . . . . 4134 1 568 . 1 1 92 92 ILE HA H 1 4.15 0.03 . 1 . . . . . . . . 4134 1 569 . 1 1 92 92 ILE HB H 1 1.88 0.03 . 1 . . . . . . . . 4134 1 570 . 1 1 92 92 ILE CA C 13 61.3 0.2 . 1 . . . . . . . . 4134 1 571 . 1 1 92 92 ILE CB C 13 38.5 0.2 . 1 . . . . . . . . 4134 1 572 . 1 1 92 92 ILE N N 15 121.56 0.05 . 1 . . . . . . . . 4134 1 573 . 1 1 93 93 LEU H H 1 8.39 0.01 . 1 . . . . . . . . 4134 1 574 . 1 1 93 93 LEU HA H 1 4.31 0.03 . 1 . . . . . . . . 4134 1 575 . 1 1 93 93 LEU HB2 H 1 1.65 0.03 . 4 . . . . . . . . 4134 1 576 . 1 1 93 93 LEU HB3 H 1 1.65 0.03 . 4 . . . . . . . . 4134 1 577 . 1 1 93 93 LEU HG H 1 1.65 0.03 . 4 . . . . . . . . 4134 1 578 . 1 1 93 93 LEU HD11 H 1 0.86 0.03 . 2 . . . . . . . . 4134 1 579 . 1 1 93 93 LEU HD12 H 1 0.86 0.03 . 2 . . . . . . . . 4134 1 580 . 1 1 93 93 LEU HD13 H 1 0.86 0.03 . 2 . . . . . . . . 4134 1 581 . 1 1 93 93 LEU CA C 13 55.3 0.2 . 1 . . . . . . . . 4134 1 582 . 1 1 93 93 LEU CB C 13 42.4 0.2 . 1 . . . . . . . . 4134 1 583 . 1 1 93 93 LEU N N 15 125.74 0.05 . 1 . . . . . . . . 4134 1 584 . 1 1 94 94 GLY H H 1 8.36 0.01 . 1 . . . . . . . . 4134 1 585 . 1 1 94 94 GLY HA2 H 1 3.92 0.03 . 2 . . . . . . . . 4134 1 586 . 1 1 94 94 GLY CA C 13 45.4 0.2 . 1 . . . . . . . . 4134 1 587 . 1 1 94 94 GLY N N 15 109.64 0.05 . 1 . . . . . . . . 4134 1 588 . 1 1 95 95 ALA H H 1 8.21 0.01 . 1 . . . . . . . . 4134 1 589 . 1 1 95 95 ALA HA H 1 4.31 0.03 . 1 . . . . . . . . 4134 1 590 . 1 1 95 95 ALA HB1 H 1 1.4 0.03 . 1 . . . . . . . . 4134 1 591 . 1 1 95 95 ALA HB2 H 1 1.4 0.03 . 1 . . . . . . . . 4134 1 592 . 1 1 95 95 ALA HB3 H 1 1.4 0.03 . 1 . . . . . . . . 4134 1 593 . 1 1 95 95 ALA CA C 13 52.7 0.2 . 1 . . . . . . . . 4134 1 594 . 1 1 95 95 ALA CB C 13 19.6 0.2 . 1 . . . . . . . . 4134 1 595 . 1 1 95 95 ALA N N 15 123.8 0.05 . 1 . . . . . . . . 4134 1 596 . 1 1 96 96 LYS H H 1 8.45 0.01 . 1 . . . . . . . . 4134 1 597 . 1 1 96 96 LYS HA H 1 4.31 0.03 . 1 . . . . . . . . 4134 1 598 . 1 1 96 96 LYS HB2 H 1 1.81 0.03 . 2 . . . . . . . . 4134 1 599 . 1 1 96 96 LYS HG2 H 1 1.4 0.03 . 2 . . . . . . . . 4134 1 600 . 1 1 96 96 LYS CA C 13 56.6 0.2 . 1 . . . . . . . . 4134 1 601 . 1 1 96 96 LYS CB C 13 32.9 0.2 . 1 . . . . . . . . 4134 1 602 . 1 1 96 96 LYS N N 15 120.4 0.05 . 1 . . . . . . . . 4134 1 603 . 1 1 97 97 GLY H H 1 8.39 0.01 . 1 . . . . . . . . 4134 1 604 . 1 1 97 97 GLY HA2 H 1 3.92 0.03 . 2 . . . . . . . . 4134 1 605 . 1 1 97 97 GLY CA C 13 45.4 0.2 . 1 . . . . . . . . 4134 1 606 . 1 1 97 97 GLY N N 15 109.64 0.05 . 1 . . . . . . . . 4134 1 607 . 1 1 98 98 LYS H H 1 8.2 0.01 . 1 . . . . . . . . 4134 1 608 . 1 1 98 98 LYS HA H 1 4.28 0.03 . 1 . . . . . . . . 4134 1 609 . 1 1 98 98 LYS CA C 13 56.2 0.2 . 1 . . . . . . . . 4134 1 610 . 1 1 98 98 LYS CB C 13 33.4 0.2 . 1 . . . . . . . . 4134 1 611 . 1 1 98 98 LYS N N 15 120.88 0.05 . 1 . . . . . . . . 4134 1 612 . 1 1 99 99 LEU H H 1 8.3 0.01 . 1 . . . . . . . . 4134 1 613 . 1 1 99 99 LEU HA H 1 4.39 0.03 . 1 . . . . . . . . 4134 1 614 . 1 1 99 99 LEU HB2 H 1 1.57 0.03 . 4 . . . . . . . . 4134 1 615 . 1 1 99 99 LEU HB3 H 1 1.57 0.03 . 4 . . . . . . . . 4134 1 616 . 1 1 99 99 LEU HG H 1 1.57 0.03 . 4 . . . . . . . . 4134 1 617 . 1 1 99 99 LEU CA C 13 54.9 0.2 . 1 . . . . . . . . 4134 1 618 . 1 1 99 99 LEU CB C 13 42.4 0.2 . 1 . . . . . . . . 4134 1 619 . 1 1 99 99 LEU N N 15 123.23 0.05 . 1 . . . . . . . . 4134 1 620 . 1 1 100 100 PHE H H 1 8.4 0.01 . 1 . . . . . . . . 4134 1 621 . 1 1 100 100 PHE HA H 1 4.62 0.03 . 1 . . . . . . . . 4134 1 622 . 1 1 100 100 PHE HB2 H 1 2.98 0.03 . 2 . . . . . . . . 4134 1 623 . 1 1 100 100 PHE CA C 13 57.4 0.2 . 1 . . . . . . . . 4134 1 624 . 1 1 100 100 PHE CB C 13 39.8 0.2 . 1 . . . . . . . . 4134 1 625 . 1 1 100 100 PHE N N 15 121.96 0.05 . 1 . . . . . . . . 4134 1 626 . 1 1 101 101 LYS H H 1 8.4 0.01 . 1 . . . . . . . . 4134 1 627 . 1 1 101 101 LYS HA H 1 4.39 0.03 . 1 . . . . . . . . 4134 1 628 . 1 1 101 101 LYS HB2 H 1 1.73 0.03 . 2 . . . . . . . . 4134 1 629 . 1 1 101 101 LYS CA C 13 56.2 0.2 . 1 . . . . . . . . 4134 1 630 . 1 1 101 101 LYS CB C 13 33.4 0.2 . 1 . . . . . . . . 4134 1 631 . 1 1 101 101 LYS N N 15 123.81 0.05 . 1 . . . . . . . . 4134 1 632 . 1 1 102 102 THR H H 1 8.29 0.01 . 1 . . . . . . . . 4134 1 633 . 1 1 102 102 THR HG21 H 1 1.22 0.03 . 1 . . . . . . . . 4134 1 634 . 1 1 102 102 THR HG22 H 1 1.22 0.03 . 1 . . . . . . . . 4134 1 635 . 1 1 102 102 THR HG23 H 1 1.22 0.03 . 1 . . . . . . . . 4134 1 636 . 1 1 102 102 THR CA C 13 61.7 0.2 . 1 . . . . . . . . 4134 1 637 . 1 1 102 102 THR CB C 13 69.9 0.2 . 1 . . . . . . . . 4134 1 638 . 1 1 102 102 THR N N 15 116.39 0.05 . 1 . . . . . . . . 4134 1 639 . 1 1 103 103 LYS H H 1 8.6 0.01 . 1 . . . . . . . . 4134 1 640 . 1 1 103 103 LYS HA H 1 4.39 0.03 . 1 . . . . . . . . 4134 1 641 . 1 1 103 103 LYS HB2 H 1 1.81 0.03 . 2 . . . . . . . . 4134 1 642 . 1 1 103 103 LYS CA C 13 56.6 0.2 . 1 . . . . . . . . 4134 1 643 . 1 1 103 103 LYS CB C 13 33.4 0.2 . 1 . . . . . . . . 4134 1 644 . 1 1 103 103 LYS N N 15 124.02 0.05 . 1 . . . . . . . . 4134 1 645 . 1 1 104 104 THR H H 1 8.28 0.01 . 1 . . . . . . . . 4134 1 646 . 1 1 104 104 THR HA H 1 4.31 0.03 . 1 . . . . . . . . 4134 1 647 . 1 1 104 104 THR HG21 H 1 1.22 0.03 . 1 . . . . . . . . 4134 1 648 . 1 1 104 104 THR HG22 H 1 1.22 0.03 . 1 . . . . . . . . 4134 1 649 . 1 1 104 104 THR HG23 H 1 1.22 0.03 . 1 . . . . . . . . 4134 1 650 . 1 1 104 104 THR CA C 13 62.2 0.2 . 1 . . . . . . . . 4134 1 651 . 1 1 104 104 THR CB C 13 69.9 0.2 . 1 . . . . . . . . 4134 1 652 . 1 1 104 104 THR N N 15 115.21 0.05 . 1 . . . . . . . . 4134 1 653 . 1 1 105 105 GLY H H 1 8.49 0.01 . 1 . . . . . . . . 4134 1 654 . 1 1 105 105 GLY HA2 H 1 4 0.03 . 2 . . . . . . . . 4134 1 655 . 1 1 105 105 GLY CA C 13 45.4 0.2 . 1 . . . . . . . . 4134 1 656 . 1 1 105 105 GLY N N 15 111.21 0.05 . 1 . . . . . . . . 4134 1 657 . 1 1 106 106 GLU H H 1 8.27 0.01 . 1 . . . . . . . . 4134 1 658 . 1 1 106 106 GLU HA H 1 4.39 0.03 . 1 . . . . . . . . 4134 1 659 . 1 1 106 106 GLU HB2 H 1 2.04 0.03 . 2 . . . . . . . . 4134 1 660 . 1 1 106 106 GLU HG2 H 1 2.45 0.03 . 2 . . . . . . . . 4134 1 661 . 1 1 106 106 GLU CA C 13 55.7 0.2 . 1 . . . . . . . . 4134 1 662 . 1 1 106 106 GLU CB C 13 29.1 0.2 . 1 . . . . . . . . 4134 1 663 . 1 1 106 106 GLU N N 15 119.91 0.05 . 1 . . . . . . . . 4134 1 664 . 1 1 107 107 LEU H H 1 8.45 0.01 . 5 . . . . . . . . 4134 1 665 . 1 1 107 107 LEU HA H 1 4.31 0.03 . 5 . . . . . . . . 4134 1 666 . 1 1 107 107 LEU HB2 H 1 1.57 0.03 . 5 . . . . . . . . 4134 1 667 . 1 1 107 107 LEU HB3 H 1 1.57 0.03 . 5 . . . . . . . . 4134 1 668 . 1 1 107 107 LEU HG H 1 1.57 0.03 . 5 . . . . . . . . 4134 1 669 . 1 1 107 107 LEU CA C 13 55.3 0.2 . 5 . . . . . . . . 4134 1 670 . 1 1 107 107 LEU CB C 13 42.4 0.2 . 5 . . . . . . . . 4134 1 671 . 1 1 107 107 LEU N N 15 123.81 0.05 . 5 . . . . . . . . 4134 1 672 . 1 1 108 108 SER H H 1 8.43 0.01 . 1 . . . . . . . . 4134 1 673 . 1 1 108 108 SER HA H 1 4.47 0.03 . 1 . . . . . . . . 4134 1 674 . 1 1 108 108 SER HB2 H 1 3.84 0.03 . 2 . . . . . . . . 4134 1 675 . 1 1 108 108 SER CA C 13 57.9 0.2 . 1 . . . . . . . . 4134 1 676 . 1 1 108 108 SER CB C 13 63.9 0.2 . 1 . . . . . . . . 4134 1 677 . 1 1 108 108 SER N N 15 117.18 0.05 . 1 . . . . . . . . 4134 1 678 . 1 1 109 109 ILE H H 1 8.21 0.01 . 1 . . . . . . . . 4134 1 679 . 1 1 109 109 ILE HA H 1 4.18 0.03 . 1 . . . . . . . . 4134 1 680 . 1 1 109 109 ILE CA C 13 61.3 0.2 . 1 . . . . . . . . 4134 1 681 . 1 1 109 109 ILE CB C 13 39 0.2 . 1 . . . . . . . . 4134 1 682 . 1 1 109 109 ILE N N 15 122.46 0.05 . 1 . . . . . . . . 4134 1 683 . 1 1 110 110 HIS H H 1 8.68 0.01 . 1 . . . . . . . . 4134 1 684 . 1 1 110 110 HIS HA H 1 4.78 0.03 . 1 . . . . . . . . 4134 1 685 . 1 1 110 110 HIS HB2 H 1 3.22 0.03 . 2 . . . . . . . . 4134 1 686 . 1 1 110 110 HIS CA C 13 55.3 0.2 . 1 . . . . . . . . 4134 1 687 . 1 1 110 110 HIS CB C 13 29.1 0.2 . 1 . . . . . . . . 4134 1 688 . 1 1 110 110 HIS N N 15 122.43 0.05 . 1 . . . . . . . . 4134 1 689 . 1 1 111 111 CYS H H 1 8.53 0.01 . 1 . . . . . . . . 4134 1 690 . 1 1 111 111 CYS HA H 1 4.68 0.03 . 1 . . . . . . . . 4134 1 691 . 1 1 111 111 CYS HB2 H 1 2.95 0.03 . 2 . . . . . . . . 4134 1 692 . 1 1 111 111 CYS CA C 13 58.7 0.2 . 1 . . . . . . . . 4134 1 693 . 1 1 111 111 CYS CB C 13 28.2 0.2 . 1 . . . . . . . . 4134 1 694 . 1 1 111 111 CYS N N 15 121.73 0.05 . 1 . . . . . . . . 4134 1 695 . 1 1 112 112 THR H H 1 8.51 0.01 . 1 . . . . . . . . 4134 1 696 . 1 1 112 112 THR HA H 1 4.31 0.03 . 1 . . . . . . . . 4134 1 697 . 1 1 112 112 THR CA C 13 62.2 0.2 . 1 . . . . . . . . 4134 1 698 . 1 1 112 112 THR CB C 13 69.5 0.2 . 1 . . . . . . . . 4134 1 699 . 1 1 112 112 THR N N 15 117.75 0.05 . 1 . . . . . . . . 4134 1 700 . 1 1 113 113 GLU H H 1 8.42 0.01 . 1 . . . . . . . . 4134 1 701 . 1 1 113 113 GLU HA H 1 4.39 0.03 . 1 . . . . . . . . 4134 1 702 . 1 1 113 113 GLU HB2 H 1 2.04 0.03 . 2 . . . . . . . . 4134 1 703 . 1 1 113 113 GLU CA C 13 55.7 0.2 . 1 . . . . . . . . 4134 1 704 . 1 1 113 113 GLU CB C 13 29.1 0.2 . 1 . . . . . . . . 4134 1 705 . 1 1 113 113 GLU N N 15 123.24 0.05 . 1 . . . . . . . . 4134 1 706 . 1 1 114 114 LEU H H 1 8.39 0.01 . 5 . . . . . . . . 4134 1 707 . 1 1 114 114 LEU HA H 1 4.31 0.03 . 5 . . . . . . . . 4134 1 708 . 1 1 114 114 LEU HB2 H 1 1.57 0.03 . 5 . . . . . . . . 4134 1 709 . 1 1 114 114 LEU HB3 H 1 1.57 0.03 . 5 . . . . . . . . 4134 1 710 . 1 1 114 114 LEU HG H 1 1.57 0.03 . 5 . . . . . . . . 4134 1 711 . 1 1 114 114 LEU CA C 13 55.3 0.2 . 5 . . . . . . . . 4134 1 712 . 1 1 114 114 LEU CB C 13 42.4 0.2 . 5 . . . . . . . . 4134 1 713 . 1 1 114 114 LEU N N 15 124.3 0.05 . 5 . . . . . . . . 4134 1 714 . 1 1 115 115 ARG H H 1 8.48 0.01 . 1 . . . . . . . . 4134 1 715 . 1 1 115 115 ARG HA H 1 4.31 0.03 . 1 . . . . . . . . 4134 1 716 . 1 1 115 115 ARG HB2 H 1 1.81 0.03 . 1 . . . . . . . . 4134 1 717 . 1 1 115 115 ARG HB3 H 1 1.81 0.03 . 1 . . . . . . . . 4134 1 718 . 1 1 115 115 ARG CA C 13 55.7 0.2 . 1 . . . . . . . . 4134 1 719 . 1 1 115 115 ARG CB C 13 30.8 0.2 . 1 . . . . . . . . 4134 1 720 . 1 1 115 115 ARG N N 15 122.67 0.05 . 1 . . . . . . . . 4134 1 721 . 1 1 116 116 LEU H H 1 8.37 0.01 . 1 . . . . . . . . 4134 1 722 . 1 1 116 116 LEU HA H 1 4.39 0.03 . 1 . . . . . . . . 4134 1 723 . 1 1 116 116 LEU HB2 H 1 1.65 0.03 . 4 . . . . . . . . 4134 1 724 . 1 1 116 116 LEU HB3 H 1 1.65 0.03 . 4 . . . . . . . . 4134 1 725 . 1 1 116 116 LEU HG H 1 1.65 0.03 . 4 . . . . . . . . 4134 1 726 . 1 1 116 116 LEU CA C 13 54.9 0.2 . 1 . . . . . . . . 4134 1 727 . 1 1 116 116 LEU CB C 13 42.4 0.2 . 1 . . . . . . . . 4134 1 728 . 1 1 116 116 LEU N N 15 124.01 0.05 . 1 . . . . . . . . 4134 1 729 . 1 1 117 117 LEU H H 1 8.45 0.01 . 1 . . . . . . . . 4134 1 730 . 1 1 117 117 LEU HB2 H 1 1.63 0.03 . 4 . . . . . . . . 4134 1 731 . 1 1 117 117 LEU HB3 H 1 1.63 0.03 . 4 . . . . . . . . 4134 1 732 . 1 1 117 117 LEU HG H 1 1.63 0.03 . 4 . . . . . . . . 4134 1 733 . 1 1 117 117 LEU CA C 13 54.9 0.2 . 1 . . . . . . . . 4134 1 734 . 1 1 117 117 LEU CB C 13 42.4 0.2 . 1 . . . . . . . . 4134 1 735 . 1 1 117 117 LEU N N 15 123.81 0.05 . 1 . . . . . . . . 4134 1 736 . 1 1 118 118 THR H H 1 8.18 0.01 . 1 . . . . . . . . 4134 1 737 . 1 1 118 118 THR HA H 1 4.31 0.03 . 1 . . . . . . . . 4134 1 738 . 1 1 118 118 THR CA C 13 61.7 0.2 . 1 . . . . . . . . 4134 1 739 . 1 1 118 118 THR CB C 13 69.9 0.2 . 1 . . . . . . . . 4134 1 740 . 1 1 118 118 THR N N 15 115.74 0.05 . 1 . . . . . . . . 4134 1 741 . 1 1 119 119 LYS H H 1 8.45 0.01 . 1 . . . . . . . . 4134 1 742 . 1 1 119 119 LYS HA H 1 4.31 0.03 . 1 . . . . . . . . 4134 1 743 . 1 1 119 119 LYS HB2 H 1 1.81 0.03 . 2 . . . . . . . . 4134 1 744 . 1 1 119 119 LYS CA C 13 56.2 0.2 . 1 . . . . . . . . 4134 1 745 . 1 1 119 119 LYS CB C 13 33.4 0.2 . 1 . . . . . . . . 4134 1 746 . 1 1 119 119 LYS N N 15 124.3 0.05 . 1 . . . . . . . . 4134 1 747 . 1 1 120 120 ALA H H 1 8.54 0.01 . 1 . . . . . . . . 4134 1 748 . 1 1 120 120 ALA HA H 1 4.31 0.03 . 1 . . . . . . . . 4134 1 749 . 1 1 120 120 ALA HB1 H 1 1.42 0.03 . 1 . . . . . . . . 4134 1 750 . 1 1 120 120 ALA HB2 H 1 1.42 0.03 . 1 . . . . . . . . 4134 1 751 . 1 1 120 120 ALA HB3 H 1 1.42 0.03 . 1 . . . . . . . . 4134 1 752 . 1 1 120 120 ALA CA C 13 51.9 0.2 . 1 . . . . . . . . 4134 1 753 . 1 1 120 120 ALA CB C 13 19.2 0.2 . 1 . . . . . . . . 4134 1 754 . 1 1 120 120 ALA N N 15 127.72 0.05 . 1 . . . . . . . . 4134 1 stop_ save_